data_2YP2 # _entry.id 2YP2 # _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 2YP2 PDBE EBI-54619 WWPDB D_1290054619 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 2YP3 unspecified 'HAEMAGGLUTININ OF 2004 HUMAN H3N2 VIRUS IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6SLN' PDB 2YP4 unspecified 'HAEMAGGLUTININ OF 2004 HUMAN H3N2 VIRUS IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE LSTC' PDB 2YP5 unspecified 'HAEMAGGLUTININ OF 2004 HUMAN H3N2 VIRUS IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3SLN' PDB 2YP7 unspecified 'HAEMAGGLUTININ OF 2005 HUMAN H3N2 VIRUS' PDB 2YP8 unspecified 'HAEMAGGLUTININ OF 2005 HUMAN H3N2 VIRUS IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6SLN' PDB 2YP9 unspecified 'HAEMAGGLUTININ OF 2005 HUMAN H3N2 VIRUS IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3SLN' PDB 2YPG unspecified 'HAEMAGGLUTININ OF 1968 HUMAN H3N2 VIRUS IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE LSTC' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2YP2 _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2012-10-29 _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 'Xiong, X.' 1 'Lin, Y.P.' 2 'Wharton, S.A.' 3 'Martin, S.R.' 4 'Coombs, P.J.' 5 'Vachieri, S.G.' 6 'Christodoulou, E.' 7 'Walker, P.A.' 8 'Liu, J.' 9 'Skehel, J.J.' 10 'Gamblin, S.J.' 11 'Hay, A.J.' 12 'Daniels, R.S.' 13 'McCauley, J.W.' 14 # _citation.id primary _citation.title 'Evolution of the Receptor Binding Properties of the Influenza A(H3N2) Hemagglutinin.' _citation.journal_abbrev Proc.Natl.Acad.Sci.USA _citation.journal_volume 109 _citation.page_first 21474 _citation.page_last ? _citation.year 2012 _citation.journal_id_ASTM PNASA6 _citation.country US _citation.journal_id_ISSN 0027-8424 _citation.journal_id_CSD 0040 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 23236176 _citation.pdbx_database_id_DOI 10.1073/PNAS.1218841110 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Lin, Y.P.' 1 primary 'Xiong, X.' 2 primary 'Wharton, S.A.' 3 primary 'Martin, S.R.' 4 primary 'Coombs, P.J.' 5 primary 'Vachieri, S.G.' 6 primary 'Christodoulou, E.' 7 primary 'Walker, P.A.' 8 primary 'Liu, J.' 9 primary 'Skehel, J.J.' 10 primary 'Gamblin, S.J.' 11 primary 'Hay, A.J.' 12 primary 'Daniels, R.S.' 13 primary 'Mccauley, J.W.' 14 # _cell.entry_id 2YP2 _cell.length_a 100.920 _cell.length_b 100.920 _cell.length_c 387.180 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 18 _cell.pdbx_unique_axis ? # _symmetry.entry_id 2YP2 _symmetry.space_group_name_H-M 'H 3 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 155 # 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 HEMAGGLUTININ 56457.117 1 ? YES 'TRYPSIN RELEASED ECTODOMAIN, RESIDUES 17-519' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 10 ? ? ? ? 3 non-polymer man ALPHA-D-MANNOSE 180.156 2 ? ? ? ? 4 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305 3 ? ? ? ? 5 non-polymer syn 'TRIS(HYDROXYETHYL)AMINOMETHANE' 163.215 1 ? ? ? ? 6 water nat water 18.015 428 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name HAEMAGGLUTININ # _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 ;QKLPGNDNSTATLCLGHHAVPNGTIVKTITNDQIEVTNATELVQSSSTGGICDSPHQILDGENCTLIDALLGDPQCDGFQ NKKWDLFVERSKAYSNCYPYDVPDYASLRSLVASSGTLEFNNESFNWTGVTQNGTSSACKRRSNNSFFSRLNWLTHLKFK YPALNVTMPNNEKFDKLYIWGVHHPGTDNDQISLYAQASGRITVSTKRSQQTVIPNIGSRPRVRDIPSRISIYWTIVKPG DILLINSTGNLIAPRGYFKIRSGKSSIMRSDAPIGKCNSECITPNGSIPNDKPFQNVNRITYGACPRYVKQNTLKLATGM RNVPEKQTQGIFGAIAGFIENGWEGMVDGWYGFRHQNSEGIGQAADLKSTQAAINQINGKLNRLIGKTNEKFHQIEKEFS EVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFERTKKQLRENAEDMGNGCFKIYHKCDNACIGS IRNGTYDHDVYRDEALNNRFQIK ; _entity_poly.pdbx_seq_one_letter_code_can ;QKLPGNDNSTATLCLGHHAVPNGTIVKTITNDQIEVTNATELVQSSSTGGICDSPHQILDGENCTLIDALLGDPQCDGFQ NKKWDLFVERSKAYSNCYPYDVPDYASLRSLVASSGTLEFNNESFNWTGVTQNGTSSACKRRSNNSFFSRLNWLTHLKFK YPALNVTMPNNEKFDKLYIWGVHHPGTDNDQISLYAQASGRITVSTKRSQQTVIPNIGSRPRVRDIPSRISIYWTIVKPG DILLINSTGNLIAPRGYFKIRSGKSSIMRSDAPIGKCNSECITPNGSIPNDKPFQNVNRITYGACPRYVKQNTLKLATGM RNVPEKQTQGIFGAIAGFIENGWEGMVDGWYGFRHQNSEGIGQAADLKSTQAAINQINGKLNRLIGKTNEKFHQIEKEFS EVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFERTKKQLRENAEDMGNGCFKIYHKCDNACIGS IRNGTYDHDVYRDEALNNRFQIK ; _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 GLN n 1 2 LYS n 1 3 LEU n 1 4 PRO n 1 5 GLY n 1 6 ASN n 1 7 ASP n 1 8 ASN n 1 9 SER n 1 10 THR n 1 11 ALA n 1 12 THR n 1 13 LEU n 1 14 CYS n 1 15 LEU n 1 16 GLY n 1 17 HIS n 1 18 HIS n 1 19 ALA n 1 20 VAL n 1 21 PRO n 1 22 ASN n 1 23 GLY n 1 24 THR n 1 25 ILE n 1 26 VAL n 1 27 LYS n 1 28 THR n 1 29 ILE n 1 30 THR n 1 31 ASN n 1 32 ASP n 1 33 GLN n 1 34 ILE n 1 35 GLU n 1 36 VAL n 1 37 THR n 1 38 ASN n 1 39 ALA n 1 40 THR n 1 41 GLU n 1 42 LEU n 1 43 VAL n 1 44 GLN n 1 45 SER n 1 46 SER n 1 47 SER n 1 48 THR n 1 49 GLY n 1 50 GLY n 1 51 ILE n 1 52 CYS n 1 53 ASP n 1 54 SER n 1 55 PRO n 1 56 HIS n 1 57 GLN n 1 58 ILE n 1 59 LEU n 1 60 ASP n 1 61 GLY n 1 62 GLU n 1 63 ASN n 1 64 CYS n 1 65 THR n 1 66 LEU n 1 67 ILE n 1 68 ASP n 1 69 ALA n 1 70 LEU n 1 71 LEU n 1 72 GLY n 1 73 ASP n 1 74 PRO n 1 75 GLN n 1 76 CYS n 1 77 ASP n 1 78 GLY n 1 79 PHE n 1 80 GLN n 1 81 ASN n 1 82 LYS n 1 83 LYS n 1 84 TRP n 1 85 ASP n 1 86 LEU n 1 87 PHE n 1 88 VAL n 1 89 GLU n 1 90 ARG n 1 91 SER n 1 92 LYS n 1 93 ALA n 1 94 TYR n 1 95 SER n 1 96 ASN n 1 97 CYS n 1 98 TYR n 1 99 PRO n 1 100 TYR n 1 101 ASP n 1 102 VAL n 1 103 PRO n 1 104 ASP n 1 105 TYR n 1 106 ALA n 1 107 SER n 1 108 LEU n 1 109 ARG n 1 110 SER n 1 111 LEU n 1 112 VAL n 1 113 ALA n 1 114 SER n 1 115 SER n 1 116 GLY n 1 117 THR n 1 118 LEU n 1 119 GLU n 1 120 PHE n 1 121 ASN n 1 122 ASN n 1 123 GLU n 1 124 SER n 1 125 PHE n 1 126 ASN n 1 127 TRP n 1 128 THR n 1 129 GLY n 1 130 VAL n 1 131 THR n 1 132 GLN n 1 133 ASN n 1 134 GLY n 1 135 THR n 1 136 SER n 1 137 SER n 1 138 ALA n 1 139 CYS n 1 140 LYS n 1 141 ARG n 1 142 ARG n 1 143 SER n 1 144 ASN n 1 145 ASN n 1 146 SER n 1 147 PHE n 1 148 PHE n 1 149 SER n 1 150 ARG n 1 151 LEU n 1 152 ASN n 1 153 TRP n 1 154 LEU n 1 155 THR n 1 156 HIS n 1 157 LEU n 1 158 LYS n 1 159 PHE n 1 160 LYS n 1 161 TYR n 1 162 PRO n 1 163 ALA n 1 164 LEU n 1 165 ASN n 1 166 VAL n 1 167 THR n 1 168 MET n 1 169 PRO n 1 170 ASN n 1 171 ASN n 1 172 GLU n 1 173 LYS n 1 174 PHE n 1 175 ASP n 1 176 LYS n 1 177 LEU n 1 178 TYR n 1 179 ILE n 1 180 TRP n 1 181 GLY n 1 182 VAL n 1 183 HIS n 1 184 HIS n 1 185 PRO n 1 186 GLY n 1 187 THR n 1 188 ASP n 1 189 ASN n 1 190 ASP n 1 191 GLN n 1 192 ILE n 1 193 SER n 1 194 LEU n 1 195 TYR n 1 196 ALA n 1 197 GLN n 1 198 ALA n 1 199 SER n 1 200 GLY n 1 201 ARG n 1 202 ILE n 1 203 THR n 1 204 VAL n 1 205 SER n 1 206 THR n 1 207 LYS n 1 208 ARG n 1 209 SER n 1 210 GLN n 1 211 GLN n 1 212 THR n 1 213 VAL n 1 214 ILE n 1 215 PRO n 1 216 ASN n 1 217 ILE n 1 218 GLY n 1 219 SER n 1 220 ARG n 1 221 PRO n 1 222 ARG n 1 223 VAL n 1 224 ARG n 1 225 ASP n 1 226 ILE n 1 227 PRO n 1 228 SER n 1 229 ARG n 1 230 ILE n 1 231 SER n 1 232 ILE n 1 233 TYR n 1 234 TRP n 1 235 THR n 1 236 ILE n 1 237 VAL n 1 238 LYS n 1 239 PRO n 1 240 GLY n 1 241 ASP n 1 242 ILE n 1 243 LEU n 1 244 LEU n 1 245 ILE n 1 246 ASN n 1 247 SER n 1 248 THR n 1 249 GLY n 1 250 ASN n 1 251 LEU n 1 252 ILE n 1 253 ALA n 1 254 PRO n 1 255 ARG n 1 256 GLY n 1 257 TYR n 1 258 PHE n 1 259 LYS n 1 260 ILE n 1 261 ARG n 1 262 SER n 1 263 GLY n 1 264 LYS n 1 265 SER n 1 266 SER n 1 267 ILE n 1 268 MET n 1 269 ARG n 1 270 SER n 1 271 ASP n 1 272 ALA n 1 273 PRO n 1 274 ILE n 1 275 GLY n 1 276 LYS n 1 277 CYS n 1 278 ASN n 1 279 SER n 1 280 GLU n 1 281 CYS n 1 282 ILE n 1 283 THR n 1 284 PRO n 1 285 ASN n 1 286 GLY n 1 287 SER n 1 288 ILE n 1 289 PRO n 1 290 ASN n 1 291 ASP n 1 292 LYS n 1 293 PRO n 1 294 PHE n 1 295 GLN n 1 296 ASN n 1 297 VAL n 1 298 ASN n 1 299 ARG n 1 300 ILE n 1 301 THR n 1 302 TYR n 1 303 GLY n 1 304 ALA n 1 305 CYS n 1 306 PRO n 1 307 ARG n 1 308 TYR n 1 309 VAL n 1 310 LYS n 1 311 GLN n 1 312 ASN n 1 313 THR n 1 314 LEU n 1 315 LYS n 1 316 LEU n 1 317 ALA n 1 318 THR n 1 319 GLY n 1 320 MET n 1 321 ARG n 1 322 ASN n 1 323 VAL n 1 324 PRO n 1 325 GLU n 1 326 LYS n 1 327 GLN n 1 328 THR n 1 329 GLN n 1 330 GLY n 1 331 ILE n 1 332 PHE n 1 333 GLY n 1 334 ALA n 1 335 ILE n 1 336 ALA n 1 337 GLY n 1 338 PHE n 1 339 ILE n 1 340 GLU n 1 341 ASN n 1 342 GLY n 1 343 TRP n 1 344 GLU n 1 345 GLY n 1 346 MET n 1 347 VAL n 1 348 ASP n 1 349 GLY n 1 350 TRP n 1 351 TYR n 1 352 GLY n 1 353 PHE n 1 354 ARG n 1 355 HIS n 1 356 GLN n 1 357 ASN n 1 358 SER n 1 359 GLU n 1 360 GLY n 1 361 ILE n 1 362 GLY n 1 363 GLN n 1 364 ALA n 1 365 ALA n 1 366 ASP n 1 367 LEU n 1 368 LYS n 1 369 SER n 1 370 THR n 1 371 GLN n 1 372 ALA n 1 373 ALA n 1 374 ILE n 1 375 ASN n 1 376 GLN n 1 377 ILE n 1 378 ASN n 1 379 GLY n 1 380 LYS n 1 381 LEU n 1 382 ASN n 1 383 ARG n 1 384 LEU n 1 385 ILE n 1 386 GLY n 1 387 LYS n 1 388 THR n 1 389 ASN n 1 390 GLU n 1 391 LYS n 1 392 PHE n 1 393 HIS n 1 394 GLN n 1 395 ILE n 1 396 GLU n 1 397 LYS n 1 398 GLU n 1 399 PHE n 1 400 SER n 1 401 GLU n 1 402 VAL n 1 403 GLU n 1 404 GLY n 1 405 ARG n 1 406 ILE n 1 407 GLN n 1 408 ASP n 1 409 LEU n 1 410 GLU n 1 411 LYS n 1 412 TYR n 1 413 VAL n 1 414 GLU n 1 415 ASP n 1 416 THR n 1 417 LYS n 1 418 ILE n 1 419 ASP n 1 420 LEU n 1 421 TRP n 1 422 SER n 1 423 TYR n 1 424 ASN n 1 425 ALA n 1 426 GLU n 1 427 LEU n 1 428 LEU n 1 429 VAL n 1 430 ALA n 1 431 LEU n 1 432 GLU n 1 433 ASN n 1 434 GLN n 1 435 HIS n 1 436 THR n 1 437 ILE n 1 438 ASP n 1 439 LEU n 1 440 THR n 1 441 ASP n 1 442 SER n 1 443 GLU n 1 444 MET n 1 445 ASN n 1 446 LYS n 1 447 LEU n 1 448 PHE n 1 449 GLU n 1 450 ARG n 1 451 THR n 1 452 LYS n 1 453 LYS n 1 454 GLN n 1 455 LEU n 1 456 ARG n 1 457 GLU n 1 458 ASN n 1 459 ALA n 1 460 GLU n 1 461 ASP n 1 462 MET n 1 463 GLY n 1 464 ASN n 1 465 GLY n 1 466 CYS n 1 467 PHE n 1 468 LYS n 1 469 ILE n 1 470 TYR n 1 471 HIS n 1 472 LYS n 1 473 CYS n 1 474 ASP n 1 475 ASN n 1 476 ALA n 1 477 CYS n 1 478 ILE n 1 479 GLY n 1 480 SER n 1 481 ILE n 1 482 ARG n 1 483 ASN n 1 484 GLY n 1 485 THR n 1 486 TYR n 1 487 ASP n 1 488 HIS n 1 489 ASP n 1 490 VAL n 1 491 TYR n 1 492 ARG n 1 493 ASP n 1 494 GLU n 1 495 ALA n 1 496 LEU n 1 497 ASN n 1 498 ASN n 1 499 ARG n 1 500 PHE n 1 501 GLN n 1 502 ILE n 1 503 LYS 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 ? _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 '(A/FINLAND/486/2004 (H3N2))' _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 'INFLUENZA A VIRUS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 11320 _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 'FALL ARMYWORM' _entity_src_gen.pdbx_host_org_scientific_name 'SPODOPTERA FRUGIPERDA' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 7108 _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 SF9 _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 BACULOVIRUS _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name PACGP67A _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code A0FCI1_9INFA _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession A0FCI1 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 2YP2 _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 503 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession A0FCI1 _struct_ref_seq.db_align_beg 17 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 519 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 503 # _struct_ref_seq_dif.align_id 1 _struct_ref_seq_dif.pdbx_pdb_id_code 2YP2 _struct_ref_seq_dif.mon_id GLN _struct_ref_seq_dif.pdbx_pdb_strand_id A _struct_ref_seq_dif.seq_num 329 _struct_ref_seq_dif.pdbx_pdb_ins_code ? _struct_ref_seq_dif.pdbx_seq_db_name UNP _struct_ref_seq_dif.pdbx_seq_db_accession_code A0FCI1 _struct_ref_seq_dif.db_mon_id ARG _struct_ref_seq_dif.pdbx_seq_db_seq_num 345 _struct_ref_seq_dif.details 'engineered mutation' _struct_ref_seq_dif.pdbx_auth_seq_num 329 _struct_ref_seq_dif.pdbx_ordinal 1 # 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 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 EPE non-polymer . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S' 238.305 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 TAM non-polymer . 'TRIS(HYDROXYETHYL)AMINOMETHANE' ? 'C7 H17 N O3' 163.215 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 2YP2 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.36 _exptl_crystal.density_percent_sol 63.40 _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 ? _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details 'SITTING DROP, DEGLYCOSYLATED PROTEIN, 0.1 M HEPES PH 7.5, 0.2 M KCL, 30% PENTAERYTHRITOL PROPOXYLATE (5/4 PO/OH)' # _diffrn.id 1 _diffrn.ambient_temp 77 _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 2011-12-18 _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 0.976254 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'DIAMOND BEAMLINE I03' _diffrn_source.pdbx_synchrotron_site Diamond _diffrn_source.pdbx_synchrotron_beamline I03 _diffrn_source.pdbx_wavelength 0.976254 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 2YP2 _reflns.observed_criterion_sigma_I 3.3 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 64.87 _reflns.d_resolution_high 1.90 _reflns.number_obs 60416 _reflns.number_all ? _reflns.percent_possible_obs 100.0 _reflns.pdbx_Rmerge_I_obs 0.08 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 13.50 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 6.8 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 2YP2 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 57367 _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 129.06 _refine.ls_d_res_high 1.90 _refine.ls_percent_reflns_obs 99.99 _refine.ls_R_factor_obs 0.17668 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.17572 _refine.ls_R_factor_R_free 0.19501 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 3048 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.960 _refine.correlation_coeff_Fo_to_Fc_free 0.951 _refine.B_iso_mean 30.546 _refine.aniso_B[1][1] 0.69 _refine.aniso_B[2][2] 0.69 _refine.aniso_B[3][3] -1.04 _refine.aniso_B[1][2] 0.35 _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 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.' _refine.pdbx_starting_model ? _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 0.115 _refine.pdbx_overall_ESU_R_Free 0.106 _refine.overall_SU_ML 0.069 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 4.373 _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 3877 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 218 _refine_hist.number_atoms_solvent 428 _refine_hist.number_atoms_total 4523 _refine_hist.d_res_high 1.90 _refine_hist.d_res_low 129.06 # 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 0.009 0.020 ? 4202 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 2865 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.365 1.997 ? 5705 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.817 3.003 ? 6946 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.777 5.000 ? 493 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 35.060 24.824 ? 199 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 11.886 15.000 ? 688 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 13.961 15.000 ? 25 'X-RAY DIFFRACTION' ? r_chiral_restr 0.077 0.200 ? 647 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.005 0.021 ? 4551 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 806 '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 ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.900 _refine_ls_shell.d_res_low 1.949 _refine_ls_shell.number_reflns_R_work 3931 _refine_ls_shell.R_factor_R_work 0.221 _refine_ls_shell.percent_reflns_obs 99.93 _refine_ls_shell.R_factor_R_free 0.256 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 226 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 2YP2 _struct.title 'Haemagglutinin of 2004 Human H3N2 Virus' _struct.pdbx_descriptor HEMAGGLUTININ _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 2YP2 _struct_keywords.pdbx_keywords 'VIRAL PROTEIN' _struct_keywords.text 'VIRAL PROTEIN, RECEPTOR BINDING, MEMBRANE FUSION, INFLUENZA VIRUS EVOLUTION, GLYCOPROTEIN' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 3 ? E N N 2 ? F N N 2 ? G N N 2 ? H N N 2 ? I N N 3 ? J N N 2 ? K N N 2 ? L N N 2 ? M N N 2 ? N N N 4 ? O N N 4 ? P N N 4 ? Q N N 5 ? R N N 6 ? # _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 THR A 65 ? GLY A 72 ? THR A 65 GLY A 72 1 ? 8 HELX_P HELX_P2 2 ASP A 73 ? GLN A 80 ? ASP A 73 GLN A 80 5 ? 8 HELX_P HELX_P3 3 ASP A 104 ? GLY A 116 ? ASP A 104 GLY A 116 1 ? 13 HELX_P HELX_P4 4 THR A 187 ? ALA A 196 ? THR A 187 ALA A 196 1 ? 10 HELX_P HELX_P5 5 ASP A 366 ? ILE A 385 ? ASP A 366 ILE A 385 1 ? 20 HELX_P HELX_P6 6 GLY A 404 ? ARG A 456 ? GLY A 404 ARG A 456 1 ? 53 HELX_P HELX_P7 7 ASP A 474 ? ASN A 483 ? ASP A 474 ASN A 483 1 ? 10 HELX_P HELX_P8 8 ASP A 487 ? PHE A 500 ? ASP A 487 PHE A 500 1 ? 14 # _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 14 SG ? ? ? 1_555 A CYS 466 SG ? ? A CYS 14 A CYS 466 1_555 ? ? ? ? ? ? ? 2.078 ? disulf2 disulf ? ? A CYS 52 SG ? ? ? 1_555 A CYS 277 SG ? ? A CYS 52 A CYS 277 1_555 ? ? ? ? ? ? ? 2.107 ? disulf3 disulf ? ? A CYS 64 SG ? ? ? 1_555 A CYS 76 SG ? ? A CYS 64 A CYS 76 1_555 ? ? ? ? ? ? ? 2.116 ? disulf4 disulf ? ? A CYS 97 SG ? ? ? 1_555 A CYS 139 SG ? ? A CYS 97 A CYS 139 1_555 ? ? ? ? ? ? ? 2.070 ? disulf5 disulf ? ? A CYS 281 SG ? ? ? 1_555 A CYS 305 SG ? ? A CYS 281 A CYS 305 1_555 ? ? ? ? ? ? ? 2.059 ? disulf6 disulf ? ? A CYS 473 SG ? ? ? 1_555 A CYS 477 SG ? ? A CYS 473 A CYS 477 1_555 ? ? ? ? ? ? ? 2.892 ? covale1 covale ? ? A ASN 38 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 38 A NAG 801 1_555 ? ? ? ? ? ? ? 1.444 ? covale2 covale ? ? A ASN 63 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 63 A NAG 804 1_555 ? ? ? ? ? ? ? 1.430 ? covale3 covale ? ? A ASN 133 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 133 A NAG 805 1_555 ? ? ? ? ? ? ? 1.439 ? covale4 covale ? ? A ASN 165 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 165 A NAG 806 1_555 ? ? ? ? ? ? ? 1.429 ? covale5 covale ? ? A ASN 246 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 246 A NAG 809 1_555 ? ? ? ? ? ? ? 1.460 ? covale6 covale ? ? A ASN 285 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 285 A NAG 812 1_555 ? ? ? ? ? ? ? 1.434 ? covale7 covale ? ? A ASN 483 ND2 ? ? ? 1_555 M NAG . C1 ? ? A ASN 483 A NAG 813 1_555 ? ? ? ? ? ? ? 1.459 ? covale8 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 801 A NAG 802 1_555 ? ? ? ? ? ? ? 1.447 ? covale9 covale ? ? D MAN . C1 ? ? ? 1_555 C NAG . O4 ? ? A MAN 803 A NAG 802 1_555 ? ? ? ? ? ? ? 1.449 ? covale10 covale ? ? G NAG . O4 ? ? ? 1_555 H NAG . C1 ? ? A NAG 806 A NAG 807 1_555 ? ? ? ? ? ? ? 1.433 ? covale11 covale ? ? I MAN . C1 ? ? ? 1_555 H NAG . O4 ? ? A MAN 808 A NAG 807 1_555 ? ? ? ? ? ? ? 1.453 ? covale12 covale ? ? J NAG . O4 ? ? ? 1_555 K NAG . C1 ? ? A NAG 809 A NAG 810 1_555 ? ? ? ? ? ? ? 1.446 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id SER _struct_mon_prot_cis.label_seq_id 54 _struct_mon_prot_cis.label_asym_id A _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code ? _struct_mon_prot_cis.auth_comp_id SER _struct_mon_prot_cis.auth_seq_id 54 _struct_mon_prot_cis.auth_asym_id A _struct_mon_prot_cis.pdbx_label_comp_id_2 PRO _struct_mon_prot_cis.pdbx_label_seq_id_2 55 _struct_mon_prot_cis.pdbx_label_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_ins_code_2 ? _struct_mon_prot_cis.pdbx_auth_comp_id_2 PRO _struct_mon_prot_cis.pdbx_auth_seq_id_2 55 _struct_mon_prot_cis.pdbx_auth_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle 1.32 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 5 ? AB ? 2 ? AC ? 2 ? AD ? 3 ? AE ? 2 ? AF ? 3 ? AG ? 5 ? AH ? 5 ? AI ? 2 ? AJ ? 4 ? AK ? 4 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA 1 2 ? anti-parallel AA 2 3 ? anti-parallel AA 3 4 ? anti-parallel AA 4 5 ? anti-parallel AB 1 2 ? anti-parallel AC 1 2 ? anti-parallel AD 1 2 ? parallel AD 2 3 ? parallel AE 1 2 ? parallel AF 1 2 ? parallel AF 2 3 ? parallel AG 1 2 ? parallel AG 2 3 ? anti-parallel AG 3 4 ? anti-parallel AG 4 5 ? anti-parallel AH 1 2 ? parallel AH 2 3 ? anti-parallel AH 3 4 ? anti-parallel AH 4 5 ? anti-parallel AI 1 2 ? anti-parallel AJ 1 2 ? anti-parallel AJ 2 3 ? anti-parallel AJ 3 4 ? anti-parallel AK 1 2 ? anti-parallel AK 2 3 ? anti-parallel AK 3 4 ? 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 GLY A 360 ? ALA A 365 ? GLY A 360 ALA A 365 AA 2 TYR A 351 ? ASN A 357 ? TYR A 351 ASN A 357 AA 3 ALA A 11 ? HIS A 17 ? ALA A 11 HIS A 17 AA 4 CYS A 466 ? ILE A 469 ? CYS A 466 ILE A 469 AA 5 ALA A 459 ? ASP A 461 ? ALA A 459 ASP A 461 AB 1 THR A 24 ? VAL A 26 ? THR A 24 VAL A 26 AB 2 ILE A 34 ? VAL A 36 ? ILE A 34 VAL A 36 AC 1 ALA A 39 ? GLU A 41 ? ALA A 39 GLU A 41 AC 2 LYS A 315 ? ALA A 317 ? LYS A 315 ALA A 317 AD 1 VAL A 43 ? GLN A 44 ? VAL A 43 GLN A 44 AD 2 PHE A 294 ? GLN A 295 ? PHE A 294 GLN A 295 AD 3 ARG A 307 ? TYR A 308 ? ARG A 307 TYR A 308 AE 1 ILE A 51 ? SER A 54 ? ILE A 51 SER A 54 AE 2 ILE A 274 ? ASN A 278 ? ILE A 274 ASN A 278 AF 1 ILE A 58 ? ASP A 60 ? ILE A 58 ASP A 60 AF 2 LEU A 86 ? GLU A 89 ? LEU A 86 GLU A 89 AF 3 SER A 266 ? ARG A 269 ? SER A 266 ARG A 269 AG 1 TYR A 100 ? ASP A 101 ? TYR A 100 ASP A 101 AG 2 ARG A 229 ? VAL A 237 ? ARG A 229 VAL A 237 AG 3 LYS A 176 ? HIS A 184 ? LYS A 176 HIS A 184 AG 4 LEU A 251 ? PRO A 254 ? LEU A 251 PRO A 254 AG 5 LEU A 151 ? TRP A 153 ? LEU A 151 TRP A 153 AH 1 TYR A 100 ? ASP A 101 ? TYR A 100 ASP A 101 AH 2 ARG A 229 ? VAL A 237 ? ARG A 229 VAL A 237 AH 3 LYS A 176 ? HIS A 184 ? LYS A 176 HIS A 184 AH 4 GLY A 256 ? LYS A 259 ? GLY A 256 LYS A 259 AH 5 PHE A 120 ? ASN A 122 ? PHE A 120 ASN A 122 AI 1 SER A 136 ? ARG A 141 ? SER A 136 ARG A 141 AI 2 ASN A 144 ? SER A 146 ? ASN A 144 SER A 146 AJ 1 LEU A 164 ? PRO A 169 ? LEU A 164 PRO A 169 AJ 2 ILE A 242 ? SER A 247 ? ILE A 242 SER A 247 AJ 3 ILE A 202 ? SER A 205 ? ILE A 202 SER A 205 AJ 4 GLN A 210 ? VAL A 213 ? GLN A 210 VAL A 213 AK 1 GLY A 286 ? ILE A 288 ? GLY A 286 ILE A 288 AK 2 CYS A 281 ? THR A 283 ? CYS A 281 THR A 283 AK 3 TYR A 302 ? CYS A 305 ? TYR A 302 CYS A 305 AK 4 ASN A 389 ? LYS A 391 ? ASN A 389 LYS A 391 # 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 ALA A 364 ? N ALA A 364 O PHE A 353 ? O PHE A 353 AA 2 3 N GLN A 356 ? N GLN A 356 O THR A 12 ? O THR A 12 AA 3 4 N LEU A 13 ? N LEU A 13 O PHE A 467 ? O PHE A 467 AA 4 5 N LYS A 468 ? N LYS A 468 O GLU A 460 ? O GLU A 460 AB 1 2 N VAL A 26 ? N VAL A 26 O ILE A 34 ? O ILE A 34 AC 1 2 N THR A 40 ? N THR A 40 O LEU A 316 ? O LEU A 316 AD 1 2 N GLN A 44 ? N GLN A 44 O PHE A 294 ? O PHE A 294 AD 2 3 N GLN A 295 ? N GLN A 295 O ARG A 307 ? O ARG A 307 AE 1 2 N ASP A 53 ? N ASP A 53 O GLY A 275 ? O GLY A 275 AF 1 2 N LEU A 59 ? N LEU A 59 O LEU A 86 ? O LEU A 86 AF 2 3 N PHE A 87 ? N PHE A 87 O SER A 266 ? O SER A 266 AG 1 2 N ASP A 101 ? N ASP A 101 O ILE A 230 ? O ILE A 230 AG 2 3 N VAL A 237 ? N VAL A 237 O LYS A 176 ? O LYS A 176 AG 3 4 N GLY A 181 ? N GLY A 181 O ILE A 252 ? O ILE A 252 AG 4 5 N ALA A 253 ? N ALA A 253 O ASN A 152 ? O ASN A 152 AH 1 2 N ASP A 101 ? N ASP A 101 O ILE A 230 ? O ILE A 230 AH 2 3 N VAL A 237 ? N VAL A 237 O LYS A 176 ? O LYS A 176 AH 3 4 N LEU A 177 ? N LEU A 177 O PHE A 258 ? O PHE A 258 AH 4 5 N TYR A 257 ? N TYR A 257 O ASN A 121 ? O ASN A 121 AI 1 2 N ARG A 141 ? N ARG A 141 O ASN A 144 ? O ASN A 144 AJ 1 2 N MET A 168 ? N MET A 168 O LEU A 243 ? O LEU A 243 AJ 2 3 N ASN A 246 ? N ASN A 246 O THR A 203 ? O THR A 203 AJ 3 4 N VAL A 204 ? N VAL A 204 O GLN A 211 ? O GLN A 211 AK 1 2 N ILE A 288 ? N ILE A 288 O CYS A 281 ? O CYS A 281 AK 2 3 N ILE A 282 ? N ILE A 282 O TYR A 302 ? O TYR A 302 AK 3 4 N CYS A 305 ? N CYS A 305 O ASN A 389 ? O ASN A 389 # 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 ? ? ? ? 11 'BINDING SITE FOR RESIDUE EPE A 1504' AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EPE A 1505' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE TAM A 1507' AC4 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE EPE A 1506' AC5 Software ? ? ? ? 4 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 38 RESIDUES 801 TO 803' AC6 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A 804 BOUND TO ASN A 63' AC7 Software ? ? ? ? 3 'BINDING SITE FOR MONO-SACCHARIDE NAG A 805 BOUND TO ASN A 133' AC8 Software ? ? ? ? 10 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 165 RESIDUES 806 TO 808' AC9 Software ? ? ? ? 10 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 246 RESIDUES 809 TO 810' BC1 Software ? ? ? ? 6 'BINDING SITE FOR MONO-SACCHARIDE NAG A 812 BOUND TO ASN A 285' BC2 Software ? ? ? ? 3 'BINDING SITE FOR MONO-SACCHARIDE NAG A 813 BOUND TO ASN A 483' # 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 11 ASP A 77 ? ASP A 77 . ? 1_555 ? 2 AC1 11 GLN A 80 ? GLN A 80 . ? 1_555 ? 3 AC1 11 ARG A 142 ? ARG A 142 . ? 1_555 ? 4 AC1 11 SER A 146 ? SER A 146 . ? 1_555 ? 5 AC1 11 PHE A 147 ? PHE A 147 . ? 1_555 ? 6 AC1 11 PHE A 148 ? PHE A 148 . ? 1_555 ? 7 AC1 11 SER A 149 ? SER A 149 . ? 1_555 ? 8 AC1 11 LEU A 151 ? LEU A 151 . ? 1_555 ? 9 AC1 11 ARG A 255 ? ARG A 255 . ? 1_555 ? 10 AC1 11 NAG F . ? NAG A 805 . ? 1_555 ? 11 AC1 11 HOH R . ? HOH A 2150 . ? 1_555 ? 12 AC2 4 SER A 95 ? SER A 95 . ? 1_555 ? 13 AC2 4 PRO A 99 ? PRO A 99 . ? 1_555 ? 14 AC2 4 TYR A 100 ? TYR A 100 . ? 1_555 ? 15 AC2 4 ARG A 224 ? ARG A 224 . ? 1_555 ? 16 AC3 3 GLU A 426 ? GLU A 426 . ? 3_655 ? 17 AC3 3 HOH R . ? HOH A 2324 . ? 1_555 ? 18 AC3 3 HOH R . ? HOH A 2426 . ? 1_555 ? 19 AC4 8 PRO A 55 ? PRO A 55 . ? 16_544 ? 20 AC4 8 ASN A 81 ? ASN A 81 . ? 1_555 ? 21 AC4 8 PHE A 120 ? PHE A 120 . ? 1_555 ? 22 AC4 8 ASN A 121 ? ASN A 121 . ? 1_555 ? 23 AC4 8 ASN A 122 ? ASN A 122 . ? 1_555 ? 24 AC4 8 GLU A 280 ? GLU A 280 . ? 16_544 ? 25 AC4 8 GLU A 390 ? GLU A 390 . ? 16_544 ? 26 AC4 8 HOH R . ? HOH A 2093 . ? 1_555 ? 27 AC5 4 ASN A 38 ? ASN A 38 . ? 1_555 ? 28 AC5 4 THR A 318 ? THR A 318 . ? 1_555 ? 29 AC5 4 LEU A 381 ? LEU A 381 . ? 1_555 ? 30 AC5 4 NAG F . ? NAG A 805 . ? 16_544 ? 31 AC6 2 ASN A 63 ? ASN A 63 . ? 1_555 ? 32 AC6 2 TYR A 94 ? TYR A 94 . ? 1_555 ? 33 AC7 3 ASN A 133 ? ASN A 133 . ? 1_555 ? 34 AC7 3 MAN D . ? MAN A 803 . ? 16_544 ? 35 AC7 3 EPE N . ? EPE A 1504 . ? 1_555 ? 36 AC8 10 ASN A 165 ? ASN A 165 . ? 1_555 ? 37 AC8 10 SER A 219 ? SER A 219 . ? 3_655 ? 38 AC8 10 PRO A 221 ? PRO A 221 . ? 3_655 ? 39 AC8 10 ARG A 222 ? ARG A 222 . ? 3_655 ? 40 AC8 10 ASP A 225 ? ASP A 225 . ? 3_655 ? 41 AC8 10 ILE A 242 ? ILE A 242 . ? 1_555 ? 42 AC8 10 NAG J . ? NAG A 809 . ? 1_555 ? 43 AC8 10 HOH R . ? HOH A 2176 . ? 1_555 ? 44 AC8 10 HOH R . ? HOH A 2218 . ? 3_655 ? 45 AC8 10 HOH R . ? HOH A 2422 . ? 1_555 ? 46 AC9 10 ALA A 163 ? ALA A 163 . ? 1_555 ? 47 AC9 10 LEU A 164 ? LEU A 164 . ? 1_555 ? 48 AC9 10 ASN A 165 ? ASN A 165 . ? 1_555 ? 49 AC9 10 ARG A 201 ? ARG A 201 . ? 1_555 ? 50 AC9 10 ASN A 246 ? ASN A 246 . ? 1_555 ? 51 AC9 10 SER A 247 ? SER A 247 . ? 1_555 ? 52 AC9 10 THR A 248 ? THR A 248 . ? 1_555 ? 53 AC9 10 NAG G . ? NAG A 806 . ? 1_555 ? 54 AC9 10 HOH R . ? HOH A 2202 . ? 1_555 ? 55 AC9 10 HOH R . ? HOH A 2424 . ? 1_555 ? 56 BC1 6 SER A 45 ? SER A 45 . ? 1_555 ? 57 BC1 6 ASN A 285 ? ASN A 285 . ? 1_555 ? 58 BC1 6 VAL A 297 ? VAL A 297 . ? 1_555 ? 59 BC1 6 ASN A 298 ? ASN A 298 . ? 1_555 ? 60 BC1 6 HOH R . ? HOH A 2256 . ? 1_555 ? 61 BC1 6 HOH R . ? HOH A 2266 . ? 1_555 ? 62 BC2 3 ALA A 476 ? ALA A 476 . ? 1_555 ? 63 BC2 3 ASN A 483 ? ASN A 483 . ? 1_555 ? 64 BC2 3 THR A 485 ? THR A 485 . ? 1_555 ? # _database_PDB_matrix.entry_id 2YP2 _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 2YP2 _atom_sites.fract_transf_matrix[1][1] 0.009909 _atom_sites.fract_transf_matrix[1][2] 0.005721 _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] 0.011442 _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] 0.002583 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ASN A 1 8 ? 33.498 -42.126 11.051 1.00 68.52 ? 8 ASN A N 1 ATOM 2 C CA . ASN A 1 8 ? 33.610 -41.880 12.517 1.00 65.94 ? 8 ASN A CA 1 ATOM 3 C C . ASN A 1 8 ? 34.584 -40.736 12.792 1.00 61.59 ? 8 ASN A C 1 ATOM 4 O O . ASN A 1 8 ? 35.802 -40.935 12.876 1.00 61.15 ? 8 ASN A O 1 ATOM 5 C CB . ASN A 1 8 ? 34.039 -43.155 13.251 1.00 69.15 ? 8 ASN A CB 1 ATOM 6 C CG . ASN A 1 8 ? 35.338 -43.742 12.715 1.00 71.73 ? 8 ASN A CG 1 ATOM 7 O OD1 . ASN A 1 8 ? 35.780 -43.417 11.605 1.00 72.15 ? 8 ASN A OD1 1 ATOM 8 N ND2 . ASN A 1 8 ? 35.961 -44.612 13.508 1.00 73.08 ? 8 ASN A ND2 1 ATOM 9 N N . SER A 1 9 ? 34.045 -39.527 12.904 1.00 57.23 ? 9 SER A N 1 ATOM 10 C CA . SER A 1 9 ? 34.871 -38.323 13.064 1.00 51.41 ? 9 SER A CA 1 ATOM 11 C C . SER A 1 9 ? 35.570 -37.898 11.762 1.00 44.65 ? 9 SER A C 1 ATOM 12 O O . SER A 1 9 ? 36.189 -36.851 11.733 1.00 41.95 ? 9 SER A O 1 ATOM 13 C CB . SER A 1 9 ? 35.902 -38.514 14.196 1.00 52.55 ? 9 SER A CB 1 ATOM 14 O OG . SER A 1 9 ? 37.115 -39.100 13.741 1.00 52.29 ? 9 SER A OG 1 ATOM 15 N N . THR A 1 10 ? 35.484 -38.698 10.696 1.00 41.50 ? 10 THR A N 1 ATOM 16 C CA . THR A 1 10 ? 36.036 -38.303 9.390 1.00 38.65 ? 10 THR A CA 1 ATOM 17 C C . THR A 1 10 ? 35.115 -38.684 8.235 1.00 36.14 ? 10 THR A C 1 ATOM 18 O O . THR A 1 10 ? 34.124 -39.369 8.412 1.00 36.39 ? 10 THR A O 1 ATOM 19 C CB . THR A 1 10 ? 37.411 -38.941 9.131 1.00 39.94 ? 10 THR A CB 1 ATOM 20 O OG1 . THR A 1 10 ? 37.253 -40.353 9.034 1.00 42.38 ? 10 THR A OG1 1 ATOM 21 C CG2 . THR A 1 10 ? 38.393 -38.614 10.254 1.00 41.20 ? 10 THR A CG2 1 ATOM 22 N N . ALA A 1 11 ? 35.454 -38.215 7.045 1.00 31.36 ? 11 ALA A N 1 ATOM 23 C CA . ALA A 1 11 ? 34.691 -38.520 5.861 1.00 30.28 ? 11 ALA A CA 1 ATOM 24 C C . ALA A 1 11 ? 35.681 -38.640 4.721 1.00 28.79 ? 11 ALA A C 1 ATOM 25 O O . ALA A 1 11 ? 36.823 -38.218 4.859 1.00 27.35 ? 11 ALA A O 1 ATOM 26 C CB . ALA A 1 11 ? 33.702 -37.402 5.583 1.00 30.09 ? 11 ALA A CB 1 ATOM 27 N N . THR A 1 12 ? 35.235 -39.218 3.615 1.00 27.99 ? 12 THR A N 1 ATOM 28 C CA . THR A 1 12 ? 36.038 -39.336 2.394 1.00 27.84 ? 12 THR A CA 1 ATOM 29 C C . THR A 1 12 ? 35.310 -38.665 1.257 1.00 27.05 ? 12 THR A C 1 ATOM 30 O O . THR A 1 12 ? 34.100 -38.827 1.122 1.00 27.71 ? 12 THR A O 1 ATOM 31 C CB . THR A 1 12 ? 36.275 -40.822 2.052 1.00 28.65 ? 12 THR A CB 1 ATOM 32 O OG1 . THR A 1 12 ? 36.926 -41.431 3.159 1.00 29.83 ? 12 THR A OG1 1 ATOM 33 C CG2 . THR A 1 12 ? 37.158 -41.005 0.807 1.00 29.55 ? 12 THR A CG2 1 ATOM 34 N N . LEU A 1 13 ? 36.040 -37.892 0.459 1.00 26.42 ? 13 LEU A N 1 ATOM 35 C CA . LEU A 1 13 ? 35.499 -37.276 -0.731 1.00 26.41 ? 13 LEU A CA 1 ATOM 36 C C . LEU A 1 13 ? 36.399 -37.586 -1.928 1.00 27.23 ? 13 LEU A C 1 ATOM 37 O O . LEU A 1 13 ? 37.567 -37.191 -1.955 1.00 27.18 ? 13 LEU A O 1 ATOM 38 C CB . LEU A 1 13 ? 35.336 -35.773 -0.527 1.00 25.48 ? 13 LEU A CB 1 ATOM 39 C CG . LEU A 1 13 ? 34.768 -34.990 -1.715 1.00 26.09 ? 13 LEU A CG 1 ATOM 40 C CD1 . LEU A 1 13 ? 33.318 -35.400 -1.985 1.00 25.66 ? 13 LEU A CD1 1 ATOM 41 C CD2 . LEU A 1 13 ? 34.911 -33.487 -1.490 1.00 26.34 ? 13 LEU A CD2 1 ATOM 42 N N . CYS A 1 14 ? 35.847 -38.301 -2.908 1.00 28.80 ? 14 CYS A N 1 ATOM 43 C CA . CYS A 1 14 ? 36.590 -38.732 -4.093 1.00 28.84 ? 14 CYS A CA 1 ATOM 44 C C . CYS A 1 14 ? 36.141 -37.946 -5.303 1.00 27.95 ? 14 CYS A C 1 ATOM 45 O O . CYS A 1 14 ? 34.959 -37.626 -5.440 1.00 26.64 ? 14 CYS A O 1 ATOM 46 C CB . CYS A 1 14 ? 36.363 -40.235 -4.347 1.00 31.47 ? 14 CYS A CB 1 ATOM 47 S SG . CYS A 1 14 ? 37.003 -41.322 -3.047 1.00 35.72 ? 14 CYS A SG 1 ATOM 48 N N . LEU A 1 15 ? 37.096 -37.580 -6.167 1.00 26.70 ? 15 LEU A N 1 ATOM 49 C CA . LEU A 1 15 ? 36.781 -36.953 -7.440 1.00 26.46 ? 15 LEU A CA 1 ATOM 50 C C . LEU A 1 15 ? 36.965 -37.993 -8.530 1.00 26.59 ? 15 LEU A C 1 ATOM 51 O O . LEU A 1 15 ? 37.904 -38.790 -8.464 1.00 28.04 ? 15 LEU A O 1 ATOM 52 C CB . LEU A 1 15 ? 37.685 -35.759 -7.680 1.00 27.38 ? 15 LEU A CB 1 ATOM 53 C CG . LEU A 1 15 ? 37.198 -34.527 -6.903 1.00 28.75 ? 15 LEU A CG 1 ATOM 54 C CD1 . LEU A 1 15 ? 37.595 -34.631 -5.436 1.00 30.15 ? 15 LEU A CD1 1 ATOM 55 C CD2 . LEU A 1 15 ? 37.726 -33.262 -7.503 1.00 33.53 ? 15 LEU A CD2 1 ATOM 56 N N . GLY A 1 16 ? 36.079 -38.002 -9.518 1.00 25.21 ? 16 GLY A N 1 ATOM 57 C CA . GLY A 1 16 ? 36.166 -38.987 -10.586 1.00 24.79 ? 16 GLY A CA 1 ATOM 58 C C . GLY A 1 16 ? 35.516 -38.565 -11.881 1.00 24.72 ? 16 GLY A C 1 ATOM 59 O O . GLY A 1 16 ? 34.971 -37.472 -12.001 1.00 23.02 ? 16 GLY A O 1 ATOM 60 N N . HIS A 1 17 ? 35.578 -39.461 -12.853 1.00 25.00 ? 17 HIS A N 1 ATOM 61 C CA . HIS A 1 17 ? 35.010 -39.223 -14.164 1.00 24.98 ? 17 HIS A CA 1 ATOM 62 C C . HIS A 1 17 ? 34.382 -40.486 -14.655 1.00 25.74 ? 17 HIS A C 1 ATOM 63 O O . HIS A 1 17 ? 34.724 -41.567 -14.183 1.00 27.74 ? 17 HIS A O 1 ATOM 64 C CB . HIS A 1 17 ? 36.092 -38.744 -15.131 1.00 24.49 ? 17 HIS A CB 1 ATOM 65 C CG . HIS A 1 17 ? 37.186 -39.746 -15.361 1.00 25.45 ? 17 HIS A CG 1 ATOM 66 N ND1 . HIS A 1 17 ? 36.992 -40.887 -16.045 1.00 26.03 ? 17 HIS A ND1 1 ATOM 67 C CD2 . HIS A 1 17 ? 38.508 -39.757 -14.953 1.00 26.73 ? 17 HIS A CD2 1 ATOM 68 C CE1 . HIS A 1 17 ? 38.133 -41.608 -16.040 1.00 27.07 ? 17 HIS A CE1 1 ATOM 69 N NE2 . HIS A 1 17 ? 39.057 -40.919 -15.380 1.00 27.83 ? 17 HIS A NE2 1 ATOM 70 N N . HIS A 1 18 ? 33.459 -40.370 -15.602 1.00 25.66 ? 18 HIS A N 1 ATOM 71 C CA . HIS A 1 18 ? 32.749 -41.514 -16.126 1.00 26.22 ? 18 HIS A CA 1 ATOM 72 C C . HIS A 1 18 ? 33.602 -42.419 -16.979 1.00 27.25 ? 18 HIS A C 1 ATOM 73 O O . HIS A 1 18 ? 34.727 -42.092 -17.353 1.00 26.71 ? 18 HIS A O 1 ATOM 74 C CB . HIS A 1 18 ? 31.478 -41.097 -16.866 1.00 26.56 ? 18 HIS A CB 1 ATOM 75 C CG . HIS A 1 18 ? 31.726 -40.545 -18.251 1.00 27.12 ? 18 HIS A CG 1 ATOM 76 N ND1 . HIS A 1 18 ? 30.787 -40.548 -19.210 1.00 28.02 ? 18 HIS A ND1 1 ATOM 77 C CD2 . HIS A 1 18 ? 32.868 -39.978 -18.816 1.00 26.84 ? 18 HIS A CD2 1 ATOM 78 C CE1 . HIS A 1 18 ? 31.297 -39.989 -20.336 1.00 28.24 ? 18 HIS A CE1 1 ATOM 79 N NE2 . HIS A 1 18 ? 32.567 -39.640 -20.091 1.00 26.27 ? 18 HIS A NE2 1 ATOM 80 N N . ALA A 1 19 ? 33.053 -43.589 -17.250 1.00 27.51 ? 19 ALA A N 1 ATOM 81 C CA . ALA A 1 19 ? 33.642 -44.580 -18.123 1.00 29.02 ? 19 ALA A CA 1 ATOM 82 C C . ALA A 1 19 ? 32.460 -45.321 -18.742 1.00 31.03 ? 19 ALA A C 1 ATOM 83 O O . ALA A 1 19 ? 31.365 -45.293 -18.188 1.00 32.49 ? 19 ALA A O 1 ATOM 84 C CB . ALA A 1 19 ? 34.544 -45.529 -17.345 1.00 29.46 ? 19 ALA A CB 1 ATOM 85 N N . VAL A 1 20 ? 32.670 -45.974 -19.874 1.00 32.01 ? 20 VAL A N 1 ATOM 86 C CA . VAL A 1 20 ? 31.572 -46.599 -20.597 1.00 34.62 ? 20 VAL A CA 1 ATOM 87 C C . VAL A 1 20 ? 31.986 -48.015 -20.916 1.00 37.41 ? 20 VAL A C 1 ATOM 88 O O . VAL A 1 20 ? 33.185 -48.313 -20.957 1.00 37.15 ? 20 VAL A O 1 ATOM 89 C CB . VAL A 1 20 ? 31.180 -45.830 -21.875 1.00 35.08 ? 20 VAL A CB 1 ATOM 90 C CG1 . VAL A 1 20 ? 30.756 -44.410 -21.527 1.00 35.23 ? 20 VAL A CG1 1 ATOM 91 C CG2 . VAL A 1 20 ? 32.311 -45.834 -22.898 1.00 33.56 ? 20 VAL A CG2 1 ATOM 92 N N . PRO A 1 21 ? 31.000 -48.912 -21.078 1.00 41.62 ? 21 PRO A N 1 ATOM 93 C CA . PRO A 1 21 ? 31.367 -50.300 -21.341 1.00 44.43 ? 21 PRO A CA 1 ATOM 94 C C . PRO A 1 21 ? 31.843 -50.540 -22.777 1.00 45.65 ? 21 PRO A C 1 ATOM 95 O O . PRO A 1 21 ? 32.587 -51.485 -23.000 1.00 50.82 ? 21 PRO A O 1 ATOM 96 C CB . PRO A 1 21 ? 30.075 -51.072 -21.032 1.00 43.96 ? 21 PRO A CB 1 ATOM 97 C CG . PRO A 1 21 ? 28.976 -50.093 -21.322 1.00 44.09 ? 21 PRO A CG 1 ATOM 98 C CD . PRO A 1 21 ? 29.539 -48.730 -20.974 1.00 42.57 ? 21 PRO A CD 1 ATOM 99 N N . ASN A 1 22 ? 31.441 -49.686 -23.721 1.00 45.14 ? 22 ASN A N 1 ATOM 100 C CA . ASN A 1 22 ? 31.756 -49.867 -25.148 1.00 45.42 ? 22 ASN A CA 1 ATOM 101 C C . ASN A 1 22 ? 32.581 -48.704 -25.753 1.00 41.23 ? 22 ASN A C 1 ATOM 102 O O . ASN A 1 22 ? 32.077 -47.959 -26.594 1.00 39.05 ? 22 ASN A O 1 ATOM 103 C CB . ASN A 1 22 ? 30.455 -50.002 -25.947 1.00 47.20 ? 22 ASN A CB 1 ATOM 104 C CG . ASN A 1 22 ? 29.580 -48.758 -25.842 1.00 51.37 ? 22 ASN A CG 1 ATOM 105 O OD1 . ASN A 1 22 ? 29.629 -48.025 -24.829 1.00 54.40 ? 22 ASN A OD1 1 ATOM 106 N ND2 . ASN A 1 22 ? 28.795 -48.492 -26.891 1.00 53.28 ? 22 ASN A ND2 1 ATOM 107 N N . GLY A 1 23 ? 33.841 -48.577 -25.353 1.00 40.16 ? 23 GLY A N 1 ATOM 108 C CA . GLY A 1 23 ? 34.684 -47.446 -25.804 1.00 39.57 ? 23 GLY A CA 1 ATOM 109 C C . GLY A 1 23 ? 35.205 -47.677 -27.214 1.00 38.94 ? 23 GLY A C 1 ATOM 110 O O . GLY A 1 23 ? 35.036 -48.771 -27.756 1.00 38.52 ? 23 GLY A O 1 ATOM 111 N N . THR A 1 24 ? 35.847 -46.664 -27.800 1.00 35.25 ? 24 THR A N 1 ATOM 112 C CA . THR A 1 24 ? 36.361 -46.743 -29.177 1.00 34.63 ? 24 THR A CA 1 ATOM 113 C C . THR A 1 24 ? 37.819 -46.325 -29.252 1.00 31.41 ? 24 THR A C 1 ATOM 114 O O . THR A 1 24 ? 38.233 -45.392 -28.570 1.00 29.40 ? 24 THR A O 1 ATOM 115 C CB . THR A 1 24 ? 35.608 -45.793 -30.125 1.00 37.92 ? 24 THR A CB 1 ATOM 116 O OG1 . THR A 1 24 ? 34.216 -45.774 -29.813 1.00 43.76 ? 24 THR A OG1 1 ATOM 117 C CG2 . THR A 1 24 ? 35.771 -46.229 -31.561 1.00 39.04 ? 24 THR A CG2 1 ATOM 118 N N . ILE A 1 25 ? 38.568 -46.962 -30.137 1.00 27.99 ? 25 ILE A N 1 ATOM 119 C CA . ILE A 1 25 ? 39.995 -46.717 -30.240 1.00 28.83 ? 25 ILE A CA 1 ATOM 120 C C . ILE A 1 25 ? 40.245 -45.565 -31.204 1.00 25.62 ? 25 ILE A C 1 ATOM 121 O O . ILE A 1 25 ? 39.673 -45.521 -32.287 1.00 24.40 ? 25 ILE A O 1 ATOM 122 C CB . ILE A 1 25 ? 40.748 -47.981 -30.701 1.00 30.54 ? 25 ILE A CB 1 ATOM 123 C CG1 . ILE A 1 25 ? 40.559 -49.083 -29.660 1.00 32.97 ? 25 ILE A CG1 1 ATOM 124 C CG2 . ILE A 1 25 ? 42.237 -47.689 -30.888 1.00 31.12 ? 25 ILE A CG2 1 ATOM 125 C CD1 . ILE A 1 25 ? 41.310 -48.852 -28.382 1.00 34.56 ? 25 ILE A CD1 1 ATOM 126 N N . VAL A 1 26 ? 41.072 -44.615 -30.785 1.00 24.42 ? 26 VAL A N 1 ATOM 127 C CA . VAL A 1 26 ? 41.514 -43.534 -31.664 1.00 22.98 ? 26 VAL A CA 1 ATOM 128 C C . VAL A 1 26 ? 43.022 -43.403 -31.596 1.00 23.53 ? 26 VAL A C 1 ATOM 129 O O . VAL A 1 26 ? 43.672 -44.022 -30.737 1.00 23.64 ? 26 VAL A O 1 ATOM 130 C CB . VAL A 1 26 ? 40.885 -42.172 -31.283 1.00 21.70 ? 26 VAL A CB 1 ATOM 131 C CG1 . VAL A 1 26 ? 39.369 -42.240 -31.403 1.00 21.33 ? 26 VAL A CG1 1 ATOM 132 C CG2 . VAL A 1 26 ? 41.342 -41.736 -29.889 1.00 20.69 ? 26 VAL A CG2 1 ATOM 133 N N . LYS A 1 27 ? 43.566 -42.583 -32.490 1.00 23.85 ? 27 LYS A N 1 ATOM 134 C CA . LYS A 1 27 ? 44.993 -42.257 -32.504 1.00 24.89 ? 27 LYS A CA 1 ATOM 135 C C . LYS A 1 27 ? 45.273 -40.833 -32.016 1.00 24.42 ? 27 LYS A C 1 ATOM 136 O O . LYS A 1 27 ? 44.619 -39.893 -32.415 1.00 22.30 ? 27 LYS A O 1 ATOM 137 C CB . LYS A 1 27 ? 45.523 -42.390 -33.932 1.00 27.17 ? 27 LYS A CB 1 ATOM 138 C CG . LYS A 1 27 ? 46.955 -41.928 -34.157 1.00 30.46 ? 27 LYS A CG 1 ATOM 139 C CD . LYS A 1 27 ? 47.343 -42.150 -35.617 1.00 33.11 ? 27 LYS A CD 1 ATOM 140 C CE . LYS A 1 27 ? 48.666 -41.473 -35.969 1.00 35.71 ? 27 LYS A CE 1 ATOM 141 N NZ . LYS A 1 27 ? 48.996 -41.732 -37.401 1.00 36.85 ? 27 LYS A NZ 1 ATOM 142 N N . THR A 1 28 ? 46.276 -40.663 -31.179 1.00 24.66 ? 28 THR A N 1 ATOM 143 C CA . THR A 1 28 ? 46.693 -39.318 -30.778 1.00 25.48 ? 28 THR A CA 1 ATOM 144 C C . THR A 1 28 ? 48.171 -39.144 -31.148 1.00 27.70 ? 28 THR A C 1 ATOM 145 O O . THR A 1 28 ? 48.782 -40.026 -31.729 1.00 28.83 ? 28 THR A O 1 ATOM 146 C CB . THR A 1 28 ? 46.521 -39.082 -29.267 1.00 25.54 ? 28 THR A CB 1 ATOM 147 O OG1 . THR A 1 28 ? 47.376 -39.974 -28.543 1.00 26.14 ? 28 THR A OG1 1 ATOM 148 C CG2 . THR A 1 28 ? 45.084 -39.291 -28.797 1.00 26.78 ? 28 THR A CG2 1 ATOM 149 N N . ILE A 1 29 ? 48.765 -38.014 -30.784 1.00 28.25 ? 29 ILE A N 1 ATOM 150 C CA . ILE A 1 29 ? 50.211 -37.859 -30.926 1.00 29.73 ? 29 ILE A CA 1 ATOM 151 C C . ILE A 1 29 ? 50.955 -38.760 -29.937 1.00 30.64 ? 29 ILE A C 1 ATOM 152 O O . ILE A 1 29 ? 51.982 -39.296 -30.268 1.00 32.58 ? 29 ILE A O 1 ATOM 153 C CB . ILE A 1 29 ? 50.648 -36.399 -30.697 1.00 30.48 ? 29 ILE A CB 1 ATOM 154 C CG1 . ILE A 1 29 ? 49.947 -35.495 -31.703 1.00 31.97 ? 29 ILE A CG1 1 ATOM 155 C CG2 . ILE A 1 29 ? 52.164 -36.289 -30.832 1.00 31.49 ? 29 ILE A CG2 1 ATOM 156 C CD1 . ILE A 1 29 ? 50.356 -35.772 -33.141 1.00 34.64 ? 29 ILE A CD1 1 ATOM 157 N N . THR A 1 30 ? 50.425 -38.924 -28.730 1.00 30.74 ? 30 THR A N 1 ATOM 158 C CA . THR A 1 30 ? 51.070 -39.741 -27.694 1.00 32.37 ? 30 THR A CA 1 ATOM 159 C C . THR A 1 30 ? 50.877 -41.250 -27.924 1.00 34.62 ? 30 THR A C 1 ATOM 160 O O . THR A 1 30 ? 51.777 -42.030 -27.673 1.00 32.55 ? 30 THR A O 1 ATOM 161 C CB . THR A 1 30 ? 50.529 -39.381 -26.294 1.00 32.39 ? 30 THR A CB 1 ATOM 162 O OG1 . THR A 1 30 ? 50.774 -37.993 -26.038 1.00 32.51 ? 30 THR A OG1 1 ATOM 163 C CG2 . THR A 1 30 ? 51.189 -40.231 -25.185 1.00 32.85 ? 30 THR A CG2 1 ATOM 164 N N . ASN A 1 31 ? 49.698 -41.652 -28.393 1.00 33.29 ? 31 ASN A N 1 ATOM 165 C CA . ASN A 1 31 ? 49.362 -43.081 -28.523 1.00 35.06 ? 31 ASN A CA 1 ATOM 166 C C . ASN A 1 31 ? 48.846 -43.417 -29.926 1.00 33.63 ? 31 ASN A C 1 ATOM 167 O O . ASN A 1 31 ? 47.893 -42.795 -30.403 1.00 31.41 ? 31 ASN A O 1 ATOM 168 C CB . ASN A 1 31 ? 48.267 -43.435 -27.507 1.00 36.66 ? 31 ASN A CB 1 ATOM 169 C CG . ASN A 1 31 ? 48.747 -43.393 -26.072 1.00 39.04 ? 31 ASN A CG 1 ATOM 170 O OD1 . ASN A 1 31 ? 49.499 -44.263 -25.635 1.00 44.37 ? 31 ASN A OD1 1 ATOM 171 N ND2 . ASN A 1 31 ? 48.292 -42.396 -25.319 1.00 38.01 ? 31 ASN A ND2 1 ATOM 172 N N . ASP A 1 32 ? 49.435 -44.414 -30.570 1.00 33.72 ? 32 ASP A N 1 ATOM 173 C CA . ASP A 1 32 ? 48.841 -44.988 -31.779 1.00 35.21 ? 32 ASP A CA 1 ATOM 174 C C . ASP A 1 32 ? 47.405 -45.489 -31.550 1.00 33.08 ? 32 ASP A C 1 ATOM 175 O O . ASP A 1 32 ? 46.573 -45.369 -32.426 1.00 31.12 ? 32 ASP A O 1 ATOM 176 C CB . ASP A 1 32 ? 49.685 -46.153 -32.292 1.00 41.54 ? 32 ASP A CB 1 ATOM 177 C CG . ASP A 1 32 ? 50.991 -45.699 -32.918 1.00 47.96 ? 32 ASP A CG 1 ATOM 178 O OD1 . ASP A 1 32 ? 51.038 -44.575 -33.478 1.00 54.44 ? 32 ASP A OD1 1 ATOM 179 O OD2 . ASP A 1 32 ? 51.968 -46.476 -32.850 1.00 55.90 ? 32 ASP A OD2 1 ATOM 180 N N . GLN A 1 33 ? 47.133 -46.033 -30.371 1.00 30.96 ? 33 GLN A N 1 ATOM 181 C CA . GLN A 1 33 ? 45.800 -46.541 -30.018 1.00 32.33 ? 33 GLN A CA 1 ATOM 182 C C . GLN A 1 33 ? 45.483 -46.166 -28.580 1.00 30.84 ? 33 GLN A C 1 ATOM 183 O O . GLN A 1 33 ? 46.245 -46.497 -27.660 1.00 32.14 ? 33 GLN A O 1 ATOM 184 C CB . GLN A 1 33 ? 45.748 -48.072 -30.177 1.00 35.69 ? 33 GLN A CB 1 ATOM 185 C CG . GLN A 1 33 ? 45.886 -48.562 -31.615 1.00 38.83 ? 33 GLN A CG 1 ATOM 186 C CD . GLN A 1 33 ? 45.388 -49.989 -31.835 1.00 43.72 ? 33 GLN A CD 1 ATOM 187 O OE1 . GLN A 1 33 ? 45.368 -50.812 -30.919 1.00 49.61 ? 33 GLN A OE1 1 ATOM 188 N NE2 . GLN A 1 33 ? 44.979 -50.282 -33.056 1.00 47.33 ? 33 GLN A NE2 1 ATOM 189 N N . ILE A 1 34 ? 44.400 -45.431 -28.368 1.00 27.36 ? 34 ILE A N 1 ATOM 190 C CA . ILE A 1 34 ? 43.949 -45.140 -27.016 1.00 26.35 ? 34 ILE A CA 1 ATOM 191 C C . ILE A 1 34 ? 42.451 -45.215 -27.052 1.00 25.28 ? 34 ILE A C 1 ATOM 192 O O . ILE A 1 34 ? 41.827 -44.706 -27.989 1.00 23.77 ? 34 ILE A O 1 ATOM 193 C CB . ILE A 1 34 ? 44.455 -43.764 -26.474 1.00 27.16 ? 34 ILE A CB 1 ATOM 194 C CG1 . ILE A 1 34 ? 43.921 -43.502 -25.061 1.00 28.20 ? 34 ILE A CG1 1 ATOM 195 C CG2 . ILE A 1 34 ? 44.062 -42.620 -27.391 1.00 26.37 ? 34 ILE A CG2 1 ATOM 196 C CD1 . ILE A 1 34 ? 44.581 -42.332 -24.361 1.00 28.84 ? 34 ILE A CD1 1 ATOM 197 N N . GLU A 1 35 ? 41.872 -45.888 -26.056 1.00 25.08 ? 35 GLU A N 1 ATOM 198 C CA . GLU A 1 35 ? 40.439 -45.996 -25.982 1.00 25.87 ? 35 GLU A CA 1 ATOM 199 C C . GLU A 1 35 ? 39.835 -44.748 -25.318 1.00 24.17 ? 35 GLU A C 1 ATOM 200 O O . GLU A 1 35 ? 40.239 -44.342 -24.231 1.00 24.52 ? 35 GLU A O 1 ATOM 201 C CB . GLU A 1 35 ? 40.022 -47.273 -25.241 1.00 28.59 ? 35 GLU A CB 1 ATOM 202 C CG . GLU A 1 35 ? 38.564 -47.622 -25.422 1.00 31.96 ? 35 GLU A CG 1 ATOM 203 C CD . GLU A 1 35 ? 38.185 -48.881 -24.655 1.00 36.99 ? 35 GLU A CD 1 ATOM 204 O OE1 . GLU A 1 35 ? 38.667 -49.977 -25.025 1.00 41.98 ? 35 GLU A OE1 1 ATOM 205 O OE2 . GLU A 1 35 ? 37.413 -48.763 -23.682 1.00 37.88 ? 35 GLU A OE2 1 ATOM 206 N N . VAL A 1 36 ? 38.833 -44.204 -25.975 1.00 23.30 ? 36 VAL A N 1 ATOM 207 C CA . VAL A 1 36 ? 38.040 -43.083 -25.502 1.00 22.95 ? 36 VAL A CA 1 ATOM 208 C C . VAL A 1 36 ? 36.572 -43.491 -25.395 1.00 23.75 ? 36 VAL A C 1 ATOM 209 O O . VAL A 1 36 ? 36.179 -44.547 -25.895 1.00 23.84 ? 36 VAL A O 1 ATOM 210 C CB . VAL A 1 36 ? 38.226 -41.841 -26.423 1.00 22.32 ? 36 VAL A CB 1 ATOM 211 C CG1 . VAL A 1 36 ? 39.657 -41.336 -26.315 1.00 20.94 ? 36 VAL A CG1 1 ATOM 212 C CG2 . VAL A 1 36 ? 37.840 -42.113 -27.905 1.00 21.04 ? 36 VAL A CG2 1 ATOM 213 N N . THR A 1 37 ? 35.766 -42.671 -24.727 1.00 23.52 ? 37 THR A N 1 ATOM 214 C CA . THR A 1 37 ? 34.387 -43.030 -24.467 1.00 24.54 ? 37 THR A CA 1 ATOM 215 C C . THR A 1 37 ? 33.540 -42.953 -25.725 1.00 25.32 ? 37 THR A C 1 ATOM 216 O O . THR A 1 37 ? 32.552 -43.642 -25.840 1.00 24.70 ? 37 THR A O 1 ATOM 217 C CB . THR A 1 37 ? 33.770 -42.148 -23.379 1.00 24.71 ? 37 THR A CB 1 ATOM 218 O OG1 . THR A 1 37 ? 33.730 -40.797 -23.824 1.00 25.68 ? 37 THR A OG1 1 ATOM 219 C CG2 . THR A 1 37 ? 34.588 -42.230 -22.066 1.00 23.28 ? 37 THR A CG2 1 ATOM 220 N N . ASN A 1 38 ? 33.948 -42.136 -26.692 1.00 24.90 ? 38 ASN A N 1 ATOM 221 C CA . ASN A 1 38 ? 33.161 -41.990 -27.898 1.00 26.67 ? 38 ASN A CA 1 ATOM 222 C C . ASN A 1 38 ? 34.028 -41.361 -28.971 1.00 24.80 ? 38 ASN A C 1 ATOM 223 O O . ASN A 1 38 ? 34.989 -40.650 -28.650 1.00 22.47 ? 38 ASN A O 1 ATOM 224 C CB . ASN A 1 38 ? 31.954 -41.106 -27.596 1.00 29.04 ? 38 ASN A CB 1 ATOM 225 C CG . ASN A 1 38 ? 30.918 -41.124 -28.690 1.00 33.63 ? 38 ASN A CG 1 ATOM 226 O OD1 . ASN A 1 38 ? 30.782 -42.080 -29.444 1.00 32.65 ? 38 ASN A OD1 1 ATOM 227 N ND2 . ASN A 1 38 ? 30.169 -40.032 -28.766 1.00 41.59 ? 38 ASN A ND2 1 ATOM 228 N N . ALA A 1 39 ? 33.688 -41.636 -30.227 1.00 24.31 ? 39 ALA A N 1 ATOM 229 C CA . ALA A 1 39 ? 34.354 -41.008 -31.361 1.00 24.40 ? 39 ALA A CA 1 ATOM 230 C C . ALA A 1 39 ? 33.380 -40.876 -32.534 1.00 25.22 ? 39 ALA A C 1 ATOM 231 O O . ALA A 1 39 ? 32.279 -41.463 -32.534 1.00 25.30 ? 39 ALA A O 1 ATOM 232 C CB . ALA A 1 39 ? 35.600 -41.809 -31.749 1.00 23.03 ? 39 ALA A CB 1 ATOM 233 N N . THR A 1 40 ? 33.752 -40.063 -33.509 1.00 24.65 ? 40 THR A N 1 ATOM 234 C CA . THR A 1 40 ? 32.946 -39.905 -34.724 1.00 25.87 ? 40 THR A CA 1 ATOM 235 C C . THR A 1 40 ? 33.845 -40.027 -35.967 1.00 24.75 ? 40 THR A C 1 ATOM 236 O O . THR A 1 40 ? 35.005 -39.655 -35.944 1.00 23.93 ? 40 THR A O 1 ATOM 237 C CB . THR A 1 40 ? 32.154 -38.579 -34.705 1.00 26.78 ? 40 THR A CB 1 ATOM 238 O OG1 . THR A 1 40 ? 31.089 -38.636 -35.661 1.00 30.75 ? 40 THR A OG1 1 ATOM 239 C CG2 . THR A 1 40 ? 33.026 -37.404 -35.040 1.00 28.01 ? 40 THR A CG2 1 ATOM 240 N N . GLU A 1 41 ? 33.300 -40.583 -37.035 1.00 23.89 ? 41 GLU A N 1 ATOM 241 C CA . GLU A 1 41 ? 34.039 -40.811 -38.266 1.00 24.14 ? 41 GLU A CA 1 ATOM 242 C C . GLU A 1 41 ? 34.170 -39.531 -39.116 1.00 23.14 ? 41 GLU A C 1 ATOM 243 O O . GLU A 1 41 ? 33.166 -38.844 -39.401 1.00 22.81 ? 41 GLU A O 1 ATOM 244 C CB . GLU A 1 41 ? 33.333 -41.928 -39.056 1.00 25.57 ? 41 GLU A CB 1 ATOM 245 C CG . GLU A 1 41 ? 33.927 -42.269 -40.408 1.00 25.77 ? 41 GLU A CG 1 ATOM 246 C CD . GLU A 1 41 ? 35.370 -42.713 -40.314 1.00 26.62 ? 41 GLU A CD 1 ATOM 247 O OE1 . GLU A 1 41 ? 35.619 -43.812 -39.775 1.00 27.48 ? 41 GLU A OE1 1 ATOM 248 O OE2 . GLU A 1 41 ? 36.267 -41.956 -40.748 1.00 23.22 ? 41 GLU A OE2 1 ATOM 249 N N . LEU A 1 42 ? 35.389 -39.220 -39.568 1.00 21.30 ? 42 LEU A N 1 ATOM 250 C CA . LEU A 1 42 ? 35.602 -38.022 -40.398 1.00 20.99 ? 42 LEU A CA 1 ATOM 251 C C . LEU A 1 42 ? 35.799 -38.295 -41.901 1.00 20.05 ? 42 LEU A C 1 ATOM 252 O O . LEU A 1 42 ? 35.942 -37.361 -42.684 1.00 18.95 ? 42 LEU A O 1 ATOM 253 C CB . LEU A 1 42 ? 36.789 -37.225 -39.877 1.00 21.43 ? 42 LEU A CB 1 ATOM 254 C CG . LEU A 1 42 ? 36.584 -36.585 -38.499 1.00 22.06 ? 42 LEU A CG 1 ATOM 255 C CD1 . LEU A 1 42 ? 37.768 -35.694 -38.174 1.00 21.97 ? 42 LEU A CD1 1 ATOM 256 C CD2 . LEU A 1 42 ? 35.299 -35.774 -38.381 1.00 21.75 ? 42 LEU A CD2 1 ATOM 257 N N . VAL A 1 43 ? 35.857 -39.560 -42.291 1.00 19.47 ? 43 VAL A N 1 ATOM 258 C CA . VAL A 1 43 ? 36.004 -39.943 -43.695 1.00 19.97 ? 43 VAL A CA 1 ATOM 259 C C . VAL A 1 43 ? 34.703 -40.578 -44.185 1.00 21.07 ? 43 VAL A C 1 ATOM 260 O O . VAL A 1 43 ? 34.291 -41.623 -43.686 1.00 20.66 ? 43 VAL A O 1 ATOM 261 C CB . VAL A 1 43 ? 37.162 -40.937 -43.919 1.00 19.92 ? 43 VAL A CB 1 ATOM 262 C CG1 . VAL A 1 43 ? 37.275 -41.298 -45.398 1.00 20.33 ? 43 VAL A CG1 1 ATOM 263 C CG2 . VAL A 1 43 ? 38.489 -40.357 -43.405 1.00 20.06 ? 43 VAL A CG2 1 ATOM 264 N N . GLN A 1 44 ? 34.077 -39.941 -45.172 1.00 20.77 ? 44 GLN A N 1 ATOM 265 C CA . GLN A 1 44 ? 32.892 -40.485 -45.819 1.00 21.45 ? 44 GLN A CA 1 ATOM 266 C C . GLN A 1 44 ? 33.343 -41.586 -46.775 1.00 22.77 ? 44 GLN A C 1 ATOM 267 O O . GLN A 1 44 ? 34.144 -41.343 -47.686 1.00 21.08 ? 44 GLN A O 1 ATOM 268 C CB . GLN A 1 44 ? 32.145 -39.390 -46.588 1.00 21.20 ? 44 GLN A CB 1 ATOM 269 C CG . GLN A 1 44 ? 30.839 -39.838 -47.223 1.00 21.77 ? 44 GLN A CG 1 ATOM 270 C CD . GLN A 1 44 ? 29.817 -40.238 -46.196 1.00 22.22 ? 44 GLN A CD 1 ATOM 271 O OE1 . GLN A 1 44 ? 29.720 -39.606 -45.151 1.00 23.54 ? 44 GLN A OE1 1 ATOM 272 N NE2 . GLN A 1 44 ? 29.069 -41.304 -46.468 1.00 22.14 ? 44 GLN A NE2 1 ATOM 273 N N . SER A 1 45 ? 32.851 -42.798 -46.570 1.00 23.00 ? 45 SER A N 1 ATOM 274 C CA . SER A 1 45 ? 33.285 -43.912 -47.424 1.00 26.51 ? 45 SER A CA 1 ATOM 275 C C . SER A 1 45 ? 32.176 -44.621 -48.195 1.00 29.67 ? 45 SER A C 1 ATOM 276 O O . SER A 1 45 ? 32.449 -45.554 -48.951 1.00 32.48 ? 45 SER A O 1 ATOM 277 C CB . SER A 1 45 ? 34.131 -44.900 -46.616 1.00 27.34 ? 45 SER A CB 1 ATOM 278 O OG . SER A 1 45 ? 33.348 -45.476 -45.600 1.00 30.76 ? 45 SER A OG 1 ATOM 279 N N . SER A 1 46 ? 30.935 -44.183 -48.049 1.00 31.55 ? 46 SER A N 1 ATOM 280 C CA . SER A 1 46 ? 29.840 -44.782 -48.815 1.00 34.85 ? 46 SER A CA 1 ATOM 281 C C . SER A 1 46 ? 29.109 -43.733 -49.643 1.00 35.94 ? 46 SER A C 1 ATOM 282 O O . SER A 1 46 ? 29.104 -42.540 -49.291 1.00 31.23 ? 46 SER A O 1 ATOM 283 C CB . SER A 1 46 ? 28.855 -45.441 -47.861 1.00 36.33 ? 46 SER A CB 1 ATOM 284 O OG . SER A 1 46 ? 28.329 -44.480 -46.958 1.00 37.70 ? 46 SER A OG 1 ATOM 285 N N . SER A 1 47 ? 28.506 -44.186 -50.745 1.00 37.55 ? 47 SER A N 1 ATOM 286 C CA . SER A 1 47 ? 27.554 -43.400 -51.528 1.00 39.80 ? 47 SER A CA 1 ATOM 287 C C . SER A 1 47 ? 26.265 -44.206 -51.634 1.00 43.04 ? 47 SER A C 1 ATOM 288 O O . SER A 1 47 ? 26.315 -45.417 -51.616 1.00 43.54 ? 47 SER A O 1 ATOM 289 C CB . SER A 1 47 ? 28.070 -43.160 -52.954 1.00 41.67 ? 47 SER A CB 1 ATOM 290 O OG . SER A 1 47 ? 27.048 -42.565 -53.765 1.00 42.28 ? 47 SER A OG 1 ATOM 291 N N . THR A 1 48 ? 25.134 -43.518 -51.760 1.00 45.72 ? 48 THR A N 1 ATOM 292 C CA . THR A 1 48 ? 23.849 -44.132 -52.128 1.00 49.17 ? 48 THR A CA 1 ATOM 293 C C . THR A 1 48 ? 23.918 -44.894 -53.447 1.00 47.44 ? 48 THR A C 1 ATOM 294 O O . THR A 1 48 ? 23.184 -45.855 -53.655 1.00 50.48 ? 48 THR A O 1 ATOM 295 C CB . THR A 1 48 ? 22.772 -43.052 -52.342 1.00 51.30 ? 48 THR A CB 1 ATOM 296 O OG1 . THR A 1 48 ? 22.754 -42.164 -51.217 1.00 56.13 ? 48 THR A OG1 1 ATOM 297 C CG2 . THR A 1 48 ? 21.390 -43.687 -52.554 1.00 53.48 ? 48 THR A CG2 1 ATOM 298 N N . GLY A 1 49 ? 24.784 -44.444 -54.352 1.00 44.28 ? 49 GLY A N 1 ATOM 299 C CA . GLY A 1 49 ? 24.912 -45.085 -55.648 1.00 43.44 ? 49 GLY A CA 1 ATOM 300 C C . GLY A 1 49 ? 24.162 -44.332 -56.735 1.00 41.60 ? 49 GLY A C 1 ATOM 301 O O . GLY A 1 49 ? 24.327 -44.662 -57.915 1.00 43.83 ? 49 GLY A O 1 ATOM 302 N N . GLY A 1 50 ? 23.344 -43.335 -56.358 1.00 35.18 ? 50 GLY A N 1 ATOM 303 C CA . GLY A 1 50 ? 22.678 -42.480 -57.348 1.00 32.24 ? 50 GLY A CA 1 ATOM 304 C C . GLY A 1 50 ? 23.092 -41.020 -57.305 1.00 28.12 ? 50 GLY A C 1 ATOM 305 O O . GLY A 1 50 ? 23.433 -40.506 -56.248 1.00 25.60 ? 50 GLY A O 1 ATOM 306 N N . ILE A 1 51 ? 23.042 -40.360 -58.462 1.00 26.12 ? 51 ILE A N 1 ATOM 307 C CA . ILE A 1 51 ? 23.270 -38.926 -58.564 1.00 26.67 ? 51 ILE A CA 1 ATOM 308 C C . ILE A 1 51 ? 21.934 -38.202 -58.316 1.00 27.35 ? 51 ILE A C 1 ATOM 309 O O . ILE A 1 51 ? 21.001 -38.367 -59.095 1.00 27.07 ? 51 ILE A O 1 ATOM 310 C CB . ILE A 1 51 ? 23.833 -38.550 -59.956 1.00 26.58 ? 51 ILE A CB 1 ATOM 311 C CG1 . ILE A 1 51 ? 25.274 -39.050 -60.087 1.00 28.18 ? 51 ILE A CG1 1 ATOM 312 C CG2 . ILE A 1 51 ? 23.816 -37.028 -60.156 1.00 27.68 ? 51 ILE A CG2 1 ATOM 313 C CD1 . ILE A 1 51 ? 25.822 -39.011 -61.500 1.00 28.59 ? 51 ILE A CD1 1 ATOM 314 N N . CYS A 1 52 ? 21.861 -37.414 -57.242 1.00 27.18 ? 52 CYS A N 1 ATOM 315 C CA . CYS A 1 52 ? 20.664 -36.626 -56.934 1.00 27.90 ? 52 CYS A CA 1 ATOM 316 C C . CYS A 1 52 ? 20.485 -35.471 -57.913 1.00 27.07 ? 52 CYS A C 1 ATOM 317 O O . CYS A 1 52 ? 21.442 -34.727 -58.196 1.00 24.19 ? 52 CYS A O 1 ATOM 318 C CB . CYS A 1 52 ? 20.719 -36.112 -55.500 1.00 30.89 ? 52 CYS A CB 1 ATOM 319 S SG . CYS A 1 52 ? 20.608 -37.444 -54.255 1.00 33.99 ? 52 CYS A SG 1 ATOM 320 N N . ASP A 1 53 ? 19.258 -35.320 -58.415 1.00 25.59 ? 53 ASP A N 1 ATOM 321 C CA . ASP A 1 53 ? 18.952 -34.315 -59.432 1.00 27.15 ? 53 ASP A CA 1 ATOM 322 C C . ASP A 1 53 ? 18.783 -32.908 -58.865 1.00 26.19 ? 53 ASP A C 1 ATOM 323 O O . ASP A 1 53 ? 18.545 -31.983 -59.630 1.00 26.67 ? 53 ASP A O 1 ATOM 324 C CB . ASP A 1 53 ? 17.701 -34.708 -60.241 1.00 28.58 ? 53 ASP A CB 1 ATOM 325 C CG . ASP A 1 53 ? 16.412 -34.629 -59.431 1.00 30.28 ? 53 ASP A CG 1 ATOM 326 O OD1 . ASP A 1 53 ? 16.426 -34.240 -58.229 1.00 31.98 ? 53 ASP A OD1 1 ATOM 327 O OD2 . ASP A 1 53 ? 15.359 -34.965 -60.011 1.00 34.16 ? 53 ASP A OD2 1 ATOM 328 N N . SER A 1 54 ? 18.906 -32.764 -57.545 1.00 25.50 ? 54 SER A N 1 ATOM 329 C CA . SER A 1 54 ? 18.879 -31.473 -56.846 1.00 25.54 ? 54 SER A CA 1 ATOM 330 C C . SER A 1 54 ? 20.073 -31.390 -55.892 1.00 25.01 ? 54 SER A C 1 ATOM 331 O O . SER A 1 54 ? 20.527 -32.439 -55.372 1.00 24.45 ? 54 SER A O 1 ATOM 332 C CB . SER A 1 54 ? 17.579 -31.351 -56.049 1.00 26.34 ? 54 SER A CB 1 ATOM 333 O OG . SER A 1 54 ? 16.469 -31.624 -56.881 1.00 26.39 ? 54 SER A OG 1 ATOM 334 N N . PRO A 1 55 ? 20.591 -30.178 -55.635 1.00 23.98 ? 55 PRO A N 1 ATOM 335 C CA . PRO A 1 55 ? 20.178 -28.871 -56.110 1.00 25.07 ? 55 PRO A CA 1 ATOM 336 C C . PRO A 1 55 ? 20.874 -28.374 -57.389 1.00 24.45 ? 55 PRO A C 1 ATOM 337 O O . PRO A 1 55 ? 20.603 -27.233 -57.833 1.00 24.62 ? 55 PRO A O 1 ATOM 338 C CB . PRO A 1 55 ? 20.564 -27.985 -54.951 1.00 24.98 ? 55 PRO A CB 1 ATOM 339 C CG . PRO A 1 55 ? 21.890 -28.551 -54.500 1.00 24.57 ? 55 PRO A CG 1 ATOM 340 C CD . PRO A 1 55 ? 21.736 -30.052 -54.710 1.00 24.67 ? 55 PRO A CD 1 ATOM 341 N N . HIS A 1 56 ? 21.744 -29.194 -57.979 1.00 22.91 ? 56 HIS A N 1 ATOM 342 C CA . HIS A 1 56 ? 22.458 -28.816 -59.191 1.00 23.13 ? 56 HIS A CA 1 ATOM 343 C C . HIS A 1 56 ? 21.644 -29.231 -60.374 1.00 23.44 ? 56 HIS A C 1 ATOM 344 O O . HIS A 1 56 ? 20.914 -30.240 -60.310 1.00 23.61 ? 56 HIS A O 1 ATOM 345 C CB . HIS A 1 56 ? 23.832 -29.488 -59.251 1.00 23.80 ? 56 HIS A CB 1 ATOM 346 C CG . HIS A 1 56 ? 24.675 -29.244 -58.026 1.00 23.45 ? 56 HIS A CG 1 ATOM 347 N ND1 . HIS A 1 56 ? 25.158 -28.030 -57.717 1.00 23.95 ? 56 HIS A ND1 1 ATOM 348 C CD2 . HIS A 1 56 ? 25.112 -30.114 -57.020 1.00 23.65 ? 56 HIS A CD2 1 ATOM 349 C CE1 . HIS A 1 56 ? 25.872 -28.109 -56.576 1.00 24.18 ? 56 HIS A CE1 1 ATOM 350 N NE2 . HIS A 1 56 ? 25.837 -29.383 -56.146 1.00 24.03 ? 56 HIS A NE2 1 ATOM 351 N N . GLN A 1 57 ? 21.745 -28.461 -61.455 1.00 22.37 ? 57 GLN A N 1 ATOM 352 C CA . GLN A 1 57 ? 21.063 -28.803 -62.696 1.00 22.14 ? 57 GLN A CA 1 ATOM 353 C C . GLN A 1 57 ? 21.869 -29.855 -63.428 1.00 21.81 ? 57 GLN A C 1 ATOM 354 O O . GLN A 1 57 ? 22.957 -29.576 -63.943 1.00 20.87 ? 57 GLN A O 1 ATOM 355 C CB . GLN A 1 57 ? 20.888 -27.580 -63.611 1.00 21.75 ? 57 GLN A CB 1 ATOM 356 C CG . GLN A 1 57 ? 20.094 -27.915 -64.868 1.00 21.63 ? 57 GLN A CG 1 ATOM 357 C CD . GLN A 1 57 ? 19.804 -26.718 -65.740 1.00 22.01 ? 57 GLN A CD 1 ATOM 358 O OE1 . GLN A 1 57 ? 20.576 -25.737 -65.779 1.00 22.90 ? 57 GLN A OE1 1 ATOM 359 N NE2 . GLN A 1 57 ? 18.720 -26.812 -66.501 1.00 21.45 ? 57 GLN A NE2 1 ATOM 360 N N . ILE A 1 58 ? 21.317 -31.058 -63.484 1.00 22.82 ? 58 ILE A N 1 ATOM 361 C CA . ILE A 1 58 ? 21.952 -32.211 -64.108 1.00 23.60 ? 58 ILE A CA 1 ATOM 362 C C . ILE A 1 58 ? 21.435 -32.395 -65.520 1.00 24.91 ? 58 ILE A C 1 ATOM 363 O O . ILE A 1 58 ? 20.231 -32.256 -65.759 1.00 26.26 ? 58 ILE A O 1 ATOM 364 C CB . ILE A 1 58 ? 21.625 -33.506 -63.341 1.00 25.24 ? 58 ILE A CB 1 ATOM 365 C CG1 . ILE A 1 58 ? 21.972 -33.359 -61.857 1.00 25.81 ? 58 ILE A CG1 1 ATOM 366 C CG2 . ILE A 1 58 ? 22.375 -34.701 -63.953 1.00 25.91 ? 58 ILE A CG2 1 ATOM 367 C CD1 . ILE A 1 58 ? 23.427 -33.043 -61.537 1.00 26.17 ? 58 ILE A CD1 1 ATOM 368 N N . LEU A 1 59 ? 22.331 -32.659 -66.466 1.00 23.81 ? 59 LEU A N 1 ATOM 369 C CA . LEU A 1 59 ? 21.928 -33.061 -67.813 1.00 24.59 ? 59 LEU A CA 1 ATOM 370 C C . LEU A 1 59 ? 22.516 -34.442 -68.073 1.00 25.16 ? 59 LEU A C 1 ATOM 371 O O . LEU A 1 59 ? 23.741 -34.593 -68.202 1.00 24.45 ? 59 LEU A O 1 ATOM 372 C CB . LEU A 1 59 ? 22.394 -32.073 -68.874 1.00 24.53 ? 59 LEU A CB 1 ATOM 373 C CG . LEU A 1 59 ? 21.922 -32.335 -70.305 1.00 25.48 ? 59 LEU A CG 1 ATOM 374 C CD1 . LEU A 1 59 ? 20.434 -32.690 -70.331 1.00 26.81 ? 59 LEU A CD1 1 ATOM 375 C CD2 . LEU A 1 59 ? 22.203 -31.118 -71.185 1.00 24.76 ? 59 LEU A CD2 1 ATOM 376 N N . ASP A 1 60 ? 21.641 -35.439 -68.108 1.00 24.67 ? 60 ASP A N 1 ATOM 377 C CA . ASP A 1 60 ? 22.038 -36.814 -68.422 1.00 25.46 ? 60 ASP A CA 1 ATOM 378 C C . ASP A 1 60 ? 22.194 -36.973 -69.919 1.00 25.57 ? 60 ASP A C 1 ATOM 379 O O . ASP A 1 60 ? 21.200 -36.905 -70.654 1.00 25.79 ? 60 ASP A O 1 ATOM 380 C CB . ASP A 1 60 ? 20.955 -37.767 -67.946 1.00 26.68 ? 60 ASP A CB 1 ATOM 381 C CG . ASP A 1 60 ? 21.367 -39.247 -68.045 1.00 27.53 ? 60 ASP A CG 1 ATOM 382 O OD1 . ASP A 1 60 ? 22.317 -39.588 -68.793 1.00 28.40 ? 60 ASP A OD1 1 ATOM 383 O OD2 . ASP A 1 60 ? 20.746 -40.052 -67.331 1.00 28.50 ? 60 ASP A OD2 1 ATOM 384 N N . GLY A 1 61 ? 23.418 -37.206 -70.378 1.00 25.25 ? 61 GLY A N 1 ATOM 385 C CA . GLY A 1 61 ? 23.691 -37.340 -71.801 1.00 25.92 ? 61 GLY A CA 1 ATOM 386 C C . GLY A 1 61 ? 23.076 -38.573 -72.459 1.00 27.17 ? 61 GLY A C 1 ATOM 387 O O . GLY A 1 61 ? 22.983 -38.643 -73.684 1.00 27.46 ? 61 GLY A O 1 ATOM 388 N N . GLU A 1 62 ? 22.673 -39.547 -71.650 1.00 28.14 ? 62 GLU A N 1 ATOM 389 C CA . GLU A 1 62 ? 22.116 -40.811 -72.147 1.00 30.34 ? 62 GLU A CA 1 ATOM 390 C C . GLU A 1 62 ? 23.030 -41.428 -73.217 1.00 29.41 ? 62 GLU A C 1 ATOM 391 O O . GLU A 1 62 ? 24.171 -41.773 -72.907 1.00 28.03 ? 62 GLU A O 1 ATOM 392 C CB . GLU A 1 62 ? 20.655 -40.602 -72.590 1.00 33.68 ? 62 GLU A CB 1 ATOM 393 C CG . GLU A 1 62 ? 19.812 -40.059 -71.433 1.00 37.04 ? 62 GLU A CG 1 ATOM 394 C CD . GLU A 1 62 ? 18.312 -40.019 -71.674 1.00 42.21 ? 62 GLU A CD 1 ATOM 395 O OE1 . GLU A 1 62 ? 17.829 -39.126 -72.406 1.00 46.43 ? 62 GLU A OE1 1 ATOM 396 O OE2 . GLU A 1 62 ? 17.606 -40.846 -71.061 1.00 48.79 ? 62 GLU A OE2 1 ATOM 397 N N . ASN A 1 63 ? 22.565 -41.581 -74.458 1.00 29.15 ? 63 ASN A N 1 ATOM 398 C CA . ASN A 1 63 ? 23.431 -42.143 -75.512 1.00 31.27 ? 63 ASN A CA 1 ATOM 399 C C . ASN A 1 63 ? 24.375 -41.152 -76.201 1.00 30.37 ? 63 ASN A C 1 ATOM 400 O O . ASN A 1 63 ? 25.087 -41.531 -77.123 1.00 28.82 ? 63 ASN A O 1 ATOM 401 C CB . ASN A 1 63 ? 22.579 -42.788 -76.598 1.00 34.07 ? 63 ASN A CB 1 ATOM 402 C CG . ASN A 1 63 ? 21.968 -44.085 -76.151 1.00 37.16 ? 63 ASN A CG 1 ATOM 403 O OD1 . ASN A 1 63 ? 22.526 -44.817 -75.333 1.00 36.13 ? 63 ASN A OD1 1 ATOM 404 N ND2 . ASN A 1 63 ? 20.807 -44.373 -76.695 1.00 42.59 ? 63 ASN A ND2 1 ATOM 405 N N . CYS A 1 64 ? 24.362 -39.892 -75.760 1.00 29.72 ? 64 CYS A N 1 ATOM 406 C CA . CYS A 1 64 ? 25.101 -38.813 -76.400 1.00 29.94 ? 64 CYS A CA 1 ATOM 407 C C . CYS A 1 64 ? 26.247 -38.307 -75.533 1.00 28.24 ? 64 CYS A C 1 ATOM 408 O O . CYS A 1 64 ? 26.074 -38.063 -74.332 1.00 27.40 ? 64 CYS A O 1 ATOM 409 C CB . CYS A 1 64 ? 24.149 -37.628 -76.649 1.00 33.23 ? 64 CYS A CB 1 ATOM 410 S SG . CYS A 1 64 ? 22.806 -37.948 -77.845 1.00 39.72 ? 64 CYS A SG 1 ATOM 411 N N . THR A 1 65 ? 27.402 -38.122 -76.153 1.00 26.42 ? 65 THR A N 1 ATOM 412 C CA . THR A 1 65 ? 28.456 -37.322 -75.564 1.00 26.28 ? 65 THR A CA 1 ATOM 413 C C . THR A 1 65 ? 28.081 -35.850 -75.721 1.00 24.73 ? 65 THR A C 1 ATOM 414 O O . THR A 1 65 ? 27.209 -35.497 -76.544 1.00 25.19 ? 65 THR A O 1 ATOM 415 C CB . THR A 1 65 ? 29.783 -37.590 -76.255 1.00 26.83 ? 65 THR A CB 1 ATOM 416 O OG1 . THR A 1 65 ? 29.700 -37.114 -77.597 1.00 27.61 ? 65 THR A OG1 1 ATOM 417 C CG2 . THR A 1 65 ? 30.113 -39.112 -76.248 1.00 28.29 ? 65 THR A CG2 1 ATOM 418 N N . LEU A 1 66 ? 28.754 -34.991 -74.962 1.00 23.53 ? 66 LEU A N 1 ATOM 419 C CA . LEU A 1 66 ? 28.540 -33.552 -75.061 1.00 23.14 ? 66 LEU A CA 1 ATOM 420 C C . LEU A 1 66 ? 28.853 -33.098 -76.478 1.00 23.28 ? 66 LEU A C 1 ATOM 421 O O . LEU A 1 66 ? 28.090 -32.311 -77.068 1.00 21.15 ? 66 LEU A O 1 ATOM 422 C CB . LEU A 1 66 ? 29.416 -32.799 -74.047 1.00 23.22 ? 66 LEU A CB 1 ATOM 423 C CG . LEU A 1 66 ? 29.418 -31.272 -74.146 1.00 22.97 ? 66 LEU A CG 1 ATOM 424 C CD1 . LEU A 1 66 ? 27.967 -30.817 -74.133 1.00 22.50 ? 66 LEU A CD1 1 ATOM 425 C CD2 . LEU A 1 66 ? 30.257 -30.642 -73.010 1.00 21.56 ? 66 LEU A CD2 1 ATOM 426 N N . ILE A 1 67 ? 29.954 -33.598 -77.032 1.00 24.38 ? 67 ILE A N 1 ATOM 427 C CA . ILE A 1 67 ? 30.353 -33.178 -78.391 1.00 25.58 ? 67 ILE A CA 1 ATOM 428 C C . ILE A 1 67 ? 29.312 -33.643 -79.419 1.00 25.60 ? 67 ILE A C 1 ATOM 429 O O . ILE A 1 67 ? 28.982 -32.888 -80.344 1.00 26.28 ? 67 ILE A O 1 ATOM 430 C CB . ILE A 1 67 ? 31.786 -33.629 -78.770 1.00 26.61 ? 67 ILE A CB 1 ATOM 431 C CG1 . ILE A 1 67 ? 32.846 -32.891 -77.928 1.00 28.28 ? 67 ILE A CG1 1 ATOM 432 C CG2 . ILE A 1 67 ? 32.082 -33.382 -80.254 1.00 26.62 ? 67 ILE A CG2 1 ATOM 433 C CD1 . ILE A 1 67 ? 32.702 -31.390 -77.880 1.00 29.53 ? 67 ILE A CD1 1 ATOM 434 N N . ASP A 1 68 ? 28.746 -34.841 -79.249 1.00 26.84 ? 68 ASP A N 1 ATOM 435 C CA . ASP A 1 68 ? 27.655 -35.283 -80.146 1.00 27.91 ? 68 ASP A CA 1 ATOM 436 C C . ASP A 1 68 ? 26.439 -34.350 -80.058 1.00 27.42 ? 68 ASP A C 1 ATOM 437 O O . ASP A 1 68 ? 25.819 -34.010 -81.081 1.00 26.63 ? 68 ASP A O 1 ATOM 438 C CB . ASP A 1 68 ? 27.193 -36.717 -79.858 1.00 29.45 ? 68 ASP A CB 1 ATOM 439 C CG . ASP A 1 68 ? 28.168 -37.782 -80.367 1.00 32.87 ? 68 ASP A CG 1 ATOM 440 O OD1 . ASP A 1 68 ? 28.957 -37.500 -81.285 1.00 33.41 ? 68 ASP A OD1 1 ATOM 441 O OD2 . ASP A 1 68 ? 28.143 -38.914 -79.813 1.00 38.19 ? 68 ASP A OD2 1 ATOM 442 N N . ALA A 1 69 ? 26.087 -33.953 -78.839 1.00 26.43 ? 69 ALA A N 1 ATOM 443 C CA . ALA A 1 69 ? 24.984 -33.031 -78.618 1.00 26.49 ? 69 ALA A CA 1 ATOM 444 C C . ALA A 1 69 ? 25.281 -31.642 -79.187 1.00 26.43 ? 69 ALA A C 1 ATOM 445 O O . ALA A 1 69 ? 24.373 -30.977 -79.698 1.00 27.45 ? 69 ALA A O 1 ATOM 446 C CB . ALA A 1 69 ? 24.630 -32.953 -77.126 1.00 26.87 ? 69 ALA A CB 1 ATOM 447 N N . LEU A 1 70 ? 26.541 -31.214 -79.127 1.00 25.43 ? 70 LEU A N 1 ATOM 448 C CA . LEU A 1 70 ? 26.974 -29.940 -79.721 1.00 25.51 ? 70 LEU A CA 1 ATOM 449 C C . LEU A 1 70 ? 26.797 -29.937 -81.260 1.00 26.19 ? 70 LEU A C 1 ATOM 450 O O . LEU A 1 70 ? 26.177 -29.041 -81.831 1.00 26.84 ? 70 LEU A O 1 ATOM 451 C CB . LEU A 1 70 ? 28.445 -29.689 -79.376 1.00 25.20 ? 70 LEU A CB 1 ATOM 452 C CG . LEU A 1 70 ? 29.146 -28.407 -79.852 1.00 24.98 ? 70 LEU A CG 1 ATOM 453 C CD1 . LEU A 1 70 ? 28.755 -27.231 -78.976 1.00 24.02 ? 70 LEU A CD1 1 ATOM 454 C CD2 . LEU A 1 70 ? 30.670 -28.573 -79.865 1.00 25.10 ? 70 LEU A CD2 1 ATOM 455 N N . LEU A 1 71 ? 27.367 -30.935 -81.910 1.00 26.22 ? 71 LEU A N 1 ATOM 456 C CA . LEU A 1 71 ? 27.320 -31.026 -83.358 1.00 27.34 ? 71 LEU A CA 1 ATOM 457 C C . LEU A 1 71 ? 25.882 -31.200 -83.840 1.00 27.38 ? 71 LEU A C 1 ATOM 458 O O . LEU A 1 71 ? 25.516 -30.695 -84.891 1.00 28.37 ? 71 LEU A O 1 ATOM 459 C CB . LEU A 1 71 ? 28.191 -32.190 -83.832 1.00 27.66 ? 71 LEU A CB 1 ATOM 460 C CG . LEU A 1 71 ? 29.689 -32.090 -83.506 1.00 28.39 ? 71 LEU A CG 1 ATOM 461 C CD1 . LEU A 1 71 ? 30.461 -33.240 -84.141 1.00 29.06 ? 71 LEU A CD1 1 ATOM 462 C CD2 . LEU A 1 71 ? 30.297 -30.765 -83.922 1.00 27.89 ? 71 LEU A CD2 1 ATOM 463 N N . GLY A 1 72 ? 25.076 -31.908 -83.062 1.00 27.99 ? 72 GLY A N 1 ATOM 464 C CA . GLY A 1 72 ? 23.670 -32.114 -83.404 1.00 29.17 ? 72 GLY A CA 1 ATOM 465 C C . GLY A 1 72 ? 23.396 -33.433 -84.112 1.00 31.37 ? 72 GLY A C 1 ATOM 466 O O . GLY A 1 72 ? 22.629 -33.479 -85.084 1.00 29.47 ? 72 GLY A O 1 ATOM 467 N N . ASP A 1 73 ? 24.020 -34.499 -83.609 1.00 31.55 ? 73 ASP A N 1 ATOM 468 C CA . ASP A 1 73 ? 23.697 -35.879 -83.986 1.00 33.58 ? 73 ASP A CA 1 ATOM 469 C C . ASP A 1 73 ? 22.183 -36.072 -83.772 1.00 34.08 ? 73 ASP A C 1 ATOM 470 O O . ASP A 1 73 ? 21.648 -35.630 -82.761 1.00 33.99 ? 73 ASP A O 1 ATOM 471 C CB . ASP A 1 73 ? 24.535 -36.812 -83.098 1.00 34.31 ? 73 ASP A CB 1 ATOM 472 C CG . ASP A 1 73 ? 24.390 -38.311 -83.442 1.00 37.84 ? 73 ASP A CG 1 ATOM 473 O OD1 . ASP A 1 73 ? 23.344 -38.738 -83.976 1.00 40.56 ? 73 ASP A OD1 1 ATOM 474 O OD2 . ASP A 1 73 ? 25.329 -39.072 -83.140 1.00 36.55 ? 73 ASP A OD2 1 ATOM 475 N N . PRO A 1 74 ? 21.470 -36.676 -84.742 1.00 36.40 ? 74 PRO A N 1 ATOM 476 C CA . PRO A 1 74 ? 20.002 -36.786 -84.621 1.00 36.94 ? 74 PRO A CA 1 ATOM 477 C C . PRO A 1 74 ? 19.456 -37.337 -83.298 1.00 37.14 ? 74 PRO A C 1 ATOM 478 O O . PRO A 1 74 ? 18.486 -36.788 -82.763 1.00 36.60 ? 74 PRO A O 1 ATOM 479 C CB . PRO A 1 74 ? 19.635 -37.696 -85.795 1.00 39.36 ? 74 PRO A CB 1 ATOM 480 C CG . PRO A 1 74 ? 20.624 -37.295 -86.839 1.00 39.12 ? 74 PRO A CG 1 ATOM 481 C CD . PRO A 1 74 ? 21.920 -37.059 -86.094 1.00 37.86 ? 74 PRO A CD 1 ATOM 482 N N . GLN A 1 75 ? 20.086 -38.364 -82.741 1.00 36.53 ? 75 GLN A N 1 ATOM 483 C CA . GLN A 1 75 ? 19.622 -38.870 -81.450 1.00 37.70 ? 75 GLN A CA 1 ATOM 484 C C . GLN A 1 75 ? 19.769 -37.870 -80.294 1.00 35.51 ? 75 GLN A C 1 ATOM 485 O O . GLN A 1 75 ? 19.197 -38.085 -79.235 1.00 33.80 ? 75 GLN A O 1 ATOM 486 C CB . GLN A 1 75 ? 20.257 -40.216 -81.106 1.00 39.06 ? 75 GLN A CB 1 ATOM 487 C CG . GLN A 1 75 ? 21.734 -40.190 -80.816 1.00 40.73 ? 75 GLN A CG 1 ATOM 488 C CD . GLN A 1 75 ? 22.299 -41.586 -80.623 1.00 43.69 ? 75 GLN A CD 1 ATOM 489 O OE1 . GLN A 1 75 ? 21.607 -42.584 -80.822 1.00 47.10 ? 75 GLN A OE1 1 ATOM 490 N NE2 . GLN A 1 75 ? 23.565 -41.661 -80.251 1.00 41.29 ? 75 GLN A NE2 1 ATOM 491 N N . CYS A 1 76 ? 20.497 -36.771 -80.511 1.00 33.34 ? 76 CYS A N 1 ATOM 492 C CA . CYS A 1 76 ? 20.684 -35.743 -79.485 1.00 32.91 ? 76 CYS A CA 1 ATOM 493 C C . CYS A 1 76 ? 19.830 -34.492 -79.707 1.00 31.92 ? 76 CYS A C 1 ATOM 494 O O . CYS A 1 76 ? 20.049 -33.483 -79.039 1.00 29.83 ? 76 CYS A O 1 ATOM 495 C CB . CYS A 1 76 ? 22.158 -35.314 -79.409 1.00 34.74 ? 76 CYS A CB 1 ATOM 496 S SG . CYS A 1 76 ? 23.329 -36.681 -79.457 1.00 37.14 ? 76 CYS A SG 1 ATOM 497 N N . ASP A 1 77 ? 18.844 -34.551 -80.609 1.00 30.58 ? 77 ASP A N 1 ATOM 498 C CA . ASP A 1 77 ? 18.043 -33.362 -80.926 1.00 31.66 ? 77 ASP A CA 1 ATOM 499 C C . ASP A 1 77 ? 17.325 -32.790 -79.700 1.00 30.75 ? 77 ASP A C 1 ATOM 500 O O . ASP A 1 77 ? 17.078 -31.575 -79.612 1.00 30.26 ? 77 ASP A O 1 ATOM 501 C CB . ASP A 1 77 ? 17.012 -33.685 -82.020 1.00 32.94 ? 77 ASP A CB 1 ATOM 502 C CG . ASP A 1 77 ? 17.642 -33.814 -83.407 1.00 34.84 ? 77 ASP A CG 1 ATOM 503 O OD1 . ASP A 1 77 ? 18.820 -33.410 -83.595 1.00 34.27 ? 77 ASP A OD1 1 ATOM 504 O OD2 . ASP A 1 77 ? 16.942 -34.301 -84.328 1.00 35.95 ? 77 ASP A OD2 1 ATOM 505 N N . GLY A 1 78 ? 16.974 -33.666 -78.764 1.00 30.79 ? 78 GLY A N 1 ATOM 506 C CA . GLY A 1 78 ? 16.278 -33.251 -77.552 1.00 31.08 ? 78 GLY A CA 1 ATOM 507 C C . GLY A 1 78 ? 17.130 -32.360 -76.646 1.00 29.86 ? 78 GLY A C 1 ATOM 508 O O . GLY A 1 78 ? 16.582 -31.687 -75.760 1.00 29.71 ? 78 GLY A O 1 ATOM 509 N N . PHE A 1 79 ? 18.450 -32.346 -76.868 1.00 29.10 ? 79 PHE A N 1 ATOM 510 C CA . PHE A 1 79 ? 19.364 -31.528 -76.057 1.00 29.41 ? 79 PHE A CA 1 ATOM 511 C C . PHE A 1 79 ? 19.508 -30.088 -76.523 1.00 28.04 ? 79 PHE A C 1 ATOM 512 O O . PHE A 1 79 ? 20.202 -29.310 -75.866 1.00 26.20 ? 79 PHE A O 1 ATOM 513 C CB . PHE A 1 79 ? 20.772 -32.134 -76.019 1.00 32.46 ? 79 PHE A CB 1 ATOM 514 C CG . PHE A 1 79 ? 20.857 -33.449 -75.309 1.00 34.17 ? 79 PHE A CG 1 ATOM 515 C CD1 . PHE A 1 79 ? 20.700 -34.634 -75.999 1.00 36.80 ? 79 PHE A CD1 1 ATOM 516 C CD2 . PHE A 1 79 ? 21.157 -33.507 -73.961 1.00 37.76 ? 79 PHE A CD2 1 ATOM 517 C CE1 . PHE A 1 79 ? 20.807 -35.859 -75.357 1.00 36.55 ? 79 PHE A CE1 1 ATOM 518 C CE2 . PHE A 1 79 ? 21.265 -34.735 -73.312 1.00 38.35 ? 79 PHE A CE2 1 ATOM 519 C CZ . PHE A 1 79 ? 21.077 -35.911 -74.015 1.00 35.70 ? 79 PHE A CZ 1 ATOM 520 N N . GLN A 1 80 ? 18.891 -29.727 -77.654 1.00 26.51 ? 80 GLN A N 1 ATOM 521 C CA . GLN A 1 80 ? 19.115 -28.406 -78.245 1.00 26.39 ? 80 GLN A CA 1 ATOM 522 C C . GLN A 1 80 ? 18.882 -27.299 -77.231 1.00 25.98 ? 80 GLN A C 1 ATOM 523 O O . GLN A 1 80 ? 17.875 -27.283 -76.543 1.00 24.50 ? 80 GLN A O 1 ATOM 524 C CB . GLN A 1 80 ? 18.223 -28.181 -79.483 1.00 27.92 ? 80 GLN A CB 1 ATOM 525 C CG . GLN A 1 80 ? 18.722 -28.926 -80.714 1.00 28.91 ? 80 GLN A CG 1 ATOM 526 C CD . GLN A 1 80 ? 18.096 -28.428 -82.019 1.00 31.19 ? 80 GLN A CD 1 ATOM 527 O OE1 . GLN A 1 80 ? 17.163 -27.618 -82.016 1.00 29.89 ? 80 GLN A OE1 1 ATOM 528 N NE2 . GLN A 1 80 ? 18.652 -28.877 -83.142 1.00 31.70 ? 80 GLN A NE2 1 ATOM 529 N N . ASN A 1 81 ? 19.843 -26.386 -77.140 1.00 25.08 ? 81 ASN A N 1 ATOM 530 C CA . ASN A 1 81 ? 19.739 -25.199 -76.309 1.00 25.18 ? 81 ASN A CA 1 ATOM 531 C C . ASN A 1 81 ? 19.686 -25.414 -74.790 1.00 24.93 ? 81 ASN A C 1 ATOM 532 O O . ASN A 1 81 ? 19.494 -24.459 -74.051 1.00 26.01 ? 81 ASN A O 1 ATOM 533 C CB . ASN A 1 81 ? 18.564 -24.307 -76.761 1.00 26.80 ? 81 ASN A CB 1 ATOM 534 C CG . ASN A 1 81 ? 18.722 -23.832 -78.198 1.00 27.16 ? 81 ASN A CG 1 ATOM 535 O OD1 . ASN A 1 81 ? 19.706 -23.175 -78.545 1.00 28.29 ? 81 ASN A OD1 1 ATOM 536 N ND2 . ASN A 1 81 ? 17.781 -24.199 -79.040 1.00 28.37 ? 81 ASN A ND2 1 ATOM 537 N N . LYS A 1 82 ? 19.894 -26.634 -74.317 1.00 24.91 ? 82 LYS A N 1 ATOM 538 C CA . LYS A 1 82 ? 19.827 -26.895 -72.870 1.00 25.72 ? 82 LYS A CA 1 ATOM 539 C C . LYS A 1 82 ? 21.081 -26.370 -72.153 1.00 24.35 ? 82 LYS A C 1 ATOM 540 O O . LYS A 1 82 ? 22.148 -26.215 -72.768 1.00 23.68 ? 82 LYS A O 1 ATOM 541 C CB . LYS A 1 82 ? 19.645 -28.390 -72.593 1.00 27.34 ? 82 LYS A CB 1 ATOM 542 C CG . LYS A 1 82 ? 18.260 -28.909 -72.928 1.00 30.46 ? 82 LYS A CG 1 ATOM 543 C CD . LYS A 1 82 ? 18.123 -30.415 -72.738 1.00 32.73 ? 82 LYS A CD 1 ATOM 544 C CE . LYS A 1 82 ? 18.085 -30.864 -71.286 1.00 34.54 ? 82 LYS A CE 1 ATOM 545 N NZ . LYS A 1 82 ? 17.025 -30.316 -70.405 1.00 38.14 ? 82 LYS A NZ 1 ATOM 546 N N . LYS A 1 83 ? 20.930 -26.128 -70.851 1.00 23.81 ? 83 LYS A N 1 ATOM 547 C CA . LYS A 1 83 ? 22.005 -25.710 -69.990 1.00 23.72 ? 83 LYS A CA 1 ATOM 548 C C . LYS A 1 83 ? 22.180 -26.759 -68.879 1.00 23.14 ? 83 LYS A C 1 ATOM 549 O O . LYS A 1 83 ? 21.298 -27.616 -68.652 1.00 22.41 ? 83 LYS A O 1 ATOM 550 C CB . LYS A 1 83 ? 21.705 -24.336 -69.379 1.00 25.08 ? 83 LYS A CB 1 ATOM 551 C CG . LYS A 1 83 ? 21.457 -23.237 -70.400 1.00 26.15 ? 83 LYS A CG 1 ATOM 552 C CD . LYS A 1 83 ? 21.481 -21.881 -69.705 1.00 27.30 ? 83 LYS A CD 1 ATOM 553 C CE . LYS A 1 83 ? 20.818 -20.812 -70.544 1.00 29.16 ? 83 LYS A CE 1 ATOM 554 N NZ . LYS A 1 83 ? 19.339 -20.945 -70.601 1.00 28.72 ? 83 LYS A NZ 1 ATOM 555 N N . TRP A 1 84 ? 23.306 -26.681 -68.189 1.00 21.81 ? 84 TRP A N 1 ATOM 556 C CA . TRP A 1 84 ? 23.593 -27.590 -67.067 1.00 20.96 ? 84 TRP A CA 1 ATOM 557 C C . TRP A 1 84 ? 24.533 -26.971 -66.104 1.00 20.70 ? 84 TRP A C 1 ATOM 558 O O . TRP A 1 84 ? 25.321 -26.085 -66.466 1.00 21.11 ? 84 TRP A O 1 ATOM 559 C CB . TRP A 1 84 ? 24.206 -28.906 -67.538 1.00 20.49 ? 84 TRP A CB 1 ATOM 560 C CG . TRP A 1 84 ? 25.495 -28.720 -68.301 1.00 20.73 ? 84 TRP A CG 1 ATOM 561 C CD1 . TRP A 1 84 ? 26.809 -28.782 -67.828 1.00 20.19 ? 84 TRP A CD1 1 ATOM 562 C CD2 . TRP A 1 84 ? 25.613 -28.408 -69.721 1.00 20.66 ? 84 TRP A CD2 1 ATOM 563 N NE1 . TRP A 1 84 ? 27.693 -28.517 -68.831 1.00 20.39 ? 84 TRP A NE1 1 ATOM 564 C CE2 . TRP A 1 84 ? 27.036 -28.303 -70.002 1.00 20.72 ? 84 TRP A CE2 1 ATOM 565 C CE3 . TRP A 1 84 ? 24.706 -28.232 -70.750 1.00 21.02 ? 84 TRP A CE3 1 ATOM 566 C CZ2 . TRP A 1 84 ? 27.508 -28.007 -71.272 1.00 20.62 ? 84 TRP A CZ2 1 ATOM 567 C CZ3 . TRP A 1 84 ? 25.181 -27.954 -72.019 1.00 21.11 ? 84 TRP A CZ3 1 ATOM 568 C CH2 . TRP A 1 84 ? 26.560 -27.813 -72.273 1.00 21.20 ? 84 TRP A CH2 1 ATOM 569 N N . ASP A 1 85 ? 24.479 -27.458 -64.872 1.00 20.09 ? 85 ASP A N 1 ATOM 570 C CA . ASP A 1 85 ? 25.590 -27.330 -63.937 1.00 19.95 ? 85 ASP A CA 1 ATOM 571 C C . ASP A 1 85 ? 26.531 -28.503 -64.158 1.00 19.95 ? 85 ASP A C 1 ATOM 572 O O . ASP A 1 85 ? 27.758 -28.337 -64.200 1.00 20.02 ? 85 ASP A O 1 ATOM 573 C CB . ASP A 1 85 ? 25.106 -27.311 -62.482 1.00 20.75 ? 85 ASP A CB 1 ATOM 574 C CG . ASP A 1 85 ? 24.294 -26.059 -62.145 1.00 21.95 ? 85 ASP A CG 1 ATOM 575 O OD1 . ASP A 1 85 ? 24.605 -24.994 -62.728 1.00 21.82 ? 85 ASP A OD1 1 ATOM 576 O OD2 . ASP A 1 85 ? 23.364 -26.148 -61.286 1.00 21.92 ? 85 ASP A OD2 1 ATOM 577 N N . LEU A 1 86 ? 25.970 -29.690 -64.314 1.00 19.42 ? 86 LEU A N 1 ATOM 578 C CA . LEU A 1 86 ? 26.768 -30.893 -64.547 1.00 19.50 ? 86 LEU A CA 1 ATOM 579 C C . LEU A 1 86 ? 26.189 -31.731 -65.652 1.00 19.66 ? 86 LEU A C 1 ATOM 580 O O . LEU A 1 86 ? 25.080 -32.219 -65.551 1.00 20.92 ? 86 LEU A O 1 ATOM 581 C CB . LEU A 1 86 ? 26.891 -31.742 -63.264 1.00 19.44 ? 86 LEU A CB 1 ATOM 582 C CG . LEU A 1 86 ? 27.900 -32.906 -63.358 1.00 19.74 ? 86 LEU A CG 1 ATOM 583 C CD1 . LEU A 1 86 ? 29.333 -32.376 -63.553 1.00 19.61 ? 86 LEU A CD1 1 ATOM 584 C CD2 . LEU A 1 86 ? 27.816 -33.776 -62.124 1.00 19.60 ? 86 LEU A CD2 1 ATOM 585 N N . PHE A 1 87 ? 26.968 -31.897 -66.710 1.00 20.44 ? 87 PHE A N 1 ATOM 586 C CA . PHE A 1 87 ? 26.656 -32.793 -67.801 1.00 20.97 ? 87 PHE A CA 1 ATOM 587 C C . PHE A 1 87 ? 27.212 -34.168 -67.453 1.00 21.17 ? 87 PHE A C 1 ATOM 588 O O . PHE A 1 87 ? 28.402 -34.301 -67.125 1.00 21.25 ? 87 PHE A O 1 ATOM 589 C CB . PHE A 1 87 ? 27.257 -32.269 -69.100 1.00 21.35 ? 87 PHE A CB 1 ATOM 590 C CG . PHE A 1 87 ? 26.750 -32.979 -70.332 1.00 22.89 ? 87 PHE A CG 1 ATOM 591 C CD1 . PHE A 1 87 ? 27.143 -34.279 -70.617 1.00 22.63 ? 87 PHE A CD1 1 ATOM 592 C CD2 . PHE A 1 87 ? 25.836 -32.349 -71.190 1.00 23.59 ? 87 PHE A CD2 1 ATOM 593 C CE1 . PHE A 1 87 ? 26.670 -34.930 -71.756 1.00 24.06 ? 87 PHE A CE1 1 ATOM 594 C CE2 . PHE A 1 87 ? 25.361 -32.994 -72.326 1.00 24.21 ? 87 PHE A CE2 1 ATOM 595 C CZ . PHE A 1 87 ? 25.781 -34.289 -72.608 1.00 24.36 ? 87 PHE A CZ 1 ATOM 596 N N . VAL A 1 88 ? 26.363 -35.192 -67.494 1.00 21.36 ? 88 VAL A N 1 ATOM 597 C CA . VAL A 1 88 ? 26.799 -36.543 -67.132 1.00 22.30 ? 88 VAL A CA 1 ATOM 598 C C . VAL A 1 88 ? 26.881 -37.394 -68.384 1.00 23.37 ? 88 VAL A C 1 ATOM 599 O O . VAL A 1 88 ? 25.858 -37.622 -69.040 1.00 24.09 ? 88 VAL A O 1 ATOM 600 C CB . VAL A 1 88 ? 25.867 -37.203 -66.081 1.00 22.22 ? 88 VAL A CB 1 ATOM 601 C CG1 . VAL A 1 88 ? 26.301 -38.649 -65.783 1.00 23.19 ? 88 VAL A CG1 1 ATOM 602 C CG2 . VAL A 1 88 ? 25.802 -36.360 -64.816 1.00 21.97 ? 88 VAL A CG2 1 ATOM 603 N N . GLU A 1 89 ? 28.094 -37.850 -68.705 1.00 24.27 ? 89 GLU A N 1 ATOM 604 C CA . GLU A 1 89 ? 28.351 -38.690 -69.884 1.00 25.70 ? 89 GLU A CA 1 ATOM 605 C C . GLU A 1 89 ? 28.421 -40.148 -69.478 1.00 25.54 ? 89 GLU A C 1 ATOM 606 O O . GLU A 1 89 ? 29.173 -40.495 -68.554 1.00 24.43 ? 89 GLU A O 1 ATOM 607 C CB . GLU A 1 89 ? 29.705 -38.353 -70.541 1.00 26.49 ? 89 GLU A CB 1 ATOM 608 C CG . GLU A 1 89 ? 29.657 -37.128 -71.405 1.00 28.00 ? 89 GLU A CG 1 ATOM 609 C CD . GLU A 1 89 ? 30.910 -36.886 -72.262 1.00 27.57 ? 89 GLU A CD 1 ATOM 610 O OE1 . GLU A 1 89 ? 32.047 -37.246 -71.864 1.00 26.56 ? 89 GLU A OE1 1 ATOM 611 O OE2 . GLU A 1 89 ? 30.735 -36.270 -73.324 1.00 26.74 ? 89 GLU A OE2 1 ATOM 612 N N . ARG A 1 90 ? 27.692 -40.982 -70.212 1.00 25.83 ? 90 ARG A N 1 ATOM 613 C CA . ARG A 1 90 ? 27.549 -42.402 -69.911 1.00 27.37 ? 90 ARG A CA 1 ATOM 614 C C . ARG A 1 90 ? 28.512 -43.208 -70.746 1.00 28.15 ? 90 ARG A C 1 ATOM 615 O O . ARG A 1 90 ? 28.760 -42.866 -71.902 1.00 27.96 ? 90 ARG A O 1 ATOM 616 C CB . ARG A 1 90 ? 26.119 -42.885 -70.225 1.00 27.47 ? 90 ARG A CB 1 ATOM 617 C CG . ARG A 1 90 ? 24.990 -42.010 -69.678 1.00 27.99 ? 90 ARG A CG 1 ATOM 618 C CD . ARG A 1 90 ? 25.210 -41.672 -68.216 1.00 27.84 ? 90 ARG A CD 1 ATOM 619 N NE . ARG A 1 90 ? 23.996 -41.347 -67.470 1.00 26.69 ? 90 ARG A NE 1 ATOM 620 C CZ . ARG A 1 90 ? 23.881 -41.496 -66.159 1.00 26.45 ? 90 ARG A CZ 1 ATOM 621 N NH1 . ARG A 1 90 ? 24.887 -41.978 -65.441 1.00 25.54 ? 90 ARG A NH1 1 ATOM 622 N NH2 . ARG A 1 90 ? 22.746 -41.194 -65.554 1.00 26.46 ? 90 ARG A NH2 1 ATOM 623 N N . SER A 1 91 ? 28.999 -44.316 -70.196 1.00 28.99 ? 91 SER A N 1 ATOM 624 C CA . SER A 1 91 ? 29.915 -45.174 -70.946 1.00 31.31 ? 91 SER A CA 1 ATOM 625 C C . SER A 1 91 ? 29.243 -45.832 -72.159 1.00 32.20 ? 91 SER A C 1 ATOM 626 O O . SER A 1 91 ? 29.917 -46.144 -73.122 1.00 34.10 ? 91 SER A O 1 ATOM 627 C CB . SER A 1 91 ? 30.539 -46.236 -70.041 1.00 31.93 ? 91 SER A CB 1 ATOM 628 O OG . SER A 1 91 ? 29.550 -47.139 -69.633 1.00 32.36 ? 91 SER A OG 1 ATOM 629 N N . LYS A 1 92 ? 27.926 -46.011 -72.134 1.00 33.31 ? 92 LYS A N 1 ATOM 630 C CA . LYS A 1 92 ? 27.195 -46.592 -73.289 1.00 35.84 ? 92 LYS A CA 1 ATOM 631 C C . LYS A 1 92 ? 27.086 -45.625 -74.476 1.00 33.81 ? 92 LYS A C 1 ATOM 632 O O . LYS A 1 92 ? 26.603 -45.998 -75.546 1.00 33.20 ? 92 LYS A O 1 ATOM 633 C CB . LYS A 1 92 ? 25.769 -46.990 -72.875 1.00 38.44 ? 92 LYS A CB 1 ATOM 634 C CG . LYS A 1 92 ? 24.818 -45.796 -72.701 1.00 41.47 ? 92 LYS A CG 1 ATOM 635 C CD . LYS A 1 92 ? 23.521 -46.158 -71.988 1.00 45.30 ? 92 LYS A CD 1 ATOM 636 C CE . LYS A 1 92 ? 22.592 -44.949 -71.881 1.00 47.70 ? 92 LYS A CE 1 ATOM 637 N NZ . LYS A 1 92 ? 21.172 -45.324 -71.622 1.00 47.75 ? 92 LYS A NZ 1 ATOM 638 N N . ALA A 1 93 ? 27.482 -44.370 -74.283 1.00 32.25 ? 93 ALA A N 1 ATOM 639 C CA . ALA A 1 93 ? 27.229 -43.342 -75.294 1.00 31.31 ? 93 ALA A CA 1 ATOM 640 C C . ALA A 1 93 ? 27.915 -43.730 -76.612 1.00 31.77 ? 93 ALA A C 1 ATOM 641 O O . ALA A 1 93 ? 29.002 -44.309 -76.613 1.00 31.21 ? 93 ALA A O 1 ATOM 642 C CB . ALA A 1 93 ? 27.706 -41.976 -74.812 1.00 30.45 ? 93 ALA A CB 1 ATOM 643 N N . TYR A 1 94 ? 27.272 -43.419 -77.728 1.00 31.64 ? 94 TYR A N 1 ATOM 644 C CA . TYR A 1 94 ? 27.846 -43.742 -79.041 1.00 33.47 ? 94 TYR A CA 1 ATOM 645 C C . TYR A 1 94 ? 27.418 -42.734 -80.097 1.00 33.04 ? 94 TYR A C 1 ATOM 646 O O . TYR A 1 94 ? 26.339 -42.164 -80.014 1.00 31.04 ? 94 TYR A O 1 ATOM 647 C CB . TYR A 1 94 ? 27.451 -45.161 -79.472 1.00 35.22 ? 94 TYR A CB 1 ATOM 648 C CG . TYR A 1 94 ? 25.958 -45.366 -79.649 1.00 35.93 ? 94 TYR A CG 1 ATOM 649 C CD1 . TYR A 1 94 ? 25.148 -45.691 -78.568 1.00 37.12 ? 94 TYR A CD1 1 ATOM 650 C CD2 . TYR A 1 94 ? 25.364 -45.242 -80.899 1.00 38.36 ? 94 TYR A CD2 1 ATOM 651 C CE1 . TYR A 1 94 ? 23.786 -45.894 -78.717 1.00 38.41 ? 94 TYR A CE1 1 ATOM 652 C CE2 . TYR A 1 94 ? 23.999 -45.427 -81.068 1.00 39.96 ? 94 TYR A CE2 1 ATOM 653 C CZ . TYR A 1 94 ? 23.211 -45.755 -79.969 1.00 40.68 ? 94 TYR A CZ 1 ATOM 654 O OH . TYR A 1 94 ? 21.853 -45.935 -80.125 1.00 41.73 ? 94 TYR A OH 1 ATOM 655 N N . SER A 1 95 ? 28.277 -42.515 -81.086 1.00 34.53 ? 95 SER A N 1 ATOM 656 C CA . SER A 1 95 ? 27.970 -41.617 -82.195 1.00 35.11 ? 95 SER A CA 1 ATOM 657 C C . SER A 1 95 ? 27.191 -42.344 -83.278 1.00 35.98 ? 95 SER A C 1 ATOM 658 O O . SER A 1 95 ? 27.460 -43.510 -83.574 1.00 36.08 ? 95 SER A O 1 ATOM 659 C CB . SER A 1 95 ? 29.253 -41.044 -82.788 1.00 36.51 ? 95 SER A CB 1 ATOM 660 O OG . SER A 1 95 ? 29.930 -40.256 -81.830 1.00 36.81 ? 95 SER A OG 1 ATOM 661 N N . ASN A 1 96 ? 26.214 -41.658 -83.867 1.00 35.72 ? 96 ASN A N 1 ATOM 662 C CA . ASN A 1 96 ? 25.347 -42.296 -84.861 1.00 37.46 ? 96 ASN A CA 1 ATOM 663 C C . ASN A 1 96 ? 25.084 -41.395 -86.078 1.00 35.82 ? 96 ASN A C 1 ATOM 664 O O . ASN A 1 96 ? 23.985 -41.356 -86.628 1.00 35.95 ? 96 ASN A O 1 ATOM 665 C CB . ASN A 1 96 ? 24.038 -42.737 -84.192 1.00 39.01 ? 96 ASN A CB 1 ATOM 666 C CG . ASN A 1 96 ? 23.374 -43.895 -84.913 1.00 41.22 ? 96 ASN A CG 1 ATOM 667 O OD1 . ASN A 1 96 ? 24.041 -44.684 -85.591 1.00 43.59 ? 96 ASN A OD1 1 ATOM 668 N ND2 . ASN A 1 96 ? 22.058 -44.009 -84.769 1.00 40.61 ? 96 ASN A ND2 1 ATOM 669 N N . CYS A 1 97 ? 26.115 -40.674 -86.500 1.00 35.31 ? 97 CYS A N 1 ATOM 670 C CA . CYS A 1 97 ? 26.013 -39.766 -87.629 1.00 35.43 ? 97 CYS A CA 1 ATOM 671 C C . CYS A 1 97 ? 27.275 -39.981 -88.447 1.00 33.68 ? 97 CYS A C 1 ATOM 672 O O . CYS A 1 97 ? 27.838 -41.085 -88.436 1.00 33.31 ? 97 CYS A O 1 ATOM 673 C CB . CYS A 1 97 ? 25.814 -38.334 -87.110 1.00 37.37 ? 97 CYS A CB 1 ATOM 674 S SG . CYS A 1 97 ? 25.323 -37.022 -88.282 1.00 41.39 ? 97 CYS A SG 1 ATOM 675 N N . TYR A 1 98 ? 27.743 -38.963 -89.147 1.00 34.23 ? 98 TYR A N 1 ATOM 676 C CA . TYR A 1 98 ? 28.929 -39.125 -89.996 1.00 34.64 ? 98 TYR A CA 1 ATOM 677 C C . TYR A 1 98 ? 30.170 -39.289 -89.125 1.00 34.26 ? 98 TYR A C 1 ATOM 678 O O . TYR A 1 98 ? 30.283 -38.597 -88.105 1.00 33.71 ? 98 TYR A O 1 ATOM 679 C CB . TYR A 1 98 ? 29.073 -37.907 -90.894 1.00 35.74 ? 98 TYR A CB 1 ATOM 680 C CG . TYR A 1 98 ? 29.716 -38.168 -92.227 1.00 35.69 ? 98 TYR A CG 1 ATOM 681 C CD1 . TYR A 1 98 ? 28.938 -38.503 -93.334 1.00 36.68 ? 98 TYR A CD1 1 ATOM 682 C CD2 . TYR A 1 98 ? 31.089 -38.033 -92.399 1.00 35.34 ? 98 TYR A CD2 1 ATOM 683 C CE1 . TYR A 1 98 ? 29.512 -38.730 -94.573 1.00 36.39 ? 98 TYR A CE1 1 ATOM 684 C CE2 . TYR A 1 98 ? 31.674 -38.245 -93.637 1.00 36.38 ? 98 TYR A CE2 1 ATOM 685 C CZ . TYR A 1 98 ? 30.875 -38.598 -94.724 1.00 37.03 ? 98 TYR A CZ 1 ATOM 686 O OH . TYR A 1 98 ? 31.436 -38.807 -95.963 1.00 35.60 ? 98 TYR A OH 1 ATOM 687 N N . PRO A 1 99 ? 31.086 -40.214 -89.490 1.00 32.99 ? 99 PRO A N 1 ATOM 688 C CA . PRO A 1 99 ? 32.261 -40.372 -88.650 1.00 33.06 ? 99 PRO A CA 1 ATOM 689 C C . PRO A 1 99 ? 33.109 -39.101 -88.617 1.00 32.59 ? 99 PRO A C 1 ATOM 690 O O . PRO A 1 99 ? 33.310 -38.438 -89.642 1.00 30.89 ? 99 PRO A O 1 ATOM 691 C CB . PRO A 1 99 ? 33.031 -41.550 -89.281 1.00 34.47 ? 99 PRO A CB 1 ATOM 692 C CG . PRO A 1 99 ? 32.406 -41.777 -90.617 1.00 34.42 ? 99 PRO A CG 1 ATOM 693 C CD . PRO A 1 99 ? 31.005 -41.257 -90.530 1.00 33.95 ? 99 PRO A CD 1 ATOM 694 N N . TYR A 1 100 ? 33.549 -38.730 -87.426 1.00 31.21 ? 100 TYR A N 1 ATOM 695 C CA . TYR A 1 100 ? 34.305 -37.508 -87.279 1.00 30.51 ? 100 TYR A CA 1 ATOM 696 C C . TYR A 1 100 ? 35.409 -37.672 -86.251 1.00 30.43 ? 100 TYR A C 1 ATOM 697 O O . TYR A 1 100 ? 35.405 -38.610 -85.461 1.00 28.87 ? 100 TYR A O 1 ATOM 698 C CB . TYR A 1 100 ? 33.355 -36.359 -86.888 1.00 31.43 ? 100 TYR A CB 1 ATOM 699 C CG . TYR A 1 100 ? 32.821 -36.455 -85.475 1.00 31.67 ? 100 TYR A CG 1 ATOM 700 C CD1 . TYR A 1 100 ? 31.667 -37.168 -85.199 1.00 32.84 ? 100 TYR A CD1 1 ATOM 701 C CD2 . TYR A 1 100 ? 33.492 -35.845 -84.405 1.00 32.13 ? 100 TYR A CD2 1 ATOM 702 C CE1 . TYR A 1 100 ? 31.171 -37.272 -83.904 1.00 33.91 ? 100 TYR A CE1 1 ATOM 703 C CE2 . TYR A 1 100 ? 33.011 -35.949 -83.102 1.00 32.21 ? 100 TYR A CE2 1 ATOM 704 C CZ . TYR A 1 100 ? 31.847 -36.663 -82.852 1.00 33.30 ? 100 TYR A CZ 1 ATOM 705 O OH . TYR A 1 100 ? 31.341 -36.772 -81.571 1.00 32.78 ? 100 TYR A OH 1 ATOM 706 N N . ASP A 1 101 ? 36.377 -36.765 -86.304 1.00 31.08 ? 101 ASP A N 1 ATOM 707 C CA . ASP A 1 101 ? 37.318 -36.593 -85.212 1.00 31.94 ? 101 ASP A CA 1 ATOM 708 C C . ASP A 1 101 ? 37.456 -35.105 -84.917 1.00 29.75 ? 101 ASP A C 1 ATOM 709 O O . ASP A 1 101 ? 37.115 -34.263 -85.755 1.00 27.78 ? 101 ASP A O 1 ATOM 710 C CB . ASP A 1 101 ? 38.667 -37.207 -85.554 1.00 36.20 ? 101 ASP A CB 1 ATOM 711 C CG . ASP A 1 101 ? 39.190 -36.745 -86.888 1.00 40.82 ? 101 ASP A CG 1 ATOM 712 O OD1 . ASP A 1 101 ? 39.570 -35.560 -86.989 1.00 45.69 ? 101 ASP A OD1 1 ATOM 713 O OD2 . ASP A 1 101 ? 39.216 -37.570 -87.844 1.00 49.34 ? 101 ASP A OD2 1 ATOM 714 N N . VAL A 1 102 ? 37.952 -34.807 -83.725 1.00 27.71 ? 102 VAL A N 1 ATOM 715 C CA . VAL A 1 102 ? 38.195 -33.449 -83.275 1.00 27.02 ? 102 VAL A CA 1 ATOM 716 C C . VAL A 1 102 ? 39.643 -33.399 -82.808 1.00 28.11 ? 102 VAL A C 1 ATOM 717 O O . VAL A 1 102 ? 39.991 -33.953 -81.737 1.00 26.41 ? 102 VAL A O 1 ATOM 718 C CB . VAL A 1 102 ? 37.276 -33.052 -82.097 1.00 27.08 ? 102 VAL A CB 1 ATOM 719 C CG1 . VAL A 1 102 ? 37.416 -31.553 -81.780 1.00 25.78 ? 102 VAL A CG1 1 ATOM 720 C CG2 . VAL A 1 102 ? 35.814 -33.427 -82.401 1.00 26.54 ? 102 VAL A CG2 1 ATOM 721 N N . PRO A 1 103 ? 40.511 -32.752 -83.604 1.00 28.79 ? 103 PRO A N 1 ATOM 722 C CA . PRO A 1 103 ? 41.837 -32.497 -83.073 1.00 30.16 ? 103 PRO A CA 1 ATOM 723 C C . PRO A 1 103 ? 41.681 -31.691 -81.767 1.00 31.33 ? 103 PRO A C 1 ATOM 724 O O . PRO A 1 103 ? 40.900 -30.760 -81.719 1.00 36.06 ? 103 PRO A O 1 ATOM 725 C CB . PRO A 1 103 ? 42.517 -31.679 -84.184 1.00 30.27 ? 103 PRO A CB 1 ATOM 726 C CG . PRO A 1 103 ? 41.785 -32.058 -85.442 1.00 29.99 ? 103 PRO A CG 1 ATOM 727 C CD . PRO A 1 103 ? 40.366 -32.329 -85.015 1.00 29.53 ? 103 PRO A CD 1 ATOM 728 N N . ASP A 1 104 ? 42.375 -32.064 -80.711 1.00 32.96 ? 104 ASP A N 1 ATOM 729 C CA . ASP A 1 104 ? 42.106 -31.485 -79.360 1.00 32.90 ? 104 ASP A CA 1 ATOM 730 C C . ASP A 1 104 ? 40.626 -31.574 -78.917 1.00 29.30 ? 104 ASP A C 1 ATOM 731 O O . ASP A 1 104 ? 40.048 -30.630 -78.356 1.00 27.54 ? 104 ASP A O 1 ATOM 732 C CB . ASP A 1 104 ? 42.613 -30.040 -79.230 1.00 36.01 ? 104 ASP A CB 1 ATOM 733 C CG . ASP A 1 104 ? 43.092 -29.685 -77.776 1.00 41.20 ? 104 ASP A CG 1 ATOM 734 O OD1 . ASP A 1 104 ? 43.061 -30.531 -76.791 1.00 41.85 ? 104 ASP A OD1 1 ATOM 735 O OD2 . ASP A 1 104 ? 43.534 -28.517 -77.621 1.00 46.09 ? 104 ASP A OD2 1 ATOM 736 N N . TYR A 1 105 ? 40.055 -32.748 -79.128 1.00 26.74 ? 105 TYR A N 1 ATOM 737 C CA . TYR A 1 105 ? 38.761 -33.130 -78.573 1.00 25.42 ? 105 TYR A CA 1 ATOM 738 C C . TYR A 1 105 ? 38.631 -32.754 -77.093 1.00 23.96 ? 105 TYR A C 1 ATOM 739 O O . TYR A 1 105 ? 37.634 -32.150 -76.689 1.00 23.67 ? 105 TYR A O 1 ATOM 740 C CB . TYR A 1 105 ? 38.599 -34.649 -78.735 1.00 25.82 ? 105 TYR A CB 1 ATOM 741 C CG . TYR A 1 105 ? 37.250 -35.194 -78.306 1.00 26.57 ? 105 TYR A CG 1 ATOM 742 C CD1 . TYR A 1 105 ? 37.000 -35.515 -76.974 1.00 26.37 ? 105 TYR A CD1 1 ATOM 743 C CD2 . TYR A 1 105 ? 36.232 -35.406 -79.232 1.00 26.32 ? 105 TYR A CD2 1 ATOM 744 C CE1 . TYR A 1 105 ? 35.759 -36.016 -76.573 1.00 26.51 ? 105 TYR A CE1 1 ATOM 745 C CE2 . TYR A 1 105 ? 34.994 -35.911 -78.836 1.00 27.26 ? 105 TYR A CE2 1 ATOM 746 C CZ . TYR A 1 105 ? 34.767 -36.207 -77.496 1.00 26.78 ? 105 TYR A CZ 1 ATOM 747 O OH . TYR A 1 105 ? 33.549 -36.726 -77.081 1.00 28.18 ? 105 TYR A OH 1 ATOM 748 N N . ALA A 1 106 ? 39.640 -33.086 -76.291 1.00 23.53 ? 106 ALA A N 1 ATOM 749 C CA . ALA A 1 106 ? 39.567 -32.860 -74.841 1.00 22.70 ? 106 ALA A CA 1 ATOM 750 C C . ALA A 1 106 ? 39.377 -31.395 -74.498 1.00 22.69 ? 106 ALA A C 1 ATOM 751 O O . ALA A 1 106 ? 38.638 -31.094 -73.585 1.00 21.66 ? 106 ALA A O 1 ATOM 752 C CB . ALA A 1 106 ? 40.798 -33.396 -74.099 1.00 22.34 ? 106 ALA A CB 1 ATOM 753 N N . SER A 1 107 ? 40.033 -30.498 -75.232 1.00 22.61 ? 107 SER A N 1 ATOM 754 C CA . SER A 1 107 ? 39.858 -29.068 -74.990 1.00 22.88 ? 107 SER A CA 1 ATOM 755 C C . SER A 1 107 ? 38.492 -28.538 -75.394 1.00 22.29 ? 107 SER A C 1 ATOM 756 O O . SER A 1 107 ? 37.907 -27.729 -74.679 1.00 22.19 ? 107 SER A O 1 ATOM 757 C CB . SER A 1 107 ? 40.980 -28.265 -75.652 1.00 23.53 ? 107 SER A CB 1 ATOM 758 O OG . SER A 1 107 ? 42.184 -28.440 -74.901 1.00 23.61 ? 107 SER A OG 1 ATOM 759 N N . LEU A 1 108 ? 37.957 -28.988 -76.516 1.00 22.06 ? 108 LEU A N 1 ATOM 760 C CA . LEU A 1 108 ? 36.636 -28.498 -76.937 1.00 22.08 ? 108 LEU A CA 1 ATOM 761 C C . LEU A 1 108 ? 35.576 -29.008 -75.955 1.00 21.35 ? 108 LEU A C 1 ATOM 762 O O . LEU A 1 108 ? 34.671 -28.263 -75.525 1.00 20.91 ? 108 LEU A O 1 ATOM 763 C CB . LEU A 1 108 ? 36.302 -28.947 -78.355 1.00 22.06 ? 108 LEU A CB 1 ATOM 764 C CG . LEU A 1 108 ? 34.925 -28.510 -78.899 1.00 22.49 ? 108 LEU A CG 1 ATOM 765 C CD1 . LEU A 1 108 ? 34.749 -26.998 -78.865 1.00 22.05 ? 108 LEU A CD1 1 ATOM 766 C CD2 . LEU A 1 108 ? 34.683 -29.071 -80.295 1.00 22.48 ? 108 LEU A CD2 1 ATOM 767 N N . ARG A 1 109 ? 35.704 -30.278 -75.584 1.00 20.70 ? 109 ARG A N 1 ATOM 768 C CA . ARG A 1 109 ? 34.816 -30.856 -74.582 1.00 20.64 ? 109 ARG A CA 1 ATOM 769 C C . ARG A 1 109 ? 34.847 -30.059 -73.273 1.00 20.44 ? 109 ARG A C 1 ATOM 770 O O . ARG A 1 109 ? 33.803 -29.735 -72.706 1.00 19.42 ? 109 ARG A O 1 ATOM 771 C CB . ARG A 1 109 ? 35.154 -32.327 -74.359 1.00 20.73 ? 109 ARG A CB 1 ATOM 772 C CG . ARG A 1 109 ? 34.387 -33.006 -73.233 1.00 21.10 ? 109 ARG A CG 1 ATOM 773 C CD . ARG A 1 109 ? 34.732 -34.499 -73.199 1.00 21.26 ? 109 ARG A CD 1 ATOM 774 N NE . ARG A 1 109 ? 34.104 -35.223 -72.094 1.00 20.66 ? 109 ARG A NE 1 ATOM 775 C CZ . ARG A 1 109 ? 34.533 -35.242 -70.829 1.00 21.22 ? 109 ARG A CZ 1 ATOM 776 N NH1 . ARG A 1 109 ? 35.598 -34.567 -70.448 1.00 20.99 ? 109 ARG A NH1 1 ATOM 777 N NH2 . ARG A 1 109 ? 33.875 -35.959 -69.917 1.00 20.96 ? 109 ARG A NH2 1 ATOM 778 N N . SER A 1 110 ? 36.049 -29.745 -72.809 1.00 20.89 ? 110 SER A N 1 ATOM 779 C CA . SER A 1 110 ? 36.241 -28.981 -71.591 1.00 21.43 ? 110 SER A CA 1 ATOM 780 C C . SER A 1 110 ? 35.676 -27.560 -71.670 1.00 21.79 ? 110 SER A C 1 ATOM 781 O O . SER A 1 110 ? 35.045 -27.086 -70.729 1.00 21.60 ? 110 SER A O 1 ATOM 782 C CB . SER A 1 110 ? 37.721 -28.879 -71.231 1.00 21.96 ? 110 SER A CB 1 ATOM 783 O OG . SER A 1 110 ? 37.871 -28.052 -70.073 1.00 22.61 ? 110 SER A OG 1 ATOM 784 N N . LEU A 1 111 ? 35.947 -26.858 -72.751 1.00 21.90 ? 111 LEU A N 1 ATOM 785 C CA . LEU A 1 111 ? 35.469 -25.481 -72.840 1.00 22.77 ? 111 LEU A CA 1 ATOM 786 C C . LEU A 1 111 ? 33.947 -25.409 -72.957 1.00 21.74 ? 111 LEU A C 1 ATOM 787 O O . LEU A 1 111 ? 33.344 -24.532 -72.329 1.00 22.13 ? 111 LEU A O 1 ATOM 788 C CB . LEU A 1 111 ? 36.185 -24.690 -73.923 1.00 23.52 ? 111 LEU A CB 1 ATOM 789 C CG . LEU A 1 111 ? 35.910 -24.931 -75.373 1.00 24.19 ? 111 LEU A CG 1 ATOM 790 C CD1 . LEU A 1 111 ? 34.731 -24.052 -75.762 1.00 25.26 ? 111 LEU A CD1 1 ATOM 791 C CD2 . LEU A 1 111 ? 37.153 -24.578 -76.187 1.00 25.19 ? 111 LEU A CD2 1 ATOM 792 N N . VAL A 1 112 ? 33.325 -26.333 -73.682 1.00 21.16 ? 112 VAL A N 1 ATOM 793 C CA . VAL A 1 112 ? 31.842 -26.372 -73.740 1.00 21.87 ? 112 VAL A CA 1 ATOM 794 C C . VAL A 1 112 ? 31.256 -26.789 -72.376 1.00 21.32 ? 112 VAL A C 1 ATOM 795 O O . VAL A 1 112 ? 30.289 -26.188 -71.882 1.00 21.18 ? 112 VAL A O 1 ATOM 796 C CB . VAL A 1 112 ? 31.313 -27.263 -74.889 1.00 21.75 ? 112 VAL A CB 1 ATOM 797 C CG1 . VAL A 1 112 ? 29.775 -27.261 -74.898 1.00 22.54 ? 112 VAL A CG1 1 ATOM 798 C CG2 . VAL A 1 112 ? 31.842 -26.761 -76.252 1.00 22.05 ? 112 VAL A CG2 1 ATOM 799 N N . ALA A 1 113 ? 31.877 -27.787 -71.739 1.00 20.67 ? 113 ALA A N 1 ATOM 800 C CA . ALA A 1 113 ? 31.422 -28.256 -70.428 1.00 20.55 ? 113 ALA A CA 1 ATOM 801 C C . ALA A 1 113 ? 31.402 -27.142 -69.403 1.00 20.63 ? 113 ALA A C 1 ATOM 802 O O . ALA A 1 113 ? 30.426 -27.014 -68.650 1.00 20.51 ? 113 ALA A O 1 ATOM 803 C CB . ALA A 1 113 ? 32.311 -29.407 -69.910 1.00 19.48 ? 113 ALA A CB 1 ATOM 804 N N . SER A 1 114 ? 32.492 -26.369 -69.374 1.00 20.36 ? 114 SER A N 1 ATOM 805 C CA . SER A 1 114 ? 32.673 -25.267 -68.443 1.00 22.36 ? 114 SER A CA 1 ATOM 806 C C . SER A 1 114 ? 31.722 -24.100 -68.720 1.00 22.60 ? 114 SER A C 1 ATOM 807 O O . SER A 1 114 ? 31.276 -23.427 -67.778 1.00 24.74 ? 114 SER A O 1 ATOM 808 C CB . SER A 1 114 ? 34.124 -24.757 -68.470 1.00 22.80 ? 114 SER A CB 1 ATOM 809 O OG . SER A 1 114 ? 34.276 -23.701 -67.537 1.00 26.32 ? 114 SER A OG 1 ATOM 810 N N . SER A 1 115 ? 31.437 -23.858 -69.996 1.00 22.52 ? 115 SER A N 1 ATOM 811 C CA . SER A 1 115 ? 30.460 -22.849 -70.401 1.00 23.48 ? 115 SER A CA 1 ATOM 812 C C . SER A 1 115 ? 29.030 -23.204 -69.942 1.00 22.94 ? 115 SER A C 1 ATOM 813 O O . SER A 1 115 ? 28.265 -22.323 -69.510 1.00 24.64 ? 115 SER A O 1 ATOM 814 C CB . SER A 1 115 ? 30.574 -22.603 -71.914 1.00 23.94 ? 115 SER A CB 1 ATOM 815 O OG . SER A 1 115 ? 29.509 -21.854 -72.454 1.00 25.40 ? 115 SER A OG 1 ATOM 816 N N . GLY A 1 116 ? 28.672 -24.478 -69.990 1.00 22.17 ? 116 GLY A N 1 ATOM 817 C CA . GLY A 1 116 ? 27.406 -24.935 -69.390 1.00 21.95 ? 116 GLY A CA 1 ATOM 818 C C . GLY A 1 116 ? 26.166 -24.655 -70.214 1.00 22.06 ? 116 GLY A C 1 ATOM 819 O O . GLY A 1 116 ? 25.061 -24.648 -69.680 1.00 21.51 ? 116 GLY A O 1 ATOM 820 N N . THR A 1 117 ? 26.334 -24.438 -71.513 1.00 22.48 ? 117 THR A N 1 ATOM 821 C CA . THR A 1 117 ? 25.186 -24.143 -72.365 1.00 23.08 ? 117 THR A CA 1 ATOM 822 C C . THR A 1 117 ? 25.363 -24.631 -73.788 1.00 23.22 ? 117 THR A C 1 ATOM 823 O O . THR A 1 117 ? 26.453 -24.568 -74.359 1.00 22.94 ? 117 THR A O 1 ATOM 824 C CB . THR A 1 117 ? 24.842 -22.632 -72.383 1.00 23.83 ? 117 THR A CB 1 ATOM 825 O OG1 . THR A 1 117 ? 23.679 -22.423 -73.207 1.00 24.21 ? 117 THR A OG1 1 ATOM 826 C CG2 . THR A 1 117 ? 26.024 -21.754 -72.891 1.00 24.07 ? 117 THR A CG2 1 ATOM 827 N N . LEU A 1 118 ? 24.271 -25.129 -74.354 1.00 23.61 ? 118 LEU A N 1 ATOM 828 C CA . LEU A 1 118 ? 24.228 -25.476 -75.759 1.00 24.01 ? 118 LEU A CA 1 ATOM 829 C C . LEU A 1 118 ? 23.405 -24.445 -76.549 1.00 24.64 ? 118 LEU A C 1 ATOM 830 O O . LEU A 1 118 ? 23.008 -24.712 -77.671 1.00 26.16 ? 118 LEU A O 1 ATOM 831 C CB . LEU A 1 118 ? 23.647 -26.871 -75.921 1.00 24.37 ? 118 LEU A CB 1 ATOM 832 C CG . LEU A 1 118 ? 24.608 -28.008 -75.644 1.00 23.83 ? 118 LEU A CG 1 ATOM 833 C CD1 . LEU A 1 118 ? 23.893 -29.344 -75.562 1.00 24.82 ? 118 LEU A CD1 1 ATOM 834 C CD2 . LEU A 1 118 ? 25.699 -28.050 -76.697 1.00 24.88 ? 118 LEU A CD2 1 ATOM 835 N N . GLU A 1 119 ? 23.175 -23.260 -75.980 1.00 25.81 ? 119 GLU A N 1 ATOM 836 C CA . GLU A 1 119 ? 22.404 -22.228 -76.703 1.00 26.71 ? 119 GLU A CA 1 ATOM 837 C C . GLU A 1 119 ? 23.071 -21.887 -78.028 1.00 26.70 ? 119 GLU A C 1 ATOM 838 O O . GLU A 1 119 ? 24.260 -21.550 -78.059 1.00 25.76 ? 119 GLU A O 1 ATOM 839 C CB . GLU A 1 119 ? 22.303 -20.939 -75.913 1.00 28.20 ? 119 GLU A CB 1 ATOM 840 C CG . GLU A 1 119 ? 21.474 -21.039 -74.666 1.00 30.44 ? 119 GLU A CG 1 ATOM 841 C CD . GLU A 1 119 ? 21.774 -19.886 -73.736 1.00 32.68 ? 119 GLU A CD 1 ATOM 842 O OE1 . GLU A 1 119 ? 22.800 -19.942 -72.981 1.00 30.87 ? 119 GLU A OE1 1 ATOM 843 O OE2 . GLU A 1 119 ? 21.002 -18.904 -73.815 1.00 32.34 ? 119 GLU A OE2 1 ATOM 844 N N . PHE A 1 120 ? 22.271 -21.916 -79.094 1.00 26.64 ? 120 PHE A N 1 ATOM 845 C CA . PHE A 1 120 ? 22.740 -21.759 -80.450 1.00 27.46 ? 120 PHE A CA 1 ATOM 846 C C . PHE A 1 120 ? 21.855 -20.731 -81.152 1.00 28.95 ? 120 PHE A C 1 ATOM 847 O O . PHE A 1 120 ? 20.638 -20.807 -81.064 1.00 29.93 ? 120 PHE A O 1 ATOM 848 C CB . PHE A 1 120 ? 22.651 -23.086 -81.190 1.00 26.77 ? 120 PHE A CB 1 ATOM 849 C CG . PHE A 1 120 ? 23.219 -23.047 -82.581 1.00 27.52 ? 120 PHE A CG 1 ATOM 850 C CD1 . PHE A 1 120 ? 24.573 -23.264 -82.799 1.00 27.59 ? 120 PHE A CD1 1 ATOM 851 C CD2 . PHE A 1 120 ? 22.397 -22.814 -83.678 1.00 27.59 ? 120 PHE A CD2 1 ATOM 852 C CE1 . PHE A 1 120 ? 25.105 -23.229 -84.078 1.00 28.57 ? 120 PHE A CE1 1 ATOM 853 C CE2 . PHE A 1 120 ? 22.919 -22.787 -84.956 1.00 28.41 ? 120 PHE A CE2 1 ATOM 854 C CZ . PHE A 1 120 ? 24.268 -22.996 -85.162 1.00 29.25 ? 120 PHE A CZ 1 ATOM 855 N N . ASN A 1 121 ? 22.488 -19.798 -81.847 1.00 29.91 ? 121 ASN A N 1 ATOM 856 C CA . ASN A 1 121 ? 21.782 -18.774 -82.612 1.00 33.18 ? 121 ASN A CA 1 ATOM 857 C C . ASN A 1 121 ? 22.108 -18.951 -84.085 1.00 33.27 ? 121 ASN A C 1 ATOM 858 O O . ASN A 1 121 ? 23.275 -18.897 -84.489 1.00 32.10 ? 121 ASN A O 1 ATOM 859 C CB . ASN A 1 121 ? 22.189 -17.377 -82.141 1.00 35.74 ? 121 ASN A CB 1 ATOM 860 C CG . ASN A 1 121 ? 21.515 -16.963 -80.839 1.00 39.84 ? 121 ASN A CG 1 ATOM 861 O OD1 . ASN A 1 121 ? 20.543 -17.576 -80.391 1.00 44.63 ? 121 ASN A OD1 1 ATOM 862 N ND2 . ASN A 1 121 ? 22.036 -15.904 -80.218 1.00 44.01 ? 121 ASN A ND2 1 ATOM 863 N N . ASN A 1 122 ? 21.078 -19.191 -84.889 1.00 34.35 ? 122 ASN A N 1 ATOM 864 C CA . ASN A 1 122 ? 21.253 -19.329 -86.333 1.00 35.18 ? 122 ASN A CA 1 ATOM 865 C C . ASN A 1 122 ? 21.649 -18.010 -86.953 1.00 34.53 ? 122 ASN A C 1 ATOM 866 O O . ASN A 1 122 ? 21.219 -16.953 -86.488 1.00 33.08 ? 122 ASN A O 1 ATOM 867 C CB . ASN A 1 122 ? 19.974 -19.867 -86.986 1.00 38.52 ? 122 ASN A CB 1 ATOM 868 C CG . ASN A 1 122 ? 19.776 -21.352 -86.724 1.00 39.95 ? 122 ASN A CG 1 ATOM 869 O OD1 . ASN A 1 122 ? 20.375 -22.196 -87.383 1.00 43.31 ? 122 ASN A OD1 1 ATOM 870 N ND2 . ASN A 1 122 ? 18.947 -21.672 -85.751 1.00 41.28 ? 122 ASN A ND2 1 ATOM 871 N N . GLU A 1 123 ? 22.480 -18.073 -87.993 1.00 34.43 ? 123 GLU A N 1 ATOM 872 C CA . GLU A 1 123 ? 22.850 -16.899 -88.765 1.00 35.46 ? 123 GLU A CA 1 ATOM 873 C C . GLU A 1 123 ? 22.736 -17.201 -90.252 1.00 36.48 ? 123 GLU A C 1 ATOM 874 O O . GLU A 1 123 ? 22.861 -18.354 -90.665 1.00 34.66 ? 123 GLU A O 1 ATOM 875 C CB . GLU A 1 123 ? 24.286 -16.461 -88.458 1.00 34.68 ? 123 GLU A CB 1 ATOM 876 C CG . GLU A 1 123 ? 24.507 -15.976 -87.033 1.00 34.33 ? 123 GLU A CG 1 ATOM 877 C CD . GLU A 1 123 ? 25.949 -15.569 -86.775 1.00 33.95 ? 123 GLU A CD 1 ATOM 878 O OE1 . GLU A 1 123 ? 26.864 -16.389 -87.045 1.00 33.07 ? 123 GLU A OE1 1 ATOM 879 O OE2 . GLU A 1 123 ? 26.160 -14.431 -86.301 1.00 33.72 ? 123 GLU A OE2 1 ATOM 880 N N . SER A 1 124 ? 22.526 -16.144 -91.042 1.00 38.73 ? 124 SER A N 1 ATOM 881 C CA . SER A 1 124 ? 22.329 -16.248 -92.498 1.00 39.76 ? 124 SER A CA 1 ATOM 882 C C . SER A 1 124 ? 23.628 -15.996 -93.223 1.00 40.08 ? 124 SER A C 1 ATOM 883 O O . SER A 1 124 ? 23.935 -14.866 -93.594 1.00 38.51 ? 124 SER A O 1 ATOM 884 C CB . SER A 1 124 ? 21.293 -15.224 -92.991 1.00 42.57 ? 124 SER A CB 1 ATOM 885 O OG . SER A 1 124 ? 20.100 -15.304 -92.229 1.00 45.42 ? 124 SER A OG 1 ATOM 886 N N . PHE A 1 125 ? 24.395 -17.058 -93.421 1.00 39.58 ? 125 PHE A N 1 ATOM 887 C CA . PHE A 1 125 ? 25.623 -16.968 -94.177 1.00 39.89 ? 125 PHE A CA 1 ATOM 888 C C . PHE A 1 125 ? 25.255 -16.866 -95.639 1.00 42.06 ? 125 PHE A C 1 ATOM 889 O O . PHE A 1 125 ? 24.259 -17.425 -96.062 1.00 44.16 ? 125 PHE A O 1 ATOM 890 C CB . PHE A 1 125 ? 26.495 -18.205 -93.947 1.00 39.22 ? 125 PHE A CB 1 ATOM 891 C CG . PHE A 1 125 ? 27.210 -18.190 -92.635 1.00 37.41 ? 125 PHE A CG 1 ATOM 892 C CD1 . PHE A 1 125 ? 26.585 -18.635 -91.485 1.00 37.61 ? 125 PHE A CD1 1 ATOM 893 C CD2 . PHE A 1 125 ? 28.498 -17.683 -92.544 1.00 37.91 ? 125 PHE A CD2 1 ATOM 894 C CE1 . PHE A 1 125 ? 27.239 -18.595 -90.267 1.00 36.26 ? 125 PHE A CE1 1 ATOM 895 C CE2 . PHE A 1 125 ? 29.163 -17.647 -91.327 1.00 38.16 ? 125 PHE A CE2 1 ATOM 896 C CZ . PHE A 1 125 ? 28.527 -18.097 -90.188 1.00 36.07 ? 125 PHE A CZ 1 ATOM 897 N N . ASN A 1 126 ? 26.060 -16.156 -96.407 1.00 42.10 ? 126 ASN A N 1 ATOM 898 C CA . ASN A 1 126 ? 25.792 -16.022 -97.823 1.00 45.28 ? 126 ASN A CA 1 ATOM 899 C C . ASN A 1 126 ? 26.505 -17.130 -98.599 1.00 43.65 ? 126 ASN A C 1 ATOM 900 O O . ASN A 1 126 ? 27.674 -16.984 -98.974 1.00 43.00 ? 126 ASN A O 1 ATOM 901 C CB . ASN A 1 126 ? 26.225 -14.633 -98.285 1.00 48.44 ? 126 ASN A CB 1 ATOM 902 C CG . ASN A 1 126 ? 25.771 -14.329 -99.687 1.00 50.94 ? 126 ASN A CG 1 ATOM 903 O OD1 . ASN A 1 126 ? 25.653 -15.229 -100.515 1.00 51.77 ? 126 ASN A OD1 1 ATOM 904 N ND2 . ASN A 1 126 ? 25.504 -13.058 -99.961 1.00 54.88 ? 126 ASN A ND2 1 ATOM 905 N N . TRP A 1 127 ? 25.799 -18.243 -98.816 1.00 42.16 ? 127 TRP A N 1 ATOM 906 C CA . TRP A 1 127 ? 26.330 -19.370 -99.588 1.00 42.47 ? 127 TRP A CA 1 ATOM 907 C C . TRP A 1 127 ? 25.858 -19.358 -101.014 1.00 45.08 ? 127 TRP A C 1 ATOM 908 O O . TRP A 1 127 ? 25.437 -20.382 -101.557 1.00 44.82 ? 127 TRP A O 1 ATOM 909 C CB . TRP A 1 127 ? 25.940 -20.703 -98.966 1.00 41.18 ? 127 TRP A CB 1 ATOM 910 C CG . TRP A 1 127 ? 26.366 -20.842 -97.526 1.00 39.25 ? 127 TRP A CG 1 ATOM 911 C CD1 . TRP A 1 127 ? 25.570 -21.180 -96.454 1.00 38.87 ? 127 TRP A CD1 1 ATOM 912 C CD2 . TRP A 1 127 ? 27.706 -20.632 -96.960 1.00 39.12 ? 127 TRP A CD2 1 ATOM 913 N NE1 . TRP A 1 127 ? 26.289 -21.207 -95.298 1.00 38.38 ? 127 TRP A NE1 1 ATOM 914 C CE2 . TRP A 1 127 ? 27.578 -20.890 -95.523 1.00 37.78 ? 127 TRP A CE2 1 ATOM 915 C CE3 . TRP A 1 127 ? 28.951 -20.280 -97.476 1.00 39.36 ? 127 TRP A CE3 1 ATOM 916 C CZ2 . TRP A 1 127 ? 28.655 -20.786 -94.655 1.00 38.09 ? 127 TRP A CZ2 1 ATOM 917 C CZ3 . TRP A 1 127 ? 30.042 -20.187 -96.591 1.00 39.80 ? 127 TRP A CZ3 1 ATOM 918 C CH2 . TRP A 1 127 ? 29.894 -20.430 -95.210 1.00 38.47 ? 127 TRP A CH2 1 ATOM 919 N N . THR A 1 128 ? 25.929 -18.202 -101.643 1.00 48.66 ? 128 THR A N 1 ATOM 920 C CA . THR A 1 128 ? 25.535 -18.095 -103.037 1.00 50.24 ? 128 THR A CA 1 ATOM 921 C C . THR A 1 128 ? 26.488 -18.918 -103.912 1.00 49.21 ? 128 THR A C 1 ATOM 922 O O . THR A 1 128 ? 27.709 -18.801 -103.797 1.00 49.21 ? 128 THR A O 1 ATOM 923 C CB . THR A 1 128 ? 25.506 -16.620 -103.478 1.00 54.69 ? 128 THR A CB 1 ATOM 924 O OG1 . THR A 1 128 ? 26.715 -15.972 -103.057 1.00 58.50 ? 128 THR A OG1 1 ATOM 925 C CG2 . THR A 1 128 ? 24.306 -15.904 -102.857 1.00 52.87 ? 128 THR A CG2 1 ATOM 926 N N . GLY A 1 129 ? 25.917 -19.780 -104.753 1.00 49.82 ? 129 GLY A N 1 ATOM 927 C CA . GLY A 1 129 ? 26.679 -20.511 -105.770 1.00 48.83 ? 129 GLY A CA 1 ATOM 928 C C . GLY A 1 129 ? 26.959 -21.969 -105.460 1.00 46.86 ? 129 GLY A C 1 ATOM 929 O O . GLY A 1 129 ? 27.551 -22.667 -106.280 1.00 45.90 ? 129 GLY A O 1 ATOM 930 N N . VAL A 1 130 ? 26.554 -22.435 -104.276 1.00 44.80 ? 130 VAL A N 1 ATOM 931 C CA . VAL A 1 130 ? 26.712 -23.840 -103.910 1.00 43.31 ? 130 VAL A CA 1 ATOM 932 C C . VAL A 1 130 ? 25.382 -24.420 -103.450 1.00 42.45 ? 130 VAL A C 1 ATOM 933 O O . VAL A 1 130 ? 24.435 -23.675 -103.203 1.00 41.12 ? 130 VAL A O 1 ATOM 934 C CB . VAL A 1 130 ? 27.766 -24.028 -102.785 1.00 42.41 ? 130 VAL A CB 1 ATOM 935 C CG1 . VAL A 1 130 ? 29.138 -23.547 -103.260 1.00 42.76 ? 130 VAL A CG1 1 ATOM 936 C CG2 . VAL A 1 130 ? 27.322 -23.318 -101.504 1.00 41.24 ? 130 VAL A CG2 1 ATOM 937 N N . THR A 1 131 ? 25.324 -25.749 -103.349 1.00 40.61 ? 131 THR A N 1 ATOM 938 C CA . THR A 1 131 ? 24.153 -26.444 -102.822 1.00 41.24 ? 131 THR A CA 1 ATOM 939 C C . THR A 1 131 ? 24.344 -26.625 -101.311 1.00 40.12 ? 131 THR A C 1 ATOM 940 O O . THR A 1 131 ? 25.427 -27.014 -100.860 1.00 38.28 ? 131 THR A O 1 ATOM 941 C CB . THR A 1 131 ? 23.956 -27.826 -103.478 1.00 42.15 ? 131 THR A CB 1 ATOM 942 O OG1 . THR A 1 131 ? 23.905 -27.684 -104.903 1.00 43.09 ? 131 THR A OG1 1 ATOM 943 C CG2 . THR A 1 131 ? 22.662 -28.480 -103.009 1.00 43.24 ? 131 THR A CG2 1 ATOM 944 N N . GLN A 1 132 ? 23.292 -26.349 -100.548 1.00 39.86 ? 132 GLN A N 1 ATOM 945 C CA . GLN A 1 132 ? 23.344 -26.430 -99.094 1.00 39.98 ? 132 GLN A CA 1 ATOM 946 C C . GLN A 1 132 ? 22.679 -27.717 -98.656 1.00 40.35 ? 132 GLN A C 1 ATOM 947 O O . GLN A 1 132 ? 22.076 -28.416 -99.472 1.00 38.61 ? 132 GLN A O 1 ATOM 948 C CB . GLN A 1 132 ? 22.622 -25.235 -98.455 1.00 40.38 ? 132 GLN A CB 1 ATOM 949 C CG . GLN A 1 132 ? 23.249 -23.886 -98.761 1.00 40.65 ? 132 GLN A CG 1 ATOM 950 C CD . GLN A 1 132 ? 22.634 -22.751 -97.956 1.00 41.98 ? 132 GLN A CD 1 ATOM 951 O OE1 . GLN A 1 132 ? 22.502 -22.836 -96.726 1.00 42.12 ? 132 GLN A OE1 1 ATOM 952 N NE2 . GLN A 1 132 ? 22.268 -21.675 -98.640 1.00 40.73 ? 132 GLN A NE2 1 ATOM 953 N N . ASN A 1 133 ? 22.800 -28.014 -97.363 1.00 38.41 ? 133 ASN A N 1 ATOM 954 C CA . ASN A 1 133 ? 22.058 -29.084 -96.710 1.00 39.33 ? 133 ASN A CA 1 ATOM 955 C C . ASN A 1 133 ? 22.355 -30.494 -97.217 1.00 38.52 ? 133 ASN A C 1 ATOM 956 O O . ASN A 1 133 ? 21.459 -31.339 -97.288 1.00 37.38 ? 133 ASN A O 1 ATOM 957 C CB . ASN A 1 133 ? 20.552 -28.799 -96.774 1.00 42.71 ? 133 ASN A CB 1 ATOM 958 C CG . ASN A 1 133 ? 20.152 -27.579 -95.974 1.00 47.77 ? 133 ASN A CG 1 ATOM 959 O OD1 . ASN A 1 133 ? 20.966 -26.986 -95.255 1.00 44.38 ? 133 ASN A OD1 1 ATOM 960 N ND2 . ASN A 1 133 ? 18.882 -27.198 -96.081 1.00 56.22 ? 133 ASN A ND2 1 ATOM 961 N N . GLY A 1 134 ? 23.619 -30.773 -97.517 1.00 37.09 ? 134 GLY A N 1 ATOM 962 C CA . GLY A 1 134 ? 24.005 -32.133 -97.881 1.00 37.84 ? 134 GLY A CA 1 ATOM 963 C C . GLY A 1 134 ? 23.588 -33.105 -96.783 1.00 37.58 ? 134 GLY A C 1 ATOM 964 O O . GLY A 1 134 ? 23.621 -32.767 -95.584 1.00 36.05 ? 134 GLY A O 1 ATOM 965 N N . THR A 1 135 ? 23.184 -34.302 -97.194 1.00 36.94 ? 135 THR A N 1 ATOM 966 C CA . THR A 1 135 ? 22.741 -35.332 -96.271 1.00 38.83 ? 135 THR A CA 1 ATOM 967 C C . THR A 1 135 ? 23.478 -36.641 -96.542 1.00 39.06 ? 135 THR A C 1 ATOM 968 O O . THR A 1 135 ? 24.151 -36.780 -97.565 1.00 38.93 ? 135 THR A O 1 ATOM 969 C CB . THR A 1 135 ? 21.226 -35.575 -96.371 1.00 41.18 ? 135 THR A CB 1 ATOM 970 O OG1 . THR A 1 135 ? 20.902 -36.054 -97.679 1.00 41.07 ? 135 THR A OG1 1 ATOM 971 C CG2 . THR A 1 135 ? 20.436 -34.280 -96.089 1.00 41.69 ? 135 THR A CG2 1 ATOM 972 N N . SER A 1 136 ? 23.333 -37.584 -95.612 1.00 38.68 ? 136 SER A N 1 ATOM 973 C CA . SER A 1 136 ? 23.997 -38.875 -95.683 1.00 39.26 ? 136 SER A CA 1 ATOM 974 C C . SER A 1 136 ? 23.121 -39.966 -95.081 1.00 40.10 ? 136 SER A C 1 ATOM 975 O O . SER A 1 136 ? 22.403 -39.737 -94.097 1.00 39.48 ? 136 SER A O 1 ATOM 976 C CB . SER A 1 136 ? 25.338 -38.800 -94.941 1.00 38.52 ? 136 SER A CB 1 ATOM 977 O OG . SER A 1 136 ? 25.899 -40.080 -94.719 1.00 37.86 ? 136 SER A OG 1 ATOM 978 N N . SER A 1 137 ? 23.195 -41.164 -95.666 1.00 41.16 ? 137 SER A N 1 ATOM 979 C CA . SER A 1 137 ? 22.499 -42.340 -95.121 1.00 42.27 ? 137 SER A CA 1 ATOM 980 C C . SER A 1 137 ? 23.112 -42.817 -93.798 1.00 42.27 ? 137 SER A C 1 ATOM 981 O O . SER A 1 137 ? 22.476 -43.571 -93.061 1.00 40.41 ? 137 SER A O 1 ATOM 982 C CB . SER A 1 137 ? 22.506 -43.492 -96.133 1.00 44.42 ? 137 SER A CB 1 ATOM 983 O OG . SER A 1 137 ? 23.810 -44.018 -96.250 1.00 44.84 ? 137 SER A OG 1 ATOM 984 N N . ALA A 1 138 ? 24.336 -42.368 -93.503 1.00 41.61 ? 138 ALA A N 1 ATOM 985 C CA . ALA A 1 138 ? 24.990 -42.645 -92.213 1.00 42.94 ? 138 ALA A CA 1 ATOM 986 C C . ALA A 1 138 ? 24.437 -41.786 -91.058 1.00 42.70 ? 138 ALA A C 1 ATOM 987 O O . ALA A 1 138 ? 24.785 -42.001 -89.894 1.00 44.73 ? 138 ALA A O 1 ATOM 988 C CB . ALA A 1 138 ? 26.498 -42.440 -92.340 1.00 41.12 ? 138 ALA A CB 1 ATOM 989 N N . CYS A 1 139 ? 23.579 -40.821 -91.374 1.00 42.45 ? 139 CYS A N 1 ATOM 990 C CA . CYS A 1 139 ? 23.045 -39.919 -90.374 1.00 43.45 ? 139 CYS A CA 1 ATOM 991 C C . CYS A 1 139 ? 21.554 -39.728 -90.584 1.00 45.20 ? 139 CYS A C 1 ATOM 992 O O . CYS A 1 139 ? 21.129 -38.707 -91.095 1.00 48.14 ? 139 CYS A O 1 ATOM 993 C CB . CYS A 1 139 ? 23.793 -38.583 -90.438 1.00 43.76 ? 139 CYS A CB 1 ATOM 994 S SG . CYS A 1 139 ? 23.453 -37.469 -89.049 1.00 44.34 ? 139 CYS A SG 1 ATOM 995 N N . LYS A 1 140 ? 20.768 -40.723 -90.177 1.00 45.23 ? 140 LYS A N 1 ATOM 996 C CA . LYS A 1 140 ? 19.317 -40.696 -90.363 1.00 47.06 ? 140 LYS A CA 1 ATOM 997 C C . LYS A 1 140 ? 18.635 -39.851 -89.309 1.00 46.24 ? 140 LYS A C 1 ATOM 998 O O . LYS A 1 140 ? 18.944 -39.979 -88.122 1.00 45.01 ? 140 LYS A O 1 ATOM 999 C CB . LYS A 1 140 ? 18.726 -42.107 -90.258 1.00 48.04 ? 140 LYS A CB 1 ATOM 1000 C CG . LYS A 1 140 ? 19.293 -43.121 -91.231 1.00 48.66 ? 140 LYS A CG 1 ATOM 1001 C CD . LYS A 1 140 ? 18.746 -42.921 -92.624 1.00 49.11 ? 140 LYS A CD 1 ATOM 1002 C CE . LYS A 1 140 ? 18.932 -44.178 -93.448 1.00 50.38 ? 140 LYS A CE 1 ATOM 1003 N NZ . LYS A 1 140 ? 18.433 -43.959 -94.828 1.00 51.08 ? 140 LYS A NZ 1 ATOM 1004 N N . ARG A 1 141 ? 17.687 -39.019 -89.736 1.00 45.01 ? 141 ARG A N 1 ATOM 1005 C CA . ARG A 1 141 ? 16.806 -38.285 -88.820 1.00 47.33 ? 141 ARG A CA 1 ATOM 1006 C C . ARG A 1 141 ? 15.350 -38.554 -89.240 1.00 51.02 ? 141 ARG A C 1 ATOM 1007 O O . ARG A 1 141 ? 14.957 -38.236 -90.366 1.00 49.09 ? 141 ARG A O 1 ATOM 1008 C CB . ARG A 1 141 ? 17.121 -36.780 -88.852 1.00 45.47 ? 141 ARG A CB 1 ATOM 1009 C CG . ARG A 1 141 ? 16.206 -35.914 -87.996 1.00 45.35 ? 141 ARG A CG 1 ATOM 1010 C CD . ARG A 1 141 ? 16.684 -34.469 -87.954 1.00 44.65 ? 141 ARG A CD 1 ATOM 1011 N NE . ARG A 1 141 ? 17.755 -34.255 -86.966 1.00 42.77 ? 141 ARG A NE 1 ATOM 1012 C CZ . ARG A 1 141 ? 19.046 -34.032 -87.237 1.00 42.63 ? 141 ARG A CZ 1 ATOM 1013 N NH1 . ARG A 1 141 ? 19.508 -34.007 -88.489 1.00 42.59 ? 141 ARG A NH1 1 ATOM 1014 N NH2 . ARG A 1 141 ? 19.904 -33.838 -86.228 1.00 41.95 ? 141 ARG A NH2 1 ATOM 1015 N N . ARG A 1 142 ? 14.566 -39.155 -88.344 1.00 54.68 ? 142 ARG A N 1 ATOM 1016 C CA . ARG A 1 142 ? 13.191 -39.564 -88.662 1.00 58.57 ? 142 ARG A CA 1 ATOM 1017 C C . ARG A 1 142 ? 13.183 -40.375 -89.961 1.00 58.46 ? 142 ARG A C 1 ATOM 1018 O O . ARG A 1 142 ? 12.514 -40.011 -90.920 1.00 58.17 ? 142 ARG A O 1 ATOM 1019 C CB . ARG A 1 142 ? 12.268 -38.341 -88.783 1.00 61.92 ? 142 ARG A CB 1 ATOM 1020 C CG . ARG A 1 142 ? 12.155 -37.511 -87.510 1.00 65.74 ? 142 ARG A CG 1 ATOM 1021 C CD . ARG A 1 142 ? 11.364 -36.228 -87.743 1.00 70.17 ? 142 ARG A CD 1 ATOM 1022 N NE . ARG A 1 142 ? 12.214 -35.078 -88.078 1.00 73.51 ? 142 ARG A NE 1 ATOM 1023 C CZ . ARG A 1 142 ? 12.806 -34.274 -87.188 1.00 74.44 ? 142 ARG A CZ 1 ATOM 1024 N NH1 . ARG A 1 142 ? 12.669 -34.477 -85.880 1.00 72.33 ? 142 ARG A NH1 1 ATOM 1025 N NH2 . ARG A 1 142 ? 13.548 -33.252 -87.609 1.00 74.81 ? 142 ARG A NH2 1 ATOM 1026 N N . SER A 1 143 ? 13.983 -41.444 -89.981 1.00 58.93 ? 143 SER A N 1 ATOM 1027 C CA . SER A 1 143 ? 14.084 -42.386 -91.114 1.00 58.96 ? 143 SER A CA 1 ATOM 1028 C C . SER A 1 143 ? 14.539 -41.804 -92.467 1.00 57.76 ? 143 SER A C 1 ATOM 1029 O O . SER A 1 143 ? 14.536 -42.514 -93.478 1.00 61.70 ? 143 SER A O 1 ATOM 1030 C CB . SER A 1 143 ? 12.770 -43.161 -91.279 1.00 61.26 ? 143 SER A CB 1 ATOM 1031 O OG . SER A 1 143 ? 12.645 -44.129 -90.249 1.00 63.96 ? 143 SER A OG 1 ATOM 1032 N N . ASN A 1 144 ? 14.953 -40.539 -92.484 1.00 53.70 ? 144 ASN A N 1 ATOM 1033 C CA . ASN A 1 144 ? 15.421 -39.886 -93.697 1.00 51.05 ? 144 ASN A CA 1 ATOM 1034 C C . ASN A 1 144 ? 16.903 -39.531 -93.604 1.00 48.64 ? 144 ASN A C 1 ATOM 1035 O O . ASN A 1 144 ? 17.398 -39.215 -92.515 1.00 43.93 ? 144 ASN A O 1 ATOM 1036 C CB . ASN A 1 144 ? 14.610 -38.618 -93.941 1.00 53.52 ? 144 ASN A CB 1 ATOM 1037 C CG . ASN A 1 144 ? 13.267 -38.902 -94.591 1.00 57.03 ? 144 ASN A CG 1 ATOM 1038 O OD1 . ASN A 1 144 ? 12.839 -40.054 -94.699 1.00 58.00 ? 144 ASN A OD1 1 ATOM 1039 N ND2 . ASN A 1 144 ? 12.604 -37.850 -95.043 1.00 59.17 ? 144 ASN A ND2 1 ATOM 1040 N N . ASN A 1 145 ? 17.598 -39.585 -94.743 1.00 44.81 ? 145 ASN A N 1 ATOM 1041 C CA . ASN A 1 145 ? 18.996 -39.142 -94.817 1.00 43.03 ? 145 ASN A CA 1 ATOM 1042 C C . ASN A 1 145 ? 19.111 -37.702 -94.317 1.00 41.06 ? 145 ASN A C 1 ATOM 1043 O O . ASN A 1 145 ? 18.313 -36.840 -94.691 1.00 40.42 ? 145 ASN A O 1 ATOM 1044 C CB . ASN A 1 145 ? 19.528 -39.222 -96.251 1.00 42.37 ? 145 ASN A CB 1 ATOM 1045 C CG . ASN A 1 145 ? 19.753 -40.648 -96.725 1.00 42.59 ? 145 ASN A CG 1 ATOM 1046 O OD1 . ASN A 1 145 ? 19.459 -41.607 -96.013 1.00 42.15 ? 145 ASN A OD1 1 ATOM 1047 N ND2 . ASN A 1 145 ? 20.283 -40.792 -97.949 1.00 42.05 ? 145 ASN A ND2 1 ATOM 1048 N N . SER A 1 146 ? 20.106 -37.446 -93.472 1.00 40.88 ? 146 SER A N 1 ATOM 1049 C CA . SER A 1 146 ? 20.237 -36.146 -92.827 1.00 38.61 ? 146 SER A CA 1 ATOM 1050 C C . SER A 1 146 ? 21.709 -35.882 -92.490 1.00 37.14 ? 146 SER A C 1 ATOM 1051 O O . SER A 1 146 ? 22.613 -36.442 -93.125 1.00 35.71 ? 146 SER A O 1 ATOM 1052 C CB . SER A 1 146 ? 19.354 -36.093 -91.567 1.00 40.01 ? 146 SER A CB 1 ATOM 1053 O OG . SER A 1 146 ? 19.061 -34.749 -91.179 1.00 38.68 ? 146 SER A OG 1 ATOM 1054 N N . PHE A 1 147 ? 21.932 -35.021 -91.502 1.00 34.07 ? 147 PHE A N 1 ATOM 1055 C CA . PHE A 1 147 ? 23.270 -34.566 -91.148 1.00 33.30 ? 147 PHE A CA 1 ATOM 1056 C C . PHE A 1 147 ? 23.216 -33.874 -89.789 1.00 30.92 ? 147 PHE A C 1 ATOM 1057 O O . PHE A 1 147 ? 22.134 -33.570 -89.261 1.00 30.56 ? 147 PHE A O 1 ATOM 1058 C CB . PHE A 1 147 ? 23.767 -33.573 -92.197 1.00 33.47 ? 147 PHE A CB 1 ATOM 1059 C CG . PHE A 1 147 ? 25.257 -33.397 -92.227 1.00 34.08 ? 147 PHE A CG 1 ATOM 1060 C CD1 . PHE A 1 147 ? 26.094 -34.465 -92.534 1.00 34.33 ? 147 PHE A CD1 1 ATOM 1061 C CD2 . PHE A 1 147 ? 25.825 -32.152 -91.971 1.00 34.26 ? 147 PHE A CD2 1 ATOM 1062 C CE1 . PHE A 1 147 ? 27.468 -34.296 -92.589 1.00 34.21 ? 147 PHE A CE1 1 ATOM 1063 C CE2 . PHE A 1 147 ? 27.201 -31.980 -92.017 1.00 34.56 ? 147 PHE A CE2 1 ATOM 1064 C CZ . PHE A 1 147 ? 28.025 -33.052 -92.325 1.00 34.31 ? 147 PHE A CZ 1 ATOM 1065 N N . PHE A 1 148 ? 24.386 -33.609 -89.232 1.00 29.90 ? 148 PHE A N 1 ATOM 1066 C CA . PHE A 1 148 ? 24.476 -32.834 -87.996 1.00 29.28 ? 148 PHE A CA 1 ATOM 1067 C C . PHE A 1 148 ? 23.609 -31.584 -88.079 1.00 29.53 ? 148 PHE A C 1 ATOM 1068 O O . PHE A 1 148 ? 23.701 -30.830 -89.045 1.00 29.30 ? 148 PHE A O 1 ATOM 1069 C CB . PHE A 1 148 ? 25.927 -32.424 -87.783 1.00 29.87 ? 148 PHE A CB 1 ATOM 1070 C CG . PHE A 1 148 ? 26.852 -33.584 -87.558 1.00 29.96 ? 148 PHE A CG 1 ATOM 1071 C CD1 . PHE A 1 148 ? 26.802 -34.302 -86.383 1.00 31.15 ? 148 PHE A CD1 1 ATOM 1072 C CD2 . PHE A 1 148 ? 27.758 -33.963 -88.535 1.00 32.39 ? 148 PHE A CD2 1 ATOM 1073 C CE1 . PHE A 1 148 ? 27.668 -35.372 -86.158 1.00 31.84 ? 148 PHE A CE1 1 ATOM 1074 C CE2 . PHE A 1 148 ? 28.623 -35.035 -88.327 1.00 32.37 ? 148 PHE A CE2 1 ATOM 1075 C CZ . PHE A 1 148 ? 28.569 -35.742 -87.137 1.00 32.36 ? 148 PHE A CZ 1 ATOM 1076 N N . SER A 1 149 ? 22.758 -31.373 -87.080 1.00 29.19 ? 149 SER A N 1 ATOM 1077 C CA . SER A 1 149 ? 21.822 -30.245 -87.103 1.00 30.78 ? 149 SER A CA 1 ATOM 1078 C C . SER A 1 149 ? 22.505 -28.884 -87.193 1.00 30.86 ? 149 SER A C 1 ATOM 1079 O O . SER A 1 149 ? 21.976 -27.956 -87.818 1.00 29.08 ? 149 SER A O 1 ATOM 1080 C CB . SER A 1 149 ? 20.897 -30.281 -85.885 1.00 31.97 ? 149 SER A CB 1 ATOM 1081 O OG . SER A 1 149 ? 21.583 -29.955 -84.678 1.00 30.85 ? 149 SER A OG 1 ATOM 1082 N N . ARG A 1 150 ? 23.684 -28.753 -86.585 1.00 28.05 ? 150 ARG A N 1 ATOM 1083 C CA . ARG A 1 150 ? 24.342 -27.447 -86.521 1.00 27.75 ? 150 ARG A CA 1 ATOM 1084 C C . ARG A 1 150 ? 25.360 -27.186 -87.622 1.00 27.62 ? 150 ARG A C 1 ATOM 1085 O O . ARG A 1 150 ? 25.972 -26.102 -87.674 1.00 26.72 ? 150 ARG A O 1 ATOM 1086 C CB . ARG A 1 150 ? 24.975 -27.233 -85.140 1.00 27.06 ? 150 ARG A CB 1 ATOM 1087 C CG . ARG A 1 150 ? 24.018 -27.497 -83.983 1.00 27.12 ? 150 ARG A CG 1 ATOM 1088 C CD . ARG A 1 150 ? 22.758 -26.641 -84.089 1.00 27.86 ? 150 ARG A CD 1 ATOM 1089 N NE . ARG A 1 150 ? 22.025 -26.579 -82.825 1.00 27.00 ? 150 ARG A NE 1 ATOM 1090 C CZ . ARG A 1 150 ? 20.867 -25.948 -82.661 1.00 26.71 ? 150 ARG A CZ 1 ATOM 1091 N NH1 . ARG A 1 150 ? 20.278 -25.349 -83.695 1.00 26.73 ? 150 ARG A NH1 1 ATOM 1092 N NH2 . ARG A 1 150 ? 20.303 -25.909 -81.462 1.00 26.01 ? 150 ARG A NH2 1 ATOM 1093 N N . LEU A 1 151 ? 25.536 -28.158 -88.516 1.00 27.90 ? 151 LEU A N 1 ATOM 1094 C CA . LEU A 1 151 ? 26.484 -28.040 -89.590 1.00 27.87 ? 151 LEU A CA 1 ATOM 1095 C C . LEU A 1 151 ? 25.775 -28.085 -90.950 1.00 29.85 ? 151 LEU A C 1 ATOM 1096 O O . LEU A 1 151 ? 24.663 -28.614 -91.082 1.00 31.53 ? 151 LEU A O 1 ATOM 1097 C CB . LEU A 1 151 ? 27.545 -29.135 -89.469 1.00 28.17 ? 151 LEU A CB 1 ATOM 1098 C CG . LEU A 1 151 ? 28.419 -29.000 -88.199 1.00 27.88 ? 151 LEU A CG 1 ATOM 1099 C CD1 . LEU A 1 151 ? 29.288 -30.226 -88.008 1.00 27.05 ? 151 LEU A CD1 1 ATOM 1100 C CD2 . LEU A 1 151 ? 29.281 -27.732 -88.234 1.00 27.99 ? 151 LEU A CD2 1 ATOM 1101 N N . ASN A 1 152 ? 26.437 -27.512 -91.942 1.00 30.73 ? 152 ASN A N 1 ATOM 1102 C CA . ASN A 1 152 ? 25.865 -27.325 -93.287 1.00 31.05 ? 152 ASN A CA 1 ATOM 1103 C C . ASN A 1 152 ? 26.840 -27.851 -94.317 1.00 31.59 ? 152 ASN A C 1 ATOM 1104 O O . ASN A 1 152 ? 27.867 -27.232 -94.602 1.00 32.18 ? 152 ASN A O 1 ATOM 1105 C CB . ASN A 1 152 ? 25.554 -25.849 -93.537 1.00 30.86 ? 152 ASN A CB 1 ATOM 1106 C CG . ASN A 1 152 ? 24.729 -25.625 -94.801 1.00 32.46 ? 152 ASN A CG 1 ATOM 1107 O OD1 . ASN A 1 152 ? 24.514 -26.556 -95.601 1.00 32.35 ? 152 ASN A OD1 1 ATOM 1108 N ND2 . ASN A 1 152 ? 24.285 -24.387 -95.000 1.00 31.52 ? 152 ASN A ND2 1 ATOM 1109 N N . TRP A 1 153 ? 26.519 -29.015 -94.861 1.00 32.51 ? 153 TRP A N 1 ATOM 1110 C CA . TRP A 1 153 ? 27.356 -29.642 -95.855 1.00 33.32 ? 153 TRP A CA 1 ATOM 1111 C C . TRP A 1 153 ? 27.094 -29.040 -97.211 1.00 34.35 ? 153 TRP A C 1 ATOM 1112 O O . TRP A 1 153 ? 26.080 -29.336 -97.835 1.00 34.63 ? 153 TRP A O 1 ATOM 1113 C CB . TRP A 1 153 ? 27.059 -31.131 -95.885 1.00 34.35 ? 153 TRP A CB 1 ATOM 1114 C CG . TRP A 1 153 ? 28.064 -31.948 -96.642 1.00 34.36 ? 153 TRP A CG 1 ATOM 1115 C CD1 . TRP A 1 153 ? 29.129 -31.501 -97.418 1.00 34.58 ? 153 TRP A CD1 1 ATOM 1116 C CD2 . TRP A 1 153 ? 28.111 -33.408 -96.734 1.00 35.21 ? 153 TRP A CD2 1 ATOM 1117 N NE1 . TRP A 1 153 ? 29.826 -32.560 -97.945 1.00 35.01 ? 153 TRP A NE1 1 ATOM 1118 C CE2 . TRP A 1 153 ? 29.264 -33.730 -97.578 1.00 35.47 ? 153 TRP A CE2 1 ATOM 1119 C CE3 . TRP A 1 153 ? 27.353 -34.441 -96.206 1.00 36.55 ? 153 TRP A CE3 1 ATOM 1120 C CZ2 . TRP A 1 153 ? 29.625 -35.042 -97.865 1.00 37.23 ? 153 TRP A CZ2 1 ATOM 1121 C CZ3 . TRP A 1 153 ? 27.719 -35.762 -96.508 1.00 37.80 ? 153 TRP A CZ3 1 ATOM 1122 C CH2 . TRP A 1 153 ? 28.835 -36.053 -97.317 1.00 38.41 ? 153 TRP A CH2 1 ATOM 1123 N N . LEU A 1 154 ? 28.022 -28.198 -97.675 1.00 33.70 ? 154 LEU A N 1 ATOM 1124 C CA . LEU A 1 154 ? 27.895 -27.516 -98.962 1.00 35.07 ? 154 LEU A CA 1 ATOM 1125 C C . LEU A 1 154 ? 28.525 -28.368 -100.071 1.00 35.50 ? 154 LEU A C 1 ATOM 1126 O O . LEU A 1 154 ? 29.615 -28.935 -99.894 1.00 34.15 ? 154 LEU A O 1 ATOM 1127 C CB . LEU A 1 154 ? 28.602 -26.160 -98.915 1.00 35.22 ? 154 LEU A CB 1 ATOM 1128 C CG . LEU A 1 154 ? 28.279 -25.261 -97.716 1.00 35.93 ? 154 LEU A CG 1 ATOM 1129 C CD1 . LEU A 1 154 ? 29.183 -24.033 -97.727 1.00 36.83 ? 154 LEU A CD1 1 ATOM 1130 C CD2 . LEU A 1 154 ? 26.819 -24.861 -97.702 1.00 35.72 ? 154 LEU A CD2 1 ATOM 1131 N N . THR A 1 155 ? 27.844 -28.460 -101.208 1.00 36.17 ? 155 THR A N 1 ATOM 1132 C CA . THR A 1 155 ? 28.350 -29.218 -102.362 1.00 37.08 ? 155 THR A CA 1 ATOM 1133 C C . THR A 1 155 ? 28.151 -28.394 -103.637 1.00 37.67 ? 155 THR A C 1 ATOM 1134 O O . THR A 1 155 ? 27.595 -27.306 -103.593 1.00 37.24 ? 155 THR A O 1 ATOM 1135 C CB . THR A 1 155 ? 27.644 -30.589 -102.517 1.00 37.93 ? 155 THR A CB 1 ATOM 1136 O OG1 . THR A 1 155 ? 26.236 -30.394 -102.696 1.00 38.02 ? 155 THR A OG1 1 ATOM 1137 C CG2 . THR A 1 155 ? 27.903 -31.475 -101.298 1.00 37.48 ? 155 THR A CG2 1 ATOM 1138 N N . HIS A 1 156 ? 28.625 -28.905 -104.767 1.00 39.51 ? 156 HIS A N 1 ATOM 1139 C CA . HIS A 1 156 ? 28.599 -28.128 -105.992 1.00 41.78 ? 156 HIS A CA 1 ATOM 1140 C C . HIS A 1 156 ? 27.187 -27.844 -106.398 1.00 43.03 ? 156 HIS A C 1 ATOM 1141 O O . HIS A 1 156 ? 26.256 -28.548 -105.976 1.00 43.39 ? 156 HIS A O 1 ATOM 1142 C CB . HIS A 1 156 ? 29.346 -28.842 -107.106 1.00 42.58 ? 156 HIS A CB 1 ATOM 1143 C CG . HIS A 1 156 ? 28.610 -30.019 -107.691 1.00 44.05 ? 156 HIS A CG 1 ATOM 1144 N ND1 . HIS A 1 156 ? 27.490 -29.879 -108.437 1.00 46.21 ? 156 HIS A ND1 1 ATOM 1145 C CD2 . HIS A 1 156 ? 28.897 -31.379 -107.661 1.00 44.83 ? 156 HIS A CD2 1 ATOM 1146 C CE1 . HIS A 1 156 ? 27.072 -31.094 -108.843 1.00 46.91 ? 156 HIS A CE1 1 ATOM 1147 N NE2 . HIS A 1 156 ? 27.938 -32.012 -108.372 1.00 46.42 ? 156 HIS A NE2 1 ATOM 1148 N N . LEU A 1 157 ? 27.026 -26.792 -107.199 1.00 46.25 ? 157 LEU A N 1 ATOM 1149 C CA . LEU A 1 157 ? 25.744 -26.441 -107.821 1.00 46.90 ? 157 LEU A CA 1 ATOM 1150 C C . LEU A 1 157 ? 25.950 -26.415 -109.331 1.00 48.72 ? 157 LEU A C 1 ATOM 1151 O O . LEU A 1 157 ? 26.750 -25.623 -109.828 1.00 48.61 ? 157 LEU A O 1 ATOM 1152 C CB . LEU A 1 157 ? 25.283 -25.058 -107.349 1.00 46.94 ? 157 LEU A CB 1 ATOM 1153 C CG . LEU A 1 157 ? 23.983 -24.520 -107.957 1.00 47.59 ? 157 LEU A CG 1 ATOM 1154 C CD1 . LEU A 1 157 ? 22.778 -25.309 -107.443 1.00 47.35 ? 157 LEU A CD1 1 ATOM 1155 C CD2 . LEU A 1 157 ? 23.830 -23.033 -107.678 1.00 46.72 ? 157 LEU A CD2 1 ATOM 1156 N N . LYS A 1 158 ? 25.254 -27.294 -110.050 1.00 51.07 ? 158 LYS A N 1 ATOM 1157 C CA . LYS A 1 158 ? 25.404 -27.413 -111.512 1.00 53.79 ? 158 LYS A CA 1 ATOM 1158 C C . LYS A 1 158 ? 26.850 -27.707 -111.910 1.00 53.31 ? 158 LYS A C 1 ATOM 1159 O O . LYS A 1 158 ? 27.342 -27.197 -112.916 1.00 53.11 ? 158 LYS A O 1 ATOM 1160 C CB . LYS A 1 158 ? 24.937 -26.132 -112.224 1.00 56.98 ? 158 LYS A CB 1 ATOM 1161 C CG . LYS A 1 158 ? 23.558 -25.639 -111.821 1.00 59.94 ? 158 LYS A CG 1 ATOM 1162 C CD . LYS A 1 158 ? 22.463 -26.594 -112.271 1.00 63.37 ? 158 LYS A CD 1 ATOM 1163 C CE . LYS A 1 158 ? 21.080 -25.988 -112.075 1.00 64.89 ? 158 LYS A CE 1 ATOM 1164 N NZ . LYS A 1 158 ? 20.904 -24.713 -112.825 1.00 67.90 ? 158 LYS A NZ 1 ATOM 1165 N N . PHE A 1 159 ? 27.528 -28.514 -111.100 1.00 50.62 ? 159 PHE A N 1 ATOM 1166 C CA . PHE A 1 159 ? 28.941 -28.858 -111.300 1.00 50.58 ? 159 PHE A CA 1 ATOM 1167 C C . PHE A 1 159 ? 29.895 -27.665 -111.240 1.00 48.93 ? 159 PHE A C 1 ATOM 1168 O O . PHE A 1 159 ? 30.982 -27.710 -111.804 1.00 47.05 ? 159 PHE A O 1 ATOM 1169 C CB . PHE A 1 159 ? 29.125 -29.652 -112.597 1.00 53.52 ? 159 PHE A CB 1 ATOM 1170 C CG . PHE A 1 159 ? 28.199 -30.820 -112.701 1.00 55.97 ? 159 PHE A CG 1 ATOM 1171 C CD1 . PHE A 1 159 ? 28.464 -31.990 -111.999 1.00 55.75 ? 159 PHE A CD1 1 ATOM 1172 C CD2 . PHE A 1 159 ? 27.041 -30.743 -113.467 1.00 57.77 ? 159 PHE A CD2 1 ATOM 1173 C CE1 . PHE A 1 159 ? 27.597 -33.070 -112.063 1.00 57.63 ? 159 PHE A CE1 1 ATOM 1174 C CE2 . PHE A 1 159 ? 26.171 -31.821 -113.546 1.00 59.37 ? 159 PHE A CE2 1 ATOM 1175 C CZ . PHE A 1 159 ? 26.448 -32.986 -112.841 1.00 59.51 ? 159 PHE A CZ 1 ATOM 1176 N N . LYS A 1 160 ? 29.491 -26.609 -110.536 1.00 49.12 ? 160 LYS A N 1 ATOM 1177 C CA . LYS A 1 160 ? 30.412 -25.540 -110.162 1.00 49.47 ? 160 LYS A CA 1 ATOM 1178 C C . LYS A 1 160 ? 30.419 -25.383 -108.638 1.00 47.27 ? 160 LYS A C 1 ATOM 1179 O O . LYS A 1 160 ? 29.397 -25.553 -107.976 1.00 44.08 ? 160 LYS A O 1 ATOM 1180 C CB . LYS A 1 160 ? 30.033 -24.214 -110.816 1.00 53.74 ? 160 LYS A CB 1 ATOM 1181 C CG . LYS A 1 160 ? 30.454 -24.101 -112.280 1.00 57.66 ? 160 LYS A CG 1 ATOM 1182 C CD . LYS A 1 160 ? 30.765 -22.656 -112.656 1.00 60.31 ? 160 LYS A CD 1 ATOM 1183 C CE . LYS A 1 160 ? 30.737 -22.443 -114.163 1.00 63.10 ? 160 LYS A CE 1 ATOM 1184 N NZ . LYS A 1 160 ? 31.710 -23.324 -114.868 1.00 65.14 ? 160 LYS A NZ 1 ATOM 1185 N N . TYR A 1 161 ? 31.591 -25.086 -108.105 1.00 46.60 ? 161 TYR A N 1 ATOM 1186 C CA . TYR A 1 161 ? 31.748 -24.731 -106.707 1.00 45.25 ? 161 TYR A CA 1 ATOM 1187 C C . TYR A 1 161 ? 32.673 -23.520 -106.726 1.00 46.06 ? 161 TYR A C 1 ATOM 1188 O O . TYR A 1 161 ? 33.891 -23.670 -106.747 1.00 45.90 ? 161 TYR A O 1 ATOM 1189 C CB . TYR A 1 161 ? 32.340 -25.900 -105.926 1.00 44.65 ? 161 TYR A CB 1 ATOM 1190 C CG . TYR A 1 161 ? 32.313 -25.755 -104.413 1.00 42.59 ? 161 TYR A CG 1 ATOM 1191 C CD1 . TYR A 1 161 ? 33.032 -24.748 -103.765 1.00 42.60 ? 161 TYR A CD1 1 ATOM 1192 C CD2 . TYR A 1 161 ? 31.577 -26.641 -103.623 1.00 42.85 ? 161 TYR A CD2 1 ATOM 1193 C CE1 . TYR A 1 161 ? 33.020 -24.631 -102.376 1.00 40.19 ? 161 TYR A CE1 1 ATOM 1194 C CE2 . TYR A 1 161 ? 31.564 -26.533 -102.235 1.00 40.35 ? 161 TYR A CE2 1 ATOM 1195 C CZ . TYR A 1 161 ? 32.286 -25.522 -101.616 1.00 40.92 ? 161 TYR A CZ 1 ATOM 1196 O OH . TYR A 1 161 ? 32.276 -25.406 -100.227 1.00 38.31 ? 161 TYR A OH 1 ATOM 1197 N N . PRO A 1 162 ? 32.093 -22.313 -106.790 1.00 48.02 ? 162 PRO A N 1 ATOM 1198 C CA . PRO A 1 162 ? 32.928 -21.124 -106.874 1.00 49.51 ? 162 PRO A CA 1 ATOM 1199 C C . PRO A 1 162 ? 33.601 -20.867 -105.541 1.00 49.21 ? 162 PRO A C 1 ATOM 1200 O O . PRO A 1 162 ? 33.057 -21.240 -104.503 1.00 50.04 ? 162 PRO A O 1 ATOM 1201 C CB . PRO A 1 162 ? 31.937 -20.005 -107.221 1.00 51.52 ? 162 PRO A CB 1 ATOM 1202 C CG . PRO A 1 162 ? 30.609 -20.493 -106.763 1.00 52.67 ? 162 PRO A CG 1 ATOM 1203 C CD . PRO A 1 162 ? 30.654 -21.996 -106.791 1.00 51.54 ? 162 PRO A CD 1 ATOM 1204 N N . ALA A 1 163 ? 34.779 -20.256 -105.578 1.00 48.68 ? 163 ALA A N 1 ATOM 1205 C CA . ALA A 1 163 ? 35.532 -19.965 -104.370 1.00 48.19 ? 163 ALA A CA 1 ATOM 1206 C C . ALA A 1 163 ? 34.651 -19.191 -103.408 1.00 47.42 ? 163 ALA A C 1 ATOM 1207 O O . ALA A 1 163 ? 34.007 -18.222 -103.795 1.00 48.40 ? 163 ALA A O 1 ATOM 1208 C CB . ALA A 1 163 ? 36.779 -19.169 -104.698 1.00 49.36 ? 163 ALA A CB 1 ATOM 1209 N N . LEU A 1 164 ? 34.579 -19.658 -102.166 1.00 43.66 ? 164 LEU A N 1 ATOM 1210 C CA . LEU A 1 164 ? 33.808 -18.968 -101.151 1.00 43.79 ? 164 LEU A CA 1 ATOM 1211 C C . LEU A 1 164 ? 34.727 -18.023 -100.404 1.00 42.00 ? 164 LEU A C 1 ATOM 1212 O O . LEU A 1 164 ? 35.874 -18.353 -100.122 1.00 41.00 ? 164 LEU A O 1 ATOM 1213 C CB . LEU A 1 164 ? 33.171 -19.950 -100.178 1.00 43.16 ? 164 LEU A CB 1 ATOM 1214 C CG . LEU A 1 164 ? 32.150 -20.905 -100.794 1.00 44.89 ? 164 LEU A CG 1 ATOM 1215 C CD1 . LEU A 1 164 ? 31.679 -21.885 -99.733 1.00 45.11 ? 164 LEU A CD1 1 ATOM 1216 C CD2 . LEU A 1 164 ? 30.968 -20.159 -101.396 1.00 45.10 ? 164 LEU A CD2 1 ATOM 1217 N N . ASN A 1 165 ? 34.210 -16.843 -100.111 1.00 41.07 ? 165 ASN A N 1 ATOM 1218 C CA . ASN A 1 165 ? 34.909 -15.870 -99.322 1.00 42.62 ? 165 ASN A CA 1 ATOM 1219 C C . ASN A 1 165 ? 33.849 -15.120 -98.526 1.00 43.26 ? 165 ASN A C 1 ATOM 1220 O O . ASN A 1 165 ? 33.408 -14.035 -98.906 1.00 44.87 ? 165 ASN A O 1 ATOM 1221 C CB . ASN A 1 165 ? 35.721 -14.962 -100.223 1.00 45.52 ? 165 ASN A CB 1 ATOM 1222 C CG . ASN A 1 165 ? 36.490 -13.919 -99.453 1.00 47.87 ? 165 ASN A CG 1 ATOM 1223 O OD1 . ASN A 1 165 ? 37.244 -14.226 -98.521 1.00 49.11 ? 165 ASN A OD1 1 ATOM 1224 N ND2 . ASN A 1 165 ? 36.301 -12.668 -99.842 1.00 48.94 ? 165 ASN A ND2 1 ATOM 1225 N N . VAL A 1 166 ? 33.420 -15.747 -97.431 1.00 41.53 ? 166 VAL A N 1 ATOM 1226 C CA . VAL A 1 166 ? 32.206 -15.349 -96.730 1.00 40.00 ? 166 VAL A CA 1 ATOM 1227 C C . VAL A 1 166 ? 32.530 -14.771 -95.361 1.00 39.62 ? 166 VAL A C 1 ATOM 1228 O O . VAL A 1 166 ? 33.385 -15.294 -94.636 1.00 37.36 ? 166 VAL A O 1 ATOM 1229 C CB . VAL A 1 166 ? 31.249 -16.547 -96.596 1.00 40.38 ? 166 VAL A CB 1 ATOM 1230 C CG1 . VAL A 1 166 ? 30.011 -16.160 -95.817 1.00 41.07 ? 166 VAL A CG1 1 ATOM 1231 C CG2 . VAL A 1 166 ? 30.864 -17.056 -97.987 1.00 41.60 ? 166 VAL A CG2 1 ATOM 1232 N N . THR A 1 167 ? 31.811 -13.714 -95.011 1.00 39.21 ? 167 THR A N 1 ATOM 1233 C CA . THR A 1 167 ? 32.035 -12.983 -93.777 1.00 42.18 ? 167 THR A CA 1 ATOM 1234 C C . THR A 1 167 ? 30.842 -13.028 -92.803 1.00 40.70 ? 167 THR A C 1 ATOM 1235 O O . THR A 1 167 ? 29.664 -13.066 -93.215 1.00 40.27 ? 167 THR A O 1 ATOM 1236 C CB . THR A 1 167 ? 32.348 -11.512 -94.113 1.00 45.15 ? 167 THR A CB 1 ATOM 1237 O OG1 . THR A 1 167 ? 33.042 -10.918 -93.015 1.00 51.64 ? 167 THR A OG1 1 ATOM 1238 C CG2 . THR A 1 167 ? 31.079 -10.731 -94.402 1.00 46.50 ? 167 THR A CG2 1 ATOM 1239 N N . MET A 1 168 ? 31.145 -12.990 -91.505 1.00 38.53 ? 168 MET A N 1 ATOM 1240 C CA . MET A 1 168 ? 30.110 -12.813 -90.485 1.00 37.96 ? 168 MET A CA 1 ATOM 1241 C C . MET A 1 168 ? 30.626 -11.969 -89.315 1.00 38.16 ? 168 MET A C 1 ATOM 1242 O O . MET A 1 168 ? 31.381 -12.475 -88.473 1.00 37.83 ? 168 MET A O 1 ATOM 1243 C CB . MET A 1 168 ? 29.610 -14.170 -89.980 1.00 37.14 ? 168 MET A CB 1 ATOM 1244 C CG . MET A 1 168 ? 28.375 -14.093 -89.098 1.00 36.42 ? 168 MET A CG 1 ATOM 1245 S SD . MET A 1 168 ? 26.890 -13.430 -89.919 1.00 38.86 ? 168 MET A SD 1 ATOM 1246 C CE . MET A 1 168 ? 26.643 -14.712 -91.154 1.00 37.12 ? 168 MET A CE 1 ATOM 1247 N N . PRO A 1 169 ? 30.219 -10.687 -89.249 1.00 39.40 ? 169 PRO A N 1 ATOM 1248 C CA . PRO A 1 169 ? 30.684 -9.821 -88.167 1.00 39.60 ? 169 PRO A CA 1 ATOM 1249 C C . PRO A 1 169 ? 30.036 -10.156 -86.834 1.00 37.98 ? 169 PRO A C 1 ATOM 1250 O O . PRO A 1 169 ? 28.872 -10.551 -86.799 1.00 37.55 ? 169 PRO A O 1 ATOM 1251 C CB . PRO A 1 169 ? 30.236 -8.433 -88.618 1.00 41.95 ? 169 PRO A CB 1 ATOM 1252 C CG . PRO A 1 169 ? 29.008 -8.688 -89.412 1.00 42.56 ? 169 PRO A CG 1 ATOM 1253 C CD . PRO A 1 169 ? 29.264 -9.983 -90.134 1.00 41.28 ? 169 PRO A CD 1 ATOM 1254 N N . ASN A 1 170 ? 30.789 -10.006 -85.749 1.00 37.76 ? 170 ASN A N 1 ATOM 1255 C CA . ASN A 1 170 ? 30.218 -10.058 -84.411 1.00 37.52 ? 170 ASN A CA 1 ATOM 1256 C C . ASN A 1 170 ? 29.932 -8.638 -83.944 1.00 39.20 ? 170 ASN A C 1 ATOM 1257 O O . ASN A 1 170 ? 30.833 -7.921 -83.502 1.00 37.98 ? 170 ASN A O 1 ATOM 1258 C CB . ASN A 1 170 ? 31.131 -10.770 -83.401 1.00 36.70 ? 170 ASN A CB 1 ATOM 1259 C CG . ASN A 1 170 ? 30.502 -10.872 -82.017 1.00 37.19 ? 170 ASN A CG 1 ATOM 1260 O OD1 . ASN A 1 170 ? 29.447 -10.281 -81.752 1.00 37.23 ? 170 ASN A OD1 1 ATOM 1261 N ND2 . ASN A 1 170 ? 31.151 -11.614 -81.118 1.00 37.11 ? 170 ASN A ND2 1 ATOM 1262 N N . ASN A 1 171 ? 28.666 -8.256 -84.063 1.00 41.11 ? 171 ASN A N 1 ATOM 1263 C CA . ASN A 1 171 ? 28.183 -6.950 -83.623 1.00 43.67 ? 171 ASN A CA 1 ATOM 1264 C C . ASN A 1 171 ? 27.448 -7.041 -82.301 1.00 44.60 ? 171 ASN A C 1 ATOM 1265 O O . ASN A 1 171 ? 26.716 -6.123 -81.944 1.00 46.25 ? 171 ASN A O 1 ATOM 1266 C CB . ASN A 1 171 ? 27.268 -6.350 -84.693 1.00 44.26 ? 171 ASN A CB 1 ATOM 1267 C CG . ASN A 1 171 ? 28.008 -6.050 -85.968 1.00 45.34 ? 171 ASN A CG 1 ATOM 1268 O OD1 . ASN A 1 171 ? 29.152 -5.587 -85.937 1.00 46.57 ? 171 ASN A OD1 1 ATOM 1269 N ND2 . ASN A 1 171 ? 27.377 -6.323 -87.101 1.00 47.65 ? 171 ASN A ND2 1 ATOM 1270 N N . GLU A 1 172 ? 27.649 -8.147 -81.584 1.00 42.98 ? 172 GLU A N 1 ATOM 1271 C CA . GLU A 1 172 ? 27.038 -8.360 -80.279 1.00 44.26 ? 172 GLU A CA 1 ATOM 1272 C C . GLU A 1 172 ? 28.002 -7.894 -79.215 1.00 44.77 ? 172 GLU A C 1 ATOM 1273 O O . GLU A 1 172 ? 29.158 -7.595 -79.514 1.00 43.02 ? 172 GLU A O 1 ATOM 1274 C CB . GLU A 1 172 ? 26.730 -9.838 -80.034 1.00 44.54 ? 172 GLU A CB 1 ATOM 1275 C CG . GLU A 1 172 ? 25.905 -10.496 -81.118 1.00 46.54 ? 172 GLU A CG 1 ATOM 1276 C CD . GLU A 1 172 ? 24.536 -9.867 -81.269 1.00 48.99 ? 172 GLU A CD 1 ATOM 1277 O OE1 . GLU A 1 172 ? 23.950 -9.452 -80.253 1.00 52.85 ? 172 GLU A OE1 1 ATOM 1278 O OE2 . GLU A 1 172 ? 24.057 -9.776 -82.410 1.00 54.25 ? 172 GLU A OE2 1 ATOM 1279 N N . LYS A 1 173 ? 27.514 -7.858 -77.975 1.00 45.10 ? 173 LYS A N 1 ATOM 1280 C CA . LYS A 1 173 ? 28.331 -7.525 -76.811 1.00 47.69 ? 173 LYS A CA 1 ATOM 1281 C C . LYS A 1 173 ? 28.930 -8.759 -76.133 1.00 45.45 ? 173 LYS A C 1 ATOM 1282 O O . LYS A 1 173 ? 29.623 -8.621 -75.134 1.00 45.81 ? 173 LYS A O 1 ATOM 1283 C CB . LYS A 1 173 ? 27.506 -6.713 -75.801 1.00 51.07 ? 173 LYS A CB 1 ATOM 1284 C CG . LYS A 1 173 ? 27.229 -5.295 -76.281 1.00 56.06 ? 173 LYS A CG 1 ATOM 1285 C CD . LYS A 1 173 ? 26.431 -4.466 -75.283 1.00 60.02 ? 173 LYS A CD 1 ATOM 1286 C CE . LYS A 1 173 ? 26.096 -3.103 -75.874 1.00 62.12 ? 173 LYS A CE 1 ATOM 1287 N NZ . LYS A 1 173 ? 25.368 -2.232 -74.906 1.00 65.93 ? 173 LYS A NZ 1 ATOM 1288 N N . PHE A 1 174 ? 28.693 -9.949 -76.694 1.00 43.21 ? 174 PHE A N 1 ATOM 1289 C CA . PHE A 1 174 ? 29.243 -11.211 -76.170 1.00 40.57 ? 174 PHE A CA 1 ATOM 1290 C C . PHE A 1 174 ? 30.032 -11.993 -77.240 1.00 39.16 ? 174 PHE A C 1 ATOM 1291 O O . PHE A 1 174 ? 29.870 -11.761 -78.443 1.00 36.57 ? 174 PHE A O 1 ATOM 1292 C CB . PHE A 1 174 ? 28.115 -12.107 -75.634 1.00 40.57 ? 174 PHE A CB 1 ATOM 1293 C CG . PHE A 1 174 ? 26.976 -12.279 -76.597 1.00 41.60 ? 174 PHE A CG 1 ATOM 1294 C CD1 . PHE A 1 174 ? 27.063 -13.194 -77.643 1.00 41.28 ? 174 PHE A CD1 1 ATOM 1295 C CD2 . PHE A 1 174 ? 25.827 -11.508 -76.478 1.00 43.54 ? 174 PHE A CD2 1 ATOM 1296 C CE1 . PHE A 1 174 ? 26.026 -13.338 -78.544 1.00 42.23 ? 174 PHE A CE1 1 ATOM 1297 C CE2 . PHE A 1 174 ? 24.779 -11.648 -77.378 1.00 44.08 ? 174 PHE A CE2 1 ATOM 1298 C CZ . PHE A 1 174 ? 24.882 -12.564 -78.417 1.00 44.36 ? 174 PHE A CZ 1 ATOM 1299 N N . ASP A 1 175 ? 30.844 -12.948 -76.789 1.00 36.55 ? 175 ASP A N 1 ATOM 1300 C CA . ASP A 1 175 ? 31.646 -13.795 -77.689 1.00 36.50 ? 175 ASP A CA 1 ATOM 1301 C C . ASP A 1 175 ? 30.800 -14.844 -78.374 1.00 33.75 ? 175 ASP A C 1 ATOM 1302 O O . ASP A 1 175 ? 29.805 -15.297 -77.827 1.00 33.25 ? 175 ASP A O 1 ATOM 1303 C CB . ASP A 1 175 ? 32.736 -14.542 -76.924 1.00 38.21 ? 175 ASP A CB 1 ATOM 1304 C CG . ASP A 1 175 ? 33.799 -13.627 -76.349 1.00 41.65 ? 175 ASP A CG 1 ATOM 1305 O OD1 . ASP A 1 175 ? 33.802 -12.421 -76.660 1.00 42.82 ? 175 ASP A OD1 1 ATOM 1306 O OD2 . ASP A 1 175 ? 34.651 -14.132 -75.584 1.00 41.34 ? 175 ASP A OD2 1 ATOM 1307 N N . LYS A 1 176 ? 31.235 -15.249 -79.561 1.00 31.60 ? 176 LYS A N 1 ATOM 1308 C CA . LYS A 1 176 ? 30.545 -16.256 -80.335 1.00 29.73 ? 176 LYS A CA 1 ATOM 1309 C C . LYS A 1 176 ? 31.466 -17.454 -80.527 1.00 28.37 ? 176 LYS A C 1 ATOM 1310 O O . LYS A 1 176 ? 32.640 -17.293 -80.919 1.00 28.57 ? 176 LYS A O 1 ATOM 1311 C CB . LYS A 1 176 ? 30.187 -15.696 -81.714 1.00 30.31 ? 176 LYS A CB 1 ATOM 1312 C CG . LYS A 1 176 ? 29.172 -14.571 -81.726 1.00 31.70 ? 176 LYS A CG 1 ATOM 1313 C CD . LYS A 1 176 ? 29.034 -14.075 -83.161 1.00 32.70 ? 176 LYS A CD 1 ATOM 1314 C CE . LYS A 1 176 ? 27.904 -13.091 -83.372 1.00 33.77 ? 176 LYS A CE 1 ATOM 1315 N NZ . LYS A 1 176 ? 27.696 -12.864 -84.834 1.00 34.19 ? 176 LYS A NZ 1 ATOM 1316 N N . LEU A 1 177 ? 30.940 -18.645 -80.275 1.00 27.07 ? 177 LEU A N 1 ATOM 1317 C CA . LEU A 1 177 ? 31.684 -19.885 -80.548 1.00 26.06 ? 177 LEU A CA 1 ATOM 1318 C C . LEU A 1 177 ? 31.186 -20.532 -81.824 1.00 25.56 ? 177 LEU A C 1 ATOM 1319 O O . LEU A 1 177 ? 30.040 -20.971 -81.896 1.00 26.03 ? 177 LEU A O 1 ATOM 1320 C CB . LEU A 1 177 ? 31.577 -20.865 -79.368 1.00 25.87 ? 177 LEU A CB 1 ATOM 1321 C CG . LEU A 1 177 ? 32.117 -22.293 -79.575 1.00 25.32 ? 177 LEU A CG 1 ATOM 1322 C CD1 . LEU A 1 177 ? 33.614 -22.306 -79.847 1.00 25.15 ? 177 LEU A CD1 1 ATOM 1323 C CD2 . LEU A 1 177 ? 31.799 -23.148 -78.342 1.00 25.02 ? 177 LEU A CD2 1 ATOM 1324 N N . TYR A 1 178 ? 32.066 -20.625 -82.815 1.00 26.00 ? 178 TYR A N 1 ATOM 1325 C CA . TYR A 1 178 ? 31.756 -21.268 -84.090 1.00 27.02 ? 178 TYR A CA 1 ATOM 1326 C C . TYR A 1 178 ? 32.380 -22.645 -84.189 1.00 27.57 ? 178 TYR A C 1 ATOM 1327 O O . TYR A 1 178 ? 33.575 -22.807 -83.903 1.00 27.63 ? 178 TYR A O 1 ATOM 1328 C CB . TYR A 1 178 ? 32.251 -20.416 -85.251 1.00 27.12 ? 178 TYR A CB 1 ATOM 1329 C CG . TYR A 1 178 ? 31.417 -19.184 -85.498 1.00 27.36 ? 178 TYR A CG 1 ATOM 1330 C CD1 . TYR A 1 178 ? 30.246 -19.257 -86.245 1.00 28.29 ? 178 TYR A CD1 1 ATOM 1331 C CD2 . TYR A 1 178 ? 31.793 -17.945 -84.980 1.00 27.85 ? 178 TYR A CD2 1 ATOM 1332 C CE1 . TYR A 1 178 ? 29.475 -18.128 -86.491 1.00 28.78 ? 178 TYR A CE1 1 ATOM 1333 C CE2 . TYR A 1 178 ? 31.036 -16.809 -85.221 1.00 28.59 ? 178 TYR A CE2 1 ATOM 1334 C CZ . TYR A 1 178 ? 29.871 -16.907 -85.977 1.00 29.34 ? 178 TYR A CZ 1 ATOM 1335 O OH . TYR A 1 178 ? 29.111 -15.777 -86.207 1.00 30.86 ? 178 TYR A OH 1 ATOM 1336 N N . ILE A 1 179 ? 31.561 -23.624 -84.574 1.00 26.10 ? 179 ILE A N 1 ATOM 1337 C CA . ILE A 1 179 ? 31.999 -24.999 -84.812 1.00 26.52 ? 179 ILE A CA 1 ATOM 1338 C C . ILE A 1 179 ? 31.836 -25.297 -86.295 1.00 27.59 ? 179 ILE A C 1 ATOM 1339 O O . ILE A 1 179 ? 30.765 -25.042 -86.866 1.00 26.68 ? 179 ILE A O 1 ATOM 1340 C CB . ILE A 1 179 ? 31.111 -25.997 -84.034 1.00 26.85 ? 179 ILE A CB 1 ATOM 1341 C CG1 . ILE A 1 179 ? 31.023 -25.613 -82.553 1.00 27.04 ? 179 ILE A CG1 1 ATOM 1342 C CG2 . ILE A 1 179 ? 31.641 -27.408 -84.189 1.00 27.04 ? 179 ILE A CG2 1 ATOM 1343 C CD1 . ILE A 1 179 ? 32.366 -25.629 -81.810 1.00 25.43 ? 179 ILE A CD1 1 ATOM 1344 N N . TRP A 1 180 ? 32.893 -25.803 -86.915 1.00 26.98 ? 180 TRP A N 1 ATOM 1345 C CA . TRP A 1 180 ? 32.913 -26.046 -88.352 1.00 28.43 ? 180 TRP A CA 1 ATOM 1346 C C . TRP A 1 180 ? 33.781 -27.222 -88.642 1.00 29.01 ? 180 TRP A C 1 ATOM 1347 O O . TRP A 1 180 ? 34.411 -27.780 -87.728 1.00 28.78 ? 180 TRP A O 1 ATOM 1348 C CB . TRP A 1 180 ? 33.362 -24.806 -89.104 1.00 28.60 ? 180 TRP A CB 1 ATOM 1349 C CG . TRP A 1 180 ? 34.668 -24.209 -88.637 1.00 28.78 ? 180 TRP A CG 1 ATOM 1350 C CD1 . TRP A 1 180 ? 34.860 -23.280 -87.609 1.00 29.11 ? 180 TRP A CD1 1 ATOM 1351 C CD2 . TRP A 1 180 ? 36.004 -24.478 -89.168 1.00 28.86 ? 180 TRP A CD2 1 ATOM 1352 N NE1 . TRP A 1 180 ? 36.190 -22.975 -87.473 1.00 29.51 ? 180 TRP A NE1 1 ATOM 1353 C CE2 . TRP A 1 180 ? 36.931 -23.658 -88.385 1.00 29.59 ? 180 TRP A CE2 1 ATOM 1354 C CE3 . TRP A 1 180 ? 36.508 -25.292 -90.173 1.00 29.64 ? 180 TRP A CE3 1 ATOM 1355 C CZ2 . TRP A 1 180 ? 38.303 -23.666 -88.625 1.00 30.18 ? 180 TRP A CZ2 1 ATOM 1356 C CZ3 . TRP A 1 180 ? 37.886 -25.282 -90.419 1.00 30.47 ? 180 TRP A CZ3 1 ATOM 1357 C CH2 . TRP A 1 180 ? 38.767 -24.505 -89.645 1.00 29.43 ? 180 TRP A CH2 1 ATOM 1358 N N . GLY A 1 181 ? 33.808 -27.661 -89.893 1.00 29.33 ? 181 GLY A N 1 ATOM 1359 C CA . GLY A 1 181 ? 34.534 -28.881 -90.195 1.00 29.03 ? 181 GLY A CA 1 ATOM 1360 C C . GLY A 1 181 ? 35.086 -28.960 -91.590 1.00 29.97 ? 181 GLY A C 1 ATOM 1361 O O . GLY A 1 181 ? 34.753 -28.153 -92.451 1.00 28.74 ? 181 GLY A O 1 ATOM 1362 N N . VAL A 1 182 ? 35.933 -29.958 -91.791 1.00 30.21 ? 182 VAL A N 1 ATOM 1363 C CA . VAL A 1 182 ? 36.535 -30.229 -93.079 1.00 31.50 ? 182 VAL A CA 1 ATOM 1364 C C . VAL A 1 182 ? 36.235 -31.670 -93.439 1.00 30.80 ? 182 VAL A C 1 ATOM 1365 O O . VAL A 1 182 ? 36.466 -32.575 -92.645 1.00 30.17 ? 182 VAL A O 1 ATOM 1366 C CB . VAL A 1 182 ? 38.059 -29.995 -93.043 1.00 32.67 ? 182 VAL A CB 1 ATOM 1367 C CG1 . VAL A 1 182 ? 38.710 -30.441 -94.353 1.00 33.70 ? 182 VAL A CG1 1 ATOM 1368 C CG2 . VAL A 1 182 ? 38.329 -28.515 -92.785 1.00 33.62 ? 182 VAL A CG2 1 ATOM 1369 N N . HIS A 1 183 ? 35.690 -31.868 -94.630 1.00 31.77 ? 183 HIS A N 1 ATOM 1370 C CA . HIS A 1 183 ? 35.354 -33.201 -95.109 1.00 32.60 ? 183 HIS A CA 1 ATOM 1371 C C . HIS A 1 183 ? 36.526 -33.784 -95.854 1.00 32.45 ? 183 HIS A C 1 ATOM 1372 O O . HIS A 1 183 ? 37.089 -33.139 -96.747 1.00 31.46 ? 183 HIS A O 1 ATOM 1373 C CB . HIS A 1 183 ? 34.127 -33.127 -96.010 1.00 33.78 ? 183 HIS A CB 1 ATOM 1374 C CG . HIS A 1 183 ? 33.646 -34.461 -96.485 1.00 34.95 ? 183 HIS A CG 1 ATOM 1375 N ND1 . HIS A 1 183 ? 33.537 -34.764 -97.797 1.00 36.35 ? 183 HIS A ND1 1 ATOM 1376 C CD2 . HIS A 1 183 ? 33.247 -35.597 -95.782 1.00 35.40 ? 183 HIS A CD2 1 ATOM 1377 C CE1 . HIS A 1 183 ? 33.084 -36.029 -97.924 1.00 36.91 ? 183 HIS A CE1 1 ATOM 1378 N NE2 . HIS A 1 183 ? 32.911 -36.541 -96.695 1.00 35.87 ? 183 HIS A NE2 1 ATOM 1379 N N . HIS A 1 184 ? 36.920 -34.991 -95.455 1.00 32.69 ? 184 HIS A N 1 ATOM 1380 C CA . HIS A 1 184 ? 37.987 -35.746 -96.089 1.00 32.40 ? 184 HIS A CA 1 ATOM 1381 C C . HIS A 1 184 ? 37.350 -36.905 -96.833 1.00 32.06 ? 184 HIS A C 1 ATOM 1382 O O . HIS A 1 184 ? 37.018 -37.915 -96.220 1.00 31.54 ? 184 HIS A O 1 ATOM 1383 C CB . HIS A 1 184 ? 38.943 -36.299 -95.034 1.00 32.18 ? 184 HIS A CB 1 ATOM 1384 C CG . HIS A 1 184 ? 39.596 -35.248 -94.162 1.00 32.55 ? 184 HIS A CG 1 ATOM 1385 N ND1 . HIS A 1 184 ? 40.619 -34.491 -94.583 1.00 32.12 ? 184 HIS A ND1 1 ATOM 1386 C CD2 . HIS A 1 184 ? 39.350 -34.880 -92.834 1.00 32.01 ? 184 HIS A CD2 1 ATOM 1387 C CE1 . HIS A 1 184 ? 41.019 -33.673 -93.582 1.00 34.06 ? 184 HIS A CE1 1 ATOM 1388 N NE2 . HIS A 1 184 ? 40.242 -33.911 -92.510 1.00 32.77 ? 184 HIS A NE2 1 ATOM 1389 N N . PRO A 1 185 ? 37.156 -36.779 -98.163 1.00 33.53 ? 185 PRO A N 1 ATOM 1390 C CA . PRO A 1 185 ? 36.452 -37.836 -98.913 1.00 34.22 ? 185 PRO A CA 1 ATOM 1391 C C . PRO A 1 185 ? 37.265 -39.126 -99.063 1.00 35.26 ? 185 PRO A C 1 ATOM 1392 O O . PRO A 1 185 ? 38.490 -39.082 -99.080 1.00 35.33 ? 185 PRO A O 1 ATOM 1393 C CB . PRO A 1 185 ? 36.199 -37.200 -100.282 1.00 34.82 ? 185 PRO A CB 1 ATOM 1394 C CG . PRO A 1 185 ? 36.525 -35.754 -100.130 1.00 34.34 ? 185 PRO A CG 1 ATOM 1395 C CD . PRO A 1 185 ? 37.506 -35.645 -99.024 1.00 33.72 ? 185 PRO A CD 1 ATOM 1396 N N . GLY A 1 186 ? 36.575 -40.262 -99.155 1.00 36.42 ? 186 GLY A N 1 ATOM 1397 C CA . GLY A 1 186 ? 37.231 -41.558 -99.277 1.00 38.17 ? 186 GLY A CA 1 ATOM 1398 C C . GLY A 1 186 ? 38.057 -41.710 -100.549 1.00 40.31 ? 186 GLY A C 1 ATOM 1399 O O . GLY A 1 186 ? 39.136 -42.320 -100.522 1.00 40.40 ? 186 GLY A O 1 ATOM 1400 N N . THR A 1 187 ? 37.563 -41.138 -101.649 1.00 40.43 ? 187 THR A N 1 ATOM 1401 C CA . THR A 1 187 ? 38.182 -41.287 -102.977 1.00 43.31 ? 187 THR A CA 1 ATOM 1402 C C . THR A 1 187 ? 38.195 -39.984 -103.799 1.00 43.17 ? 187 THR A C 1 ATOM 1403 O O . THR A 1 187 ? 37.418 -39.059 -103.541 1.00 39.43 ? 187 THR A O 1 ATOM 1404 C CB . THR A 1 187 ? 37.434 -42.366 -103.799 1.00 44.86 ? 187 THR A CB 1 ATOM 1405 O OG1 . THR A 1 187 ? 36.112 -41.906 -104.126 1.00 45.28 ? 187 THR A OG1 1 ATOM 1406 C CG2 . THR A 1 187 ? 37.334 -43.676 -103.007 1.00 43.86 ? 187 THR A CG2 1 ATOM 1407 N N . ASP A 1 188 ? 39.067 -39.935 -104.805 1.00 45.52 ? 188 ASP A N 1 ATOM 1408 C CA . ASP A 1 188 ? 39.086 -38.821 -105.769 1.00 48.93 ? 188 ASP A CA 1 ATOM 1409 C C . ASP A 1 188 ? 37.743 -38.674 -106.493 1.00 48.32 ? 188 ASP A C 1 ATOM 1410 O O . ASP A 1 188 ? 37.355 -37.563 -106.847 1.00 45.36 ? 188 ASP A O 1 ATOM 1411 C CB . ASP A 1 188 ? 40.188 -39.007 -106.822 1.00 51.96 ? 188 ASP A CB 1 ATOM 1412 C CG . ASP A 1 188 ? 41.593 -38.913 -106.244 1.00 55.51 ? 188 ASP A CG 1 ATOM 1413 O OD1 . ASP A 1 188 ? 41.821 -38.159 -105.265 1.00 58.04 ? 188 ASP A OD1 1 ATOM 1414 O OD2 . ASP A 1 188 ? 42.490 -39.593 -106.788 1.00 58.90 ? 188 ASP A OD2 1 ATOM 1415 N N . ASN A 1 189 ? 37.054 -39.795 -106.719 1.00 49.24 ? 189 ASN A N 1 ATOM 1416 C CA . ASN A 1 189 ? 35.725 -39.790 -107.342 1.00 50.43 ? 189 ASN A CA 1 ATOM 1417 C C . ASN A 1 189 ? 34.697 -39.046 -106.513 1.00 48.34 ? 189 ASN A C 1 ATOM 1418 O O . ASN A 1 189 ? 33.895 -38.286 -107.049 1.00 46.92 ? 189 ASN A O 1 ATOM 1419 C CB . ASN A 1 189 ? 35.220 -41.219 -107.561 1.00 53.18 ? 189 ASN A CB 1 ATOM 1420 C CG . ASN A 1 189 ? 35.684 -41.809 -108.871 1.00 56.67 ? 189 ASN A CG 1 ATOM 1421 O OD1 . ASN A 1 189 ? 36.532 -41.236 -109.560 1.00 59.53 ? 189 ASN A OD1 1 ATOM 1422 N ND2 . ASN A 1 189 ? 35.125 -42.963 -109.228 1.00 58.31 ? 189 ASN A ND2 1 ATOM 1423 N N . ASP A 1 190 ? 34.714 -39.281 -105.201 1.00 47.54 ? 190 ASP A N 1 ATOM 1424 C CA . ASP A 1 190 ? 33.802 -38.584 -104.297 1.00 45.53 ? 190 ASP A CA 1 ATOM 1425 C C . ASP A 1 190 ? 34.116 -37.098 -104.253 1.00 42.15 ? 190 ASP A C 1 ATOM 1426 O O . ASP A 1 190 ? 33.206 -36.288 -104.200 1.00 41.12 ? 190 ASP A O 1 ATOM 1427 C CB . ASP A 1 190 ? 33.848 -39.181 -102.885 1.00 48.66 ? 190 ASP A CB 1 ATOM 1428 C CG . ASP A 1 190 ? 33.076 -40.493 -102.779 1.00 52.27 ? 190 ASP A CG 1 ATOM 1429 O OD1 . ASP A 1 190 ? 32.962 -41.199 -103.797 1.00 54.73 ? 190 ASP A OD1 1 ATOM 1430 O OD2 . ASP A 1 190 ? 32.577 -40.816 -101.678 1.00 55.49 ? 190 ASP A OD2 1 ATOM 1431 N N . GLN A 1 191 ? 35.400 -36.745 -104.281 1.00 40.46 ? 191 GLN A N 1 ATOM 1432 C CA . GLN A 1 191 ? 35.816 -35.336 -104.297 1.00 39.73 ? 191 GLN A CA 1 ATOM 1433 C C . GLN A 1 191 ? 35.196 -34.582 -105.467 1.00 39.67 ? 191 GLN A C 1 ATOM 1434 O O . GLN A 1 191 ? 34.635 -33.503 -105.298 1.00 39.31 ? 191 GLN A O 1 ATOM 1435 C CB . GLN A 1 191 ? 37.342 -35.211 -104.369 1.00 38.25 ? 191 GLN A CB 1 ATOM 1436 C CG . GLN A 1 191 ? 37.865 -33.787 -104.504 1.00 37.39 ? 191 GLN A CG 1 ATOM 1437 C CD . GLN A 1 191 ? 37.723 -32.961 -103.224 1.00 37.29 ? 191 GLN A CD 1 ATOM 1438 O OE1 . GLN A 1 191 ? 37.753 -33.498 -102.112 1.00 36.69 ? 191 GLN A OE1 1 ATOM 1439 N NE2 . GLN A 1 191 ? 37.621 -31.643 -103.380 1.00 35.93 ? 191 GLN A NE2 1 ATOM 1440 N N . ILE A 1 192 ? 35.315 -35.150 -106.657 1.00 41.30 ? 192 ILE A N 1 ATOM 1441 C CA . ILE A 1 192 ? 34.787 -34.498 -107.866 1.00 42.56 ? 192 ILE A CA 1 ATOM 1442 C C . ILE A 1 192 ? 33.259 -34.506 -107.844 1.00 42.95 ? 192 ILE A C 1 ATOM 1443 O O . ILE A 1 192 ? 32.612 -33.495 -108.101 1.00 42.95 ? 192 ILE A O 1 ATOM 1444 C CB . ILE A 1 192 ? 35.315 -35.194 -109.128 1.00 44.59 ? 192 ILE A CB 1 ATOM 1445 C CG1 . ILE A 1 192 ? 36.848 -35.081 -109.183 1.00 45.30 ? 192 ILE A CG1 1 ATOM 1446 C CG2 . ILE A 1 192 ? 34.670 -34.600 -110.377 1.00 45.93 ? 192 ILE A CG2 1 ATOM 1447 C CD1 . ILE A 1 192 ? 37.380 -33.671 -109.374 1.00 46.03 ? 192 ILE A CD1 1 ATOM 1448 N N . SER A 1 193 ? 32.689 -35.645 -107.476 1.00 43.97 ? 193 SER A N 1 ATOM 1449 C CA . SER A 1 193 ? 31.247 -35.785 -107.365 1.00 44.71 ? 193 SER A CA 1 ATOM 1450 C C . SER A 1 193 ? 30.632 -34.787 -106.372 1.00 43.66 ? 193 SER A C 1 ATOM 1451 O O . SER A 1 193 ? 29.530 -34.279 -106.596 1.00 42.48 ? 193 SER A O 1 ATOM 1452 C CB . SER A 1 193 ? 30.915 -37.219 -106.953 1.00 47.76 ? 193 SER A CB 1 ATOM 1453 O OG . SER A 1 193 ? 29.521 -37.421 -106.890 1.00 52.15 ? 193 SER A OG 1 ATOM 1454 N N . LEU A 1 194 ? 31.345 -34.490 -105.283 1.00 39.96 ? 194 LEU A N 1 ATOM 1455 C CA . LEU A 1 194 ? 30.827 -33.560 -104.290 1.00 39.37 ? 194 LEU A CA 1 ATOM 1456 C C . LEU A 1 194 ? 31.149 -32.088 -104.581 1.00 38.55 ? 194 LEU A C 1 ATOM 1457 O O . LEU A 1 194 ? 30.279 -31.218 -104.435 1.00 38.93 ? 194 LEU A O 1 ATOM 1458 C CB . LEU A 1 194 ? 31.354 -33.928 -102.895 1.00 38.37 ? 194 LEU A CB 1 ATOM 1459 C CG . LEU A 1 194 ? 30.827 -35.224 -102.271 1.00 38.97 ? 194 LEU A CG 1 ATOM 1460 C CD1 . LEU A 1 194 ? 31.726 -35.652 -101.111 1.00 36.89 ? 194 LEU A CD1 1 ATOM 1461 C CD2 . LEU A 1 194 ? 29.382 -35.081 -101.812 1.00 38.76 ? 194 LEU A CD2 1 ATOM 1462 N N . TYR A 1 195 ? 32.392 -31.797 -104.960 1.00 37.23 ? 195 TYR A N 1 ATOM 1463 C CA . TYR A 1 195 ? 32.856 -30.403 -105.020 1.00 38.74 ? 195 TYR A CA 1 ATOM 1464 C C . TYR A 1 195 ? 33.253 -29.927 -106.428 1.00 41.58 ? 195 TYR A C 1 ATOM 1465 O O . TYR A 1 195 ? 33.575 -28.745 -106.620 1.00 42.63 ? 195 TYR A O 1 ATOM 1466 C CB . TYR A 1 195 ? 33.994 -30.202 -104.006 1.00 37.72 ? 195 TYR A CB 1 ATOM 1467 C CG . TYR A 1 195 ? 33.641 -30.781 -102.647 1.00 35.25 ? 195 TYR A CG 1 ATOM 1468 C CD1 . TYR A 1 195 ? 32.609 -30.239 -101.892 1.00 34.91 ? 195 TYR A CD1 1 ATOM 1469 C CD2 . TYR A 1 195 ? 34.302 -31.901 -102.143 1.00 35.52 ? 195 TYR A CD2 1 ATOM 1470 C CE1 . TYR A 1 195 ? 32.257 -30.771 -100.674 1.00 34.37 ? 195 TYR A CE1 1 ATOM 1471 C CE2 . TYR A 1 195 ? 33.962 -32.444 -100.913 1.00 34.41 ? 195 TYR A CE2 1 ATOM 1472 C CZ . TYR A 1 195 ? 32.939 -31.866 -100.185 1.00 34.41 ? 195 TYR A CZ 1 ATOM 1473 O OH . TYR A 1 195 ? 32.574 -32.392 -98.979 1.00 34.92 ? 195 TYR A OH 1 ATOM 1474 N N . ALA A 1 196 ? 33.228 -30.847 -107.399 1.00 43.78 ? 196 ALA A N 1 ATOM 1475 C CA . ALA A 1 196 ? 33.455 -30.539 -108.826 1.00 46.55 ? 196 ALA A CA 1 ATOM 1476 C C . ALA A 1 196 ? 34.902 -30.186 -109.179 1.00 48.28 ? 196 ALA A C 1 ATOM 1477 O O . ALA A 1 196 ? 35.181 -29.819 -110.318 1.00 51.22 ? 196 ALA A O 1 ATOM 1478 C CB . ALA A 1 196 ? 32.506 -29.444 -109.298 1.00 46.17 ? 196 ALA A CB 1 ATOM 1479 N N . GLN A 1 197 ? 35.820 -30.311 -108.225 1.00 47.63 ? 197 GLN A N 1 ATOM 1480 C CA . GLN A 1 197 ? 37.222 -29.952 -108.452 1.00 48.56 ? 197 GLN A CA 1 ATOM 1481 C C . GLN A 1 197 ? 38.112 -30.581 -107.383 1.00 46.61 ? 197 GLN A C 1 ATOM 1482 O O . GLN A 1 197 ? 37.609 -31.090 -106.388 1.00 45.64 ? 197 GLN A O 1 ATOM 1483 C CB . GLN A 1 197 ? 37.394 -28.424 -108.477 1.00 49.87 ? 197 GLN A CB 1 ATOM 1484 C CG . GLN A 1 197 ? 36.903 -27.701 -107.228 1.00 50.70 ? 197 GLN A CG 1 ATOM 1485 C CD . GLN A 1 197 ? 36.286 -26.339 -107.513 1.00 53.16 ? 197 GLN A CD 1 ATOM 1486 O OE1 . GLN A 1 197 ? 36.170 -25.913 -108.663 1.00 56.15 ? 197 GLN A OE1 1 ATOM 1487 N NE2 . GLN A 1 197 ? 35.869 -25.655 -106.461 1.00 53.70 ? 197 GLN A NE2 1 ATOM 1488 N N . ALA A 1 198 ? 39.425 -30.554 -107.611 1.00 45.51 ? 198 ALA A N 1 ATOM 1489 C CA . ALA A 1 198 ? 40.406 -31.136 -106.687 1.00 45.29 ? 198 ALA A CA 1 ATOM 1490 C C . ALA A 1 198 ? 40.410 -30.379 -105.348 1.00 43.18 ? 198 ALA A C 1 ATOM 1491 O O . ALA A 1 198 ? 40.025 -29.219 -105.280 1.00 42.78 ? 198 ALA A O 1 ATOM 1492 C CB . ALA A 1 198 ? 41.800 -31.110 -107.309 1.00 44.33 ? 198 ALA A CB 1 ATOM 1493 N N . SER A 1 199 ? 40.849 -31.049 -104.292 1.00 43.67 ? 199 SER A N 1 ATOM 1494 C CA . SER A 1 199 ? 40.783 -30.474 -102.953 1.00 43.61 ? 199 SER A CA 1 ATOM 1495 C C . SER A 1 199 ? 41.805 -29.361 -102.802 1.00 44.18 ? 199 SER A C 1 ATOM 1496 O O . SER A 1 199 ? 42.868 -29.366 -103.438 1.00 45.51 ? 199 SER A O 1 ATOM 1497 C CB . SER A 1 199 ? 41.006 -31.547 -101.886 1.00 42.69 ? 199 SER A CB 1 ATOM 1498 O OG . SER A 1 199 ? 42.292 -32.113 -102.001 1.00 43.67 ? 199 SER A OG 1 ATOM 1499 N N . GLY A 1 200 ? 41.456 -28.396 -101.967 1.00 45.06 ? 200 GLY A N 1 ATOM 1500 C CA . GLY A 1 200 ? 42.337 -27.293 -101.633 1.00 45.57 ? 200 GLY A CA 1 ATOM 1501 C C . GLY A 1 200 ? 42.034 -26.859 -100.214 1.00 45.53 ? 200 GLY A C 1 ATOM 1502 O O . GLY A 1 200 ? 41.028 -27.267 -99.625 1.00 47.09 ? 200 GLY A O 1 ATOM 1503 N N . ARG A 1 201 ? 42.884 -25.997 -99.685 1.00 44.20 ? 201 ARG A N 1 ATOM 1504 C CA . ARG A 1 201 ? 42.834 -25.653 -98.275 1.00 42.66 ? 201 ARG A CA 1 ATOM 1505 C C . ARG A 1 201 ? 41.599 -24.842 -97.914 1.00 41.34 ? 201 ARG A C 1 ATOM 1506 O O . ARG A 1 201 ? 40.960 -24.215 -98.772 1.00 39.25 ? 201 ARG A O 1 ATOM 1507 C CB . ARG A 1 201 ? 44.100 -24.895 -97.882 1.00 44.20 ? 201 ARG A CB 1 ATOM 1508 C CG . ARG A 1 201 ? 44.215 -23.523 -98.515 1.00 44.40 ? 201 ARG A CG 1 ATOM 1509 C CD . ARG A 1 201 ? 45.664 -23.112 -98.694 1.00 45.39 ? 201 ARG A CD 1 ATOM 1510 N NE . ARG A 1 201 ? 45.735 -21.775 -99.275 1.00 45.78 ? 201 ARG A NE 1 ATOM 1511 C CZ . ARG A 1 201 ? 45.854 -21.511 -100.577 1.00 46.96 ? 201 ARG A CZ 1 ATOM 1512 N NH1 . ARG A 1 201 ? 45.940 -22.491 -101.475 1.00 46.57 ? 201 ARG A NH1 1 ATOM 1513 N NH2 . ARG A 1 201 ? 45.899 -20.248 -100.980 1.00 46.46 ? 201 ARG A NH2 1 ATOM 1514 N N . ILE A 1 202 ? 41.264 -24.893 -96.630 1.00 37.20 ? 202 ILE A N 1 ATOM 1515 C CA . ILE A 1 202 ? 40.210 -24.069 -96.053 1.00 35.61 ? 202 ILE A CA 1 ATOM 1516 C C . ILE A 1 202 ? 40.879 -23.141 -95.058 1.00 34.66 ? 202 ILE A C 1 ATOM 1517 O O . ILE A 1 202 ? 41.694 -23.593 -94.232 1.00 34.23 ? 202 ILE A O 1 ATOM 1518 C CB . ILE A 1 202 ? 39.152 -24.942 -95.355 1.00 34.82 ? 202 ILE A CB 1 ATOM 1519 C CG1 . ILE A 1 202 ? 38.400 -25.772 -96.399 1.00 35.34 ? 202 ILE A CG1 1 ATOM 1520 C CG2 . ILE A 1 202 ? 38.172 -24.099 -94.537 1.00 33.81 ? 202 ILE A CG2 1 ATOM 1521 C CD1 . ILE A 1 202 ? 37.497 -26.823 -95.799 1.00 35.01 ? 202 ILE A CD1 1 ATOM 1522 N N . THR A 1 203 ? 40.569 -21.853 -95.140 1.00 34.43 ? 203 THR A N 1 ATOM 1523 C CA . THR A 1 203 ? 41.091 -20.884 -94.170 1.00 34.33 ? 203 THR A CA 1 ATOM 1524 C C . THR A 1 203 ? 39.950 -20.163 -93.482 1.00 34.45 ? 203 THR A C 1 ATOM 1525 O O . THR A 1 203 ? 39.066 -19.592 -94.120 1.00 35.28 ? 203 THR A O 1 ATOM 1526 C CB . THR A 1 203 ? 42.102 -19.895 -94.802 1.00 36.12 ? 203 THR A CB 1 ATOM 1527 O OG1 . THR A 1 203 ? 43.232 -20.634 -95.279 1.00 36.04 ? 203 THR A OG1 1 ATOM 1528 C CG2 . THR A 1 203 ? 42.589 -18.854 -93.771 1.00 35.77 ? 203 THR A CG2 1 ATOM 1529 N N . VAL A 1 204 ? 39.959 -20.245 -92.155 1.00 31.86 ? 204 VAL A N 1 ATOM 1530 C CA . VAL A 1 204 ? 38.986 -19.575 -91.338 1.00 31.00 ? 204 VAL A CA 1 ATOM 1531 C C . VAL A 1 204 ? 39.765 -18.613 -90.460 1.00 31.17 ? 204 VAL A C 1 ATOM 1532 O O . VAL A 1 204 ? 40.647 -19.027 -89.711 1.00 29.96 ? 204 VAL A O 1 ATOM 1533 C CB . VAL A 1 204 ? 38.179 -20.566 -90.477 1.00 30.74 ? 204 VAL A CB 1 ATOM 1534 C CG1 . VAL A 1 204 ? 37.247 -19.813 -89.534 1.00 29.19 ? 204 VAL A CG1 1 ATOM 1535 C CG2 . VAL A 1 204 ? 37.406 -21.529 -91.375 1.00 29.64 ? 204 VAL A CG2 1 ATOM 1536 N N . SER A 1 205 ? 39.443 -17.331 -90.564 1.00 31.23 ? 205 SER A N 1 ATOM 1537 C CA . SER A 1 205 ? 40.235 -16.312 -89.911 1.00 33.00 ? 205 SER A CA 1 ATOM 1538 C C . SER A 1 205 ? 39.396 -15.219 -89.273 1.00 33.61 ? 205 SER A C 1 ATOM 1539 O O . SER A 1 205 ? 38.206 -15.055 -89.559 1.00 33.31 ? 205 SER A O 1 ATOM 1540 C CB . SER A 1 205 ? 41.214 -15.703 -90.918 1.00 33.38 ? 205 SER A CB 1 ATOM 1541 O OG . SER A 1 205 ? 40.516 -15.103 -92.006 1.00 34.64 ? 205 SER A OG 1 ATOM 1542 N N . THR A 1 206 ? 40.050 -14.499 -88.370 1.00 34.00 ? 206 THR A N 1 ATOM 1543 C CA . THR A 1 206 ? 39.518 -13.325 -87.718 1.00 32.95 ? 206 THR A CA 1 ATOM 1544 C C . THR A 1 206 ? 40.641 -12.286 -87.731 1.00 34.26 ? 206 THR A C 1 ATOM 1545 O O . THR A 1 206 ? 41.731 -12.530 -88.263 1.00 34.02 ? 206 THR A O 1 ATOM 1546 C CB . THR A 1 206 ? 39.098 -13.621 -86.253 1.00 33.42 ? 206 THR A CB 1 ATOM 1547 O OG1 . THR A 1 206 ? 40.263 -13.900 -85.458 1.00 33.68 ? 206 THR A OG1 1 ATOM 1548 C CG2 . THR A 1 206 ? 38.108 -14.815 -86.165 1.00 32.07 ? 206 THR A CG2 1 ATOM 1549 N N . LYS A 1 207 ? 40.382 -11.125 -87.153 1.00 35.21 ? 207 LYS A N 1 ATOM 1550 C CA . LYS A 1 207 ? 41.437 -10.154 -86.943 1.00 37.92 ? 207 LYS A CA 1 ATOM 1551 C C . LYS A 1 207 ? 42.577 -10.682 -86.075 1.00 39.36 ? 207 LYS A C 1 ATOM 1552 O O . LYS A 1 207 ? 43.716 -10.268 -86.266 1.00 39.69 ? 207 LYS A O 1 ATOM 1553 C CB . LYS A 1 207 ? 40.888 -8.884 -86.327 1.00 39.53 ? 207 LYS A CB 1 ATOM 1554 C CG . LYS A 1 207 ? 40.015 -8.082 -87.274 1.00 41.09 ? 207 LYS A CG 1 ATOM 1555 C CD . LYS A 1 207 ? 39.610 -6.779 -86.612 1.00 43.06 ? 207 LYS A CD 1 ATOM 1556 C CE . LYS A 1 207 ? 38.164 -6.441 -86.898 1.00 44.80 ? 207 LYS A CE 1 ATOM 1557 N NZ . LYS A 1 207 ? 37.799 -5.149 -86.255 1.00 46.18 ? 207 LYS A NZ 1 ATOM 1558 N N . ARG A 1 208 ? 42.291 -11.604 -85.153 1.00 39.71 ? 208 ARG A N 1 ATOM 1559 C CA . ARG A 1 208 ? 43.314 -12.062 -84.205 1.00 42.21 ? 208 ARG A CA 1 ATOM 1560 C C . ARG A 1 208 ? 43.806 -13.490 -84.423 1.00 41.51 ? 208 ARG A C 1 ATOM 1561 O O . ARG A 1 208 ? 44.748 -13.913 -83.756 1.00 41.47 ? 208 ARG A O 1 ATOM 1562 C CB . ARG A 1 208 ? 42.808 -11.914 -82.766 1.00 44.87 ? 208 ARG A CB 1 ATOM 1563 C CG . ARG A 1 208 ? 41.681 -12.871 -82.413 1.00 46.52 ? 208 ARG A CG 1 ATOM 1564 C CD . ARG A 1 208 ? 41.428 -12.956 -80.917 1.00 50.54 ? 208 ARG A CD 1 ATOM 1565 N NE . ARG A 1 208 ? 40.369 -13.929 -80.643 1.00 52.78 ? 208 ARG A NE 1 ATOM 1566 C CZ . ARG A 1 208 ? 39.959 -14.297 -79.430 1.00 53.48 ? 208 ARG A CZ 1 ATOM 1567 N NH1 . ARG A 1 208 ? 40.514 -13.771 -78.340 1.00 54.79 ? 208 ARG A NH1 1 ATOM 1568 N NH2 . ARG A 1 208 ? 38.981 -15.193 -79.309 1.00 52.41 ? 208 ARG A NH2 1 ATOM 1569 N N . SER A 1 209 ? 43.196 -14.236 -85.341 1.00 39.03 ? 209 SER A N 1 ATOM 1570 C CA . SER A 1 209 ? 43.520 -15.659 -85.478 1.00 38.71 ? 209 SER A CA 1 ATOM 1571 C C . SER A 1 209 ? 43.336 -16.138 -86.892 1.00 36.88 ? 209 SER A C 1 ATOM 1572 O O . SER A 1 209 ? 42.604 -15.541 -87.676 1.00 35.23 ? 209 SER A O 1 ATOM 1573 C CB . SER A 1 209 ? 42.630 -16.508 -84.549 1.00 39.19 ? 209 SER A CB 1 ATOM 1574 O OG . SER A 1 209 ? 41.269 -16.464 -84.978 1.00 41.33 ? 209 SER A OG 1 ATOM 1575 N N . GLN A 1 210 ? 43.996 -17.237 -87.214 1.00 35.82 ? 210 GLN A N 1 ATOM 1576 C CA . GLN A 1 210 ? 43.804 -17.877 -88.496 1.00 36.41 ? 210 GLN A CA 1 ATOM 1577 C C . GLN A 1 210 ? 44.031 -19.366 -88.334 1.00 36.90 ? 210 GLN A C 1 ATOM 1578 O O . GLN A 1 210 ? 44.926 -19.784 -87.584 1.00 36.16 ? 210 GLN A O 1 ATOM 1579 C CB . GLN A 1 210 ? 44.767 -17.313 -89.537 1.00 38.52 ? 210 GLN A CB 1 ATOM 1580 C CG . GLN A 1 210 ? 46.226 -17.271 -89.106 1.00 40.13 ? 210 GLN A CG 1 ATOM 1581 C CD . GLN A 1 210 ? 47.146 -16.772 -90.204 1.00 43.92 ? 210 GLN A CD 1 ATOM 1582 O OE1 . GLN A 1 210 ? 46.707 -16.519 -91.320 1.00 46.62 ? 210 GLN A OE1 1 ATOM 1583 N NE2 . GLN A 1 210 ? 48.430 -16.634 -89.892 1.00 44.41 ? 210 GLN A NE2 1 ATOM 1584 N N . GLN A 1 211 ? 43.214 -20.155 -89.022 1.00 34.43 ? 211 GLN A N 1 ATOM 1585 C CA . GLN A 1 211 ? 43.355 -21.590 -89.037 1.00 33.98 ? 211 GLN A CA 1 ATOM 1586 C C . GLN A 1 211 ? 43.188 -22.059 -90.463 1.00 32.95 ? 211 GLN A C 1 ATOM 1587 O O . GLN A 1 211 ? 42.128 -21.864 -91.062 1.00 32.45 ? 211 GLN A O 1 ATOM 1588 C CB . GLN A 1 211 ? 42.258 -22.256 -88.196 1.00 34.95 ? 211 GLN A CB 1 ATOM 1589 C CG . GLN A 1 211 ? 42.238 -21.895 -86.716 1.00 37.21 ? 211 GLN A CG 1 ATOM 1590 C CD . GLN A 1 211 ? 40.840 -22.022 -86.116 1.00 37.44 ? 211 GLN A CD 1 ATOM 1591 O OE1 . GLN A 1 211 ? 40.019 -21.107 -86.213 1.00 42.05 ? 211 GLN A OE1 1 ATOM 1592 N NE2 . GLN A 1 211 ? 40.576 -23.145 -85.500 1.00 37.76 ? 211 GLN A NE2 1 ATOM 1593 N N . THR A 1 212 ? 44.213 -22.703 -90.995 1.00 32.57 ? 212 THR A N 1 ATOM 1594 C CA . THR A 1 212 ? 44.154 -23.281 -92.336 1.00 33.15 ? 212 THR A CA 1 ATOM 1595 C C . THR A 1 212 ? 44.221 -24.796 -92.214 1.00 33.89 ? 212 THR A C 1 ATOM 1596 O O . THR A 1 212 ? 45.075 -25.332 -91.504 1.00 33.52 ? 212 THR A O 1 ATOM 1597 C CB . THR A 1 212 ? 45.300 -22.767 -93.223 1.00 33.86 ? 212 THR A CB 1 ATOM 1598 O OG1 . THR A 1 212 ? 45.169 -21.351 -93.396 1.00 33.38 ? 212 THR A OG1 1 ATOM 1599 C CG2 . THR A 1 212 ? 45.281 -23.455 -94.582 1.00 34.09 ? 212 THR A CG2 1 ATOM 1600 N N . VAL A 1 213 ? 43.300 -25.481 -92.880 1.00 32.99 ? 213 VAL A N 1 ATOM 1601 C CA . VAL A 1 213 ? 43.218 -26.927 -92.812 1.00 32.91 ? 213 VAL A CA 1 ATOM 1602 C C . VAL A 1 213 ? 43.175 -27.513 -94.221 1.00 34.13 ? 213 VAL A C 1 ATOM 1603 O O . VAL A 1 213 ? 42.474 -27.003 -95.086 1.00 34.09 ? 213 VAL A O 1 ATOM 1604 C CB . VAL A 1 213 ? 41.980 -27.394 -92.024 1.00 32.99 ? 213 VAL A CB 1 ATOM 1605 C CG1 . VAL A 1 213 ? 41.964 -28.912 -91.938 1.00 33.42 ? 213 VAL A CG1 1 ATOM 1606 C CG2 . VAL A 1 213 ? 41.973 -26.781 -90.627 1.00 32.93 ? 213 VAL A CG2 1 ATOM 1607 N N . ILE A 1 214 ? 43.940 -28.581 -94.433 1.00 35.10 ? 214 ILE A N 1 ATOM 1608 C CA . ILE A 1 214 ? 44.047 -29.233 -95.747 1.00 36.14 ? 214 ILE A CA 1 ATOM 1609 C C . ILE A 1 214 ? 43.199 -30.499 -95.775 1.00 35.31 ? 214 ILE A C 1 ATOM 1610 O O . ILE A 1 214 ? 43.458 -31.421 -95.016 1.00 34.27 ? 214 ILE A O 1 ATOM 1611 C CB . ILE A 1 214 ? 45.497 -29.638 -96.057 1.00 36.86 ? 214 ILE A CB 1 ATOM 1612 C CG1 . ILE A 1 214 ? 46.409 -28.407 -96.010 1.00 38.34 ? 214 ILE A CG1 1 ATOM 1613 C CG2 . ILE A 1 214 ? 45.590 -30.333 -97.419 1.00 37.77 ? 214 ILE A CG2 1 ATOM 1614 C CD1 . ILE A 1 214 ? 47.875 -28.750 -95.836 1.00 40.52 ? 214 ILE A CD1 1 ATOM 1615 N N . PRO A 1 215 ? 42.190 -30.554 -96.663 1.00 35.55 ? 215 PRO A N 1 ATOM 1616 C CA . PRO A 1 215 ? 41.458 -31.814 -96.831 1.00 35.43 ? 215 PRO A CA 1 ATOM 1617 C C . PRO A 1 215 ? 42.366 -32.871 -97.440 1.00 35.75 ? 215 PRO A C 1 ATOM 1618 O O . PRO A 1 215 ? 43.131 -32.562 -98.345 1.00 34.77 ? 215 PRO A O 1 ATOM 1619 C CB . PRO A 1 215 ? 40.329 -31.456 -97.803 1.00 36.42 ? 215 PRO A CB 1 ATOM 1620 C CG . PRO A 1 215 ? 40.265 -29.962 -97.817 1.00 35.80 ? 215 PRO A CG 1 ATOM 1621 C CD . PRO A 1 215 ? 41.650 -29.482 -97.510 1.00 35.81 ? 215 PRO A CD 1 ATOM 1622 N N . ASN A 1 216 ? 42.300 -34.093 -96.918 1.00 35.88 ? 216 ASN A N 1 ATOM 1623 C CA . ASN A 1 216 ? 43.165 -35.182 -97.352 1.00 35.91 ? 216 ASN A CA 1 ATOM 1624 C C . ASN A 1 216 ? 42.311 -36.345 -97.814 1.00 35.54 ? 216 ASN A C 1 ATOM 1625 O O . ASN A 1 216 ? 41.667 -37.021 -97.008 1.00 35.05 ? 216 ASN A O 1 ATOM 1626 C CB . ASN A 1 216 ? 44.094 -35.655 -96.225 1.00 36.29 ? 216 ASN A CB 1 ATOM 1627 C CG . ASN A 1 216 ? 45.039 -34.572 -95.740 1.00 37.73 ? 216 ASN A CG 1 ATOM 1628 O OD1 . ASN A 1 216 ? 45.136 -34.298 -94.526 1.00 38.59 ? 216 ASN A OD1 1 ATOM 1629 N ND2 . ASN A 1 216 ? 45.758 -33.966 -96.668 1.00 36.62 ? 216 ASN A ND2 1 ATOM 1630 N N . ILE A 1 217 ? 42.329 -36.596 -99.120 1.00 36.18 ? 217 ILE A N 1 ATOM 1631 C CA . ILE A 1 217 ? 41.517 -37.649 -99.713 1.00 35.74 ? 217 ILE A CA 1 ATOM 1632 C C . ILE A 1 217 ? 42.123 -39.003 -99.397 1.00 36.32 ? 217 ILE A C 1 ATOM 1633 O O . ILE A 1 217 ? 43.343 -39.172 -99.425 1.00 36.76 ? 217 ILE A O 1 ATOM 1634 C CB . ILE A 1 217 ? 41.387 -37.435 -101.245 1.00 36.60 ? 217 ILE A CB 1 ATOM 1635 C CG1 . ILE A 1 217 ? 40.600 -36.143 -101.514 1.00 36.06 ? 217 ILE A CG1 1 ATOM 1636 C CG2 . ILE A 1 217 ? 40.734 -38.645 -101.919 1.00 37.47 ? 217 ILE A CG2 1 ATOM 1637 C CD1 . ILE A 1 217 ? 40.880 -35.503 -102.862 1.00 36.88 ? 217 ILE A CD1 1 ATOM 1638 N N . GLY A 1 218 ? 41.274 -39.977 -99.085 1.00 37.41 ? 218 GLY A N 1 ATOM 1639 C CA . GLY A 1 218 ? 41.752 -41.344 -98.870 1.00 38.39 ? 218 GLY A CA 1 ATOM 1640 C C . GLY A 1 218 ? 40.795 -42.171 -98.040 1.00 38.71 ? 218 GLY A C 1 ATOM 1641 O O . GLY A 1 218 ? 40.050 -41.642 -97.215 1.00 38.06 ? 218 GLY A O 1 ATOM 1642 N N . SER A 1 219 ? 40.819 -43.479 -98.260 1.00 38.96 ? 219 SER A N 1 ATOM 1643 C CA . SER A 1 219 ? 39.993 -44.384 -97.476 1.00 39.62 ? 219 SER A CA 1 ATOM 1644 C C . SER A 1 219 ? 40.581 -44.534 -96.073 1.00 38.39 ? 219 SER A C 1 ATOM 1645 O O . SER A 1 219 ? 41.778 -44.770 -95.920 1.00 40.52 ? 219 SER A O 1 ATOM 1646 C CB . SER A 1 219 ? 39.904 -45.753 -98.141 1.00 41.36 ? 219 SER A CB 1 ATOM 1647 O OG . SER A 1 219 ? 39.381 -45.642 -99.446 1.00 43.66 ? 219 SER A OG 1 ATOM 1648 N N . ARG A 1 220 ? 39.729 -44.352 -95.067 1.00 35.96 ? 220 ARG A N 1 ATOM 1649 C CA . ARG A 1 220 ? 40.006 -44.779 -93.697 1.00 36.28 ? 220 ARG A CA 1 ATOM 1650 C C . ARG A 1 220 ? 39.184 -46.048 -93.471 1.00 35.93 ? 220 ARG A C 1 ATOM 1651 O O . ARG A 1 220 ? 38.266 -46.337 -94.257 1.00 36.86 ? 220 ARG A O 1 ATOM 1652 C CB . ARG A 1 220 ? 39.592 -43.704 -92.683 1.00 35.65 ? 220 ARG A CB 1 ATOM 1653 C CG . ARG A 1 220 ? 40.518 -42.497 -92.598 1.00 35.72 ? 220 ARG A CG 1 ATOM 1654 C CD . ARG A 1 220 ? 40.342 -41.551 -93.776 1.00 35.50 ? 220 ARG A CD 1 ATOM 1655 N NE . ARG A 1 220 ? 40.957 -40.238 -93.534 1.00 36.16 ? 220 ARG A NE 1 ATOM 1656 C CZ . ARG A 1 220 ? 41.209 -39.324 -94.474 1.00 37.11 ? 220 ARG A CZ 1 ATOM 1657 N NH1 . ARG A 1 220 ? 40.896 -39.548 -95.746 1.00 36.80 ? 220 ARG A NH1 1 ATOM 1658 N NH2 . ARG A 1 220 ? 41.779 -38.166 -94.141 1.00 38.38 ? 220 ARG A NH2 1 ATOM 1659 N N . PRO A 1 221 ? 39.489 -46.807 -92.409 1.00 35.31 ? 221 PRO A N 1 ATOM 1660 C CA . PRO A 1 221 ? 38.649 -47.975 -92.154 1.00 35.60 ? 221 PRO A CA 1 ATOM 1661 C C . PRO A 1 221 ? 37.191 -47.568 -91.966 1.00 36.04 ? 221 PRO A C 1 ATOM 1662 O O . PRO A 1 221 ? 36.897 -46.552 -91.347 1.00 35.88 ? 221 PRO A O 1 ATOM 1663 C CB . PRO A 1 221 ? 39.262 -48.576 -90.885 1.00 35.85 ? 221 PRO A CB 1 ATOM 1664 C CG . PRO A 1 221 ? 40.712 -48.202 -91.001 1.00 35.64 ? 221 PRO A CG 1 ATOM 1665 C CD . PRO A 1 221 ? 40.659 -46.788 -91.513 1.00 35.73 ? 221 PRO A CD 1 ATOM 1666 N N . ARG A 1 222 ? 36.279 -48.328 -92.550 1.00 36.08 ? 222 ARG A N 1 ATOM 1667 C CA . ARG A 1 222 ? 34.895 -47.907 -92.553 1.00 37.23 ? 222 ARG A CA 1 ATOM 1668 C C . ARG A 1 222 ? 34.326 -47.875 -91.155 1.00 36.66 ? 222 ARG A C 1 ATOM 1669 O O . ARG A 1 222 ? 34.572 -48.762 -90.344 1.00 36.34 ? 222 ARG A O 1 ATOM 1670 C CB . ARG A 1 222 ? 34.060 -48.793 -93.462 1.00 39.89 ? 222 ARG A CB 1 ATOM 1671 C CG . ARG A 1 222 ? 34.406 -48.589 -94.913 1.00 41.48 ? 222 ARG A CG 1 ATOM 1672 C CD . ARG A 1 222 ? 33.420 -49.326 -95.788 1.00 44.71 ? 222 ARG A CD 1 ATOM 1673 N NE . ARG A 1 222 ? 33.646 -49.064 -97.202 1.00 46.17 ? 222 ARG A NE 1 ATOM 1674 C CZ . ARG A 1 222 ? 32.768 -49.345 -98.162 1.00 49.27 ? 222 ARG A CZ 1 ATOM 1675 N NH1 . ARG A 1 222 ? 31.588 -49.886 -97.863 1.00 49.19 ? 222 ARG A NH1 1 ATOM 1676 N NH2 . ARG A 1 222 ? 33.067 -49.070 -99.425 1.00 50.10 ? 222 ARG A NH2 1 ATOM 1677 N N . VAL A 1 223 ? 33.613 -46.793 -90.866 1.00 36.79 ? 223 VAL A N 1 ATOM 1678 C CA . VAL A 1 223 ? 32.879 -46.642 -89.622 1.00 36.57 ? 223 VAL A CA 1 ATOM 1679 C C . VAL A 1 223 ? 31.423 -46.417 -90.033 1.00 37.92 ? 223 VAL A C 1 ATOM 1680 O O . VAL A 1 223 ? 31.122 -45.503 -90.804 1.00 36.23 ? 223 VAL A O 1 ATOM 1681 C CB . VAL A 1 223 ? 33.398 -45.450 -88.809 1.00 36.51 ? 223 VAL A CB 1 ATOM 1682 C CG1 . VAL A 1 223 ? 32.421 -45.103 -87.686 1.00 35.67 ? 223 VAL A CG1 1 ATOM 1683 C CG2 . VAL A 1 223 ? 34.799 -45.746 -88.265 1.00 36.26 ? 223 VAL A CG2 1 ATOM 1684 N N . ARG A 1 224 ? 30.534 -47.261 -89.521 1.00 39.92 ? 224 ARG A N 1 ATOM 1685 C CA . ARG A 1 224 ? 29.133 -47.263 -89.933 1.00 40.37 ? 224 ARG A CA 1 ATOM 1686 C C . ARG A 1 224 ? 29.057 -47.184 -91.467 1.00 40.63 ? 224 ARG A C 1 ATOM 1687 O O . ARG A 1 224 ? 28.294 -46.412 -92.042 1.00 42.15 ? 224 ARG A O 1 ATOM 1688 C CB . ARG A 1 224 ? 28.373 -46.147 -89.199 1.00 41.08 ? 224 ARG A CB 1 ATOM 1689 C CG . ARG A 1 224 ? 28.472 -46.282 -87.670 1.00 41.05 ? 224 ARG A CG 1 ATOM 1690 C CD . ARG A 1 224 ? 27.716 -45.206 -86.889 1.00 41.24 ? 224 ARG A CD 1 ATOM 1691 N NE . ARG A 1 224 ? 28.322 -43.877 -87.007 1.00 39.78 ? 224 ARG A NE 1 ATOM 1692 C CZ . ARG A 1 224 ? 29.402 -43.458 -86.347 1.00 41.08 ? 224 ARG A CZ 1 ATOM 1693 N NH1 . ARG A 1 224 ? 30.045 -44.250 -85.492 1.00 42.49 ? 224 ARG A NH1 1 ATOM 1694 N NH2 . ARG A 1 224 ? 29.856 -42.227 -86.546 1.00 41.33 ? 224 ARG A NH2 1 ATOM 1695 N N . ASP A 1 225 ? 29.904 -47.994 -92.103 1.00 42.26 ? 225 ASP A N 1 ATOM 1696 C CA . ASP A 1 225 ? 30.022 -48.129 -93.563 1.00 43.52 ? 225 ASP A CA 1 ATOM 1697 C C . ASP A 1 225 ? 30.604 -46.916 -94.322 1.00 41.56 ? 225 ASP A C 1 ATOM 1698 O O . ASP A 1 225 ? 30.544 -46.872 -95.553 1.00 39.86 ? 225 ASP A O 1 ATOM 1699 C CB . ASP A 1 225 ? 28.668 -48.550 -94.177 1.00 46.70 ? 225 ASP A CB 1 ATOM 1700 C CG . ASP A 1 225 ? 28.826 -49.366 -95.480 1.00 52.00 ? 225 ASP A CG 1 ATOM 1701 O OD1 . ASP A 1 225 ? 29.800 -50.147 -95.614 1.00 54.34 ? 225 ASP A OD1 1 ATOM 1702 O OD2 . ASP A 1 225 ? 27.966 -49.225 -96.381 1.00 57.50 ? 225 ASP A OD2 1 ATOM 1703 N N . ILE A 1 226 ? 31.198 -45.954 -93.618 1.00 36.38 ? 226 ILE A N 1 ATOM 1704 C CA . ILE A 1 226 ? 31.717 -44.751 -94.264 1.00 34.73 ? 226 ILE A CA 1 ATOM 1705 C C . ILE A 1 226 ? 33.248 -44.702 -94.154 1.00 34.33 ? 226 ILE A C 1 ATOM 1706 O O . ILE A 1 226 ? 33.790 -44.663 -93.028 1.00 32.93 ? 226 ILE A O 1 ATOM 1707 C CB . ILE A 1 226 ? 31.111 -43.477 -93.628 1.00 35.39 ? 226 ILE A CB 1 ATOM 1708 C CG1 . ILE A 1 226 ? 29.594 -43.422 -93.852 1.00 36.58 ? 226 ILE A CG1 1 ATOM 1709 C CG2 . ILE A 1 226 ? 31.784 -42.229 -94.171 1.00 33.82 ? 226 ILE A CG2 1 ATOM 1710 C CD1 . ILE A 1 226 ? 29.172 -43.327 -95.309 1.00 36.11 ? 226 ILE A CD1 1 ATOM 1711 N N . PRO A 1 227 ? 33.949 -44.695 -95.302 1.00 34.24 ? 227 PRO A N 1 ATOM 1712 C CA . PRO A 1 227 ? 35.411 -44.598 -95.322 1.00 34.61 ? 227 PRO A CA 1 ATOM 1713 C C . PRO A 1 227 ? 35.945 -43.163 -95.276 1.00 33.66 ? 227 PRO A C 1 ATOM 1714 O O . PRO A 1 227 ? 37.143 -42.962 -95.105 1.00 33.84 ? 227 PRO A O 1 ATOM 1715 C CB . PRO A 1 227 ? 35.781 -45.259 -96.657 1.00 35.08 ? 227 PRO A CB 1 ATOM 1716 C CG . PRO A 1 227 ? 34.637 -44.953 -97.541 1.00 35.17 ? 227 PRO A CG 1 ATOM 1717 C CD . PRO A 1 227 ? 33.409 -44.940 -96.663 1.00 35.41 ? 227 PRO A CD 1 ATOM 1718 N N . SER A 1 228 ? 35.061 -42.188 -95.428 1.00 34.17 ? 228 SER A N 1 ATOM 1719 C CA . SER A 1 228 ? 35.409 -40.772 -95.319 1.00 33.89 ? 228 SER A CA 1 ATOM 1720 C C . SER A 1 228 ? 35.429 -40.317 -93.854 1.00 32.30 ? 228 SER A C 1 ATOM 1721 O O . SER A 1 228 ? 35.001 -41.054 -92.973 1.00 30.97 ? 228 SER A O 1 ATOM 1722 C CB . SER A 1 228 ? 34.373 -39.934 -96.060 1.00 35.93 ? 228 SER A CB 1 ATOM 1723 O OG . SER A 1 228 ? 34.329 -40.224 -97.443 1.00 38.56 ? 228 SER A OG 1 ATOM 1724 N N . ARG A 1 229 ? 35.903 -39.088 -93.608 1.00 31.88 ? 229 ARG A N 1 ATOM 1725 C CA . ARG A 1 229 ? 35.882 -38.482 -92.277 1.00 30.81 ? 229 ARG A CA 1 ATOM 1726 C C . ARG A 1 229 ? 35.564 -36.993 -92.357 1.00 30.78 ? 229 ARG A C 1 ATOM 1727 O O . ARG A 1 229 ? 35.795 -36.352 -93.382 1.00 32.50 ? 229 ARG A O 1 ATOM 1728 C CB . ARG A 1 229 ? 37.252 -38.631 -91.595 1.00 31.33 ? 229 ARG A CB 1 ATOM 1729 C CG . ARG A 1 229 ? 37.682 -40.062 -91.307 1.00 32.27 ? 229 ARG A CG 1 ATOM 1730 C CD . ARG A 1 229 ? 36.817 -40.737 -90.239 1.00 32.27 ? 229 ARG A CD 1 ATOM 1731 N NE . ARG A 1 229 ? 37.397 -42.038 -89.875 1.00 32.93 ? 229 ARG A NE 1 ATOM 1732 C CZ . ARG A 1 229 ? 37.003 -43.221 -90.349 1.00 34.23 ? 229 ARG A CZ 1 ATOM 1733 N NH1 . ARG A 1 229 ? 35.993 -43.316 -91.235 1.00 33.67 ? 229 ARG A NH1 1 ATOM 1734 N NH2 . ARG A 1 229 ? 37.628 -44.322 -89.948 1.00 32.87 ? 229 ARG A NH2 1 ATOM 1735 N N . ILE A 1 230 ? 35.033 -36.455 -91.264 1.00 29.90 ? 230 ILE A N 1 ATOM 1736 C CA . ILE A 1 230 ? 34.973 -35.008 -91.054 1.00 29.22 ? 230 ILE A CA 1 ATOM 1737 C C . ILE A 1 230 ? 35.881 -34.660 -89.857 1.00 28.49 ? 230 ILE A C 1 ATOM 1738 O O . ILE A 1 230 ? 35.766 -35.274 -88.814 1.00 28.46 ? 230 ILE A O 1 ATOM 1739 C CB . ILE A 1 230 ? 33.532 -34.544 -90.774 1.00 29.33 ? 230 ILE A CB 1 ATOM 1740 C CG1 . ILE A 1 230 ? 32.659 -34.784 -92.021 1.00 30.32 ? 230 ILE A CG1 1 ATOM 1741 C CG2 . ILE A 1 230 ? 33.529 -33.068 -90.387 1.00 29.93 ? 230 ILE A CG2 1 ATOM 1742 C CD1 . ILE A 1 230 ? 31.210 -34.388 -91.851 1.00 31.88 ? 230 ILE A CD1 1 ATOM 1743 N N . SER A 1 231 ? 36.787 -33.697 -90.024 1.00 27.65 ? 231 SER A N 1 ATOM 1744 C CA . SER A 1 231 ? 37.561 -33.172 -88.904 1.00 28.29 ? 231 SER A CA 1 ATOM 1745 C C . SER A 1 231 ? 36.943 -31.851 -88.415 1.00 27.17 ? 231 SER A C 1 ATOM 1746 O O . SER A 1 231 ? 36.645 -30.957 -89.211 1.00 26.43 ? 231 SER A O 1 ATOM 1747 C CB . SER A 1 231 ? 39.035 -32.999 -89.302 1.00 29.10 ? 231 SER A CB 1 ATOM 1748 O OG . SER A 1 231 ? 39.626 -34.281 -89.499 1.00 30.56 ? 231 SER A OG 1 ATOM 1749 N N . ILE A 1 232 ? 36.745 -31.751 -87.109 1.00 26.87 ? 232 ILE A N 1 ATOM 1750 C CA . ILE A 1 232 ? 36.017 -30.630 -86.495 1.00 26.85 ? 232 ILE A CA 1 ATOM 1751 C C . ILE A 1 232 ? 36.966 -29.615 -85.850 1.00 28.19 ? 232 ILE A C 1 ATOM 1752 O O . ILE A 1 232 ? 37.909 -30.003 -85.122 1.00 27.45 ? 232 ILE A O 1 ATOM 1753 C CB . ILE A 1 232 ? 35.034 -31.147 -85.417 1.00 27.27 ? 232 ILE A CB 1 ATOM 1754 C CG1 . ILE A 1 232 ? 33.970 -32.053 -86.037 1.00 27.61 ? 232 ILE A CG1 1 ATOM 1755 C CG2 . ILE A 1 232 ? 34.393 -29.995 -84.640 1.00 27.11 ? 232 ILE A CG2 1 ATOM 1756 C CD1 . ILE A 1 232 ? 33.036 -31.356 -87.020 1.00 29.10 ? 232 ILE A CD1 1 ATOM 1757 N N . TYR A 1 233 ? 36.690 -28.330 -86.113 1.00 26.94 ? 233 TYR A N 1 ATOM 1758 C CA . TYR A 1 233 ? 37.476 -27.193 -85.644 1.00 27.65 ? 233 TYR A CA 1 ATOM 1759 C C . TYR A 1 233 ? 36.545 -26.173 -85.011 1.00 26.85 ? 233 TYR A C 1 ATOM 1760 O O . TYR A 1 233 ? 35.324 -26.225 -85.203 1.00 26.06 ? 233 TYR A O 1 ATOM 1761 C CB . TYR A 1 233 ? 38.274 -26.542 -86.795 1.00 28.32 ? 233 TYR A CB 1 ATOM 1762 C CG . TYR A 1 233 ? 39.262 -27.519 -87.375 1.00 29.47 ? 233 TYR A CG 1 ATOM 1763 C CD1 . TYR A 1 233 ? 38.869 -28.434 -88.340 1.00 29.76 ? 233 TYR A CD1 1 ATOM 1764 C CD2 . TYR A 1 233 ? 40.570 -27.587 -86.897 1.00 30.61 ? 233 TYR A CD2 1 ATOM 1765 C CE1 . TYR A 1 233 ? 39.745 -29.381 -88.828 1.00 30.87 ? 233 TYR A CE1 1 ATOM 1766 C CE2 . TYR A 1 233 ? 41.459 -28.529 -87.383 1.00 31.10 ? 233 TYR A CE2 1 ATOM 1767 C CZ . TYR A 1 233 ? 41.042 -29.419 -88.353 1.00 31.86 ? 233 TYR A CZ 1 ATOM 1768 O OH . TYR A 1 233 ? 41.916 -30.359 -88.841 1.00 33.89 ? 233 TYR A OH 1 ATOM 1769 N N . TRP A 1 234 ? 37.120 -25.257 -84.236 1.00 26.76 ? 234 TRP A N 1 ATOM 1770 C CA . TRP A 1 234 ? 36.336 -24.208 -83.617 1.00 27.08 ? 234 TRP A CA 1 ATOM 1771 C C . TRP A 1 234 ? 37.072 -22.902 -83.594 1.00 27.20 ? 234 TRP A C 1 ATOM 1772 O O . TRP A 1 234 ? 38.307 -22.852 -83.629 1.00 27.36 ? 234 TRP A O 1 ATOM 1773 C CB . TRP A 1 234 ? 35.888 -24.621 -82.220 1.00 28.57 ? 234 TRP A CB 1 ATOM 1774 C CG . TRP A 1 234 ? 36.963 -24.584 -81.165 1.00 30.40 ? 234 TRP A CG 1 ATOM 1775 C CD1 . TRP A 1 234 ? 37.303 -23.523 -80.319 1.00 31.78 ? 234 TRP A CD1 1 ATOM 1776 C CD2 . TRP A 1 234 ? 37.842 -25.670 -80.786 1.00 32.32 ? 234 TRP A CD2 1 ATOM 1777 N NE1 . TRP A 1 234 ? 38.319 -23.881 -79.484 1.00 33.22 ? 234 TRP A NE1 1 ATOM 1778 C CE2 . TRP A 1 234 ? 38.688 -25.156 -79.712 1.00 32.40 ? 234 TRP A CE2 1 ATOM 1779 C CE3 . TRP A 1 234 ? 38.005 -26.976 -81.209 1.00 33.74 ? 234 TRP A CE3 1 ATOM 1780 C CZ2 . TRP A 1 234 ? 39.643 -25.925 -79.111 1.00 34.75 ? 234 TRP A CZ2 1 ATOM 1781 C CZ3 . TRP A 1 234 ? 38.981 -27.757 -80.589 1.00 35.43 ? 234 TRP A CZ3 1 ATOM 1782 C CH2 . TRP A 1 234 ? 39.785 -27.237 -79.564 1.00 35.85 ? 234 TRP A CH2 1 ATOM 1783 N N . THR A 1 235 ? 36.301 -21.837 -83.557 1.00 26.75 ? 235 THR A N 1 ATOM 1784 C CA . THR A 1 235 ? 36.818 -20.479 -83.576 1.00 27.92 ? 235 THR A CA 1 ATOM 1785 C C . THR A 1 235 ? 35.936 -19.622 -82.689 1.00 28.70 ? 235 THR A C 1 ATOM 1786 O O . THR A 1 235 ? 34.702 -19.629 -82.829 1.00 28.44 ? 235 THR A O 1 ATOM 1787 C CB . THR A 1 235 ? 36.790 -19.902 -85.013 1.00 28.20 ? 235 THR A CB 1 ATOM 1788 O OG1 . THR A 1 235 ? 37.392 -20.831 -85.936 1.00 27.61 ? 235 THR A OG1 1 ATOM 1789 C CG2 . THR A 1 235 ? 37.509 -18.517 -85.093 1.00 29.36 ? 235 THR A CG2 1 ATOM 1790 N N . ILE A 1 236 ? 36.557 -18.863 -81.789 1.00 29.01 ? 236 ILE A N 1 ATOM 1791 C CA . ILE A 1 236 ? 35.825 -17.925 -80.943 1.00 29.74 ? 236 ILE A CA 1 ATOM 1792 C C . ILE A 1 236 ? 36.008 -16.530 -81.519 1.00 30.21 ? 236 ILE A C 1 ATOM 1793 O O . ILE A 1 236 ? 37.140 -16.103 -81.779 1.00 32.41 ? 236 ILE A O 1 ATOM 1794 C CB . ILE A 1 236 ? 36.295 -18.007 -79.469 1.00 30.62 ? 236 ILE A CB 1 ATOM 1795 C CG1 . ILE A 1 236 ? 35.858 -19.352 -78.869 1.00 31.85 ? 236 ILE A CG1 1 ATOM 1796 C CG2 . ILE A 1 236 ? 35.712 -16.860 -78.643 1.00 31.63 ? 236 ILE A CG2 1 ATOM 1797 C CD1 . ILE A 1 236 ? 36.580 -19.762 -77.591 1.00 31.92 ? 236 ILE A CD1 1 ATOM 1798 N N . VAL A 1 237 ? 34.905 -15.825 -81.739 1.00 30.62 ? 237 VAL A N 1 ATOM 1799 C CA . VAL A 1 237 ? 34.935 -14.490 -82.335 1.00 31.77 ? 237 VAL A CA 1 ATOM 1800 C C . VAL A 1 237 ? 34.441 -13.451 -81.324 1.00 33.32 ? 237 VAL A C 1 ATOM 1801 O O . VAL A 1 237 ? 33.307 -13.507 -80.863 1.00 32.91 ? 237 VAL A O 1 ATOM 1802 C CB . VAL A 1 237 ? 34.079 -14.439 -83.616 1.00 32.59 ? 237 VAL A CB 1 ATOM 1803 C CG1 . VAL A 1 237 ? 34.081 -13.045 -84.225 1.00 31.84 ? 237 VAL A CG1 1 ATOM 1804 C CG2 . VAL A 1 237 ? 34.578 -15.475 -84.626 1.00 32.35 ? 237 VAL A CG2 1 ATOM 1805 N N . LYS A 1 238 ? 35.305 -12.497 -81.011 1.00 34.78 ? 238 LYS A N 1 ATOM 1806 C CA . LYS A 1 238 ? 35.029 -11.440 -80.040 1.00 37.12 ? 238 LYS A CA 1 ATOM 1807 C C . LYS A 1 238 ? 34.136 -10.349 -80.614 1.00 37.45 ? 238 LYS A C 1 ATOM 1808 O O . LYS A 1 238 ? 34.085 -10.165 -81.832 1.00 37.94 ? 238 LYS A O 1 ATOM 1809 C CB . LYS A 1 238 ? 36.333 -10.767 -79.607 1.00 39.79 ? 238 LYS A CB 1 ATOM 1810 C CG . LYS A 1 238 ? 37.451 -11.704 -79.173 1.00 41.72 ? 238 LYS A CG 1 ATOM 1811 C CD . LYS A 1 238 ? 37.125 -12.465 -77.908 1.00 41.05 ? 238 LYS A CD 1 ATOM 1812 C CE . LYS A 1 238 ? 37.330 -11.613 -76.671 1.00 42.79 ? 238 LYS A CE 1 ATOM 1813 N NZ . LYS A 1 238 ? 36.752 -12.299 -75.489 1.00 42.36 ? 238 LYS A NZ 1 ATOM 1814 N N . PRO A 1 239 ? 33.464 -9.584 -79.737 1.00 37.96 ? 239 PRO A N 1 ATOM 1815 C CA . PRO A 1 239 ? 32.767 -8.366 -80.174 1.00 39.93 ? 239 PRO A CA 1 ATOM 1816 C C . PRO A 1 239 ? 33.704 -7.461 -80.949 1.00 39.93 ? 239 PRO A C 1 ATOM 1817 O O . PRO A 1 239 ? 34.838 -7.274 -80.540 1.00 38.42 ? 239 PRO A O 1 ATOM 1818 C CB . PRO A 1 239 ? 32.365 -7.701 -78.847 1.00 40.65 ? 239 PRO A CB 1 ATOM 1819 C CG . PRO A 1 239 ? 32.266 -8.845 -77.891 1.00 39.87 ? 239 PRO A CG 1 ATOM 1820 C CD . PRO A 1 239 ? 33.392 -9.750 -78.277 1.00 38.71 ? 239 PRO A CD 1 ATOM 1821 N N . GLY A 1 240 ? 33.247 -6.951 -82.086 1.00 42.25 ? 240 GLY A N 1 ATOM 1822 C CA . GLY A 1 240 ? 34.061 -6.073 -82.927 1.00 43.60 ? 240 GLY A CA 1 ATOM 1823 C C . GLY A 1 240 ? 34.936 -6.815 -83.915 1.00 42.55 ? 240 GLY A C 1 ATOM 1824 O O . GLY A 1 240 ? 35.536 -6.207 -84.789 1.00 43.71 ? 240 GLY A O 1 ATOM 1825 N N . ASP A 1 241 ? 35.035 -8.132 -83.774 1.00 42.04 ? 241 ASP A N 1 ATOM 1826 C CA . ASP A 1 241 ? 35.784 -8.938 -84.725 1.00 40.22 ? 241 ASP A CA 1 ATOM 1827 C C . ASP A 1 241 ? 34.826 -9.521 -85.771 1.00 39.96 ? 241 ASP A C 1 ATOM 1828 O O . ASP A 1 241 ? 33.604 -9.320 -85.697 1.00 38.46 ? 241 ASP A O 1 ATOM 1829 C CB . ASP A 1 241 ? 36.568 -10.036 -84.007 1.00 40.18 ? 241 ASP A CB 1 ATOM 1830 C CG . ASP A 1 241 ? 37.877 -10.391 -84.715 1.00 41.29 ? 241 ASP A CG 1 ATOM 1831 O OD1 . ASP A 1 241 ? 37.985 -10.198 -85.956 1.00 42.72 ? 241 ASP A OD1 1 ATOM 1832 O OD2 . ASP A 1 241 ? 38.808 -10.859 -84.026 1.00 42.41 ? 241 ASP A OD2 1 ATOM 1833 N N . ILE A 1 242 ? 35.407 -10.195 -86.761 1.00 38.48 ? 242 ILE A N 1 ATOM 1834 C CA . ILE A 1 242 ? 34.701 -10.723 -87.929 1.00 39.69 ? 242 ILE A CA 1 ATOM 1835 C C . ILE A 1 242 ? 35.223 -12.115 -88.260 1.00 37.82 ? 242 ILE A C 1 ATOM 1836 O O . ILE A 1 242 ? 36.426 -12.336 -88.251 1.00 39.77 ? 242 ILE A O 1 ATOM 1837 C CB . ILE A 1 242 ? 34.979 -9.848 -89.179 1.00 41.22 ? 242 ILE A CB 1 ATOM 1838 C CG1 . ILE A 1 242 ? 34.545 -8.394 -88.951 1.00 42.79 ? 242 ILE A CG1 1 ATOM 1839 C CG2 . ILE A 1 242 ? 34.279 -10.415 -90.401 1.00 41.82 ? 242 ILE A CG2 1 ATOM 1840 C CD1 . ILE A 1 242 ? 35.121 -7.430 -89.980 1.00 44.72 ? 242 ILE A CD1 1 ATOM 1841 N N . LEU A 1 243 ? 34.321 -13.044 -88.548 1.00 36.10 ? 243 LEU A N 1 ATOM 1842 C CA . LEU A 1 243 ? 34.681 -14.361 -89.030 1.00 33.59 ? 243 LEU A CA 1 ATOM 1843 C C . LEU A 1 243 ? 34.757 -14.299 -90.551 1.00 35.64 ? 243 LEU A C 1 ATOM 1844 O O . LEU A 1 243 ? 33.838 -13.785 -91.182 1.00 36.10 ? 243 LEU A O 1 ATOM 1845 C CB . LEU A 1 243 ? 33.603 -15.360 -88.644 1.00 32.30 ? 243 LEU A CB 1 ATOM 1846 C CG . LEU A 1 243 ? 33.887 -16.828 -88.928 1.00 31.96 ? 243 LEU A CG 1 ATOM 1847 C CD1 . LEU A 1 243 ? 34.983 -17.343 -87.996 1.00 30.58 ? 243 LEU A CD1 1 ATOM 1848 C CD2 . LEU A 1 243 ? 32.621 -17.658 -88.762 1.00 31.51 ? 243 LEU A CD2 1 ATOM 1849 N N . LEU A 1 244 ? 35.835 -14.818 -91.125 1.00 34.72 ? 244 LEU A N 1 ATOM 1850 C CA . LEU A 1 244 ? 35.977 -14.925 -92.576 1.00 37.03 ? 244 LEU A CA 1 ATOM 1851 C C . LEU A 1 244 ? 36.283 -16.377 -92.946 1.00 36.50 ? 244 LEU A C 1 ATOM 1852 O O . LEU A 1 244 ? 37.221 -16.982 -92.413 1.00 36.47 ? 244 LEU A O 1 ATOM 1853 C CB . LEU A 1 244 ? 37.070 -13.977 -93.076 1.00 38.36 ? 244 LEU A CB 1 ATOM 1854 C CG . LEU A 1 244 ? 37.279 -13.797 -94.581 1.00 39.76 ? 244 LEU A CG 1 ATOM 1855 C CD1 . LEU A 1 244 ? 35.962 -13.595 -95.324 1.00 41.85 ? 244 LEU A CD1 1 ATOM 1856 C CD2 . LEU A 1 244 ? 38.194 -12.600 -94.812 1.00 41.03 ? 244 LEU A CD2 1 ATOM 1857 N N . ILE A 1 245 ? 35.458 -16.935 -93.836 1.00 35.52 ? 245 ILE A N 1 ATOM 1858 C CA . ILE A 1 245 ? 35.582 -18.311 -94.298 1.00 34.64 ? 245 ILE A CA 1 ATOM 1859 C C . ILE A 1 245 ? 35.937 -18.306 -95.796 1.00 36.15 ? 245 ILE A C 1 ATOM 1860 O O . ILE A 1 245 ? 35.232 -17.707 -96.603 1.00 35.95 ? 245 ILE A O 1 ATOM 1861 C CB . ILE A 1 245 ? 34.274 -19.103 -94.057 1.00 34.78 ? 245 ILE A CB 1 ATOM 1862 C CG1 . ILE A 1 245 ? 33.940 -19.140 -92.556 1.00 34.64 ? 245 ILE A CG1 1 ATOM 1863 C CG2 . ILE A 1 245 ? 34.376 -20.510 -94.634 1.00 34.61 ? 245 ILE A CG2 1 ATOM 1864 C CD1 . ILE A 1 245 ? 32.614 -19.782 -92.217 1.00 34.89 ? 245 ILE A CD1 1 ATOM 1865 N N . ASN A 1 246 ? 37.013 -19.003 -96.138 1.00 36.43 ? 246 ASN A N 1 ATOM 1866 C CA . ASN A 1 246 ? 37.613 -18.982 -97.478 1.00 39.06 ? 246 ASN A CA 1 ATOM 1867 C C . ASN A 1 246 ? 37.843 -20.440 -97.892 1.00 38.70 ? 246 ASN A C 1 ATOM 1868 O O . ASN A 1 246 ? 38.617 -21.154 -97.246 1.00 39.50 ? 246 ASN A O 1 ATOM 1869 C CB . ASN A 1 246 ? 38.930 -18.198 -97.386 1.00 41.15 ? 246 ASN A CB 1 ATOM 1870 C CG . ASN A 1 246 ? 39.534 -17.799 -98.742 1.00 44.78 ? 246 ASN A CG 1 ATOM 1871 O OD1 . ASN A 1 246 ? 40.715 -17.463 -98.792 1.00 45.63 ? 246 ASN A OD1 1 ATOM 1872 N ND2 . ASN A 1 246 ? 38.760 -17.819 -99.816 1.00 48.15 ? 246 ASN A ND2 1 ATOM 1873 N N . SER A 1 247 ? 37.155 -20.892 -98.941 1.00 38.48 ? 247 SER A N 1 ATOM 1874 C CA . SER A 1 247 ? 37.171 -22.305 -99.324 1.00 37.98 ? 247 SER A CA 1 ATOM 1875 C C . SER A 1 247 ? 36.784 -22.516 -100.785 1.00 38.88 ? 247 SER A C 1 ATOM 1876 O O . SER A 1 247 ? 36.032 -21.722 -101.347 1.00 37.84 ? 247 SER A O 1 ATOM 1877 C CB . SER A 1 247 ? 36.186 -23.083 -98.458 1.00 38.41 ? 247 SER A CB 1 ATOM 1878 O OG . SER A 1 247 ? 36.053 -24.429 -98.882 1.00 38.63 ? 247 SER A OG 1 ATOM 1879 N N . THR A 1 248 ? 37.282 -23.608 -101.363 1.00 39.16 ? 248 THR A N 1 ATOM 1880 C CA . THR A 1 248 ? 36.902 -24.047 -102.710 1.00 41.81 ? 248 THR A CA 1 ATOM 1881 C C . THR A 1 248 ? 36.324 -25.467 -102.714 1.00 41.33 ? 248 THR A C 1 ATOM 1882 O O . THR A 1 248 ? 36.231 -26.116 -103.773 1.00 42.01 ? 248 THR A O 1 ATOM 1883 C CB . THR A 1 248 ? 38.123 -24.045 -103.634 1.00 43.71 ? 248 THR A CB 1 ATOM 1884 O OG1 . THR A 1 248 ? 39.156 -24.828 -103.019 1.00 45.27 ? 248 THR A OG1 1 ATOM 1885 C CG2 . THR A 1 248 ? 38.609 -22.610 -103.869 1.00 43.60 ? 248 THR A CG2 1 ATOM 1886 N N . GLY A 1 249 ? 35.914 -25.937 -101.537 1.00 38.91 ? 249 GLY A N 1 ATOM 1887 C CA . GLY A 1 249 ? 35.360 -27.277 -101.387 1.00 37.22 ? 249 GLY A CA 1 ATOM 1888 C C . GLY A 1 249 ? 35.656 -27.846 -100.019 1.00 35.59 ? 249 GLY A C 1 ATOM 1889 O O . GLY A 1 249 ? 36.464 -27.294 -99.271 1.00 35.03 ? 249 GLY A O 1 ATOM 1890 N N . ASN A 1 250 ? 34.998 -28.957 -99.705 1.00 34.52 ? 250 ASN A N 1 ATOM 1891 C CA . ASN A 1 250 ? 35.278 -29.752 -98.501 1.00 33.95 ? 250 ASN A CA 1 ATOM 1892 C C . ASN A 1 250 ? 34.895 -29.081 -97.177 1.00 32.71 ? 250 ASN A C 1 ATOM 1893 O O . ASN A 1 250 ? 35.238 -29.578 -96.106 1.00 32.07 ? 250 ASN A O 1 ATOM 1894 C CB . ASN A 1 250 ? 36.751 -30.176 -98.475 1.00 33.20 ? 250 ASN A CB 1 ATOM 1895 C CG . ASN A 1 250 ? 37.172 -30.929 -99.733 1.00 33.56 ? 250 ASN A CG 1 ATOM 1896 O OD1 . ASN A 1 250 ? 37.421 -30.322 -100.782 1.00 34.67 ? 250 ASN A OD1 1 ATOM 1897 N ND2 . ASN A 1 250 ? 37.268 -32.251 -99.627 1.00 30.99 ? 250 ASN A ND2 1 ATOM 1898 N N . LEU A 1 251 ? 34.173 -27.969 -97.268 1.00 32.29 ? 251 LEU A N 1 ATOM 1899 C CA . LEU A 1 251 ? 33.764 -27.193 -96.111 1.00 32.11 ? 251 LEU A CA 1 ATOM 1900 C C . LEU A 1 251 ? 32.467 -27.732 -95.529 1.00 32.02 ? 251 LEU A C 1 ATOM 1901 O O . LEU A 1 251 ? 31.445 -27.796 -96.215 1.00 31.56 ? 251 LEU A O 1 ATOM 1902 C CB . LEU A 1 251 ? 33.577 -25.712 -96.488 1.00 31.65 ? 251 LEU A CB 1 ATOM 1903 C CG . LEU A 1 251 ? 33.140 -24.784 -95.341 1.00 32.39 ? 251 LEU A CG 1 ATOM 1904 C CD1 . LEU A 1 251 ? 34.175 -24.724 -94.211 1.00 30.59 ? 251 LEU A CD1 1 ATOM 1905 C CD2 . LEU A 1 251 ? 32.838 -23.393 -95.889 1.00 31.49 ? 251 LEU A CD2 1 ATOM 1906 N N . ILE A 1 252 ? 32.518 -28.114 -94.256 1.00 30.35 ? 252 ILE A N 1 ATOM 1907 C CA . ILE A 1 252 ? 31.331 -28.362 -93.468 1.00 30.50 ? 252 ILE A CA 1 ATOM 1908 C C . ILE A 1 252 ? 31.090 -27.072 -92.673 1.00 30.23 ? 252 ILE A C 1 ATOM 1909 O O . ILE A 1 252 ? 31.756 -26.796 -91.663 1.00 28.22 ? 252 ILE A O 1 ATOM 1910 C CB . ILE A 1 252 ? 31.526 -29.586 -92.556 1.00 31.60 ? 252 ILE A CB 1 ATOM 1911 C CG1 . ILE A 1 252 ? 31.869 -30.832 -93.391 1.00 32.40 ? 252 ILE A CG1 1 ATOM 1912 C CG2 . ILE A 1 252 ? 30.283 -29.872 -91.724 1.00 31.10 ? 252 ILE A CG2 1 ATOM 1913 C CD1 . ILE A 1 252 ? 30.867 -31.150 -94.497 1.00 32.22 ? 252 ILE A CD1 1 ATOM 1914 N N . ALA A 1 253 ? 30.141 -26.275 -93.147 1.00 29.50 ? 253 ALA A N 1 ATOM 1915 C CA . ALA A 1 253 ? 29.966 -24.913 -92.663 1.00 29.78 ? 253 ALA A CA 1 ATOM 1916 C C . ALA A 1 253 ? 29.129 -24.840 -91.387 1.00 29.08 ? 253 ALA A C 1 ATOM 1917 O O . ALA A 1 253 ? 28.266 -25.695 -91.145 1.00 27.65 ? 253 ALA A O 1 ATOM 1918 C CB . ALA A 1 253 ? 29.337 -24.055 -93.752 1.00 30.47 ? 253 ALA A CB 1 ATOM 1919 N N . PRO A 1 254 ? 29.373 -23.800 -90.569 1.00 29.63 ? 254 PRO A N 1 ATOM 1920 C CA . PRO A 1 254 ? 28.523 -23.514 -89.412 1.00 29.94 ? 254 PRO A CA 1 ATOM 1921 C C . PRO A 1 254 ? 27.177 -22.927 -89.855 1.00 30.63 ? 254 PRO A C 1 ATOM 1922 O O . PRO A 1 254 ? 27.111 -22.308 -90.921 1.00 30.18 ? 254 PRO A O 1 ATOM 1923 C CB . PRO A 1 254 ? 29.333 -22.466 -88.647 1.00 30.53 ? 254 PRO A CB 1 ATOM 1924 C CG . PRO A 1 254 ? 30.072 -21.723 -89.720 1.00 30.92 ? 254 PRO A CG 1 ATOM 1925 C CD . PRO A 1 254 ? 30.401 -22.757 -90.770 1.00 30.35 ? 254 PRO A CD 1 ATOM 1926 N N . ARG A 1 255 ? 26.129 -23.136 -89.056 1.00 30.21 ? 255 ARG A N 1 ATOM 1927 C CA . ARG A 1 255 ? 24.802 -22.547 -89.319 1.00 31.80 ? 255 ARG A CA 1 ATOM 1928 C C . ARG A 1 255 ? 24.543 -21.338 -88.427 1.00 31.62 ? 255 ARG A C 1 ATOM 1929 O O . ARG A 1 255 ? 23.469 -20.705 -88.480 1.00 32.04 ? 255 ARG A O 1 ATOM 1930 C CB . ARG A 1 255 ? 23.705 -23.583 -89.090 1.00 31.90 ? 255 ARG A CB 1 ATOM 1931 C CG . ARG A 1 255 ? 23.732 -24.718 -90.088 1.00 32.01 ? 255 ARG A CG 1 ATOM 1932 C CD . ARG A 1 255 ? 22.463 -25.538 -90.016 1.00 32.99 ? 255 ARG A CD 1 ATOM 1933 N NE . ARG A 1 255 ? 22.519 -26.676 -90.932 1.00 33.52 ? 255 ARG A NE 1 ATOM 1934 C CZ . ARG A 1 255 ? 22.107 -26.654 -92.205 1.00 34.59 ? 255 ARG A CZ 1 ATOM 1935 N NH1 . ARG A 1 255 ? 21.570 -25.563 -92.747 1.00 34.83 ? 255 ARG A NH1 1 ATOM 1936 N NH2 . ARG A 1 255 ? 22.216 -27.753 -92.936 1.00 34.43 ? 255 ARG A NH2 1 ATOM 1937 N N . GLY A 1 256 ? 25.532 -21.021 -87.602 1.00 30.35 ? 256 GLY A N 1 ATOM 1938 C CA . GLY A 1 256 ? 25.371 -20.033 -86.548 1.00 30.04 ? 256 GLY A CA 1 ATOM 1939 C C . GLY A 1 256 ? 26.438 -20.240 -85.504 1.00 28.50 ? 256 GLY A C 1 ATOM 1940 O O . GLY A 1 256 ? 27.456 -20.890 -85.779 1.00 28.30 ? 256 GLY A O 1 ATOM 1941 N N . TYR A 1 257 ? 26.207 -19.701 -84.316 1.00 28.42 ? 257 TYR A N 1 ATOM 1942 C CA . TYR A 1 257 ? 27.183 -19.778 -83.233 1.00 29.10 ? 257 TYR A CA 1 ATOM 1943 C C . TYR A 1 257 ? 26.550 -20.239 -81.941 1.00 28.27 ? 257 TYR A C 1 ATOM 1944 O O . TYR A 1 257 ? 25.351 -20.078 -81.731 1.00 28.97 ? 257 TYR A O 1 ATOM 1945 C CB . TYR A 1 257 ? 27.822 -18.409 -82.994 1.00 29.28 ? 257 TYR A CB 1 ATOM 1946 C CG . TYR A 1 257 ? 26.832 -17.347 -82.588 1.00 30.16 ? 257 TYR A CG 1 ATOM 1947 C CD1 . TYR A 1 257 ? 26.513 -17.143 -81.257 1.00 30.51 ? 257 TYR A CD1 1 ATOM 1948 C CD2 . TYR A 1 257 ? 26.194 -16.564 -83.546 1.00 31.56 ? 257 TYR A CD2 1 ATOM 1949 C CE1 . TYR A 1 257 ? 25.601 -16.182 -80.879 1.00 31.81 ? 257 TYR A CE1 1 ATOM 1950 C CE2 . TYR A 1 257 ? 25.262 -15.600 -83.180 1.00 32.51 ? 257 TYR A CE2 1 ATOM 1951 C CZ . TYR A 1 257 ? 24.979 -15.411 -81.849 1.00 32.75 ? 257 TYR A CZ 1 ATOM 1952 O OH . TYR A 1 257 ? 24.084 -14.466 -81.448 1.00 33.48 ? 257 TYR A OH 1 ATOM 1953 N N . PHE A 1 258 ? 27.382 -20.790 -81.065 1.00 27.23 ? 258 PHE A N 1 ATOM 1954 C CA . PHE A 1 258 ? 26.980 -21.082 -79.706 1.00 27.20 ? 258 PHE A CA 1 ATOM 1955 C C . PHE A 1 258 ? 27.346 -19.902 -78.852 1.00 30.20 ? 258 PHE A C 1 ATOM 1956 O O . PHE A 1 258 ? 28.372 -19.230 -79.087 1.00 29.84 ? 258 PHE A O 1 ATOM 1957 C CB . PHE A 1 258 ? 27.692 -22.334 -79.196 1.00 25.60 ? 258 PHE A CB 1 ATOM 1958 C CG . PHE A 1 258 ? 27.289 -23.567 -79.926 1.00 24.50 ? 258 PHE A CG 1 ATOM 1959 C CD1 . PHE A 1 258 ? 27.906 -23.917 -81.094 1.00 25.04 ? 258 PHE A CD1 1 ATOM 1960 C CD2 . PHE A 1 258 ? 26.240 -24.344 -79.456 1.00 25.31 ? 258 PHE A CD2 1 ATOM 1961 C CE1 . PHE A 1 258 ? 27.552 -25.069 -81.762 1.00 25.41 ? 258 PHE A CE1 1 ATOM 1962 C CE2 . PHE A 1 258 ? 25.838 -25.474 -80.134 1.00 24.90 ? 258 PHE A CE2 1 ATOM 1963 C CZ . PHE A 1 258 ? 26.492 -25.840 -81.284 1.00 25.79 ? 258 PHE A CZ 1 ATOM 1964 N N . LYS A 1 259 ? 26.487 -19.635 -77.885 1.00 32.06 ? 259 LYS A N 1 ATOM 1965 C CA . LYS A 1 259 ? 26.831 -18.750 -76.814 1.00 36.82 ? 259 LYS A CA 1 ATOM 1966 C C . LYS A 1 259 ? 27.972 -19.431 -76.079 1.00 37.74 ? 259 LYS A C 1 ATOM 1967 O O . LYS A 1 259 ? 28.071 -20.677 -76.042 1.00 37.90 ? 259 LYS A O 1 ATOM 1968 C CB . LYS A 1 259 ? 25.641 -18.547 -75.889 1.00 40.79 ? 259 LYS A CB 1 ATOM 1969 C CG . LYS A 1 259 ? 24.509 -17.766 -76.533 1.00 43.43 ? 259 LYS A CG 1 ATOM 1970 C CD . LYS A 1 259 ? 24.424 -16.341 -76.005 1.00 47.45 ? 259 LYS A CD 1 ATOM 1971 C CE . LYS A 1 259 ? 23.214 -15.626 -76.581 1.00 50.15 ? 259 LYS A CE 1 ATOM 1972 N NZ . LYS A 1 259 ? 22.809 -14.456 -75.754 1.00 53.22 ? 259 LYS A NZ 1 ATOM 1973 N N . ILE A 1 260 ? 28.876 -18.631 -75.559 1.00 36.46 ? 260 ILE A N 1 ATOM 1974 C CA . ILE A 1 260 ? 29.865 -19.162 -74.670 1.00 36.41 ? 260 ILE A CA 1 ATOM 1975 C C . ILE A 1 260 ? 29.775 -18.329 -73.397 1.00 37.08 ? 260 ILE A C 1 ATOM 1976 O O . ILE A 1 260 ? 29.855 -17.102 -73.446 1.00 38.10 ? 260 ILE A O 1 ATOM 1977 C CB . ILE A 1 260 ? 31.248 -19.218 -75.346 1.00 37.52 ? 260 ILE A CB 1 ATOM 1978 C CG1 . ILE A 1 260 ? 32.298 -19.754 -74.373 1.00 38.75 ? 260 ILE A CG1 1 ATOM 1979 C CG2 . ILE A 1 260 ? 31.633 -17.872 -75.923 1.00 37.97 ? 260 ILE A CG2 1 ATOM 1980 C CD1 . ILE A 1 260 ? 33.474 -20.415 -75.064 1.00 38.66 ? 260 ILE A CD1 1 ATOM 1981 N N . ARG A 1 261 ? 29.517 -19.001 -72.276 1.00 36.07 ? 261 ARG A N 1 ATOM 1982 C CA . ARG A 1 261 ? 29.320 -18.341 -70.984 1.00 37.58 ? 261 ARG A CA 1 ATOM 1983 C C . ARG A 1 261 ? 30.457 -18.738 -70.064 1.00 36.31 ? 261 ARG A C 1 ATOM 1984 O O . ARG A 1 261 ? 31.168 -19.700 -70.335 1.00 34.28 ? 261 ARG A O 1 ATOM 1985 C CB . ARG A 1 261 ? 27.975 -18.762 -70.373 1.00 40.07 ? 261 ARG A CB 1 ATOM 1986 C CG . ARG A 1 261 ? 26.778 -18.335 -71.226 1.00 43.71 ? 261 ARG A CG 1 ATOM 1987 C CD . ARG A 1 261 ? 25.422 -18.632 -70.575 1.00 48.08 ? 261 ARG A CD 1 ATOM 1988 N NE . ARG A 1 261 ? 24.301 -18.281 -71.464 1.00 51.17 ? 261 ARG A NE 1 ATOM 1989 C CZ . ARG A 1 261 ? 23.806 -17.050 -71.635 1.00 55.41 ? 261 ARG A CZ 1 ATOM 1990 N NH1 . ARG A 1 261 ? 24.304 -16.010 -70.973 1.00 55.95 ? 261 ARG A NH1 1 ATOM 1991 N NH2 . ARG A 1 261 ? 22.793 -16.849 -72.480 1.00 56.66 ? 261 ARG A NH2 1 ATOM 1992 N N . SER A 1 262 ? 30.642 -17.988 -68.985 1.00 38.11 ? 262 SER A N 1 ATOM 1993 C CA . SER A 1 262 ? 31.512 -18.448 -67.900 1.00 38.98 ? 262 SER A CA 1 ATOM 1994 C C . SER A 1 262 ? 30.682 -18.692 -66.652 1.00 37.75 ? 262 SER A C 1 ATOM 1995 O O . SER A 1 262 ? 29.705 -17.989 -66.376 1.00 36.23 ? 262 SER A O 1 ATOM 1996 C CB . SER A 1 262 ? 32.629 -17.451 -67.615 1.00 41.91 ? 262 SER A CB 1 ATOM 1997 O OG . SER A 1 262 ? 32.106 -16.224 -67.168 1.00 45.45 ? 262 SER A OG 1 ATOM 1998 N N . GLY A 1 263 ? 31.059 -19.709 -65.901 1.00 34.98 ? 263 GLY A N 1 ATOM 1999 C CA . GLY A 1 263 ? 30.424 -19.958 -64.628 1.00 34.92 ? 263 GLY A CA 1 ATOM 2000 C C . GLY A 1 263 ? 30.964 -21.262 -64.091 1.00 33.24 ? 263 GLY A C 1 ATOM 2001 O O . GLY A 1 263 ? 32.092 -21.637 -64.403 1.00 33.88 ? 263 GLY A O 1 ATOM 2002 N N . LYS A 1 264 ? 30.116 -21.967 -63.357 1.00 31.46 ? 264 LYS A N 1 ATOM 2003 C CA . LYS A 1 264 ? 30.542 -23.073 -62.518 1.00 30.44 ? 264 LYS A CA 1 ATOM 2004 C C . LYS A 1 264 ? 30.181 -24.449 -63.082 1.00 25.75 ? 264 LYS A C 1 ATOM 2005 O O . LYS A 1 264 ? 30.148 -25.412 -62.345 1.00 24.56 ? 264 LYS A O 1 ATOM 2006 C CB . LYS A 1 264 ? 29.920 -22.868 -61.139 1.00 33.33 ? 264 LYS A CB 1 ATOM 2007 C CG . LYS A 1 264 ? 30.418 -21.576 -60.475 1.00 37.75 ? 264 LYS A CG 1 ATOM 2008 C CD . LYS A 1 264 ? 29.634 -21.251 -59.209 1.00 41.61 ? 264 LYS A CD 1 ATOM 2009 C CE . LYS A 1 264 ? 30.368 -20.205 -58.358 1.00 44.62 ? 264 LYS A CE 1 ATOM 2010 N NZ . LYS A 1 264 ? 29.720 -20.055 -57.019 1.00 46.30 ? 264 LYS A NZ 1 ATOM 2011 N N . SER A 1 265 ? 29.927 -24.540 -64.385 1.00 23.43 ? 265 SER A N 1 ATOM 2012 C CA . SER A 1 265 ? 29.472 -25.807 -64.969 1.00 22.01 ? 265 SER A CA 1 ATOM 2013 C C . SER A 1 265 ? 30.643 -26.755 -65.209 1.00 21.63 ? 265 SER A C 1 ATOM 2014 O O . SER A 1 265 ? 31.789 -26.325 -65.338 1.00 20.39 ? 265 SER A O 1 ATOM 2015 C CB . SER A 1 265 ? 28.699 -25.557 -66.266 1.00 22.70 ? 265 SER A CB 1 ATOM 2016 O OG . SER A 1 265 ? 27.541 -24.776 -65.990 1.00 22.72 ? 265 SER A OG 1 ATOM 2017 N N . SER A 1 266 ? 30.342 -28.042 -65.277 1.00 20.67 ? 266 SER A N 1 ATOM 2018 C CA . SER A 1 266 ? 31.355 -29.043 -65.585 1.00 21.03 ? 266 SER A CA 1 ATOM 2019 C C . SER A 1 266 ? 30.695 -30.260 -66.232 1.00 20.60 ? 266 SER A C 1 ATOM 2020 O O . SER A 1 266 ? 29.508 -30.228 -66.601 1.00 20.34 ? 266 SER A O 1 ATOM 2021 C CB . SER A 1 266 ? 32.137 -29.438 -64.306 1.00 21.81 ? 266 SER A CB 1 ATOM 2022 O OG . SER A 1 266 ? 33.309 -30.209 -64.623 1.00 22.95 ? 266 SER A OG 1 ATOM 2023 N N . ILE A 1 267 ? 31.480 -31.319 -66.361 1.00 20.10 ? 267 ILE A N 1 ATOM 2024 C CA . ILE A 1 267 ? 31.094 -32.575 -66.989 1.00 20.01 ? 267 ILE A CA 1 ATOM 2025 C C . ILE A 1 267 ? 31.736 -33.705 -66.202 1.00 20.45 ? 267 ILE A C 1 ATOM 2026 O O . ILE A 1 267 ? 32.856 -33.540 -65.673 1.00 19.23 ? 267 ILE A O 1 ATOM 2027 C CB . ILE A 1 267 ? 31.546 -32.604 -68.480 1.00 20.52 ? 267 ILE A CB 1 ATOM 2028 C CG1 . ILE A 1 267 ? 31.029 -33.863 -69.202 1.00 21.07 ? 267 ILE A CG1 1 ATOM 2029 C CG2 . ILE A 1 267 ? 33.059 -32.482 -68.627 1.00 20.91 ? 267 ILE A CG2 1 ATOM 2030 C CD1 . ILE A 1 267 ? 31.056 -33.735 -70.723 1.00 21.33 ? 267 ILE A CD1 1 ATOM 2031 N N . MET A 1 268 ? 31.028 -34.830 -66.087 1.00 20.59 ? 268 MET A N 1 ATOM 2032 C CA . MET A 1 268 ? 31.496 -35.972 -65.330 1.00 21.58 ? 268 MET A CA 1 ATOM 2033 C C . MET A 1 268 ? 31.112 -37.246 -66.081 1.00 22.10 ? 268 MET A C 1 ATOM 2034 O O . MET A 1 268 ? 30.023 -37.322 -66.656 1.00 22.14 ? 268 MET A O 1 ATOM 2035 C CB . MET A 1 268 ? 30.854 -35.987 -63.944 1.00 21.88 ? 268 MET A CB 1 ATOM 2036 C CG . MET A 1 268 ? 31.445 -36.983 -62.965 1.00 22.67 ? 268 MET A CG 1 ATOM 2037 S SD . MET A 1 268 ? 30.647 -36.930 -61.346 1.00 24.04 ? 268 MET A SD 1 ATOM 2038 C CE . MET A 1 268 ? 31.300 -35.394 -60.655 1.00 22.88 ? 268 MET A CE 1 ATOM 2039 N N . ARG A 1 269 ? 32.023 -38.205 -66.103 1.00 21.80 ? 269 ARG A N 1 ATOM 2040 C CA . ARG A 1 269 ? 31.734 -39.543 -66.622 1.00 22.55 ? 269 ARG A CA 1 ATOM 2041 C C . ARG A 1 269 ? 31.234 -40.399 -65.462 1.00 22.66 ? 269 ARG A C 1 ATOM 2042 O O . ARG A 1 269 ? 31.943 -40.566 -64.447 1.00 21.89 ? 269 ARG A O 1 ATOM 2043 C CB . ARG A 1 269 ? 32.981 -40.171 -67.213 1.00 24.01 ? 269 ARG A CB 1 ATOM 2044 C CG . ARG A 1 269 ? 33.654 -39.320 -68.284 1.00 24.68 ? 269 ARG A CG 1 ATOM 2045 C CD . ARG A 1 269 ? 34.682 -40.128 -69.067 1.00 25.81 ? 269 ARG A CD 1 ATOM 2046 N NE . ARG A 1 269 ? 35.290 -39.337 -70.145 1.00 26.38 ? 269 ARG A NE 1 ATOM 2047 C CZ . ARG A 1 269 ? 36.320 -38.506 -69.987 1.00 27.51 ? 269 ARG A CZ 1 ATOM 2048 N NH1 . ARG A 1 269 ? 36.881 -38.329 -68.796 1.00 28.37 ? 269 ARG A NH1 1 ATOM 2049 N NH2 . ARG A 1 269 ? 36.796 -37.836 -71.026 1.00 28.11 ? 269 ARG A NH2 1 ATOM 2050 N N . SER A 1 270 ? 30.025 -40.926 -65.605 1.00 22.63 ? 270 SER A N 1 ATOM 2051 C CA . SER A 1 270 ? 29.412 -41.780 -64.613 1.00 23.93 ? 270 SER A CA 1 ATOM 2052 C C . SER A 1 270 ? 28.313 -42.646 -65.233 1.00 25.64 ? 270 SER A C 1 ATOM 2053 O O . SER A 1 270 ? 27.595 -42.207 -66.134 1.00 25.41 ? 270 SER A O 1 ATOM 2054 C CB . SER A 1 270 ? 28.793 -40.936 -63.504 1.00 23.69 ? 270 SER A CB 1 ATOM 2055 O OG . SER A 1 270 ? 28.110 -41.772 -62.576 1.00 24.34 ? 270 SER A OG 1 ATOM 2056 N N . ASP A 1 271 ? 28.173 -43.858 -64.721 1.00 26.82 ? 271 ASP A N 1 ATOM 2057 C CA . ASP A 1 271 ? 27.001 -44.676 -65.026 1.00 29.15 ? 271 ASP A CA 1 ATOM 2058 C C . ASP A 1 271 ? 25.970 -44.740 -63.900 1.00 29.29 ? 271 ASP A C 1 ATOM 2059 O O . ASP A 1 271 ? 25.029 -45.530 -63.960 1.00 28.50 ? 271 ASP A O 1 ATOM 2060 C CB . ASP A 1 271 ? 27.473 -46.067 -65.449 1.00 31.05 ? 271 ASP A CB 1 ATOM 2061 C CG . ASP A 1 271 ? 28.205 -46.028 -66.770 1.00 32.95 ? 271 ASP A CG 1 ATOM 2062 O OD1 . ASP A 1 271 ? 27.859 -45.164 -67.630 1.00 33.34 ? 271 ASP A OD1 1 ATOM 2063 O OD2 . ASP A 1 271 ? 29.147 -46.824 -66.946 1.00 35.51 ? 271 ASP A OD2 1 ATOM 2064 N N . ALA A 1 272 ? 26.102 -43.879 -62.893 1.00 27.88 ? 272 ALA A N 1 ATOM 2065 C CA . ALA A 1 272 ? 25.169 -43.889 -61.763 1.00 27.93 ? 272 ALA A CA 1 ATOM 2066 C C . ALA A 1 272 ? 23.799 -43.393 -62.213 1.00 27.68 ? 272 ALA A C 1 ATOM 2067 O O . ALA A 1 272 ? 23.724 -42.447 -62.984 1.00 26.99 ? 272 ALA A O 1 ATOM 2068 C CB . ALA A 1 272 ? 25.707 -43.035 -60.615 1.00 26.79 ? 272 ALA A CB 1 ATOM 2069 N N . PRO A 1 273 ? 22.708 -44.043 -61.760 1.00 28.74 ? 273 PRO A N 1 ATOM 2070 C CA . PRO A 1 273 ? 21.391 -43.514 -62.150 1.00 29.97 ? 273 PRO A CA 1 ATOM 2071 C C . PRO A 1 273 ? 21.101 -42.149 -61.516 1.00 29.43 ? 273 PRO A C 1 ATOM 2072 O O . PRO A 1 273 ? 21.635 -41.837 -60.458 1.00 28.51 ? 273 PRO A O 1 ATOM 2073 C CB . PRO A 1 273 ? 20.412 -44.583 -61.641 1.00 31.13 ? 273 PRO A CB 1 ATOM 2074 C CG . PRO A 1 273 ? 21.135 -45.283 -60.554 1.00 32.15 ? 273 PRO A CG 1 ATOM 2075 C CD . PRO A 1 273 ? 22.601 -45.241 -60.916 1.00 30.80 ? 273 PRO A CD 1 ATOM 2076 N N . ILE A 1 274 ? 20.282 -41.334 -62.169 1.00 30.39 ? 274 ILE A N 1 ATOM 2077 C CA . ILE A 1 274 ? 19.889 -40.054 -61.594 1.00 31.75 ? 274 ILE A CA 1 ATOM 2078 C C . ILE A 1 274 ? 18.617 -40.250 -60.782 1.00 34.16 ? 274 ILE A C 1 ATOM 2079 O O . ILE A 1 274 ? 17.662 -40.825 -61.280 1.00 34.44 ? 274 ILE A O 1 ATOM 2080 C CB . ILE A 1 274 ? 19.716 -38.980 -62.672 1.00 32.84 ? 274 ILE A CB 1 ATOM 2081 C CG1 . ILE A 1 274 ? 21.072 -38.724 -63.355 1.00 33.49 ? 274 ILE A CG1 1 ATOM 2082 C CG2 . ILE A 1 274 ? 19.220 -37.676 -62.067 1.00 33.12 ? 274 ILE A CG2 1 ATOM 2083 C CD1 . ILE A 1 274 ? 20.897 -38.273 -64.767 1.00 35.02 ? 274 ILE A CD1 1 ATOM 2084 N N . GLY A 1 275 ? 18.634 -39.794 -59.531 1.00 34.41 ? 275 GLY A N 1 ATOM 2085 C CA . GLY A 1 275 ? 17.495 -39.939 -58.615 1.00 35.28 ? 275 GLY A CA 1 ATOM 2086 C C . GLY A 1 275 ? 16.832 -38.614 -58.255 1.00 35.56 ? 275 GLY A C 1 ATOM 2087 O O . GLY A 1 275 ? 17.440 -37.533 -58.357 1.00 32.02 ? 275 GLY A O 1 ATOM 2088 N N . LYS A 1 276 ? 15.584 -38.697 -57.814 1.00 35.76 ? 276 LYS A N 1 ATOM 2089 C CA . LYS A 1 276 ? 14.859 -37.524 -57.343 1.00 37.96 ? 276 LYS A CA 1 ATOM 2090 C C . LYS A 1 276 ? 15.152 -37.327 -55.867 1.00 36.84 ? 276 LYS A C 1 ATOM 2091 O O . LYS A 1 276 ? 14.447 -37.823 -55.009 1.00 36.90 ? 276 LYS A O 1 ATOM 2092 C CB . LYS A 1 276 ? 13.361 -37.672 -57.612 1.00 42.58 ? 276 LYS A CB 1 ATOM 2093 C CG . LYS A 1 276 ? 13.063 -37.785 -59.105 1.00 46.14 ? 276 LYS A CG 1 ATOM 2094 C CD . LYS A 1 276 ? 11.613 -37.472 -59.443 1.00 50.18 ? 276 LYS A CD 1 ATOM 2095 C CE . LYS A 1 276 ? 11.291 -37.825 -60.890 1.00 51.87 ? 276 LYS A CE 1 ATOM 2096 N NZ . LYS A 1 276 ? 12.029 -36.978 -61.876 1.00 54.70 ? 276 LYS A NZ 1 ATOM 2097 N N . CYS A 1 277 ? 16.243 -36.639 -55.579 1.00 34.84 ? 277 CYS A N 1 ATOM 2098 C CA . CYS A 1 277 ? 16.707 -36.429 -54.207 1.00 33.99 ? 277 CYS A CA 1 ATOM 2099 C C . CYS A 1 277 ? 17.602 -35.201 -54.228 1.00 30.63 ? 277 CYS A C 1 ATOM 2100 O O . CYS A 1 277 ? 17.830 -34.620 -55.301 1.00 29.01 ? 277 CYS A O 1 ATOM 2101 C CB . CYS A 1 277 ? 17.467 -37.647 -53.640 1.00 37.29 ? 277 CYS A CB 1 ATOM 2102 S SG . CYS A 1 277 ? 18.765 -38.365 -54.694 1.00 43.18 ? 277 CYS A SG 1 ATOM 2103 N N . ASN A 1 278 ? 18.077 -34.794 -53.056 1.00 28.10 ? 278 ASN A N 1 ATOM 2104 C CA . ASN A 1 278 ? 18.799 -33.548 -52.924 1.00 27.89 ? 278 ASN A CA 1 ATOM 2105 C C . ASN A 1 278 ? 20.118 -33.816 -52.220 1.00 27.61 ? 278 ASN A C 1 ATOM 2106 O O . ASN A 1 278 ? 20.106 -34.256 -51.079 1.00 25.76 ? 278 ASN A O 1 ATOM 2107 C CB . ASN A 1 278 ? 17.945 -32.579 -52.109 1.00 28.22 ? 278 ASN A CB 1 ATOM 2108 C CG . ASN A 1 278 ? 18.453 -31.156 -52.170 1.00 29.00 ? 278 ASN A CG 1 ATOM 2109 O OD1 . ASN A 1 278 ? 19.605 -30.896 -51.846 1.00 30.20 ? 278 ASN A OD1 1 ATOM 2110 N ND2 . ASN A 1 278 ? 17.579 -30.219 -52.545 1.00 29.28 ? 278 ASN A ND2 1 ATOM 2111 N N . SER A 1 279 ? 21.234 -33.581 -52.898 1.00 27.11 ? 279 SER A N 1 ATOM 2112 C CA . SER A 1 279 ? 22.549 -33.711 -52.278 1.00 28.07 ? 279 SER A CA 1 ATOM 2113 C C . SER A 1 279 ? 23.547 -32.742 -52.917 1.00 27.24 ? 279 SER A C 1 ATOM 2114 O O . SER A 1 279 ? 23.606 -32.616 -54.136 1.00 25.54 ? 279 SER A O 1 ATOM 2115 C CB . SER A 1 279 ? 23.034 -35.170 -52.393 1.00 30.03 ? 279 SER A CB 1 ATOM 2116 O OG . SER A 1 279 ? 24.321 -35.326 -51.832 1.00 32.81 ? 279 SER A OG 1 ATOM 2117 N N . GLU A 1 280 ? 24.330 -32.051 -52.092 1.00 26.99 ? 280 GLU A N 1 ATOM 2118 C CA . GLU A 1 280 ? 25.258 -31.031 -52.603 1.00 27.83 ? 280 GLU A CA 1 ATOM 2119 C C . GLU A 1 280 ? 26.477 -31.598 -53.340 1.00 26.24 ? 280 GLU A C 1 ATOM 2120 O O . GLU A 1 280 ? 27.042 -30.922 -54.199 1.00 25.87 ? 280 GLU A O 1 ATOM 2121 C CB . GLU A 1 280 ? 25.764 -30.139 -51.463 1.00 30.12 ? 280 GLU A CB 1 ATOM 2122 C CG . GLU A 1 280 ? 24.701 -29.311 -50.766 1.00 34.31 ? 280 GLU A CG 1 ATOM 2123 C CD . GLU A 1 280 ? 24.281 -28.080 -51.542 1.00 37.39 ? 280 GLU A CD 1 ATOM 2124 O OE1 . GLU A 1 280 ? 25.072 -27.582 -52.395 1.00 40.72 ? 280 GLU A OE1 1 ATOM 2125 O OE2 . GLU A 1 280 ? 23.148 -27.601 -51.287 1.00 40.20 ? 280 GLU A OE2 1 ATOM 2126 N N . CYS A 1 281 ? 26.924 -32.798 -52.958 1.00 25.42 ? 281 CYS A N 1 ATOM 2127 C CA . CYS A 1 281 ? 28.187 -33.359 -53.477 1.00 24.52 ? 281 CYS A CA 1 ATOM 2128 C C . CYS A 1 281 ? 27.928 -34.517 -54.405 1.00 23.78 ? 281 CYS A C 1 ATOM 2129 O O . CYS A 1 281 ? 27.261 -35.481 -54.013 1.00 24.06 ? 281 CYS A O 1 ATOM 2130 C CB . CYS A 1 281 ? 29.071 -33.846 -52.335 1.00 25.67 ? 281 CYS A CB 1 ATOM 2131 S SG . CYS A 1 281 ? 30.648 -34.504 -52.922 1.00 26.61 ? 281 CYS A SG 1 ATOM 2132 N N . ILE A 1 282 ? 28.427 -34.399 -55.634 1.00 22.59 ? 282 ILE A N 1 ATOM 2133 C CA . ILE A 1 282 ? 28.310 -35.443 -56.643 1.00 22.34 ? 282 ILE A CA 1 ATOM 2134 C C . ILE A 1 282 ? 29.675 -36.068 -56.947 1.00 21.47 ? 282 ILE A C 1 ATOM 2135 O O . ILE A 1 282 ? 30.665 -35.361 -57.133 1.00 20.89 ? 282 ILE A O 1 ATOM 2136 C CB . ILE A 1 282 ? 27.736 -34.856 -57.945 1.00 22.26 ? 282 ILE A CB 1 ATOM 2137 C CG1 . ILE A 1 282 ? 26.366 -34.247 -57.664 1.00 23.34 ? 282 ILE A CG1 1 ATOM 2138 C CG2 . ILE A 1 282 ? 27.644 -35.922 -59.030 1.00 22.44 ? 282 ILE A CG2 1 ATOM 2139 C CD1 . ILE A 1 282 ? 25.774 -33.453 -58.840 1.00 23.79 ? 282 ILE A CD1 1 ATOM 2140 N N . THR A 1 283 ? 29.714 -37.400 -57.010 1.00 21.21 ? 283 THR A N 1 ATOM 2141 C CA . THR A 1 283 ? 30.892 -38.145 -57.453 1.00 20.68 ? 283 THR A CA 1 ATOM 2142 C C . THR A 1 283 ? 30.397 -39.111 -58.531 1.00 21.15 ? 283 THR A C 1 ATOM 2143 O O . THR A 1 283 ? 29.184 -39.347 -58.601 1.00 21.02 ? 283 THR A O 1 ATOM 2144 C CB . THR A 1 283 ? 31.551 -38.982 -56.327 1.00 20.97 ? 283 THR A CB 1 ATOM 2145 O OG1 . THR A 1 283 ? 30.822 -40.202 -56.114 1.00 20.82 ? 283 THR A OG1 1 ATOM 2146 C CG2 . THR A 1 283 ? 31.667 -38.186 -55.014 1.00 21.01 ? 283 THR A CG2 1 ATOM 2147 N N . PRO A 1 284 ? 31.303 -39.693 -59.328 1.00 21.25 ? 284 PRO A N 1 ATOM 2148 C CA . PRO A 1 284 ? 30.900 -40.709 -60.313 1.00 22.28 ? 284 PRO A CA 1 ATOM 2149 C C . PRO A 1 284 ? 30.197 -41.930 -59.713 1.00 23.29 ? 284 PRO A C 1 ATOM 2150 O O . PRO A 1 284 ? 29.443 -42.620 -60.420 1.00 23.03 ? 284 PRO A O 1 ATOM 2151 C CB . PRO A 1 284 ? 32.222 -41.134 -60.944 1.00 22.34 ? 284 PRO A CB 1 ATOM 2152 C CG . PRO A 1 284 ? 33.109 -39.948 -60.786 1.00 21.96 ? 284 PRO A CG 1 ATOM 2153 C CD . PRO A 1 284 ? 32.740 -39.383 -59.450 1.00 21.93 ? 284 PRO A CD 1 ATOM 2154 N N . ASN A 1 285 ? 30.442 -42.203 -58.433 1.00 23.70 ? 285 ASN A N 1 ATOM 2155 C CA . ASN A 1 285 ? 29.778 -43.324 -57.766 1.00 25.88 ? 285 ASN A CA 1 ATOM 2156 C C . ASN A 1 285 ? 28.393 -42.953 -57.306 1.00 25.54 ? 285 ASN A C 1 ATOM 2157 O O . ASN A 1 285 ? 27.685 -43.808 -56.810 1.00 26.99 ? 285 ASN A O 1 ATOM 2158 C CB . ASN A 1 285 ? 30.533 -43.743 -56.511 1.00 27.63 ? 285 ASN A CB 1 ATOM 2159 C CG . ASN A 1 285 ? 31.998 -43.960 -56.747 1.00 29.21 ? 285 ASN A CG 1 ATOM 2160 O OD1 . ASN A 1 285 ? 32.759 -43.039 -57.049 1.00 27.74 ? 285 ASN A OD1 1 ATOM 2161 N ND2 . ASN A 1 285 ? 32.410 -45.176 -56.574 1.00 36.67 ? 285 ASN A ND2 1 ATOM 2162 N N . GLY A 1 286 ? 28.006 -41.686 -57.431 1.00 24.53 ? 286 GLY A N 1 ATOM 2163 C CA . GLY A 1 286 ? 26.778 -41.207 -56.836 1.00 24.40 ? 286 GLY A CA 1 ATOM 2164 C C . GLY A 1 286 ? 27.006 -40.006 -55.948 1.00 24.84 ? 286 GLY A C 1 ATOM 2165 O O . GLY A 1 286 ? 28.153 -39.626 -55.659 1.00 23.43 ? 286 GLY A O 1 ATOM 2166 N N . SER A 1 287 ? 25.911 -39.405 -55.497 1.00 24.86 ? 287 SER A N 1 ATOM 2167 C CA . SER A 1 287 ? 26.004 -38.310 -54.546 1.00 25.30 ? 287 SER A CA 1 ATOM 2168 C C . SER A 1 287 ? 26.455 -38.869 -53.201 1.00 25.51 ? 287 SER A C 1 ATOM 2169 O O . SER A 1 287 ? 26.170 -40.015 -52.875 1.00 25.12 ? 287 SER A O 1 ATOM 2170 C CB . SER A 1 287 ? 24.668 -37.578 -54.420 1.00 26.10 ? 287 SER A CB 1 ATOM 2171 O OG . SER A 1 287 ? 24.321 -36.942 -55.657 1.00 27.14 ? 287 SER A OG 1 ATOM 2172 N N . ILE A 1 288 ? 27.196 -38.078 -52.444 1.00 24.73 ? 288 ILE A N 1 ATOM 2173 C CA . ILE A 1 288 ? 27.589 -38.484 -51.105 1.00 25.91 ? 288 ILE A CA 1 ATOM 2174 C C . ILE A 1 288 ? 27.234 -37.389 -50.129 1.00 26.46 ? 288 ILE A C 1 ATOM 2175 O O . ILE A 1 288 ? 27.273 -36.204 -50.475 1.00 27.82 ? 288 ILE A O 1 ATOM 2176 C CB . ILE A 1 288 ? 29.103 -38.817 -51.000 1.00 24.90 ? 288 ILE A CB 1 ATOM 2177 C CG1 . ILE A 1 288 ? 29.960 -37.581 -51.301 1.00 25.00 ? 288 ILE A CG1 1 ATOM 2178 C CG2 . ILE A 1 288 ? 29.477 -39.948 -51.956 1.00 25.63 ? 288 ILE A CG2 1 ATOM 2179 C CD1 . ILE A 1 288 ? 31.452 -37.780 -51.046 1.00 25.11 ? 288 ILE A CD1 1 ATOM 2180 N N . PRO A 1 289 ? 26.895 -37.769 -48.896 1.00 27.49 ? 289 PRO A N 1 ATOM 2181 C CA . PRO A 1 289 ? 26.718 -36.777 -47.859 1.00 28.43 ? 289 PRO A CA 1 ATOM 2182 C C . PRO A 1 289 ? 27.972 -35.927 -47.672 1.00 27.82 ? 289 PRO A C 1 ATOM 2183 O O . PRO A 1 289 ? 29.084 -36.440 -47.835 1.00 26.64 ? 289 PRO A O 1 ATOM 2184 C CB . PRO A 1 289 ? 26.479 -37.609 -46.592 1.00 28.66 ? 289 PRO A CB 1 ATOM 2185 C CG . PRO A 1 289 ? 26.167 -38.973 -47.041 1.00 30.51 ? 289 PRO A CG 1 ATOM 2186 C CD . PRO A 1 289 ? 26.720 -39.144 -48.417 1.00 29.00 ? 289 PRO A CD 1 ATOM 2187 N N . ASN A 1 290 ? 27.798 -34.657 -47.330 1.00 27.25 ? 290 ASN A N 1 ATOM 2188 C CA . ASN A 1 290 ? 28.944 -33.776 -47.161 1.00 27.64 ? 290 ASN A CA 1 ATOM 2189 C C . ASN A 1 290 ? 29.125 -33.241 -45.731 1.00 27.71 ? 290 ASN A C 1 ATOM 2190 O O . ASN A 1 290 ? 29.751 -32.206 -45.518 1.00 29.92 ? 290 ASN A O 1 ATOM 2191 C CB . ASN A 1 290 ? 28.892 -32.641 -48.180 1.00 28.13 ? 290 ASN A CB 1 ATOM 2192 C CG . ASN A 1 290 ? 27.782 -31.648 -47.913 1.00 28.99 ? 290 ASN A CG 1 ATOM 2193 O OD1 . ASN A 1 290 ? 26.912 -31.868 -47.063 1.00 28.80 ? 290 ASN A OD1 1 ATOM 2194 N ND2 . ASN A 1 290 ? 27.796 -30.561 -48.657 1.00 27.87 ? 290 ASN A ND2 1 ATOM 2195 N N . ASP A 1 291 ? 28.611 -33.971 -44.754 1.00 27.22 ? 291 ASP A N 1 ATOM 2196 C CA . ASP A 1 291 ? 28.811 -33.594 -43.373 1.00 28.32 ? 291 ASP A CA 1 ATOM 2197 C C . ASP A 1 291 ? 30.296 -33.754 -42.946 1.00 27.15 ? 291 ASP A C 1 ATOM 2198 O O . ASP A 1 291 ? 30.815 -32.908 -42.217 1.00 28.60 ? 291 ASP A O 1 ATOM 2199 C CB . ASP A 1 291 ? 27.844 -34.346 -42.434 1.00 29.62 ? 291 ASP A CB 1 ATOM 2200 C CG . ASP A 1 291 ? 27.914 -35.867 -42.579 1.00 32.34 ? 291 ASP A CG 1 ATOM 2201 O OD1 . ASP A 1 291 ? 27.472 -36.414 -43.612 1.00 34.32 ? 291 ASP A OD1 1 ATOM 2202 O OD2 . ASP A 1 291 ? 28.408 -36.536 -41.651 1.00 36.21 ? 291 ASP A OD2 1 ATOM 2203 N N . LYS A 1 292 ? 30.980 -34.777 -43.440 1.00 24.49 ? 292 LYS A N 1 ATOM 2204 C CA . LYS A 1 292 ? 32.350 -35.074 -42.987 1.00 22.89 ? 292 LYS A CA 1 ATOM 2205 C C . LYS A 1 292 ? 33.356 -34.220 -43.759 1.00 21.28 ? 292 LYS A C 1 ATOM 2206 O O . LYS A 1 292 ? 33.084 -33.819 -44.894 1.00 21.28 ? 292 LYS A O 1 ATOM 2207 C CB . LYS A 1 292 ? 32.632 -36.567 -43.138 1.00 23.03 ? 292 LYS A CB 1 ATOM 2208 C CG . LYS A 1 292 ? 31.696 -37.450 -42.313 1.00 24.04 ? 292 LYS A CG 1 ATOM 2209 C CD . LYS A 1 292 ? 31.910 -38.913 -42.593 1.00 24.48 ? 292 LYS A CD 1 ATOM 2210 C CE . LYS A 1 292 ? 30.930 -39.791 -41.805 1.00 26.64 ? 292 LYS A CE 1 ATOM 2211 N NZ . LYS A 1 292 ? 29.532 -39.599 -42.285 1.00 27.60 ? 292 LYS A NZ 1 ATOM 2212 N N . PRO A 1 293 ? 34.520 -33.936 -43.162 1.00 20.46 ? 293 PRO A N 1 ATOM 2213 C CA . PRO A 1 293 ? 35.486 -33.088 -43.877 1.00 19.93 ? 293 PRO A CA 1 ATOM 2214 C C . PRO A 1 293 ? 36.251 -33.803 -45.006 1.00 19.49 ? 293 PRO A C 1 ATOM 2215 O O . PRO A 1 293 ? 36.782 -33.133 -45.909 1.00 19.20 ? 293 PRO A O 1 ATOM 2216 C CB . PRO A 1 293 ? 36.424 -32.625 -42.760 1.00 20.09 ? 293 PRO A CB 1 ATOM 2217 C CG . PRO A 1 293 ? 36.394 -33.722 -41.760 1.00 20.10 ? 293 PRO A CG 1 ATOM 2218 C CD . PRO A 1 293 ? 34.950 -34.205 -41.779 1.00 20.26 ? 293 PRO A CD 1 ATOM 2219 N N . PHE A 1 294 ? 36.325 -35.128 -44.924 1.00 18.61 ? 294 PHE A N 1 ATOM 2220 C CA . PHE A 1 294 ? 37.105 -35.950 -45.835 1.00 18.49 ? 294 PHE A CA 1 ATOM 2221 C C . PHE A 1 294 ? 36.225 -37.074 -46.410 1.00 18.45 ? 294 PHE A C 1 ATOM 2222 O O . PHE A 1 294 ? 35.168 -37.414 -45.859 1.00 17.93 ? 294 PHE A O 1 ATOM 2223 C CB . PHE A 1 294 ? 38.318 -36.567 -45.101 1.00 18.95 ? 294 PHE A CB 1 ATOM 2224 C CG . PHE A 1 294 ? 39.167 -35.544 -44.382 1.00 19.04 ? 294 PHE A CG 1 ATOM 2225 C CD1 . PHE A 1 294 ? 39.838 -34.584 -45.090 1.00 19.18 ? 294 PHE A CD1 1 ATOM 2226 C CD2 . PHE A 1 294 ? 39.251 -35.535 -42.995 1.00 19.77 ? 294 PHE A CD2 1 ATOM 2227 C CE1 . PHE A 1 294 ? 40.592 -33.597 -44.447 1.00 19.92 ? 294 PHE A CE1 1 ATOM 2228 C CE2 . PHE A 1 294 ? 40.014 -34.576 -42.350 1.00 19.76 ? 294 PHE A CE2 1 ATOM 2229 C CZ . PHE A 1 294 ? 40.683 -33.603 -43.074 1.00 19.28 ? 294 PHE A CZ 1 ATOM 2230 N N . GLN A 1 295 ? 36.678 -37.641 -47.510 1.00 18.45 ? 295 GLN A N 1 ATOM 2231 C CA . GLN A 1 295 ? 36.009 -38.749 -48.158 1.00 18.63 ? 295 GLN A CA 1 ATOM 2232 C C . GLN A 1 295 ? 37.013 -39.581 -48.927 1.00 19.00 ? 295 GLN A C 1 ATOM 2233 O O . GLN A 1 295 ? 38.025 -39.072 -49.374 1.00 19.01 ? 295 GLN A O 1 ATOM 2234 C CB . GLN A 1 295 ? 34.882 -38.233 -49.074 1.00 18.66 ? 295 GLN A CB 1 ATOM 2235 C CG . GLN A 1 295 ? 35.294 -37.284 -50.176 1.00 18.11 ? 295 GLN A CG 1 ATOM 2236 C CD . GLN A 1 295 ? 35.612 -37.920 -51.510 1.00 18.48 ? 295 GLN A CD 1 ATOM 2237 O OE1 . GLN A 1 295 ? 35.446 -39.136 -51.721 1.00 19.03 ? 295 GLN A OE1 1 ATOM 2238 N NE2 . GLN A 1 295 ? 36.066 -37.083 -52.446 1.00 17.71 ? 295 GLN A NE2 1 ATOM 2239 N N . ASN A 1 296 ? 36.732 -40.879 -49.045 1.00 19.57 ? 296 ASN A N 1 ATOM 2240 C CA A ASN A 1 296 ? 37.544 -41.825 -49.773 0.50 19.62 ? 296 ASN A CA 1 ATOM 2241 C CA B ASN A 1 296 ? 37.566 -41.764 -49.854 0.50 20.32 ? 296 ASN A CA 1 ATOM 2242 C C . ASN A 1 296 ? 36.740 -42.485 -50.906 1.00 20.30 ? 296 ASN A C 1 ATOM 2243 O O . ASN A 1 296 ? 37.107 -43.555 -51.394 1.00 21.62 ? 296 ASN A O 1 ATOM 2244 C CB A ASN A 1 296 ? 38.022 -42.877 -48.776 0.50 19.36 ? 296 ASN A CB 1 ATOM 2245 C CB B ASN A 1 296 ? 38.330 -42.770 -48.994 0.50 20.99 ? 296 ASN A CB 1 ATOM 2246 C CG A ASN A 1 296 ? 39.072 -43.806 -49.336 0.50 19.04 ? 296 ASN A CG 1 ATOM 2247 C CG B ASN A 1 296 ? 37.491 -43.954 -48.603 0.50 21.89 ? 296 ASN A CG 1 ATOM 2248 O OD1 A ASN A 1 296 ? 38.966 -45.016 -49.162 0.50 19.08 ? 296 ASN A OD1 1 ATOM 2249 O OD1 B ASN A 1 296 ? 36.271 -43.833 -48.436 0.50 23.32 ? 296 ASN A OD1 1 ATOM 2250 N ND2 A ASN A 1 296 ? 40.094 -43.258 -49.999 0.50 18.66 ? 296 ASN A ND2 1 ATOM 2251 N ND2 B ASN A 1 296 ? 38.123 -45.118 -48.501 0.50 22.69 ? 296 ASN A ND2 1 ATOM 2252 N N . VAL A 1 297 ? 35.640 -41.863 -51.304 1.00 20.23 ? 297 VAL A N 1 ATOM 2253 C CA . VAL A 1 297 ? 34.773 -42.445 -52.333 1.00 20.21 ? 297 VAL A CA 1 ATOM 2254 C C . VAL A 1 297 ? 35.360 -42.251 -53.740 1.00 20.03 ? 297 VAL A C 1 ATOM 2255 O O . VAL A 1 297 ? 35.507 -43.224 -54.492 1.00 19.47 ? 297 VAL A O 1 ATOM 2256 C CB . VAL A 1 297 ? 33.350 -41.885 -52.244 1.00 20.70 ? 297 VAL A CB 1 ATOM 2257 C CG1 . VAL A 1 297 ? 32.511 -42.338 -53.450 1.00 21.26 ? 297 VAL A CG1 1 ATOM 2258 C CG2 . VAL A 1 297 ? 32.718 -42.304 -50.906 1.00 20.76 ? 297 VAL A CG2 1 ATOM 2259 N N . ASN A 1 298 ? 35.747 -41.020 -54.092 1.00 19.31 ? 298 ASN A N 1 ATOM 2260 C CA . ASN A 1 298 ? 36.278 -40.760 -55.436 1.00 19.26 ? 298 ASN A CA 1 ATOM 2261 C C . ASN A 1 298 ? 37.026 -39.439 -55.457 1.00 19.40 ? 298 ASN A C 1 ATOM 2262 O O . ASN A 1 298 ? 36.576 -38.426 -54.869 1.00 18.71 ? 298 ASN A O 1 ATOM 2263 C CB . ASN A 1 298 ? 35.137 -40.746 -56.474 1.00 19.83 ? 298 ASN A CB 1 ATOM 2264 C CG . ASN A 1 298 ? 35.600 -41.086 -57.896 1.00 20.25 ? 298 ASN A CG 1 ATOM 2265 O OD1 . ASN A 1 298 ? 36.479 -40.421 -58.463 1.00 20.42 ? 298 ASN A OD1 1 ATOM 2266 N ND2 . ASN A 1 298 ? 35.020 -42.154 -58.476 1.00 20.39 ? 298 ASN A ND2 1 ATOM 2267 N N . ARG A 1 299 ? 38.165 -39.440 -56.140 1.00 19.44 ? 299 ARG A N 1 ATOM 2268 C CA . ARG A 1 299 ? 38.904 -38.195 -56.355 1.00 20.89 ? 299 ARG A CA 1 ATOM 2269 C C . ARG A 1 299 ? 38.165 -37.218 -57.284 1.00 19.94 ? 299 ARG A C 1 ATOM 2270 O O . ARG A 1 299 ? 38.446 -36.022 -57.268 1.00 19.09 ? 299 ARG A O 1 ATOM 2271 C CB . ARG A 1 299 ? 40.311 -38.469 -56.885 1.00 22.98 ? 299 ARG A CB 1 ATOM 2272 C CG . ARG A 1 299 ? 40.385 -39.059 -58.281 1.00 26.31 ? 299 ARG A CG 1 ATOM 2273 C CD . ARG A 1 299 ? 41.849 -39.372 -58.641 1.00 30.88 ? 299 ARG A CD 1 ATOM 2274 N NE . ARG A 1 299 ? 42.467 -40.386 -57.780 1.00 31.60 ? 299 ARG A NE 1 ATOM 2275 C CZ . ARG A 1 299 ? 43.792 -40.609 -57.698 1.00 34.39 ? 299 ARG A CZ 1 ATOM 2276 N NH1 . ARG A 1 299 ? 44.694 -39.886 -58.396 1.00 34.40 ? 299 ARG A NH1 1 ATOM 2277 N NH2 . ARG A 1 299 ? 44.240 -41.562 -56.906 1.00 35.55 ? 299 ARG A NH2 1 ATOM 2278 N N . ILE A 1 300 ? 37.249 -37.734 -58.096 1.00 19.39 ? 300 ILE A N 1 ATOM 2279 C CA . ILE A 1 300 ? 36.415 -36.890 -58.972 1.00 19.54 ? 300 ILE A CA 1 ATOM 2280 C C . ILE A 1 300 ? 35.183 -36.432 -58.207 1.00 20.28 ? 300 ILE A C 1 ATOM 2281 O O . ILE A 1 300 ? 34.376 -37.258 -57.733 1.00 19.15 ? 300 ILE A O 1 ATOM 2282 C CB . ILE A 1 300 ? 35.991 -37.630 -60.253 1.00 20.04 ? 300 ILE A CB 1 ATOM 2283 C CG1 . ILE A 1 300 ? 37.230 -38.040 -61.062 1.00 20.18 ? 300 ILE A CG1 1 ATOM 2284 C CG2 . ILE A 1 300 ? 35.044 -36.749 -61.114 1.00 18.94 ? 300 ILE A CG2 1 ATOM 2285 C CD1 . ILE A 1 300 ? 36.948 -39.151 -62.093 1.00 20.98 ? 300 ILE A CD1 1 ATOM 2286 N N . THR A 1 301 ? 35.035 -35.113 -58.053 1.00 20.74 ? 301 THR A N 1 ATOM 2287 C CA . THR A 1 301 ? 33.890 -34.558 -57.328 1.00 21.78 ? 301 THR A CA 1 ATOM 2288 C C . THR A 1 301 ? 33.381 -33.266 -58.015 1.00 21.68 ? 301 THR A C 1 ATOM 2289 O O . THR A 1 301 ? 34.113 -32.608 -58.794 1.00 22.92 ? 301 THR A O 1 ATOM 2290 C CB . THR A 1 301 ? 34.190 -34.237 -55.841 1.00 23.10 ? 301 THR A CB 1 ATOM 2291 O OG1 . THR A 1 301 ? 34.993 -33.040 -55.740 1.00 25.39 ? 301 THR A OG1 1 ATOM 2292 C CG2 . THR A 1 301 ? 34.899 -35.393 -55.149 1.00 24.02 ? 301 THR A CG2 1 ATOM 2293 N N . TYR A 1 302 ? 32.138 -32.930 -57.703 1.00 21.01 ? 302 TYR A N 1 ATOM 2294 C CA . TYR A 1 302 ? 31.498 -31.685 -58.152 1.00 20.72 ? 302 TYR A CA 1 ATOM 2295 C C . TYR A 1 302 ? 30.615 -31.192 -57.019 1.00 20.58 ? 302 TYR A C 1 ATOM 2296 O O . TYR A 1 302 ? 29.858 -31.963 -56.440 1.00 21.35 ? 302 TYR A O 1 ATOM 2297 C CB . TYR A 1 302 ? 30.690 -31.872 -59.457 1.00 21.23 ? 302 TYR A CB 1 ATOM 2298 C CG . TYR A 1 302 ? 30.047 -30.562 -59.916 1.00 21.05 ? 302 TYR A CG 1 ATOM 2299 C CD1 . TYR A 1 302 ? 28.796 -30.188 -59.469 1.00 22.28 ? 302 TYR A CD1 1 ATOM 2300 C CD2 . TYR A 1 302 ? 30.722 -29.682 -60.758 1.00 21.53 ? 302 TYR A CD2 1 ATOM 2301 C CE1 . TYR A 1 302 ? 28.218 -28.983 -59.852 1.00 22.11 ? 302 TYR A CE1 1 ATOM 2302 C CE2 . TYR A 1 302 ? 30.141 -28.475 -61.150 1.00 22.13 ? 302 TYR A CE2 1 ATOM 2303 C CZ . TYR A 1 302 ? 28.893 -28.144 -60.699 1.00 22.12 ? 302 TYR A CZ 1 ATOM 2304 O OH . TYR A 1 302 ? 28.338 -26.924 -61.065 1.00 23.37 ? 302 TYR A OH 1 ATOM 2305 N N . GLY A 1 303 ? 30.757 -29.922 -56.646 1.00 20.72 ? 303 GLY A N 1 ATOM 2306 C CA . GLY A 1 303 ? 29.882 -29.312 -55.652 1.00 21.65 ? 303 GLY A CA 1 ATOM 2307 C C . GLY A 1 303 ? 30.570 -29.157 -54.311 1.00 22.65 ? 303 GLY A C 1 ATOM 2308 O O . GLY A 1 303 ? 31.802 -29.185 -54.244 1.00 22.07 ? 303 GLY A O 1 ATOM 2309 N N . ALA A 1 304 ? 29.780 -28.998 -53.255 1.00 23.03 ? 304 ALA A N 1 ATOM 2310 C CA . ALA A 1 304 ? 30.321 -28.803 -51.892 1.00 23.91 ? 304 ALA A CA 1 ATOM 2311 C C . ALA A 1 304 ? 30.667 -30.158 -51.335 1.00 24.28 ? 304 ALA A C 1 ATOM 2312 O O . ALA A 1 304 ? 29.808 -30.860 -50.807 1.00 25.31 ? 304 ALA A O 1 ATOM 2313 C CB . ALA A 1 304 ? 29.321 -28.075 -50.998 1.00 24.68 ? 304 ALA A CB 1 ATOM 2314 N N . CYS A 1 305 ? 31.936 -30.543 -51.474 1.00 24.47 ? 305 CYS A N 1 ATOM 2315 C CA . CYS A 1 305 ? 32.347 -31.919 -51.234 1.00 24.63 ? 305 CYS A CA 1 ATOM 2316 C C . CYS A 1 305 ? 33.437 -32.052 -50.161 1.00 22.84 ? 305 CYS A C 1 ATOM 2317 O O . CYS A 1 305 ? 34.310 -31.189 -50.057 1.00 21.96 ? 305 CYS A O 1 ATOM 2318 C CB . CYS A 1 305 ? 32.923 -32.503 -52.514 1.00 25.75 ? 305 CYS A CB 1 ATOM 2319 S SG . CYS A 1 305 ? 31.644 -32.881 -53.706 1.00 28.43 ? 305 CYS A SG 1 ATOM 2320 N N . PRO A 1 306 ? 33.400 -33.138 -49.396 1.00 20.93 ? 306 PRO A N 1 ATOM 2321 C CA . PRO A 1 306 ? 34.562 -33.401 -48.540 1.00 20.76 ? 306 PRO A CA 1 ATOM 2322 C C . PRO A 1 306 ? 35.815 -33.572 -49.414 1.00 20.04 ? 306 PRO A C 1 ATOM 2323 O O . PRO A 1 306 ? 35.710 -33.928 -50.580 1.00 19.85 ? 306 PRO A O 1 ATOM 2324 C CB . PRO A 1 306 ? 34.186 -34.708 -47.817 1.00 20.95 ? 306 PRO A CB 1 ATOM 2325 C CG . PRO A 1 306 ? 32.685 -34.834 -47.991 1.00 21.51 ? 306 PRO A CG 1 ATOM 2326 C CD . PRO A 1 306 ? 32.391 -34.194 -49.297 1.00 21.39 ? 306 PRO A CD 1 ATOM 2327 N N . ARG A 1 307 ? 36.994 -33.358 -48.839 1.00 19.97 ? 307 ARG A N 1 ATOM 2328 C CA . ARG A 1 307 ? 38.236 -33.523 -49.581 1.00 19.47 ? 307 ARG A CA 1 ATOM 2329 C C . ARG A 1 307 ? 38.623 -34.999 -49.664 1.00 18.21 ? 307 ARG A C 1 ATOM 2330 O O . ARG A 1 307 ? 38.535 -35.724 -48.675 1.00 17.83 ? 307 ARG A O 1 ATOM 2331 C CB . ARG A 1 307 ? 39.358 -32.721 -48.905 1.00 19.83 ? 307 ARG A CB 1 ATOM 2332 C CG . ARG A 1 307 ? 39.155 -31.204 -49.041 1.00 21.29 ? 307 ARG A CG 1 ATOM 2333 C CD . ARG A 1 307 ? 40.424 -30.439 -48.701 1.00 21.25 ? 307 ARG A CD 1 ATOM 2334 N NE . ARG A 1 307 ? 40.324 -28.990 -48.991 1.00 21.63 ? 307 ARG A NE 1 ATOM 2335 C CZ . ARG A 1 307 ? 40.542 -28.428 -50.181 1.00 21.19 ? 307 ARG A CZ 1 ATOM 2336 N NH1 . ARG A 1 307 ? 40.845 -29.135 -51.251 1.00 20.98 ? 307 ARG A NH1 1 ATOM 2337 N NH2 . ARG A 1 307 ? 40.453 -27.115 -50.305 1.00 22.65 ? 307 ARG A NH2 1 ATOM 2338 N N . TYR A 1 308 ? 39.106 -35.407 -50.831 1.00 17.73 ? 308 TYR A N 1 ATOM 2339 C CA . TYR A 1 308 ? 39.538 -36.787 -51.050 1.00 18.14 ? 308 TYR A CA 1 ATOM 2340 C C . TYR A 1 308 ? 40.846 -37.090 -50.338 1.00 18.06 ? 308 TYR A C 1 ATOM 2341 O O . TYR A 1 308 ? 41.839 -36.351 -50.502 1.00 18.50 ? 308 TYR A O 1 ATOM 2342 C CB . TYR A 1 308 ? 39.719 -37.081 -52.520 1.00 18.37 ? 308 TYR A CB 1 ATOM 2343 C CG . TYR A 1 308 ? 40.046 -38.547 -52.768 1.00 19.04 ? 308 TYR A CG 1 ATOM 2344 C CD1 . TYR A 1 308 ? 39.043 -39.506 -52.771 1.00 19.52 ? 308 TYR A CD1 1 ATOM 2345 C CD2 . TYR A 1 308 ? 41.353 -38.964 -52.906 1.00 19.65 ? 308 TYR A CD2 1 ATOM 2346 C CE1 . TYR A 1 308 ? 39.325 -40.840 -52.998 1.00 20.44 ? 308 TYR A CE1 1 ATOM 2347 C CE2 . TYR A 1 308 ? 41.668 -40.296 -53.104 1.00 20.97 ? 308 TYR A CE2 1 ATOM 2348 C CZ . TYR A 1 308 ? 40.629 -41.233 -53.162 1.00 21.11 ? 308 TYR A CZ 1 ATOM 2349 O OH . TYR A 1 308 ? 40.918 -42.543 -53.356 1.00 22.61 ? 308 TYR A OH 1 ATOM 2350 N N . VAL A 1 309 ? 40.846 -38.172 -49.577 1.00 18.19 ? 309 VAL A N 1 ATOM 2351 C CA . VAL A 1 309 ? 42.023 -38.670 -48.909 1.00 17.98 ? 309 VAL A CA 1 ATOM 2352 C C . VAL A 1 309 ? 42.164 -40.174 -49.163 1.00 19.54 ? 309 VAL A C 1 ATOM 2353 O O . VAL A 1 309 ? 41.190 -40.860 -49.512 1.00 19.03 ? 309 VAL A O 1 ATOM 2354 C CB . VAL A 1 309 ? 41.974 -38.393 -47.387 1.00 17.24 ? 309 VAL A CB 1 ATOM 2355 C CG1 . VAL A 1 309 ? 41.943 -36.869 -47.119 1.00 17.06 ? 309 VAL A CG1 1 ATOM 2356 C CG2 . VAL A 1 309 ? 40.791 -39.102 -46.700 1.00 17.29 ? 309 VAL A CG2 1 ATOM 2357 N N . LYS A 1 310 ? 43.362 -40.683 -48.924 1.00 20.18 ? 310 LYS A N 1 ATOM 2358 C CA . LYS A 1 310 ? 43.623 -42.116 -49.070 1.00 22.14 ? 310 LYS A CA 1 ATOM 2359 C C . LYS A 1 310 ? 43.101 -42.975 -47.934 1.00 22.23 ? 310 LYS A C 1 ATOM 2360 O O . LYS A 1 310 ? 42.821 -44.149 -48.159 1.00 22.08 ? 310 LYS A O 1 ATOM 2361 C CB . LYS A 1 310 ? 45.102 -42.357 -49.276 1.00 25.12 ? 310 LYS A CB 1 ATOM 2362 C CG . LYS A 1 310 ? 45.581 -41.801 -50.605 1.00 27.83 ? 310 LYS A CG 1 ATOM 2363 C CD . LYS A 1 310 ? 47.049 -42.096 -50.857 1.00 31.78 ? 310 LYS A CD 1 ATOM 2364 C CE . LYS A 1 310 ? 47.919 -41.603 -49.721 1.00 34.59 ? 310 LYS A CE 1 ATOM 2365 N NZ . LYS A 1 310 ? 49.367 -41.584 -50.104 1.00 40.08 ? 310 LYS A NZ 1 ATOM 2366 N N . GLN A 1 311 ? 42.958 -42.414 -46.735 1.00 21.09 ? 311 GLN A N 1 ATOM 2367 C CA . GLN A 1 311 ? 42.532 -43.173 -45.571 1.00 21.60 ? 311 GLN A CA 1 ATOM 2368 C C . GLN A 1 311 ? 41.089 -43.607 -45.745 1.00 23.04 ? 311 GLN A C 1 ATOM 2369 O O . GLN A 1 311 ? 40.275 -42.859 -46.296 1.00 21.94 ? 311 GLN A O 1 ATOM 2370 C CB . GLN A 1 311 ? 42.665 -42.336 -44.301 1.00 21.09 ? 311 GLN A CB 1 ATOM 2371 C CG . GLN A 1 311 ? 44.107 -41.958 -43.935 1.00 20.54 ? 311 GLN A CG 1 ATOM 2372 C CD . GLN A 1 311 ? 44.499 -40.580 -44.431 1.00 20.11 ? 311 GLN A CD 1 ATOM 2373 O OE1 . GLN A 1 311 ? 44.090 -40.171 -45.517 1.00 19.24 ? 311 GLN A OE1 1 ATOM 2374 N NE2 . GLN A 1 311 ? 45.318 -39.872 -43.645 1.00 19.16 ? 311 GLN A NE2 1 ATOM 2375 N N . ASN A 1 312 ? 40.747 -44.805 -45.279 1.00 24.00 ? 312 ASN A N 1 ATOM 2376 C CA . ASN A 1 312 ? 39.329 -45.198 -45.341 1.00 26.64 ? 312 ASN A CA 1 ATOM 2377 C C . ASN A 1 312 ? 38.580 -44.923 -44.031 1.00 25.20 ? 312 ASN A C 1 ATOM 2378 O O . ASN A 1 312 ? 37.363 -45.019 -44.005 1.00 25.53 ? 312 ASN A O 1 ATOM 2379 C CB . ASN A 1 312 ? 39.138 -46.646 -45.842 1.00 29.96 ? 312 ASN A CB 1 ATOM 2380 C CG . ASN A 1 312 ? 39.848 -47.650 -44.999 1.00 33.51 ? 312 ASN A CG 1 ATOM 2381 O OD1 . ASN A 1 312 ? 40.231 -47.369 -43.875 1.00 36.85 ? 312 ASN A OD1 1 ATOM 2382 N ND2 . ASN A 1 312 ? 40.038 -48.856 -45.548 1.00 39.84 ? 312 ASN A ND2 1 ATOM 2383 N N . THR A 1 313 ? 39.311 -44.503 -42.993 1.00 23.71 ? 313 THR A N 1 ATOM 2384 C CA . THR A 1 313 ? 38.738 -44.123 -41.711 1.00 23.97 ? 313 THR A CA 1 ATOM 2385 C C . THR A 1 313 ? 39.689 -43.192 -40.952 1.00 23.54 ? 313 THR A C 1 ATOM 2386 O O . THR A 1 313 ? 40.917 -43.376 -40.972 1.00 23.41 ? 313 THR A O 1 ATOM 2387 C CB . THR A 1 313 ? 38.403 -45.359 -40.822 1.00 25.64 ? 313 THR A CB 1 ATOM 2388 O OG1 . THR A 1 313 ? 37.897 -44.911 -39.561 1.00 26.72 ? 313 THR A OG1 1 ATOM 2389 C CG2 . THR A 1 313 ? 39.640 -46.223 -40.564 1.00 26.12 ? 313 THR A CG2 1 ATOM 2390 N N . LEU A 1 314 ? 39.122 -42.158 -40.343 1.00 22.56 ? 314 LEU A N 1 ATOM 2391 C CA . LEU A 1 314 ? 39.828 -41.322 -39.389 1.00 22.06 ? 314 LEU A CA 1 ATOM 2392 C C . LEU A 1 314 ? 38.847 -41.009 -38.262 1.00 22.27 ? 314 LEU A C 1 ATOM 2393 O O . LEU A 1 314 ? 37.871 -40.289 -38.475 1.00 22.15 ? 314 LEU A O 1 ATOM 2394 C CB . LEU A 1 314 ? 40.299 -40.030 -40.060 1.00 21.77 ? 314 LEU A CB 1 ATOM 2395 C CG . LEU A 1 314 ? 41.475 -40.104 -41.020 1.00 21.94 ? 314 LEU A CG 1 ATOM 2396 C CD1 . LEU A 1 314 ? 41.599 -38.794 -41.786 1.00 21.83 ? 314 LEU A CD1 1 ATOM 2397 C CD2 . LEU A 1 314 ? 42.786 -40.412 -40.274 1.00 22.26 ? 314 LEU A CD2 1 ATOM 2398 N N . LYS A 1 315 ? 39.109 -41.510 -37.069 1.00 21.37 ? 315 LYS A N 1 ATOM 2399 C CA . LYS A 1 315 ? 38.178 -41.298 -35.962 1.00 22.79 ? 315 LYS A CA 1 ATOM 2400 C C . LYS A 1 315 ? 38.585 -40.124 -35.077 1.00 21.90 ? 315 LYS A C 1 ATOM 2401 O O . LYS A 1 315 ? 39.681 -40.110 -34.522 1.00 21.09 ? 315 LYS A O 1 ATOM 2402 C CB . LYS A 1 315 ? 38.107 -42.562 -35.100 1.00 25.37 ? 315 LYS A CB 1 ATOM 2403 C CG . LYS A 1 315 ? 37.551 -43.777 -35.834 1.00 29.15 ? 315 LYS A CG 1 ATOM 2404 C CD . LYS A 1 315 ? 36.075 -43.619 -36.134 1.00 32.57 ? 315 LYS A CD 1 ATOM 2405 C CE . LYS A 1 315 ? 35.212 -44.335 -35.093 1.00 36.79 ? 315 LYS A CE 1 ATOM 2406 N NZ . LYS A 1 315 ? 33.838 -43.739 -35.041 1.00 41.88 ? 315 LYS A NZ 1 ATOM 2407 N N . LEU A 1 316 ? 37.665 -39.187 -34.898 1.00 21.89 ? 316 LEU A N 1 ATOM 2408 C CA . LEU A 1 316 ? 37.859 -38.043 -34.025 1.00 21.13 ? 316 LEU A CA 1 ATOM 2409 C C . LEU A 1 316 ? 37.249 -38.374 -32.664 1.00 21.53 ? 316 LEU A C 1 ATOM 2410 O O . LEU A 1 316 ? 36.054 -38.663 -32.590 1.00 21.04 ? 316 LEU A O 1 ATOM 2411 C CB . LEU A 1 316 ? 37.120 -36.853 -34.612 1.00 21.69 ? 316 LEU A CB 1 ATOM 2412 C CG . LEU A 1 316 ? 37.261 -35.532 -33.884 1.00 22.08 ? 316 LEU A CG 1 ATOM 2413 C CD1 . LEU A 1 316 ? 38.641 -34.947 -34.158 1.00 21.94 ? 316 LEU A CD1 1 ATOM 2414 C CD2 . LEU A 1 316 ? 36.144 -34.567 -34.324 1.00 23.05 ? 316 LEU A CD2 1 ATOM 2415 N N . ALA A 1 317 ? 38.061 -38.308 -31.612 1.00 21.15 ? 317 ALA A N 1 ATOM 2416 C CA . ALA A 1 317 ? 37.581 -38.445 -30.237 1.00 21.92 ? 317 ALA A CA 1 ATOM 2417 C C . ALA A 1 317 ? 36.521 -37.390 -29.903 1.00 22.11 ? 317 ALA A C 1 ATOM 2418 O O . ALA A 1 317 ? 36.725 -36.206 -30.152 1.00 22.17 ? 317 ALA A O 1 ATOM 2419 C CB . ALA A 1 317 ? 38.760 -38.326 -29.268 1.00 21.42 ? 317 ALA A CB 1 ATOM 2420 N N . THR A 1 318 ? 35.396 -37.836 -29.332 1.00 21.99 ? 318 THR A N 1 ATOM 2421 C CA . THR A 1 318 ? 34.380 -36.944 -28.831 1.00 22.62 ? 318 THR A CA 1 ATOM 2422 C C . THR A 1 318 ? 34.096 -37.215 -27.334 1.00 23.63 ? 318 THR A C 1 ATOM 2423 O O . THR A 1 318 ? 33.048 -36.868 -26.817 1.00 25.94 ? 318 THR A O 1 ATOM 2424 C CB . THR A 1 318 ? 33.104 -37.072 -29.671 1.00 23.08 ? 318 THR A CB 1 ATOM 2425 O OG1 . THR A 1 318 ? 32.628 -38.419 -29.635 1.00 23.74 ? 318 THR A OG1 1 ATOM 2426 C CG2 . THR A 1 318 ? 33.385 -36.682 -31.137 1.00 23.47 ? 318 THR A CG2 1 ATOM 2427 N N . GLY A 1 319 ? 35.040 -37.834 -26.657 1.00 23.22 ? 319 GLY A N 1 ATOM 2428 C CA . GLY A 1 319 ? 34.945 -38.059 -25.228 1.00 23.83 ? 319 GLY A CA 1 ATOM 2429 C C . GLY A 1 319 ? 36.324 -38.288 -24.676 1.00 23.59 ? 319 GLY A C 1 ATOM 2430 O O . GLY A 1 319 ? 37.324 -38.344 -25.427 1.00 24.54 ? 319 GLY A O 1 ATOM 2431 N N . MET A 1 320 ? 36.400 -38.401 -23.360 1.00 23.43 ? 320 MET A N 1 ATOM 2432 C CA . MET A 1 320 ? 37.668 -38.590 -22.671 1.00 23.10 ? 320 MET A CA 1 ATOM 2433 C C . MET A 1 320 ? 38.212 -40.003 -22.787 1.00 23.20 ? 320 MET A C 1 ATOM 2434 O O . MET A 1 320 ? 37.542 -40.912 -23.299 1.00 24.57 ? 320 MET A O 1 ATOM 2435 C CB . MET A 1 320 ? 37.518 -38.215 -21.193 1.00 23.30 ? 320 MET A CB 1 ATOM 2436 C CG . MET A 1 320 ? 36.603 -39.151 -20.421 1.00 23.70 ? 320 MET A CG 1 ATOM 2437 S SD . MET A 1 320 ? 36.443 -38.645 -18.703 1.00 25.14 ? 320 MET A SD 1 ATOM 2438 C CE . MET A 1 320 ? 35.301 -37.305 -18.885 1.00 22.92 ? 320 MET A CE 1 ATOM 2439 N N . ARG A 1 321 ? 39.411 -40.203 -22.259 1.00 23.66 ? 321 ARG A N 1 ATOM 2440 C CA . ARG A 1 321 ? 39.978 -41.535 -22.143 1.00 25.18 ? 321 ARG A CA 1 ATOM 2441 C C . ARG A 1 321 ? 39.011 -42.429 -21.354 1.00 26.00 ? 321 ARG A C 1 ATOM 2442 O O . ARG A 1 321 ? 38.425 -41.991 -20.347 1.00 24.31 ? 321 ARG A O 1 ATOM 2443 C CB . ARG A 1 321 ? 41.332 -41.513 -21.451 1.00 26.87 ? 321 ARG A CB 1 ATOM 2444 C CG . ARG A 1 321 ? 41.279 -41.074 -19.992 1.00 29.87 ? 321 ARG A CG 1 ATOM 2445 C CD . ARG A 1 321 ? 42.629 -41.113 -19.294 1.00 32.86 ? 321 ARG A CD 1 ATOM 2446 N NE . ARG A 1 321 ? 43.562 -40.082 -19.760 1.00 33.18 ? 321 ARG A NE 1 ATOM 2447 C CZ . ARG A 1 321 ? 44.635 -40.307 -20.518 1.00 33.92 ? 321 ARG A CZ 1 ATOM 2448 N NH1 . ARG A 1 321 ? 44.925 -41.525 -20.956 1.00 35.76 ? 321 ARG A NH1 1 ATOM 2449 N NH2 . ARG A 1 321 ? 45.428 -39.290 -20.849 1.00 35.01 ? 321 ARG A NH2 1 ATOM 2450 N N . ASN A 1 322 ? 38.841 -43.653 -21.839 1.00 25.98 ? 322 ASN A N 1 ATOM 2451 C CA . ASN A 1 322 ? 37.946 -44.630 -21.219 1.00 27.92 ? 322 ASN A CA 1 ATOM 2452 C C . ASN A 1 322 ? 38.781 -45.578 -20.365 1.00 28.80 ? 322 ASN A C 1 ATOM 2453 O O . ASN A 1 322 ? 39.670 -46.249 -20.877 1.00 27.71 ? 322 ASN A O 1 ATOM 2454 C CB . ASN A 1 322 ? 37.196 -45.431 -22.276 1.00 27.65 ? 322 ASN A CB 1 ATOM 2455 C CG . ASN A 1 322 ? 35.965 -46.119 -21.710 1.00 28.75 ? 322 ASN A CG 1 ATOM 2456 O OD1 . ASN A 1 322 ? 35.237 -45.547 -20.886 1.00 27.51 ? 322 ASN A OD1 1 ATOM 2457 N ND2 . ASN A 1 322 ? 35.727 -47.355 -22.145 1.00 29.16 ? 322 ASN A ND2 1 ATOM 2458 N N . VAL A 1 323 ? 38.515 -45.600 -19.061 1.00 31.42 ? 323 VAL A N 1 ATOM 2459 C CA . VAL A 1 323 ? 39.375 -46.287 -18.110 1.00 32.61 ? 323 VAL A CA 1 ATOM 2460 C C . VAL A 1 323 ? 38.479 -47.215 -17.286 1.00 35.45 ? 323 VAL A C 1 ATOM 2461 O O . VAL A 1 323 ? 37.580 -46.744 -16.601 1.00 34.65 ? 323 VAL A O 1 ATOM 2462 C CB . VAL A 1 323 ? 40.132 -45.295 -17.192 1.00 33.86 ? 323 VAL A CB 1 ATOM 2463 C CG1 . VAL A 1 323 ? 41.086 -46.031 -16.271 1.00 34.82 ? 323 VAL A CG1 1 ATOM 2464 C CG2 . VAL A 1 323 ? 40.914 -44.277 -18.013 1.00 33.23 ? 323 VAL A CG2 1 ATOM 2465 N N . PRO A 1 324 ? 38.726 -48.535 -17.353 1.00 39.53 ? 324 PRO A N 1 ATOM 2466 C CA . PRO A 1 324 ? 37.965 -49.514 -16.540 1.00 41.07 ? 324 PRO A CA 1 ATOM 2467 C C . PRO A 1 324 ? 37.890 -49.134 -15.056 1.00 41.74 ? 324 PRO A C 1 ATOM 2468 O O . PRO A 1 324 ? 38.814 -48.502 -14.518 1.00 42.31 ? 324 PRO A O 1 ATOM 2469 C CB . PRO A 1 324 ? 38.763 -50.817 -16.688 1.00 41.39 ? 324 PRO A CB 1 ATOM 2470 C CG . PRO A 1 324 ? 39.695 -50.619 -17.834 1.00 42.86 ? 324 PRO A CG 1 ATOM 2471 C CD . PRO A 1 324 ? 39.917 -49.138 -17.988 1.00 40.95 ? 324 PRO A CD 1 ATOM 2472 N N . GLU A 1 325 ? 36.790 -49.494 -14.408 1.00 45.14 ? 325 GLU A N 1 ATOM 2473 C CA . GLU A 1 325 ? 36.675 -49.334 -12.961 1.00 48.39 ? 325 GLU A CA 1 ATOM 2474 C C . GLU A 1 325 ? 37.437 -50.468 -12.264 1.00 53.78 ? 325 GLU A C 1 ATOM 2475 O O . GLU A 1 325 ? 37.204 -51.637 -12.553 1.00 55.28 ? 325 GLU A O 1 ATOM 2476 C CB . GLU A 1 325 ? 35.208 -49.328 -12.531 1.00 47.65 ? 325 GLU A CB 1 ATOM 2477 C CG . GLU A 1 325 ? 35.026 -48.999 -11.054 1.00 47.61 ? 325 GLU A CG 1 ATOM 2478 C CD . GLU A 1 325 ? 33.771 -48.199 -10.760 1.00 46.07 ? 325 GLU A CD 1 ATOM 2479 O OE1 . GLU A 1 325 ? 32.831 -48.221 -11.589 1.00 44.75 ? 325 GLU A OE1 1 ATOM 2480 O OE2 . GLU A 1 325 ? 33.733 -47.550 -9.684 1.00 44.86 ? 325 GLU A OE2 1 ATOM 2481 N N . LYS A 1 326 ? 38.359 -50.119 -11.368 1.00 60.06 ? 326 LYS A N 1 ATOM 2482 C CA . LYS A 1 326 ? 39.155 -51.127 -10.660 1.00 65.99 ? 326 LYS A CA 1 ATOM 2483 C C . LYS A 1 326 ? 38.269 -51.912 -9.687 1.00 69.99 ? 326 LYS A C 1 ATOM 2484 O O . LYS A 1 326 ? 37.308 -51.369 -9.132 1.00 65.81 ? 326 LYS A O 1 ATOM 2485 C CB . LYS A 1 326 ? 40.357 -50.488 -9.942 1.00 67.18 ? 326 LYS A CB 1 ATOM 2486 C CG . LYS A 1 326 ? 40.006 -49.646 -8.724 1.00 69.96 ? 326 LYS A CG 1 ATOM 2487 C CD . LYS A 1 326 ? 41.253 -49.110 -8.028 1.00 71.68 ? 326 LYS A CD 1 ATOM 2488 C CE . LYS A 1 326 ? 40.904 -48.197 -6.855 1.00 71.86 ? 326 LYS A CE 1 ATOM 2489 N NZ . LYS A 1 326 ? 39.879 -48.784 -5.939 1.00 68.55 ? 326 LYS A NZ 1 ATOM 2490 N N . GLN A 1 327 ? 38.600 -53.188 -9.498 1.00 77.81 ? 327 GLN A N 1 ATOM 2491 C CA . GLN A 1 327 ? 37.755 -54.122 -8.743 1.00 84.64 ? 327 GLN A CA 1 ATOM 2492 C C . GLN A 1 327 ? 37.879 -53.960 -7.225 1.00 86.91 ? 327 GLN A C 1 ATOM 2493 O O . GLN A 1 327 ? 38.938 -53.598 -6.706 1.00 86.60 ? 327 GLN A O 1 ATOM 2494 C CB . GLN A 1 327 ? 38.089 -55.567 -9.132 1.00 87.25 ? 327 GLN A CB 1 ATOM 2495 C CG . GLN A 1 327 ? 37.026 -56.582 -8.738 1.00 89.86 ? 327 GLN A CG 1 ATOM 2496 C CD . GLN A 1 327 ? 37.347 -57.982 -9.225 1.00 91.11 ? 327 GLN A CD 1 ATOM 2497 O OE1 . GLN A 1 327 ? 36.687 -58.504 -10.124 1.00 91.90 ? 327 GLN A OE1 1 ATOM 2498 N NE2 . GLN A 1 327 ? 38.370 -58.595 -8.638 1.00 91.12 ? 327 GLN A NE2 1 ATOM 2499 N N . THR A 1 328 ? 36.783 -54.245 -6.527 1.00 92.54 ? 328 THR A N 1 ATOM 2500 C CA . THR A 1 328 ? 36.724 -54.138 -5.068 1.00 95.78 ? 328 THR A CA 1 ATOM 2501 C C . THR A 1 328 ? 37.607 -55.194 -4.397 1.00 95.81 ? 328 THR A C 1 ATOM 2502 O O . THR A 1 328 ? 38.678 -54.881 -3.878 1.00 93.72 ? 328 THR A O 1 ATOM 2503 C CB . THR A 1 328 ? 35.273 -54.294 -4.559 1.00 97.22 ? 328 THR A CB 1 ATOM 2504 O OG1 . THR A 1 328 ? 35.209 -53.958 -3.168 1.00 97.56 ? 328 THR A OG1 1 ATOM 2505 C CG2 . THR A 1 328 ? 34.766 -55.726 -4.773 1.00 95.46 ? 328 THR A CG2 1 ATOM 2506 N N . ALA A 1 334 ? 35.231 -49.470 -0.034 1.00 51.93 ? 334 ALA A N 1 ATOM 2507 C CA . ALA A 1 334 ? 36.011 -48.232 0.047 1.00 48.87 ? 334 ALA A CA 1 ATOM 2508 C C . ALA A 1 334 ? 36.074 -47.558 -1.322 1.00 47.52 ? 334 ALA A C 1 ATOM 2509 O O . ALA A 1 334 ? 36.713 -48.057 -2.254 1.00 49.53 ? 334 ALA A O 1 ATOM 2510 C CB . ALA A 1 334 ? 37.416 -48.506 0.569 1.00 50.19 ? 334 ALA A CB 1 ATOM 2511 N N . ILE A 1 335 ? 35.413 -46.413 -1.430 1.00 42.68 ? 335 ILE A N 1 ATOM 2512 C CA . ILE A 1 335 ? 35.341 -45.675 -2.688 1.00 37.60 ? 335 ILE A CA 1 ATOM 2513 C C . ILE A 1 335 ? 36.731 -45.217 -3.138 1.00 35.82 ? 335 ILE A C 1 ATOM 2514 O O . ILE A 1 335 ? 37.676 -45.211 -2.363 1.00 34.80 ? 335 ILE A O 1 ATOM 2515 C CB . ILE A 1 335 ? 34.362 -44.498 -2.567 1.00 36.50 ? 335 ILE A CB 1 ATOM 2516 C CG1 . ILE A 1 335 ? 34.700 -43.615 -1.358 1.00 36.00 ? 335 ILE A CG1 1 ATOM 2517 C CG2 . ILE A 1 335 ? 32.934 -45.019 -2.441 1.00 37.38 ? 335 ILE A CG2 1 ATOM 2518 C CD1 . ILE A 1 335 ? 34.025 -42.264 -1.397 1.00 35.82 ? 335 ILE A CD1 1 ATOM 2519 N N . ALA A 1 336 ? 36.856 -44.854 -4.404 1.00 33.37 ? 336 ALA A N 1 ATOM 2520 C CA . ALA A 1 336 ? 38.150 -44.482 -4.961 1.00 32.93 ? 336 ALA A CA 1 ATOM 2521 C C . ALA A 1 336 ? 37.935 -43.483 -6.081 1.00 31.52 ? 336 ALA A C 1 ATOM 2522 O O . ALA A 1 336 ? 36.884 -43.473 -6.718 1.00 30.73 ? 336 ALA A O 1 ATOM 2523 C CB . ALA A 1 336 ? 38.895 -45.718 -5.458 1.00 33.55 ? 336 ALA A CB 1 ATOM 2524 N N . GLY A 1 337 ? 38.929 -42.628 -6.286 1.00 31.27 ? 337 GLY A N 1 ATOM 2525 C CA . GLY A 1 337 ? 38.839 -41.511 -7.211 1.00 30.42 ? 337 GLY A CA 1 ATOM 2526 C C . GLY A 1 337 ? 39.498 -41.818 -8.536 1.00 30.22 ? 337 GLY A C 1 ATOM 2527 O O . GLY A 1 337 ? 39.789 -42.980 -8.835 1.00 29.88 ? 337 GLY A O 1 ATOM 2528 N N . PHE A 1 338 ? 39.765 -40.769 -9.304 1.00 29.26 ? 338 PHE A N 1 ATOM 2529 C CA . PHE A 1 338 ? 40.169 -40.926 -10.701 1.00 30.88 ? 338 PHE A CA 1 ATOM 2530 C C . PHE A 1 338 ? 41.542 -41.554 -10.962 1.00 31.14 ? 338 PHE A C 1 ATOM 2531 O O . PHE A 1 338 ? 41.825 -41.874 -12.094 1.00 32.34 ? 338 PHE A O 1 ATOM 2532 C CB . PHE A 1 338 ? 40.087 -39.593 -11.450 1.00 30.68 ? 338 PHE A CB 1 ATOM 2533 C CG . PHE A 1 338 ? 41.104 -38.568 -11.010 1.00 30.42 ? 338 PHE A CG 1 ATOM 2534 C CD1 . PHE A 1 338 ? 40.850 -37.733 -9.937 1.00 31.05 ? 338 PHE A CD1 1 ATOM 2535 C CD2 . PHE A 1 338 ? 42.290 -38.411 -11.693 1.00 32.46 ? 338 PHE A CD2 1 ATOM 2536 C CE1 . PHE A 1 338 ? 41.770 -36.788 -9.529 1.00 31.93 ? 338 PHE A CE1 1 ATOM 2537 C CE2 . PHE A 1 338 ? 43.218 -37.462 -11.296 1.00 31.65 ? 338 PHE A CE2 1 ATOM 2538 C CZ . PHE A 1 338 ? 42.959 -36.646 -10.215 1.00 32.04 ? 338 PHE A CZ 1 ATOM 2539 N N . ILE A 1 339 ? 42.411 -41.686 -9.969 1.00 33.25 ? 339 ILE A N 1 ATOM 2540 C CA . ILE A 1 339 ? 43.760 -42.185 -10.253 1.00 35.65 ? 339 ILE A CA 1 ATOM 2541 C C . ILE A 1 339 ? 43.662 -43.639 -10.766 1.00 37.90 ? 339 ILE A C 1 ATOM 2542 O O . ILE A 1 339 ? 43.263 -44.531 -10.037 1.00 37.80 ? 339 ILE A O 1 ATOM 2543 C CB . ILE A 1 339 ? 44.694 -42.045 -9.039 1.00 36.73 ? 339 ILE A CB 1 ATOM 2544 C CG1 . ILE A 1 339 ? 44.855 -40.571 -8.680 1.00 35.74 ? 339 ILE A CG1 1 ATOM 2545 C CG2 . ILE A 1 339 ? 46.065 -42.647 -9.334 1.00 37.59 ? 339 ILE A CG2 1 ATOM 2546 C CD1 . ILE A 1 339 ? 45.630 -39.771 -9.698 1.00 37.63 ? 339 ILE A CD1 1 ATOM 2547 N N . GLU A 1 340 ? 43.930 -43.824 -12.059 1.00 41.39 ? 340 GLU A N 1 ATOM 2548 C CA . GLU A 1 340 ? 43.839 -45.136 -12.739 1.00 44.77 ? 340 GLU A CA 1 ATOM 2549 C C . GLU A 1 340 ? 42.486 -45.828 -12.548 1.00 41.77 ? 340 GLU A C 1 ATOM 2550 O O . GLU A 1 340 ? 42.434 -47.006 -12.251 1.00 41.96 ? 340 GLU A O 1 ATOM 2551 C CB . GLU A 1 340 ? 44.966 -46.070 -12.261 1.00 49.60 ? 340 GLU A CB 1 ATOM 2552 C CG . GLU A 1 340 ? 46.372 -45.508 -12.432 1.00 54.89 ? 340 GLU A CG 1 ATOM 2553 C CD . GLU A 1 340 ? 46.844 -45.480 -13.877 1.00 60.13 ? 340 GLU A CD 1 ATOM 2554 O OE1 . GLU A 1 340 ? 46.580 -46.456 -14.623 1.00 65.33 ? 340 GLU A OE1 1 ATOM 2555 O OE2 . GLU A 1 340 ? 47.495 -44.482 -14.266 1.00 66.18 ? 340 GLU A OE2 1 ATOM 2556 N N . ASN A 1 341 ? 41.388 -45.101 -12.749 1.00 40.50 ? 341 ASN A N 1 ATOM 2557 C CA . ASN A 1 341 ? 40.073 -45.601 -12.356 1.00 36.87 ? 341 ASN A CA 1 ATOM 2558 C C . ASN A 1 341 ? 38.885 -44.750 -12.852 1.00 36.11 ? 341 ASN A C 1 ATOM 2559 O O . ASN A 1 341 ? 38.720 -43.621 -12.414 1.00 38.78 ? 341 ASN A O 1 ATOM 2560 C CB . ASN A 1 341 ? 40.053 -45.637 -10.829 1.00 38.14 ? 341 ASN A CB 1 ATOM 2561 C CG . ASN A 1 341 ? 38.774 -46.221 -10.277 1.00 37.79 ? 341 ASN A CG 1 ATOM 2562 O OD1 . ASN A 1 341 ? 38.343 -47.300 -10.711 1.00 37.36 ? 341 ASN A OD1 1 ATOM 2563 N ND2 . ASN A 1 341 ? 38.140 -45.499 -9.339 1.00 34.68 ? 341 ASN A ND2 1 ATOM 2564 N N . GLY A 1 342 ? 38.073 -45.267 -13.762 1.00 32.58 ? 342 GLY A N 1 ATOM 2565 C CA . GLY A 1 342 ? 36.854 -44.579 -14.180 1.00 32.29 ? 342 GLY A CA 1 ATOM 2566 C C . GLY A 1 342 ? 35.625 -45.115 -13.461 1.00 32.09 ? 342 GLY A C 1 ATOM 2567 O O . GLY A 1 342 ? 35.682 -46.184 -12.870 1.00 33.09 ? 342 GLY A O 1 ATOM 2568 N N . TRP A 1 343 ? 34.521 -44.372 -13.523 1.00 30.85 ? 343 TRP A N 1 ATOM 2569 C CA . TRP A 1 343 ? 33.289 -44.717 -12.814 1.00 31.56 ? 343 TRP A CA 1 ATOM 2570 C C . TRP A 1 343 ? 32.220 -45.047 -13.802 1.00 33.58 ? 343 TRP A C 1 ATOM 2571 O O . TRP A 1 343 ? 31.574 -44.150 -14.347 1.00 31.45 ? 343 TRP A O 1 ATOM 2572 C CB . TRP A 1 343 ? 32.817 -43.555 -11.961 1.00 29.53 ? 343 TRP A CB 1 ATOM 2573 C CG . TRP A 1 343 ? 33.669 -43.196 -10.773 1.00 27.85 ? 343 TRP A CG 1 ATOM 2574 C CD1 . TRP A 1 343 ? 34.679 -43.939 -10.176 1.00 27.35 ? 343 TRP A CD1 1 ATOM 2575 C CD2 . TRP A 1 343 ? 33.554 -41.986 -9.965 1.00 27.01 ? 343 TRP A CD2 1 ATOM 2576 N NE1 . TRP A 1 343 ? 35.200 -43.283 -9.096 1.00 27.01 ? 343 TRP A NE1 1 ATOM 2577 C CE2 . TRP A 1 343 ? 34.561 -42.099 -8.912 1.00 26.59 ? 343 TRP A CE2 1 ATOM 2578 C CE3 . TRP A 1 343 ? 32.758 -40.858 -10.018 1.00 27.12 ? 343 TRP A CE3 1 ATOM 2579 C CZ2 . TRP A 1 343 ? 34.749 -41.108 -7.976 1.00 26.58 ? 343 TRP A CZ2 1 ATOM 2580 C CZ3 . TRP A 1 343 ? 32.949 -39.864 -9.057 1.00 27.01 ? 343 TRP A CZ3 1 ATOM 2581 C CH2 . TRP A 1 343 ? 33.924 -39.989 -8.061 1.00 26.53 ? 343 TRP A CH2 1 ATOM 2582 N N . GLU A 1 344 ? 32.016 -46.335 -14.049 1.00 37.76 ? 344 GLU A N 1 ATOM 2583 C CA . GLU A 1 344 ? 30.990 -46.755 -15.013 1.00 41.21 ? 344 GLU A CA 1 ATOM 2584 C C . GLU A 1 344 ? 29.586 -46.396 -14.530 1.00 41.51 ? 344 GLU A C 1 ATOM 2585 O O . GLU A 1 344 ? 28.709 -46.045 -15.326 1.00 39.57 ? 344 GLU A O 1 ATOM 2586 C CB . GLU A 1 344 ? 31.121 -48.241 -15.326 1.00 46.03 ? 344 GLU A CB 1 ATOM 2587 C CG . GLU A 1 344 ? 32.449 -48.555 -16.006 1.00 48.98 ? 344 GLU A CG 1 ATOM 2588 C CD . GLU A 1 344 ? 32.576 -49.990 -16.480 1.00 55.52 ? 344 GLU A CD 1 ATOM 2589 O OE1 . GLU A 1 344 ? 31.581 -50.537 -17.013 1.00 58.77 ? 344 GLU A OE1 1 ATOM 2590 O OE2 . GLU A 1 344 ? 33.688 -50.556 -16.323 1.00 59.24 ? 344 GLU A OE2 1 ATOM 2591 N N . GLY A 1 345 ? 29.403 -46.412 -13.216 1.00 40.99 ? 345 GLY A N 1 ATOM 2592 C CA . GLY A 1 345 ? 28.143 -46.001 -12.610 1.00 41.91 ? 345 GLY A CA 1 ATOM 2593 C C . GLY A 1 345 ? 27.798 -44.526 -12.668 1.00 42.71 ? 345 GLY A C 1 ATOM 2594 O O . GLY A 1 345 ? 26.718 -44.142 -12.230 1.00 43.00 ? 345 GLY A O 1 ATOM 2595 N N . MET A 1 346 ? 28.682 -43.669 -13.185 1.00 42.33 ? 346 MET A N 1 ATOM 2596 C CA . MET A 1 346 ? 28.304 -42.272 -13.331 1.00 42.51 ? 346 MET A CA 1 ATOM 2597 C C . MET A 1 346 ? 27.762 -41.998 -14.719 1.00 43.01 ? 346 MET A C 1 ATOM 2598 O O . MET A 1 346 ? 28.523 -41.909 -15.691 1.00 39.72 ? 346 MET A O 1 ATOM 2599 C CB . MET A 1 346 ? 29.436 -41.308 -13.032 1.00 44.22 ? 346 MET A CB 1 ATOM 2600 C CG . MET A 1 346 ? 28.916 -39.882 -13.073 1.00 46.10 ? 346 MET A CG 1 ATOM 2601 S SD . MET A 1 346 ? 29.849 -38.823 -12.006 1.00 50.11 ? 346 MET A SD 1 ATOM 2602 C CE . MET A 1 346 ? 31.357 -38.883 -12.978 1.00 43.74 ? 346 MET A CE 1 ATOM 2603 N N . VAL A 1 347 ? 26.448 -41.806 -14.777 1.00 43.58 ? 347 VAL A N 1 ATOM 2604 C CA . VAL A 1 347 ? 25.708 -41.708 -16.023 1.00 45.01 ? 347 VAL A CA 1 ATOM 2605 C C . VAL A 1 347 ? 25.021 -40.351 -16.241 1.00 44.78 ? 347 VAL A C 1 ATOM 2606 O O . VAL A 1 347 ? 24.504 -40.103 -17.325 1.00 47.14 ? 347 VAL A O 1 ATOM 2607 C CB . VAL A 1 347 ? 24.659 -42.838 -16.091 1.00 47.43 ? 347 VAL A CB 1 ATOM 2608 C CG1 . VAL A 1 347 ? 25.350 -44.194 -16.131 1.00 46.72 ? 347 VAL A CG1 1 ATOM 2609 C CG2 . VAL A 1 347 ? 23.713 -42.763 -14.898 1.00 47.45 ? 347 VAL A CG2 1 ATOM 2610 N N . ASP A 1 348 ? 25.009 -39.467 -15.244 1.00 43.35 ? 348 ASP A N 1 ATOM 2611 C CA . ASP A 1 348 ? 24.402 -38.137 -15.426 1.00 42.76 ? 348 ASP A CA 1 ATOM 2612 C C . ASP A 1 348 ? 25.401 -36.983 -15.534 1.00 40.13 ? 348 ASP A C 1 ATOM 2613 O O . ASP A 1 348 ? 25.026 -35.812 -15.564 1.00 40.86 ? 348 ASP A O 1 ATOM 2614 C CB . ASP A 1 348 ? 23.384 -37.842 -14.321 1.00 46.47 ? 348 ASP A CB 1 ATOM 2615 C CG . ASP A 1 348 ? 24.006 -37.741 -12.944 1.00 49.38 ? 348 ASP A CG 1 ATOM 2616 O OD1 . ASP A 1 348 ? 25.125 -38.280 -12.715 1.00 52.17 ? 348 ASP A OD1 1 ATOM 2617 O OD2 . ASP A 1 348 ? 23.345 -37.127 -12.077 1.00 52.03 ? 348 ASP A OD2 1 ATOM 2618 N N . GLY A 1 349 ? 26.675 -37.311 -15.611 1.00 36.86 ? 349 GLY A N 1 ATOM 2619 C CA . GLY A 1 349 ? 27.691 -36.299 -15.824 1.00 33.72 ? 349 GLY A CA 1 ATOM 2620 C C . GLY A 1 349 ? 28.962 -36.982 -16.263 1.00 31.28 ? 349 GLY A C 1 ATOM 2621 O O . GLY A 1 349 ? 29.070 -38.198 -16.201 1.00 31.47 ? 349 GLY A O 1 ATOM 2622 N N . TRP A 1 350 ? 29.937 -36.193 -16.694 1.00 28.37 ? 350 TRP A N 1 ATOM 2623 C CA . TRP A 1 350 ? 31.232 -36.731 -17.071 1.00 27.14 ? 350 TRP A CA 1 ATOM 2624 C C . TRP A 1 350 ? 32.212 -36.731 -15.954 1.00 25.73 ? 350 TRP A C 1 ATOM 2625 O O . TRP A 1 350 ? 33.156 -37.515 -15.977 1.00 25.65 ? 350 TRP A O 1 ATOM 2626 C CB . TRP A 1 350 ? 31.803 -35.877 -18.191 1.00 27.60 ? 350 TRP A CB 1 ATOM 2627 C CG . TRP A 1 350 ? 31.215 -36.175 -19.530 1.00 27.84 ? 350 TRP A CG 1 ATOM 2628 C CD1 . TRP A 1 350 ? 30.018 -36.808 -19.827 1.00 29.50 ? 350 TRP A CD1 1 ATOM 2629 C CD2 . TRP A 1 350 ? 31.797 -35.828 -20.813 1.00 27.77 ? 350 TRP A CD2 1 ATOM 2630 N NE1 . TRP A 1 350 ? 29.845 -36.899 -21.175 1.00 29.59 ? 350 TRP A NE1 1 ATOM 2631 C CE2 . TRP A 1 350 ? 30.876 -36.320 -21.825 1.00 28.49 ? 350 TRP A CE2 1 ATOM 2632 C CE3 . TRP A 1 350 ? 32.962 -35.200 -21.206 1.00 27.42 ? 350 TRP A CE3 1 ATOM 2633 C CZ2 . TRP A 1 350 ? 31.130 -36.176 -23.179 1.00 27.91 ? 350 TRP A CZ2 1 ATOM 2634 C CZ3 . TRP A 1 350 ? 33.211 -35.049 -22.582 1.00 27.59 ? 350 TRP A CZ3 1 ATOM 2635 C CH2 . TRP A 1 350 ? 32.311 -35.520 -23.535 1.00 27.53 ? 350 TRP A CH2 1 ATOM 2636 N N . TYR A 1 351 ? 32.064 -35.783 -15.026 1.00 25.76 ? 351 TYR A N 1 ATOM 2637 C CA . TYR A 1 351 ? 32.914 -35.679 -13.834 1.00 25.43 ? 351 TYR A CA 1 ATOM 2638 C C . TYR A 1 351 ? 32.011 -35.546 -12.615 1.00 26.63 ? 351 TYR A C 1 ATOM 2639 O O . TYR A 1 351 ? 30.878 -35.079 -12.737 1.00 26.44 ? 351 TYR A O 1 ATOM 2640 C CB . TYR A 1 351 ? 33.794 -34.447 -13.877 1.00 25.86 ? 351 TYR A CB 1 ATOM 2641 C CG . TYR A 1 351 ? 34.594 -34.321 -15.158 1.00 25.10 ? 351 TYR A CG 1 ATOM 2642 C CD1 . TYR A 1 351 ? 34.066 -33.661 -16.267 1.00 25.46 ? 351 TYR A CD1 1 ATOM 2643 C CD2 . TYR A 1 351 ? 35.862 -34.876 -15.256 1.00 24.91 ? 351 TYR A CD2 1 ATOM 2644 C CE1 . TYR A 1 351 ? 34.806 -33.544 -17.446 1.00 25.51 ? 351 TYR A CE1 1 ATOM 2645 C CE2 . TYR A 1 351 ? 36.597 -34.785 -16.442 1.00 24.62 ? 351 TYR A CE2 1 ATOM 2646 C CZ . TYR A 1 351 ? 36.056 -34.110 -17.520 1.00 24.87 ? 351 TYR A CZ 1 ATOM 2647 O OH . TYR A 1 351 ? 36.766 -33.993 -18.690 1.00 25.32 ? 351 TYR A OH 1 ATOM 2648 N N . GLY A 1 352 ? 32.533 -35.903 -11.451 1.00 26.74 ? 352 GLY A N 1 ATOM 2649 C CA . GLY A 1 352 ? 31.732 -35.816 -10.230 1.00 27.75 ? 352 GLY A CA 1 ATOM 2650 C C . GLY A 1 352 ? 32.464 -36.174 -8.965 1.00 27.99 ? 352 GLY A C 1 ATOM 2651 O O . GLY A 1 352 ? 33.692 -36.319 -8.937 1.00 26.03 ? 352 GLY A O 1 ATOM 2652 N N . PHE A 1 353 ? 31.656 -36.328 -7.915 1.00 28.19 ? 353 PHE A N 1 ATOM 2653 C CA . PHE A 1 353 ? 32.098 -36.563 -6.563 1.00 28.73 ? 353 PHE A CA 1 ATOM 2654 C C . PHE A 1 353 ? 31.456 -37.837 -6.046 1.00 28.53 ? 353 PHE A C 1 ATOM 2655 O O . PHE A 1 353 ? 30.268 -38.065 -6.293 1.00 28.54 ? 353 PHE A O 1 ATOM 2656 C CB . PHE A 1 353 ? 31.610 -35.438 -5.660 1.00 29.24 ? 353 PHE A CB 1 ATOM 2657 C CG . PHE A 1 353 ? 32.078 -34.068 -6.050 1.00 30.69 ? 353 PHE A CG 1 ATOM 2658 C CD1 . PHE A 1 353 ? 31.338 -33.286 -6.924 1.00 31.46 ? 353 PHE A CD1 1 ATOM 2659 C CD2 . PHE A 1 353 ? 33.227 -33.530 -5.488 1.00 31.02 ? 353 PHE A CD2 1 ATOM 2660 C CE1 . PHE A 1 353 ? 31.754 -32.008 -7.262 1.00 32.23 ? 353 PHE A CE1 1 ATOM 2661 C CE2 . PHE A 1 353 ? 33.643 -32.252 -5.821 1.00 32.14 ? 353 PHE A CE2 1 ATOM 2662 C CZ . PHE A 1 353 ? 32.912 -31.492 -6.710 1.00 32.40 ? 353 PHE A CZ 1 ATOM 2663 N N . ARG A 1 354 ? 32.226 -38.651 -5.333 1.00 27.75 ? 354 ARG A N 1 ATOM 2664 C CA . ARG A 1 354 ? 31.669 -39.694 -4.470 1.00 27.97 ? 354 ARG A CA 1 ATOM 2665 C C . ARG A 1 354 ? 32.142 -39.433 -3.051 1.00 28.26 ? 354 ARG A C 1 ATOM 2666 O O . ARG A 1 354 ? 33.274 -39.016 -2.833 1.00 27.83 ? 354 ARG A O 1 ATOM 2667 C CB . ARG A 1 354 ? 32.106 -41.095 -4.889 1.00 28.49 ? 354 ARG A CB 1 ATOM 2668 C CG . ARG A 1 354 ? 31.300 -41.660 -6.045 1.00 29.48 ? 354 ARG A CG 1 ATOM 2669 C CD . ARG A 1 354 ? 31.777 -43.039 -6.484 1.00 29.94 ? 354 ARG A CD 1 ATOM 2670 N NE . ARG A 1 354 ? 31.072 -43.454 -7.688 1.00 30.40 ? 354 ARG A NE 1 ATOM 2671 C CZ . ARG A 1 354 ? 31.336 -44.547 -8.402 1.00 31.14 ? 354 ARG A CZ 1 ATOM 2672 N NH1 . ARG A 1 354 ? 32.315 -45.371 -8.061 1.00 31.47 ? 354 ARG A NH1 1 ATOM 2673 N NH2 . ARG A 1 354 ? 30.596 -44.819 -9.468 1.00 31.79 ? 354 ARG A NH2 1 ATOM 2674 N N . HIS A 1 355 ? 31.285 -39.705 -2.079 1.00 28.15 ? 355 HIS A N 1 ATOM 2675 C CA . HIS A 1 355 ? 31.627 -39.444 -0.697 1.00 28.54 ? 355 HIS A CA 1 ATOM 2676 C C . HIS A 1 355 ? 31.200 -40.570 0.161 1.00 29.09 ? 355 HIS A C 1 ATOM 2677 O O . HIS A 1 355 ? 30.307 -41.343 -0.214 1.00 27.70 ? 355 HIS A O 1 ATOM 2678 C CB . HIS A 1 355 ? 30.976 -38.147 -0.228 1.00 28.88 ? 355 HIS A CB 1 ATOM 2679 C CG . HIS A 1 355 ? 29.463 -38.229 -0.132 1.00 29.64 ? 355 HIS A CG 1 ATOM 2680 N ND1 . HIS A 1 355 ? 28.653 -37.817 -1.117 1.00 29.95 ? 355 HIS A ND1 1 ATOM 2681 C CD2 . HIS A 1 355 ? 28.629 -38.731 0.881 1.00 31.14 ? 355 HIS A CD2 1 ATOM 2682 C CE1 . HIS A 1 355 ? 27.362 -38.031 -0.758 1.00 31.15 ? 355 HIS A CE1 1 ATOM 2683 N NE2 . HIS A 1 355 ? 27.354 -38.589 0.460 1.00 30.47 ? 355 HIS A NE2 1 ATOM 2684 N N . GLN A 1 356 ? 31.875 -40.676 1.303 1.00 30.16 ? 356 GLN A N 1 ATOM 2685 C CA . GLN A 1 356 ? 31.514 -41.550 2.392 1.00 31.78 ? 356 GLN A CA 1 ATOM 2686 C C . GLN A 1 356 ? 31.526 -40.731 3.676 1.00 31.68 ? 356 GLN A C 1 ATOM 2687 O O . GLN A 1 356 ? 32.550 -40.136 4.035 1.00 30.21 ? 356 GLN A O 1 ATOM 2688 C CB . GLN A 1 356 ? 32.509 -42.698 2.524 1.00 35.02 ? 356 GLN A CB 1 ATOM 2689 C CG . GLN A 1 356 ? 32.124 -43.681 3.617 1.00 38.88 ? 356 GLN A CG 1 ATOM 2690 C CD . GLN A 1 356 ? 32.943 -44.949 3.592 1.00 42.94 ? 356 GLN A CD 1 ATOM 2691 O OE1 . GLN A 1 356 ? 34.133 -44.930 3.276 1.00 49.65 ? 356 GLN A OE1 1 ATOM 2692 N NE2 . GLN A 1 356 ? 32.311 -46.064 3.944 1.00 47.26 ? 356 GLN A NE2 1 ATOM 2693 N N . ASN A 1 357 ? 30.397 -40.714 4.373 1.00 30.81 ? 357 ASN A N 1 ATOM 2694 C CA . ASN A 1 357 ? 30.265 -39.987 5.622 1.00 31.06 ? 357 ASN A CA 1 ATOM 2695 C C . ASN A 1 357 ? 29.314 -40.751 6.539 1.00 32.77 ? 357 ASN A C 1 ATOM 2696 O O . ASN A 1 357 ? 29.015 -41.918 6.273 1.00 30.99 ? 357 ASN A O 1 ATOM 2697 C CB . ASN A 1 357 ? 29.797 -38.550 5.339 1.00 31.18 ? 357 ASN A CB 1 ATOM 2698 C CG . ASN A 1 357 ? 28.379 -38.473 4.771 1.00 30.82 ? 357 ASN A CG 1 ATOM 2699 O OD1 . ASN A 1 357 ? 27.640 -39.474 4.731 1.00 31.00 ? 357 ASN A OD1 1 ATOM 2700 N ND2 . ASN A 1 357 ? 27.977 -37.273 4.371 1.00 30.25 ? 357 ASN A ND2 1 ATOM 2701 N N . SER A 1 358 ? 28.879 -40.099 7.626 1.00 35.87 ? 358 SER A N 1 ATOM 2702 C CA . SER A 1 358 ? 27.944 -40.675 8.604 1.00 38.58 ? 358 SER A CA 1 ATOM 2703 C C . SER A 1 358 ? 26.627 -41.163 8.016 1.00 38.93 ? 358 SER A C 1 ATOM 2704 O O . SER A 1 358 ? 26.001 -42.067 8.575 1.00 42.16 ? 358 SER A O 1 ATOM 2705 C CB . SER A 1 358 ? 27.623 -39.632 9.704 1.00 40.83 ? 358 SER A CB 1 ATOM 2706 O OG . SER A 1 358 ? 27.388 -38.330 9.143 1.00 43.41 ? 358 SER A OG 1 ATOM 2707 N N . GLU A 1 359 ? 26.196 -40.543 6.927 1.00 37.53 ? 359 GLU A N 1 ATOM 2708 C CA . GLU A 1 359 ? 24.894 -40.801 6.326 1.00 38.42 ? 359 GLU A CA 1 ATOM 2709 C C . GLU A 1 359 ? 24.938 -41.773 5.134 1.00 37.30 ? 359 GLU A C 1 ATOM 2710 O O . GLU A 1 359 ? 23.892 -42.044 4.540 1.00 39.15 ? 359 GLU A O 1 ATOM 2711 C CB . GLU A 1 359 ? 24.251 -39.474 5.911 1.00 39.31 ? 359 GLU A CB 1 ATOM 2712 C CG . GLU A 1 359 ? 24.128 -38.470 7.056 1.00 41.74 ? 359 GLU A CG 1 ATOM 2713 C CD . GLU A 1 359 ? 23.303 -37.242 6.703 1.00 44.06 ? 359 GLU A CD 1 ATOM 2714 O OE1 . GLU A 1 359 ? 22.059 -37.347 6.667 1.00 46.93 ? 359 GLU A OE1 1 ATOM 2715 O OE2 . GLU A 1 359 ? 23.876 -36.158 6.448 1.00 44.79 ? 359 GLU A OE2 1 ATOM 2716 N N . GLY A 1 360 ? 26.123 -42.295 4.790 1.00 34.45 ? 360 GLY A N 1 ATOM 2717 C CA . GLY A 1 360 ? 26.245 -43.332 3.760 1.00 32.94 ? 360 GLY A CA 1 ATOM 2718 C C . GLY A 1 360 ? 27.270 -42.990 2.682 1.00 31.99 ? 360 GLY A C 1 ATOM 2719 O O . GLY A 1 360 ? 28.215 -42.252 2.946 1.00 30.09 ? 360 GLY A O 1 ATOM 2720 N N . ILE A 1 361 ? 27.075 -43.551 1.491 1.00 32.13 ? 361 ILE A N 1 ATOM 2721 C CA . ILE A 1 361 ? 27.975 -43.359 0.343 1.00 33.57 ? 361 ILE A CA 1 ATOM 2722 C C . ILE A 1 361 ? 27.164 -42.819 -0.795 1.00 33.84 ? 361 ILE A C 1 ATOM 2723 O O . ILE A 1 361 ? 26.129 -43.395 -1.148 1.00 33.85 ? 361 ILE A O 1 ATOM 2724 C CB . ILE A 1 361 ? 28.640 -44.666 -0.103 1.00 35.29 ? 361 ILE A CB 1 ATOM 2725 C CG1 . ILE A 1 361 ? 29.625 -45.137 0.954 1.00 37.02 ? 361 ILE A CG1 1 ATOM 2726 C CG2 . ILE A 1 361 ? 29.375 -44.467 -1.438 1.00 36.91 ? 361 ILE A CG2 1 ATOM 2727 C CD1 . ILE A 1 361 ? 29.719 -46.646 1.066 1.00 38.99 ? 361 ILE A CD1 1 ATOM 2728 N N . GLY A 1 362 ? 27.599 -41.691 -1.349 1.00 31.73 ? 362 GLY A N 1 ATOM 2729 C CA . GLY A 1 362 ? 26.816 -41.014 -2.370 1.00 32.53 ? 362 GLY A CA 1 ATOM 2730 C C . GLY A 1 362 ? 27.650 -40.551 -3.554 1.00 32.08 ? 362 GLY A C 1 ATOM 2731 O O . GLY A 1 362 ? 28.880 -40.536 -3.492 1.00 30.45 ? 362 GLY A O 1 ATOM 2732 N N . GLN A 1 363 ? 26.950 -40.188 -4.618 1.00 32.27 ? 363 GLN A N 1 ATOM 2733 C CA . GLN A 1 363 ? 27.545 -39.750 -5.867 1.00 32.27 ? 363 GLN A CA 1 ATOM 2734 C C . GLN A 1 363 ? 26.761 -38.562 -6.374 1.00 32.47 ? 363 GLN A C 1 ATOM 2735 O O . GLN A 1 363 ? 25.540 -38.552 -6.269 1.00 32.86 ? 363 GLN A O 1 ATOM 2736 C CB . GLN A 1 363 ? 27.468 -40.885 -6.875 1.00 33.74 ? 363 GLN A CB 1 ATOM 2737 C CG . GLN A 1 363 ? 28.153 -40.619 -8.194 1.00 34.99 ? 363 GLN A CG 1 ATOM 2738 C CD . GLN A 1 363 ? 28.044 -41.809 -9.120 1.00 35.88 ? 363 GLN A CD 1 ATOM 2739 O OE1 . GLN A 1 363 ? 28.916 -42.668 -9.128 1.00 37.56 ? 363 GLN A OE1 1 ATOM 2740 N NE2 . GLN A 1 363 ? 26.940 -41.890 -9.870 1.00 36.35 ? 363 GLN A NE2 1 ATOM 2741 N N . ALA A 1 364 ? 27.456 -37.568 -6.941 1.00 30.24 ? 364 ALA A N 1 ATOM 2742 C CA . ALA A 1 364 ? 26.831 -36.452 -7.619 1.00 29.70 ? 364 ALA A CA 1 ATOM 2743 C C . ALA A 1 364 ? 27.732 -35.993 -8.773 1.00 30.12 ? 364 ALA A C 1 ATOM 2744 O O . ALA A 1 364 ? 28.961 -35.923 -8.618 1.00 27.42 ? 364 ALA A O 1 ATOM 2745 C CB . ALA A 1 364 ? 26.607 -35.297 -6.655 1.00 29.22 ? 364 ALA A CB 1 ATOM 2746 N N . ALA A 1 365 ? 27.112 -35.657 -9.897 1.00 31.21 ? 365 ALA A N 1 ATOM 2747 C CA . ALA A 1 365 ? 27.819 -35.151 -11.056 1.00 31.88 ? 365 ALA A CA 1 ATOM 2748 C C . ALA A 1 365 ? 28.179 -33.683 -10.832 1.00 32.93 ? 365 ALA A C 1 ATOM 2749 O O . ALA A 1 365 ? 27.473 -32.976 -10.117 1.00 33.53 ? 365 ALA A O 1 ATOM 2750 C CB . ALA A 1 365 ? 26.965 -35.315 -12.300 1.00 33.42 ? 365 ALA A CB 1 ATOM 2751 N N . ASP A 1 366 ? 29.298 -33.232 -11.410 1.00 32.11 ? 366 ASP A N 1 ATOM 2752 C CA . ASP A 1 366 ? 29.660 -31.816 -11.413 1.00 33.27 ? 366 ASP A CA 1 ATOM 2753 C C . ASP A 1 366 ? 29.337 -31.228 -12.780 1.00 35.46 ? 366 ASP A C 1 ATOM 2754 O O . ASP A 1 366 ? 29.987 -31.568 -13.779 1.00 33.83 ? 366 ASP A O 1 ATOM 2755 C CB . ASP A 1 366 ? 31.149 -31.605 -11.114 1.00 33.49 ? 366 ASP A CB 1 ATOM 2756 C CG . ASP A 1 366 ? 31.521 -30.123 -11.036 1.00 35.80 ? 366 ASP A CG 1 ATOM 2757 O OD1 . ASP A 1 366 ? 31.196 -29.478 -10.023 1.00 36.51 ? 366 ASP A OD1 1 ATOM 2758 O OD2 . ASP A 1 366 ? 32.124 -29.580 -11.990 1.00 35.84 ? 366 ASP A OD2 1 ATOM 2759 N N . LEU A 1 367 ? 28.355 -30.332 -12.815 1.00 36.52 ? 367 LEU A N 1 ATOM 2760 C CA . LEU A 1 367 ? 27.805 -29.844 -14.075 1.00 38.79 ? 367 LEU A CA 1 ATOM 2761 C C . LEU A 1 367 ? 28.823 -28.969 -14.796 1.00 38.18 ? 367 LEU A C 1 ATOM 2762 O O . LEU A 1 367 ? 29.030 -29.146 -15.995 1.00 37.74 ? 367 LEU A O 1 ATOM 2763 C CB . LEU A 1 367 ? 26.480 -29.100 -13.834 1.00 42.04 ? 367 LEU A CB 1 ATOM 2764 C CG . LEU A 1 367 ? 25.740 -28.417 -15.007 1.00 45.39 ? 367 LEU A CG 1 ATOM 2765 C CD1 . LEU A 1 367 ? 26.357 -27.066 -15.370 1.00 45.94 ? 367 LEU A CD1 1 ATOM 2766 C CD2 . LEU A 1 367 ? 25.645 -29.316 -16.243 1.00 46.82 ? 367 LEU A CD2 1 ATOM 2767 N N . LYS A 1 368 ? 29.474 -28.066 -14.064 1.00 37.21 ? 368 LYS A N 1 ATOM 2768 C CA . LYS A 1 368 ? 30.391 -27.093 -14.646 1.00 39.16 ? 368 LYS A CA 1 ATOM 2769 C C . LYS A 1 368 ? 31.495 -27.750 -15.458 1.00 37.46 ? 368 LYS A C 1 ATOM 2770 O O . LYS A 1 368 ? 31.719 -27.392 -16.624 1.00 36.37 ? 368 LYS A O 1 ATOM 2771 C CB . LYS A 1 368 ? 31.042 -26.237 -13.558 1.00 41.52 ? 368 LYS A CB 1 ATOM 2772 C CG . LYS A 1 368 ? 32.024 -25.193 -14.091 1.00 45.14 ? 368 LYS A CG 1 ATOM 2773 C CD . LYS A 1 368 ? 32.956 -24.697 -12.989 1.00 48.81 ? 368 LYS A CD 1 ATOM 2774 C CE . LYS A 1 368 ? 33.845 -23.531 -13.421 1.00 51.05 ? 368 LYS A CE 1 ATOM 2775 N NZ . LYS A 1 368 ? 34.663 -23.067 -12.257 1.00 52.64 ? 368 LYS A NZ 1 ATOM 2776 N N . SER A 1 369 ? 32.208 -28.677 -14.825 1.00 34.63 ? 369 SER A N 1 ATOM 2777 C CA . SER A 1 369 ? 33.306 -29.382 -15.487 1.00 33.49 ? 369 SER A CA 1 ATOM 2778 C C . SER A 1 369 ? 32.802 -30.192 -16.678 1.00 32.25 ? 369 SER A C 1 ATOM 2779 O O . SER A 1 369 ? 33.424 -30.206 -17.748 1.00 30.55 ? 369 SER A O 1 ATOM 2780 C CB . SER A 1 369 ? 34.036 -30.283 -14.492 1.00 33.00 ? 369 SER A CB 1 ATOM 2781 O OG . SER A 1 369 ? 33.144 -31.225 -13.942 1.00 34.95 ? 369 SER A OG 1 ATOM 2782 N N . THR A 1 370 ? 31.665 -30.852 -16.505 1.00 30.99 ? 370 THR A N 1 ATOM 2783 C CA . THR A 1 370 ? 31.078 -31.655 -17.567 1.00 31.02 ? 370 THR A CA 1 ATOM 2784 C C . THR A 1 370 ? 30.726 -30.783 -18.781 1.00 32.23 ? 370 THR A C 1 ATOM 2785 O O . THR A 1 370 ? 31.027 -31.126 -19.930 1.00 29.90 ? 370 THR A O 1 ATOM 2786 C CB . THR A 1 370 ? 29.809 -32.364 -17.076 1.00 31.77 ? 370 THR A CB 1 ATOM 2787 O OG1 . THR A 1 370 ? 30.158 -33.293 -16.046 1.00 30.05 ? 370 THR A OG1 1 ATOM 2788 C CG2 . THR A 1 370 ? 29.089 -33.079 -18.241 1.00 30.52 ? 370 THR A CG2 1 ATOM 2789 N N . GLN A 1 371 ? 30.119 -29.635 -18.520 1.00 33.29 ? 371 GLN A N 1 ATOM 2790 C CA . GLN A 1 371 ? 29.699 -28.753 -19.599 1.00 34.91 ? 371 GLN A CA 1 ATOM 2791 C C . GLN A 1 371 ? 30.880 -28.089 -20.312 1.00 33.30 ? 371 GLN A C 1 ATOM 2792 O O . GLN A 1 371 ? 30.820 -27.863 -21.513 1.00 31.82 ? 371 GLN A O 1 ATOM 2793 C CB . GLN A 1 371 ? 28.730 -27.691 -19.077 1.00 38.40 ? 371 GLN A CB 1 ATOM 2794 C CG . GLN A 1 371 ? 27.901 -27.049 -20.179 1.00 43.02 ? 371 GLN A CG 1 ATOM 2795 C CD . GLN A 1 371 ? 27.075 -28.066 -20.946 1.00 45.04 ? 371 GLN A CD 1 ATOM 2796 O OE1 . GLN A 1 371 ? 26.409 -28.925 -20.349 1.00 47.82 ? 371 GLN A OE1 1 ATOM 2797 N NE2 . GLN A 1 371 ? 27.120 -27.982 -22.275 1.00 47.39 ? 371 GLN A NE2 1 ATOM 2798 N N . ALA A 1 372 ? 31.929 -27.765 -19.567 1.00 32.58 ? 372 ALA A N 1 ATOM 2799 C CA . ALA A 1 372 ? 33.158 -27.204 -20.138 1.00 32.65 ? 372 ALA A CA 1 ATOM 2800 C C . ALA A 1 372 ? 33.784 -28.153 -21.176 1.00 31.72 ? 372 ALA A C 1 ATOM 2801 O O . ALA A 1 372 ? 34.163 -27.732 -22.277 1.00 30.97 ? 372 ALA A O 1 ATOM 2802 C CB . ALA A 1 372 ? 34.150 -26.899 -19.023 1.00 31.79 ? 372 ALA A CB 1 ATOM 2803 N N . ALA A 1 373 ? 33.863 -29.437 -20.837 1.00 30.70 ? 373 ALA A N 1 ATOM 2804 C CA . ALA A 1 373 ? 34.352 -30.460 -21.768 1.00 30.10 ? 373 ALA A CA 1 ATOM 2805 C C . ALA A 1 373 ? 33.441 -30.632 -22.977 1.00 30.66 ? 373 ALA A C 1 ATOM 2806 O O . ALA A 1 373 ? 33.900 -30.660 -24.133 1.00 30.17 ? 373 ALA A O 1 ATOM 2807 C CB . ALA A 1 373 ? 34.515 -31.788 -21.046 1.00 29.42 ? 373 ALA A CB 1 ATOM 2808 N N . ILE A 1 374 ? 32.148 -30.741 -22.723 1.00 30.01 ? 374 ILE A N 1 ATOM 2809 C CA . ILE A 1 374 ? 31.192 -30.939 -23.798 1.00 31.94 ? 374 ILE A CA 1 ATOM 2810 C C . ILE A 1 374 ? 31.200 -29.756 -24.765 1.00 32.54 ? 374 ILE A C 1 ATOM 2811 O O . ILE A 1 374 ? 31.210 -29.951 -25.986 1.00 31.73 ? 374 ILE A O 1 ATOM 2812 C CB . ILE A 1 374 ? 29.788 -31.224 -23.241 1.00 31.93 ? 374 ILE A CB 1 ATOM 2813 C CG1 . ILE A 1 374 ? 29.776 -32.632 -22.649 1.00 32.50 ? 374 ILE A CG1 1 ATOM 2814 C CG2 . ILE A 1 374 ? 28.728 -31.064 -24.325 1.00 33.53 ? 374 ILE A CG2 1 ATOM 2815 C CD1 . ILE A 1 374 ? 28.565 -32.958 -21.803 1.00 32.14 ? 374 ILE A CD1 1 ATOM 2816 N N . ASN A 1 375 ? 31.245 -28.540 -24.223 1.00 33.52 ? 375 ASN A N 1 ATOM 2817 C CA . ASN A 1 375 ? 31.254 -27.329 -25.052 1.00 35.79 ? 375 ASN A CA 1 ATOM 2818 C C . ASN A 1 375 ? 32.460 -27.265 -25.979 1.00 34.68 ? 375 ASN A C 1 ATOM 2819 O O . ASN A 1 375 ? 32.326 -26.896 -27.136 1.00 33.27 ? 375 ASN A O 1 ATOM 2820 C CB . ASN A 1 375 ? 31.212 -26.061 -24.185 1.00 37.54 ? 375 ASN A CB 1 ATOM 2821 C CG . ASN A 1 375 ? 29.837 -25.802 -23.597 1.00 38.90 ? 375 ASN A CG 1 ATOM 2822 O OD1 . ASN A 1 375 ? 28.831 -26.337 -24.063 1.00 40.01 ? 375 ASN A OD1 1 ATOM 2823 N ND2 . ASN A 1 375 ? 29.792 -24.982 -22.555 1.00 41.75 ? 375 ASN A ND2 1 ATOM 2824 N N . GLN A 1 376 ? 33.628 -27.645 -25.472 1.00 33.39 ? 376 GLN A N 1 ATOM 2825 C CA . GLN A 1 376 ? 34.844 -27.600 -26.261 1.00 33.19 ? 376 GLN A CA 1 ATOM 2826 C C . GLN A 1 376 ? 34.846 -28.656 -27.348 1.00 31.39 ? 376 GLN A C 1 ATOM 2827 O O . GLN A 1 376 ? 35.291 -28.398 -28.453 1.00 30.14 ? 376 GLN A O 1 ATOM 2828 C CB . GLN A 1 376 ? 36.060 -27.767 -25.366 1.00 33.43 ? 376 GLN A CB 1 ATOM 2829 C CG . GLN A 1 376 ? 36.302 -26.560 -24.478 1.00 34.67 ? 376 GLN A CG 1 ATOM 2830 C CD . GLN A 1 376 ? 37.423 -26.816 -23.522 1.00 34.44 ? 376 GLN A CD 1 ATOM 2831 O OE1 . GLN A 1 376 ? 38.567 -26.890 -23.922 1.00 36.25 ? 376 GLN A OE1 1 ATOM 2832 N NE2 . GLN A 1 376 ? 37.094 -26.987 -22.246 1.00 38.62 ? 376 GLN A NE2 1 ATOM 2833 N N . ILE A 1 377 ? 34.350 -29.848 -27.027 1.00 30.02 ? 377 ILE A N 1 ATOM 2834 C CA . ILE A 1 377 ? 34.230 -30.905 -28.020 1.00 30.28 ? 377 ILE A CA 1 ATOM 2835 C C . ILE A 1 377 ? 33.226 -30.494 -29.103 1.00 31.03 ? 377 ILE A C 1 ATOM 2836 O O . ILE A 1 377 ? 33.475 -30.689 -30.293 1.00 29.98 ? 377 ILE A O 1 ATOM 2837 C CB . ILE A 1 377 ? 33.873 -32.243 -27.371 1.00 29.25 ? 377 ILE A CB 1 ATOM 2838 C CG1 . ILE A 1 377 ? 35.086 -32.746 -26.561 1.00 30.28 ? 377 ILE A CG1 1 ATOM 2839 C CG2 . ILE A 1 377 ? 33.443 -33.260 -28.418 1.00 29.20 ? 377 ILE A CG2 1 ATOM 2840 C CD1 . ILE A 1 377 ? 34.808 -33.942 -25.660 1.00 29.74 ? 377 ILE A CD1 1 ATOM 2841 N N . ASN A 1 378 ? 32.113 -29.896 -28.701 1.00 31.86 ? 378 ASN A N 1 ATOM 2842 C CA . ASN A 1 378 ? 31.139 -29.396 -29.685 1.00 33.50 ? 378 ASN A CA 1 ATOM 2843 C C . ASN A 1 378 ? 31.720 -28.297 -30.557 1.00 34.23 ? 378 ASN A C 1 ATOM 2844 O O . ASN A 1 378 ? 31.416 -28.231 -31.746 1.00 34.96 ? 378 ASN A O 1 ATOM 2845 C CB . ASN A 1 378 ? 29.847 -28.945 -29.007 1.00 34.57 ? 378 ASN A CB 1 ATOM 2846 C CG . ASN A 1 378 ? 28.965 -30.116 -28.635 1.00 35.78 ? 378 ASN A CG 1 ATOM 2847 O OD1 . ASN A 1 378 ? 29.122 -31.210 -29.169 1.00 37.00 ? 378 ASN A OD1 1 ATOM 2848 N ND2 . ASN A 1 378 ? 28.046 -29.903 -27.717 1.00 36.33 ? 378 ASN A ND2 1 ATOM 2849 N N . GLY A 1 379 ? 32.580 -27.469 -29.975 1.00 33.98 ? 379 GLY A N 1 ATOM 2850 C CA . GLY A 1 379 ? 33.316 -26.459 -30.724 1.00 36.26 ? 379 GLY A CA 1 ATOM 2851 C C . GLY A 1 379 ? 34.118 -27.031 -31.879 1.00 36.53 ? 379 GLY A C 1 ATOM 2852 O O . GLY A 1 379 ? 34.084 -26.506 -32.996 1.00 35.13 ? 379 GLY A O 1 ATOM 2853 N N . LYS A 1 380 ? 34.853 -28.110 -31.632 1.00 35.26 ? 380 LYS A N 1 ATOM 2854 C CA . LYS A 1 380 ? 35.687 -28.636 -32.694 1.00 35.33 ? 380 LYS A CA 1 ATOM 2855 C C . LYS A 1 380 ? 34.853 -29.410 -33.692 1.00 33.52 ? 380 LYS A C 1 ATOM 2856 O O . LYS A 1 380 ? 35.141 -29.375 -34.875 1.00 34.25 ? 380 LYS A O 1 ATOM 2857 C CB . LYS A 1 380 ? 36.929 -29.372 -32.168 1.00 37.65 ? 380 LYS A CB 1 ATOM 2858 C CG . LYS A 1 380 ? 36.713 -30.628 -31.407 1.00 38.74 ? 380 LYS A CG 1 ATOM 2859 C CD . LYS A 1 380 ? 38.048 -31.228 -30.971 1.00 38.16 ? 380 LYS A CD 1 ATOM 2860 C CE . LYS A 1 380 ? 38.786 -30.353 -29.966 1.00 37.41 ? 380 LYS A CE 1 ATOM 2861 N NZ . LYS A 1 380 ? 40.059 -30.987 -29.551 1.00 35.46 ? 380 LYS A NZ 1 ATOM 2862 N N . LEU A 1 381 ? 33.781 -30.044 -33.242 1.00 32.94 ? 381 LEU A N 1 ATOM 2863 C CA . LEU A 1 381 ? 32.834 -30.639 -34.167 1.00 33.47 ? 381 LEU A CA 1 ATOM 2864 C C . LEU A 1 381 ? 32.244 -29.573 -35.091 1.00 36.09 ? 381 LEU A C 1 ATOM 2865 O O . LEU A 1 381 ? 32.058 -29.803 -36.283 1.00 35.06 ? 381 LEU A O 1 ATOM 2866 C CB . LEU A 1 381 ? 31.713 -31.370 -33.426 1.00 33.70 ? 381 LEU A CB 1 ATOM 2867 C CG . LEU A 1 381 ? 32.100 -32.711 -32.785 1.00 32.78 ? 381 LEU A CG 1 ATOM 2868 C CD1 . LEU A 1 381 ? 30.970 -33.256 -31.910 1.00 32.33 ? 381 LEU A CD1 1 ATOM 2869 C CD2 . LEU A 1 381 ? 32.492 -33.708 -33.856 1.00 32.32 ? 381 LEU A CD2 1 ATOM 2870 N N . ASN A 1 382 ? 31.980 -28.395 -34.543 1.00 36.91 ? 382 ASN A N 1 ATOM 2871 C CA . ASN A 1 382 ? 31.456 -27.314 -35.352 1.00 40.29 ? 382 ASN A CA 1 ATOM 2872 C C . ASN A 1 382 ? 32.386 -26.813 -36.453 1.00 38.95 ? 382 ASN A C 1 ATOM 2873 O O . ASN A 1 382 ? 31.912 -26.361 -37.493 1.00 39.17 ? 382 ASN A O 1 ATOM 2874 C CB . ASN A 1 382 ? 31.012 -26.154 -34.491 1.00 43.59 ? 382 ASN A CB 1 ATOM 2875 C CG . ASN A 1 382 ? 29.547 -25.915 -34.620 1.00 49.67 ? 382 ASN A CG 1 ATOM 2876 O OD1 . ASN A 1 382 ? 29.121 -25.146 -35.488 1.00 52.41 ? 382 ASN A OD1 1 ATOM 2877 N ND2 . ASN A 1 382 ? 28.752 -26.637 -33.824 1.00 51.67 ? 382 ASN A ND2 1 ATOM 2878 N N . ARG A 1 383 ? 33.690 -26.893 -36.224 1.00 37.16 ? 383 ARG A N 1 ATOM 2879 C CA . ARG A 1 383 ? 34.670 -26.508 -37.224 1.00 37.03 ? 383 ARG A CA 1 ATOM 2880 C C . ARG A 1 383 ? 34.829 -27.562 -38.308 1.00 34.82 ? 383 ARG A C 1 ATOM 2881 O O . ARG A 1 383 ? 35.202 -27.242 -39.424 1.00 34.96 ? 383 ARG A O 1 ATOM 2882 C CB . ARG A 1 383 ? 36.036 -26.290 -36.578 1.00 40.72 ? 383 ARG A CB 1 ATOM 2883 C CG . ARG A 1 383 ? 36.067 -25.152 -35.586 1.00 45.38 ? 383 ARG A CG 1 ATOM 2884 C CD . ARG A 1 383 ? 37.489 -24.812 -35.141 1.00 49.02 ? 383 ARG A CD 1 ATOM 2885 N NE . ARG A 1 383 ? 37.898 -25.542 -33.942 1.00 51.52 ? 383 ARG A NE 1 ATOM 2886 C CZ . ARG A 1 383 ? 37.379 -25.354 -32.724 1.00 53.54 ? 383 ARG A CZ 1 ATOM 2887 N NH1 . ARG A 1 383 ? 36.406 -24.467 -32.526 1.00 56.35 ? 383 ARG A NH1 1 ATOM 2888 N NH2 . ARG A 1 383 ? 37.819 -26.069 -31.691 1.00 54.04 ? 383 ARG A NH2 1 ATOM 2889 N N . LEU A 1 384 ? 34.578 -28.817 -37.969 1.00 32.66 ? 384 LEU A N 1 ATOM 2890 C CA . LEU A 1 384 ? 34.926 -29.937 -38.844 1.00 32.06 ? 384 LEU A CA 1 ATOM 2891 C C . LEU A 1 384 ? 33.745 -30.522 -39.592 1.00 32.26 ? 384 LEU A C 1 ATOM 2892 O O . LEU A 1 384 ? 33.940 -31.126 -40.644 1.00 30.99 ? 384 LEU A O 1 ATOM 2893 C CB . LEU A 1 384 ? 35.602 -31.037 -38.040 1.00 30.97 ? 384 LEU A CB 1 ATOM 2894 C CG . LEU A 1 384 ? 37.016 -30.664 -37.560 1.00 31.92 ? 384 LEU A CG 1 ATOM 2895 C CD1 . LEU A 1 384 ? 37.569 -31.640 -36.514 1.00 31.25 ? 384 LEU A CD1 1 ATOM 2896 C CD2 . LEU A 1 384 ? 37.943 -30.548 -38.759 1.00 32.11 ? 384 LEU A CD2 1 ATOM 2897 N N . ILE A 1 385 ? 32.545 -30.399 -39.026 1.00 30.93 ? 385 ILE A N 1 ATOM 2898 C CA . ILE A 1 385 ? 31.359 -31.059 -39.549 1.00 31.85 ? 385 ILE A CA 1 ATOM 2899 C C . ILE A 1 385 ? 30.468 -30.061 -40.280 1.00 33.49 ? 385 ILE A C 1 ATOM 2900 O O . ILE A 1 385 ? 30.168 -28.983 -39.758 1.00 34.37 ? 385 ILE A O 1 ATOM 2901 C CB . ILE A 1 385 ? 30.550 -31.736 -38.415 1.00 32.53 ? 385 ILE A CB 1 ATOM 2902 C CG1 . ILE A 1 385 ? 31.408 -32.775 -37.669 1.00 32.91 ? 385 ILE A CG1 1 ATOM 2903 C CG2 . ILE A 1 385 ? 29.287 -32.383 -38.961 1.00 32.62 ? 385 ILE A CG2 1 ATOM 2904 C CD1 . ILE A 1 385 ? 32.011 -33.852 -38.549 1.00 32.34 ? 385 ILE A CD1 1 ATOM 2905 N N . GLY A 1 386 ? 30.084 -30.414 -41.505 1.00 33.66 ? 386 GLY A N 1 ATOM 2906 C CA . GLY A 1 386 ? 29.212 -29.587 -42.334 1.00 34.61 ? 386 GLY A CA 1 ATOM 2907 C C . GLY A 1 386 ? 29.846 -28.304 -42.826 1.00 35.59 ? 386 GLY A C 1 ATOM 2908 O O . GLY A 1 386 ? 29.149 -27.308 -42.996 1.00 34.47 ? 386 GLY A O 1 ATOM 2909 N N . LYS A 1 387 ? 31.159 -28.324 -43.074 1.00 34.60 ? 387 LYS A N 1 ATOM 2910 C CA . LYS A 1 387 ? 31.894 -27.115 -43.433 1.00 34.49 ? 387 LYS A CA 1 ATOM 2911 C C . LYS A 1 387 ? 32.660 -27.231 -44.764 1.00 34.47 ? 387 LYS A C 1 ATOM 2912 O O . LYS A 1 387 ? 33.580 -26.467 -45.022 1.00 35.33 ? 387 LYS A O 1 ATOM 2913 C CB . LYS A 1 387 ? 32.838 -26.728 -42.297 1.00 35.96 ? 387 LYS A CB 1 ATOM 2914 C CG . LYS A 1 387 ? 32.126 -26.381 -41.001 1.00 37.29 ? 387 LYS A CG 1 ATOM 2915 C CD . LYS A 1 387 ? 31.401 -25.038 -41.099 1.00 39.86 ? 387 LYS A CD 1 ATOM 2916 C CE . LYS A 1 387 ? 30.852 -24.571 -39.755 1.00 40.84 ? 387 LYS A CE 1 ATOM 2917 N NZ . LYS A 1 387 ? 29.963 -25.592 -39.132 1.00 43.59 ? 387 LYS A NZ 1 ATOM 2918 N N . THR A 1 388 ? 32.241 -28.152 -45.630 1.00 32.65 ? 388 THR A N 1 ATOM 2919 C CA . THR A 1 388 ? 32.932 -28.377 -46.897 1.00 32.82 ? 388 THR A CA 1 ATOM 2920 C C . THR A 1 388 ? 32.833 -27.165 -47.825 1.00 35.28 ? 388 THR A C 1 ATOM 2921 O O . THR A 1 388 ? 31.927 -26.316 -47.698 1.00 33.21 ? 388 THR A O 1 ATOM 2922 C CB . THR A 1 388 ? 32.419 -29.640 -47.637 1.00 32.00 ? 388 THR A CB 1 ATOM 2923 O OG1 . THR A 1 388 ? 31.049 -29.464 -48.025 1.00 31.81 ? 388 THR A OG1 1 ATOM 2924 C CG2 . THR A 1 388 ? 32.566 -30.882 -46.742 1.00 30.18 ? 388 THR A CG2 1 ATOM 2925 N N . ASN A 1 389 ? 33.797 -27.090 -48.736 1.00 35.11 ? 389 ASN A N 1 ATOM 2926 C CA . ASN A 1 389 ? 33.866 -26.004 -49.695 1.00 38.18 ? 389 ASN A CA 1 ATOM 2927 C C . ASN A 1 389 ? 33.546 -26.559 -51.076 1.00 35.44 ? 389 ASN A C 1 ATOM 2928 O O . ASN A 1 389 ? 33.805 -27.730 -51.341 1.00 34.58 ? 389 ASN A O 1 ATOM 2929 C CB . ASN A 1 389 ? 35.266 -25.391 -49.666 1.00 41.79 ? 389 ASN A CB 1 ATOM 2930 C CG . ASN A 1 389 ? 35.534 -24.619 -48.377 1.00 46.79 ? 389 ASN A CG 1 ATOM 2931 O OD1 . ASN A 1 389 ? 34.605 -24.188 -47.682 1.00 49.72 ? 389 ASN A OD1 1 ATOM 2932 N ND2 . ASN A 1 389 ? 36.804 -24.439 -48.060 1.00 49.07 ? 389 ASN A ND2 1 ATOM 2933 N N . GLU A 1 390 ? 32.978 -25.715 -51.930 1.00 33.28 ? 390 GLU A N 1 ATOM 2934 C CA . GLU A 1 390 ? 32.637 -26.088 -53.294 1.00 31.29 ? 390 GLU A CA 1 ATOM 2935 C C . GLU A 1 390 ? 33.797 -26.003 -54.280 1.00 28.59 ? 390 GLU A C 1 ATOM 2936 O O . GLU A 1 390 ? 34.540 -25.010 -54.280 1.00 27.53 ? 390 GLU A O 1 ATOM 2937 C CB . GLU A 1 390 ? 31.530 -25.154 -53.798 1.00 34.68 ? 390 GLU A CB 1 ATOM 2938 C CG . GLU A 1 390 ? 30.175 -25.377 -53.159 1.00 37.71 ? 390 GLU A CG 1 ATOM 2939 C CD . GLU A 1 390 ? 29.089 -24.598 -53.869 1.00 40.99 ? 390 GLU A CD 1 ATOM 2940 O OE1 . GLU A 1 390 ? 29.164 -23.360 -53.791 1.00 39.98 ? 390 GLU A OE1 1 ATOM 2941 O OE2 . GLU A 1 390 ? 28.206 -25.229 -54.529 1.00 42.99 ? 390 GLU A OE2 1 ATOM 2942 N N . LYS A 1 391 ? 33.924 -27.021 -55.136 1.00 25.97 ? 391 LYS A N 1 ATOM 2943 C CA . LYS A 1 391 ? 34.731 -26.958 -56.359 1.00 25.66 ? 391 LYS A CA 1 ATOM 2944 C C . LYS A 1 391 ? 33.902 -27.390 -57.570 1.00 25.18 ? 391 LYS A C 1 ATOM 2945 O O . LYS A 1 391 ? 32.928 -28.137 -57.435 1.00 23.37 ? 391 LYS A O 1 ATOM 2946 C CB . LYS A 1 391 ? 35.963 -27.846 -56.271 1.00 27.25 ? 391 LYS A CB 1 ATOM 2947 C CG . LYS A 1 391 ? 36.872 -27.547 -55.073 1.00 28.49 ? 391 LYS A CG 1 ATOM 2948 C CD . LYS A 1 391 ? 37.645 -26.263 -55.268 1.00 29.12 ? 391 LYS A CD 1 ATOM 2949 C CE . LYS A 1 391 ? 38.658 -26.059 -54.156 1.00 31.01 ? 391 LYS A CE 1 ATOM 2950 N NZ . LYS A 1 391 ? 39.211 -24.688 -54.131 1.00 29.07 ? 391 LYS A NZ 1 ATOM 2951 N N . PHE A 1 392 ? 34.285 -26.906 -58.743 1.00 23.28 ? 392 PHE A N 1 ATOM 2952 C CA . PHE A 1 392 ? 33.437 -27.036 -59.914 1.00 23.87 ? 392 PHE A CA 1 ATOM 2953 C C . PHE A 1 392 ? 34.233 -27.712 -61.017 1.00 22.97 ? 392 PHE A C 1 ATOM 2954 O O . PHE A 1 392 ? 34.610 -28.864 -60.841 1.00 22.60 ? 392 PHE A O 1 ATOM 2955 C CB . PHE A 1 392 ? 32.827 -25.667 -60.273 1.00 25.27 ? 392 PHE A CB 1 ATOM 2956 C CG . PHE A 1 392 ? 32.004 -25.075 -59.139 1.00 26.40 ? 392 PHE A CG 1 ATOM 2957 C CD1 . PHE A 1 392 ? 30.857 -25.710 -58.715 1.00 27.25 ? 392 PHE A CD1 1 ATOM 2958 C CD2 . PHE A 1 392 ? 32.431 -23.942 -58.463 1.00 28.07 ? 392 PHE A CD2 1 ATOM 2959 C CE1 . PHE A 1 392 ? 30.118 -25.214 -57.643 1.00 28.44 ? 392 PHE A CE1 1 ATOM 2960 C CE2 . PHE A 1 392 ? 31.692 -23.421 -57.402 1.00 28.67 ? 392 PHE A CE2 1 ATOM 2961 C CZ . PHE A 1 392 ? 30.528 -24.056 -57.004 1.00 28.71 ? 392 PHE A CZ 1 ATOM 2962 N N . HIS A 1 393 ? 34.493 -27.041 -62.133 1.00 22.72 ? 393 HIS A N 1 ATOM 2963 C CA . HIS A 1 393 ? 35.275 -27.658 -63.197 1.00 22.82 ? 393 HIS A CA 1 ATOM 2964 C C . HIS A 1 393 ? 36.734 -27.705 -62.813 1.00 22.83 ? 393 HIS A C 1 ATOM 2965 O O . HIS A 1 393 ? 37.323 -26.691 -62.412 1.00 22.53 ? 393 HIS A O 1 ATOM 2966 C CB . HIS A 1 393 ? 35.116 -26.891 -64.480 1.00 23.46 ? 393 HIS A CB 1 ATOM 2967 C CG . HIS A 1 393 ? 35.565 -27.639 -65.691 1.00 24.11 ? 393 HIS A CG 1 ATOM 2968 N ND1 . HIS A 1 393 ? 35.110 -28.864 -65.996 1.00 25.21 ? 393 HIS A ND1 1 ATOM 2969 C CD2 . HIS A 1 393 ? 36.476 -27.307 -66.672 1.00 25.00 ? 393 HIS A CD2 1 ATOM 2970 C CE1 . HIS A 1 393 ? 35.672 -29.279 -67.139 1.00 25.14 ? 393 HIS A CE1 1 ATOM 2971 N NE2 . HIS A 1 393 ? 36.507 -28.334 -67.552 1.00 25.63 ? 393 HIS A NE2 1 ATOM 2972 N N . GLN A 1 394 ? 37.351 -28.858 -62.981 1.00 22.24 ? 394 GLN A N 1 ATOM 2973 C CA A GLN A 1 394 ? 38.714 -29.078 -62.491 0.50 22.91 ? 394 GLN A CA 1 ATOM 2974 C CA B GLN A 1 394 ? 38.728 -29.048 -62.503 0.50 22.98 ? 394 GLN A CA 1 ATOM 2975 C C . GLN A 1 394 ? 39.597 -29.595 -63.635 1.00 23.42 ? 394 GLN A C 1 ATOM 2976 O O . GLN A 1 394 ? 39.681 -28.955 -64.684 1.00 26.60 ? 394 GLN A O 1 ATOM 2977 C CB A GLN A 1 394 ? 38.651 -30.018 -61.276 0.50 22.83 ? 394 GLN A CB 1 ATOM 2978 C CB B GLN A 1 394 ? 38.726 -29.913 -61.234 0.50 23.01 ? 394 GLN A CB 1 ATOM 2979 C CG A GLN A 1 394 ? 37.849 -29.423 -60.122 0.50 23.16 ? 394 GLN A CG 1 ATOM 2980 C CG B GLN A 1 394 ? 38.103 -29.192 -60.044 0.50 23.47 ? 394 GLN A CG 1 ATOM 2981 C CD A GLN A 1 394 ? 37.433 -30.427 -59.072 0.50 23.28 ? 394 GLN A CD 1 ATOM 2982 C CD B GLN A 1 394 ? 38.312 -29.907 -58.723 0.50 23.70 ? 394 GLN A CD 1 ATOM 2983 O OE1 A GLN A 1 394 ? 38.281 -31.037 -58.424 0.50 24.04 ? 394 GLN A OE1 1 ATOM 2984 O OE1 B GLN A 1 394 ? 38.194 -31.124 -58.639 0.50 24.64 ? 394 GLN A OE1 1 ATOM 2985 N NE2 A GLN A 1 394 ? 36.118 -30.570 -58.863 0.50 23.49 ? 394 GLN A NE2 1 ATOM 2986 N NE2 B GLN A 1 394 ? 38.624 -29.144 -57.681 0.50 23.58 ? 394 GLN A NE2 1 ATOM 2987 N N . ILE A 1 395 ? 40.279 -30.717 -63.443 1.00 22.16 ? 395 ILE A N 1 ATOM 2988 C CA . ILE A 1 395 ? 40.996 -31.387 -64.521 1.00 21.71 ? 395 ILE A CA 1 ATOM 2989 C C . ILE A 1 395 ? 40.433 -32.797 -64.572 1.00 21.56 ? 395 ILE A C 1 ATOM 2990 O O . ILE A 1 395 ? 39.780 -33.248 -63.611 1.00 21.25 ? 395 ILE A O 1 ATOM 2991 C CB . ILE A 1 395 ? 42.525 -31.444 -64.281 1.00 21.74 ? 395 ILE A CB 1 ATOM 2992 C CG1 . ILE A 1 395 ? 42.846 -32.188 -62.971 1.00 21.94 ? 395 ILE A CG1 1 ATOM 2993 C CG2 . ILE A 1 395 ? 43.111 -30.023 -64.272 1.00 21.64 ? 395 ILE A CG2 1 ATOM 2994 C CD1 . ILE A 1 395 ? 44.312 -32.542 -62.789 1.00 21.74 ? 395 ILE A CD1 1 ATOM 2995 N N . GLU A 1 396 ? 40.695 -33.500 -65.664 1.00 21.41 ? 396 GLU A N 1 ATOM 2996 C CA . GLU A 1 396 ? 40.358 -34.913 -65.756 1.00 22.00 ? 396 GLU A CA 1 ATOM 2997 C C . GLU A 1 396 ? 41.332 -35.742 -64.907 1.00 21.25 ? 396 GLU A C 1 ATOM 2998 O O . GLU A 1 396 ? 42.503 -35.375 -64.731 1.00 20.57 ? 396 GLU A O 1 ATOM 2999 C CB . GLU A 1 396 ? 40.364 -35.380 -67.220 1.00 23.80 ? 396 GLU A CB 1 ATOM 3000 C CG . GLU A 1 396 ? 39.365 -34.615 -68.105 1.00 25.20 ? 396 GLU A CG 1 ATOM 3001 C CD . GLU A 1 396 ? 37.897 -34.780 -67.700 1.00 27.32 ? 396 GLU A CD 1 ATOM 3002 O OE1 . GLU A 1 396 ? 37.521 -35.837 -67.130 1.00 28.73 ? 396 GLU A OE1 1 ATOM 3003 O OE2 . GLU A 1 396 ? 37.087 -33.855 -67.986 1.00 28.09 ? 396 GLU A OE2 1 ATOM 3004 N N . LYS A 1 397 ? 40.825 -36.836 -64.365 1.00 20.94 ? 397 LYS A N 1 ATOM 3005 C CA . LYS A 1 397 ? 41.561 -37.667 -63.421 1.00 21.24 ? 397 LYS A CA 1 ATOM 3006 C C . LYS A 1 397 ? 41.567 -39.156 -63.784 1.00 22.39 ? 397 LYS A C 1 ATOM 3007 O O . LYS A 1 397 ? 42.218 -39.943 -63.108 1.00 22.47 ? 397 LYS A O 1 ATOM 3008 C CB . LYS A 1 397 ? 40.975 -37.436 -62.024 1.00 21.00 ? 397 LYS A CB 1 ATOM 3009 C CG . LYS A 1 397 ? 41.185 -35.977 -61.579 1.00 21.40 ? 397 LYS A CG 1 ATOM 3010 C CD . LYS A 1 397 ? 40.549 -35.645 -60.252 1.00 21.44 ? 397 LYS A CD 1 ATOM 3011 C CE . LYS A 1 397 ? 40.576 -34.132 -59.990 1.00 21.53 ? 397 LYS A CE 1 ATOM 3012 N NZ . LYS A 1 397 ? 40.140 -33.830 -58.599 1.00 21.67 ? 397 LYS A NZ 1 ATOM 3013 N N . GLU A 1 398 ? 40.852 -39.523 -64.839 1.00 22.65 ? 398 GLU A N 1 ATOM 3014 C CA . GLU A 1 398 ? 40.893 -40.873 -65.427 1.00 24.47 ? 398 GLU A CA 1 ATOM 3015 C C . GLU A 1 398 ? 41.012 -40.687 -66.924 1.00 24.47 ? 398 GLU A C 1 ATOM 3016 O O . GLU A 1 398 ? 40.449 -39.722 -67.482 1.00 23.57 ? 398 GLU A O 1 ATOM 3017 C CB . GLU A 1 398 ? 39.611 -41.659 -65.118 1.00 27.50 ? 398 GLU A CB 1 ATOM 3018 C CG . GLU A 1 398 ? 39.396 -41.926 -63.642 1.00 30.26 ? 398 GLU A CG 1 ATOM 3019 C CD . GLU A 1 398 ? 38.209 -42.843 -63.364 1.00 34.41 ? 398 GLU A CD 1 ATOM 3020 O OE1 . GLU A 1 398 ? 37.614 -43.382 -64.322 1.00 38.33 ? 398 GLU A OE1 1 ATOM 3021 O OE2 . GLU A 1 398 ? 37.883 -43.049 -62.172 1.00 37.75 ? 398 GLU A OE2 1 ATOM 3022 N N . PHE A 1 399 ? 41.716 -41.609 -67.586 1.00 24.03 ? 399 PHE A N 1 ATOM 3023 C CA . PHE A 1 399 ? 42.013 -41.477 -69.021 1.00 24.54 ? 399 PHE A CA 1 ATOM 3024 C C . PHE A 1 399 ? 41.822 -42.811 -69.739 1.00 26.75 ? 399 PHE A C 1 ATOM 3025 O O . PHE A 1 399 ? 42.317 -43.821 -69.266 1.00 26.59 ? 399 PHE A O 1 ATOM 3026 C CB . PHE A 1 399 ? 43.468 -41.002 -69.172 1.00 24.09 ? 399 PHE A CB 1 ATOM 3027 C CG . PHE A 1 399 ? 43.737 -39.735 -68.431 1.00 23.13 ? 399 PHE A CG 1 ATOM 3028 C CD1 . PHE A 1 399 ? 44.087 -39.757 -67.084 1.00 23.28 ? 399 PHE A CD1 1 ATOM 3029 C CD2 . PHE A 1 399 ? 43.541 -38.521 -69.054 1.00 23.76 ? 399 PHE A CD2 1 ATOM 3030 C CE1 . PHE A 1 399 ? 44.268 -38.573 -66.387 1.00 23.54 ? 399 PHE A CE1 1 ATOM 3031 C CE2 . PHE A 1 399 ? 43.725 -37.325 -68.366 1.00 23.65 ? 399 PHE A CE2 1 ATOM 3032 C CZ . PHE A 1 399 ? 44.089 -37.357 -67.028 1.00 23.67 ? 399 PHE A CZ 1 ATOM 3033 N N . SER A 1 400 ? 41.116 -42.788 -70.862 1.00 28.51 ? 400 SER A N 1 ATOM 3034 C CA . SER A 1 400 ? 40.897 -43.995 -71.670 1.00 31.49 ? 400 SER A CA 1 ATOM 3035 C C . SER A 1 400 ? 41.997 -44.280 -72.713 1.00 32.88 ? 400 SER A C 1 ATOM 3036 O O . SER A 1 400 ? 42.084 -45.406 -73.219 1.00 32.79 ? 400 SER A O 1 ATOM 3037 C CB . SER A 1 400 ? 39.542 -43.897 -72.347 1.00 32.03 ? 400 SER A CB 1 ATOM 3038 O OG . SER A 1 400 ? 39.510 -42.770 -73.202 1.00 35.16 ? 400 SER A OG 1 ATOM 3039 N N . GLU A 1 401 ? 42.835 -43.288 -73.023 1.00 32.22 ? 401 GLU A N 1 ATOM 3040 C CA . GLU A 1 401 ? 43.940 -43.468 -73.981 1.00 33.95 ? 401 GLU A CA 1 ATOM 3041 C C . GLU A 1 401 ? 45.276 -43.098 -73.365 1.00 32.54 ? 401 GLU A C 1 ATOM 3042 O O . GLU A 1 401 ? 45.346 -42.275 -72.455 1.00 31.01 ? 401 GLU A O 1 ATOM 3043 C CB . GLU A 1 401 ? 43.757 -42.599 -75.236 1.00 36.65 ? 401 GLU A CB 1 ATOM 3044 C CG . GLU A 1 401 ? 42.625 -43.033 -76.141 1.00 41.60 ? 401 GLU A CG 1 ATOM 3045 C CD . GLU A 1 401 ? 41.283 -42.594 -75.620 1.00 44.81 ? 401 GLU A CD 1 ATOM 3046 O OE1 . GLU A 1 401 ? 41.169 -41.405 -75.238 1.00 49.36 ? 401 GLU A OE1 1 ATOM 3047 O OE2 . GLU A 1 401 ? 40.351 -43.436 -75.584 1.00 46.73 ? 401 GLU A OE2 1 ATOM 3048 N N . VAL A 1 402 ? 46.329 -43.689 -73.908 1.00 31.47 ? 402 VAL A N 1 ATOM 3049 C CA . VAL A 1 402 ? 47.708 -43.361 -73.559 1.00 31.09 ? 402 VAL A CA 1 ATOM 3050 C C . VAL A 1 402 ? 48.115 -42.095 -74.326 1.00 30.12 ? 402 VAL A C 1 ATOM 3051 O O . VAL A 1 402 ? 47.905 -42.012 -75.542 1.00 28.67 ? 402 VAL A O 1 ATOM 3052 C CB . VAL A 1 402 ? 48.621 -44.564 -73.928 1.00 32.51 ? 402 VAL A CB 1 ATOM 3053 C CG1 . VAL A 1 402 ? 50.087 -44.182 -73.923 1.00 31.83 ? 402 VAL A CG1 1 ATOM 3054 C CG2 . VAL A 1 402 ? 48.367 -45.718 -72.963 1.00 33.86 ? 402 VAL A CG2 1 ATOM 3055 N N . GLU A 1 403 ? 48.694 -41.112 -73.638 1.00 29.31 ? 403 GLU A N 1 ATOM 3056 C CA . GLU A 1 403 ? 49.062 -39.826 -74.268 1.00 29.30 ? 403 GLU A CA 1 ATOM 3057 C C . GLU A 1 403 ? 50.482 -39.307 -73.984 1.00 28.68 ? 403 GLU A C 1 ATOM 3058 O O . GLU A 1 403 ? 51.021 -38.510 -74.756 1.00 30.33 ? 403 GLU A O 1 ATOM 3059 C CB . GLU A 1 403 ? 48.078 -38.730 -73.830 1.00 30.09 ? 403 GLU A CB 1 ATOM 3060 C CG . GLU A 1 403 ? 46.633 -38.981 -74.221 1.00 30.86 ? 403 GLU A CG 1 ATOM 3061 C CD . GLU A 1 403 ? 45.695 -37.953 -73.619 1.00 31.81 ? 403 GLU A CD 1 ATOM 3062 O OE1 . GLU A 1 403 ? 45.555 -37.897 -72.373 1.00 31.62 ? 403 GLU A OE1 1 ATOM 3063 O OE2 . GLU A 1 403 ? 45.099 -37.185 -74.391 1.00 32.95 ? 403 GLU A OE2 1 ATOM 3064 N N . GLY A 1 404 ? 51.068 -39.703 -72.863 1.00 26.68 ? 404 GLY A N 1 ATOM 3065 C CA . GLY A 1 404 ? 52.426 -39.308 -72.532 1.00 25.73 ? 404 GLY A CA 1 ATOM 3066 C C . GLY A 1 404 ? 52.435 -38.023 -71.699 1.00 24.68 ? 404 GLY A C 1 ATOM 3067 O O . GLY A 1 404 ? 51.699 -37.915 -70.732 1.00 23.79 ? 404 GLY A O 1 ATOM 3068 N N . ARG A 1 405 ? 53.235 -37.053 -72.120 1.00 23.97 ? 405 ARG A N 1 ATOM 3069 C CA . ARG A 1 405 ? 53.618 -35.910 -71.281 1.00 23.86 ? 405 ARG A CA 1 ATOM 3070 C C . ARG A 1 405 ? 52.498 -35.170 -70.528 1.00 23.28 ? 405 ARG A C 1 ATOM 3071 O O . ARG A 1 405 ? 52.605 -34.965 -69.321 1.00 22.09 ? 405 ARG A O 1 ATOM 3072 C CB . ARG A 1 405 ? 54.363 -34.915 -72.145 1.00 24.47 ? 405 ARG A CB 1 ATOM 3073 C CG . ARG A 1 405 ? 55.140 -33.881 -71.367 1.00 24.92 ? 405 ARG A CG 1 ATOM 3074 C CD . ARG A 1 405 ? 55.973 -33.025 -72.331 1.00 25.46 ? 405 ARG A CD 1 ATOM 3075 N NE . ARG A 1 405 ? 56.751 -32.072 -71.563 1.00 25.60 ? 405 ARG A NE 1 ATOM 3076 C CZ . ARG A 1 405 ? 57.698 -31.294 -72.061 1.00 26.13 ? 405 ARG A CZ 1 ATOM 3077 N NH1 . ARG A 1 405 ? 57.990 -31.341 -73.344 1.00 25.74 ? 405 ARG A NH1 1 ATOM 3078 N NH2 . ARG A 1 405 ? 58.356 -30.479 -71.254 1.00 26.47 ? 405 ARG A NH2 1 ATOM 3079 N N . ILE A 1 406 ? 51.480 -34.696 -71.238 1.00 22.76 ? 406 ILE A N 1 ATOM 3080 C CA . ILE A 1 406 ? 50.437 -33.891 -70.588 1.00 23.40 ? 406 ILE A CA 1 ATOM 3081 C C . ILE A 1 406 ? 49.668 -34.718 -69.548 1.00 22.70 ? 406 ILE A C 1 ATOM 3082 O O . ILE A 1 406 ? 49.394 -34.255 -68.432 1.00 20.62 ? 406 ILE A O 1 ATOM 3083 C CB . ILE A 1 406 ? 49.453 -33.289 -71.613 1.00 25.14 ? 406 ILE A CB 1 ATOM 3084 C CG1 . ILE A 1 406 ? 48.434 -32.384 -70.922 1.00 25.21 ? 406 ILE A CG1 1 ATOM 3085 C CG2 . ILE A 1 406 ? 48.665 -34.382 -72.330 1.00 25.29 ? 406 ILE A CG2 1 ATOM 3086 C CD1 . ILE A 1 406 ? 49.014 -31.094 -70.390 1.00 27.18 ? 406 ILE A CD1 1 ATOM 3087 N N . GLN A 1 407 ? 49.358 -35.961 -69.906 1.00 21.81 ? 407 GLN A N 1 ATOM 3088 C CA . GLN A 1 407 ? 48.679 -36.864 -68.985 1.00 21.92 ? 407 GLN A CA 1 ATOM 3089 C C . GLN A 1 407 ? 49.541 -37.224 -67.779 1.00 20.93 ? 407 GLN A C 1 ATOM 3090 O O . GLN A 1 407 ? 49.030 -37.347 -66.672 1.00 20.67 ? 407 GLN A O 1 ATOM 3091 C CB . GLN A 1 407 ? 48.230 -38.129 -69.732 1.00 22.00 ? 407 GLN A CB 1 ATOM 3092 C CG . GLN A 1 407 ? 47.300 -39.005 -68.921 1.00 22.20 ? 407 GLN A CG 1 ATOM 3093 C CD . GLN A 1 407 ? 46.911 -40.284 -69.651 1.00 23.05 ? 407 GLN A CD 1 ATOM 3094 O OE1 . GLN A 1 407 ? 47.145 -41.375 -69.140 1.00 24.47 ? 407 GLN A OE1 1 ATOM 3095 N NE2 . GLN A 1 407 ? 46.326 -40.155 -70.837 1.00 22.33 ? 407 GLN A NE2 1 ATOM 3096 N N . ASP A 1 408 ? 50.844 -37.402 -67.985 1.00 21.01 ? 408 ASP A N 1 ATOM 3097 C CA . ASP A 1 408 ? 51.764 -37.649 -66.880 1.00 21.01 ? 408 ASP A CA 1 ATOM 3098 C C . ASP A 1 408 ? 51.661 -36.476 -65.875 1.00 20.39 ? 408 ASP A C 1 ATOM 3099 O O . ASP A 1 408 ? 51.640 -36.690 -64.659 1.00 19.26 ? 408 ASP A O 1 ATOM 3100 C CB . ASP A 1 408 ? 53.202 -37.709 -67.350 1.00 22.47 ? 408 ASP A CB 1 ATOM 3101 C CG . ASP A 1 408 ? 53.522 -38.939 -68.196 1.00 24.32 ? 408 ASP A CG 1 ATOM 3102 O OD1 . ASP A 1 408 ? 52.776 -39.967 -68.151 1.00 24.56 ? 408 ASP A OD1 1 ATOM 3103 O OD2 . ASP A 1 408 ? 54.552 -38.830 -68.918 1.00 24.65 ? 408 ASP A OD2 1 ATOM 3104 N N . LEU A 1 409 ? 51.597 -35.255 -66.411 1.00 19.66 ? 409 LEU A N 1 ATOM 3105 C CA . LEU A 1 409 ? 51.521 -34.052 -65.549 1.00 19.73 ? 409 LEU A CA 1 ATOM 3106 C C . LEU A 1 409 ? 50.179 -33.986 -64.807 1.00 19.17 ? 409 LEU A C 1 ATOM 3107 O O . LEU A 1 409 ? 50.158 -33.767 -63.600 1.00 18.70 ? 409 LEU A O 1 ATOM 3108 C CB . LEU A 1 409 ? 51.749 -32.804 -66.383 1.00 19.75 ? 409 LEU A CB 1 ATOM 3109 C CG . LEU A 1 409 ? 51.904 -31.480 -65.630 1.00 19.89 ? 409 LEU A CG 1 ATOM 3110 C CD1 . LEU A 1 409 ? 52.931 -31.570 -64.505 1.00 19.78 ? 409 LEU A CD1 1 ATOM 3111 C CD2 . LEU A 1 409 ? 52.276 -30.434 -66.669 1.00 20.46 ? 409 LEU A CD2 1 ATOM 3112 N N . GLU A 1 410 ? 49.082 -34.237 -65.515 1.00 19.62 ? 410 GLU A N 1 ATOM 3113 C CA . GLU A 1 410 ? 47.741 -34.232 -64.895 1.00 20.34 ? 410 GLU A CA 1 ATOM 3114 C C . GLU A 1 410 ? 47.690 -35.236 -63.743 1.00 20.10 ? 410 GLU A C 1 ATOM 3115 O O . GLU A 1 410 ? 47.228 -34.926 -62.637 1.00 19.04 ? 410 GLU A O 1 ATOM 3116 C CB . GLU A 1 410 ? 46.651 -34.522 -65.931 1.00 21.45 ? 410 GLU A CB 1 ATOM 3117 C CG . GLU A 1 410 ? 46.442 -33.366 -66.887 1.00 22.49 ? 410 GLU A CG 1 ATOM 3118 C CD . GLU A 1 410 ? 45.732 -33.710 -68.211 1.00 25.77 ? 410 GLU A CD 1 ATOM 3119 O OE1 . GLU A 1 410 ? 45.775 -34.887 -68.664 1.00 26.94 ? 410 GLU A OE1 1 ATOM 3120 O OE2 . GLU A 1 410 ? 45.156 -32.764 -68.841 1.00 27.20 ? 410 GLU A OE2 1 ATOM 3121 N N . LYS A 1 411 ? 48.189 -36.437 -63.990 1.00 19.56 ? 411 LYS A N 1 ATOM 3122 C CA . LYS A 1 411 ? 48.237 -37.470 -62.958 1.00 20.46 ? 411 LYS A CA 1 ATOM 3123 C C . LYS A 1 411 ? 49.122 -37.113 -61.784 1.00 19.25 ? 411 LYS A C 1 ATOM 3124 O O . LYS A 1 411 ? 48.768 -37.368 -60.641 1.00 18.78 ? 411 LYS A O 1 ATOM 3125 C CB . LYS A 1 411 ? 48.687 -38.806 -63.543 1.00 21.65 ? 411 LYS A CB 1 ATOM 3126 C CG . LYS A 1 411 ? 47.645 -39.437 -64.461 1.00 23.29 ? 411 LYS A CG 1 ATOM 3127 C CD . LYS A 1 411 ? 48.120 -40.839 -64.875 1.00 25.48 ? 411 LYS A CD 1 ATOM 3128 C CE . LYS A 1 411 ? 47.112 -41.543 -65.746 1.00 27.42 ? 411 LYS A CE 1 ATOM 3129 N NZ . LYS A 1 411 ? 47.456 -42.983 -65.969 1.00 29.03 ? 411 LYS A NZ 1 ATOM 3130 N N . TYR A 1 412 ? 50.258 -36.489 -62.059 1.00 18.79 ? 412 TYR A N 1 ATOM 3131 C CA . TYR A 1 412 ? 51.200 -36.164 -60.992 1.00 18.53 ? 412 TYR A CA 1 ATOM 3132 C C . TYR A 1 412 ? 50.655 -35.045 -60.122 1.00 17.82 ? 412 TYR A C 1 ATOM 3133 O O . TYR A 1 412 ? 50.822 -35.068 -58.924 1.00 17.78 ? 412 TYR A O 1 ATOM 3134 C CB . TYR A 1 412 ? 52.530 -35.734 -61.583 1.00 18.76 ? 412 TYR A CB 1 ATOM 3135 C CG . TYR A 1 412 ? 53.653 -35.508 -60.613 1.00 19.26 ? 412 TYR A CG 1 ATOM 3136 C CD1 . TYR A 1 412 ? 54.317 -36.575 -60.028 1.00 19.64 ? 412 TYR A CD1 1 ATOM 3137 C CD2 . TYR A 1 412 ? 54.124 -34.211 -60.332 1.00 19.36 ? 412 TYR A CD2 1 ATOM 3138 C CE1 . TYR A 1 412 ? 55.397 -36.375 -59.179 1.00 19.78 ? 412 TYR A CE1 1 ATOM 3139 C CE2 . TYR A 1 412 ? 55.205 -34.005 -59.487 1.00 19.72 ? 412 TYR A CE2 1 ATOM 3140 C CZ . TYR A 1 412 ? 55.836 -35.098 -58.905 1.00 19.91 ? 412 TYR A CZ 1 ATOM 3141 O OH . TYR A 1 412 ? 56.906 -34.944 -58.065 1.00 20.12 ? 412 TYR A OH 1 ATOM 3142 N N . VAL A 1 413 ? 49.958 -34.100 -60.732 1.00 17.99 ? 413 VAL A N 1 ATOM 3143 C CA . VAL A 1 413 ? 49.375 -32.993 -59.988 1.00 17.76 ? 413 VAL A CA 1 ATOM 3144 C C . VAL A 1 413 ? 48.340 -33.541 -58.992 1.00 17.90 ? 413 VAL A C 1 ATOM 3145 O O . VAL A 1 413 ? 48.340 -33.176 -57.813 1.00 17.44 ? 413 VAL A O 1 ATOM 3146 C CB . VAL A 1 413 ? 48.747 -31.992 -60.960 1.00 17.85 ? 413 VAL A CB 1 ATOM 3147 C CG1 . VAL A 1 413 ? 47.847 -31.023 -60.213 1.00 18.17 ? 413 VAL A CG1 1 ATOM 3148 C CG2 . VAL A 1 413 ? 49.841 -31.204 -61.702 1.00 18.13 ? 413 VAL A CG2 1 ATOM 3149 N N . GLU A 1 414 ? 47.521 -34.482 -59.454 1.00 18.41 ? 414 GLU A N 1 ATOM 3150 C CA . GLU A 1 414 ? 46.464 -35.022 -58.614 1.00 19.47 ? 414 GLU A CA 1 ATOM 3151 C C . GLU A 1 414 ? 47.043 -35.911 -57.513 1.00 19.33 ? 414 GLU A C 1 ATOM 3152 O O . GLU A 1 414 ? 46.655 -35.794 -56.344 1.00 18.43 ? 414 GLU A O 1 ATOM 3153 C CB . GLU A 1 414 ? 45.448 -35.772 -59.461 1.00 20.51 ? 414 GLU A CB 1 ATOM 3154 C CG . GLU A 1 414 ? 44.203 -36.225 -58.688 1.00 21.91 ? 414 GLU A CG 1 ATOM 3155 C CD . GLU A 1 414 ? 43.341 -35.096 -58.135 1.00 23.09 ? 414 GLU A CD 1 ATOM 3156 O OE1 . GLU A 1 414 ? 43.606 -33.907 -58.433 1.00 25.31 ? 414 GLU A OE1 1 ATOM 3157 O OE2 . GLU A 1 414 ? 42.364 -35.391 -57.395 1.00 24.34 ? 414 GLU A OE2 1 ATOM 3158 N N . ASP A 1 415 ? 47.969 -36.800 -57.867 1.00 19.78 ? 415 ASP A N 1 ATOM 3159 C CA . ASP A 1 415 ? 48.660 -37.617 -56.855 1.00 20.58 ? 415 ASP A CA 1 ATOM 3160 C C . ASP A 1 415 ? 49.305 -36.749 -55.775 1.00 19.41 ? 415 ASP A C 1 ATOM 3161 O O . ASP A 1 415 ? 49.218 -37.073 -54.586 1.00 19.11 ? 415 ASP A O 1 ATOM 3162 C CB . ASP A 1 415 ? 49.753 -38.474 -57.483 1.00 22.33 ? 415 ASP A CB 1 ATOM 3163 C CG . ASP A 1 415 ? 50.203 -39.601 -56.574 1.00 25.71 ? 415 ASP A CG 1 ATOM 3164 O OD1 . ASP A 1 415 ? 49.353 -40.314 -56.021 1.00 29.04 ? 415 ASP A OD1 1 ATOM 3165 O OD2 . ASP A 1 415 ? 51.416 -39.768 -56.382 1.00 29.23 ? 415 ASP A OD2 1 ATOM 3166 N N . THR A 1 416 ? 49.977 -35.681 -56.200 1.00 18.38 ? 416 THR A N 1 ATOM 3167 C CA . THR A 1 416 ? 50.644 -34.755 -55.286 1.00 18.04 ? 416 THR A CA 1 ATOM 3168 C C . THR A 1 416 ? 49.652 -34.140 -54.317 1.00 17.10 ? 416 THR A C 1 ATOM 3169 O O . THR A 1 416 ? 49.861 -34.139 -53.112 1.00 16.66 ? 416 THR A O 1 ATOM 3170 C CB . THR A 1 416 ? 51.367 -33.657 -56.074 1.00 18.14 ? 416 THR A CB 1 ATOM 3171 O OG1 . THR A 1 416 ? 52.408 -34.273 -56.840 1.00 19.14 ? 416 THR A OG1 1 ATOM 3172 C CG2 . THR A 1 416 ? 52.007 -32.607 -55.131 1.00 18.19 ? 416 THR A CG2 1 ATOM 3173 N N . LYS A 1 417 ? 48.539 -33.664 -54.865 1.00 16.53 ? 417 LYS A N 1 ATOM 3174 C CA . LYS A 1 417 ? 47.481 -33.046 -54.060 1.00 16.50 ? 417 LYS A CA 1 ATOM 3175 C C . LYS A 1 417 ? 46.903 -34.022 -53.031 1.00 16.18 ? 417 LYS A C 1 ATOM 3176 O O . LYS A 1 417 ? 46.761 -33.703 -51.860 1.00 15.59 ? 417 LYS A O 1 ATOM 3177 C CB . LYS A 1 417 ? 46.366 -32.539 -54.979 1.00 16.37 ? 417 LYS A CB 1 ATOM 3178 C CG . LYS A 1 417 ? 45.167 -31.989 -54.232 1.00 16.84 ? 417 LYS A CG 1 ATOM 3179 C CD . LYS A 1 417 ? 44.097 -31.406 -55.162 1.00 17.47 ? 417 LYS A CD 1 ATOM 3180 C CE . LYS A 1 417 ? 42.809 -31.118 -54.399 1.00 17.85 ? 417 LYS A CE 1 ATOM 3181 N NZ . LYS A 1 417 ? 41.701 -30.691 -55.332 1.00 19.08 ? 417 LYS A NZ 1 ATOM 3182 N N . ILE A 1 418 ? 46.589 -35.221 -53.477 1.00 16.07 ? 418 ILE A N 1 ATOM 3183 C CA . ILE A 1 418 ? 45.961 -36.205 -52.592 1.00 16.11 ? 418 ILE A CA 1 ATOM 3184 C C . ILE A 1 418 ? 46.924 -36.602 -51.477 1.00 15.96 ? 418 ILE A C 1 ATOM 3185 O O . ILE A 1 418 ? 46.511 -36.758 -50.333 1.00 15.27 ? 418 ILE A O 1 ATOM 3186 C CB . ILE A 1 418 ? 45.528 -37.439 -53.380 1.00 16.54 ? 418 ILE A CB 1 ATOM 3187 C CG1 . ILE A 1 418 ? 44.401 -37.059 -54.337 1.00 16.69 ? 418 ILE A CG1 1 ATOM 3188 C CG2 . ILE A 1 418 ? 45.059 -38.538 -52.439 1.00 16.57 ? 418 ILE A CG2 1 ATOM 3189 C CD1 . ILE A 1 418 ? 44.093 -38.137 -55.389 1.00 17.80 ? 418 ILE A CD1 1 ATOM 3190 N N . ASP A 1 419 ? 48.205 -36.737 -51.783 1.00 15.92 ? 419 ASP A N 1 ATOM 3191 C CA . ASP A 1 419 ? 49.132 -37.124 -50.711 1.00 16.41 ? 419 ASP A CA 1 ATOM 3192 C C . ASP A 1 419 ? 49.253 -35.993 -49.676 1.00 15.76 ? 419 ASP A C 1 ATOM 3193 O O . ASP A 1 419 ? 49.354 -36.258 -48.473 1.00 15.79 ? 419 ASP A O 1 ATOM 3194 C CB . ASP A 1 419 ? 50.519 -37.453 -51.260 1.00 17.42 ? 419 ASP A CB 1 ATOM 3195 C CG . ASP A 1 419 ? 50.602 -38.864 -51.865 1.00 19.58 ? 419 ASP A CG 1 ATOM 3196 O OD1 . ASP A 1 419 ? 49.604 -39.654 -51.758 1.00 20.67 ? 419 ASP A OD1 1 ATOM 3197 O OD2 . ASP A 1 419 ? 51.676 -39.156 -52.430 1.00 20.90 ? 419 ASP A OD2 1 ATOM 3198 N N . LEU A 1 420 ? 49.265 -34.746 -50.135 1.00 15.40 ? 420 LEU A N 1 ATOM 3199 C CA . LEU A 1 420 ? 49.349 -33.610 -49.202 1.00 15.39 ? 420 LEU A CA 1 ATOM 3200 C C . LEU A 1 420 ? 48.118 -33.472 -48.303 1.00 15.28 ? 420 LEU A C 1 ATOM 3201 O O . LEU A 1 420 ? 48.253 -33.291 -47.087 1.00 15.51 ? 420 LEU A O 1 ATOM 3202 C CB . LEU A 1 420 ? 49.671 -32.314 -49.934 1.00 15.30 ? 420 LEU A CB 1 ATOM 3203 C CG . LEU A 1 420 ? 51.129 -32.226 -50.365 1.00 15.31 ? 420 LEU A CG 1 ATOM 3204 C CD1 . LEU A 1 420 ? 51.306 -31.245 -51.540 1.00 15.34 ? 420 LEU A CD1 1 ATOM 3205 C CD2 . LEU A 1 420 ? 52.076 -31.881 -49.212 1.00 15.54 ? 420 LEU A CD2 1 ATOM 3206 N N . TRP A 1 421 ? 46.930 -33.628 -48.880 1.00 15.54 ? 421 TRP A N 1 ATOM 3207 C CA . TRP A 1 421 ? 45.707 -33.661 -48.079 1.00 15.56 ? 421 TRP A CA 1 ATOM 3208 C C . TRP A 1 421 ? 45.597 -34.819 -47.123 1.00 15.70 ? 421 TRP A C 1 ATOM 3209 O O . TRP A 1 421 ? 45.117 -34.638 -45.992 1.00 15.59 ? 421 TRP A O 1 ATOM 3210 C CB . TRP A 1 421 ? 44.472 -33.527 -48.982 1.00 15.44 ? 421 TRP A CB 1 ATOM 3211 C CG . TRP A 1 421 ? 44.250 -32.087 -49.318 1.00 15.48 ? 421 TRP A CG 1 ATOM 3212 C CD1 . TRP A 1 421 ? 44.383 -31.462 -50.554 1.00 15.65 ? 421 TRP A CD1 1 ATOM 3213 C CD2 . TRP A 1 421 ? 43.947 -31.014 -48.367 1.00 15.56 ? 421 TRP A CD2 1 ATOM 3214 N NE1 . TRP A 1 421 ? 44.154 -30.110 -50.429 1.00 15.94 ? 421 TRP A NE1 1 ATOM 3215 C CE2 . TRP A 1 421 ? 43.907 -29.782 -49.136 1.00 16.05 ? 421 TRP A CE2 1 ATOM 3216 C CE3 . TRP A 1 421 ? 43.705 -30.971 -46.994 1.00 15.85 ? 421 TRP A CE3 1 ATOM 3217 C CZ2 . TRP A 1 421 ? 43.625 -28.550 -48.543 1.00 16.05 ? 421 TRP A CZ2 1 ATOM 3218 C CZ3 . TRP A 1 421 ? 43.462 -29.729 -46.404 1.00 16.25 ? 421 TRP A CZ3 1 ATOM 3219 C CH2 . TRP A 1 421 ? 43.408 -28.558 -47.163 1.00 16.42 ? 421 TRP A CH2 1 ATOM 3220 N N . SER A 1 422 ? 46.000 -36.012 -47.558 1.00 15.71 ? 422 SER A N 1 ATOM 3221 C CA . SER A 1 422 ? 45.981 -37.186 -46.702 1.00 16.06 ? 422 SER A CA 1 ATOM 3222 C C . SER A 1 422 ? 46.887 -37.010 -45.489 1.00 15.98 ? 422 SER A C 1 ATOM 3223 O O . SER A 1 422 ? 46.504 -37.367 -44.370 1.00 15.52 ? 422 SER A O 1 ATOM 3224 C CB . SER A 1 422 ? 46.371 -38.459 -47.466 1.00 16.22 ? 422 SER A CB 1 ATOM 3225 O OG . SER A 1 422 ? 45.515 -38.657 -48.600 1.00 16.61 ? 422 SER A OG 1 ATOM 3226 N N . TYR A 1 423 ? 48.051 -36.396 -45.710 1.00 16.23 ? 423 TYR A N 1 ATOM 3227 C CA . TYR A 1 423 ? 48.969 -36.008 -44.631 1.00 16.74 ? 423 TYR A CA 1 ATOM 3228 C C . TYR A 1 423 ? 48.296 -34.994 -43.702 1.00 16.31 ? 423 TYR A C 1 ATOM 3229 O O . TYR A 1 423 ? 48.303 -35.179 -42.494 1.00 15.92 ? 423 TYR A O 1 ATOM 3230 C CB . TYR A 1 423 ? 50.301 -35.421 -45.187 1.00 17.20 ? 423 TYR A CB 1 ATOM 3231 C CG . TYR A 1 423 ? 51.189 -34.964 -44.072 1.00 17.82 ? 423 TYR A CG 1 ATOM 3232 C CD1 . TYR A 1 423 ? 51.996 -35.877 -43.413 1.00 18.72 ? 423 TYR A CD1 1 ATOM 3233 C CD2 . TYR A 1 423 ? 51.171 -33.659 -43.625 1.00 18.01 ? 423 TYR A CD2 1 ATOM 3234 C CE1 . TYR A 1 423 ? 52.786 -35.506 -42.346 1.00 19.31 ? 423 TYR A CE1 1 ATOM 3235 C CE2 . TYR A 1 423 ? 51.953 -33.261 -42.558 1.00 18.62 ? 423 TYR A CE2 1 ATOM 3236 C CZ . TYR A 1 423 ? 52.771 -34.204 -41.922 1.00 19.71 ? 423 TYR A CZ 1 ATOM 3237 O OH . TYR A 1 423 ? 53.567 -33.885 -40.853 1.00 21.69 ? 423 TYR A OH 1 ATOM 3238 N N . ASN A 1 424 ? 47.707 -33.923 -44.259 1.00 16.14 ? 424 ASN A N 1 ATOM 3239 C CA . ASN A 1 424 ? 47.046 -32.914 -43.405 1.00 16.17 ? 424 ASN A CA 1 ATOM 3240 C C . ASN A 1 424 ? 45.923 -33.543 -42.553 1.00 16.20 ? 424 ASN A C 1 ATOM 3241 O O . ASN A 1 424 ? 45.813 -33.264 -41.362 1.00 16.42 ? 424 ASN A O 1 ATOM 3242 C CB . ASN A 1 424 ? 46.424 -31.810 -44.227 1.00 16.07 ? 424 ASN A CB 1 ATOM 3243 C CG . ASN A 1 424 ? 47.448 -30.911 -44.874 1.00 16.17 ? 424 ASN A CG 1 ATOM 3244 O OD1 . ASN A 1 424 ? 48.593 -30.826 -44.416 1.00 16.43 ? 424 ASN A OD1 1 ATOM 3245 N ND2 . ASN A 1 424 ? 47.023 -30.187 -45.898 1.00 15.73 ? 424 ASN A ND2 1 ATOM 3246 N N . ALA A 1 425 ? 45.177 -34.449 -43.152 1.00 16.07 ? 425 ALA A N 1 ATOM 3247 C CA . ALA A 1 425 ? 44.078 -35.151 -42.435 1.00 17.20 ? 425 ALA A CA 1 ATOM 3248 C C . ALA A 1 425 ? 44.591 -35.996 -41.268 1.00 17.80 ? 425 ALA A C 1 ATOM 3249 O O . ALA A 1 425 ? 44.068 -35.932 -40.137 1.00 18.73 ? 425 ALA A O 1 ATOM 3250 C CB . ALA A 1 425 ? 43.294 -36.030 -43.399 1.00 16.31 ? 425 ALA A CB 1 ATOM 3251 N N . GLU A 1 426 ? 45.622 -36.792 -41.536 1.00 18.87 ? 426 GLU A N 1 ATOM 3252 C CA . GLU A 1 426 ? 46.263 -37.613 -40.523 1.00 20.09 ? 426 GLU A CA 1 ATOM 3253 C C . GLU A 1 426 ? 46.798 -36.773 -39.346 1.00 19.65 ? 426 GLU A C 1 ATOM 3254 O O . GLU A 1 426 ? 46.485 -37.054 -38.178 1.00 19.33 ? 426 GLU A O 1 ATOM 3255 C CB . GLU A 1 426 ? 47.391 -38.433 -41.148 1.00 21.65 ? 426 GLU A CB 1 ATOM 3256 C CG . GLU A 1 426 ? 47.884 -39.583 -40.276 1.00 24.03 ? 426 GLU A CG 1 ATOM 3257 C CD . GLU A 1 426 ? 46.904 -40.764 -40.199 1.00 25.54 ? 426 GLU A CD 1 ATOM 3258 O OE1 . GLU A 1 426 ? 46.268 -41.101 -41.212 1.00 25.47 ? 426 GLU A OE1 1 ATOM 3259 O OE2 . GLU A 1 426 ? 46.772 -41.357 -39.106 1.00 29.22 ? 426 GLU A OE2 1 ATOM 3260 N N . LEU A 1 427 ? 47.531 -35.710 -39.647 1.00 19.01 ? 427 LEU A N 1 ATOM 3261 C CA . LEU A 1 427 ? 48.034 -34.825 -38.604 1.00 19.26 ? 427 LEU A CA 1 ATOM 3262 C C . LEU A 1 427 ? 46.927 -34.094 -37.827 1.00 18.89 ? 427 LEU A C 1 ATOM 3263 O O . LEU A 1 427 ? 46.968 -34.033 -36.602 1.00 19.08 ? 427 LEU A O 1 ATOM 3264 C CB . LEU A 1 427 ? 49.000 -33.816 -39.187 1.00 19.44 ? 427 LEU A CB 1 ATOM 3265 C CG . LEU A 1 427 ? 49.639 -32.855 -38.192 1.00 19.86 ? 427 LEU A CG 1 ATOM 3266 C CD1 . LEU A 1 427 ? 50.469 -33.622 -37.141 1.00 20.17 ? 427 LEU A CD1 1 ATOM 3267 C CD2 . LEU A 1 427 ? 50.513 -31.843 -38.949 1.00 20.61 ? 427 LEU A CD2 1 ATOM 3268 N N . LEU A 1 428 ? 45.921 -33.600 -38.531 1.00 18.75 ? 428 LEU A N 1 ATOM 3269 C CA . LEU A 1 428 ? 44.830 -32.847 -37.910 1.00 19.56 ? 428 LEU A CA 1 ATOM 3270 C C . LEU A 1 428 ? 44.084 -33.685 -36.883 1.00 19.02 ? 428 LEU A C 1 ATOM 3271 O O . LEU A 1 428 ? 43.812 -33.244 -35.749 1.00 18.43 ? 428 LEU A O 1 ATOM 3272 C CB . LEU A 1 428 ? 43.856 -32.338 -38.982 1.00 20.23 ? 428 LEU A CB 1 ATOM 3273 C CG . LEU A 1 428 ? 42.697 -31.487 -38.445 1.00 21.87 ? 428 LEU A CG 1 ATOM 3274 C CD1 . LEU A 1 428 ? 43.228 -30.279 -37.661 1.00 23.28 ? 428 LEU A CD1 1 ATOM 3275 C CD2 . LEU A 1 428 ? 41.824 -31.041 -39.621 1.00 22.42 ? 428 LEU A CD2 1 ATOM 3276 N N . VAL A 1 429 ? 43.790 -34.919 -37.243 1.00 19.41 ? 429 VAL A N 1 ATOM 3277 C CA . VAL A 1 429 ? 43.032 -35.771 -36.344 1.00 19.91 ? 429 VAL A CA 1 ATOM 3278 C C . VAL A 1 429 ? 43.878 -36.206 -35.128 1.00 20.11 ? 429 VAL A C 1 ATOM 3279 O O . VAL A 1 429 ? 43.382 -36.203 -33.987 1.00 20.04 ? 429 VAL A O 1 ATOM 3280 C CB . VAL A 1 429 ? 42.419 -36.956 -37.098 1.00 21.13 ? 429 VAL A CB 1 ATOM 3281 C CG1 . VAL A 1 429 ? 41.668 -37.866 -36.128 1.00 22.55 ? 429 VAL A CG1 1 ATOM 3282 C CG2 . VAL A 1 429 ? 41.482 -36.415 -38.173 1.00 21.11 ? 429 VAL A CG2 1 ATOM 3283 N N . ALA A 1 430 ? 45.154 -36.517 -35.349 1.00 19.86 ? 430 ALA A N 1 ATOM 3284 C CA . ALA A 1 430 ? 46.060 -36.843 -34.262 1.00 20.50 ? 430 ALA A CA 1 ATOM 3285 C C . ALA A 1 430 ? 46.202 -35.640 -33.283 1.00 20.24 ? 430 ALA A C 1 ATOM 3286 O O . ALA A 1 430 ? 46.141 -35.817 -32.036 1.00 20.33 ? 430 ALA A O 1 ATOM 3287 C CB . ALA A 1 430 ? 47.433 -37.263 -34.795 1.00 19.98 ? 430 ALA A CB 1 ATOM 3288 N N . LEU A 1 431 ? 46.354 -34.443 -33.837 1.00 19.75 ? 431 LEU A N 1 ATOM 3289 C CA . LEU A 1 431 ? 46.440 -33.213 -33.017 1.00 20.26 ? 431 LEU A CA 1 ATOM 3290 C C . LEU A 1 431 ? 45.152 -32.886 -32.261 1.00 20.33 ? 431 LEU A C 1 ATOM 3291 O O . LEU A 1 431 ? 45.198 -32.553 -31.075 1.00 20.69 ? 431 LEU A O 1 ATOM 3292 C CB . LEU A 1 431 ? 46.846 -32.011 -33.854 1.00 20.17 ? 431 LEU A CB 1 ATOM 3293 C CG . LEU A 1 431 ? 48.289 -31.941 -34.349 1.00 20.92 ? 431 LEU A CG 1 ATOM 3294 C CD1 . LEU A 1 431 ? 48.377 -30.731 -35.279 1.00 21.46 ? 431 LEU A CD1 1 ATOM 3295 C CD2 . LEU A 1 431 ? 49.326 -31.865 -33.220 1.00 21.32 ? 431 LEU A CD2 1 ATOM 3296 N N . GLU A 1 432 ? 44.018 -32.949 -32.944 1.00 21.06 ? 432 GLU A N 1 ATOM 3297 C CA . GLU A 1 432 ? 42.734 -32.733 -32.297 1.00 22.06 ? 432 GLU A CA 1 ATOM 3298 C C . GLU A 1 432 ? 42.484 -33.766 -31.192 1.00 21.06 ? 432 GLU A C 1 ATOM 3299 O O . GLU A 1 432 ? 42.040 -33.392 -30.116 1.00 21.09 ? 432 GLU A O 1 ATOM 3300 C CB . GLU A 1 432 ? 41.593 -32.743 -33.303 1.00 23.67 ? 432 GLU A CB 1 ATOM 3301 C CG . GLU A 1 432 ? 41.628 -31.564 -34.240 1.00 26.58 ? 432 GLU A CG 1 ATOM 3302 C CD . GLU A 1 432 ? 41.074 -30.283 -33.626 1.00 30.42 ? 432 GLU A CD 1 ATOM 3303 O OE1 . GLU A 1 432 ? 40.820 -30.215 -32.388 1.00 33.08 ? 432 GLU A OE1 1 ATOM 3304 O OE2 . GLU A 1 432 ? 40.901 -29.333 -34.402 1.00 37.20 ? 432 GLU A OE2 1 ATOM 3305 N N . ASN A 1 433 ? 42.758 -35.044 -31.451 1.00 19.49 ? 433 ASN A N 1 ATOM 3306 C CA . ASN A 1 433 ? 42.545 -36.078 -30.445 1.00 19.32 ? 433 ASN A CA 1 ATOM 3307 C C . ASN A 1 433 ? 43.451 -35.910 -29.237 1.00 20.00 ? 433 ASN A C 1 ATOM 3308 O O . ASN A 1 433 ? 43.003 -36.091 -28.106 1.00 19.65 ? 433 ASN A O 1 ATOM 3309 C CB . ASN A 1 433 ? 42.706 -37.466 -31.029 1.00 18.92 ? 433 ASN A CB 1 ATOM 3310 C CG . ASN A 1 433 ? 41.606 -37.822 -32.000 1.00 18.65 ? 433 ASN A CG 1 ATOM 3311 O OD1 . ASN A 1 433 ? 40.597 -37.141 -32.077 1.00 19.09 ? 433 ASN A OD1 1 ATOM 3312 N ND2 . ASN A 1 433 ? 41.808 -38.897 -32.762 1.00 18.30 ? 433 ASN A ND2 1 ATOM 3313 N N . GLN A 1 434 ? 44.697 -35.501 -29.463 1.00 20.06 ? 434 GLN A N 1 ATOM 3314 C CA . GLN A 1 434 ? 45.589 -35.200 -28.374 1.00 21.46 ? 434 GLN A CA 1 ATOM 3315 C C . GLN A 1 434 ? 45.030 -34.045 -27.548 1.00 21.01 ? 434 GLN A C 1 ATOM 3316 O O . GLN A 1 434 ? 45.057 -34.093 -26.324 1.00 20.53 ? 434 GLN A O 1 ATOM 3317 C CB . GLN A 1 434 ? 46.988 -34.847 -28.873 1.00 23.70 ? 434 GLN A CB 1 ATOM 3318 C CG . GLN A 1 434 ? 47.976 -34.598 -27.738 1.00 25.82 ? 434 GLN A CG 1 ATOM 3319 C CD . GLN A 1 434 ? 48.250 -35.872 -26.993 1.00 29.28 ? 434 GLN A CD 1 ATOM 3320 O OE1 . GLN A 1 434 ? 48.645 -36.880 -27.611 1.00 31.15 ? 434 GLN A OE1 1 ATOM 3321 N NE2 . GLN A 1 434 ? 47.934 -35.895 -25.669 1.00 32.86 ? 434 GLN A NE2 1 ATOM 3322 N N . HIS A 1 435 ? 44.477 -33.051 -28.222 1.00 21.68 ? 435 HIS A N 1 ATOM 3323 C CA . HIS A 1 435 ? 43.925 -31.879 -27.543 1.00 23.33 ? 435 HIS A CA 1 ATOM 3324 C C . HIS A 1 435 ? 42.680 -32.264 -26.751 1.00 23.13 ? 435 HIS A C 1 ATOM 3325 O O . HIS A 1 435 ? 42.475 -31.784 -25.638 1.00 23.14 ? 435 HIS A O 1 ATOM 3326 C CB . HIS A 1 435 ? 43.603 -30.776 -28.554 1.00 24.36 ? 435 HIS A CB 1 ATOM 3327 C CG . HIS A 1 435 ? 43.042 -29.519 -27.926 1.00 26.20 ? 435 HIS A CG 1 ATOM 3328 N ND1 . HIS A 1 435 ? 41.712 -29.246 -27.901 1.00 27.73 ? 435 HIS A ND1 1 ATOM 3329 C CD2 . HIS A 1 435 ? 43.676 -28.450 -27.298 1.00 27.81 ? 435 HIS A CD2 1 ATOM 3330 C CE1 . HIS A 1 435 ? 41.508 -28.061 -27.280 1.00 28.13 ? 435 HIS A CE1 1 ATOM 3331 N NE2 . HIS A 1 435 ? 42.709 -27.565 -26.928 1.00 29.09 ? 435 HIS A NE2 1 ATOM 3332 N N . THR A 1 436 ? 41.871 -33.157 -27.292 1.00 22.68 ? 436 THR A N 1 ATOM 3333 C CA . THR A 1 436 ? 40.673 -33.654 -26.573 1.00 22.24 ? 436 THR A CA 1 ATOM 3334 C C . THR A 1 436 ? 41.014 -34.431 -25.309 1.00 22.53 ? 436 THR A C 1 ATOM 3335 O O . THR A 1 436 ? 40.416 -34.179 -24.234 1.00 22.97 ? 436 THR A O 1 ATOM 3336 C CB . THR A 1 436 ? 39.782 -34.442 -27.524 1.00 22.11 ? 436 THR A CB 1 ATOM 3337 O OG1 . THR A 1 436 ? 39.322 -33.549 -28.537 1.00 21.77 ? 436 THR A OG1 1 ATOM 3338 C CG2 . THR A 1 436 ? 38.563 -35.084 -26.792 1.00 22.02 ? 436 THR A CG2 1 ATOM 3339 N N . ILE A 1 437 ? 41.980 -35.344 -25.408 1.00 22.23 ? 437 ILE A N 1 ATOM 3340 C CA . ILE A 1 437 ? 42.504 -36.036 -24.254 1.00 23.72 ? 437 ILE A CA 1 ATOM 3341 C C . ILE A 1 437 ? 43.047 -35.041 -23.220 1.00 24.36 ? 437 ILE A C 1 ATOM 3342 O O . ILE A 1 437 ? 42.705 -35.129 -22.029 1.00 23.91 ? 437 ILE A O 1 ATOM 3343 C CB . ILE A 1 437 ? 43.558 -37.085 -24.669 1.00 23.97 ? 437 ILE A CB 1 ATOM 3344 C CG1 . ILE A 1 437 ? 42.906 -38.193 -25.507 1.00 24.59 ? 437 ILE A CG1 1 ATOM 3345 C CG2 . ILE A 1 437 ? 44.303 -37.631 -23.452 1.00 23.94 ? 437 ILE A CG2 1 ATOM 3346 C CD1 . ILE A 1 437 ? 41.721 -38.866 -24.858 1.00 25.86 ? 437 ILE A CD1 1 ATOM 3347 N N . ASP A 1 438 ? 43.862 -34.082 -23.666 1.00 24.19 ? 438 ASP A N 1 ATOM 3348 C CA . ASP A 1 438 ? 44.403 -33.032 -22.774 1.00 25.22 ? 438 ASP A CA 1 ATOM 3349 C C . ASP A 1 438 ? 43.342 -32.162 -22.076 1.00 24.37 ? 438 ASP A C 1 ATOM 3350 O O . ASP A 1 438 ? 43.428 -31.975 -20.876 1.00 25.50 ? 438 ASP A O 1 ATOM 3351 C CB . ASP A 1 438 ? 45.377 -32.102 -23.522 1.00 27.38 ? 438 ASP A CB 1 ATOM 3352 C CG . ASP A 1 438 ? 46.653 -32.792 -23.967 1.00 29.52 ? 438 ASP A CG 1 ATOM 3353 O OD1 . ASP A 1 438 ? 46.869 -33.950 -23.587 1.00 31.87 ? 438 ASP A OD1 1 ATOM 3354 O OD2 . ASP A 1 438 ? 47.455 -32.153 -24.729 1.00 31.94 ? 438 ASP A OD2 1 ATOM 3355 N N . LEU A 1 439 ? 42.355 -31.659 -22.806 1.00 23.35 ? 439 LEU A N 1 ATOM 3356 C CA . LEU A 1 439 ? 41.312 -30.806 -22.250 1.00 23.87 ? 439 LEU A CA 1 ATOM 3357 C C . LEU A 1 439 ? 40.387 -31.592 -21.292 1.00 23.77 ? 439 LEU A C 1 ATOM 3358 O O . LEU A 1 439 ? 39.944 -31.042 -20.303 1.00 23.01 ? 439 LEU A O 1 ATOM 3359 C CB . LEU A 1 439 ? 40.471 -30.124 -23.343 1.00 24.61 ? 439 LEU A CB 1 ATOM 3360 C CG . LEU A 1 439 ? 39.298 -30.826 -24.071 1.00 24.98 ? 439 LEU A CG 1 ATOM 3361 C CD1 . LEU A 1 439 ? 37.980 -30.720 -23.281 1.00 24.62 ? 439 LEU A CD1 1 ATOM 3362 C CD2 . LEU A 1 439 ? 39.105 -30.236 -25.472 1.00 25.43 ? 439 LEU A CD2 1 ATOM 3363 N N . THR A 1 440 ? 40.144 -32.869 -21.574 1.00 22.85 ? 440 THR A N 1 ATOM 3364 C CA . THR A 1 440 ? 39.280 -33.663 -20.690 1.00 24.02 ? 440 THR A CA 1 ATOM 3365 C C . THR A 1 440 ? 40.044 -34.075 -19.439 1.00 25.21 ? 440 THR A C 1 ATOM 3366 O O . THR A 1 440 ? 39.482 -34.023 -18.329 1.00 28.09 ? 440 THR A O 1 ATOM 3367 C CB . THR A 1 440 ? 38.623 -34.873 -21.389 1.00 23.25 ? 440 THR A CB 1 ATOM 3368 O OG1 . THR A 1 440 ? 39.602 -35.682 -22.032 1.00 22.48 ? 440 THR A OG1 1 ATOM 3369 C CG2 . THR A 1 440 ? 37.579 -34.451 -22.378 1.00 23.46 ? 440 THR A CG2 1 ATOM 3370 N N . ASP A 1 441 ? 41.316 -34.465 -19.586 1.00 25.35 ? 441 ASP A N 1 ATOM 3371 C CA . ASP A 1 441 ? 42.185 -34.687 -18.430 1.00 26.80 ? 441 ASP A CA 1 ATOM 3372 C C . ASP A 1 441 ? 42.257 -33.383 -17.601 1.00 28.27 ? 441 ASP A C 1 ATOM 3373 O O . ASP A 1 441 ? 42.236 -33.417 -16.349 1.00 27.79 ? 441 ASP A O 1 ATOM 3374 C CB . ASP A 1 441 ? 43.606 -35.084 -18.821 1.00 27.86 ? 441 ASP A CB 1 ATOM 3375 C CG . ASP A 1 441 ? 43.741 -36.524 -19.311 1.00 29.72 ? 441 ASP A CG 1 ATOM 3376 O OD1 . ASP A 1 441 ? 42.798 -37.328 -19.218 1.00 29.57 ? 441 ASP A OD1 1 ATOM 3377 O OD2 . ASP A 1 441 ? 44.851 -36.867 -19.800 1.00 31.00 ? 441 ASP A OD2 1 ATOM 3378 N N . SER A 1 442 ? 42.376 -32.244 -18.284 1.00 27.72 ? 442 SER A N 1 ATOM 3379 C CA . SER A 1 442 ? 42.509 -30.971 -17.560 1.00 29.26 ? 442 SER A CA 1 ATOM 3380 C C . SER A 1 442 ? 41.269 -30.643 -16.704 1.00 28.16 ? 442 SER A C 1 ATOM 3381 O O . SER A 1 442 ? 41.423 -30.209 -15.564 1.00 29.78 ? 442 SER A O 1 ATOM 3382 C CB . SER A 1 442 ? 42.817 -29.808 -18.508 1.00 30.05 ? 442 SER A CB 1 ATOM 3383 O OG . SER A 1 442 ? 42.938 -28.612 -17.747 1.00 32.25 ? 442 SER A OG 1 ATOM 3384 N N . GLU A 1 443 ? 40.065 -30.824 -17.230 1.00 27.66 ? 443 GLU A N 1 ATOM 3385 C CA . GLU A 1 443 ? 38.848 -30.605 -16.408 1.00 29.01 ? 443 GLU A CA 1 ATOM 3386 C C . GLU A 1 443 ? 38.853 -31.449 -15.140 1.00 28.43 ? 443 GLU A C 1 ATOM 3387 O O . GLU A 1 443 ? 38.452 -30.965 -14.089 1.00 29.76 ? 443 GLU A O 1 ATOM 3388 C CB . GLU A 1 443 ? 37.546 -30.824 -17.188 1.00 29.57 ? 443 GLU A CB 1 ATOM 3389 C CG . GLU A 1 443 ? 37.249 -29.804 -18.277 1.00 31.43 ? 443 GLU A CG 1 ATOM 3390 C CD . GLU A 1 443 ? 37.301 -28.348 -17.799 1.00 33.53 ? 443 GLU A CD 1 ATOM 3391 O OE1 . GLU A 1 443 ? 36.808 -28.036 -16.691 1.00 35.12 ? 443 GLU A OE1 1 ATOM 3392 O OE2 . GLU A 1 443 ? 37.836 -27.507 -18.541 1.00 34.90 ? 443 GLU A OE2 1 ATOM 3393 N N . MET A 1 444 ? 39.346 -32.680 -15.217 1.00 28.81 ? 444 MET A N 1 ATOM 3394 C CA . MET A 1 444 ? 39.435 -33.547 -14.035 1.00 28.79 ? 444 MET A CA 1 ATOM 3395 C C . MET A 1 444 ? 40.415 -32.967 -13.031 1.00 30.32 ? 444 MET A C 1 ATOM 3396 O O . MET A 1 444 ? 40.124 -32.908 -11.828 1.00 28.24 ? 444 MET A O 1 ATOM 3397 C CB . MET A 1 444 ? 39.873 -34.971 -14.406 1.00 28.48 ? 444 MET A CB 1 ATOM 3398 C CG . MET A 1 444 ? 39.926 -35.949 -13.236 1.00 28.54 ? 444 MET A CG 1 ATOM 3399 S SD . MET A 1 444 ? 38.263 -36.511 -12.745 1.00 27.82 ? 444 MET A SD 1 ATOM 3400 C CE . MET A 1 444 ? 37.844 -35.217 -11.570 1.00 29.98 ? 444 MET A CE 1 ATOM 3401 N N . ASN A 1 445 ? 41.582 -32.554 -13.522 1.00 30.30 ? 445 ASN A N 1 ATOM 3402 C CA . ASN A 1 445 ? 42.626 -32.023 -12.647 1.00 32.47 ? 445 ASN A CA 1 ATOM 3403 C C . ASN A 1 445 ? 42.223 -30.710 -11.993 1.00 30.67 ? 445 ASN A C 1 ATOM 3404 O O . ASN A 1 445 ? 42.502 -30.519 -10.818 1.00 31.57 ? 445 ASN A O 1 ATOM 3405 C CB . ASN A 1 445 ? 43.964 -31.864 -13.400 1.00 35.55 ? 445 ASN A CB 1 ATOM 3406 C CG . ASN A 1 445 ? 44.566 -33.199 -13.808 1.00 38.72 ? 445 ASN A CG 1 ATOM 3407 O OD1 . ASN A 1 445 ? 44.520 -34.169 -13.053 1.00 39.70 ? 445 ASN A OD1 1 ATOM 3408 N ND2 . ASN A 1 445 ? 45.161 -33.247 -15.006 1.00 41.89 ? 445 ASN A ND2 1 ATOM 3409 N N . LYS A 1 446 ? 41.541 -29.844 -12.732 1.00 30.13 ? 446 LYS A N 1 ATOM 3410 C CA . LYS A 1 446 ? 41.088 -28.559 -12.208 1.00 32.74 ? 446 LYS A CA 1 ATOM 3411 C C . LYS A 1 446 ? 40.032 -28.774 -11.104 1.00 33.38 ? 446 LYS A C 1 ATOM 3412 O O . LYS A 1 446 ? 40.054 -28.092 -10.084 1.00 33.86 ? 446 LYS A O 1 ATOM 3413 C CB . LYS A 1 446 ? 40.522 -27.669 -13.320 1.00 34.45 ? 446 LYS A CB 1 ATOM 3414 C CG . LYS A 1 446 ? 41.591 -27.175 -14.310 1.00 35.47 ? 446 LYS A CG 1 ATOM 3415 C CD . LYS A 1 446 ? 41.067 -26.127 -15.295 1.00 37.76 ? 446 LYS A CD 1 ATOM 3416 C CE . LYS A 1 446 ? 40.064 -26.682 -16.282 1.00 38.94 ? 446 LYS A CE 1 ATOM 3417 N NZ . LYS A 1 446 ? 39.476 -25.615 -17.156 1.00 39.72 ? 446 LYS A NZ 1 ATOM 3418 N N . LEU A 1 447 ? 39.146 -29.745 -11.302 1.00 32.26 ? 447 LEU A N 1 ATOM 3419 C CA . LEU A 1 447 ? 38.106 -30.047 -10.319 1.00 32.60 ? 447 LEU A CA 1 ATOM 3420 C C . LEU A 1 447 ? 38.775 -30.468 -9.024 1.00 31.96 ? 447 LEU A C 1 ATOM 3421 O O . LEU A 1 447 ? 38.427 -29.978 -7.941 1.00 33.45 ? 447 LEU A O 1 ATOM 3422 C CB . LEU A 1 447 ? 37.188 -31.147 -10.851 1.00 32.90 ? 447 LEU A CB 1 ATOM 3423 C CG . LEU A 1 447 ? 35.994 -31.579 -9.976 1.00 34.45 ? 447 LEU A CG 1 ATOM 3424 C CD1 . LEU A 1 447 ? 35.126 -30.377 -9.611 1.00 34.57 ? 447 LEU A CD1 1 ATOM 3425 C CD2 . LEU A 1 447 ? 35.187 -32.667 -10.660 1.00 33.81 ? 447 LEU A CD2 1 ATOM 3426 N N . PHE A 1 448 ? 39.761 -31.354 -9.135 1.00 30.46 ? 448 PHE A N 1 ATOM 3427 C CA . PHE A 1 448 ? 40.505 -31.831 -7.978 1.00 30.60 ? 448 PHE A CA 1 ATOM 3428 C C . PHE A 1 448 ? 41.233 -30.696 -7.273 1.00 31.27 ? 448 PHE A C 1 ATOM 3429 O O . PHE A 1 448 ? 41.192 -30.597 -6.038 1.00 28.35 ? 448 PHE A O 1 ATOM 3430 C CB . PHE A 1 448 ? 41.482 -32.934 -8.387 1.00 30.20 ? 448 PHE A CB 1 ATOM 3431 C CG . PHE A 1 448 ? 42.218 -33.546 -7.243 1.00 30.23 ? 448 PHE A CG 1 ATOM 3432 C CD1 . PHE A 1 448 ? 41.662 -34.578 -6.512 1.00 29.99 ? 448 PHE A CD1 1 ATOM 3433 C CD2 . PHE A 1 448 ? 43.481 -33.088 -6.894 1.00 30.97 ? 448 PHE A CD2 1 ATOM 3434 C CE1 . PHE A 1 448 ? 42.342 -35.143 -5.442 1.00 30.93 ? 448 PHE A CE1 1 ATOM 3435 C CE2 . PHE A 1 448 ? 44.170 -33.646 -5.832 1.00 30.47 ? 448 PHE A CE2 1 ATOM 3436 C CZ . PHE A 1 448 ? 43.608 -34.680 -5.109 1.00 31.16 ? 448 PHE A CZ 1 ATOM 3437 N N . GLU A 1 449 ? 41.915 -29.849 -8.045 1.00 32.80 ? 449 GLU A N 1 ATOM 3438 C CA . GLU A 1 449 ? 42.596 -28.694 -7.448 1.00 36.83 ? 449 GLU A CA 1 ATOM 3439 C C . GLU A 1 449 ? 41.674 -27.715 -6.759 1.00 34.81 ? 449 GLU A C 1 ATOM 3440 O O . GLU A 1 449 ? 41.998 -27.270 -5.673 1.00 35.31 ? 449 GLU A O 1 ATOM 3441 C CB . GLU A 1 449 ? 43.442 -27.944 -8.487 1.00 42.30 ? 449 GLU A CB 1 ATOM 3442 C CG . GLU A 1 449 ? 44.702 -28.697 -8.856 1.00 47.35 ? 449 GLU A CG 1 ATOM 3443 C CD . GLU A 1 449 ? 45.587 -28.975 -7.647 1.00 51.47 ? 449 GLU A CD 1 ATOM 3444 O OE1 . GLU A 1 449 ? 45.849 -28.022 -6.867 1.00 55.41 ? 449 GLU A OE1 1 ATOM 3445 O OE2 . GLU A 1 449 ? 46.005 -30.150 -7.472 1.00 53.34 ? 449 GLU A OE2 1 ATOM 3446 N N . ARG A 1 450 ? 40.554 -27.362 -7.388 1.00 35.83 ? 450 ARG A N 1 ATOM 3447 C CA . ARG A 1 450 ? 39.552 -26.482 -6.780 1.00 38.01 ? 450 ARG A CA 1 ATOM 3448 C C . ARG A 1 450 ? 39.081 -27.028 -5.423 1.00 35.71 ? 450 ARG A C 1 ATOM 3449 O O . ARG A 1 450 ? 38.868 -26.285 -4.468 1.00 35.52 ? 450 ARG A O 1 ATOM 3450 C CB . ARG A 1 450 ? 38.309 -26.341 -7.673 1.00 41.48 ? 450 ARG A CB 1 ATOM 3451 C CG . ARG A 1 450 ? 38.504 -25.589 -8.979 1.00 47.19 ? 450 ARG A CG 1 ATOM 3452 C CD . ARG A 1 450 ? 37.209 -24.987 -9.529 1.00 50.49 ? 450 ARG A CD 1 ATOM 3453 N NE . ARG A 1 450 ? 36.173 -25.948 -9.951 1.00 52.77 ? 450 ARG A NE 1 ATOM 3454 C CZ . ARG A 1 450 ? 36.153 -26.616 -11.116 1.00 54.85 ? 450 ARG A CZ 1 ATOM 3455 N NH1 . ARG A 1 450 ? 37.137 -26.491 -11.996 1.00 52.91 ? 450 ARG A NH1 1 ATOM 3456 N NH2 . ARG A 1 450 ? 35.139 -27.441 -11.397 1.00 56.11 ? 450 ARG A NH2 1 ATOM 3457 N N . THR A 1 451 ? 38.886 -28.335 -5.353 1.00 32.37 ? 451 THR A N 1 ATOM 3458 C CA . THR A 1 451 ? 38.388 -28.974 -4.141 1.00 29.97 ? 451 THR A CA 1 ATOM 3459 C C . THR A 1 451 ? 39.443 -28.922 -3.052 1.00 29.83 ? 451 THR A C 1 ATOM 3460 O O . THR A 1 451 ? 39.157 -28.537 -1.930 1.00 30.45 ? 451 THR A O 1 ATOM 3461 C CB . THR A 1 451 ? 37.989 -30.429 -4.453 1.00 28.93 ? 451 THR A CB 1 ATOM 3462 O OG1 . THR A 1 451 ? 36.977 -30.421 -5.464 1.00 28.66 ? 451 THR A OG1 1 ATOM 3463 C CG2 . THR A 1 451 ? 37.462 -31.127 -3.222 1.00 26.13 ? 451 THR A CG2 1 ATOM 3464 N N . LYS A 1 452 ? 40.675 -29.263 -3.413 1.00 31.18 ? 452 LYS A N 1 ATOM 3465 C CA . LYS A 1 452 ? 41.807 -29.219 -2.509 1.00 33.60 ? 452 LYS A CA 1 ATOM 3466 C C . LYS A 1 452 ? 41.933 -27.834 -1.879 1.00 35.06 ? 452 LYS A C 1 ATOM 3467 O O . LYS A 1 452 ? 42.184 -27.703 -0.658 1.00 32.57 ? 452 LYS A O 1 ATOM 3468 C CB . LYS A 1 452 ? 43.096 -29.554 -3.259 1.00 37.15 ? 452 LYS A CB 1 ATOM 3469 C CG . LYS A 1 452 ? 44.345 -29.532 -2.396 1.00 40.49 ? 452 LYS A CG 1 ATOM 3470 C CD . LYS A 1 452 ? 45.584 -29.877 -3.200 1.00 45.25 ? 452 LYS A CD 1 ATOM 3471 C CE . LYS A 1 452 ? 46.772 -30.087 -2.268 1.00 48.74 ? 452 LYS A CE 1 ATOM 3472 N NZ . LYS A 1 452 ? 46.485 -31.193 -1.293 1.00 50.05 ? 452 LYS A NZ 1 ATOM 3473 N N . LYS A 1 453 ? 41.742 -26.810 -2.703 1.00 35.77 ? 453 LYS A N 1 ATOM 3474 C CA . LYS A 1 453 ? 41.910 -25.443 -2.222 1.00 38.11 ? 453 LYS A CA 1 ATOM 3475 C C . LYS A 1 453 ? 40.796 -25.068 -1.248 1.00 35.16 ? 453 LYS A C 1 ATOM 3476 O O . LYS A 1 453 ? 41.064 -24.365 -0.284 1.00 35.26 ? 453 LYS A O 1 ATOM 3477 C CB . LYS A 1 453 ? 41.987 -24.435 -3.372 1.00 40.87 ? 453 LYS A CB 1 ATOM 3478 C CG . LYS A 1 453 ? 43.091 -24.652 -4.399 1.00 43.75 ? 453 LYS A CG 1 ATOM 3479 C CD . LYS A 1 453 ? 44.497 -24.785 -3.816 1.00 45.58 ? 453 LYS A CD 1 ATOM 3480 C CE . LYS A 1 453 ? 45.548 -24.994 -4.910 1.00 48.09 ? 453 LYS A CE 1 ATOM 3481 N NZ . LYS A 1 453 ? 46.036 -23.769 -5.613 1.00 47.29 ? 453 LYS A NZ 1 ATOM 3482 N N . GLN A 1 454 ? 39.563 -25.545 -1.464 1.00 33.85 ? 454 GLN A N 1 ATOM 3483 C CA . GLN A 1 454 ? 38.473 -25.238 -0.536 1.00 33.61 ? 454 GLN A CA 1 ATOM 3484 C C . GLN A 1 454 ? 38.757 -25.829 0.845 1.00 30.72 ? 454 GLN A C 1 ATOM 3485 O O . GLN A 1 454 ? 38.401 -25.233 1.869 1.00 30.37 ? 454 GLN A O 1 ATOM 3486 C CB . GLN A 1 454 ? 37.131 -25.814 -0.992 1.00 34.09 ? 454 GLN A CB 1 ATOM 3487 C CG . GLN A 1 454 ? 36.417 -25.090 -2.103 1.00 38.39 ? 454 GLN A CG 1 ATOM 3488 C CD . GLN A 1 454 ? 35.069 -25.717 -2.387 1.00 39.25 ? 454 GLN A CD 1 ATOM 3489 O OE1 . GLN A 1 454 ? 34.083 -25.408 -1.732 1.00 39.45 ? 454 GLN A OE1 1 ATOM 3490 N NE2 . GLN A 1 454 ? 35.026 -26.605 -3.360 1.00 38.48 ? 454 GLN A NE2 1 ATOM 3491 N N . LEU A 1 455 ? 39.320 -27.035 0.852 1.00 28.07 ? 455 LEU A N 1 ATOM 3492 C CA . LEU A 1 455 ? 39.470 -27.831 2.066 1.00 27.31 ? 455 LEU A CA 1 ATOM 3493 C C . LEU A 1 455 ? 40.570 -27.316 2.970 1.00 27.21 ? 455 LEU A C 1 ATOM 3494 O O . LEU A 1 455 ? 40.525 -27.534 4.159 1.00 25.64 ? 455 LEU A O 1 ATOM 3495 C CB . LEU A 1 455 ? 39.694 -29.317 1.707 1.00 26.88 ? 455 LEU A CB 1 ATOM 3496 C CG . LEU A 1 455 ? 38.477 -29.973 1.063 1.00 25.40 ? 455 LEU A CG 1 ATOM 3497 C CD1 . LEU A 1 455 ? 38.793 -31.378 0.569 1.00 26.19 ? 455 LEU A CD1 1 ATOM 3498 C CD2 . LEU A 1 455 ? 37.294 -30.003 2.037 1.00 25.98 ? 455 LEU A CD2 1 ATOM 3499 N N . ARG A 1 456 ? 41.555 -26.620 2.404 1.00 28.76 ? 456 ARG A N 1 ATOM 3500 C CA . ARG A 1 456 ? 42.615 -25.987 3.186 1.00 30.81 ? 456 ARG A CA 1 ATOM 3501 C C . ARG A 1 456 ? 43.286 -27.022 4.078 1.00 30.29 ? 456 ARG A C 1 ATOM 3502 O O . ARG A 1 456 ? 43.684 -28.065 3.593 1.00 29.30 ? 456 ARG A O 1 ATOM 3503 C CB . ARG A 1 456 ? 42.082 -24.794 3.985 1.00 32.99 ? 456 ARG A CB 1 ATOM 3504 C CG . ARG A 1 456 ? 41.728 -23.587 3.150 1.00 35.14 ? 456 ARG A CG 1 ATOM 3505 C CD . ARG A 1 456 ? 42.973 -22.778 2.792 1.00 36.65 ? 456 ARG A CD 1 ATOM 3506 N NE . ARG A 1 456 ? 43.598 -22.088 3.930 1.00 37.72 ? 456 ARG A NE 1 ATOM 3507 C CZ . ARG A 1 456 ? 43.378 -20.824 4.299 1.00 37.63 ? 456 ARG A CZ 1 ATOM 3508 N NH1 . ARG A 1 456 ? 42.495 -20.049 3.669 1.00 39.06 ? 456 ARG A NH1 1 ATOM 3509 N NH2 . ARG A 1 456 ? 44.038 -20.326 5.326 1.00 39.38 ? 456 ARG A NH2 1 ATOM 3510 N N . GLU A 1 457 ? 43.363 -26.775 5.376 1.00 31.50 ? 457 GLU A N 1 ATOM 3511 C CA . GLU A 1 457 ? 44.033 -27.699 6.277 1.00 32.47 ? 457 GLU A CA 1 ATOM 3512 C C . GLU A 1 457 ? 43.077 -28.731 6.873 1.00 30.01 ? 457 GLU A C 1 ATOM 3513 O O . GLU A 1 457 ? 43.441 -29.422 7.825 1.00 30.22 ? 457 GLU A O 1 ATOM 3514 C CB . GLU A 1 457 ? 44.695 -26.911 7.396 1.00 34.96 ? 457 GLU A CB 1 ATOM 3515 C CG . GLU A 1 457 ? 45.693 -25.889 6.893 1.00 39.29 ? 457 GLU A CG 1 ATOM 3516 C CD . GLU A 1 457 ? 46.795 -26.522 6.075 1.00 41.75 ? 457 GLU A CD 1 ATOM 3517 O OE1 . GLU A 1 457 ? 47.231 -27.629 6.442 1.00 46.35 ? 457 GLU A OE1 1 ATOM 3518 O OE2 . GLU A 1 457 ? 47.235 -25.928 5.069 1.00 45.28 ? 457 GLU A OE2 1 ATOM 3519 N N . ASN A 1 458 ? 41.858 -28.838 6.338 1.00 27.45 ? 458 ASN A N 1 ATOM 3520 C CA . ASN A 1 458 ? 40.855 -29.727 6.945 1.00 27.11 ? 458 ASN A CA 1 ATOM 3521 C C . ASN A 1 458 ? 40.859 -31.127 6.351 1.00 25.05 ? 458 ASN A C 1 ATOM 3522 O O . ASN A 1 458 ? 40.095 -31.981 6.791 1.00 24.95 ? 458 ASN A O 1 ATOM 3523 C CB . ASN A 1 458 ? 39.449 -29.132 6.833 1.00 26.64 ? 458 ASN A CB 1 ATOM 3524 C CG . ASN A 1 458 ? 39.310 -27.813 7.577 1.00 27.91 ? 458 ASN A CG 1 ATOM 3525 O OD1 . ASN A 1 458 ? 40.226 -27.398 8.292 1.00 28.30 ? 458 ASN A OD1 1 ATOM 3526 N ND2 . ASN A 1 458 ? 38.151 -27.156 7.427 1.00 28.31 ? 458 ASN A ND2 1 ATOM 3527 N N . ALA A 1 459 ? 41.696 -31.341 5.352 1.00 24.56 ? 459 ALA A N 1 ATOM 3528 C CA . ALA A 1 459 ? 41.752 -32.599 4.617 1.00 24.64 ? 459 ALA A CA 1 ATOM 3529 C C . ALA A 1 459 ? 43.150 -32.928 4.170 1.00 26.22 ? 459 ALA A C 1 ATOM 3530 O O . ALA A 1 459 ? 43.984 -32.030 4.002 1.00 27.89 ? 459 ALA A O 1 ATOM 3531 C CB . ALA A 1 459 ? 40.841 -32.540 3.393 1.00 23.89 ? 459 ALA A CB 1 ATOM 3532 N N . GLU A 1 460 ? 43.401 -34.216 3.947 1.00 26.36 ? 460 GLU A N 1 ATOM 3533 C CA . GLU A 1 460 ? 44.627 -34.679 3.309 1.00 27.92 ? 460 GLU A CA 1 ATOM 3534 C C . GLU A 1 460 ? 44.333 -35.491 2.045 1.00 28.52 ? 460 GLU A C 1 ATOM 3535 O O . GLU A 1 460 ? 43.336 -36.216 1.955 1.00 27.25 ? 460 GLU A O 1 ATOM 3536 C CB . GLU A 1 460 ? 45.467 -35.502 4.288 1.00 28.64 ? 460 GLU A CB 1 ATOM 3537 C CG . GLU A 1 460 ? 46.028 -34.664 5.429 1.00 29.17 ? 460 GLU A CG 1 ATOM 3538 C CD . GLU A 1 460 ? 46.760 -35.465 6.493 1.00 30.24 ? 460 GLU A CD 1 ATOM 3539 O OE1 . GLU A 1 460 ? 47.187 -36.618 6.232 1.00 31.47 ? 460 GLU A OE1 1 ATOM 3540 O OE2 . GLU A 1 460 ? 46.917 -34.923 7.603 1.00 30.10 ? 460 GLU A OE2 1 ATOM 3541 N N . ASP A 1 461 ? 45.225 -35.356 1.075 1.00 28.59 ? 461 ASP A N 1 ATOM 3542 C CA . ASP A 1 461 ? 45.161 -36.074 -0.178 1.00 30.62 ? 461 ASP A CA 1 ATOM 3543 C C . ASP A 1 461 ? 45.612 -37.538 0.021 1.00 32.09 ? 461 ASP A C 1 ATOM 3544 O O . ASP A 1 461 ? 46.748 -37.785 0.409 1.00 32.11 ? 461 ASP A O 1 ATOM 3545 C CB . ASP A 1 461 ? 46.099 -35.355 -1.152 1.00 32.29 ? 461 ASP A CB 1 ATOM 3546 C CG . ASP A 1 461 ? 46.061 -35.915 -2.561 1.00 33.59 ? 461 ASP A CG 1 ATOM 3547 O OD1 . ASP A 1 461 ? 45.615 -37.059 -2.795 1.00 33.78 ? 461 ASP A OD1 1 ATOM 3548 O OD2 . ASP A 1 461 ? 46.535 -35.178 -3.452 1.00 36.08 ? 461 ASP A OD2 1 ATOM 3549 N N . MET A 1 462 ? 44.731 -38.494 -0.255 1.00 31.35 ? 462 MET A N 1 ATOM 3550 C CA . MET A 1 462 ? 45.043 -39.923 -0.034 1.00 33.85 ? 462 MET A CA 1 ATOM 3551 C C . MET A 1 462 ? 45.794 -40.567 -1.212 1.00 35.39 ? 462 MET A C 1 ATOM 3552 O O . MET A 1 462 ? 46.141 -41.752 -1.162 1.00 37.38 ? 462 MET A O 1 ATOM 3553 C CB . MET A 1 462 ? 43.750 -40.708 0.232 1.00 34.19 ? 462 MET A CB 1 ATOM 3554 C CG . MET A 1 462 ? 42.991 -40.301 1.487 1.00 36.10 ? 462 MET A CG 1 ATOM 3555 S SD . MET A 1 462 ? 41.274 -40.888 1.519 1.00 38.68 ? 462 MET A SD 1 ATOM 3556 C CE . MET A 1 462 ? 41.506 -42.613 1.100 1.00 40.20 ? 462 MET A CE 1 ATOM 3557 N N . GLY A 1 463 ? 46.013 -39.811 -2.286 1.00 34.52 ? 463 GLY A N 1 ATOM 3558 C CA . GLY A 1 463 ? 46.826 -40.284 -3.405 1.00 35.58 ? 463 GLY A CA 1 ATOM 3559 C C . GLY A 1 463 ? 46.086 -41.075 -4.470 1.00 36.41 ? 463 GLY A C 1 ATOM 3560 O O . GLY A 1 463 ? 46.688 -41.462 -5.472 1.00 37.21 ? 463 GLY A O 1 ATOM 3561 N N . ASN A 1 464 ? 44.787 -41.295 -4.269 1.00 34.13 ? 464 ASN A N 1 ATOM 3562 C CA . ASN A 1 464 ? 43.941 -42.034 -5.209 1.00 35.36 ? 464 ASN A CA 1 ATOM 3563 C C . ASN A 1 464 ? 42.830 -41.168 -5.834 1.00 33.01 ? 464 ASN A C 1 ATOM 3564 O O . ASN A 1 464 ? 41.825 -41.692 -6.305 1.00 34.48 ? 464 ASN A O 1 ATOM 3565 C CB . ASN A 1 464 ? 43.302 -43.236 -4.496 1.00 36.56 ? 464 ASN A CB 1 ATOM 3566 C CG . ASN A 1 464 ? 42.416 -42.819 -3.335 1.00 36.74 ? 464 ASN A CG 1 ATOM 3567 O OD1 . ASN A 1 464 ? 42.491 -41.679 -2.853 1.00 34.31 ? 464 ASN A OD1 1 ATOM 3568 N ND2 . ASN A 1 464 ? 41.566 -43.730 -2.885 1.00 38.39 ? 464 ASN A ND2 1 ATOM 3569 N N . GLY A 1 465 ? 43.009 -39.855 -5.823 1.00 30.60 ? 465 GLY A N 1 ATOM 3570 C CA . GLY A 1 465 ? 41.960 -38.926 -6.235 1.00 29.57 ? 465 GLY A CA 1 ATOM 3571 C C . GLY A 1 465 ? 40.908 -38.642 -5.179 1.00 28.30 ? 465 GLY A C 1 ATOM 3572 O O . GLY A 1 465 ? 39.854 -38.089 -5.510 1.00 28.71 ? 465 GLY A O 1 ATOM 3573 N N . CYS A 1 466 ? 41.194 -38.998 -3.923 1.00 27.87 ? 466 CYS A N 1 ATOM 3574 C CA . CYS A 1 466 ? 40.298 -38.744 -2.802 1.00 28.09 ? 466 CYS A CA 1 ATOM 3575 C C . CYS A 1 466 ? 40.981 -37.952 -1.709 1.00 27.52 ? 466 CYS A C 1 ATOM 3576 O O . CYS A 1 466 ? 42.210 -38.008 -1.534 1.00 27.76 ? 466 CYS A O 1 ATOM 3577 C CB . CYS A 1 466 ? 39.750 -40.041 -2.177 1.00 31.78 ? 466 CYS A CB 1 ATOM 3578 S SG . CYS A 1 466 ? 39.064 -41.278 -3.312 1.00 36.71 ? 466 CYS A SG 1 ATOM 3579 N N . PHE A 1 467 ? 40.151 -37.223 -0.976 1.00 25.89 ? 467 PHE A N 1 ATOM 3580 C CA . PHE A 1 467 ? 40.524 -36.546 0.230 1.00 25.65 ? 467 PHE A CA 1 ATOM 3581 C C . PHE A 1 467 ? 39.975 -37.250 1.467 1.00 25.88 ? 467 PHE A C 1 ATOM 3582 O O . PHE A 1 467 ? 38.834 -37.709 1.482 1.00 25.78 ? 467 PHE A O 1 ATOM 3583 C CB . PHE A 1 467 ? 39.986 -35.135 0.221 1.00 24.86 ? 467 PHE A CB 1 ATOM 3584 C CG . PHE A 1 467 ? 40.501 -34.310 -0.909 1.00 25.44 ? 467 PHE A CG 1 ATOM 3585 C CD1 . PHE A 1 467 ? 41.727 -33.696 -0.816 1.00 26.92 ? 467 PHE A CD1 1 ATOM 3586 C CD2 . PHE A 1 467 ? 39.756 -34.143 -2.045 1.00 25.69 ? 467 PHE A CD2 1 ATOM 3587 C CE1 . PHE A 1 467 ? 42.222 -32.932 -1.866 1.00 27.54 ? 467 PHE A CE1 1 ATOM 3588 C CE2 . PHE A 1 467 ? 40.236 -33.388 -3.099 1.00 27.33 ? 467 PHE A CE2 1 ATOM 3589 C CZ . PHE A 1 467 ? 41.469 -32.778 -3.011 1.00 27.18 ? 467 PHE A CZ 1 ATOM 3590 N N . LYS A 1 468 ? 40.799 -37.310 2.497 1.00 26.49 ? 468 LYS A N 1 ATOM 3591 C CA . LYS A 1 468 ? 40.334 -37.676 3.818 1.00 27.48 ? 468 LYS A CA 1 ATOM 3592 C C . LYS A 1 468 ? 40.029 -36.379 4.534 1.00 26.53 ? 468 LYS A C 1 ATOM 3593 O O . LYS A 1 468 ? 40.935 -35.579 4.800 1.00 26.21 ? 468 LYS A O 1 ATOM 3594 C CB . LYS A 1 468 ? 41.382 -38.471 4.582 1.00 30.19 ? 468 LYS A CB 1 ATOM 3595 C CG . LYS A 1 468 ? 40.919 -38.914 5.961 1.00 32.30 ? 468 LYS A CG 1 ATOM 3596 C CD . LYS A 1 468 ? 41.990 -39.764 6.627 1.00 36.92 ? 468 LYS A CD 1 ATOM 3597 C CE . LYS A 1 468 ? 41.642 -40.115 8.069 1.00 39.24 ? 468 LYS A CE 1 ATOM 3598 N NZ . LYS A 1 468 ? 42.741 -40.915 8.689 1.00 42.70 ? 468 LYS A NZ 1 ATOM 3599 N N . ILE A 1 469 ? 38.750 -36.177 4.841 1.00 26.00 ? 469 ILE A N 1 ATOM 3600 C CA . ILE A 1 469 ? 38.296 -34.982 5.528 1.00 25.41 ? 469 ILE A CA 1 ATOM 3601 C C . ILE A 1 469 ? 38.272 -35.295 7.022 1.00 26.38 ? 469 ILE A C 1 ATOM 3602 O O . ILE A 1 469 ? 37.585 -36.214 7.466 1.00 26.69 ? 469 ILE A O 1 ATOM 3603 C CB . ILE A 1 469 ? 36.918 -34.528 5.008 1.00 25.52 ? 469 ILE A CB 1 ATOM 3604 C CG1 . ILE A 1 469 ? 37.009 -34.194 3.508 1.00 24.53 ? 469 ILE A CG1 1 ATOM 3605 C CG2 . ILE A 1 469 ? 36.415 -33.326 5.789 1.00 24.93 ? 469 ILE A CG2 1 ATOM 3606 C CD1 . ILE A 1 469 ? 35.666 -33.962 2.842 1.00 25.68 ? 469 ILE A CD1 1 ATOM 3607 N N . TYR A 1 470 ? 39.025 -34.532 7.806 1.00 27.38 ? 470 TYR A N 1 ATOM 3608 C CA . TYR A 1 470 ? 39.257 -34.883 9.216 1.00 28.96 ? 470 TYR A CA 1 ATOM 3609 C C . TYR A 1 470 ? 38.221 -34.284 10.176 1.00 29.06 ? 470 TYR A C 1 ATOM 3610 O O . TYR A 1 470 ? 38.535 -33.937 11.311 1.00 30.05 ? 470 TYR A O 1 ATOM 3611 C CB . TYR A 1 470 ? 40.676 -34.482 9.625 1.00 29.95 ? 470 TYR A CB 1 ATOM 3612 C CG . TYR A 1 470 ? 41.744 -35.422 9.137 1.00 30.81 ? 470 TYR A CG 1 ATOM 3613 C CD1 . TYR A 1 470 ? 42.287 -35.290 7.860 1.00 30.30 ? 470 TYR A CD1 1 ATOM 3614 C CD2 . TYR A 1 470 ? 42.240 -36.423 9.958 1.00 32.30 ? 470 TYR A CD2 1 ATOM 3615 C CE1 . TYR A 1 470 ? 43.281 -36.144 7.417 1.00 31.74 ? 470 TYR A CE1 1 ATOM 3616 C CE2 . TYR A 1 470 ? 43.240 -37.287 9.519 1.00 34.25 ? 470 TYR A CE2 1 ATOM 3617 C CZ . TYR A 1 470 ? 43.755 -37.142 8.249 1.00 32.64 ? 470 TYR A CZ 1 ATOM 3618 O OH . TYR A 1 470 ? 44.746 -37.974 7.818 1.00 35.26 ? 470 TYR A OH 1 ATOM 3619 N N . HIS A 1 471 ? 36.984 -34.168 9.712 1.00 28.83 ? 471 HIS A N 1 ATOM 3620 C CA . HIS A 1 471 ? 35.881 -33.771 10.566 1.00 29.66 ? 471 HIS A CA 1 ATOM 3621 C C . HIS A 1 471 ? 34.606 -34.422 10.129 1.00 30.13 ? 471 HIS A C 1 ATOM 3622 O O . HIS A 1 471 ? 34.480 -34.909 9.016 1.00 29.03 ? 471 HIS A O 1 ATOM 3623 C CB . HIS A 1 471 ? 35.732 -32.250 10.607 1.00 29.34 ? 471 HIS A CB 1 ATOM 3624 C CG . HIS A 1 471 ? 35.412 -31.621 9.278 1.00 28.08 ? 471 HIS A CG 1 ATOM 3625 N ND1 . HIS A 1 471 ? 34.150 -31.576 8.776 1.00 28.32 ? 471 HIS A ND1 1 ATOM 3626 C CD2 . HIS A 1 471 ? 36.223 -30.962 8.368 1.00 27.36 ? 471 HIS A CD2 1 ATOM 3627 C CE1 . HIS A 1 471 ? 34.177 -30.950 7.591 1.00 28.58 ? 471 HIS A CE1 1 ATOM 3628 N NE2 . HIS A 1 471 ? 35.447 -30.572 7.343 1.00 27.28 ? 471 HIS A NE2 1 ATOM 3629 N N . LYS A 1 472 ? 33.634 -34.442 11.019 1.00 31.90 ? 472 LYS A N 1 ATOM 3630 C CA . LYS A 1 472 ? 32.329 -34.944 10.672 1.00 34.29 ? 472 LYS A CA 1 ATOM 3631 C C . LYS A 1 472 ? 31.814 -34.085 9.534 1.00 32.95 ? 472 LYS A C 1 ATOM 3632 O O . LYS A 1 472 ? 31.776 -32.865 9.644 1.00 31.65 ? 472 LYS A O 1 ATOM 3633 C CB . LYS A 1 472 ? 31.390 -34.861 11.884 1.00 37.43 ? 472 LYS A CB 1 ATOM 3634 C CG . LYS A 1 472 ? 29.959 -35.239 11.556 1.00 41.23 ? 472 LYS A CG 1 ATOM 3635 C CD . LYS A 1 472 ? 29.052 -35.245 12.781 1.00 45.32 ? 472 LYS A CD 1 ATOM 3636 C CE . LYS A 1 472 ? 27.630 -35.604 12.375 1.00 47.88 ? 472 LYS A CE 1 ATOM 3637 N NZ . LYS A 1 472 ? 26.681 -35.563 13.523 1.00 53.28 ? 472 LYS A NZ 1 ATOM 3638 N N . CYS A 1 473 ? 31.422 -34.718 8.441 1.00 33.45 ? 473 CYS A N 1 ATOM 3639 C CA . CYS A 1 473 ? 31.056 -33.976 7.241 1.00 34.96 ? 473 CYS A CA 1 ATOM 3640 C C . CYS A 1 473 ? 29.787 -34.605 6.671 1.00 35.92 ? 473 CYS A C 1 ATOM 3641 O O . CYS A 1 473 ? 29.860 -35.508 5.849 1.00 37.55 ? 473 CYS A O 1 ATOM 3642 C CB . CYS A 1 473 ? 32.249 -33.978 6.250 1.00 36.10 ? 473 CYS A CB 1 ATOM 3643 S SG . CYS A 1 473 ? 32.064 -32.887 4.828 1.00 43.31 ? 473 CYS A SG 1 ATOM 3644 N N . ASP A 1 474 ? 28.633 -34.128 7.140 1.00 34.79 ? 474 ASP A N 1 ATOM 3645 C CA . ASP A 1 474 ? 27.331 -34.685 6.784 1.00 35.73 ? 474 ASP A CA 1 ATOM 3646 C C . ASP A 1 474 ? 26.916 -34.304 5.356 1.00 34.65 ? 474 ASP A C 1 ATOM 3647 O O . ASP A 1 474 ? 27.669 -33.666 4.625 1.00 32.43 ? 474 ASP A O 1 ATOM 3648 C CB . ASP A 1 474 ? 26.254 -34.280 7.824 1.00 37.27 ? 474 ASP A CB 1 ATOM 3649 C CG . ASP A 1 474 ? 25.938 -32.776 7.837 1.00 38.33 ? 474 ASP A CG 1 ATOM 3650 O OD1 . ASP A 1 474 ? 26.294 -32.010 6.910 1.00 35.72 ? 474 ASP A OD1 1 ATOM 3651 O OD2 . ASP A 1 474 ? 25.310 -32.344 8.823 1.00 39.97 ? 474 ASP A OD2 1 ATOM 3652 N N . ASN A 1 475 ? 25.727 -34.713 4.943 1.00 33.88 ? 475 ASN A N 1 ATOM 3653 C CA . ASN A 1 475 ? 25.335 -34.535 3.548 1.00 34.39 ? 475 ASN A CA 1 ATOM 3654 C C . ASN A 1 475 ? 25.327 -33.069 3.111 1.00 33.51 ? 475 ASN A C 1 ATOM 3655 O O . ASN A 1 475 ? 25.726 -32.748 1.995 1.00 32.96 ? 475 ASN A O 1 ATOM 3656 C CB . ASN A 1 475 ? 23.972 -35.179 3.290 1.00 36.50 ? 475 ASN A CB 1 ATOM 3657 C CG . ASN A 1 475 ? 24.052 -36.690 3.162 1.00 37.11 ? 475 ASN A CG 1 ATOM 3658 O OD1 . ASN A 1 475 ? 25.135 -37.271 3.139 1.00 36.67 ? 475 ASN A OD1 1 ATOM 3659 N ND2 . ASN A 1 475 ? 22.894 -37.334 3.066 1.00 38.69 ? 475 ASN A ND2 1 ATOM 3660 N N . ALA A 1 476 ? 24.878 -32.189 3.996 1.00 33.97 ? 476 ALA A N 1 ATOM 3661 C CA . ALA A 1 476 ? 24.849 -30.760 3.693 1.00 35.10 ? 476 ALA A CA 1 ATOM 3662 C C . ALA A 1 476 ? 26.270 -30.203 3.592 1.00 32.66 ? 476 ALA A C 1 ATOM 3663 O O . ALA A 1 476 ? 26.552 -29.355 2.760 1.00 33.84 ? 476 ALA A O 1 ATOM 3664 C CB . ALA A 1 476 ? 24.046 -30.007 4.743 1.00 36.35 ? 476 ALA A CB 1 ATOM 3665 N N . CYS A 1 477 ? 27.158 -30.704 4.429 1.00 31.67 ? 477 CYS A N 1 ATOM 3666 C CA . CYS A 1 477 ? 28.554 -30.295 4.406 1.00 31.86 ? 477 CYS A CA 1 ATOM 3667 C C . CYS A 1 477 ? 29.217 -30.702 3.104 1.00 30.11 ? 477 CYS A C 1 ATOM 3668 O O . CYS A 1 477 ? 29.887 -29.899 2.461 1.00 30.50 ? 477 CYS A O 1 ATOM 3669 C CB . CYS A 1 477 ? 29.278 -30.930 5.578 1.00 33.35 ? 477 CYS A CB 1 ATOM 3670 S SG . CYS A 1 477 ? 30.974 -30.373 5.753 1.00 36.71 ? 477 CYS A SG 1 ATOM 3671 N N . ILE A 1 478 ? 29.016 -31.948 2.702 1.00 29.66 ? 478 ILE A N 1 ATOM 3672 C CA . ILE A 1 478 ? 29.533 -32.416 1.432 1.00 29.37 ? 478 ILE A CA 1 ATOM 3673 C C . ILE A 1 478 ? 28.974 -31.560 0.292 1.00 29.94 ? 478 ILE A C 1 ATOM 3674 O O . ILE A 1 478 ? 29.718 -31.141 -0.598 1.00 30.25 ? 478 ILE A O 1 ATOM 3675 C CB . ILE A 1 478 ? 29.187 -33.891 1.168 1.00 29.53 ? 478 ILE A CB 1 ATOM 3676 C CG1 . ILE A 1 478 ? 29.897 -34.821 2.162 1.00 29.54 ? 478 ILE A CG1 1 ATOM 3677 C CG2 . ILE A 1 478 ? 29.568 -34.266 -0.264 1.00 29.80 ? 478 ILE A CG2 1 ATOM 3678 C CD1 . ILE A 1 478 ? 31.401 -34.873 2.022 1.00 28.94 ? 478 ILE A CD1 1 ATOM 3679 N N . GLY A 1 479 ? 27.669 -31.299 0.327 1.00 30.76 ? 479 GLY A N 1 ATOM 3680 C CA . GLY A 1 479 ? 27.011 -30.442 -0.660 1.00 31.27 ? 479 GLY A CA 1 ATOM 3681 C C . GLY A 1 479 ? 27.629 -29.053 -0.735 1.00 31.99 ? 479 GLY A C 1 ATOM 3682 O O . GLY A 1 479 ? 27.807 -28.521 -1.824 1.00 32.55 ? 479 GLY A O 1 ATOM 3683 N N . SER A 1 480 ? 27.994 -28.493 0.413 1.00 31.56 ? 480 SER A N 1 ATOM 3684 C CA . SER A 1 480 ? 28.662 -27.178 0.470 1.00 32.93 ? 480 SER A CA 1 ATOM 3685 C C . SER A 1 480 ? 30.014 -27.169 -0.258 1.00 32.40 ? 480 SER A C 1 ATOM 3686 O O . SER A 1 480 ? 30.373 -26.186 -0.910 1.00 32.87 ? 480 SER A O 1 ATOM 3687 C CB . SER A 1 480 ? 28.833 -26.713 1.919 1.00 34.35 ? 480 SER A CB 1 ATOM 3688 O OG . SER A 1 480 ? 29.942 -27.314 2.574 1.00 33.62 ? 480 SER A OG 1 ATOM 3689 N N . ILE A 1 481 ? 30.738 -28.278 -0.170 1.00 30.63 ? 481 ILE A N 1 ATOM 3690 C CA . ILE A 1 481 ? 32.005 -28.432 -0.878 1.00 30.06 ? 481 ILE A CA 1 ATOM 3691 C C . ILE A 1 481 ? 31.746 -28.481 -2.372 1.00 32.06 ? 481 ILE A C 1 ATOM 3692 O O . ILE A 1 481 ? 32.367 -27.745 -3.146 1.00 32.69 ? 481 ILE A O 1 ATOM 3693 C CB . ILE A 1 481 ? 32.749 -29.701 -0.451 1.00 28.53 ? 481 ILE A CB 1 ATOM 3694 C CG1 . ILE A 1 481 ? 33.113 -29.607 1.031 1.00 28.17 ? 481 ILE A CG1 1 ATOM 3695 C CG2 . ILE A 1 481 ? 33.999 -29.891 -1.299 1.00 28.21 ? 481 ILE A CG2 1 ATOM 3696 C CD1 . ILE A 1 481 ? 33.580 -30.898 1.639 1.00 27.56 ? 481 ILE A CD1 1 ATOM 3697 N N . ARG A 1 482 ? 30.819 -29.344 -2.770 1.00 33.34 ? 482 ARG A N 1 ATOM 3698 C CA . ARG A 1 482 ? 30.444 -29.503 -4.168 1.00 34.57 ? 482 ARG A CA 1 ATOM 3699 C C . ARG A 1 482 ? 29.928 -28.208 -4.781 1.00 38.89 ? 482 ARG A C 1 ATOM 3700 O O . ARG A 1 482 ? 30.187 -27.924 -5.954 1.00 39.85 ? 482 ARG A O 1 ATOM 3701 C CB . ARG A 1 482 ? 29.361 -30.566 -4.309 1.00 35.07 ? 482 ARG A CB 1 ATOM 3702 C CG . ARG A 1 482 ? 29.800 -31.978 -3.994 1.00 33.70 ? 482 ARG A CG 1 ATOM 3703 C CD . ARG A 1 482 ? 28.792 -33.001 -4.487 1.00 35.02 ? 482 ARG A CD 1 ATOM 3704 N NE . ARG A 1 482 ? 27.455 -32.711 -4.004 1.00 36.97 ? 482 ARG A NE 1 ATOM 3705 C CZ . ARG A 1 482 ? 26.682 -33.539 -3.300 1.00 38.58 ? 482 ARG A CZ 1 ATOM 3706 N NH1 . ARG A 1 482 ? 27.050 -34.787 -3.015 1.00 37.67 ? 482 ARG A NH1 1 ATOM 3707 N NH2 . ARG A 1 482 ? 25.485 -33.111 -2.909 1.00 39.82 ? 482 ARG A NH2 1 ATOM 3708 N N . ASN A 1 483 ? 29.201 -27.436 -3.980 1.00 42.51 ? 483 ASN A N 1 ATOM 3709 C CA . ASN A 1 483 ? 28.555 -26.201 -4.410 1.00 48.84 ? 483 ASN A CA 1 ATOM 3710 C C . ASN A 1 483 ? 29.479 -24.980 -4.278 1.00 48.19 ? 483 ASN A C 1 ATOM 3711 O O . ASN A 1 483 ? 29.119 -23.882 -4.672 1.00 48.85 ? 483 ASN A O 1 ATOM 3712 C CB . ASN A 1 483 ? 27.287 -26.007 -3.562 1.00 56.95 ? 483 ASN A CB 1 ATOM 3713 C CG . ASN A 1 483 ? 26.275 -25.067 -4.189 1.00 66.75 ? 483 ASN A CG 1 ATOM 3714 O OD1 . ASN A 1 483 ? 26.516 -24.503 -5.260 1.00 69.65 ? 483 ASN A OD1 1 ATOM 3715 N ND2 . ASN A 1 483 ? 25.119 -24.884 -3.520 1.00 77.00 ? 483 ASN A ND2 1 ATOM 3716 N N . GLY A 1 484 ? 30.662 -25.171 -3.702 1.00 45.15 ? 484 GLY A N 1 ATOM 3717 C CA . GLY A 1 484 ? 31.636 -24.090 -3.564 1.00 44.79 ? 484 GLY A CA 1 ATOM 3718 C C . GLY A 1 484 ? 31.374 -23.126 -2.419 1.00 44.92 ? 484 GLY A C 1 ATOM 3719 O O . GLY A 1 484 ? 31.920 -22.020 -2.413 1.00 45.17 ? 484 GLY A O 1 ATOM 3720 N N . THR A 1 485 ? 30.559 -23.535 -1.446 1.00 42.07 ? 485 THR A N 1 ATOM 3721 C CA . THR A 1 485 ? 30.225 -22.679 -0.310 1.00 42.45 ? 485 THR A CA 1 ATOM 3722 C C . THR A 1 485 ? 30.771 -23.156 1.044 1.00 39.61 ? 485 THR A C 1 ATOM 3723 O O . THR A 1 485 ? 30.475 -22.567 2.065 1.00 40.03 ? 485 THR A O 1 ATOM 3724 C CB . THR A 1 485 ? 28.704 -22.474 -0.195 1.00 44.07 ? 485 THR A CB 1 ATOM 3725 O OG1 . THR A 1 485 ? 28.063 -23.714 0.137 1.00 43.50 ? 485 THR A OG1 1 ATOM 3726 C CG2 . THR A 1 485 ? 28.152 -21.925 -1.511 1.00 46.28 ? 485 THR A CG2 1 ATOM 3727 N N . TYR A 1 486 ? 31.590 -24.202 1.037 1.00 37.87 ? 486 TYR A N 1 ATOM 3728 C CA . TYR A 1 486 ? 32.225 -24.723 2.254 1.00 34.69 ? 486 TYR A CA 1 ATOM 3729 C C . TYR A 1 486 ? 33.086 -23.656 2.903 1.00 35.22 ? 486 TYR A C 1 ATOM 3730 O O . TYR A 1 486 ? 33.903 -23.035 2.238 1.00 34.73 ? 486 TYR A O 1 ATOM 3731 C CB . TYR A 1 486 ? 33.080 -25.921 1.865 1.00 32.45 ? 486 TYR A CB 1 ATOM 3732 C CG . TYR A 1 486 ? 33.908 -26.575 2.946 1.00 30.56 ? 486 TYR A CG 1 ATOM 3733 C CD1 . TYR A 1 486 ? 33.360 -27.530 3.782 1.00 29.45 ? 486 TYR A CD1 1 ATOM 3734 C CD2 . TYR A 1 486 ? 35.268 -26.295 3.072 1.00 28.82 ? 486 TYR A CD2 1 ATOM 3735 C CE1 . TYR A 1 486 ? 34.136 -28.163 4.748 1.00 28.38 ? 486 TYR A CE1 1 ATOM 3736 C CE2 . TYR A 1 486 ? 36.047 -26.930 4.014 1.00 27.93 ? 486 TYR A CE2 1 ATOM 3737 C CZ . TYR A 1 486 ? 35.484 -27.862 4.852 1.00 27.40 ? 486 TYR A CZ 1 ATOM 3738 O OH . TYR A 1 486 ? 36.270 -28.488 5.787 1.00 26.58 ? 486 TYR A OH 1 ATOM 3739 N N . ASP A 1 487 ? 32.888 -23.440 4.199 1.00 35.07 ? 487 ASP A N 1 ATOM 3740 C CA . ASP A 1 487 ? 33.689 -22.486 4.961 1.00 36.90 ? 487 ASP A CA 1 ATOM 3741 C C . ASP A 1 487 ? 34.651 -23.276 5.852 1.00 34.79 ? 487 ASP A C 1 ATOM 3742 O O . ASP A 1 487 ? 34.250 -23.834 6.872 1.00 34.61 ? 487 ASP A O 1 ATOM 3743 C CB . ASP A 1 487 ? 32.781 -21.590 5.800 1.00 40.15 ? 487 ASP A CB 1 ATOM 3744 C CG . ASP A 1 487 ? 33.536 -20.469 6.493 1.00 42.92 ? 487 ASP A CG 1 ATOM 3745 O OD1 . ASP A 1 487 ? 34.781 -20.563 6.646 1.00 42.89 ? 487 ASP A OD1 1 ATOM 3746 O OD2 . ASP A 1 487 ? 32.870 -19.482 6.881 1.00 45.61 ? 487 ASP A OD2 1 ATOM 3747 N N . HIS A 1 488 ? 35.921 -23.314 5.464 1.00 32.23 ? 488 HIS A N 1 ATOM 3748 C CA . HIS A 1 488 ? 36.896 -24.166 6.151 1.00 31.90 ? 488 HIS A CA 1 ATOM 3749 C C . HIS A 1 488 ? 37.090 -23.742 7.575 1.00 31.96 ? 488 HIS A C 1 ATOM 3750 O O . HIS A 1 488 ? 37.431 -24.563 8.423 1.00 30.75 ? 488 HIS A O 1 ATOM 3751 C CB . HIS A 1 488 ? 38.238 -24.161 5.415 1.00 31.29 ? 488 HIS A CB 1 ATOM 3752 C CG . HIS A 1 488 ? 39.063 -22.942 5.689 1.00 32.21 ? 488 HIS A CG 1 ATOM 3753 N ND1 . HIS A 1 488 ? 40.107 -22.961 6.523 1.00 33.47 ? 488 HIS A ND1 1 ATOM 3754 C CD2 . HIS A 1 488 ? 38.943 -21.635 5.229 1.00 33.96 ? 488 HIS A CD2 1 ATOM 3755 C CE1 . HIS A 1 488 ? 40.644 -21.720 6.600 1.00 35.77 ? 488 HIS A CE1 1 ATOM 3756 N NE2 . HIS A 1 488 ? 39.933 -20.909 5.803 1.00 35.32 ? 488 HIS A NE2 1 ATOM 3757 N N . ASP A 1 489 ? 36.875 -22.464 7.872 1.00 34.43 ? 489 ASP A N 1 ATOM 3758 C CA . ASP A 1 489 ? 37.125 -21.958 9.232 1.00 38.34 ? 489 ASP A CA 1 ATOM 3759 C C . ASP A 1 489 ? 36.214 -22.581 10.285 1.00 37.39 ? 489 ASP A C 1 ATOM 3760 O O . ASP A 1 489 ? 36.618 -22.738 11.427 1.00 36.94 ? 489 ASP A O 1 ATOM 3761 C CB . ASP A 1 489 ? 36.990 -20.434 9.301 1.00 42.63 ? 489 ASP A CB 1 ATOM 3762 C CG . ASP A 1 489 ? 38.210 -19.721 8.780 1.00 46.96 ? 489 ASP A CG 1 ATOM 3763 O OD1 . ASP A 1 489 ? 39.343 -20.132 9.121 1.00 51.90 ? 489 ASP A OD1 1 ATOM 3764 O OD2 . ASP A 1 489 ? 38.041 -18.738 8.027 1.00 52.42 ? 489 ASP A OD2 1 ATOM 3765 N N . VAL A 1 490 ? 35.000 -22.938 9.881 1.00 37.42 ? 490 VAL A N 1 ATOM 3766 C CA . VAL A 1 490 ? 34.001 -23.527 10.781 1.00 38.07 ? 490 VAL A CA 1 ATOM 3767 C C . VAL A 1 490 ? 34.491 -24.849 11.381 1.00 36.35 ? 490 VAL A C 1 ATOM 3768 O O . VAL A 1 490 ? 34.180 -25.190 12.534 1.00 35.03 ? 490 VAL A O 1 ATOM 3769 C CB . VAL A 1 490 ? 32.677 -23.773 10.020 1.00 39.08 ? 490 VAL A CB 1 ATOM 3770 C CG1 . VAL A 1 490 ? 31.672 -24.535 10.869 1.00 43.16 ? 490 VAL A CG1 1 ATOM 3771 C CG2 . VAL A 1 490 ? 32.090 -22.451 9.548 1.00 42.25 ? 490 VAL A CG2 1 ATOM 3772 N N . TYR A 1 491 ? 35.260 -25.589 10.595 1.00 32.77 ? 491 TYR A N 1 ATOM 3773 C CA . TYR A 1 491 ? 35.648 -26.952 10.946 1.00 32.57 ? 491 TYR A CA 1 ATOM 3774 C C . TYR A 1 491 ? 37.112 -27.086 11.323 1.00 31.79 ? 491 TYR A C 1 ATOM 3775 O O . TYR A 1 491 ? 37.529 -28.153 11.722 1.00 31.86 ? 491 TYR A O 1 ATOM 3776 C CB . TYR A 1 491 ? 35.364 -27.897 9.772 1.00 31.84 ? 491 TYR A CB 1 ATOM 3777 C CG . TYR A 1 491 ? 33.952 -27.850 9.275 1.00 33.81 ? 491 TYR A CG 1 ATOM 3778 C CD1 . TYR A 1 491 ? 32.953 -28.585 9.900 1.00 35.24 ? 491 TYR A CD1 1 ATOM 3779 C CD2 . TYR A 1 491 ? 33.599 -27.072 8.174 1.00 34.75 ? 491 TYR A CD2 1 ATOM 3780 C CE1 . TYR A 1 491 ? 31.645 -28.558 9.433 1.00 36.76 ? 491 TYR A CE1 1 ATOM 3781 C CE2 . TYR A 1 491 ? 32.287 -27.020 7.720 1.00 35.84 ? 491 TYR A CE2 1 ATOM 3782 C CZ . TYR A 1 491 ? 31.316 -27.776 8.348 1.00 37.22 ? 491 TYR A CZ 1 ATOM 3783 O OH . TYR A 1 491 ? 30.008 -27.739 7.895 1.00 40.15 ? 491 TYR A OH 1 ATOM 3784 N N . ARG A 1 492 ? 37.895 -26.014 11.189 1.00 31.23 ? 492 ARG A N 1 ATOM 3785 C CA . ARG A 1 492 ? 39.340 -26.117 11.272 1.00 31.45 ? 492 ARG A CA 1 ATOM 3786 C C . ARG A 1 492 ? 39.848 -26.597 12.626 1.00 32.78 ? 492 ARG A C 1 ATOM 3787 O O . ARG A 1 492 ? 40.752 -27.433 12.690 1.00 32.85 ? 492 ARG A O 1 ATOM 3788 C CB . ARG A 1 492 ? 39.971 -24.768 10.906 1.00 32.42 ? 492 ARG A CB 1 ATOM 3789 C CG . ARG A 1 492 ? 41.479 -24.744 10.942 1.00 33.17 ? 492 ARG A CG 1 ATOM 3790 C CD . ARG A 1 492 ? 41.942 -23.341 10.602 1.00 34.45 ? 492 ARG A CD 1 ATOM 3791 N NE . ARG A 1 492 ? 43.380 -23.173 10.684 1.00 35.32 ? 492 ARG A NE 1 ATOM 3792 C CZ . ARG A 1 492 ? 44.222 -23.144 9.653 1.00 35.72 ? 492 ARG A CZ 1 ATOM 3793 N NH1 . ARG A 1 492 ? 43.799 -23.309 8.405 1.00 35.42 ? 492 ARG A NH1 1 ATOM 3794 N NH2 . ARG A 1 492 ? 45.516 -22.948 9.876 1.00 37.07 ? 492 ARG A NH2 1 ATOM 3795 N N . ASP A 1 493 ? 39.284 -26.062 13.704 1.00 33.88 ? 493 ASP A N 1 ATOM 3796 C CA . ASP A 1 493 ? 39.600 -26.545 15.052 1.00 36.88 ? 493 ASP A CA 1 ATOM 3797 C C . ASP A 1 493 ? 39.428 -28.076 15.177 1.00 35.75 ? 493 ASP A C 1 ATOM 3798 O O . ASP A 1 493 ? 40.343 -28.783 15.618 1.00 34.82 ? 493 ASP A O 1 ATOM 3799 C CB . ASP A 1 493 ? 38.728 -25.834 16.091 1.00 40.92 ? 493 ASP A CB 1 ATOM 3800 C CG . ASP A 1 493 ? 39.225 -24.419 16.428 1.00 45.01 ? 493 ASP A CG 1 ATOM 3801 O OD1 . ASP A 1 493 ? 40.293 -24.007 15.938 1.00 47.26 ? 493 ASP A OD1 1 ATOM 3802 O OD2 . ASP A 1 493 ? 38.543 -23.716 17.210 1.00 49.98 ? 493 ASP A OD2 1 ATOM 3803 N N . GLU A 1 494 ? 38.260 -28.573 14.793 1.00 34.40 ? 494 GLU A N 1 ATOM 3804 C CA . GLU A 1 494 ? 37.976 -30.008 14.837 1.00 34.28 ? 494 GLU A CA 1 ATOM 3805 C C . GLU A 1 494 ? 38.981 -30.752 13.963 1.00 33.33 ? 494 GLU A C 1 ATOM 3806 O O . GLU A 1 494 ? 39.595 -31.722 14.395 1.00 31.82 ? 494 GLU A O 1 ATOM 3807 C CB . GLU A 1 494 ? 36.550 -30.291 14.359 1.00 34.59 ? 494 GLU A CB 1 ATOM 3808 C CG . GLU A 1 494 ? 36.155 -31.769 14.295 1.00 36.05 ? 494 GLU A CG 1 ATOM 3809 C CD . GLU A 1 494 ? 34.720 -31.999 13.808 1.00 36.38 ? 494 GLU A CD 1 ATOM 3810 O OE1 . GLU A 1 494 ? 33.989 -31.013 13.550 1.00 37.58 ? 494 GLU A OE1 1 ATOM 3811 O OE2 . GLU A 1 494 ? 34.310 -33.173 13.652 1.00 35.22 ? 494 GLU A OE2 1 ATOM 3812 N N . ALA A 1 495 ? 39.153 -30.290 12.730 1.00 32.47 ? 495 ALA A N 1 ATOM 3813 C CA . ALA A 1 495 ? 40.014 -31.003 11.788 1.00 32.16 ? 495 ALA A CA 1 ATOM 3814 C C . ALA A 1 495 ? 41.470 -31.050 12.255 1.00 32.64 ? 495 ALA A C 1 ATOM 3815 O O . ALA A 1 495 ? 42.099 -32.099 12.203 1.00 32.50 ? 495 ALA A O 1 ATOM 3816 C CB . ALA A 1 495 ? 39.895 -30.390 10.398 1.00 31.90 ? 495 ALA A CB 1 ATOM 3817 N N . LEU A 1 496 ? 42.003 -29.926 12.738 1.00 34.63 ? 496 LEU A N 1 ATOM 3818 C CA . LEU A 1 496 ? 43.406 -29.881 13.183 1.00 36.78 ? 496 LEU A CA 1 ATOM 3819 C C . LEU A 1 496 ? 43.661 -30.799 14.378 1.00 38.95 ? 496 LEU A C 1 ATOM 3820 O O . LEU A 1 496 ? 44.711 -31.441 14.467 1.00 40.74 ? 496 LEU A O 1 ATOM 3821 C CB . LEU A 1 496 ? 43.850 -28.445 13.517 1.00 37.70 ? 496 LEU A CB 1 ATOM 3822 C CG . LEU A 1 496 ? 44.012 -27.499 12.321 1.00 37.51 ? 496 LEU A CG 1 ATOM 3823 C CD1 . LEU A 1 496 ? 44.449 -26.121 12.807 1.00 39.67 ? 496 LEU A CD1 1 ATOM 3824 C CD2 . LEU A 1 496 ? 44.979 -28.061 11.288 1.00 37.91 ? 496 LEU A CD2 1 ATOM 3825 N N . ASN A 1 497 ? 42.702 -30.859 15.289 1.00 39.77 ? 497 ASN A N 1 ATOM 3826 C CA . ASN A 1 497 ? 42.769 -31.810 16.388 1.00 42.13 ? 497 ASN A CA 1 ATOM 3827 C C . ASN A 1 497 ? 42.816 -33.255 15.920 1.00 40.73 ? 497 ASN A C 1 ATOM 3828 O O . ASN A 1 497 ? 43.606 -34.040 16.443 1.00 40.38 ? 497 ASN A O 1 ATOM 3829 C CB . ASN A 1 497 ? 41.598 -31.624 17.349 1.00 45.46 ? 497 ASN A CB 1 ATOM 3830 C CG . ASN A 1 497 ? 41.982 -30.819 18.551 1.00 51.28 ? 497 ASN A CG 1 ATOM 3831 O OD1 . ASN A 1 497 ? 42.901 -31.196 19.287 1.00 56.07 ? 497 ASN A OD1 1 ATOM 3832 N ND2 . ASN A 1 497 ? 41.295 -29.699 18.766 1.00 54.81 ? 497 ASN A ND2 1 ATOM 3833 N N . ASN A 1 498 ? 41.990 -33.604 14.934 1.00 38.06 ? 498 ASN A N 1 ATOM 3834 C CA . ASN A 1 498 ? 41.993 -34.972 14.410 1.00 38.87 ? 498 ASN A CA 1 ATOM 3835 C C . ASN A 1 498 ? 43.263 -35.307 13.614 1.00 38.53 ? 498 ASN A C 1 ATOM 3836 O O . ASN A 1 498 ? 43.817 -36.389 13.756 1.00 39.13 ? 498 ASN A O 1 ATOM 3837 C CB . ASN A 1 498 ? 40.744 -35.240 13.570 1.00 38.13 ? 498 ASN A CB 1 ATOM 3838 C CG . ASN A 1 498 ? 39.491 -35.349 14.409 1.00 40.77 ? 498 ASN A CG 1 ATOM 3839 O OD1 . ASN A 1 498 ? 39.559 -35.672 15.598 1.00 43.06 ? 498 ASN A OD1 1 ATOM 3840 N ND2 . ASN A 1 498 ? 38.337 -35.079 13.803 1.00 40.54 ? 498 ASN A ND2 1 ATOM 3841 N N . ARG A 1 499 ? 43.720 -34.372 12.796 1.00 38.08 ? 499 ARG A N 1 ATOM 3842 C CA . ARG A 1 499 ? 44.921 -34.570 11.973 1.00 40.27 ? 499 ARG A CA 1 ATOM 3843 C C . ARG A 1 499 ? 46.181 -34.697 12.781 1.00 44.91 ? 499 ARG A C 1 ATOM 3844 O O . ARG A 1 499 ? 46.950 -35.629 12.595 1.00 46.58 ? 499 ARG A O 1 ATOM 3845 C CB . ARG A 1 499 ? 45.127 -33.396 11.031 1.00 38.45 ? 499 ARG A CB 1 ATOM 3846 C CG . ARG A 1 499 ? 44.244 -33.422 9.821 1.00 35.85 ? 499 ARG A CG 1 ATOM 3847 C CD . ARG A 1 499 ? 44.576 -32.262 8.908 1.00 35.99 ? 499 ARG A CD 1 ATOM 3848 N NE . ARG A 1 499 ? 45.845 -32.423 8.212 1.00 35.25 ? 499 ARG A NE 1 ATOM 3849 C CZ . ARG A 1 499 ? 46.538 -31.426 7.664 1.00 37.26 ? 499 ARG A CZ 1 ATOM 3850 N NH1 . ARG A 1 499 ? 46.111 -30.166 7.727 1.00 37.77 ? 499 ARG A NH1 1 ATOM 3851 N NH2 . ARG A 1 499 ? 47.679 -31.682 7.055 1.00 38.97 ? 499 ARG A NH2 1 ATOM 3852 N N . PHE A 1 500 ? 46.400 -33.724 13.656 1.00 48.46 ? 500 PHE A N 1 ATOM 3853 C CA . PHE A 1 500 ? 47.618 -33.656 14.441 1.00 53.32 ? 500 PHE A CA 1 ATOM 3854 C C . PHE A 1 500 ? 47.294 -34.114 15.844 1.00 58.86 ? 500 PHE A C 1 ATOM 3855 O O . PHE A 1 500 ? 47.146 -33.313 16.760 1.00 63.10 ? 500 PHE A O 1 ATOM 3856 C CB . PHE A 1 500 ? 48.206 -32.240 14.390 1.00 52.90 ? 500 PHE A CB 1 ATOM 3857 C CG . PHE A 1 500 ? 48.396 -31.727 12.985 1.00 51.78 ? 500 PHE A CG 1 ATOM 3858 C CD1 . PHE A 1 500 ? 49.041 -32.506 12.030 1.00 52.28 ? 500 PHE A CD1 1 ATOM 3859 C CD2 . PHE A 1 500 ? 47.924 -30.481 12.610 1.00 52.58 ? 500 PHE A CD2 1 ATOM 3860 C CE1 . PHE A 1 500 ? 49.213 -32.056 10.727 1.00 53.02 ? 500 PHE A CE1 1 ATOM 3861 C CE2 . PHE A 1 500 ? 48.084 -30.023 11.304 1.00 52.12 ? 500 PHE A CE2 1 ATOM 3862 C CZ . PHE A 1 500 ? 48.739 -30.807 10.362 1.00 52.89 ? 500 PHE A CZ 1 ATOM 3863 N N . GLN A 1 501 ? 47.129 -35.425 15.975 1.00 63.97 ? 501 GLN A N 1 ATOM 3864 C CA . GLN A 1 501 ? 46.980 -36.066 17.268 1.00 69.88 ? 501 GLN A CA 1 ATOM 3865 C C . GLN A 1 501 ? 48.006 -37.182 17.387 1.00 75.21 ? 501 GLN A C 1 ATOM 3866 O O . GLN A 1 501 ? 48.277 -37.894 16.409 1.00 76.46 ? 501 GLN A O 1 ATOM 3867 C CB . GLN A 1 501 ? 45.568 -36.633 17.443 1.00 70.39 ? 501 GLN A CB 1 ATOM 3868 C CG . GLN A 1 501 ? 45.189 -37.757 16.482 1.00 70.56 ? 501 GLN A CG 1 ATOM 3869 C CD . GLN A 1 501 ? 43.734 -38.178 16.609 1.00 70.81 ? 501 GLN A CD 1 ATOM 3870 O OE1 . GLN A 1 501 ? 43.162 -38.760 15.688 1.00 71.07 ? 501 GLN A OE1 1 ATOM 3871 N NE2 . GLN A 1 501 ? 43.128 -37.881 17.752 1.00 73.71 ? 501 GLN A NE2 1 ATOM 3872 N N . ILE A 1 502 ? 48.572 -37.328 18.584 1.00 78.74 ? 502 ILE A N 1 ATOM 3873 C CA . ILE A 1 502 ? 49.444 -38.459 18.890 1.00 81.99 ? 502 ILE A CA 1 ATOM 3874 C C . ILE A 1 502 ? 48.507 -39.656 19.064 1.00 83.71 ? 502 ILE A C 1 ATOM 3875 O O . ILE A 1 502 ? 47.590 -39.613 19.890 1.00 86.25 ? 502 ILE A O 1 ATOM 3876 C CB . ILE A 1 502 ? 50.301 -38.271 20.178 1.00 84.50 ? 502 ILE A CB 1 ATOM 3877 C CG1 . ILE A 1 502 ? 50.550 -36.790 20.526 1.00 83.80 ? 502 ILE A CG1 1 ATOM 3878 C CG2 . ILE A 1 502 ? 51.624 -39.016 20.044 1.00 85.60 ? 502 ILE A CG2 1 ATOM 3879 C CD1 . ILE A 1 502 ? 49.482 -36.165 21.409 1.00 82.87 ? 502 ILE A CD1 1 ATOM 3880 N N . LYS A 1 503 ? 48.720 -40.707 18.277 1.00 83.90 ? 503 LYS A N 1 ATOM 3881 C CA . LYS A 1 503 ? 47.838 -41.881 18.290 1.00 84.18 ? 503 LYS A CA 1 ATOM 3882 C C . LYS A 1 503 ? 48.287 -42.941 19.296 1.00 87.45 ? 503 LYS A C 1 ATOM 3883 O O . LYS A 1 503 ? 49.446 -42.979 19.705 1.00 88.55 ? 503 LYS A O 1 ATOM 3884 C CB . LYS A 1 503 ? 47.755 -42.494 16.891 1.00 83.34 ? 503 LYS A CB 1 ATOM 3885 C CG . LYS A 1 503 ? 46.741 -41.828 15.971 1.00 79.56 ? 503 LYS A CG 1 ATOM 3886 C CD . LYS A 1 503 ? 47.005 -42.196 14.515 1.00 79.42 ? 503 LYS A CD 1 ATOM 3887 C CE . LYS A 1 503 ? 45.752 -42.662 13.786 1.00 76.95 ? 503 LYS A CE 1 ATOM 3888 N NZ . LYS A 1 503 ? 44.869 -41.526 13.407 1.00 73.86 ? 503 LYS A NZ 1 HETATM 3889 C C1 . NAG B 2 . ? 29.152 -39.723 -29.744 1.00 47.11 ? 801 NAG A C1 1 HETATM 3890 C C2 . NAG B 2 . ? 27.688 -39.703 -29.318 1.00 52.56 ? 801 NAG A C2 1 HETATM 3891 C C3 . NAG B 2 . ? 26.749 -39.225 -30.417 1.00 55.53 ? 801 NAG A C3 1 HETATM 3892 C C4 . NAG B 2 . ? 27.228 -37.914 -31.053 1.00 56.60 ? 801 NAG A C4 1 HETATM 3893 C C5 . NAG B 2 . ? 28.718 -37.953 -31.430 1.00 55.15 ? 801 NAG A C5 1 HETATM 3894 C C6 . NAG B 2 . ? 29.226 -36.534 -31.707 1.00 54.50 ? 801 NAG A C6 1 HETATM 3895 C C7 . NAG B 2 . ? 27.164 -41.333 -27.568 1.00 55.80 ? 801 NAG A C7 1 HETATM 3896 C C8 . NAG B 2 . ? 26.834 -42.761 -27.241 1.00 57.29 ? 801 NAG A C8 1 HETATM 3897 N N2 . NAG B 2 . ? 27.343 -41.042 -28.858 1.00 54.26 ? 801 NAG A N2 1 HETATM 3898 O O3 . NAG B 2 . ? 25.490 -39.016 -29.820 1.00 55.38 ? 801 NAG A O3 1 HETATM 3899 O O4 . NAG B 2 . ? 26.506 -37.685 -32.258 1.00 62.68 ? 801 NAG A O4 1 HETATM 3900 O O5 . NAG B 2 . ? 29.579 -38.560 -30.474 1.00 46.79 ? 801 NAG A O5 1 HETATM 3901 O O6 . NAG B 2 . ? 29.248 -35.767 -30.516 1.00 54.48 ? 801 NAG A O6 1 HETATM 3902 O O7 . NAG B 2 . ? 27.250 -40.502 -26.665 1.00 56.94 ? 801 NAG A O7 1 HETATM 3903 C C1 . NAG C 2 . ? 25.683 -36.495 -32.276 1.00 67.04 ? 802 NAG A C1 1 HETATM 3904 C C2 . NAG C 2 . ? 25.503 -36.081 -33.739 1.00 68.48 ? 802 NAG A C2 1 HETATM 3905 C C3 . NAG C 2 . ? 24.388 -35.055 -33.971 1.00 70.40 ? 802 NAG A C3 1 HETATM 3906 C C4 . NAG C 2 . ? 23.134 -35.298 -33.138 1.00 73.79 ? 802 NAG A C4 1 HETATM 3907 C C5 . NAG C 2 . ? 23.504 -35.660 -31.695 1.00 73.02 ? 802 NAG A C5 1 HETATM 3908 C C6 . NAG C 2 . ? 22.288 -36.082 -30.868 1.00 72.53 ? 802 NAG A C6 1 HETATM 3909 C C7 . NAG C 2 . ? 27.545 -36.272 -35.082 1.00 64.72 ? 802 NAG A C7 1 HETATM 3910 C C8 . NAG C 2 . ? 28.783 -35.595 -35.586 1.00 63.61 ? 802 NAG A C8 1 HETATM 3911 N N2 . NAG C 2 . ? 26.748 -35.552 -34.295 1.00 67.23 ? 802 NAG A N2 1 HETATM 3912 O O3 . NAG C 2 . ? 24.022 -35.050 -35.333 1.00 66.74 ? 802 NAG A O3 1 HETATM 3913 O O4 . NAG C 2 . ? 22.395 -34.086 -33.192 1.00 80.06 ? 802 NAG A O4 1 HETATM 3914 O O5 . NAG C 2 . ? 24.428 -36.737 -31.668 1.00 69.13 ? 802 NAG A O5 1 HETATM 3915 O O6 . NAG C 2 . ? 21.828 -37.346 -31.302 1.00 72.66 ? 802 NAG A O6 1 HETATM 3916 O O7 . NAG C 2 . ? 27.305 -37.433 -35.395 1.00 65.72 ? 802 NAG A O7 1 HETATM 3917 C C1 . MAN D 3 . ? 20.983 -34.205 -33.497 1.00 88.05 ? 803 MAN A C1 1 HETATM 3918 C C2 . MAN D 3 . ? 20.721 -33.520 -34.847 1.00 88.62 ? 803 MAN A C2 1 HETATM 3919 C C3 . MAN D 3 . ? 19.267 -33.099 -35.108 1.00 90.75 ? 803 MAN A C3 1 HETATM 3920 C C4 . MAN D 3 . ? 18.376 -33.312 -33.890 1.00 94.36 ? 803 MAN A C4 1 HETATM 3921 C C5 . MAN D 3 . ? 19.121 -32.812 -32.663 1.00 96.20 ? 803 MAN A C5 1 HETATM 3922 C C6 . MAN D 3 . ? 18.205 -32.736 -31.442 1.00 93.54 ? 803 MAN A C6 1 HETATM 3923 O O2 . MAN D 3 . ? 21.139 -34.412 -35.890 1.00 82.38 ? 803 MAN A O2 1 HETATM 3924 O O3 . MAN D 3 . ? 18.728 -33.825 -36.220 1.00 90.93 ? 803 MAN A O3 1 HETATM 3925 O O4 . MAN D 3 . ? 17.131 -32.615 -34.027 1.00 91.30 ? 803 MAN A O4 1 HETATM 3926 O O5 . MAN D 3 . ? 20.221 -33.685 -32.391 1.00 94.97 ? 803 MAN A O5 1 HETATM 3927 O O6 . MAN D 3 . ? 17.383 -31.567 -31.536 1.00 90.81 ? 803 MAN A O6 1 HETATM 3928 C C1 . NAG E 2 . ? 20.092 -45.581 -76.421 1.00 44.42 ? 804 NAG A C1 1 HETATM 3929 C C2 . NAG E 2 . ? 18.575 -45.575 -76.347 1.00 49.03 ? 804 NAG A C2 1 HETATM 3930 C C3 . NAG E 2 . ? 18.003 -46.971 -76.148 1.00 53.66 ? 804 NAG A C3 1 HETATM 3931 C C4 . NAG E 2 . ? 18.574 -47.872 -77.234 1.00 54.40 ? 804 NAG A C4 1 HETATM 3932 C C5 . NAG E 2 . ? 20.095 -47.870 -77.056 1.00 53.78 ? 804 NAG A C5 1 HETATM 3933 C C6 . NAG E 2 . ? 20.815 -48.836 -77.985 1.00 51.77 ? 804 NAG A C6 1 HETATM 3934 C C7 . NAG E 2 . ? 17.662 -43.466 -75.538 1.00 52.57 ? 804 NAG A C7 1 HETATM 3935 C C8 . NAG E 2 . ? 17.258 -42.645 -74.347 1.00 54.32 ? 804 NAG A C8 1 HETATM 3936 N N2 . NAG E 2 . ? 18.146 -44.679 -75.285 1.00 51.98 ? 804 NAG A N2 1 HETATM 3937 O O3 . NAG E 2 . ? 16.602 -46.887 -76.238 1.00 53.17 ? 804 NAG A O3 1 HETATM 3938 O O4 . NAG E 2 . ? 18.035 -49.178 -77.147 1.00 59.11 ? 804 NAG A O4 1 HETATM 3939 O O5 . NAG E 2 . ? 20.561 -46.559 -77.325 1.00 48.13 ? 804 NAG A O5 1 HETATM 3940 O O6 . NAG E 2 . ? 20.498 -48.472 -79.310 1.00 52.72 ? 804 NAG A O6 1 HETATM 3941 O O7 . NAG E 2 . ? 17.546 -43.016 -76.680 1.00 57.11 ? 804 NAG A O7 1 HETATM 3942 C C1 . NAG F 2 . ? 18.412 -26.062 -95.334 1.00 59.37 ? 805 NAG A C1 1 HETATM 3943 C C2 . NAG F 2 . ? 17.052 -26.141 -94.630 1.00 71.14 ? 805 NAG A C2 1 HETATM 3944 C C3 . NAG F 2 . ? 15.909 -25.330 -95.270 1.00 71.62 ? 805 NAG A C3 1 HETATM 3945 C C4 . NAG F 2 . ? 16.394 -24.187 -96.159 1.00 70.57 ? 805 NAG A C4 1 HETATM 3946 C C5 . NAG F 2 . ? 17.520 -24.724 -97.028 1.00 67.25 ? 805 NAG A C5 1 HETATM 3947 C C6 . NAG F 2 . ? 17.998 -23.768 -98.113 1.00 67.99 ? 805 NAG A C6 1 HETATM 3948 C C7 . NAG F 2 . ? 16.328 -28.157 -93.400 1.00 82.26 ? 805 NAG A C7 1 HETATM 3949 C C8 . NAG F 2 . ? 15.976 -29.614 -93.523 1.00 80.93 ? 805 NAG A C8 1 HETATM 3950 N N2 . NAG F 2 . ? 16.675 -27.546 -94.540 1.00 76.44 ? 805 NAG A N2 1 HETATM 3951 O O3 . NAG F 2 . ? 15.064 -24.830 -94.255 1.00 71.49 ? 805 NAG A O3 1 HETATM 3952 O O4 . NAG F 2 . ? 15.333 -23.689 -96.946 1.00 72.03 ? 805 NAG A O4 1 HETATM 3953 O O5 . NAG F 2 . ? 18.577 -24.913 -96.124 1.00 70.68 ? 805 NAG A O5 1 HETATM 3954 O O6 . NAG F 2 . ? 18.639 -24.518 -99.119 1.00 66.51 ? 805 NAG A O6 1 HETATM 3955 O O7 . NAG F 2 . ? 16.290 -27.604 -92.299 1.00 80.49 ? 805 NAG A O7 1 HETATM 3956 C C1 . NAG G 2 . ? 36.934 -11.545 -99.226 1.00 42.12 ? 806 NAG A C1 1 HETATM 3957 C C2 . NAG G 2 . ? 37.749 -10.563 -100.068 1.00 45.40 ? 806 NAG A C2 1 HETATM 3958 C C3 . NAG G 2 . ? 38.251 -9.371 -99.271 1.00 46.16 ? 806 NAG A C3 1 HETATM 3959 C C4 . NAG G 2 . ? 37.129 -8.752 -98.460 1.00 44.46 ? 806 NAG A C4 1 HETATM 3960 C C5 . NAG G 2 . ? 36.526 -9.847 -97.593 1.00 45.05 ? 806 NAG A C5 1 HETATM 3961 C C6 . NAG G 2 . ? 35.408 -9.322 -96.705 1.00 45.24 ? 806 NAG A C6 1 HETATM 3962 C C7 . NAG G 2 . ? 38.907 -11.418 -102.062 1.00 53.24 ? 806 NAG A C7 1 HETATM 3963 C C8 . NAG G 2 . ? 40.121 -12.108 -102.616 1.00 51.04 ? 806 NAG A C8 1 HETATM 3964 N N2 . NAG G 2 . ? 38.860 -11.230 -100.732 1.00 49.87 ? 806 NAG A N2 1 HETATM 3965 O O3 . NAG G 2 . ? 38.785 -8.414 -100.156 1.00 48.00 ? 806 NAG A O3 1 HETATM 3966 O O4 . NAG G 2 . ? 37.697 -7.783 -97.613 1.00 45.00 ? 806 NAG A O4 1 HETATM 3967 O O5 . NAG G 2 . ? 36.005 -10.894 -98.390 1.00 41.09 ? 806 NAG A O5 1 HETATM 3968 O O6 . NAG G 2 . ? 34.334 -8.921 -97.522 1.00 51.11 ? 806 NAG A O6 1 HETATM 3969 O O7 . NAG G 2 . ? 38.011 -11.057 -102.830 1.00 52.63 ? 806 NAG A O7 1 HETATM 3970 C C1 . NAG H 2 . ? 37.212 -6.446 -97.788 1.00 47.96 ? 807 NAG A C1 1 HETATM 3971 C C2 . NAG H 2 . ? 37.584 -5.665 -96.534 1.00 46.98 ? 807 NAG A C2 1 HETATM 3972 C C3 . NAG H 2 . ? 37.236 -4.179 -96.662 1.00 51.31 ? 807 NAG A C3 1 HETATM 3973 C C4 . NAG H 2 . ? 37.588 -3.568 -98.025 1.00 56.93 ? 807 NAG A C4 1 HETATM 3974 C C5 . NAG H 2 . ? 37.191 -4.533 -99.151 1.00 55.60 ? 807 NAG A C5 1 HETATM 3975 C C6 . NAG H 2 . ? 37.598 -4.063 -100.548 1.00 57.63 ? 807 NAG A C6 1 HETATM 3976 C C7 . NAG H 2 . ? 37.556 -6.909 -94.408 1.00 45.72 ? 807 NAG A C7 1 HETATM 3977 C C8 . NAG H 2 . ? 36.706 -7.435 -93.284 1.00 43.06 ? 807 NAG A C8 1 HETATM 3978 N N2 . NAG H 2 . ? 36.915 -6.236 -95.368 1.00 44.95 ? 807 NAG A N2 1 HETATM 3979 O O3 . NAG H 2 . ? 37.890 -3.455 -95.640 1.00 47.31 ? 807 NAG A O3 1 HETATM 3980 O O4 . NAG H 2 . ? 36.900 -2.321 -98.131 1.00 65.82 ? 807 NAG A O4 1 HETATM 3981 O O5 . NAG H 2 . ? 37.774 -5.804 -98.922 1.00 50.35 ? 807 NAG A O5 1 HETATM 3982 O O6 . NAG H 2 . ? 39.004 -4.081 -100.686 1.00 61.68 ? 807 NAG A O6 1 HETATM 3983 O O7 . NAG H 2 . ? 38.775 -7.115 -94.415 1.00 40.47 ? 807 NAG A O7 1 HETATM 3984 C C1 . MAN I 3 . ? 37.717 -1.144 -98.372 1.00 74.25 ? 808 MAN A C1 1 HETATM 3985 C C2 . MAN I 3 . ? 37.571 -0.104 -97.260 1.00 77.54 ? 808 MAN A C2 1 HETATM 3986 C C3 . MAN I 3 . ? 38.488 1.104 -97.499 1.00 80.12 ? 808 MAN A C3 1 HETATM 3987 C C4 . MAN I 3 . ? 39.112 1.096 -98.896 1.00 81.00 ? 808 MAN A C4 1 HETATM 3988 C C5 . MAN I 3 . ? 38.126 0.642 -99.978 1.00 81.74 ? 808 MAN A C5 1 HETATM 3989 C C6 . MAN I 3 . ? 38.867 0.293 -101.269 1.00 82.26 ? 808 MAN A C6 1 HETATM 3990 O O2 . MAN I 3 . ? 37.833 -0.681 -95.975 1.00 75.22 ? 808 MAN A O2 1 HETATM 3991 O O3 . MAN I 3 . ? 39.541 1.148 -96.528 1.00 79.33 ? 808 MAN A O3 1 HETATM 3992 O O4 . MAN I 3 . ? 39.572 2.412 -99.225 1.00 80.38 ? 808 MAN A O4 1 HETATM 3993 O O5 . MAN I 3 . ? 37.331 -0.486 -99.584 1.00 78.72 ? 808 MAN A O5 1 HETATM 3994 O O6 . MAN I 3 . ? 39.405 1.485 -101.855 1.00 82.13 ? 808 MAN A O6 1 HETATM 3995 C C1 . NAG J 2 . ? 39.352 -17.425 -101.091 1.00 46.42 ? 809 NAG A C1 1 HETATM 3996 C C2 . NAG J 2 . ? 39.917 -18.585 -101.910 1.00 48.15 ? 809 NAG A C2 1 HETATM 3997 C C3 . NAG J 2 . ? 40.577 -18.075 -103.184 1.00 53.23 ? 809 NAG A C3 1 HETATM 3998 C C4 . NAG J 2 . ? 39.655 -17.126 -103.946 1.00 56.14 ? 809 NAG A C4 1 HETATM 3999 C C5 . NAG J 2 . ? 39.068 -16.062 -103.022 1.00 55.56 ? 809 NAG A C5 1 HETATM 4000 C C6 . NAG J 2 . ? 37.991 -15.280 -103.763 1.00 57.52 ? 809 NAG A C6 1 HETATM 4001 C C7 . NAG J 2 . ? 40.883 -20.548 -100.776 1.00 52.48 ? 809 NAG A C7 1 HETATM 4002 C C8 . NAG J 2 . ? 42.107 -21.064 -100.066 1.00 54.12 ? 809 NAG A C8 1 HETATM 4003 N N2 . NAG J 2 . ? 40.964 -19.289 -101.197 1.00 48.25 ? 809 NAG A N2 1 HETATM 4004 O O3 . NAG J 2 . ? 40.946 -19.198 -103.962 1.00 47.14 ? 809 NAG A O3 1 HETATM 4005 O O4 . NAG J 2 . ? 40.376 -16.508 -105.003 1.00 64.71 ? 809 NAG A O4 1 HETATM 4006 O O5 . NAG J 2 . ? 38.467 -16.642 -101.872 1.00 50.42 ? 809 NAG A O5 1 HETATM 4007 O O6 . NAG J 2 . ? 37.461 -14.312 -102.890 1.00 61.39 ? 809 NAG A O6 1 HETATM 4008 O O7 . NAG J 2 . ? 39.894 -21.267 -100.926 1.00 52.57 ? 809 NAG A O7 1 HETATM 4009 C C1 . NAG K 2 . ? 39.905 -16.910 -106.310 1.00 69.56 ? 810 NAG A C1 1 HETATM 4010 C C2 . NAG K 2 . ? 40.621 -16.037 -107.345 1.00 72.17 ? 810 NAG A C2 1 HETATM 4011 C C3 . NAG K 2 . ? 40.411 -16.525 -108.779 1.00 75.80 ? 810 NAG A C3 1 HETATM 4012 C C4 . NAG K 2 . ? 40.565 -18.041 -108.879 1.00 79.75 ? 810 NAG A C4 1 HETATM 4013 C C5 . NAG K 2 . ? 39.658 -18.701 -107.839 1.00 78.32 ? 810 NAG A C5 1 HETATM 4014 C C6 . NAG K 2 . ? 39.638 -20.231 -107.911 1.00 77.86 ? 810 NAG A C6 1 HETATM 4015 C C7 . NAG K 2 . ? 40.937 -13.665 -106.766 1.00 67.44 ? 810 NAG A C7 1 HETATM 4016 C C8 . NAG K 2 . ? 40.295 -12.313 -106.662 1.00 66.28 ? 810 NAG A C8 1 HETATM 4017 N N2 . NAG K 2 . ? 40.160 -14.662 -107.192 1.00 70.21 ? 810 NAG A N2 1 HETATM 4018 O O3 . NAG K 2 . ? 41.348 -15.901 -109.626 1.00 74.96 ? 810 NAG A O3 1 HETATM 4019 O O4 . NAG K 2 . ? 40.269 -18.471 -110.194 1.00 82.23 ? 810 NAG A O4 1 HETATM 4020 O O5 . NAG K 2 . ? 40.116 -18.287 -106.565 1.00 73.77 ? 810 NAG A O5 1 HETATM 4021 O O6 . NAG K 2 . ? 40.845 -20.779 -107.423 1.00 75.32 ? 810 NAG A O6 1 HETATM 4022 O O7 . NAG K 2 . ? 42.121 -13.804 -106.470 1.00 67.62 ? 810 NAG A O7 1 HETATM 4023 C C1 . NAG L 2 . ? 33.805 -45.487 -56.695 1.00 38.79 ? 812 NAG A C1 1 HETATM 4024 C C2 . NAG L 2 . ? 34.141 -46.631 -55.731 1.00 45.03 ? 812 NAG A C2 1 HETATM 4025 C C3 . NAG L 2 . ? 35.607 -47.047 -55.870 1.00 48.57 ? 812 NAG A C3 1 HETATM 4026 C C4 . NAG L 2 . ? 36.031 -47.134 -57.331 1.00 50.38 ? 812 NAG A C4 1 HETATM 4027 C C5 . NAG L 2 . ? 35.619 -45.861 -58.083 1.00 50.96 ? 812 NAG A C5 1 HETATM 4028 C C6 . NAG L 2 . ? 36.058 -45.826 -59.546 1.00 51.92 ? 812 NAG A C6 1 HETATM 4029 C C7 . NAG L 2 . ? 32.694 -46.654 -53.730 1.00 45.80 ? 812 NAG A C7 1 HETATM 4030 C C8 . NAG L 2 . ? 32.505 -46.342 -52.272 1.00 43.38 ? 812 NAG A C8 1 HETATM 4031 N N2 . NAG L 2 . ? 33.871 -46.335 -54.314 1.00 44.02 ? 812 NAG A N2 1 HETATM 4032 O O3 . NAG L 2 . ? 35.806 -48.265 -55.179 1.00 50.82 ? 812 NAG A O3 1 HETATM 4033 O O4 . NAG L 2 . ? 37.436 -47.242 -57.355 1.00 57.23 ? 812 NAG A O4 1 HETATM 4034 O O5 . NAG L 2 . ? 34.211 -45.717 -58.015 1.00 44.98 ? 812 NAG A O5 1 HETATM 4035 O O6 . NAG L 2 . ? 35.577 -46.966 -60.214 1.00 56.47 ? 812 NAG A O6 1 HETATM 4036 O O7 . NAG L 2 . ? 31.752 -47.167 -54.340 1.00 45.98 ? 812 NAG A O7 1 HETATM 4037 C C1 . NAG M 2 . ? 24.719 -25.516 -2.267 1.00 74.04 ? 813 NAG A C1 1 HETATM 4038 C C2 . NAG M 2 . ? 24.323 -27.007 -2.250 1.00 84.10 ? 813 NAG A C2 1 HETATM 4039 C C3 . NAG M 2 . ? 23.649 -27.404 -0.937 1.00 80.75 ? 813 NAG A C3 1 HETATM 4040 C C4 . NAG M 2 . ? 24.590 -26.983 0.186 1.00 78.46 ? 813 NAG A C4 1 HETATM 4041 C C5 . NAG M 2 . ? 24.765 -25.463 0.129 1.00 77.76 ? 813 NAG A C5 1 HETATM 4042 C C6 . NAG M 2 . ? 25.522 -24.977 1.370 1.00 78.12 ? 813 NAG A C6 1 HETATM 4043 C C7 . NAG M 2 . ? 23.873 -28.243 -4.329 1.00 96.51 ? 813 NAG A C7 1 HETATM 4044 C C8 . NAG M 2 . ? 22.883 -28.501 -5.431 1.00 95.60 ? 813 NAG A C8 1 HETATM 4045 N N2 . NAG M 2 . ? 23.485 -27.372 -3.388 1.00 90.26 ? 813 NAG A N2 1 HETATM 4046 O O3 . NAG M 2 . ? 23.402 -28.793 -0.897 1.00 77.94 ? 813 NAG A O3 1 HETATM 4047 O O4 . NAG M 2 . ? 24.157 -27.457 1.446 1.00 71.88 ? 813 NAG A O4 1 HETATM 4048 O O5 . NAG M 2 . ? 25.426 -25.120 -1.092 1.00 75.01 ? 813 NAG A O5 1 HETATM 4049 O O6 . NAG M 2 . ? 25.764 -23.588 1.334 1.00 84.41 ? 813 NAG A O6 1 HETATM 4050 O O7 . NAG M 2 . ? 24.969 -28.819 -4.328 1.00 97.25 ? 813 NAG A O7 1 HETATM 4051 N N1 . EPE N 4 . ? 17.796 -30.011 -89.014 1.00 82.49 ? 1504 EPE A N1 1 HETATM 4052 C C2 . EPE N 4 . ? 17.109 -30.605 -90.167 1.00 79.18 ? 1504 EPE A C2 1 HETATM 4053 C C3 . EPE N 4 . ? 18.172 -31.385 -90.925 1.00 75.91 ? 1504 EPE A C3 1 HETATM 4054 N N4 . EPE N 4 . ? 19.354 -30.565 -91.301 1.00 69.41 ? 1504 EPE A N4 1 HETATM 4055 C C5 . EPE N 4 . ? 19.789 -29.535 -90.325 1.00 70.89 ? 1504 EPE A C5 1 HETATM 4056 C C6 . EPE N 4 . ? 18.653 -28.922 -89.508 1.00 75.60 ? 1504 EPE A C6 1 HETATM 4057 C C7 . EPE N 4 . ? 20.469 -31.493 -91.569 1.00 59.82 ? 1504 EPE A C7 1 HETATM 4058 C C8 . EPE N 4 . ? 21.521 -30.803 -92.419 1.00 55.72 ? 1504 EPE A C8 1 HETATM 4059 O O8 . EPE N 4 . ? 22.608 -30.317 -91.609 1.00 38.48 ? 1504 EPE A O8 1 HETATM 4060 C C9 . EPE N 4 . ? 16.837 -29.566 -87.996 1.00 90.11 ? 1504 EPE A C9 1 HETATM 4061 C C10 . EPE N 4 . ? 16.483 -30.778 -87.139 1.00 94.96 ? 1504 EPE A C10 1 HETATM 4062 S S . EPE N 4 . ? 15.945 -30.330 -85.632 1.00 104.45 ? 1504 EPE A S 1 HETATM 4063 O O1S . EPE N 4 . ? 17.031 -30.474 -84.704 1.00 105.49 ? 1504 EPE A O1S 1 HETATM 4064 O O2S . EPE N 4 . ? 14.857 -31.191 -85.252 1.00 102.63 ? 1504 EPE A O2S 1 HETATM 4065 O O3S . EPE N 4 . ? 15.428 -28.773 -85.615 1.00 104.51 ? 1504 EPE A O3S 1 HETATM 4066 N N1 . EPE O 4 . ? 35.082 -40.978 -81.505 1.00 58.51 ? 1505 EPE A N1 1 HETATM 4067 C C2 . EPE O 4 . ? 36.548 -40.867 -81.406 1.00 61.79 ? 1505 EPE A C2 1 HETATM 4068 C C3 . EPE O 4 . ? 36.992 -40.906 -79.943 1.00 62.61 ? 1505 EPE A C3 1 HETATM 4069 N N4 . EPE O 4 . ? 36.324 -39.867 -79.138 1.00 62.04 ? 1505 EPE A N4 1 HETATM 4070 C C5 . EPE O 4 . ? 34.861 -39.887 -79.351 1.00 62.28 ? 1505 EPE A C5 1 HETATM 4071 C C6 . EPE O 4 . ? 34.498 -39.810 -80.832 1.00 60.79 ? 1505 EPE A C6 1 HETATM 4072 C C7 . EPE O 4 . ? 36.564 -40.088 -77.694 1.00 67.34 ? 1505 EPE A C7 1 HETATM 4073 C C8 . EPE O 4 . ? 38.050 -40.101 -77.331 1.00 68.35 ? 1505 EPE A C8 1 HETATM 4074 O O8 . EPE O 4 . ? 38.758 -39.108 -78.085 1.00 72.77 ? 1505 EPE A O8 1 HETATM 4075 C C9 . EPE O 4 . ? 34.737 -41.130 -82.939 1.00 54.66 ? 1505 EPE A C9 1 HETATM 4076 C C10 . EPE O 4 . ? 33.278 -40.829 -83.283 1.00 51.11 ? 1505 EPE A C10 1 HETATM 4077 S S . EPE O 4 . ? 32.808 -41.630 -84.692 1.00 47.61 ? 1505 EPE A S 1 HETATM 4078 O O1S . EPE O 4 . ? 33.931 -41.821 -85.570 1.00 45.07 ? 1505 EPE A O1S 1 HETATM 4079 O O2S . EPE O 4 . ? 31.797 -40.834 -85.324 1.00 42.01 ? 1505 EPE A O2S 1 HETATM 4080 O O3S . EPE O 4 . ? 32.200 -43.073 -84.207 1.00 45.88 ? 1505 EPE A O3S 1 HETATM 4081 N N1 . EPE P 4 . ? 17.358 -19.364 -79.618 1.00 66.03 ? 1506 EPE A N1 1 HETATM 4082 C C2 . EPE P 4 . ? 16.070 -18.841 -79.108 1.00 66.52 ? 1506 EPE A C2 1 HETATM 4083 C C3 . EPE P 4 . ? 16.171 -18.537 -77.613 1.00 66.07 ? 1506 EPE A C3 1 HETATM 4084 N N4 . EPE P 4 . ? 16.524 -19.764 -76.853 1.00 67.19 ? 1506 EPE A N4 1 HETATM 4085 C C5 . EPE P 4 . ? 17.798 -20.326 -77.368 1.00 64.88 ? 1506 EPE A C5 1 HETATM 4086 C C6 . EPE P 4 . ? 17.736 -20.581 -78.878 1.00 63.50 ? 1506 EPE A C6 1 HETATM 4087 C C7 . EPE P 4 . ? 16.523 -19.444 -75.400 1.00 63.97 ? 1506 EPE A C7 1 HETATM 4088 C C8 . EPE P 4 . ? 17.427 -20.299 -74.511 1.00 63.56 ? 1506 EPE A C8 1 HETATM 4089 O O8 . EPE P 4 . ? 16.898 -21.617 -74.409 1.00 57.83 ? 1506 EPE A O8 1 HETATM 4090 C C9 . EPE P 4 . ? 17.276 -19.678 -81.057 1.00 62.24 ? 1506 EPE A C9 1 HETATM 4091 C C10 . EPE P 4 . ? 17.654 -18.446 -81.870 1.00 64.55 ? 1506 EPE A C10 1 HETATM 4092 S S . EPE P 4 . ? 17.421 -18.667 -83.511 1.00 64.82 ? 1506 EPE A S 1 HETATM 4093 O O1S . EPE P 4 . ? 17.298 -17.371 -84.119 1.00 63.82 ? 1506 EPE A O1S 1 HETATM 4094 O O2S . EPE P 4 . ? 16.226 -19.443 -83.760 1.00 61.65 ? 1506 EPE A O2S 1 HETATM 4095 O O3S . EPE P 4 . ? 18.688 -19.476 -84.132 1.00 54.95 ? 1506 EPE A O3S 1 HETATM 4096 C C . TAM Q 5 . ? 40.095 -26.131 -40.697 1.00 63.85 ? 1507 TAM A C 1 HETATM 4097 C C1 . TAM Q 5 . ? 41.344 -25.688 -39.922 1.00 60.76 ? 1507 TAM A C1 1 HETATM 4098 C C2 . TAM Q 5 . ? 40.062 -27.656 -40.866 1.00 62.93 ? 1507 TAM A C2 1 HETATM 4099 C C3 . TAM Q 5 . ? 39.984 -25.421 -42.060 1.00 64.97 ? 1507 TAM A C3 1 HETATM 4100 C C4 . TAM Q 5 . ? 41.603 -26.519 -38.670 1.00 59.99 ? 1507 TAM A C4 1 HETATM 4101 C C5 . TAM Q 5 . ? 39.159 -28.194 -41.983 1.00 62.85 ? 1507 TAM A C5 1 HETATM 4102 C C6 . TAM Q 5 . ? 40.480 -23.985 -42.062 1.00 65.71 ? 1507 TAM A C6 1 HETATM 4103 N N . TAM Q 5 . ? 38.945 -25.757 -39.875 1.00 65.43 ? 1507 TAM A N 1 HETATM 4104 O O4 . TAM Q 5 . ? 42.326 -25.731 -37.727 1.00 62.28 ? 1507 TAM A O4 1 HETATM 4105 O O5 . TAM Q 5 . ? 39.893 -28.466 -43.187 1.00 63.94 ? 1507 TAM A O5 1 HETATM 4106 O O6 . TAM Q 5 . ? 39.914 -23.279 -43.170 1.00 69.32 ? 1507 TAM A O6 1 HETATM 4107 O O . HOH R 6 . ? 35.659 -35.365 14.082 1.00 43.54 ? 2001 HOH A O 1 HETATM 4108 O O . HOH R 6 . ? 36.071 -38.551 17.124 1.00 59.05 ? 2002 HOH A O 1 HETATM 4109 O O . HOH R 6 . ? 31.004 -37.757 8.690 1.00 32.80 ? 2003 HOH A O 1 HETATM 4110 O O . HOH R 6 . ? 37.821 -44.262 2.131 1.00 57.17 ? 2004 HOH A O 1 HETATM 4111 O O . HOH R 6 . ? 43.810 -42.710 -15.924 1.00 36.32 ? 2005 HOH A O 1 HETATM 4112 O O . HOH R 6 . ? 36.866 -41.881 -11.659 1.00 27.15 ? 2006 HOH A O 1 HETATM 4113 O O . HOH R 6 . ? 37.040 -43.228 -18.354 1.00 25.92 ? 2007 HOH A O 1 HETATM 4114 O O . HOH R 6 . ? 41.425 -41.801 -14.791 1.00 47.87 ? 2008 HOH A O 1 HETATM 4115 O O . HOH R 6 . ? 33.708 -38.502 -22.205 1.00 24.07 ? 2009 HOH A O 1 HETATM 4116 O O . HOH R 6 . ? 34.908 -50.358 -23.780 1.00 48.03 ? 2010 HOH A O 1 HETATM 4117 O O . HOH R 6 . ? 28.045 -34.970 -25.977 1.00 52.80 ? 2011 HOH A O 1 HETATM 4118 O O . HOH R 6 . ? 32.393 -45.740 -28.010 1.00 44.43 ? 2012 HOH A O 1 HETATM 4119 O O . HOH R 6 . ? 37.525 -49.217 -31.545 1.00 37.40 ? 2013 HOH A O 1 HETATM 4120 O O . HOH R 6 . ? 41.988 -41.609 -34.696 1.00 20.85 ? 2014 HOH A O 1 HETATM 4121 O O . HOH R 6 . ? 50.579 -41.622 -33.074 1.00 48.40 ? 2015 HOH A O 1 HETATM 4122 O O . HOH R 6 . ? 46.835 -39.900 -25.748 1.00 29.73 ? 2016 HOH A O 1 HETATM 4123 O O . HOH R 6 . ? 22.544 -21.978 -66.107 1.00 29.63 ? 2017 HOH A O 1 HETATM 4124 O O . HOH R 6 . ? 18.427 -34.180 -73.285 1.00 46.47 ? 2018 HOH A O 1 HETATM 4125 O O . HOH R 6 . ? 53.989 -44.979 -28.310 1.00 47.27 ? 2019 HOH A O 1 HETATM 4126 O O . HOH R 6 . ? 47.902 -41.598 -22.790 1.00 53.85 ? 2020 HOH A O 1 HETATM 4127 O O . HOH R 6 . ? 50.672 -46.316 -22.799 1.00 55.56 ? 2021 HOH A O 1 HETATM 4128 O O . HOH R 6 . ? 49.229 -46.964 -28.443 1.00 48.10 ? 2022 HOH A O 1 HETATM 4129 O O . HOH R 6 . ? 54.400 -46.559 -33.451 1.00 42.56 ? 2023 HOH A O 1 HETATM 4130 O O . HOH R 6 . ? 46.440 -46.989 -24.425 1.00 54.35 ? 2024 HOH A O 1 HETATM 4131 O O . HOH R 6 . ? 44.104 -49.643 -27.011 1.00 49.93 ? 2025 HOH A O 1 HETATM 4132 O O . HOH R 6 . ? 49.073 -49.659 -32.546 1.00 62.46 ? 2026 HOH A O 1 HETATM 4133 O O . HOH R 6 . ? 43.243 -47.105 -23.978 1.00 33.30 ? 2027 HOH A O 1 HETATM 4134 O O . HOH R 6 . ? 41.883 -45.346 -22.226 1.00 33.57 ? 2028 HOH A O 1 HETATM 4135 O O . HOH R 6 . ? 31.014 -39.838 -24.063 1.00 51.30 ? 2029 HOH A O 1 HETATM 4136 O O . HOH R 6 . ? 29.958 -42.960 -32.017 1.00 52.45 ? 2030 HOH A O 1 HETATM 4137 O O . HOH R 6 . ? 30.511 -37.970 -26.514 1.00 34.94 ? 2031 HOH A O 1 HETATM 4138 O O . HOH R 6 . ? 29.592 -41.123 -33.930 1.00 60.91 ? 2032 HOH A O 1 HETATM 4139 O O . HOH R 6 . ? 23.358 -45.140 -68.411 1.00 47.89 ? 2033 HOH A O 1 HETATM 4140 O O . HOH R 6 . ? 30.777 -38.115 -38.252 1.00 33.55 ? 2034 HOH A O 1 HETATM 4141 O O . HOH R 6 . ? 30.742 -41.947 -36.725 1.00 32.29 ? 2035 HOH A O 1 HETATM 4142 O O . HOH R 6 . ? 26.546 -49.171 -79.463 1.00 72.44 ? 2036 HOH A O 1 HETATM 4143 O O . HOH R 6 . ? 34.933 -44.246 -43.253 1.00 22.89 ? 2037 HOH A O 1 HETATM 4144 O O . HOH R 6 . ? 33.763 -45.582 -39.015 1.00 42.97 ? 2038 HOH A O 1 HETATM 4145 O O . HOH R 6 . ? 32.605 -44.297 -79.321 1.00 58.85 ? 2039 HOH A O 1 HETATM 4146 O O . HOH R 6 . ? 26.712 -38.983 -43.560 1.00 44.11 ? 2040 HOH A O 1 HETATM 4147 O O . HOH R 6 . ? 26.995 -41.551 -44.265 1.00 39.97 ? 2041 HOH A O 1 HETATM 4148 O O . HOH R 6 . ? 30.238 -36.626 -45.381 1.00 28.37 ? 2042 HOH A O 1 HETATM 4149 O O . HOH R 6 . ? 31.028 -43.263 -44.240 1.00 34.19 ? 2043 HOH A O 1 HETATM 4150 O O . HOH R 6 . ? 42.654 -27.760 -84.181 1.00 40.50 ? 2044 HOH A O 1 HETATM 4151 O O . HOH R 6 . ? 41.175 -36.898 -75.237 1.00 40.80 ? 2045 HOH A O 1 HETATM 4152 O O . HOH R 6 . ? 35.039 -46.000 -49.928 1.00 50.25 ? 2046 HOH A O 1 HETATM 4153 O O . HOH R 6 . ? 41.285 -35.923 -70.902 1.00 24.20 ? 2047 HOH A O 1 HETATM 4154 O O . HOH R 6 . ? 38.482 -36.466 -74.146 1.00 28.59 ? 2048 HOH A O 1 HETATM 4155 O O . HOH R 6 . ? 26.046 -42.938 -48.365 1.00 46.30 ? 2049 HOH A O 1 HETATM 4156 O O . HOH R 6 . ? 37.150 -22.848 -70.665 1.00 28.85 ? 2050 HOH A O 1 HETATM 4157 O O . HOH R 6 . ? 28.730 -47.080 -50.880 1.00 45.69 ? 2051 HOH A O 1 HETATM 4158 O O . HOH R 6 . ? 26.089 -47.815 -49.593 1.00 63.11 ? 2052 HOH A O 1 HETATM 4159 O O . HOH R 6 . ? 35.147 -19.284 -68.764 1.00 47.32 ? 2053 HOH A O 1 HETATM 4160 O O . HOH R 6 . ? 25.062 -41.214 -50.715 1.00 47.68 ? 2054 HOH A O 1 HETATM 4161 O O . HOH R 6 . ? 22.944 -40.470 -49.321 1.00 52.48 ? 2055 HOH A O 1 HETATM 4162 O O . HOH R 6 . ? 26.099 -46.357 -59.263 1.00 55.53 ? 2056 HOH A O 1 HETATM 4163 O O . HOH R 6 . ? 16.370 -20.488 -90.196 1.00 63.71 ? 2057 HOH A O 1 HETATM 4164 O O . HOH R 6 . ? 23.506 -34.552 -56.147 1.00 27.87 ? 2058 HOH A O 1 HETATM 4165 O O . HOH R 6 . ? 21.940 -31.978 -58.352 1.00 23.49 ? 2059 HOH A O 1 HETATM 4166 O O . HOH R 6 . ? 18.617 -31.393 -62.326 1.00 20.14 ? 2060 HOH A O 1 HETATM 4167 O O . HOH R 6 . ? 14.260 -33.931 -56.831 1.00 40.69 ? 2061 HOH A O 1 HETATM 4168 O O . HOH R 6 . ? 13.315 -33.308 -60.606 1.00 45.38 ? 2062 HOH A O 1 HETATM 4169 O O . HOH R 6 . ? 15.444 -36.824 -62.016 1.00 42.06 ? 2063 HOH A O 1 HETATM 4170 O O . HOH R 6 . ? 18.989 -26.041 -59.825 1.00 24.50 ? 2064 HOH A O 1 HETATM 4171 O O . HOH R 6 . ? 24.511 -25.441 -58.752 1.00 35.89 ? 2065 HOH A O 1 HETATM 4172 O O . HOH R 6 . ? 27.366 -27.697 -53.743 1.00 32.19 ? 2066 HOH A O 1 HETATM 4173 O O . HOH R 6 . ? 19.992 -23.052 -66.441 1.00 27.84 ? 2067 HOH A O 1 HETATM 4174 O O . HOH R 6 . ? 22.582 -24.357 -64.507 1.00 29.49 ? 2068 HOH A O 1 HETATM 4175 O O . HOH R 6 . ? 16.823 -28.984 -66.041 1.00 23.68 ? 2069 HOH A O 1 HETATM 4176 O O . HOH R 6 . ? 19.167 -29.173 -68.869 1.00 37.33 ? 2070 HOH A O 1 HETATM 4177 O O . HOH R 6 . ? 17.452 -33.079 -63.805 1.00 38.85 ? 2071 HOH A O 1 HETATM 4178 O O . HOH R 6 . ? 18.393 -31.072 -67.130 1.00 39.78 ? 2072 HOH A O 1 HETATM 4179 O O . HOH R 6 . ? 18.912 -35.103 -68.195 1.00 31.49 ? 2073 HOH A O 1 HETATM 4180 O O . HOH R 6 . ? 18.561 -36.494 -70.653 1.00 35.68 ? 2074 HOH A O 1 HETATM 4181 O O . HOH R 6 . ? 20.641 -42.514 -68.148 1.00 37.13 ? 2075 HOH A O 1 HETATM 4182 O O . HOH R 6 . ? 18.229 -39.392 -66.494 1.00 33.82 ? 2076 HOH A O 1 HETATM 4183 O O . HOH R 6 . ? 26.081 -39.838 -72.207 1.00 25.38 ? 2077 HOH A O 1 HETATM 4184 O O . HOH R 6 . ? 20.331 -40.121 -75.984 1.00 37.89 ? 2078 HOH A O 1 HETATM 4185 O O . HOH R 6 . ? 25.008 -39.169 -80.239 1.00 40.79 ? 2079 HOH A O 1 HETATM 4186 O O . HOH R 6 . ? 31.909 -37.651 -78.947 1.00 31.51 ? 2080 HOH A O 1 HETATM 4187 O O . HOH R 6 . ? 32.107 -34.990 -75.370 1.00 24.30 ? 2081 HOH A O 1 HETATM 4188 O O . HOH R 6 . ? 27.750 -37.938 -83.749 1.00 33.22 ? 2082 HOH A O 1 HETATM 4189 O O . HOH R 6 . ? 30.196 -40.527 -79.252 1.00 49.04 ? 2083 HOH A O 1 HETATM 4190 O O . HOH R 6 . ? 34.166 -17.214 -72.401 1.00 36.35 ? 2084 HOH A O 1 HETATM 4191 O O . HOH R 6 . ? 21.658 -31.525 -80.275 1.00 28.73 ? 2085 HOH A O 1 HETATM 4192 O O . HOH R 6 . ? 23.546 -28.340 -80.660 1.00 28.32 ? 2086 HOH A O 1 HETATM 4193 O O . HOH R 6 . ? 21.521 -40.359 -84.521 1.00 41.03 ? 2087 HOH A O 1 HETATM 4194 O O . HOH R 6 . ? 17.456 -36.255 -78.180 1.00 44.11 ? 2088 HOH A O 1 HETATM 4195 O O . HOH R 6 . ? 14.809 -30.129 -80.043 1.00 40.41 ? 2089 HOH A O 1 HETATM 4196 O O . HOH R 6 . ? 20.428 -31.265 -82.860 1.00 32.04 ? 2090 HOH A O 1 HETATM 4197 O O . HOH R 6 . ? 14.181 -32.989 -74.894 1.00 36.32 ? 2091 HOH A O 1 HETATM 4198 O O . HOH R 6 . ? 21.976 -26.480 -79.297 1.00 26.85 ? 2092 HOH A O 1 HETATM 4199 O O . HOH R 6 . ? 18.331 -22.891 -72.148 1.00 32.21 ? 2093 HOH A O 1 HETATM 4200 O O . HOH R 6 . ? 18.745 -23.138 -81.714 1.00 37.23 ? 2094 HOH A O 1 HETATM 4201 O O . HOH R 6 . ? 17.190 -32.855 -68.576 1.00 36.99 ? 2095 HOH A O 1 HETATM 4202 O O . HOH R 6 . ? 16.280 -27.799 -69.654 1.00 31.39 ? 2096 HOH A O 1 HETATM 4203 O O . HOH R 6 . ? 49.186 -31.595 -98.570 1.00 41.84 ? 2097 HOH A O 1 HETATM 4204 O O . HOH R 6 . ? 50.459 -29.132 -97.560 0.33 60.24 ? 2098 HOH A O 1 HETATM 4205 O O . HOH R 6 . ? 24.762 -23.090 -67.332 1.00 30.09 ? 2099 HOH A O 1 HETATM 4206 O O . HOH R 6 . ? 23.970 -22.819 -61.320 1.00 33.27 ? 2100 HOH A O 1 HETATM 4207 O O . HOH R 6 . ? 26.740 -23.451 -63.611 1.00 45.20 ? 2101 HOH A O 1 HETATM 4208 O O . HOH R 6 . ? 21.330 -24.786 -60.489 1.00 33.85 ? 2102 HOH A O 1 HETATM 4209 O O . HOH R 6 . ? 31.404 -42.216 -69.449 1.00 42.72 ? 2103 HOH A O 1 HETATM 4210 O O . HOH R 6 . ? 33.176 -39.400 -72.165 1.00 37.30 ? 2104 HOH A O 1 HETATM 4211 O O . HOH R 6 . ? 44.735 -29.056 -85.389 1.00 41.90 ? 2105 HOH A O 1 HETATM 4212 O O . HOH R 6 . ? 30.734 -41.451 -72.929 1.00 40.74 ? 2106 HOH A O 1 HETATM 4213 O O . HOH R 6 . ? 26.204 -46.261 -69.552 1.00 31.32 ? 2107 HOH A O 1 HETATM 4214 O O . HOH R 6 . ? 31.126 -44.854 -75.009 1.00 48.58 ? 2108 HOH A O 1 HETATM 4215 O O . HOH R 6 . ? 27.728 -48.336 -76.702 1.00 51.82 ? 2109 HOH A O 1 HETATM 4216 O O . HOH R 6 . ? 19.986 -47.367 -73.059 1.00 59.59 ? 2110 HOH A O 1 HETATM 4217 O O . HOH R 6 . ? 31.190 -42.488 -75.364 1.00 46.22 ? 2111 HOH A O 1 HETATM 4218 O O . HOH R 6 . ? 30.701 -43.694 -81.302 1.00 50.28 ? 2112 HOH A O 1 HETATM 4219 O O . HOH R 6 . ? 22.231 -42.659 -88.449 1.00 46.05 ? 2113 HOH A O 1 HETATM 4220 O O . HOH R 6 . ? 28.729 -39.366 -85.936 1.00 35.27 ? 2114 HOH A O 1 HETATM 4221 O O . HOH R 6 . ? 29.961 -40.097 -97.697 1.00 37.45 ? 2115 HOH A O 1 HETATM 4222 O O . HOH R 6 . ? 37.955 -42.064 -68.821 1.00 47.03 ? 2116 HOH A O 1 HETATM 4223 O O . HOH R 6 . ? 39.650 -40.217 -86.981 1.00 43.91 ? 2117 HOH A O 1 HETATM 4224 O O . HOH R 6 . ? 38.255 -37.097 -81.952 1.00 31.45 ? 2118 HOH A O 1 HETATM 4225 O O . HOH R 6 . ? 41.645 -36.378 -82.344 1.00 49.58 ? 2119 HOH A O 1 HETATM 4226 O O . HOH R 6 . ? 42.391 -35.201 -79.698 1.00 42.18 ? 2120 HOH A O 1 HETATM 4227 O O . HOH R 6 . ? 39.988 -29.002 -83.596 1.00 35.50 ? 2121 HOH A O 1 HETATM 4228 O O . HOH R 6 . ? 23.049 -36.688 -48.469 1.00 47.86 ? 2122 HOH A O 1 HETATM 4229 O O . HOH R 6 . ? 44.079 -32.833 -75.822 1.00 28.97 ? 2123 HOH A O 1 HETATM 4230 O O . HOH R 6 . ? 42.025 -34.611 -76.953 1.00 30.66 ? 2124 HOH A O 1 HETATM 4231 O O . HOH R 6 . ? 33.935 -38.480 -74.846 1.00 44.35 ? 2125 HOH A O 1 HETATM 4232 O O . HOH R 6 . ? 37.691 -32.896 -71.623 1.00 21.03 ? 2126 HOH A O 1 HETATM 4233 O O . HOH R 6 . ? 34.869 -35.872 -67.338 1.00 24.22 ? 2127 HOH A O 1 HETATM 4234 O O . HOH R 6 . ? 38.714 -35.423 -71.648 1.00 21.74 ? 2128 HOH A O 1 HETATM 4235 O O . HOH R 6 . ? 37.470 -31.506 -69.083 1.00 24.40 ? 2129 HOH A O 1 HETATM 4236 O O . HOH R 6 . ? 49.711 -41.083 -60.548 1.00 46.55 ? 2130 HOH A O 1 HETATM 4237 O O . HOH R 6 . ? 34.735 -22.261 -71.505 1.00 24.81 ? 2131 HOH A O 1 HETATM 4238 O O . HOH R 6 . ? 29.221 -22.291 -66.234 1.00 29.98 ? 2132 HOH A O 1 HETATM 4239 O O . HOH R 6 . ? 33.148 -23.951 -65.070 1.00 26.00 ? 2133 HOH A O 1 HETATM 4240 O O . HOH R 6 . ? 33.269 -20.992 -67.163 1.00 36.91 ? 2134 HOH A O 1 HETATM 4241 O O . HOH R 6 . ? 26.023 -21.080 -68.730 1.00 51.66 ? 2135 HOH A O 1 HETATM 4242 O O . HOH R 6 . ? 28.767 -22.992 -74.865 1.00 37.77 ? 2136 HOH A O 1 HETATM 4243 O O . HOH R 6 . ? 45.301 -45.236 -43.315 1.00 47.41 ? 2137 HOH A O 1 HETATM 4244 O O . HOH R 6 . ? 41.639 -38.121 -15.621 1.00 55.64 ? 2138 HOH A O 1 HETATM 4245 O O . HOH R 6 . ? 19.432 -16.999 -89.542 1.00 57.79 ? 2139 HOH A O 1 HETATM 4246 O O . HOH R 6 . ? 21.387 -20.806 -89.860 1.00 41.09 ? 2140 HOH A O 1 HETATM 4247 O O . HOH R 6 . ? 20.975 -25.178 -86.453 1.00 35.81 ? 2141 HOH A O 1 HETATM 4248 O O . HOH R 6 . ? 17.871 -23.607 -84.637 1.00 54.07 ? 2142 HOH A O 1 HETATM 4249 O O . HOH R 6 . ? 24.675 -12.451 -87.154 1.00 42.69 ? 2143 HOH A O 1 HETATM 4250 O O . HOH R 6 . ? 22.513 -13.589 -89.755 1.00 47.29 ? 2144 HOH A O 1 HETATM 4251 O O . HOH R 6 . ? 27.906 -14.089 -95.270 1.00 44.37 ? 2145 HOH A O 1 HETATM 4252 O O . HOH R 6 . ? 25.205 -22.284 -92.892 1.00 34.99 ? 2146 HOH A O 1 HETATM 4253 O O . HOH R 6 . ? 24.787 -30.322 -100.309 1.00 41.20 ? 2147 HOH A O 1 HETATM 4254 O O . HOH R 6 . ? 21.753 -20.844 -94.622 1.00 46.54 ? 2148 HOH A O 1 HETATM 4255 O O . HOH R 6 . ? 23.619 -36.288 -0.386 1.00 53.77 ? 2149 HOH A O 1 HETATM 4256 O O . HOH R 6 . ? 23.944 -30.243 -94.278 1.00 31.89 ? 2150 HOH A O 1 HETATM 4257 O O . HOH R 6 . ? 21.450 -38.333 -98.852 1.00 50.77 ? 2151 HOH A O 1 HETATM 4258 O O . HOH R 6 . ? 26.134 -35.554 -100.043 1.00 60.03 ? 2152 HOH A O 1 HETATM 4259 O O . HOH R 6 . ? 27.278 -40.420 -97.097 1.00 40.91 ? 2153 HOH A O 1 HETATM 4260 O O . HOH R 6 . ? 24.178 -41.003 -98.528 1.00 51.19 ? 2154 HOH A O 1 HETATM 4261 O O . HOH R 6 . ? 25.414 -45.529 -94.858 1.00 52.61 ? 2155 HOH A O 1 HETATM 4262 O O . HOH R 6 . ? 15.889 -42.069 -88.092 1.00 57.04 ? 2156 HOH A O 1 HETATM 4263 O O . HOH R 6 . ? 15.705 -38.638 -85.445 1.00 57.75 ? 2157 HOH A O 1 HETATM 4264 O O . HOH R 6 . ? 34.177 -21.782 -61.202 1.00 56.49 ? 2158 HOH A O 1 HETATM 4265 O O . HOH R 6 . ? 38.566 -22.051 -62.305 1.00 45.99 ? 2159 HOH A O 1 HETATM 4266 O O . HOH R 6 . ? 49.034 -44.701 -69.183 1.00 42.44 ? 2160 HOH A O 1 HETATM 4267 O O . HOH R 6 . ? 16.263 -40.575 -97.019 1.00 59.21 ? 2161 HOH A O 1 HETATM 4268 O O . HOH R 6 . ? 16.535 -36.250 -96.826 1.00 50.03 ? 2162 HOH A O 1 HETATM 4269 O O . HOH R 6 . ? 51.984 -39.530 -60.874 1.00 29.20 ? 2163 HOH A O 1 HETATM 4270 O O . HOH R 6 . ? 28.128 -25.037 -86.094 1.00 34.66 ? 2164 HOH A O 1 HETATM 4271 O O . HOH R 6 . ? 49.817 -32.358 -29.499 1.00 44.37 ? 2165 HOH A O 1 HETATM 4272 O O . HOH R 6 . ? 31.818 -27.735 -98.901 1.00 33.49 ? 2166 HOH A O 1 HETATM 4273 O O . HOH R 6 . ? 25.787 -31.095 -105.227 1.00 41.30 ? 2167 HOH A O 1 HETATM 4274 O O . HOH R 6 . ? 47.457 -27.830 -27.123 1.00 41.43 ? 2168 HOH A O 1 HETATM 4275 O O . HOH R 6 . ? 50.064 -29.104 -27.746 0.33 53.39 ? 2169 HOH A O 1 HETATM 4276 O O . HOH R 6 . ? 27.222 -33.461 -105.143 1.00 50.91 ? 2170 HOH A O 1 HETATM 4277 O O . HOH R 6 . ? 36.637 -23.500 -5.482 1.00 55.09 ? 2171 HOH A O 1 HETATM 4278 O O . HOH R 6 . ? 33.741 -25.009 -109.888 1.00 49.75 ? 2172 HOH A O 1 HETATM 4279 O O . HOH R 6 . ? 37.338 -21.444 -0.766 1.00 38.56 ? 2173 HOH A O 1 HETATM 4280 O O . HOH R 6 . ? 31.857 -15.902 -101.449 1.00 41.51 ? 2174 HOH A O 1 HETATM 4281 O O . HOH R 6 . ? 31.901 -13.236 -101.291 1.00 51.60 ? 2175 HOH A O 1 HETATM 4282 O O . HOH R 6 . ? 32.879 -11.346 -98.145 1.00 50.85 ? 2176 HOH A O 1 HETATM 4283 O O . HOH R 6 . ? 34.409 -12.037 -102.001 1.00 52.84 ? 2177 HOH A O 1 HETATM 4284 O O . HOH R 6 . ? 29.678 -12.542 -97.081 1.00 44.93 ? 2178 HOH A O 1 HETATM 4285 O O . HOH R 6 . ? 27.134 -10.976 -93.368 1.00 53.55 ? 2179 HOH A O 1 HETATM 4286 O O . HOH R 6 . ? 30.343 -13.370 -86.119 1.00 29.04 ? 2180 HOH A O 1 HETATM 4287 O O . HOH R 6 . ? 26.489 -10.047 -84.721 1.00 37.11 ? 2181 HOH A O 1 HETATM 4288 O O . HOH R 6 . ? 26.313 -10.379 -87.726 1.00 43.14 ? 2182 HOH A O 1 HETATM 4289 O O . HOH R 6 . ? 30.092 -5.534 -80.978 1.00 52.36 ? 2183 HOH A O 1 HETATM 4290 O O . HOH R 6 . ? 29.036 -5.025 -89.535 1.00 48.76 ? 2184 HOH A O 1 HETATM 4291 O O . HOH R 6 . ? 28.777 -1.969 -86.623 1.00 64.50 ? 2185 HOH A O 1 HETATM 4292 O O . HOH R 6 . ? 24.692 -8.105 -77.990 1.00 46.37 ? 2186 HOH A O 1 HETATM 4293 O O . HOH R 6 . ? 35.612 -27.278 17.357 1.00 52.25 ? 2187 HOH A O 1 HETATM 4294 O O . HOH R 6 . ? 30.955 -13.384 -73.991 1.00 41.96 ? 2188 HOH A O 1 HETATM 4295 O O . HOH R 6 . ? 28.342 -15.805 -75.545 1.00 32.28 ? 2189 HOH A O 1 HETATM 4296 O O . HOH R 6 . ? 35.348 -16.673 -74.885 1.00 42.27 ? 2190 HOH A O 1 HETATM 4297 O O . HOH R 6 . ? 28.737 -23.059 -84.682 1.00 24.49 ? 2191 HOH A O 1 HETATM 4298 O O . HOH R 6 . ? 41.914 -32.229 -90.687 1.00 36.27 ? 2192 HOH A O 1 HETATM 4299 O O . HOH R 6 . ? 38.472 -42.506 -107.163 1.00 49.84 ? 2193 HOH A O 1 HETATM 4300 O O . HOH R 6 . ? 33.114 -38.969 -99.551 1.00 44.63 ? 2194 HOH A O 1 HETATM 4301 O O . HOH R 6 . ? 40.222 -24.631 -110.838 1.00 60.16 ? 2195 HOH A O 1 HETATM 4302 O O . HOH R 6 . ? 40.428 -29.748 -110.291 1.00 53.62 ? 2196 HOH A O 1 HETATM 4303 O O . HOH R 6 . ? 42.319 -33.361 -105.137 1.00 46.95 ? 2197 HOH A O 1 HETATM 4304 O O . HOH R 6 . ? 43.757 -30.705 -100.248 1.00 41.95 ? 2198 HOH A O 1 HETATM 4305 O O . HOH R 6 . ? 43.656 -34.607 -100.769 1.00 44.94 ? 2199 HOH A O 1 HETATM 4306 O O . HOH R 6 . ? 38.846 -27.865 -101.309 1.00 40.38 ? 2200 HOH A O 1 HETATM 4307 O O . HOH R 6 . ? 38.621 -25.555 -99.674 1.00 41.54 ? 2201 HOH A O 1 HETATM 4308 O O . HOH R 6 . ? 40.876 -23.877 -101.556 1.00 40.29 ? 2202 HOH A O 1 HETATM 4309 O O . HOH R 6 . ? 44.727 -19.880 -97.437 1.00 47.24 ? 2203 HOH A O 1 HETATM 4310 O O . HOH R 6 . ? 40.175 -16.800 -93.973 1.00 41.30 ? 2204 HOH A O 1 HETATM 4311 O O . HOH R 6 . ? 40.566 -18.703 -87.006 1.00 44.61 ? 2205 HOH A O 1 HETATM 4312 O O . HOH R 6 . ? 39.311 -15.138 -83.176 1.00 44.23 ? 2206 HOH A O 1 HETATM 4313 O O . HOH R 6 . ? 37.967 -12.627 -82.384 1.00 41.47 ? 2207 HOH A O 1 HETATM 4314 O O . HOH R 6 . ? 46.202 -17.576 -85.261 1.00 44.83 ? 2208 HOH A O 1 HETATM 4315 O O . HOH R 6 . ? 47.457 -19.801 -92.252 1.00 40.19 ? 2209 HOH A O 1 HETATM 4316 O O . HOH R 6 . ? 40.106 -25.775 -83.747 1.00 29.30 ? 2210 HOH A O 1 HETATM 4317 O O . HOH R 6 . ? 42.329 -25.015 -85.550 1.00 45.50 ? 2211 HOH A O 1 HETATM 4318 O O . HOH R 6 . ? 45.846 -29.378 -92.161 1.00 36.50 ? 2212 HOH A O 1 HETATM 4319 O O . HOH R 6 . ? 44.124 -31.872 -92.473 1.00 33.92 ? 2213 HOH A O 1 HETATM 4320 O O . HOH R 6 . ? 45.842 -33.634 -99.339 1.00 45.02 ? 2214 HOH A O 1 HETATM 4321 O O . HOH R 6 . ? 48.286 -32.750 -96.202 1.00 40.88 ? 2215 HOH A O 1 HETATM 4322 O O . HOH R 6 . ? 42.815 -45.190 -99.571 1.00 54.00 ? 2216 HOH A O 1 HETATM 4323 O O . HOH R 6 . ? 44.012 -43.021 -96.302 1.00 39.27 ? 2217 HOH A O 1 HETATM 4324 O O . HOH R 6 . ? 38.060 -48.274 -96.103 1.00 36.56 ? 2218 HOH A O 1 HETATM 4325 O O . HOH R 6 . ? 35.955 -51.005 -90.886 1.00 41.77 ? 2219 HOH A O 1 HETATM 4326 O O . HOH R 6 . ? 31.361 -49.958 -91.082 1.00 44.64 ? 2220 HOH A O 1 HETATM 4327 O O . HOH R 6 . ? 31.302 -49.521 -87.394 1.00 59.75 ? 2221 HOH A O 1 HETATM 4328 O O . HOH R 6 . ? 25.539 -46.108 -92.209 1.00 44.86 ? 2222 HOH A O 1 HETATM 4329 O O . HOH R 6 . ? 32.423 -41.993 -97.810 1.00 43.97 ? 2223 HOH A O 1 HETATM 4330 O O . HOH R 6 . ? 39.883 -42.191 -88.737 1.00 36.96 ? 2224 HOH A O 1 HETATM 4331 O O . HOH R 6 . ? 44.318 -30.338 -87.756 1.00 48.93 ? 2225 HOH A O 1 HETATM 4332 O O . HOH R 6 . ? 40.410 -23.338 -81.824 1.00 45.84 ? 2226 HOH A O 1 HETATM 4333 O O . HOH R 6 . ? 39.727 -22.372 -77.915 1.00 40.12 ? 2227 HOH A O 1 HETATM 4334 O O . HOH R 6 . ? 39.724 -19.119 -81.538 1.00 41.51 ? 2228 HOH A O 1 HETATM 4335 O O . HOH R 6 . ? 39.984 -9.056 -82.221 1.00 47.04 ? 2229 HOH A O 1 HETATM 4336 O O . HOH R 6 . ? 21.054 -22.969 -91.863 1.00 41.70 ? 2230 HOH A O 1 HETATM 4337 O O . HOH R 6 . ? 33.839 -19.870 -70.970 1.00 34.25 ? 2231 HOH A O 1 HETATM 4338 O O . HOH R 6 . ? 28.995 -15.430 -68.954 1.00 50.57 ? 2232 HOH A O 1 HETATM 4339 O O . HOH R 6 . ? 34.907 -19.928 -64.596 1.00 61.57 ? 2233 HOH A O 1 HETATM 4340 O O . HOH R 6 . ? 31.471 -18.047 -61.499 1.00 60.45 ? 2234 HOH A O 1 HETATM 4341 O O . HOH R 6 . ? 27.530 -20.900 -62.930 1.00 35.60 ? 2235 HOH A O 1 HETATM 4342 O O . HOH R 6 . ? 35.504 -32.873 -65.784 1.00 32.73 ? 2236 HOH A O 1 HETATM 4343 O O . HOH R 6 . ? 34.232 -31.525 -61.365 1.00 42.01 ? 2237 HOH A O 1 HETATM 4344 O O . HOH R 6 . ? 36.059 -31.332 -63.542 1.00 30.46 ? 2238 HOH A O 1 HETATM 4345 O O . HOH R 6 . ? 33.525 -33.927 -63.073 1.00 41.61 ? 2239 HOH A O 1 HETATM 4346 O O . HOH R 6 . ? 34.586 -37.656 -64.864 1.00 23.64 ? 2240 HOH A O 1 HETATM 4347 O O . HOH R 6 . ? 34.246 -41.770 -63.674 1.00 35.24 ? 2241 HOH A O 1 HETATM 4348 O O . HOH R 6 . ? 36.414 -39.496 -65.858 1.00 23.84 ? 2242 HOH A O 1 HETATM 4349 O O . HOH R 6 . ? 39.972 -38.033 -69.574 1.00 20.52 ? 2243 HOH A O 1 HETATM 4350 O O . HOH R 6 . ? 39.517 -40.203 -71.176 1.00 31.48 ? 2244 HOH A O 1 HETATM 4351 O O . HOH R 6 . ? 36.337 -38.378 -73.779 1.00 38.72 ? 2245 HOH A O 1 HETATM 4352 O O . HOH R 6 . ? 29.678 -44.771 -62.485 1.00 34.09 ? 2246 HOH A O 1 HETATM 4353 O O . HOH R 6 . ? 22.831 -45.303 -65.773 1.00 51.41 ? 2247 HOH A O 1 HETATM 4354 O O . HOH R 6 . ? 19.138 -42.223 -64.465 1.00 37.29 ? 2248 HOH A O 1 HETATM 4355 O O . HOH R 6 . ? 14.044 -41.119 -57.808 1.00 44.75 ? 2249 HOH A O 1 HETATM 4356 O O . HOH R 6 . ? 16.723 -35.928 -50.862 1.00 44.51 ? 2250 HOH A O 1 HETATM 4357 O O . HOH R 6 . ? 20.187 -37.045 -50.284 1.00 53.75 ? 2251 HOH A O 1 HETATM 4358 O O . HOH R 6 . ? 20.802 -28.723 -50.830 1.00 30.05 ? 2252 HOH A O 1 HETATM 4359 O O . HOH R 6 . ? 24.184 -37.909 -50.569 1.00 37.91 ? 2253 HOH A O 1 HETATM 4360 O O . HOH R 6 . ? 26.175 -33.787 -50.294 1.00 30.60 ? 2254 HOH A O 1 HETATM 4361 O O . HOH R 6 . ? 23.765 -32.193 -49.253 1.00 32.54 ? 2255 HOH A O 1 HETATM 4362 O O . HOH R 6 . ? 32.726 -44.725 -59.973 1.00 46.03 ? 2256 HOH A O 1 HETATM 4363 O O . HOH R 6 . ? 30.379 -47.126 -57.290 1.00 45.19 ? 2257 HOH A O 1 HETATM 4364 O O . HOH R 6 . ? 24.916 -34.026 -46.983 1.00 40.38 ? 2258 HOH A O 1 HETATM 4365 O O . HOH R 6 . ? 29.594 -29.556 -45.814 1.00 37.86 ? 2259 HOH A O 1 HETATM 4366 O O . HOH R 6 . ? 26.567 -27.930 -48.215 1.00 39.35 ? 2260 HOH A O 1 HETATM 4367 O O . HOH R 6 . ? 32.876 -30.639 -42.976 1.00 29.38 ? 2261 HOH A O 1 HETATM 4368 O O . HOH R 6 . ? 24.873 -35.313 -43.939 1.00 49.16 ? 2262 HOH A O 1 HETATM 4369 O O . HOH R 6 . ? 29.207 -36.140 -39.283 1.00 34.08 ? 2263 HOH A O 1 HETATM 4370 O O . HOH R 6 . ? 36.569 -30.429 -46.184 1.00 24.89 ? 2264 HOH A O 1 HETATM 4371 O O . HOH R 6 . ? 39.204 -44.400 -52.920 1.00 38.00 ? 2265 HOH A O 1 HETATM 4372 O O . HOH R 6 . ? 35.969 -46.053 -52.382 1.00 37.88 ? 2266 HOH A O 1 HETATM 4373 O O . HOH R 6 . ? 42.266 -45.276 -50.673 1.00 41.09 ? 2267 HOH A O 1 HETATM 4374 O O . HOH R 6 . ? 37.756 -44.187 -55.710 1.00 46.41 ? 2268 HOH A O 1 HETATM 4375 O O . HOH R 6 . ? 38.421 -41.791 -60.010 1.00 28.63 ? 2269 HOH A O 1 HETATM 4376 O O . HOH R 6 . ? 39.209 -42.125 -57.150 1.00 26.87 ? 2270 HOH A O 1 HETATM 4377 O O . HOH R 6 . ? 35.284 -42.739 -61.226 1.00 31.34 ? 2271 HOH A O 1 HETATM 4378 O O . HOH R 6 . ? 39.311 -34.159 -55.476 1.00 26.78 ? 2272 HOH A O 1 HETATM 4379 O O . HOH R 6 . ? 41.275 -41.498 -60.658 1.00 45.30 ? 2273 HOH A O 1 HETATM 4380 O O . HOH R 6 . ? 41.741 -42.688 -56.087 1.00 47.22 ? 2274 HOH A O 1 HETATM 4381 O O . HOH R 6 . ? 47.165 -39.490 -60.390 1.00 26.59 ? 2275 HOH A O 1 HETATM 4382 O O . HOH R 6 . ? 44.430 -38.700 -61.641 1.00 27.61 ? 2276 HOH A O 1 HETATM 4383 O O . HOH R 6 . ? 43.993 -42.713 -54.404 1.00 47.05 ? 2277 HOH A O 1 HETATM 4384 O O . HOH R 6 . ? 37.194 -33.582 -59.701 1.00 26.21 ? 2278 HOH A O 1 HETATM 4385 O O . HOH R 6 . ? 33.932 -30.603 -55.484 1.00 26.16 ? 2279 HOH A O 1 HETATM 4386 O O . HOH R 6 . ? 37.544 -32.258 -56.165 1.00 34.38 ? 2280 HOH A O 1 HETATM 4387 O O . HOH R 6 . ? 36.340 -32.683 -52.926 1.00 37.42 ? 2281 HOH A O 1 HETATM 4388 O O . HOH R 6 . ? 27.004 -24.723 -59.516 1.00 38.49 ? 2282 HOH A O 1 HETATM 4389 O O . HOH R 6 . ? 34.953 -29.614 -52.717 1.00 32.95 ? 2283 HOH A O 1 HETATM 4390 O O . HOH R 6 . ? 35.696 -29.370 -48.705 1.00 33.11 ? 2284 HOH A O 1 HETATM 4391 O O . HOH R 6 . ? 40.278 -26.506 -47.176 1.00 46.15 ? 2285 HOH A O 1 HETATM 4392 O O . HOH R 6 . ? 41.045 -32.103 -51.784 1.00 23.37 ? 2286 HOH A O 1 HETATM 4393 O O . HOH R 6 . ? 37.673 -29.276 -52.215 1.00 44.14 ? 2287 HOH A O 1 HETATM 4394 O O . HOH R 6 . ? 38.895 -33.537 -52.994 1.00 25.02 ? 2288 HOH A O 1 HETATM 4395 O O . HOH R 6 . ? 42.617 -34.236 -52.072 1.00 21.29 ? 2289 HOH A O 1 HETATM 4396 O O . HOH R 6 . ? 42.948 -46.752 -46.846 1.00 54.94 ? 2290 HOH A O 1 HETATM 4397 O O . HOH R 6 . ? 46.729 -44.294 -46.296 1.00 53.85 ? 2291 HOH A O 1 HETATM 4398 O O . HOH R 6 . ? 42.869 -46.198 -43.894 1.00 44.17 ? 2292 HOH A O 1 HETATM 4399 O O . HOH R 6 . ? 42.315 -48.557 -42.366 1.00 54.74 ? 2293 HOH A O 1 HETATM 4400 O O . HOH R 6 . ? 36.511 -48.661 -43.287 1.00 69.42 ? 2294 HOH A O 1 HETATM 4401 O O . HOH R 6 . ? 42.665 -44.149 -39.244 1.00 44.87 ? 2295 HOH A O 1 HETATM 4402 O O . HOH R 6 . ? 37.817 -47.019 -37.671 1.00 50.88 ? 2296 HOH A O 1 HETATM 4403 O O . HOH R 6 . ? 41.240 -43.441 -36.800 1.00 31.11 ? 2297 HOH A O 1 HETATM 4404 O O . HOH R 6 . ? 39.075 -34.980 -30.798 1.00 22.15 ? 2298 HOH A O 1 HETATM 4405 O O . HOH R 6 . ? 30.301 -34.092 -26.841 1.00 52.54 ? 2299 HOH A O 1 HETATM 4406 O O . HOH R 6 . ? 39.435 -37.429 -17.733 1.00 43.54 ? 2300 HOH A O 1 HETATM 4407 O O . HOH R 6 . ? 40.940 -37.847 -21.213 1.00 26.68 ? 2301 HOH A O 1 HETATM 4408 O O . HOH R 6 . ? 43.861 -44.093 -20.633 1.00 37.50 ? 2302 HOH A O 1 HETATM 4409 O O . HOH R 6 . ? 41.481 -49.025 -14.201 1.00 44.22 ? 2303 HOH A O 1 HETATM 4410 O O . HOH R 6 . ? 30.633 -47.128 -10.885 1.00 40.40 ? 2304 HOH A O 1 HETATM 4411 O O . HOH R 6 . ? 35.892 -46.759 -8.212 1.00 36.02 ? 2305 HOH A O 1 HETATM 4412 O O . HOH R 6 . ? 34.414 -45.493 -6.010 1.00 36.62 ? 2306 HOH A O 1 HETATM 4413 O O . HOH R 6 . ? 41.967 -44.753 -7.806 1.00 41.10 ? 2307 HOH A O 1 HETATM 4414 O O . HOH R 6 . ? 26.438 -46.659 -8.433 1.00 63.35 ? 2308 HOH A O 1 HETATM 4415 O O . HOH R 6 . ? 24.347 -35.996 -9.947 1.00 41.88 ? 2309 HOH A O 1 HETATM 4416 O O . HOH R 6 . ? 25.940 -35.837 -24.208 1.00 63.59 ? 2310 HOH A O 1 HETATM 4417 O O . HOH R 6 . ? 29.141 -36.664 -3.661 1.00 33.37 ? 2311 HOH A O 1 HETATM 4418 O O . HOH R 6 . ? 27.903 -45.848 -5.996 1.00 58.31 ? 2312 HOH A O 1 HETATM 4419 O O . HOH R 6 . ? 25.903 -39.825 2.482 1.00 31.80 ? 2313 HOH A O 1 HETATM 4420 O O . HOH R 6 . ? 22.356 -40.249 3.031 1.00 45.39 ? 2314 HOH A O 1 HETATM 4421 O O . HOH R 6 . ? 22.951 -32.905 6.068 1.00 42.23 ? 2315 HOH A O 1 HETATM 4422 O O . HOH R 6 . ? 23.533 -41.684 -0.694 0.50 36.12 ? 2316 HOH A O 1 HETATM 4423 O O . HOH R 6 . ? 24.824 -37.000 -3.162 1.00 53.95 ? 2317 HOH A O 1 HETATM 4424 O O . HOH R 6 . ? 27.992 -31.924 -7.583 1.00 40.54 ? 2318 HOH A O 1 HETATM 4425 O O . HOH R 6 . ? 27.261 -29.391 -10.278 1.00 38.83 ? 2319 HOH A O 1 HETATM 4426 O O . HOH R 6 . ? 29.345 -29.660 -8.255 1.00 44.25 ? 2320 HOH A O 1 HETATM 4427 O O . HOH R 6 . ? 30.518 -25.037 -28.066 1.00 51.56 ? 2321 HOH A O 1 HETATM 4428 O O . HOH R 6 . ? 39.782 -28.357 -20.229 1.00 34.50 ? 2322 HOH A O 1 HETATM 4429 O O . HOH R 6 . ? 35.181 -24.566 -40.118 1.00 48.65 ? 2323 HOH A O 1 HETATM 4430 O O . HOH R 6 . ? 36.229 -28.207 -42.074 1.00 42.66 ? 2324 HOH A O 1 HETATM 4431 O O . HOH R 6 . ? 34.960 -29.385 -44.192 1.00 31.49 ? 2325 HOH A O 1 HETATM 4432 O O . HOH R 6 . ? 33.426 -23.480 -44.836 1.00 55.35 ? 2326 HOH A O 1 HETATM 4433 O O . HOH R 6 . ? 32.314 -23.023 -50.931 1.00 49.03 ? 2327 HOH A O 1 HETATM 4434 O O . HOH R 6 . ? 36.654 -24.130 -52.701 1.00 51.21 ? 2328 HOH A O 1 HETATM 4435 O O . HOH R 6 . ? 26.657 -24.209 -56.538 1.00 43.27 ? 2329 HOH A O 1 HETATM 4436 O O . HOH R 6 . ? 36.543 -25.078 -58.896 1.00 28.76 ? 2330 HOH A O 1 HETATM 4437 O O . HOH R 6 . ? 34.570 -24.071 -62.668 1.00 30.76 ? 2331 HOH A O 1 HETATM 4438 O O . HOH R 6 . ? 39.032 -26.323 -65.105 1.00 44.73 ? 2332 HOH A O 1 HETATM 4439 O O . HOH R 6 . ? 36.945 -24.234 -61.781 1.00 36.62 ? 2333 HOH A O 1 HETATM 4440 O O . HOH R 6 . ? 39.164 -30.441 -54.532 1.00 36.67 ? 2334 HOH A O 1 HETATM 4441 O O . HOH R 6 . ? 37.656 -34.133 -62.364 1.00 32.77 ? 2335 HOH A O 1 HETATM 4442 O O . HOH R 6 . ? 41.830 -31.834 -67.865 1.00 26.57 ? 2336 HOH A O 1 HETATM 4443 O O . HOH R 6 . ? 44.561 -36.184 -62.964 1.00 21.98 ? 2337 HOH A O 1 HETATM 4444 O O . HOH R 6 . ? 35.733 -35.227 -64.097 1.00 38.21 ? 2338 HOH A O 1 HETATM 4445 O O . HOH R 6 . ? 38.092 -37.380 -64.968 1.00 27.93 ? 2339 HOH A O 1 HETATM 4446 O O . HOH R 6 . ? 44.305 -41.659 -63.696 1.00 37.75 ? 2340 HOH A O 1 HETATM 4447 O O . HOH R 6 . ? 43.266 -43.381 -65.808 1.00 28.83 ? 2341 HOH A O 1 HETATM 4448 O O . HOH R 6 . ? 38.867 -44.481 -68.258 1.00 58.62 ? 2342 HOH A O 1 HETATM 4449 O O . HOH R 6 . ? 42.335 -40.312 -72.702 1.00 41.16 ? 2343 HOH A O 1 HETATM 4450 O O . HOH R 6 . ? 40.725 -47.595 -72.150 1.00 55.22 ? 2344 HOH A O 1 HETATM 4451 O O . HOH R 6 . ? 44.299 -47.231 -72.990 1.00 53.28 ? 2345 HOH A O 1 HETATM 4452 O O . HOH R 6 . ? 46.511 -43.850 -69.813 1.00 34.95 ? 2346 HOH A O 1 HETATM 4453 O O . HOH R 6 . ? 45.719 -45.995 -75.924 1.00 34.67 ? 2347 HOH A O 1 HETATM 4454 O O . HOH R 6 . ? 46.455 -43.451 -77.964 1.00 52.41 ? 2348 HOH A O 1 HETATM 4455 O O . HOH R 6 . ? 49.874 -41.572 -71.035 1.00 25.87 ? 2349 HOH A O 1 HETATM 4456 O O . HOH R 6 . ? 51.261 -35.441 -74.079 1.00 30.20 ? 2350 HOH A O 1 HETATM 4457 O O . HOH R 6 . ? 42.554 -37.473 -72.783 1.00 30.16 ? 2351 HOH A O 1 HETATM 4458 O O . HOH R 6 . ? 50.266 -40.770 -68.341 1.00 30.97 ? 2352 HOH A O 1 HETATM 4459 O O . HOH R 6 . ? 52.699 -39.060 -63.517 1.00 23.45 ? 2353 HOH A O 1 HETATM 4460 O O . HOH R 6 . ? 53.542 -42.225 -69.594 1.00 30.30 ? 2354 HOH A O 1 HETATM 4461 O O . HOH R 6 . ? 56.893 -37.983 -67.881 1.00 30.17 ? 2355 HOH A O 1 HETATM 4462 O O . HOH R 6 . ? 42.504 -33.865 -69.559 1.00 30.68 ? 2356 HOH A O 1 HETATM 4463 O O . HOH R 6 . ? 44.058 -30.616 -67.785 1.00 21.63 ? 2357 HOH A O 1 HETATM 4464 O O . HOH R 6 . ? 45.448 -44.236 -67.156 1.00 40.76 ? 2358 HOH A O 1 HETATM 4465 O O . HOH R 6 . ? 49.669 -30.623 -56.999 1.00 33.24 ? 2359 HOH A O 1 HETATM 4466 O O . HOH R 6 . ? 41.912 -34.470 -54.870 1.00 26.48 ? 2360 HOH A O 1 HETATM 4467 O O . HOH R 6 . ? 48.264 -40.236 -54.024 1.00 39.07 ? 2361 HOH A O 1 HETATM 4468 O O . HOH R 6 . ? 53.639 -40.527 -58.902 1.00 40.88 ? 2362 HOH A O 1 HETATM 4469 O O . HOH R 6 . ? 52.973 -38.793 -57.593 1.00 39.85 ? 2363 HOH A O 1 HETATM 4470 O O . HOH R 6 . ? 53.432 -36.770 -56.171 1.00 22.09 ? 2364 HOH A O 1 HETATM 4471 O O . HOH R 6 . ? 50.404 -38.611 -47.615 1.00 26.83 ? 2365 HOH A O 1 HETATM 4472 O O . HOH R 6 . ? 53.233 -37.251 -53.448 1.00 18.53 ? 2366 HOH A O 1 HETATM 4473 O O . HOH R 6 . ? 50.290 -31.185 -46.476 1.00 18.69 ? 2367 HOH A O 1 HETATM 4474 O O . HOH R 6 . ? 44.512 -28.163 -52.474 1.00 15.23 ? 2368 HOH A O 1 HETATM 4475 O O . HOH R 6 . ? 53.762 -31.286 -40.360 1.00 18.65 ? 2369 HOH A O 1 HETATM 4476 O O . HOH R 6 . ? 49.281 -30.275 -41.830 1.00 19.42 ? 2370 HOH A O 1 HETATM 4477 O O . HOH R 6 . ? 45.787 -39.559 -37.245 1.00 28.18 ? 2371 HOH A O 1 HETATM 4478 O O . HOH R 6 . ? 45.712 -43.687 -41.223 1.00 43.34 ? 2372 HOH A O 1 HETATM 4479 O O . HOH R 6 . ? 44.860 -43.046 -38.374 1.00 41.78 ? 2373 HOH A O 1 HETATM 4480 O O . HOH R 6 . ? 47.307 -31.371 -29.786 1.00 26.87 ? 2374 HOH A O 1 HETATM 4481 O O . HOH R 6 . ? 46.979 -30.671 -27.165 1.00 38.30 ? 2375 HOH A O 1 HETATM 4482 O O . HOH R 6 . ? 45.720 -31.986 -19.544 1.00 41.50 ? 2376 HOH A O 1 HETATM 4483 O O . HOH R 6 . ? 37.065 -28.650 -14.004 1.00 32.44 ? 2377 HOH A O 1 HETATM 4484 O O . HOH R 6 . ? 35.873 -25.790 -15.945 1.00 37.90 ? 2378 HOH A O 1 HETATM 4485 O O . HOH R 6 . ? 45.058 -31.620 -9.835 1.00 52.41 ? 2379 HOH A O 1 HETATM 4486 O O . HOH R 6 . ? 45.933 -31.414 -16.697 1.00 48.07 ? 2380 HOH A O 1 HETATM 4487 O O . HOH R 6 . ? 41.393 -25.684 -10.434 1.00 43.02 ? 2381 HOH A O 1 HETATM 4488 O O . HOH R 6 . ? 47.471 -31.893 -6.050 1.00 47.00 ? 2382 HOH A O 1 HETATM 4489 O O . HOH R 6 . ? 39.302 -23.676 -4.595 1.00 37.14 ? 2383 HOH A O 1 HETATM 4490 O O . HOH R 6 . ? 35.105 -28.433 -5.439 1.00 42.24 ? 2384 HOH A O 1 HETATM 4491 O O . HOH R 6 . ? 43.523 -29.008 1.231 1.00 38.25 ? 2385 HOH A O 1 HETATM 4492 O O . HOH R 6 . ? 47.208 -32.839 -3.199 1.00 48.33 ? 2386 HOH A O 1 HETATM 4493 O O . HOH R 6 . ? 44.428 -31.573 0.919 1.00 46.98 ? 2387 HOH A O 1 HETATM 4494 O O . HOH R 6 . ? 38.573 -22.569 1.674 1.00 42.44 ? 2388 HOH A O 1 HETATM 4495 O O . HOH R 6 . ? 34.179 -23.075 -0.345 1.00 50.63 ? 2389 HOH A O 1 HETATM 4496 O O . HOH R 6 . ? 45.534 -24.773 3.715 1.00 41.54 ? 2390 HOH A O 1 HETATM 4497 O O . HOH R 6 . ? 40.685 -20.610 1.639 1.00 32.29 ? 2391 HOH A O 1 HETATM 4498 O O . HOH R 6 . ? 42.646 -16.981 4.865 1.00 42.53 ? 2392 HOH A O 1 HETATM 4499 O O . HOH R 6 . ? 41.624 -25.142 7.385 1.00 29.41 ? 2393 HOH A O 1 HETATM 4500 O O . HOH R 6 . ? 47.752 -34.068 1.633 1.00 39.65 ? 2394 HOH A O 1 HETATM 4501 O O . HOH R 6 . ? 45.147 -38.263 -5.345 1.00 33.46 ? 2395 HOH A O 1 HETATM 4502 O O . HOH R 6 . ? 49.268 -36.310 0.345 1.00 56.80 ? 2396 HOH A O 1 HETATM 4503 O O . HOH R 6 . ? 49.315 -41.203 -6.395 1.00 47.47 ? 2397 HOH A O 1 HETATM 4504 O O . HOH R 6 . ? 41.427 -39.810 11.628 1.00 59.70 ? 2398 HOH A O 1 HETATM 4505 O O . HOH R 6 . ? 45.578 -39.697 10.021 1.00 45.17 ? 2399 HOH A O 1 HETATM 4506 O O . HOH R 6 . ? 28.975 -31.940 9.184 1.00 30.76 ? 2400 HOH A O 1 HETATM 4507 O O . HOH R 6 . ? 31.732 -31.307 12.008 1.00 33.77 ? 2401 HOH A O 1 HETATM 4508 O O . HOH R 6 . ? 26.157 -29.488 7.565 1.00 33.75 ? 2402 HOH A O 1 HETATM 4509 O O . HOH R 6 . ? 25.599 -34.400 -0.149 1.00 55.85 ? 2403 HOH A O 1 HETATM 4510 O O . HOH R 6 . ? 29.522 -26.694 5.378 1.00 40.13 ? 2404 HOH A O 1 HETATM 4511 O O . HOH R 6 . ? 32.874 -27.573 -6.342 1.00 48.55 ? 2405 HOH A O 1 HETATM 4512 O O . HOH R 6 . ? 25.790 -31.434 -6.023 1.00 51.73 ? 2406 HOH A O 1 HETATM 4513 O O . HOH R 6 . ? 36.377 -22.181 2.865 1.00 38.52 ? 2407 HOH A O 1 HETATM 4514 O O . HOH R 6 . ? 30.657 -24.264 5.502 1.00 40.71 ? 2408 HOH A O 1 HETATM 4515 O O . HOH R 6 . ? 36.724 -18.931 5.228 1.00 58.88 ? 2409 HOH A O 1 HETATM 4516 O O . HOH R 6 . ? 37.050 -24.069 13.785 1.00 36.59 ? 2410 HOH A O 1 HETATM 4517 O O . HOH R 6 . ? 33.670 -28.344 13.808 1.00 37.81 ? 2411 HOH A O 1 HETATM 4518 O O . HOH R 6 . ? 35.897 -26.771 14.407 1.00 35.90 ? 2412 HOH A O 1 HETATM 4519 O O . HOH R 6 . ? 33.313 -23.543 14.496 1.00 49.41 ? 2413 HOH A O 1 HETATM 4520 O O . HOH R 6 . ? 28.342 -29.462 9.354 1.00 41.12 ? 2414 HOH A O 1 HETATM 4521 O O . HOH R 6 . ? 43.761 -22.524 13.377 1.00 41.46 ? 2415 HOH A O 1 HETATM 4522 O O . HOH R 6 . ? 37.615 -25.480 19.373 1.00 62.53 ? 2416 HOH A O 1 HETATM 4523 O O . HOH R 6 . ? 38.441 -33.137 16.827 1.00 41.35 ? 2417 HOH A O 1 HETATM 4524 O O . HOH R 6 . ? 46.555 -29.150 17.282 1.00 59.90 ? 2418 HOH A O 1 HETATM 4525 O O . HOH R 6 . ? 45.534 -38.381 12.589 1.00 48.75 ? 2419 HOH A O 1 HETATM 4526 O O . HOH R 6 . ? 22.660 -43.003 -29.553 1.00 67.49 ? 2420 HOH A O 1 HETATM 4527 O O . HOH R 6 . ? 14.733 -51.249 -77.442 1.00 61.04 ? 2421 HOH A O 1 HETATM 4528 O O . HOH R 6 . ? 41.074 -7.432 -98.456 1.00 43.77 ? 2422 HOH A O 1 HETATM 4529 O O . HOH R 6 . ? 34.116 -9.776 -100.753 1.00 68.35 ? 2423 HOH A O 1 HETATM 4530 O O . HOH R 6 . ? 43.980 -14.432 -104.708 1.00 55.33 ? 2424 HOH A O 1 HETATM 4531 O O . HOH R 6 . ? 31.953 -49.132 -56.794 1.00 59.55 ? 2425 HOH A O 1 HETATM 4532 O O . HOH R 6 . ? 41.498 -22.766 -44.768 1.00 57.18 ? 2426 HOH A O 1 HETATM 4533 O O . HOH R 6 . ? 31.781 2.497 -93.528 1.00 68.27 ? 2427 HOH A O 1 HETATM 4534 O O . HOH R 6 . ? 50.432 -29.138 -101.935 0.33 59.58 ? 2428 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 . ASN A 8 ? 0.9039 0.8883 0.8112 -0.1264 0.0158 0.0834 8 ASN A N 2 C CA . ASN A 8 ? 0.8711 0.8581 0.7760 -0.1270 0.0179 0.0841 8 ASN A CA 3 C C . ASN A 8 ? 0.8118 0.8033 0.7249 -0.1167 0.0200 0.0809 8 ASN A C 4 O O . ASN A 8 ? 0.8118 0.7910 0.7204 -0.1108 0.0176 0.0796 8 ASN A O 5 C CB . ASN A 8 ? 0.9237 0.8915 0.8122 -0.1313 0.0141 0.0864 8 ASN A CB 6 C CG . ASN A 8 ? 0.9650 0.9140 0.8462 -0.1247 0.0095 0.0849 8 ASN A CG 7 O OD1 . ASN A 8 ? 0.9680 0.9175 0.8555 -0.1188 0.0088 0.0826 8 ASN A OD1 8 N ND2 . ASN A 8 ? 0.9922 0.9247 0.8597 -0.1254 0.0064 0.0861 8 ASN A ND2 9 N N . SER A 9 ? 0.7465 0.7560 0.6716 -0.1144 0.0243 0.0796 9 SER A N 10 C CA . SER A 9 ? 0.6685 0.6831 0.6017 -0.1052 0.0264 0.0766 9 SER A CA 11 C C . SER A 9 ? 0.5816 0.5939 0.5207 -0.0984 0.0252 0.0740 9 SER A C 12 O O . SER A 9 ? 0.5435 0.5607 0.4896 -0.0914 0.0269 0.0715 9 SER A O 13 C CB . SER A 9 ? 0.6885 0.6933 0.6148 -0.1023 0.0255 0.0765 9 SER A CB 14 O OG . SER A 9 ? 0.6924 0.6816 0.6126 -0.0978 0.0217 0.0754 9 SER A OG 15 N N . THR A 10 ? 0.5454 0.5501 0.4811 -0.1006 0.0222 0.0746 10 THR A N 16 C CA . THR A 10 ? 0.5078 0.5116 0.4492 -0.0947 0.0212 0.0722 10 THR A CA 17 C C . THR A 10 ? 0.4743 0.4809 0.4176 -0.0991 0.0203 0.0731 10 THR A C 18 O O . THR A 10 ? 0.4784 0.4864 0.4176 -0.1070 0.0200 0.0756 10 THR A O 19 C CB . THR A 10 ? 0.5317 0.5196 0.4660 -0.0899 0.0173 0.0710 10 THR A CB 20 O OG1 . THR A 10 ? 0.5711 0.5454 0.4937 -0.0953 0.0135 0.0732 10 THR A OG1 21 C CG2 . THR A 10 ? 0.5494 0.5343 0.4814 -0.0854 0.0179 0.0699 10 THR A CG2 22 N N . ALA A 11 ? 0.4113 0.4193 0.3608 -0.0941 0.0198 0.0710 11 ALA A N 23 C CA . ALA A 11 ? 0.3961 0.4064 0.3478 -0.0973 0.0188 0.0715 11 ALA A CA 24 C C . ALA A 11 ? 0.3802 0.3816 0.3318 -0.0916 0.0161 0.0695 11 ALA A C 25 O O . ALA A 11 ? 0.3630 0.3608 0.3154 -0.0851 0.0160 0.0674 11 ALA A O 26 C CB . ALA A 11 ? 0.3840 0.4123 0.3469 -0.0970 0.0226 0.0707 11 ALA A CB 27 N N . THR A 12 ? 0.3713 0.3701 0.3221 -0.0943 0.0141 0.0700 12 THR A N 28 C CA . THR A 12 ? 0.3715 0.3633 0.3228 -0.0892 0.0115 0.0681 12 THR A CA 29 C C . THR A 12 ? 0.3548 0.3574 0.3155 -0.0888 0.0131 0.0672 12 THR A C 30 O O . THR A 12 ? 0.3603 0.3700 0.3225 -0.0948 0.0140 0.0689 12 THR A O 31 C CB . THR A 12 ? 0.3912 0.3666 0.3305 -0.0923 0.0067 0.0694 12 THR A CB 32 O OG1 . THR A 12 ? 0.4128 0.3777 0.3426 -0.0924 0.0051 0.0701 12 THR A OG1 33 C CG2 . THR A 12 ? 0.4051 0.3733 0.3443 -0.0865 0.0038 0.0672 12 THR A CG2 34 N N . LEU A 13 ? 0.3442 0.3487 0.3109 -0.0820 0.0135 0.0647 13 LEU A N 35 C CA . LEU A 13 ? 0.3386 0.3513 0.3133 -0.0808 0.0144 0.0637 13 LEU A CA 36 C C . LEU A 13 ? 0.3522 0.3565 0.3256 -0.0766 0.0115 0.0620 13 LEU A C 37 O O . LEU A 13 ? 0.3525 0.3537 0.3263 -0.0707 0.0113 0.0600 13 LEU A O 38 C CB . LEU A 13 ? 0.3195 0.3451 0.3035 -0.0768 0.0184 0.0621 13 LEU A CB 39 C CG . LEU A 13 ? 0.3216 0.3558 0.3137 -0.0749 0.0195 0.0609 13 LEU A CG 40 C CD1 . LEU A 13 ? 0.3134 0.3548 0.3066 -0.0811 0.0197 0.0626 13 LEU A CD1 41 C CD2 . LEU A 13 ? 0.3195 0.3625 0.3185 -0.0697 0.0226 0.0589 13 LEU A CD2 42 N N . CYS A 14 ? 0.3737 0.3750 0.3453 -0.0798 0.0093 0.0628 14 CYS A N 43 C CA . CYS A 14 ? 0.3776 0.3707 0.3472 -0.0763 0.0062 0.0614 14 CYS A CA 44 C C . CYS A 14 ? 0.3604 0.3625 0.3388 -0.0745 0.0076 0.0602 14 CYS A C 45 O O . CYS A 14 ? 0.3391 0.3506 0.3222 -0.0782 0.0094 0.0612 14 CYS A O 46 C CB . CYS A 14 ? 0.4186 0.3992 0.3779 -0.0811 0.0020 0.0631 14 CYS A CB 47 S SG . CYS A 14 ? 0.4815 0.4478 0.4277 -0.0827 -0.0006 0.0645 14 CYS A SG 48 N N . LEU A 15 ? 0.3446 0.3445 0.3252 -0.0686 0.0067 0.0578 15 LEU A N 49 C CA . LEU A 15 ? 0.3372 0.3433 0.3247 -0.0668 0.0074 0.0567 15 LEU A CA 50 C C . LEU A 15 ? 0.3434 0.3406 0.3261 -0.0672 0.0035 0.0566 15 LEU A C 51 O O . LEU A 15 ? 0.3678 0.3543 0.3433 -0.0652 0.0006 0.0560 15 LEU A O 52 C CB . LEU A 15 ? 0.3456 0.3561 0.3386 -0.0605 0.0093 0.0542 15 LEU A CB 53 C CG . LEU A 15 ? 0.3574 0.3783 0.3563 -0.0601 0.0132 0.0542 15 LEU A CG 54 C CD1 . LEU A 15 ? 0.3771 0.3959 0.3723 -0.0606 0.0141 0.0548 15 LEU A CD1 55 C CD2 . LEU A 15 ? 0.4145 0.4401 0.4191 -0.0551 0.0149 0.0520 15 LEU A CD2 56 N N . GLY A 16 ? 0.3234 0.3247 0.3095 -0.0695 0.0034 0.0571 16 GLY A N 57 C CA . GLY A 16 ? 0.3225 0.3152 0.3039 -0.0702 -0.0003 0.0570 16 GLY A CA 58 C C . GLY A 16 ? 0.3174 0.3167 0.3051 -0.0700 0.0001 0.0565 16 GLY A C 59 O O . GLY A 16 ? 0.2893 0.2999 0.2852 -0.0691 0.0032 0.0560 16 GLY A O 60 N N . HIS A 17 ? 0.3249 0.3165 0.3083 -0.0706 -0.0033 0.0564 17 HIS A N 61 C CA . HIS A 17 ? 0.3214 0.3177 0.3098 -0.0706 -0.0035 0.0559 17 HIS A CA 62 C C . HIS A 17 ? 0.3358 0.3245 0.3176 -0.0758 -0.0069 0.0574 17 HIS A C 63 O O . HIS A 17 ? 0.3682 0.3452 0.3405 -0.0778 -0.0099 0.0584 17 HIS A O 64 C CB . HIS A 17 ? 0.3148 0.3099 0.3057 -0.0638 -0.0040 0.0533 17 HIS A CB 65 C CG . HIS A 17 ? 0.3338 0.3164 0.3165 -0.0610 -0.0079 0.0523 17 HIS A CG 66 N ND1 . HIS A 17 ? 0.3464 0.3199 0.3225 -0.0630 -0.0117 0.0528 17 HIS A ND1 67 C CD2 . HIS A 17 ? 0.3527 0.3307 0.3321 -0.0560 -0.0086 0.0506 17 HIS A CD2 68 C CE1 . HIS A 17 ? 0.3656 0.3287 0.3342 -0.0590 -0.0149 0.0515 17 HIS A CE1 69 N NE2 . HIS A 17 ? 0.3732 0.3397 0.3442 -0.0547 -0.0130 0.0500 17 HIS A NE2 70 N N . HIS A 18 ? 0.3313 0.3259 0.3175 -0.0781 -0.0068 0.0577 18 HIS A N 71 C CA . HIS A 18 ? 0.3425 0.3309 0.3227 -0.0838 -0.0100 0.0592 18 HIS A CA 72 C C . HIS A 18 ? 0.3625 0.3373 0.3355 -0.0809 -0.0143 0.0582 18 HIS A C 73 O O . HIS A 18 ? 0.3562 0.3285 0.3301 -0.0740 -0.0147 0.0560 18 HIS A O 74 C CB . HIS A 18 ? 0.3406 0.3406 0.3279 -0.0870 -0.0085 0.0597 18 HIS A CB 75 C CG . HIS A 18 ? 0.3448 0.3476 0.3378 -0.0819 -0.0087 0.0576 18 HIS A CG 76 N ND1 . HIS A 18 ? 0.3531 0.3617 0.3497 -0.0843 -0.0090 0.0578 18 HIS A ND1 77 C CD2 . HIS A 18 ? 0.3413 0.3419 0.3365 -0.0745 -0.0086 0.0554 18 HIS A CD2 78 C CE1 . HIS A 18 ? 0.3543 0.3636 0.3551 -0.0785 -0.0091 0.0558 18 HIS A CE1 79 N NE2 . HIS A 18 ? 0.3311 0.3358 0.3310 -0.0727 -0.0088 0.0543 18 HIS A NE2 80 N N . ALA A 19 ? 0.3713 0.3374 0.3363 -0.0864 -0.0178 0.0598 19 ALA A N 81 C CA . ALA A 19 ? 0.3978 0.3502 0.3546 -0.0844 -0.0225 0.0589 19 ALA A CA 82 C C . ALA A 19 ? 0.4247 0.3756 0.3785 -0.0919 -0.0245 0.0607 19 ALA A C 83 O O . ALA A 19 ? 0.4403 0.3983 0.3957 -0.0990 -0.0227 0.0628 19 ALA A O 84 C CB . ALA A 19 ? 0.4124 0.3495 0.3572 -0.0833 -0.0258 0.0591 19 ALA A CB 85 N N . VAL A 20 ? 0.4414 0.3839 0.3908 -0.0904 -0.0281 0.0598 20 VAL A N 86 C CA . VAL A 20 ? 0.4754 0.4172 0.4226 -0.0971 -0.0300 0.0613 20 VAL A CA 87 C C . VAL A 20 ? 0.5222 0.4443 0.4549 -0.0982 -0.0359 0.0616 20 VAL A C 88 O O . VAL A 20 ? 0.5242 0.4360 0.4513 -0.0914 -0.0383 0.0598 20 VAL A O 89 C CB . VAL A 20 ? 0.4738 0.4271 0.4317 -0.0945 -0.0284 0.0598 20 VAL A CB 90 C CG1 . VAL A 20 ? 0.4654 0.4368 0.4362 -0.0930 -0.0229 0.0595 20 VAL A CG1 91 C CG2 . VAL A 20 ? 0.4570 0.4038 0.4142 -0.0861 -0.0306 0.0572 20 VAL A CG2 92 N N . PRO A 21 ? 0.5796 0.4963 0.5054 -0.1069 -0.0384 0.0638 21 PRO A N 93 C CA . PRO A 21 ? 0.6273 0.5233 0.5374 -0.1082 -0.0445 0.0641 21 PRO A CA 94 C C . PRO A 21 ? 0.6448 0.5354 0.5543 -0.1023 -0.0475 0.0619 21 PRO A C 95 O O . PRO A 21 ? 0.7200 0.5933 0.6173 -0.0992 -0.0525 0.0610 21 PRO A O 96 C CB . PRO A 21 ? 0.6244 0.5179 0.5277 -0.1204 -0.0458 0.0674 21 PRO A CB 97 C CG . PRO A 21 ? 0.6140 0.5291 0.5319 -0.1239 -0.0410 0.0678 21 PRO A CG 98 C CD . PRO A 21 ? 0.5859 0.5149 0.5167 -0.1160 -0.0361 0.0659 21 PRO A CD 99 N N . ASN A 22 ? 0.6293 0.5342 0.5513 -0.1005 -0.0448 0.0608 22 ASN A N 100 C CA . ASN A 22 ? 0.6341 0.5354 0.5562 -0.0957 -0.0474 0.0587 22 ASN A CA 101 C C . ASN A 22 ? 0.5733 0.4857 0.5072 -0.0860 -0.0443 0.0558 22 ASN A C 102 O O . ASN A 22 ? 0.5383 0.4627 0.4824 -0.0855 -0.0419 0.0552 22 ASN A O 103 C CB . ASN A 22 ? 0.6535 0.5609 0.5787 -0.1029 -0.0475 0.0601 22 ASN A CB 104 C CG . ASN A 22 ? 0.6942 0.6231 0.6343 -0.1048 -0.0418 0.0605 22 ASN A CG 105 O OD1 . ASN A 22 ? 0.7278 0.6654 0.6735 -0.1044 -0.0380 0.0609 22 ASN A OD1 106 N ND2 . ASN A 22 ? 0.7134 0.6509 0.6600 -0.1064 -0.0413 0.0602 22 ASN A ND2 107 N N . GLY A 23 ? 0.5620 0.4700 0.4938 -0.0787 -0.0446 0.0540 23 GLY A N 108 C CA . GLY A 23 ? 0.5474 0.4661 0.4896 -0.0704 -0.0415 0.0514 23 GLY A CA 109 C C . GLY A 23 ? 0.5409 0.4561 0.4823 -0.0649 -0.0443 0.0490 23 GLY A C 110 O O . GLY A 23 ? 0.5429 0.4458 0.4746 -0.0667 -0.0489 0.0493 23 GLY A O 111 N N . THR A 24 ? 0.4878 0.4132 0.4384 -0.0586 -0.0416 0.0468 24 THR A N 112 C CA . THR A 24 ? 0.4801 0.4044 0.4311 -0.0532 -0.0437 0.0445 24 THR A CA 113 C C . THR A 24 ? 0.4384 0.3645 0.3905 -0.0446 -0.0433 0.0415 24 THR A C 114 O O . THR A 24 ? 0.4079 0.3428 0.3663 -0.0429 -0.0395 0.0411 24 THR A O 115 C CB . THR A 24 ? 0.5137 0.4510 0.4760 -0.0543 -0.0406 0.0445 24 THR A CB 116 O OG1 . THR A 24 ? 0.5853 0.5269 0.5502 -0.0623 -0.0392 0.0472 24 THR A OG1 117 C CG2 . THR A 24 ? 0.5298 0.4632 0.4901 -0.0514 -0.0437 0.0429 24 THR A CG2 118 N N . ILE A 25 ? 0.3993 0.3185 0.3457 -0.0393 -0.0471 0.0392 25 ILE A N 119 C CA . ILE A 25 ? 0.4093 0.3305 0.3554 -0.0310 -0.0474 0.0361 25 ILE A CA 120 C C . ILE A 25 ? 0.3605 0.2953 0.3176 -0.0280 -0.0440 0.0345 25 ILE A C 121 O O . ILE A 25 ? 0.3434 0.2801 0.3033 -0.0292 -0.0444 0.0346 25 ILE A O 122 C CB . ILE A 25 ? 0.4397 0.3471 0.3734 -0.0259 -0.0534 0.0340 25 ILE A CB 123 C CG1 . ILE A 25 ? 0.4796 0.3720 0.4010 -0.0289 -0.0568 0.0356 25 ILE A CG1 124 C CG2 . ILE A 25 ? 0.4453 0.3575 0.3795 -0.0170 -0.0535 0.0303 25 ILE A CG2 125 C CD1 . ILE A 25 ? 0.4999 0.3932 0.4201 -0.0266 -0.0554 0.0352 25 ILE A CD1 126 N N . VAL A 26 ? 0.3403 0.2843 0.3031 -0.0246 -0.0407 0.0332 26 VAL A N 127 C CA . VAL A 26 ? 0.3153 0.2710 0.2866 -0.0216 -0.0378 0.0315 26 VAL A CA 128 C C . VAL A 26 ? 0.3218 0.2805 0.2915 -0.0148 -0.0382 0.0283 26 VAL A C 129 O O . VAL A 26 ? 0.3274 0.2802 0.2904 -0.0125 -0.0402 0.0276 26 VAL A O 130 C CB . VAL A 26 ? 0.2919 0.2588 0.2734 -0.0253 -0.0325 0.0331 26 VAL A CB 131 C CG1 . VAL A 26 ? 0.2866 0.2531 0.2705 -0.0316 -0.0320 0.0358 26 VAL A CG1 132 C CG2 . VAL A 26 ? 0.2782 0.2475 0.2603 -0.0254 -0.0301 0.0335 26 VAL A CG2 133 N N . LYS A 27 ? 0.3207 0.2890 0.2962 -0.0120 -0.0363 0.0265 27 LYS A N 134 C CA . LYS A 27 ? 0.3318 0.3065 0.3073 -0.0063 -0.0360 0.0234 27 LYS A CA 135 C C . LYS A 27 ? 0.3194 0.3055 0.3030 -0.0078 -0.0309 0.0236 27 LYS A C 136 O O . LYS A 27 ? 0.2883 0.2801 0.2786 -0.0111 -0.0278 0.0250 27 LYS A O 137 C CB . LYS A 27 ? 0.3597 0.3374 0.3350 -0.0021 -0.0378 0.0209 27 LYS A CB 138 C CG . LYS A 27 ? 0.3979 0.3851 0.3742 0.0031 -0.0370 0.0175 27 LYS A CG 139 C CD . LYS A 27 ? 0.4308 0.4208 0.4065 0.0069 -0.0390 0.0152 27 LYS A CD 140 C CE . LYS A 27 ? 0.4586 0.4612 0.4370 0.0108 -0.0374 0.0120 27 LYS A CE 141 N NZ . LYS A 27 ? 0.4723 0.4779 0.4498 0.0144 -0.0395 0.0097 27 LYS A NZ 142 N N . THR A 28 ? 0.3218 0.3110 0.3040 -0.0052 -0.0301 0.0222 28 THR A N 143 C CA . THR A 28 ? 0.3264 0.3262 0.3152 -0.0064 -0.0256 0.0221 28 THR A CA 144 C C . THR A 28 ? 0.3523 0.3599 0.3403 -0.0013 -0.0260 0.0185 28 THR A C 145 O O . THR A 28 ? 0.3691 0.3744 0.3520 0.0033 -0.0296 0.0161 28 THR A O 146 C CB . THR A 28 ? 0.3275 0.3260 0.3165 -0.0089 -0.0237 0.0237 28 THR A CB 147 O OG1 . THR A 28 ? 0.3391 0.3329 0.3211 -0.0050 -0.0265 0.0221 28 THR A OG1 148 C CG2 . THR A 28 ? 0.3452 0.3375 0.3348 -0.0141 -0.0233 0.0271 28 THR A CG2 149 N N . ILE A 29 ? 0.3546 0.3716 0.3471 -0.0023 -0.0224 0.0179 29 ILE A N 150 C CA . ILE A 29 ? 0.3708 0.3965 0.3622 0.0017 -0.0225 0.0145 29 ILE A CA 151 C C . ILE A 29 ? 0.3855 0.4077 0.3708 0.0059 -0.0251 0.0129 29 ILE A C 152 O O . ILE A 29 ? 0.4102 0.4358 0.3917 0.0113 -0.0276 0.0096 29 ILE A O 153 C CB . ILE A 29 ? 0.3750 0.4110 0.3718 -0.0012 -0.0181 0.0145 29 ILE A CB 154 C CG1 . ILE A 29 ? 0.3915 0.4299 0.3931 -0.0049 -0.0159 0.0160 29 ILE A CG1 155 C CG2 . ILE A 29 ? 0.3848 0.4311 0.3803 0.0024 -0.0183 0.0109 29 ILE A CG2 156 C CD1 . ILE A 29 ? 0.4243 0.4664 0.4253 -0.0022 -0.0177 0.0139 29 ILE A CD1 157 N N . THR A 30 ? 0.3895 0.4051 0.3734 0.0036 -0.0247 0.0151 30 THR A N 158 C CA . THR A 30 ? 0.4137 0.4248 0.3913 0.0073 -0.0271 0.0138 30 THR A CA 159 C C . THR A 30 ? 0.4493 0.4480 0.4180 0.0110 -0.0324 0.0133 30 THR A C 160 O O . THR A 30 ? 0.4259 0.4227 0.3880 0.0168 -0.0357 0.0106 30 THR A O 161 C CB . THR A 30 ? 0.4146 0.4225 0.3934 0.0032 -0.0247 0.0165 30 THR A CB 162 O OG1 . THR A 30 ? 0.4104 0.4287 0.3961 0.0002 -0.0201 0.0168 30 THR A OG1 163 C CG2 . THR A 30 ? 0.4247 0.4272 0.3962 0.0070 -0.0273 0.0153 30 THR A CG2 164 N N . ASN A 31 ? 0.4355 0.4257 0.4037 0.0076 -0.0335 0.0158 31 ASN A N 165 C CA . ASN A 31 ? 0.4657 0.4420 0.4244 0.0097 -0.0387 0.0159 31 ASN A CA 166 C C . ASN A 31 ? 0.4483 0.4222 0.4071 0.0097 -0.0406 0.0158 31 ASN A C 167 O O . ASN A 31 ? 0.4173 0.3936 0.3825 0.0046 -0.0380 0.0181 31 ASN A O 168 C CB . ASN A 31 ? 0.4902 0.4562 0.4465 0.0042 -0.0386 0.0196 31 ASN A CB 169 C CG . ASN A 31 ? 0.5214 0.4867 0.4753 0.0047 -0.0378 0.0197 31 ASN A CG 170 O OD1 . ASN A 31 ? 0.5938 0.5528 0.5391 0.0098 -0.0414 0.0177 31 ASN A OD1 171 N ND2 . ASN A 31 ? 0.5040 0.4752 0.4649 -0.0001 -0.0332 0.0219 31 ASN A ND2 172 N N . ASP A 32 ? 0.4536 0.4224 0.4048 0.0157 -0.0453 0.0131 32 ASP A N 173 C CA . ASP A 32 ? 0.4753 0.4383 0.4243 0.0157 -0.0480 0.0133 32 ASP A CA 174 C C . ASP A 32 ? 0.4530 0.4040 0.3996 0.0093 -0.0489 0.0172 32 ASP A C 175 O O . ASP A 32 ? 0.4271 0.3779 0.3771 0.0060 -0.0485 0.0185 32 ASP A O 176 C CB . ASP A 32 ? 0.5609 0.5176 0.4998 0.0237 -0.0537 0.0098 32 ASP A CB 177 C CG . ASP A 32 ? 0.6366 0.6072 0.5784 0.0300 -0.0530 0.0056 32 ASP A CG 178 O OD1 . ASP A 32 ? 0.7111 0.6947 0.6626 0.0274 -0.0488 0.0057 32 ASP A OD1 179 O OD2 . ASP A 32 ? 0.7404 0.7091 0.6743 0.0376 -0.0570 0.0022 32 ASP A OD2 180 N N . GLN A 33 ? 0.4313 0.3729 0.3721 0.0073 -0.0500 0.0188 33 GLN A N 181 C CA . GLN A 33 ? 0.4533 0.3840 0.3910 0.0004 -0.0509 0.0225 33 GLN A CA 182 C C . GLN A 33 ? 0.4338 0.3648 0.3731 -0.0039 -0.0480 0.0249 33 GLN A C 183 O O . GLN A 33 ? 0.4531 0.3808 0.3869 -0.0006 -0.0492 0.0238 33 GLN A O 184 C CB . GLN A 33 ? 0.5061 0.4196 0.4299 0.0026 -0.0573 0.0221 33 GLN A CB 185 C CG . GLN A 33 ? 0.5476 0.4589 0.4687 0.0065 -0.0606 0.0200 33 GLN A CG 186 C CD . GLN A 33 ? 0.6203 0.5129 0.5280 0.0060 -0.0667 0.0207 33 GLN A CD 187 O OE1 . GLN A 33 ? 0.7026 0.5822 0.5999 0.0055 -0.0697 0.0215 33 GLN A OE1 188 N NE2 . GLN A 33 ? 0.6668 0.5572 0.5741 0.0060 -0.0687 0.0203 33 GLN A NE2 189 N N . ILE A 34 ? 0.3854 0.3215 0.3326 -0.0108 -0.0441 0.0280 34 ILE A N 190 C CA . ILE A 34 ? 0.3722 0.3082 0.3205 -0.0154 -0.0416 0.0304 34 ILE A CA 191 C C . ILE A 34 ? 0.3590 0.2924 0.3091 -0.0232 -0.0407 0.0338 34 ILE A C 192 O O . ILE A 34 ? 0.3355 0.2752 0.2924 -0.0251 -0.0391 0.0343 34 ILE A O 193 C CB . ILE A 34 ? 0.3747 0.3245 0.3326 -0.0148 -0.0363 0.0299 34 ILE A CB 194 C CG1 . ILE A 34 ? 0.3878 0.3370 0.3465 -0.0195 -0.0339 0.0324 34 ILE A CG1 195 C CG2 . ILE A 34 ? 0.3574 0.3186 0.3258 -0.0164 -0.0327 0.0300 34 ILE A CG2 196 C CD1 . ILE A 34 ? 0.3899 0.3501 0.3555 -0.0182 -0.0297 0.0316 34 ILE A CD1 197 N N . GLU A 35 ? 0.3615 0.2859 0.3052 -0.0277 -0.0420 0.0362 35 GLU A N 198 C CA . GLU A 35 ? 0.3714 0.2947 0.3165 -0.0357 -0.0412 0.0394 35 GLU A CA 199 C C . GLU A 35 ? 0.3419 0.2782 0.2979 -0.0395 -0.0355 0.0411 35 GLU A C 200 O O . GLU A 35 ? 0.3453 0.2842 0.3021 -0.0390 -0.0333 0.0412 35 GLU A O 201 C CB . GLU A 35 ? 0.4152 0.3232 0.3478 -0.0397 -0.0451 0.0413 35 GLU A CB 202 C CG . GLU A 35 ? 0.4588 0.3646 0.3909 -0.0483 -0.0453 0.0443 35 GLU A CG 203 C CD . GLU A 35 ? 0.5322 0.4223 0.4508 -0.0532 -0.0493 0.0464 35 GLU A CD 204 O OE1 . GLU A 35 ? 0.6043 0.4797 0.5109 -0.0503 -0.0546 0.0453 35 GLU A OE1 205 O OE2 . GLU A 35 ? 0.5425 0.4346 0.4619 -0.0598 -0.0471 0.0491 35 GLU A OE2 206 N N . VAL A 36 ? 0.3260 0.2697 0.2893 -0.0433 -0.0333 0.0422 36 VAL A N 207 C CA . VAL A 36 ? 0.3145 0.2699 0.2873 -0.0470 -0.0285 0.0438 36 VAL A CA 208 C C . VAL A 36 ? 0.3251 0.2799 0.2974 -0.0546 -0.0287 0.0466 36 VAL A C 209 O O . VAL A 36 ? 0.3315 0.2773 0.2969 -0.0572 -0.0324 0.0472 36 VAL A O 210 C CB . VAL A 36 ? 0.2994 0.2664 0.2821 -0.0436 -0.0254 0.0422 36 VAL A CB 211 C CG1 . VAL A 36 ? 0.2809 0.2504 0.2643 -0.0373 -0.0246 0.0397 36 VAL A CG1 212 C CG2 . VAL A 36 ? 0.2831 0.2495 0.2666 -0.0433 -0.0274 0.0416 36 VAL A CG2 213 N N . THR A 37 ? 0.3166 0.2813 0.2958 -0.0583 -0.0247 0.0481 37 THR A N 214 C CA . THR A 37 ? 0.3290 0.2953 0.3079 -0.0659 -0.0246 0.0506 37 THR A CA 215 C C . THR A 37 ? 0.3359 0.3068 0.3190 -0.0675 -0.0251 0.0506 37 THR A C 216 O O . THR A 37 ? 0.3298 0.2987 0.3099 -0.0736 -0.0266 0.0523 37 THR A O 217 C CB . THR A 37 ? 0.3256 0.3025 0.3107 -0.0687 -0.0203 0.0519 37 THR A CB 218 O OG1 . THR A 37 ? 0.3305 0.3194 0.3257 -0.0651 -0.0167 0.0507 37 THR A OG1 219 C CG2 . THR A 37 ? 0.3104 0.2828 0.2913 -0.0673 -0.0198 0.0520 37 THR A CG2 220 N N . ASN A 38 ? 0.3266 0.3033 0.3160 -0.0623 -0.0238 0.0487 38 ASN A N 221 C CA . ASN A 38 ? 0.3460 0.3275 0.3396 -0.0634 -0.0241 0.0486 38 ASN A CA 222 C C . ASN A 38 ? 0.3205 0.3039 0.3178 -0.0567 -0.0239 0.0461 38 ASN A C 223 O O . ASN A 38 ? 0.2895 0.2752 0.2889 -0.0522 -0.0220 0.0448 38 ASN A O 224 C CB . ASN A 38 ? 0.3690 0.3635 0.3707 -0.0669 -0.0205 0.0498 38 ASN A CB 225 C CG . ASN A 38 ? 0.4243 0.4239 0.4295 -0.0693 -0.0211 0.0500 38 ASN A CG 226 O OD1 . ASN A 38 ? 0.4161 0.4083 0.4162 -0.0712 -0.0246 0.0501 38 ASN A OD1 227 N ND2 . ASN A 38 ? 0.5181 0.5304 0.5316 -0.0690 -0.0179 0.0499 38 ASN A ND2 228 N N . ALA A 39 ? 0.3144 0.2970 0.3120 -0.0566 -0.0258 0.0456 39 ALA A N 229 C CA . ALA A 39 ? 0.3133 0.2988 0.3147 -0.0510 -0.0255 0.0435 39 ALA A CA 230 C C . ALA A 39 ? 0.3209 0.3109 0.3262 -0.0526 -0.0258 0.0437 39 ALA A C 231 O O . ALA A 39 ? 0.3224 0.3122 0.3265 -0.0581 -0.0270 0.0453 39 ALA A O 232 C CB . ALA A 39 ? 0.3016 0.2774 0.2959 -0.0465 -0.0289 0.0417 39 ALA A CB 233 N N . THR A 40 ? 0.3105 0.3054 0.3206 -0.0483 -0.0247 0.0420 40 THR A N 234 C CA . THR A 40 ? 0.3235 0.3222 0.3370 -0.0489 -0.0252 0.0419 40 THR A CA 235 C C . THR A 40 ? 0.3111 0.3062 0.3230 -0.0441 -0.0272 0.0399 40 THR A C 236 O O . THR A 40 ? 0.3009 0.2956 0.3124 -0.0397 -0.0265 0.0383 40 THR A O 237 C CB . THR A 40 ? 0.3283 0.3388 0.3501 -0.0491 -0.0214 0.0422 40 THR A CB 238 O OG1 . THR A 40 ? 0.3765 0.3908 0.4009 -0.0510 -0.0223 0.0425 40 THR A OG1 239 C CG2 . THR A 40 ? 0.3417 0.3557 0.3668 -0.0438 -0.0192 0.0407 40 THR A CG2 240 N N . GLU A 41 ? 0.3012 0.2942 0.3121 -0.0451 -0.0297 0.0398 41 GLU A N 241 C CA . GLU A 41 ? 0.3062 0.2957 0.3151 -0.0408 -0.0319 0.0379 41 GLU A CA 242 C C . GLU A 41 ? 0.2884 0.2865 0.3041 -0.0375 -0.0292 0.0367 41 GLU A C 243 O O . GLU A 41 ? 0.2803 0.2852 0.3012 -0.0393 -0.0274 0.0375 41 GLU A O 244 C CB . GLU A 41 ? 0.3278 0.3111 0.3324 -0.0436 -0.0358 0.0383 41 GLU A CB 245 C CG . GLU A 41 ? 0.3324 0.3119 0.3346 -0.0394 -0.0384 0.0364 41 GLU A CG 246 C CD . GLU A 41 ? 0.3472 0.3205 0.3437 -0.0343 -0.0402 0.0344 41 GLU A CD 247 O OE1 . GLU A 41 ? 0.3640 0.3274 0.3525 -0.0350 -0.0433 0.0346 41 GLU A OE1 248 O OE2 . GLU A 41 ? 0.3014 0.2797 0.3010 -0.0296 -0.0385 0.0326 41 GLU A OE2 249 N N . LEU A 42 ? 0.2655 0.2632 0.2804 -0.0327 -0.0291 0.0348 42 LEU A N 250 C CA . LEU A 42 ? 0.2576 0.2622 0.2774 -0.0300 -0.0267 0.0338 42 LEU A CA 251 C C . LEU A 42 ? 0.2466 0.2499 0.2654 -0.0276 -0.0290 0.0324 42 LEU A C 252 O O . LEU A 42 ? 0.2299 0.2381 0.2520 -0.0257 -0.0273 0.0317 42 LEU A O 253 C CB . LEU A 42 ? 0.2621 0.2695 0.2824 -0.0272 -0.0244 0.0327 42 LEU A CB 254 C CG . LEU A 42 ? 0.2684 0.2787 0.2909 -0.0291 -0.0214 0.0340 42 LEU A CG 255 C CD1 . LEU A 42 ? 0.2661 0.2794 0.2890 -0.0265 -0.0191 0.0327 42 LEU A CD1 256 C CD2 . LEU A 42 ? 0.2610 0.2768 0.2885 -0.0316 -0.0192 0.0355 42 LEU A CD2 257 N N . VAL A 43 ? 0.2433 0.2394 0.2568 -0.0275 -0.0328 0.0320 43 VAL A N 258 C CA . VAL A 43 ? 0.2509 0.2451 0.2628 -0.0251 -0.0353 0.0306 43 VAL A CA 259 C C . VAL A 43 ? 0.2657 0.2574 0.2774 -0.0288 -0.0374 0.0319 43 VAL A C 260 O O . VAL A 43 ? 0.2643 0.2493 0.2714 -0.0319 -0.0399 0.0329 43 VAL A O 261 C CB . VAL A 43 ? 0.2548 0.2422 0.2598 -0.0212 -0.0387 0.0286 43 VAL A CB 262 C CG1 . VAL A 43 ? 0.2609 0.2470 0.2645 -0.0186 -0.0412 0.0271 43 VAL A CG1 263 C CG2 . VAL A 43 ? 0.2552 0.2464 0.2604 -0.0176 -0.0367 0.0270 43 VAL A CG2 264 N N . GLN A 44 ? 0.2585 0.2556 0.2748 -0.0288 -0.0365 0.0319 44 GLN A N 265 C CA . GLN A 44 ? 0.2674 0.2634 0.2838 -0.0320 -0.0386 0.0328 44 GLN A CA 266 C C . GLN A 44 ? 0.2889 0.2770 0.2993 -0.0300 -0.0428 0.0314 44 GLN A C 267 O O . GLN A 44 ? 0.2672 0.2561 0.2774 -0.0255 -0.0432 0.0296 44 GLN A O 268 C CB . GLN A 44 ? 0.2593 0.2637 0.2822 -0.0317 -0.0363 0.0329 44 GLN A CB 269 C CG . GLN A 44 ? 0.2658 0.2714 0.2899 -0.0350 -0.0381 0.0337 44 GLN A CG 270 C CD . GLN A 44 ? 0.2709 0.2778 0.2953 -0.0406 -0.0379 0.0356 44 GLN A CD 271 O OE1 . GLN A 44 ? 0.2852 0.2965 0.3123 -0.0415 -0.0350 0.0364 44 GLN A OE1 272 N NE2 . GLN A 44 ? 0.2723 0.2752 0.2934 -0.0447 -0.0410 0.0363 44 GLN A NE2 273 N N . SER A 45 ? 0.2963 0.2765 0.3010 -0.0333 -0.0462 0.0322 45 SER A N 274 C CA . SER A 45 ? 0.3462 0.3172 0.3438 -0.0311 -0.0508 0.0308 45 SER A CA 275 C C . SER A 45 ? 0.3878 0.3556 0.3836 -0.0350 -0.0536 0.0316 45 SER A C 276 O O . SER A 45 ? 0.4284 0.3878 0.4177 -0.0333 -0.0577 0.0305 45 SER A O 277 C CB . SER A 45 ? 0.3630 0.3238 0.3520 -0.0298 -0.0534 0.0303 45 SER A CB 278 O OG . SER A 45 ? 0.4088 0.3650 0.3947 -0.0358 -0.0541 0.0325 45 SER A OG 279 N N . SER A 46 ? 0.4076 0.3822 0.4088 -0.0399 -0.0518 0.0333 46 SER A N 280 C CA . SER A 46 ? 0.4502 0.4235 0.4504 -0.0439 -0.0543 0.0340 46 SER A CA 281 C C . SER A 46 ? 0.4573 0.4419 0.4661 -0.0433 -0.0518 0.0338 46 SER A C 282 O O . SER A 46 ? 0.3925 0.3862 0.4079 -0.0417 -0.0478 0.0340 46 SER A O 283 C CB . SER A 46 ? 0.4706 0.4417 0.4681 -0.0514 -0.0551 0.0362 46 SER A CB 284 O OG . SER A 46 ? 0.4819 0.4637 0.4866 -0.0535 -0.0508 0.0374 46 SER A OG 285 N N . SER A 47 ? 0.4784 0.4619 0.4862 -0.0443 -0.0543 0.0335 47 SER A N 286 C CA . SER A 47 ? 0.5012 0.4947 0.5161 -0.0447 -0.0527 0.0335 47 SER A CA 287 C C . SER A 47 ? 0.5428 0.5362 0.5561 -0.0514 -0.0551 0.0348 47 SER A C 288 O O . SER A 47 ? 0.5552 0.5383 0.5607 -0.0543 -0.0589 0.0351 47 SER A O 289 C CB . SER A 47 ? 0.5250 0.5178 0.5402 -0.0394 -0.0538 0.0317 47 SER A CB 290 O OG . SER A 47 ? 0.5281 0.5293 0.5490 -0.0401 -0.0529 0.0317 47 SER A OG 291 N N . THR A 48 ? 0.5706 0.5755 0.5908 -0.0537 -0.0531 0.0353 48 THR A N 292 C CA . THR A 48 ? 0.6135 0.6212 0.6335 -0.0597 -0.0552 0.0361 48 THR A CA 293 C C . THR A 48 ? 0.5955 0.5959 0.6110 -0.0588 -0.0591 0.0351 48 THR A C 294 O O . THR A 48 ? 0.6365 0.6334 0.6478 -0.0645 -0.0622 0.0358 48 THR A O 295 C CB . THR A 48 ? 0.6324 0.6554 0.6613 -0.0597 -0.0523 0.0361 48 THR A CB 296 O OG1 . THR A 48 ? 0.6897 0.7199 0.7230 -0.0591 -0.0484 0.0367 48 THR A OG1 297 C CG2 . THR A 48 ? 0.6582 0.6864 0.6872 -0.0667 -0.0542 0.0368 48 THR A CG2 298 N N . GLY A 49 ? 0.5559 0.5544 0.5721 -0.0519 -0.0590 0.0334 49 GLY A N 299 C CA . GLY A 49 ? 0.5487 0.5409 0.5609 -0.0502 -0.0626 0.0322 49 GLY A CA 300 C C . GLY A 49 ? 0.5200 0.5219 0.5387 -0.0486 -0.0616 0.0315 49 GLY A C 301 O O . GLY A 49 ? 0.5502 0.5482 0.5667 -0.0462 -0.0641 0.0303 49 GLY A O 302 N N . GLY A 50 ? 0.4320 0.4463 0.4582 -0.0496 -0.0583 0.0321 50 GLY A N 303 C CA . GLY A 50 ? 0.3897 0.4132 0.4218 -0.0469 -0.0572 0.0312 50 GLY A CA 304 C C . GLY A 50 ? 0.3336 0.3636 0.3710 -0.0412 -0.0533 0.0306 50 GLY A C 305 O O . GLY A 50 ? 0.3006 0.3323 0.3394 -0.0408 -0.0507 0.0312 50 GLY A O 306 N N . ILE A 51 ? 0.3065 0.3395 0.3462 -0.0369 -0.0532 0.0294 51 ILE A N 307 C CA . ILE A 51 ? 0.3103 0.3488 0.3540 -0.0318 -0.0500 0.0289 51 ILE A CA 308 C C . ILE A 51 ? 0.3132 0.3634 0.3624 -0.0329 -0.0484 0.0291 51 ILE A C 309 O O . ILE A 51 ? 0.3075 0.3625 0.3583 -0.0338 -0.0500 0.0286 51 ILE A O 310 C CB . ILE A 51 ? 0.3105 0.3461 0.3531 -0.0268 -0.0507 0.0275 51 ILE A CB 311 C CG1 . ILE A 51 ? 0.3357 0.3618 0.3732 -0.0247 -0.0517 0.0269 51 ILE A CG1 312 C CG2 . ILE A 51 ? 0.3215 0.3627 0.3673 -0.0224 -0.0478 0.0271 51 ILE A CG2 313 C CD1 . ILE A 51 ? 0.3425 0.3655 0.3780 -0.0208 -0.0532 0.0255 51 ILE A CD1 314 N N . CYS A 52 ? 0.3085 0.3637 0.3603 -0.0325 -0.0454 0.0297 52 CYS A N 315 C CA . CYS A 52 ? 0.3120 0.3791 0.3688 -0.0323 -0.0438 0.0296 52 CYS A CA 316 C C . CYS A 52 ? 0.2999 0.3702 0.3583 -0.0264 -0.0431 0.0283 52 CYS A C 317 O O . CYS A 52 ? 0.2659 0.3306 0.3223 -0.0220 -0.0419 0.0279 52 CYS A O 318 C CB . CYS A 52 ? 0.3483 0.4188 0.4065 -0.0330 -0.0409 0.0304 52 CYS A CB 319 S SG . CYS A 52 ? 0.3888 0.4573 0.4452 -0.0408 -0.0417 0.0320 52 CYS A SG 320 N N . ASP A 53 ? 0.2770 0.3565 0.3385 -0.0264 -0.0439 0.0276 53 ASP A N 321 C CA . ASP A 53 ? 0.2956 0.3779 0.3579 -0.0207 -0.0439 0.0263 53 ASP A CA 322 C C . ASP A 53 ? 0.2815 0.3684 0.3450 -0.0160 -0.0412 0.0259 53 ASP A C 323 O O . ASP A 53 ? 0.2874 0.3755 0.3504 -0.0109 -0.0412 0.0248 53 ASP A O 324 C CB . ASP A 53 ? 0.3101 0.4007 0.3750 -0.0221 -0.0462 0.0255 53 ASP A CB 325 C CG . ASP A 53 ? 0.3256 0.4299 0.3949 -0.0246 -0.0454 0.0253 53 ASP A CG 326 O OD1 . ASP A 53 ? 0.3456 0.4532 0.4160 -0.0250 -0.0432 0.0259 53 ASP A OD1 327 O OD2 . ASP A 53 ? 0.3711 0.4838 0.4427 -0.0262 -0.0472 0.0246 53 ASP A OD2 328 N N . SER A 54 ? 0.2719 0.3606 0.3363 -0.0177 -0.0392 0.0267 54 SER A N 329 C CA . SER A 54 ? 0.2714 0.3628 0.3360 -0.0134 -0.0366 0.0263 54 SER A CA 330 C C . SER A 54 ? 0.2682 0.3517 0.3304 -0.0143 -0.0347 0.0274 54 SER A C 331 O O . SER A 54 ? 0.2622 0.3423 0.3241 -0.0192 -0.0351 0.0285 54 SER A O 332 C CB . SER A 54 ? 0.2756 0.3806 0.3445 -0.0145 -0.0360 0.0260 54 SER A CB 333 O OG . SER A 54 ? 0.2725 0.3861 0.3440 -0.0147 -0.0380 0.0249 54 SER A OG 334 N N . PRO A 55 ? 0.2570 0.3372 0.3168 -0.0099 -0.0327 0.0272 55 PRO A N 335 C CA . PRO A 55 ? 0.2707 0.3525 0.3291 -0.0039 -0.0324 0.0260 55 PRO A CA 336 C C . PRO A 55 ? 0.2673 0.3403 0.3212 -0.0006 -0.0332 0.0256 55 PRO A C 337 O O . PRO A 55 ? 0.2706 0.3429 0.3218 0.0044 -0.0332 0.0247 55 PRO A O 338 C CB . PRO A 55 ? 0.2707 0.3510 0.3275 -0.0023 -0.0299 0.0264 55 PRO A CB 339 C CG . PRO A 55 ? 0.2688 0.3407 0.3238 -0.0058 -0.0290 0.0276 55 PRO A CG 340 C CD . PRO A 55 ? 0.2687 0.3421 0.3263 -0.0109 -0.0308 0.0281 55 PRO A CD 341 N N . HIS A 56 ? 0.2503 0.3169 0.3030 -0.0032 -0.0342 0.0260 56 HIS A N 342 C CA . HIS A 56 ? 0.2570 0.3162 0.3055 -0.0006 -0.0350 0.0256 56 HIS A CA 343 C C . HIS A 56 ? 0.2593 0.3219 0.3093 0.0001 -0.0375 0.0248 56 HIS A C 344 O O . HIS A 56 ? 0.2582 0.3267 0.3121 -0.0031 -0.0389 0.0248 56 HIS A O 345 C CB . HIS A 56 ? 0.2687 0.3203 0.3150 -0.0032 -0.0349 0.0262 56 HIS A CB 346 C CG . HIS A 56 ? 0.2656 0.3145 0.3109 -0.0045 -0.0326 0.0270 56 HIS A CG 347 N ND1 . HIS A 56 ? 0.2742 0.3197 0.3160 -0.0021 -0.0307 0.0271 56 HIS A ND1 348 C CD2 . HIS A 56 ? 0.2676 0.3163 0.3144 -0.0082 -0.0321 0.0278 56 HIS A CD2 349 C CE1 . HIS A 56 ? 0.2776 0.3216 0.3193 -0.0042 -0.0289 0.0278 56 HIS A CE1 350 N NE2 . HIS A 56 ? 0.2740 0.3200 0.3188 -0.0077 -0.0297 0.0282 56 HIS A NE2 351 N N . GLN A 57 ? 0.2481 0.3070 0.2946 0.0040 -0.0381 0.0241 57 GLN A N 352 C CA . GLN A 57 ? 0.2441 0.3054 0.2914 0.0051 -0.0405 0.0232 57 GLN A CA 353 C C . GLN A 57 ? 0.2419 0.2981 0.2884 0.0024 -0.0419 0.0234 57 GLN A C 354 O O . GLN A 57 ? 0.2339 0.2826 0.2763 0.0033 -0.0415 0.0235 57 GLN A O 355 C CB . GLN A 57 ? 0.2416 0.3000 0.2845 0.0106 -0.0409 0.0223 57 GLN A CB 356 C CG . GLN A 57 ? 0.2386 0.3003 0.2826 0.0121 -0.0434 0.0213 57 GLN A CG 357 C CD . GLN A 57 ? 0.2460 0.3049 0.2853 0.0178 -0.0441 0.0204 57 GLN A CD 358 O OE1 . GLN A 57 ? 0.2620 0.3125 0.2952 0.0199 -0.0429 0.0207 57 GLN A OE1 359 N NE2 . GLN A 57 ? 0.2362 0.3013 0.2774 0.0201 -0.0461 0.0192 57 GLN A NE2 360 N N . ILE A 58 ? 0.2523 0.3125 0.3023 -0.0010 -0.0437 0.0234 58 ILE A N 361 C CA . ILE A 58 ? 0.2641 0.3194 0.3130 -0.0036 -0.0456 0.0235 58 ILE A CA 362 C C . ILE A 58 ? 0.2805 0.3365 0.3291 -0.0019 -0.0480 0.0225 58 ILE A C 363 O O . ILE A 58 ? 0.2943 0.3576 0.3457 -0.0012 -0.0490 0.0219 58 ILE A O 364 C CB . ILE A 58 ? 0.2833 0.3409 0.3347 -0.0089 -0.0466 0.0242 58 ILE A CB 365 C CG1 . ILE A 58 ? 0.2902 0.3480 0.3422 -0.0108 -0.0443 0.0251 58 ILE A CG1 366 C CG2 . ILE A 58 ? 0.2951 0.3456 0.3438 -0.0109 -0.0489 0.0241 58 ILE A CG2 367 C CD1 . ILE A 58 ? 0.2985 0.3486 0.3470 -0.0096 -0.0426 0.0255 58 ILE A CD1 368 N N . LEU A 59 ? 0.2701 0.3194 0.3153 -0.0010 -0.0490 0.0222 59 LEU A N 369 C CA . LEU A 59 ? 0.2801 0.3294 0.3248 0.0000 -0.0517 0.0213 59 LEU A CA 370 C C . LEU A 59 ? 0.2892 0.3339 0.3328 -0.0029 -0.0538 0.0212 59 LEU A C 371 O O . LEU A 59 ? 0.2834 0.3219 0.3236 -0.0023 -0.0534 0.0212 59 LEU A O 372 C CB . LEU A 59 ? 0.2818 0.3272 0.3228 0.0044 -0.0513 0.0207 59 LEU A CB 373 C CG . LEU A 59 ? 0.2940 0.3398 0.3344 0.0060 -0.0539 0.0197 59 LEU A CG 374 C CD1 . LEU A 59 ? 0.3066 0.3607 0.3514 0.0051 -0.0555 0.0192 59 LEU A CD1 375 C CD2 . LEU A 59 ? 0.2873 0.3297 0.3235 0.0104 -0.0532 0.0193 59 LEU A CD2 376 N N . ASP A 60 ? 0.2812 0.3290 0.3269 -0.0062 -0.0561 0.0212 60 ASP A N 377 C CA . ASP A 60 ? 0.2938 0.3361 0.3371 -0.0089 -0.0588 0.0210 60 ASP A CA 378 C C . ASP A 60 ? 0.2969 0.3364 0.3380 -0.0063 -0.0610 0.0199 60 ASP A C 379 O O . ASP A 60 ? 0.2976 0.3416 0.3405 -0.0059 -0.0624 0.0194 60 ASP A O 380 C CB . ASP A 60 ? 0.3072 0.3536 0.3527 -0.0141 -0.0606 0.0215 60 ASP A CB 381 C CG . ASP A 60 ? 0.3219 0.3605 0.3634 -0.0175 -0.0637 0.0215 60 ASP A CG 382 O OD1 . ASP A 60 ? 0.3366 0.3680 0.3742 -0.0150 -0.0650 0.0207 60 ASP A OD1 383 O OD2 . ASP A 60 ? 0.3338 0.3736 0.3755 -0.0227 -0.0648 0.0223 60 ASP A OD2 384 N N . GLY A 61 ? 0.2965 0.3291 0.3337 -0.0044 -0.0613 0.0194 61 GLY A N 385 C CA . GLY A 61 ? 0.3067 0.3366 0.3413 -0.0017 -0.0633 0.0182 61 GLY A CA 386 C C . GLY A 61 ? 0.3233 0.3516 0.3572 -0.0038 -0.0671 0.0176 61 GLY A C 387 O O . GLY A 61 ? 0.3277 0.3552 0.3602 -0.0017 -0.0689 0.0167 61 GLY A O 388 N N . GLU A 62 ? 0.3359 0.3633 0.3699 -0.0083 -0.0685 0.0183 62 GLU A N 389 C CA . GLU A 62 ? 0.3655 0.3899 0.3974 -0.0114 -0.0724 0.0179 62 GLU A CA 390 C C . GLU A 62 ? 0.3579 0.3747 0.3847 -0.0084 -0.0749 0.0165 62 GLU A C 391 O O . GLU A 62 ? 0.3436 0.3544 0.3667 -0.0070 -0.0749 0.0162 62 GLU A O 392 C CB . GLU A 62 ? 0.4037 0.4363 0.4396 -0.0131 -0.0732 0.0178 62 GLU A CB 393 C CG . GLU A 62 ? 0.4419 0.4829 0.4825 -0.0158 -0.0708 0.0189 62 GLU A CG 394 C CD . GLU A 62 ? 0.5027 0.5535 0.5474 -0.0182 -0.0718 0.0187 62 GLU A CD 395 O OE1 . GLU A 62 ? 0.5534 0.6100 0.6005 -0.0143 -0.0712 0.0179 62 GLU A OE1 396 O OE2 . GLU A 62 ? 0.5851 0.6383 0.6302 -0.0241 -0.0731 0.0194 62 GLU A OE2 397 N N . ASN A 63 ? 0.3546 0.3718 0.3809 -0.0071 -0.0772 0.0156 63 ASN A N 398 C CA . ASN A 63 ? 0.3853 0.3959 0.4067 -0.0038 -0.0796 0.0141 63 ASN A CA 399 C C . ASN A 63 ? 0.3737 0.3853 0.3947 0.0014 -0.0773 0.0134 63 ASN A C 400 O O . ASN A 63 ? 0.3567 0.3644 0.3739 0.0044 -0.0791 0.0120 63 ASN A O 401 C CB . ASN A 63 ? 0.4212 0.4313 0.4417 -0.0048 -0.0832 0.0133 63 ASN A CB 402 C CG . ASN A 63 ? 0.4628 0.4684 0.4805 -0.0102 -0.0865 0.0138 63 ASN A CG 403 O OD1 . ASN A 63 ? 0.4532 0.4523 0.4671 -0.0121 -0.0873 0.0141 63 ASN A OD1 404 N ND2 . ASN A 63 ? 0.5300 0.5390 0.5491 -0.0131 -0.0886 0.0137 63 ASN A ND2 405 N N . CYS A 64 ? 0.3626 0.3795 0.3870 0.0024 -0.0736 0.0142 64 CYS A N 406 C CA . CYS A 64 ? 0.3653 0.3833 0.3889 0.0065 -0.0714 0.0138 64 CYS A CA 407 C C . CYS A 64 ? 0.3444 0.3616 0.3670 0.0071 -0.0684 0.0142 64 CYS A C 408 O O . CYS A 64 ? 0.3325 0.3512 0.3573 0.0049 -0.0665 0.0153 64 CYS A O 409 C CB . CYS A 64 ? 0.4039 0.4277 0.4308 0.0074 -0.0697 0.0143 64 CYS A CB 410 S SG . CYS A 64 ? 0.4846 0.5113 0.5130 0.0076 -0.0729 0.0136 64 CYS A SG 411 N N . THR A 65 ? 0.3231 0.3385 0.3422 0.0100 -0.0679 0.0132 65 THR A N 412 C CA . THR A 65 ? 0.3213 0.3376 0.3395 0.0107 -0.0647 0.0135 65 THR A CA 413 C C . THR A 65 ? 0.3003 0.3196 0.3197 0.0113 -0.0619 0.0145 65 THR A C 414 O O . THR A 65 ? 0.3055 0.3259 0.3255 0.0123 -0.0629 0.0144 65 THR A O 415 C CB . THR A 65 ? 0.3301 0.3451 0.3441 0.0133 -0.0652 0.0120 65 THR A CB 416 O OG1 . THR A 65 ? 0.3402 0.3562 0.3527 0.0154 -0.0656 0.0114 65 THR A OG1 417 C CG2 . THR A 65 ? 0.3508 0.3616 0.3623 0.0137 -0.0687 0.0106 65 THR A CG2 418 N N . LEU A 66 ? 0.2851 0.3050 0.3039 0.0109 -0.0588 0.0152 66 LEU A N 419 C CA . LEU A 66 ? 0.2801 0.3010 0.2981 0.0116 -0.0564 0.0161 66 LEU A CA 420 C C . LEU A 66 ? 0.2834 0.3034 0.2977 0.0138 -0.0569 0.0153 66 LEU A C 421 O O . LEU A 66 ? 0.2567 0.2766 0.2703 0.0151 -0.0570 0.0157 66 LEU A O 422 C CB . LEU A 66 ? 0.2815 0.3023 0.2982 0.0104 -0.0531 0.0168 66 LEU A CB 423 C CG . LEU A 66 ? 0.2796 0.2994 0.2935 0.0110 -0.0507 0.0177 66 LEU A CG 424 C CD1 . LEU A 66 ? 0.2726 0.2933 0.2888 0.0120 -0.0514 0.0183 66 LEU A CD1 425 C CD2 . LEU A 66 ? 0.2624 0.2818 0.2750 0.0092 -0.0478 0.0185 66 LEU A CD2 426 N N . ILE A 67 ? 0.2983 0.3179 0.3098 0.0145 -0.0575 0.0142 67 ILE A N 427 C CA . ILE A 67 ? 0.3149 0.3342 0.3225 0.0163 -0.0579 0.0135 67 ILE A CA 428 C C . ILE A 67 ? 0.3150 0.3338 0.3236 0.0179 -0.0608 0.0129 67 ILE A C 429 O O . ILE A 67 ? 0.3246 0.3428 0.3310 0.0193 -0.0608 0.0130 67 ILE A O 430 C CB . ILE A 67 ? 0.3286 0.3493 0.3329 0.0169 -0.0578 0.0121 67 ILE A CB 431 C CG1 . ILE A 67 ? 0.3498 0.3720 0.3524 0.0151 -0.0545 0.0126 67 ILE A CG1 432 C CG2 . ILE A 67 ? 0.3299 0.3510 0.3305 0.0186 -0.0586 0.0112 67 ILE A CG2 433 C CD1 . ILE A 67 ? 0.3671 0.3878 0.3670 0.0137 -0.0519 0.0142 67 ILE A CD1 434 N N . ASP A 68 ? 0.3298 0.3484 0.3414 0.0175 -0.0634 0.0124 68 ASP A N 435 C CA . ASP A 68 ? 0.3430 0.3615 0.3558 0.0185 -0.0663 0.0119 68 ASP A CA 436 C C . ASP A 68 ? 0.3354 0.3558 0.3505 0.0186 -0.0655 0.0129 68 ASP A C 437 O O . ASP A 68 ? 0.3256 0.3463 0.3398 0.0204 -0.0667 0.0125 68 ASP A O 438 C CB . ASP A 68 ? 0.3621 0.3796 0.3770 0.0171 -0.0693 0.0113 68 ASP A CB 439 C CG . ASP A 68 ? 0.4075 0.4222 0.4190 0.0185 -0.0715 0.0097 68 ASP A CG 440 O OD1 . ASP A 68 ? 0.4153 0.4303 0.4236 0.0209 -0.0713 0.0087 68 ASP A OD1 441 O OD2 . ASP A 68 ? 0.4759 0.4879 0.4872 0.0172 -0.0736 0.0093 68 ASP A OD2 442 N N . ALA A 69 ? 0.3215 0.3433 0.3392 0.0169 -0.0637 0.0140 69 ALA A N 443 C CA . ALA A 69 ? 0.3209 0.3451 0.3404 0.0176 -0.0629 0.0147 69 ALA A CA 444 C C . ALA A 69 ? 0.3225 0.3443 0.3373 0.0200 -0.0612 0.0151 69 ALA A C 445 O O . ALA A 69 ? 0.3353 0.3578 0.3496 0.0222 -0.0618 0.0150 69 ALA A O 446 C CB . ALA A 69 ? 0.3237 0.3503 0.3467 0.0154 -0.0612 0.0157 69 ALA A CB 447 N N . LEU A 70 ? 0.3121 0.3311 0.3229 0.0194 -0.0592 0.0153 70 LEU A N 448 C CA . LEU A 70 ? 0.3163 0.3318 0.3211 0.0207 -0.0577 0.0158 70 LEU A CA 449 C C . LEU A 70 ? 0.3262 0.3406 0.3280 0.0229 -0.0598 0.0149 70 LEU A C 450 O O . LEU A 70 ? 0.3362 0.3484 0.3349 0.0250 -0.0601 0.0152 70 LEU A O 451 C CB . LEU A 70 ? 0.3140 0.3281 0.3153 0.0187 -0.0554 0.0161 70 LEU A CB 452 C CG . LEU A 70 ? 0.3150 0.3251 0.3088 0.0184 -0.0536 0.0167 70 LEU A CG 453 C CD1 . LEU A 70 ? 0.3045 0.3115 0.2963 0.0182 -0.0517 0.0180 70 LEU A CD1 454 C CD2 . LEU A 70 ? 0.3171 0.3285 0.3082 0.0162 -0.0520 0.0164 70 LEU A CD2 455 N N . LEU A 71 ? 0.3261 0.3415 0.3283 0.0227 -0.0612 0.0139 71 LEU A N 456 C CA . LEU A 71 ? 0.3416 0.3561 0.3409 0.0247 -0.0631 0.0130 71 LEU A CA 457 C C . LEU A 71 ? 0.3408 0.3565 0.3429 0.0267 -0.0656 0.0126 71 LEU A C 458 O O . LEU A 71 ? 0.3548 0.3690 0.3539 0.0289 -0.0666 0.0124 71 LEU A O 459 C CB . LEU A 71 ? 0.3451 0.3610 0.3446 0.0245 -0.0645 0.0117 71 LEU A CB 460 C CG . LEU A 71 ? 0.3552 0.3717 0.3517 0.0231 -0.0623 0.0115 71 LEU A CG 461 C CD1 . LEU A 71 ? 0.3633 0.3815 0.3592 0.0242 -0.0642 0.0097 71 LEU A CD1 462 C CD2 . LEU A 71 ? 0.3515 0.3662 0.3419 0.0225 -0.0600 0.0123 71 LEU A CD2 463 N N . GLY A 72 ? 0.3456 0.3644 0.3534 0.0256 -0.0665 0.0126 72 GLY A N 464 C CA . GLY A 72 ? 0.3584 0.3802 0.3696 0.0269 -0.0688 0.0121 72 GLY A CA 465 C C . GLY A 72 ? 0.3852 0.4082 0.3984 0.0264 -0.0720 0.0110 72 GLY A C 466 O O . GLY A 72 ? 0.3608 0.3849 0.3740 0.0283 -0.0741 0.0102 72 GLY A O 467 N N . ASP A 73 ? 0.3873 0.4096 0.4018 0.0242 -0.0725 0.0107 73 ASP A N 468 C CA . ASP A 73 ? 0.4126 0.4348 0.4285 0.0231 -0.0758 0.0097 73 ASP A CA 469 C C . ASP A 73 ? 0.4159 0.4425 0.4362 0.0218 -0.0773 0.0098 73 ASP A C 470 O O . ASP A 73 ? 0.4127 0.4426 0.4360 0.0205 -0.0757 0.0107 73 ASP A O 471 C CB . ASP A 73 ? 0.4226 0.4426 0.4384 0.0209 -0.0758 0.0097 73 ASP A CB 472 C CG . ASP A 73 ? 0.4683 0.4857 0.4836 0.0198 -0.0796 0.0086 73 ASP A CG 473 O OD1 . ASP A 73 ? 0.5018 0.5205 0.5186 0.0192 -0.0821 0.0082 73 ASP A OD1 474 O OD2 . ASP A 73 ? 0.4539 0.4678 0.4667 0.0196 -0.0802 0.0080 73 ASP A OD2 475 N N . PRO A 74 ? 0.4449 0.4724 0.4655 0.0223 -0.0804 0.0088 74 PRO A N 476 C CA . PRO A 74 ? 0.4484 0.4818 0.4733 0.0210 -0.0818 0.0087 74 PRO A CA 477 C C . PRO A 74 ? 0.4485 0.4853 0.4773 0.0166 -0.0816 0.0095 74 PRO A C 478 O O . PRO A 74 ? 0.4383 0.4817 0.4707 0.0162 -0.0807 0.0098 74 PRO A O 479 C CB . PRO A 74 ? 0.4797 0.5121 0.5035 0.0211 -0.0855 0.0075 74 PRO A CB 480 C CG . PRO A 74 ? 0.4797 0.5075 0.4988 0.0248 -0.0852 0.0069 74 PRO A CG 481 C CD . PRO A 74 ? 0.4657 0.4899 0.4827 0.0246 -0.0825 0.0076 74 PRO A CD 482 N N . GLN A 75 ? 0.4425 0.4750 0.4702 0.0136 -0.0823 0.0097 75 GLN A N 483 C CA . GLN A 75 ? 0.4556 0.4905 0.4862 0.0090 -0.0820 0.0106 75 GLN A CA 484 C C . GLN A 75 ? 0.4261 0.4640 0.4589 0.0093 -0.0783 0.0118 75 GLN A C 485 O O . GLN A 75 ? 0.4023 0.4439 0.4381 0.0058 -0.0777 0.0125 75 GLN A O 486 C CB . GLN A 75 ? 0.4761 0.5041 0.5036 0.0059 -0.0841 0.0106 75 GLN A CB 487 C CG . GLN A 75 ? 0.5004 0.5224 0.5245 0.0079 -0.0826 0.0106 75 GLN A CG 488 C CD . GLN A 75 ? 0.5417 0.5563 0.5617 0.0059 -0.0854 0.0101 75 GLN A CD 489 O OE1 . GLN A 75 ? 0.5859 0.5986 0.6048 0.0029 -0.0887 0.0098 75 GLN A OE1 490 N NE2 . GLN A 75 ? 0.5138 0.5240 0.5308 0.0076 -0.0843 0.0099 75 GLN A NE2 491 N N . CYS A 76 ? 0.3999 0.4359 0.4307 0.0131 -0.0758 0.0119 76 CYS A N 492 C CA . CYS A 76 ? 0.3936 0.4313 0.4254 0.0136 -0.0724 0.0129 76 CYS A CA 493 C C . CYS A 76 ? 0.3792 0.4217 0.4120 0.0168 -0.0714 0.0128 76 CYS A C 494 O O . CYS A 76 ? 0.3529 0.3953 0.3851 0.0182 -0.0687 0.0135 76 CYS A O 495 C CB . CYS A 76 ? 0.4201 0.4519 0.4479 0.0151 -0.0703 0.0132 76 CYS A CB 496 S SG . CYS A 76 ? 0.4533 0.4794 0.4784 0.0134 -0.0719 0.0127 76 CYS A SG 497 N N . ASP A 77 ? 0.3605 0.4069 0.3944 0.0182 -0.0736 0.0119 77 ASP A N 498 C CA . ASP A 77 ? 0.3729 0.4233 0.4068 0.0223 -0.0731 0.0114 77 ASP A CA 499 C C . ASP A 77 ? 0.3580 0.4149 0.3953 0.0220 -0.0713 0.0119 77 ASP A C 500 O O . ASP A 77 ? 0.3522 0.4097 0.3877 0.0260 -0.0700 0.0118 77 ASP A O 501 C CB . ASP A 77 ? 0.3870 0.4420 0.4222 0.0236 -0.0761 0.0101 77 ASP A CB 502 C CG . ASP A 77 ? 0.4148 0.4634 0.4456 0.0257 -0.0776 0.0096 77 ASP A CG 503 O OD1 . ASP A 77 ? 0.4114 0.4530 0.4378 0.0270 -0.0761 0.0101 77 ASP A OD1 504 O OD2 . ASP A 77 ? 0.4275 0.4789 0.4592 0.0262 -0.0803 0.0085 77 ASP A OD2 505 N N . GLY A 78 ? 0.3556 0.4169 0.3971 0.0173 -0.0714 0.0123 78 GLY A N 506 C CA . GLY A 78 ? 0.3557 0.4243 0.4008 0.0165 -0.0698 0.0126 78 GLY A CA 507 C C . GLY A 78 ? 0.3425 0.4065 0.3853 0.0178 -0.0666 0.0136 78 GLY A C 508 O O . GLY A 78 ? 0.3382 0.4075 0.3829 0.0189 -0.0651 0.0137 78 GLY A O 509 N N . PHE A 79 ? 0.3374 0.3921 0.3761 0.0179 -0.0657 0.0143 79 PHE A N 510 C CA . PHE A 79 ? 0.3438 0.3938 0.3798 0.0186 -0.0627 0.0153 79 PHE A CA 511 C C . PHE A 79 ? 0.3293 0.3755 0.3603 0.0234 -0.0617 0.0152 79 PHE A C 512 O O . PHE A 79 ? 0.3084 0.3504 0.3364 0.0238 -0.0593 0.0160 79 PHE A O 513 C CB . PHE A 79 ? 0.3857 0.4285 0.4192 0.0162 -0.0621 0.0159 79 PHE A CB 514 C CG . PHE A 79 ? 0.4059 0.4497 0.4424 0.0116 -0.0629 0.0162 79 PHE A CG 515 C CD1 . PHE A 79 ? 0.4392 0.4825 0.4762 0.0098 -0.0658 0.0156 79 PHE A CD1 516 C CD2 . PHE A 79 ? 0.4508 0.4951 0.4889 0.0092 -0.0610 0.0171 79 PHE A CD2 517 C CE1 . PHE A 79 ? 0.4361 0.4783 0.4742 0.0055 -0.0670 0.0159 79 PHE A CE1 518 C CE2 . PHE A 79 ? 0.4578 0.5017 0.4975 0.0049 -0.0620 0.0175 79 PHE A CE2 519 C CZ . PHE A 79 ? 0.4248 0.4673 0.4641 0.0030 -0.0651 0.0169 79 PHE A CZ 520 N N . GLN A 80 ? 0.3103 0.3571 0.3395 0.0269 -0.0635 0.0142 80 GLN A N 521 C CA . GLN A 80 ? 0.3129 0.3539 0.3355 0.0314 -0.0629 0.0141 80 GLN A CA 522 C C . GLN A 80 ? 0.3084 0.3494 0.3293 0.0335 -0.0610 0.0145 80 GLN A C 523 O O . GLN A 80 ? 0.2856 0.3344 0.3108 0.0343 -0.0612 0.0139 80 GLN A O 524 C CB . GLN A 80 ? 0.3322 0.3751 0.3535 0.0353 -0.0655 0.0128 80 GLN A CB 525 C CG . GLN A 80 ? 0.3462 0.3859 0.3663 0.0343 -0.0672 0.0125 80 GLN A CG 526 C CD . GLN A 80 ? 0.3764 0.4155 0.3932 0.0387 -0.0693 0.0115 80 GLN A CD 527 O OE1 . GLN A 80 ? 0.3592 0.4012 0.3750 0.0428 -0.0699 0.0107 80 GLN A OE1 528 N NE2 . GLN A 80 ? 0.3850 0.4200 0.3993 0.0383 -0.0706 0.0112 80 GLN A NE2 529 N N . ASN A 81 ? 0.3021 0.3344 0.3164 0.0342 -0.0593 0.0154 81 ASN A N 530 C CA . ASN A 81 ? 0.3054 0.3350 0.3159 0.0366 -0.0577 0.0157 81 ASN A CA 531 C C . ASN A 81 ? 0.2992 0.3335 0.3145 0.0342 -0.0558 0.0163 81 ASN A C 532 O O . ASN A 81 ? 0.3143 0.3471 0.3268 0.0365 -0.0547 0.0164 81 ASN A O 533 C CB . ASN A 81 ? 0.3265 0.3577 0.3341 0.0427 -0.0595 0.0145 81 ASN A CB 534 C CG . ASN A 81 ? 0.3357 0.3598 0.3363 0.0455 -0.0611 0.0141 81 ASN A CG 535 O OD1 . ASN A 81 ? 0.3560 0.3700 0.3489 0.0450 -0.0602 0.0151 81 ASN A OD1 536 N ND2 . ASN A 81 ? 0.3483 0.3781 0.3516 0.0480 -0.0636 0.0128 81 ASN A ND2 537 N N . LYS A 82 ? 0.2953 0.3342 0.3169 0.0296 -0.0555 0.0166 82 LYS A N 538 C CA . LYS A 82 ? 0.3025 0.3459 0.3286 0.0269 -0.0538 0.0172 82 LYS A CA 539 C C . LYS A 82 ? 0.2891 0.3250 0.3111 0.0253 -0.0512 0.0185 82 LYS A C 540 O O . LYS A 82 ? 0.2845 0.3132 0.3017 0.0245 -0.0508 0.0189 82 LYS A O 541 C CB . LYS A 82 ? 0.3187 0.3682 0.3517 0.0223 -0.0547 0.0173 82 LYS A CB 542 C CG . LYS A 82 ? 0.3535 0.4125 0.3913 0.0227 -0.0569 0.0162 82 LYS A CG 543 C CD . LYS A 82 ? 0.3791 0.4422 0.4220 0.0173 -0.0581 0.0164 82 LYS A CD 544 C CE . LYS A 82 ? 0.3995 0.4665 0.4461 0.0133 -0.0565 0.0172 82 LYS A CE 545 N NZ . LYS A 82 ? 0.4410 0.5172 0.4909 0.0145 -0.0557 0.0169 82 LYS A NZ 546 N N . LYS A 83 ? 0.2807 0.3193 0.3047 0.0246 -0.0495 0.0189 83 LYS A N 547 C CA . LYS A 83 ? 0.2823 0.3153 0.3034 0.0226 -0.0470 0.0200 83 LYS A CA 548 C C . LYS A 83 ? 0.2712 0.3091 0.2986 0.0182 -0.0461 0.0206 83 LYS A C 549 O O . LYS A 83 ? 0.2574 0.3031 0.2907 0.0169 -0.0472 0.0202 83 LYS A O 550 C CB . LYS A 83 ? 0.3020 0.3322 0.3184 0.0262 -0.0460 0.0200 83 LYS A CB 551 C CG . LYS A 83 ? 0.3203 0.3443 0.3290 0.0309 -0.0473 0.0195 83 LYS A CG 552 C CD . LYS A 83 ? 0.3391 0.3570 0.3410 0.0338 -0.0462 0.0197 83 LYS A CD 553 C CE . LYS A 83 ? 0.3668 0.3798 0.3612 0.0397 -0.0481 0.0187 83 LYS A CE 554 N NZ . LYS A 83 ? 0.3564 0.3792 0.3555 0.0441 -0.0500 0.0171 83 LYS A NZ 555 N N . TRP A 84 ? 0.2566 0.2900 0.2821 0.0158 -0.0441 0.0215 84 TRP A N 556 C CA . TRP A 84 ? 0.2432 0.2797 0.2733 0.0119 -0.0431 0.0221 84 TRP A CA 557 C C . TRP A 84 ? 0.2422 0.2746 0.2695 0.0109 -0.0405 0.0230 84 TRP A C 558 O O . TRP A 84 ? 0.2515 0.2775 0.2728 0.0119 -0.0396 0.0232 84 TRP A O 559 C CB . TRP A 84 ? 0.2369 0.2728 0.2688 0.0089 -0.0444 0.0220 84 TRP A CB 560 C CG . TRP A 84 ? 0.2437 0.2732 0.2705 0.0091 -0.0440 0.0220 84 TRP A CG 561 C CD1 . TRP A 84 ? 0.2388 0.2649 0.2635 0.0071 -0.0424 0.0224 84 TRP A CD1 562 C CD2 . TRP A 84 ? 0.2450 0.2715 0.2681 0.0112 -0.0453 0.0214 84 TRP A CD2 563 N NE1 . TRP A 84 ? 0.2441 0.2664 0.2642 0.0077 -0.0425 0.0220 84 TRP A NE1 564 C CE2 . TRP A 84 ? 0.2488 0.2707 0.2676 0.0101 -0.0442 0.0215 84 TRP A CE2 565 C CE3 . TRP A 84 ? 0.2493 0.2771 0.2722 0.0139 -0.0473 0.0207 84 TRP A CE3 566 C CZ2 . TRP A 84 ? 0.2500 0.2688 0.2643 0.0113 -0.0450 0.0210 84 TRP A CZ2 567 C CZ3 . TRP A 84 ? 0.2534 0.2770 0.2716 0.0153 -0.0481 0.0203 84 TRP A CZ3 568 C CH2 . TRP A 84 ? 0.2574 0.2765 0.2713 0.0139 -0.0469 0.0205 84 TRP A CH2 569 N N . ASP A 85 ? 0.2320 0.2679 0.2632 0.0084 -0.0395 0.0235 85 ASP A N 570 C CA . ASP A 85 ? 0.2320 0.2644 0.2616 0.0063 -0.0373 0.0243 85 ASP A CA 571 C C . ASP A 85 ? 0.2320 0.2631 0.2626 0.0034 -0.0379 0.0242 85 ASP A C 572 O O . ASP A 85 ? 0.2354 0.2624 0.2625 0.0026 -0.0369 0.0243 85 ASP A O 573 C CB . ASP A 85 ? 0.2395 0.2762 0.2726 0.0052 -0.0359 0.0248 85 ASP A CB 574 C CG . ASP A 85 ? 0.2550 0.2927 0.2863 0.0088 -0.0352 0.0246 85 ASP A CG 575 O OD1 . ASP A 85 ? 0.2573 0.2890 0.2825 0.0114 -0.0350 0.0244 85 ASP A OD1 576 O OD2 . ASP A 85 ? 0.2509 0.2954 0.2863 0.0089 -0.0349 0.0245 85 ASP A OD2 577 N N . LEU A 86 ? 0.2229 0.2574 0.2575 0.0019 -0.0399 0.0240 86 LEU A N 578 C CA . LEU A 86 ? 0.2246 0.2571 0.2592 -0.0001 -0.0412 0.0237 86 LEU A CA 579 C C . LEU A 86 ? 0.2259 0.2593 0.2615 0.0000 -0.0441 0.0230 86 LEU A C 580 O O . LEU A 86 ? 0.2394 0.2770 0.2784 -0.0010 -0.0454 0.0230 86 LEU A O 581 C CB . LEU A 86 ? 0.2226 0.2561 0.2597 -0.0032 -0.0408 0.0243 86 LEU A CB 582 C CG . LEU A 86 ? 0.2281 0.2581 0.2637 -0.0046 -0.0421 0.0239 86 LEU A CG 583 C CD1 . LEU A 86 ? 0.2288 0.2556 0.2605 -0.0033 -0.0406 0.0235 86 LEU A CD1 584 C CD2 . LEU A 86 ? 0.2257 0.2559 0.2629 -0.0077 -0.0422 0.0246 86 LEU A CD2 585 N N . PHE A 87 ? 0.2380 0.2679 0.2705 0.0012 -0.0451 0.0223 87 PHE A N 586 C CA . PHE A 87 ? 0.2447 0.2744 0.2774 0.0015 -0.0480 0.0214 87 PHE A CA 587 C C . PHE A 87 ? 0.2480 0.2755 0.2806 -0.0006 -0.0496 0.0212 87 PHE A C 588 O O . PHE A 87 ? 0.2507 0.2755 0.2810 -0.0006 -0.0487 0.0210 87 PHE A O 589 C CB . PHE A 87 ? 0.2517 0.2788 0.2805 0.0041 -0.0483 0.0207 87 PHE A CB 590 C CG . PHE A 87 ? 0.2711 0.2983 0.3001 0.0050 -0.0512 0.0198 87 PHE A CG 591 C CD1 . PHE A 87 ? 0.2686 0.2939 0.2972 0.0040 -0.0536 0.0191 87 PHE A CD1 592 C CD2 . PHE A 87 ? 0.2793 0.3082 0.3085 0.0071 -0.0520 0.0196 87 PHE A CD2 593 C CE1 . PHE A 87 ? 0.2870 0.3119 0.3153 0.0048 -0.0565 0.0182 87 PHE A CE1 594 C CE2 . PHE A 87 ? 0.2871 0.3163 0.3165 0.0078 -0.0547 0.0187 87 PHE A CE2 595 C CZ . PHE A 87 ? 0.2898 0.3170 0.3188 0.0065 -0.0570 0.0180 87 PHE A CZ 596 N N . VAL A 88 ? 0.2495 0.2779 0.2841 -0.0026 -0.0520 0.0212 88 VAL A N 597 C CA . VAL A 88 ? 0.2632 0.2878 0.2963 -0.0048 -0.0541 0.0210 88 VAL A CA 598 C C . VAL A 88 ? 0.2787 0.3000 0.3092 -0.0037 -0.0574 0.0198 88 VAL A C 599 O O . VAL A 88 ? 0.2866 0.3099 0.3186 -0.0043 -0.0592 0.0197 88 VAL A O 600 C CB . VAL A 88 ? 0.2608 0.2872 0.2963 -0.0089 -0.0547 0.0220 88 VAL A CB 601 C CG1 . VAL A 88 ? 0.2762 0.2965 0.3084 -0.0112 -0.0574 0.0218 88 VAL A CG1 602 C CG2 . VAL A 88 ? 0.2556 0.2854 0.2935 -0.0097 -0.0514 0.0231 88 VAL A CG2 603 N N . GLU A 89 ? 0.2927 0.3098 0.3194 -0.0018 -0.0581 0.0187 89 GLU A N 604 C CA . GLU A 89 ? 0.3130 0.3266 0.3365 -0.0001 -0.0614 0.0173 89 GLU A CA 605 C C . GLU A 89 ? 0.3139 0.3219 0.3344 -0.0019 -0.0646 0.0170 89 GLU A C 606 O O . GLU A 89 ? 0.3014 0.3067 0.3200 -0.0023 -0.0641 0.0171 89 GLU A O 607 C CB . GLU A 89 ? 0.3244 0.3374 0.3447 0.0034 -0.0606 0.0160 89 GLU A CB 608 C CG . GLU A 89 ? 0.3421 0.3585 0.3631 0.0052 -0.0587 0.0160 89 GLU A CG 609 C CD . GLU A 89 ? 0.3379 0.3544 0.3552 0.0081 -0.0583 0.0146 89 GLU A CD 610 O OE1 . GLU A 89 ? 0.3259 0.3420 0.3410 0.0089 -0.0580 0.0138 89 GLU A OE1 611 O OE2 . GLU A 89 ? 0.3272 0.3449 0.3439 0.0096 -0.0582 0.0144 89 GLU A OE2 612 N N . ARG A 90 ? 0.3188 0.3242 0.3381 -0.0029 -0.0680 0.0166 90 ARG A N 613 C CA . ARG A 90 ? 0.3421 0.3406 0.3572 -0.0054 -0.0716 0.0165 90 ARG A CA 614 C C . ARG A 90 ? 0.3560 0.3483 0.3652 -0.0016 -0.0746 0.0145 90 ARG A C 615 O O . ARG A 90 ? 0.3530 0.3472 0.3621 0.0016 -0.0749 0.0133 90 ARG A O 616 C CB . ARG A 90 ? 0.3426 0.3419 0.3591 -0.0093 -0.0739 0.0171 90 ARG A CB 617 C CG . ARG A 90 ? 0.3442 0.3521 0.3671 -0.0122 -0.0712 0.0186 90 ARG A CG 618 C CD . ARG A 90 ? 0.3411 0.3506 0.3657 -0.0141 -0.0684 0.0199 90 ARG A CD 619 N NE . ARG A 90 ? 0.3228 0.3391 0.3520 -0.0181 -0.0670 0.0212 90 ARG A NE 620 C CZ . ARG A 90 ? 0.3194 0.3362 0.3493 -0.0216 -0.0657 0.0224 90 ARG A CZ 621 N NH1 . ARG A 90 ? 0.3114 0.3215 0.3374 -0.0214 -0.0658 0.0225 90 ARG A NH1 622 N NH2 . ARG A 90 ? 0.3156 0.3400 0.3498 -0.0251 -0.0645 0.0235 90 ARG A NH2 623 N N . SER A 91 ? 0.3710 0.3556 0.3746 -0.0020 -0.0773 0.0140 91 SER A N 624 C CA . SER A 91 ? 0.4047 0.3830 0.4018 0.0022 -0.0807 0.0118 91 SER A CA 625 C C . SER A 91 ? 0.4180 0.3927 0.4125 0.0022 -0.0844 0.0110 91 SER A C 626 O O . SER A 91 ? 0.4440 0.4166 0.4348 0.0066 -0.0864 0.0090 91 SER A O 627 C CB . SER A 91 ? 0.4176 0.3872 0.4081 0.0022 -0.0831 0.0114 91 SER A CB 628 O OG . SER A 91 ? 0.4263 0.3893 0.4140 -0.0028 -0.0860 0.0126 91 SER A OG 629 N N . LYS A 92 ? 0.4313 0.4063 0.4280 -0.0027 -0.0854 0.0125 92 LYS A N 630 C CA . LYS A 92 ? 0.4648 0.4373 0.4596 -0.0033 -0.0889 0.0118 92 LYS A CA 631 C C . LYS A 92 ? 0.4351 0.4151 0.4343 -0.0001 -0.0871 0.0111 92 LYS A C 632 O O . LYS A 92 ? 0.4283 0.4069 0.4262 0.0003 -0.0898 0.0103 92 LYS A O 633 C CB . LYS A 92 ? 0.4973 0.4698 0.4934 -0.0102 -0.0901 0.0135 92 LYS A CB 634 C CG . LYS A 92 ? 0.5287 0.5131 0.5338 -0.0124 -0.0862 0.0149 92 LYS A CG 635 C CD . LYS A 92 ? 0.5759 0.5624 0.5828 -0.0195 -0.0868 0.0166 92 LYS A CD 636 C CE . LYS A 92 ? 0.5993 0.5984 0.6147 -0.0204 -0.0832 0.0175 92 LYS A CE 637 N NZ . LYS A 92 ? 0.5976 0.6014 0.6151 -0.0269 -0.0844 0.0185 92 LYS A NZ 638 N N . ALA A 93 ? 0.4111 0.3987 0.4153 0.0018 -0.0827 0.0115 93 ALA A N 639 C CA . ALA A 93 ? 0.3957 0.3900 0.4038 0.0040 -0.0809 0.0113 93 ALA A CA 640 C C . ALA A 93 ? 0.4039 0.3953 0.4077 0.0085 -0.0833 0.0092 93 ALA A C 641 O O . ALA A 93 ? 0.3998 0.3870 0.3989 0.0115 -0.0847 0.0078 93 ALA A O 642 C CB . ALA A 93 ? 0.3813 0.3820 0.3934 0.0053 -0.0761 0.0121 93 ALA A CB 643 N N . TYR A 94 ? 0.4008 0.3949 0.4062 0.0093 -0.0840 0.0089 94 TYR A N 644 C CA . TYR A 94 ? 0.4260 0.4180 0.4275 0.0135 -0.0863 0.0070 94 TYR A CA 645 C C . TYR A 94 ? 0.4176 0.4155 0.4223 0.0150 -0.0847 0.0070 94 TYR A C 646 O O . TYR A 94 ? 0.3894 0.3912 0.3984 0.0126 -0.0836 0.0083 94 TYR A O 647 C CB . TYR A 94 ? 0.4525 0.4367 0.4490 0.0126 -0.0914 0.0060 94 TYR A CB 648 C CG . TYR A 94 ? 0.4604 0.4453 0.4594 0.0082 -0.0930 0.0071 94 TYR A CG 649 C CD1 . TYR A 94 ? 0.4751 0.4595 0.4757 0.0027 -0.0931 0.0087 94 TYR A CD1 650 C CD2 . TYR A 94 ? 0.4902 0.4772 0.4900 0.0094 -0.0945 0.0064 94 TYR A CD2 651 C CE1 . TYR A 94 ? 0.4899 0.4766 0.4928 -0.0017 -0.0945 0.0095 94 TYR A CE1 652 C CE2 . TYR A 94 ? 0.5090 0.4980 0.5113 0.0053 -0.0959 0.0072 94 TYR A CE2 653 C CZ . TYR A 94 ? 0.5175 0.5068 0.5214 -0.0003 -0.0959 0.0087 94 TYR A CZ 654 O OH . TYR A 94 ? 0.5286 0.5215 0.5351 -0.0047 -0.0973 0.0093 94 TYR A OH 655 N N . SER A 95 ? 0.4369 0.4356 0.4391 0.0192 -0.0848 0.0055 95 SER A N 656 C CA . SER A 95 ? 0.4424 0.4453 0.4461 0.0209 -0.0837 0.0054 95 SER A CA 657 C C . SER A 95 ? 0.4547 0.4551 0.4570 0.0213 -0.0875 0.0045 95 SER A C 658 O O . SER A 95 ? 0.4593 0.4542 0.4573 0.0222 -0.0912 0.0031 95 SER A O 659 C CB . SER A 95 ? 0.4602 0.4656 0.4614 0.0245 -0.0819 0.0043 95 SER A CB 660 O OG . SER A 95 ? 0.4626 0.4709 0.4651 0.0237 -0.0781 0.0052 95 SER A OG 661 N N . ASN A 96 ? 0.4491 0.4532 0.4546 0.0208 -0.0870 0.0052 96 ASN A N 662 C CA . ASN A 96 ? 0.4720 0.4745 0.4767 0.0207 -0.0906 0.0044 96 ASN A CA 663 C C . ASN A 96 ? 0.4497 0.4560 0.4552 0.0234 -0.0899 0.0041 96 ASN A C 664 O O . ASN A 96 ? 0.4500 0.4582 0.4575 0.0226 -0.0913 0.0042 96 ASN A O 665 C CB . ASN A 96 ? 0.4904 0.4935 0.4983 0.0159 -0.0919 0.0055 96 ASN A CB 666 C CG . ASN A 96 ? 0.5206 0.5196 0.5258 0.0146 -0.0966 0.0046 96 ASN A CG 667 O OD1 . ASN A 96 ? 0.5543 0.5475 0.5543 0.0171 -0.0994 0.0030 96 ASN A OD1 668 N ND2 . ASN A 96 ? 0.5108 0.5130 0.5192 0.0107 -0.0976 0.0053 96 ASN A ND2 669 N N . CYS A 97 ? 0.4434 0.4511 0.4470 0.0265 -0.0877 0.0037 97 CYS A N 670 C CA . CYS A 97 ? 0.4443 0.4545 0.4472 0.0289 -0.0868 0.0035 97 CYS A CA 671 C C . CYS A 97 ? 0.4240 0.4332 0.4222 0.0322 -0.0872 0.0019 97 CYS A C 672 O O . CYS A 97 ? 0.4213 0.4274 0.4168 0.0331 -0.0896 0.0005 97 CYS A O 673 C CB . CYS A 97 ? 0.4669 0.4806 0.4721 0.0283 -0.0829 0.0052 97 CYS A CB 674 S SG . CYS A 97 ? 0.5175 0.5332 0.5216 0.0307 -0.0819 0.0055 97 CYS A SG 675 N N . TYR A 98 ? 0.4307 0.4425 0.4273 0.0339 -0.0850 0.0020 98 TYR A N 676 C CA . TYR A 98 ? 0.4371 0.4497 0.4292 0.0368 -0.0853 0.0004 98 TYR A CA 677 C C . TYR A 98 ? 0.4323 0.4462 0.4232 0.0366 -0.0835 0.0000 98 TYR A C 678 O O . TYR A 98 ? 0.4242 0.4393 0.4171 0.0344 -0.0805 0.0014 98 TYR A O 679 C CB . TYR A 98 ? 0.4509 0.4659 0.4410 0.0377 -0.0832 0.0009 98 TYR A CB 680 C CG . TYR A 98 ? 0.4513 0.4673 0.4372 0.0407 -0.0847 -0.0008 98 TYR A CG 681 C CD1 . TYR A 98 ? 0.4646 0.4790 0.4500 0.0424 -0.0876 -0.0015 98 TYR A CD1 682 C CD2 . TYR A 98 ? 0.4469 0.4663 0.4294 0.0417 -0.0831 -0.0018 98 TYR A CD2 683 C CE1 . TYR A 98 ? 0.4618 0.4773 0.4433 0.0452 -0.0889 -0.0032 98 TYR A CE1 684 C CE2 . TYR A 98 ? 0.4607 0.4822 0.4393 0.0445 -0.0843 -0.0036 98 TYR A CE2 685 C CZ . TYR A 98 ? 0.4699 0.4890 0.4480 0.0463 -0.0873 -0.0042 98 TYR A CZ 686 O OH . TYR A 98 ? 0.4523 0.4736 0.4264 0.0492 -0.0885 -0.0060 98 TYR A OH 687 N N . PRO A 99 ? 0.4174 0.4310 0.4048 0.0394 -0.0856 -0.0022 99 PRO A N 688 C CA . PRO A 99 ? 0.4180 0.4337 0.4042 0.0397 -0.0841 -0.0028 99 PRO A CA 689 C C . PRO A 99 ? 0.4103 0.4319 0.3959 0.0388 -0.0797 -0.0021 99 PRO A C 690 O O . PRO A 99 ? 0.3886 0.4129 0.3720 0.0395 -0.0789 -0.0022 99 PRO A O 691 C CB . PRO A 99 ? 0.4376 0.4525 0.4194 0.0439 -0.0875 -0.0057 99 PRO A CB 692 C CG . PRO A 99 ? 0.4380 0.4512 0.4184 0.0457 -0.0901 -0.0065 99 PRO A CG 693 C CD . PRO A 99 ? 0.4315 0.4424 0.4159 0.0424 -0.0898 -0.0042 99 PRO A CD 694 N N . TYR A 100 ? 0.3920 0.4149 0.3790 0.0367 -0.0771 -0.0011 100 TYR A N 695 C CA . TYR A 100 ? 0.3818 0.4095 0.3678 0.0349 -0.0730 -0.0002 100 TYR A CA 696 C C . TYR A 100 ? 0.3797 0.4109 0.3654 0.0345 -0.0714 -0.0008 100 TYR A C 697 O O . TYR A 100 ? 0.3605 0.3891 0.3473 0.0353 -0.0731 -0.0015 100 TYR A O 698 C CB . TYR A 100 ? 0.3934 0.4188 0.3817 0.0317 -0.0708 0.0024 100 TYR A CB 699 C CG . TYR A 100 ? 0.3960 0.4190 0.3882 0.0295 -0.0700 0.0038 100 TYR A CG 700 C CD1 . TYR A 100 ? 0.4110 0.4302 0.4064 0.0293 -0.0725 0.0041 100 TYR A CD1 701 C CD2 . TYR A 100 ? 0.4011 0.4260 0.3936 0.0274 -0.0668 0.0047 100 TYR A CD2 702 C CE1 . TYR A 100 ? 0.4239 0.4417 0.4228 0.0270 -0.0718 0.0054 100 TYR A CE1 703 C CE2 . TYR A 100 ? 0.4016 0.4246 0.3976 0.0255 -0.0662 0.0059 100 TYR A CE2 704 C CZ . TYR A 100 ? 0.4154 0.4349 0.4146 0.0253 -0.0686 0.0063 100 TYR A CZ 705 O OH . TYR A 100 ? 0.4082 0.4264 0.4107 0.0230 -0.0679 0.0075 100 TYR A OH 706 N N . ASP A 101 ? 0.3868 0.4237 0.3703 0.0331 -0.0682 -0.0007 101 ASP A N 707 C CA . ASP A 101 ? 0.3964 0.4371 0.3801 0.0317 -0.0658 -0.0008 101 ASP A CA 708 C C . ASP A 101 ? 0.3684 0.4106 0.3513 0.0274 -0.0617 0.0013 101 ASP A C 709 O O . ASP A 101 ? 0.3446 0.3856 0.3253 0.0262 -0.0609 0.0023 101 ASP A O 710 C CB . ASP A 101 ? 0.4489 0.4969 0.4296 0.0347 -0.0664 -0.0037 101 ASP A CB 711 C CG . ASP A 101 ? 0.5068 0.5603 0.4839 0.0353 -0.0659 -0.0047 101 ASP A CG 712 O OD1 . ASP A 101 ? 0.5679 0.6248 0.5432 0.0316 -0.0626 -0.0034 101 ASP A OD1 713 O OD2 . ASP A 101 ? 0.6150 0.6690 0.5905 0.0392 -0.0690 -0.0068 101 ASP A OD2 714 N N . VAL A 102 ? 0.3416 0.3854 0.3256 0.0253 -0.0594 0.0020 102 VAL A N 715 C CA . VAL A 102 ? 0.3331 0.3776 0.3156 0.0210 -0.0557 0.0039 102 VAL A CA 716 C C . VAL A 102 ? 0.3449 0.3975 0.3257 0.0200 -0.0537 0.0026 102 VAL A C 717 O O . VAL A 102 ? 0.3221 0.3759 0.3053 0.0206 -0.0536 0.0020 102 VAL A O 718 C CB . VAL A 102 ? 0.3347 0.3733 0.3206 0.0190 -0.0547 0.0062 102 VAL A CB 719 C CG1 . VAL A 102 ? 0.3196 0.3571 0.3025 0.0149 -0.0512 0.0083 102 VAL A CG1 720 C CG2 . VAL A 102 ? 0.3290 0.3615 0.3177 0.0206 -0.0572 0.0069 102 VAL A CG2 721 N N . PRO A 103 ? 0.3529 0.4115 0.3292 0.0183 -0.0520 0.0021 103 PRO A N 722 C CA . PRO A 103 ? 0.3679 0.4352 0.3425 0.0163 -0.0496 0.0011 103 PRO A CA 723 C C . PRO A 103 ? 0.3836 0.4472 0.3593 0.0123 -0.0469 0.0034 103 PRO A C 724 O O . PRO A 103 ? 0.4463 0.5028 0.4209 0.0096 -0.0458 0.0059 103 PRO A O 725 C CB . PRO A 103 ? 0.3694 0.4421 0.3383 0.0136 -0.0480 0.0010 103 PRO A CB 726 C CG . PRO A 103 ? 0.3673 0.4364 0.3356 0.0167 -0.0507 0.0005 103 PRO A CG 727 C CD . PRO A 103 ? 0.3636 0.4222 0.3360 0.0183 -0.0525 0.0021 103 PRO A CD 728 N N . ASP A 104 ? 0.4022 0.4701 0.3798 0.0124 -0.0461 0.0025 104 ASP A N 729 C CA . ASP A 104 ? 0.4023 0.4660 0.3818 0.0093 -0.0440 0.0046 104 ASP A CA 730 C C . ASP A 104 ? 0.3588 0.4122 0.3420 0.0102 -0.0453 0.0065 104 ASP A C 731 O O . ASP A 104 ? 0.3384 0.3864 0.3213 0.0073 -0.0436 0.0088 104 ASP A O 732 C CB . ASP A 104 ? 0.4428 0.5076 0.4177 0.0035 -0.0405 0.0063 104 ASP A CB 733 C CG . ASP A 104 ? 0.5078 0.5738 0.4839 0.0007 -0.0381 0.0070 104 ASP A CG 734 O OD1 . ASP A 104 ? 0.5143 0.5806 0.4950 0.0032 -0.0390 0.0062 104 ASP A OD1 735 O OD2 . ASP A 104 ? 0.5711 0.6374 0.5427 -0.0043 -0.0354 0.0084 104 ASP A OD2 736 N N . TYR A 105 ? 0.3262 0.3773 0.3123 0.0143 -0.0486 0.0054 105 TYR A N 737 C CA . TYR A 105 ? 0.3107 0.3542 0.3008 0.0151 -0.0501 0.0067 105 TYR A CA 738 C C . TYR A 105 ? 0.2920 0.3336 0.2845 0.0126 -0.0481 0.0082 105 TYR A C 739 O O . TYR A 105 ? 0.2897 0.3260 0.2837 0.0111 -0.0474 0.0103 105 TYR A O 740 C CB . TYR A 105 ? 0.3153 0.3581 0.3073 0.0192 -0.0538 0.0048 105 TYR A CB 741 C CG . TYR A 105 ? 0.3261 0.3617 0.3217 0.0195 -0.0559 0.0059 105 TYR A CG 742 C CD1 . TYR A 105 ? 0.3234 0.3566 0.3218 0.0185 -0.0556 0.0067 105 TYR A CD1 743 C CD2 . TYR A 105 ? 0.3240 0.3559 0.3201 0.0207 -0.0581 0.0062 105 TYR A CD2 744 C CE1 . TYR A 105 ? 0.3260 0.3537 0.3275 0.0181 -0.0574 0.0078 105 TYR A CE1 745 C CE2 . TYR A 105 ? 0.3365 0.3632 0.3359 0.0204 -0.0600 0.0071 105 TYR A CE2 746 C CZ . TYR A 105 ? 0.3302 0.3551 0.3323 0.0189 -0.0595 0.0080 105 TYR A CZ 747 O OH . TYR A 105 ? 0.3482 0.3690 0.3533 0.0180 -0.0613 0.0090 105 TYR A OH 748 N N . ALA A 106 ? 0.2849 0.3312 0.2776 0.0126 -0.0472 0.0071 106 ALA A N 749 C CA . ALA A 106 ? 0.2742 0.3188 0.2692 0.0105 -0.0455 0.0084 106 ALA A CA 750 C C . ALA A 106 ? 0.2754 0.3178 0.2687 0.0065 -0.0423 0.0107 106 ALA A C 751 O O . ALA A 106 ? 0.2630 0.3010 0.2587 0.0054 -0.0416 0.0123 106 ALA A O 752 C CB . ALA A 106 ? 0.2677 0.3184 0.2625 0.0113 -0.0450 0.0066 106 ALA A CB 753 N N . SER A 107 ? 0.2749 0.3203 0.2636 0.0044 -0.0406 0.0107 107 SER A N 754 C CA . SER A 107 ? 0.2808 0.3223 0.2661 0.0005 -0.0380 0.0129 107 SER A CA 755 C C . SER A 107 ? 0.2761 0.3095 0.2611 0.0011 -0.0389 0.0146 107 SER A C 756 O O . SER A 107 ? 0.2766 0.3050 0.2612 -0.0003 -0.0377 0.0163 107 SER A O 757 C CB . SER A 107 ? 0.2895 0.3357 0.2686 -0.0027 -0.0361 0.0125 107 SER A CB 758 O OG . SER A 107 ? 0.2879 0.3418 0.2672 -0.0043 -0.0345 0.0114 107 SER A OG 759 N N . LEU A 108 ? 0.2734 0.3060 0.2587 0.0037 -0.0412 0.0139 108 LEU A N 760 C CA . LEU A 108 ? 0.2760 0.3018 0.2610 0.0047 -0.0423 0.0153 108 LEU A CA 761 C C . LEU A 108 ? 0.2655 0.2890 0.2566 0.0062 -0.0432 0.0159 108 LEU A C 762 O O . LEU A 108 ? 0.2615 0.2804 0.2525 0.0059 -0.0427 0.0174 108 LEU A O 763 C CB . LEU A 108 ? 0.2759 0.3019 0.2602 0.0072 -0.0447 0.0143 108 LEU A CB 764 C CG . LEU A 108 ? 0.2834 0.3035 0.2676 0.0089 -0.0461 0.0154 108 LEU A CG 765 C CD1 . LEU A 108 ? 0.2818 0.2962 0.2599 0.0068 -0.0443 0.0171 108 LEU A CD1 766 C CD2 . LEU A 108 ? 0.2832 0.3040 0.2668 0.0114 -0.0486 0.0142 108 LEU A CD2 767 N N . ARG A 109 ? 0.2549 0.2813 0.2503 0.0077 -0.0447 0.0147 109 ARG A N 768 C CA . ARG A 109 ? 0.2529 0.2775 0.2535 0.0082 -0.0456 0.0152 109 ARG A CA 769 C C . ARG A 109 ? 0.2507 0.2742 0.2516 0.0059 -0.0429 0.0167 109 ARG A C 770 O O . ARG A 109 ? 0.2379 0.2587 0.2411 0.0058 -0.0428 0.0179 109 ARG A O 771 C CB . ARG A 109 ? 0.2524 0.2792 0.2557 0.0097 -0.0477 0.0137 109 ARG A CB 772 C CG . ARG A 109 ? 0.2563 0.2812 0.2641 0.0093 -0.0485 0.0143 109 ARG A CG 773 C CD . ARG A 109 ? 0.2581 0.2831 0.2665 0.0110 -0.0513 0.0127 109 ARG A CD 774 N NE . ARG A 109 ? 0.2503 0.2727 0.2617 0.0100 -0.0522 0.0134 109 ARG A NE 775 C CZ . ARG A 109 ? 0.2570 0.2799 0.2693 0.0086 -0.0507 0.0138 109 ARG A CZ 776 N NH1 . ARG A 109 ? 0.2536 0.2795 0.2642 0.0081 -0.0481 0.0137 109 ARG A NH1 777 N NH2 . ARG A 109 ? 0.2538 0.2740 0.2683 0.0074 -0.0518 0.0145 109 ARG A NH2 778 N N . SER A 110 ? 0.2563 0.2825 0.2549 0.0040 -0.0408 0.0164 110 SER A N 779 C CA . SER A 110 ? 0.2635 0.2887 0.2618 0.0016 -0.0383 0.0176 110 SER A CA 780 C C . SER A 110 ? 0.2712 0.2912 0.2655 0.0004 -0.0369 0.0193 110 SER A C 781 O O . SER A 110 ? 0.2692 0.2865 0.2648 0.0000 -0.0360 0.0204 110 SER A O 782 C CB . SER A 110 ? 0.2696 0.2994 0.2654 -0.0003 -0.0364 0.0168 110 SER A CB 783 O OG . SER A 110 ? 0.2786 0.3068 0.2736 -0.0029 -0.0339 0.0181 110 SER A OG 784 N N . LEU A 111 ? 0.2749 0.2933 0.2637 -0.0001 -0.0367 0.0193 111 LEU A N 785 C CA . LEU A 111 ? 0.2900 0.3019 0.2733 -0.0011 -0.0358 0.0209 111 LEU A CA 786 C C . LEU A 111 ? 0.2774 0.2856 0.2631 0.0020 -0.0375 0.0214 111 LEU A C 787 O O . LEU A 111 ? 0.2844 0.2881 0.2682 0.0022 -0.0367 0.0225 111 LEU A O 788 C CB . LEU A 111 ? 0.3026 0.3129 0.2780 -0.0031 -0.0352 0.0210 111 LEU A CB 789 C CG . LEU A 111 ? 0.3117 0.3218 0.2855 -0.0012 -0.0372 0.0203 111 LEU A CG 790 C CD1 . LEU A 111 ? 0.3290 0.3312 0.2992 0.0005 -0.0382 0.0214 111 LEU A CD1 791 C CD2 . LEU A 111 ? 0.3256 0.3384 0.2931 -0.0044 -0.0361 0.0199 111 LEU A CD2 792 N N . VAL A 112 ? 0.2680 0.2784 0.2577 0.0046 -0.0399 0.0205 112 VAL A N 793 C CA . VAL A 112 ? 0.2764 0.2851 0.2693 0.0074 -0.0416 0.0207 112 VAL A CA 794 C C . VAL A 112 ? 0.2667 0.2776 0.2656 0.0073 -0.0412 0.0211 112 VAL A C 795 O O . VAL A 112 ? 0.2654 0.2746 0.2648 0.0086 -0.0411 0.0218 112 VAL A O 796 C CB . VAL A 112 ? 0.2733 0.2841 0.2688 0.0097 -0.0443 0.0197 112 VAL A CB 797 C CG1 . VAL A 112 ? 0.2823 0.2927 0.2811 0.0122 -0.0460 0.0198 112 VAL A CG1 798 C CG2 . VAL A 112 ? 0.2800 0.2886 0.2691 0.0098 -0.0447 0.0194 112 VAL A CG2 799 N N . ALA A 113 ? 0.2559 0.2706 0.2587 0.0060 -0.0410 0.0206 113 ALA A N 800 C CA . ALA A 113 ? 0.2521 0.2686 0.2600 0.0054 -0.0406 0.0210 113 ALA A CA 801 C C . ALA A 113 ? 0.2545 0.2687 0.2604 0.0044 -0.0382 0.0222 113 ALA A C 802 O O . ALA A 113 ? 0.2518 0.2666 0.2608 0.0051 -0.0382 0.0227 113 ALA A O 803 C CB . ALA A 113 ? 0.2367 0.2561 0.2472 0.0041 -0.0408 0.0202 113 ALA A CB 804 N N . SER A 114 ? 0.2535 0.2656 0.2541 0.0025 -0.0363 0.0224 114 SER A N 805 C CA . SER A 114 ? 0.2811 0.2900 0.2783 0.0012 -0.0341 0.0235 114 SER A CA 806 C C . SER A 114 ? 0.2875 0.2908 0.2803 0.0032 -0.0344 0.0242 114 SER A C 807 O O . SER A 114 ? 0.3155 0.3167 0.3077 0.0036 -0.0334 0.0249 114 SER A O 808 C CB . SER A 114 ? 0.2888 0.2970 0.2805 -0.0019 -0.0321 0.0235 114 SER A CB 809 O OG . SER A 114 ? 0.3359 0.3402 0.3238 -0.0035 -0.0302 0.0246 114 SER A OG 810 N N . SER A 115 ? 0.2884 0.2893 0.2777 0.0048 -0.0359 0.0239 115 SER A N 811 C CA . SER A 115 ? 0.3039 0.2995 0.2887 0.0076 -0.0368 0.0243 115 SER A CA 812 C C . SER A 115 ? 0.2937 0.2929 0.2848 0.0109 -0.0381 0.0239 115 SER A C 813 O O . SER A 115 ? 0.3171 0.3134 0.3056 0.0133 -0.0381 0.0242 115 SER A O 814 C CB . SER A 115 ? 0.3126 0.3050 0.2920 0.0084 -0.0382 0.0240 115 SER A CB 815 O OG . SER A 115 ? 0.3338 0.3216 0.3095 0.0120 -0.0398 0.0240 115 SER A OG 816 N N . GLY A 116 ? 0.2792 0.2850 0.2780 0.0110 -0.0393 0.0232 116 GLY A N 817 C CA . GLY A 116 ? 0.2726 0.2835 0.2779 0.0127 -0.0403 0.0230 116 GLY A CA 818 C C . GLY A 116 ? 0.2737 0.2854 0.2788 0.0165 -0.0424 0.0223 116 GLY A C 819 O O . GLY A 116 ? 0.2641 0.2801 0.2729 0.0184 -0.0429 0.0220 116 GLY A O 820 N N . THR A 117 ? 0.2817 0.2899 0.2824 0.0177 -0.0436 0.0220 117 THR A N 821 C CA . THR A 117 ? 0.2893 0.2980 0.2893 0.0216 -0.0458 0.0212 117 THR A CA 822 C C . THR A 117 ? 0.2917 0.2998 0.2906 0.0219 -0.0476 0.0206 117 THR A C 823 O O . THR A 117 ? 0.2909 0.2951 0.2855 0.0200 -0.0469 0.0209 117 THR A O 824 C CB . THR A 117 ? 0.3039 0.3057 0.2957 0.0250 -0.0457 0.0214 117 THR A CB 825 O OG1 . THR A 117 ? 0.3084 0.3115 0.2997 0.0295 -0.0480 0.0204 117 THR A OG1 826 C CG2 . THR A 117 ? 0.3135 0.3056 0.2954 0.0232 -0.0446 0.0223 117 THR A CG2 827 N N . LEU A 118 ? 0.2937 0.3065 0.2966 0.0242 -0.0498 0.0197 118 LEU A N 828 C CA . LEU A 118 ? 0.2995 0.3115 0.3011 0.0253 -0.0518 0.0190 118 LEU A CA 829 C C . LEU A 118 ? 0.3104 0.3190 0.3065 0.0299 -0.0532 0.0186 118 LEU A C 830 O O . LEU A 118 ? 0.3295 0.3388 0.3254 0.0316 -0.0553 0.0178 118 LEU A O 831 C CB . LEU A 118 ? 0.2991 0.3184 0.3085 0.0243 -0.0536 0.0182 118 LEU A CB 832 C CG . LEU A 118 ? 0.2909 0.3112 0.3033 0.0205 -0.0532 0.0184 118 LEU A CG 833 C CD1 . LEU A 118 ? 0.2991 0.3253 0.3183 0.0192 -0.0552 0.0178 118 LEU A CD1 834 C CD2 . LEU A 118 ? 0.3071 0.3233 0.3147 0.0202 -0.0533 0.0182 118 LEU A CD2 835 N N . GLU A 119 ? 0.3285 0.3327 0.3195 0.0320 -0.0524 0.0190 119 GLU A N 836 C CA . GLU A 119 ? 0.3436 0.3433 0.3279 0.0371 -0.0541 0.0184 119 GLU A CA 837 C C . GLU A 119 ? 0.3485 0.3406 0.3252 0.0369 -0.0548 0.0187 119 GLU A C 838 O O . GLU A 119 ? 0.3405 0.3265 0.3117 0.0335 -0.0532 0.0197 119 GLU A O 839 C CB . GLU A 119 ? 0.3669 0.3602 0.3444 0.0394 -0.0532 0.0188 119 GLU A CB 840 C CG . GLU A 119 ? 0.3906 0.3913 0.3743 0.0408 -0.0527 0.0183 119 GLU A CG 841 C CD . GLU A 119 ? 0.4237 0.4172 0.4005 0.0417 -0.0512 0.0190 119 GLU A CD 842 O OE1 . GLU A 119 ? 0.4018 0.3928 0.3784 0.0372 -0.0488 0.0202 119 GLU A OE1 843 O OE2 . GLU A 119 ? 0.4227 0.4124 0.3934 0.0472 -0.0526 0.0182 119 GLU A OE2 844 N N . PHE A 120 ? 0.3477 0.3408 0.3237 0.0405 -0.0573 0.0177 120 PHE A N 845 C CA . PHE A 120 ? 0.3620 0.3494 0.3318 0.0405 -0.0584 0.0177 120 PHE A CA 846 C C . PHE A 120 ? 0.3854 0.3671 0.3475 0.0462 -0.0606 0.0171 120 PHE A C 847 O O . PHE A 120 ? 0.3944 0.3820 0.3606 0.0505 -0.0623 0.0158 120 PHE A O 848 C CB . PHE A 120 ? 0.3483 0.3430 0.3256 0.0393 -0.0597 0.0169 120 PHE A CB 849 C CG . PHE A 120 ? 0.3612 0.3512 0.3329 0.0390 -0.0606 0.0169 120 PHE A CG 850 C CD1 . PHE A 120 ? 0.3639 0.3514 0.3330 0.0347 -0.0590 0.0177 120 PHE A CD1 851 C CD2 . PHE A 120 ? 0.3634 0.3523 0.3324 0.0431 -0.0632 0.0160 120 PHE A CD2 852 C CE1 . PHE A 120 ? 0.3790 0.3632 0.3430 0.0344 -0.0598 0.0176 120 PHE A CE1 853 C CE2 . PHE A 120 ? 0.3770 0.3616 0.3406 0.0428 -0.0640 0.0161 120 PHE A CE2 854 C CZ . PHE A 120 ? 0.3892 0.3716 0.3503 0.0383 -0.0623 0.0169 120 PHE A CZ 855 N N . ASN A 121 ? 0.4000 0.4028 0.3337 0.0603 0.0097 0.0675 121 ASN A N 856 C CA . ASN A 121 ? 0.4390 0.4469 0.3748 0.0678 0.0136 0.0741 121 ASN A CA 857 C C . ASN A 121 ? 0.4375 0.4540 0.3722 0.0701 0.0093 0.0754 121 ASN A C 858 O O . ASN A 121 ? 0.4264 0.4368 0.3561 0.0683 0.0090 0.0734 121 ASN A O 859 C CB . ASN A 121 ? 0.4776 0.4713 0.4089 0.0704 0.0220 0.0766 121 ASN A CB 860 C CG . ASN A 121 ? 0.5316 0.5180 0.4639 0.0704 0.0275 0.0770 121 ASN A CG 861 O OD1 . ASN A 121 ? 0.5880 0.5819 0.5256 0.0699 0.0259 0.0769 121 ASN A OD1 862 N ND2 . ASN A 121 ? 0.5913 0.5625 0.5181 0.0707 0.0345 0.0775 121 ASN A ND2 863 N N . ASN A 122 ? 0.4448 0.4759 0.3843 0.0739 0.0060 0.0788 122 ASN A N 864 C CA . ASN A 122 ? 0.4532 0.4927 0.3906 0.0766 0.0019 0.0806 122 ASN A CA 865 C C . ASN A 122 ? 0.4486 0.4818 0.3814 0.0826 0.0076 0.0857 122 ASN A C 866 O O . ASN A 122 ? 0.4318 0.4595 0.3656 0.0869 0.0142 0.0899 122 ASN A O 867 C CB . ASN A 122 ? 0.4877 0.5446 0.4312 0.0791 -0.0035 0.0830 122 ASN A CB 868 C CG . ASN A 122 ? 0.5026 0.5663 0.4491 0.0724 -0.0103 0.0773 122 ASN A CG 869 O OD1 . ASN A 122 ? 0.5456 0.6114 0.4884 0.0691 -0.0157 0.0735 122 ASN A OD1 870 N ND2 . ASN A 122 ? 0.5164 0.5826 0.4693 0.0704 -0.0097 0.0765 122 ASN A ND2 871 N N . GLU A 123 ? 0.4493 0.4821 0.3765 0.0829 0.0058 0.0853 123 GLU A N 872 C CA . GLU A 123 ? 0.4658 0.4933 0.3880 0.0886 0.0110 0.0905 123 GLU A CA 873 C C . GLU A 123 ? 0.4763 0.5143 0.3954 0.0918 0.0062 0.0927 123 GLU A C 874 O O . GLU A 123 ? 0.4509 0.4962 0.3697 0.0879 -0.0006 0.0885 123 GLU A O 875 C CB . GLU A 123 ? 0.4627 0.4751 0.3796 0.0851 0.0156 0.0876 123 GLU A CB 876 C CG . GLU A 123 ? 0.4621 0.4622 0.3801 0.0820 0.0209 0.0856 123 GLU A CG 877 C CD . GLU A 123 ? 0.4633 0.4498 0.3767 0.0780 0.0247 0.0825 123 GLU A CD 878 O OE1 . GLU A 123 ? 0.4522 0.4397 0.3646 0.0733 0.0204 0.0779 123 GLU A OE1 879 O OE2 . GLU A 123 ? 0.4651 0.4399 0.3762 0.0794 0.0319 0.0847 123 GLU A OE2 880 N N . SER A 124 ? 0.5062 0.5436 0.4218 0.0991 0.0101 0.0993 124 SER A N 881 C CA . SER A 124 ? 0.5176 0.5642 0.4288 0.1034 0.0060 0.1027 124 SER A CA 882 C C . SER A 124 ? 0.5276 0.5649 0.4301 0.1026 0.0088 0.1018 124 SER A C 883 O O . SER A 124 ? 0.5120 0.5412 0.4098 0.1074 0.0153 0.1067 124 SER A O 884 C CB . SER A 124 ? 0.5511 0.6029 0.4631 0.1126 0.0086 0.1113 124 SER A CB 885 O OG . SER A 124 ? 0.5815 0.6413 0.5029 0.1138 0.0076 0.1127 124 SER A OG 886 N N . PHE A 125 ? 0.5217 0.5598 0.4222 0.0966 0.0043 0.0955 125 PHE A N 887 C CA . PHE A 125 ? 0.5305 0.5614 0.4236 0.0957 0.0066 0.0943 125 PHE A CA 888 C C . PHE A 125 ? 0.5578 0.5960 0.4440 0.1013 0.0041 0.0988 125 PHE A C 889 O O . PHE A 125 ? 0.5798 0.6307 0.4674 0.1029 -0.0024 0.0998 125 PHE A O 890 C CB . PHE A 125 ? 0.5221 0.5523 0.4156 0.0881 0.0024 0.0864 125 PHE A CB 891 C CG . PHE A 125 ? 0.5009 0.5214 0.3989 0.0826 0.0055 0.0821 125 PHE A CG 892 C CD1 . PHE A 125 ? 0.5006 0.5232 0.4051 0.0795 0.0032 0.0796 125 PHE A CD1 893 C CD2 . PHE A 125 ? 0.5118 0.5210 0.4074 0.0806 0.0110 0.0808 125 PHE A CD2 894 C CE1 . PHE A 125 ? 0.4858 0.4988 0.3931 0.0746 0.0058 0.0758 125 PHE A CE1 895 C CE2 . PHE A 125 ? 0.5166 0.5172 0.4161 0.0754 0.0132 0.0768 125 PHE A CE2 896 C CZ . PHE A 125 ? 0.4877 0.4900 0.3925 0.0726 0.0105 0.0744 125 PHE A CZ 897 N N . ASN A 126 ? 0.5636 0.5938 0.4422 0.1040 0.0093 0.1016 126 ASN A N 898 C CA . ASN A 126 ? 0.6049 0.6405 0.4750 0.1095 0.0074 0.1061 126 ASN A CA 899 C C . ASN A 126 ? 0.5853 0.6234 0.4498 0.1053 0.0028 0.1007 126 ASN A C 900 O O . ASN A 126 ? 0.5817 0.6109 0.4410 0.1038 0.0074 0.0992 126 ASN A O 901 C CB . ASN A 126 ? 0.6506 0.6755 0.5144 0.1151 0.0162 0.1125 126 ASN A CB 902 C CG . ASN A 126 ? 0.6836 0.7136 0.5381 0.1222 0.0146 0.1186 126 ASN A CG 903 O OD1 . ASN A 126 ? 0.6929 0.7314 0.5427 0.1212 0.0078 0.1164 126 ASN A OD1 904 N ND2 . ASN A 126 ? 0.7366 0.7610 0.5875 0.1293 0.0208 0.1262 126 ASN A ND2 905 N N . TRP A 127 ? 0.5620 0.6120 0.4278 0.1033 -0.0058 0.0976 127 TRP A N 906 C CA . TRP A 127 ? 0.5671 0.6198 0.4268 0.0995 -0.0107 0.0924 127 TRP A CA 907 C C . TRP A 127 ? 0.6014 0.6606 0.4509 0.1045 -0.0143 0.0963 127 TRP A C 908 O O . TRP A 127 ? 0.5961 0.6641 0.4427 0.1024 -0.0219 0.0931 127 TRP A O 909 C CB . TRP A 127 ? 0.5462 0.6062 0.4123 0.0933 -0.0180 0.0858 127 TRP A CB 910 C CG . TRP A 127 ? 0.5207 0.5745 0.3959 0.0881 -0.0154 0.0817 127 TRP A CG 911 C CD1 . TRP A 127 ? 0.5112 0.5698 0.3956 0.0856 -0.0182 0.0802 127 TRP A CD1 912 C CD2 . TRP A 127 ? 0.5229 0.5644 0.3989 0.0848 -0.0094 0.0787 127 TRP A CD2 913 N NE1 . TRP A 127 ? 0.5064 0.5561 0.3958 0.0812 -0.0147 0.0765 127 TRP A NE1 914 C CE2 . TRP A 127 ? 0.5034 0.5432 0.3887 0.0804 -0.0098 0.0754 127 TRP A CE2 915 C CE3 . TRP A 127 ? 0.5306 0.5633 0.4013 0.0849 -0.0040 0.0784 127 TRP A CE3 916 C CZ2 . TRP A 127 ? 0.5098 0.5394 0.3981 0.0763 -0.0056 0.0720 127 TRP A CZ2 917 C CZ3 . TRP A 127 ? 0.5378 0.5612 0.4132 0.0805 0.0003 0.0749 127 TRP A CZ3 918 C CH2 . TRP A 127 ? 0.5186 0.5406 0.4024 0.0763 -0.0008 0.0717 127 TRP A CH2 919 N N . THR A 128 ? 0.6503 0.7047 0.4935 0.1110 -0.0088 0.1032 128 THR A N 920 C CA . THR A 128 ? 0.6725 0.7319 0.5043 0.1163 -0.0118 0.1075 128 THR A CA 921 C C . THR A 128 ? 0.6640 0.7198 0.4857 0.1129 -0.0128 0.1025 128 THR A C 922 O O . THR A 128 ? 0.6682 0.7129 0.4884 0.1104 -0.0062 0.1000 128 THR A O 923 C CB . THR A 128 ? 0.7328 0.7856 0.5593 0.1243 -0.0046 0.1163 128 THR A CB 924 O OG1 . THR A 128 ? 0.7860 0.8240 0.6126 0.1226 0.0050 0.1156 128 THR A OG1 925 C CG2 . THR A 128 ? 0.7049 0.7639 0.5399 0.1292 -0.0052 0.1219 128 THR A CG2 926 N N . GLY A 129 ? 0.6708 0.7360 0.4860 0.1126 -0.0210 0.1008 129 GLY A N 927 C CA . GLY A 129 ? 0.6634 0.7251 0.4665 0.1105 -0.0219 0.0969 129 GLY A CA 928 C C . GLY A 129 ? 0.6368 0.7009 0.4426 0.1028 -0.0271 0.0878 129 GLY A C 929 O O . GLY A 129 ? 0.6289 0.6900 0.4247 0.1009 -0.0280 0.0840 129 GLY A O 930 N N . VAL A 130 ? 0.6049 0.6734 0.4238 0.0984 -0.0301 0.0843 130 VAL A N 931 C CA . VAL A 130 ? 0.5843 0.6549 0.4061 0.0912 -0.0352 0.0760 130 VAL A CA 932 C C . VAL A 130 ? 0.5667 0.6500 0.3961 0.0890 -0.0436 0.0750 130 VAL A C 933 O O . VAL A 130 ? 0.5457 0.6359 0.3807 0.0930 -0.0445 0.0806 130 VAL A O 934 C CB . VAL A 130 ? 0.5731 0.6345 0.4035 0.0864 -0.0298 0.0714 130 VAL A CB 935 C CG1 . VAL A 130 ? 0.5835 0.6333 0.4077 0.0878 -0.0216 0.0718 130 VAL A CG1 936 C CG2 . VAL A 130 ? 0.5540 0.6159 0.3970 0.0868 -0.0275 0.0741 130 VAL A CG2 937 N N . THR A 131 ? 0.5422 0.6285 0.3721 0.0828 -0.0494 0.0679 131 THR A N 938 C CA . THR A 131 ? 0.5437 0.6414 0.3818 0.0793 -0.0570 0.0659 131 THR A CA 939 C C . THR A 131 ? 0.5263 0.6203 0.3774 0.0751 -0.0543 0.0629 131 THR A C 940 O O . THR A 131 ? 0.5063 0.5904 0.3576 0.0717 -0.0504 0.0585 131 THR A O 941 C CB . THR A 131 ? 0.5561 0.6580 0.3873 0.0741 -0.0645 0.0594 131 THR A CB 942 O OG1 . THR A 131 ? 0.5722 0.6757 0.3893 0.0777 -0.0668 0.0616 131 THR A OG1 943 C CG2 . THR A 131 ? 0.5627 0.6773 0.4027 0.0704 -0.0724 0.0578 131 THR A CG2 944 N N . GLN A 132 ? 0.5169 0.6190 0.3785 0.0756 -0.0563 0.0656 132 GLN A N 945 C CA . GLN A 132 ? 0.5157 0.6143 0.3887 0.0721 -0.0536 0.0635 132 GLN A CA 946 C C . GLN A 132 ? 0.5165 0.6220 0.3945 0.0656 -0.0604 0.0579 132 GLN A C 947 O O . GLN A 132 ? 0.4931 0.6070 0.3668 0.0641 -0.0671 0.0562 132 GLN A O 948 C CB . GLN A 132 ? 0.5171 0.6188 0.3984 0.0770 -0.0501 0.0702 132 GLN A CB 949 C CG . GLN A 132 ? 0.5247 0.6181 0.4015 0.0832 -0.0425 0.0759 132 GLN A CG 950 C CD . GLN A 132 ? 0.5387 0.6324 0.4237 0.0875 -0.0380 0.0818 132 GLN A CD 951 O OE1 . GLN A 132 ? 0.5382 0.6297 0.4321 0.0844 -0.0362 0.0798 132 GLN A OE1 952 N NE2 . GLN A 132 ? 0.5234 0.6190 0.4049 0.0949 -0.0356 0.0890 132 GLN A NE2 953 N N . ASN A 133 ? 0.4905 0.5917 0.3771 0.0616 -0.0584 0.0550 133 ASN A N 954 C CA . ASN A 133 ? 0.4979 0.6050 0.3912 0.0556 -0.0636 0.0506 133 ASN A CA 955 C C . ASN A 133 ? 0.4901 0.5962 0.3769 0.0498 -0.0687 0.0436 133 ASN A C 956 O O . ASN A 133 ? 0.4721 0.5868 0.3613 0.0458 -0.0748 0.0410 133 ASN A O 957 C CB . ASN A 133 ? 0.5335 0.6553 0.4338 0.0576 -0.0677 0.0548 133 ASN A CB 958 C CG . ASN A 133 ? 0.5948 0.7168 0.5034 0.0624 -0.0622 0.0609 133 ASN A CG 959 O OD1 . ASN A 133 ? 0.5555 0.6661 0.4647 0.0634 -0.0555 0.0614 133 ASN A OD1 960 N ND2 . ASN A 133 ? 0.6953 0.8303 0.6106 0.0654 -0.0650 0.0655 133 ASN A ND2 961 N N . GLY A 134 ? 0.4781 0.5734 0.3574 0.0492 -0.0658 0.0403 134 GLY A N 962 C CA . GLY A 134 ? 0.4907 0.5829 0.3640 0.0438 -0.0695 0.0334 134 GLY A CA 963 C C . GLY A 134 ? 0.4848 0.5771 0.3657 0.0376 -0.0720 0.0289 134 GLY A C 964 O O . GLY A 134 ? 0.4638 0.5528 0.3530 0.0372 -0.0686 0.0300 134 GLY A O 965 N N . THR A 135 ? 0.4769 0.5722 0.3542 0.0326 -0.0777 0.0239 135 THR A N 966 C CA . THR A 135 ? 0.4990 0.5940 0.3823 0.0262 -0.0802 0.0194 135 THR A CA 967 C C . THR A 135 ? 0.5075 0.5937 0.3829 0.0215 -0.0816 0.0123 135 THR A C 968 O O . THR A 135 ? 0.5104 0.5927 0.3758 0.0231 -0.0814 0.0109 135 THR A O 969 C CB . THR A 135 ? 0.5222 0.6313 0.4111 0.0236 -0.0862 0.0203 135 THR A CB 970 O OG1 . THR A 135 ? 0.5218 0.6367 0.4019 0.0227 -0.0918 0.0184 135 THR A OG1 971 C CG2 . THR A 135 ? 0.5227 0.6410 0.4201 0.0289 -0.0845 0.0277 135 THR A CG2 972 N N . SER A 136 ? 0.5024 0.5849 0.3823 0.0160 -0.0826 0.0082 136 SER A N 973 C CA . SER A 136 ? 0.5150 0.5879 0.3885 0.0116 -0.0834 0.0016 136 SER A CA 974 C C . SER A 136 ? 0.5237 0.5986 0.4012 0.0046 -0.0873 -0.0023 136 SER A C 975 O O . SER A 136 ? 0.5111 0.5903 0.3983 0.0033 -0.0870 -0.0002 136 SER A O 976 C CB . SER A 136 ? 0.5097 0.5700 0.3838 0.0133 -0.0777 0.0008 136 SER A CB 977 O OG . SER A 136 ? 0.5058 0.5567 0.3760 0.0091 -0.0782 -0.0050 136 SER A OG 978 N N . SER A 137 ? 0.5410 0.6119 0.4106 0.0001 -0.0905 -0.0082 137 SER A N 979 C CA . SER A 137 ? 0.5545 0.6248 0.4267 -0.0071 -0.0936 -0.0127 137 SER A CA 980 C C . SER A 137 ? 0.5571 0.6158 0.4332 -0.0088 -0.0897 -0.0144 137 SER A C 981 O O . SER A 137 ? 0.5323 0.5904 0.4126 -0.0143 -0.0911 -0.0167 137 SER A O 982 C CB . SER A 137 ? 0.5865 0.6536 0.4477 -0.0115 -0.0975 -0.0189 137 SER A CB 983 O OG . SER A 137 ? 0.5992 0.6520 0.4523 -0.0102 -0.0939 -0.0222 137 SER A OG 984 N N . ALA A 138 ? 0.5520 0.6019 0.4268 -0.0042 -0.0850 -0.0131 138 ALA A N 985 C CA . ALA A 138 ? 0.5710 0.6106 0.4498 -0.0049 -0.0815 -0.0138 138 ALA A CA 986 C C . ALA A 138 ? 0.5631 0.6070 0.4521 -0.0039 -0.0796 -0.0092 138 ALA A C 987 O O . ALA A 138 ? 0.5904 0.6265 0.4825 -0.0050 -0.0774 -0.0095 138 ALA A O 988 C CB . ALA A 138 ? 0.5525 0.5826 0.4272 -0.0004 -0.0775 -0.0140 138 ALA A CB 989 N N . CYS A 139 ? 0.5545 0.6103 0.4481 -0.0017 -0.0805 -0.0047 139 CYS A N 990 C CA . CYS A 139 ? 0.5628 0.6225 0.4655 -0.0001 -0.0780 -0.0001 139 CYS A CA 991 C C . CYS A 139 ? 0.5783 0.6520 0.4870 -0.0017 -0.0812 0.0020 139 CYS A C 992 O O . CYS A 139 ? 0.6115 0.6945 0.5228 0.0025 -0.0812 0.0066 139 CYS A O 993 C CB . CYS A 139 ? 0.5669 0.6255 0.4700 0.0064 -0.0739 0.0045 139 CYS A CB 994 S SG . CYS A 139 ? 0.5713 0.6298 0.4835 0.0086 -0.0694 0.0095 139 CYS A SG 995 N N . LYS A 140 ? 0.5772 0.6524 0.4887 -0.0080 -0.0838 -0.0012 140 LYS A N 996 C CA . LYS A 140 ? 0.5932 0.6828 0.5119 -0.0105 -0.0872 0.0002 140 LYS A CA 997 C C . LYS A 140 ? 0.5778 0.6721 0.5070 -0.0087 -0.0838 0.0051 140 LYS A C 998 O O . LYS A 140 ? 0.5647 0.6496 0.4957 -0.0099 -0.0799 0.0047 140 LYS A O 999 C CB . LYS A 140 ? 0.6060 0.6949 0.5243 -0.0187 -0.0907 -0.0052 140 LYS A CB 1000 C CG . LYS A 140 ? 0.6195 0.7024 0.5267 -0.0216 -0.0940 -0.0109 140 LYS A CG 1001 C CD . LYS A 140 ? 0.6222 0.7172 0.5264 -0.0210 -0.0992 -0.0105 140 LYS A CD 1002 C CE . LYS A 140 ? 0.6434 0.7331 0.5374 -0.0263 -0.1030 -0.0173 140 LYS A CE 1003 N NZ . LYS A 140 ? 0.6500 0.7510 0.5395 -0.0257 -0.1084 -0.0170 140 LYS A NZ 1004 N N . ARG A 141 ? 0.5552 0.6639 0.4910 -0.0058 -0.0851 0.0097 141 ARG A N 1005 C CA . ARG A 141 ? 0.5787 0.6938 0.5255 -0.0043 -0.0819 0.0143 141 ARG A CA 1006 C C . ARG A 141 ? 0.6170 0.7492 0.5723 -0.0074 -0.0866 0.0149 141 ARG A C 1007 O O . ARG A 141 ? 0.5888 0.7325 0.5437 -0.0051 -0.0909 0.0167 141 ARG A O 1008 C CB . ARG A 141 ? 0.5545 0.6704 0.5024 0.0038 -0.0778 0.0204 141 ARG A CB 1009 C CG . ARG A 141 ? 0.5473 0.6697 0.5060 0.0064 -0.0739 0.0255 141 ARG A CG 1010 C CD . ARG A 141 ? 0.5396 0.6590 0.4976 0.0142 -0.0690 0.0310 141 ARG A CD 1011 N NE . ARG A 141 ? 0.5226 0.6259 0.4763 0.0146 -0.0637 0.0300 141 ARG A NE 1012 C CZ . ARG A 141 ? 0.5272 0.6200 0.4726 0.0168 -0.0623 0.0289 141 ARG A CZ 1013 N NH1 . ARG A 141 ? 0.5277 0.6232 0.4671 0.0189 -0.0653 0.0286 141 ARG A NH1 1014 N NH2 . ARG A 141 ? 0.5237 0.6033 0.4666 0.0166 -0.0580 0.0281 141 ARG A NH2 1015 N N . ARG A 142 ? 0.6602 0.7942 0.6231 -0.0128 -0.0857 0.0135 142 ARG A N 1016 C CA . ARG A 142 ? 0.7008 0.8512 0.6732 -0.0172 -0.0902 0.0135 142 ARG A CA 1017 C C . ARG A 142 ? 0.7002 0.8553 0.6657 -0.0210 -0.0976 0.0091 142 ARG A C 1018 O O . ARG A 142 ? 0.6905 0.8605 0.6589 -0.0192 -0.1024 0.0113 142 ARG A O 1019 C CB . ARG A 142 ? 0.7344 0.9004 0.7176 -0.0112 -0.0894 0.0205 142 ARG A CB 1020 C CG . ARG A 142 ? 0.7820 0.9436 0.7720 -0.0075 -0.0817 0.0248 142 ARG A CG 1021 C CD . ARG A 142 ? 0.8303 1.0060 0.8297 -0.0003 -0.0804 0.0320 142 ARG A CD 1022 N NE . ARG A 142 ? 0.8769 1.0464 0.8696 0.0078 -0.0775 0.0359 142 ARG A NE 1023 C CZ . ARG A 142 ? 0.8932 1.0508 0.8842 0.0119 -0.0703 0.0384 142 ARG A CZ 1024 N NH1 . ARG A 142 ? 0.8678 1.0180 0.8624 0.0091 -0.0653 0.0375 142 ARG A NH1 1025 N NH2 . ARG A 142 ? 0.9015 1.0543 0.8865 0.0188 -0.0681 0.0417 142 ARG A NH2 1026 N N . SER A 143 ? 0.7140 0.8554 0.6695 -0.0257 -0.0982 0.0030 143 SER A N 1027 C CA . SER A 143 ? 0.7171 0.8591 0.6639 -0.0302 -0.1044 -0.0023 143 SER A CA 1028 C C . SER A 143 ? 0.7034 0.8493 0.6418 -0.0248 -0.1078 -0.0008 143 SER A C 1029 O O . SER A 143 ? 0.7554 0.9027 0.6859 -0.0284 -0.1131 -0.0050 143 SER A O 1030 C CB . SER A 143 ? 0.7393 0.8943 0.6940 -0.0380 -0.1095 -0.0047 143 SER A CB 1031 O OG . SER A 143 ? 0.7757 0.9218 0.7327 -0.0448 -0.1068 -0.0085 143 SER A OG 1032 N N . ASN A 144 ? 0.6517 0.7981 0.5906 -0.0165 -0.1043 0.0048 144 ASN A N 1033 C CA . ASN A 144 ? 0.6199 0.7689 0.5505 -0.0108 -0.1063 0.0070 144 ASN A CA 1034 C C . ASN A 144 ? 0.5979 0.7309 0.5193 -0.0061 -0.1010 0.0069 144 ASN A C 1035 O O . ASN A 144 ? 0.5400 0.6641 0.4648 -0.0046 -0.0953 0.0082 144 ASN A O 1036 C CB . ASN A 144 ? 0.6434 0.8074 0.5825 -0.0044 -0.1068 0.0144 144 ASN A CB 1037 C CG . ASN A 144 ? 0.6794 0.8621 0.6250 -0.0078 -0.1141 0.0146 144 ASN A CG 1038 O OD1 . ASN A 144 ? 0.6912 0.8757 0.6366 -0.0158 -0.1185 0.0090 144 ASN A OD1 1039 N ND2 . ASN A 144 ? 0.7000 0.8966 0.6515 -0.0016 -0.1156 0.0211 144 ASN A ND2 1040 N N . ASN A 145 ? 0.5543 0.6840 0.4642 -0.0041 -0.1029 0.0054 145 ASN A N 1041 C CA . ASN A 145 ? 0.5388 0.6553 0.4407 0.0008 -0.0979 0.0059 145 ASN A CA 1042 C C . ASN A 145 ? 0.5112 0.6294 0.4194 0.0079 -0.0928 0.0128 145 ASN A C 1043 O O . ASN A 145 ? 0.4976 0.6278 0.4104 0.0117 -0.0942 0.0180 145 ASN A O 1044 C CB . ASN A 145 ? 0.5350 0.6505 0.4242 0.0028 -0.1005 0.0044 145 ASN A CB 1045 C CG . ASN A 145 ? 0.5429 0.6520 0.4232 -0.0037 -0.1039 -0.0031 145 ASN A CG 1046 O OD1 . ASN A 145 ? 0.5373 0.6431 0.4211 -0.0099 -0.1047 -0.0072 145 ASN A OD1 1047 N ND2 . ASN A 145 ? 0.5411 0.6474 0.4090 -0.0022 -0.1056 -0.0049 145 ASN A ND2 1048 N N . SER A 146 ? 0.5131 0.6189 0.4211 0.0096 -0.0870 0.0129 146 SER A N 1049 C CA . SER A 146 ? 0.4827 0.5878 0.3964 0.0152 -0.0816 0.0188 146 SER A CA 1050 C C . SER A 146 ? 0.4706 0.5613 0.3792 0.0176 -0.0764 0.0180 146 SER A C 1051 O O . SER A 146 ? 0.4575 0.5414 0.3577 0.0169 -0.0769 0.0144 146 SER A O 1052 C CB . SER A 146 ? 0.4956 0.6041 0.4204 0.0129 -0.0801 0.0202 146 SER A CB 1053 O OG . SER A 146 ? 0.4756 0.5876 0.4065 0.0188 -0.0760 0.0266 146 SER A OG 1054 N N . PHE A 147 ? 0.4313 0.5178 0.3454 0.0202 -0.0713 0.0214 147 PHE A N 1055 C CA . PHE A 147 ? 0.4266 0.5011 0.3374 0.0227 -0.0664 0.0214 147 PHE A CA 1056 C C . PHE A 147 ? 0.3957 0.4658 0.3132 0.0234 -0.0619 0.0240 147 PHE A C 1057 O O . PHE A 147 ? 0.3866 0.4635 0.3110 0.0233 -0.0618 0.0266 147 PHE A O 1058 C CB . PHE A 147 ? 0.4299 0.5057 0.3359 0.0285 -0.0644 0.0251 147 PHE A CB 1059 C CG . PHE A 147 ? 0.4430 0.5076 0.3442 0.0301 -0.0604 0.0238 147 PHE A CG 1060 C CD1 . PHE A 147 ? 0.4502 0.5084 0.3458 0.0272 -0.0618 0.0185 147 PHE A CD1 1061 C CD2 . PHE A 147 ? 0.4461 0.5066 0.3488 0.0344 -0.0550 0.0280 147 PHE A CD2 1062 C CE1 . PHE A 147 ? 0.4527 0.5019 0.3453 0.0288 -0.0580 0.0175 147 PHE A CE1 1063 C CE2 . PHE A 147 ? 0.4541 0.5053 0.3536 0.0354 -0.0513 0.0268 147 PHE A CE2 1064 C CZ . PHE A 147 ? 0.4541 0.5003 0.3491 0.0327 -0.0529 0.0216 147 PHE A CZ 1065 N N . PHE A 148 ? 0.3871 0.4462 0.3028 0.0242 -0.0581 0.0232 148 PHE A N 1066 C CA . PHE A 148 ? 0.3795 0.4330 0.2997 0.0251 -0.0536 0.0256 148 PHE A CA 1067 C C . PHE A 148 ? 0.3789 0.4395 0.3035 0.0296 -0.0510 0.0316 148 PHE A C 1068 O O . PHE A 148 ? 0.3754 0.4399 0.2977 0.0341 -0.0501 0.0349 148 PHE A O 1069 C CB . PHE A 148 ? 0.3916 0.4345 0.3087 0.0265 -0.0501 0.0250 148 PHE A CB 1070 C CG . PHE A 148 ? 0.3964 0.4317 0.3102 0.0228 -0.0521 0.0196 148 PHE A CG 1071 C CD1 . PHE A 148 ? 0.4127 0.4423 0.3282 0.0188 -0.0528 0.0169 148 PHE A CD1 1072 C CD2 . PHE A 148 ? 0.4294 0.4631 0.3382 0.0237 -0.0528 0.0174 148 PHE A CD2 1073 C CE1 . PHE A 148 ? 0.4251 0.4472 0.3375 0.0160 -0.0546 0.0124 148 PHE A CE1 1074 C CE2 . PHE A 148 ? 0.4323 0.4589 0.3385 0.0209 -0.0543 0.0127 148 PHE A CE2 1075 C CZ . PHE A 148 ? 0.4334 0.4543 0.3415 0.0172 -0.0553 0.0103 148 PHE A CZ 1076 N N . SER A 149 ? 0.3720 0.4341 0.3027 0.0287 -0.0494 0.0332 149 SER A N 1077 C CA . SER A 149 ? 0.3881 0.4574 0.3238 0.0333 -0.0466 0.0391 149 SER A CA 1078 C C . SER A 149 ? 0.3918 0.4551 0.3253 0.0386 -0.0412 0.0430 149 SER A C 1079 O O . SER A 149 ? 0.3667 0.4364 0.3015 0.0438 -0.0397 0.0481 149 SER A O 1080 C CB . SER A 149 ? 0.4008 0.4707 0.3432 0.0313 -0.0447 0.0397 149 SER A CB 1081 O OG . SER A 149 ? 0.3914 0.4484 0.3323 0.0303 -0.0402 0.0389 149 SER A OG 1082 N N . ARG A 150 ? 0.3615 0.4126 0.2916 0.0373 -0.0383 0.0409 150 ARG A N 1083 C CA . ARG A 150 ? 0.3605 0.4048 0.2890 0.0413 -0.0327 0.0443 150 ARG A CA 1084 C C . ARG A 150 ? 0.3612 0.4037 0.2843 0.0436 -0.0324 0.0445 150 ARG A C 1085 O O . ARG A 150 ? 0.3523 0.3889 0.2738 0.0466 -0.0275 0.0472 150 ARG A O 1086 C CB . ARG A 150 ? 0.3558 0.3879 0.2842 0.0387 -0.0292 0.0425 150 ARG A CB 1087 C CG . ARG A 150 ? 0.3552 0.3874 0.2877 0.0363 -0.0287 0.0423 150 ARG A CG 1088 C CD . ARG A 150 ? 0.3603 0.4003 0.2977 0.0407 -0.0259 0.0477 150 ARG A CD 1089 N NE . ARG A 150 ? 0.3493 0.3864 0.2902 0.0392 -0.0231 0.0480 150 ARG A NE 1090 C CZ . ARG A 150 ? 0.3417 0.3849 0.2879 0.0426 -0.0201 0.0523 150 ARG A CZ 1091 N NH1 . ARG A 150 ? 0.3377 0.3911 0.2867 0.0478 -0.0203 0.0569 150 ARG A NH1 1092 N NH2 . ARG A 150 ? 0.3335 0.3725 0.2822 0.0410 -0.0168 0.0523 150 ARG A NH2 1093 N N . LEU A 151 ? 0.3643 0.4113 0.2842 0.0420 -0.0371 0.0415 151 LEU A N 1094 C CA . LEU A 151 ? 0.3664 0.4117 0.2808 0.0439 -0.0366 0.0412 151 LEU A CA 1095 C C . LEU A 151 ? 0.3891 0.4447 0.3004 0.0469 -0.0398 0.0435 151 LEU A C 1096 O O . LEU A 151 ? 0.4064 0.4712 0.3201 0.0459 -0.0441 0.0435 151 LEU A O 1097 C CB . LEU A 151 ? 0.3730 0.4122 0.2848 0.0397 -0.0388 0.0354 151 LEU A CB 1098 C CG . LEU A 151 ? 0.3720 0.4009 0.2863 0.0372 -0.0360 0.0335 151 LEU A CG 1099 C CD1 . LEU A 151 ? 0.3635 0.3878 0.2762 0.0332 -0.0389 0.0279 151 LEU A CD1 1100 C CD2 . LEU A 151 ? 0.3755 0.3984 0.2893 0.0401 -0.0303 0.0364 151 LEU A CD2 1101 N N . ASN A 152 ? 0.4025 0.4565 0.3083 0.0505 -0.0375 0.0456 152 ASN A N 1102 C CA . ASN A 152 ? 0.4054 0.4678 0.3064 0.0544 -0.0398 0.0486 152 ASN A CA 1103 C C . ASN A 152 ? 0.4159 0.4753 0.3090 0.0540 -0.0405 0.0457 152 ASN A C 1104 O O . ASN A 152 ? 0.4269 0.4791 0.3167 0.0560 -0.0356 0.0468 152 ASN A O 1105 C CB . ASN A 152 ? 0.4027 0.4658 0.3039 0.0607 -0.0350 0.0557 152 ASN A CB 1106 C CG . ASN A 152 ? 0.4209 0.4942 0.3180 0.0651 -0.0382 0.0597 152 ASN A CG 1107 O OD1 . ASN A 152 ? 0.4190 0.4982 0.3117 0.0632 -0.0439 0.0569 152 ASN A OD1 1108 N ND2 . ASN A 152 ? 0.4084 0.4831 0.3060 0.0711 -0.0345 0.0664 152 ASN A ND2 1109 N N . TRP A 153 ? 0.4270 0.4913 0.3167 0.0510 -0.0463 0.0418 153 TRP A N 1110 C CA . TRP A 153 ? 0.4412 0.5023 0.3225 0.0504 -0.0470 0.0385 153 TRP A CA 1111 C C . TRP A 153 ? 0.4552 0.5210 0.3287 0.0554 -0.0471 0.0426 153 TRP A C 1112 O O . TRP A 153 ? 0.4564 0.5315 0.3276 0.0557 -0.0525 0.0434 153 TRP A O 1113 C CB . TRP A 153 ? 0.4539 0.5174 0.3338 0.0452 -0.0530 0.0325 153 TRP A CB 1114 C CG . TRP A 153 ? 0.4586 0.5162 0.3305 0.0438 -0.0530 0.0279 153 TRP A CG 1115 C CD1 . TRP A 153 ? 0.4654 0.5174 0.3311 0.0470 -0.0484 0.0289 153 TRP A CD1 1116 C CD2 . TRP A 153 ? 0.4710 0.5271 0.3396 0.0389 -0.0573 0.0215 153 TRP A CD2 1117 N NE1 . TRP A 153 ? 0.4744 0.5218 0.3338 0.0447 -0.0494 0.0236 153 TRP A NE1 1118 C CE2 . TRP A 153 ? 0.4793 0.5285 0.3398 0.0400 -0.0547 0.0190 153 TRP A CE2 1119 C CE3 . TRP A 153 ? 0.4860 0.5450 0.3576 0.0339 -0.0622 0.0178 153 TRP A CE3 1120 C CZ2 . TRP A 153 ? 0.5047 0.5498 0.3600 0.0364 -0.0570 0.0130 153 TRP A CZ2 1121 C CZ3 . TRP A 153 ? 0.5053 0.5597 0.3712 0.0300 -0.0648 0.0116 153 TRP A CZ3 1122 C CH2 . TRP A 153 ? 0.5180 0.5654 0.3759 0.0314 -0.0622 0.0093 153 TRP A CH2 1123 N N . LEU A 154 ? 0.4505 0.5099 0.3199 0.0590 -0.0412 0.0453 154 LEU A N 1124 C CA . LEU A 154 ? 0.4700 0.5318 0.3307 0.0643 -0.0402 0.0498 154 LEU A CA 1125 C C . LEU A 154 ? 0.4797 0.5393 0.3298 0.0632 -0.0417 0.0458 154 LEU A C 1126 O O . LEU A 154 ? 0.4653 0.5172 0.3150 0.0605 -0.0392 0.0414 154 LEU A O 1127 C CB . LEU A 154 ? 0.4742 0.5289 0.3351 0.0686 -0.0322 0.0548 154 LEU A CB 1128 C CG . LEU A 154 ? 0.4804 0.5337 0.3510 0.0693 -0.0289 0.0581 154 LEU A CG 1129 C CD1 . LEU A 154 ? 0.4951 0.5393 0.3647 0.0725 -0.0206 0.0618 154 LEU A CD1 1130 C CD2 . LEU A 154 ? 0.4735 0.5366 0.3470 0.0724 -0.0323 0.0626 154 LEU A CD2 1131 N N . THR A 155 ? 0.4889 0.5549 0.3303 0.0654 -0.0458 0.0475 155 THR A N 1132 C CA . THR A 155 ? 0.5053 0.5687 0.3346 0.0647 -0.0472 0.0439 155 THR A CA 1133 C C . THR A 155 ? 0.5158 0.5810 0.3341 0.0705 -0.0461 0.0494 155 THR A C 1134 O O . THR A 155 ? 0.5084 0.5772 0.3293 0.0751 -0.0448 0.0559 155 THR A O 1135 C CB . THR A 155 ? 0.5150 0.5840 0.3420 0.0595 -0.0553 0.0382 155 THR A CB 1136 O OG1 . THR A 155 ? 0.5117 0.5926 0.3402 0.0605 -0.0616 0.0414 155 THR A OG1 1137 C CG2 . THR A 155 ? 0.5073 0.5729 0.3436 0.0538 -0.0560 0.0327 155 THR A CG2 1138 N N . HIS A 156 ? 0.5447 0.6064 0.3501 0.0707 -0.0464 0.0470 156 HIS A N 1139 C CA . HIS A 156 ? 0.5775 0.6390 0.3709 0.0764 -0.0445 0.0522 156 HIS A CA 1140 C C . HIS A 156 ? 0.5900 0.6632 0.3815 0.0789 -0.0517 0.0564 156 HIS A C 1141 O O . HIS A 156 ? 0.5897 0.6717 0.3871 0.0751 -0.0590 0.0537 156 HIS A O 1142 C CB . HIS A 156 ? 0.5946 0.6496 0.3735 0.0757 -0.0436 0.0482 156 HIS A CB 1143 C CG . HIS A 156 ? 0.6139 0.6746 0.3850 0.0720 -0.0523 0.0432 156 HIS A CG 1144 N ND1 . HIS A 156 ? 0.6406 0.7105 0.4047 0.0739 -0.0592 0.0462 156 HIS A ND1 1145 C CD2 . HIS A 156 ? 0.6257 0.6833 0.3943 0.0663 -0.0551 0.0353 156 HIS A CD2 1146 C CE1 . HIS A 156 ? 0.6506 0.7234 0.4083 0.0690 -0.0663 0.0401 156 HIS A CE1 1147 N NE2 . HIS A 156 ? 0.6463 0.7108 0.4064 0.0644 -0.0634 0.0334 156 HIS A NE2 1148 N N . LEU A 157 ? 0.6332 0.7068 0.4171 0.0853 -0.0493 0.0633 157 LEU A N 1149 C CA . LEU A 157 ? 0.6389 0.7238 0.4190 0.0891 -0.0562 0.0683 157 LEU A CA 1150 C C . LEU A 157 ? 0.6691 0.7514 0.4303 0.0924 -0.0568 0.0697 157 LEU A C 1151 O O . LEU A 157 ? 0.6733 0.7464 0.4271 0.0968 -0.0491 0.0735 157 LEU A O 1152 C CB . LEU A 157 ? 0.6359 0.7234 0.4240 0.0951 -0.0525 0.0766 157 LEU A CB 1153 C CG . LEU A 157 ? 0.6409 0.7405 0.4264 0.1004 -0.0587 0.0832 157 LEU A CG 1154 C CD1 . LEU A 157 ? 0.6299 0.7435 0.4254 0.0961 -0.0682 0.0803 157 LEU A CD1 1155 C CD2 . LEU A 157 ? 0.6290 0.7268 0.4191 0.1076 -0.0525 0.0919 157 LEU A CD2 1156 N N . LYS A 158 ? 0.6993 0.7888 0.4522 0.0898 -0.0657 0.0665 158 LYS A N 1157 C CA . LYS A 158 ? 0.7414 0.8280 0.4744 0.0922 -0.0673 0.0669 158 LYS A CA 1158 C C . LYS A 158 ? 0.7434 0.8151 0.4670 0.0912 -0.0590 0.0630 158 LYS A C 1159 O O . LYS A 158 ? 0.7479 0.8128 0.4570 0.0957 -0.0546 0.0663 158 LYS A O 1160 C CB . LYS A 158 ? 0.7830 0.8726 0.5092 0.1007 -0.0664 0.0765 158 LYS A CB 1161 C CG . LYS A 158 ? 0.8120 0.9164 0.5489 0.1034 -0.0732 0.0819 158 LYS A CG 1162 C CD . LYS A 158 ? 0.8520 0.9696 0.5860 0.0995 -0.0856 0.0784 158 LYS A CD 1163 C CE . LYS A 158 ? 0.8627 0.9963 0.6065 0.1034 -0.0922 0.0849 158 LYS A CE 1164 N NZ . LYS A 158 ? 0.9037 1.0372 0.6391 0.1130 -0.0898 0.0947 158 LYS A NZ 1165 N N . PHE A 159 ? 0.7082 0.7748 0.4402 0.0855 -0.0566 0.0562 159 PHE A N 1166 C CA . PHE A 159 ? 0.7139 0.7673 0.4406 0.0843 -0.0484 0.0521 159 PHE A CA 1167 C C . PHE A 159 ? 0.6952 0.7401 0.4235 0.0892 -0.0376 0.0576 159 PHE A C 1168 O O . PHE A 159 ? 0.6776 0.7124 0.3977 0.0900 -0.0305 0.0562 159 PHE A O 1169 C CB . PHE A 159 ? 0.7590 0.8081 0.4661 0.0834 -0.0507 0.0481 159 PHE A CB 1170 C CG . PHE A 159 ? 0.7884 0.8452 0.4930 0.0779 -0.0613 0.0424 159 PHE A CG 1171 C CD1 . PHE A 159 ? 0.7841 0.8385 0.4957 0.0714 -0.0627 0.0345 159 PHE A CD1 1172 C CD2 . PHE A 159 ? 0.8109 0.8774 0.5066 0.0793 -0.0701 0.0450 159 PHE A CD2 1173 C CE1 . PHE A 159 ? 0.8064 0.8672 0.5159 0.0658 -0.0721 0.0291 159 PHE A CE1 1174 C CE2 . PHE A 159 ? 0.8292 0.9032 0.5234 0.0735 -0.0801 0.0394 159 PHE A CE2 1175 C CZ . PHE A 159 ? 0.8298 0.9005 0.5308 0.0665 -0.0808 0.0314 159 PHE A CZ 1176 N N . LYS A 160 ? 0.6927 0.7414 0.4321 0.0923 -0.0359 0.0637 160 LYS A N 1177 C CA . LYS A 160 ? 0.6982 0.7385 0.4428 0.0953 -0.0256 0.0678 160 LYS A CA 1178 C C . LYS A 160 ? 0.6634 0.7054 0.4273 0.0923 -0.0245 0.0669 160 LYS A C 1179 O O . LYS A 160 ? 0.6170 0.6681 0.3894 0.0909 -0.0311 0.0669 160 LYS A O 1180 C CB . LYS A 160 ? 0.7547 0.7948 0.4922 0.1026 -0.0227 0.0769 160 LYS A CB 1181 C CG . LYS A 160 ? 0.8131 0.8469 0.5307 0.1063 -0.0198 0.0788 160 LYS A CG 1182 C CD . LYS A 160 ? 0.8503 0.8775 0.5634 0.1130 -0.0113 0.0873 160 LYS A CD 1183 C CE . LYS A 160 ? 0.8941 0.9175 0.5858 0.1178 -0.0108 0.0909 160 LYS A CE 1184 N NZ . LYS A 160 ? 0.9263 0.9417 0.6069 0.1148 -0.0076 0.0848 160 LYS A NZ 1185 N N . TYR A 161 ? 0.6556 0.6889 0.4259 0.0912 -0.0162 0.0658 161 TYR A N 1186 C CA . TYR A 161 ? 0.6332 0.6661 0.4199 0.0890 -0.0139 0.0657 161 TYR A CA 1187 C C . TYR A 161 ? 0.6462 0.6701 0.4336 0.0921 -0.0036 0.0703 161 TYR A C 1188 O O . TYR A 161 ? 0.6464 0.6629 0.4347 0.0903 0.0025 0.0675 161 TYR A O 1189 C CB . TYR A 161 ? 0.6234 0.6549 0.4181 0.0826 -0.0155 0.0578 161 TYR A CB 1190 C CG . TYR A 161 ? 0.5916 0.6239 0.4023 0.0795 -0.0154 0.0568 161 TYR A CG 1191 C CD1 . TYR A 161 ? 0.5914 0.6175 0.4096 0.0805 -0.0079 0.0596 161 TYR A CD1 1192 C CD2 . TYR A 161 ? 0.5906 0.6291 0.4083 0.0753 -0.0226 0.0527 161 TYR A CD2 1193 C CE1 . TYR A 161 ? 0.5564 0.5826 0.3879 0.0774 -0.0080 0.0584 161 TYR A CE1 1194 C CE2 . TYR A 161 ? 0.5545 0.5929 0.3855 0.0726 -0.0223 0.0518 161 TYR A CE2 1195 C CZ . TYR A 161 ? 0.5617 0.5938 0.3991 0.0737 -0.0152 0.0546 161 TYR A CZ 1196 O OH . TYR A 161 ? 0.5249 0.5562 0.3742 0.0707 -0.0150 0.0535 161 TYR A OH 1197 N N . PRO A 162 ? 0.6710 0.6956 0.4578 0.0972 -0.0015 0.0777 162 PRO A N 1198 C CA . PRO A 162 ? 0.6931 0.7083 0.4796 0.1001 0.0085 0.0824 162 PRO A CA 1199 C C . PRO A 162 ? 0.6857 0.6967 0.4871 0.0960 0.0128 0.0801 162 PRO A C 1200 O O . PRO A 162 ? 0.6911 0.7073 0.5027 0.0930 0.0078 0.0776 162 PRO A O 1201 C CB . PRO A 162 ? 0.7193 0.7369 0.5012 0.1066 0.0084 0.0908 162 PRO A CB 1202 C CG . PRO A 162 ? 0.7281 0.7574 0.5154 0.1061 -0.0012 0.0901 162 PRO A CG 1203 C CD . PRO A 162 ? 0.7125 0.7465 0.4994 0.1004 -0.0081 0.0822 162 PRO A CD 1204 N N . ALA A 163 ? 0.6817 0.6836 0.4842 0.0958 0.0219 0.0808 163 ALA A N 1205 C CA . ALA A 163 ? 0.6724 0.6701 0.4885 0.0916 0.0261 0.0786 163 ALA A CA 1206 C C . ALA A 163 ? 0.6595 0.6589 0.4830 0.0927 0.0247 0.0821 163 ALA A C 1207 O O . ALA A 163 ? 0.6740 0.6725 0.4923 0.0979 0.0268 0.0887 163 ALA A O 1208 C CB . ALA A 163 ? 0.6907 0.6787 0.5060 0.0920 0.0365 0.0805 163 ALA A CB 1209 N N . LEU A 164 ? 0.6073 0.6092 0.4423 0.0880 0.0212 0.0778 164 LEU A N 1210 C CA . LEU A 164 ? 0.6063 0.6088 0.4485 0.0886 0.0206 0.0806 164 LEU A CA 1211 C C . LEU A 164 ? 0.5846 0.5777 0.4335 0.0866 0.0286 0.0813 164 LEU A C 1212 O O . LEU A 164 ? 0.5717 0.5610 0.4252 0.0822 0.0312 0.0769 164 LEU A O 1213 C CB . LEU A 164 ? 0.5933 0.6029 0.4434 0.0845 0.0127 0.0758 164 LEU A CB 1214 C CG . LEU A 164 ? 0.6136 0.6332 0.4585 0.0856 0.0042 0.0747 164 LEU A CG 1215 C CD1 . LEU A 164 ? 0.6117 0.6367 0.4653 0.0806 -0.0023 0.0695 164 LEU A CD1 1216 C CD2 . LEU A 164 ? 0.6164 0.6410 0.4559 0.0918 0.0028 0.0816 164 LEU A CD2 1217 N N . ASN A 165 ? 0.5739 0.5632 0.4232 0.0899 0.0325 0.0868 165 ASN A N 1218 C CA . ASN A 165 ? 0.5948 0.5745 0.4498 0.0878 0.0398 0.0876 165 ASN A CA 1219 C C . ASN A 165 ? 0.6020 0.5814 0.4602 0.0903 0.0396 0.0913 165 ASN A C 1220 O O . ASN A 165 ? 0.6254 0.6005 0.4787 0.0956 0.0444 0.0978 165 ASN A O 1221 C CB . ASN A 165 ? 0.6366 0.6079 0.4851 0.0903 0.0487 0.0916 165 ASN A CB 1222 C CG . ASN A 165 ? 0.6678 0.6287 0.5222 0.0875 0.0566 0.0922 165 ASN A CG 1223 O OD1 . ASN A 165 ? 0.6810 0.6404 0.5445 0.0813 0.0563 0.0869 165 ASN A OD1 1224 N ND2 . ASN A 165 ? 0.6858 0.6391 0.5346 0.0920 0.0636 0.0987 165 ASN A ND2 1225 N N . VAL A 166 ? 0.5760 0.5597 0.4420 0.0866 0.0341 0.0873 166 VAL A N 1226 C CA . VAL A 166 ? 0.5549 0.5410 0.4238 0.0891 0.0322 0.0902 166 VAL A CA 1227 C C . VAL A 166 ? 0.5504 0.5282 0.4264 0.0852 0.0361 0.0884 166 VAL A C 1228 O O . VAL A 166 ? 0.5208 0.4963 0.4022 0.0789 0.0351 0.0827 166 VAL A O 1229 C CB . VAL A 166 ? 0.5549 0.5531 0.4262 0.0882 0.0227 0.0873 166 VAL A CB 1230 C CG1 . VAL A 166 ? 0.5611 0.5625 0.4369 0.0906 0.0213 0.0902 166 VAL A CG1 1231 C CG2 . VAL A 166 ? 0.5704 0.5765 0.4335 0.0920 0.0186 0.0891 166 VAL A CG2 1232 N N . THR A 167 ? 0.5468 0.5203 0.4225 0.0892 0.0402 0.0935 167 THR A N 1233 C CA . THR A 167 ? 0.5861 0.5499 0.4664 0.0862 0.0449 0.0926 167 THR A CA 1234 C C . THR A 167 ? 0.5648 0.5320 0.4494 0.0872 0.0420 0.0931 167 THR A C 1235 O O . THR A 167 ? 0.5570 0.5323 0.4406 0.0927 0.0392 0.0972 167 THR A O 1236 C CB . THR A 167 ? 0.6293 0.5814 0.5048 0.0897 0.0546 0.0982 167 THR A CB 1237 O OG1 . THR A 167 ? 0.7138 0.6548 0.5932 0.0845 0.0595 0.0954 167 THR A OG1 1238 C CG2 . THR A 167 ? 0.6471 0.6003 0.5191 0.0978 0.0565 0.1055 167 THR A CG2 1239 N N . MET A 168 ? 0.5378 0.4987 0.4273 0.0819 0.0429 0.0891 168 MET A N 1240 C CA . MET A 168 ? 0.5296 0.4904 0.4223 0.0829 0.0424 0.0899 168 MET A CA 1241 C C . MET A 168 ? 0.5363 0.4833 0.4300 0.0791 0.0485 0.0883 168 MET A C 1242 O O . MET A 168 ? 0.5322 0.4761 0.4289 0.0722 0.0464 0.0823 168 MET A O 1243 C CB . MET A 168 ? 0.5141 0.4853 0.4117 0.0795 0.0339 0.0852 168 MET A CB 1244 C CG . MET A 168 ? 0.5029 0.4766 0.4041 0.0812 0.0332 0.0866 168 MET A CG 1245 S SD . MET A 168 ? 0.5315 0.5132 0.4317 0.0911 0.0344 0.0951 168 MET A SD 1246 C CE . MET A 168 ? 0.5043 0.5020 0.4038 0.0916 0.0252 0.0940 168 MET A CE 1247 N N . PRO A 169 ? 0.5560 0.4942 0.4466 0.0837 0.0560 0.0936 169 PRO A N 1248 C CA . PRO A 169 ? 0.5635 0.4871 0.4537 0.0800 0.0623 0.0920 169 PRO A CA 1249 C C . PRO A 169 ? 0.5421 0.4652 0.4356 0.0774 0.0600 0.0889 169 PRO A C 1250 O O . PRO A 169 ? 0.5330 0.4650 0.4287 0.0813 0.0567 0.0910 169 PRO A O 1251 C CB . PRO A 169 ? 0.5978 0.5131 0.4831 0.0869 0.0709 0.0992 169 PRO A CB 1252 C CG . PRO A 169 ? 0.6013 0.5290 0.4867 0.0948 0.0675 0.1045 169 PRO A CG 1253 C CD . PRO A 169 ? 0.5801 0.5211 0.4672 0.0926 0.0590 0.1014 169 PRO A CD 1254 N N . ASN A 170 ? 0.5426 0.4556 0.4364 0.0706 0.0615 0.0840 170 ASN A N 1255 C CA . ASN A 170 ? 0.5407 0.4492 0.4354 0.0684 0.0613 0.0817 170 ASN A CA 1256 C C . ASN A 170 ? 0.5683 0.4623 0.4585 0.0710 0.0708 0.0852 170 ASN A C 1257 O O . ASN A 170 ? 0.5583 0.4392 0.4455 0.0665 0.0755 0.0830 170 ASN A O 1258 C CB . ASN A 170 ? 0.5308 0.4362 0.4272 0.0595 0.0569 0.0742 170 ASN A CB 1259 C CG . ASN A 170 ? 0.5389 0.4393 0.4348 0.0573 0.0566 0.0718 170 ASN A CG 1260 O OD1 . ASN A 170 ? 0.5408 0.4383 0.4351 0.0622 0.0611 0.0757 170 ASN A OD1 1261 N ND2 . ASN A 170 ? 0.5381 0.4369 0.4349 0.0502 0.0517 0.0656 170 ASN A ND2 1262 N N . ASN A 171 ? 0.5917 0.4884 0.4819 0.0784 0.0734 0.0906 171 ASN A N 1263 C CA . ASN A 171 ? 0.6299 0.5133 0.5159 0.0823 0.0827 0.0946 171 ASN A CA 1264 C C . ASN A 171 ? 0.6428 0.5222 0.5294 0.0810 0.0835 0.0924 171 ASN A C 1265 O O . ASN A 171 ? 0.6673 0.5384 0.5514 0.0859 0.0907 0.0963 171 ASN A O 1266 C CB . ASN A 171 ? 0.6358 0.5245 0.5214 0.0925 0.0861 0.1029 171 ASN A CB 1267 C CG . ASN A 171 ? 0.6503 0.5394 0.5330 0.0942 0.0872 0.1056 171 ASN A CG 1268 O OD1 . ASN A 171 ? 0.6705 0.5488 0.5500 0.0893 0.0909 0.1031 171 ASN A OD1 1269 N ND2 . ASN A 171 ? 0.6749 0.5768 0.5587 0.1010 0.0841 0.1106 171 ASN A ND2 1270 N N . GLU A 172 ? 0.6196 0.5042 0.5090 0.0747 0.0764 0.0864 172 GLU A N 1271 C CA . GLU A 172 ? 0.6374 0.5178 0.5265 0.0726 0.0767 0.0838 172 GLU A CA 1272 C C . GLU A 172 ? 0.6514 0.5149 0.5346 0.0651 0.0797 0.0786 172 GLU A C 1273 O O . GLU A 172 ? 0.6316 0.4896 0.5130 0.0610 0.0802 0.0765 172 GLU A O 1274 C CB . GLU A 172 ? 0.6346 0.5287 0.5290 0.0696 0.0674 0.0801 172 GLU A CB 1275 C CG . GLU A 172 ? 0.6519 0.5640 0.5522 0.0752 0.0626 0.0840 172 GLU A CG 1276 C CD . GLU A 172 ? 0.6811 0.5965 0.5836 0.0836 0.0675 0.0906 172 GLU A CD 1277 O OE1 . GLU A 172 ? 0.7331 0.6406 0.6344 0.0842 0.0724 0.0907 172 GLU A OE1 1278 O OE2 . GLU A 172 ? 0.7433 0.6692 0.6485 0.0899 0.0665 0.0958 172 GLU A OE2 1279 N N . LYS A 173 ? 0.6590 0.5149 0.5395 0.0632 0.0817 0.0763 173 LYS A N 1280 C CA . LYS A 173 ? 0.6993 0.5394 0.5733 0.0555 0.0835 0.0708 173 LYS A CA 1281 C C . LYS A 173 ? 0.6689 0.5137 0.5442 0.0479 0.0745 0.0642 173 LYS A C 1282 O O . LYS A 173 ? 0.6790 0.5122 0.5490 0.0412 0.0745 0.0592 173 LYS A O 1283 C CB . LYS A 173 ? 0.7486 0.5751 0.6167 0.0578 0.0916 0.0720 173 LYS A CB 1284 C CG . LYS A 173 ? 0.8164 0.6326 0.6810 0.0639 0.1017 0.0776 173 LYS A CG 1285 C CD . LYS A 173 ? 0.8734 0.6751 0.7318 0.0664 0.1105 0.0787 173 LYS A CD 1286 C CE . LYS A 173 ? 0.9042 0.6964 0.7597 0.0737 0.1207 0.0850 173 LYS A CE 1287 N NZ . LYS A 173 ? 0.9599 0.7362 0.8087 0.0764 0.1303 0.0860 173 LYS A NZ 1288 N N . PHE A 174 ? 0.6328 0.4942 0.5147 0.0489 0.0668 0.0641 174 PHE A N 1289 C CA . PHE A 174 ? 0.5970 0.4638 0.4806 0.0424 0.0581 0.0584 174 PHE A CA 1290 C C . PHE A 174 ? 0.5732 0.4522 0.4623 0.0414 0.0514 0.0574 174 PHE A C 1291 O O . PHE A 174 ? 0.5370 0.4233 0.4291 0.0464 0.0527 0.0616 174 PHE A O 1292 C CB . PHE A 174 ? 0.5938 0.4679 0.4795 0.0439 0.0551 0.0584 174 PHE A CB 1293 C CG . PHE A 174 ? 0.6002 0.4880 0.4921 0.0515 0.0553 0.0639 174 PHE A CG 1294 C CD1 . PHE A 174 ? 0.5891 0.4922 0.4869 0.0524 0.0485 0.0642 174 PHE A CD1 1295 C CD2 . PHE A 174 ? 0.6255 0.5111 0.5174 0.0577 0.0623 0.0687 174 PHE A CD2 1296 C CE1 . PHE A 174 ? 0.5950 0.5111 0.4982 0.0590 0.0481 0.0692 174 PHE A CE1 1297 C CE2 . PHE A 174 ? 0.6256 0.5251 0.5240 0.0647 0.0619 0.0741 174 PHE A CE2 1298 C CZ . PHE A 174 ? 0.6223 0.5371 0.5261 0.0651 0.0545 0.0742 174 PHE A CZ 1299 N N . ASP A 175 ? 0.5392 0.4203 0.4293 0.0351 0.0444 0.0521 175 ASP A N 1300 C CA . ASP A 175 ? 0.5332 0.4252 0.4284 0.0338 0.0381 0.0505 175 ASP A CA 1301 C C . ASP A 175 ? 0.4918 0.3988 0.3917 0.0376 0.0332 0.0522 175 ASP A C 1302 O O . ASP A 175 ? 0.4845 0.3940 0.3845 0.0387 0.0322 0.0525 175 ASP A O 1303 C CB . ASP A 175 ? 0.5555 0.4454 0.4508 0.0264 0.0319 0.0444 175 ASP A CB 1304 C CG . ASP A 175 ? 0.6045 0.4815 0.4963 0.0213 0.0351 0.0420 175 ASP A CG 1305 O OD1 . ASP A 175 ? 0.6226 0.4922 0.5120 0.0233 0.0424 0.0448 175 ASP A OD1 1306 O OD2 . ASP A 175 ? 0.6015 0.4761 0.4930 0.0153 0.0301 0.0371 175 ASP A OD2 1307 N N . LYS A 176 ? 0.4601 0.3766 0.3637 0.0391 0.0304 0.0530 176 LYS A N 1308 C CA . LYS A 176 ? 0.4306 0.3610 0.3379 0.0422 0.0253 0.0542 176 LYS A CA 1309 C C . LYS A 176 ? 0.4107 0.3468 0.3204 0.0379 0.0182 0.0496 176 LYS A C 1310 O O . LYS A 176 ? 0.4136 0.3477 0.3240 0.0357 0.0183 0.0480 176 LYS A O 1311 C CB . LYS A 176 ? 0.4356 0.3721 0.3436 0.0485 0.0283 0.0595 176 LYS A CB 1312 C CG . LYS A 176 ? 0.4550 0.3880 0.3614 0.0543 0.0352 0.0651 176 LYS A CG 1313 C CD . LYS A 176 ? 0.4657 0.4045 0.3721 0.0603 0.0373 0.0703 176 LYS A CD 1314 C CE . LYS A 176 ? 0.4798 0.4178 0.3853 0.0675 0.0432 0.0768 176 LYS A CE 1315 N NZ . LYS A 176 ? 0.4825 0.4286 0.3878 0.0736 0.0433 0.0818 176 LYS A NZ 1316 N N . LEU A 177 ? 0.3913 0.3343 0.3028 0.0368 0.0125 0.0475 177 LEU A N 1317 C CA . LEU A 177 ? 0.3758 0.3248 0.2895 0.0337 0.0058 0.0435 177 LEU A CA 1318 C C . LEU A 177 ? 0.3646 0.3257 0.2805 0.0373 0.0029 0.0453 177 LEU A C 1319 O O . LEU A 177 ? 0.3680 0.3358 0.2849 0.0393 0.0012 0.0467 177 LEU A O 1320 C CB . LEU A 177 ? 0.3743 0.3211 0.2874 0.0293 0.0011 0.0394 177 LEU A CB 1321 C CG . LEU A 177 ? 0.3646 0.3174 0.2797 0.0267 -0.0059 0.0356 177 LEU A CG 1322 C CD1 . LEU A 177 ? 0.3627 0.3136 0.2793 0.0243 -0.0071 0.0331 177 LEU A CD1 1323 C CD2 . LEU A 177 ? 0.3626 0.3119 0.2760 0.0231 -0.0095 0.0325 177 LEU A CD2 1324 N N . TYR A 178 ? 0.3691 0.3332 0.2857 0.0377 0.0023 0.0449 178 TYR A N 1325 C CA . TYR A 178 ? 0.3783 0.3529 0.2954 0.0408 -0.0005 0.0460 178 TYR A CA 1326 C C . TYR A 178 ? 0.3834 0.3620 0.3019 0.0374 -0.0066 0.0413 178 TYR A C 1327 O O . TYR A 178 ? 0.3853 0.3594 0.3048 0.0342 -0.0072 0.0382 178 TYR A O 1328 C CB . TYR A 178 ? 0.3800 0.3547 0.2956 0.0442 0.0038 0.0493 178 TYR A CB 1329 C CG . TYR A 178 ? 0.3842 0.3573 0.2980 0.0492 0.0094 0.0551 178 TYR A CG 1330 C CD1 . TYR A 178 ? 0.3931 0.3750 0.3065 0.0541 0.0083 0.0588 178 TYR A CD1 1331 C CD2 . TYR A 178 ? 0.3944 0.3569 0.3069 0.0491 0.0158 0.0567 178 TYR A CD2 1332 C CE1 . TYR A 178 ? 0.4002 0.3809 0.3122 0.0594 0.0135 0.0646 178 TYR A CE1 1333 C CE2 . TYR A 178 ? 0.4053 0.3652 0.3157 0.0541 0.0216 0.0622 178 TYR A CE2 1334 C CZ . TYR A 178 ? 0.4116 0.3809 0.3221 0.0597 0.0204 0.0663 178 TYR A CZ 1335 O OH . TYR A 178 ? 0.4322 0.3992 0.3410 0.0654 0.0260 0.0722 178 TYR A OH 1336 N N . ILE A 179 ? 0.3621 0.3488 0.2807 0.0381 -0.0110 0.0407 179 ILE A N 1337 C CA . ILE A 179 ? 0.3660 0.3564 0.2850 0.0356 -0.0166 0.0365 179 ILE A CA 1338 C C . ILE A 179 ? 0.3775 0.3759 0.2947 0.0387 -0.0177 0.0377 179 ILE A C 1339 O O . ILE A 179 ? 0.3643 0.3689 0.2805 0.0419 -0.0176 0.0410 179 ILE A O 1340 C CB . ILE A 179 ? 0.3693 0.3617 0.2889 0.0331 -0.0209 0.0343 179 ILE A CB 1341 C CG1 . ILE A 179 ? 0.3744 0.3586 0.2942 0.0305 -0.0193 0.0337 179 ILE A CG1 1342 C CG2 . ILE A 179 ? 0.3712 0.3654 0.2906 0.0303 -0.0262 0.0297 179 ILE A CG2 1343 C CD1 . ILE A 179 ? 0.3568 0.3327 0.2765 0.0271 -0.0196 0.0306 179 ILE A CD1 1344 N N . TRP A 180 ? 0.3701 0.3684 0.2866 0.0379 -0.0187 0.0352 180 TRP A N 1345 C CA . TRP A 180 ? 0.3876 0.3917 0.3009 0.0408 -0.0191 0.0361 180 TRP A CA 1346 C C . TRP A 180 ? 0.3949 0.3993 0.3080 0.0386 -0.0223 0.0315 180 TRP A C 1347 O O . TRP A 180 ? 0.3924 0.3925 0.3084 0.0351 -0.0241 0.0280 180 TRP A O 1348 C CB . TRP A 180 ? 0.3908 0.3930 0.3025 0.0443 -0.0133 0.0401 180 TRP A CB 1349 C CG . TRP A 180 ? 0.3948 0.3894 0.3093 0.0424 -0.0093 0.0392 180 TRP A CG 1350 C CD1 . TRP A 180 ? 0.4004 0.3881 0.3174 0.0408 -0.0060 0.0401 180 TRP A CD1 1351 C CD2 . TRP A 180 ? 0.3959 0.3892 0.3114 0.0414 -0.0080 0.0369 180 TRP A CD2 1352 N NE1 . TRP A 180 ? 0.4062 0.3890 0.3258 0.0386 -0.0034 0.0385 180 TRP A NE1 1353 C CE2 . TRP A 180 ? 0.4061 0.3925 0.3258 0.0390 -0.0043 0.0367 180 TRP A CE2 1354 C CE3 . TRP A 180 ? 0.4052 0.4021 0.3187 0.0422 -0.0094 0.0350 180 TRP A CE3 1355 C CZ2 . TRP A 180 ? 0.4129 0.3976 0.3360 0.0375 -0.0023 0.0348 180 TRP A CZ2 1356 C CZ3 . TRP A 180 ? 0.4156 0.4100 0.3320 0.0412 -0.0066 0.0333 180 TRP A CZ3 1357 C CH2 . TRP A 180 ? 0.4024 0.3915 0.3243 0.0388 -0.0033 0.0332 180 TRP A CH2 1358 N N . GLY A 181 ? 0.3988 0.4077 0.3079 0.0405 -0.0232 0.0313 181 GLY A N 1359 C CA . GLY A 181 ? 0.3954 0.4040 0.3036 0.0387 -0.0260 0.0267 181 GLY A CA 1360 C C . GLY A 181 ? 0.4081 0.4185 0.3117 0.0413 -0.0241 0.0269 181 GLY A C 1361 O O . GLY A 181 ? 0.3932 0.4058 0.2930 0.0447 -0.0213 0.0308 181 GLY A O 1362 N N . VAL A 182 ? 0.4119 0.4207 0.3153 0.0399 -0.0254 0.0228 182 VAL A N 1363 C CA . VAL A 182 ? 0.4296 0.4391 0.3281 0.0420 -0.0234 0.0221 182 VAL A CA 1364 C C . VAL A 182 ? 0.4217 0.4325 0.3158 0.0406 -0.0282 0.0178 182 VAL A C 1365 O O . VAL A 182 ? 0.4135 0.4219 0.3108 0.0377 -0.0311 0.0142 182 VAL A O 1366 C CB . VAL A 182 ? 0.4442 0.4496 0.3473 0.0420 -0.0189 0.0212 182 VAL A CB 1367 C CG1 . VAL A 182 ? 0.4590 0.4645 0.3568 0.0442 -0.0164 0.0200 182 VAL A CG1 1368 C CG2 . VAL A 182 ? 0.4558 0.4592 0.3624 0.0430 -0.0138 0.0254 182 VAL A CG2 1369 N N . HIS A 183 ? 0.4355 0.4498 0.3216 0.0424 -0.0290 0.0183 183 HIS A N 1370 C CA . HIS A 183 ? 0.4476 0.4627 0.3280 0.0408 -0.0333 0.0141 183 HIS A CA 1371 C C . HIS A 183 ? 0.4482 0.4592 0.3254 0.0418 -0.0304 0.0111 183 HIS A C 1372 O O . HIS A 183 ? 0.4370 0.4474 0.3108 0.0448 -0.0257 0.0133 183 HIS A O 1373 C CB . HIS A 183 ? 0.4630 0.4842 0.3360 0.0419 -0.0363 0.0158 183 HIS A CB 1374 C CG . HIS A 183 ? 0.4797 0.5018 0.3464 0.0394 -0.0412 0.0112 183 HIS A CG 1375 N ND1 . HIS A 183 ? 0.5003 0.5236 0.3570 0.0408 -0.0417 0.0104 183 HIS A ND1 1376 C CD2 . HIS A 183 ? 0.4851 0.5061 0.3537 0.0352 -0.0457 0.0071 183 HIS A CD2 1377 C CE1 . HIS A 183 ? 0.5090 0.5320 0.3614 0.0373 -0.0465 0.0056 183 HIS A CE1 1378 N NE2 . HIS A 183 ? 0.4937 0.5152 0.3536 0.0339 -0.0487 0.0037 183 HIS A NE2 1379 N N . HIS A 184 ? 0.4521 0.4596 0.3304 0.0394 -0.0327 0.0064 184 HIS A N 1380 C CA . HIS A 184 ? 0.4507 0.4539 0.3262 0.0404 -0.0302 0.0031 184 HIS A CA 1381 C C . HIS A 184 ? 0.4498 0.4524 0.3156 0.0391 -0.0338 -0.0006 184 HIS A C 1382 O O . HIS A 184 ? 0.4438 0.4443 0.3102 0.0361 -0.0379 -0.0040 184 HIS A O 1383 C CB . HIS A 184 ? 0.4465 0.4455 0.3306 0.0390 -0.0301 0.0006 184 HIS A CB 1384 C CG . HIS A 184 ? 0.4477 0.4470 0.3418 0.0393 -0.0274 0.0036 184 HIS A CG 1385 N ND1 . HIS A 184 ? 0.4412 0.4404 0.3386 0.0416 -0.0217 0.0055 184 HIS A ND1 1386 C CD2 . HIS A 184 ? 0.4385 0.4378 0.3396 0.0371 -0.0297 0.0047 184 HIS A CD2 1387 C CE1 . HIS A 184 ? 0.4628 0.4620 0.3692 0.0405 -0.0208 0.0075 184 HIS A CE1 1388 N NE2 . HIS A 184 ? 0.4460 0.4450 0.3541 0.0379 -0.0257 0.0070 184 HIS A NE2 1389 N N . PRO A 185 ? 0.4715 0.4752 0.3272 0.0412 -0.0325 -0.0001 185 PRO A N 1390 C CA . PRO A 185 ? 0.4839 0.4871 0.3291 0.0394 -0.0365 -0.0039 185 PRO A CA 1391 C C . PRO A 185 ? 0.5005 0.4962 0.3427 0.0386 -0.0355 -0.0094 185 PRO A C 1392 O O . PRO A 185 ? 0.5015 0.4933 0.3474 0.0409 -0.0303 -0.0097 185 PRO A O 1393 C CB . PRO A 185 ? 0.4941 0.4999 0.3290 0.0424 -0.0347 -0.0013 185 PRO A CB 1394 C CG . PRO A 185 ? 0.4852 0.4935 0.3259 0.0455 -0.0302 0.0043 185 PRO A CG 1395 C CD . PRO A 185 ? 0.4744 0.4795 0.3271 0.0450 -0.0274 0.0040 185 PRO A CD 1396 N N . GLY A 186 ? 0.5179 0.5118 0.3540 0.0352 -0.0401 -0.0137 186 GLY A N 1397 C CA . GLY A 186 ? 0.5441 0.5298 0.3765 0.0344 -0.0392 -0.0190 186 GLY A CA 1398 C C . GLY A 186 ? 0.5757 0.5568 0.3988 0.0377 -0.0340 -0.0205 186 GLY A C 1399 O O . GLY A 186 ? 0.5785 0.5531 0.4033 0.0393 -0.0300 -0.0230 186 GLY A O 1400 N N . THR A 187 ? 0.5794 0.5638 0.3929 0.0389 -0.0338 -0.0187 187 THR A N 1401 C CA . THR A 187 ? 0.6214 0.6009 0.4232 0.0418 -0.0290 -0.0201 187 THR A CA 1402 C C . THR A 187 ? 0.6194 0.6034 0.4174 0.0454 -0.0256 -0.0149 187 THR A C 1403 O O . THR A 187 ? 0.5685 0.5597 0.3699 0.0454 -0.0285 -0.0105 187 THR A O 1404 C CB . THR A 187 ? 0.6472 0.6230 0.4342 0.0388 -0.0332 -0.0252 187 THR A CB 1405 O OG1 . THR A 187 ? 0.6515 0.6352 0.4335 0.0368 -0.0392 -0.0231 187 THR A OG1 1406 C CG2 . THR A 187 ? 0.6354 0.6059 0.4252 0.0349 -0.0363 -0.0304 187 THR A CG2 1407 N N . ASP A 188 ? 0.6535 0.6323 0.4438 0.0487 -0.0192 -0.0153 188 ASP A N 1408 C CA . ASP A 188 ? 0.6982 0.6793 0.4816 0.0523 -0.0154 -0.0106 188 ASP A CA 1409 C C . ASP A 188 ? 0.6930 0.6787 0.4641 0.0511 -0.0217 -0.0097 188 ASP A C 1410 O O . ASP A 188 ? 0.6544 0.6450 0.4238 0.0535 -0.0213 -0.0043 188 ASP A O 1411 C CB . ASP A 188 ? 0.7419 0.7156 0.5167 0.0557 -0.0073 -0.0121 188 ASP A CB 1412 C CG . ASP A 188 ? 0.7833 0.7544 0.5714 0.0577 -0.0002 -0.0118 188 ASP A CG 1413 O OD1 . ASP A 188 ? 0.8089 0.7848 0.6116 0.0576 0.0000 -0.0084 188 ASP A OD1 1414 O OD2 . ASP A 188 ? 0.8299 0.7942 0.6138 0.0594 0.0052 -0.0151 188 ASP A OD2 1415 N N . ASN A 189 ? 0.7081 0.6920 0.4708 0.0474 -0.0275 -0.0148 189 ASN A N 1416 C CA . ASN A 189 ? 0.7248 0.7141 0.4769 0.0455 -0.0347 -0.0145 189 ASN A CA 1417 C C . ASN A 189 ? 0.6913 0.6912 0.4542 0.0443 -0.0402 -0.0101 189 ASN A C 1418 O O . ASN A 189 ? 0.6727 0.6793 0.4306 0.0458 -0.0431 -0.0060 189 ASN A O 1419 C CB . ASN A 189 ? 0.7640 0.7492 0.5074 0.0406 -0.0399 -0.0216 189 ASN A CB 1420 C CG . ASN A 189 ? 0.8171 0.7934 0.5425 0.0417 -0.0367 -0.0254 189 ASN A CG 1421 O OD1 . ASN A 189 ? 0.8564 0.8288 0.5767 0.0463 -0.0295 -0.0231 189 ASN A OD1 1422 N ND2 . ASN A 189 ? 0.8427 0.8150 0.5576 0.0372 -0.0415 -0.0315 189 ASN A ND2 1423 N N . ASP A 190 ? 0.6760 0.6770 0.4530 0.0419 -0.0416 -0.0109 190 ASP A N 1424 C CA . ASP A 190 ? 0.6439 0.6540 0.4319 0.0409 -0.0458 -0.0068 190 ASP A CA 1425 C C . ASP A 190 ? 0.5983 0.6116 0.3916 0.0456 -0.0411 0.0000 190 ASP A C 1426 O O . ASP A 190 ? 0.5821 0.6031 0.3772 0.0466 -0.0441 0.0045 190 ASP A O 1427 C CB . ASP A 190 ? 0.6796 0.6886 0.4803 0.0373 -0.0475 -0.0092 190 ASP A CB 1428 C CG . ASP A 190 ? 0.7271 0.7351 0.5237 0.0319 -0.0537 -0.0149 190 ASP A CG 1429 O OD1 . ASP A 190 ? 0.7637 0.7683 0.5473 0.0307 -0.0551 -0.0187 190 ASP A OD1 1430 O OD2 . ASP A 190 ? 0.7640 0.7742 0.5701 0.0285 -0.0570 -0.0156 190 ASP A OD2 1431 N N . GLN A 191 ? 0.5780 0.5853 0.3739 0.0485 -0.0335 0.0008 191 GLN A N 1432 C CA . GLN A 191 ? 0.5667 0.5756 0.3671 0.0526 -0.0280 0.0070 191 GLN A CA 1433 C C . GLN A 191 ? 0.5689 0.5810 0.3574 0.0559 -0.0284 0.0112 191 GLN A C 1434 O O . GLN A 191 ? 0.5613 0.5788 0.3533 0.0581 -0.0287 0.0169 191 GLN A O 1435 C CB . GLN A 191 ? 0.5492 0.5512 0.3529 0.0548 -0.0196 0.0065 191 GLN A CB 1436 C CG . GLN A 191 ? 0.5369 0.5393 0.3441 0.0586 -0.0130 0.0126 191 GLN A CG 1437 C CD . GLN A 191 ? 0.5296 0.5356 0.3513 0.0578 -0.0135 0.0159 191 GLN A CD 1438 O OE1 . GLN A 191 ? 0.5188 0.5251 0.3501 0.0546 -0.0164 0.0132 191 GLN A OE1 1439 N NE2 . GLN A 191 ? 0.5117 0.5193 0.3341 0.0607 -0.0100 0.0218 191 GLN A NE2 1440 N N . ILE A 192 ? 0.5957 0.6040 0.3695 0.0565 -0.0280 0.0086 192 ILE A N 1441 C CA . ILE A 192 ? 0.6154 0.6260 0.3756 0.0599 -0.0285 0.0125 192 ILE A CA 1442 C C . ILE A 192 ? 0.6177 0.6378 0.3763 0.0582 -0.0379 0.0137 192 ILE A C 1443 O O . ILE A 192 ? 0.6161 0.6421 0.3736 0.0614 -0.0390 0.0197 192 ILE A O 1444 C CB . ILE A 192 ? 0.6492 0.6522 0.3927 0.0606 -0.0259 0.0087 192 ILE A CB 1445 C CG1 . ILE A 192 ? 0.6600 0.6545 0.4064 0.0629 -0.0158 0.0082 192 ILE A CG1 1446 C CG2 . ILE A 192 ? 0.6707 0.6759 0.3984 0.0638 -0.0276 0.0125 192 ILE A CG2 1447 C CD1 . ILE A 192 ? 0.6684 0.6627 0.4175 0.0675 -0.0085 0.0149 192 ILE A CD1 1448 N N . SER A 193 ? 0.6297 0.6516 0.3894 0.0531 -0.0443 0.0083 193 SER A N 1449 C CA . SER A 193 ? 0.6356 0.6674 0.3958 0.0506 -0.0533 0.0088 193 SER A CA 1450 C C . SER A 193 ? 0.6147 0.6546 0.3894 0.0519 -0.0543 0.0145 193 SER A C 1451 O O . SER A 193 ? 0.5968 0.6460 0.3709 0.0531 -0.0593 0.0184 193 SER A O 1452 C CB . SER A 193 ? 0.6743 0.7049 0.4354 0.0442 -0.0586 0.0015 193 SER A CB 1453 O OG . SER A 193 ? 0.7262 0.7669 0.4882 0.0411 -0.0673 0.0015 193 SER A OG 1454 N N . LEU A 194 ? 0.5648 0.6012 0.3523 0.0520 -0.0494 0.0151 194 LEU A N 1455 C CA . LEU A 194 ? 0.5510 0.5933 0.3513 0.0531 -0.0495 0.0201 194 LEU A CA 1456 C C . LEU A 194 ? 0.5408 0.5827 0.3411 0.0589 -0.0436 0.0272 194 LEU A C 1457 O O . LEU A 194 ? 0.5422 0.5910 0.3459 0.0614 -0.0454 0.0325 194 LEU A O 1458 C CB . LEU A 194 ? 0.5352 0.5738 0.3488 0.0498 -0.0477 0.0173 194 LEU A CB 1459 C CG . LEU A 194 ? 0.5414 0.5810 0.3581 0.0440 -0.0537 0.0115 194 LEU A CG 1460 C CD1 . LEU A 194 ? 0.5141 0.5469 0.3404 0.0418 -0.0505 0.0086 194 LEU A CD1 1461 C CD2 . LEU A 194 ? 0.5334 0.5833 0.3557 0.0422 -0.0600 0.0136 194 LEU A CD2 1462 N N . TYR A 195 ? 0.5280 0.5615 0.3250 0.0612 -0.0361 0.0274 195 TYR A N 1463 C CA . TYR A 195 ? 0.5471 0.5785 0.3462 0.0659 -0.0292 0.0337 195 TYR A CA 1464 C C . TYR A 195 ? 0.5892 0.6167 0.3739 0.0703 -0.0249 0.0366 195 TYR A C 1465 O O . TYR A 195 ? 0.6032 0.6285 0.3878 0.0745 -0.0190 0.0423 195 TYR A O 1466 C CB . TYR A 195 ? 0.5322 0.5576 0.3432 0.0646 -0.0231 0.0326 195 TYR A CB 1467 C CG . TYR A 195 ? 0.4960 0.5239 0.3191 0.0602 -0.0275 0.0295 195 TYR A CG 1468 C CD1 . TYR A 195 ? 0.4873 0.5215 0.3175 0.0601 -0.0308 0.0327 195 TYR A CD1 1469 C CD2 . TYR A 195 ? 0.4995 0.5234 0.3263 0.0563 -0.0281 0.0234 195 TYR A CD2 1470 C CE1 . TYR A 195 ? 0.4766 0.5125 0.3166 0.0561 -0.0344 0.0300 195 TYR A CE1 1471 C CE2 . TYR A 195 ? 0.4817 0.5072 0.3182 0.0524 -0.0320 0.0207 195 TYR A CE2 1472 C CZ . TYR A 195 ? 0.4777 0.5090 0.3205 0.0522 -0.0350 0.0240 195 TYR A CZ 1473 O OH . TYR A 195 ? 0.4809 0.5132 0.3325 0.0483 -0.0385 0.0216 195 TYR A OH 1474 N N . ALA A 196 ? 0.6217 0.6478 0.3936 0.0693 -0.0276 0.0325 196 ALA A N 1475 C CA . ALA A 196 ? 0.6636 0.6859 0.4189 0.0733 -0.0246 0.0348 196 ALA A CA 1476 C C . ALA A 196 ? 0.6895 0.7021 0.4429 0.0755 -0.0142 0.0352 196 ALA A C 1477 O O . ALA A 196 ? 0.7326 0.7410 0.4725 0.0791 -0.0102 0.0376 196 ALA A O 1478 C CB . ALA A 196 ? 0.6584 0.6868 0.4090 0.0779 -0.0268 0.0422 196 ALA A CB 1479 N N . GLN A 197 ? 0.6779 0.6871 0.4446 0.0733 -0.0098 0.0328 197 GLN A N 1480 C CA . GLN A 197 ? 0.6919 0.6933 0.4599 0.0750 0.0001 0.0332 197 GLN A CA 1481 C C . GLN A 197 ? 0.6630 0.6624 0.4454 0.0714 0.0019 0.0285 197 GLN A C 1482 O O . GLN A 197 ? 0.6464 0.6498 0.4377 0.0680 -0.0040 0.0260 197 GLN A O 1483 C CB . GLN A 197 ? 0.7079 0.7084 0.4785 0.0789 0.0063 0.0406 197 GLN A CB 1484 C CG . GLN A 197 ? 0.7121 0.7172 0.4971 0.0779 0.0042 0.0436 197 GLN A CG 1485 C CD . GLN A 197 ? 0.7438 0.7503 0.5255 0.0824 0.0060 0.0514 197 GLN A CD 1486 O OE1 . GLN A 197 ? 0.7869 0.7912 0.5551 0.0864 0.0083 0.0550 197 GLN A OE1 1487 N NE2 . GLN A 197 ? 0.7458 0.7553 0.5393 0.0819 0.0051 0.0542 197 GLN A NE2 1488 N N . ALA A 198 ? 0.6505 0.6437 0.4347 0.0723 0.0101 0.0275 198 ALA A N 1489 C CA . ALA A 198 ? 0.6438 0.6352 0.4416 0.0695 0.0122 0.0234 198 ALA A CA 1490 C C . ALA A 198 ? 0.6105 0.6053 0.4246 0.0679 0.0117 0.0259 198 ALA A C 1491 O O . ALA A 198 ? 0.6046 0.6010 0.4197 0.0697 0.0132 0.0313 198 ALA A O 1492 C CB . ALA A 198 ? 0.6339 0.6193 0.4310 0.0714 0.0218 0.0227 198 ALA A CB 1493 N N . SER A 199 ? 0.6125 0.6078 0.4386 0.0647 0.0097 0.0220 199 SER A N 1494 C CA . SER A 199 ? 0.6062 0.6042 0.4463 0.0626 0.0081 0.0236 199 SER A CA 1495 C C . SER A 199 ? 0.6115 0.6073 0.4595 0.0637 0.0162 0.0270 199 SER A C 1496 O O . SER A 199 ? 0.6298 0.6221 0.4771 0.0651 0.0230 0.0265 199 SER A O 1497 C CB . SER A 199 ? 0.5913 0.5898 0.4407 0.0590 0.0036 0.0184 199 SER A CB 1498 O OG . SER A 199 ? 0.6036 0.5985 0.4571 0.0591 0.0082 0.0153 199 SER A OG 1499 N N . GLY A 200 ? 0.6197 0.6171 0.4751 0.0630 0.0158 0.0305 200 GLY A N 1500 C CA . GLY A 200 ? 0.6242 0.6192 0.4881 0.0629 0.0227 0.0335 200 GLY A CA 1501 C C . GLY A 200 ? 0.6194 0.6160 0.4943 0.0600 0.0193 0.0340 200 GLY A C 1502 O O . GLY A 200 ? 0.6384 0.6379 0.5129 0.0588 0.0124 0.0330 200 GLY A O 1503 N N . ARG A 201 ? 0.6003 0.5946 0.4845 0.0588 0.0246 0.0355 201 ARG A N 1504 C CA . ARG A 201 ? 0.5771 0.5718 0.4719 0.0554 0.0218 0.0351 201 ARG A CA 1505 C C . ARG A 201 ? 0.5614 0.5563 0.4529 0.0563 0.0196 0.0390 201 ARG A C 1506 O O . ARG A 201 ? 0.5381 0.5325 0.4206 0.0599 0.0218 0.0432 201 ARG A O 1507 C CB . ARG A 201 ? 0.5939 0.5862 0.4991 0.0534 0.0281 0.0357 201 ARG A CB 1508 C CG . ARG A 201 ? 0.5989 0.5873 0.5005 0.0554 0.0359 0.0409 201 ARG A CG 1509 C CD . ARG A 201 ? 0.6094 0.5960 0.5191 0.0539 0.0434 0.0406 201 ARG A CD 1510 N NE . ARG A 201 ? 0.6174 0.5991 0.5230 0.0556 0.0513 0.0458 201 ARG A NE 1511 C CZ . ARG A 201 ? 0.6362 0.6155 0.5324 0.0592 0.0573 0.0487 201 ARG A CZ 1512 N NH1 . ARG A 201 ? 0.6329 0.6141 0.5222 0.0615 0.0566 0.0466 201 ARG A NH1 1513 N NH2 . ARG A 201 ? 0.6328 0.6068 0.5255 0.0605 0.0645 0.0537 201 ARG A NH2 1514 N N . ILE A 202 ? 0.5064 0.5019 0.4050 0.0533 0.0152 0.0376 202 ILE A N 1515 C CA . ILE A 202 ? 0.4868 0.4818 0.3845 0.0538 0.0139 0.0411 202 ILE A CA 1516 C C . ILE A 202 ? 0.4733 0.4638 0.3797 0.0510 0.0176 0.0417 202 ILE A C 1517 O O . ILE A 202 ? 0.4652 0.4554 0.3799 0.0473 0.0160 0.0380 202 ILE A O 1518 C CB . ILE A 202 ? 0.4755 0.4743 0.3731 0.0524 0.0059 0.0387 202 ILE A CB 1519 C CG1 . ILE A 202 ? 0.4837 0.4869 0.3720 0.0548 0.0022 0.0382 202 ILE A CG1 1520 C CG2 . ILE A 202 ? 0.4624 0.4606 0.3614 0.0526 0.0051 0.0419 202 ILE A CG2 1521 C CD1 . ILE A 202 ? 0.4781 0.4852 0.3668 0.0527 -0.0054 0.0350 202 ILE A CD1 1522 N N . THR A 203 ? 0.4723 0.4591 0.3766 0.0527 0.0224 0.0465 203 THR A N 1523 C CA . THR A 203 ? 0.4705 0.4519 0.3818 0.0497 0.0260 0.0471 203 THR A CA 1524 C C . THR A 203 ? 0.4735 0.4527 0.3828 0.0506 0.0250 0.0501 203 THR A C 1525 O O . THR A 203 ? 0.4862 0.4654 0.3886 0.0549 0.0267 0.0546 203 THR A O 1526 C CB . THR A 203 ? 0.4944 0.4712 0.4067 0.0499 0.0347 0.0496 203 THR A CB 1527 O OG1 . THR A 203 ? 0.4912 0.4706 0.4074 0.0487 0.0357 0.0464 203 THR A OG1 1528 C CG2 . THR A 203 ? 0.4897 0.4604 0.4089 0.0461 0.0382 0.0499 203 THR A CG2 1529 N N . VAL A 204 ? 0.4392 0.4167 0.3546 0.0466 0.0219 0.0474 204 VAL A N 1530 C CA . VAL A 204 ? 0.4297 0.4040 0.3439 0.0469 0.0216 0.0496 204 VAL A CA 1531 C C . VAL A 204 ? 0.4328 0.3993 0.3520 0.0431 0.0260 0.0493 204 VAL A C 1532 O O . VAL A 204 ? 0.4155 0.3815 0.3412 0.0384 0.0238 0.0451 204 VAL A O 1533 C CB . VAL A 204 ? 0.4247 0.4029 0.3401 0.0454 0.0141 0.0466 204 VAL A CB 1534 C CG1 . VAL A 204 ? 0.4066 0.3808 0.3215 0.0455 0.0147 0.0489 204 VAL A CG1 1535 C CG2 . VAL A 204 ? 0.4099 0.3958 0.3204 0.0485 0.0096 0.0467 204 VAL A CG2 1536 N N . SER A 205 ? 0.4367 0.3970 0.3527 0.0451 0.0321 0.0537 205 SER A N 1537 C CA . SER A 205 ? 0.4608 0.4126 0.3804 0.0413 0.0373 0.0535 205 SER A CA 1538 C C . SER A 205 ? 0.4722 0.4163 0.3883 0.0425 0.0407 0.0567 205 SER A C 1539 O O . SER A 205 ? 0.4697 0.4153 0.3806 0.0474 0.0405 0.0604 205 SER A O 1540 C CB . SER A 205 ? 0.4662 0.4158 0.3860 0.0418 0.0443 0.0554 205 SER A CB 1541 O OG . SER A 205 ? 0.4853 0.4339 0.3970 0.0479 0.0487 0.0611 205 SER A OG 1542 N N . THR A 206 ? 0.4788 0.4148 0.3981 0.0376 0.0436 0.0550 206 THR A N 1543 C CA . THR A 206 ? 0.4699 0.3961 0.3859 0.0378 0.0484 0.0575 206 THR A CA 1544 C C . THR A 206 ? 0.4887 0.4062 0.4068 0.0339 0.0554 0.0575 206 THR A C 1545 O O . THR A 206 ? 0.4830 0.4037 0.4058 0.0315 0.0563 0.0558 206 THR A O 1546 C CB . THR A 206 ? 0.4764 0.4000 0.3935 0.0342 0.0437 0.0541 206 THR A CB 1547 O OG1 . THR A 206 ? 0.4782 0.4003 0.4012 0.0272 0.0411 0.0488 206 THR A OG1 1548 C CG2 . THR A 206 ? 0.4563 0.3891 0.3728 0.0368 0.0363 0.0532 206 THR A CG2 1549 N N . LYS A 207 ? 0.5055 0.4119 0.4203 0.0332 0.0609 0.0593 207 LYS A N 1550 C CA . LYS A 207 ? 0.5421 0.4393 0.4593 0.0280 0.0671 0.0584 207 LYS A CA 1551 C C . LYS A 207 ? 0.5569 0.4562 0.4823 0.0200 0.0622 0.0520 207 LYS A C 1552 O O . LYS A 207 ? 0.5601 0.4573 0.4904 0.0156 0.0658 0.0507 207 LYS A O 1553 C CB . LYS A 207 ? 0.5690 0.4527 0.4804 0.0282 0.0733 0.0608 207 LYS A CB 1554 C CG . LYS A 207 ? 0.5924 0.4722 0.4964 0.0361 0.0800 0.0679 207 LYS A CG 1555 C CD . LYS A 207 ? 0.6242 0.4890 0.5228 0.0359 0.0871 0.0700 207 LYS A CD 1556 C CE . LYS A 207 ? 0.6487 0.5126 0.5406 0.0446 0.0892 0.0759 207 LYS A CE 1557 N NZ . LYS A 207 ? 0.6733 0.5215 0.5598 0.0448 0.0970 0.0780 207 LYS A NZ 1558 N N . ARG A 208 ? 0.5593 0.4630 0.4863 0.0181 0.0542 0.0482 208 ARG A N 1559 C CA . ARG A 208 ? 0.5882 0.4932 0.5223 0.0107 0.0491 0.0424 208 ARG A CA 1560 C C . ARG A 208 ? 0.5730 0.4904 0.5135 0.0105 0.0416 0.0393 208 ARG A C 1561 O O . ARG A 208 ? 0.5695 0.4893 0.5167 0.0050 0.0372 0.0350 208 ARG A O 1562 C CB . ARG A 208 ? 0.6255 0.5232 0.5559 0.0075 0.0460 0.0399 208 ARG A CB 1563 C CG . ARG A 208 ? 0.6460 0.5486 0.5729 0.0113 0.0400 0.0399 208 ARG A CG 1564 C CD . ARG A 208 ? 0.6999 0.5963 0.6241 0.0071 0.0360 0.0364 208 ARG A CD 1565 N NE . ARG A 208 ? 0.7273 0.6291 0.6488 0.0105 0.0307 0.0365 208 ARG A NE 1566 C CZ . ARG A 208 ? 0.7384 0.6365 0.6569 0.0081 0.0265 0.0339 208 ARG A CZ 1567 N NH1 . ARG A 208 ? 0.7586 0.6474 0.6755 0.0021 0.0265 0.0307 208 ARG A NH1 1568 N NH2 . ARG A 208 ? 0.7236 0.6272 0.6402 0.0114 0.0224 0.0343 208 ARG A NH2 1569 N N . SER A 209 ? 0.5398 0.4650 0.4781 0.0163 0.0399 0.0415 209 SER A N 1570 C CA . SER A 209 ? 0.5306 0.4663 0.4736 0.0164 0.0327 0.0384 209 SER A CA 1571 C C . SER A 209 ? 0.5058 0.4485 0.4470 0.0219 0.0342 0.0410 209 SER A C 1572 O O . SER A 209 ? 0.4876 0.4282 0.4224 0.0267 0.0389 0.0455 209 SER A O 1573 C CB . SER A 209 ? 0.5371 0.4743 0.4773 0.0166 0.0255 0.0364 209 SER A CB 1574 O OG . SER A 209 ? 0.5664 0.5041 0.4995 0.0222 0.0265 0.0401 209 SER A OG 1575 N N . GLN A 210 ? 0.4879 0.4387 0.4343 0.0215 0.0300 0.0382 210 GLN A N 1576 C CA . GLN A 210 ? 0.4941 0.4514 0.4377 0.0264 0.0304 0.0398 210 GLN A CA 1577 C C . GLN A 210 ? 0.4966 0.4614 0.4438 0.0259 0.0230 0.0358 210 GLN A C 1578 O O . GLN A 210 ? 0.4843 0.4505 0.4391 0.0217 0.0197 0.0320 210 GLN A O 1579 C CB . GLN A 210 ? 0.5202 0.4772 0.4662 0.0268 0.0376 0.0415 210 GLN A CB 1580 C CG . GLN A 210 ? 0.5366 0.4945 0.4935 0.0212 0.0383 0.0382 210 GLN A CG 1581 C CD . GLN A 210 ? 0.5836 0.5419 0.5433 0.0217 0.0461 0.0401 210 GLN A CD 1582 O OE1 . GLN A 210 ? 0.6205 0.5779 0.5729 0.0265 0.0508 0.0438 210 GLN A OE1 1583 N NE2 . GLN A 210 ? 0.5856 0.5454 0.5560 0.0167 0.0475 0.0375 210 GLN A NE2 1584 N N . GLN A 211 ? 0.4656 0.4351 0.4072 0.0301 0.0203 0.0366 211 GLN A N 1585 C CA . GLN A 211 ? 0.4572 0.4329 0.4007 0.0302 0.0141 0.0330 211 GLN A CA 1586 C C . GLN A 211 ? 0.4445 0.4244 0.3829 0.0347 0.0159 0.0344 211 GLN A C 1587 O O . GLN A 211 ? 0.4406 0.4209 0.3712 0.0384 0.0164 0.0375 211 GLN A O 1588 C CB . GLN A 211 ? 0.4705 0.4466 0.4107 0.0300 0.0076 0.0317 211 GLN A CB 1589 C CG . GLN A 211 ? 0.5000 0.4710 0.4428 0.0259 0.0053 0.0302 211 GLN A CG 1590 C CD . GLN A 211 ? 0.5053 0.4748 0.4423 0.0269 0.0023 0.0312 211 GLN A CD 1591 O OE1 . GLN A 211 ? 0.5662 0.5325 0.4989 0.0290 0.0060 0.0347 211 GLN A OE1 1592 N NE2 . GLN A 211 ? 0.5084 0.4802 0.4458 0.0257 -0.0039 0.0282 211 GLN A NE2 1593 N N . THR A 212 ? 0.4371 0.4204 0.3799 0.0345 0.0165 0.0322 212 THR A N 1594 C CA . THR A 212 ? 0.4452 0.4319 0.3824 0.0384 0.0180 0.0328 212 THR A CA 1595 C C . THR A 212 ? 0.4527 0.4436 0.3910 0.0382 0.0118 0.0285 212 THR A C 1596 O O . THR A 212 ? 0.4450 0.4370 0.3915 0.0355 0.0093 0.0253 212 THR A O 1597 C CB . THR A 212 ? 0.4533 0.4396 0.3936 0.0390 0.0256 0.0339 212 THR A CB 1598 O OG1 . THR A 212 ? 0.4497 0.4309 0.3877 0.0393 0.0318 0.0382 212 THR A OG1 1599 C CG2 . THR A 212 ? 0.4577 0.4466 0.3910 0.0430 0.0271 0.0341 212 THR A CG2 1600 N N . VAL A 213 ? 0.4436 0.4366 0.3733 0.0411 0.0090 0.0286 213 VAL A N 1601 C CA . VAL A 213 ? 0.4419 0.4376 0.3710 0.0409 0.0033 0.0246 213 VAL A CA 1602 C C . VAL A 213 ? 0.4593 0.4568 0.3806 0.0443 0.0051 0.0244 213 VAL A C 1603 O O . VAL A 213 ? 0.4615 0.4590 0.3745 0.0470 0.0073 0.0276 213 VAL A O 1604 C CB . VAL A 213 ? 0.4438 0.4398 0.3697 0.0398 -0.0031 0.0239 213 VAL A CB 1605 C CG1 . VAL A 213 ? 0.4490 0.4467 0.3741 0.0392 -0.0085 0.0196 213 VAL A CG1 1606 C CG2 . VAL A 213 ? 0.4420 0.4352 0.3738 0.0366 -0.0044 0.0241 213 VAL A CG2 1607 N N . ILE A 214 ? 0.4704 0.4689 0.3941 0.0442 0.0042 0.0208 214 ILE A N 1608 C CA . ILE A 214 ? 0.4860 0.4850 0.4020 0.0472 0.0063 0.0198 214 ILE A CA 1609 C C . ILE A 214 ? 0.4774 0.4771 0.3868 0.0471 -0.0001 0.0167 214 ILE A C 1610 O O . ILE A 214 ? 0.4628 0.4622 0.3770 0.0452 -0.0041 0.0132 214 ILE A O 1611 C CB . ILE A 214 ? 0.4928 0.4919 0.4156 0.0476 0.0106 0.0177 214 ILE A CB 1612 C CG1 . ILE A 214 ? 0.5091 0.5078 0.4396 0.0469 0.0172 0.0205 214 ILE A CG1 1613 C CG2 . ILE A 214 ? 0.5078 0.5061 0.4211 0.0508 0.0133 0.0165 214 ILE A CG2 1614 C CD1 . ILE A 214 ? 0.5323 0.5328 0.4745 0.0461 0.0201 0.0182 214 ILE A CD1 1615 N N . PRO A 215 ? 0.4840 0.4845 0.3822 0.0490 -0.0012 0.0179 215 PRO A N 1616 C CA . PRO A 215 ? 0.4845 0.4856 0.3761 0.0484 -0.0069 0.0144 215 PRO A CA 1617 C C . PRO A 215 ? 0.4897 0.4885 0.3798 0.0493 -0.0051 0.0105 215 PRO A C 1618 O O . PRO A 215 ? 0.4784 0.4761 0.3664 0.0517 0.0008 0.0114 215 PRO A O 1619 C CB . PRO A 215 ? 0.5001 0.5033 0.3804 0.0504 -0.0077 0.0171 215 PRO A CB 1620 C CG . PRO A 215 ? 0.4915 0.4950 0.3735 0.0521 -0.0034 0.0225 215 PRO A CG 1621 C CD . PRO A 215 ? 0.4895 0.4904 0.3806 0.0516 0.0023 0.0226 215 PRO A CD 1622 N N . ASN A 216 ? 0.4915 0.4891 0.3826 0.0475 -0.0098 0.0063 216 ASN A N 1623 C CA . ASN A 216 ? 0.4932 0.4878 0.3834 0.0485 -0.0082 0.0024 216 ASN A CA 1624 C C . ASN A 216 ? 0.4927 0.4853 0.3723 0.0477 -0.0127 -0.0010 216 ASN A C 1625 O O . ASN A 216 ? 0.4862 0.4785 0.3668 0.0451 -0.0184 -0.0030 216 ASN A O 1626 C CB . ASN A 216 ? 0.4942 0.4879 0.3966 0.0472 -0.0092 0.0004 216 ASN A CB 1627 C CG . ASN A 216 ? 0.5079 0.5038 0.4216 0.0473 -0.0052 0.0032 216 ASN A CG 1628 O OD1 . ASN A 216 ? 0.5156 0.5125 0.4381 0.0450 -0.0082 0.0037 216 ASN A OD1 1629 N ND2 . ASN A 216 ? 0.4937 0.4901 0.4073 0.0496 0.0016 0.0049 216 ASN A ND2 1630 N N . ILE A 217 ? 0.5049 0.4957 0.3737 0.0498 -0.0098 -0.0019 217 ILE A N 1631 C CA . ILE A 217 ? 0.5040 0.4926 0.3611 0.0487 -0.0138 -0.0054 217 ILE A CA 1632 C C . ILE A 217 ? 0.5127 0.4960 0.3713 0.0481 -0.0145 -0.0104 217 ILE A C 1633 O O . ILE A 217 ? 0.5170 0.4980 0.3814 0.0502 -0.0096 -0.0112 217 ILE A O 1634 C CB . ILE A 217 ? 0.5198 0.5073 0.3633 0.0513 -0.0103 -0.0048 217 ILE A CB 1635 C CG1 . ILE A 217 ? 0.5121 0.5047 0.3532 0.0522 -0.0107 0.0005 217 ILE A CG1 1636 C CG2 . ILE A 217 ? 0.5363 0.5203 0.3670 0.0498 -0.0142 -0.0094 217 ILE A CG2 1637 C CD1 . ILE A 217 ? 0.5263 0.5176 0.3573 0.0557 -0.0049 0.0030 217 ILE A CD1 1638 N N . GLY A 218 ? 0.5286 0.5100 0.3827 0.0451 -0.0204 -0.0137 218 GLY A N 1639 C CA . GLY A 218 ? 0.5433 0.5182 0.3968 0.0446 -0.0209 -0.0185 218 GLY A CA 1640 C C . GLY A 218 ? 0.5480 0.5216 0.4009 0.0405 -0.0278 -0.0209 218 GLY A C 1641 O O . GLY A 218 ? 0.5367 0.5148 0.3946 0.0383 -0.0317 -0.0186 218 GLY A O 1642 N N . SER A 219 ? 0.5558 0.5224 0.4021 0.0395 -0.0287 -0.0257 219 SER A N 1643 C CA . SER A 219 ? 0.5653 0.5292 0.4108 0.0354 -0.0345 -0.0284 219 SER A CA 1644 C C . SER A 219 ? 0.5461 0.5086 0.4037 0.0355 -0.0353 -0.0276 219 SER A C 1645 O O . SER A 219 ? 0.5723 0.5317 0.4355 0.0386 -0.0317 -0.0280 219 SER A O 1646 C CB . SER A 219 ? 0.5939 0.5493 0.4281 0.0343 -0.0346 -0.0340 219 SER A CB 1647 O OG . SER A 219 ? 0.6270 0.5832 0.4488 0.0340 -0.0342 -0.0350 219 SER A OG 1648 N N . ARG A 220 ? 0.5131 0.4784 0.3748 0.0322 -0.0401 -0.0262 220 ARG A N 1649 C CA . ARG A 220 ? 0.5156 0.4777 0.3852 0.0312 -0.0423 -0.0263 220 ARG A CA 1650 C C . ARG A 220 ? 0.5154 0.4713 0.3782 0.0274 -0.0462 -0.0302 220 ARG A C 1651 O O . ARG A 220 ? 0.5301 0.4865 0.3838 0.0248 -0.0478 -0.0322 220 ARG A O 1652 C CB . ARG A 220 ? 0.5027 0.4710 0.3806 0.0298 -0.0445 -0.0222 220 ARG A CB 1653 C CG . ARG A 220 ? 0.4992 0.4721 0.3855 0.0329 -0.0408 -0.0185 220 ARG A CG 1654 C CD . ARG A 220 ? 0.4961 0.4742 0.3783 0.0346 -0.0376 -0.0163 220 ARG A CD 1655 N NE . ARG A 220 ? 0.5002 0.4828 0.3906 0.0365 -0.0345 -0.0123 220 ARG A NE 1656 C CZ . ARG A 220 ? 0.5117 0.4977 0.4005 0.0388 -0.0302 -0.0098 220 ARG A CZ 1657 N NH1 . ARG A 220 ? 0.5113 0.4970 0.3900 0.0400 -0.0287 -0.0109 220 ARG A NH1 1658 N NH2 . ARG A 220 ? 0.5241 0.5132 0.4208 0.0399 -0.0272 -0.0063 220 ARG A NH2 1659 N N . PRO A 221 ? 0.5083 0.4582 0.3750 0.0267 -0.0477 -0.0313 221 PRO A N 1660 C CA . PRO A 221 ? 0.5164 0.4598 0.3764 0.0226 -0.0510 -0.0348 221 PRO A CA 1661 C C . PRO A 221 ? 0.5205 0.4697 0.3789 0.0179 -0.0549 -0.0338 221 PRO A C 1662 O O . PRO A 221 ? 0.5140 0.4699 0.3791 0.0178 -0.0559 -0.0299 221 PRO A O 1663 C CB . PRO A 221 ? 0.5198 0.4567 0.3856 0.0234 -0.0519 -0.0347 221 PRO A CB 1664 C CG . PRO A 221 ? 0.5145 0.4524 0.3872 0.0288 -0.0481 -0.0332 221 PRO A CG 1665 C CD . PRO A 221 ? 0.5111 0.4590 0.3872 0.0298 -0.0465 -0.0299 221 PRO A CD 1666 N N . ARG A 222 ? 0.5247 0.4717 0.3744 0.0141 -0.0570 -0.0372 222 ARG A N 1667 C CA . ARG A 222 ? 0.5370 0.4915 0.3858 0.0099 -0.0606 -0.0361 222 ARG A CA 1668 C C . ARG A 222 ? 0.5276 0.4823 0.3830 0.0071 -0.0631 -0.0343 222 ARG A C 1669 O O . ARG A 222 ? 0.5262 0.4723 0.3818 0.0059 -0.0634 -0.0361 222 ARG A O 1670 C CB . ARG A 222 ? 0.5749 0.5272 0.4133 0.0058 -0.0627 -0.0406 222 ARG A CB 1671 C CG . ARG A 222 ? 0.5971 0.5510 0.4279 0.0084 -0.0607 -0.0417 222 ARG A CG 1672 C CD . ARG A 222 ? 0.6418 0.5950 0.4619 0.0035 -0.0638 -0.0460 222 ARG A CD 1673 N NE . ARG A 222 ? 0.6628 0.6175 0.4739 0.0058 -0.0622 -0.0469 222 ARG A NE 1674 C CZ . ARG A 222 ? 0.7044 0.6616 0.5058 0.0022 -0.0654 -0.0496 222 ARG A CZ 1675 N NH1 . ARG A 222 ? 0.7029 0.6622 0.5037 -0.0040 -0.0705 -0.0517 222 ARG A NH1 1676 N NH2 . ARG A 222 ? 0.7178 0.6755 0.5100 0.0048 -0.0637 -0.0501 222 ARG A NH2 1677 N N . VAL A 223 ? 0.5244 0.4884 0.3850 0.0065 -0.0643 -0.0305 223 VAL A N 1678 C CA . VAL A 223 ? 0.5194 0.4845 0.3855 0.0035 -0.0663 -0.0286 223 VAL A CA 1679 C C . VAL A 223 ? 0.5341 0.5077 0.3989 -0.0002 -0.0691 -0.0283 223 VAL A C 1680 O O . VAL A 223 ? 0.5095 0.4921 0.3746 0.0015 -0.0690 -0.0259 223 VAL A O 1681 C CB . VAL A 223 ? 0.5148 0.4832 0.3890 0.0067 -0.0646 -0.0240 223 VAL A CB 1682 C CG1 . VAL A 223 ? 0.5018 0.4727 0.3805 0.0036 -0.0663 -0.0217 223 VAL A CG1 1683 C CG2 . VAL A 223 ? 0.5134 0.4741 0.3901 0.0099 -0.0628 -0.0244 223 VAL A CG2 1684 N N . ARG A 224 ? 0.5606 0.5317 0.4244 -0.0054 -0.0715 -0.0305 224 ARG A N 1685 C CA . ARG A 224 ? 0.5637 0.5431 0.4268 -0.0097 -0.0745 -0.0309 224 ARG A CA 1686 C C . ARG A 224 ? 0.5675 0.5520 0.4240 -0.0089 -0.0755 -0.0324 224 ARG A C 1687 O O . ARG A 224 ? 0.5827 0.5782 0.4406 -0.0087 -0.0773 -0.0300 224 ARG A O 1688 C CB . ARG A 224 ? 0.5668 0.5553 0.4384 -0.0095 -0.0747 -0.0259 224 ARG A CB 1689 C CG . ARG A 224 ? 0.5671 0.5491 0.4434 -0.0106 -0.0735 -0.0248 224 ARG A CG 1690 C CD . ARG A 224 ? 0.5645 0.5541 0.4484 -0.0103 -0.0729 -0.0201 224 ARG A CD 1691 N NE . ARG A 224 ? 0.5434 0.5373 0.4307 -0.0050 -0.0707 -0.0161 224 ARG A NE 1692 C CZ . ARG A 224 ? 0.5613 0.5491 0.4502 -0.0018 -0.0684 -0.0147 224 ARG A CZ 1693 N NH1 . ARG A 224 ? 0.5830 0.5606 0.4707 -0.0027 -0.0683 -0.0166 224 ARG A NH1 1694 N NH2 . ARG A 224 ? 0.5620 0.5542 0.4540 0.0023 -0.0663 -0.0112 224 ARG A NH2 1695 N N . ASP A 225 ? 0.5937 0.5694 0.4426 -0.0079 -0.0742 -0.0363 225 ASP A N 1696 C CA . ASP A 225 ? 0.6122 0.5891 0.4522 -0.0071 -0.0745 -0.0387 225 ASP A CA 1697 C C . ASP A 225 ? 0.5852 0.5684 0.4255 -0.0012 -0.0721 -0.0349 225 ASP A C 1698 O O . ASP A 225 ? 0.5654 0.5510 0.3979 -0.0004 -0.0726 -0.0362 225 ASP A O 1699 C CB . ASP A 225 ? 0.6517 0.6349 0.4875 -0.0129 -0.0792 -0.0411 225 ASP A CB 1700 C CG . ASP A 225 ? 0.7249 0.7030 0.5479 -0.0143 -0.0799 -0.0463 225 ASP A CG 1701 O OD1 . ASP A 225 ? 0.7605 0.7265 0.5777 -0.0129 -0.0768 -0.0497 225 ASP A OD1 1702 O OD2 . ASP A 225 ? 0.7932 0.7794 0.6118 -0.0167 -0.0836 -0.0470 225 ASP A OD2 1703 N N . ILE A 226 ? 0.5162 0.5013 0.3647 0.0027 -0.0695 -0.0305 226 ILE A N 1704 C CA . ILE A 226 ? 0.4931 0.4838 0.3425 0.0079 -0.0668 -0.0266 226 ILE A CA 1705 C C . ILE A 226 ? 0.4899 0.4734 0.3409 0.0123 -0.0620 -0.0266 226 ILE A C 1706 O O . ILE A 226 ? 0.4709 0.4508 0.3291 0.0129 -0.0609 -0.0255 226 ILE A O 1707 C CB . ILE A 226 ? 0.4955 0.4953 0.3536 0.0090 -0.0671 -0.0211 226 ILE A CB 1708 C CG1 . ILE A 226 ? 0.5077 0.5166 0.3654 0.0054 -0.0716 -0.0205 226 ILE A CG1 1709 C CG2 . ILE A 226 ? 0.4741 0.4775 0.3333 0.0144 -0.0635 -0.0170 226 ILE A CG2 1710 C CD1 . ILE A 226 ? 0.5027 0.5173 0.3521 0.0059 -0.0735 -0.0211 226 ILE A CD1 1711 N N . PRO A 227 ? 0.4917 0.4733 0.3360 0.0154 -0.0592 -0.0277 227 PRO A N 1712 C CA . PRO A 227 ? 0.4973 0.4736 0.3441 0.0198 -0.0542 -0.0275 227 PRO A CA 1713 C C . PRO A 227 ? 0.4810 0.4632 0.3346 0.0238 -0.0510 -0.0223 227 PRO A C 1714 O O . PRO A 227 ? 0.4827 0.4619 0.3409 0.0270 -0.0470 -0.0216 227 PRO A O 1715 C CB . PRO A 227 ? 0.5086 0.4801 0.3440 0.0209 -0.0523 -0.0312 227 PRO A CB 1716 C CG . PRO A 227 ? 0.5099 0.4882 0.3380 0.0189 -0.0555 -0.0308 227 PRO A CG 1717 C CD . PRO A 227 ? 0.5095 0.4932 0.3428 0.0144 -0.0607 -0.0299 227 PRO A CD 1718 N N . SER A 228 ? 0.4845 0.4749 0.3389 0.0236 -0.0525 -0.0186 228 SER A N 1719 C CA . SER A 228 ? 0.4772 0.4725 0.3376 0.0270 -0.0493 -0.0135 228 SER A CA 1720 C C . SER A 228 ? 0.4535 0.4491 0.3244 0.0260 -0.0499 -0.0112 228 SER A C 1721 O O . SER A 228 ? 0.4369 0.4299 0.3097 0.0227 -0.0530 -0.0132 228 SER A O 1722 C CB . SER A 228 ? 0.5017 0.5051 0.3581 0.0275 -0.0508 -0.0103 228 SER A CB 1723 O OG . SER A 228 ? 0.5386 0.5420 0.3842 0.0285 -0.0505 -0.0119 228 SER A OG 1724 N N . ARG A 229 ? 0.4453 0.4435 0.3221 0.0286 -0.0467 -0.0070 229 ARG A N 1725 C CA . ARG A 229 ? 0.4289 0.4272 0.3144 0.0277 -0.0470 -0.0047 229 ARG A CA 1726 C C . ARG A 229 ? 0.4259 0.4295 0.3140 0.0297 -0.0446 0.0003 229 ARG A C 1727 O O . ARG A 229 ? 0.4480 0.4540 0.3328 0.0326 -0.0416 0.0023 229 ARG A O 1728 C CB . ARG A 229 ? 0.4352 0.4283 0.3269 0.0287 -0.0448 -0.0056 229 ARG A CB 1729 C CG . ARG A 229 ? 0.4496 0.4364 0.3399 0.0274 -0.0467 -0.0101 229 ARG A CG 1730 C CD . ARG A 229 ? 0.4504 0.4347 0.3409 0.0235 -0.0511 -0.0114 229 ARG A CD 1731 N NE . ARG A 229 ? 0.4616 0.4385 0.3511 0.0229 -0.0523 -0.0151 229 ARG A NE 1732 C CZ . ARG A 229 ? 0.4817 0.4547 0.3642 0.0212 -0.0539 -0.0189 229 ARG A CZ 1733 N NH1 . ARG A 229 ? 0.4755 0.4521 0.3513 0.0194 -0.0552 -0.0197 229 ARG A NH1 1734 N NH2 . ARG A 229 ? 0.4671 0.4324 0.3491 0.0212 -0.0543 -0.0218 229 ARG A NH2 1735 N N . ILE A 230 ? 0.4125 0.4171 0.3061 0.0283 -0.0457 0.0025 230 ILE A N 1736 C CA . ILE A 230 ? 0.4019 0.4090 0.2993 0.0303 -0.0426 0.0072 230 ILE A CA 1737 C C . ILE A 230 ? 0.3919 0.3941 0.2963 0.0295 -0.0410 0.0073 230 ILE A C 1738 O O . ILE A 230 ? 0.3918 0.3908 0.2985 0.0268 -0.0438 0.0054 230 ILE A O 1739 C CB . ILE A 230 ? 0.4014 0.4137 0.2989 0.0295 -0.0446 0.0099 230 ILE A CB 1740 C CG1 . ILE A 230 ? 0.4141 0.4326 0.3050 0.0304 -0.0466 0.0101 230 ILE A CG1 1741 C CG2 . ILE A 230 ? 0.4075 0.4204 0.3090 0.0317 -0.0408 0.0146 230 ILE A CG2 1742 C CD1 . ILE A 230 ? 0.4311 0.4566 0.3233 0.0300 -0.0490 0.0129 230 ILE A CD1 1743 N N . SER A 231 ? 0.3805 0.3820 0.2880 0.0316 -0.0367 0.0095 231 SER A N 1744 C CA . SER A 231 ? 0.3875 0.3853 0.3018 0.0304 -0.0355 0.0100 231 SER A CA 1745 C C . SER A 231 ? 0.3726 0.3710 0.2885 0.0306 -0.0334 0.0140 231 SER A C 1746 O O . SER A 231 ? 0.3630 0.3642 0.2768 0.0332 -0.0301 0.0173 231 SER A O 1747 C CB . SER A 231 ? 0.3970 0.3934 0.3150 0.0319 -0.0320 0.0094 231 SER A CB 1748 O OG . SER A 231 ? 0.4163 0.4111 0.3338 0.0317 -0.0339 0.0056 231 SER A OG 1749 N N . ILE A 232 ? 0.3690 0.3641 0.2879 0.0282 -0.0350 0.0138 232 ILE A N 1750 C CA . ILE A 232 ? 0.3687 0.3632 0.2883 0.0282 -0.0331 0.0172 232 ILE A CA 1751 C C . ILE A 232 ? 0.3857 0.3756 0.3095 0.0275 -0.0298 0.0183 232 ILE A C 1752 O O . ILE A 232 ? 0.3765 0.3628 0.3037 0.0254 -0.0314 0.0157 232 ILE A O 1753 C CB . ILE A 232 ? 0.3746 0.3676 0.2936 0.0256 -0.0365 0.0163 232 ILE A CB 1754 C CG1 . ILE A 232 ? 0.3785 0.3766 0.2940 0.0256 -0.0396 0.0154 232 ILE A CG1 1755 C CG2 . ILE A 232 ? 0.3730 0.3639 0.2929 0.0256 -0.0339 0.0195 232 ILE A CG2 1756 C CD1 . ILE A 232 ? 0.3957 0.4005 0.3092 0.0285 -0.0380 0.0189 232 ILE A CD1 1757 N N . TYR A 233 ? 0.3700 0.3599 0.2934 0.0293 -0.0253 0.0220 233 TYR A N 1758 C CA . TYR A 233 ? 0.3795 0.3647 0.3061 0.0286 -0.0214 0.0234 233 TYR A CA 1759 C C . TYR A 233 ? 0.3709 0.3532 0.2960 0.0288 -0.0190 0.0265 233 TYR A C 1760 O O . TYR A 233 ? 0.3607 0.3462 0.2829 0.0306 -0.0196 0.0283 233 TYR A O 1761 C CB . TYR A 233 ? 0.3873 0.3740 0.3146 0.0309 -0.0166 0.0251 233 TYR A CB 1762 C CG . TYR A 233 ? 0.4003 0.3895 0.3297 0.0309 -0.0181 0.0221 233 TYR A CG 1763 C CD1 . TYR A 233 ? 0.4040 0.3974 0.3291 0.0329 -0.0200 0.0211 233 TYR A CD1 1764 C CD2 . TYR A 233 ? 0.4134 0.4005 0.3489 0.0287 -0.0179 0.0199 233 TYR A CD2 1765 C CE1 . TYR A 233 ? 0.4173 0.4118 0.3436 0.0330 -0.0210 0.0181 233 TYR A CE1 1766 C CE2 . TYR A 233 ? 0.4180 0.4075 0.3561 0.0291 -0.0191 0.0172 233 TYR A CE2 1767 C CZ . TYR A 233 ? 0.4283 0.4209 0.3614 0.0314 -0.0203 0.0163 233 TYR A CZ 1768 O OH . TYR A 233 ? 0.4528 0.4467 0.3878 0.0321 -0.0208 0.0135 233 TYR A OH 1769 N N . TRP A 234 ? 0.3711 0.3472 0.2981 0.0270 -0.0162 0.0269 234 TRP A N 1770 C CA . TRP A 234 ? 0.3773 0.3490 0.3023 0.0273 -0.0129 0.0297 234 TRP A CA 1771 C C . TRP A 234 ? 0.3804 0.3465 0.3065 0.0269 -0.0074 0.0314 234 TRP A C 1772 O O . TRP A 234 ? 0.3816 0.3464 0.3114 0.0248 -0.0070 0.0295 234 TRP A O 1773 C CB . TRP A 234 ? 0.3980 0.3654 0.3221 0.0242 -0.0161 0.0276 234 TRP A CB 1774 C CG . TRP A 234 ? 0.4227 0.3836 0.3487 0.0200 -0.0176 0.0247 234 TRP A CG 1775 C CD1 . TRP A 234 ? 0.4430 0.3960 0.3684 0.0177 -0.0145 0.0250 234 TRP A CD1 1776 C CD2 . TRP A 234 ? 0.4459 0.4074 0.3744 0.0174 -0.0228 0.0208 234 TRP A CD2 1777 N NE1 . TRP A 234 ? 0.4617 0.4113 0.3891 0.0138 -0.0181 0.0216 234 TRP A NE1 1778 C CE2 . TRP A 234 ? 0.4489 0.4036 0.3786 0.0137 -0.0231 0.0192 234 TRP A CE2 1779 C CE3 . TRP A 234 ? 0.4619 0.4284 0.3915 0.0179 -0.0271 0.0186 234 TRP A CE3 1780 C CZ2 . TRP A 234 ? 0.4778 0.4320 0.4103 0.0110 -0.0279 0.0159 234 TRP A CZ2 1781 C CZ3 . TRP A 234 ? 0.4830 0.4479 0.4152 0.0155 -0.0313 0.0153 234 TRP A CZ3 1782 C CH2 . TRP A 234 ? 0.4896 0.4490 0.4235 0.0123 -0.0320 0.0142 234 TRP A CH2 1783 N N . THR A 235 ? 0.3766 0.3395 0.3000 0.0291 -0.0028 0.0351 235 THR A N 1784 C CA . THR A 235 ? 0.3937 0.3500 0.3170 0.0290 0.0033 0.0373 235 THR A CA 1785 C C . THR A 235 ? 0.4069 0.3563 0.3270 0.0293 0.0064 0.0393 235 THR A C 1786 O O . THR A 235 ? 0.4033 0.3558 0.3212 0.0328 0.0067 0.0420 235 THR A O 1787 C CB . THR A 235 ? 0.3965 0.3563 0.3185 0.0336 0.0079 0.0412 235 THR A CB 1788 O OG1 . THR A 235 ? 0.3862 0.3529 0.3099 0.0341 0.0051 0.0395 235 THR A OG1 1789 C CG2 . THR A 235 ? 0.4138 0.3658 0.3359 0.0330 0.0150 0.0433 235 THR A CG2 1790 N N . ILE A 236 ? 0.4140 0.3542 0.3339 0.0256 0.0089 0.0380 236 ILE A N 1791 C CA . ILE A 236 ? 0.4274 0.3590 0.3433 0.0257 0.0130 0.0397 236 ILE A CA 1792 C C . ILE A 236 ? 0.4358 0.3617 0.3501 0.0279 0.0208 0.0434 236 ILE A C 1793 O O . ILE A 236 ? 0.4639 0.3871 0.3804 0.0253 0.0228 0.0424 236 ILE A O 1794 C CB . ILE A 236 ? 0.4417 0.3651 0.3564 0.0199 0.0106 0.0356 236 ILE A CB 1795 C CG1 . ILE A 236 ? 0.4559 0.3838 0.3705 0.0187 0.0037 0.0328 236 ILE A CG1 1796 C CG2 . ILE A 236 ? 0.4600 0.3723 0.3694 0.0198 0.0162 0.0372 236 ILE A CG2 1797 C CD1 . ILE A 236 ? 0.4589 0.3809 0.3727 0.0131 -0.0005 0.0283 236 ILE A CD1 1798 N N . VAL A 237 ? 0.4427 0.3669 0.3537 0.0327 0.0253 0.0479 237 VAL A N 1799 C CA . VAL A 237 ? 0.4600 0.3782 0.3687 0.0358 0.0332 0.0522 237 VAL A CA 1800 C C . VAL A 237 ? 0.4853 0.3912 0.3896 0.0353 0.0386 0.0532 237 VAL A C 1801 O O . VAL A 237 ? 0.4806 0.3868 0.3831 0.0380 0.0388 0.0548 237 VAL A O 1802 C CB . VAL A 237 ? 0.4680 0.3943 0.3758 0.0430 0.0346 0.0575 237 VAL A CB 1803 C CG1 . VAL A 237 ? 0.4620 0.3811 0.3665 0.0467 0.0431 0.0625 237 VAL A CG1 1804 C CG2 . VAL A 237 ? 0.4604 0.3975 0.3710 0.0432 0.0296 0.0561 237 VAL A CG2 1805 N N . LYS A 238 ? 0.5078 0.4031 0.4106 0.0317 0.0433 0.0523 238 LYS A N 1806 C CA . LYS A 238 ? 0.5438 0.4251 0.4414 0.0304 0.0490 0.0525 238 LYS A CA 1807 C C . LYS A 238 ? 0.5507 0.4276 0.4447 0.0372 0.0571 0.0588 238 LYS A C 1808 O O . LYS A 238 ? 0.5546 0.4370 0.4497 0.0419 0.0591 0.0628 238 LYS A O 1809 C CB . LYS A 238 ? 0.5810 0.4523 0.4783 0.0236 0.0514 0.0491 238 LYS A CB 1810 C CG . LYS A 238 ? 0.6023 0.4783 0.5044 0.0170 0.0438 0.0434 238 LYS A CG 1811 C CD . LYS A 238 ? 0.5948 0.4698 0.4949 0.0138 0.0380 0.0395 238 LYS A CD 1812 C CE . LYS A 238 ? 0.6238 0.4839 0.5180 0.0088 0.0410 0.0370 238 LYS A CE 1813 N NZ . LYS A 238 ? 0.6204 0.4784 0.5105 0.0071 0.0364 0.0343 238 LYS A NZ 1814 N N . PRO A 239 ? 0.5624 0.4282 0.4513 0.0380 0.0621 0.0597 239 PRO A N 1815 C CA . PRO A 239 ? 0.5911 0.4497 0.4761 0.0443 0.0709 0.0657 239 PRO A CA 1816 C C . PRO A 239 ? 0.5935 0.4458 0.4775 0.0435 0.0765 0.0673 239 PRO A C 1817 O O . PRO A 239 ? 0.5766 0.4224 0.4608 0.0365 0.0764 0.0630 239 PRO A O 1818 C CB . PRO A 239 ? 0.6070 0.4513 0.4863 0.0422 0.0755 0.0642 239 PRO A CB 1819 C CG . PRO A 239 ? 0.5949 0.4441 0.4756 0.0379 0.0678 0.0592 239 PRO A CG 1820 C CD . PRO A 239 ? 0.5757 0.4337 0.4614 0.0329 0.0604 0.0553 239 PRO A CD 1821 N N . GLY A 240 ? 0.6223 0.4774 0.5056 0.0508 0.0808 0.0735 240 GLY A N 1822 C CA . GLY A 240 ? 0.6420 0.4907 0.5237 0.0508 0.0870 0.0759 240 GLY A CA 1823 C C . GLY A 240 ? 0.6235 0.4833 0.5099 0.0492 0.0823 0.0747 240 GLY A C 1824 O O . GLY A 240 ? 0.6396 0.4962 0.5250 0.0501 0.0873 0.0772 240 GLY A O 1825 N N . ASP A 241 ? 0.6113 0.4833 0.5026 0.0468 0.0734 0.0707 241 ASP A N 1826 C CA . ASP A 241 ? 0.5833 0.4661 0.4788 0.0459 0.0690 0.0696 241 ASP A CA 1827 C C . ASP A 241 ? 0.5760 0.4712 0.4711 0.0535 0.0660 0.0739 241 ASP A C 1828 O O . ASP A 241 ? 0.5573 0.4537 0.4502 0.0590 0.0668 0.0777 241 ASP A O 1829 C CB . ASP A 241 ? 0.5793 0.4673 0.4801 0.0388 0.0611 0.0627 241 ASP A CB 1830 C CG . ASP A 241 ? 0.5902 0.4829 0.4957 0.0353 0.0599 0.0604 241 ASP A CG 1831 O OD1 . ASP A 241 ? 0.6075 0.5036 0.5121 0.0395 0.0631 0.0642 241 ASP A OD1 1832 O OD2 . ASP A 241 ? 0.6028 0.4957 0.5127 0.0286 0.0559 0.0550 241 ASP A OD2 1833 N N . ILE A 242 ? 0.5536 0.4577 0.4508 0.0536 0.0629 0.0734 242 ILE A N 1834 C CA . ILE A 242 ? 0.5655 0.4809 0.4613 0.0601 0.0601 0.0772 242 ILE A CA 1835 C C . ILE A 242 ? 0.5368 0.4634 0.4367 0.0572 0.0523 0.0727 242 ILE A C 1836 O O . ILE A 242 ? 0.5609 0.4862 0.4639 0.0521 0.0522 0.0690 242 ILE A O 1837 C CB . ILE A 242 ? 0.5877 0.4996 0.4790 0.0646 0.0669 0.0826 242 ILE A CB 1838 C CG1 . ILE A 242 ? 0.6133 0.5125 0.4999 0.0680 0.0756 0.0875 242 ILE A CG1 1839 C CG2 . ILE A 242 ? 0.5923 0.5157 0.4809 0.0711 0.0633 0.0863 242 ILE A CG2 1840 C CD1 . ILE A 242 ? 0.6416 0.5337 0.5237 0.0706 0.0836 0.0920 242 ILE A CD1 1841 N N . LEU A 243 ? 0.5114 0.4488 0.4114 0.0602 0.0461 0.0730 243 LEU A N 1842 C CA . LEU A 243 ? 0.4753 0.4230 0.3777 0.0585 0.0393 0.0694 243 LEU A CA 1843 C C . LEU A 243 ? 0.5013 0.4535 0.3994 0.0632 0.0409 0.0731 243 LEU A C 1844 O O . LEU A 243 ? 0.5080 0.4618 0.4017 0.0694 0.0428 0.0786 243 LEU A O 1845 C CB . LEU A 243 ? 0.4556 0.4120 0.3594 0.0592 0.0322 0.0680 243 LEU A CB 1846 C CG . LEU A 243 ? 0.4476 0.4132 0.3536 0.0567 0.0247 0.0635 243 LEU A CG 1847 C CD1 . LEU A 243 ? 0.4298 0.3916 0.3403 0.0499 0.0226 0.0575 243 LEU A CD1 1848 C CD2 . LEU A 243 ? 0.4387 0.4131 0.3453 0.0583 0.0187 0.0634 243 LEU A CD2 1849 N N . LEU A 244 ? 0.4885 0.4426 0.3878 0.0607 0.0403 0.0702 244 LEU A N 1850 C CA . LEU A 244 ? 0.5180 0.4763 0.4123 0.0647 0.0415 0.0730 244 LEU A CA 1851 C C . LEU A 244 ? 0.5079 0.4751 0.4037 0.0627 0.0347 0.0684 244 LEU A C 1852 O O . LEU A 244 ? 0.5057 0.4727 0.4071 0.0575 0.0328 0.0632 244 LEU A O 1853 C CB . LEU A 244 ? 0.5382 0.4881 0.4313 0.0641 0.0498 0.0748 244 LEU A CB 1854 C CG . LEU A 244 ? 0.5577 0.5088 0.4440 0.0687 0.0534 0.0787 244 LEU A CG 1855 C CD1 . LEU A 244 ? 0.5852 0.5406 0.4640 0.0760 0.0520 0.0844 244 LEU A CD1 1856 C CD2 . LEU A 244 ? 0.5777 0.5182 0.4631 0.0678 0.0630 0.0811 244 LEU A CD2 1857 N N . ILE A 245 ? 0.4945 0.4697 0.3853 0.0670 0.0308 0.0702 245 ILE A N 1858 C CA . ILE A 245 ? 0.4809 0.4639 0.3713 0.0656 0.0245 0.0661 245 ILE A CA 1859 C C . ILE A 245 ? 0.5020 0.4864 0.3850 0.0692 0.0270 0.0683 245 ILE A C 1860 O O . ILE A 245 ? 0.5014 0.4867 0.3776 0.0746 0.0288 0.0737 245 ILE A O 1861 C CB . ILE A 245 ? 0.4799 0.4713 0.3701 0.0666 0.0170 0.0655 245 ILE A CB 1862 C CG1 . ILE A 245 ? 0.4766 0.4659 0.3734 0.0631 0.0151 0.0632 245 ILE A CG1 1863 C CG2 . ILE A 245 ? 0.4760 0.4744 0.3645 0.0652 0.0109 0.0612 245 ILE A CG2 1864 C CD1 . ILE A 245 ? 0.4770 0.4738 0.3746 0.0639 0.0090 0.0631 245 ILE A CD1 1865 N N . ASN A 246 ? 0.5051 0.4897 0.3893 0.0664 0.0271 0.0643 246 ASN A N 1866 C CA . ASN A 246 ? 0.5408 0.5248 0.4183 0.0690 0.0310 0.0658 246 ASN A CA 1867 C C . ASN A 246 ? 0.5346 0.5245 0.4110 0.0674 0.0254 0.0607 246 ASN A C 1868 O O . ASN A 246 ? 0.5423 0.5323 0.4259 0.0630 0.0237 0.0556 246 ASN A O 1869 C CB . ASN A 246 ? 0.5684 0.5447 0.4501 0.0667 0.0390 0.0660 246 ASN A CB 1870 C CG . ASN A 246 ? 0.6179 0.5913 0.4922 0.0699 0.0456 0.0690 246 ASN A CG 1871 O OD1 . ASN A 246 ? 0.6288 0.5977 0.5073 0.0674 0.0517 0.0681 246 ASN A OD1 1872 N ND2 . ASN A 246 ? 0.6634 0.6393 0.5269 0.0752 0.0446 0.0726 246 ASN A ND2 1873 N N . SER A 247 ? 0.5334 0.5280 0.4005 0.0710 0.0224 0.0620 247 SER A N 1874 C CA . SER A 247 ? 0.5261 0.5258 0.3908 0.0695 0.0166 0.0571 247 SER A CA 1875 C C . SER A 247 ? 0.5410 0.5431 0.3931 0.0736 0.0160 0.0591 247 SER A C 1876 O O . SER A 247 ? 0.5298 0.5325 0.3753 0.0780 0.0170 0.0646 247 SER A O 1877 C CB . SER A 247 ? 0.5283 0.5337 0.3970 0.0672 0.0084 0.0543 247 SER A CB 1878 O OG . SER A 247 ? 0.5309 0.5407 0.3960 0.0658 0.0028 0.0498 247 SER A OG 1879 N N . THR A 248 ? 0.5454 0.5485 0.3937 0.0723 0.0142 0.0546 248 THR A N 1880 C CA . THR A 248 ? 0.5827 0.5878 0.4178 0.0754 0.0125 0.0552 248 THR A CA 1881 C C . THR A 248 ? 0.5756 0.5862 0.4086 0.0728 0.0041 0.0499 248 THR A C 1882 O O . THR A 248 ? 0.5876 0.5990 0.4097 0.0740 0.0023 0.0483 248 THR A O 1883 C CB . THR A 248 ? 0.6105 0.6099 0.4403 0.0763 0.0196 0.0546 248 THR A CB 1884 O OG1 . THR A 248 ? 0.6277 0.6257 0.4666 0.0722 0.0204 0.0489 248 THR A OG1 1885 C CG2 . THR A 248 ? 0.6111 0.6046 0.4406 0.0791 0.0285 0.0604 248 THR A CG2 1886 N N . GLY A 249 ? 0.5407 0.5545 0.3832 0.0693 -0.0008 0.0470 249 GLY A N 1887 C CA . GLY A 249 ? 0.5181 0.5363 0.3598 0.0662 -0.0085 0.0419 249 GLY A CA 1888 C C . GLY A 249 ? 0.4939 0.5113 0.3471 0.0616 -0.0106 0.0377 249 GLY A C 1889 O O . GLY A 249 ? 0.4853 0.4987 0.3468 0.0607 -0.0062 0.0382 249 GLY A O 1890 N N . ASN A 250 ? 0.4790 0.5001 0.3325 0.0587 -0.0175 0.0337 250 ASN A N 1891 C CA . ASN A 250 ? 0.4692 0.4889 0.3316 0.0543 -0.0201 0.0292 250 ASN A CA 1892 C C . ASN A 250 ? 0.4502 0.4703 0.3222 0.0530 -0.0204 0.0313 250 ASN A C 1893 O O . ASN A 250 ? 0.4405 0.4584 0.3197 0.0497 -0.0218 0.0281 250 ASN A O 1894 C CB . ASN A 250 ? 0.4608 0.4746 0.3260 0.0533 -0.0159 0.0258 250 ASN A CB 1895 C CG . ASN A 250 ? 0.4692 0.4814 0.3245 0.0546 -0.0150 0.0232 250 ASN A CG 1896 O OD1 . ASN A 250 ? 0.4860 0.4971 0.3340 0.0579 -0.0106 0.0260 250 ASN A OD1 1897 N ND2 . ASN A 250 ? 0.4374 0.4485 0.2916 0.0519 -0.0187 0.0177 250 ASN A ND2 1898 N N . LEU A 251 ? 0.4443 0.4668 0.3157 0.0559 -0.0189 0.0367 251 LEU A N 1899 C CA . LEU A 251 ? 0.4396 0.4617 0.3188 0.0554 -0.0181 0.0392 251 LEU A CA 1900 C C . LEU A 251 ? 0.4357 0.4637 0.3171 0.0536 -0.0243 0.0384 251 LEU A C 1901 O O . LEU A 251 ? 0.4291 0.4638 0.3059 0.0555 -0.0277 0.0403 251 LEU A O 1902 C CB . LEU A 251 ? 0.4347 0.4557 0.3120 0.0598 -0.0128 0.0456 251 LEU A CB 1903 C CG . LEU A 251 ? 0.4424 0.4616 0.3267 0.0597 -0.0110 0.0485 251 LEU A CG 1904 C CD1 . LEU A 251 ? 0.4194 0.4318 0.3111 0.0558 -0.0084 0.0456 251 LEU A CD1 1905 C CD2 . LEU A 251 ? 0.4325 0.4505 0.3134 0.0648 -0.0058 0.0552 251 LEU A CD2 1906 N N . ILE A 252 ? 0.4129 0.4387 0.3013 0.0499 -0.0259 0.0357 252 ILE A N 1907 C CA . ILE A 252 ? 0.4122 0.4423 0.3043 0.0482 -0.0300 0.0358 252 ILE A CA 1908 C C . ILE A 252 ? 0.4080 0.4357 0.3048 0.0500 -0.0258 0.0402 252 ILE A C 1909 O O . ILE A 252 ? 0.3832 0.4043 0.2846 0.0479 -0.0233 0.0391 252 ILE A O 1910 C CB . ILE A 252 ? 0.4258 0.4536 0.3213 0.0432 -0.0338 0.0302 252 ILE A CB 1911 C CG1 . ILE A 252 ? 0.4374 0.4659 0.3275 0.0417 -0.0370 0.0257 252 ILE A CG1 1912 C CG2 . ILE A 252 ? 0.4167 0.4487 0.3161 0.0411 -0.0375 0.0303 252 ILE A CG2 1913 C CD1 . ILE A 252 ? 0.4347 0.4708 0.3185 0.0430 -0.0407 0.0265 252 ILE A CD1 1914 N N . ALA A 253 ? 0.3976 0.4303 0.2929 0.0540 -0.0251 0.0453 253 ALA A N 1915 C CA . ALA A 253 ? 0.4013 0.4307 0.2993 0.0568 -0.0198 0.0502 253 ALA A CA 1916 C C . ALA A 253 ? 0.3902 0.4200 0.2944 0.0551 -0.0208 0.0504 253 ALA A C 1917 O O . ALA A 253 ? 0.3694 0.4054 0.2756 0.0530 -0.0258 0.0485 253 ALA A O 1918 C CB . ALA A 253 ? 0.4101 0.4441 0.3034 0.0627 -0.0182 0.0561 253 ALA A CB 1919 N N . PRO A 254 ? 0.3987 0.4214 0.3056 0.0557 -0.0155 0.0526 254 PRO A N 1920 C CA . PRO A 254 ? 0.4012 0.4233 0.3128 0.0550 -0.0149 0.0537 254 PRO A CA 1921 C C . PRO A 254 ? 0.4072 0.4372 0.3194 0.0601 -0.0148 0.0592 254 PRO A C 1922 O O . PRO A 254 ? 0.4017 0.4344 0.3102 0.0648 -0.0131 0.0632 254 PRO A O 1923 C CB . PRO A 254 ? 0.4123 0.4232 0.3246 0.0546 -0.0087 0.0546 254 PRO A CB 1924 C CG . PRO A 254 ? 0.4193 0.4279 0.3275 0.0579 -0.0047 0.0573 254 PRO A CG 1925 C CD . PRO A 254 ? 0.4111 0.4257 0.3162 0.0574 -0.0091 0.0546 254 PRO A CD 1926 N N . ARG A 255 ? 0.3989 0.4329 0.3160 0.0592 -0.0164 0.0594 255 ARG A N 1927 C CA . ARG A 255 ? 0.4153 0.4576 0.3351 0.0642 -0.0159 0.0649 255 ARG A CA 1928 C C . ARG A 255 ? 0.4147 0.4498 0.3369 0.0668 -0.0092 0.0686 255 ARG A C 1929 O O . ARG A 255 ? 0.4171 0.4578 0.3424 0.0715 -0.0075 0.0736 255 ARG A O 1930 C CB . ARG A 255 ? 0.4115 0.4642 0.3361 0.0616 -0.0218 0.0630 255 ARG A CB 1931 C CG . ARG A 255 ? 0.4113 0.4719 0.3330 0.0595 -0.0286 0.0598 255 ARG A CG 1932 C CD . ARG A 255 ? 0.4180 0.4904 0.3449 0.0576 -0.0341 0.0590 255 ARG A CD 1933 N NE . ARG A 255 ? 0.4240 0.5024 0.3472 0.0548 -0.0406 0.0552 255 ARG A NE 1934 C CZ . ARG A 255 ? 0.4356 0.5231 0.3553 0.0578 -0.0441 0.0575 255 ARG A CZ 1935 N NH1 . ARG A 255 ? 0.4370 0.5294 0.3570 0.0643 -0.0420 0.0640 255 ARG A NH1 1936 N NH2 . ARG A 255 ? 0.4338 0.5250 0.3491 0.0544 -0.0498 0.0532 255 ARG A NH2 1937 N N . GLY A 256 ? 0.4032 0.4260 0.3240 0.0637 -0.0053 0.0661 256 GLY A N 1938 C CA . GLY A 256 ? 0.4017 0.4157 0.3239 0.0646 0.0008 0.0681 256 GLY A CA 1939 C C . GLY A 256 ? 0.3864 0.3890 0.3073 0.0588 0.0018 0.0631 256 GLY A C 1940 O O . GLY A 256 ? 0.3850 0.3862 0.3041 0.0553 -0.0010 0.0591 256 GLY A O 1941 N N . TYR A 257 ? 0.3878 0.3824 0.3095 0.0578 0.0058 0.0632 257 TYR A N 1942 C CA . TYR A 257 ? 0.4009 0.3840 0.3207 0.0523 0.0067 0.0587 257 TYR A CA 1943 C C . TYR A 257 ? 0.3908 0.3714 0.3119 0.0492 0.0059 0.0565 257 TYR A C 1944 O O . TYR A 257 ? 0.3972 0.3823 0.3211 0.0520 0.0074 0.0594 257 TYR A O 1945 C CB . TYR A 257 ? 0.4082 0.3794 0.3248 0.0535 0.0138 0.0607 257 TYR A CB 1946 C CG . TYR A 257 ? 0.4206 0.3883 0.3371 0.0579 0.0200 0.0654 257 TYR A CG 1947 C CD1 . TYR A 257 ? 0.4279 0.3874 0.3437 0.0556 0.0227 0.0640 257 TYR A CD1 1948 C CD2 . TYR A 257 ? 0.4365 0.4090 0.3534 0.0647 0.0232 0.0714 257 TYR A CD2 1949 C CE1 . TYR A 257 ? 0.4457 0.4014 0.3614 0.0600 0.0290 0.0683 257 TYR A CE1 1950 C CE2 . TYR A 257 ? 0.4495 0.4189 0.3668 0.0695 0.0292 0.0761 257 TYR A CE2 1951 C CZ . TYR A 257 ? 0.4555 0.4163 0.3724 0.0671 0.0323 0.0744 257 TYR A CZ 1952 O OH . TYR A 257 ? 0.4659 0.4228 0.3831 0.0719 0.0389 0.0788 257 TYR A OH 1953 N N . PHE A 258 ? 0.3805 0.3539 0.2999 0.0436 0.0038 0.0515 258 PHE A N 1954 C CA . PHE A 258 ? 0.3824 0.3500 0.3010 0.0404 0.0040 0.0494 258 PHE A CA 1955 C C . PHE A 258 ? 0.4261 0.3803 0.3407 0.0400 0.0103 0.0500 258 PHE A C 1956 O O . PHE A 258 ? 0.4245 0.3724 0.3369 0.0394 0.0123 0.0497 258 PHE A O 1957 C CB . PHE A 258 ? 0.3628 0.3290 0.2805 0.0347 -0.0019 0.0438 258 PHE A CB 1958 C CG . PHE A 258 ? 0.3441 0.3217 0.2648 0.0344 -0.0078 0.0426 258 PHE A CG 1959 C CD1 . PHE A 258 ? 0.3488 0.3323 0.2700 0.0352 -0.0107 0.0421 258 PHE A CD1 1960 C CD2 . PHE A 258 ? 0.3522 0.3344 0.2749 0.0332 -0.0098 0.0421 258 PHE A CD2 1961 C CE1 . PHE A 258 ? 0.3499 0.3427 0.2728 0.0346 -0.0160 0.0405 258 PHE A CE1 1962 C CE2 . PHE A 258 ? 0.3428 0.3351 0.2682 0.0323 -0.0151 0.0407 258 PHE A CE2 1963 C CZ . PHE A 258 ? 0.3525 0.3498 0.2775 0.0330 -0.0184 0.0398 258 PHE A CZ 1964 N N . LYS A 259 ? 0.4515 0.4013 0.3652 0.0403 0.0136 0.0509 259 LYS A N 1965 C CA . LYS A 259 ? 0.5184 0.4536 0.4267 0.0385 0.0188 0.0502 259 LYS A CA 1966 C C . LYS A 259 ? 0.5334 0.4621 0.4384 0.0320 0.0142 0.0446 259 LYS A C 1967 O O . LYS A 259 ? 0.5329 0.4673 0.4395 0.0293 0.0079 0.0416 259 LYS A O 1968 C CB . LYS A 259 ? 0.5699 0.5021 0.4777 0.0399 0.0230 0.0518 259 LYS A CB 1969 C CG . LYS A 259 ? 0.5999 0.5384 0.5117 0.0469 0.0281 0.0578 259 LYS A CG 1970 C CD . LYS A 259 ? 0.6566 0.5822 0.5639 0.0495 0.0369 0.0603 259 LYS A CD 1971 C CE . LYS A 259 ? 0.6870 0.6193 0.5990 0.0572 0.0421 0.0667 259 LYS A CE 1972 N NZ . LYS A 259 ? 0.7317 0.6509 0.6394 0.0597 0.0512 0.0688 259 LYS A NZ 1973 N N . ILE A 260 ? 0.5226 0.4395 0.4230 0.0295 0.0169 0.0431 260 ILE A N 1974 C CA . ILE A 260 ? 0.5255 0.4354 0.4223 0.0234 0.0127 0.0381 260 ILE A CA 1975 C C . ILE A 260 ? 0.5412 0.4365 0.4309 0.0213 0.0176 0.0373 260 ILE A C 1976 O O . ILE A 260 ? 0.5574 0.4453 0.4447 0.0229 0.0238 0.0392 260 ILE A O 1977 C CB . ILE A 260 ? 0.5381 0.4499 0.4372 0.0214 0.0095 0.0362 260 ILE A CB 1978 C CG1 . ILE A 260 ? 0.5568 0.4621 0.4531 0.0153 0.0047 0.0312 260 ILE A CG1 1979 C CG2 . ILE A 260 ? 0.5454 0.4528 0.4442 0.0235 0.0156 0.0388 260 ILE A CG2 1980 C CD1 . ILE A 260 ? 0.5520 0.4638 0.4530 0.0136 -0.0006 0.0289 260 ILE A CD1 1981 N N . ARG A 261 ? 0.5314 0.4220 0.4169 0.0181 0.0153 0.0346 261 ARG A N 1982 C CA . ARG A 261 ? 0.5582 0.4343 0.4353 0.0160 0.0198 0.0335 261 ARG A CA 1983 C C . ARG A 261 ? 0.5467 0.4145 0.4181 0.0096 0.0146 0.0285 261 ARG A C 1984 O O . ARG A 261 ? 0.5176 0.3921 0.3925 0.0074 0.0075 0.0263 261 ARG A O 1985 C CB . ARG A 261 ? 0.5899 0.4666 0.4659 0.0177 0.0221 0.0349 261 ARG A CB 1986 C CG . ARG A 261 ? 0.6308 0.5167 0.5133 0.0243 0.0271 0.0402 261 ARG A CG 1987 C CD . ARG A 261 ? 0.6858 0.5725 0.5684 0.0261 0.0305 0.0418 261 ARG A CD 1988 N NE . ARG A 261 ? 0.7185 0.6164 0.6091 0.0326 0.0342 0.0470 261 ARG A NE 1989 C CZ . ARG A 261 ? 0.7735 0.6676 0.6641 0.0375 0.0420 0.0510 261 ARG A CZ 1990 N NH1 . ARG A 261 ? 0.7883 0.6666 0.6707 0.0364 0.0474 0.0502 261 ARG A NH1 1991 N NH2 . ARG A 261 ? 0.7826 0.6886 0.6813 0.0437 0.0442 0.0560 261 ARG A NH2 1992 N N . SER A 262 ? 0.5773 0.4305 0.4399 0.0067 0.0180 0.0269 262 SER A N 1993 C CA . SER A 262 ? 0.5934 0.4383 0.4491 0.0006 0.0126 0.0222 262 SER A CA 1994 C C . SER A 262 ? 0.5840 0.4195 0.4307 -0.0004 0.0147 0.0214 262 SER A C 1995 O O . SER A 262 ? 0.5678 0.3976 0.4113 0.0023 0.0223 0.0238 262 SER A O 1996 C CB . SER A 262 ? 0.6352 0.4701 0.4868 -0.0032 0.0135 0.0200 262 SER A CB 1997 O OG . SER A 262 ? 0.6864 0.5092 0.5313 -0.0024 0.0220 0.0212 262 SER A OG 1998 N N . GLY A 263 ? 0.5508 0.3846 0.3935 -0.0041 0.0082 0.0184 263 GLY A N 1999 C CA . GLY A 263 ? 0.5570 0.3801 0.3895 -0.0059 0.0099 0.0173 263 GLY A CA 2000 C C . GLY A 263 ? 0.5363 0.3605 0.3662 -0.0093 0.0014 0.0144 263 GLY A C 2001 O O . GLY A 263 ? 0.5416 0.3702 0.3751 -0.0114 -0.0053 0.0124 263 GLY A O 2002 N N . LYS A 264 ? 0.4087 0.3916 0.3950 0.0162 0.0055 0.0523 264 LYS A N 2003 C CA . LYS A 264 ? 0.3929 0.3793 0.3844 0.0136 0.0037 0.0506 264 LYS A CA 2004 C C . LYS A 264 ? 0.3271 0.3232 0.3277 0.0116 0.0002 0.0510 264 LYS A C 2005 O O . LYS A 264 ? 0.3095 0.3091 0.3145 0.0104 -0.0011 0.0509 264 LYS A O 2006 C CB . LYS A 264 ? 0.4304 0.4154 0.4206 0.0169 0.0060 0.0528 264 LYS A CB 2007 C CG . LYS A 264 ? 0.4936 0.4672 0.4735 0.0183 0.0093 0.0519 264 LYS A CG 2008 C CD . LYS A 264 ? 0.5437 0.5158 0.5215 0.0226 0.0119 0.0545 264 LYS A CD 2009 C CE . LYS A 264 ? 0.5893 0.5492 0.5566 0.0227 0.0146 0.0527 264 LYS A CE 2010 N NZ . LYS A 264 ? 0.6116 0.5702 0.5773 0.0264 0.0169 0.0547 264 LYS A NZ 2011 N N . SER A 265 ? 0.2959 0.2957 0.2986 0.0110 -0.0011 0.0516 265 SER A N 2012 C CA . SER A 265 ? 0.2725 0.2808 0.2828 0.0091 -0.0045 0.0523 265 SER A CA 2013 C C . SER A 265 ? 0.2671 0.2752 0.2794 0.0047 -0.0073 0.0481 265 SER A C 2014 O O . SER A 265 ? 0.2545 0.2575 0.2627 0.0031 -0.0067 0.0447 265 SER A O 2015 C CB . SER A 265 ? 0.2794 0.2919 0.2910 0.0101 -0.0051 0.0546 265 SER A CB 2016 O OG . SER A 265 ? 0.2797 0.2935 0.2898 0.0147 -0.0026 0.0589 265 SER A OG 2017 N N . SER A 266 ? 0.2511 0.2649 0.2692 0.0030 -0.0103 0.0483 266 SER A N 2018 C CA . SER A 266 ? 0.2551 0.2689 0.2748 -0.0003 -0.0132 0.0445 266 SER A CA 2019 C C . SER A 266 ? 0.2460 0.2657 0.2709 -0.0020 -0.0167 0.0458 266 SER A C 2020 O O . SER A 266 ? 0.2404 0.2648 0.2675 -0.0009 -0.0169 0.0495 266 SER A O 2021 C CB . SER A 266 ? 0.2662 0.2770 0.2854 -0.0011 -0.0131 0.0423 266 SER A CB 2022 O OG . SER A 266 ? 0.2807 0.2908 0.3003 -0.0037 -0.0155 0.0383 266 SER A OG 2023 N N . ILE A 267 ? 0.2393 0.2587 0.2655 -0.0045 -0.0195 0.0426 267 ILE A N 2024 C CA . ILE A 267 ? 0.2360 0.2589 0.2654 -0.0066 -0.0232 0.0429 267 ILE A CA 2025 C C . ILE A 267 ? 0.2420 0.2629 0.2721 -0.0080 -0.0254 0.0405 267 ILE A C 2026 O O . ILE A 267 ? 0.2284 0.2457 0.2564 -0.0078 -0.0245 0.0373 267 ILE A O 2027 C CB . ILE A 267 ? 0.2426 0.2658 0.2711 -0.0079 -0.0246 0.0409 267 ILE A CB 2028 C CG1 . ILE A 267 ? 0.2478 0.2739 0.2788 -0.0101 -0.0285 0.0415 267 ILE A CG1 2029 C CG2 . ILE A 267 ? 0.2497 0.2691 0.2754 -0.0085 -0.0243 0.0361 267 ILE A CG2 2030 C CD1 . ILE A 267 ? 0.2509 0.2783 0.2812 -0.0111 -0.0295 0.0408 267 ILE A CD1 2031 N N . MET A 268 ? 0.2421 0.2654 0.2747 -0.0096 -0.0284 0.0423 268 MET A N 2032 C CA . MET A 268 ? 0.2554 0.2763 0.2881 -0.0109 -0.0307 0.0405 268 MET A CA 2033 C C . MET A 268 ? 0.2615 0.2831 0.2949 -0.0134 -0.0349 0.0407 268 MET A C 2034 O O . MET A 268 ? 0.2601 0.2858 0.2951 -0.0145 -0.0358 0.0440 268 MET A O 2035 C CB . MET A 268 ? 0.2585 0.2802 0.2925 -0.0103 -0.0297 0.0432 268 MET A CB 2036 C CG . MET A 268 ? 0.2698 0.2882 0.3034 -0.0113 -0.0316 0.0413 268 MET A CG 2037 S SD . MET A 268 ? 0.2861 0.3059 0.3211 -0.0107 -0.0301 0.0447 268 MET A SD 2038 C CE . MET A 268 ? 0.2730 0.2903 0.3058 -0.0077 -0.0252 0.0436 268 MET A CE 2039 N N . ARG A 269 ? 0.2596 0.2773 0.2913 -0.0142 -0.0374 0.0371 269 ARG A N 2040 C CA . ARG A 269 ? 0.2699 0.2861 0.3006 -0.0166 -0.0417 0.0370 269 ARG A CA 2041 C C . ARG A 269 ? 0.2715 0.2866 0.3027 -0.0180 -0.0434 0.0389 269 ARG A C 2042 O O . ARG A 269 ? 0.2630 0.2750 0.2934 -0.0169 -0.0429 0.0371 269 ARG A O 2043 C CB . ARG A 269 ? 0.2908 0.3027 0.3186 -0.0162 -0.0435 0.0322 269 ARG A CB 2044 C CG . ARG A 269 ? 0.2991 0.3123 0.3262 -0.0150 -0.0417 0.0299 269 ARG A CG 2045 C CD . ARG A 269 ? 0.3154 0.3255 0.3396 -0.0147 -0.0441 0.0256 269 ARG A CD 2046 N NE . ARG A 269 ? 0.3222 0.3342 0.3458 -0.0140 -0.0425 0.0236 269 ARG A NE 2047 C CZ . ARG A 269 ? 0.3364 0.3493 0.3595 -0.0124 -0.0398 0.0212 269 ARG A CZ 2048 N NH1 . ARG A 269 ? 0.3475 0.3595 0.3708 -0.0113 -0.0384 0.0204 269 ARG A NH1 2049 N NH2 . ARG A 269 ? 0.3436 0.3585 0.3658 -0.0123 -0.0386 0.0196 269 ARG A NH2 2050 N N . SER A 270 ? 0.2699 0.2878 0.3021 -0.0205 -0.0454 0.0427 270 SER A N 2051 C CA . SER A 270 ? 0.2864 0.3038 0.3187 -0.0226 -0.0474 0.0450 270 SER A CA 2052 C C . SER A 270 ? 0.3076 0.3269 0.3394 -0.0266 -0.0510 0.0482 270 SER A C 2053 O O . SER A 270 ? 0.3025 0.3269 0.3359 -0.0273 -0.0507 0.0506 270 SER A O 2054 C CB . SER A 270 ? 0.2809 0.3029 0.3162 -0.0212 -0.0441 0.0483 270 SER A CB 2055 O OG . SER A 270 ? 0.2888 0.3113 0.3244 -0.0236 -0.0461 0.0509 270 SER A OG 2056 N N . ASP A 271 ? 0.3247 0.3400 0.3540 -0.0294 -0.0545 0.0485 271 ASP A N 2057 C CA . ASP A 271 ? 0.3539 0.3713 0.3824 -0.0340 -0.0579 0.0524 271 ASP A CA 2058 C C . ASP A 271 ? 0.3530 0.3758 0.3840 -0.0359 -0.0576 0.0570 271 ASP A C 2059 O O . ASP A 271 ? 0.3427 0.3674 0.3727 -0.0405 -0.0607 0.0604 271 ASP A O 2060 C CB . ASP A 271 ? 0.3829 0.3913 0.4054 -0.0366 -0.0627 0.0497 271 ASP A CB 2061 C CG . ASP A 271 ? 0.4089 0.4140 0.4290 -0.0352 -0.0632 0.0460 271 ASP A CG 2062 O OD1 . ASP A 271 ? 0.4109 0.4218 0.4338 -0.0346 -0.0613 0.0472 271 ASP A OD1 2063 O OD2 . ASP A 271 ? 0.4457 0.4423 0.4609 -0.0344 -0.0654 0.0420 271 ASP A OD2 2064 N N . ALA A 272 ? 0.3332 0.3589 0.3672 -0.0327 -0.0538 0.0574 272 ALA A N 2065 C CA . ALA A 272 ? 0.3312 0.3624 0.3677 -0.0340 -0.0531 0.0617 272 ALA A CA 2066 C C . ALA A 272 ? 0.3233 0.3651 0.3633 -0.0352 -0.0523 0.0670 272 ALA A C 2067 O O . ALA A 272 ? 0.3126 0.3582 0.3546 -0.0326 -0.0498 0.0671 272 ALA A O 2068 C CB . ALA A 272 ? 0.3162 0.3471 0.3544 -0.0299 -0.0490 0.0605 272 ALA A CB 2069 N N . PRO A 273 ? 0.3347 0.3817 0.3753 -0.0393 -0.0544 0.0715 273 PRO A N 2070 C CA . PRO A 273 ? 0.3451 0.4040 0.3896 -0.0401 -0.0533 0.0768 273 PRO A CA 2071 C C . PRO A 273 ? 0.3345 0.4004 0.3833 -0.0347 -0.0480 0.0786 273 PRO A C 2072 O O . PRO A 273 ? 0.3239 0.3866 0.3726 -0.0320 -0.0457 0.0770 273 PRO A O 2073 C CB . PRO A 273 ? 0.3587 0.4215 0.4025 -0.0460 -0.0569 0.0810 273 PRO A CB 2074 C CG . PRO A 273 ? 0.3755 0.4297 0.4163 -0.0466 -0.0581 0.0784 273 PRO A CG 2075 C CD . PRO A 273 ? 0.3631 0.4061 0.4009 -0.0434 -0.0578 0.0721 273 PRO A CD 2076 N N . ILE A 274 ? 0.3426 0.4175 0.3944 -0.0330 -0.0460 0.0819 274 ILE A N 2077 C CA . ILE A 274 ? 0.3567 0.4381 0.4116 -0.0276 -0.0411 0.0841 274 ILE A CA 2078 C C . ILE A 274 ? 0.3826 0.4749 0.4404 -0.0292 -0.0410 0.0898 274 ILE A C 2079 O O . ILE A 274 ? 0.3832 0.4831 0.4422 -0.0334 -0.0437 0.0937 274 ILE A O 2080 C CB . ILE A 274 ? 0.3689 0.4539 0.4250 -0.0240 -0.0387 0.0846 274 ILE A CB 2081 C CG1 . ILE A 274 ? 0.3817 0.4559 0.4347 -0.0225 -0.0384 0.0787 274 ILE A CG1 2082 C CG2 . ILE A 274 ? 0.3697 0.4606 0.4278 -0.0182 -0.0337 0.0871 274 ILE A CG2 2083 C CD1 . ILE A 274 ? 0.4002 0.4768 0.4535 -0.0220 -0.0385 0.0790 274 ILE A CD1 2084 N N . GLY A 275 ? 0.3852 0.4782 0.4437 -0.0260 -0.0379 0.0902 275 GLY A N 2085 C CA . GLY A 275 ? 0.3919 0.4954 0.4530 -0.0270 -0.0374 0.0955 275 GLY A CA 2086 C C . GLY A 275 ? 0.3917 0.5038 0.4555 -0.0206 -0.0323 0.0986 275 GLY A C 2087 O O . GLY A 275 ? 0.3489 0.4559 0.4115 -0.0150 -0.0287 0.0959 275 GLY A O 2088 N N . LYS A 276 ? 0.3889 0.5140 0.4558 -0.0214 -0.0320 0.1042 276 LYS A N 2089 C CA . LYS A 276 ? 0.4131 0.5470 0.4822 -0.0148 -0.0272 0.1075 276 LYS A CA 2090 C C . LYS A 276 ? 0.4003 0.5310 0.4682 -0.0124 -0.0246 0.1066 276 LYS A C 2091 O O . LYS A 276 ? 0.3980 0.5362 0.4676 -0.0146 -0.0251 0.1101 276 LYS A O 2092 C CB . LYS A 276 ? 0.4646 0.6156 0.5377 -0.0164 -0.0280 0.1143 276 LYS A CB 2093 C CG . LYS A 276 ? 0.5082 0.6626 0.5822 -0.0187 -0.0304 0.1153 276 LYS A CG 2094 C CD . LYS A 276 ? 0.5520 0.7243 0.6302 -0.0177 -0.0297 0.1220 276 LYS A CD 2095 C CE . LYS A 276 ? 0.5720 0.7479 0.6510 -0.0217 -0.0331 0.1233 276 LYS A CE 2096 N NZ . LYS A 276 ? 0.6113 0.7786 0.6884 -0.0173 -0.0314 0.1195 276 LYS A NZ 2097 N N . CYS A 277 ? 0.3800 0.4990 0.4448 -0.0083 -0.0219 0.1019 277 CYS A N 2098 C CA . CYS A 277 ? 0.3715 0.4853 0.4344 -0.0061 -0.0195 0.1002 277 CYS A CA 2099 C C . CYS A 277 ? 0.3334 0.4375 0.3928 -0.0001 -0.0155 0.0964 277 CYS A C 2100 O O . CYS A 277 ? 0.3138 0.4156 0.3725 0.0017 -0.0150 0.0951 277 CYS A O 2101 C CB . CYS A 277 ? 0.4166 0.5223 0.4779 -0.0119 -0.0232 0.0973 277 CYS A CB 2102 S SG . CYS A 277 ? 0.4963 0.5893 0.5550 -0.0158 -0.0272 0.0915 277 CYS A SG 2103 N N . ASN A 278 ? 0.3040 0.4024 0.3609 0.0025 -0.0128 0.0947 278 ASN A N 2104 C CA . ASN A 278 ? 0.3057 0.3955 0.3585 0.0081 -0.0087 0.0917 278 ASN A CA 2105 C C . ASN A 278 ? 0.3073 0.3849 0.3568 0.0063 -0.0093 0.0866 278 ASN A C 2106 O O . ASN A 278 ? 0.2838 0.3614 0.3334 0.0051 -0.0093 0.0870 278 ASN A O 2107 C CB . ASN A 278 ? 0.3081 0.4039 0.3602 0.0142 -0.0042 0.0952 278 ASN A CB 2108 C CG . ASN A 278 ? 0.3225 0.4098 0.3693 0.0205 0.0000 0.0930 278 ASN A CG 2109 O OD1 . ASN A 278 ? 0.3430 0.4184 0.3857 0.0204 0.0007 0.0885 278 ASN A OD1 2110 N ND2 . ASN A 278 ? 0.3242 0.4176 0.3705 0.0262 0.0030 0.0964 278 ASN A ND2 2111 N N . SER A 279 ? 0.3050 0.3731 0.3519 0.0060 -0.0097 0.0821 279 SER A N 2112 C CA . SER A 279 ? 0.3218 0.3790 0.3654 0.0048 -0.0099 0.0774 279 SER A CA 2113 C C . SER A 279 ? 0.3156 0.3641 0.3552 0.0072 -0.0080 0.0735 279 SER A C 2114 O O . SER A 279 ? 0.2938 0.3427 0.3338 0.0069 -0.0090 0.0730 279 SER A O 2115 C CB . SER A 279 ? 0.3467 0.4021 0.3921 -0.0010 -0.0149 0.0755 279 SER A CB 2116 O OG . SER A 279 ? 0.3861 0.4319 0.4285 -0.0019 -0.0152 0.0710 279 SER A OG 2117 N N . GLU A 280 ? 0.3165 0.3571 0.3517 0.0093 -0.0054 0.0710 280 GLU A N 2118 C CA . GLU A 280 ? 0.3315 0.3638 0.3620 0.0112 -0.0033 0.0677 280 GLU A CA 2119 C C . GLU A 280 ? 0.3132 0.3402 0.3435 0.0075 -0.0063 0.0632 280 GLU A C 2120 O O . GLU A 280 ? 0.3108 0.3337 0.3385 0.0083 -0.0055 0.0612 280 GLU A O 2121 C CB . GLU A 280 ? 0.3648 0.3897 0.3897 0.0139 0.0002 0.0663 280 GLU A CB 2122 C CG . GLU A 280 ? 0.4174 0.4455 0.4406 0.0189 0.0039 0.0701 280 GLU A CG 2123 C CD . GLU A 280 ? 0.4578 0.4849 0.4775 0.0235 0.0068 0.0714 280 GLU A CD 2124 O OE1 . GLU A 280 ? 0.5033 0.5240 0.5199 0.0230 0.0068 0.0686 280 GLU A OE1 2125 O OE2 . GLU A 280 ? 0.4915 0.5244 0.5113 0.0279 0.0093 0.0754 280 GLU A OE2 2126 N N . CYS A 281 ? 0.3021 0.3288 0.3346 0.0037 -0.0096 0.0617 281 CYS A N 2127 C CA . CYS A 281 ? 0.2928 0.3141 0.3246 0.0008 -0.0123 0.0572 281 CYS A CA 2128 C C . CYS A 281 ? 0.2810 0.3062 0.3163 -0.0023 -0.0165 0.0576 281 CYS A C 2129 O O . CYS A 281 ? 0.2822 0.3115 0.3202 -0.0044 -0.0188 0.0598 281 CYS A O 2130 C CB . CYS A 281 ? 0.3094 0.3260 0.3398 -0.0006 -0.0129 0.0547 281 CYS A CB 2131 S SG . CYS A 281 ? 0.3235 0.3347 0.3529 -0.0033 -0.0159 0.0494 281 CYS A SG 2132 N N . ILE A 282 ? 0.2665 0.2903 0.3014 -0.0027 -0.0174 0.0554 282 ILE A N 2133 C CA . ILE A 282 ? 0.2619 0.2879 0.2991 -0.0057 -0.0214 0.0552 282 ILE A CA 2134 C C . ILE A 282 ? 0.2533 0.2735 0.2888 -0.0074 -0.0238 0.0503 282 ILE A C 2135 O O . ILE A 282 ? 0.2481 0.2643 0.2811 -0.0062 -0.0221 0.0473 282 ILE A O 2136 C CB . ILE A 282 ? 0.2593 0.2890 0.2972 -0.0046 -0.0208 0.0567 282 ILE A CB 2137 C CG1 . ILE A 282 ? 0.2703 0.3067 0.3099 -0.0023 -0.0185 0.0617 282 ILE A CG1 2138 C CG2 . ILE A 282 ? 0.2605 0.2919 0.3001 -0.0079 -0.0250 0.0563 282 ILE A CG2 2139 C CD1 . ILE A 282 ? 0.2747 0.3147 0.3145 -0.0003 -0.0173 0.0636 282 ILE A CD1 2140 N N . THR A 283 ? 0.2498 0.2696 0.2862 -0.0103 -0.0278 0.0498 283 THR A N 2141 C CA . THR A 283 ? 0.2453 0.2603 0.2801 -0.0115 -0.0304 0.0455 283 THR A CA 2142 C C . THR A 283 ? 0.2504 0.2670 0.2861 -0.0139 -0.0342 0.0462 283 THR A C 2143 O O . THR A 283 ? 0.2465 0.2678 0.2841 -0.0153 -0.0350 0.0502 283 THR A O 2144 C CB . THR A 283 ? 0.2507 0.2616 0.2844 -0.0124 -0.0321 0.0437 283 THR A CB 2145 O OG1 . THR A 283 ? 0.2482 0.2599 0.2827 -0.0150 -0.0356 0.0458 283 THR A OG1 2146 C CG2 . THR A 283 ? 0.2516 0.2619 0.2847 -0.0107 -0.0287 0.0443 283 THR A CG2 2147 N N . PRO A 284 ? 0.2535 0.2664 0.2874 -0.0145 -0.0365 0.0426 284 PRO A N 2148 C CA . PRO A 284 ? 0.2668 0.2796 0.3002 -0.0169 -0.0404 0.0429 284 PRO A CA 2149 C C . PRO A 284 ? 0.2799 0.2919 0.3130 -0.0199 -0.0438 0.0452 284 PRO A C 2150 O O . PRO A 284 ? 0.2763 0.2896 0.3090 -0.0227 -0.0467 0.0471 284 PRO A O 2151 C CB . PRO A 284 ? 0.2700 0.2779 0.3007 -0.0162 -0.0420 0.0380 284 PRO A CB 2152 C CG . PRO A 284 ? 0.2652 0.2732 0.2959 -0.0136 -0.0382 0.0358 284 PRO A CG 2153 C CD . PRO A 284 ? 0.2640 0.2731 0.2958 -0.0128 -0.0356 0.0380 284 PRO A CD 2154 N N . ASN A 285 ? 0.2860 0.2958 0.3186 -0.0198 -0.0436 0.0451 285 ASN A N 2155 C CA . ASN A 285 ? 0.3142 0.3230 0.3461 -0.0229 -0.0468 0.0474 285 ASN A CA 2156 C C . ASN A 285 ? 0.3064 0.3225 0.3413 -0.0241 -0.0454 0.0526 285 ASN A C 2157 O O . ASN A 285 ? 0.3248 0.3415 0.3593 -0.0273 -0.0480 0.0553 285 ASN A O 2158 C CB . ASN A 285 ? 0.3384 0.3424 0.3687 -0.0223 -0.0471 0.0455 285 ASN A CB 2159 C CG . ASN A 285 ? 0.3614 0.3595 0.3890 -0.0201 -0.0478 0.0404 285 ASN A CG 2160 O OD1 . ASN A 285 ? 0.3422 0.3412 0.3704 -0.0175 -0.0450 0.0380 285 ASN A OD1 2161 N ND2 . ASN A 285 ? 0.4589 0.4511 0.4832 -0.0212 -0.0515 0.0388 285 ASN A ND2 2162 N N . GLY A 286 ? 0.2909 0.3125 0.3284 -0.0216 -0.0414 0.0543 286 GLY A N 2163 C CA . GLY A 286 ? 0.2858 0.3149 0.3263 -0.0216 -0.0394 0.0591 286 GLY A CA 2164 C C . GLY A 286 ? 0.2909 0.3207 0.3320 -0.0177 -0.0347 0.0590 286 GLY A C 2165 O O . GLY A 286 ? 0.2756 0.2997 0.3147 -0.0157 -0.0333 0.0552 286 GLY A O 2166 N N . SER A 287 ? 0.2881 0.3248 0.3314 -0.0166 -0.0323 0.0633 287 SER A N 2167 C CA . SER A 287 ? 0.2938 0.3306 0.3368 -0.0128 -0.0279 0.0636 287 SER A CA 2168 C C . SER A 287 ? 0.2982 0.3311 0.3400 -0.0139 -0.0285 0.0625 287 SER A C 2169 O O . SER A 287 ? 0.2930 0.3262 0.3351 -0.0174 -0.0319 0.0636 287 SER A O 2170 C CB . SER A 287 ? 0.3002 0.3458 0.3455 -0.0108 -0.0252 0.0685 287 SER A CB 2171 O OG . SER A 287 ? 0.3120 0.3609 0.3582 -0.0093 -0.0244 0.0694 287 SER A OG 2172 N N . ILE A 288 ? 0.2903 0.3190 0.3302 -0.0111 -0.0254 0.0604 288 ILE A N 2173 C CA . ILE A 288 ? 0.3066 0.3321 0.3454 -0.0118 -0.0255 0.0596 288 ILE A CA 2174 C C . ILE A 288 ? 0.3134 0.3404 0.3515 -0.0086 -0.0210 0.0614 288 ILE A C 2175 O O . ILE A 288 ? 0.3311 0.3578 0.3680 -0.0053 -0.0176 0.0612 288 ILE A O 2176 C CB . ILE A 288 ? 0.2975 0.3148 0.3337 -0.0122 -0.0268 0.0545 288 ILE A CB 2177 C CG1 . ILE A 288 ? 0.3005 0.3146 0.3346 -0.0093 -0.0234 0.0518 288 ILE A CG1 2178 C CG2 . ILE A 288 ? 0.3075 0.3227 0.3436 -0.0148 -0.0313 0.0526 288 ILE A CG2 2179 C CD1 . ILE A 288 ? 0.3049 0.3127 0.3365 -0.0095 -0.0242 0.0472 288 ILE A CD1 2180 N N . PRO A 289 ? 0.3259 0.3540 0.3643 -0.0094 -0.0209 0.0631 289 PRO A N 2181 C CA . PRO A 289 ? 0.3384 0.3665 0.3751 -0.0063 -0.0167 0.0641 289 PRO A CA 2182 C C . PRO A 289 ? 0.3346 0.3547 0.3675 -0.0042 -0.0144 0.0600 289 PRO A C 2183 O O . PRO A 289 ? 0.3217 0.3366 0.3536 -0.0060 -0.0166 0.0564 289 PRO A O 2184 C CB . PRO A 289 ? 0.3409 0.3698 0.3781 -0.0086 -0.0181 0.0655 289 PRO A CB 2185 C CG . PRO A 289 ? 0.3629 0.3940 0.4023 -0.0129 -0.0229 0.0665 289 PRO A CG 2186 C CD . PRO A 289 ? 0.3447 0.3731 0.3840 -0.0135 -0.0249 0.0639 289 PRO A CD 2187 N N . ASN A 290 ? 0.3286 0.3477 0.3588 -0.0006 -0.0100 0.0608 290 ASN A N 2188 C CA . ASN A 290 ? 0.3377 0.3490 0.3633 0.0007 -0.0078 0.0572 290 ASN A CA 2189 C C . ASN A 290 ? 0.3410 0.3486 0.3631 0.0020 -0.0049 0.0572 290 ASN A C 2190 O O . ASN A 290 ? 0.3726 0.3742 0.3899 0.0038 -0.0021 0.0553 290 ASN A O 2191 C CB . ASN A 290 ? 0.3449 0.3552 0.3684 0.0034 -0.0054 0.0570 290 ASN A CB 2192 C CG . ASN A 290 ? 0.3554 0.3686 0.3775 0.0076 -0.0016 0.0606 290 ASN A CG 2193 O OD1 . ASN A 290 ? 0.3509 0.3688 0.3745 0.0085 -0.0008 0.0637 290 ASN A OD1 2194 N ND2 . ASN A 290 ? 0.3431 0.3538 0.3620 0.0104 0.0007 0.0604 290 ASN A ND2 2195 N N . ASP A 291 ? 0.3332 0.3439 0.3572 0.0008 -0.0059 0.0592 291 ASP A N 2196 C CA . ASP A 291 ? 0.3493 0.3565 0.3701 0.0017 -0.0036 0.0590 291 ASP A CA 2197 C C . ASP A 291 ? 0.3380 0.3377 0.3559 -0.0003 -0.0047 0.0547 291 ASP A C 2198 O O . ASP A 291 ? 0.3597 0.3539 0.3728 0.0008 -0.0018 0.0534 291 ASP A O 2199 C CB . ASP A 291 ? 0.3629 0.3760 0.3865 0.0007 -0.0043 0.0625 291 ASP A CB 2200 C CG . ASP A 291 ? 0.3952 0.4108 0.4228 -0.0036 -0.0093 0.0624 291 ASP A CG 2201 O OD1 . ASP A 291 ? 0.4178 0.4375 0.4484 -0.0050 -0.0118 0.0634 291 ASP A OD1 2202 O OD2 . ASP A 291 ? 0.4454 0.4580 0.4723 -0.0059 -0.0109 0.0613 291 ASP A OD2 2203 N N . LYS A 292 ? 0.3036 0.3030 0.3240 -0.0033 -0.0086 0.0525 292 LYS A N 2204 C CA . LYS A 292 ? 0.2858 0.2797 0.3041 -0.0051 -0.0100 0.0488 292 LYS A CA 2205 C C . LYS A 292 ? 0.2677 0.2576 0.2829 -0.0045 -0.0087 0.0456 292 LYS A C 2206 O O . LYS A 292 ? 0.2671 0.2585 0.2830 -0.0034 -0.0083 0.0459 292 LYS A O 2207 C CB . LYS A 292 ? 0.2862 0.2812 0.3076 -0.0080 -0.0147 0.0479 292 LYS A CB 2208 C CG . LYS A 292 ? 0.2970 0.2955 0.3207 -0.0094 -0.0163 0.0510 292 LYS A CG 2209 C CD . LYS A 292 ? 0.3019 0.3002 0.3276 -0.0123 -0.0212 0.0503 292 LYS A CD 2210 C CE . LYS A 292 ? 0.3278 0.3293 0.3551 -0.0144 -0.0230 0.0537 292 LYS A CE 2211 N NZ . LYS A 292 ? 0.3368 0.3452 0.3666 -0.0141 -0.0221 0.0578 292 LYS A NZ 2212 N N . PRO A 293 ? 0.2601 0.2451 0.2719 -0.0054 -0.0082 0.0428 293 PRO A N 2213 C CA . PRO A 293 ? 0.2556 0.2373 0.2641 -0.0054 -0.0070 0.0400 293 PRO A CA 2214 C C . PRO A 293 ? 0.2486 0.2322 0.2597 -0.0068 -0.0103 0.0374 293 PRO A C 2215 O O . PRO A 293 ? 0.2458 0.2284 0.2551 -0.0067 -0.0094 0.0357 293 PRO A O 2216 C CB . PRO A 293 ? 0.2608 0.2376 0.2646 -0.0065 -0.0056 0.0382 293 PRO A CB 2217 C CG . PRO A 293 ? 0.2597 0.2379 0.2660 -0.0077 -0.0078 0.0387 293 PRO A CG 2218 C CD . PRO A 293 ? 0.2591 0.2416 0.2691 -0.0066 -0.0082 0.0423 293 PRO A CD 2219 N N . PHE A 294 ? 0.2355 0.2213 0.2502 -0.0080 -0.0139 0.0371 294 PHE A N 2220 C CA . PHE A 294 ? 0.2330 0.2199 0.2496 -0.0089 -0.0173 0.0345 294 PHE A CA 2221 C C . PHE A 294 ? 0.2301 0.2200 0.2506 -0.0093 -0.0204 0.0362 294 PHE A C 2222 O O . PHE A 294 ? 0.2226 0.2140 0.2446 -0.0095 -0.0206 0.0393 294 PHE A O 2223 C CB . PHE A 294 ? 0.2397 0.2249 0.2553 -0.0101 -0.0191 0.0318 294 PHE A CB 2224 C CG . PHE A 294 ? 0.2431 0.2256 0.2546 -0.0105 -0.0163 0.0304 294 PHE A CG 2225 C CD1 . PHE A 294 ? 0.2459 0.2278 0.2548 -0.0106 -0.0146 0.0286 294 PHE A CD1 2226 C CD2 . PHE A 294 ? 0.2536 0.2340 0.2634 -0.0111 -0.0155 0.0310 294 PHE A CD2 2227 C CE1 . PHE A 294 ? 0.2579 0.2368 0.2620 -0.0116 -0.0121 0.0275 294 PHE A CE1 2228 C CE2 . PHE A 294 ? 0.2561 0.2334 0.2613 -0.0119 -0.0130 0.0298 294 PHE A CE2 2229 C CZ . PHE A 294 ? 0.2512 0.2277 0.2534 -0.0123 -0.0114 0.0281 294 PHE A CZ 2230 N N . GLN A 295 ? 0.2296 0.2202 0.2512 -0.0096 -0.0229 0.0342 295 GLN A N 2231 C CA . GLN A 295 ? 0.2304 0.2227 0.2546 -0.0104 -0.0263 0.0354 295 GLN A CA 2232 C C . GLN A 295 ? 0.2357 0.2267 0.2595 -0.0105 -0.0295 0.0320 295 GLN A C 2233 O O . GLN A 295 ? 0.2362 0.2271 0.2588 -0.0097 -0.0286 0.0292 295 GLN A O 2234 C CB . GLN A 295 ? 0.2291 0.2248 0.2549 -0.0099 -0.0251 0.0381 295 GLN A CB 2235 C CG . GLN A 295 ? 0.2224 0.2184 0.2472 -0.0087 -0.0232 0.0365 295 GLN A CG 2236 C CD . GLN A 295 ? 0.2265 0.2233 0.2523 -0.0092 -0.0261 0.0347 295 GLN A CD 2237 O OE1 . GLN A 295 ? 0.2331 0.2298 0.2601 -0.0103 -0.0297 0.0347 295 GLN A OE1 2238 N NE2 . GLN A 295 ? 0.2168 0.2141 0.2417 -0.0084 -0.0244 0.0331 295 GLN A NE2 2239 N N . ASN A 296 ? 0.2430 0.2331 0.2675 -0.0115 -0.0334 0.0324 296 ASN A N 2240 C CA A ASN A 296 ? 0.2445 0.2327 0.2680 -0.0111 -0.0368 0.0294 296 ASN A CA 2241 C CA B ASN A 296 ? 0.2534 0.2417 0.2769 -0.0110 -0.0366 0.0293 296 ASN A CA 2242 C C . ASN A 296 ? 0.2528 0.2414 0.2770 -0.0120 -0.0393 0.0306 296 ASN A C 2243 O O . ASN A 296 ? 0.2710 0.2567 0.2936 -0.0121 -0.0429 0.0289 296 ASN A O 2244 C CB A ASN A 296 ? 0.2429 0.2275 0.2649 -0.0114 -0.0395 0.0286 296 ASN A CB 2245 C CB B ASN A 296 ? 0.2635 0.2484 0.2853 -0.0109 -0.0393 0.0276 296 ASN A CB 2246 C CG A ASN A 296 ? 0.2404 0.2225 0.2604 -0.0100 -0.0427 0.0251 296 ASN A CG 2247 C CG B ASN A 296 ? 0.2760 0.2582 0.2974 -0.0126 -0.0426 0.0298 296 ASN A CG 2248 O OD1 A ASN A 296 ? 0.2428 0.2210 0.2611 -0.0105 -0.0463 0.0251 296 ASN A OD1 2249 O OD1 B ASN A 296 ? 0.2931 0.2770 0.3158 -0.0143 -0.0420 0.0334 296 ASN A OD1 2250 N ND2 A ASN A 296 ? 0.2350 0.2191 0.2548 -0.0084 -0.0414 0.0221 296 ASN A ND2 2251 N ND2 B ASN A 296 ? 0.2884 0.2663 0.3072 -0.0122 -0.0462 0.0279 296 ASN A ND2 2252 N N . VAL A 297 ? 0.2502 0.2421 0.2763 -0.0127 -0.0375 0.0336 297 VAL A N 2253 C CA . VAL A 297 ? 0.2493 0.2423 0.2761 -0.0141 -0.0399 0.0352 297 VAL A CA 2254 C C . VAL A 297 ? 0.2471 0.2404 0.2734 -0.0130 -0.0402 0.0326 297 VAL A C 2255 O O . VAL A 297 ? 0.2413 0.2321 0.2661 -0.0136 -0.0436 0.0313 297 VAL A O 2256 C CB . VAL A 297 ? 0.2532 0.2509 0.2824 -0.0151 -0.0380 0.0397 297 VAL A CB 2257 C CG1 . VAL A 297 ? 0.2593 0.2592 0.2893 -0.0167 -0.0403 0.0414 297 VAL A CG1 2258 C CG2 . VAL A 297 ? 0.2538 0.2516 0.2833 -0.0165 -0.0384 0.0425 297 VAL A CG2 2259 N N . ASN A 298 ? 0.2371 0.2327 0.2640 -0.0115 -0.0368 0.0317 298 ASN A N 2260 C CA . ASN A 298 ? 0.2362 0.2327 0.2627 -0.0108 -0.0368 0.0293 298 ASN A CA 2261 C C . ASN A 298 ? 0.2378 0.2355 0.2637 -0.0094 -0.0331 0.0278 298 ASN A C 2262 O O . ASN A 298 ? 0.2286 0.2273 0.2548 -0.0091 -0.0299 0.0298 298 ASN A O 2263 C CB . ASN A 298 ? 0.2422 0.2412 0.2701 -0.0118 -0.0375 0.0320 298 ASN A CB 2264 C CG . ASN A 298 ? 0.2480 0.2466 0.2749 -0.0117 -0.0393 0.0295 298 ASN A CG 2265 O OD1 . ASN A 298 ? 0.2500 0.2493 0.2763 -0.0103 -0.0377 0.0269 298 ASN A OD1 2266 N ND2 . ASN A 298 ? 0.2503 0.2475 0.2766 -0.0133 -0.0429 0.0304 298 ASN A ND2 2267 N N . ARG A 299 ? 0.2387 0.2363 0.2633 -0.0086 -0.0336 0.0242 299 ARG A N 2268 C CA . ARG A 299 ? 0.2570 0.2561 0.2806 -0.0081 -0.0304 0.0227 299 ARG A CA 2269 C C . ARG A 299 ? 0.2442 0.2451 0.2682 -0.0082 -0.0283 0.0245 299 ARG A C 2270 O O . ARG A 299 ? 0.2340 0.2350 0.2564 -0.0080 -0.0252 0.0244 299 ARG A O 2271 C CB . ARG A 299 ? 0.2836 0.2836 0.3058 -0.0074 -0.0315 0.0187 299 ARG A CB 2272 C CG . ARG A 299 ? 0.3254 0.3263 0.3477 -0.0070 -0.0338 0.0172 299 ARG A CG 2273 C CD . ARG A 299 ? 0.3832 0.3857 0.4041 -0.0057 -0.0347 0.0131 299 ARG A CD 2274 N NE . ARG A 299 ? 0.3932 0.3939 0.4134 -0.0045 -0.0369 0.0117 299 ARG A NE 2275 C CZ . ARG A 299 ? 0.4282 0.4310 0.4472 -0.0030 -0.0374 0.0085 299 ARG A CZ 2276 N NH1 . ARG A 299 ? 0.4271 0.4344 0.4456 -0.0029 -0.0358 0.0064 299 ARG A NH1 2277 N NH2 . ARG A 299 ? 0.4438 0.4448 0.4620 -0.0016 -0.0396 0.0075 299 ARG A NH2 2278 N N . ILE A 300 ? 0.2364 0.2384 0.2619 -0.0086 -0.0301 0.0263 300 ILE A N 2279 C CA . ILE A 300 ? 0.2372 0.2414 0.2635 -0.0086 -0.0283 0.0285 300 ILE A CA 2280 C C . ILE A 300 ? 0.2459 0.2510 0.2733 -0.0083 -0.0265 0.0326 300 ILE A C 2281 O O . ILE A 300 ? 0.2308 0.2367 0.2599 -0.0091 -0.0283 0.0349 300 ILE A O 2282 C CB . ILE A 300 ? 0.2429 0.2484 0.2701 -0.0093 -0.0312 0.0286 300 ILE A CB 2283 C CG1 . ILE A 300 ? 0.2454 0.2502 0.2710 -0.0090 -0.0328 0.0243 300 ILE A CG1 2284 C CG2 . ILE A 300 ? 0.2277 0.2360 0.2558 -0.0092 -0.0294 0.0313 300 ILE A CG2 2285 C CD1 . ILE A 300 ? 0.2557 0.2601 0.2814 -0.0097 -0.0364 0.0238 300 ILE A CD1 2286 N N . THR A 301 ? 0.2523 0.2573 0.2782 -0.0071 -0.0228 0.0337 301 THR A N 2287 C CA . THR A 301 ? 0.2649 0.2709 0.2914 -0.0060 -0.0206 0.0376 301 THR A CA 2288 C C . THR A 301 ? 0.2639 0.2706 0.2889 -0.0044 -0.0176 0.0393 301 THR A C 2289 O O . THR A 301 ? 0.2810 0.2860 0.3036 -0.0044 -0.0167 0.0371 301 THR A O 2290 C CB . THR A 301 ? 0.2831 0.2864 0.3079 -0.0055 -0.0187 0.0376 301 THR A CB 2291 O OG1 . THR A 301 ? 0.3147 0.3145 0.3354 -0.0048 -0.0157 0.0358 301 THR A OG1 2292 C CG2 . THR A 301 ? 0.2951 0.2970 0.3205 -0.0069 -0.0214 0.0355 301 THR A CG2 2293 N N . TYR A 302 ? 0.2543 0.2636 0.2804 -0.0029 -0.0162 0.0432 302 TYR A N 2294 C CA . TYR A 302 ? 0.2511 0.2607 0.2753 -0.0005 -0.0131 0.0455 302 TYR A CA 2295 C C . TYR A 302 ? 0.2492 0.2595 0.2730 0.0017 -0.0105 0.0487 302 TYR A C 2296 O O . TYR A 302 ? 0.2565 0.2709 0.2835 0.0013 -0.0117 0.0511 302 TYR A O 2297 C CB . TYR A 302 ? 0.2550 0.2696 0.2820 -0.0007 -0.0145 0.0474 302 TYR A CB 2298 C CG . TYR A 302 ? 0.2534 0.2681 0.2780 0.0022 -0.0114 0.0498 302 TYR A CG 2299 C CD1 . TYR A 302 ? 0.2674 0.2859 0.2930 0.0049 -0.0096 0.0540 302 TYR A CD1 2300 C CD2 . TYR A 302 ? 0.2619 0.2729 0.2829 0.0025 -0.0101 0.0477 302 TYR A CD2 2301 C CE1 . TYR A 302 ? 0.2663 0.2845 0.2892 0.0083 -0.0066 0.0562 302 TYR A CE1 2302 C CE2 . TYR A 302 ? 0.2709 0.2809 0.2888 0.0054 -0.0073 0.0499 302 TYR A CE2 2303 C CZ . TYR A 302 ? 0.2694 0.2828 0.2882 0.0085 -0.0056 0.0541 302 TYR A CZ 2304 O OH . TYR A 302 ? 0.2869 0.2988 0.3020 0.0121 -0.0027 0.0562 302 TYR A OH 2305 N N . GLY A 303 ? 0.2541 0.2599 0.2730 0.0041 -0.0068 0.0488 303 GLY A N 2306 C CA . GLY A 303 ? 0.2664 0.2723 0.2838 0.0072 -0.0039 0.0520 303 GLY A CA 2307 C C . GLY A 303 ? 0.2819 0.2826 0.2961 0.0069 -0.0025 0.0503 303 GLY A C 2308 O O . GLY A 303 ? 0.2768 0.2729 0.2887 0.0047 -0.0032 0.0467 303 GLY A O 2309 N N . ALA A 304 ? 0.2863 0.2881 0.3002 0.0091 -0.0007 0.0531 304 ALA A N 2310 C CA . ALA A 304 ? 0.3004 0.2971 0.3109 0.0090 0.0008 0.0518 304 ALA A CA 2311 C C . ALA A 304 ? 0.3027 0.3020 0.3175 0.0058 -0.0024 0.0508 304 ALA A C 2312 O O . ALA A 304 ? 0.3128 0.3172 0.3314 0.0058 -0.0033 0.0534 304 ALA A O 2313 C CB . ALA A 304 ? 0.3109 0.3077 0.3189 0.0130 0.0042 0.0552 304 ALA A CB 2314 N N . CYS A 305 ? 0.3064 0.3024 0.3206 0.0030 -0.0042 0.0469 305 CYS A N 2315 C CA . CYS A 305 ? 0.3064 0.3046 0.3245 0.0001 -0.0079 0.0455 305 CYS A CA 2316 C C . CYS A 305 ? 0.2862 0.2797 0.3018 -0.0012 -0.0079 0.0428 305 CYS A C 2317 O O . CYS A 305 ? 0.2782 0.2670 0.2892 -0.0013 -0.0060 0.0407 305 CYS A O 2318 C CB . CYS A 305 ? 0.3196 0.3190 0.3397 -0.0016 -0.0109 0.0432 305 CYS A CB 2319 S SG . CYS A 305 ? 0.3499 0.3558 0.3743 -0.0012 -0.0124 0.0464 305 CYS A SG 2320 N N . PRO A 306 ? 0.2606 0.2557 0.2789 -0.0027 -0.0102 0.0431 306 PRO A N 2321 C CA . PRO A 306 ? 0.2602 0.2517 0.2766 -0.0042 -0.0109 0.0402 306 PRO A CA 2322 C C . PRO A 306 ? 0.2516 0.2420 0.2675 -0.0056 -0.0126 0.0364 306 PRO A C 2323 O O . PRO A 306 ? 0.2477 0.2405 0.2657 -0.0058 -0.0144 0.0360 306 PRO A O 2324 C CB . PRO A 306 ? 0.2608 0.2545 0.2806 -0.0055 -0.0138 0.0413 306 PRO A CB 2325 C CG . PRO A 306 ? 0.2653 0.2638 0.2880 -0.0046 -0.0135 0.0455 306 PRO A CG 2326 C CD . PRO A 306 ? 0.2632 0.2633 0.2860 -0.0034 -0.0126 0.0458 306 PRO A CD 2327 N N . ARG A 307 ? 0.2528 0.2402 0.2658 -0.0066 -0.0122 0.0337 307 ARG A N 2328 C CA . ARG A 307 ? 0.2464 0.2341 0.2589 -0.0078 -0.0138 0.0302 307 ARG A CA 2329 C C . ARG A 307 ? 0.2286 0.2185 0.2446 -0.0085 -0.0178 0.0288 307 ARG A C 2330 O O . ARG A 307 ? 0.2237 0.2130 0.2406 -0.0089 -0.0191 0.0293 307 ARG A O 2331 C CB . ARG A 307 ? 0.2537 0.2381 0.2616 -0.0090 -0.0119 0.0281 307 ARG A CB 2332 C CG . ARG A 307 ? 0.2752 0.2558 0.2779 -0.0085 -0.0081 0.0290 307 ARG A CG 2333 C CD . ARG A 307 ? 0.2774 0.2550 0.2749 -0.0106 -0.0068 0.0265 307 ARG A CD 2334 N NE . ARG A 307 ? 0.2859 0.2586 0.2771 -0.0106 -0.0036 0.0271 307 ARG A NE 2335 C CZ . ARG A 307 ? 0.2807 0.2537 0.2705 -0.0110 -0.0032 0.0263 307 ARG A CZ 2336 N NH1 . ARG A 307 ? 0.2749 0.2530 0.2691 -0.0114 -0.0057 0.0249 307 ARG A NH1 2337 N NH2 . ARG A 307 ? 0.3034 0.2707 0.2865 -0.0111 -0.0003 0.0269 307 ARG A NH2 2338 N N . TYR A 308 ? 0.2215 0.2133 0.2387 -0.0086 -0.0198 0.0268 308 TYR A N 2339 C CA . TYR A 308 ? 0.2256 0.2185 0.2449 -0.0088 -0.0237 0.0251 308 TYR A CA 2340 C C . TYR A 308 ? 0.2252 0.2176 0.2431 -0.0091 -0.0246 0.0223 308 TYR A C 2341 O O . TYR A 308 ? 0.2313 0.2245 0.2470 -0.0095 -0.0230 0.0202 308 TYR A O 2342 C CB . TYR A 308 ? 0.2275 0.2224 0.2479 -0.0085 -0.0254 0.0236 308 TYR A CB 2343 C CG . TYR A 308 ? 0.2356 0.2304 0.2571 -0.0082 -0.0295 0.0220 308 TYR A CG 2344 C CD1 . TYR A 308 ? 0.2416 0.2354 0.2646 -0.0086 -0.0320 0.0242 308 TYR A CD1 2345 C CD2 . TYR A 308 ? 0.2434 0.2390 0.2640 -0.0075 -0.0309 0.0186 308 TYR A CD2 2346 C CE1 . TYR A 308 ? 0.2538 0.2460 0.2766 -0.0083 -0.0359 0.0227 308 TYR A CE1 2347 C CE2 . TYR A 308 ? 0.2605 0.2550 0.2811 -0.0066 -0.0346 0.0171 308 TYR A CE2 2348 C CZ . TYR A 308 ? 0.2629 0.2549 0.2842 -0.0070 -0.0371 0.0192 308 TYR A CZ 2349 O OH . TYR A 308 ? 0.2831 0.2725 0.3032 -0.0062 -0.0409 0.0177 308 TYR A OH 2350 N N . VAL A 309 ? 0.2269 0.2182 0.2457 -0.0090 -0.0270 0.0224 309 VAL A N 2351 C CA . VAL A 309 ? 0.2246 0.2159 0.2425 -0.0088 -0.0284 0.0200 309 VAL A CA 2352 C C . VAL A 309 ? 0.2444 0.2349 0.2632 -0.0078 -0.0326 0.0189 309 VAL A C 2353 O O . VAL A 309 ? 0.2380 0.2271 0.2579 -0.0080 -0.0345 0.0207 309 VAL A O 2354 C CB . VAL A 309 ? 0.2163 0.2055 0.2329 -0.0097 -0.0269 0.0213 309 VAL A CB 2355 C CG1 . VAL A 309 ? 0.2151 0.2037 0.2292 -0.0105 -0.0227 0.0220 309 VAL A CG1 2356 C CG2 . VAL A 309 ? 0.2172 0.2045 0.2352 -0.0099 -0.0281 0.0242 309 VAL A CG2 2357 N N . LYS A 310 ? 0.2525 0.2438 0.2703 -0.0068 -0.0342 0.0162 310 LYS A N 2358 C CA . LYS A 310 ? 0.2780 0.2675 0.2955 -0.0053 -0.0382 0.0150 310 LYS A CA 2359 C C . LYS A 310 ? 0.2807 0.2662 0.2978 -0.0058 -0.0401 0.0167 310 LYS A C 2360 O O . LYS A 310 ? 0.2801 0.2623 0.2963 -0.0051 -0.0435 0.0167 310 LYS A O 2361 C CB . LYS A 310 ? 0.3152 0.3076 0.3316 -0.0033 -0.0392 0.0115 310 LYS A CB 2362 C CG . LYS A 310 ? 0.3480 0.3445 0.3647 -0.0028 -0.0381 0.0097 310 LYS A CG 2363 C CD . LYS A 310 ? 0.3969 0.3978 0.4128 -0.0006 -0.0392 0.0063 310 LYS A CD 2364 C CE . LYS A 310 ? 0.4317 0.4353 0.4470 -0.0014 -0.0377 0.0059 310 LYS A CE 2365 N NZ . LYS A 310 ? 0.4992 0.5094 0.5140 0.0001 -0.0380 0.0030 310 LYS A NZ 2366 N N . GLN A 311 ? 0.2664 0.2516 0.2834 -0.0071 -0.0380 0.0182 311 GLN A N 2367 C CA . GLN A 311 ? 0.2741 0.2559 0.2905 -0.0078 -0.0397 0.0199 311 GLN A CA 2368 C C . GLN A 311 ? 0.2927 0.2724 0.3101 -0.0092 -0.0407 0.0230 311 GLN A C 2369 O O . GLN A 311 ? 0.2777 0.2594 0.2965 -0.0099 -0.0386 0.0247 311 GLN A O 2370 C CB . GLN A 311 ? 0.2676 0.2499 0.2836 -0.0090 -0.0368 0.0209 311 GLN A CB 2371 C CG . GLN A 311 ? 0.2603 0.2449 0.2750 -0.0083 -0.0360 0.0182 311 GLN A CG 2372 C CD . GLN A 311 ? 0.2540 0.2417 0.2683 -0.0090 -0.0325 0.0174 311 GLN A CD 2373 O OE1 . GLN A 311 ? 0.2423 0.2311 0.2574 -0.0089 -0.0317 0.0175 311 GLN A OE1 2374 N NE2 . GLN A 311 ? 0.2421 0.2311 0.2547 -0.0100 -0.0306 0.0166 311 GLN A NE2 2375 N N . ASN A 312 ? 0.3065 0.2824 0.3227 -0.0097 -0.0441 0.0239 312 ASN A N 2376 C CA . ASN A 312 ? 0.3401 0.3149 0.3570 -0.0118 -0.0451 0.0273 312 ASN A CA 2377 C C . ASN A 312 ? 0.3216 0.2966 0.3392 -0.0137 -0.0435 0.0304 312 ASN A C 2378 O O . ASN A 312 ? 0.3251 0.3011 0.3437 -0.0155 -0.0436 0.0336 312 ASN A O 2379 C CB . ASN A 312 ? 0.3846 0.3546 0.3991 -0.0122 -0.0499 0.0270 312 ASN A CB 2380 C CG . ASN A 312 ? 0.4321 0.3974 0.4436 -0.0114 -0.0528 0.0257 312 ASN A CG 2381 O OD1 . ASN A 312 ? 0.4742 0.4399 0.4858 -0.0113 -0.0515 0.0258 312 ASN A OD1 2382 N ND2 . ASN A 312 ? 0.5151 0.4752 0.5232 -0.0106 -0.0570 0.0244 312 ASN A ND2 2383 N N . THR A 313 ? 0.3029 0.2779 0.3198 -0.0131 -0.0419 0.0294 313 THR A N 2384 C CA . THR A 313 ? 0.3061 0.2813 0.3231 -0.0146 -0.0399 0.0319 313 THR A CA 2385 C C . THR A 313 ? 0.3007 0.2767 0.3169 -0.0138 -0.0369 0.0303 313 THR A C 2386 O O . THR A 313 ? 0.2996 0.2751 0.3146 -0.0126 -0.0380 0.0273 313 THR A O 2387 C CB . THR A 313 ? 0.3290 0.3006 0.3446 -0.0161 -0.0433 0.0334 313 THR A CB 2388 O OG1 . THR A 313 ? 0.3423 0.3147 0.3581 -0.0174 -0.0411 0.0357 313 THR A OG1 2389 C CG2 . THR A 313 ? 0.3372 0.3050 0.3503 -0.0147 -0.0464 0.0304 313 THR A CG2 2390 N N . LEU A 314 ? 0.2877 0.2651 0.3041 -0.0144 -0.0332 0.0322 314 LEU A N 2391 C CA . LEU A 314 ? 0.2822 0.2591 0.2967 -0.0144 -0.0305 0.0313 314 LEU A CA 2392 C C . LEU A 314 ? 0.2851 0.2616 0.2992 -0.0155 -0.0285 0.0345 314 LEU A C 2393 O O . LEU A 314 ? 0.2829 0.2611 0.2977 -0.0152 -0.0259 0.0367 314 LEU A O 2394 C CB . LEU A 314 ? 0.2784 0.2568 0.2920 -0.0136 -0.0272 0.0299 314 LEU A CB 2395 C CG . LEU A 314 ? 0.2801 0.2599 0.2936 -0.0127 -0.0285 0.0265 314 LEU A CG 2396 C CD1 . LEU A 314 ? 0.2785 0.2596 0.2911 -0.0126 -0.0252 0.0259 314 LEU A CD1 2397 C CD2 . LEU A 314 ? 0.2847 0.2643 0.2966 -0.0128 -0.0297 0.0242 314 LEU A CD2 2398 N N . LYS A 315 ? 0.2748 0.2493 0.2877 -0.0164 -0.0295 0.0347 315 LYS A N 2399 C CA . LYS A 315 ? 0.2929 0.2674 0.3054 -0.0174 -0.0278 0.0377 315 LYS A CA 2400 C C . LYS A 315 ? 0.2830 0.2563 0.2927 -0.0173 -0.0239 0.0373 315 LYS A C 2401 O O . LYS A 315 ? 0.2739 0.2455 0.2816 -0.0177 -0.0243 0.0352 315 LYS A O 2402 C CB . LYS A 315 ? 0.3264 0.2989 0.3386 -0.0190 -0.0313 0.0386 315 LYS A CB 2403 C CG . LYS A 315 ? 0.3738 0.3460 0.3875 -0.0197 -0.0353 0.0395 315 LYS A CG 2404 C CD . LYS A 315 ? 0.4154 0.3910 0.4310 -0.0206 -0.0342 0.0431 315 LYS A CD 2405 C CE . LYS A 315 ? 0.4689 0.4445 0.4843 -0.0230 -0.0356 0.0462 315 LYS A CE 2406 N NZ . LYS A 315 ? 0.5310 0.5119 0.5483 -0.0234 -0.0328 0.0500 315 LYS A NZ 2407 N N . LEU A 316 ? 0.2828 0.2569 0.2918 -0.0167 -0.0203 0.0396 316 LEU A N 2408 C CA . LEU A 316 ? 0.2753 0.2471 0.2805 -0.0165 -0.0164 0.0396 316 LEU A CA 2409 C C . LEU A 316 ? 0.2807 0.2521 0.2852 -0.0174 -0.0161 0.0419 316 LEU A C 2410 O O . LEU A 316 ? 0.2728 0.2470 0.2793 -0.0172 -0.0160 0.0449 316 LEU A O 2411 C CB . LEU A 316 ? 0.2825 0.2549 0.2866 -0.0146 -0.0126 0.0409 316 LEU A CB 2412 C CG . LEU A 316 ? 0.2905 0.2591 0.2891 -0.0140 -0.0083 0.0408 316 LEU A CG 2413 C CD1 . LEU A 316 ? 0.2908 0.2565 0.2862 -0.0150 -0.0080 0.0375 316 LEU A CD1 2414 C CD2 . LEU A 316 ? 0.3029 0.2722 0.3005 -0.0114 -0.0048 0.0431 316 LEU A CD2 2415 N N . ALA A 317 ? 0.2777 0.2462 0.2794 -0.0186 -0.0159 0.0407 317 ALA A N 2416 C CA . ALA A 317 ? 0.2884 0.2559 0.2885 -0.0195 -0.0151 0.0427 317 ALA A CA 2417 C C . ALA A 317 ? 0.2914 0.2592 0.2895 -0.0179 -0.0106 0.0451 317 ALA A C 2418 O O . ALA A 317 ? 0.2940 0.2595 0.2887 -0.0166 -0.0073 0.0442 317 ALA A O 2419 C CB . ALA A 317 ? 0.2843 0.2485 0.2810 -0.0209 -0.0152 0.0406 317 ALA A CB 2420 N N . THR A 318 ? 0.2883 0.2590 0.2881 -0.0180 -0.0106 0.0483 318 THR A N 2421 C CA . THR A 318 ? 0.2967 0.2684 0.2944 -0.0161 -0.0064 0.0509 318 THR A CA 2422 C C . THR A 318 ? 0.3101 0.2813 0.3061 -0.0174 -0.0059 0.0525 318 THR A C 2423 O O . THR A 318 ? 0.3387 0.3125 0.3341 -0.0160 -0.0033 0.0553 318 THR A O 2424 C CB . THR A 318 ? 0.2991 0.2768 0.3007 -0.0146 -0.0062 0.0537 318 THR A CB 2425 O OG1 . THR A 318 ? 0.3049 0.2865 0.3107 -0.0170 -0.0102 0.0554 318 THR A OG1 2426 C CG2 . THR A 318 ? 0.3037 0.2815 0.3065 -0.0132 -0.0064 0.0521 318 THR A CG2 2427 N N . GLY A 319 ? 0.3063 0.2745 0.3013 -0.0198 -0.0084 0.0507 319 GLY A N 2428 C CA . GLY A 319 ? 0.3151 0.2821 0.3080 -0.0212 -0.0080 0.0519 319 GLY A CA 2429 C C . GLY A 319 ? 0.3143 0.2768 0.3048 -0.0232 -0.0099 0.0490 319 GLY A C 2430 O O . GLY A 319 ? 0.3267 0.2879 0.3177 -0.0234 -0.0116 0.0463 319 GLY A O 2431 N N . MET A 320 ? 0.3138 0.2745 0.3017 -0.0247 -0.0095 0.0497 320 MET A N 2432 C CA . MET A 320 ? 0.3118 0.2687 0.2971 -0.0266 -0.0111 0.0473 320 MET A CA 2433 C C . MET A 320 ? 0.3116 0.2695 0.3003 -0.0283 -0.0163 0.0466 320 MET A C 2434 O O . MET A 320 ? 0.3267 0.2873 0.3192 -0.0284 -0.0189 0.0481 320 MET A O 2435 C CB . MET A 320 ? 0.3167 0.2710 0.2976 -0.0276 -0.0088 0.0485 320 MET A CB 2436 C CG . MET A 320 ? 0.3200 0.2772 0.3032 -0.0288 -0.0103 0.0514 320 MET A CG 2437 S SD . MET A 320 ? 0.3410 0.2954 0.3188 -0.0299 -0.0073 0.0526 320 MET A SD 2438 C CE . MET A 320 ? 0.3135 0.2687 0.2886 -0.0263 -0.0016 0.0544 320 MET A CE 2439 N N . ARG A 321 ? 0.3189 0.2743 0.3057 -0.0297 -0.0179 0.0445 321 ARG A N 2440 C CA . ARG A 321 ? 0.3375 0.2928 0.3262 -0.0308 -0.0228 0.0438 321 ARG A CA 2441 C C . ARG A 321 ? 0.3475 0.3033 0.3371 -0.0323 -0.0244 0.0468 321 ARG A C 2442 O O . ARG A 321 ? 0.3268 0.2823 0.3142 -0.0331 -0.0218 0.0486 321 ARG A O 2443 C CB . ARG A 321 ? 0.3605 0.3138 0.3465 -0.0319 -0.0238 0.0416 321 ARG A CB 2444 C CG . ARG A 321 ? 0.4005 0.3515 0.3826 -0.0337 -0.0217 0.0427 321 ARG A CG 2445 C CD . ARG A 321 ? 0.4398 0.3894 0.4193 -0.0351 -0.0230 0.0407 321 ARG A CD 2446 N NE . ARG A 321 ? 0.4447 0.3942 0.4218 -0.0350 -0.0210 0.0383 321 ARG A NE 2447 C CZ . ARG A 321 ? 0.4528 0.4046 0.4314 -0.0345 -0.0232 0.0360 321 ARG A CZ 2448 N NH1 . ARG A 321 ? 0.4743 0.4280 0.4565 -0.0333 -0.0274 0.0355 321 ARG A NH1 2449 N NH2 . ARG A 321 ? 0.4674 0.4194 0.4433 -0.0351 -0.0211 0.0342 321 ARG A NH2 2450 N N . ASN A 322 ? 0.3461 0.3024 0.3383 -0.0327 -0.0287 0.0473 322 ASN A N 2451 C CA . ASN A 322 ? 0.3705 0.3270 0.3632 -0.0347 -0.0310 0.0502 322 ASN A CA 2452 C C . ASN A 322 ? 0.3834 0.3363 0.3742 -0.0362 -0.0347 0.0493 322 ASN A C 2453 O O . ASN A 322 ? 0.3703 0.3213 0.3613 -0.0354 -0.0380 0.0472 322 ASN A O 2454 C CB . ASN A 322 ? 0.3655 0.3237 0.3612 -0.0348 -0.0337 0.0514 322 ASN A CB 2455 C CG . ASN A 322 ? 0.3788 0.3387 0.3748 -0.0374 -0.0348 0.0551 322 ASN A CG 2456 O OD1 . ASN A 322 ? 0.3625 0.3249 0.3578 -0.0380 -0.0316 0.0574 322 ASN A OD1 2457 N ND2 . ASN A 322 ? 0.3844 0.3428 0.3808 -0.0390 -0.0394 0.0559 322 ASN A ND2 2458 N N . VAL A 323 ? 0.4177 0.3697 0.4063 -0.0382 -0.0339 0.0510 323 VAL A N 2459 C CA . VAL A 323 ? 0.4346 0.3833 0.4208 -0.0395 -0.0367 0.0502 323 VAL A CA 2460 C C . VAL A 323 ? 0.4712 0.4190 0.4566 -0.0422 -0.0389 0.0534 323 VAL A C 2461 O O . VAL A 323 ? 0.4605 0.4106 0.4454 -0.0435 -0.0360 0.0558 323 VAL A O 2462 C CB . VAL A 323 ? 0.4517 0.3996 0.4350 -0.0396 -0.0335 0.0490 323 VAL A CB 2463 C CG1 . VAL A 323 ? 0.4656 0.4106 0.4466 -0.0408 -0.0367 0.0481 323 VAL A CG1 2464 C CG2 . VAL A 323 ? 0.4435 0.3923 0.4269 -0.0375 -0.0311 0.0462 323 VAL A CG2 2465 N N . PRO A 324 ? 0.5242 0.4687 0.5089 -0.0432 -0.0440 0.0534 324 PRO A N 2466 C CA . PRO A 324 ? 0.5448 0.4877 0.5279 -0.0464 -0.0467 0.0564 324 PRO A CA 2467 C C . PRO A 324 ? 0.5540 0.4970 0.5348 -0.0483 -0.0446 0.0577 324 PRO A C 2468 O O . PRO A 324 ? 0.5619 0.5041 0.5413 -0.0473 -0.0428 0.0558 324 PRO A O 2469 C CB . PRO A 324 ? 0.5515 0.4886 0.5324 -0.0463 -0.0524 0.0551 324 PRO A CB 2470 C CG . PRO A 324 ? 0.5697 0.5067 0.5521 -0.0427 -0.0529 0.0518 324 PRO A CG 2471 C CD . PRO A 324 ? 0.5433 0.4848 0.5276 -0.0411 -0.0476 0.0505 324 PRO A CD 2472 N N . GLU A 325 ? 0.5967 0.5413 0.5770 -0.0512 -0.0446 0.0611 325 GLU A N 2473 C CA . GLU A 325 ? 0.6388 0.5832 0.6165 -0.0533 -0.0432 0.0626 325 GLU A CA 2474 C C . GLU A 325 ? 0.7100 0.6486 0.6847 -0.0550 -0.0481 0.0621 325 GLU A C 2475 O O . GLU A 325 ? 0.7303 0.6658 0.7040 -0.0566 -0.0526 0.0632 325 GLU A O 2476 C CB . GLU A 325 ? 0.6276 0.5767 0.6060 -0.0558 -0.0415 0.0665 325 GLU A CB 2477 C CG . GLU A 325 ? 0.6278 0.5775 0.6035 -0.0576 -0.0392 0.0680 325 GLU A CG 2478 C CD . GLU A 325 ? 0.6057 0.5621 0.5825 -0.0577 -0.0345 0.0708 325 GLU A CD 2479 O OE1 . GLU A 325 ? 0.5864 0.5477 0.5661 -0.0574 -0.0341 0.0726 325 GLU A OE1 2480 O OE2 . GLU A 325 ? 0.5911 0.5479 0.5655 -0.0578 -0.0312 0.0713 325 GLU A OE2 2481 N N . LYS A 326 ? 0.7910 0.7276 0.7634 -0.0547 -0.0473 0.0606 326 LYS A N 2482 C CA . LYS A 326 ? 0.8689 0.8002 0.8382 -0.0558 -0.0517 0.0602 326 LYS A CA 2483 C C . LYS A 326 ? 0.9206 0.8508 0.8876 -0.0599 -0.0536 0.0637 326 LYS A C 2484 O O . LYS A 326 ? 0.8662 0.8004 0.8336 -0.0617 -0.0502 0.0660 326 LYS A O 2485 C CB . LYS A 326 ? 0.8846 0.8153 0.8523 -0.0547 -0.0502 0.0579 326 LYS A CB 2486 C CG . LYS A 326 ? 0.9199 0.8523 0.8858 -0.0567 -0.0461 0.0593 326 LYS A CG 2487 C CD . LYS A 326 ? 0.9429 0.8741 0.9065 -0.0562 -0.0452 0.0571 326 LYS A CD 2488 C CE . LYS A 326 ? 0.9457 0.8777 0.9067 -0.0581 -0.0410 0.0582 326 LYS A CE 2489 N NZ . LYS A 326 ? 0.9043 0.8361 0.8639 -0.0611 -0.0416 0.0615 326 LYS A NZ 2490 N N . GLN A 327 ? 1.0225 0.9470 0.9866 -0.0611 -0.0590 0.0640 327 GLN A N 2491 C CA . GLN A 327 ? 1.1108 1.0331 1.0721 -0.0655 -0.0618 0.0674 327 GLN A CA 2492 C C . GLN A 327 ? 1.1405 1.0624 1.0991 -0.0678 -0.0607 0.0685 327 GLN A C 2493 O O . GLN A 327 ? 1.1374 1.0579 1.0950 -0.0661 -0.0601 0.0664 327 GLN A O 2494 C CB . GLN A 327 ? 1.1476 1.0622 1.1054 -0.0659 -0.0683 0.0672 327 GLN A CB 2495 C CG . GLN A 327 ? 1.1824 1.0945 1.1371 -0.0709 -0.0716 0.0709 327 GLN A CG 2496 C CD . GLN A 327 ? 1.2029 1.1058 1.1529 -0.0711 -0.0780 0.0706 327 GLN A CD 2497 O OE1 . GLN A 327 ? 1.2135 1.1151 1.1631 -0.0724 -0.0801 0.0716 327 GLN A OE1 2498 N NE2 . GLN A 327 ? 1.2066 1.1028 1.1526 -0.0698 -0.0813 0.0692 327 GLN A NE2 2499 N N . THR A 328 ? 1.2116 1.1354 1.1690 -0.0718 -0.0605 0.0720 328 THR A N 2500 C CA . THR A 328 ? 1.2535 1.1774 1.2083 -0.0745 -0.0594 0.0735 328 THR A CA 2501 C C . THR A 328 ? 1.2579 1.1740 1.2081 -0.0756 -0.0646 0.0731 328 THR A C 2502 O O . THR A 328 ? 1.2324 1.1468 1.1816 -0.0737 -0.0642 0.0709 328 THR A O 2503 C CB . THR A 328 ? 1.2702 1.1987 1.2248 -0.0788 -0.0584 0.0777 328 THR A CB 2504 O OG1 . THR A 328 ? 1.2749 1.2045 1.2272 -0.0808 -0.0562 0.0789 328 THR A OG1 2505 C CG2 . THR A 328 ? 1.2503 1.1744 1.2021 -0.0825 -0.0642 0.0800 328 THR A CG2 2506 N N . ALA A 334 ? 0.6948 0.6349 0.6433 -0.0771 -0.0357 0.0775 334 ALA A N 2507 C CA . ALA A 334 ? 0.6571 0.5955 0.6041 -0.0741 -0.0316 0.0746 334 ALA A CA 2508 C C . ALA A 334 ? 0.6384 0.5785 0.5887 -0.0703 -0.0297 0.0726 334 ALA A C 2509 O O . ALA A 334 ? 0.6637 0.6017 0.6163 -0.0692 -0.0330 0.0709 334 ALA A O 2510 C CB . ALA A 334 ? 0.6767 0.6092 0.6210 -0.0749 -0.0345 0.0722 334 ALA A CB 2511 N N . ILE A 335 ? 0.5760 0.5194 0.5261 -0.0679 -0.0242 0.0729 335 ILE A N 2512 C CA . ILE A 335 ? 0.5102 0.4553 0.4629 -0.0642 -0.0218 0.0714 335 ILE A CA 2513 C C . ILE A 335 ? 0.4896 0.4299 0.4414 -0.0626 -0.0223 0.0675 335 ILE A C 2514 O O . ILE A 335 ? 0.4792 0.4154 0.4277 -0.0641 -0.0233 0.0662 335 ILE A O 2515 C CB . ILE A 335 ? 0.4954 0.4444 0.4469 -0.0617 -0.0157 0.0726 335 ILE A CB 2516 C CG1 . ILE A 335 ? 0.4923 0.4377 0.4377 -0.0619 -0.0120 0.0718 335 ILE A CG1 2517 C CG2 . ILE A 335 ? 0.5033 0.4595 0.4572 -0.0630 -0.0155 0.0765 335 ILE A CG2 2518 C CD1 . ILE A 335 ? 0.4904 0.4373 0.4331 -0.0582 -0.0057 0.0720 335 ILE A CD1 2519 N N . ALA A 336 ? 0.4573 0.3985 0.4120 -0.0598 -0.0218 0.0660 336 ALA A N 2520 C CA . ALA A 336 ? 0.4530 0.3908 0.4072 -0.0585 -0.0225 0.0625 336 ALA A CA 2521 C C . ALA A 336 ? 0.4342 0.3736 0.3898 -0.0552 -0.0190 0.0613 336 ALA A C 2522 O O . ALA A 336 ? 0.4219 0.3652 0.3804 -0.0538 -0.0178 0.0630 336 ALA A O 2523 C CB . ALA A 336 ? 0.4604 0.3970 0.4174 -0.0592 -0.0284 0.0616 336 ALA A CB 2524 N N . GLY A 337 ? 0.4329 0.3692 0.3860 -0.0542 -0.0175 0.0585 337 GLY A N 2525 C CA . GLY A 337 ? 0.4222 0.3585 0.3749 -0.0513 -0.0138 0.0571 337 GLY A CA 2526 C C . GLY A 337 ? 0.4180 0.3553 0.3748 -0.0500 -0.0165 0.0551 337 GLY A C 2527 O O . GLY A 337 ? 0.4122 0.3505 0.3724 -0.0507 -0.0212 0.0551 337 GLY A O 2528 N N . PHE A 338 ? 0.4066 0.3429 0.3622 -0.0480 -0.0136 0.0533 338 PHE A N 2529 C CA . PHE A 338 ? 0.4251 0.3632 0.3847 -0.0462 -0.0154 0.0516 338 PHE A CA 2530 C C . PHE A 338 ? 0.4282 0.3659 0.3891 -0.0472 -0.0196 0.0493 338 PHE A C 2531 O O . PHE A 338 ? 0.4415 0.3811 0.4060 -0.0456 -0.0215 0.0481 338 PHE A O 2532 C CB . PHE A 338 ? 0.4237 0.3607 0.3812 -0.0440 -0.0112 0.0504 338 PHE A CB 2533 C CG . PHE A 338 ? 0.4239 0.3564 0.3752 -0.0452 -0.0090 0.0483 338 PHE A CG 2534 C CD1 . PHE A 338 ? 0.4354 0.3639 0.3803 -0.0460 -0.0054 0.0489 338 PHE A CD1 2535 C CD2 . PHE A 338 ? 0.4497 0.3821 0.4013 -0.0456 -0.0106 0.0457 338 PHE A CD2 2536 C CE1 . PHE A 338 ? 0.4503 0.3740 0.3887 -0.0476 -0.0035 0.0471 338 PHE A CE1 2537 C CE2 . PHE A 338 ? 0.4427 0.3713 0.3882 -0.0474 -0.0088 0.0439 338 PHE A CE2 2538 C CZ . PHE A 338 ? 0.4515 0.3754 0.3902 -0.0486 -0.0053 0.0446 338 PHE A CZ 2539 N N . ILE A 339 ? 0.4566 0.3923 0.4144 -0.0494 -0.0208 0.0486 339 ILE A N 2540 C CA . ILE A 339 ? 0.4863 0.4227 0.4452 -0.0497 -0.0244 0.0464 339 ILE A CA 2541 C C . ILE A 339 ? 0.5127 0.4508 0.4763 -0.0487 -0.0294 0.0470 339 ILE A C 2542 O O . ILE A 339 ? 0.5117 0.4489 0.4754 -0.0500 -0.0317 0.0488 339 ILE A O 2543 C CB . ILE A 339 ? 0.5022 0.4367 0.4567 -0.0523 -0.0248 0.0459 339 ILE A CB 2544 C CG1 . ILE A 339 ? 0.4925 0.4242 0.4412 -0.0535 -0.0201 0.0451 339 ILE A CG1 2545 C CG2 . ILE A 339 ? 0.5117 0.4484 0.4678 -0.0522 -0.0288 0.0439 339 ILE A CG2 2546 C CD1 . ILE A 339 ? 0.5162 0.4488 0.4645 -0.0527 -0.0190 0.0428 339 ILE A CD1 2547 N N . GLU A 340 ? 0.5551 0.4951 0.5221 -0.0465 -0.0308 0.0455 340 GLU A N 2548 C CA . GLU A 340 ? 0.5965 0.5372 0.5672 -0.0451 -0.0354 0.0457 340 GLU A CA 2549 C C . GLU A 340 ? 0.5583 0.4983 0.5302 -0.0460 -0.0362 0.0486 340 GLU A C 2550 O O . GLU A 340 ? 0.5613 0.4996 0.5334 -0.0468 -0.0402 0.0496 340 GLU A O 2551 C CB . GLU A 340 ? 0.6583 0.5981 0.6282 -0.0453 -0.0397 0.0447 340 GLU A CB 2552 C CG . GLU A 340 ? 0.7247 0.6668 0.6938 -0.0447 -0.0395 0.0421 340 GLU A CG 2553 C CD . GLU A 340 ? 0.7891 0.7340 0.7612 -0.0419 -0.0402 0.0400 340 GLU A CD 2554 O OE1 . GLU A 340 ? 0.8543 0.7988 0.8289 -0.0399 -0.0434 0.0400 340 GLU A OE1 2555 O OE2 . GLU A 340 ? 0.8652 0.8125 0.8366 -0.0419 -0.0378 0.0383 340 GLU A OE2 2556 N N . ASN A 341 ? 0.5416 0.4831 0.5140 -0.0458 -0.0324 0.0501 341 ASN A N 2557 C CA . ASN A 341 ? 0.4951 0.4373 0.4682 -0.0472 -0.0325 0.0533 341 ASN A CA 2558 C C . ASN A 341 ? 0.4840 0.4294 0.4584 -0.0460 -0.0283 0.0549 341 ASN A C 2559 O O . ASN A 341 ? 0.5187 0.4641 0.4905 -0.0455 -0.0238 0.0549 341 ASN A O 2560 C CB . ASN A 341 ? 0.5130 0.4535 0.4825 -0.0497 -0.0320 0.0547 341 ASN A CB 2561 C CG . ASN A 341 ? 0.5080 0.4499 0.4779 -0.0517 -0.0324 0.0582 341 ASN A CG 2562 O OD1 . ASN A 341 ? 0.5018 0.4439 0.4737 -0.0525 -0.0361 0.0594 341 ASN A OD1 2563 N ND2 . ASN A 341 ? 0.4690 0.4119 0.4365 -0.0525 -0.0284 0.0598 341 ASN A ND2 2564 N N . GLY A 342 ? 0.4373 0.3852 0.4151 -0.0455 -0.0297 0.0562 342 GLY A N 2565 C CA . GLY A 342 ? 0.4318 0.3837 0.4111 -0.0443 -0.0260 0.0581 342 GLY A CA 2566 C C . GLY A 342 ? 0.4282 0.3831 0.4078 -0.0465 -0.0262 0.0619 342 GLY A C 2567 O O . GLY A 342 ? 0.4416 0.3949 0.4206 -0.0492 -0.0299 0.0629 342 GLY A O 2568 N N . TRP A 343 ? 0.4108 0.3703 0.3910 -0.0453 -0.0221 0.0640 343 TRP A N 2569 C CA . TRP A 343 ? 0.4181 0.3821 0.3986 -0.0472 -0.0216 0.0678 343 TRP A CA 2570 C C . TRP A 343 ? 0.4405 0.4104 0.4250 -0.0470 -0.0223 0.0701 343 TRP A C 2571 O O . TRP A 343 ? 0.4116 0.3857 0.3974 -0.0441 -0.0184 0.0708 343 TRP A O 2572 C CB . TRP A 343 ? 0.3929 0.3586 0.3705 -0.0455 -0.0160 0.0688 343 TRP A CB 2573 C CG . TRP A 343 ? 0.3750 0.3353 0.3478 -0.0464 -0.0149 0.0672 343 TRP A CG 2574 C CD1 . TRP A 343 ? 0.3708 0.3263 0.3420 -0.0490 -0.0186 0.0658 343 TRP A CD1 2575 C CD2 . TRP A 343 ? 0.3663 0.3252 0.3345 -0.0446 -0.0097 0.0671 343 TRP A CD2 2576 N NE1 . TRP A 343 ? 0.3692 0.3212 0.3358 -0.0493 -0.0162 0.0648 343 TRP A NE1 2577 C CE2 . TRP A 343 ? 0.3642 0.3176 0.3284 -0.0469 -0.0108 0.0655 343 TRP A CE2 2578 C CE3 . TRP A 343 ? 0.3675 0.3288 0.3340 -0.0413 -0.0044 0.0681 343 TRP A CE3 2579 C CZ2 . TRP A 343 ? 0.3670 0.3171 0.3256 -0.0462 -0.0068 0.0649 343 TRP A CZ2 2580 C CZ3 . TRP A 343 ? 0.3695 0.3269 0.3299 -0.0402 -0.0003 0.0674 343 TRP A CZ3 2581 C CH2 . TRP A 343 ? 0.3666 0.3183 0.3230 -0.0429 -0.0015 0.0658 343 TRP A CH2 2582 N N . GLU A 344 ? 0.4928 0.4628 0.4789 -0.0501 -0.0272 0.0714 344 GLU A N 2583 C CA . GLU A 344 ? 0.5335 0.5090 0.5230 -0.0507 -0.0285 0.0738 344 GLU A CA 2584 C C . GLU A 344 ? 0.5342 0.5182 0.5246 -0.0512 -0.0252 0.0779 344 GLU A C 2585 O O . GLU A 344 ? 0.5064 0.4970 0.4998 -0.0497 -0.0235 0.0797 344 GLU A O 2586 C CB . GLU A 344 ? 0.5958 0.5680 0.5852 -0.0544 -0.0348 0.0743 344 GLU A CB 2587 C CG . GLU A 344 ? 0.6357 0.6006 0.6245 -0.0528 -0.0377 0.0703 344 GLU A CG 2588 C CD . GLU A 344 ? 0.7204 0.6809 0.7082 -0.0555 -0.0439 0.0705 344 GLU A CD 2589 O OE1 . GLU A 344 ? 0.7599 0.7238 0.7490 -0.0578 -0.0456 0.0732 344 GLU A OE1 2590 O OE2 . GLU A 344 ? 0.7706 0.7241 0.7560 -0.0552 -0.0471 0.0680 344 GLU A OE2 2591 N N . GLY A 345 ? 0.5283 0.5127 0.5162 -0.0529 -0.0241 0.0794 345 GLY A N 2592 C CA . GLY A 345 ? 0.5370 0.5300 0.5254 -0.0529 -0.0206 0.0832 345 GLY A CA 2593 C C . GLY A 345 ? 0.5460 0.5424 0.5340 -0.0477 -0.0142 0.0829 345 GLY A C 2594 O O . GLY A 345 ? 0.5470 0.5513 0.5354 -0.0468 -0.0110 0.0861 345 GLY A O 2595 N N . MET A 346 ? 0.5436 0.5343 0.5304 -0.0441 -0.0123 0.0793 346 MET A N 2596 C CA . MET A 346 ? 0.5456 0.5385 0.5312 -0.0391 -0.0064 0.0791 346 MET A CA 2597 C C . MET A 346 ? 0.5490 0.5467 0.5384 -0.0366 -0.0059 0.0797 346 MET A C 2598 O O . MET A 346 ? 0.5085 0.5017 0.4988 -0.0356 -0.0073 0.0768 346 MET A O 2599 C CB . MET A 346 ? 0.5717 0.5559 0.5526 -0.0367 -0.0039 0.0753 346 MET A CB 2600 C CG . MET A 346 ? 0.5960 0.5815 0.5741 -0.0317 0.0021 0.0755 346 MET A CG 2601 S SD . MET A 346 ? 0.6525 0.6286 0.6228 -0.0303 0.0057 0.0727 346 MET A SD 2602 C CE . MET A 346 ? 0.5741 0.5427 0.5449 -0.0312 0.0025 0.0683 346 MET A CE 2603 N N . VAL A 347 ? 0.5522 0.5596 0.5438 -0.0353 -0.0035 0.0834 347 VAL A N 2604 C CA . VAL A 347 ? 0.5667 0.5808 0.5625 -0.0336 -0.0034 0.0849 347 VAL A CA 2605 C C . VAL A 347 ? 0.5628 0.5811 0.5575 -0.0275 0.0025 0.0858 347 VAL A C 2606 O O . VAL A 347 ? 0.5899 0.6132 0.5877 -0.0253 0.0030 0.0867 347 VAL A O 2607 C CB . VAL A 347 ? 0.5931 0.6163 0.5927 -0.0379 -0.0068 0.0891 347 VAL A CB 2608 C CG1 . VAL A 347 ? 0.5859 0.6033 0.5858 -0.0435 -0.0131 0.0880 347 VAL A CG1 2609 C CG2 . VAL A 347 ? 0.5911 0.6219 0.5896 -0.0384 -0.0042 0.0928 347 VAL A CG2 2610 N N . ASP A 348 ? 0.5469 0.5631 0.5369 -0.0246 0.0069 0.0856 348 ASP A N 2611 C CA . ASP A 348 ? 0.5394 0.5581 0.5270 -0.0181 0.0127 0.0862 348 ASP A CA 2612 C C . ASP A 348 ? 0.5119 0.5191 0.4936 -0.0146 0.0156 0.0821 348 ASP A C 2613 O O . ASP A 348 ? 0.5226 0.5292 0.5005 -0.0091 0.0204 0.0823 348 ASP A O 2614 C CB . ASP A 348 ? 0.5847 0.6106 0.5703 -0.0163 0.0163 0.0896 348 ASP A CB 2615 C CG . ASP A 348 ? 0.6257 0.6444 0.6058 -0.0177 0.0173 0.0882 348 ASP A CG 2616 O OD1 . ASP A 348 ? 0.6643 0.6744 0.6433 -0.0218 0.0138 0.0853 348 ASP A OD1 2617 O OD2 . ASP A 348 ? 0.6594 0.6813 0.6359 -0.0146 0.0216 0.0900 348 ASP A OD2 2618 N N . GLY A 349 ? 0.4738 0.4721 0.4545 -0.0176 0.0125 0.0786 349 GLY A N 2619 C CA . GLY A 349 ? 0.4393 0.4273 0.4146 -0.0153 0.0146 0.0748 349 GLY A CA 2620 C C . GLY A 349 ? 0.4097 0.3918 0.3867 -0.0192 0.0099 0.0715 349 GLY A C 2621 O O . GLY A 349 ? 0.4101 0.3946 0.3911 -0.0234 0.0054 0.0722 349 GLY A O 2622 N N . TRP A 350 ? 0.3768 0.3509 0.3501 -0.0179 0.0110 0.0681 350 TRP A N 2623 C CA . TRP A 350 ? 0.3626 0.3315 0.3369 -0.0211 0.0070 0.0649 350 TRP A CA 2624 C C . TRP A 350 ? 0.3485 0.3107 0.3181 -0.0237 0.0066 0.0630 350 TRP A C 2625 O O . TRP A 350 ? 0.3476 0.3077 0.3189 -0.0269 0.0026 0.0612 350 TRP A O 2626 C CB . TRP A 350 ? 0.3702 0.3351 0.3431 -0.0188 0.0083 0.0624 350 TRP A CB 2627 C CG . TRP A 350 ? 0.3694 0.3401 0.3481 -0.0175 0.0069 0.0634 350 TRP A CG 2628 C CD1 . TRP A 350 ? 0.3858 0.3654 0.3697 -0.0173 0.0060 0.0668 350 TRP A CD1 2629 C CD2 . TRP A 350 ? 0.3690 0.3375 0.3486 -0.0165 0.0063 0.0611 350 TRP A CD2 2630 N NE1 . TRP A 350 ? 0.3845 0.3671 0.3724 -0.0163 0.0048 0.0667 350 TRP A NE1 2631 C CE2 . TRP A 350 ? 0.3736 0.3497 0.3592 -0.0156 0.0049 0.0633 350 TRP A CE2 2632 C CE3 . TRP A 350 ? 0.3680 0.3295 0.3440 -0.0166 0.0066 0.0576 350 TRP A CE3 2633 C CZ2 . TRP A 350 ? 0.3654 0.3416 0.3533 -0.0146 0.0040 0.0619 350 TRP A CZ2 2634 C CZ3 . TRP A 350 ? 0.3691 0.3312 0.3476 -0.0155 0.0056 0.0562 350 TRP A CZ3 2635 C CH2 . TRP A 350 ? 0.3642 0.3332 0.3485 -0.0144 0.0044 0.0583 350 TRP A CH2 2636 N N . TYR A 351 ? 0.3523 0.3108 0.3154 -0.0219 0.0108 0.0632 351 TYR A N 2637 C CA . TYR A 351 ? 0.3521 0.3042 0.3099 -0.0244 0.0109 0.0616 351 TYR A CA 2638 C C . TYR A 351 ? 0.3675 0.3217 0.3224 -0.0237 0.0137 0.0643 351 TYR A C 2639 O O . TYR A 351 ? 0.3636 0.3224 0.3185 -0.0200 0.0170 0.0667 351 TYR A O 2640 C CB . TYR A 351 ? 0.3630 0.3062 0.3134 -0.0233 0.0137 0.0587 351 TYR A CB 2641 C CG . TYR A 351 ? 0.3531 0.2947 0.3055 -0.0234 0.0119 0.0562 351 TYR A CG 2642 C CD1 . TYR A 351 ? 0.3571 0.2999 0.3102 -0.0198 0.0140 0.0564 351 TYR A CD1 2643 C CD2 . TYR A 351 ? 0.3510 0.2905 0.3047 -0.0269 0.0081 0.0537 351 TYR A CD2 2644 C CE1 . TYR A 351 ? 0.3576 0.2991 0.3124 -0.0201 0.0123 0.0542 351 TYR A CE1 2645 C CE2 . TYR A 351 ? 0.3469 0.2858 0.3026 -0.0269 0.0065 0.0515 351 TYR A CE2 2646 C CZ . TYR A 351 ? 0.3497 0.2894 0.3058 -0.0237 0.0086 0.0517 351 TYR A CZ 2647 O OH . TYR A 351 ? 0.3548 0.2941 0.3127 -0.0238 0.0072 0.0495 351 TYR A OH 2648 N N . GLY A 352 ? 0.3709 0.3220 0.3231 -0.0268 0.0126 0.0639 352 GLY A N 2649 C CA . GLY A 352 ? 0.3840 0.3371 0.3332 -0.0264 0.0152 0.0663 352 GLY A CA 2650 C C . GLY A 352 ? 0.3898 0.3383 0.3354 -0.0302 0.0137 0.0655 352 GLY A C 2651 O O . GLY A 352 ? 0.3672 0.3103 0.3116 -0.0330 0.0113 0.0628 352 GLY A O 2652 N N . PHE A 353 ? 0.3916 0.3435 0.3359 -0.0303 0.0154 0.0681 353 PHE A N 2653 C CA . PHE A 353 ? 0.4011 0.3493 0.3412 -0.0335 0.0149 0.0679 353 PHE A CA 2654 C C . PHE A 353 ? 0.3943 0.3500 0.3397 -0.0366 0.0117 0.0709 353 PHE A C 2655 O O . PHE A 353 ? 0.3903 0.3543 0.3394 -0.0350 0.0126 0.0739 353 PHE A O 2656 C CB . PHE A 353 ? 0.4113 0.3562 0.3434 -0.0304 0.0205 0.0685 353 PHE A CB 2657 C CG . PHE A 353 ? 0.4349 0.3712 0.3597 -0.0272 0.0242 0.0659 353 PHE A CG 2658 C CD1 . PHE A 353 ? 0.4442 0.3822 0.3687 -0.0220 0.0275 0.0665 353 PHE A CD1 2659 C CD2 . PHE A 353 ? 0.4447 0.3713 0.3624 -0.0295 0.0244 0.0631 353 PHE A CD2 2660 C CE1 . PHE A 353 ? 0.4595 0.3886 0.3763 -0.0192 0.0308 0.0643 353 PHE A CE1 2661 C CE2 . PHE A 353 ? 0.4644 0.3823 0.3743 -0.0271 0.0277 0.0609 353 PHE A CE2 2662 C CZ . PHE A 353 ? 0.4677 0.3863 0.3769 -0.0220 0.0309 0.0614 353 PHE A CZ 2663 N N . ARG A 354 ? 0.3853 0.3382 0.3306 -0.0410 0.0080 0.0702 354 ARG A N 2664 C CA . ARG A 354 ? 0.3858 0.3436 0.3332 -0.0443 0.0057 0.0730 354 ARG A CA 2665 C C . ARG A 354 ? 0.3934 0.3459 0.3344 -0.0462 0.0070 0.0725 354 ARG A C 2666 O O . ARG A 354 ? 0.3918 0.3367 0.3287 -0.0471 0.0068 0.0696 354 ARG A O 2667 C CB . ARG A 354 ? 0.3902 0.3492 0.3431 -0.0482 -0.0006 0.0731 354 ARG A CB 2668 C CG . ARG A 354 ? 0.3982 0.3642 0.3576 -0.0475 -0.0024 0.0749 354 ARG A CG 2669 C CD . ARG A 354 ? 0.4029 0.3683 0.3663 -0.0512 -0.0088 0.0747 354 ARG A CD 2670 N NE . ARG A 354 ? 0.4051 0.3760 0.3738 -0.0505 -0.0103 0.0761 354 ARG A NE 2671 C CZ . ARG A 354 ? 0.4135 0.3839 0.3855 -0.0527 -0.0155 0.0759 354 ARG A CZ 2672 N NH1 . ARG A 354 ? 0.4201 0.3847 0.3909 -0.0554 -0.0198 0.0743 354 ARG A NH1 2673 N NH2 . ARG A 354 ? 0.4187 0.3942 0.3948 -0.0521 -0.0164 0.0774 354 ARG A NH2 2674 N N . HIS A 355 ? 0.3908 0.3477 0.3308 -0.0472 0.0081 0.0753 355 HIS A N 2675 C CA . HIS A 355 ? 0.3994 0.3517 0.3331 -0.0489 0.0096 0.0750 355 HIS A CA 2676 C C . HIS A 355 ? 0.4042 0.3610 0.3400 -0.0530 0.0067 0.0778 355 HIS A C 2677 O O . HIS A 355 ? 0.3821 0.3470 0.3234 -0.0539 0.0048 0.0806 355 HIS A O 2678 C CB . HIS A 355 ? 0.4062 0.3575 0.3335 -0.0445 0.0161 0.0754 355 HIS A CB 2679 C CG . HIS A 355 ? 0.4116 0.3731 0.3415 -0.0422 0.0186 0.0793 355 HIS A CG 2680 N ND1 . HIS A 355 ? 0.4125 0.3797 0.3455 -0.0379 0.0208 0.0804 355 HIS A ND1 2681 C CD2 . HIS A 355 ? 0.4284 0.3963 0.3583 -0.0439 0.0191 0.0825 355 HIS A CD2 2682 C CE1 . HIS A 355 ? 0.4237 0.4010 0.3587 -0.0368 0.0227 0.0842 355 HIS A CE1 2683 N NE2 . HIS A 355 ? 0.4155 0.3933 0.3486 -0.0406 0.0216 0.0854 355 HIS A NE2 2684 N N . GLN A 356 ? 0.4210 0.3725 0.3521 -0.0560 0.0059 0.0770 356 GLN A N 2685 C CA . GLN A 356 ? 0.4406 0.3950 0.3716 -0.0599 0.0039 0.0795 356 GLN A CA 2686 C C . GLN A 356 ? 0.4432 0.3939 0.3665 -0.0595 0.0081 0.0793 356 GLN A C 2687 O O . GLN A 356 ? 0.4291 0.3715 0.3472 -0.0597 0.0089 0.0765 356 GLN A O 2688 C CB . GLN A 356 ? 0.4822 0.4329 0.4151 -0.0645 -0.0022 0.0785 356 GLN A CB 2689 C CG . GLN A 356 ? 0.5304 0.4837 0.4630 -0.0689 -0.0047 0.0813 356 GLN A CG 2690 C CD . GLN A 356 ? 0.5822 0.5321 0.5169 -0.0730 -0.0113 0.0808 356 GLN A CD 2691 O OE1 . GLN A 356 ? 0.6694 0.6134 0.6036 -0.0728 -0.0134 0.0779 356 GLN A OE1 2692 N NE2 . GLN A 356 ? 0.6350 0.5888 0.5716 -0.0766 -0.0147 0.0839 356 GLN A NE2 2693 N N . ASN A 357 ? 0.4303 0.3874 0.3528 -0.0590 0.0108 0.0824 357 ASN A N 2694 C CA . ASN A 357 ? 0.4369 0.3911 0.3518 -0.0583 0.0150 0.0825 357 ASN A CA 2695 C C . ASN A 357 ? 0.4556 0.4177 0.3717 -0.0610 0.0145 0.0863 357 ASN A C 2696 O O . ASN A 357 ? 0.4291 0.3969 0.3512 -0.0645 0.0100 0.0884 357 ASN A O 2697 C CB . ASN A 357 ? 0.4406 0.3933 0.3507 -0.0520 0.0214 0.0816 357 ASN A CB 2698 C CG . ASN A 357 ? 0.4310 0.3946 0.3454 -0.0481 0.0240 0.0847 357 ASN A CG 2699 O OD1 . ASN A 357 ? 0.4280 0.4012 0.3486 -0.0506 0.0214 0.0879 357 ASN A OD1 2700 N ND2 . ASN A 357 ? 0.4254 0.3878 0.3360 -0.0420 0.0292 0.0840 357 ASN A ND2 2701 N N . SER A 358 ? 0.4970 0.4589 0.4069 -0.0597 0.0189 0.0871 358 SER A N 2702 C CA . SER A 358 ? 0.5285 0.4984 0.4386 -0.0620 0.0193 0.0908 358 SER A CA 2703 C C . SER A 358 ? 0.5264 0.5096 0.4432 -0.0611 0.0193 0.0946 358 SER A C 2704 O O . SER A 358 ? 0.5641 0.5546 0.4832 -0.0651 0.0171 0.0979 358 SER A O 2705 C CB . SER A 358 ? 0.5608 0.5283 0.4622 -0.0590 0.0252 0.0907 358 SER A CB 2706 O OG . SER A 358 ? 0.5954 0.5605 0.4931 -0.0522 0.0306 0.0892 358 SER A OG 2707 N N . GLU A 359 ? 0.5068 0.4930 0.4260 -0.0561 0.0217 0.0943 359 GLU A N 2708 C CA . GLU A 359 ? 0.5117 0.5112 0.4368 -0.0544 0.0226 0.0980 359 GLU A CA 2709 C C . GLU A 359 ? 0.4937 0.4966 0.4268 -0.0573 0.0172 0.0986 359 GLU A C 2710 O O . GLU A 359 ? 0.5117 0.5258 0.4499 -0.0565 0.0174 0.1017 359 GLU A O 2711 C CB . GLU A 359 ? 0.5230 0.5249 0.4454 -0.0464 0.0291 0.0977 359 GLU A CB 2712 C CG . GLU A 359 ? 0.5581 0.5561 0.4715 -0.0429 0.0347 0.0972 359 GLU A CG 2713 C CD . GLU A 359 ? 0.5875 0.5888 0.4977 -0.0345 0.0412 0.0976 359 GLU A CD 2714 O OE1 . GLU A 359 ? 0.6182 0.6330 0.5318 -0.0322 0.0433 0.1013 359 GLU A OE1 2715 O OE2 . GLU A 359 ? 0.6023 0.5930 0.5063 -0.0301 0.0442 0.0943 359 GLU A OE2 2716 N N . GLY A 360 ? 0.4605 0.4542 0.3943 -0.0605 0.0125 0.0957 360 GLY A N 2717 C CA . GLY A 360 ? 0.4385 0.4340 0.3789 -0.0636 0.0069 0.0962 360 GLY A CA 2718 C C . GLY A 360 ? 0.4288 0.4161 0.3702 -0.0614 0.0057 0.0922 360 GLY A C 2719 O O . GLY A 360 ? 0.4095 0.3877 0.3461 -0.0597 0.0073 0.0889 360 GLY A O 2720 N N . ILE A 361 ? 0.4276 0.4184 0.3748 -0.0617 0.0026 0.0928 361 ILE A N 2721 C CA . ILE A 361 ? 0.4473 0.4317 0.3964 -0.0599 0.0010 0.0894 361 ILE A CA 2722 C C . ILE A 361 ? 0.4472 0.4383 0.4000 -0.0556 0.0036 0.0903 361 ILE A C 2723 O O . ILE A 361 ? 0.4428 0.4434 0.3998 -0.0568 0.0025 0.0937 361 ILE A O 2724 C CB . ILE A 361 ? 0.4691 0.4501 0.4214 -0.0645 -0.0059 0.0888 361 ILE A CB 2725 C CG1 . ILE A 361 ? 0.4950 0.4683 0.4433 -0.0681 -0.0086 0.0874 361 ILE A CG1 2726 C CG2 . ILE A 361 ? 0.4902 0.4670 0.4451 -0.0620 -0.0072 0.0857 361 ILE A CG2 2727 C CD1 . ILE A 361 ? 0.5194 0.4922 0.4696 -0.0735 -0.0150 0.0890 361 ILE A CD1 2728 N N . GLY A 362 ? 0.4228 0.4091 0.3734 -0.0508 0.0070 0.0874 362 GLY A N 2729 C CA . GLY A 362 ? 0.4301 0.4223 0.3833 -0.0459 0.0102 0.0883 362 GLY A CA 2730 C C . GLY A 362 ? 0.4263 0.4121 0.3804 -0.0435 0.0096 0.0848 362 GLY A C 2731 O O . GLY A 362 ? 0.4095 0.3861 0.3612 -0.0450 0.0077 0.0815 362 GLY A O 2732 N N . GLN A 363 ? 0.4256 0.4172 0.3832 -0.0400 0.0113 0.0858 363 GLN A N 2733 C CA . GLN A 363 ? 0.4265 0.4138 0.3855 -0.0375 0.0109 0.0830 363 GLN A CA 2734 C C . GLN A 363 ? 0.4284 0.4191 0.3861 -0.0313 0.0164 0.0837 363 GLN A C 2735 O O . GLN A 363 ? 0.4294 0.4300 0.3890 -0.0296 0.0185 0.0873 363 GLN A O 2736 C CB . GLN A 363 ? 0.4415 0.4328 0.4074 -0.0406 0.0057 0.0839 363 GLN A CB 2737 C CG . GLN A 363 ? 0.4581 0.4451 0.4259 -0.0387 0.0045 0.0810 363 GLN A CG 2738 C CD . GLN A 363 ? 0.4662 0.4568 0.4401 -0.0419 -0.0007 0.0819 363 GLN A CD 2739 O OE1 . GLN A 363 ? 0.4890 0.4744 0.4634 -0.0454 -0.0053 0.0802 363 GLN A OE1 2740 N NE2 . GLN A 363 ? 0.4678 0.4674 0.4459 -0.0407 -0.0001 0.0847 363 GLN A NE2 2741 N N . ALA A 364 ? 0.4040 0.3868 0.3581 -0.0279 0.0185 0.0805 364 ALA A N 2742 C CA . ALA A 364 ? 0.3972 0.3816 0.3497 -0.0218 0.0232 0.0808 364 ALA A CA 2743 C C . ALA A 364 ? 0.4049 0.3823 0.3573 -0.0206 0.0223 0.0774 364 ALA A C 2744 O O . ALA A 364 ? 0.3748 0.3429 0.3241 -0.0230 0.0207 0.0741 364 ALA A O 2745 C CB . ALA A 364 ? 0.3953 0.3755 0.3392 -0.0177 0.0289 0.0807 364 ALA A CB 2746 N N . ALA A 365 ? 0.4159 0.3981 0.3716 -0.0170 0.0235 0.0783 365 ALA A N 2747 C CA . ALA A 365 ? 0.4264 0.4029 0.3819 -0.0155 0.0231 0.0754 365 ALA A CA 2748 C C . ALA A 365 ? 0.4460 0.4129 0.3923 -0.0113 0.0280 0.0732 365 ALA A C 2749 O O . ALA A 365 ? 0.4551 0.4225 0.3963 -0.0076 0.0324 0.0747 365 ALA A O 2750 C CB . ALA A 365 ? 0.4408 0.4260 0.4027 -0.0133 0.0226 0.0774 365 ALA A CB 2751 N N . ASP A 366 ? 0.4395 0.3975 0.3830 -0.0120 0.0272 0.0697 366 ASP A N 2752 C CA . ASP A 366 ? 0.4606 0.4086 0.3948 -0.0084 0.0314 0.0676 366 ASP A CA 2753 C C . ASP A 366 ? 0.4874 0.4366 0.4232 -0.0044 0.0327 0.0674 366 ASP A C 2754 O O . ASP A 366 ? 0.4655 0.4142 0.4055 -0.0065 0.0295 0.0657 366 ASP A O 2755 C CB . ASP A 366 ? 0.4687 0.4060 0.3977 -0.0123 0.0298 0.0639 366 ASP A CB 2756 C CG . ASP A 366 ? 0.5054 0.4313 0.4233 -0.0094 0.0341 0.0618 366 ASP A CG 2757 O OD1 . ASP A 366 ? 0.5186 0.4400 0.4286 -0.0074 0.0378 0.0624 366 ASP A OD1 2758 O OD2 . ASP A 366 ? 0.5081 0.4291 0.4244 -0.0090 0.0339 0.0597 366 ASP A OD2 2759 N N . LEU A 367 ? 0.5018 0.4521 0.4336 0.0015 0.0373 0.0692 367 LEU A N 2760 C CA . LEU A 367 ? 0.5289 0.4822 0.4628 0.0059 0.0386 0.0699 367 LEU A CA 2761 C C . LEU A 367 ? 0.5268 0.4688 0.4549 0.0061 0.0390 0.0663 367 LEU A C 2762 O O . LEU A 367 ? 0.5188 0.4629 0.4519 0.0056 0.0369 0.0656 367 LEU A O 2763 C CB . LEU A 367 ? 0.5695 0.5274 0.5002 0.0129 0.0437 0.0729 367 LEU A CB 2764 C CG . LEU A 367 ? 0.6107 0.5718 0.5421 0.0188 0.0460 0.0741 367 LEU A CG 2765 C CD1 . LEU A 367 ? 0.6257 0.5729 0.5467 0.0221 0.0489 0.0712 367 LEU A CD1 2766 C CD2 . LEU A 367 ? 0.6222 0.5923 0.5645 0.0162 0.0417 0.0748 367 LEU A CD2 2767 N N . LYS A 368 ? 0.5221 0.4521 0.4396 0.0062 0.0415 0.0642 368 LYS A N 2768 C CA . LYS A 368 ? 0.5531 0.4715 0.4631 0.0062 0.0424 0.0611 368 LYS A CA 2769 C C . LYS A 368 ? 0.5295 0.4483 0.4454 0.0009 0.0376 0.0587 368 LYS A C 2770 O O . LYS A 368 ? 0.5158 0.4332 0.4326 0.0018 0.0372 0.0576 368 LYS A O 2771 C CB . LYS A 368 ? 0.5915 0.4970 0.4890 0.0053 0.0449 0.0591 368 LYS A CB 2772 C CG . LYS A 368 ? 0.6445 0.5373 0.5330 0.0044 0.0457 0.0560 368 LYS A CG 2773 C CD . LYS A 368 ? 0.6984 0.5796 0.5763 0.0007 0.0464 0.0539 368 LYS A CD 2774 C CE . LYS A 368 ? 0.7351 0.6026 0.6018 -0.0002 0.0476 0.0511 368 LYS A CE 2775 N NZ . LYS A 368 ? 0.7624 0.6191 0.6183 -0.0041 0.0483 0.0495 368 LYS A NZ 2776 N N . SER A 369 ? 0.4920 0.4123 0.4115 -0.0045 0.0340 0.0579 369 SER A N 2777 C CA . SER A 369 ? 0.4754 0.3965 0.4003 -0.0093 0.0294 0.0557 369 SER A CA 2778 C C . SER A 369 ? 0.4529 0.3838 0.3883 -0.0085 0.0267 0.0570 369 SER A C 2779 O O . SER A 369 ? 0.4308 0.3611 0.3687 -0.0095 0.0247 0.0552 369 SER A O 2780 C CB . SER A 369 ? 0.4685 0.3901 0.3952 -0.0144 0.0262 0.0551 369 SER A CB 2781 O OG . SER A 369 ? 0.4883 0.4184 0.4210 -0.0144 0.0252 0.0579 369 SER A OG 2782 N N . THR A 370 ? 0.4319 0.3721 0.3732 -0.0070 0.0266 0.0601 370 THR A N 2783 C CA . THR A 370 ? 0.4261 0.3756 0.3767 -0.0067 0.0239 0.0617 370 THR A CA 2784 C C . THR A 370 ? 0.4419 0.3909 0.3917 -0.0024 0.0262 0.0616 370 THR A C 2785 O O . THR A 370 ? 0.4100 0.3612 0.3647 -0.0034 0.0235 0.0606 370 THR A O 2786 C CB . THR A 370 ? 0.4306 0.3903 0.3863 -0.0058 0.0240 0.0656 370 THR A CB 2787 O OG1 . THR A 370 ? 0.4081 0.3685 0.3652 -0.0102 0.0213 0.0657 370 THR A OG1 2788 C CG2 . THR A 370 ? 0.4086 0.3780 0.3730 -0.0054 0.0216 0.0676 370 THR A CG2 2789 N N . GLN A 371 ? 0.4590 0.4042 0.4016 0.0024 0.0310 0.0625 371 GLN A N 2790 C CA . GLN A 371 ? 0.4805 0.4246 0.4213 0.0070 0.0334 0.0626 371 GLN A CA 2791 C C . GLN A 371 ? 0.4649 0.3993 0.4009 0.0054 0.0329 0.0591 371 GLN A C 2792 O O . GLN A 371 ? 0.4450 0.3807 0.3833 0.0069 0.0325 0.0588 371 GLN A O 2793 C CB . GLN A 371 ? 0.5278 0.4699 0.4612 0.0132 0.0389 0.0646 371 GLN A CB 2794 C CG . GLN A 371 ? 0.5852 0.5303 0.5191 0.0188 0.0411 0.0661 371 GLN A CG 2795 C CD . GLN A 371 ? 0.6020 0.5614 0.5477 0.0185 0.0384 0.0688 371 GLN A CD 2796 O OE1 . GLN A 371 ? 0.6323 0.6010 0.5835 0.0173 0.0373 0.0714 371 GLN A OE1 2797 N NE2 . GLN A 371 ? 0.6302 0.5911 0.5793 0.0192 0.0371 0.0684 371 GLN A NE2 2798 N N . ALA A 372 ? 0.4610 0.3863 0.3902 0.0022 0.0329 0.0566 372 ALA A N 2799 C CA . ALA A 372 ? 0.4663 0.3831 0.3908 -0.0004 0.0320 0.0532 372 ALA A CA 2800 C C . ALA A 372 ? 0.4494 0.3724 0.3833 -0.0038 0.0273 0.0520 372 ALA A C 2801 O O . ALA A 372 ? 0.4407 0.3617 0.3742 -0.0035 0.0270 0.0506 372 ALA A O 2802 C CB . ALA A 372 ? 0.4610 0.3690 0.3776 -0.0041 0.0323 0.0512 372 ALA A CB 2803 N N . ALA A 373 ? 0.4315 0.3616 0.3732 -0.0069 0.0237 0.0526 373 ALA A N 2804 C CA . ALA A 373 ? 0.4191 0.3550 0.3694 -0.0096 0.0191 0.0517 373 ALA A CA 2805 C C . ALA A 373 ? 0.4220 0.3647 0.3783 -0.0066 0.0189 0.0534 373 ALA A C 2806 O O . ALA A 373 ? 0.4146 0.3579 0.3735 -0.0071 0.0172 0.0519 373 ALA A O 2807 C CB . ALA A 373 ? 0.4070 0.3479 0.3629 -0.0130 0.0154 0.0523 373 ALA A CB 2808 N N . ILE A 374 ? 0.4110 0.3595 0.3695 -0.0035 0.0206 0.0567 374 ILE A N 2809 C CA . ILE A 374 ? 0.4310 0.3872 0.3954 -0.0009 0.0203 0.0588 374 ILE A CA 2810 C C . ILE A 374 ? 0.4416 0.3931 0.4015 0.0025 0.0231 0.0578 374 ILE A C 2811 O O . ILE A 374 ? 0.4288 0.3835 0.3932 0.0026 0.0213 0.0575 374 ILE A O 2812 C CB . ILE A 374 ? 0.4272 0.3915 0.3944 0.0015 0.0219 0.0628 374 ILE A CB 2813 C CG1 . ILE A 374 ? 0.4304 0.4005 0.4037 -0.0028 0.0179 0.0638 374 ILE A CG1 2814 C CG2 . ILE A 374 ? 0.4436 0.4153 0.4149 0.0052 0.0228 0.0652 374 ILE A CG2 2815 C CD1 . ILE A 374 ? 0.4228 0.4005 0.3977 -0.0016 0.0193 0.0676 374 ILE A CD1 2816 N N . ASN A 375 ? 0.4600 0.4031 0.4104 0.0052 0.0272 0.0573 375 ASN A N 2817 C CA . ASN A 375 ? 0.4928 0.4297 0.4371 0.0086 0.0300 0.0565 375 ASN A CA 2818 C C . ASN A 375 ? 0.4802 0.4129 0.4245 0.0051 0.0275 0.0532 375 ASN A C 2819 O O . ASN A 375 ? 0.4618 0.3950 0.4070 0.0069 0.0277 0.0531 375 ASN A O 2820 C CB . ASN A 375 ? 0.5225 0.4489 0.4547 0.0115 0.0346 0.0562 375 ASN A CB 2821 C CG . ASN A 375 ? 0.5386 0.4693 0.4698 0.0171 0.0381 0.0596 375 ASN A CG 2822 O OD1 . ASN A 375 ? 0.5465 0.4881 0.4854 0.0194 0.0376 0.0624 375 ASN A OD1 2823 N ND2 . ASN A 375 ? 0.5809 0.5032 0.5021 0.0192 0.0417 0.0594 375 ASN A ND2 2824 N N . GLN A 376 ? 0.4653 0.3946 0.4087 0.0003 0.0252 0.0508 376 GLN A N 2825 C CA . GLN A 376 ? 0.4637 0.3900 0.4070 -0.0031 0.0229 0.0478 376 GLN A CA 2826 C C . GLN A 376 ? 0.4346 0.3697 0.3882 -0.0042 0.0190 0.0478 376 GLN A C 2827 O O . GLN A 376 ? 0.4188 0.3533 0.3729 -0.0045 0.0182 0.0463 376 GLN A O 2828 C CB . GLN A 376 ? 0.4695 0.3912 0.4093 -0.0078 0.0214 0.0455 376 GLN A CB 2829 C CG . GLN A 376 ? 0.4928 0.4037 0.4206 -0.0076 0.0251 0.0449 376 GLN A CG 2830 C CD . GLN A 376 ? 0.4919 0.3996 0.4170 -0.0125 0.0234 0.0430 376 GLN A CD 2831 O OE1 . GLN A 376 ? 0.5150 0.4220 0.4401 -0.0163 0.0212 0.0407 376 GLN A OE1 2832 N NE2 . GLN A 376 ? 0.5459 0.4526 0.4688 -0.0125 0.0245 0.0442 376 GLN A NE2 2833 N N . ILE A 377 ? 0.4121 0.3550 0.3732 -0.0050 0.0165 0.0494 377 ILE A N 2834 C CA . ILE A 377 ? 0.4099 0.3604 0.3799 -0.0060 0.0128 0.0497 377 ILE A CA 2835 C C . ILE A 377 ? 0.4175 0.3718 0.3896 -0.0022 0.0143 0.0516 377 ILE A C 2836 O O . ILE A 377 ? 0.4023 0.3586 0.3779 -0.0026 0.0124 0.0506 377 ILE A O 2837 C CB . ILE A 377 ? 0.3928 0.3495 0.3689 -0.0079 0.0098 0.0513 377 ILE A CB 2838 C CG1 . ILE A 377 ? 0.4074 0.3607 0.3822 -0.0118 0.0074 0.0489 377 ILE A CG1 2839 C CG2 . ILE A 377 ? 0.3869 0.3510 0.3712 -0.0084 0.0063 0.0522 377 ILE A CG2 2840 C CD1 . ILE A 377 ? 0.3979 0.3551 0.3767 -0.0139 0.0048 0.0504 377 ILE A CD1 2841 N N . ASN A 378 ? 0.4285 0.3837 0.3981 0.0016 0.0178 0.0543 378 ASN A N 2842 C CA . ASN A 378 ? 0.4476 0.4064 0.4185 0.0057 0.0196 0.0563 378 ASN A CA 2843 C C . ASN A 378 ? 0.4612 0.4127 0.4264 0.0070 0.0213 0.0541 378 ASN A C 2844 O O . ASN A 378 ? 0.4684 0.4232 0.4367 0.0084 0.0207 0.0545 378 ASN A O 2845 C CB . ASN A 378 ? 0.4610 0.4227 0.4299 0.0102 0.0233 0.0597 378 ASN A CB 2846 C CG . ASN A 378 ? 0.4701 0.4426 0.4468 0.0091 0.0212 0.0627 378 ASN A CG 2847 O OD1 . ASN A 378 ? 0.4814 0.4591 0.4651 0.0057 0.0171 0.0626 378 ASN A OD1 2848 N ND2 . ASN A 378 ? 0.4766 0.4520 0.4516 0.0119 0.0240 0.0655 378 ASN A ND2 2849 N N . GLY A 379 ? 0.4642 0.4059 0.4208 0.0060 0.0231 0.0519 379 GLY A N 2850 C CA . GLY A 379 ? 0.4979 0.4317 0.4481 0.0059 0.0242 0.0496 379 GLY A CA 2851 C C . GLY A 379 ? 0.4984 0.4354 0.4542 0.0027 0.0206 0.0475 379 GLY A C 2852 O O . GLY A 379 ? 0.4812 0.4173 0.4362 0.0040 0.0210 0.0472 379 GLY A O 2853 N N . LYS A 380 ? 0.4792 0.4199 0.4403 -0.0013 0.0169 0.0461 380 LYS A N 2854 C CA . LYS A 380 ? 0.4777 0.4211 0.4433 -0.0039 0.0136 0.0440 380 LYS A CA 2855 C C . LYS A 380 ? 0.4492 0.4010 0.4232 -0.0024 0.0116 0.0457 380 LYS A C 2856 O O . LYS A 380 ? 0.4573 0.4104 0.4333 -0.0026 0.0104 0.0445 380 LYS A O 2857 C CB . LYS A 380 ? 0.5067 0.4501 0.4736 -0.0084 0.0105 0.0415 380 LYS A CB 2858 C CG . LYS A 380 ? 0.5169 0.4654 0.4896 -0.0096 0.0079 0.0425 380 LYS A CG 2859 C CD . LYS A 380 ? 0.5096 0.4575 0.4826 -0.0134 0.0051 0.0399 380 LYS A CD 2860 C CE . LYS A 380 ? 0.5053 0.4461 0.4701 -0.0152 0.0073 0.0387 380 LYS A CE 2861 N NZ . LYS A 380 ? 0.4800 0.4216 0.4457 -0.0188 0.0043 0.0365 380 LYS A NZ 2862 N N . LEU A 381 ? 0.4386 0.3961 0.4169 -0.0010 0.0114 0.0485 381 LEU A N 2863 C CA . LEU A 381 ? 0.4403 0.4057 0.4255 0.0004 0.0100 0.0507 381 LEU A CA 2864 C C . LEU A 381 ? 0.4747 0.4391 0.4573 0.0041 0.0128 0.0517 381 LEU A C 2865 O O . LEU A 381 ? 0.4591 0.4274 0.4457 0.0043 0.0113 0.0518 381 LEU A O 2866 C CB . LEU A 381 ? 0.4397 0.4116 0.4289 0.0010 0.0097 0.0541 381 LEU A CB 2867 C CG . LEU A 381 ? 0.4258 0.4003 0.4194 -0.0028 0.0058 0.0537 381 LEU A CG 2868 C CD1 . LEU A 381 ? 0.4173 0.3975 0.4134 -0.0023 0.0061 0.0572 381 LEU A CD1 2869 C CD2 . LEU A 381 ? 0.4170 0.3947 0.4161 -0.0051 0.0015 0.0524 381 LEU A CD2 2870 N N . ASN A 382 ? 0.4896 0.4480 0.4646 0.0071 0.0170 0.0523 382 ASN A N 2871 C CA . ASN A 382 ? 0.5346 0.4906 0.5057 0.0111 0.0198 0.0532 382 ASN A CA 2872 C C . ASN A 382 ? 0.5199 0.4712 0.4885 0.0095 0.0191 0.0504 382 ASN A C 2873 O O . ASN A 382 ? 0.5222 0.4747 0.4911 0.0120 0.0198 0.0513 382 ASN A O 2874 C CB . ASN A 382 ? 0.5816 0.5308 0.5437 0.0150 0.0244 0.0543 382 ASN A CB 2875 C CG . ASN A 382 ? 0.6560 0.6113 0.6198 0.0204 0.0267 0.0581 382 ASN A CG 2876 O OD1 . ASN A 382 ? 0.6920 0.6461 0.6533 0.0240 0.0285 0.0589 382 ASN A OD1 2877 N ND2 . ASN A 382 ? 0.6773 0.6401 0.6457 0.0209 0.0265 0.0607 382 ASN A ND2 2878 N N . ARG A 383 ? 0.4997 0.4462 0.4659 0.0054 0.0176 0.0472 383 ARG A N 2879 C CA . ARG A 383 ? 0.4998 0.4430 0.4640 0.0033 0.0166 0.0445 383 ARG A CA 2880 C C . ARG A 383 ? 0.4662 0.4173 0.4392 0.0015 0.0127 0.0439 383 ARG A C 2881 O O . ARG A 383 ? 0.4682 0.4188 0.4410 0.0011 0.0122 0.0426 383 ARG A O 2882 C CB . ARG A 383 ? 0.5504 0.4874 0.5093 -0.0008 0.0161 0.0416 383 ARG A CB 2883 C CG . ARG A 383 ? 0.6161 0.5434 0.5644 0.0001 0.0198 0.0417 383 ARG A CG 2884 C CD . ARG A 383 ? 0.6664 0.5874 0.6086 -0.0046 0.0192 0.0387 383 ARG A CD 2885 N NE . ARG A 383 ? 0.6969 0.6195 0.6409 -0.0070 0.0178 0.0383 383 ARG A NE 2886 C CZ . ARG A 383 ? 0.7249 0.6441 0.6652 -0.0056 0.0199 0.0397 383 ARG A CZ 2887 N NH1 . ARG A 383 ? 0.7640 0.6784 0.6985 -0.0012 0.0236 0.0417 383 ARG A NH1 2888 N NH2 . ARG A 383 ? 0.7300 0.6510 0.6722 -0.0082 0.0184 0.0393 383 ARG A NH2 2889 N N . LEU A 384 ? 0.4343 0.3921 0.4146 0.0004 0.0100 0.0447 384 LEU A N 2890 C CA . LEU A 384 ? 0.4223 0.3860 0.4098 -0.0017 0.0059 0.0436 384 LEU A CA 2891 C C . LEU A 384 ? 0.4203 0.3913 0.4141 0.0000 0.0048 0.0463 384 LEU A C 2892 O O . LEU A 384 ? 0.4015 0.3760 0.3996 -0.0010 0.0020 0.0454 384 LEU A O 2893 C CB . LEU A 384 ? 0.4070 0.3721 0.3973 -0.0047 0.0029 0.0423 384 LEU A CB 2894 C CG . LEU A 384 ? 0.4225 0.3823 0.4080 -0.0074 0.0029 0.0392 384 LEU A CG 2895 C CD1 . LEU A 384 ? 0.4130 0.3739 0.4005 -0.0097 0.0005 0.0384 384 LEU A CD1 2896 C CD2 . LEU A 384 ? 0.4246 0.3848 0.4104 -0.0088 0.0015 0.0366 384 LEU A CD2 2897 N N . ILE A 385 ? 0.4024 0.3761 0.3966 0.0026 0.0067 0.0497 385 ILE A N 2898 C CA . ILE A 385 ? 0.4093 0.3912 0.4097 0.0037 0.0054 0.0528 385 ILE A CA 2899 C C . ILE A 385 ? 0.4303 0.4133 0.4289 0.0078 0.0084 0.0549 385 ILE A C 2900 O O . ILE A 385 ? 0.4448 0.4235 0.4375 0.0110 0.0123 0.0558 385 ILE A O 2901 C CB . ILE A 385 ? 0.4155 0.4019 0.4184 0.0035 0.0052 0.0555 385 ILE A CB 2902 C CG1 . ILE A 385 ? 0.4203 0.4052 0.4246 -0.0003 0.0020 0.0536 385 ILE A CG1 2903 C CG2 . ILE A 385 ? 0.4115 0.4072 0.4204 0.0042 0.0039 0.0591 385 ILE A CG2 2904 C CD1 . ILE A 385 ? 0.4111 0.3978 0.4198 -0.0032 -0.0024 0.0517 385 ILE A CD1 2905 N N . GLY A 386 ? 0.4291 0.4173 0.4323 0.0078 0.0066 0.0556 386 GLY A N 2906 C CA . GLY A 386 ? 0.4406 0.4310 0.4430 0.0116 0.0089 0.0579 386 GLY A CA 2907 C C . GLY A 386 ? 0.4582 0.4403 0.4536 0.0133 0.0114 0.0558 386 GLY A C 2908 O O . GLY A 386 ? 0.4457 0.4265 0.4373 0.0175 0.0146 0.0577 386 GLY A O 2909 N N . LYS A 387 ? 0.4481 0.4248 0.4415 0.0100 0.0100 0.0520 387 LYS A N 2910 C CA . LYS A 387 ? 0.4521 0.4204 0.4380 0.0106 0.0122 0.0499 387 LYS A CA 2911 C C . LYS A 387 ? 0.4512 0.4197 0.4387 0.0082 0.0099 0.0474 387 LYS A C 2912 O O . LYS A 387 ? 0.4662 0.4282 0.4480 0.0070 0.0108 0.0450 387 LYS A O 2913 C CB . LYS A 387 ? 0.4754 0.4359 0.4550 0.0088 0.0134 0.0477 387 LYS A CB 2914 C CG . LYS A 387 ? 0.4940 0.4527 0.4702 0.0115 0.0162 0.0499 387 LYS A CG 2915 C CD . LYS A 387 ? 0.5307 0.4841 0.4995 0.0164 0.0203 0.0517 387 LYS A CD 2916 C CE . LYS A 387 ? 0.5460 0.4960 0.5097 0.0193 0.0235 0.0534 387 LYS A CE 2917 N NZ . LYS A 387 ? 0.5751 0.5348 0.5463 0.0199 0.0225 0.0560 387 LYS A NZ 2918 N N . THR A 388 ? 0.4231 0.3992 0.4179 0.0076 0.0071 0.0483 388 THR A N 2919 C CA . THR A 388 ? 0.4244 0.4014 0.4211 0.0055 0.0048 0.0460 388 THR A CA 2920 C C . THR A 388 ? 0.4585 0.4317 0.4503 0.0075 0.0071 0.0461 388 THR A C 2921 O O . THR A 388 ? 0.4338 0.4056 0.4224 0.0114 0.0101 0.0487 388 THR A O 2922 C CB . THR A 388 ? 0.4086 0.3938 0.4134 0.0044 0.0012 0.0470 388 THR A CB 2923 O OG1 . THR A 388 ? 0.4037 0.3940 0.4108 0.0073 0.0023 0.0508 388 THR A OG1 2924 C CG2 . THR A 388 ? 0.3833 0.3711 0.3920 0.0021 -0.0013 0.0468 388 THR A CG2 2925 N N . ASN A 389 ? 0.4570 0.4286 0.4481 0.0051 0.0057 0.0433 389 ASN A N 2926 C CA . ASN A 389 ? 0.4988 0.4665 0.4850 0.0062 0.0075 0.0431 389 ASN A CA 2927 C C . ASN A 389 ? 0.4601 0.4342 0.4522 0.0060 0.0051 0.0434 389 ASN A C 2928 O O . ASN A 389 ? 0.4454 0.4248 0.4435 0.0037 0.0019 0.0424 389 ASN A O 2929 C CB . ASN A 389 ? 0.5489 0.5099 0.5289 0.0031 0.0078 0.0396 389 ASN A CB 2930 C CG . ASN A 389 ? 0.6173 0.5705 0.5897 0.0033 0.0105 0.0395 389 ASN A CG 2931 O OD1 . ASN A 389 ? 0.6561 0.6071 0.6260 0.0067 0.0130 0.0420 389 ASN A OD1 2932 N ND2 . ASN A 389 ? 0.6488 0.5982 0.6173 -0.0004 0.0101 0.0366 389 ASN A ND2 2933 N N . GLU A 390 ? 0.4340 0.4070 0.4235 0.0084 0.0068 0.0449 390 GLU A N 2934 C CA . GLU A 390 ? 0.4053 0.3838 0.3995 0.0083 0.0048 0.0454 390 GLU A CA 2935 C C . GLU A 390 ? 0.3722 0.3488 0.3650 0.0051 0.0034 0.0420 390 GLU A C 2936 O O . GLU A 390 ? 0.3635 0.3332 0.3492 0.0043 0.0052 0.0404 390 GLU A O 2937 C CB . GLU A 390 ? 0.4492 0.4274 0.4408 0.0125 0.0073 0.0486 390 GLU A CB 2938 C CG . GLU A 390 ? 0.4847 0.4682 0.4795 0.0160 0.0083 0.0526 390 GLU A CG 2939 C CD . GLU A 390 ? 0.5262 0.5115 0.5197 0.0204 0.0103 0.0559 390 GLU A CD 2940 O OE1 . GLU A 390 ? 0.5187 0.4961 0.5042 0.0231 0.0133 0.0559 390 GLU A OE1 2941 O OE2 . GLU A 390 ? 0.5464 0.5406 0.5464 0.0209 0.0086 0.0584 390 GLU A OE2 2942 N N . LYS A 391 ? 0.3349 0.3177 0.3339 0.0033 0.0001 0.0411 391 LYS A N 2943 C CA . LYS A 391 ? 0.3311 0.3141 0.3297 0.0011 -0.0011 0.0386 391 LYS A CA 2944 C C . LYS A 391 ? 0.3215 0.3102 0.3248 0.0020 -0.0028 0.0403 391 LYS A C 2945 O O . LYS A 391 ? 0.2952 0.2891 0.3036 0.0030 -0.0040 0.0428 391 LYS A O 2946 C CB . LYS A 391 ? 0.3500 0.3345 0.3508 -0.0021 -0.0038 0.0350 391 LYS A CB 2947 C CG . LYS A 391 ? 0.3686 0.3486 0.3652 -0.0035 -0.0026 0.0333 391 LYS A CG 2948 C CD . LYS A 391 ? 0.3812 0.3550 0.3701 -0.0047 -0.0003 0.0318 391 LYS A CD 2949 C CE . LYS A 391 ? 0.4077 0.3778 0.3926 -0.0070 0.0003 0.0299 391 LYS A CE 2950 N NZ . LYS A 391 ? 0.3886 0.3514 0.3644 -0.0083 0.0028 0.0293 391 LYS A NZ 2951 N N . PHE A 392 ? 0.2983 0.2863 0.2998 0.0012 -0.0029 0.0391 392 PHE A N 2952 C CA . PHE A 392 ? 0.3033 0.2957 0.3079 0.0022 -0.0039 0.0410 392 PHE A CA 2953 C C . PHE A 392 ? 0.2901 0.2853 0.2972 -0.0005 -0.0067 0.0382 392 PHE A C 2954 O O . PHE A 392 ? 0.2831 0.2812 0.2941 -0.0021 -0.0094 0.0366 392 PHE A O 2955 C CB . PHE A 392 ? 0.3240 0.3126 0.3233 0.0051 -0.0008 0.0433 392 PHE A CB 2956 C CG . PHE A 392 ? 0.3401 0.3261 0.3367 0.0086 0.0019 0.0461 392 PHE A CG 2957 C CD1 . PHE A 392 ? 0.3470 0.3392 0.3489 0.0106 0.0015 0.0493 392 PHE A CD1 2958 C CD2 . PHE A 392 ? 0.3668 0.3442 0.3554 0.0096 0.0049 0.0455 392 PHE A CD2 2959 C CE1 . PHE A 392 ? 0.3633 0.3541 0.3629 0.0141 0.0041 0.0519 392 PHE A CE1 2960 C CE2 . PHE A 392 ? 0.3764 0.3510 0.3618 0.0132 0.0076 0.0480 392 PHE A CE2 2961 C CZ . PHE A 392 ? 0.3725 0.3543 0.3638 0.0156 0.0073 0.0512 392 PHE A CZ 2962 N N . HIS A 393 ? 0.2881 0.2822 0.2926 -0.0009 -0.0063 0.0374 393 HIS A N 2963 C CA . HIS A 393 ? 0.2878 0.2847 0.2942 -0.0034 -0.0088 0.0346 393 HIS A CA 2964 C C . HIS A 393 ? 0.2894 0.2843 0.2934 -0.0059 -0.0090 0.0308 393 HIS A C 2965 O O . HIS A 393 ? 0.2891 0.2791 0.2875 -0.0065 -0.0067 0.0300 393 HIS A O 2966 C CB . HIS A 393 ? 0.2967 0.2934 0.3009 -0.0033 -0.0081 0.0351 393 HIS A CB 2967 C CG . HIS A 393 ? 0.3027 0.3035 0.3099 -0.0053 -0.0109 0.0330 393 HIS A CG 2968 N ND1 . HIS A 393 ? 0.3131 0.3187 0.3257 -0.0055 -0.0138 0.0334 393 HIS A ND1 2969 C CD2 . HIS A 393 ? 0.3148 0.3154 0.3196 -0.0073 -0.0112 0.0304 393 HIS A CD2 2970 C CE1 . HIS A 393 ? 0.3112 0.3191 0.3246 -0.0072 -0.0157 0.0311 393 HIS A CE1 2971 N NE2 . HIS A 393 ? 0.3198 0.3251 0.3288 -0.0082 -0.0141 0.0293 393 HIS A NE2 2972 N N . GLN A 394 ? 0.2794 0.2781 0.2872 -0.0073 -0.0118 0.0284 394 GLN A N 2973 C CA A GLN A 394 ? 0.2886 0.2868 0.2950 -0.0091 -0.0123 0.0250 394 GLN A CA 2974 C CA B GLN A 394 ? 0.2895 0.2877 0.2958 -0.0092 -0.0122 0.0250 394 GLN A CA 2975 C C . GLN A 394 ? 0.2933 0.2954 0.3009 -0.0106 -0.0144 0.0220 394 GLN A C 2976 O O . GLN A 394 ? 0.3342 0.3365 0.3398 -0.0113 -0.0138 0.0218 394 GLN A O 2977 C CB A GLN A 394 ? 0.2864 0.2851 0.2957 -0.0086 -0.0135 0.0251 394 GLN A CB 2978 C CB B GLN A 394 ? 0.2889 0.2874 0.2978 -0.0087 -0.0132 0.0250 394 GLN A CB 2979 C CG A GLN A 394 ? 0.2923 0.2876 0.3000 -0.0071 -0.0111 0.0280 394 GLN A CG 2980 C CG B GLN A 394 ? 0.2969 0.2912 0.3033 -0.0075 -0.0106 0.0275 394 GLN A CG 2981 C CD A GLN A 394 ? 0.2922 0.2886 0.3034 -0.0065 -0.0125 0.0289 394 GLN A CD 2982 C CD B GLN A 394 ? 0.2994 0.2935 0.3073 -0.0075 -0.0113 0.0271 394 GLN A CD 2983 O OE1 A GLN A 394 ? 0.3017 0.2982 0.3134 -0.0075 -0.0137 0.0268 394 GLN A OE1 2984 O OE1 B GLN A 394 ? 0.3089 0.3060 0.3211 -0.0075 -0.0140 0.0268 394 GLN A OE1 2985 N NE2 A GLN A 394 ? 0.2938 0.2914 0.3073 -0.0048 -0.0123 0.0324 394 GLN A NE2 2986 N NE2 B GLN A 394 ? 0.3007 0.2905 0.3044 -0.0077 -0.0090 0.0272 394 GLN A NE2 2987 N N . ILE A 395 ? 0.2756 0.2805 0.2859 -0.0109 -0.0168 0.0197 395 ILE A N 2988 C CA . ILE A 395 ? 0.2681 0.2769 0.2797 -0.0115 -0.0190 0.0169 395 ILE A CA 2989 C C . ILE A 395 ? 0.2644 0.2746 0.2801 -0.0103 -0.0221 0.0172 395 ILE A C 2990 O O . ILE A 395 ? 0.2604 0.2690 0.2778 -0.0095 -0.0225 0.0191 395 ILE A O 2991 C CB . ILE A 395 ? 0.2682 0.2794 0.2782 -0.0127 -0.0192 0.0134 395 ILE A CB 2992 C CG1 . ILE A 395 ? 0.2705 0.2812 0.2818 -0.0120 -0.0200 0.0129 395 ILE A CG1 2993 C CG2 . ILE A 395 ? 0.2692 0.2786 0.2741 -0.0148 -0.0163 0.0132 395 ILE A CG2 2994 C CD1 . ILE A 395 ? 0.2669 0.2813 0.2775 -0.0126 -0.0209 0.0095 395 ILE A CD1 2995 N N . GLU A 396 ? 0.2613 0.2740 0.2781 -0.0103 -0.0243 0.0155 396 GLU A N 2996 C CA . GLU A 396 ? 0.2678 0.2808 0.2872 -0.0094 -0.0276 0.0152 396 GLU A CA 2997 C C . GLU A 396 ? 0.2583 0.2712 0.2775 -0.0086 -0.0290 0.0126 396 GLU A C 2998 O O . GLU A 396 ? 0.2497 0.2645 0.2673 -0.0088 -0.0280 0.0102 396 GLU A O 2999 C CB . GLU A 396 ? 0.2899 0.3047 0.3094 -0.0095 -0.0295 0.0140 396 GLU A CB 3000 C CG . GLU A 396 ? 0.3075 0.3227 0.3272 -0.0102 -0.0284 0.0167 396 GLU A CG 3001 C CD . GLU A 396 ? 0.3340 0.3481 0.3558 -0.0101 -0.0287 0.0207 396 GLU A CD 3002 O OE1 . GLU A 396 ? 0.3516 0.3647 0.3749 -0.0100 -0.0310 0.0213 396 GLU A OE1 3003 O OE2 . GLU A 396 ? 0.3436 0.3581 0.3654 -0.0101 -0.0268 0.0235 396 GLU A OE2 3004 N N . LYS A 397 ? 0.2547 0.2656 0.2753 -0.0079 -0.0313 0.0135 397 LYS A N 3005 C CA . LYS A 397 ? 0.2589 0.2688 0.2792 -0.0069 -0.0328 0.0116 397 LYS A CA 3006 C C . LYS A 397 ? 0.2741 0.2823 0.2942 -0.0058 -0.0366 0.0103 397 LYS A C 3007 O O . LYS A 397 ? 0.2757 0.2827 0.2951 -0.0045 -0.0382 0.0086 397 LYS A O 3008 C CB . LYS A 397 ? 0.2563 0.2640 0.2774 -0.0073 -0.0316 0.0142 397 LYS A CB 3009 C CG . LYS A 397 ? 0.2616 0.2698 0.2815 -0.0082 -0.0278 0.0149 397 LYS A CG 3010 C CD . LYS A 397 ? 0.2629 0.2686 0.2829 -0.0083 -0.0262 0.0175 397 LYS A CD 3011 C CE . LYS A 397 ? 0.2652 0.2699 0.2827 -0.0090 -0.0225 0.0185 397 LYS A CE 3012 N NZ . LYS A 397 ? 0.2682 0.2701 0.2851 -0.0088 -0.0208 0.0206 397 LYS A NZ 3013 N N . GLU A 398 ? 0.2776 0.2852 0.2978 -0.0063 -0.0382 0.0111 398 GLU A N 3014 C CA . GLU A 398 ? 0.3020 0.3070 0.3206 -0.0054 -0.0419 0.0096 398 GLU A CA 3015 C C . GLU A 398 ? 0.3016 0.3086 0.3193 -0.0055 -0.0421 0.0083 398 GLU A C 3016 O O . GLU A 398 ? 0.2891 0.2983 0.3081 -0.0069 -0.0401 0.0101 398 GLU A O 3017 C CB . GLU A 398 ? 0.3416 0.3427 0.3605 -0.0069 -0.0442 0.0127 398 GLU A CB 3018 C CG . GLU A 398 ? 0.3770 0.3759 0.3965 -0.0070 -0.0443 0.0142 398 GLU A CG 3019 C CD . GLU A 398 ? 0.4308 0.4262 0.4501 -0.0088 -0.0470 0.0171 398 GLU A CD 3020 O OE1 . GLU A 398 ? 0.4813 0.4755 0.4994 -0.0100 -0.0492 0.0178 398 GLU A OE1 3021 O OE2 . GLU A 398 ? 0.4734 0.4674 0.4933 -0.0094 -0.0471 0.0188 398 GLU A OE2 3022 N N . PHE A 399 ? 0.2973 0.3032 0.3125 -0.0037 -0.0445 0.0052 399 PHE A N 3023 C CA . PHE A 399 ? 0.3033 0.3115 0.3173 -0.0035 -0.0446 0.0034 399 PHE A CA 3024 C C . PHE A 399 ? 0.3340 0.3375 0.3447 -0.0026 -0.0484 0.0022 399 PHE A C 3025 O O . PHE A 399 ? 0.3340 0.3339 0.3422 -0.0005 -0.0506 0.0003 399 PHE A O 3026 C CB . PHE A 399 ? 0.2961 0.3094 0.3096 -0.0017 -0.0429 0.0000 399 PHE A CB 3027 C CG . PHE A 399 ? 0.2821 0.2989 0.2975 -0.0030 -0.0395 0.0010 399 PHE A CG 3028 C CD1 . PHE A 399 ? 0.2840 0.3002 0.3000 -0.0025 -0.0389 0.0012 399 PHE A CD1 3029 C CD2 . PHE A 399 ? 0.2890 0.3087 0.3051 -0.0050 -0.0370 0.0021 399 PHE A CD2 3030 C CE1 . PHE A 399 ? 0.2864 0.3048 0.3033 -0.0041 -0.0358 0.0023 399 PHE A CE1 3031 C CE2 . PHE A 399 ? 0.2869 0.3082 0.3034 -0.0064 -0.0339 0.0033 399 PHE A CE2 3032 C CZ . PHE A 399 ? 0.2872 0.3077 0.3041 -0.0060 -0.0333 0.0033 399 PHE A CZ 3033 N N . SER A 400 ? 0.3565 0.3597 0.3667 -0.0042 -0.0492 0.0032 400 SER A N 3034 C CA . SER A 400 ? 0.3974 0.3954 0.4035 -0.0038 -0.0528 0.0021 400 SER A CA 3035 C C . SER A 400 ? 0.4156 0.4150 0.4186 -0.0011 -0.0533 -0.0020 400 SER A C 3036 O O . SER A 400 ? 0.4178 0.4118 0.4161 0.0002 -0.0563 -0.0038 400 SER A O 3037 C CB . SER A 400 ? 0.4043 0.4014 0.4111 -0.0072 -0.0537 0.0055 400 SER A CB 3038 O OG . SER A 400 ? 0.4413 0.4439 0.4503 -0.0081 -0.0512 0.0059 400 SER A OG 3039 N N . GLU A 401 ? 0.4042 0.4105 0.4092 -0.0004 -0.0503 -0.0036 401 GLU A N 3040 C CA . GLU A 401 ? 0.4260 0.4353 0.4285 0.0022 -0.0504 -0.0075 401 GLU A CA 3041 C C . GLU A 401 ? 0.4060 0.4210 0.4094 0.0046 -0.0485 -0.0099 401 GLU A C 3042 O O . GLU A 401 ? 0.3846 0.4025 0.3911 0.0033 -0.0462 -0.0085 401 GLU A O 3043 C CB . GLU A 401 ? 0.4586 0.4721 0.4619 0.0002 -0.0489 -0.0071 401 GLU A CB 3044 C CG . GLU A 401 ? 0.5233 0.5323 0.5249 -0.0018 -0.0510 -0.0053 401 GLU A CG 3045 C CD . GLU A 401 ? 0.5634 0.5710 0.5681 -0.0052 -0.0507 -0.0008 401 GLU A CD 3046 O OE1 . GLU A 401 ? 0.6184 0.6303 0.6267 -0.0064 -0.0476 0.0010 401 GLU A OE1 3047 O OE2 . GLU A 401 ? 0.5900 0.5921 0.5932 -0.0065 -0.0534 0.0010 401 GLU A OE2 3048 N N . VAL A 402 ? 0.3927 0.4097 0.3932 0.0082 -0.0493 -0.0136 402 VAL A N 3049 C CA . VAL A 402 ? 0.3851 0.4096 0.3863 0.0106 -0.0476 -0.0161 402 VAL A CA 3050 C C . VAL A 402 ? 0.3694 0.4021 0.3726 0.0084 -0.0446 -0.0163 402 VAL A C 3051 O O . VAL A 402 ? 0.3514 0.3846 0.3533 0.0077 -0.0449 -0.0168 402 VAL A O 3052 C CB . VAL A 402 ? 0.4049 0.4285 0.4017 0.0159 -0.0498 -0.0199 402 VAL A CB 3053 C CG1 . VAL A 402 ? 0.3927 0.4264 0.3901 0.0185 -0.0479 -0.0226 402 VAL A CG1 3054 C CG2 . VAL A 402 ? 0.4256 0.4409 0.4199 0.0181 -0.0525 -0.0197 402 VAL A CG2 3055 N N . GLU A 403 ? 0.3564 0.3950 0.3622 0.0069 -0.0420 -0.0159 403 GLU A N 3056 C CA . GLU A 403 ? 0.3536 0.3991 0.3605 0.0040 -0.0392 -0.0157 403 GLU A CA 3057 C C . GLU A 403 ? 0.3425 0.3974 0.3496 0.0045 -0.0373 -0.0177 403 GLU A C 3058 O O . GLU A 403 ? 0.3614 0.4228 0.3682 0.0027 -0.0357 -0.0185 403 GLU A O 3059 C CB . GLU A 403 ? 0.3639 0.4066 0.3728 -0.0001 -0.0373 -0.0120 403 GLU A CB 3060 C CG . GLU A 403 ? 0.3758 0.4116 0.3850 -0.0013 -0.0386 -0.0094 403 GLU A CG 3061 C CD . GLU A 403 ? 0.3879 0.4214 0.3991 -0.0045 -0.0367 -0.0057 403 GLU A CD 3062 O OE1 . GLU A 403 ? 0.3858 0.4173 0.3982 -0.0045 -0.0362 -0.0044 403 GLU A OE1 3063 O OE2 . GLU A 403 ? 0.4022 0.4359 0.4136 -0.0067 -0.0356 -0.0040 403 GLU A OE2 3064 N N . GLY A 404 ? 0.3167 0.3726 0.3243 0.0065 -0.0376 -0.0184 404 GLY A N 3065 C CA . GLY A 404 ? 0.3013 0.3669 0.3091 0.0069 -0.0362 -0.0202 404 GLY A CA 3066 C C . GLY A 404 ? 0.2870 0.3542 0.2962 0.0024 -0.0336 -0.0179 404 GLY A C 3067 O O . GLY A 404 ? 0.2775 0.3384 0.2877 0.0012 -0.0335 -0.0157 404 GLY A O 3068 N N . ARG A 405 ? 0.2756 0.3509 0.2843 -0.0003 -0.0315 -0.0185 405 ARG A N 3069 C CA . ARG A 405 ? 0.2733 0.3513 0.2819 -0.0044 -0.0293 -0.0171 405 ARG A CA 3070 C C . ARG A 405 ? 0.2688 0.3379 0.2776 -0.0076 -0.0281 -0.0138 405 ARG A C 3071 O O . ARG A 405 ? 0.2541 0.3218 0.2631 -0.0084 -0.0275 -0.0128 405 ARG A O 3072 C CB . ARG A 405 ? 0.2788 0.3649 0.2859 -0.0078 -0.0275 -0.0177 405 ARG A CB 3073 C CG . ARG A 405 ? 0.2832 0.3743 0.2891 -0.0120 -0.0255 -0.0170 405 ARG A CG 3074 C CD . ARG A 405 ? 0.2878 0.3878 0.2916 -0.0155 -0.0241 -0.0178 405 ARG A CD 3075 N NE . ARG A 405 ? 0.2887 0.3933 0.2905 -0.0201 -0.0225 -0.0171 405 ARG A NE 3076 C CZ . ARG A 405 ? 0.2931 0.4068 0.2927 -0.0240 -0.0213 -0.0176 405 ARG A CZ 3077 N NH1 . ARG A 405 ? 0.2863 0.4058 0.2856 -0.0237 -0.0214 -0.0190 405 ARG A NH1 3078 N NH2 . ARG A 405 ? 0.2972 0.4140 0.2944 -0.0285 -0.0201 -0.0167 405 ARG A NH2 3079 N N . ILE A 406 ? 0.2642 0.3280 0.2726 -0.0093 -0.0277 -0.0120 406 ILE A N 3080 C CA . ILE A 406 ? 0.2748 0.3311 0.2829 -0.0119 -0.0263 -0.0088 406 ILE A CA 3081 C C . ILE A 406 ? 0.2675 0.3173 0.2775 -0.0096 -0.0276 -0.0075 406 ILE A C 3082 O O . ILE A 406 ? 0.2423 0.2887 0.2522 -0.0109 -0.0265 -0.0057 406 ILE A O 3083 C CB . ILE A 406 ? 0.2984 0.3508 0.3058 -0.0136 -0.0257 -0.0070 406 ILE A CB 3084 C CG1 . ILE A 406 ? 0.3019 0.3471 0.3085 -0.0157 -0.0240 -0.0037 406 ILE A CG1 3085 C CG2 . ILE A 406 ? 0.3008 0.3501 0.3098 -0.0107 -0.0281 -0.0072 406 ILE A CG2 3086 C CD1 . ILE A 406 ? 0.3278 0.3736 0.3311 -0.0193 -0.0214 -0.0030 406 ILE A CD1 3087 N N . GLN A 407 ? 0.2564 0.3045 0.2677 -0.0062 -0.0302 -0.0085 407 GLN A N 3088 C CA . GLN A 407 ? 0.2594 0.3015 0.2719 -0.0042 -0.0319 -0.0075 407 GLN A CA 3089 C C . GLN A 407 ? 0.2460 0.2904 0.2587 -0.0028 -0.0321 -0.0086 407 GLN A C 3090 O O . GLN A 407 ? 0.2439 0.2838 0.2575 -0.0030 -0.0322 -0.0068 407 GLN A O 3091 C CB . GLN A 407 ? 0.2613 0.3005 0.2738 -0.0013 -0.0348 -0.0084 407 GLN A CB 3092 C CG . GLN A 407 ? 0.2661 0.2980 0.2792 -0.0002 -0.0368 -0.0067 407 GLN A CG 3093 C CD . GLN A 407 ? 0.2786 0.3066 0.2903 0.0020 -0.0400 -0.0077 407 GLN A CD 3094 O OE1 . GLN A 407 ? 0.2980 0.3230 0.3085 0.0047 -0.0422 -0.0089 407 GLN A OE1 3095 N NE2 . GLN A 407 ? 0.2700 0.2973 0.2812 0.0009 -0.0403 -0.0072 407 GLN A NE2 3096 N N . ASP A 408 ? 0.2447 0.2966 0.2568 -0.0014 -0.0322 -0.0113 408 ASP A N 3097 C CA . ASP A 408 ? 0.2434 0.2989 0.2557 -0.0003 -0.0322 -0.0123 408 ASP A CA 3098 C C . ASP A 408 ? 0.2360 0.2904 0.2480 -0.0043 -0.0298 -0.0101 408 ASP A C 3099 O O . ASP A 408 ? 0.2224 0.2744 0.2349 -0.0040 -0.0299 -0.0093 408 ASP A O 3100 C CB . ASP A 408 ? 0.2587 0.3247 0.2704 0.0010 -0.0321 -0.0152 408 ASP A CB 3101 C CG . ASP A 408 ? 0.2817 0.3493 0.2928 0.0059 -0.0345 -0.0178 408 ASP A CG 3102 O OD1 . ASP A 408 ? 0.2874 0.3472 0.2982 0.0087 -0.0368 -0.0176 408 ASP A OD1 3103 O OD2 . ASP A 408 ? 0.2831 0.3599 0.2936 0.0068 -0.0340 -0.0200 408 ASP A OD2 3104 N N . LEU A 409 ? 0.2268 0.2824 0.2375 -0.0081 -0.0276 -0.0092 409 LEU A N 3105 C CA . LEU A 409 ? 0.2290 0.2824 0.2380 -0.0120 -0.0251 -0.0072 409 LEU A CA 3106 C C . LEU A 409 ? 0.2249 0.2689 0.2345 -0.0121 -0.0248 -0.0043 409 LEU A C 3107 O O . LEU A 409 ? 0.2199 0.2614 0.2290 -0.0129 -0.0241 -0.0032 409 LEU A O 3108 C CB . LEU A 409 ? 0.2295 0.2852 0.2356 -0.0159 -0.0231 -0.0069 409 LEU A CB 3109 C CG . LEU A 409 ? 0.2332 0.2866 0.2357 -0.0204 -0.0206 -0.0053 409 LEU A CG 3110 C CD1 . LEU A 409 ? 0.2305 0.2884 0.2326 -0.0211 -0.0205 -0.0061 409 LEU A CD1 3111 C CD2 . LEU A 409 ? 0.2406 0.2969 0.2398 -0.0240 -0.0192 -0.0055 409 LEU A CD2 3112 N N . GLU A 410 ? 0.2317 0.2712 0.2423 -0.0111 -0.0256 -0.0031 410 GLU A N 3113 C CA . GLU A 410 ? 0.2430 0.2751 0.2546 -0.0109 -0.0254 -0.0001 410 GLU A CA 3114 C C . GLU A 410 ? 0.2401 0.2700 0.2533 -0.0088 -0.0270 -0.0001 410 GLU A C 3115 O O . GLU A 410 ? 0.2281 0.2542 0.2412 -0.0096 -0.0260 0.0017 410 GLU A O 3116 C CB . GLU A 410 ? 0.2576 0.2868 0.2703 -0.0101 -0.0264 0.0010 410 GLU A CB 3117 C CG . GLU A 410 ? 0.2713 0.3009 0.2821 -0.0124 -0.0245 0.0018 410 GLU A CG 3118 C CD . GLU A 410 ? 0.3126 0.3419 0.3244 -0.0117 -0.0257 0.0021 410 GLU A CD 3119 O OE1 . GLU A 410 ? 0.3266 0.3569 0.3399 -0.0096 -0.0283 0.0006 410 GLU A OE1 3120 O OE2 . GLU A 410 ? 0.3317 0.3595 0.3422 -0.0133 -0.0242 0.0039 410 GLU A OE2 3121 N N . LYS A 411 ? 0.2322 0.2645 0.2464 -0.0060 -0.0296 -0.0023 411 LYS A N 3122 C CA . LYS A 411 ? 0.2440 0.2740 0.2591 -0.0038 -0.0315 -0.0025 411 LYS A CA 3123 C C . LYS A 411 ? 0.2280 0.2608 0.2426 -0.0046 -0.0303 -0.0030 411 LYS A C 3124 O O . LYS A 411 ? 0.2231 0.2521 0.2381 -0.0044 -0.0306 -0.0017 411 LYS A O 3125 C CB . LYS A 411 ? 0.2587 0.2900 0.2738 -0.0002 -0.0345 -0.0051 411 LYS A CB 3126 C CG . LYS A 411 ? 0.2809 0.3076 0.2961 0.0004 -0.0364 -0.0043 411 LYS A CG 3127 C CD . LYS A 411 ? 0.3094 0.3354 0.3232 0.0042 -0.0395 -0.0068 411 LYS A CD 3128 C CE . LYS A 411 ? 0.3361 0.3566 0.3490 0.0045 -0.0417 -0.0061 411 LYS A CE 3129 N NZ . LYS A 411 ? 0.3585 0.3758 0.3686 0.0083 -0.0451 -0.0084 411 LYS A NZ 3130 N N . TYR A 412 ? 0.2204 0.2599 0.2337 -0.0058 -0.0291 -0.0047 412 TYR A N 3131 C CA . TYR A 412 ? 0.2161 0.2591 0.2285 -0.0069 -0.0281 -0.0052 412 TYR A CA 3132 C C . TYR A 412 ? 0.2092 0.2475 0.2201 -0.0104 -0.0257 -0.0027 412 TYR A C 3133 O O . TYR A 412 ? 0.2093 0.2463 0.2199 -0.0108 -0.0254 -0.0021 412 TYR A O 3134 C CB . TYR A 412 ? 0.2163 0.2688 0.2276 -0.0079 -0.0274 -0.0074 412 TYR A CB 3135 C CG . TYR A 412 ? 0.2210 0.2792 0.2315 -0.0091 -0.0269 -0.0081 412 TYR A CG 3136 C CD1 . TYR A 412 ? 0.2241 0.2858 0.2360 -0.0055 -0.0289 -0.0096 412 TYR A CD1 3137 C CD2 . TYR A 412 ? 0.2225 0.2829 0.2302 -0.0139 -0.0245 -0.0073 412 TYR A CD2 3138 C CE1 . TYR A 412 ? 0.2240 0.2922 0.2353 -0.0066 -0.0285 -0.0101 412 TYR A CE1 3139 C CE2 . TYR A 412 ? 0.2253 0.2918 0.2320 -0.0156 -0.0241 -0.0079 412 TYR A CE2 3140 C CZ . TYR A 412 ? 0.2256 0.2965 0.2344 -0.0118 -0.0261 -0.0092 412 TYR A CZ 3141 O OH . TYR A 412 ? 0.2261 0.3039 0.2343 -0.0133 -0.0259 -0.0097 412 TYR A OH 3142 N N . VAL A 413 ? 0.2129 0.2480 0.2224 -0.0126 -0.0239 -0.0012 413 VAL A N 3143 C CA . VAL A 413 ? 0.2128 0.2422 0.2197 -0.0153 -0.0214 0.0012 413 VAL A CA 3144 C C . VAL A 413 ? 0.2160 0.2393 0.2247 -0.0137 -0.0219 0.0032 413 VAL A C 3145 O O . VAL A 413 ? 0.2115 0.2321 0.2187 -0.0148 -0.0208 0.0043 413 VAL A O 3146 C CB . VAL A 413 ? 0.2155 0.2424 0.2204 -0.0171 -0.0197 0.0024 413 VAL A CB 3147 C CG1 . VAL A 413 ? 0.2230 0.2423 0.2251 -0.0185 -0.0173 0.0053 413 VAL A CG1 3148 C CG2 . VAL A 413 ? 0.2181 0.2505 0.2200 -0.0200 -0.0186 0.0008 413 VAL A CG2 3149 N N . GLU A 414 ? 0.2221 0.2436 0.2336 -0.0112 -0.0239 0.0037 414 GLU A N 3150 C CA . GLU A 414 ? 0.2367 0.2530 0.2498 -0.0100 -0.0246 0.0059 414 GLU A CA 3151 C C . GLU A 414 ? 0.2344 0.2513 0.2484 -0.0087 -0.0263 0.0049 414 GLU A C 3152 O O . GLU A 414 ? 0.2243 0.2377 0.2379 -0.0093 -0.0255 0.0066 414 GLU A O 3153 C CB . GLU A 414 ? 0.2498 0.2642 0.2651 -0.0084 -0.0265 0.0068 414 GLU A CB 3154 C CG . GLU A 414 ? 0.2686 0.2783 0.2855 -0.0079 -0.0271 0.0097 414 GLU A CG 3155 C CD . GLU A 414 ? 0.2849 0.2916 0.3007 -0.0092 -0.0241 0.0127 414 GLU A CD 3156 O OE1 . GLU A 414 ? 0.3138 0.3206 0.3271 -0.0106 -0.0216 0.0127 414 GLU A OE1 3157 O OE2 . GLU A 414 ? 0.3012 0.3050 0.3183 -0.0088 -0.0243 0.0151 414 GLU A OE2 3158 N N . ASP A 415 ? 0.2386 0.2597 0.2532 -0.0068 -0.0285 0.0023 415 ASP A N 3159 C CA . ASP A 415 ? 0.2483 0.2704 0.2632 -0.0053 -0.0301 0.0012 415 ASP A CA 3160 C C . ASP A 415 ? 0.2335 0.2571 0.2468 -0.0077 -0.0279 0.0015 415 ASP A C 3161 O O . ASP A 415 ? 0.2306 0.2517 0.2439 -0.0075 -0.0283 0.0023 415 ASP A O 3162 C CB . ASP A 415 ? 0.2685 0.2962 0.2837 -0.0025 -0.0322 -0.0018 415 ASP A CB 3163 C CG . ASP A 415 ? 0.3114 0.3386 0.3268 0.0001 -0.0346 -0.0027 415 ASP A CG 3164 O OD1 . ASP A 415 ? 0.3555 0.3764 0.3713 0.0009 -0.0361 -0.0013 415 ASP A OD1 3165 O OD2 . ASP A 415 ? 0.3540 0.3873 0.3690 0.0014 -0.0350 -0.0047 415 ASP A OD2 3166 N N . THR A 416 ? 0.2198 0.2474 0.2311 -0.0101 -0.0258 0.0008 416 THR A N 3167 C CA . THR A 416 ? 0.2160 0.2447 0.2245 -0.0132 -0.0238 0.0011 416 THR A CA 3168 C C . THR A 416 ? 0.2072 0.2282 0.2142 -0.0147 -0.0220 0.0038 416 THR A C 3169 O O . THR A 416 ? 0.2023 0.2220 0.2084 -0.0154 -0.0217 0.0043 416 THR A O 3170 C CB . THR A 416 ? 0.2168 0.2499 0.2226 -0.0163 -0.0220 0.0002 416 THR A CB 3171 O OG1 . THR A 416 ? 0.2261 0.2677 0.2334 -0.0147 -0.0236 -0.0023 416 THR A OG1 3172 C CG2 . THR A 416 ? 0.2188 0.2519 0.2205 -0.0203 -0.0199 0.0007 416 THR A CG2 3173 N N . LYS A 417 ? 0.2016 0.2180 0.2084 -0.0148 -0.0208 0.0056 417 LYS A N 3174 C CA . LYS A 417 ? 0.2041 0.2135 0.2093 -0.0156 -0.0189 0.0083 417 LYS A CA 3175 C C . LYS A 417 ? 0.2000 0.2069 0.2077 -0.0137 -0.0204 0.0095 417 LYS A C 3176 O O . LYS A 417 ? 0.1941 0.1978 0.2002 -0.0146 -0.0192 0.0107 417 LYS A O 3177 C CB . LYS A 417 ? 0.2035 0.2098 0.2086 -0.0152 -0.0178 0.0101 417 LYS A CB 3178 C CG . LYS A 417 ? 0.2119 0.2119 0.2158 -0.0150 -0.0158 0.0132 417 LYS A CG 3179 C CD . LYS A 417 ? 0.2207 0.2185 0.2244 -0.0143 -0.0146 0.0151 417 LYS A CD 3180 C CE . LYS A 417 ? 0.2272 0.2201 0.2306 -0.0130 -0.0130 0.0183 417 LYS A CE 3181 N NZ . LYS A 417 ? 0.2430 0.2349 0.2468 -0.0118 -0.0121 0.0204 417 LYS A NZ 3182 N N . ILE A 418 ? 0.1971 0.2051 0.2083 -0.0113 -0.0231 0.0090 418 ILE A N 3183 C CA . ILE A 418 ? 0.1980 0.2029 0.2111 -0.0098 -0.0249 0.0103 418 ILE A CA 3184 C C . ILE A 418 ? 0.1957 0.2021 0.2083 -0.0099 -0.0257 0.0091 418 ILE A C 3185 O O . ILE A 418 ? 0.1882 0.1914 0.2006 -0.0101 -0.0255 0.0106 418 ILE A O 3186 C CB . ILE A 418 ? 0.2025 0.2076 0.2182 -0.0077 -0.0280 0.0099 418 ILE A CB 3187 C CG1 . ILE A 418 ? 0.2047 0.2082 0.2212 -0.0079 -0.0273 0.0118 418 ILE A CG1 3188 C CG2 . ILE A 418 ? 0.2036 0.2055 0.2205 -0.0066 -0.0303 0.0110 418 ILE A CG2 3189 C CD1 . ILE A 418 ? 0.2180 0.2219 0.2362 -0.0064 -0.0303 0.0110 418 ILE A CD1 3190 N N . ASP A 419 ? 0.1937 0.2055 0.2057 -0.0096 -0.0265 0.0064 419 ASP A N 3191 C CA . ASP A 419 ? 0.1993 0.2133 0.2109 -0.0095 -0.0274 0.0054 419 ASP A CA 3192 C C . ASP A 419 ? 0.1927 0.2048 0.2013 -0.0127 -0.0245 0.0067 419 ASP A C 3193 O O . ASP A 419 ? 0.1937 0.2042 0.2019 -0.0129 -0.0248 0.0073 419 ASP A O 3194 C CB . ASP A 419 ? 0.2094 0.2310 0.2212 -0.0084 -0.0286 0.0025 419 ASP A CB 3195 C CG . ASP A 419 ? 0.2359 0.2584 0.2496 -0.0044 -0.0320 0.0010 419 ASP A CG 3196 O OD1 . ASP A 419 ? 0.2513 0.2679 0.2660 -0.0029 -0.0336 0.0023 419 ASP A OD1 3197 O OD2 . ASP A 419 ? 0.2504 0.2794 0.2642 -0.0027 -0.0330 -0.0013 419 ASP A OD2 3198 N N . LEU A 420 ? 0.1891 0.2009 0.1950 -0.0152 -0.0219 0.0070 420 LEU A N 3199 C CA . LEU A 420 ? 0.1916 0.2000 0.1931 -0.0184 -0.0192 0.0082 420 LEU A CA 3200 C C . LEU A 420 ? 0.1927 0.1939 0.1937 -0.0180 -0.0180 0.0108 420 LEU A C 3201 O O . LEU A 420 ? 0.1971 0.1959 0.1960 -0.0192 -0.0172 0.0115 420 LEU A O 3202 C CB . LEU A 420 ? 0.1916 0.2003 0.1892 -0.0213 -0.0168 0.0079 420 LEU A CB 3203 C CG . LEU A 420 ? 0.1893 0.2061 0.1861 -0.0230 -0.0175 0.0055 420 LEU A CG 3204 C CD1 . LEU A 420 ? 0.1904 0.2082 0.1843 -0.0253 -0.0160 0.0051 420 LEU A CD1 3205 C CD2 . LEU A 420 ? 0.1928 0.2112 0.1864 -0.0259 -0.0170 0.0052 420 LEU A CD2 3206 N N . TRP A 421 ? 0.1963 0.1947 0.1994 -0.0162 -0.0179 0.0124 421 TRP A N 3207 C CA . TRP A 421 ? 0.1982 0.1913 0.2015 -0.0154 -0.0170 0.0151 421 TRP A CA 3208 C C . TRP A 421 ? 0.1991 0.1922 0.2051 -0.0142 -0.0193 0.0154 421 TRP A C 3209 O O . TRP A 421 ? 0.1994 0.1889 0.2040 -0.0147 -0.0181 0.0171 421 TRP A O 3210 C CB . TRP A 421 ? 0.1967 0.1882 0.2016 -0.0140 -0.0165 0.0169 421 TRP A CB 3211 C CG . TRP A 421 ? 0.1998 0.1882 0.2003 -0.0152 -0.0132 0.0177 421 TRP A CG 3212 C CD1 . TRP A 421 ? 0.2019 0.1914 0.2012 -0.0156 -0.0125 0.0170 421 TRP A CD1 3213 C CD2 . TRP A 421 ? 0.2043 0.1871 0.1997 -0.0162 -0.0101 0.0193 421 TRP A CD2 3214 N NE1 . TRP A 421 ? 0.2091 0.1936 0.2028 -0.0168 -0.0093 0.0182 421 TRP A NE1 3215 C CE2 . TRP A 421 ? 0.2129 0.1930 0.2038 -0.0170 -0.0078 0.0195 421 TRP A CE2 3216 C CE3 . TRP A 421 ? 0.2097 0.1891 0.2034 -0.0163 -0.0092 0.0205 421 TRP A CE3 3217 C CZ2 . TRP A 421 ? 0.2173 0.1908 0.2017 -0.0178 -0.0046 0.0208 421 TRP A CZ2 3218 C CZ3 . TRP A 421 ? 0.2188 0.1921 0.2062 -0.0171 -0.0059 0.0217 421 TRP A CZ3 3219 C CH2 . TRP A 421 ? 0.2237 0.1938 0.2063 -0.0177 -0.0037 0.0219 421 TRP A CH2 3220 N N . SER A 422 ? 0.1971 0.1935 0.2062 -0.0126 -0.0225 0.0138 422 SER A N 3221 C CA . SER A 422 ? 0.2012 0.1969 0.2120 -0.0114 -0.0251 0.0140 422 SER A CA 3222 C C . SER A 422 ? 0.2007 0.1969 0.2094 -0.0127 -0.0246 0.0133 422 SER A C 3223 O O . SER A 422 ? 0.1959 0.1892 0.2045 -0.0128 -0.0249 0.0147 422 SER A O 3224 C CB . SER A 422 ? 0.2016 0.1998 0.2148 -0.0091 -0.0287 0.0122 422 SER A CB 3225 O OG . SER A 422 ? 0.2062 0.2036 0.2210 -0.0083 -0.0293 0.0129 422 SER A OG 3226 N N . TYR A 423 ? 0.2032 0.2034 0.2100 -0.0140 -0.0238 0.0114 423 TYR A N 3227 C CA . TYR A 423 ? 0.2101 0.2114 0.2143 -0.0161 -0.0230 0.0109 423 TYR A CA 3228 C C . TYR A 423 ? 0.2079 0.2033 0.2085 -0.0183 -0.0199 0.0130 423 TYR A C 3229 O O . TYR A 423 ? 0.2039 0.1973 0.2036 -0.0189 -0.0200 0.0138 423 TYR A O 3230 C CB . TYR A 423 ? 0.2145 0.2221 0.2169 -0.0178 -0.0225 0.0087 423 TYR A CB 3231 C CG . TYR A 423 ? 0.2229 0.2319 0.2223 -0.0205 -0.0217 0.0085 423 TYR A CG 3232 C CD1 . TYR A 423 ? 0.2324 0.2456 0.2333 -0.0192 -0.0241 0.0075 423 TYR A CD1 3233 C CD2 . TYR A 423 ? 0.2282 0.2335 0.2225 -0.0241 -0.0187 0.0094 423 TYR A CD2 3234 C CE1 . TYR A 423 ? 0.2402 0.2550 0.2384 -0.0218 -0.0235 0.0075 423 TYR A CE1 3235 C CE2 . TYR A 423 ? 0.2368 0.2428 0.2277 -0.0270 -0.0181 0.0094 423 TYR A CE2 3236 C CZ . TYR A 423 ? 0.2481 0.2594 0.2413 -0.0260 -0.0206 0.0084 423 TYR A CZ 3237 O OH . TYR A 423 ? 0.2736 0.2864 0.2638 -0.0289 -0.0203 0.0084 423 TYR A OH 3238 N N . ASN A 424 ? 0.2075 0.1999 0.2057 -0.0193 -0.0173 0.0140 424 ASN A N 3239 C CA . ASN A 424 ? 0.2114 0.1975 0.2053 -0.0207 -0.0142 0.0160 424 ASN A CA 3240 C C . ASN A 424 ? 0.2122 0.1949 0.2082 -0.0189 -0.0145 0.0182 424 ASN A C 3241 O O . ASN A 424 ? 0.2171 0.1964 0.2104 -0.0199 -0.0133 0.0193 424 ASN A O 3242 C CB . ASN A 424 ? 0.2123 0.1950 0.2033 -0.0210 -0.0116 0.0169 424 ASN A CB 3243 C CG . ASN A 424 ? 0.2143 0.1987 0.2013 -0.0237 -0.0106 0.0152 424 ASN A CG 3244 O OD1 . ASN A 424 ? 0.2173 0.2045 0.2023 -0.0261 -0.0111 0.0137 424 ASN A OD1 3245 N ND2 . ASN A 424 ? 0.2098 0.1925 0.1952 -0.0236 -0.0092 0.0156 424 ASN A ND2 3246 N N . ALA A 425 ? 0.2086 0.1926 0.2092 -0.0166 -0.0165 0.0189 425 ALA A N 3247 C CA . ALA A 425 ? 0.2229 0.2047 0.2258 -0.0154 -0.0172 0.0212 425 ALA A CA 3248 C C . ALA A 425 ? 0.2302 0.2122 0.2336 -0.0157 -0.0192 0.0208 425 ALA A C 3249 O O . ALA A 425 ? 0.2435 0.2225 0.2456 -0.0162 -0.0182 0.0226 425 ALA A O 3250 C CB . ALA A 425 ? 0.2096 0.1931 0.2168 -0.0135 -0.0194 0.0219 425 ALA A CB 3251 N N . GLU A 426 ? 0.2421 0.2277 0.2470 -0.0153 -0.0220 0.0185 426 GLU A N 3252 C CA . GLU A 426 ? 0.2572 0.2434 0.2624 -0.0153 -0.0241 0.0179 426 GLU A CA 3253 C C . GLU A 426 ? 0.2535 0.2383 0.2547 -0.0177 -0.0219 0.0180 426 GLU A C 3254 O O . GLU A 426 ? 0.2505 0.2327 0.2511 -0.0182 -0.0220 0.0194 426 GLU A O 3255 C CB . GLU A 426 ? 0.2748 0.2659 0.2816 -0.0139 -0.0270 0.0152 426 GLU A CB 3256 C CG . GLU A 426 ? 0.3047 0.2959 0.3122 -0.0128 -0.0300 0.0147 426 GLU A CG 3257 C CD . GLU A 426 ? 0.3245 0.3120 0.3339 -0.0112 -0.0327 0.0162 426 GLU A CD 3258 O OE1 . GLU A 426 ? 0.3233 0.3102 0.3342 -0.0101 -0.0336 0.0164 426 GLU A OE1 3259 O OE2 . GLU A 426 ? 0.3720 0.3571 0.3809 -0.0115 -0.0339 0.0172 426 GLU A OE2 3260 N N . LEU A 427 ? 0.2459 0.2320 0.2440 -0.0196 -0.0198 0.0169 427 LEU A N 3261 C CA . LEU A 427 ? 0.2514 0.2354 0.2447 -0.0225 -0.0177 0.0171 427 LEU A CA 3262 C C . LEU A 427 ? 0.2501 0.2274 0.2403 -0.0230 -0.0147 0.0195 427 LEU A C 3263 O O . LEU A 427 ? 0.2541 0.2287 0.2419 -0.0242 -0.0141 0.0203 427 LEU A O 3264 C CB . LEU A 427 ? 0.2542 0.2405 0.2439 -0.0249 -0.0162 0.0155 427 LEU A CB 3265 C CG . LEU A 427 ? 0.2623 0.2462 0.2459 -0.0286 -0.0142 0.0156 427 LEU A CG 3266 C CD1 . LEU A 427 ? 0.2647 0.2520 0.2494 -0.0292 -0.0164 0.0150 427 LEU A CD1 3267 C CD2 . LEU A 427 ? 0.2723 0.2584 0.2520 -0.0316 -0.0130 0.0142 427 LEU A CD2 3268 N N . LEU A 428 ? 0.2491 0.2238 0.2393 -0.0217 -0.0130 0.0208 428 LEU A N 3269 C CA . LEU A 428 ? 0.2624 0.2313 0.2493 -0.0214 -0.0099 0.0232 428 LEU A CA 3270 C C . LEU A 428 ? 0.2551 0.2232 0.2444 -0.0203 -0.0109 0.0250 428 LEU A C 3271 O O . LEU A 428 ? 0.2501 0.2142 0.2359 -0.0211 -0.0090 0.0262 428 LEU A O 3272 C CB . LEU A 428 ? 0.2710 0.2388 0.2585 -0.0195 -0.0084 0.0243 428 LEU A CB 3273 C CG . LEU A 428 ? 0.2949 0.2573 0.2787 -0.0183 -0.0050 0.0269 428 LEU A CG 3274 C CD1 . LEU A 428 ? 0.3175 0.2738 0.2931 -0.0205 -0.0021 0.0265 428 LEU A CD1 3275 C CD2 . LEU A 428 ? 0.3015 0.2640 0.2863 -0.0162 -0.0038 0.0280 428 LEU A CD2 3276 N N . VAL A 429 ? 0.2570 0.2285 0.2519 -0.0188 -0.0140 0.0251 429 VAL A N 3277 C CA . VAL A 429 ? 0.2629 0.2336 0.2599 -0.0182 -0.0152 0.0271 429 VAL A CA 3278 C C . VAL A 429 ? 0.2660 0.2363 0.2616 -0.0198 -0.0165 0.0262 429 VAL A C 3279 O O . VAL A 429 ? 0.2665 0.2342 0.2606 -0.0203 -0.0156 0.0279 429 VAL A O 3280 C CB . VAL A 429 ? 0.2757 0.2490 0.2779 -0.0167 -0.0183 0.0277 429 VAL A CB 3281 C CG1 . VAL A 429 ? 0.2934 0.2659 0.2972 -0.0168 -0.0199 0.0298 429 VAL A CG1 3282 C CG2 . VAL A 429 ? 0.2749 0.2488 0.2782 -0.0154 -0.0167 0.0289 429 VAL A CG2 3283 N N . ALA A 430 ? 0.2618 0.2351 0.2577 -0.0204 -0.0185 0.0238 430 ALA A N 3284 C CA . ALA A 430 ? 0.2703 0.2440 0.2647 -0.0218 -0.0197 0.0230 430 ALA A CA 3285 C C . ALA A 430 ? 0.2701 0.2400 0.2587 -0.0243 -0.0163 0.0235 430 ALA A C 3286 O O . ALA A 430 ? 0.2725 0.2402 0.2595 -0.0253 -0.0162 0.0245 430 ALA A O 3287 C CB . ALA A 430 ? 0.2615 0.2404 0.2570 -0.0217 -0.0221 0.0203 430 ALA A CB 3288 N N . LEU A 431 ? 0.2656 0.2340 0.2505 -0.0253 -0.0135 0.0230 431 LEU A N 3289 C CA . LEU A 431 ? 0.2762 0.2393 0.2541 -0.0277 -0.0102 0.0235 431 LEU A CA 3290 C C . LEU A 431 ? 0.2795 0.2373 0.2555 -0.0265 -0.0077 0.0260 431 LEU A C 3291 O O . LEU A 431 ? 0.2867 0.2408 0.2585 -0.0280 -0.0064 0.0267 431 LEU A O 3292 C CB . LEU A 431 ? 0.2770 0.2387 0.2505 -0.0292 -0.0080 0.0225 431 LEU A CB 3293 C CG . LEU A 431 ? 0.2849 0.2518 0.2579 -0.0316 -0.0095 0.0201 431 LEU A CG 3294 C CD1 . LEU A 431 ? 0.2941 0.2585 0.2625 -0.0329 -0.0072 0.0196 431 LEU A CD1 3295 C CD2 . LEU A 431 ? 0.2909 0.2585 0.2605 -0.0348 -0.0100 0.0195 431 LEU A CD2 3296 N N . GLU A 432 ? 0.2879 0.2456 0.2667 -0.0239 -0.0071 0.0275 432 GLU A N 3297 C CA . GLU A 432 ? 0.3019 0.2563 0.2797 -0.0222 -0.0048 0.0302 432 GLU A CA 3298 C C . GLU A 432 ? 0.2880 0.2436 0.2685 -0.0225 -0.0067 0.0313 432 GLU A C 3299 O O . GLU A 432 ? 0.2908 0.2428 0.2677 -0.0227 -0.0047 0.0327 432 GLU A O 3300 C CB . GLU A 432 ? 0.3207 0.2767 0.3019 -0.0194 -0.0042 0.0317 432 GLU A CB 3301 C CG . GLU A 432 ? 0.3596 0.3131 0.3369 -0.0189 -0.0017 0.0311 432 GLU A CG 3302 C CD . GLU A 432 ? 0.4131 0.3596 0.3829 -0.0182 0.0024 0.0325 432 GLU A CD 3303 O OE1 . GLU A 432 ? 0.4487 0.3923 0.4157 -0.0184 0.0036 0.0336 432 GLU A OE1 3304 O OE2 . GLU A 432 ? 0.5012 0.4448 0.4674 -0.0172 0.0045 0.0324 432 GLU A OE2 3305 N N . ASN A 433 ? 0.2648 0.2247 0.2508 -0.0223 -0.0106 0.0307 433 ASN A N 3306 C CA . ASN A 433 ? 0.2618 0.2223 0.2499 -0.0227 -0.0128 0.0318 433 ASN A CA 3307 C C . ASN A 433 ? 0.2723 0.2308 0.2565 -0.0249 -0.0126 0.0309 433 ASN A C 3308 O O . ASN A 433 ? 0.2690 0.2256 0.2520 -0.0255 -0.0122 0.0325 433 ASN A O 3309 C CB . ASN A 433 ? 0.2537 0.2179 0.2472 -0.0219 -0.0171 0.0312 433 ASN A CB 3310 C CG . ASN A 433 ? 0.2484 0.2143 0.2456 -0.0202 -0.0177 0.0327 433 ASN A CG 3311 O OD1 . ASN A 433 ? 0.2545 0.2196 0.2509 -0.0193 -0.0149 0.0347 433 ASN A OD1 3312 N ND2 . ASN A 433 ? 0.2421 0.2103 0.2429 -0.0195 -0.0213 0.0318 433 ASN A ND2 3313 N N . GLN A 434 ? 0.2736 0.2329 0.2556 -0.0265 -0.0129 0.0286 434 GLN A N 3314 C CA . GLN A 434 ? 0.2932 0.2510 0.2710 -0.0291 -0.0125 0.0279 434 GLN A CA 3315 C C . GLN A 434 ? 0.2917 0.2433 0.2630 -0.0301 -0.0085 0.0292 434 GLN A C 3316 O O . GLN A 434 ? 0.2873 0.2365 0.2560 -0.0314 -0.0081 0.0300 434 GLN A O 3317 C CB . GLN A 434 ? 0.3210 0.2818 0.2973 -0.0309 -0.0133 0.0254 434 GLN A CB 3318 C CG . GLN A 434 ? 0.3495 0.3098 0.3215 -0.0340 -0.0133 0.0248 434 GLN A CG 3319 C CD . GLN A 434 ? 0.3912 0.3542 0.3668 -0.0335 -0.0167 0.0249 434 GLN A CD 3320 O OE1 . GLN A 434 ? 0.4117 0.3795 0.3922 -0.0316 -0.0200 0.0240 434 GLN A OE1 3321 N NE2 . GLN A 434 ? 0.4387 0.3981 0.4116 -0.0347 -0.0160 0.0263 434 GLN A NE2 3322 N N . HIS A 435 ? 0.3021 0.2508 0.2707 -0.0290 -0.0055 0.0296 435 HIS A N 3323 C CA . HIS A 435 ? 0.3277 0.2695 0.2891 -0.0292 -0.0015 0.0308 435 HIS A CA 3324 C C . HIS A 435 ? 0.3250 0.2660 0.2878 -0.0272 -0.0005 0.0333 435 HIS A C 3325 O O . HIS A 435 ? 0.3284 0.2647 0.2859 -0.0279 0.0015 0.0342 435 HIS A O 3326 C CB . HIS A 435 ? 0.3429 0.2816 0.3008 -0.0280 0.0011 0.0306 435 HIS A CB 3327 C CG . HIS A 435 ? 0.3719 0.3023 0.3211 -0.0276 0.0054 0.0317 435 HIS A CG 3328 N ND1 . HIS A 435 ? 0.3920 0.3205 0.3409 -0.0240 0.0078 0.0339 435 HIS A ND1 3329 C CD2 . HIS A 435 ? 0.3979 0.3211 0.3374 -0.0304 0.0076 0.0309 435 HIS A CD2 3330 C CE1 . HIS A 435 ? 0.4031 0.3231 0.3425 -0.0239 0.0115 0.0344 435 HIS A CE1 3331 N NE2 . HIS A 435 ? 0.4185 0.3346 0.3518 -0.0280 0.0113 0.0324 435 HIS A NE2 3332 N N . THR A 436 ? 0.3155 0.2611 0.2852 -0.0250 -0.0023 0.0346 436 THR A N 3333 C CA . THR A 436 ? 0.3089 0.2552 0.2806 -0.0235 -0.0019 0.0373 436 THR A CA 3334 C C . THR A 436 ? 0.3125 0.2589 0.2844 -0.0255 -0.0038 0.0376 436 THR A C 3335 O O . THR A 436 ? 0.3200 0.2639 0.2888 -0.0254 -0.0017 0.0393 436 THR A O 3336 C CB . THR A 436 ? 0.3033 0.2548 0.2819 -0.0214 -0.0036 0.0387 436 THR A CB 3337 O OG1 . THR A 436 ? 0.2997 0.2504 0.2770 -0.0193 -0.0012 0.0389 436 THR A OG1 3338 C CG2 . THR A 436 ? 0.3006 0.2543 0.2817 -0.0205 -0.0037 0.0418 436 THR A CG2 3339 N N . ILE A 437 ? 0.3067 0.2559 0.2818 -0.0270 -0.0076 0.0360 437 ILE A N 3340 C CA . ILE A 437 ? 0.3258 0.2749 0.3005 -0.0290 -0.0096 0.0359 437 ILE A CA 3341 C C . ILE A 437 ? 0.3379 0.2822 0.3054 -0.0311 -0.0069 0.0354 437 ILE A C 3342 O O . ILE A 437 ? 0.3336 0.2758 0.2989 -0.0319 -0.0061 0.0367 437 ILE A O 3343 C CB . ILE A 437 ? 0.3263 0.2792 0.3050 -0.0296 -0.0140 0.0340 437 ILE A CB 3344 C CG1 . ILE A 437 ? 0.3311 0.2873 0.3159 -0.0277 -0.0169 0.0348 437 ILE A CG1 3345 C CG2 . ILE A 437 ? 0.3266 0.2790 0.3038 -0.0316 -0.0159 0.0337 437 ILE A CG2 3346 C CD1 . ILE A 437 ? 0.3466 0.3026 0.3331 -0.0275 -0.0174 0.0376 437 ILE A CD1 3347 N N . ASP A 438 ? 0.3377 0.2801 0.3010 -0.0323 -0.0054 0.0335 438 ASP A N 3348 C CA . ASP A 438 ? 0.3555 0.2922 0.3105 -0.0348 -0.0028 0.0330 438 ASP A CA 3349 C C . ASP A 438 ? 0.3487 0.2792 0.2980 -0.0336 0.0013 0.0348 438 ASP A C 3350 O O . ASP A 438 ? 0.3657 0.2927 0.3104 -0.0352 0.0023 0.0353 438 ASP A O 3351 C CB . ASP A 438 ? 0.3847 0.3201 0.3355 -0.0367 -0.0020 0.0309 438 ASP A CB 3352 C CG . ASP A 438 ? 0.4082 0.3500 0.3631 -0.0384 -0.0056 0.0289 438 ASP A CG 3353 O OD1 . ASP A 438 ? 0.4349 0.3810 0.3948 -0.0380 -0.0088 0.0290 438 ASP A OD1 3354 O OD2 . ASP A 438 ? 0.4394 0.3820 0.3920 -0.0399 -0.0054 0.0273 438 ASP A OD2 3355 N N . LEU A 439 ? 0.3360 0.2655 0.2854 -0.0305 0.0036 0.0359 439 LEU A N 3356 C CA . LEU A 439 ? 0.3463 0.2705 0.2901 -0.0283 0.0077 0.0377 439 LEU A CA 3357 C C . LEU A 439 ? 0.3430 0.2698 0.2901 -0.0272 0.0074 0.0401 439 LEU A C 3358 O O . LEU A 439 ? 0.3369 0.2592 0.2783 -0.0267 0.0103 0.0412 439 LEU A O 3359 C CB . LEU A 439 ? 0.3559 0.2794 0.2996 -0.0247 0.0101 0.0385 439 LEU A CB 3360 C CG . LEU A 439 ? 0.3558 0.2858 0.3074 -0.0213 0.0093 0.0405 439 LEU A CG 3361 C CD1 . LEU A 439 ? 0.3515 0.2816 0.3021 -0.0185 0.0120 0.0434 439 LEU A CD1 3362 C CD2 . LEU A 439 ? 0.3612 0.2915 0.3133 -0.0192 0.0103 0.0401 439 LEU A CD2 3363 N N . THR A 440 ? 0.3263 0.2600 0.2819 -0.0270 0.0040 0.0409 440 THR A N 3364 C CA . THR A 440 ? 0.3393 0.2756 0.2977 -0.0265 0.0034 0.0433 440 THR A CA 3365 C C . THR A 440 ? 0.3556 0.2902 0.3118 -0.0297 0.0018 0.0427 440 THR A C 3366 O O . THR A 440 ? 0.3936 0.3265 0.3470 -0.0298 0.0035 0.0443 440 THR A O 3367 C CB . THR A 440 ? 0.3243 0.2677 0.2914 -0.0256 0.0002 0.0447 440 THR A CB 3368 O OG1 . THR A 440 ? 0.3124 0.2581 0.2835 -0.0271 -0.0038 0.0426 440 THR A OG1 3369 C CG2 . THR A 440 ? 0.3255 0.2712 0.2945 -0.0223 0.0021 0.0461 440 THR A CG2 3370 N N . ASP A 441 ? 0.3568 0.2921 0.3139 -0.0322 -0.0011 0.0404 441 ASP A N 3371 C CA . ASP A 441 ? 0.3769 0.3102 0.3309 -0.0353 -0.0023 0.0397 441 ASP A CA 3372 C C . ASP A 441 ? 0.4011 0.3273 0.3457 -0.0363 0.0018 0.0396 441 ASP A C 3373 O O . ASP A 441 ? 0.3969 0.3206 0.3381 -0.0379 0.0024 0.0403 441 ASP A O 3374 C CB . ASP A 441 ? 0.3890 0.3248 0.3447 -0.0374 -0.0056 0.0373 441 ASP A CB 3375 C CG . ASP A 441 ? 0.4081 0.3496 0.3715 -0.0367 -0.0102 0.0372 441 ASP A CG 3376 O OD1 . ASP A 441 ? 0.4042 0.3475 0.3716 -0.0354 -0.0114 0.0391 441 ASP A OD1 3377 O OD2 . ASP A 441 ? 0.4228 0.3670 0.3880 -0.0374 -0.0129 0.0352 441 ASP A OD2 3378 N N . SER A 442 ? 0.3970 0.3193 0.3369 -0.0357 0.0045 0.0385 442 SER A N 3379 C CA . SER A 442 ? 0.4227 0.3366 0.3522 -0.0368 0.0082 0.0382 442 SER A CA 3380 C C . SER A 442 ? 0.4110 0.3216 0.3370 -0.0342 0.0116 0.0405 442 SER A C 3381 O O . SER A 442 ? 0.4356 0.3409 0.3547 -0.0358 0.0133 0.0406 442 SER A O 3382 C CB . SER A 442 ? 0.4361 0.3455 0.3602 -0.0365 0.0104 0.0368 442 SER A CB 3383 O OG . SER A 442 ? 0.4708 0.3707 0.3836 -0.0378 0.0138 0.0365 442 SER A OG 3384 N N . GLU A 443 ? 0.4020 0.3162 0.3325 -0.0302 0.0127 0.0424 443 GLU A N 3385 C CA . GLU A 443 ? 0.4204 0.3334 0.3483 -0.0274 0.0158 0.0448 443 GLU A CA 3386 C C . GLU A 443 ? 0.4119 0.3269 0.3413 -0.0297 0.0142 0.0459 443 GLU A C 3387 O O . GLU A 443 ? 0.4322 0.3429 0.3554 -0.0292 0.0170 0.0468 443 GLU A O 3388 C CB . GLU A 443 ? 0.4237 0.3424 0.3574 -0.0231 0.0167 0.0470 443 GLU A CB 3389 C CG . GLU A 443 ? 0.4491 0.3650 0.3799 -0.0199 0.0194 0.0466 443 GLU A CG 3390 C CD . GLU A 443 ? 0.4834 0.3886 0.4019 -0.0186 0.0238 0.0460 443 GLU A CD 3391 O OE1 . GLU A 443 ? 0.5064 0.4082 0.4196 -0.0176 0.0264 0.0472 443 GLU A OE1 3392 O OE2 . GLU A 443 ? 0.5042 0.4040 0.4179 -0.0188 0.0247 0.0443 443 GLU A OE2 3393 N N . MET A 444 ? 0.4123 0.3331 0.3491 -0.0320 0.0097 0.0456 444 MET A N 3394 C CA . MET A 444 ? 0.4111 0.3334 0.3491 -0.0344 0.0076 0.0465 444 MET A CA 3395 C C . MET A 444 ? 0.4353 0.3513 0.3655 -0.0376 0.0084 0.0450 444 MET A C 3396 O O . MET A 444 ? 0.4111 0.3245 0.3372 -0.0384 0.0098 0.0461 444 MET A O 3397 C CB . MET A 444 ? 0.4024 0.3309 0.3488 -0.0360 0.0023 0.0463 444 MET A CB 3398 C CG . MET A 444 ? 0.4023 0.3322 0.3500 -0.0384 0.0000 0.0474 444 MET A CG 3399 S SD . MET A 444 ? 0.3906 0.3248 0.3414 -0.0367 0.0009 0.0512 444 MET A SD 3400 C CE . MET A 444 ? 0.4230 0.3513 0.3644 -0.0359 0.0065 0.0519 444 MET A CE 3401 N N . ASN A 445 ? 0.4366 0.3503 0.3644 -0.0397 0.0075 0.0426 445 ASN A N 3402 C CA . ASN A 445 ? 0.4683 0.3766 0.3886 -0.0436 0.0078 0.0412 445 ASN A CA 3403 C C . ASN A 445 ? 0.4522 0.3515 0.3617 -0.0430 0.0126 0.0414 445 ASN A C 3404 O O . ASN A 445 ? 0.4669 0.3620 0.3705 -0.0454 0.0133 0.0415 445 ASN A O 3405 C CB . ASN A 445 ? 0.5070 0.4162 0.4274 -0.0462 0.0056 0.0387 445 ASN A CB 3406 C CG . ASN A 445 ? 0.5413 0.4587 0.4709 -0.0469 0.0006 0.0382 445 ASN A CG 3407 O OD1 . ASN A 445 ? 0.5517 0.4719 0.4847 -0.0476 -0.0016 0.0392 445 ASN A OD1 3408 N ND2 . ASN A 445 ? 0.5791 0.5000 0.5123 -0.0465 -0.0009 0.0367 445 ASN A ND2 3409 N N . LYS A 446 ? 0.4473 0.3434 0.3539 -0.0396 0.0158 0.0416 446 LYS A N 3410 C CA . LYS A 446 ? 0.4873 0.3737 0.3827 -0.0381 0.0206 0.0418 446 LYS A CA 3411 C C . LYS A 446 ? 0.4957 0.3823 0.3901 -0.0359 0.0226 0.0441 446 LYS A C 3412 O O . LYS A 446 ? 0.5075 0.3865 0.3924 -0.0367 0.0252 0.0441 446 LYS A O 3413 C CB . LYS A 446 ? 0.5108 0.3942 0.4037 -0.0342 0.0233 0.0418 446 LYS A CB 3414 C CG . LYS A 446 ? 0.5251 0.4063 0.4160 -0.0368 0.0221 0.0394 446 LYS A CG 3415 C CD . LYS A 446 ? 0.5575 0.4335 0.4437 -0.0332 0.0252 0.0393 446 LYS A CD 3416 C CE . LYS A 446 ? 0.5665 0.4506 0.4624 -0.0285 0.0248 0.0408 446 LYS A CE 3417 N NZ . LYS A 446 ? 0.5798 0.4586 0.4705 -0.0245 0.0281 0.0410 446 LYS A NZ 3418 N N . LEU A 447 ? 0.4755 0.3709 0.3794 -0.0334 0.0213 0.0461 447 LEU A N 3419 C CA . LEU A 447 ? 0.4791 0.3765 0.3831 -0.0315 0.0230 0.0486 447 LEU A CA 3420 C C . LEU A 447 ? 0.4724 0.3680 0.3739 -0.0359 0.0214 0.0482 447 LEU A C 3421 O O . LEU A 447 ? 0.4954 0.3860 0.3895 -0.0355 0.0243 0.0490 447 LEU A O 3422 C CB . LEU A 447 ? 0.4756 0.3836 0.3907 -0.0295 0.0209 0.0508 447 LEU A CB 3423 C CG . LEU A 447 ? 0.4931 0.4057 0.4099 -0.0277 0.0223 0.0538 447 LEU A CG 3424 C CD1 . LEU A 447 ? 0.4991 0.4067 0.4075 -0.0232 0.0280 0.0547 447 LEU A CD1 3425 C CD2 . LEU A 447 ? 0.4780 0.4011 0.4055 -0.0266 0.0197 0.0559 447 LEU A CD2 3426 N N . PHE A 448 ? 0.4502 0.3496 0.3572 -0.0397 0.0169 0.0471 448 PHE A N 3427 C CA . PHE A 448 ? 0.4530 0.3513 0.3581 -0.0440 0.0148 0.0468 448 PHE A CA 3428 C C . PHE A 448 ? 0.4687 0.3573 0.3621 -0.0465 0.0173 0.0453 448 PHE A C 3429 O O . PHE A 448 ? 0.4347 0.3198 0.3227 -0.0481 0.0184 0.0459 448 PHE A O 3430 C CB . PHE A 448 ? 0.4433 0.3476 0.3562 -0.0469 0.0094 0.0458 448 PHE A CB 3431 C CG . PHE A 448 ? 0.4441 0.3484 0.3560 -0.0508 0.0069 0.0457 448 PHE A CG 3432 C CD1 . PHE A 448 ? 0.4382 0.3466 0.3545 -0.0510 0.0051 0.0477 448 PHE A CD1 3433 C CD2 . PHE A 448 ? 0.4565 0.3570 0.3629 -0.0546 0.0062 0.0438 448 PHE A CD2 3434 C CE1 . PHE A 448 ? 0.4506 0.3587 0.3658 -0.0546 0.0027 0.0477 448 PHE A CE1 3435 C CE2 . PHE A 448 ? 0.4504 0.3513 0.3559 -0.0582 0.0038 0.0439 448 PHE A CE2 3436 C CZ . PHE A 448 ? 0.4564 0.3610 0.3664 -0.0581 0.0020 0.0458 448 PHE A CZ 3437 N N . GLU A 449 ? 0.4591 0.4410 0.3459 -0.1049 0.1090 -0.0250 449 GLU A N 3438 C CA . GLU A 449 ? 0.5173 0.4849 0.3972 -0.1135 0.1180 -0.0276 449 GLU A CA 3439 C C . GLU A 449 ? 0.5053 0.4448 0.3723 -0.1028 0.1121 -0.0113 449 GLU A C 3440 O O . GLU A 449 ? 0.5069 0.4475 0.3869 -0.1002 0.1134 -0.0158 449 GLU A O 3441 C CB . GLU A 449 ? 0.5996 0.5551 0.4524 -0.1379 0.1337 -0.0332 449 GLU A CB 3442 C CG . GLU A 449 ? 0.6446 0.6360 0.5183 -0.1514 0.1430 -0.0581 449 GLU A CG 3443 C CD . GLU A 449 ? 0.6757 0.6935 0.5861 -0.1460 0.1426 -0.0765 449 GLU A CD 3444 O OE1 . GLU A 449 ? 0.7308 0.7359 0.6384 -0.1492 0.1473 -0.0761 449 GLU A OE1 3445 O OE2 . GLU A 449 ? 0.6784 0.7283 0.6199 -0.1375 0.1362 -0.0918 449 GLU A OE2 3446 N N . ARG A 450 ? 0.5340 0.4507 0.3766 -0.0959 0.1051 0.0050 450 ARG A N 3447 C CA . ARG A 450 ? 0.5724 0.4654 0.4061 -0.0820 0.0968 0.0178 450 ARG A CA 3448 C C . ARG A 450 ? 0.5249 0.4407 0.3910 -0.0666 0.0888 0.0146 450 ARG A C 3449 O O . ARG A 450 ? 0.5241 0.4312 0.3943 -0.0604 0.0875 0.0157 450 ARG A O 3450 C CB . ARG A 450 ? 0.6303 0.5058 0.4400 -0.0717 0.0859 0.0323 450 ARG A CB 3451 C CG . ARG A 450 ? 0.7281 0.5704 0.4945 -0.0843 0.0903 0.0410 450 ARG A CG 3452 C CD . ARG A 450 ? 0.7884 0.6026 0.5273 -0.0684 0.0756 0.0569 450 ARG A CD 3453 N NE . ARG A 450 ? 0.8051 0.6449 0.5549 -0.0542 0.0634 0.0581 450 ARG A NE 3454 C CZ . ARG A 450 ? 0.8322 0.6826 0.5691 -0.0607 0.0633 0.0583 450 ARG A CZ 3455 N NH1 . ARG A 450 ? 0.8191 0.6594 0.5316 -0.0821 0.0755 0.0571 450 ARG A NH1 3456 N NH2 . ARG A 450 ? 0.8357 0.7105 0.5855 -0.0472 0.0520 0.0575 450 ARG A NH2 3457 N N . THR A 451 ? 0.4667 0.4098 0.3534 -0.0614 0.0837 0.0107 451 THR A N 3458 C CA . THR A 451 ? 0.4220 0.3836 0.3330 -0.0497 0.0765 0.0096 451 THR A CA 3459 C C . THR A 451 ? 0.4112 0.3832 0.3388 -0.0532 0.0811 -0.0006 451 THR A C 3460 O O . THR A 451 ? 0.4162 0.3896 0.3512 -0.0466 0.0786 0.0001 451 THR A O 3461 C CB . THR A 451 ? 0.3977 0.3793 0.3219 -0.0463 0.0705 0.0084 451 THR A CB 3462 O OG1 . THR A 451 ? 0.4012 0.3769 0.3107 -0.0428 0.0659 0.0160 451 THR A OG1 3463 C CG2 . THR A 451 ? 0.3516 0.3469 0.2943 -0.0379 0.0641 0.0089 451 THR A CG2 3464 N N . LYS A 452 ? 0.4229 0.4049 0.3566 -0.0636 0.0879 -0.0126 452 LYS A N 3465 C CA . LYS A 452 ? 0.4433 0.4395 0.3939 -0.0665 0.0915 -0.0262 452 LYS A CA 3466 C C . LYS A 452 ? 0.4694 0.4505 0.4120 -0.0699 0.0976 -0.0260 452 LYS A C 3467 O O . LYS A 452 ? 0.4297 0.4215 0.3863 -0.0649 0.0956 -0.0315 452 LYS A O 3468 C CB . LYS A 452 ? 0.4815 0.4919 0.4381 -0.0791 0.0995 -0.0429 452 LYS A CB 3469 C CG . LYS A 452 ? 0.5101 0.5410 0.4873 -0.0812 0.1023 -0.0615 452 LYS A CG 3470 C CD . LYS A 452 ? 0.5604 0.6117 0.5471 -0.0937 0.1104 -0.0825 452 LYS A CD 3471 C CE . LYS A 452 ? 0.5864 0.6656 0.5997 -0.0907 0.1087 -0.1043 452 LYS A CE 3472 N NZ . LYS A 452 ? 0.5944 0.6827 0.6245 -0.0699 0.0909 -0.1008 452 LYS A NZ 3473 N N . LYS A 453 ? 0.4957 0.4497 0.4136 -0.0783 0.1042 -0.0194 453 LYS A N 3474 C CA . LYS A 453 ? 0.5357 0.4686 0.4436 -0.0831 0.1105 -0.0200 453 LYS A CA 3475 C C . LYS A 453 ? 0.4986 0.4263 0.4110 -0.0669 0.1012 -0.0117 453 LYS A C 3476 O O . LYS A 453 ? 0.4973 0.4250 0.4173 -0.0667 0.1040 -0.0182 453 LYS A O 3477 C CB . LYS A 453 ? 0.5940 0.4906 0.4682 -0.0969 0.1190 -0.0133 453 LYS A CB 3478 C CG . LYS A 453 ? 0.6316 0.5336 0.4969 -0.1178 0.1315 -0.0232 453 LYS A CG 3479 C CD . LYS A 453 ? 0.6372 0.5682 0.5264 -0.1296 0.1417 -0.0463 453 LYS A CD 3480 C CE . LYS A 453 ? 0.6679 0.6094 0.5498 -0.1519 0.1553 -0.0598 453 LYS A CE 3481 N NZ . LYS A 453 ? 0.6799 0.5887 0.5282 -0.1771 0.1718 -0.0596 453 LYS A NZ 3482 N N . GLN A 454 ? 0.4827 0.4105 0.3928 -0.0541 0.0907 -0.0004 454 GLN A N 3483 C CA . GLN A 454 ? 0.4765 0.4065 0.3939 -0.0399 0.0826 0.0034 454 GLN A CA 3484 C C . GLN A 454 ? 0.4224 0.3814 0.3633 -0.0369 0.0813 -0.0045 454 GLN A C 3485 O O . GLN A 454 ? 0.4146 0.3771 0.3623 -0.0313 0.0800 -0.0075 454 GLN A O 3486 C CB . GLN A 454 ? 0.4819 0.4161 0.3970 -0.0284 0.0723 0.0126 454 GLN A CB 3487 C CG . GLN A 454 ? 0.5538 0.4599 0.4448 -0.0239 0.0680 0.0218 454 GLN A CG 3488 C CD . GLN A 454 ? 0.5587 0.4788 0.4538 -0.0111 0.0569 0.0263 454 GLN A CD 3489 O OE1 . GLN A 454 ? 0.5556 0.4832 0.4599 0.0009 0.0501 0.0244 454 GLN A OE1 3490 N NE2 . GLN A 454 ? 0.5482 0.4753 0.4384 -0.0147 0.0558 0.0294 454 GLN A NE2 3491 N N . LEU A 455 ? 0.3786 0.3575 0.3303 -0.0394 0.0801 -0.0079 455 LEU A N 3492 C CA . LEU A 455 ? 0.3560 0.3579 0.3237 -0.0348 0.0752 -0.0119 455 LEU A CA 3493 C C . LEU A 455 ? 0.3487 0.3596 0.3254 -0.0386 0.0797 -0.0242 455 LEU A C 3494 O O . LEU A 455 ? 0.3211 0.3470 0.3060 -0.0338 0.0754 -0.0266 455 LEU A O 3495 C CB . LEU A 455 ? 0.3447 0.3580 0.3186 -0.0343 0.0699 -0.0110 455 LEU A CB 3496 C CG . LEU A 455 ? 0.3288 0.3389 0.2973 -0.0306 0.0648 -0.0006 455 LEU A CG 3497 C CD1 . LEU A 455 ? 0.3345 0.3514 0.3089 -0.0315 0.0606 -0.0017 455 LEU A CD1 3498 C CD2 . LEU A 455 ? 0.3332 0.3504 0.3033 -0.0245 0.0603 0.0048 455 LEU A CD2 3499 N N . ARG A 456 ? 0.3719 0.3749 0.3457 -0.0488 0.0889 -0.0331 456 ARG A N 3500 C CA . ARG A 456 ? 0.3912 0.4046 0.3747 -0.0544 0.0949 -0.0482 456 ARG A CA 3501 C C . ARG A 456 ? 0.3694 0.4116 0.3698 -0.0483 0.0871 -0.0567 456 ARG A C 3502 O O . ARG A 456 ? 0.3524 0.4030 0.3578 -0.0468 0.0826 -0.0584 456 ARG A O 3503 C CB . ARG A 456 ? 0.4230 0.4265 0.4039 -0.0522 0.0972 -0.0481 456 ARG A CB 3504 C CG . ARG A 456 ? 0.4678 0.4367 0.4305 -0.0582 0.1041 -0.0430 456 ARG A CG 3505 C CD . ARG A 456 ? 0.4916 0.4507 0.4503 -0.0754 0.1175 -0.0558 456 ARG A CD 3506 N NE . ARG A 456 ? 0.4962 0.4681 0.4688 -0.0784 0.1223 -0.0714 456 ARG A NE 3507 C CZ . ARG A 456 ? 0.5039 0.4544 0.4711 -0.0810 0.1273 -0.0742 456 ARG A CZ 3508 N NH1 . ARG A 456 ? 0.5420 0.4531 0.4888 -0.0784 0.1262 -0.0616 456 ARG A NH1 3509 N NH2 . ARG A 456 ? 0.5152 0.4833 0.4978 -0.0847 0.1320 -0.0911 456 ARG A NH2 3510 N N . GLU A 457 ? 0.3778 0.4336 0.3854 -0.0435 0.0840 -0.0618 457 GLU A N 3511 C CA . GLU A 457 ? 0.3784 0.4579 0.3971 -0.0362 0.0743 -0.0690 457 GLU A CA 3512 C C . GLU A 457 ? 0.3497 0.4288 0.3615 -0.0265 0.0624 -0.0537 457 GLU A C 3513 O O . GLU A 457 ? 0.3473 0.4395 0.3612 -0.0197 0.0526 -0.0557 457 GLU A O 3514 C CB . GLU A 457 ? 0.4014 0.4979 0.4289 -0.0372 0.0768 -0.0836 457 GLU A CB 3515 C CG . GLU A 457 ? 0.4536 0.5509 0.4879 -0.0502 0.0903 -0.1012 457 GLU A CG 3516 C CD . GLU A 457 ? 0.4774 0.5872 0.5215 -0.0546 0.0914 -0.1142 457 GLU A CD 3517 O OE1 . GLU A 457 ? 0.5263 0.6547 0.5799 -0.0436 0.0787 -0.1184 457 GLU A OE1 3518 O OE2 . GLU A 457 ? 0.5263 0.6266 0.5674 -0.0692 0.1045 -0.1211 457 GLU A OE2 3519 N N . ASN A 458 ? 0.3256 0.3895 0.3275 -0.0265 0.0630 -0.0391 458 ASN A N 3520 C CA . ASN A 458 ? 0.3237 0.3883 0.3181 -0.0216 0.0548 -0.0263 458 ASN A CA 3521 C C . ASN A 458 ? 0.3004 0.3587 0.2927 -0.0193 0.0472 -0.0196 458 ASN A C 3522 O O . ASN A 458 ? 0.3030 0.3580 0.2868 -0.0179 0.0410 -0.0090 458 ASN A O 3523 C CB . ASN A 458 ? 0.3219 0.3799 0.3102 -0.0224 0.0588 -0.0180 458 ASN A CB 3524 C CG . ASN A 458 ? 0.3352 0.3984 0.3265 -0.0227 0.0644 -0.0256 458 ASN A CG 3525 O OD1 . ASN A 458 ? 0.3348 0.4082 0.3319 -0.0237 0.0658 -0.0362 458 ASN A OD1 3526 N ND2 . ASN A 458 ? 0.3426 0.4009 0.3319 -0.0209 0.0667 -0.0224 458 ASN A ND2 3527 N N . ALA A 459 ? 0.2923 0.3491 0.2918 -0.0206 0.0486 -0.0271 459 ALA A N 3528 C CA . ALA A 459 ? 0.2948 0.3459 0.2955 -0.0183 0.0421 -0.0242 459 ALA A CA 3529 C C . ALA A 459 ? 0.3068 0.3679 0.3213 -0.0166 0.0401 -0.0405 459 ALA A C 3530 O O . ALA A 459 ? 0.3221 0.3934 0.3441 -0.0218 0.0483 -0.0541 459 ALA A O 3531 C CB . ALA A 459 ? 0.2906 0.3310 0.2859 -0.0231 0.0478 -0.0164 459 ALA A CB 3532 N N . GLU A 460 ? 0.3082 0.3665 0.3268 -0.0103 0.0297 -0.0412 460 GLU A N 3533 C CA . GLU A 460 ? 0.3183 0.3889 0.3536 -0.0075 0.0269 -0.0599 460 GLU A CA 3534 C C . GLU A 460 ? 0.3275 0.3911 0.3651 -0.0099 0.0272 -0.0589 460 GLU A C 3535 O O . GLU A 460 ? 0.3199 0.3674 0.3480 -0.0087 0.0228 -0.0442 460 GLU A O 3536 C CB . GLU A 460 ? 0.3230 0.3997 0.3654 0.0064 0.0102 -0.0679 460 GLU A CB 3537 C CG . GLU A 460 ? 0.3242 0.4159 0.3680 0.0086 0.0100 -0.0751 460 GLU A CG 3538 C CD . GLU A 460 ? 0.3357 0.4318 0.3814 0.0248 -0.0094 -0.0808 460 GLU A CD 3539 O OE1 . GLU A 460 ? 0.3513 0.4413 0.4029 0.0359 -0.0234 -0.0855 460 GLU A OE1 3540 O OE2 . GLU A 460 ? 0.3327 0.4376 0.3731 0.0272 -0.0117 -0.0812 460 GLU A OE2 3541 N N . ASP A 461 ? 0.3189 0.3975 0.3697 -0.0149 0.0336 -0.0770 461 ASP A N 3542 C CA . ASP A 461 ? 0.3430 0.4215 0.3987 -0.0180 0.0348 -0.0815 461 ASP A CA 3543 C C . ASP A 461 ? 0.3572 0.4352 0.4266 -0.0040 0.0179 -0.0896 461 ASP A C 3544 O O . ASP A 461 ? 0.3465 0.4405 0.4327 0.0048 0.0099 -0.1084 461 ASP A O 3545 C CB . ASP A 461 ? 0.3548 0.4530 0.4188 -0.0305 0.0485 -0.1012 461 ASP A CB 3546 C CG . ASP A 461 ? 0.3688 0.4714 0.4357 -0.0372 0.0529 -0.1078 461 ASP A CG 3547 O OD1 . ASP A 461 ? 0.3723 0.4678 0.4433 -0.0293 0.0429 -0.1041 461 ASP A OD1 3548 O OD2 . ASP A 461 ? 0.3978 0.5112 0.4616 -0.0524 0.0673 -0.1183 461 ASP A OD2 3549 N N . MET A 462 ? 0.3564 0.4157 0.4191 -0.0016 0.0118 -0.0771 462 MET A N 3550 C CA . MET A 462 ? 0.3886 0.4374 0.4602 0.0119 -0.0055 -0.0821 462 MET A CA 3551 C C . MET A 462 ? 0.3954 0.4602 0.4891 0.0131 -0.0061 -0.1053 462 MET A C 3552 O O . MET A 462 ? 0.4198 0.4759 0.5244 0.0258 -0.0213 -0.1135 462 MET A O 3553 C CB . MET A 462 ? 0.4086 0.4277 0.4624 0.0111 -0.0106 -0.0597 462 MET A CB 3554 C CG . MET A 462 ? 0.4448 0.4497 0.4772 0.0096 -0.0114 -0.0393 462 MET A CG 3555 S SD . MET A 462 ? 0.4921 0.4729 0.5043 0.0000 -0.0087 -0.0166 462 MET A SD 3556 C CE . MET A 462 ? 0.5171 0.4750 0.5352 0.0069 -0.0229 -0.0217 462 MET A CE 3557 N N . GLY A 463 ? 0.3757 0.4617 0.4740 -0.0005 0.0100 -0.1159 463 GLY A N 3558 C CA . GLY A 463 ? 0.3744 0.4834 0.4940 -0.0024 0.0122 -0.1418 463 GLY A CA 3559 C C . GLY A 463 ? 0.3879 0.4892 0.5062 -0.0068 0.0135 -0.1388 463 GLY A C 3560 O O . GLY A 463 ? 0.3852 0.5078 0.5207 -0.0100 0.0166 -0.1612 463 GLY A O 3561 N N . ASN A 464 ? 0.3740 0.4491 0.4733 -0.0083 0.0121 -0.1139 464 ASN A N 3562 C CA . ASN A 464 ? 0.3926 0.4609 0.4899 -0.0131 0.0133 -0.1104 464 ASN A CA 3563 C C . ASN A 464 ? 0.3702 0.4376 0.4463 -0.0270 0.0270 -0.0937 464 ASN A C 3564 O O . ASN A 464 ? 0.3936 0.4526 0.4638 -0.0301 0.0267 -0.0853 464 ASN A O 3565 C CB . ASN A 464 ? 0.4188 0.4570 0.5134 -0.0033 -0.0013 -0.0986 464 ASN A CB 3566 C CG . ASN A 464 ? 0.4356 0.4525 0.5078 -0.0042 -0.0021 -0.0731 464 ASN A CG 3567 O OD1 . ASN A 464 ? 0.4050 0.4299 0.4685 -0.0072 0.0046 -0.0668 464 ASN A OD1 3568 N ND2 . ASN A 464 ? 0.4686 0.4588 0.5310 -0.0033 -0.0095 -0.0597 464 ASN A ND2 3569 N N . GLY A 465 ? 0.3409 0.4160 0.4055 -0.0346 0.0377 -0.0899 465 GLY A N 3570 C CA . GLY A 465 ? 0.3377 0.4061 0.3795 -0.0436 0.0470 -0.0727 465 GLY A CA 3571 C C . GLY A 465 ? 0.3319 0.3823 0.3611 -0.0389 0.0430 -0.0516 465 GLY A C 3572 O O . GLY A 465 ? 0.3436 0.3894 0.3576 -0.0429 0.0472 -0.0390 465 GLY A O 3573 N N . CYS A 466 ? 0.3273 0.3695 0.3621 -0.0303 0.0344 -0.0492 466 CYS A N 3574 C CA . CYS A 466 ? 0.3386 0.3672 0.3613 -0.0279 0.0317 -0.0317 466 CYS A CA 3575 C C . CYS A 466 ? 0.3310 0.3614 0.3529 -0.0242 0.0314 -0.0320 466 CYS A C 3576 O O . CYS A 466 ? 0.3269 0.3666 0.3610 -0.0201 0.0286 -0.0464 466 CYS A O 3577 C CB . CYS A 466 ? 0.3908 0.4032 0.4135 -0.0236 0.0212 -0.0248 466 CYS A CB 3578 S SG . CYS A 466 ? 0.4524 0.4614 0.4808 -0.0277 0.0197 -0.0285 466 CYS A SG 3579 N N . PHE A 467 ? 0.3164 0.3413 0.3258 -0.0254 0.0341 -0.0186 467 PHE A N 3580 C CA . PHE A 467 ? 0.3138 0.3397 0.3208 -0.0222 0.0332 -0.0170 467 PHE A CA 3581 C C . PHE A 467 ? 0.3229 0.3379 0.3223 -0.0182 0.0244 -0.0061 467 PHE A C 3582 O O . PHE A 467 ? 0.3269 0.3343 0.3182 -0.0221 0.0243 0.0042 467 PHE A O 3583 C CB . PHE A 467 ? 0.3064 0.3339 0.3041 -0.0269 0.0428 -0.0116 467 PHE A CB 3584 C CG . PHE A 467 ? 0.3130 0.3438 0.3095 -0.0334 0.0521 -0.0191 467 PHE A CG 3585 C CD1 . PHE A 467 ? 0.3272 0.3658 0.3298 -0.0366 0.0571 -0.0319 467 PHE A CD1 3586 C CD2 . PHE A 467 ? 0.3208 0.3470 0.3080 -0.0377 0.0561 -0.0140 467 PHE A CD2 3587 C CE1 . PHE A 467 ? 0.3368 0.3759 0.3338 -0.0469 0.0678 -0.0389 467 PHE A CE1 3588 C CE2 . PHE A 467 ? 0.3447 0.3696 0.3239 -0.0458 0.0647 -0.0191 467 PHE A CE2 3589 C CZ . PHE A 467 ? 0.3400 0.3698 0.3228 -0.0519 0.0715 -0.0310 467 PHE A CZ 3590 N N . LYS A 468 ? 0.3299 0.3456 0.3307 -0.0118 0.0174 -0.0096 468 LYS A N 3591 C CA . LYS A 468 ? 0.3506 0.3560 0.3375 -0.0101 0.0105 0.0019 468 LYS A CA 3592 C C . LYS A 468 ? 0.3363 0.3532 0.3185 -0.0133 0.0184 0.0040 468 LYS A C 3593 O O . LYS A 468 ? 0.3257 0.3546 0.3154 -0.0104 0.0203 -0.0060 468 LYS A O 3594 C CB . LYS A 468 ? 0.3872 0.3853 0.3745 0.0006 -0.0042 -0.0027 468 LYS A CB 3595 C CG . LYS A 468 ? 0.4263 0.4090 0.3916 0.0008 -0.0122 0.0115 468 LYS A CG 3596 C CD . LYS A 468 ? 0.4899 0.4604 0.4522 0.0146 -0.0306 0.0076 468 LYS A CD 3597 C CE . LYS A 468 ? 0.5347 0.4877 0.4684 0.0142 -0.0394 0.0229 468 LYS A CE 3598 N NZ . LYS A 468 ? 0.5852 0.5237 0.5134 0.0310 -0.0608 0.0192 468 LYS A NZ 3599 N N . ILE A 469 ? 0.3335 0.3490 0.3052 -0.0197 0.0233 0.0146 469 ILE A N 3600 C CA . ILE A 469 ? 0.3231 0.3501 0.2920 -0.0220 0.0302 0.0151 469 ILE A CA 3601 C C . ILE A 469 ? 0.3398 0.3664 0.2959 -0.0222 0.0245 0.0204 469 ILE A C 3602 O O . ILE A 469 ? 0.3519 0.3682 0.2941 -0.0274 0.0209 0.0304 469 ILE A O 3603 C CB . ILE A 469 ? 0.3236 0.3547 0.2912 -0.0272 0.0377 0.0194 469 ILE A CB 3604 C CG1 . ILE A 469 ? 0.3094 0.3384 0.2842 -0.0263 0.0417 0.0153 469 ILE A CG1 3605 C CG2 . ILE A 469 ? 0.3124 0.3555 0.2793 -0.0275 0.0431 0.0173 469 ILE A CG2 3606 C CD1 . ILE A 469 ? 0.3235 0.3558 0.2964 -0.0283 0.0451 0.0188 469 ILE A CD1 3607 N N . TYR A 470 ? 0.3480 0.3855 0.3067 -0.0183 0.0241 0.0135 470 TYR A N 3608 C CA . TYR A 470 ? 0.3727 0.4105 0.3170 -0.0170 0.0163 0.0174 470 TYR A CA 3609 C C . TYR A 470 ? 0.3735 0.4230 0.3076 -0.0251 0.0231 0.0214 470 TYR A C 3610 O O . TYR A 470 ? 0.3850 0.4446 0.3119 -0.0244 0.0209 0.0190 470 TYR A O 3611 C CB . TYR A 470 ? 0.3788 0.4270 0.3322 -0.0080 0.0106 0.0048 470 TYR A CB 3612 C CG . TYR A 470 ? 0.3904 0.4298 0.3504 0.0014 -0.0010 -0.0005 470 TYR A CG 3613 C CD1 . TYR A 470 ? 0.3764 0.4195 0.3554 0.0025 0.0034 -0.0114 470 TYR A CD1 3614 C CD2 . TYR A 470 ? 0.4179 0.4452 0.3641 0.0098 -0.0174 0.0039 470 TYR A CD2 3615 C CE1 . TYR A 470 ? 0.3921 0.4325 0.3812 0.0117 -0.0071 -0.0207 470 TYR A CE1 3616 C CE2 . TYR A 470 ? 0.4421 0.4618 0.3972 0.0219 -0.0307 -0.0041 470 TYR A CE2 3617 C CZ . TYR A 470 ? 0.4105 0.4397 0.3897 0.0228 -0.0250 -0.0180 470 TYR A CZ 3618 O OH . TYR A 470 ? 0.4401 0.4673 0.4320 0.0349 -0.0377 -0.0301 470 TYR A OH 3619 N N . HIS A 471 ? 0.3696 0.4212 0.3044 -0.0324 0.0311 0.0250 471 HIS A N 3620 C CA . HIS A 471 ? 0.3776 0.4441 0.3050 -0.0409 0.0376 0.0259 471 HIS A CA 3621 C C . HIS A 471 ? 0.3859 0.4502 0.3086 -0.0504 0.0417 0.0318 471 HIS A C 3622 O O . HIS A 471 ? 0.3734 0.4270 0.3025 -0.0490 0.0410 0.0338 471 HIS A O 3623 C CB . HIS A 471 ? 0.3620 0.4475 0.3051 -0.0373 0.0453 0.0139 471 HIS A CB 3624 C CG . HIS A 471 ? 0.3421 0.4243 0.3002 -0.0328 0.0497 0.0099 471 HIS A CG 3625 N ND1 . HIS A 471 ? 0.3422 0.4301 0.3034 -0.0354 0.0534 0.0102 471 HIS A ND1 3626 C CD2 . HIS A 471 ? 0.3325 0.4061 0.3009 -0.0266 0.0508 0.0048 471 HIS A CD2 3627 C CE1 . HIS A 471 ? 0.3450 0.4252 0.3156 -0.0288 0.0545 0.0075 471 HIS A CE1 3628 N NE2 . HIS A 471 ? 0.3312 0.4010 0.3043 -0.0250 0.0539 0.0050 471 HIS A NE2 3629 N N . LYS A 472 ? 0.4073 0.4853 0.3195 -0.0615 0.0470 0.0324 472 LYS A N 3630 C CA . LYS A 472 ? 0.4360 0.5197 0.3469 -0.0728 0.0531 0.0334 472 LYS A CA 3631 C C . LYS A 472 ? 0.4068 0.5033 0.3416 -0.0641 0.0567 0.0236 472 LYS A C 3632 O O . LYS A 472 ? 0.3810 0.4927 0.3286 -0.0565 0.0592 0.0139 472 LYS A O 3633 C CB . LYS A 472 ? 0.4727 0.5778 0.3714 -0.0876 0.0605 0.0304 472 LYS A CB 3634 C CG . LYS A 472 ? 0.5146 0.6351 0.4166 -0.1009 0.0688 0.0257 472 LYS A CG 3635 C CD . LYS A 472 ? 0.5627 0.7077 0.4515 -0.1195 0.0781 0.0204 472 LYS A CD 3636 C CE . LYS A 472 ? 0.5853 0.7516 0.4821 -0.1335 0.0873 0.0111 472 LYS A CE 3637 N NZ . LYS A 472 ? 0.6470 0.8441 0.5334 -0.1544 0.0988 0.0016 472 LYS A NZ 3638 N N . CYS A 473 ? 0.4144 0.5027 0.3536 -0.0649 0.0561 0.0260 473 CYS A N 3639 C CA . CYS A 473 ? 0.4253 0.5207 0.3822 -0.0549 0.0567 0.0188 473 CYS A CA 3640 C C . CYS A 473 ? 0.4323 0.5393 0.3929 -0.0627 0.0597 0.0158 473 CYS A C 3641 O O . CYS A 473 ? 0.4581 0.5517 0.4170 -0.0652 0.0575 0.0206 473 CYS A O 3642 C CB . CYS A 473 ? 0.4458 0.5199 0.4058 -0.0453 0.0516 0.0224 473 CYS A CB 3643 S SG . CYS A 473 ? 0.5328 0.6076 0.5051 -0.0337 0.0518 0.0165 473 CYS A SG 3644 N N . ASP A 474 ? 0.4062 0.5416 0.3738 -0.0667 0.0648 0.0052 474 ASP A N 3645 C CA . ASP A 474 ? 0.4095 0.5649 0.3829 -0.0762 0.0689 -0.0023 474 ASP A CA 3646 C C . ASP A 474 ? 0.3891 0.5496 0.3779 -0.0628 0.0641 -0.0084 474 ASP A C 3647 O O . ASP A 474 ? 0.3659 0.5096 0.3565 -0.0483 0.0584 -0.0044 474 ASP A O 3648 C CB . ASP A 474 ? 0.4155 0.6066 0.3938 -0.0856 0.0764 -0.0161 474 ASP A CB 3649 C CG . ASP A 474 ? 0.4154 0.6280 0.4127 -0.0683 0.0738 -0.0305 474 ASP A CG 3650 O OD1 . ASP A 474 ? 0.3838 0.5838 0.3895 -0.0497 0.0664 -0.0301 474 ASP A OD1 3651 O OD2 . ASP A 474 ? 0.4249 0.6662 0.4272 -0.0742 0.0794 -0.0432 474 ASP A OD2 3652 N N . ASN A 475 ? 0.3685 0.5524 0.3664 -0.0687 0.0665 -0.0186 475 ASN A N 3653 C CA . ASN A 475 ? 0.3699 0.5580 0.3788 -0.0564 0.0603 -0.0236 475 ASN A CA 3654 C C . ASN A 475 ? 0.3550 0.5457 0.3723 -0.0343 0.0527 -0.0292 475 ASN A C 3655 O O . ASN A 475 ? 0.3547 0.5281 0.3692 -0.0221 0.0458 -0.0241 475 ASN A O 3656 C CB . ASN A 475 ? 0.3822 0.6023 0.4021 -0.0667 0.0642 -0.0378 475 ASN A CB 3657 C CG . ASN A 475 ? 0.3980 0.6042 0.4079 -0.0866 0.0696 -0.0307 475 ASN A CG 3658 O OD1 . ASN A 475 ? 0.4087 0.5801 0.4045 -0.0891 0.0681 -0.0153 475 ASN A OD1 3659 N ND2 . ASN A 475 ? 0.4060 0.6398 0.4243 -0.1006 0.0756 -0.0441 475 ASN A ND2 3660 N N . ALA A 476 ? 0.3516 0.5617 0.3771 -0.0301 0.0538 -0.0398 476 ALA A N 3661 C CA . ALA A 476 ? 0.3647 0.5718 0.3969 -0.0086 0.0456 -0.0457 476 ALA A CA 3662 C C . ALA A 476 ? 0.3512 0.5198 0.3699 -0.0030 0.0441 -0.0311 476 ALA A C 3663 O O . ALA A 476 ? 0.3741 0.5227 0.3889 0.0115 0.0370 -0.0282 476 ALA A O 3664 C CB . ALA A 476 ? 0.3649 0.6039 0.4120 -0.0061 0.0476 -0.0637 476 ALA A CB 3665 N N . CYS A 477 ? 0.3450 0.5032 0.3548 -0.0155 0.0506 -0.0224 477 CYS A N 3666 C CA . CYS A 477 ? 0.3607 0.4890 0.3606 -0.0124 0.0502 -0.0121 477 CYS A CA 3667 C C . CYS A 477 ? 0.3492 0.4539 0.3410 -0.0104 0.0471 -0.0024 477 CYS A C 3668 O O . CYS A 477 ? 0.3629 0.4466 0.3490 -0.0024 0.0447 0.0008 477 CYS A O 3669 C CB . CYS A 477 ? 0.3825 0.5095 0.3751 -0.0251 0.0555 -0.0068 477 CYS A CB 3670 S SG . CYS A 477 ? 0.4360 0.5369 0.4216 -0.0213 0.0552 -0.0003 477 CYS A SG 3671 N N . ILE A 478 ? 0.3429 0.4507 0.3332 -0.0194 0.0479 0.0010 478 ILE A N 3672 C CA . ILE A 478 ? 0.3465 0.4378 0.3314 -0.0183 0.0452 0.0070 478 ILE A CA 3673 C C . ILE A 478 ? 0.3544 0.4446 0.3385 -0.0054 0.0392 0.0040 478 ILE A C 3674 O O . ILE A 478 ? 0.3688 0.4378 0.3426 -0.0013 0.0374 0.0095 478 ILE A O 3675 C CB . ILE A 478 ? 0.3462 0.4433 0.3323 -0.0295 0.0465 0.0082 478 ILE A CB 3676 C CG1 . ILE A 478 ? 0.3519 0.4385 0.3320 -0.0408 0.0495 0.0144 478 ILE A CG1 3677 C CG2 . ILE A 478 ? 0.3543 0.4402 0.3375 -0.0269 0.0435 0.0106 478 ILE A CG2 3678 C CD1 . ILE A 478 ? 0.3534 0.4177 0.3285 -0.0378 0.0476 0.0202 478 ILE A CD1 3679 N N . GLY A 479 ? 0.3539 0.4674 0.3473 0.0005 0.0357 -0.0057 479 GLY A N 3680 C CA . GLY A 479 ? 0.3613 0.4740 0.3528 0.0165 0.0264 -0.0097 479 GLY A CA 3681 C C . GLY A 479 ? 0.3834 0.4681 0.3638 0.0279 0.0228 -0.0052 479 GLY A C 3682 O O . GLY A 479 ? 0.4029 0.4656 0.3682 0.0361 0.0166 0.0005 479 GLY A O 3683 N N . SER A 480 ? 0.3768 0.4603 0.3620 0.0264 0.0273 -0.0076 480 SER A N 3684 C CA . SER A 480 ? 0.4069 0.4618 0.3825 0.0343 0.0259 -0.0047 480 SER A CA 3685 C C . SER A 480 ? 0.4169 0.4397 0.3742 0.0268 0.0302 0.0072 480 SER A C 3686 O O . SER A 480 ? 0.4384 0.4311 0.3793 0.0324 0.0273 0.0119 480 SER A O 3687 C CB . SER A 480 ? 0.4177 0.4830 0.4045 0.0318 0.0313 -0.0121 480 SER A CB 3688 O OG . SER A 480 ? 0.4100 0.4726 0.3947 0.0176 0.0401 -0.0065 480 SER A OG 3689 N N . ILE A 481 ? 0.3919 0.4207 0.3511 0.0135 0.0368 0.0110 481 ILE A N 3690 C CA . ILE A 481 ? 0.3959 0.4035 0.3427 0.0054 0.0414 0.0177 481 ILE A CA 3691 C C . ILE A 481 ? 0.4298 0.4263 0.3620 0.0082 0.0368 0.0225 481 ILE A C 3692 O O . ILE A 481 ? 0.4528 0.4229 0.3661 0.0070 0.0378 0.0275 481 ILE A O 3693 C CB . ILE A 481 ? 0.3700 0.3888 0.3251 -0.0059 0.0464 0.0179 481 ILE A CB 3694 C CG1 . ILE A 481 ? 0.3595 0.3869 0.3236 -0.0085 0.0497 0.0144 481 ILE A CG1 3695 C CG2 . ILE A 481 ? 0.3737 0.3775 0.3204 -0.0131 0.0505 0.0200 481 ILE A CG2 3696 C CD1 . ILE A 481 ? 0.3469 0.3836 0.3164 -0.0164 0.0508 0.0155 481 ILE A CD1 3697 N N . ARG A 482 ? 0.4368 0.4537 0.3761 0.0102 0.0322 0.0203 482 ARG A N 3698 C CA . ARG A 482 ? 0.4580 0.4708 0.3847 0.0135 0.0266 0.0231 482 ARG A CA 3699 C C . ARG A 482 ? 0.5258 0.5176 0.4340 0.0276 0.0174 0.0263 482 ARG A C 3700 O O . ARG A 482 ? 0.5526 0.5239 0.4376 0.0277 0.0145 0.0331 482 ARG A O 3701 C CB . ARG A 482 ? 0.4493 0.4925 0.3907 0.0140 0.0230 0.0165 482 ARG A CB 3702 C CG . ARG A 482 ? 0.4237 0.4792 0.3773 0.0000 0.0300 0.0151 482 ARG A CG 3703 C CD . ARG A 482 ? 0.4292 0.5086 0.3925 -0.0019 0.0273 0.0086 482 ARG A CD 3704 N NE . ARG A 482 ? 0.4425 0.5453 0.4168 0.0053 0.0229 0.0001 482 ARG A NE 3705 C CZ . ARG A 482 ? 0.4494 0.5770 0.4392 -0.0029 0.0265 -0.0079 482 ARG A CZ 3706 N NH1 . ARG A 482 ? 0.4368 0.5637 0.4305 -0.0181 0.0332 -0.0062 482 ARG A NH1 3707 N NH2 . ARG A 482 ? 0.4528 0.6061 0.4540 0.0039 0.0229 -0.0192 482 ARG A NH2 3708 N N . ASN A 483 ? 0.5672 0.5633 0.4845 0.0394 0.0121 0.0208 483 ASN A N 3709 C CA . ASN A 483 ? 0.6591 0.6345 0.5618 0.0573 -0.0002 0.0216 483 ASN A CA 3710 C C . ASN A 483 ? 0.6716 0.6045 0.5547 0.0560 0.0030 0.0289 483 ASN A C 3711 O O . ASN A 483 ? 0.6959 0.5994 0.5608 0.0698 -0.0073 0.0321 483 ASN A O 3712 C CB . ASN A 483 ? 0.7435 0.7493 0.6708 0.0713 -0.0076 0.0072 483 ASN A CB 3713 C CG . ASN A 483 ? 0.8739 0.8698 0.7922 0.0949 -0.0256 0.0035 483 ASN A CG 3714 O OD1 . ASN A 483 ? 0.9328 0.8926 0.8210 0.1011 -0.0334 0.0149 483 ASN A OD1 3715 N ND2 . ASN A 483 ? 0.9846 1.0131 0.9279 0.1086 -0.0331 -0.0135 483 ASN A ND2 3716 N N . GLY A 484 ? 0.6332 0.5622 0.5199 0.0397 0.0166 0.0304 484 GLY A N 3717 C CA . GLY A 484 ? 0.6465 0.5387 0.5164 0.0341 0.0226 0.0347 484 GLY A CA 3718 C C . GLY A 484 ? 0.6453 0.5339 0.5276 0.0430 0.0209 0.0270 484 GLY A C 3719 O O . GLY A 484 ? 0.6660 0.5182 0.5320 0.0419 0.0229 0.0297 484 GLY A O 3720 N N . THR A 485 ? 0.5874 0.5134 0.4975 0.0500 0.0184 0.0161 485 THR A N 3721 C CA . THR A 485 ? 0.5857 0.5161 0.5109 0.0585 0.0170 0.0053 485 THR A CA 3722 C C . THR A 485 ? 0.5333 0.4920 0.4794 0.0463 0.0285 -0.0020 485 THR A C 3723 O O . THR A 485 ? 0.5302 0.5000 0.4907 0.0514 0.0285 -0.0128 485 THR A O 3724 C CB . THR A 485 ? 0.5940 0.5465 0.5338 0.0784 0.0035 -0.0056 485 THR A CB 3725 O OG1 . THR A 485 ? 0.5645 0.5636 0.5246 0.0732 0.0059 -0.0121 485 THR A OG1 3726 C CG2 . THR A 485 ? 0.6397 0.5622 0.5563 0.0942 -0.0113 0.0013 485 THR A CG2 3727 N N . TYR A 486 ? 0.5077 0.4768 0.4541 0.0311 0.0370 0.0031 486 TYR A N 3728 C CA . TYR A 486 ? 0.4554 0.4465 0.4161 0.0205 0.0455 -0.0016 486 TYR A CA 3729 C C . TYR A 486 ? 0.4679 0.4426 0.4276 0.0178 0.0511 -0.0066 486 TYR A C 3730 O O . TYR A 486 ? 0.4771 0.4208 0.4215 0.0133 0.0545 -0.0023 486 TYR A O 3731 C CB . TYR A 486 ? 0.4269 0.4218 0.3841 0.0080 0.0504 0.0050 486 TYR A CB 3732 C CG . TYR A 486 ? 0.3943 0.4057 0.3611 -0.0012 0.0561 0.0020 486 TYR A CG 3733 C CD1 . TYR A 486 ? 0.3686 0.4057 0.3445 -0.0036 0.0550 0.0008 486 TYR A CD1 3734 C CD2 . TYR A 486 ? 0.3767 0.3773 0.3408 -0.0085 0.0621 0.0001 486 TYR A CD2 3735 C CE1 . TYR A 486 ? 0.3509 0.3978 0.3296 -0.0108 0.0576 0.0002 486 TYR A CE1 3736 C CE2 . TYR A 486 ? 0.3576 0.3740 0.3296 -0.0142 0.0644 -0.0034 486 TYR A CE2 3737 C CZ . TYR A 486 ? 0.3421 0.3793 0.3197 -0.0142 0.0610 -0.0021 486 TYR A CZ 3738 O OH . TYR A 486 ? 0.3273 0.3751 0.3075 -0.0183 0.0607 -0.0039 486 TYR A OH 3739 N N . ASP A 487 ? 0.4534 0.4501 0.4287 0.0188 0.0530 -0.0168 487 ASP A N 3740 C CA . ASP A 487 ? 0.4787 0.4662 0.4568 0.0156 0.0588 -0.0246 487 ASP A CA 3741 C C . ASP A 487 ? 0.4424 0.4520 0.4273 0.0037 0.0655 -0.0266 487 ASP A C 3742 O O . ASP A 487 ? 0.4269 0.4662 0.4217 0.0028 0.0651 -0.0309 487 ASP A O 3743 C CB . ASP A 487 ? 0.5120 0.5102 0.5034 0.0267 0.0550 -0.0376 487 ASP A CB 3744 C CG . ASP A 487 ? 0.5503 0.5355 0.5448 0.0241 0.0607 -0.0474 487 ASP A CG 3745 O OD1 . ASP A 487 ? 0.5530 0.5330 0.5436 0.0117 0.0689 -0.0464 487 ASP A OD1 3746 O OD2 . ASP A 487 ? 0.5827 0.5644 0.5856 0.0352 0.0565 -0.0585 487 ASP A OD2 3747 N N . HIS A 488 ? 0.4171 0.4124 0.3950 -0.0055 0.0712 -0.0245 488 HIS A N 3748 C CA . HIS A 488 ? 0.4041 0.4197 0.3881 -0.0136 0.0742 -0.0270 488 HIS A CA 3749 C C . HIS A 488 ? 0.3946 0.4302 0.3893 -0.0139 0.0762 -0.0383 488 HIS A C 3750 O O . HIS A 488 ? 0.3706 0.4286 0.3689 -0.0167 0.0747 -0.0393 488 HIS A O 3751 C CB . HIS A 488 ? 0.4030 0.4042 0.3814 -0.0228 0.0800 -0.0279 488 HIS A CB 3752 C CG . HIS A 488 ? 0.4184 0.4076 0.3976 -0.0288 0.0879 -0.0389 488 HIS A CG 3753 N ND1 . HIS A 488 ? 0.4247 0.4324 0.4144 -0.0346 0.0920 -0.0506 488 HIS A ND1 3754 C CD2 . HIS A 488 ? 0.4543 0.4122 0.4237 -0.0299 0.0919 -0.0402 488 HIS A CD2 3755 C CE1 . HIS A 488 ? 0.4591 0.4514 0.4483 -0.0411 0.1002 -0.0608 488 HIS A CE1 3756 N NE2 . HIS A 488 ? 0.4694 0.4278 0.4447 -0.0387 0.1003 -0.0534 488 HIS A NE2 3757 N N . ASP A 489 ? 0.4278 0.4542 0.4262 -0.0107 0.0788 -0.0472 489 ASP A N 3758 C CA . ASP A 489 ? 0.4665 0.5139 0.4763 -0.0119 0.0817 -0.0609 489 ASP A CA 3759 C C . ASP A 489 ? 0.4415 0.5219 0.4571 -0.0091 0.0779 -0.0625 489 ASP A C 3760 O O . ASP A 489 ? 0.4265 0.5306 0.4462 -0.0131 0.0792 -0.0697 489 ASP A O 3761 C CB . ASP A 489 ? 0.5259 0.5540 0.5395 -0.0085 0.0850 -0.0718 489 ASP A CB 3762 C CG . ASP A 489 ? 0.5918 0.5931 0.5993 -0.0180 0.0928 -0.0754 489 ASP A CG 3763 O OD1 . ASP A 489 ? 0.6478 0.6646 0.6592 -0.0272 0.0975 -0.0807 489 ASP A OD1 3764 O OD2 . ASP A 489 ? 0.6765 0.6406 0.6743 -0.0167 0.0940 -0.0740 489 ASP A OD2 3765 N N . VAL A 490 ? 0.4413 0.5245 0.4560 -0.0036 0.0734 -0.0567 490 VAL A N 3766 C CA . VAL A 490 ? 0.4374 0.5527 0.4562 -0.0044 0.0718 -0.0596 490 VAL A CA 3767 C C . VAL A 490 ? 0.4140 0.5437 0.4231 -0.0139 0.0713 -0.0511 490 VAL A C 3768 O O . VAL A 490 ? 0.3895 0.5447 0.3968 -0.0194 0.0723 -0.0550 490 VAL A O 3769 C CB . VAL A 490 ? 0.4493 0.5655 0.4697 0.0018 0.0673 -0.0563 490 VAL A CB 3770 C CG1 . VAL A 490 ? 0.4883 0.6397 0.5116 -0.0038 0.0681 -0.0602 490 VAL A CG1 3771 C CG2 . VAL A 490 ? 0.4918 0.5931 0.5203 0.0149 0.0641 -0.0657 490 VAL A CG2 3772 N N . TYR A 491 ? 0.3773 0.4892 0.3784 -0.0159 0.0692 -0.0400 491 TYR A N 3773 C CA . TYR A 491 ? 0.3766 0.4939 0.3670 -0.0218 0.0655 -0.0304 491 TYR A CA 3774 C C . TYR A 491 ? 0.3677 0.4833 0.3566 -0.0226 0.0638 -0.0329 491 TYR A C 3775 O O . TYR A 491 ? 0.3711 0.4888 0.3503 -0.0246 0.0580 -0.0262 491 TYR A O 3776 C CB . TYR A 491 ? 0.3743 0.4761 0.3593 -0.0219 0.0624 -0.0184 491 TYR A CB 3777 C CG . TYR A 491 ? 0.3968 0.5031 0.3847 -0.0202 0.0628 -0.0177 491 TYR A CG 3778 C CD1 . TYR A 491 ? 0.4099 0.5349 0.3940 -0.0268 0.0632 -0.0163 491 TYR A CD1 3779 C CD2 . TYR A 491 ? 0.4117 0.5040 0.4046 -0.0125 0.0625 -0.0193 491 TYR A CD2 3780 C CE1 . TYR A 491 ? 0.4235 0.5591 0.4139 -0.0254 0.0637 -0.0198 491 TYR A CE1 3781 C CE2 . TYR A 491 ? 0.4214 0.5214 0.4186 -0.0081 0.0604 -0.0211 491 TYR A CE2 3782 C CZ . TYR A 491 ? 0.4303 0.5551 0.4288 -0.0144 0.0612 -0.0229 491 TYR A CZ 3783 O OH . TYR A 491 ? 0.4601 0.5990 0.4664 -0.0102 0.0593 -0.0287 491 TYR A OH 3784 N N . ARG A 492 ? 0.3592 0.4701 0.3572 -0.0211 0.0682 -0.0437 492 ARG A N 3785 C CA . ARG A 492 ? 0.3608 0.4725 0.3615 -0.0222 0.0673 -0.0497 492 ARG A CA 3786 C C . ARG A 492 ? 0.3717 0.5052 0.3683 -0.0221 0.0617 -0.0535 492 ARG A C 3787 O O . ARG A 492 ? 0.3733 0.5080 0.3665 -0.0199 0.0544 -0.0521 492 ARG A O 3788 C CB . ARG A 492 ? 0.3728 0.4756 0.3833 -0.0243 0.0757 -0.0626 492 ARG A CB 3789 C CG . ARG A 492 ? 0.3780 0.4870 0.3950 -0.0277 0.0771 -0.0739 492 ARG A CG 3790 C CD . ARG A 492 ? 0.3960 0.4930 0.4199 -0.0339 0.0879 -0.0868 492 ARG A CD 3791 N NE . ARG A 492 ? 0.4000 0.5085 0.4331 -0.0400 0.0919 -0.1026 492 ARG A NE 3792 C CZ . ARG A 492 ? 0.4084 0.5061 0.4425 -0.0477 0.0978 -0.1070 492 ARG A CZ 3793 N NH1 . ARG A 492 ? 0.4166 0.4890 0.4400 -0.0500 0.0998 -0.0944 492 ARG A NH1 3794 N NH2 . ARG A 492 ? 0.4153 0.5315 0.4615 -0.0541 0.1020 -0.1264 492 ARG A NH2 3795 N N . ASP A 493 ? 0.3797 0.5311 0.3762 -0.0236 0.0639 -0.0595 493 ASP A N 3796 C CA . ASP A 493 ? 0.4141 0.5865 0.4006 -0.0246 0.0580 -0.0612 493 ASP A CA 3797 C C . ASP A 493 ? 0.4093 0.5736 0.3751 -0.0250 0.0481 -0.0438 493 ASP A C 3798 O O . ASP A 493 ? 0.4005 0.5654 0.3572 -0.0211 0.0381 -0.0422 493 ASP A O 3799 C CB . ASP A 493 ? 0.4577 0.6519 0.4450 -0.0284 0.0633 -0.0695 493 ASP A CB 3800 C CG . ASP A 493 ? 0.4997 0.7050 0.5052 -0.0275 0.0702 -0.0899 493 ASP A CG 3801 O OD1 . ASP A 493 ? 0.5278 0.7246 0.5431 -0.0261 0.0717 -0.0974 493 ASP A OD1 3802 O OD2 . ASP A 493 ? 0.5547 0.7787 0.5652 -0.0296 0.0749 -0.1005 493 ASP A OD2 3803 N N . GLU A 494 ? 0.3977 0.5534 0.3559 -0.0293 0.0500 -0.0324 494 GLU A N 3804 C CA . GLU A 494 ? 0.4075 0.5500 0.3447 -0.0326 0.0424 -0.0157 494 GLU A CA 3805 C C . GLU A 494 ? 0.4015 0.5238 0.3410 -0.0252 0.0342 -0.0112 494 GLU A C 3806 O O . GLU A 494 ? 0.3901 0.5040 0.3148 -0.0219 0.0227 -0.0047 494 GLU A O 3807 C CB . GLU A 494 ? 0.4134 0.5526 0.3480 -0.0398 0.0484 -0.0085 494 GLU A CB 3808 C CG . GLU A 494 ? 0.4450 0.5667 0.3580 -0.0464 0.0428 0.0080 494 GLU A CG 3809 C CD . GLU A 494 ? 0.4479 0.5725 0.3618 -0.0554 0.0503 0.0110 494 GLU A CD 3810 O OE1 . GLU A 494 ? 0.4514 0.5933 0.3831 -0.0540 0.0579 0.0000 494 GLU A OE1 3811 O OE2 . GLU A 494 ? 0.4437 0.5528 0.3414 -0.0632 0.0478 0.0230 494 GLU A OE2 3812 N N . ALA A 495 ? 0.3875 0.5017 0.3443 -0.0223 0.0393 -0.0157 495 ALA A N 3813 C CA . ALA A 495 ? 0.3871 0.4864 0.3483 -0.0171 0.0333 -0.0142 495 ALA A CA 3814 C C . ALA A 495 ? 0.3884 0.4967 0.3549 -0.0099 0.0255 -0.0252 495 ALA A C 3815 O O . ALA A 495 ? 0.3912 0.4910 0.3525 -0.0035 0.0136 -0.0221 495 ALA A O 3816 C CB . ALA A 495 ? 0.3820 0.4729 0.3571 -0.0181 0.0418 -0.0176 495 ALA A CB 3817 N N . LEU A 496 ? 0.4039 0.5303 0.3816 -0.0103 0.0311 -0.0401 496 LEU A N 3818 C CA . LEU A 496 ? 0.4230 0.5648 0.4094 -0.0038 0.0243 -0.0552 496 LEU A CA 3819 C C . LEU A 496 ? 0.4554 0.6013 0.4232 0.0032 0.0084 -0.0494 496 LEU A C 3820 O O . LEU A 496 ? 0.4763 0.6250 0.4463 0.0135 -0.0046 -0.0558 496 LEU A O 3821 C CB . LEU A 496 ? 0.4232 0.5840 0.4251 -0.0080 0.0351 -0.0738 496 LEU A CB 3822 C CG . LEU A 496 ? 0.4187 0.5704 0.4358 -0.0150 0.0490 -0.0820 496 LEU A CG 3823 C CD1 . LEU A 496 ? 0.4373 0.6031 0.4665 -0.0205 0.0591 -0.1003 496 LEU A CD1 3824 C CD2 . LEU A 496 ? 0.4220 0.5700 0.4483 -0.0136 0.0469 -0.0880 496 LEU A CD2 3825 N N . ASN A 497 ? 0.4721 0.6185 0.4202 -0.0022 0.0089 -0.0383 497 ASN A N 3826 C CA . ASN A 497 ? 0.5126 0.6549 0.4332 0.0014 -0.0059 -0.0278 497 ASN A CA 3827 C C . ASN A 497 ? 0.5099 0.6221 0.4153 0.0069 -0.0190 -0.0125 497 ASN A C 3828 O O . ASN A 497 ? 0.5123 0.6174 0.4045 0.0180 -0.0368 -0.0109 497 ASN A O 3829 C CB . ASN A 497 ? 0.5597 0.7080 0.4595 -0.0102 0.0004 -0.0187 497 ASN A CB 3830 C CG . ASN A 497 ? 0.6240 0.8014 0.5230 -0.0102 0.0006 -0.0319 497 ASN A CG 3831 O OD1 . ASN A 497 ? 0.6863 0.8696 0.5743 -0.0013 -0.0135 -0.0349 497 ASN A OD1 3832 N ND2 . ASN A 497 ? 0.6580 0.8549 0.5695 -0.0187 0.0155 -0.0416 497 ASN A ND2 3833 N N . ASN A 498 ? 0.4815 0.5755 0.3890 0.0004 -0.0117 -0.0025 498 ASN A N 3834 C CA . ASN A 498 ? 0.5058 0.5698 0.4013 0.0044 -0.0229 0.0102 498 ASN A CA 3835 C C . ASN A 498 ? 0.4948 0.5578 0.4112 0.0187 -0.0327 -0.0025 498 ASN A C 3836 O O . ASN A 498 ? 0.5122 0.5568 0.4176 0.0297 -0.0502 0.0015 498 ASN A O 3837 C CB . ASN A 498 ? 0.5017 0.5513 0.3958 -0.0072 -0.0118 0.0213 498 ASN A CB 3838 C CG . ASN A 498 ? 0.5437 0.5919 0.4132 -0.0217 -0.0057 0.0339 498 ASN A CG 3839 O OD1 . ASN A 498 ? 0.5822 0.6279 0.4256 -0.0238 -0.0131 0.0406 498 ASN A OD1 3840 N ND2 . ASN A 498 ? 0.5372 0.5891 0.4139 -0.0323 0.0076 0.0357 498 ASN A ND2 3841 N N . ARG A 499 ? 0.4731 0.5552 0.4184 0.0181 -0.0214 -0.0192 499 ARG A N 3842 C CA . ARG A 499 ? 0.4910 0.5797 0.4593 0.0279 -0.0267 -0.0359 499 ARG A CA 3843 C C . ARG A 499 ? 0.5427 0.6483 0.5154 0.0420 -0.0422 -0.0508 499 ARG A C 3844 O O . ARG A 499 ? 0.5647 0.6639 0.5411 0.0558 -0.0585 -0.0563 499 ARG A O 3845 C CB . ARG A 499 ? 0.4542 0.5596 0.4468 0.0195 -0.0087 -0.0506 499 ARG A CB 3846 C CG . ARG A 499 ? 0.4262 0.5157 0.4199 0.0105 0.0024 -0.0410 499 ARG A CG 3847 C CD . ARG A 499 ? 0.4186 0.5189 0.4298 0.0023 0.0183 -0.0545 499 ARG A CD 3848 N NE . ARG A 499 ? 0.3988 0.5116 0.4288 0.0053 0.0169 -0.0737 499 ARG A NE 3849 C CZ . ARG A 499 ? 0.4148 0.5415 0.4592 -0.0032 0.0298 -0.0907 499 ARG A CZ 3850 N NH1 . ARG A 499 ? 0.4232 0.5477 0.4642 -0.0136 0.0438 -0.0896 499 ARG A NH1 3851 N NH2 . ARG A 499 ? 0.4253 0.5679 0.4874 -0.0022 0.0290 -0.1106 499 ARG A NH2 3852 N N . PHE A 500 ? 0.5791 0.7085 0.5536 0.0395 -0.0375 -0.0599 500 PHE A N 3853 C CA . PHE A 500 ? 0.6301 0.7835 0.6120 0.0525 -0.0509 -0.0782 500 PHE A CA 3854 C C . PHE A 500 ? 0.7139 0.8593 0.6629 0.0575 -0.0653 -0.0635 500 PHE A C 3855 O O . PHE A 500 ? 0.7631 0.9278 0.7065 0.0521 -0.0598 -0.0670 500 PHE A O 3856 C CB . PHE A 500 ? 0.6047 0.7922 0.6128 0.0449 -0.0350 -0.1021 500 PHE A CB 3857 C CG . PHE A 500 ? 0.5820 0.7712 0.6141 0.0351 -0.0183 -0.1130 500 PHE A CG 3858 C CD1 . PHE A 500 ? 0.5848 0.7712 0.6304 0.0418 -0.0247 -0.1211 500 PHE A CD1 3859 C CD2 . PHE A 500 ? 0.5892 0.7804 0.6279 0.0192 0.0029 -0.1153 500 PHE A CD2 3860 C CE1 . PHE A 500 ? 0.5875 0.7761 0.6509 0.0304 -0.0086 -0.1308 500 PHE A CE1 3861 C CE2 . PHE A 500 ? 0.5799 0.7670 0.6332 0.0089 0.0176 -0.1226 500 PHE A CE2 3862 C CZ . PHE A 500 ? 0.5858 0.7730 0.6505 0.0133 0.0126 -0.1303 500 PHE A CZ 3863 N N . GLN A 501 ? 0.7975 0.9109 0.7220 0.0664 -0.0831 -0.0463 501 GLN A N 3864 C CA . GLN A 501 ? 0.8904 0.9884 0.7763 0.0721 -0.1006 -0.0307 501 GLN A CA 3865 C C . GLN A 501 ? 0.9649 1.0478 0.8449 0.0959 -0.1293 -0.0344 501 GLN A C 3866 O O . GLN A 501 ? 0.9813 1.0479 0.8758 0.1036 -0.1350 -0.0372 501 GLN A O 3867 C CB . GLN A 501 ? 0.9199 0.9833 0.7710 0.0565 -0.0946 -0.0017 501 GLN A CB 3868 C CG . GLN A 501 ? 0.9363 0.9615 0.7828 0.0570 -0.0987 0.0115 501 GLN A CG 3869 C CD . GLN A 501 ? 0.9587 0.9566 0.7752 0.0372 -0.0884 0.0360 501 GLN A CD 3870 O OE1 . GLN A 501 ? 0.9681 0.9441 0.7880 0.0313 -0.0832 0.0438 501 GLN A OE1 3871 N NE2 . GLN A 501 ? 1.0031 1.0061 0.7911 0.0257 -0.0844 0.0458 501 GLN A NE2 3872 N N . ILE A 502 ? 1.0145 1.1036 0.8734 0.1086 -0.1486 -0.0357 502 ILE A N 3873 C CA . ILE A 502 ? 1.0674 1.1356 0.9121 0.1343 -0.1810 -0.0360 502 ILE A CA 3874 C C . ILE A 502 ? 1.1250 1.1328 0.9225 0.1292 -0.1900 -0.0017 502 ILE A C 3875 O O . ILE A 502 ? 1.1754 1.1678 0.9338 0.1127 -0.1836 0.0201 502 ILE A O 3876 C CB . ILE A 502 ? 1.0961 1.1874 0.9270 0.1509 -0.2018 -0.0466 502 ILE A CB 3877 C CG1 . ILE A 502 ? 1.0593 1.2071 0.9176 0.1405 -0.1825 -0.0695 502 ILE A CG1 3878 C CG2 . ILE A 502 ? 1.1041 1.1980 0.9502 0.1829 -0.2324 -0.0660 502 ILE A CG2 3879 C CD1 . ILE A 502 ? 1.0569 1.2058 0.8858 0.1187 -0.1663 -0.0523 502 ILE A CD1 3880 N N . LYS A 503 ? 1.1371 1.1119 0.9385 0.1411 -0.2032 0.0010 503 LYS A N 3881 C CA . LYS A 503 ? 1.1753 1.0886 0.9346 0.1340 -0.2099 0.0318 503 LYS A CA 3882 C C . LYS A 503 ? 1.2469 1.1168 0.9587 0.1537 -0.2444 0.0468 503 LYS A C 3883 O O . LYS A 503 ? 1.2523 1.1390 0.9730 0.1803 -0.2683 0.0293 503 LYS A O 3884 C CB . LYS A 503 ? 1.1612 1.0572 0.9479 0.1353 -0.2057 0.0273 503 LYS A CB 3885 C CG . LYS A 503 ? 1.1012 1.0127 0.9090 0.1091 -0.1724 0.0289 503 LYS A CG 3886 C CD . LYS A 503 ? 1.0869 0.9986 0.9321 0.1142 -0.1689 0.0148 503 LYS A CD 3887 C CE . LYS A 503 ? 1.0687 0.9510 0.9038 0.0938 -0.1531 0.0333 503 LYS A CE 3888 N NZ . LYS A 503 ? 1.0146 0.9274 0.8640 0.0711 -0.1232 0.0329 503 LYS A NZ # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'NAG A 805 WRONG CHIRALITY AT ATOM C1' # 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 GLN 1 1 ? ? ? A . n A 1 2 LYS 2 2 ? ? ? A . n A 1 3 LEU 3 3 ? ? ? A . n A 1 4 PRO 4 4 ? ? ? A . n A 1 5 GLY 5 5 ? ? ? A . n A 1 6 ASN 6 6 ? ? ? A . n A 1 7 ASP 7 7 ? ? ? A . n A 1 8 ASN 8 8 8 ASN ASN A . n A 1 9 SER 9 9 9 SER SER A . n A 1 10 THR 10 10 10 THR THR A . n A 1 11 ALA 11 11 11 ALA ALA A . n A 1 12 THR 12 12 12 THR THR A . n A 1 13 LEU 13 13 13 LEU LEU A . n A 1 14 CYS 14 14 14 CYS CYS A . n A 1 15 LEU 15 15 15 LEU LEU A . n A 1 16 GLY 16 16 16 GLY GLY A . n A 1 17 HIS 17 17 17 HIS HIS A . n A 1 18 HIS 18 18 18 HIS HIS A . n A 1 19 ALA 19 19 19 ALA ALA A . n A 1 20 VAL 20 20 20 VAL VAL A . n A 1 21 PRO 21 21 21 PRO PRO A . n A 1 22 ASN 22 22 22 ASN ASN A . n A 1 23 GLY 23 23 23 GLY GLY A . n A 1 24 THR 24 24 24 THR THR A . n A 1 25 ILE 25 25 25 ILE ILE A . n A 1 26 VAL 26 26 26 VAL VAL A . n A 1 27 LYS 27 27 27 LYS LYS A . n A 1 28 THR 28 28 28 THR THR A . n A 1 29 ILE 29 29 29 ILE ILE A . n A 1 30 THR 30 30 30 THR THR A . n A 1 31 ASN 31 31 31 ASN ASN A . n A 1 32 ASP 32 32 32 ASP ASP A . n A 1 33 GLN 33 33 33 GLN GLN A . n A 1 34 ILE 34 34 34 ILE ILE A . n A 1 35 GLU 35 35 35 GLU GLU A . n A 1 36 VAL 36 36 36 VAL VAL A . n A 1 37 THR 37 37 37 THR THR A . n A 1 38 ASN 38 38 38 ASN ASN A . n A 1 39 ALA 39 39 39 ALA ALA A . n A 1 40 THR 40 40 40 THR THR A . n A 1 41 GLU 41 41 41 GLU GLU A . n A 1 42 LEU 42 42 42 LEU LEU A . n A 1 43 VAL 43 43 43 VAL VAL A . n A 1 44 GLN 44 44 44 GLN GLN A . n A 1 45 SER 45 45 45 SER SER A . n A 1 46 SER 46 46 46 SER SER A . n A 1 47 SER 47 47 47 SER SER A . n A 1 48 THR 48 48 48 THR THR A . n A 1 49 GLY 49 49 49 GLY GLY A . n A 1 50 GLY 50 50 50 GLY GLY A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 CYS 52 52 52 CYS CYS A . n A 1 53 ASP 53 53 53 ASP ASP A . n A 1 54 SER 54 54 54 SER SER A . n A 1 55 PRO 55 55 55 PRO PRO A . n A 1 56 HIS 56 56 56 HIS HIS A . n A 1 57 GLN 57 57 57 GLN GLN A . n A 1 58 ILE 58 58 58 ILE ILE A . n A 1 59 LEU 59 59 59 LEU LEU A . n A 1 60 ASP 60 60 60 ASP ASP A . n A 1 61 GLY 61 61 61 GLY GLY A . n A 1 62 GLU 62 62 62 GLU GLU A . n A 1 63 ASN 63 63 63 ASN ASN A . n A 1 64 CYS 64 64 64 CYS CYS A . n A 1 65 THR 65 65 65 THR THR A . n A 1 66 LEU 66 66 66 LEU LEU A . n A 1 67 ILE 67 67 67 ILE ILE A . n A 1 68 ASP 68 68 68 ASP ASP A . n A 1 69 ALA 69 69 69 ALA ALA A . n A 1 70 LEU 70 70 70 LEU LEU A . n A 1 71 LEU 71 71 71 LEU LEU A . n A 1 72 GLY 72 72 72 GLY GLY A . n A 1 73 ASP 73 73 73 ASP ASP A . n A 1 74 PRO 74 74 74 PRO PRO A . n A 1 75 GLN 75 75 75 GLN GLN A . n A 1 76 CYS 76 76 76 CYS CYS A . n A 1 77 ASP 77 77 77 ASP ASP A . n A 1 78 GLY 78 78 78 GLY GLY A . n A 1 79 PHE 79 79 79 PHE PHE A . n A 1 80 GLN 80 80 80 GLN GLN A . n A 1 81 ASN 81 81 81 ASN ASN A . n A 1 82 LYS 82 82 82 LYS LYS A . n A 1 83 LYS 83 83 83 LYS LYS A . n A 1 84 TRP 84 84 84 TRP TRP A . n A 1 85 ASP 85 85 85 ASP ASP A . n A 1 86 LEU 86 86 86 LEU LEU A . n A 1 87 PHE 87 87 87 PHE PHE A . n A 1 88 VAL 88 88 88 VAL VAL A . n A 1 89 GLU 89 89 89 GLU GLU A . n A 1 90 ARG 90 90 90 ARG ARG A . n A 1 91 SER 91 91 91 SER SER A . n A 1 92 LYS 92 92 92 LYS LYS A . n A 1 93 ALA 93 93 93 ALA ALA A . n A 1 94 TYR 94 94 94 TYR TYR A . n A 1 95 SER 95 95 95 SER SER A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 CYS 97 97 97 CYS CYS A . n A 1 98 TYR 98 98 98 TYR TYR A . n A 1 99 PRO 99 99 99 PRO PRO A . n A 1 100 TYR 100 100 100 TYR TYR A . n A 1 101 ASP 101 101 101 ASP ASP A . n A 1 102 VAL 102 102 102 VAL VAL A . n A 1 103 PRO 103 103 103 PRO PRO A . n A 1 104 ASP 104 104 104 ASP ASP A . n A 1 105 TYR 105 105 105 TYR TYR A . n A 1 106 ALA 106 106 106 ALA ALA A . n A 1 107 SER 107 107 107 SER SER A . n A 1 108 LEU 108 108 108 LEU LEU A . n A 1 109 ARG 109 109 109 ARG ARG A . n A 1 110 SER 110 110 110 SER SER A . n A 1 111 LEU 111 111 111 LEU LEU A . n A 1 112 VAL 112 112 112 VAL VAL A . n A 1 113 ALA 113 113 113 ALA ALA A . n A 1 114 SER 114 114 114 SER SER A . n A 1 115 SER 115 115 115 SER SER A . n A 1 116 GLY 116 116 116 GLY GLY A . n A 1 117 THR 117 117 117 THR THR A . n A 1 118 LEU 118 118 118 LEU LEU A . n A 1 119 GLU 119 119 119 GLU GLU A . n A 1 120 PHE 120 120 120 PHE PHE A . n A 1 121 ASN 121 121 121 ASN ASN A . n A 1 122 ASN 122 122 122 ASN ASN A . n A 1 123 GLU 123 123 123 GLU GLU A . n A 1 124 SER 124 124 124 SER SER A . n A 1 125 PHE 125 125 125 PHE PHE A . n A 1 126 ASN 126 126 126 ASN ASN A . n A 1 127 TRP 127 127 127 TRP TRP A . n A 1 128 THR 128 128 128 THR THR A . n A 1 129 GLY 129 129 129 GLY GLY A . n A 1 130 VAL 130 130 130 VAL VAL A . n A 1 131 THR 131 131 131 THR THR A . n A 1 132 GLN 132 132 132 GLN GLN A . n A 1 133 ASN 133 133 133 ASN ASN A . n A 1 134 GLY 134 134 134 GLY GLY A . n A 1 135 THR 135 135 135 THR THR A . n A 1 136 SER 136 136 136 SER SER A . n A 1 137 SER 137 137 137 SER SER A . n A 1 138 ALA 138 138 138 ALA ALA A . n A 1 139 CYS 139 139 139 CYS CYS A . n A 1 140 LYS 140 140 140 LYS LYS A . n A 1 141 ARG 141 141 141 ARG ARG A . n A 1 142 ARG 142 142 142 ARG ARG A . n A 1 143 SER 143 143 143 SER SER A . n A 1 144 ASN 144 144 144 ASN ASN A . n A 1 145 ASN 145 145 145 ASN ASN A . n A 1 146 SER 146 146 146 SER SER A . n A 1 147 PHE 147 147 147 PHE PHE A . n A 1 148 PHE 148 148 148 PHE PHE A . n A 1 149 SER 149 149 149 SER SER A . n A 1 150 ARG 150 150 150 ARG ARG A . n A 1 151 LEU 151 151 151 LEU LEU A . n A 1 152 ASN 152 152 152 ASN ASN A . n A 1 153 TRP 153 153 153 TRP TRP A . n A 1 154 LEU 154 154 154 LEU LEU A . n A 1 155 THR 155 155 155 THR THR A . n A 1 156 HIS 156 156 156 HIS HIS A . n A 1 157 LEU 157 157 157 LEU LEU A . n A 1 158 LYS 158 158 158 LYS LYS A . n A 1 159 PHE 159 159 159 PHE PHE A . n A 1 160 LYS 160 160 160 LYS LYS A . n A 1 161 TYR 161 161 161 TYR TYR A . n A 1 162 PRO 162 162 162 PRO PRO A . n A 1 163 ALA 163 163 163 ALA ALA A . n A 1 164 LEU 164 164 164 LEU LEU A . n A 1 165 ASN 165 165 165 ASN ASN A . n A 1 166 VAL 166 166 166 VAL VAL A . n A 1 167 THR 167 167 167 THR THR A . n A 1 168 MET 168 168 168 MET MET A . n A 1 169 PRO 169 169 169 PRO PRO A . n A 1 170 ASN 170 170 170 ASN ASN A . n A 1 171 ASN 171 171 171 ASN ASN A . n A 1 172 GLU 172 172 172 GLU GLU A . n A 1 173 LYS 173 173 173 LYS LYS A . n A 1 174 PHE 174 174 174 PHE PHE A . n A 1 175 ASP 175 175 175 ASP ASP A . n A 1 176 LYS 176 176 176 LYS LYS A . n A 1 177 LEU 177 177 177 LEU LEU A . n A 1 178 TYR 178 178 178 TYR TYR A . n A 1 179 ILE 179 179 179 ILE ILE A . n A 1 180 TRP 180 180 180 TRP TRP A . n A 1 181 GLY 181 181 181 GLY GLY A . n A 1 182 VAL 182 182 182 VAL VAL A . n A 1 183 HIS 183 183 183 HIS HIS A . n A 1 184 HIS 184 184 184 HIS HIS A . n A 1 185 PRO 185 185 185 PRO PRO A . n A 1 186 GLY 186 186 186 GLY GLY A . n A 1 187 THR 187 187 187 THR THR A . n A 1 188 ASP 188 188 188 ASP ASP A . n A 1 189 ASN 189 189 189 ASN ASN A . n A 1 190 ASP 190 190 190 ASP ASP A . n A 1 191 GLN 191 191 191 GLN GLN A . n A 1 192 ILE 192 192 192 ILE ILE A . n A 1 193 SER 193 193 193 SER SER A . n A 1 194 LEU 194 194 194 LEU LEU A . n A 1 195 TYR 195 195 195 TYR TYR A . n A 1 196 ALA 196 196 196 ALA ALA A . n A 1 197 GLN 197 197 197 GLN GLN A . n A 1 198 ALA 198 198 198 ALA ALA A . n A 1 199 SER 199 199 199 SER SER A . n A 1 200 GLY 200 200 200 GLY GLY A . n A 1 201 ARG 201 201 201 ARG ARG A . n A 1 202 ILE 202 202 202 ILE ILE A . n A 1 203 THR 203 203 203 THR THR A . n A 1 204 VAL 204 204 204 VAL VAL A . n A 1 205 SER 205 205 205 SER SER A . n A 1 206 THR 206 206 206 THR THR A . n A 1 207 LYS 207 207 207 LYS LYS A . n A 1 208 ARG 208 208 208 ARG ARG A . n A 1 209 SER 209 209 209 SER SER A . n A 1 210 GLN 210 210 210 GLN GLN A . n A 1 211 GLN 211 211 211 GLN GLN A . n A 1 212 THR 212 212 212 THR THR A . n A 1 213 VAL 213 213 213 VAL VAL A . n A 1 214 ILE 214 214 214 ILE ILE A . n A 1 215 PRO 215 215 215 PRO PRO A . n A 1 216 ASN 216 216 216 ASN ASN A . n A 1 217 ILE 217 217 217 ILE ILE A . n A 1 218 GLY 218 218 218 GLY GLY A . n A 1 219 SER 219 219 219 SER SER A . n A 1 220 ARG 220 220 220 ARG ARG A . n A 1 221 PRO 221 221 221 PRO PRO A . n A 1 222 ARG 222 222 222 ARG ARG A . n A 1 223 VAL 223 223 223 VAL VAL A . n A 1 224 ARG 224 224 224 ARG ARG A . n A 1 225 ASP 225 225 225 ASP ASP A . n A 1 226 ILE 226 226 226 ILE ILE A . n A 1 227 PRO 227 227 227 PRO PRO A . n A 1 228 SER 228 228 228 SER SER A . n A 1 229 ARG 229 229 229 ARG ARG A . n A 1 230 ILE 230 230 230 ILE ILE A . n A 1 231 SER 231 231 231 SER SER A . n A 1 232 ILE 232 232 232 ILE ILE A . n A 1 233 TYR 233 233 233 TYR TYR A . n A 1 234 TRP 234 234 234 TRP TRP A . n A 1 235 THR 235 235 235 THR THR A . n A 1 236 ILE 236 236 236 ILE ILE A . n A 1 237 VAL 237 237 237 VAL VAL A . n A 1 238 LYS 238 238 238 LYS LYS A . n A 1 239 PRO 239 239 239 PRO PRO A . n A 1 240 GLY 240 240 240 GLY GLY A . n A 1 241 ASP 241 241 241 ASP ASP A . n A 1 242 ILE 242 242 242 ILE ILE A . n A 1 243 LEU 243 243 243 LEU LEU A . n A 1 244 LEU 244 244 244 LEU LEU A . n A 1 245 ILE 245 245 245 ILE ILE A . n A 1 246 ASN 246 246 246 ASN ASN A . n A 1 247 SER 247 247 247 SER SER A . n A 1 248 THR 248 248 248 THR THR A . n A 1 249 GLY 249 249 249 GLY GLY A . n A 1 250 ASN 250 250 250 ASN ASN A . n A 1 251 LEU 251 251 251 LEU LEU A . n A 1 252 ILE 252 252 252 ILE ILE A . n A 1 253 ALA 253 253 253 ALA ALA A . n A 1 254 PRO 254 254 254 PRO PRO A . n A 1 255 ARG 255 255 255 ARG ARG A . n A 1 256 GLY 256 256 256 GLY GLY A . n A 1 257 TYR 257 257 257 TYR TYR A . n A 1 258 PHE 258 258 258 PHE PHE A . n A 1 259 LYS 259 259 259 LYS LYS A . n A 1 260 ILE 260 260 260 ILE ILE A . n A 1 261 ARG 261 261 261 ARG ARG A . n A 1 262 SER 262 262 262 SER SER A . n A 1 263 GLY 263 263 263 GLY GLY A . n A 1 264 LYS 264 264 264 LYS LYS A . n A 1 265 SER 265 265 265 SER SER A . n A 1 266 SER 266 266 266 SER SER A . n A 1 267 ILE 267 267 267 ILE ILE A . n A 1 268 MET 268 268 268 MET MET A . n A 1 269 ARG 269 269 269 ARG ARG A . n A 1 270 SER 270 270 270 SER SER A . n A 1 271 ASP 271 271 271 ASP ASP A . n A 1 272 ALA 272 272 272 ALA ALA A . n A 1 273 PRO 273 273 273 PRO PRO A . n A 1 274 ILE 274 274 274 ILE ILE A . n A 1 275 GLY 275 275 275 GLY GLY A . n A 1 276 LYS 276 276 276 LYS LYS A . n A 1 277 CYS 277 277 277 CYS CYS A . n A 1 278 ASN 278 278 278 ASN ASN A . n A 1 279 SER 279 279 279 SER SER A . n A 1 280 GLU 280 280 280 GLU GLU A . n A 1 281 CYS 281 281 281 CYS CYS A . n A 1 282 ILE 282 282 282 ILE ILE A . n A 1 283 THR 283 283 283 THR THR A . n A 1 284 PRO 284 284 284 PRO PRO A . n A 1 285 ASN 285 285 285 ASN ASN A . n A 1 286 GLY 286 286 286 GLY GLY A . n A 1 287 SER 287 287 287 SER SER A . n A 1 288 ILE 288 288 288 ILE ILE A . n A 1 289 PRO 289 289 289 PRO PRO A . n A 1 290 ASN 290 290 290 ASN ASN A . n A 1 291 ASP 291 291 291 ASP ASP A . n A 1 292 LYS 292 292 292 LYS LYS A . n A 1 293 PRO 293 293 293 PRO PRO A . n A 1 294 PHE 294 294 294 PHE PHE A . n A 1 295 GLN 295 295 295 GLN GLN A . n A 1 296 ASN 296 296 296 ASN ASN A . n A 1 297 VAL 297 297 297 VAL VAL A . n A 1 298 ASN 298 298 298 ASN ASN A . n A 1 299 ARG 299 299 299 ARG ARG A . n A 1 300 ILE 300 300 300 ILE ILE A . n A 1 301 THR 301 301 301 THR THR A . n A 1 302 TYR 302 302 302 TYR TYR A . n A 1 303 GLY 303 303 303 GLY GLY A . n A 1 304 ALA 304 304 304 ALA ALA A . n A 1 305 CYS 305 305 305 CYS CYS A . n A 1 306 PRO 306 306 306 PRO PRO A . n A 1 307 ARG 307 307 307 ARG ARG A . n A 1 308 TYR 308 308 308 TYR TYR A . n A 1 309 VAL 309 309 309 VAL VAL A . n A 1 310 LYS 310 310 310 LYS LYS A . n A 1 311 GLN 311 311 311 GLN GLN A . n A 1 312 ASN 312 312 312 ASN ASN A . n A 1 313 THR 313 313 313 THR THR A . n A 1 314 LEU 314 314 314 LEU LEU A . n A 1 315 LYS 315 315 315 LYS LYS A . n A 1 316 LEU 316 316 316 LEU LEU A . n A 1 317 ALA 317 317 317 ALA ALA A . n A 1 318 THR 318 318 318 THR THR A . n A 1 319 GLY 319 319 319 GLY GLY A . n A 1 320 MET 320 320 320 MET MET A . n A 1 321 ARG 321 321 321 ARG ARG A . n A 1 322 ASN 322 322 322 ASN ASN A . n A 1 323 VAL 323 323 323 VAL VAL A . n A 1 324 PRO 324 324 324 PRO PRO A . n A 1 325 GLU 325 325 325 GLU GLU A . n A 1 326 LYS 326 326 326 LYS LYS A . n A 1 327 GLN 327 327 327 GLN GLN A . n A 1 328 THR 328 328 328 THR THR A . n A 1 329 GLN 329 329 ? ? ? A . n A 1 330 GLY 330 330 ? ? ? A . n A 1 331 ILE 331 331 ? ? ? A . n A 1 332 PHE 332 332 ? ? ? A . n A 1 333 GLY 333 333 ? ? ? A . n A 1 334 ALA 334 334 334 ALA ALA A . n A 1 335 ILE 335 335 335 ILE ILE A . n A 1 336 ALA 336 336 336 ALA ALA A . n A 1 337 GLY 337 337 337 GLY GLY A . n A 1 338 PHE 338 338 338 PHE PHE A . n A 1 339 ILE 339 339 339 ILE ILE A . n A 1 340 GLU 340 340 340 GLU GLU A . n A 1 341 ASN 341 341 341 ASN ASN A . n A 1 342 GLY 342 342 342 GLY GLY A . n A 1 343 TRP 343 343 343 TRP TRP A . n A 1 344 GLU 344 344 344 GLU GLU A . n A 1 345 GLY 345 345 345 GLY GLY A . n A 1 346 MET 346 346 346 MET MET A . n A 1 347 VAL 347 347 347 VAL VAL A . n A 1 348 ASP 348 348 348 ASP ASP A . n A 1 349 GLY 349 349 349 GLY GLY A . n A 1 350 TRP 350 350 350 TRP TRP A . n A 1 351 TYR 351 351 351 TYR TYR A . n A 1 352 GLY 352 352 352 GLY GLY A . n A 1 353 PHE 353 353 353 PHE PHE A . n A 1 354 ARG 354 354 354 ARG ARG A . n A 1 355 HIS 355 355 355 HIS HIS A . n A 1 356 GLN 356 356 356 GLN GLN A . n A 1 357 ASN 357 357 357 ASN ASN A . n A 1 358 SER 358 358 358 SER SER A . n A 1 359 GLU 359 359 359 GLU GLU A . n A 1 360 GLY 360 360 360 GLY GLY A . n A 1 361 ILE 361 361 361 ILE ILE A . n A 1 362 GLY 362 362 362 GLY GLY A . n A 1 363 GLN 363 363 363 GLN GLN A . n A 1 364 ALA 364 364 364 ALA ALA A . n A 1 365 ALA 365 365 365 ALA ALA A . n A 1 366 ASP 366 366 366 ASP ASP A . n A 1 367 LEU 367 367 367 LEU LEU A . n A 1 368 LYS 368 368 368 LYS LYS A . n A 1 369 SER 369 369 369 SER SER A . n A 1 370 THR 370 370 370 THR THR A . n A 1 371 GLN 371 371 371 GLN GLN A . n A 1 372 ALA 372 372 372 ALA ALA A . n A 1 373 ALA 373 373 373 ALA ALA A . n A 1 374 ILE 374 374 374 ILE ILE A . n A 1 375 ASN 375 375 375 ASN ASN A . n A 1 376 GLN 376 376 376 GLN GLN A . n A 1 377 ILE 377 377 377 ILE ILE A . n A 1 378 ASN 378 378 378 ASN ASN A . n A 1 379 GLY 379 379 379 GLY GLY A . n A 1 380 LYS 380 380 380 LYS LYS A . n A 1 381 LEU 381 381 381 LEU LEU A . n A 1 382 ASN 382 382 382 ASN ASN A . n A 1 383 ARG 383 383 383 ARG ARG A . n A 1 384 LEU 384 384 384 LEU LEU A . n A 1 385 ILE 385 385 385 ILE ILE A . n A 1 386 GLY 386 386 386 GLY GLY A . n A 1 387 LYS 387 387 387 LYS LYS A . n A 1 388 THR 388 388 388 THR THR A . n A 1 389 ASN 389 389 389 ASN ASN A . n A 1 390 GLU 390 390 390 GLU GLU A . n A 1 391 LYS 391 391 391 LYS LYS A . n A 1 392 PHE 392 392 392 PHE PHE A . n A 1 393 HIS 393 393 393 HIS HIS A . n A 1 394 GLN 394 394 394 GLN GLN A . n A 1 395 ILE 395 395 395 ILE ILE A . n A 1 396 GLU 396 396 396 GLU GLU A . n A 1 397 LYS 397 397 397 LYS LYS A . n A 1 398 GLU 398 398 398 GLU GLU A . n A 1 399 PHE 399 399 399 PHE PHE A . n A 1 400 SER 400 400 400 SER SER A . n A 1 401 GLU 401 401 401 GLU GLU A . n A 1 402 VAL 402 402 402 VAL VAL A . n A 1 403 GLU 403 403 403 GLU GLU A . n A 1 404 GLY 404 404 404 GLY GLY A . n A 1 405 ARG 405 405 405 ARG ARG A . n A 1 406 ILE 406 406 406 ILE ILE A . n A 1 407 GLN 407 407 407 GLN GLN A . n A 1 408 ASP 408 408 408 ASP ASP A . n A 1 409 LEU 409 409 409 LEU LEU A . n A 1 410 GLU 410 410 410 GLU GLU A . n A 1 411 LYS 411 411 411 LYS LYS A . n A 1 412 TYR 412 412 412 TYR TYR A . n A 1 413 VAL 413 413 413 VAL VAL A . n A 1 414 GLU 414 414 414 GLU GLU A . n A 1 415 ASP 415 415 415 ASP ASP A . n A 1 416 THR 416 416 416 THR THR A . n A 1 417 LYS 417 417 417 LYS LYS A . n A 1 418 ILE 418 418 418 ILE ILE A . n A 1 419 ASP 419 419 419 ASP ASP A . n A 1 420 LEU 420 420 420 LEU LEU A . n A 1 421 TRP 421 421 421 TRP TRP A . n A 1 422 SER 422 422 422 SER SER A . n A 1 423 TYR 423 423 423 TYR TYR A . n A 1 424 ASN 424 424 424 ASN ASN A . n A 1 425 ALA 425 425 425 ALA ALA A . n A 1 426 GLU 426 426 426 GLU GLU A . n A 1 427 LEU 427 427 427 LEU LEU A . n A 1 428 LEU 428 428 428 LEU LEU A . n A 1 429 VAL 429 429 429 VAL VAL A . n A 1 430 ALA 430 430 430 ALA ALA A . n A 1 431 LEU 431 431 431 LEU LEU A . n A 1 432 GLU 432 432 432 GLU GLU A . n A 1 433 ASN 433 433 433 ASN ASN A . n A 1 434 GLN 434 434 434 GLN GLN A . n A 1 435 HIS 435 435 435 HIS HIS A . n A 1 436 THR 436 436 436 THR THR A . n A 1 437 ILE 437 437 437 ILE ILE A . n A 1 438 ASP 438 438 438 ASP ASP A . n A 1 439 LEU 439 439 439 LEU LEU A . n A 1 440 THR 440 440 440 THR THR A . n A 1 441 ASP 441 441 441 ASP ASP A . n A 1 442 SER 442 442 442 SER SER A . n A 1 443 GLU 443 443 443 GLU GLU A . n A 1 444 MET 444 444 444 MET MET A . n A 1 445 ASN 445 445 445 ASN ASN A . n A 1 446 LYS 446 446 446 LYS LYS A . n A 1 447 LEU 447 447 447 LEU LEU A . n A 1 448 PHE 448 448 448 PHE PHE A . n A 1 449 GLU 449 449 449 GLU GLU A . n A 1 450 ARG 450 450 450 ARG ARG A . n A 1 451 THR 451 451 451 THR THR A . n A 1 452 LYS 452 452 452 LYS LYS A . n A 1 453 LYS 453 453 453 LYS LYS A . n A 1 454 GLN 454 454 454 GLN GLN A . n A 1 455 LEU 455 455 455 LEU LEU A . n A 1 456 ARG 456 456 456 ARG ARG A . n A 1 457 GLU 457 457 457 GLU GLU A . n A 1 458 ASN 458 458 458 ASN ASN A . n A 1 459 ALA 459 459 459 ALA ALA A . n A 1 460 GLU 460 460 460 GLU GLU A . n A 1 461 ASP 461 461 461 ASP ASP A . n A 1 462 MET 462 462 462 MET MET A . n A 1 463 GLY 463 463 463 GLY GLY A . n A 1 464 ASN 464 464 464 ASN ASN A . n A 1 465 GLY 465 465 465 GLY GLY A . n A 1 466 CYS 466 466 466 CYS CYS A . n A 1 467 PHE 467 467 467 PHE PHE A . n A 1 468 LYS 468 468 468 LYS LYS A . n A 1 469 ILE 469 469 469 ILE ILE A . n A 1 470 TYR 470 470 470 TYR TYR A . n A 1 471 HIS 471 471 471 HIS HIS A . n A 1 472 LYS 472 472 472 LYS LYS A . n A 1 473 CYS 473 473 473 CYS CYS A . n A 1 474 ASP 474 474 474 ASP ASP A . n A 1 475 ASN 475 475 475 ASN ASN A . n A 1 476 ALA 476 476 476 ALA ALA A . n A 1 477 CYS 477 477 477 CYS CYS A . n A 1 478 ILE 478 478 478 ILE ILE A . n A 1 479 GLY 479 479 479 GLY GLY A . n A 1 480 SER 480 480 480 SER SER A . n A 1 481 ILE 481 481 481 ILE ILE A . n A 1 482 ARG 482 482 482 ARG ARG A . n A 1 483 ASN 483 483 483 ASN ASN A . n A 1 484 GLY 484 484 484 GLY GLY A . n A 1 485 THR 485 485 485 THR THR A . n A 1 486 TYR 486 486 486 TYR TYR A . n A 1 487 ASP 487 487 487 ASP ASP A . n A 1 488 HIS 488 488 488 HIS HIS A . n A 1 489 ASP 489 489 489 ASP ASP A . n A 1 490 VAL 490 490 490 VAL VAL A . n A 1 491 TYR 491 491 491 TYR TYR A . n A 1 492 ARG 492 492 492 ARG ARG A . n A 1 493 ASP 493 493 493 ASP ASP A . n A 1 494 GLU 494 494 494 GLU GLU A . n A 1 495 ALA 495 495 495 ALA ALA A . n A 1 496 LEU 496 496 496 LEU LEU A . n A 1 497 ASN 497 497 497 ASN ASN A . n A 1 498 ASN 498 498 498 ASN ASN A . n A 1 499 ARG 499 499 499 ARG ARG A . n A 1 500 PHE 500 500 500 PHE PHE A . n A 1 501 GLN 501 501 501 GLN GLN A . n A 1 502 ILE 502 502 502 ILE ILE A . n A 1 503 LYS 503 503 503 LYS LYS A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 801 801 NAG NAG A . C 2 NAG 2 802 802 NAG NAG A . D 3 MAN 3 803 803 MAN MAN A . E 2 NAG 1 804 804 NAG NAG A . F 2 NAG 1 805 805 NAG NAG A . G 2 NAG 1 806 806 NAG NAG A . H 2 NAG 2 807 807 NAG NAG A . I 3 MAN 3 808 808 MAN MAN A . J 2 NAG 1 809 809 NAG NAG A . K 2 NAG 2 810 810 NAG NAG A . L 2 NAG 1 812 812 NAG NAG A . M 2 NAG 1 813 813 NAG NAG A . N 4 EPE 1 1504 1504 EPE EPE A . O 4 EPE 1 1505 1505 EPE EPE A . P 4 EPE 1 1506 1506 EPE EPE A . Q 5 TAM 1 1507 1507 TAM TAM A . R 6 HOH 1 2001 2001 HOH HOH A . R 6 HOH 2 2002 2002 HOH HOH A . R 6 HOH 3 2003 2003 HOH HOH A . R 6 HOH 4 2004 2004 HOH HOH A . R 6 HOH 5 2005 2005 HOH HOH A . R 6 HOH 6 2006 2006 HOH HOH A . R 6 HOH 7 2007 2007 HOH HOH A . R 6 HOH 8 2008 2008 HOH HOH A . R 6 HOH 9 2009 2009 HOH HOH A . R 6 HOH 10 2010 2010 HOH HOH A . R 6 HOH 11 2011 2011 HOH HOH A . R 6 HOH 12 2012 2012 HOH HOH A . R 6 HOH 13 2013 2013 HOH HOH A . R 6 HOH 14 2014 2014 HOH HOH A . R 6 HOH 15 2015 2015 HOH HOH A . R 6 HOH 16 2016 2016 HOH HOH A . R 6 HOH 17 2017 2017 HOH HOH A . R 6 HOH 18 2018 2018 HOH HOH A . R 6 HOH 19 2019 2019 HOH HOH A . R 6 HOH 20 2020 2020 HOH HOH A . R 6 HOH 21 2021 2021 HOH HOH A . R 6 HOH 22 2022 2022 HOH HOH A . R 6 HOH 23 2023 2023 HOH HOH A . R 6 HOH 24 2024 2024 HOH HOH A . R 6 HOH 25 2025 2025 HOH HOH A . R 6 HOH 26 2026 2026 HOH HOH A . R 6 HOH 27 2027 2027 HOH HOH A . R 6 HOH 28 2028 2028 HOH HOH A . R 6 HOH 29 2029 2029 HOH HOH A . R 6 HOH 30 2030 2030 HOH HOH A . R 6 HOH 31 2031 2031 HOH HOH A . R 6 HOH 32 2032 2032 HOH HOH A . R 6 HOH 33 2033 2033 HOH HOH A . R 6 HOH 34 2034 2034 HOH HOH A . R 6 HOH 35 2035 2035 HOH HOH A . R 6 HOH 36 2036 2036 HOH HOH A . R 6 HOH 37 2037 2037 HOH HOH A . R 6 HOH 38 2038 2038 HOH HOH A . R 6 HOH 39 2039 2039 HOH HOH A . R 6 HOH 40 2040 2040 HOH HOH A . R 6 HOH 41 2041 2041 HOH HOH A . R 6 HOH 42 2042 2042 HOH HOH A . R 6 HOH 43 2043 2043 HOH HOH A . R 6 HOH 44 2044 2044 HOH HOH A . R 6 HOH 45 2045 2045 HOH HOH A . R 6 HOH 46 2046 2046 HOH HOH A . R 6 HOH 47 2047 2047 HOH HOH A . R 6 HOH 48 2048 2048 HOH HOH A . R 6 HOH 49 2049 2049 HOH HOH A . R 6 HOH 50 2050 2050 HOH HOH A . R 6 HOH 51 2051 2051 HOH HOH A . R 6 HOH 52 2052 2052 HOH HOH A . R 6 HOH 53 2053 2053 HOH HOH A . R 6 HOH 54 2054 2054 HOH HOH A . R 6 HOH 55 2055 2055 HOH HOH A . R 6 HOH 56 2056 2056 HOH HOH A . R 6 HOH 57 2057 2057 HOH HOH A . R 6 HOH 58 2058 2058 HOH HOH A . R 6 HOH 59 2059 2059 HOH HOH A . R 6 HOH 60 2060 2060 HOH HOH A . R 6 HOH 61 2061 2061 HOH HOH A . R 6 HOH 62 2062 2062 HOH HOH A . R 6 HOH 63 2063 2063 HOH HOH A . R 6 HOH 64 2064 2064 HOH HOH A . R 6 HOH 65 2065 2065 HOH HOH A . R 6 HOH 66 2066 2066 HOH HOH A . R 6 HOH 67 2067 2067 HOH HOH A . R 6 HOH 68 2068 2068 HOH HOH A . R 6 HOH 69 2069 2069 HOH HOH A . R 6 HOH 70 2070 2070 HOH HOH A . R 6 HOH 71 2071 2071 HOH HOH A . R 6 HOH 72 2072 2072 HOH HOH A . R 6 HOH 73 2073 2073 HOH HOH A . R 6 HOH 74 2074 2074 HOH HOH A . R 6 HOH 75 2075 2075 HOH HOH A . R 6 HOH 76 2076 2076 HOH HOH A . R 6 HOH 77 2077 2077 HOH HOH A . R 6 HOH 78 2078 2078 HOH HOH A . R 6 HOH 79 2079 2079 HOH HOH A . R 6 HOH 80 2080 2080 HOH HOH A . R 6 HOH 81 2081 2081 HOH HOH A . R 6 HOH 82 2082 2082 HOH HOH A . R 6 HOH 83 2083 2083 HOH HOH A . R 6 HOH 84 2084 2084 HOH HOH A . R 6 HOH 85 2085 2085 HOH HOH A . R 6 HOH 86 2086 2086 HOH HOH A . R 6 HOH 87 2087 2087 HOH HOH A . R 6 HOH 88 2088 2088 HOH HOH A . R 6 HOH 89 2089 2089 HOH HOH A . R 6 HOH 90 2090 2090 HOH HOH A . R 6 HOH 91 2091 2091 HOH HOH A . R 6 HOH 92 2092 2092 HOH HOH A . R 6 HOH 93 2093 2093 HOH HOH A . R 6 HOH 94 2094 2094 HOH HOH A . R 6 HOH 95 2095 2095 HOH HOH A . R 6 HOH 96 2096 2096 HOH HOH A . R 6 HOH 97 2097 2097 HOH HOH A . R 6 HOH 98 2098 2098 HOH HOH A . R 6 HOH 99 2099 2099 HOH HOH A . R 6 HOH 100 2100 2100 HOH HOH A . R 6 HOH 101 2101 2101 HOH HOH A . R 6 HOH 102 2102 2102 HOH HOH A . R 6 HOH 103 2103 2103 HOH HOH A . R 6 HOH 104 2104 2104 HOH HOH A . R 6 HOH 105 2105 2105 HOH HOH A . R 6 HOH 106 2106 2106 HOH HOH A . R 6 HOH 107 2107 2107 HOH HOH A . R 6 HOH 108 2108 2108 HOH HOH A . R 6 HOH 109 2109 2109 HOH HOH A . R 6 HOH 110 2110 2110 HOH HOH A . R 6 HOH 111 2111 2111 HOH HOH A . R 6 HOH 112 2112 2112 HOH HOH A . R 6 HOH 113 2113 2113 HOH HOH A . R 6 HOH 114 2114 2114 HOH HOH A . R 6 HOH 115 2115 2115 HOH HOH A . R 6 HOH 116 2116 2116 HOH HOH A . R 6 HOH 117 2117 2117 HOH HOH A . R 6 HOH 118 2118 2118 HOH HOH A . R 6 HOH 119 2119 2119 HOH HOH A . R 6 HOH 120 2120 2120 HOH HOH A . R 6 HOH 121 2121 2121 HOH HOH A . R 6 HOH 122 2122 2122 HOH HOH A . R 6 HOH 123 2123 2123 HOH HOH A . R 6 HOH 124 2124 2124 HOH HOH A . R 6 HOH 125 2125 2125 HOH HOH A . R 6 HOH 126 2126 2126 HOH HOH A . R 6 HOH 127 2127 2127 HOH HOH A . R 6 HOH 128 2128 2128 HOH HOH A . R 6 HOH 129 2129 2129 HOH HOH A . R 6 HOH 130 2130 2130 HOH HOH A . R 6 HOH 131 2131 2131 HOH HOH A . R 6 HOH 132 2132 2132 HOH HOH A . R 6 HOH 133 2133 2133 HOH HOH A . R 6 HOH 134 2134 2134 HOH HOH A . R 6 HOH 135 2135 2135 HOH HOH A . R 6 HOH 136 2136 2136 HOH HOH A . R 6 HOH 137 2137 2137 HOH HOH A . R 6 HOH 138 2138 2138 HOH HOH A . R 6 HOH 139 2139 2139 HOH HOH A . R 6 HOH 140 2140 2140 HOH HOH A . R 6 HOH 141 2141 2141 HOH HOH A . R 6 HOH 142 2142 2142 HOH HOH A . R 6 HOH 143 2143 2143 HOH HOH A . R 6 HOH 144 2144 2144 HOH HOH A . R 6 HOH 145 2145 2145 HOH HOH A . R 6 HOH 146 2146 2146 HOH HOH A . R 6 HOH 147 2147 2147 HOH HOH A . R 6 HOH 148 2148 2148 HOH HOH A . R 6 HOH 149 2149 2149 HOH HOH A . R 6 HOH 150 2150 2150 HOH HOH A . R 6 HOH 151 2151 2151 HOH HOH A . R 6 HOH 152 2152 2152 HOH HOH A . R 6 HOH 153 2153 2153 HOH HOH A . R 6 HOH 154 2154 2154 HOH HOH A . R 6 HOH 155 2155 2155 HOH HOH A . R 6 HOH 156 2156 2156 HOH HOH A . R 6 HOH 157 2157 2157 HOH HOH A . R 6 HOH 158 2158 2158 HOH HOH A . R 6 HOH 159 2159 2159 HOH HOH A . R 6 HOH 160 2160 2160 HOH HOH A . R 6 HOH 161 2161 2161 HOH HOH A . R 6 HOH 162 2162 2162 HOH HOH A . R 6 HOH 163 2163 2163 HOH HOH A . R 6 HOH 164 2164 2164 HOH HOH A . R 6 HOH 165 2165 2165 HOH HOH A . R 6 HOH 166 2166 2166 HOH HOH A . R 6 HOH 167 2167 2167 HOH HOH A . R 6 HOH 168 2168 2168 HOH HOH A . R 6 HOH 169 2169 2169 HOH HOH A . R 6 HOH 170 2170 2170 HOH HOH A . R 6 HOH 171 2171 2171 HOH HOH A . R 6 HOH 172 2172 2172 HOH HOH A . R 6 HOH 173 2173 2173 HOH HOH A . R 6 HOH 174 2174 2174 HOH HOH A . R 6 HOH 175 2175 2175 HOH HOH A . R 6 HOH 176 2176 2176 HOH HOH A . R 6 HOH 177 2177 2177 HOH HOH A . R 6 HOH 178 2178 2178 HOH HOH A . R 6 HOH 179 2179 2179 HOH HOH A . R 6 HOH 180 2180 2180 HOH HOH A . R 6 HOH 181 2181 2181 HOH HOH A . R 6 HOH 182 2182 2182 HOH HOH A . R 6 HOH 183 2183 2183 HOH HOH A . R 6 HOH 184 2184 2184 HOH HOH A . R 6 HOH 185 2185 2185 HOH HOH A . R 6 HOH 186 2186 2186 HOH HOH A . R 6 HOH 187 2187 2187 HOH HOH A . R 6 HOH 188 2188 2188 HOH HOH A . R 6 HOH 189 2189 2189 HOH HOH A . R 6 HOH 190 2190 2190 HOH HOH A . R 6 HOH 191 2191 2191 HOH HOH A . R 6 HOH 192 2192 2192 HOH HOH A . R 6 HOH 193 2193 2193 HOH HOH A . R 6 HOH 194 2194 2194 HOH HOH A . R 6 HOH 195 2195 2195 HOH HOH A . R 6 HOH 196 2196 2196 HOH HOH A . R 6 HOH 197 2197 2197 HOH HOH A . R 6 HOH 198 2198 2198 HOH HOH A . R 6 HOH 199 2199 2199 HOH HOH A . R 6 HOH 200 2200 2200 HOH HOH A . R 6 HOH 201 2201 2201 HOH HOH A . R 6 HOH 202 2202 2202 HOH HOH A . R 6 HOH 203 2203 2203 HOH HOH A . R 6 HOH 204 2204 2204 HOH HOH A . R 6 HOH 205 2205 2205 HOH HOH A . R 6 HOH 206 2206 2206 HOH HOH A . R 6 HOH 207 2207 2207 HOH HOH A . R 6 HOH 208 2208 2208 HOH HOH A . R 6 HOH 209 2209 2209 HOH HOH A . R 6 HOH 210 2210 2210 HOH HOH A . R 6 HOH 211 2211 2211 HOH HOH A . R 6 HOH 212 2212 2212 HOH HOH A . R 6 HOH 213 2213 2213 HOH HOH A . R 6 HOH 214 2214 2214 HOH HOH A . R 6 HOH 215 2215 2215 HOH HOH A . R 6 HOH 216 2216 2216 HOH HOH A . R 6 HOH 217 2217 2217 HOH HOH A . R 6 HOH 218 2218 2218 HOH HOH A . R 6 HOH 219 2219 2219 HOH HOH A . R 6 HOH 220 2220 2220 HOH HOH A . R 6 HOH 221 2221 2221 HOH HOH A . R 6 HOH 222 2222 2222 HOH HOH A . R 6 HOH 223 2223 2223 HOH HOH A . R 6 HOH 224 2224 2224 HOH HOH A . R 6 HOH 225 2225 2225 HOH HOH A . R 6 HOH 226 2226 2226 HOH HOH A . R 6 HOH 227 2227 2227 HOH HOH A . R 6 HOH 228 2228 2228 HOH HOH A . R 6 HOH 229 2229 2229 HOH HOH A . R 6 HOH 230 2230 2230 HOH HOH A . R 6 HOH 231 2231 2231 HOH HOH A . R 6 HOH 232 2232 2232 HOH HOH A . R 6 HOH 233 2233 2233 HOH HOH A . R 6 HOH 234 2234 2234 HOH HOH A . R 6 HOH 235 2235 2235 HOH HOH A . R 6 HOH 236 2236 2236 HOH HOH A . R 6 HOH 237 2237 2237 HOH HOH A . R 6 HOH 238 2238 2238 HOH HOH A . R 6 HOH 239 2239 2239 HOH HOH A . R 6 HOH 240 2240 2240 HOH HOH A . R 6 HOH 241 2241 2241 HOH HOH A . R 6 HOH 242 2242 2242 HOH HOH A . R 6 HOH 243 2243 2243 HOH HOH A . R 6 HOH 244 2244 2244 HOH HOH A . R 6 HOH 245 2245 2245 HOH HOH A . R 6 HOH 246 2246 2246 HOH HOH A . R 6 HOH 247 2247 2247 HOH HOH A . R 6 HOH 248 2248 2248 HOH HOH A . R 6 HOH 249 2249 2249 HOH HOH A . R 6 HOH 250 2250 2250 HOH HOH A . R 6 HOH 251 2251 2251 HOH HOH A . R 6 HOH 252 2252 2252 HOH HOH A . R 6 HOH 253 2253 2253 HOH HOH A . R 6 HOH 254 2254 2254 HOH HOH A . R 6 HOH 255 2255 2255 HOH HOH A . R 6 HOH 256 2256 2256 HOH HOH A . R 6 HOH 257 2257 2257 HOH HOH A . R 6 HOH 258 2258 2258 HOH HOH A . R 6 HOH 259 2259 2259 HOH HOH A . R 6 HOH 260 2260 2260 HOH HOH A . R 6 HOH 261 2261 2261 HOH HOH A . R 6 HOH 262 2262 2262 HOH HOH A . R 6 HOH 263 2263 2263 HOH HOH A . R 6 HOH 264 2264 2264 HOH HOH A . R 6 HOH 265 2265 2265 HOH HOH A . R 6 HOH 266 2266 2266 HOH HOH A . R 6 HOH 267 2267 2267 HOH HOH A . R 6 HOH 268 2268 2268 HOH HOH A . R 6 HOH 269 2269 2269 HOH HOH A . R 6 HOH 270 2270 2270 HOH HOH A . R 6 HOH 271 2271 2271 HOH HOH A . R 6 HOH 272 2272 2272 HOH HOH A . R 6 HOH 273 2273 2273 HOH HOH A . R 6 HOH 274 2274 2274 HOH HOH A . R 6 HOH 275 2275 2275 HOH HOH A . R 6 HOH 276 2276 2276 HOH HOH A . R 6 HOH 277 2277 2277 HOH HOH A . R 6 HOH 278 2278 2278 HOH HOH A . R 6 HOH 279 2279 2279 HOH HOH A . R 6 HOH 280 2280 2280 HOH HOH A . R 6 HOH 281 2281 2281 HOH HOH A . R 6 HOH 282 2282 2282 HOH HOH A . R 6 HOH 283 2283 2283 HOH HOH A . R 6 HOH 284 2284 2284 HOH HOH A . R 6 HOH 285 2285 2285 HOH HOH A . R 6 HOH 286 2286 2286 HOH HOH A . R 6 HOH 287 2287 2287 HOH HOH A . R 6 HOH 288 2288 2288 HOH HOH A . R 6 HOH 289 2289 2289 HOH HOH A . R 6 HOH 290 2290 2290 HOH HOH A . R 6 HOH 291 2291 2291 HOH HOH A . R 6 HOH 292 2292 2292 HOH HOH A . R 6 HOH 293 2293 2293 HOH HOH A . R 6 HOH 294 2294 2294 HOH HOH A . R 6 HOH 295 2295 2295 HOH HOH A . R 6 HOH 296 2296 2296 HOH HOH A . R 6 HOH 297 2297 2297 HOH HOH A . R 6 HOH 298 2298 2298 HOH HOH A . R 6 HOH 299 2299 2299 HOH HOH A . R 6 HOH 300 2300 2300 HOH HOH A . R 6 HOH 301 2301 2301 HOH HOH A . R 6 HOH 302 2302 2302 HOH HOH A . R 6 HOH 303 2303 2303 HOH HOH A . R 6 HOH 304 2304 2304 HOH HOH A . R 6 HOH 305 2305 2305 HOH HOH A . R 6 HOH 306 2306 2306 HOH HOH A . R 6 HOH 307 2307 2307 HOH HOH A . R 6 HOH 308 2308 2308 HOH HOH A . R 6 HOH 309 2309 2309 HOH HOH A . R 6 HOH 310 2310 2310 HOH HOH A . R 6 HOH 311 2311 2311 HOH HOH A . R 6 HOH 312 2312 2312 HOH HOH A . R 6 HOH 313 2313 2313 HOH HOH A . R 6 HOH 314 2314 2314 HOH HOH A . R 6 HOH 315 2315 2315 HOH HOH A . R 6 HOH 316 2316 2316 HOH HOH A . R 6 HOH 317 2317 2317 HOH HOH A . R 6 HOH 318 2318 2318 HOH HOH A . R 6 HOH 319 2319 2319 HOH HOH A . R 6 HOH 320 2320 2320 HOH HOH A . R 6 HOH 321 2321 2321 HOH HOH A . R 6 HOH 322 2322 2322 HOH HOH A . R 6 HOH 323 2323 2323 HOH HOH A . R 6 HOH 324 2324 2324 HOH HOH A . R 6 HOH 325 2325 2325 HOH HOH A . R 6 HOH 326 2326 2326 HOH HOH A . R 6 HOH 327 2327 2327 HOH HOH A . R 6 HOH 328 2328 2328 HOH HOH A . R 6 HOH 329 2329 2329 HOH HOH A . R 6 HOH 330 2330 2330 HOH HOH A . R 6 HOH 331 2331 2331 HOH HOH A . R 6 HOH 332 2332 2332 HOH HOH A . R 6 HOH 333 2333 2333 HOH HOH A . R 6 HOH 334 2334 2334 HOH HOH A . R 6 HOH 335 2335 2335 HOH HOH A . R 6 HOH 336 2336 2336 HOH HOH A . R 6 HOH 337 2337 2337 HOH HOH A . R 6 HOH 338 2338 2338 HOH HOH A . R 6 HOH 339 2339 2339 HOH HOH A . R 6 HOH 340 2340 2340 HOH HOH A . R 6 HOH 341 2341 2341 HOH HOH A . R 6 HOH 342 2342 2342 HOH HOH A . R 6 HOH 343 2343 2343 HOH HOH A . R 6 HOH 344 2344 2344 HOH HOH A . R 6 HOH 345 2345 2345 HOH HOH A . R 6 HOH 346 2346 2346 HOH HOH A . R 6 HOH 347 2347 2347 HOH HOH A . R 6 HOH 348 2348 2348 HOH HOH A . R 6 HOH 349 2349 2349 HOH HOH A . R 6 HOH 350 2350 2350 HOH HOH A . R 6 HOH 351 2351 2351 HOH HOH A . R 6 HOH 352 2352 2352 HOH HOH A . R 6 HOH 353 2353 2353 HOH HOH A . R 6 HOH 354 2354 2354 HOH HOH A . R 6 HOH 355 2355 2355 HOH HOH A . R 6 HOH 356 2356 2356 HOH HOH A . R 6 HOH 357 2357 2357 HOH HOH A . R 6 HOH 358 2358 2358 HOH HOH A . R 6 HOH 359 2359 2359 HOH HOH A . R 6 HOH 360 2360 2360 HOH HOH A . R 6 HOH 361 2361 2361 HOH HOH A . R 6 HOH 362 2362 2362 HOH HOH A . R 6 HOH 363 2363 2363 HOH HOH A . R 6 HOH 364 2364 2364 HOH HOH A . R 6 HOH 365 2365 2365 HOH HOH A . R 6 HOH 366 2366 2366 HOH HOH A . R 6 HOH 367 2367 2367 HOH HOH A . R 6 HOH 368 2368 2368 HOH HOH A . R 6 HOH 369 2369 2369 HOH HOH A . R 6 HOH 370 2370 2370 HOH HOH A . R 6 HOH 371 2371 2371 HOH HOH A . R 6 HOH 372 2372 2372 HOH HOH A . R 6 HOH 373 2373 2373 HOH HOH A . R 6 HOH 374 2374 2374 HOH HOH A . R 6 HOH 375 2375 2375 HOH HOH A . R 6 HOH 376 2376 2376 HOH HOH A . R 6 HOH 377 2377 2377 HOH HOH A . R 6 HOH 378 2378 2378 HOH HOH A . R 6 HOH 379 2379 2379 HOH HOH A . R 6 HOH 380 2380 2380 HOH HOH A . R 6 HOH 381 2381 2381 HOH HOH A . R 6 HOH 382 2382 2382 HOH HOH A . R 6 HOH 383 2383 2383 HOH HOH A . R 6 HOH 384 2384 2384 HOH HOH A . R 6 HOH 385 2385 2385 HOH HOH A . R 6 HOH 386 2386 2386 HOH HOH A . R 6 HOH 387 2387 2387 HOH HOH A . R 6 HOH 388 2388 2388 HOH HOH A . R 6 HOH 389 2389 2389 HOH HOH A . R 6 HOH 390 2390 2390 HOH HOH A . R 6 HOH 391 2391 2391 HOH HOH A . R 6 HOH 392 2392 2392 HOH HOH A . R 6 HOH 393 2393 2393 HOH HOH A . R 6 HOH 394 2394 2394 HOH HOH A . R 6 HOH 395 2395 2395 HOH HOH A . R 6 HOH 396 2396 2396 HOH HOH A . R 6 HOH 397 2397 2397 HOH HOH A . R 6 HOH 398 2398 2398 HOH HOH A . R 6 HOH 399 2399 2399 HOH HOH A . R 6 HOH 400 2400 2400 HOH HOH A . R 6 HOH 401 2401 2401 HOH HOH A . R 6 HOH 402 2402 2402 HOH HOH A . R 6 HOH 403 2403 2403 HOH HOH A . R 6 HOH 404 2404 2404 HOH HOH A . R 6 HOH 405 2405 2405 HOH HOH A . R 6 HOH 406 2406 2406 HOH HOH A . R 6 HOH 407 2407 2407 HOH HOH A . R 6 HOH 408 2408 2408 HOH HOH A . R 6 HOH 409 2409 2409 HOH HOH A . R 6 HOH 410 2410 2410 HOH HOH A . R 6 HOH 411 2411 2411 HOH HOH A . R 6 HOH 412 2412 2412 HOH HOH A . R 6 HOH 413 2413 2413 HOH HOH A . R 6 HOH 414 2414 2414 HOH HOH A . R 6 HOH 415 2415 2415 HOH HOH A . R 6 HOH 416 2416 2416 HOH HOH A . R 6 HOH 417 2417 2417 HOH HOH A . R 6 HOH 418 2418 2418 HOH HOH A . R 6 HOH 419 2419 2419 HOH HOH A . R 6 HOH 420 2420 2420 HOH HOH A . R 6 HOH 421 2421 2421 HOH HOH A . R 6 HOH 422 2422 2422 HOH HOH A . R 6 HOH 423 2423 2423 HOH HOH A . R 6 HOH 424 2424 2424 HOH HOH A . R 6 HOH 425 2425 2425 HOH HOH A . R 6 HOH 426 2426 2426 HOH HOH A . R 6 HOH 427 2427 2427 HOH HOH A . R 6 HOH 428 2428 2428 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 38 A ASN 38 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 63 A ASN 63 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 133 A ASN 133 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 165 A ASN 165 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 246 A ASN 246 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 285 A ASN 285 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 483 A ASN 483 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details trimeric _pdbx_struct_assembly.oligomeric_count 3 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3 _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 # 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)' 27440 ? 1 MORE 154.9 ? 1 'SSA (A^2)' 61910 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_545 -y,x-y-1,z -0.5000000000 -0.8660254038 0.0000000000 50.4600000000 0.8660254038 -0.5000000000 0.0000000000 -87.3992837499 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 3_655 -x+y+1,-x,z -0.5000000000 0.8660254038 0.0000000000 100.9200000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 A HOH 2098 ? R HOH . 2 1 A HOH 2428 ? R HOH . # 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 2012-11-07 2 'Structure model' 1 1 2012-12-26 3 'Structure model' 1 2 2013-01-16 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Database references' 2 2 'Structure model' 'Structure summary' 3 3 'Structure model' 'Database references' # 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 30.2354 -36.5019 -57.8295 0.0704 0.0906 0.1033 -0.0149 -0.0418 0.0260 0.1014 0.0777 0.9120 -0.0037 0.2077 0.1314 0.0717 0.0092 -0.0420 -0.0176 -0.0162 0.0639 0.0915 -0.0613 -0.0556 'X-RAY DIFFRACTION' 2 ? refined 31.5680 -26.4862 -92.3823 0.1403 0.1638 0.0388 0.0504 -0.0225 0.0413 0.3622 0.7761 0.6725 -0.0046 -0.2539 -0.0693 0.1168 0.2077 0.0623 -0.1292 -0.0122 -0.0019 -0.0517 -0.1395 -0.1046 'X-RAY DIFFRACTION' 3 ? refined 36.8159 -36.1565 -38.1737 0.1093 0.0862 0.1173 -0.0118 -0.0127 0.0395 0.0816 0.1013 0.7601 0.0490 0.0759 -0.1291 0.0651 -0.0010 -0.0324 0.0417 0.0374 0.0381 -0.0451 -0.0524 -0.1025 'X-RAY DIFFRACTION' 4 ? refined 38.6002 -30.9354 4.8117 0.0729 0.1138 0.0547 -0.0231 0.0535 -0.0027 2.4233 1.8491 3.3239 0.6033 0.3880 2.2751 0.0731 -0.2007 0.0304 -0.0026 0.1413 -0.1166 -0.0126 0.0280 -0.2144 # 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 8 ? ? A 120 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 121 ? ? A 263 ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 264 ? ? A 448 ? ? ? ? 'X-RAY DIFFRACTION' 4 4 A 449 ? ? A 503 ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.6.0117 ? 1 MOSFLM 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 PHASER phasing . ? 4 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 SER A 9 ? ? 74.45 -6.75 2 1 ASN A 22 ? ? -119.50 69.54 3 1 GLU A 62 ? ? 50.32 -117.17 4 1 CYS A 97 ? ? -136.92 -150.74 5 1 TRP A 127 ? ? -98.12 46.39 6 1 SER A 146 ? ? -152.87 -156.15 7 1 ASN A 341 ? ? -170.79 112.16 8 1 PHE A 392 ? ? -125.09 -115.99 9 1 GLN A 394 ? ? -126.98 -126.57 10 1 GLN A 394 ? ? -128.24 -125.14 11 1 ARG A 456 ? ? 54.67 -126.02 12 1 TYR A 470 ? ? -90.26 33.90 13 1 PHE A 500 ? ? -103.72 74.85 # _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 805 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details 'WRONG HAND' _pdbx_validate_chiral.omega . # loop_ _pdbx_distant_solvent_atoms.id _pdbx_distant_solvent_atoms.PDB_model_num _pdbx_distant_solvent_atoms.auth_atom_id _pdbx_distant_solvent_atoms.label_alt_id _pdbx_distant_solvent_atoms.auth_asym_id _pdbx_distant_solvent_atoms.auth_comp_id _pdbx_distant_solvent_atoms.auth_seq_id _pdbx_distant_solvent_atoms.PDB_ins_code _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance _pdbx_distant_solvent_atoms.neighbor_ligand_distance 1 1 O ? A HOH 2098 ? 6.80 . 2 1 O ? A HOH 2427 ? . 7.26 3 1 O ? A HOH 2428 ? 7.72 . # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A GLN 1 ? A GLN 1 2 1 Y 1 A LYS 2 ? A LYS 2 3 1 Y 1 A LEU 3 ? A LEU 3 4 1 Y 1 A PRO 4 ? A PRO 4 5 1 Y 1 A GLY 5 ? A GLY 5 6 1 Y 1 A ASN 6 ? A ASN 6 7 1 Y 1 A ASP 7 ? A ASP 7 8 1 Y 1 A GLN 329 ? A GLN 329 9 1 Y 1 A GLY 330 ? A GLY 330 10 1 Y 1 A ILE 331 ? A ILE 331 11 1 Y 1 A PHE 332 ? A PHE 332 12 1 Y 1 A GLY 333 ? A GLY 333 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 ALPHA-D-MANNOSE MAN 4 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 5 'TRIS(HYDROXYETHYL)AMINOMETHANE' TAM 6 water HOH #