data_2YP3 # _entry.id 2YP3 # _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 2YP3 PDBE EBI-54633 WWPDB D_1290054633 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 2YP2 unspecified 'HAEMAGGLUTININ OF 2004 HUMAN H3N2 VIRUS' 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' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2YP3 _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 2YP3 _cell.length_a 101.130 _cell.length_b 101.130 _cell.length_c 387.880 _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 2YP3 _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 9 ? ? ? ? 3 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 4 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305 2 ? ? ? ? 5 non-polymer man 'O-SIALIC ACID' 309.270 1 ? ? ? ? 6 non-polymer man BETA-D-GALACTOSE 180.156 1 ? ? ? ? 7 non-polymer syn 'TRIS(HYDROXYETHYL)AMINOMETHANE' 163.215 1 ? ? ? ? 8 water nat water 18.015 531 ? ? ? ? # _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 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 A/FINLAND/486/2004 _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 2YP3 _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 2YP3 _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 GAL D-saccharide . BETA-D-GALACTOSE ? 'C6 H12 O6' 180.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 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 SIA non-polymer . 'O-SIALIC ACID' ? 'C11 H19 N O9' 309.270 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 2YP3 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.38 _exptl_crystal.density_percent_sol 63.62 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH ? _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 2012-02-13 _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 0.979492 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'DIAMOND BEAMLINE I04' _diffrn_source.pdbx_synchrotron_site Diamond _diffrn_source.pdbx_synchrotron_beamline I04 _diffrn_source.pdbx_wavelength 0.979492 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 2YP3 _reflns.observed_criterion_sigma_I 3.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 47.09 _reflns.d_resolution_high 1.88 _reflns.number_obs 65943 _reflns.number_all ? _reflns.percent_possible_obs 100.0 _reflns.pdbx_Rmerge_I_obs 0.13 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 9.70 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 7.2 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 2YP3 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 59519 _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 129.29 _refine.ls_d_res_high 1.88 _refine.ls_percent_reflns_obs 99.97 _refine.ls_R_factor_obs 0.17696 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.17561 _refine.ls_R_factor_R_free 0.20293 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 3177 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.958 _refine.correlation_coeff_Fo_to_Fc_free 0.947 _refine.B_iso_mean 27.181 _refine.aniso_B[1][1] 0.83 _refine.aniso_B[2][2] 0.83 _refine.aniso_B[3][3] -1.24 _refine.aniso_B[1][2] 0.41 _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 NONE _refine.pdbx_method_to_determine_struct OTHER _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 0.113 _refine.pdbx_overall_ESU_R_Free 0.108 _refine.overall_SU_ML 0.070 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 4.388 _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 210 _refine_hist.number_atoms_solvent 531 _refine_hist.number_atoms_total 4618 _refine_hist.d_res_high 1.88 _refine_hist.d_res_low 129.29 # 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 ? 4212 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 2860 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.294 1.994 ? 5727 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.818 3.003 ? 6947 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.843 5.000 ? 499 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 35.218 24.901 ? 202 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 11.599 15.000 ? 691 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 13.645 15.000 ? 25 'X-RAY DIFFRACTION' ? r_chiral_restr 0.075 0.200 ? 649 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.005 0.020 ? 4583 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 807 '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 1.880 _refine_ls_shell.d_res_low 1.929 _refine_ls_shell.number_reflns_R_work 4105 _refine_ls_shell.R_factor_R_work 0.256 _refine_ls_shell.percent_reflns_obs 100.00 _refine_ls_shell.R_factor_R_free 0.264 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 210 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 2YP3 _struct.title 'Haemagglutinin of 2004 Human H3N2 Virus in Complex with Human Receptor Analogue 6SLN' _struct.pdbx_descriptor HEMAGGLUTININ _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 2YP3 _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 2 ? E N N 2 ? F N N 2 ? G N N 3 ? H N N 2 ? I N N 2 ? J N N 2 ? K N N 4 ? L N N 4 ? M N N 5 ? N N N 6 ? O N N 2 ? P N N 7 ? Q N N 8 ? # _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 ? ? ? ? ? ? ? 2.083 ? disulf2 disulf ? ? A CYS 52 SG ? ? ? 1_555 A CYS 277 SG ? ? A CYS 52 A CYS 277 1_555 ? ? ? ? ? ? ? 2.096 ? disulf3 disulf ? ? A CYS 64 SG ? ? ? 1_555 A CYS 76 SG ? ? A CYS 64 A CYS 76 1_555 ? ? ? ? ? ? ? 2.086 ? disulf4 disulf ? ? A CYS 97 SG ? ? ? 1_555 A CYS 139 SG ? ? A CYS 97 A CYS 139 1_555 ? ? ? ? ? ? ? 2.066 ? disulf5 disulf ? ? A CYS 281 SG ? ? ? 1_555 A CYS 305 SG ? ? A CYS 281 A CYS 305 1_555 ? ? ? ? ? ? ? 2.062 ? disulf6 disulf ? ? A CYS 473 SG ? ? ? 1_555 A CYS 477 SG ? ? A CYS 473 A CYS 477 1_555 ? ? ? ? ? ? ? 2.107 ? covale1 covale ? ? A ASN 38 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 38 A NAG 1504 1_555 ? ? ? ? ? ? ? 1.441 ? covale2 covale ? ? A ASN 63 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 63 A NAG 1505 1_555 ? ? ? ? ? ? ? 1.430 ? covale3 covale ? ? A ASN 133 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 133 A NAG 1506 1_555 ? ? ? ? ? ? ? 1.446 ? covale4 covale ? ? A ASN 165 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 165 A NAG 1507 1_555 ? ? ? ? ? ? ? 1.435 ? covale5 covale ? ? A ASN 246 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 246 A NAG 1511 1_555 ? ? ? ? ? ? ? 1.455 ? covale6 covale ? ? A ASN 285 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 285 A NAG 1510 1_555 ? ? ? ? ? ? ? 1.438 ? covale7 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 1507 A NAG 1508 1_555 ? ? ? ? ? ? ? 1.438 ? covale8 covale ? ? G MAN . C1 ? ? ? 1_555 F NAG . O4 ? ? A MAN 1509 A NAG 1508 1_555 ? ? ? ? ? ? ? 1.452 ? covale9 covale ? ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? A NAG 1511 A NAG 1512 1_555 ? ? ? ? ? ? ? 1.448 ? covale10 covale ? ? N GAL . O6 ? ? ? 1_555 M SIA . C2 ? ? A GAL 1516 A SIA 1515 1_555 ? ? ? ? ? ? ? 1.428 ? covale11 covale ? ? N GAL . C1 ? ? ? 1_555 O NAG . O4 ? ? A GAL 1516 A NAG 1517 1_555 ? ? ? ? ? ? ? 1.432 ? # 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 2.37 # 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 ? 2 ? AK ? 4 ? AL ? 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 AK 1 2 ? anti-parallel AK 2 3 ? anti-parallel AK 3 4 ? anti-parallel AL 1 2 ? anti-parallel AL 2 3 ? anti-parallel AL 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 VAL A 130 ? THR A 131 ? VAL A 130 THR A 131 AI 2 THR A 155 ? HIS A 156 ? THR A 155 HIS A 156 AJ 1 SER A 136 ? ARG A 141 ? SER A 136 ARG A 141 AJ 2 ASN A 144 ? SER A 146 ? ASN A 144 SER A 146 AK 1 LEU A 164 ? PRO A 169 ? LEU A 164 PRO A 169 AK 2 ILE A 242 ? SER A 247 ? ILE A 242 SER A 247 AK 3 ILE A 202 ? SER A 205 ? ILE A 202 SER A 205 AK 4 GLN A 210 ? VAL A 213 ? GLN A 210 VAL A 213 AL 1 GLY A 286 ? ILE A 288 ? GLY A 286 ILE A 288 AL 2 CYS A 281 ? THR A 283 ? CYS A 281 THR A 283 AL 3 TYR A 302 ? CYS A 305 ? TYR A 302 CYS A 305 AL 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 THR A 131 ? N THR A 131 O THR A 155 ? O THR A 155 AJ 1 2 N ARG A 141 ? N ARG A 141 O ASN A 144 ? O ASN A 144 AK 1 2 N MET A 168 ? N MET A 168 O LEU A 243 ? O LEU A 243 AK 2 3 N ASN A 246 ? N ASN A 246 O THR A 203 ? O THR A 203 AK 3 4 N VAL A 204 ? N VAL A 204 O GLN A 211 ? O GLN A 211 AL 1 2 N ILE A 288 ? N ILE A 288 O CYS A 281 ? O CYS A 281 AL 2 3 N ILE A 282 ? N ILE A 282 O TYR A 302 ? O TYR A 302 AL 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 ? ? ? ? 9 'BINDING SITE FOR RESIDUE EPE A 1513' AC2 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE EPE A 1514' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE TAM A 1518' AC4 Software ? ? ? ? 5 'BINDING SITE FOR MONO-SACCHARIDE NAG A1504 BOUND TO ASN A 38' AC5 Software ? ? ? ? 5 'BINDING SITE FOR MONO-SACCHARIDE NAG A1505 BOUND TO ASN A 63' AC6 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A1506 BOUND TO ASN A 133' AC7 Software ? ? ? ? 11 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 165 RESIDUES 1507 TO 1509' AC8 Software ? ? ? ? 12 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 246 RESIDUES 1511 TO 1512' AC9 Software ? ? ? ? 6 'BINDING SITE FOR MONO-SACCHARIDE NAG A1510 BOUND TO ASN A 285' BC1 Software ? ? ? ? 17 'BINDING SITE FOR CHAIN A OF POLYSACCHARIDE RESIDUES 1515 TO 1517' # 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 9 ASP A 77 ? ASP A 77 . ? 1_555 ? 2 AC1 9 GLN A 80 ? GLN A 80 . ? 1_555 ? 3 AC1 9 SER A 146 ? SER A 146 . ? 1_555 ? 4 AC1 9 PHE A 147 ? PHE A 147 . ? 1_555 ? 5 AC1 9 PHE A 148 ? PHE A 148 . ? 1_555 ? 6 AC1 9 LEU A 151 ? LEU A 151 . ? 1_555 ? 7 AC1 9 ARG A 255 ? ARG A 255 . ? 1_555 ? 8 AC1 9 HOH Q . ? HOH A 2113 . ? 1_555 ? 9 AC1 9 HOH Q . ? HOH A 2178 . ? 1_555 ? 10 AC2 9 ASN A 81 ? ASN A 81 . ? 1_555 ? 11 AC2 9 GLU A 119 ? GLU A 119 . ? 1_555 ? 12 AC2 9 PHE A 120 ? PHE A 120 . ? 1_555 ? 13 AC2 9 ASN A 121 ? ASN A 121 . ? 1_555 ? 14 AC2 9 ASN A 122 ? ASN A 122 . ? 1_555 ? 15 AC2 9 GLU A 280 ? GLU A 280 . ? 10_455 ? 16 AC2 9 GLU A 390 ? GLU A 390 . ? 10_455 ? 17 AC2 9 HOH Q . ? HOH A 2115 . ? 1_555 ? 18 AC2 9 HOH Q . ? HOH A 2387 . ? 10_455 ? 19 AC3 3 TYR A 423 ? TYR A 423 . ? 2_565 ? 20 AC3 3 HOH Q . ? HOH A 2382 . ? 1_555 ? 21 AC3 3 HOH Q . ? HOH A 2528 . ? 1_555 ? 22 AC4 5 ASN A 38 ? ASN A 38 . ? 1_555 ? 23 AC4 5 THR A 318 ? THR A 318 . ? 1_555 ? 24 AC4 5 LEU A 381 ? LEU A 381 . ? 1_555 ? 25 AC4 5 HOH Q . ? HOH A 2022 . ? 1_555 ? 26 AC4 5 HOH Q . ? HOH A 2046 . ? 1_555 ? 27 AC5 5 ASN A 63 ? ASN A 63 . ? 1_555 ? 28 AC5 5 TYR A 94 ? TYR A 94 . ? 1_555 ? 29 AC5 5 HOH Q . ? HOH A 2097 . ? 1_555 ? 30 AC5 5 HOH Q . ? HOH A 2108 . ? 1_555 ? 31 AC5 5 HOH Q . ? HOH A 2516 . ? 1_555 ? 32 AC6 2 ASN A 133 ? ASN A 133 . ? 1_555 ? 33 AC6 2 HOH Q . ? HOH A 2177 . ? 1_555 ? 34 AC7 11 ASN A 165 ? ASN A 165 . ? 1_555 ? 35 AC7 11 SER A 219 ? SER A 219 . ? 2_565 ? 36 AC7 11 PRO A 221 ? PRO A 221 . ? 2_565 ? 37 AC7 11 ARG A 222 ? ARG A 222 . ? 2_565 ? 38 AC7 11 ASP A 225 ? ASP A 225 . ? 2_565 ? 39 AC7 11 NAG I . ? NAG A 1511 . ? 1_555 ? 40 AC7 11 HOH Q . ? HOH A 2206 . ? 1_555 ? 41 AC7 11 HOH Q . ? HOH A 2256 . ? 2_565 ? 42 AC7 11 HOH Q . ? HOH A 2517 . ? 1_555 ? 43 AC7 11 HOH Q . ? HOH A 2518 . ? 1_555 ? 44 AC7 11 HOH Q . ? HOH A 2519 . ? 1_555 ? 45 AC8 12 ALA A 163 ? ALA A 163 . ? 1_555 ? 46 AC8 12 LEU A 164 ? LEU A 164 . ? 1_555 ? 47 AC8 12 ASN A 165 ? ASN A 165 . ? 1_555 ? 48 AC8 12 ARG A 201 ? ARG A 201 . ? 1_555 ? 49 AC8 12 ASN A 246 ? ASN A 246 . ? 1_555 ? 50 AC8 12 SER A 247 ? SER A 247 . ? 1_555 ? 51 AC8 12 THR A 248 ? THR A 248 . ? 1_555 ? 52 AC8 12 NAG E . ? NAG A 1507 . ? 1_555 ? 53 AC8 12 HOH Q . ? HOH A 2232 . ? 1_555 ? 54 AC8 12 HOH Q . ? HOH A 2522 . ? 1_555 ? 55 AC8 12 HOH Q . ? HOH A 2523 . ? 1_555 ? 56 AC8 12 HOH Q . ? HOH A 2524 . ? 1_555 ? 57 AC9 6 SER A 45 ? SER A 45 . ? 1_555 ? 58 AC9 6 ASN A 285 ? ASN A 285 . ? 1_555 ? 59 AC9 6 VAL A 297 ? VAL A 297 . ? 1_555 ? 60 AC9 6 HOH Q . ? HOH A 2061 . ? 1_555 ? 61 AC9 6 HOH Q . ? HOH A 2302 . ? 1_555 ? 62 AC9 6 HOH Q . ? HOH A 2313 . ? 1_555 ? 63 BC1 17 TYR A 98 ? TYR A 98 . ? 1_555 ? 64 BC1 17 GLY A 134 ? GLY A 134 . ? 1_555 ? 65 BC1 17 THR A 135 ? THR A 135 . ? 1_555 ? 66 BC1 17 SER A 136 ? SER A 136 . ? 1_555 ? 67 BC1 17 SER A 137 ? SER A 137 . ? 1_555 ? 68 BC1 17 TRP A 153 ? TRP A 153 . ? 1_555 ? 69 BC1 17 LEU A 194 ? LEU A 194 . ? 1_555 ? 70 BC1 17 ARG A 222 ? ARG A 222 . ? 1_555 ? 71 BC1 17 ASP A 225 ? ASP A 225 . ? 1_555 ? 72 BC1 17 ILE A 226 ? ILE A 226 . ? 1_555 ? 73 BC1 17 SER A 228 ? SER A 228 . ? 1_555 ? 74 BC1 17 HOH Q . ? HOH A 2179 . ? 1_555 ? 75 BC1 17 HOH Q . ? HOH A 2184 . ? 1_555 ? 76 BC1 17 HOH Q . ? HOH A 2223 . ? 1_555 ? 77 BC1 17 HOH Q . ? HOH A 2525 . ? 1_555 ? 78 BC1 17 HOH Q . ? HOH A 2526 . ? 1_555 ? 79 BC1 17 HOH Q . ? HOH A 2527 . ? 1_555 ? # _database_PDB_matrix.entry_id 2YP3 _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 2YP3 _atom_sites.fract_transf_matrix[1][1] 0.009888 _atom_sites.fract_transf_matrix[1][2] 0.005709 _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] 0.011418 _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] 0.002578 _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 ? -53.147 7.789 -10.992 1.00 65.22 ? 8 ASN A N 1 ATOM 2 C CA . ASN A 1 8 ? -53.482 8.207 -12.384 1.00 63.44 ? 8 ASN A CA 1 ATOM 3 C C . ASN A 1 8 ? -52.942 9.616 -12.661 1.00 59.10 ? 8 ASN A C 1 ATOM 4 O O . ASN A 1 8 ? -53.706 10.581 -12.774 1.00 60.80 ? 8 ASN A O 1 ATOM 5 C CB . ASN A 1 8 ? -54.998 8.147 -12.605 1.00 66.41 ? 8 ASN A CB 1 ATOM 6 C CG . ASN A 1 8 ? -55.375 8.101 -14.077 1.00 69.61 ? 8 ASN A CG 1 ATOM 7 O OD1 . ASN A 1 8 ? -55.878 9.080 -14.631 1.00 72.04 ? 8 ASN A OD1 1 ATOM 8 N ND2 . ASN A 1 8 ? -55.132 6.960 -14.719 1.00 71.37 ? 8 ASN A ND2 1 ATOM 9 N N . SER A 1 9 ? -51.614 9.716 -12.754 1.00 52.08 ? 9 SER A N 1 ATOM 10 C CA . SER A 1 9 ? -50.906 10.994 -12.946 1.00 46.43 ? 9 SER A CA 1 ATOM 11 C C . SER A 1 9 ? -50.848 11.861 -11.680 1.00 40.50 ? 9 SER A C 1 ATOM 12 O O . SER A 1 9 ? -50.287 12.949 -11.713 1.00 37.25 ? 9 SER A O 1 ATOM 13 C CB . SER A 1 9 ? -51.514 11.792 -14.110 1.00 47.82 ? 9 SER A CB 1 ATOM 14 O OG . SER A 1 9 ? -52.633 12.559 -13.694 1.00 48.85 ? 9 SER A OG 1 ATOM 15 N N . THR A 1 10 ? -51.424 11.384 -10.575 1.00 36.92 ? 10 THR A N 1 ATOM 16 C CA . THR A 1 10 ? -51.352 12.081 -9.292 1.00 34.19 ? 10 THR A CA 1 ATOM 17 C C . THR A 1 10 ? -51.168 11.092 -8.155 1.00 32.00 ? 10 THR A C 1 ATOM 18 O O . THR A 1 10 ? -51.235 9.880 -8.341 1.00 31.95 ? 10 THR A O 1 ATOM 19 C CB . THR A 1 10 ? -52.625 12.888 -8.991 1.00 34.88 ? 10 THR A CB 1 ATOM 20 O OG1 . THR A 1 10 ? -53.743 12.000 -8.992 1.00 37.59 ? 10 THR A OG1 1 ATOM 21 C CG2 . THR A 1 10 ? -52.833 13.980 -10.013 1.00 37.00 ? 10 THR A CG2 1 ATOM 22 N N . ALA A 1 11 ? -50.930 11.639 -6.970 1.00 28.25 ? 11 ALA A N 1 ATOM 23 C CA . ALA A 1 11 ? -50.825 10.869 -5.768 1.00 27.29 ? 11 ALA A CA 1 ATOM 24 C C . ALA A 1 11 ? -51.482 11.668 -4.646 1.00 25.79 ? 11 ALA A C 1 ATOM 25 O O . ALA A 1 11 ? -51.706 12.870 -4.771 1.00 24.91 ? 11 ALA A O 1 ATOM 26 C CB . ALA A 1 11 ? -49.353 10.599 -5.435 1.00 26.65 ? 11 ALA A CB 1 ATOM 27 N N . THR A 1 12 ? -51.788 10.976 -3.563 1.00 25.08 ? 12 THR A N 1 ATOM 28 C CA . THR A 1 12 ? -52.289 11.605 -2.331 1.00 24.45 ? 12 THR A CA 1 ATOM 29 C C . THR A 1 12 ? -51.338 11.295 -1.211 1.00 23.59 ? 12 THR A C 1 ATOM 30 O O . THR A 1 12 ? -50.910 10.151 -1.073 1.00 24.38 ? 12 THR A O 1 ATOM 31 C CB . THR A 1 12 ? -53.694 11.072 -1.991 1.00 24.83 ? 12 THR A CB 1 ATOM 32 O OG1 . THR A 1 12 ? -54.538 11.303 -3.115 1.00 25.87 ? 12 THR A OG1 1 ATOM 33 C CG2 . THR A 1 12 ? -54.315 11.769 -0.747 1.00 24.71 ? 12 THR A CG2 1 ATOM 34 N N . LEU A 1 13 ? -50.986 12.316 -0.424 1.00 22.45 ? 13 LEU A N 1 ATOM 35 C CA . LEU A 1 13 ? -50.182 12.147 0.771 1.00 22.50 ? 13 LEU A CA 1 ATOM 36 C C . LEU A 1 13 ? -50.907 12.790 1.970 1.00 23.40 ? 13 LEU A C 1 ATOM 37 O O . LEU A 1 13 ? -51.108 14.011 2.004 1.00 23.02 ? 13 LEU A O 1 ATOM 38 C CB . LEU A 1 13 ? -48.787 12.752 0.590 1.00 21.65 ? 13 LEU A CB 1 ATOM 39 C CG . LEU A 1 13 ? -47.798 12.615 1.760 1.00 21.39 ? 13 LEU A CG 1 ATOM 40 C CD1 . LEU A 1 13 ? -47.458 11.149 2.030 1.00 22.01 ? 13 LEU A CD1 1 ATOM 41 C CD2 . LEU A 1 13 ? -46.524 13.425 1.538 1.00 21.16 ? 13 LEU A CD2 1 ATOM 42 N N . CYS A 1 14 ? -51.293 11.948 2.931 1.00 24.45 ? 14 CYS A N 1 ATOM 43 C CA . CYS A 1 14 ? -52.000 12.366 4.142 1.00 24.88 ? 14 CYS A CA 1 ATOM 44 C C . CYS A 1 14 ? -51.064 12.350 5.337 1.00 24.27 ? 14 CYS A C 1 ATOM 45 O O . CYS A 1 14 ? -50.227 11.441 5.485 1.00 23.01 ? 14 CYS A O 1 ATOM 46 C CB . CYS A 1 14 ? -53.183 11.423 4.413 1.00 26.33 ? 14 CYS A CB 1 ATOM 47 S SG . CYS A 1 14 ? -54.443 11.431 3.118 1.00 28.93 ? 14 CYS A SG 1 ATOM 48 N N . LEU A 1 15 ? -51.191 13.380 6.186 1.00 23.77 ? 15 LEU A N 1 ATOM 49 C CA . LEU A 1 15 ? -50.526 13.417 7.470 1.00 23.34 ? 15 LEU A CA 1 ATOM 50 C C . LEU A 1 15 ? -51.529 13.094 8.567 1.00 23.04 ? 15 LEU A C 1 ATOM 51 O O . LEU A 1 15 ? -52.687 13.527 8.503 1.00 23.50 ? 15 LEU A O 1 ATOM 52 C CB . LEU A 1 15 ? -49.890 14.791 7.703 1.00 24.97 ? 15 LEU A CB 1 ATOM 53 C CG . LEU A 1 15 ? -48.600 14.890 6.882 1.00 26.26 ? 15 LEU A CG 1 ATOM 54 C CD1 . LEU A 1 15 ? -48.927 15.246 5.431 1.00 28.11 ? 15 LEU A CD1 1 ATOM 55 C CD2 . LEU A 1 15 ? -47.630 15.864 7.464 1.00 30.37 ? 15 LEU A CD2 1 ATOM 56 N N . GLY A 1 16 ? -51.082 12.357 9.576 1.00 21.76 ? 16 GLY A N 1 ATOM 57 C CA . GLY A 1 16 ? -51.976 11.865 10.617 1.00 21.99 ? 16 GLY A CA 1 ATOM 58 C C . GLY A 1 16 ? -51.265 11.543 11.912 1.00 21.85 ? 16 GLY A C 1 ATOM 59 O O . GLY A 1 16 ? -50.036 11.615 12.004 1.00 20.00 ? 16 GLY A O 1 ATOM 60 N N . HIS A 1 17 ? -52.061 11.139 12.896 1.00 21.50 ? 17 HIS A N 1 ATOM 61 C CA . HIS A 1 17 ? -51.565 10.748 14.193 1.00 21.69 ? 17 HIS A CA 1 ATOM 62 C C . HIS A 1 17 ? -52.339 9.582 14.706 1.00 21.97 ? 17 HIS A C 1 ATOM 63 O O . HIS A 1 17 ? -53.466 9.337 14.271 1.00 23.44 ? 17 HIS A O 1 ATOM 64 C CB . HIS A 1 17 ? -51.663 11.938 15.163 1.00 21.25 ? 17 HIS A CB 1 ATOM 65 C CG . HIS A 1 17 ? -53.079 12.419 15.385 1.00 21.75 ? 17 HIS A CG 1 ATOM 66 N ND1 . HIS A 1 17 ? -53.993 11.699 16.073 1.00 21.19 ? 17 HIS A ND1 1 ATOM 67 C CD2 . HIS A 1 17 ? -53.724 13.583 14.981 1.00 21.92 ? 17 HIS A CD2 1 ATOM 68 C CE1 . HIS A 1 17 ? -55.165 12.363 16.078 1.00 21.83 ? 17 HIS A CE1 1 ATOM 69 N NE2 . HIS A 1 17 ? -54.996 13.514 15.422 1.00 22.14 ? 17 HIS A NE2 1 ATOM 70 N N . HIS A 1 18 ? -51.744 8.840 15.635 1.00 22.37 ? 18 HIS A N 1 ATOM 71 C CA . HIS A 1 18 ? -52.370 7.650 16.174 1.00 23.31 ? 18 HIS A CA 1 ATOM 72 C C . HIS A 1 18 ? -53.580 7.948 17.008 1.00 24.21 ? 18 HIS A C 1 ATOM 73 O O . HIS A 1 18 ? -53.882 9.099 17.334 1.00 23.29 ? 18 HIS A O 1 ATOM 74 C CB . HIS A 1 18 ? -51.361 6.768 16.927 1.00 23.34 ? 18 HIS A CB 1 ATOM 75 C CG . HIS A 1 18 ? -50.974 7.288 18.297 1.00 23.25 ? 18 HIS A CG 1 ATOM 76 N ND1 . HIS A 1 18 ? -50.420 6.499 19.239 1.00 24.26 ? 18 HIS A ND1 1 ATOM 77 C CD2 . HIS A 1 18 ? -51.111 8.557 18.871 1.00 22.93 ? 18 HIS A CD2 1 ATOM 78 C CE1 . HIS A 1 18 ? -50.200 7.231 20.361 1.00 24.39 ? 18 HIS A CE1 1 ATOM 79 N NE2 . HIS A 1 18 ? -50.623 8.492 20.129 1.00 22.35 ? 18 HIS A NE2 1 ATOM 80 N N . ALA A 1 19 ? -54.298 6.883 17.317 1.00 25.33 ? 19 ALA A N 1 ATOM 81 C CA . ALA A 1 19 ? -55.457 6.892 18.182 1.00 27.09 ? 19 ALA A CA 1 ATOM 82 C C . ALA A 1 19 ? -55.529 5.487 18.790 1.00 29.12 ? 19 ALA A C 1 ATOM 83 O O . ALA A 1 19 ? -54.997 4.534 18.218 1.00 31.22 ? 19 ALA A O 1 ATOM 84 C CB . ALA A 1 19 ? -56.725 7.213 17.399 1.00 26.91 ? 19 ALA A CB 1 ATOM 85 N N . VAL A 1 20 ? -56.145 5.362 19.956 1.00 30.65 ? 20 VAL A N 1 ATOM 86 C CA . VAL A 1 20 ? -56.180 4.085 20.662 1.00 32.19 ? 20 VAL A CA 1 ATOM 87 C C . VAL A 1 20 ? -57.620 3.737 20.959 1.00 34.49 ? 20 VAL A C 1 ATOM 88 O O . VAL A 1 20 ? -58.479 4.621 20.988 1.00 34.88 ? 20 VAL A O 1 ATOM 89 C CB . VAL A 1 20 ? -55.346 4.104 21.956 1.00 32.35 ? 20 VAL A CB 1 ATOM 90 C CG1 . VAL A 1 20 ? -53.882 4.399 21.631 1.00 32.05 ? 20 VAL A CG1 1 ATOM 91 C CG2 . VAL A 1 20 ? -55.921 5.097 22.960 1.00 30.39 ? 20 VAL A CG2 1 ATOM 92 N N . PRO A 1 21 ? -57.911 2.435 21.123 1.00 38.28 ? 21 PRO A N 1 ATOM 93 C CA . PRO A 1 21 ? -59.298 2.094 21.397 1.00 40.16 ? 21 PRO A CA 1 ATOM 94 C C . PRO A 1 21 ? -59.716 2.431 22.836 1.00 41.58 ? 21 PRO A C 1 ATOM 95 O O . PRO A 1 21 ? -60.890 2.692 23.068 1.00 45.67 ? 21 PRO A O 1 ATOM 96 C CB . PRO A 1 21 ? -59.349 0.581 21.131 1.00 40.26 ? 21 PRO A CB 1 ATOM 97 C CG . PRO A 1 21 ? -57.962 0.099 21.392 1.00 40.32 ? 21 PRO A CG 1 ATOM 98 C CD . PRO A 1 21 ? -57.052 1.241 20.994 1.00 38.90 ? 21 PRO A CD 1 ATOM 99 N N . ASN A 1 22 ? -58.766 2.445 23.774 1.00 40.84 ? 22 ASN A N 1 ATOM 100 C CA . ASN A 1 22 ? -59.075 2.654 25.199 1.00 42.02 ? 22 ASN A CA 1 ATOM 101 C C . ASN A 1 22 ? -58.446 3.937 25.771 1.00 38.09 ? 22 ASN A C 1 ATOM 102 O O . ASN A 1 22 ? -57.492 3.871 26.551 1.00 37.87 ? 22 ASN A O 1 ATOM 103 C CB . ASN A 1 22 ? -58.607 1.446 26.024 1.00 44.50 ? 22 ASN A CB 1 ATOM 104 C CG . ASN A 1 22 ? -57.113 1.177 25.868 1.00 48.65 ? 22 ASN A CG 1 ATOM 105 O OD1 . ASN A 1 22 ? -56.500 1.553 24.846 1.00 51.98 ? 22 ASN A OD1 1 ATOM 106 N ND2 . ASN A 1 22 ? -56.515 0.532 26.872 1.00 49.23 ? 22 ASN A ND2 1 ATOM 107 N N . GLY A 1 23 ? -58.995 5.092 25.408 1.00 35.85 ? 23 GLY A N 1 ATOM 108 C CA . GLY A 1 23 ? -58.449 6.381 25.881 1.00 34.99 ? 23 GLY A CA 1 ATOM 109 C C . GLY A 1 23 ? -58.863 6.684 27.316 1.00 34.07 ? 23 GLY A C 1 ATOM 110 O O . GLY A 1 23 ? -59.689 5.960 27.885 1.00 32.91 ? 23 GLY A O 1 ATOM 111 N N . THR A 1 24 ? -58.308 7.753 27.894 1.00 31.00 ? 24 THR A N 1 ATOM 112 C CA . THR A 1 24 ? -58.615 8.162 29.284 1.00 30.70 ? 24 THR A CA 1 ATOM 113 C C . THR A 1 24 ? -59.013 9.631 29.344 1.00 27.06 ? 24 THR A C 1 ATOM 114 O O . THR A 1 24 ? -58.450 10.447 28.624 1.00 25.97 ? 24 THR A O 1 ATOM 115 C CB . THR A 1 24 ? -57.402 8.003 30.227 1.00 33.13 ? 24 THR A CB 1 ATOM 116 O OG1 . THR A 1 24 ? -56.765 6.744 30.013 1.00 36.88 ? 24 THR A OG1 1 ATOM 117 C CG2 . THR A 1 24 ? -57.834 8.076 31.677 1.00 34.12 ? 24 THR A CG2 1 ATOM 118 N N . ILE A 1 25 ? -59.950 9.962 30.219 1.00 24.27 ? 25 ILE A N 1 ATOM 119 C CA . ILE A 1 25 ? -60.473 11.320 30.317 1.00 24.58 ? 25 ILE A CA 1 ATOM 120 C C . ILE A 1 25 ? -59.625 12.141 31.280 1.00 22.02 ? 25 ILE A C 1 ATOM 121 O O . ILE A 1 25 ? -59.324 11.684 32.382 1.00 21.34 ? 25 ILE A O 1 ATOM 122 C CB . ILE A 1 25 ? -61.936 11.327 30.798 1.00 25.79 ? 25 ILE A CB 1 ATOM 123 C CG1 . ILE A 1 25 ? -62.828 10.587 29.801 1.00 27.95 ? 25 ILE A CG1 1 ATOM 124 C CG2 . ILE A 1 25 ? -62.420 12.762 31.010 1.00 25.62 ? 25 ILE A CG2 1 ATOM 125 C CD1 . ILE A 1 25 ? -62.882 11.212 28.429 1.00 29.70 ? 25 ILE A CD1 1 ATOM 126 N N . VAL A 1 26 ? -59.219 13.337 30.848 1.00 21.38 ? 26 VAL A N 1 ATOM 127 C CA . VAL A 1 26 ? -58.479 14.272 31.713 1.00 20.00 ? 26 VAL A CA 1 ATOM 128 C C . VAL A 1 26 ? -59.095 15.657 31.635 1.00 20.18 ? 26 VAL A C 1 ATOM 129 O O . VAL A 1 26 ? -59.962 15.914 30.774 1.00 19.99 ? 26 VAL A O 1 ATOM 130 C CB . VAL A 1 26 ? -56.976 14.359 31.351 1.00 18.73 ? 26 VAL A CB 1 ATOM 131 C CG1 . VAL A 1 26 ? -56.324 12.981 31.437 1.00 18.38 ? 26 VAL A CG1 1 ATOM 132 C CG2 . VAL A 1 26 ? -56.784 14.997 29.964 1.00 17.82 ? 26 VAL A CG2 1 ATOM 133 N N . LYS A 1 27 ? -58.641 16.540 32.529 1.00 20.73 ? 27 LYS A N 1 ATOM 134 C CA . LYS A 1 27 ? -59.091 17.922 32.575 1.00 21.93 ? 27 LYS A CA 1 ATOM 135 C C . LYS A 1 27 ? -57.981 18.862 32.091 1.00 21.35 ? 27 LYS A C 1 ATOM 136 O O . LYS A 1 27 ? -56.835 18.703 32.460 1.00 19.30 ? 27 LYS A O 1 ATOM 137 C CB . LYS A 1 27 ? -59.500 18.290 33.997 1.00 24.53 ? 27 LYS A CB 1 ATOM 138 C CG . LYS A 1 27 ? -59.904 19.745 34.195 1.00 27.61 ? 27 LYS A CG 1 ATOM 139 C CD . LYS A 1 27 ? -60.360 20.003 35.632 1.00 30.65 ? 27 LYS A CD 1 ATOM 140 C CE . LYS A 1 27 ? -60.308 21.490 35.995 1.00 32.92 ? 27 LYS A CE 1 ATOM 141 N NZ . LYS A 1 27 ? -60.865 21.730 37.362 1.00 34.70 ? 27 LYS A NZ 1 ATOM 142 N N . THR A 1 28 ? -58.345 19.826 31.258 1.00 21.36 ? 28 THR A N 1 ATOM 143 C CA . THR A 1 28 ? -57.433 20.886 30.847 1.00 22.33 ? 28 THR A CA 1 ATOM 144 C C . THR A 1 28 ? -58.063 22.234 31.214 1.00 23.89 ? 28 THR A C 1 ATOM 145 O O . THR A 1 28 ? -59.107 22.292 31.858 1.00 25.11 ? 28 THR A O 1 ATOM 146 C CB . THR A 1 28 ? -57.152 20.837 29.336 1.00 22.00 ? 28 THR A CB 1 ATOM 147 O OG1 . THR A 1 28 ? -58.363 21.105 28.620 1.00 23.64 ? 28 THR A OG1 1 ATOM 148 C CG2 . THR A 1 28 ? -56.622 19.479 28.913 1.00 22.21 ? 28 THR A CG2 1 ATOM 149 N N . ILE A 1 29 ? -57.414 23.320 30.822 1.00 24.79 ? 29 ILE A N 1 ATOM 150 C CA . ILE A 1 29 ? -58.001 24.644 30.965 1.00 26.42 ? 29 ILE A CA 1 ATOM 151 C C . ILE A 1 29 ? -59.155 24.819 29.976 1.00 26.93 ? 29 ILE A C 1 ATOM 152 O O . ILE A 1 29 ? -60.150 25.415 30.313 1.00 29.44 ? 29 ILE A O 1 ATOM 153 C CB . ILE A 1 29 ? -56.972 25.766 30.727 1.00 27.36 ? 29 ILE A CB 1 ATOM 154 C CG1 . ILE A 1 29 ? -55.787 25.596 31.672 1.00 28.67 ? 29 ILE A CG1 1 ATOM 155 C CG2 . ILE A 1 29 ? -57.644 27.125 30.914 1.00 28.88 ? 29 ILE A CG2 1 ATOM 156 C CD1 . ILE A 1 29 ? -56.143 25.842 33.131 1.00 30.97 ? 29 ILE A CD1 1 ATOM 157 N N . THR A 1 30 ? -59.026 24.278 28.769 1.00 27.64 ? 30 THR A N 1 ATOM 158 C CA . THR A 1 30 ? -60.054 24.407 27.731 1.00 28.70 ? 30 THR A CA 1 ATOM 159 C C . THR A 1 30 ? -61.264 23.487 27.962 1.00 30.64 ? 30 THR A C 1 ATOM 160 O O . THR A 1 30 ? -62.392 23.871 27.683 1.00 29.19 ? 30 THR A O 1 ATOM 161 C CB . THR A 1 30 ? -59.451 24.079 26.358 1.00 28.60 ? 30 THR A CB 1 ATOM 162 O OG1 . THR A 1 30 ? -58.349 24.951 26.117 1.00 27.12 ? 30 THR A OG1 1 ATOM 163 C CG2 . THR A 1 30 ? -60.496 24.217 25.190 1.00 30.17 ? 30 THR A CG2 1 ATOM 164 N N . ASN A 1 31 ? -61.027 22.276 28.471 1.00 30.41 ? 31 ASN A N 1 ATOM 165 C CA . ASN A 1 31 ? -62.081 21.246 28.585 1.00 31.55 ? 31 ASN A CA 1 ATOM 166 C C . ASN A 1 31 ? -62.098 20.624 29.979 1.00 30.81 ? 31 ASN A C 1 ATOM 167 O O . ASN A 1 31 ? -61.070 20.149 30.435 1.00 28.67 ? 31 ASN A O 1 ATOM 168 C CB . ASN A 1 31 ? -61.802 20.123 27.589 1.00 33.61 ? 31 ASN A CB 1 ATOM 169 C CG . ASN A 1 31 ? -62.066 20.515 26.158 1.00 35.59 ? 31 ASN A CG 1 ATOM 170 O OD1 . ASN A 1 31 ? -63.215 20.731 25.768 1.00 40.04 ? 31 ASN A OD1 1 ATOM 171 N ND2 . ASN A 1 31 ? -61.006 20.585 25.354 1.00 34.60 ? 31 ASN A ND2 1 ATOM 172 N N . ASP A 1 32 ? -63.259 20.573 30.626 1.00 31.05 ? 32 ASP A N 1 ATOM 173 C CA . ASP A 1 32 ? -63.417 19.807 31.856 1.00 32.05 ? 32 ASP A CA 1 ATOM 174 C C . ASP A 1 32 ? -63.171 18.320 31.651 1.00 29.93 ? 32 ASP A C 1 ATOM 175 O O . ASP A 1 32 ? -62.686 17.649 32.550 1.00 27.99 ? 32 ASP A O 1 ATOM 176 C CB . ASP A 1 32 ? -64.804 20.018 32.456 1.00 37.05 ? 32 ASP A CB 1 ATOM 177 C CG . ASP A 1 32 ? -64.961 21.399 33.073 1.00 42.50 ? 32 ASP A CG 1 ATOM 178 O OD1 . ASP A 1 32 ? -63.938 21.981 33.516 1.00 46.62 ? 32 ASP A OD1 1 ATOM 179 O OD2 . ASP A 1 32 ? -66.102 21.906 33.122 1.00 48.40 ? 32 ASP A OD2 1 ATOM 180 N N . GLN A 1 33 ? -63.488 17.825 30.462 1.00 28.48 ? 33 GLN A N 1 ATOM 181 C CA . GLN A 1 33 ? -63.287 16.428 30.109 1.00 29.23 ? 33 GLN A CA 1 ATOM 182 C C . GLN A 1 33 ? -62.799 16.362 28.680 1.00 27.67 ? 33 GLN A C 1 ATOM 183 O O . GLN A 1 33 ? -63.493 16.817 27.763 1.00 29.14 ? 33 GLN A O 1 ATOM 184 C CB . GLN A 1 33 ? -64.608 15.638 30.251 1.00 32.45 ? 33 GLN A CB 1 ATOM 185 C CG . GLN A 1 33 ? -64.971 15.337 31.702 1.00 35.51 ? 33 GLN A CG 1 ATOM 186 C CD . GLN A 1 33 ? -66.193 14.445 31.874 1.00 39.69 ? 33 GLN A CD 1 ATOM 187 O OE1 . GLN A 1 33 ? -66.836 14.032 30.907 1.00 43.45 ? 33 GLN A OE1 1 ATOM 188 N NE2 . GLN A 1 33 ? -66.515 14.143 33.117 1.00 43.68 ? 33 GLN A NE2 1 ATOM 189 N N . ILE A 1 34 ? -61.606 15.822 28.476 1.00 24.57 ? 34 ILE A N 1 ATOM 190 C CA . ILE A 1 34 ? -61.113 15.568 27.129 1.00 24.04 ? 34 ILE A CA 1 ATOM 191 C C . ILE A 1 34 ? -60.408 14.237 27.138 1.00 22.87 ? 34 ILE A C 1 ATOM 192 O O . ILE A 1 34 ? -59.643 13.946 28.048 1.00 21.14 ? 34 ILE A O 1 ATOM 193 C CB . ILE A 1 34 ? -60.180 16.683 26.585 1.00 23.89 ? 34 ILE A CB 1 ATOM 194 C CG1 . ILE A 1 34 ? -59.735 16.363 25.158 1.00 25.25 ? 34 ILE A CG1 1 ATOM 195 C CG2 . ILE A 1 34 ? -58.948 16.873 27.442 1.00 23.69 ? 34 ILE A CG2 1 ATOM 196 C CD1 . ILE A 1 34 ? -59.086 17.536 24.459 1.00 25.56 ? 34 ILE A CD1 1 ATOM 197 N N . GLU A 1 35 ? -60.703 13.413 26.136 1.00 22.60 ? 35 GLU A N 1 ATOM 198 C CA . GLU A 1 35 ? -60.092 12.116 26.070 1.00 23.13 ? 35 GLU A CA 1 ATOM 199 C C . GLU A 1 35 ? -58.710 12.191 25.409 1.00 21.40 ? 35 GLU A C 1 ATOM 200 O O . GLU A 1 35 ? -58.551 12.745 24.333 1.00 21.61 ? 35 GLU A O 1 ATOM 201 C CB . GLU A 1 35 ? -61.028 11.114 25.370 1.00 25.39 ? 35 GLU A CB 1 ATOM 202 C CG . GLU A 1 35 ? -60.600 9.677 25.533 1.00 27.35 ? 35 GLU A CG 1 ATOM 203 C CD . GLU A 1 35 ? -61.442 8.741 24.677 1.00 30.54 ? 35 GLU A CD 1 ATOM 204 O OE1 . GLU A 1 35 ? -62.679 8.815 24.766 1.00 35.10 ? 35 GLU A OE1 1 ATOM 205 O OE2 . GLU A 1 35 ? -60.862 7.960 23.910 1.00 31.42 ? 35 GLU A OE2 1 ATOM 206 N N . VAL A 1 36 ? -57.729 11.599 26.077 1.00 20.41 ? 36 VAL A N 1 ATOM 207 C CA . VAL A 1 36 ? -56.378 11.461 25.579 1.00 20.34 ? 36 VAL A CA 1 ATOM 208 C C . VAL A 1 36 ? -55.996 9.983 25.471 1.00 20.77 ? 36 VAL A C 1 ATOM 209 O O . VAL A 1 36 ? -56.713 9.117 25.981 1.00 21.74 ? 36 VAL A O 1 ATOM 210 C CB . VAL A 1 36 ? -55.373 12.221 26.482 1.00 19.38 ? 36 VAL A CB 1 ATOM 211 C CG1 . VAL A 1 36 ? -55.631 13.726 26.380 1.00 18.68 ? 36 VAL A CG1 1 ATOM 212 C CG2 . VAL A 1 36 ? -55.425 11.739 27.947 1.00 18.81 ? 36 VAL A CG2 1 ATOM 213 N N . THR A 1 37 ? -54.866 9.700 24.825 1.00 20.94 ? 37 THR A N 1 ATOM 214 C CA . THR A 1 37 ? -54.466 8.321 24.563 1.00 21.81 ? 37 THR A CA 1 ATOM 215 C C . THR A 1 37 ? -54.009 7.607 25.818 1.00 22.63 ? 37 THR A C 1 ATOM 216 O O . THR A 1 37 ? -54.134 6.397 25.912 1.00 21.86 ? 37 THR A O 1 ATOM 217 C CB . THR A 1 37 ? -53.385 8.225 23.482 1.00 21.65 ? 37 THR A CB 1 ATOM 218 O OG1 . THR A 1 37 ? -52.198 8.887 23.926 1.00 21.52 ? 37 THR A OG1 1 ATOM 219 C CG2 . THR A 1 37 ? -53.878 8.868 22.151 1.00 20.55 ? 37 THR A CG2 1 ATOM 220 N N . ASN A 1 38 ? -53.534 8.366 26.808 1.00 22.62 ? 38 ASN A N 1 ATOM 221 C CA . ASN A 1 38 ? -52.999 7.773 28.003 1.00 23.63 ? 38 ASN A CA 1 ATOM 222 C C . ASN A 1 38 ? -52.826 8.857 29.060 1.00 22.21 ? 38 ASN A C 1 ATOM 223 O O . ASN A 1 38 ? -52.702 10.038 28.726 1.00 19.91 ? 38 ASN A O 1 ATOM 224 C CB . ASN A 1 38 ? -51.651 7.146 27.677 1.00 26.36 ? 38 ASN A CB 1 ATOM 225 C CG . ASN A 1 38 ? -51.148 6.220 28.752 1.00 29.59 ? 38 ASN A CG 1 ATOM 226 O OD1 . ASN A 1 38 ? -51.900 5.639 29.517 1.00 30.61 ? 38 ASN A OD1 1 ATOM 227 N ND2 . ASN A 1 38 ? -49.841 6.089 28.797 1.00 38.82 ? 38 ASN A ND2 1 ATOM 228 N N . ALA A 1 39 ? -52.843 8.434 30.313 1.00 21.24 ? 39 ALA A N 1 ATOM 229 C CA . ALA A 1 39 ? -52.669 9.341 31.437 1.00 21.42 ? 39 ALA A CA 1 ATOM 230 C C . ALA A 1 39 ? -52.045 8.574 32.599 1.00 22.11 ? 39 ALA A C 1 ATOM 231 O O . ALA A 1 39 ? -51.997 7.333 32.599 1.00 21.11 ? 39 ALA A O 1 ATOM 232 C CB . ALA A 1 39 ? -54.014 9.940 31.829 1.00 20.82 ? 39 ALA A CB 1 ATOM 233 N N . THR A 1 40 ? -51.537 9.312 33.568 1.00 21.05 ? 40 THR A N 1 ATOM 234 C CA . THR A 1 40 ? -51.011 8.707 34.776 1.00 21.52 ? 40 THR A CA 1 ATOM 235 C C . THR A 1 40 ? -51.545 9.430 36.018 1.00 20.42 ? 40 THR A C 1 ATOM 236 O O . THR A 1 40 ? -51.846 10.621 35.967 1.00 20.01 ? 40 THR A O 1 ATOM 237 C CB . THR A 1 40 ? -49.480 8.632 34.726 1.00 21.78 ? 40 THR A CB 1 ATOM 238 O OG1 . THR A 1 40 ? -49.042 7.685 35.704 1.00 24.31 ? 40 THR A OG1 1 ATOM 239 C CG2 . THR A 1 40 ? -48.832 9.972 34.987 1.00 22.29 ? 40 THR A CG2 1 ATOM 240 N N . GLU A 1 41 ? -51.734 8.673 37.091 1.00 20.27 ? 41 GLU A N 1 ATOM 241 C CA . GLU A 1 41 ? -52.324 9.168 38.328 1.00 20.03 ? 41 GLU A CA 1 ATOM 242 C C . GLU A 1 41 ? -51.278 9.905 39.168 1.00 18.90 ? 41 GLU A C 1 ATOM 243 O O . GLU A 1 41 ? -50.174 9.385 39.408 1.00 18.90 ? 41 GLU A O 1 ATOM 244 C CB . GLU A 1 41 ? -52.906 7.988 39.107 1.00 21.30 ? 41 GLU A CB 1 ATOM 245 C CG . GLU A 1 41 ? -53.534 8.313 40.446 1.00 21.16 ? 41 GLU A CG 1 ATOM 246 C CD . GLU A 1 41 ? -54.630 9.342 40.345 1.00 21.34 ? 41 GLU A CD 1 ATOM 247 O OE1 . GLU A 1 41 ? -55.680 9.013 39.744 1.00 21.99 ? 41 GLU A OE1 1 ATOM 248 O OE2 . GLU A 1 41 ? -54.449 10.491 40.838 1.00 19.21 ? 41 GLU A OE2 1 ATOM 249 N N . LEU A 1 42 ? -51.603 11.121 39.601 1.00 17.23 ? 42 LEU A N 1 ATOM 250 C CA . LEU A 1 42 ? -50.693 11.910 40.443 1.00 16.71 ? 42 LEU A CA 1 ATOM 251 C C . LEU A 1 42 ? -51.052 11.956 41.939 1.00 16.02 ? 42 LEU A C 1 ATOM 252 O O . LEU A 1 42 ? -50.315 12.548 42.716 1.00 15.37 ? 42 LEU A O 1 ATOM 253 C CB . LEU A 1 42 ? -50.600 13.340 39.931 1.00 16.86 ? 42 LEU A CB 1 ATOM 254 C CG . LEU A 1 42 ? -50.008 13.495 38.530 1.00 17.22 ? 42 LEU A CG 1 ATOM 255 C CD1 . LEU A 1 42 ? -49.802 14.960 38.235 1.00 17.14 ? 42 LEU A CD1 1 ATOM 256 C CD2 . LEU A 1 42 ? -48.693 12.736 38.364 1.00 17.18 ? 42 LEU A CD2 1 ATOM 257 N N . VAL A 1 43 ? -52.176 11.367 42.328 1.00 15.82 ? 43 VAL A N 1 ATOM 258 C CA . VAL A 1 43 ? -52.555 11.265 43.740 1.00 16.05 ? 43 VAL A CA 1 ATOM 259 C C . VAL A 1 43 ? -52.427 9.826 44.233 1.00 17.13 ? 43 VAL A C 1 ATOM 260 O O . VAL A 1 43 ? -53.158 8.938 43.774 1.00 16.86 ? 43 VAL A O 1 ATOM 261 C CB . VAL A 1 43 ? -54.000 11.742 43.995 1.00 15.88 ? 43 VAL A CB 1 ATOM 262 C CG1 . VAL A 1 43 ? -54.359 11.633 45.473 1.00 15.99 ? 43 VAL A CG1 1 ATOM 263 C CG2 . VAL A 1 43 ? -54.181 13.191 43.518 1.00 15.58 ? 43 VAL A CG2 1 ATOM 264 N N . GLN A 1 44 ? -51.529 9.620 45.194 1.00 17.62 ? 44 GLN A N 1 ATOM 265 C CA . GLN A 1 44 ? -51.411 8.332 45.875 1.00 18.74 ? 44 GLN A CA 1 ATOM 266 C C . GLN A 1 44 ? -52.604 8.152 46.813 1.00 20.15 ? 44 GLN A C 1 ATOM 267 O O . GLN A 1 44 ? -52.804 8.960 47.731 1.00 18.79 ? 44 GLN A O 1 ATOM 268 C CB . GLN A 1 44 ? -50.092 8.258 46.661 1.00 18.64 ? 44 GLN A CB 1 ATOM 269 C CG . GLN A 1 44 ? -49.831 6.906 47.292 1.00 19.00 ? 44 GLN A CG 1 ATOM 270 C CD . GLN A 1 44 ? -49.624 5.816 46.251 1.00 19.60 ? 44 GLN A CD 1 ATOM 271 O OE1 . GLN A 1 44 ? -49.021 6.056 45.206 1.00 20.95 ? 44 GLN A OE1 1 ATOM 272 N NE2 . GLN A 1 44 ? -50.132 4.616 46.530 1.00 19.90 ? 44 GLN A NE2 1 ATOM 273 N N . SER A 1 45 ? -53.402 7.108 46.596 1.00 20.68 ? 45 SER A N 1 ATOM 274 C CA . SER A 1 45 ? -54.601 6.919 47.409 1.00 24.08 ? 45 SER A CA 1 ATOM 275 C C . SER A 1 45 ? -54.648 5.619 48.213 1.00 26.03 ? 45 SER A C 1 ATOM 276 O O . SER A 1 45 ? -55.594 5.397 48.961 1.00 27.90 ? 45 SER A O 1 ATOM 277 C CB . SER A 1 45 ? -55.864 7.049 46.553 1.00 25.09 ? 45 SER A CB 1 ATOM 278 O OG . SER A 1 45 ? -55.821 6.096 45.521 1.00 28.02 ? 45 SER A OG 1 ATOM 279 N N . SER A 1 46 ? -53.638 4.773 48.088 1.00 27.37 ? 46 SER A N 1 ATOM 280 C CA . SER A 1 46 ? -53.600 3.546 48.869 1.00 30.51 ? 46 SER A CA 1 ATOM 281 C C . SER A 1 46 ? -52.314 3.437 49.679 1.00 31.14 ? 46 SER A C 1 ATOM 282 O O . SER A 1 46 ? -51.303 4.032 49.312 1.00 27.94 ? 46 SER A O 1 ATOM 283 C CB . SER A 1 46 ? -53.688 2.361 47.922 1.00 31.68 ? 46 SER A CB 1 ATOM 284 O OG . SER A 1 46 ? -52.541 2.318 47.088 1.00 32.80 ? 46 SER A OG 1 ATOM 285 N N . SER A 1 47 ? -52.373 2.651 50.759 1.00 33.31 ? 47 SER A N 1 ATOM 286 C CA . SER A 1 47 ? -51.206 2.211 51.515 1.00 33.89 ? 47 SER A CA 1 ATOM 287 C C . SER A 1 47 ? -51.246 0.676 51.643 1.00 37.88 ? 47 SER A C 1 ATOM 288 O O . SER A 1 47 ? -52.310 0.091 51.625 1.00 35.76 ? 47 SER A O 1 ATOM 289 C CB . SER A 1 47 ? -51.227 2.795 52.932 1.00 34.92 ? 47 SER A CB 1 ATOM 290 O OG . SER A 1 47 ? -50.200 2.209 53.746 1.00 34.55 ? 47 SER A OG 1 ATOM 291 N N . THR A 1 48 ? -50.075 0.060 51.795 1.00 41.00 ? 48 THR A N 1 ATOM 292 C CA . THR A 1 48 ? -49.938 -1.363 52.180 1.00 44.22 ? 48 THR A CA 1 ATOM 293 C C . THR A 1 48 ? -50.655 -1.681 53.485 1.00 44.01 ? 48 THR A C 1 ATOM 294 O O . THR A 1 48 ? -51.135 -2.803 53.705 1.00 46.57 ? 48 THR A O 1 ATOM 295 C CB . THR A 1 48 ? -48.460 -1.694 52.445 1.00 45.51 ? 48 THR A CB 1 ATOM 296 O OG1 . THR A 1 48 ? -47.669 -1.288 51.323 1.00 51.40 ? 48 THR A OG1 1 ATOM 297 C CG2 . THR A 1 48 ? -48.267 -3.181 52.719 1.00 48.49 ? 48 THR A CG2 1 ATOM 298 N N . GLY A 1 49 ? -50.687 -0.689 54.371 1.00 41.35 ? 49 GLY A N 1 ATOM 299 C CA . GLY A 1 49 ? -51.321 -0.848 55.655 1.00 39.23 ? 49 GLY A CA 1 ATOM 300 C C . GLY A 1 49 ? -50.303 -1.142 56.735 1.00 36.79 ? 49 GLY A C 1 ATOM 301 O O . GLY A 1 49 ? -50.687 -1.164 57.909 1.00 38.67 ? 49 GLY A O 1 ATOM 302 N N . GLY A 1 50 ? -49.029 -1.374 56.356 1.00 30.83 ? 50 GLY A N 1 ATOM 303 C CA . GLY A 1 50 ? -47.946 -1.517 57.328 1.00 27.21 ? 50 GLY A CA 1 ATOM 304 C C . GLY A 1 50 ? -46.913 -0.402 57.302 1.00 24.35 ? 50 GLY A C 1 ATOM 305 O O . GLY A 1 50 ? -46.645 0.167 56.240 1.00 22.27 ? 50 GLY A O 1 ATOM 306 N N . ILE A 1 51 ? -46.335 -0.099 58.472 1.00 22.49 ? 51 ILE A N 1 ATOM 307 C CA . ILE A 1 51 ? -45.206 0.833 58.583 1.00 22.24 ? 51 ILE A CA 1 ATOM 308 C C . ILE A 1 51 ? -43.898 0.056 58.366 1.00 22.91 ? 51 ILE A C 1 ATOM 309 O O . ILE A 1 51 ? -43.549 -0.816 59.173 1.00 23.42 ? 51 ILE A O 1 ATOM 310 C CB . ILE A 1 51 ? -45.189 1.544 59.950 1.00 21.68 ? 51 ILE A CB 1 ATOM 311 C CG1 . ILE A 1 51 ? -46.378 2.509 60.058 1.00 22.18 ? 51 ILE A CG1 1 ATOM 312 C CG2 . ILE A 1 51 ? -43.901 2.358 60.142 1.00 22.48 ? 51 ILE A CG2 1 ATOM 313 C CD1 . ILE A 1 51 ? -46.580 3.061 61.450 1.00 21.87 ? 51 ILE A CD1 1 ATOM 314 N N . CYS A 1 52 ? -43.208 0.359 57.272 1.00 22.26 ? 52 CYS A N 1 ATOM 315 C CA . CYS A 1 52 ? -41.922 -0.269 56.952 1.00 23.61 ? 52 CYS A CA 1 ATOM 316 C C . CYS A 1 52 ? -40.837 0.159 57.938 1.00 22.83 ? 52 CYS A C 1 ATOM 317 O O . CYS A 1 52 ? -40.682 1.357 58.227 1.00 21.05 ? 52 CYS A O 1 ATOM 318 C CB . CYS A 1 52 ? -41.521 0.067 55.516 1.00 25.29 ? 52 CYS A CB 1 ATOM 319 S SG . CYS A 1 52 ? -42.609 -0.727 54.299 1.00 27.38 ? 52 CYS A SG 1 ATOM 320 N N . ASP A 1 53 ? -40.103 -0.828 58.466 1.00 22.70 ? 53 ASP A N 1 ATOM 321 C CA . ASP A 1 53 ? -39.062 -0.564 59.475 1.00 23.32 ? 53 ASP A CA 1 ATOM 322 C C . ASP A 1 53 ? -37.791 0.035 58.910 1.00 22.50 ? 53 ASP A C 1 ATOM 323 O O . ASP A 1 53 ? -36.866 0.347 59.667 1.00 23.61 ? 53 ASP A O 1 ATOM 324 C CB . ASP A 1 53 ? -38.717 -1.844 60.261 1.00 24.25 ? 53 ASP A CB 1 ATOM 325 C CG . ASP A 1 53 ? -38.049 -2.916 59.406 1.00 25.25 ? 53 ASP A CG 1 ATOM 326 O OD1 . ASP A 1 53 ? -37.738 -2.695 58.213 1.00 25.63 ? 53 ASP A OD1 1 ATOM 327 O OD2 . ASP A 1 53 ? -37.838 -4.012 59.948 1.00 28.15 ? 53 ASP A OD2 1 ATOM 328 N N . SER A 1 54 ? -37.716 0.150 57.587 1.00 22.05 ? 54 SER A N 1 ATOM 329 C CA . SER A 1 54 ? -36.601 0.790 56.901 1.00 21.45 ? 54 SER A CA 1 ATOM 330 C C . SER A 1 54 ? -37.128 1.872 55.949 1.00 21.23 ? 54 SER A C 1 ATOM 331 O O . SER A 1 54 ? -38.235 1.717 55.413 1.00 20.69 ? 54 SER A O 1 ATOM 332 C CB . SER A 1 54 ? -35.831 -0.276 56.122 1.00 22.53 ? 54 SER A CB 1 ATOM 333 O OG . SER A 1 54 ? -35.498 -1.388 56.970 1.00 22.55 ? 54 SER A OG 1 ATOM 334 N N . PRO A 1 55 ? -36.340 2.946 55.691 1.00 20.42 ? 55 PRO A N 1 ATOM 335 C CA . PRO A 1 55 ? -34.985 3.218 56.170 1.00 20.95 ? 55 PRO A CA 1 ATOM 336 C C . PRO A 1 55 ? -34.904 4.068 57.444 1.00 20.96 ? 55 PRO A C 1 ATOM 337 O O . PRO A 1 55 ? -33.772 4.429 57.882 1.00 21.49 ? 55 PRO A O 1 ATOM 338 C CB . PRO A 1 55 ? -34.390 4.008 55.025 1.00 21.03 ? 55 PRO A CB 1 ATOM 339 C CG . PRO A 1 55 ? -35.556 4.872 54.571 1.00 20.56 ? 55 PRO A CG 1 ATOM 340 C CD . PRO A 1 55 ? -36.794 4.019 54.790 1.00 20.32 ? 55 PRO A CD 1 ATOM 341 N N . HIS A 1 56 ? -36.058 4.435 58.004 1.00 19.50 ? 56 HIS A N 1 ATOM 342 C CA . HIS A 1 56 ? -36.095 5.226 59.234 1.00 19.38 ? 56 HIS A CA 1 ATOM 343 C C . HIS A 1 56 ? -36.055 4.310 60.431 1.00 19.54 ? 56 HIS A C 1 ATOM 344 O O . HIS A 1 56 ? -36.599 3.189 60.396 1.00 19.69 ? 56 HIS A O 1 ATOM 345 C CB . HIS A 1 56 ? -37.351 6.092 59.303 1.00 19.12 ? 56 HIS A CB 1 ATOM 346 C CG . HIS A 1 56 ? -37.571 6.937 58.080 1.00 18.93 ? 56 HIS A CG 1 ATOM 347 N ND1 . HIS A 1 56 ? -36.766 7.976 57.754 1.00 19.16 ? 56 HIS A ND1 1 ATOM 348 C CD2 . HIS A 1 56 ? -38.547 6.867 57.091 1.00 18.63 ? 56 HIS A CD2 1 ATOM 349 C CE1 . HIS A 1 56 ? -37.204 8.532 56.609 1.00 19.28 ? 56 HIS A CE1 1 ATOM 350 N NE2 . HIS A 1 56 ? -38.304 7.865 56.213 1.00 18.79 ? 56 HIS A NE2 1 ATOM 351 N N . GLN A 1 57 ? -35.433 4.785 61.511 1.00 19.25 ? 57 GLN A N 1 ATOM 352 C CA . GLN A 1 57 ? -35.386 4.027 62.750 1.00 19.43 ? 57 GLN A CA 1 ATOM 353 C C . GLN A 1 57 ? -36.707 4.156 63.483 1.00 18.91 ? 57 GLN A C 1 ATOM 354 O O . GLN A 1 57 ? -37.038 5.218 64.015 1.00 17.89 ? 57 GLN A O 1 ATOM 355 C CB . GLN A 1 57 ? -34.237 4.479 63.673 1.00 19.64 ? 57 GLN A CB 1 ATOM 356 C CG . GLN A 1 57 ? -34.181 3.656 64.965 1.00 19.85 ? 57 GLN A CG 1 ATOM 357 C CD . GLN A 1 57 ? -33.010 4.010 65.871 1.00 19.89 ? 57 GLN A CD 1 ATOM 358 O OE1 . GLN A 1 57 ? -32.548 5.156 65.902 1.00 20.53 ? 57 GLN A OE1 1 ATOM 359 N NE2 . GLN A 1 57 ? -32.561 3.042 66.649 1.00 19.31 ? 57 GLN A NE2 1 ATOM 360 N N . ILE A 1 58 ? -37.446 3.056 63.526 1.00 19.83 ? 58 ILE A N 1 ATOM 361 C CA . ILE A 1 58 ? -38.766 3.025 64.138 1.00 20.11 ? 58 ILE A CA 1 ATOM 362 C C . ILE A 1 58 ? -38.663 2.515 65.566 1.00 21.70 ? 58 ILE A C 1 ATOM 363 O O . ILE A 1 58 ? -37.931 1.557 65.848 1.00 22.27 ? 58 ILE A O 1 ATOM 364 C CB . ILE A 1 58 ? -39.719 2.093 63.364 1.00 21.04 ? 58 ILE A CB 1 ATOM 365 C CG1 . ILE A 1 58 ? -39.804 2.471 61.877 1.00 21.46 ? 58 ILE A CG1 1 ATOM 366 C CG2 . ILE A 1 58 ? -41.108 2.085 64.018 1.00 21.37 ? 58 ILE A CG2 1 ATOM 367 C CD1 . ILE A 1 58 ? -40.171 3.916 61.570 1.00 22.17 ? 58 ILE A CD1 1 ATOM 368 N N . LEU A 1 59 ? -39.364 3.158 66.482 1.00 21.25 ? 59 LEU A N 1 ATOM 369 C CA . LEU A 1 59 ? -39.503 2.624 67.821 1.00 22.10 ? 59 LEU A CA 1 ATOM 370 C C . LEU A 1 59 ? -40.983 2.432 68.075 1.00 21.54 ? 59 LEU A C 1 ATOM 371 O O . LEU A 1 59 ? -41.726 3.414 68.142 1.00 21.41 ? 59 LEU A O 1 ATOM 372 C CB . LEU A 1 59 ? -38.869 3.545 68.864 1.00 22.02 ? 59 LEU A CB 1 ATOM 373 C CG . LEU A 1 59 ? -38.850 3.027 70.312 1.00 22.97 ? 59 LEU A CG 1 ATOM 374 C CD1 . LEU A 1 59 ? -38.541 1.539 70.401 1.00 24.50 ? 59 LEU A CD1 1 ATOM 375 C CD2 . LEU A 1 59 ? -37.878 3.857 71.150 1.00 22.18 ? 59 LEU A CD2 1 ATOM 376 N N . ASP A 1 60 ? -41.403 1.173 68.165 1.00 21.34 ? 60 ASP A N 1 ATOM 377 C CA . ASP A 1 60 ? -42.808 0.823 68.436 1.00 21.91 ? 60 ASP A CA 1 ATOM 378 C C . ASP A 1 60 ? -43.036 0.879 69.916 1.00 22.68 ? 60 ASP A C 1 ATOM 379 O O . ASP A 1 60 ? -42.444 0.098 70.657 1.00 23.12 ? 60 ASP A O 1 ATOM 380 C CB . ASP A 1 60 ? -43.109 -0.589 67.925 1.00 22.87 ? 60 ASP A CB 1 ATOM 381 C CG . ASP A 1 60 ? -44.580 -0.979 68.049 1.00 22.82 ? 60 ASP A CG 1 ATOM 382 O OD1 . ASP A 1 60 ? -45.359 -0.296 68.739 1.00 22.96 ? 60 ASP A OD1 1 ATOM 383 O OD2 . ASP A 1 60 ? -44.953 -1.979 67.416 1.00 23.43 ? 60 ASP A OD2 1 ATOM 384 N N . GLY A 1 61 ? -43.878 1.802 70.362 1.00 22.30 ? 61 GLY A N 1 ATOM 385 C CA . GLY A 1 61 ? -44.124 1.984 71.775 1.00 23.61 ? 61 GLY A CA 1 ATOM 386 C C . GLY A 1 61 ? -44.871 0.837 72.433 1.00 24.90 ? 61 GLY A C 1 ATOM 387 O O . GLY A 1 61 ? -44.825 0.707 73.645 1.00 25.40 ? 61 GLY A O 1 ATOM 388 N N . GLU A 1 62 ? -45.563 0.013 71.644 1.00 25.76 ? 62 GLU A N 1 ATOM 389 C CA . GLU A 1 62 ? -46.337 -1.101 72.180 1.00 28.33 ? 62 GLU A CA 1 ATOM 390 C C . GLU A 1 62 ? -47.319 -0.606 73.242 1.00 28.24 ? 62 GLU A C 1 ATOM 391 O O . GLU A 1 62 ? -48.172 0.219 72.933 1.00 27.35 ? 62 GLU A O 1 ATOM 392 C CB . GLU A 1 62 ? -45.387 -2.219 72.662 1.00 31.00 ? 62 GLU A CB 1 ATOM 393 C CG . GLU A 1 62 ? -44.404 -2.591 71.557 1.00 34.02 ? 62 GLU A CG 1 ATOM 394 C CD . GLU A 1 62 ? -43.616 -3.857 71.812 1.00 38.50 ? 62 GLU A CD 1 ATOM 395 O OE1 . GLU A 1 62 ? -42.622 -3.807 72.563 1.00 41.38 ? 62 GLU A OE1 1 ATOM 396 O OE2 . GLU A 1 62 ? -43.972 -4.895 71.210 1.00 42.92 ? 62 GLU A OE2 1 ATOM 397 N N . ASN A 1 63 ? -47.218 -1.065 74.488 1.00 28.42 ? 63 ASN A N 1 ATOM 398 C CA . ASN A 1 63 ? -48.158 -0.600 75.523 1.00 29.81 ? 63 ASN A CA 1 ATOM 399 C C . ASN A 1 63 ? -47.763 0.715 76.168 1.00 27.96 ? 63 ASN A C 1 ATOM 400 O O . ASN A 1 63 ? -48.473 1.209 77.043 1.00 26.78 ? 63 ASN A O 1 ATOM 401 C CB . ASN A 1 63 ? -48.308 -1.644 76.624 1.00 33.93 ? 63 ASN A CB 1 ATOM 402 C CG . ASN A 1 63 ? -49.091 -2.842 76.172 1.00 37.41 ? 63 ASN A CG 1 ATOM 403 O OD1 . ASN A 1 63 ? -50.043 -2.730 75.379 1.00 37.61 ? 63 ASN A OD1 1 ATOM 404 N ND2 . ASN A 1 63 ? -48.702 -3.998 76.671 1.00 42.69 ? 63 ASN A ND2 1 ATOM 405 N N . CYS A 1 64 ? -46.651 1.298 75.713 1.00 27.32 ? 64 CYS A N 1 ATOM 406 C CA . CYS A 1 64 ? -46.079 2.488 76.326 1.00 26.24 ? 64 CYS A CA 1 ATOM 407 C C . CYS A 1 64 ? -46.210 3.741 75.468 1.00 25.24 ? 64 CYS A C 1 ATOM 408 O O . CYS A 1 64 ? -45.849 3.733 74.286 1.00 23.22 ? 64 CYS A O 1 ATOM 409 C CB . CYS A 1 64 ? -44.590 2.256 76.584 1.00 28.99 ? 64 CYS A CB 1 ATOM 410 S SG . CYS A 1 64 ? -44.240 0.934 77.780 1.00 31.77 ? 64 CYS A SG 1 ATOM 411 N N . THR A 1 65 ? -46.688 4.822 76.083 1.00 23.52 ? 65 THR A N 1 ATOM 412 C CA . THR A 1 65 ? -46.539 6.146 75.508 1.00 23.01 ? 65 THR A CA 1 ATOM 413 C C . THR A 1 65 ? -45.084 6.552 75.669 1.00 22.54 ? 65 THR A C 1 ATOM 414 O O . THR A 1 65 ? -44.348 5.957 76.478 1.00 22.65 ? 65 THR A O 1 ATOM 415 C CB . THR A 1 65 ? -47.416 7.157 76.247 1.00 22.93 ? 65 THR A CB 1 ATOM 416 O OG1 . THR A 1 65 ? -47.049 7.177 77.631 1.00 22.28 ? 65 THR A OG1 1 ATOM 417 C CG2 . THR A 1 65 ? -48.914 6.791 76.117 1.00 23.79 ? 65 THR A CG2 1 ATOM 418 N N . LEU A 1 66 ? -44.674 7.570 74.920 1.00 21.19 ? 66 LEU A N 1 ATOM 419 C CA . LEU A 1 66 ? -43.333 8.128 75.071 1.00 20.70 ? 66 LEU A CA 1 ATOM 420 C C . LEU A 1 66 ? -43.113 8.616 76.506 1.00 21.29 ? 66 LEU A C 1 ATOM 421 O O . LEU A 1 66 ? -42.057 8.350 77.087 1.00 20.49 ? 66 LEU A O 1 ATOM 422 C CB . LEU A 1 66 ? -43.107 9.273 74.069 1.00 19.92 ? 66 LEU A CB 1 ATOM 423 C CG . LEU A 1 66 ? -41.747 9.991 74.157 1.00 19.60 ? 66 LEU A CG 1 ATOM 424 C CD1 . LEU A 1 66 ? -40.611 8.959 74.150 1.00 19.83 ? 66 LEU A CD1 1 ATOM 425 C CD2 . LEU A 1 66 ? -41.612 11.020 73.026 1.00 18.55 ? 66 LEU A CD2 1 ATOM 426 N N . ILE A 1 67 ? -44.094 9.336 77.073 1.00 22.02 ? 67 ILE A N 1 ATOM 427 C CA . ILE A 1 67 ? -43.932 9.891 78.421 1.00 22.49 ? 67 ILE A CA 1 ATOM 428 C C . ILE A 1 67 ? -43.785 8.750 79.447 1.00 23.10 ? 67 ILE A C 1 ATOM 429 O O . ILE A 1 67 ? -42.941 8.832 80.335 1.00 23.70 ? 67 ILE A O 1 ATOM 430 C CB . ILE A 1 67 ? -45.077 10.868 78.805 1.00 23.74 ? 67 ILE A CB 1 ATOM 431 C CG1 . ILE A 1 67 ? -45.046 12.145 77.955 1.00 24.03 ? 67 ILE A CG1 1 ATOM 432 C CG2 . ILE A 1 67 ? -45.013 11.255 80.282 1.00 23.64 ? 67 ILE A CG2 1 ATOM 433 C CD1 . ILE A 1 67 ? -43.713 12.824 77.873 1.00 24.19 ? 67 ILE A CD1 1 ATOM 434 N N . ASP A 1 68 ? -44.540 7.660 79.302 1.00 23.52 ? 68 ASP A N 1 ATOM 435 C CA . ASP A 1 68 ? -44.344 6.512 80.207 1.00 24.24 ? 68 ASP A CA 1 ATOM 436 C C . ASP A 1 68 ? -42.962 5.880 80.069 1.00 24.02 ? 68 ASP A C 1 ATOM 437 O O . ASP A 1 68 ? -42.346 5.495 81.076 1.00 23.85 ? 68 ASP A O 1 ATOM 438 C CB . ASP A 1 68 ? -45.444 5.457 80.047 1.00 24.57 ? 68 ASP A CB 1 ATOM 439 C CG . ASP A 1 68 ? -46.714 5.820 80.802 1.00 25.58 ? 68 ASP A CG 1 ATOM 440 O OD1 . ASP A 1 68 ? -46.695 6.722 81.657 1.00 27.77 ? 68 ASP A OD1 1 ATOM 441 O OD2 . ASP A 1 68 ? -47.744 5.194 80.552 1.00 27.38 ? 68 ASP A OD2 1 ATOM 442 N N . ALA A 1 69 ? -42.469 5.778 78.839 1.00 23.46 ? 69 ALA A N 1 ATOM 443 C CA . ALA A 1 69 ? -41.115 5.294 78.601 1.00 23.51 ? 69 ALA A CA 1 ATOM 444 C C . ALA A 1 69 ? -40.057 6.248 79.178 1.00 23.21 ? 69 ALA A C 1 ATOM 445 O O . ALA A 1 69 ? -39.017 5.802 79.642 1.00 23.12 ? 69 ALA A O 1 ATOM 446 C CB . ALA A 1 69 ? -40.867 5.063 77.110 1.00 23.70 ? 69 ALA A CB 1 ATOM 447 N N . LEU A 1 70 ? -40.329 7.549 79.140 1.00 22.49 ? 70 LEU A N 1 ATOM 448 C CA . LEU A 1 70 ? -39.444 8.552 79.721 1.00 22.35 ? 70 LEU A CA 1 ATOM 449 C C . LEU A 1 70 ? -39.361 8.440 81.270 1.00 23.85 ? 70 LEU A C 1 ATOM 450 O O . LEU A 1 70 ? -38.277 8.433 81.853 1.00 24.25 ? 70 LEU A O 1 ATOM 451 C CB . LEU A 1 70 ? -39.953 9.931 79.349 1.00 22.00 ? 70 LEU A CB 1 ATOM 452 C CG . LEU A 1 70 ? -39.232 11.183 79.881 1.00 21.85 ? 70 LEU A CG 1 ATOM 453 C CD1 . LEU A 1 70 ? -37.964 11.460 79.094 1.00 21.75 ? 70 LEU A CD1 1 ATOM 454 C CD2 . LEU A 1 70 ? -40.155 12.399 79.844 1.00 21.31 ? 70 LEU A CD2 1 ATOM 455 N N . LEU A 1 71 ? -40.518 8.389 81.911 1.00 24.55 ? 71 LEU A N 1 ATOM 456 C CA . LEU A 1 71 ? -40.587 8.349 83.368 1.00 25.50 ? 71 LEU A CA 1 ATOM 457 C C . LEU A 1 71 ? -40.060 7.016 83.868 1.00 25.97 ? 71 LEU A C 1 ATOM 458 O O . LEU A 1 71 ? -39.413 6.956 84.909 1.00 26.40 ? 71 LEU A O 1 ATOM 459 C CB . LEU A 1 71 ? -42.025 8.561 83.846 1.00 25.84 ? 71 LEU A CB 1 ATOM 460 C CG . LEU A 1 71 ? -42.688 9.884 83.420 1.00 26.37 ? 71 LEU A CG 1 ATOM 461 C CD1 . LEU A 1 71 ? -44.107 9.938 83.961 1.00 27.06 ? 71 LEU A CD1 1 ATOM 462 C CD2 . LEU A 1 71 ? -41.894 11.110 83.861 1.00 26.12 ? 71 LEU A CD2 1 ATOM 463 N N . GLY A 1 72 ? -40.325 5.952 83.115 1.00 25.51 ? 72 GLY A N 1 ATOM 464 C CA . GLY A 1 72 ? -39.821 4.633 83.469 1.00 26.40 ? 72 GLY A CA 1 ATOM 465 C C . GLY A 1 72 ? -40.875 3.749 84.135 1.00 27.94 ? 72 GLY A C 1 ATOM 466 O O . GLY A 1 72 ? -40.590 3.051 85.116 1.00 27.43 ? 72 GLY A O 1 ATOM 467 N N . ASP A 1 73 ? -42.091 3.789 83.598 1.00 28.37 ? 73 ASP A N 1 ATOM 468 C CA . ASP A 1 73 ? -43.148 2.828 83.932 1.00 29.53 ? 73 ASP A CA 1 ATOM 469 C C . ASP A 1 73 ? -42.562 1.404 83.722 1.00 30.24 ? 73 ASP A C 1 ATOM 470 O O . ASP A 1 73 ? -41.933 1.142 82.703 1.00 29.72 ? 73 ASP A O 1 ATOM 471 C CB . ASP A 1 73 ? -44.352 3.125 83.020 1.00 30.22 ? 73 ASP A CB 1 ATOM 472 C CG . ASP A 1 73 ? -45.554 2.218 83.264 1.00 32.05 ? 73 ASP A CG 1 ATOM 473 O OD1 . ASP A 1 73 ? -45.372 0.998 83.388 1.00 36.82 ? 73 ASP A OD1 1 ATOM 474 O OD2 . ASP A 1 73 ? -46.690 2.729 83.286 1.00 31.50 ? 73 ASP A OD2 1 ATOM 475 N N . PRO A 1 74 ? -42.719 0.497 84.698 1.00 33.14 ? 74 PRO A N 1 ATOM 476 C CA . PRO A 1 74 ? -42.086 -0.840 84.647 1.00 33.31 ? 74 PRO A CA 1 ATOM 477 C C . PRO A 1 74 ? -42.225 -1.595 83.314 1.00 33.92 ? 74 PRO A C 1 ATOM 478 O O . PRO A 1 74 ? -41.246 -2.181 82.830 1.00 35.41 ? 74 PRO A O 1 ATOM 479 C CB . PRO A 1 74 ? -42.798 -1.593 85.767 1.00 35.34 ? 74 PRO A CB 1 ATOM 480 C CG . PRO A 1 74 ? -43.104 -0.528 86.773 1.00 35.10 ? 74 PRO A CG 1 ATOM 481 C CD . PRO A 1 74 ? -43.381 0.735 85.996 1.00 34.57 ? 74 PRO A CD 1 ATOM 482 N N . GLN A 1 75 ? -43.403 -1.540 82.699 1.00 34.23 ? 75 GLN A N 1 ATOM 483 C CA . GLN A 1 75 ? -43.607 -2.210 81.410 1.00 35.01 ? 75 GLN A CA 1 ATOM 484 C C . GLN A 1 75 ? -42.784 -1.610 80.269 1.00 32.78 ? 75 GLN A C 1 ATOM 485 O O . GLN A 1 75 ? -42.669 -2.222 79.212 1.00 32.87 ? 75 GLN A O 1 ATOM 486 C CB . GLN A 1 75 ? -45.088 -2.285 81.038 1.00 36.88 ? 75 GLN A CB 1 ATOM 487 C CG . GLN A 1 75 ? -45.780 -0.965 80.795 1.00 38.41 ? 75 GLN A CG 1 ATOM 488 C CD . GLN A 1 75 ? -47.292 -1.113 80.653 1.00 41.25 ? 75 GLN A CD 1 ATOM 489 O OE1 . GLN A 1 75 ? -47.798 -2.205 80.448 1.00 44.10 ? 75 GLN A OE1 1 ATOM 490 N NE2 . GLN A 1 75 ? -48.011 -0.005 80.763 1.00 39.76 ? 75 GLN A NE2 1 ATOM 491 N N . CYS A 1 76 ? -42.200 -0.436 80.501 1.00 30.08 ? 76 CYS A N 1 ATOM 492 C CA . CYS A 1 76 ? -41.392 0.265 79.502 1.00 29.50 ? 76 CYS A CA 1 ATOM 493 C C . CYS A 1 76 ? -39.865 0.146 79.747 1.00 28.54 ? 76 CYS A C 1 ATOM 494 O O . CYS A 1 76 ? -39.066 0.785 79.058 1.00 27.07 ? 76 CYS A O 1 ATOM 495 C CB . CYS A 1 76 ? -41.800 1.743 79.474 1.00 29.45 ? 76 CYS A CB 1 ATOM 496 S SG . CYS A 1 76 ? -43.589 1.991 79.457 1.00 30.28 ? 76 CYS A SG 1 ATOM 497 N N . ASP A 1 77 ? -39.453 -0.693 80.696 1.00 28.16 ? 77 ASP A N 1 ATOM 498 C CA . ASP A 1 77 ? -38.018 -0.795 81.042 1.00 28.46 ? 77 ASP A CA 1 ATOM 499 C C . ASP A 1 77 ? -37.148 -1.130 79.822 1.00 27.18 ? 77 ASP A C 1 ATOM 500 O O . ASP A 1 77 ? -35.998 -0.685 79.721 1.00 26.86 ? 77 ASP A O 1 ATOM 501 C CB . ASP A 1 77 ? -37.793 -1.835 82.156 1.00 30.11 ? 77 ASP A CB 1 ATOM 502 C CG . ASP A 1 77 ? -38.244 -1.347 83.529 1.00 31.85 ? 77 ASP A CG 1 ATOM 503 O OD1 . ASP A 1 77 ? -38.487 -0.126 83.714 1.00 31.79 ? 77 ASP A OD1 1 ATOM 504 O OD2 . ASP A 1 77 ? -38.334 -2.191 84.452 1.00 32.91 ? 77 ASP A OD2 1 ATOM 505 N N . GLY A 1 78 ? -37.711 -1.898 78.895 1.00 26.45 ? 78 GLY A N 1 ATOM 506 C CA . GLY A 1 78 ? -37.025 -2.295 77.679 1.00 27.08 ? 78 GLY A CA 1 ATOM 507 C C . GLY A 1 78 ? -36.628 -1.123 76.783 1.00 26.11 ? 78 GLY A C 1 ATOM 508 O O . GLY A 1 78 ? -35.733 -1.263 75.936 1.00 26.43 ? 78 GLY A O 1 ATOM 509 N N . PHE A 1 79 ? -37.251 0.035 77.001 1.00 26.02 ? 79 PHE A N 1 ATOM 510 C CA . PHE A 1 79 ? -37.013 1.229 76.170 1.00 26.54 ? 79 PHE A CA 1 ATOM 511 C C . PHE A 1 79 ? -35.831 2.073 76.629 1.00 25.10 ? 79 PHE A C 1 ATOM 512 O O . PHE A 1 79 ? -35.453 3.017 75.933 1.00 23.25 ? 79 PHE A O 1 ATOM 513 C CB . PHE A 1 79 ? -38.257 2.133 76.126 1.00 28.44 ? 79 PHE A CB 1 ATOM 514 C CG . PHE A 1 79 ? -39.417 1.550 75.365 1.00 30.83 ? 79 PHE A CG 1 ATOM 515 C CD1 . PHE A 1 79 ? -40.371 0.776 76.006 1.00 31.73 ? 79 PHE A CD1 1 ATOM 516 C CD2 . PHE A 1 79 ? -39.576 1.802 74.017 1.00 33.55 ? 79 PHE A CD2 1 ATOM 517 C CE1 . PHE A 1 79 ? -41.451 0.245 75.317 1.00 31.98 ? 79 PHE A CE1 1 ATOM 518 C CE2 . PHE A 1 79 ? -40.656 1.265 73.319 1.00 34.61 ? 79 PHE A CE2 1 ATOM 519 C CZ . PHE A 1 79 ? -41.590 0.473 73.975 1.00 32.38 ? 79 PHE A CZ 1 ATOM 520 N N . GLN A 1 80 ? -35.250 1.762 77.795 1.00 23.96 ? 80 GLN A N 1 ATOM 521 C CA . GLN A 1 80 ? -34.220 2.620 78.358 1.00 23.30 ? 80 GLN A CA 1 ATOM 522 C C . GLN A 1 80 ? -33.134 2.937 77.336 1.00 22.99 ? 80 GLN A C 1 ATOM 523 O O . GLN A 1 80 ? -32.608 2.035 76.669 1.00 22.79 ? 80 GLN A O 1 ATOM 524 C CB . GLN A 1 80 ? -33.577 1.976 79.614 1.00 24.61 ? 80 GLN A CB 1 ATOM 525 C CG . GLN A 1 80 ? -34.475 2.047 80.842 1.00 25.01 ? 80 GLN A CG 1 ATOM 526 C CD . GLN A 1 80 ? -33.726 1.748 82.129 1.00 27.04 ? 80 GLN A CD 1 ATOM 527 O OE1 . GLN A 1 80 ? -32.533 1.416 82.105 1.00 26.68 ? 80 GLN A OE1 1 ATOM 528 N NE2 . GLN A 1 80 ? -34.416 1.894 83.264 1.00 27.89 ? 80 GLN A NE2 1 ATOM 529 N N . ASN A 1 81 ? -32.818 4.226 77.228 1.00 22.22 ? 81 ASN A N 1 ATOM 530 C CA . ASN A 1 81 ? -31.699 4.735 76.429 1.00 23.10 ? 81 ASN A CA 1 ATOM 531 C C . ASN A 1 81 ? -31.820 4.606 74.908 1.00 22.67 ? 81 ASN A C 1 ATOM 532 O O . ASN A 1 81 ? -30.915 4.999 74.194 1.00 23.28 ? 81 ASN A O 1 ATOM 533 C CB . ASN A 1 81 ? -30.361 4.161 76.913 1.00 24.53 ? 81 ASN A CB 1 ATOM 534 C CG . ASN A 1 81 ? -30.082 4.508 78.361 1.00 25.72 ? 81 ASN A CG 1 ATOM 535 O OD1 . ASN A 1 81 ? -30.040 5.694 78.739 1.00 24.76 ? 81 ASN A OD1 1 ATOM 536 N ND2 . ASN A 1 81 ? -29.928 3.481 79.188 1.00 24.64 ? 81 ASN A ND2 1 ATOM 537 N N . LYS A 1 82 ? -32.939 4.094 74.410 1.00 22.38 ? 82 LYS A N 1 ATOM 538 C CA . LYS A 1 82 ? -33.109 3.908 72.953 1.00 22.90 ? 82 LYS A CA 1 ATOM 539 C C . LYS A 1 82 ? -33.295 5.241 72.229 1.00 21.48 ? 82 LYS A C 1 ATOM 540 O O . LYS A 1 82 ? -33.769 6.222 72.823 1.00 20.59 ? 82 LYS A O 1 ATOM 541 C CB . LYS A 1 82 ? -34.335 3.021 72.673 1.00 24.46 ? 82 LYS A CB 1 ATOM 542 C CG . LYS A 1 82 ? -34.121 1.566 73.052 1.00 27.11 ? 82 LYS A CG 1 ATOM 543 C CD . LYS A 1 82 ? -35.381 0.726 72.896 1.00 28.66 ? 82 LYS A CD 1 ATOM 544 C CE . LYS A 1 82 ? -35.749 0.440 71.447 1.00 30.65 ? 82 LYS A CE 1 ATOM 545 N NZ . LYS A 1 82 ? -34.800 -0.372 70.642 1.00 32.53 ? 82 LYS A NZ 1 ATOM 546 N N . LYS A 1 83 ? -32.993 5.236 70.931 1.00 21.24 ? 83 LYS A N 1 ATOM 547 C CA . LYS A 1 83 ? -33.217 6.364 70.040 1.00 21.00 ? 83 LYS A CA 1 ATOM 548 C C . LYS A 1 83 ? -34.207 5.987 68.939 1.00 20.59 ? 83 LYS A C 1 ATOM 549 O O . LYS A 1 83 ? -34.535 4.802 68.745 1.00 20.54 ? 83 LYS A O 1 ATOM 550 C CB . LYS A 1 83 ? -31.888 6.808 69.408 1.00 22.07 ? 83 LYS A CB 1 ATOM 551 C CG . LYS A 1 83 ? -30.810 7.131 70.424 1.00 22.66 ? 83 LYS A CG 1 ATOM 552 C CD . LYS A 1 83 ? -29.636 7.861 69.782 1.00 23.23 ? 83 LYS A CD 1 ATOM 553 C CE . LYS A 1 83 ? -28.372 7.763 70.627 1.00 24.70 ? 83 LYS A CE 1 ATOM 554 N NZ . LYS A 1 83 ? -27.766 6.398 70.669 1.00 24.92 ? 83 LYS A NZ 1 ATOM 555 N N . TRP A 1 84 ? -34.674 7.000 68.213 1.00 19.63 ? 84 TRP A N 1 ATOM 556 C CA . TRP A 1 84 ? -35.614 6.781 67.121 1.00 19.01 ? 84 TRP A CA 1 ATOM 557 C C . TRP A 1 84 ? -35.567 7.929 66.170 1.00 18.52 ? 84 TRP A C 1 ATOM 558 O O . TRP A 1 84 ? -35.194 9.055 66.536 1.00 18.49 ? 84 TRP A O 1 ATOM 559 C CB . TRP A 1 84 ? -37.044 6.624 67.636 1.00 18.82 ? 84 TRP A CB 1 ATOM 560 C CG . TRP A 1 84 ? -37.528 7.848 68.401 1.00 19.04 ? 84 TRP A CG 1 ATOM 561 C CD1 . TRP A 1 84 ? -38.234 8.942 67.918 1.00 18.75 ? 84 TRP A CD1 1 ATOM 562 C CD2 . TRP A 1 84 ? -37.329 8.122 69.828 1.00 19.18 ? 84 TRP A CD2 1 ATOM 563 N NE1 . TRP A 1 84 ? -38.480 9.845 68.918 1.00 18.59 ? 84 TRP A NE1 1 ATOM 564 C CE2 . TRP A 1 84 ? -37.965 9.405 70.093 1.00 19.31 ? 84 TRP A CE2 1 ATOM 565 C CE3 . TRP A 1 84 ? -36.711 7.453 70.864 1.00 19.82 ? 84 TRP A CE3 1 ATOM 566 C CZ2 . TRP A 1 84 ? -37.949 9.979 71.357 1.00 19.06 ? 84 TRP A CZ2 1 ATOM 567 C CZ3 . TRP A 1 84 ? -36.715 8.020 72.131 1.00 19.89 ? 84 TRP A CZ3 1 ATOM 568 C CH2 . TRP A 1 84 ? -37.309 9.264 72.372 1.00 19.83 ? 84 TRP A CH2 1 ATOM 569 N N . ASP A 1 85 ? -35.946 7.634 64.937 1.00 18.45 ? 85 ASP A N 1 ATOM 570 C CA . ASP A 1 85 ? -36.409 8.650 64.011 1.00 17.70 ? 85 ASP A CA 1 ATOM 571 C C . ASP A 1 85 ? -37.903 8.876 64.230 1.00 17.56 ? 85 ASP A C 1 ATOM 572 O O . ASP A 1 85 ? -38.354 10.019 64.242 1.00 17.90 ? 85 ASP A O 1 ATOM 573 C CB . ASP A 1 85 ? -36.146 8.245 62.568 1.00 17.92 ? 85 ASP A CB 1 ATOM 574 C CG . ASP A 1 85 ? -34.667 8.193 62.218 1.00 18.48 ? 85 ASP A CG 1 ATOM 575 O OD1 . ASP A 1 85 ? -33.870 8.956 62.802 1.00 18.64 ? 85 ASP A OD1 1 ATOM 576 O OD2 . ASP A 1 85 ? -34.310 7.393 61.325 1.00 19.07 ? 85 ASP A OD2 1 ATOM 577 N N . LEU A 1 86 ? -38.669 7.799 64.367 1.00 17.31 ? 86 LEU A N 1 ATOM 578 C CA . LEU A 1 86 ? -40.109 7.888 64.594 1.00 16.63 ? 86 LEU A CA 1 ATOM 579 C C . LEU A 1 86 ? -40.544 6.956 65.706 1.00 16.91 ? 86 LEU A C 1 ATOM 580 O O . LEU A 1 86 ? -40.392 5.745 65.613 1.00 17.17 ? 86 LEU A O 1 ATOM 581 C CB . LEU A 1 86 ? -40.895 7.557 63.305 1.00 16.55 ? 86 LEU A CB 1 ATOM 582 C CG . LEU A 1 86 ? -42.403 7.869 63.382 1.00 16.28 ? 86 LEU A CG 1 ATOM 583 C CD1 . LEU A 1 86 ? -42.628 9.382 63.529 1.00 15.89 ? 86 LEU A CD1 1 ATOM 584 C CD2 . LEU A 1 86 ? -43.110 7.292 62.162 1.00 16.33 ? 86 LEU A CD2 1 ATOM 585 N N . PHE A 1 87 ? -41.087 7.552 66.767 1.00 17.62 ? 87 PHE A N 1 ATOM 586 C CA . PHE A 1 87 ? -41.674 6.819 67.873 1.00 18.03 ? 87 PHE A CA 1 ATOM 587 C C . PHE A 1 87 ? -43.130 6.596 67.520 1.00 18.15 ? 87 PHE A C 1 ATOM 588 O O . PHE A 1 87 ? -43.834 7.551 67.182 1.00 17.55 ? 87 PHE A O 1 ATOM 589 C CB . PHE A 1 87 ? -41.543 7.614 69.163 1.00 18.30 ? 87 PHE A CB 1 ATOM 590 C CG . PHE A 1 87 ? -41.888 6.816 70.393 1.00 19.23 ? 87 PHE A CG 1 ATOM 591 C CD1 . PHE A 1 87 ? -43.213 6.517 70.701 1.00 18.98 ? 87 PHE A CD1 1 ATOM 592 C CD2 . PHE A 1 87 ? -40.885 6.354 71.246 1.00 19.82 ? 87 PHE A CD2 1 ATOM 593 C CE1 . PHE A 1 87 ? -43.529 5.763 71.825 1.00 19.94 ? 87 PHE A CE1 1 ATOM 594 C CE2 . PHE A 1 87 ? -41.201 5.603 72.377 1.00 19.75 ? 87 PHE A CE2 1 ATOM 595 C CZ . PHE A 1 87 ? -42.527 5.313 72.670 1.00 19.79 ? 87 PHE A CZ 1 ATOM 596 N N . VAL A 1 88 ? -43.585 5.349 67.563 1.00 18.77 ? 88 VAL A N 1 ATOM 597 C CA . VAL A 1 88 ? -44.966 5.035 67.167 1.00 19.32 ? 88 VAL A CA 1 ATOM 598 C C . VAL A 1 88 ? -45.783 4.684 68.411 1.00 20.14 ? 88 VAL A C 1 ATOM 599 O O . VAL A 1 88 ? -45.493 3.716 69.084 1.00 20.85 ? 88 VAL A O 1 ATOM 600 C CB . VAL A 1 88 ? -45.035 3.920 66.099 1.00 19.72 ? 88 VAL A CB 1 ATOM 601 C CG1 . VAL A 1 88 ? -46.490 3.577 65.746 1.00 20.09 ? 88 VAL A CG1 1 ATOM 602 C CG2 . VAL A 1 88 ? -44.262 4.312 64.850 1.00 19.74 ? 88 VAL A CG2 1 ATOM 603 N N . GLU A 1 89 ? -46.785 5.509 68.720 1.00 21.13 ? 89 GLU A N 1 ATOM 604 C CA . GLU A 1 89 ? -47.628 5.327 69.900 1.00 22.18 ? 89 GLU A CA 1 ATOM 605 C C . GLU A 1 89 ? -48.920 4.664 69.503 1.00 22.67 ? 89 GLU A C 1 ATOM 606 O O . GLU A 1 89 ? -49.592 5.119 68.555 1.00 22.04 ? 89 GLU A O 1 ATOM 607 C CB . GLU A 1 89 ? -47.989 6.668 70.558 1.00 23.05 ? 89 GLU A CB 1 ATOM 608 C CG . GLU A 1 89 ? -46.979 7.190 71.519 1.00 23.48 ? 89 GLU A CG 1 ATOM 609 C CD . GLU A 1 89 ? -47.397 8.466 72.263 1.00 23.48 ? 89 GLU A CD 1 ATOM 610 O OE1 . GLU A 1 89 ? -48.317 9.209 71.823 1.00 22.08 ? 89 GLU A OE1 1 ATOM 611 O OE2 . GLU A 1 89 ? -46.752 8.726 73.300 1.00 23.09 ? 89 GLU A OE2 1 ATOM 612 N N . ARG A 1 90 ? -49.266 3.604 70.231 1.00 22.55 ? 90 ARG A N 1 ATOM 613 C CA . ARG A 1 90 ? -50.404 2.749 69.902 1.00 23.67 ? 90 ARG A CA 1 ATOM 614 C C . ARG A 1 90 ? -51.629 3.158 70.689 1.00 25.10 ? 90 ARG A C 1 ATOM 615 O O . ARG A 1 90 ? -51.507 3.574 71.850 1.00 24.24 ? 90 ARG A O 1 ATOM 616 C CB . ARG A 1 90 ? -50.072 1.285 70.260 1.00 23.56 ? 90 ARG A CB 1 ATOM 617 C CG . ARG A 1 90 ? -48.777 0.748 69.669 1.00 23.54 ? 90 ARG A CG 1 ATOM 618 C CD . ARG A 1 90 ? -48.673 1.065 68.192 1.00 22.78 ? 90 ARG A CD 1 ATOM 619 N NE . ARG A 1 90 ? -47.757 0.197 67.457 1.00 21.82 ? 90 ARG A NE 1 ATOM 620 C CZ . ARG A 1 90 ? -47.802 0.037 66.144 1.00 21.94 ? 90 ARG A CZ 1 ATOM 621 N NH1 . ARG A 1 90 ? -48.702 0.697 65.412 1.00 21.69 ? 90 ARG A NH1 1 ATOM 622 N NH2 . ARG A 1 90 ? -46.951 -0.784 65.538 1.00 22.46 ? 90 ARG A NH2 1 ATOM 623 N N . SER A 1 91 ? -52.817 2.982 70.104 1.00 26.23 ? 91 SER A N 1 ATOM 624 C CA . SER A 1 91 ? -54.042 3.350 70.817 1.00 27.90 ? 91 SER A CA 1 ATOM 625 C C . SER A 1 91 ? -54.263 2.471 72.059 1.00 29.01 ? 91 SER A C 1 ATOM 626 O O . SER A 1 91 ? -54.887 2.907 73.011 1.00 30.57 ? 91 SER A O 1 ATOM 627 C CB . SER A 1 91 ? -55.273 3.290 69.902 1.00 28.36 ? 91 SER A CB 1 ATOM 628 O OG . SER A 1 91 ? -55.524 1.957 69.495 1.00 29.09 ? 91 SER A OG 1 ATOM 629 N N . LYS A 1 92 ? -53.743 1.248 72.047 1.00 30.39 ? 92 LYS A N 1 ATOM 630 C CA . LYS A 1 92 ? -53.893 0.320 73.184 1.00 32.85 ? 92 LYS A CA 1 ATOM 631 C C . LYS A 1 92 ? -53.036 0.703 74.386 1.00 30.83 ? 92 LYS A C 1 ATOM 632 O O . LYS A 1 92 ? -53.148 0.070 75.430 1.00 29.59 ? 92 LYS A O 1 ATOM 633 C CB . LYS A 1 92 ? -53.495 -1.114 72.782 1.00 34.99 ? 92 LYS A CB 1 ATOM 634 C CG . LYS A 1 92 ? -51.976 -1.317 72.723 1.00 38.50 ? 92 LYS A CG 1 ATOM 635 C CD . LYS A 1 92 ? -51.551 -2.550 71.928 1.00 42.13 ? 92 LYS A CD 1 ATOM 636 C CE . LYS A 1 92 ? -50.029 -2.692 71.939 1.00 44.80 ? 92 LYS A CE 1 ATOM 637 N NZ . LYS A 1 92 ? -49.560 -4.078 71.670 1.00 46.25 ? 92 LYS A NZ 1 ATOM 638 N N . ALA A 1 93 ? -52.149 1.686 74.238 1.00 28.94 ? 93 ALA A N 1 ATOM 639 C CA . ALA A 1 93 ? -51.186 1.999 75.293 1.00 29.10 ? 93 ALA A CA 1 ATOM 640 C C . ALA A 1 93 ? -51.915 2.413 76.569 1.00 29.84 ? 93 ALA A C 1 ATOM 641 O O . ALA A 1 93 ? -52.937 3.087 76.518 1.00 31.12 ? 93 ALA A O 1 ATOM 642 C CB . ALA A 1 93 ? -50.215 3.099 74.853 1.00 27.82 ? 93 ALA A CB 1 ATOM 643 N N . TYR A 1 94 ? -51.378 2.008 77.708 1.00 29.64 ? 94 TYR A N 1 ATOM 644 C CA . TYR A 1 94 ? -51.973 2.342 79.008 1.00 31.30 ? 94 TYR A CA 1 ATOM 645 C C . TYR A 1 94 ? -50.863 2.490 80.058 1.00 30.76 ? 94 TYR A C 1 ATOM 646 O O . TYR A 1 94 ? -49.795 1.868 79.956 1.00 28.79 ? 94 TYR A O 1 ATOM 647 C CB . TYR A 1 94 ? -52.986 1.260 79.428 1.00 33.01 ? 94 TYR A CB 1 ATOM 648 C CG . TYR A 1 94 ? -52.374 -0.109 79.629 1.00 33.92 ? 94 TYR A CG 1 ATOM 649 C CD1 . TYR A 1 94 ? -52.278 -1.010 78.573 1.00 34.97 ? 94 TYR A CD1 1 ATOM 650 C CD2 . TYR A 1 94 ? -51.895 -0.510 80.881 1.00 35.38 ? 94 TYR A CD2 1 ATOM 651 C CE1 . TYR A 1 94 ? -51.726 -2.271 78.750 1.00 35.81 ? 94 TYR A CE1 1 ATOM 652 C CE2 . TYR A 1 94 ? -51.332 -1.764 81.068 1.00 35.87 ? 94 TYR A CE2 1 ATOM 653 C CZ . TYR A 1 94 ? -51.251 -2.645 80.003 1.00 36.76 ? 94 TYR A CZ 1 ATOM 654 O OH . TYR A 1 94 ? -50.690 -3.899 80.186 1.00 36.00 ? 94 TYR A OH 1 ATOM 655 N N . SER A 1 95 ? -51.107 3.339 81.045 1.00 30.46 ? 95 SER A N 1 ATOM 656 C CA . SER A 1 95 ? -50.166 3.526 82.149 1.00 30.66 ? 95 SER A CA 1 ATOM 657 C C . SER A 1 95 ? -50.439 2.508 83.240 1.00 31.63 ? 95 SER A C 1 ATOM 658 O O . SER A 1 95 ? -51.593 2.186 83.493 1.00 32.31 ? 95 SER A O 1 ATOM 659 C CB . SER A 1 95 ? -50.303 4.934 82.712 1.00 30.69 ? 95 SER A CB 1 ATOM 660 O OG . SER A 1 95 ? -49.938 5.881 81.736 1.00 29.36 ? 95 SER A OG 1 ATOM 661 N N . ASN A 1 96 ? -49.379 2.014 83.881 1.00 32.49 ? 96 ASN A N 1 ATOM 662 C CA . ASN A 1 96 ? -49.502 0.989 84.913 1.00 33.85 ? 96 ASN A CA 1 ATOM 663 C C . ASN A 1 96 ? -48.547 1.240 86.095 1.00 32.19 ? 96 ASN A C 1 ATOM 664 O O . ASN A 1 96 ? -47.879 0.336 86.583 1.00 31.84 ? 96 ASN A O 1 ATOM 665 C CB . ASN A 1 96 ? -49.272 -0.400 84.288 1.00 35.41 ? 96 ASN A CB 1 ATOM 666 C CG . ASN A 1 96 ? -49.926 -1.513 85.077 1.00 37.14 ? 96 ASN A CG 1 ATOM 667 O OD1 . ASN A 1 96 ? -50.911 -1.290 85.775 1.00 38.79 ? 96 ASN A OD1 1 ATOM 668 N ND2 . ASN A 1 96 ? -49.400 -2.727 84.944 1.00 37.03 ? 96 ASN A ND2 1 ATOM 669 N N . CYS A 1 97 ? -48.506 2.486 86.557 1.00 31.49 ? 97 CYS A N 1 ATOM 670 C CA . CYS A 1 97 ? -47.627 2.887 87.641 1.00 31.41 ? 97 CYS A CA 1 ATOM 671 C C . CYS A 1 97 ? -48.385 3.917 88.479 1.00 29.85 ? 97 CYS A C 1 ATOM 672 O O . CYS A 1 97 ? -49.620 3.919 88.473 1.00 29.10 ? 97 CYS A O 1 ATOM 673 C CB . CYS A 1 97 ? -46.325 3.411 87.030 1.00 32.14 ? 97 CYS A CB 1 ATOM 674 S SG . CYS A 1 97 ? -44.917 3.723 88.119 1.00 32.79 ? 97 CYS A SG 1 ATOM 675 N N . TYR A 1 98 ? -47.684 4.785 89.193 1.00 29.83 ? 98 TYR A N 1 ATOM 676 C CA . TYR A 1 98 ? -48.361 5.748 90.063 1.00 30.33 ? 98 TYR A CA 1 ATOM 677 C C . TYR A 1 98 ? -49.159 6.741 89.224 1.00 29.74 ? 98 TYR A C 1 ATOM 678 O O . TYR A 1 98 ? -48.662 7.225 88.184 1.00 28.37 ? 98 TYR A O 1 ATOM 679 C CB . TYR A 1 98 ? -47.370 6.483 90.967 1.00 30.58 ? 98 TYR A CB 1 ATOM 680 C CG . TYR A 1 98 ? -47.942 6.883 92.324 1.00 30.96 ? 98 TYR A CG 1 ATOM 681 C CD1 . TYR A 1 98 ? -47.934 5.986 93.400 1.00 31.30 ? 98 TYR A CD1 1 ATOM 682 C CD2 . TYR A 1 98 ? -48.459 8.159 92.535 1.00 31.04 ? 98 TYR A CD2 1 ATOM 683 C CE1 . TYR A 1 98 ? -48.442 6.343 94.645 1.00 31.48 ? 98 TYR A CE1 1 ATOM 684 C CE2 . TYR A 1 98 ? -48.967 8.534 93.774 1.00 31.87 ? 98 TYR A CE2 1 ATOM 685 C CZ . TYR A 1 98 ? -48.949 7.619 94.831 1.00 31.97 ? 98 TYR A CZ 1 ATOM 686 O OH . TYR A 1 98 ? -49.451 7.991 96.053 1.00 31.71 ? 98 TYR A OH 1 ATOM 687 N N . PRO A 1 99 ? -50.416 7.011 89.629 1.00 29.94 ? 99 PRO A N 1 ATOM 688 C CA . PRO A 1 99 ? -51.209 7.938 88.829 1.00 29.81 ? 99 PRO A CA 1 ATOM 689 C C . PRO A 1 99 ? -50.571 9.327 88.784 1.00 29.38 ? 99 PRO A C 1 ATOM 690 O O . PRO A 1 99 ? -50.160 9.864 89.816 1.00 28.38 ? 99 PRO A O 1 ATOM 691 C CB . PRO A 1 99 ? -52.584 7.960 89.530 1.00 30.85 ? 99 PRO A CB 1 ATOM 692 C CG . PRO A 1 99 ? -52.373 7.293 90.857 1.00 30.98 ? 99 PRO A CG 1 ATOM 693 C CD . PRO A 1 99 ? -51.226 6.354 90.673 1.00 31.32 ? 99 PRO A CD 1 ATOM 694 N N . TYR A 1 100 ? -50.444 9.875 87.579 1.00 28.78 ? 100 TYR A N 1 ATOM 695 C CA . TYR A 1 100 ? -49.785 11.155 87.393 1.00 27.76 ? 100 TYR A CA 1 ATOM 696 C C . TYR A 1 100 ? -50.452 11.971 86.293 1.00 28.77 ? 100 TYR A C 1 ATOM 697 O O . TYR A 1 100 ? -51.232 11.444 85.494 1.00 27.45 ? 100 TYR A O 1 ATOM 698 C CB . TYR A 1 100 ? -48.305 10.938 87.040 1.00 28.11 ? 100 TYR A CB 1 ATOM 699 C CG . TYR A 1 100 ? -48.080 10.441 85.632 1.00 28.20 ? 100 TYR A CG 1 ATOM 700 C CD1 . TYR A 1 100 ? -48.103 9.088 85.345 1.00 28.38 ? 100 TYR A CD1 1 ATOM 701 C CD2 . TYR A 1 100 ? -47.860 11.343 84.569 1.00 28.25 ? 100 TYR A CD2 1 ATOM 702 C CE1 . TYR A 1 100 ? -47.900 8.623 84.052 1.00 29.34 ? 100 TYR A CE1 1 ATOM 703 C CE2 . TYR A 1 100 ? -47.675 10.889 83.270 1.00 27.72 ? 100 TYR A CE2 1 ATOM 704 C CZ . TYR A 1 100 ? -47.691 9.527 83.015 1.00 28.99 ? 100 TYR A CZ 1 ATOM 705 O OH . TYR A 1 100 ? -47.489 9.052 81.729 1.00 27.97 ? 100 TYR A OH 1 ATOM 706 N N . ASP A 1 101 ? -50.135 13.263 86.273 1.00 29.16 ? 101 ASP A N 1 ATOM 707 C CA . ASP A 1 101 ? -50.436 14.125 85.144 1.00 29.01 ? 101 ASP A CA 1 ATOM 708 C C . ASP A 1 101 ? -49.203 14.972 84.838 1.00 28.46 ? 101 ASP A C 1 ATOM 709 O O . ASP A 1 101 ? -48.259 15.035 85.645 1.00 27.25 ? 101 ASP A O 1 ATOM 710 C CB . ASP A 1 101 ? -51.640 15.010 85.428 1.00 31.36 ? 101 ASP A CB 1 ATOM 711 C CG . ASP A 1 101 ? -51.509 15.786 86.731 1.00 33.72 ? 101 ASP A CG 1 ATOM 712 O OD1 . ASP A 1 101 ? -50.472 16.433 86.943 1.00 34.59 ? 101 ASP A OD1 1 ATOM 713 O OD2 . ASP A 1 101 ? -52.449 15.734 87.557 1.00 40.15 ? 101 ASP A OD2 1 ATOM 714 N N . VAL A 1 102 ? -49.232 15.611 83.675 1.00 26.31 ? 102 VAL A N 1 ATOM 715 C CA . VAL A 1 102 ? -48.183 16.511 83.237 1.00 26.05 ? 102 VAL A CA 1 ATOM 716 C C . VAL A 1 102 ? -48.853 17.778 82.749 1.00 27.15 ? 102 VAL A C 1 ATOM 717 O O . VAL A 1 102 ? -49.506 17.777 81.674 1.00 26.75 ? 102 VAL A O 1 ATOM 718 C CB . VAL A 1 102 ? -47.358 15.904 82.082 1.00 26.06 ? 102 VAL A CB 1 ATOM 719 C CG1 . VAL A 1 102 ? -46.136 16.777 81.777 1.00 24.89 ? 102 VAL A CG1 1 ATOM 720 C CG2 . VAL A 1 102 ? -46.930 14.475 82.433 1.00 25.35 ? 102 VAL A CG2 1 ATOM 721 N N . PRO A 1 103 ? -48.734 18.863 83.531 1.00 26.94 ? 103 PRO A N 1 ATOM 722 C CA . PRO A 1 103 ? -49.200 20.122 82.977 1.00 28.75 ? 103 PRO A CA 1 ATOM 723 C C . PRO A 1 103 ? -48.437 20.387 81.672 1.00 28.70 ? 103 PRO A C 1 ATOM 724 O O . PRO A 1 103 ? -47.239 20.224 81.636 1.00 31.99 ? 103 PRO A O 1 ATOM 725 C CB . PRO A 1 103 ? -48.825 21.150 84.061 1.00 28.57 ? 103 PRO A CB 1 ATOM 726 C CG . PRO A 1 103 ? -48.779 20.363 85.341 1.00 28.49 ? 103 PRO A CG 1 ATOM 727 C CD . PRO A 1 103 ? -48.317 18.984 84.945 1.00 28.18 ? 103 PRO A CD 1 ATOM 728 N N . ASP A 1 104 ? -49.115 20.773 80.611 1.00 30.49 ? 104 ASP A N 1 ATOM 729 C CA . ASP A 1 104 ? -48.455 20.852 79.284 1.00 29.26 ? 104 ASP A CA 1 ATOM 730 C C . ASP A 1 104 ? -47.742 19.536 78.877 1.00 25.36 ? 104 ASP A C 1 ATOM 731 O O . ASP A 1 104 ? -46.622 19.522 78.326 1.00 23.98 ? 104 ASP A O 1 ATOM 732 C CB . ASP A 1 104 ? -47.495 22.048 79.200 1.00 31.54 ? 104 ASP A CB 1 ATOM 733 C CG . ASP A 1 104 ? -47.341 22.607 77.758 1.00 35.27 ? 104 ASP A CG 1 ATOM 734 O OD1 . ASP A 1 104 ? -48.093 22.227 76.779 1.00 34.27 ? 104 ASP A OD1 1 ATOM 735 O OD2 . ASP A 1 104 ? -46.434 23.465 77.620 1.00 38.04 ? 104 ASP A OD2 1 ATOM 736 N N . TYR A 1 105 ? -48.446 18.441 79.115 1.00 23.79 ? 105 TYR A N 1 ATOM 737 C CA . TYR A 1 105 ? -48.125 17.137 78.563 1.00 22.75 ? 105 TYR A CA 1 ATOM 738 C C . TYR A 1 105 ? -47.725 17.218 77.084 1.00 21.72 ? 105 TYR A C 1 ATOM 739 O O . TYR A 1 105 ? -46.701 16.661 76.704 1.00 20.94 ? 105 TYR A O 1 ATOM 740 C CB . TYR A 1 105 ? -49.347 16.233 78.684 1.00 23.25 ? 105 TYR A CB 1 ATOM 741 C CG . TYR A 1 105 ? -49.133 14.777 78.267 1.00 24.34 ? 105 TYR A CG 1 ATOM 742 C CD1 . TYR A 1 105 ? -49.336 14.370 76.944 1.00 24.85 ? 105 TYR A CD1 1 ATOM 743 C CD2 . TYR A 1 105 ? -48.782 13.809 79.195 1.00 24.88 ? 105 TYR A CD2 1 ATOM 744 C CE1 . TYR A 1 105 ? -49.158 13.042 76.554 1.00 25.02 ? 105 TYR A CE1 1 ATOM 745 C CE2 . TYR A 1 105 ? -48.616 12.472 78.815 1.00 26.30 ? 105 TYR A CE2 1 ATOM 746 C CZ . TYR A 1 105 ? -48.803 12.099 77.492 1.00 25.56 ? 105 TYR A CZ 1 ATOM 747 O OH . TYR A 1 105 ? -48.652 10.783 77.116 1.00 27.61 ? 105 TYR A OH 1 ATOM 748 N N . ALA A 1 106 ? -48.524 17.917 76.266 1.00 21.12 ? 106 ALA A N 1 ATOM 749 C CA . ALA A 1 106 ? -48.257 17.951 74.805 1.00 20.66 ? 106 ALA A CA 1 ATOM 750 C C . ALA A 1 106 ? -46.904 18.534 74.485 1.00 20.43 ? 106 ALA A C 1 ATOM 751 O O . ALA A 1 106 ? -46.236 18.064 73.570 1.00 20.55 ? 106 ALA A O 1 ATOM 752 C CB . ALA A 1 106 ? -49.352 18.699 74.034 1.00 20.16 ? 106 ALA A CB 1 ATOM 753 N N . SER A 1 107 ? -46.477 19.550 75.231 1.00 20.53 ? 107 SER A N 1 ATOM 754 C CA . SER A 1 107 ? -45.151 20.114 74.985 1.00 20.69 ? 107 SER A CA 1 ATOM 755 C C . SER A 1 107 ? -44.011 19.193 75.383 1.00 20.01 ? 107 SER A C 1 ATOM 756 O O . SER A 1 107 ? -43.003 19.153 74.703 1.00 20.45 ? 107 SER A O 1 ATOM 757 C CB . SER A 1 107 ? -44.984 21.477 75.645 1.00 21.09 ? 107 SER A CB 1 ATOM 758 O OG . SER A 1 107 ? -45.759 22.440 74.956 1.00 21.40 ? 107 SER A OG 1 ATOM 759 N N . LEU A 1 108 ? -44.131 18.474 76.484 1.00 20.60 ? 108 LEU A N 1 ATOM 760 C CA . LEU A 1 108 ? -43.022 17.604 76.923 1.00 19.99 ? 108 LEU A CA 1 ATOM 761 C C . LEU A 1 108 ? -42.903 16.411 75.968 1.00 19.59 ? 108 LEU A C 1 ATOM 762 O O . LEU A 1 108 ? -41.797 16.011 75.544 1.00 19.50 ? 108 LEU A O 1 ATOM 763 C CB . LEU A 1 108 ? -43.241 17.135 78.371 1.00 20.60 ? 108 LEU A CB 1 ATOM 764 C CG . LEU A 1 108 ? -42.200 16.141 78.931 1.00 20.42 ? 108 LEU A CG 1 ATOM 765 C CD1 . LEU A 1 108 ? -40.817 16.781 78.918 1.00 21.22 ? 108 LEU A CD1 1 ATOM 766 C CD2 . LEU A 1 108 ? -42.577 15.682 80.338 1.00 20.26 ? 108 LEU A CD2 1 ATOM 767 N N . ARG A 1 109 ? -44.053 15.861 75.606 1.00 19.08 ? 109 ARG A N 1 ATOM 768 C CA . ARG A 1 109 ? -44.115 14.830 74.570 1.00 18.60 ? 109 ARG A CA 1 ATOM 769 C C . ARG A 1 109 ? -43.418 15.282 73.285 1.00 18.06 ? 109 ARG A C 1 ATOM 770 O O . ARG A 1 109 ? -42.609 14.546 72.721 1.00 17.27 ? 109 ARG A O 1 ATOM 771 C CB . ARG A 1 109 ? -45.566 14.439 74.307 1.00 18.33 ? 109 ARG A CB 1 ATOM 772 C CG . ARG A 1 109 ? -45.755 13.361 73.252 1.00 18.43 ? 109 ARG A CG 1 ATOM 773 C CD . ARG A 1 109 ? -47.223 12.939 73.192 1.00 18.51 ? 109 ARG A CD 1 ATOM 774 N NE . ARG A 1 109 ? -47.554 12.006 72.109 1.00 17.99 ? 109 ARG A NE 1 ATOM 775 C CZ . ARG A 1 109 ? -47.759 12.352 70.830 1.00 18.07 ? 109 ARG A CZ 1 ATOM 776 N NH1 . ARG A 1 109 ? -47.673 13.619 70.425 1.00 17.83 ? 109 ARG A NH1 1 ATOM 777 N NH2 . ARG A 1 109 ? -48.086 11.427 69.941 1.00 17.10 ? 109 ARG A NH2 1 ATOM 778 N N . SER A 1 110 ? -43.736 16.496 72.844 1.00 17.74 ? 110 SER A N 1 ATOM 779 C CA . SER A 1 110 ? -43.193 17.040 71.616 1.00 18.09 ? 110 SER A CA 1 ATOM 780 C C . SER A 1 110 ? -41.696 17.262 71.692 1.00 18.14 ? 110 SER A C 1 ATOM 781 O O . SER A 1 110 ? -40.964 16.945 70.747 1.00 17.29 ? 110 SER A O 1 ATOM 782 C CB . SER A 1 110 ? -43.864 18.367 71.247 1.00 18.36 ? 110 SER A CB 1 ATOM 783 O OG . SER A 1 110 ? -43.217 18.899 70.107 1.00 19.10 ? 110 SER A OG 1 ATOM 784 N N . LEU A 1 111 ? -41.236 17.845 72.792 1.00 18.08 ? 111 LEU A N 1 ATOM 785 C CA . LEU A 1 111 ? -39.807 18.137 72.875 1.00 18.90 ? 111 LEU A CA 1 ATOM 786 C C . LEU A 1 111 ? -38.976 16.877 73.001 1.00 18.19 ? 111 LEU A C 1 ATOM 787 O O . LEU A 1 111 ? -37.909 16.805 72.395 1.00 18.34 ? 111 LEU A O 1 ATOM 788 C CB . LEU A 1 111 ? -39.486 19.173 73.957 1.00 19.48 ? 111 LEU A CB 1 ATOM 789 C CG . LEU A 1 111 ? -39.558 18.806 75.410 1.00 20.03 ? 111 LEU A CG 1 ATOM 790 C CD1 . LEU A 1 111 ? -38.203 18.237 75.807 1.00 21.05 ? 111 LEU A CD1 1 ATOM 791 C CD2 . LEU A 1 111 ? -39.928 20.081 76.187 1.00 20.99 ? 111 LEU A CD2 1 ATOM 792 N N . VAL A 1 112 ? -39.478 15.872 73.707 1.00 18.32 ? 112 VAL A N 1 ATOM 793 C CA . VAL A 1 112 ? -38.765 14.570 73.783 1.00 18.88 ? 112 VAL A CA 1 ATOM 794 C C . VAL A 1 112 ? -38.805 13.840 72.416 1.00 18.43 ? 112 VAL A C 1 ATOM 795 O O . VAL A 1 112 ? -37.788 13.334 71.935 1.00 18.02 ? 112 VAL A O 1 ATOM 796 C CB . VAL A 1 112 ? -39.277 13.679 74.935 1.00 19.16 ? 112 VAL A CB 1 ATOM 797 C CG1 . VAL A 1 112 ? -38.485 12.365 74.989 1.00 18.62 ? 112 VAL A CG1 1 ATOM 798 C CG2 . VAL A 1 112 ? -39.100 14.405 76.286 1.00 19.64 ? 112 VAL A CG2 1 ATOM 799 N N . ALA A 1 113 ? -39.968 13.867 71.769 1.00 18.17 ? 113 ALA A N 1 ATOM 800 C CA . ALA A 1 113 ? -40.149 13.244 70.457 1.00 17.67 ? 113 ALA A CA 1 ATOM 801 C C . ALA A 1 113 ? -39.163 13.780 69.441 1.00 17.48 ? 113 ALA A C 1 ATOM 802 O O . ALA A 1 113 ? -38.578 13.007 68.704 1.00 17.07 ? 113 ALA A O 1 ATOM 803 C CB . ALA A 1 113 ? -41.571 13.463 69.953 1.00 16.79 ? 113 ALA A CB 1 ATOM 804 N N . SER A 1 114 ? -39.039 15.110 69.402 1.00 17.58 ? 114 SER A N 1 ATOM 805 C CA . SER A 1 114 ? -38.172 15.817 68.474 1.00 18.65 ? 114 SER A CA 1 ATOM 806 C C . SER A 1 114 ? -36.689 15.619 68.785 1.00 18.99 ? 114 SER A C 1 ATOM 807 O O . SER A 1 114 ? -35.866 15.562 67.874 1.00 19.95 ? 114 SER A O 1 ATOM 808 C CB . SER A 1 114 ? -38.510 17.310 68.479 1.00 18.96 ? 114 SER A CB 1 ATOM 809 O OG . SER A 1 114 ? -37.649 17.994 67.615 1.00 21.18 ? 114 SER A OG 1 ATOM 810 N N . SER A 1 115 ? -36.359 15.498 70.070 1.00 19.28 ? 115 SER A N 1 ATOM 811 C CA . SER A 1 115 ? -35.010 15.160 70.505 1.00 20.03 ? 115 SER A CA 1 ATOM 812 C C . SER A 1 115 ? -34.581 13.743 70.066 1.00 19.51 ? 115 SER A C 1 ATOM 813 O O . SER A 1 115 ? -33.444 13.543 69.628 1.00 20.82 ? 115 SER A O 1 ATOM 814 C CB . SER A 1 115 ? -34.907 15.344 72.029 1.00 20.59 ? 115 SER A CB 1 ATOM 815 O OG . SER A 1 115 ? -33.729 14.781 72.552 1.00 21.84 ? 115 SER A OG 1 ATOM 816 N N . GLY A 1 116 ? -35.484 12.779 70.145 1.00 18.56 ? 116 GLY A N 1 ATOM 817 C CA . GLY A 1 116 ? -35.272 11.467 69.512 1.00 18.58 ? 116 GLY A CA 1 ATOM 818 C C . GLY A 1 116 ? -34.420 10.492 70.299 1.00 19.39 ? 116 GLY A C 1 ATOM 819 O O . GLY A 1 116 ? -33.883 9.550 69.727 1.00 18.54 ? 116 GLY A O 1 ATOM 820 N N . THR A 1 117 ? -34.299 10.723 71.615 1.00 19.68 ? 117 THR A N 1 ATOM 821 C CA . THR A 1 117 ? -33.475 9.877 72.472 1.00 20.39 ? 117 THR A CA 1 ATOM 822 C C . THR A 1 117 ? -33.992 9.809 73.901 1.00 20.63 ? 117 THR A C 1 ATOM 823 O O . THR A 1 117 ? -34.502 10.790 74.461 1.00 21.28 ? 117 THR A O 1 ATOM 824 C CB . THR A 1 117 ? -31.989 10.327 72.500 1.00 20.33 ? 117 THR A CB 1 ATOM 825 O OG1 . THR A 1 117 ? -31.243 9.429 73.326 1.00 20.88 ? 117 THR A OG1 1 ATOM 826 C CG2 . THR A 1 117 ? -31.792 11.787 73.008 1.00 19.97 ? 117 THR A CG2 1 ATOM 827 N N . LEU A 1 118 ? -33.874 8.624 74.477 1.00 20.64 ? 118 LEU A N 1 ATOM 828 C CA . LEU A 1 118 ? -34.156 8.422 75.869 1.00 21.26 ? 118 LEU A CA 1 ATOM 829 C C . LEU A 1 118 ? -32.860 8.255 76.677 1.00 21.97 ? 118 LEU A C 1 ATOM 830 O O . LEU A 1 118 ? -32.896 7.804 77.816 1.00 22.91 ? 118 LEU A O 1 ATOM 831 C CB . LEU A 1 118 ? -35.040 7.191 76.030 1.00 21.40 ? 118 LEU A CB 1 ATOM 832 C CG . LEU A 1 118 ? -36.515 7.419 75.710 1.00 21.16 ? 118 LEU A CG 1 ATOM 833 C CD1 . LEU A 1 118 ? -37.253 6.089 75.580 1.00 21.88 ? 118 LEU A CD1 1 ATOM 834 C CD2 . LEU A 1 118 ? -37.155 8.320 76.739 1.00 21.77 ? 118 LEU A CD2 1 ATOM 835 N N . GLU A 1 119 ? -31.717 8.608 76.092 1.00 23.03 ? 119 GLU A N 1 ATOM 836 C CA . GLU A 1 119 ? -30.446 8.499 76.818 1.00 24.00 ? 119 GLU A CA 1 ATOM 837 C C . GLU A 1 119 ? -30.514 9.217 78.157 1.00 23.68 ? 119 GLU A C 1 ATOM 838 O O . GLU A 1 119 ? -30.831 10.415 78.219 1.00 22.44 ? 119 GLU A O 1 ATOM 839 C CB . GLU A 1 119 ? -29.289 9.085 76.035 1.00 24.70 ? 119 GLU A CB 1 ATOM 840 C CG . GLU A 1 119 ? -28.886 8.284 74.821 1.00 26.43 ? 119 GLU A CG 1 ATOM 841 C CD . GLU A 1 119 ? -28.040 9.132 73.884 1.00 28.70 ? 119 GLU A CD 1 ATOM 842 O OE1 . GLU A 1 119 ? -28.607 9.977 73.119 1.00 27.11 ? 119 GLU A OE1 1 ATOM 843 O OE2 . GLU A 1 119 ? -26.802 8.994 73.973 1.00 29.29 ? 119 GLU A OE2 1 ATOM 844 N N . PHE A 1 120 ? -30.172 8.484 79.217 1.00 23.96 ? 120 PHE A N 1 ATOM 845 C CA . PHE A 1 120 ? -30.286 8.968 80.586 1.00 24.52 ? 120 PHE A CA 1 ATOM 846 C C . PHE A 1 120 ? -28.959 8.746 81.329 1.00 26.72 ? 120 PHE A C 1 ATOM 847 O O . PHE A 1 120 ? -28.389 7.662 81.267 1.00 25.72 ? 120 PHE A O 1 ATOM 848 C CB . PHE A 1 120 ? -31.423 8.242 81.307 1.00 24.26 ? 120 PHE A CB 1 ATOM 849 C CG . PHE A 1 120 ? -31.683 8.752 82.692 1.00 24.76 ? 120 PHE A CG 1 ATOM 850 C CD1 . PHE A 1 120 ? -32.517 9.846 82.893 1.00 25.03 ? 120 PHE A CD1 1 ATOM 851 C CD2 . PHE A 1 120 ? -31.081 8.155 83.801 1.00 25.19 ? 120 PHE A CD2 1 ATOM 852 C CE1 . PHE A 1 120 ? -32.759 10.335 84.168 1.00 25.29 ? 120 PHE A CE1 1 ATOM 853 C CE2 . PHE A 1 120 ? -31.312 8.641 85.077 1.00 25.31 ? 120 PHE A CE2 1 ATOM 854 C CZ . PHE A 1 120 ? -32.148 9.736 85.263 1.00 25.85 ? 120 PHE A CZ 1 ATOM 855 N N . ASN A 1 121 ? -28.474 9.778 82.012 1.00 28.20 ? 121 ASN A N 1 ATOM 856 C CA . ASN A 1 121 ? -27.242 9.671 82.798 1.00 30.76 ? 121 ASN A CA 1 ATOM 857 C C . ASN A 1 121 ? -27.567 9.871 84.262 1.00 30.73 ? 121 ASN A C 1 ATOM 858 O O . ASN A 1 121 ? -28.069 10.920 84.656 1.00 29.61 ? 121 ASN A O 1 ATOM 859 C CB . ASN A 1 121 ? -26.215 10.708 82.345 1.00 33.91 ? 121 ASN A CB 1 ATOM 860 C CG . ASN A 1 121 ? -25.484 10.308 81.074 1.00 38.03 ? 121 ASN A CG 1 ATOM 861 O OD1 . ASN A 1 121 ? -25.713 9.238 80.519 1.00 43.08 ? 121 ASN A OD1 1 ATOM 862 N ND2 . ASN A 1 121 ? -24.590 11.180 80.604 1.00 42.23 ? 121 ASN A ND2 1 ATOM 863 N N . ASN A 1 122 ? -27.300 8.851 85.065 1.00 32.18 ? 122 ASN A N 1 ATOM 864 C CA . ASN A 1 122 ? -27.487 8.938 86.511 1.00 33.04 ? 122 ASN A CA 1 ATOM 865 C C . ASN A 1 122 ? -26.550 9.954 87.155 1.00 31.87 ? 122 ASN A C 1 ATOM 866 O O . ASN A 1 122 ? -25.408 10.105 86.728 1.00 30.90 ? 122 ASN A O 1 ATOM 867 C CB . ASN A 1 122 ? -27.305 7.558 87.139 1.00 35.61 ? 122 ASN A CB 1 ATOM 868 C CG . ASN A 1 122 ? -28.501 6.665 86.893 1.00 37.34 ? 122 ASN A CG 1 ATOM 869 O OD1 . ASN A 1 122 ? -29.573 6.900 87.442 1.00 38.70 ? 122 ASN A OD1 1 ATOM 870 N ND2 . ASN A 1 122 ? -28.340 5.667 86.034 1.00 39.74 ? 122 ASN A ND2 1 ATOM 871 N N . GLU A 1 123 ? -27.048 10.676 88.153 1.00 31.43 ? 123 GLU A N 1 ATOM 872 C CA . GLU A 1 123 ? -26.209 11.572 88.951 1.00 31.89 ? 123 GLU A CA 1 ATOM 873 C C . GLU A 1 123 ? -26.425 11.314 90.440 1.00 32.82 ? 123 GLU A C 1 ATOM 874 O O . GLU A 1 123 ? -27.496 10.874 90.861 1.00 31.23 ? 123 GLU A O 1 ATOM 875 C CB . GLU A 1 123 ? -26.464 13.051 88.633 1.00 31.42 ? 123 GLU A CB 1 ATOM 876 C CG . GLU A 1 123 ? -26.082 13.461 87.207 1.00 30.96 ? 123 GLU A CG 1 ATOM 877 C CD . GLU A 1 123 ? -26.478 14.890 86.880 1.00 30.00 ? 123 GLU A CD 1 ATOM 878 O OE1 . GLU A 1 123 ? -27.647 15.260 87.140 1.00 30.16 ? 123 GLU A OE1 1 ATOM 879 O OE2 . GLU A 1 123 ? -25.629 15.638 86.348 1.00 29.58 ? 123 GLU A OE2 1 ATOM 880 N N . SER A 1 124 ? -25.384 11.604 91.217 1.00 35.85 ? 124 SER A N 1 ATOM 881 C CA . SER A 1 124 ? -25.375 11.361 92.660 1.00 38.25 ? 124 SER A CA 1 ATOM 882 C C . SER A 1 124 ? -25.805 12.632 93.376 1.00 38.06 ? 124 SER A C 1 ATOM 883 O O . SER A 1 124 ? -24.973 13.489 93.684 1.00 38.16 ? 124 SER A O 1 ATOM 884 C CB . SER A 1 124 ? -23.965 10.967 93.137 1.00 40.68 ? 124 SER A CB 1 ATOM 885 O OG . SER A 1 124 ? -23.489 9.814 92.462 1.00 44.17 ? 124 SER A OG 1 ATOM 886 N N . PHE A 1 125 ? -27.101 12.759 93.619 1.00 37.25 ? 125 PHE A N 1 ATOM 887 C CA . PHE A 1 125 ? -27.613 13.890 94.360 1.00 39.12 ? 125 PHE A CA 1 ATOM 888 C C . PHE A 1 125 ? -27.385 13.584 95.833 1.00 41.63 ? 125 PHE A C 1 ATOM 889 O O . PHE A 1 125 ? -27.423 12.428 96.241 1.00 42.06 ? 125 PHE A O 1 ATOM 890 C CB . PHE A 1 125 ? -29.107 14.101 94.112 1.00 38.69 ? 125 PHE A CB 1 ATOM 891 C CG . PHE A 1 125 ? -29.424 14.706 92.774 1.00 36.95 ? 125 PHE A CG 1 ATOM 892 C CD1 . PHE A 1 125 ? -29.585 13.902 91.655 1.00 36.78 ? 125 PHE A CD1 1 ATOM 893 C CD2 . PHE A 1 125 ? -29.551 16.082 92.634 1.00 36.97 ? 125 PHE A CD2 1 ATOM 894 C CE1 . PHE A 1 125 ? -29.874 14.460 90.421 1.00 35.71 ? 125 PHE A CE1 1 ATOM 895 C CE2 . PHE A 1 125 ? -29.849 16.644 91.406 1.00 37.61 ? 125 PHE A CE2 1 ATOM 896 C CZ . PHE A 1 125 ? -30.004 15.830 90.294 1.00 36.11 ? 125 PHE A CZ 1 ATOM 897 N N . ASN A 1 126 ? -27.154 14.619 96.620 1.00 42.45 ? 126 ASN A N 1 ATOM 898 C CA . ASN A 1 126 ? -26.986 14.435 98.048 1.00 45.38 ? 126 ASN A CA 1 ATOM 899 C C . ASN A 1 126 ? -28.338 14.512 98.753 1.00 43.91 ? 126 ASN A C 1 ATOM 900 O O . ASN A 1 126 ? -28.802 15.601 99.109 1.00 43.21 ? 126 ASN A O 1 ATOM 901 C CB . ASN A 1 126 ? -26.000 15.470 98.598 1.00 48.47 ? 126 ASN A CB 1 ATOM 902 C CG . ASN A 1 126 ? -25.712 15.265 100.071 1.00 51.86 ? 126 ASN A CG 1 ATOM 903 O OD1 . ASN A 1 126 ? -26.481 14.601 100.773 1.00 51.48 ? 126 ASN A OD1 1 ATOM 904 N ND2 . ASN A 1 126 ? -24.606 15.835 100.549 1.00 55.09 ? 126 ASN A ND2 1 ATOM 905 N N . TRP A 1 127 ? -28.969 13.354 98.947 1.00 42.43 ? 127 TRP A N 1 ATOM 906 C CA . TRP A 1 127 ? -30.211 13.281 99.714 1.00 43.64 ? 127 TRP A CA 1 ATOM 907 C C . TRP A 1 127 ? -29.943 12.799 101.118 1.00 45.05 ? 127 TRP A C 1 ATOM 908 O O . TRP A 1 127 ? -30.554 11.833 101.589 1.00 45.71 ? 127 TRP A O 1 ATOM 909 C CB . TRP A 1 127 ? -31.233 12.365 99.050 1.00 41.92 ? 127 TRP A CB 1 ATOM 910 C CG . TRP A 1 127 ? -31.508 12.685 97.598 1.00 40.14 ? 127 TRP A CG 1 ATOM 911 C CD1 . TRP A 1 127 ? -31.410 11.823 96.518 1.00 39.89 ? 127 TRP A CD1 1 ATOM 912 C CD2 . TRP A 1 127 ? -31.933 13.972 97.020 1.00 39.16 ? 127 TRP A CD2 1 ATOM 913 N NE1 . TRP A 1 127 ? -31.744 12.465 95.348 1.00 38.69 ? 127 TRP A NE1 1 ATOM 914 C CE2 . TRP A 1 127 ? -32.059 13.749 95.576 1.00 37.38 ? 127 TRP A CE2 1 ATOM 915 C CE3 . TRP A 1 127 ? -32.211 15.233 97.530 1.00 39.39 ? 127 TRP A CE3 1 ATOM 916 C CZ2 . TRP A 1 127 ? -32.448 14.757 94.705 1.00 37.42 ? 127 TRP A CZ2 1 ATOM 917 C CZ3 . TRP A 1 127 ? -32.610 16.247 96.639 1.00 38.84 ? 127 TRP A CZ3 1 ATOM 918 C CH2 . TRP A 1 127 ? -32.719 16.011 95.257 1.00 37.78 ? 127 TRP A CH2 1 ATOM 919 N N . THR A 1 128 ? -29.021 13.461 101.800 1.00 47.69 ? 128 THR A N 1 ATOM 920 C CA . THR A 1 128 ? -28.737 13.126 103.197 1.00 48.22 ? 128 THR A CA 1 ATOM 921 C C . THR A 1 128 ? -29.837 13.698 104.095 1.00 47.08 ? 128 THR A C 1 ATOM 922 O O . THR A 1 128 ? -30.185 14.873 103.993 1.00 48.06 ? 128 THR A O 1 ATOM 923 C CB . THR A 1 128 ? -27.358 13.649 103.634 1.00 51.37 ? 128 THR A CB 1 ATOM 924 O OG1 . THR A 1 128 ? -27.231 15.029 103.266 1.00 54.33 ? 128 THR A OG1 1 ATOM 925 C CG2 . THR A 1 128 ? -26.232 12.830 102.980 1.00 50.08 ? 128 THR A CG2 1 ATOM 926 N N . GLY A 1 129 ? -30.388 12.850 104.959 1.00 47.56 ? 129 GLY A N 1 ATOM 927 C CA . GLY A 1 129 ? -31.398 13.256 105.936 1.00 46.53 ? 129 GLY A CA 1 ATOM 928 C C . GLY A 1 129 ? -32.799 12.769 105.627 1.00 45.54 ? 129 GLY A C 1 ATOM 929 O O . GLY A 1 129 ? -33.722 13.002 106.415 1.00 44.41 ? 129 GLY A O 1 ATOM 930 N N . VAL A 1 130 ? -32.972 12.119 104.470 1.00 43.84 ? 130 VAL A N 1 ATOM 931 C CA . VAL A 1 130 ? -34.272 11.568 104.066 1.00 41.12 ? 130 VAL A CA 1 ATOM 932 C C . VAL A 1 130 ? -34.130 10.117 103.601 1.00 39.59 ? 130 VAL A C 1 ATOM 933 O O . VAL A 1 130 ? -33.022 9.644 103.345 1.00 37.85 ? 130 VAL A O 1 ATOM 934 C CB . VAL A 1 130 ? -34.918 12.390 102.926 1.00 41.12 ? 130 VAL A CB 1 ATOM 935 C CG1 . VAL A 1 130 ? -35.156 13.833 103.364 1.00 40.82 ? 130 VAL A CG1 1 ATOM 936 C CG2 . VAL A 1 130 ? -34.050 12.327 101.679 1.00 40.28 ? 130 VAL A CG2 1 ATOM 937 N N . THR A 1 131 ? -35.267 9.428 103.522 1.00 38.61 ? 131 THR A N 1 ATOM 938 C CA . THR A 1 131 ? -35.359 8.082 102.984 1.00 39.17 ? 131 THR A CA 1 ATOM 939 C C . THR A 1 131 ? -35.619 8.182 101.477 1.00 39.14 ? 131 THR A C 1 ATOM 940 O O . THR A 1 131 ? -36.459 8.978 101.047 1.00 35.91 ? 131 THR A O 1 ATOM 941 C CB . THR A 1 131 ? -36.528 7.315 103.624 1.00 40.82 ? 131 THR A CB 1 ATOM 942 O OG1 . THR A 1 131 ? -36.349 7.257 105.046 1.00 41.55 ? 131 THR A OG1 1 ATOM 943 C CG2 . THR A 1 131 ? -36.622 5.892 103.069 1.00 41.87 ? 131 THR A CG2 1 ATOM 944 N N . GLN A 1 132 ? -34.897 7.379 100.696 1.00 38.86 ? 132 GLN A N 1 ATOM 945 C CA . GLN A 1 132 ? -35.029 7.358 99.230 1.00 38.28 ? 132 GLN A CA 1 ATOM 946 C C . GLN A 1 132 ? -35.810 6.135 98.779 1.00 38.74 ? 132 GLN A C 1 ATOM 947 O O . GLN A 1 132 ? -36.156 5.270 99.591 1.00 37.82 ? 132 GLN A O 1 ATOM 948 C CB . GLN A 1 132 ? -33.644 7.318 98.581 1.00 37.92 ? 132 GLN A CB 1 ATOM 949 C CG . GLN A 1 132 ? -32.718 8.425 99.039 1.00 37.67 ? 132 GLN A CG 1 ATOM 950 C CD . GLN A 1 132 ? -31.446 8.497 98.223 1.00 38.70 ? 132 GLN A CD 1 ATOM 951 O OE1 . GLN A 1 132 ? -31.467 8.356 96.989 1.00 37.73 ? 132 GLN A OE1 1 ATOM 952 N NE2 . GLN A 1 132 ? -30.324 8.728 98.902 1.00 36.52 ? 132 GLN A NE2 1 ATOM 953 N N . ASN A 1 133 ? -36.085 6.071 97.475 1.00 38.17 ? 133 ASN A N 1 ATOM 954 C CA . ASN A 1 133 ? -36.640 4.876 96.829 1.00 38.09 ? 133 ASN A CA 1 ATOM 955 C C . ASN A 1 133 ? -38.024 4.440 97.311 1.00 36.03 ? 133 ASN A C 1 ATOM 956 O O . ASN A 1 133 ? -38.314 3.246 97.379 1.00 34.99 ? 133 ASN A O 1 ATOM 957 C CB . ASN A 1 133 ? -35.653 3.701 96.925 1.00 40.97 ? 133 ASN A CB 1 ATOM 958 C CG . ASN A 1 133 ? -34.391 3.926 96.116 1.00 45.92 ? 133 ASN A CG 1 ATOM 959 O OD1 . ASN A 1 133 ? -34.210 4.981 95.493 1.00 44.12 ? 133 ASN A OD1 1 ATOM 960 N ND2 . ASN A 1 133 ? -33.510 2.926 96.109 1.00 53.61 ? 133 ASN A ND2 1 ATOM 961 N N . GLY A 1 134 ? -38.900 5.388 97.611 1.00 35.19 ? 134 GLY A N 1 ATOM 962 C CA . GLY A 1 134 ? -40.286 5.031 97.928 1.00 35.32 ? 134 GLY A CA 1 ATOM 963 C C . GLY A 1 134 ? -40.917 4.246 96.785 1.00 37.33 ? 134 GLY A C 1 ATOM 964 O O . GLY A 1 134 ? -40.590 4.476 95.597 1.00 37.07 ? 134 GLY A O 1 ATOM 965 N N . THR A 1 135 ? -41.820 3.324 97.130 1.00 37.36 ? 135 THR A N 1 ATOM 966 C CA . THR A 1 135 ? -42.485 2.487 96.140 1.00 36.38 ? 135 THR A CA 1 ATOM 967 C C . THR A 1 135 ? -43.976 2.401 96.406 1.00 36.50 ? 135 THR A C 1 ATOM 968 O O . THR A 1 135 ? -44.466 2.951 97.399 1.00 36.15 ? 135 THR A O 1 ATOM 969 C CB . THR A 1 135 ? -41.877 1.072 96.106 1.00 37.63 ? 135 THR A CB 1 ATOM 970 O OG1 . THR A 1 135 ? -42.096 0.425 97.363 1.00 36.94 ? 135 THR A OG1 1 ATOM 971 C CG2 . THR A 1 135 ? -40.369 1.131 95.818 1.00 36.23 ? 135 THR A CG2 1 ATOM 972 N N . SER A 1 136 ? -44.687 1.723 95.498 1.00 36.21 ? 136 SER A N 1 ATOM 973 C CA . SER A 1 136 ? -46.139 1.570 95.575 1.00 35.67 ? 136 SER A CA 1 ATOM 974 C C . SER A 1 136 ? -46.642 0.295 94.891 1.00 36.05 ? 136 SER A C 1 ATOM 975 O O . SER A 1 136 ? -46.028 -0.195 93.929 1.00 34.80 ? 136 SER A O 1 ATOM 976 C CB . SER A 1 136 ? -46.814 2.793 94.941 1.00 35.15 ? 136 SER A CB 1 ATOM 977 O OG . SER A 1 136 ? -48.211 2.613 94.830 1.00 34.53 ? 136 SER A OG 1 ATOM 978 N N . SER A 1 137 ? -47.779 -0.213 95.378 1.00 35.81 ? 137 SER A N 1 ATOM 979 C CA . SER A 1 137 ? -48.456 -1.374 94.784 1.00 36.47 ? 137 SER A CA 1 ATOM 980 C C . SER A 1 137 ? -49.142 -1.010 93.479 1.00 36.47 ? 137 SER A C 1 ATOM 981 O O . SER A 1 137 ? -49.484 -1.887 92.691 1.00 36.62 ? 137 SER A O 1 ATOM 982 C CB . SER A 1 137 ? -49.509 -1.950 95.748 1.00 36.83 ? 137 SER A CB 1 ATOM 983 O OG . SER A 1 137 ? -50.442 -0.948 96.128 1.00 35.44 ? 137 SER A OG 1 ATOM 984 N N . ALA A 1 138 ? -49.372 0.285 93.272 1.00 36.40 ? 138 ALA A N 1 ATOM 985 C CA . ALA A 1 138 ? -49.860 0.798 91.990 1.00 35.26 ? 138 ALA A CA 1 ATOM 986 C C . ALA A 1 138 ? -48.801 0.720 90.875 1.00 35.64 ? 138 ALA A C 1 ATOM 987 O O . ALA A 1 138 ? -49.118 0.934 89.692 1.00 36.78 ? 138 ALA A O 1 ATOM 988 C CB . ALA A 1 138 ? -50.327 2.240 92.169 1.00 33.97 ? 138 ALA A CB 1 ATOM 989 N N . CYS A 1 139 ? -47.552 0.450 91.242 1.00 35.38 ? 139 CYS A N 1 ATOM 990 C CA . CYS A 1 139 ? -46.459 0.430 90.270 1.00 36.59 ? 139 CYS A CA 1 ATOM 991 C C . CYS A 1 139 ? -45.544 -0.751 90.486 1.00 37.00 ? 139 CYS A C 1 ATOM 992 O O . CYS A 1 139 ? -44.393 -0.590 90.887 1.00 37.42 ? 139 CYS A O 1 ATOM 993 C CB . CYS A 1 139 ? -45.662 1.741 90.313 1.00 35.27 ? 139 CYS A CB 1 ATOM 994 S SG . CYS A 1 139 ? -44.430 1.908 88.978 1.00 36.19 ? 139 CYS A SG 1 ATOM 995 N N . LYS A 1 140 ? -46.046 -1.941 90.183 1.00 38.92 ? 140 LYS A N 1 ATOM 996 C CA . LYS A 1 140 ? -45.289 -3.153 90.437 1.00 41.98 ? 140 LYS A CA 1 ATOM 997 C C . LYS A 1 140 ? -44.253 -3.446 89.345 1.00 42.42 ? 140 LYS A C 1 ATOM 998 O O . LYS A 1 140 ? -44.504 -3.228 88.149 1.00 40.48 ? 140 LYS A O 1 ATOM 999 C CB . LYS A 1 140 ? -46.229 -4.350 90.640 1.00 45.88 ? 140 LYS A CB 1 ATOM 1000 C CG . LYS A 1 140 ? -47.112 -4.226 91.880 1.00 48.22 ? 140 LYS A CG 1 ATOM 1001 C CD . LYS A 1 140 ? -47.518 -5.584 92.431 1.00 50.88 ? 140 LYS A CD 1 ATOM 1002 C CE . LYS A 1 140 ? -48.672 -5.488 93.428 1.00 52.79 ? 140 LYS A CE 1 ATOM 1003 N NZ . LYS A 1 140 ? -49.940 -4.972 92.813 1.00 54.66 ? 140 LYS A NZ 1 ATOM 1004 N N . ARG A 1 141 ? -43.087 -3.927 89.780 1.00 41.14 ? 141 ARG A N 1 ATOM 1005 C CA . ARG A 1 141 ? -42.010 -4.369 88.899 1.00 43.71 ? 141 ARG A CA 1 ATOM 1006 C C . ARG A 1 141 ? -41.550 -5.751 89.373 1.00 47.98 ? 141 ARG A C 1 ATOM 1007 O O . ARG A 1 141 ? -41.118 -5.902 90.520 1.00 44.99 ? 141 ARG A O 1 ATOM 1008 C CB . ARG A 1 141 ? -40.847 -3.370 88.944 1.00 43.24 ? 141 ARG A CB 1 ATOM 1009 C CG . ARG A 1 141 ? -39.686 -3.691 88.009 1.00 42.99 ? 141 ARG A CG 1 ATOM 1010 C CD . ARG A 1 141 ? -38.632 -2.588 88.002 1.00 41.94 ? 141 ARG A CD 1 ATOM 1011 N NE . ARG A 1 141 ? -38.916 -1.511 87.033 1.00 41.15 ? 141 ARG A NE 1 ATOM 1012 C CZ . ARG A 1 141 ? -39.326 -0.272 87.326 1.00 40.87 ? 141 ARG A CZ 1 ATOM 1013 N NH1 . ARG A 1 141 ? -39.549 0.114 88.585 1.00 39.99 ? 141 ARG A NH1 1 ATOM 1014 N NH2 . ARG A 1 141 ? -39.524 0.608 86.337 1.00 39.76 ? 141 ARG A NH2 1 ATOM 1015 N N . ARG A 1 142 ? -41.655 -6.750 88.493 1.00 50.79 ? 142 ARG A N 1 ATOM 1016 C CA . ARG A 1 142 ? -41.371 -8.143 88.847 1.00 55.28 ? 142 ARG A CA 1 ATOM 1017 C C . ARG A 1 142 ? -42.128 -8.509 90.125 1.00 54.95 ? 142 ARG A C 1 ATOM 1018 O O . ARG A 1 142 ? -41.537 -8.928 91.121 1.00 54.96 ? 142 ARG A O 1 ATOM 1019 C CB . ARG A 1 142 ? -39.862 -8.378 89.000 1.00 58.00 ? 142 ARG A CB 1 ATOM 1020 C CG . ARG A 1 142 ? -39.085 -8.203 87.703 1.00 61.90 ? 142 ARG A CG 1 ATOM 1021 C CD . ARG A 1 142 ? -37.582 -8.289 87.929 1.00 65.34 ? 142 ARG A CD 1 ATOM 1022 N NE . ARG A 1 142 ? -37.059 -7.134 88.668 1.00 68.06 ? 142 ARG A NE 1 ATOM 1023 C CZ . ARG A 1 142 ? -36.634 -5.990 88.121 1.00 69.81 ? 142 ARG A CZ 1 ATOM 1024 N NH1 . ARG A 1 142 ? -36.648 -5.805 86.803 1.00 67.97 ? 142 ARG A NH1 1 ATOM 1025 N NH2 . ARG A 1 142 ? -36.181 -5.018 88.907 1.00 71.45 ? 142 ARG A NH2 1 ATOM 1026 N N . SER A 1 143 ? -43.440 -8.277 90.088 1.00 55.61 ? 143 SER A N 1 ATOM 1027 C CA . SER A 1 143 ? -44.370 -8.588 91.188 1.00 56.35 ? 143 SER A CA 1 ATOM 1028 C C . SER A 1 143 ? -44.174 -7.826 92.513 1.00 54.10 ? 143 SER A C 1 ATOM 1029 O O . SER A 1 143 ? -45.014 -7.943 93.408 1.00 56.86 ? 143 SER A O 1 ATOM 1030 C CB . SER A 1 143 ? -44.397 -10.100 91.448 1.00 58.20 ? 143 SER A CB 1 ATOM 1031 O OG . SER A 1 143 ? -44.926 -10.772 90.318 1.00 61.36 ? 143 SER A OG 1 ATOM 1032 N N . ASN A 1 144 ? -43.099 -7.047 92.637 1.00 50.08 ? 144 ASN A N 1 ATOM 1033 C CA . ASN A 1 144 ? -42.836 -6.267 93.849 1.00 48.19 ? 144 ASN A CA 1 ATOM 1034 C C . ASN A 1 144 ? -43.296 -4.828 93.691 1.00 46.81 ? 144 ASN A C 1 ATOM 1035 O O . ASN A 1 144 ? -43.276 -4.292 92.574 1.00 44.52 ? 144 ASN A O 1 ATOM 1036 C CB . ASN A 1 144 ? -41.342 -6.237 94.156 1.00 49.13 ? 144 ASN A CB 1 ATOM 1037 C CG . ASN A 1 144 ? -40.749 -7.619 94.351 1.00 53.02 ? 144 ASN A CG 1 ATOM 1038 O OD1 . ASN A 1 144 ? -39.559 -7.824 94.103 1.00 56.96 ? 144 ASN A OD1 1 ATOM 1039 N ND2 . ASN A 1 144 ? -41.569 -8.574 94.791 1.00 50.31 ? 144 ASN A ND2 1 ATOM 1040 N N . ASN A 1 145 ? -43.674 -4.199 94.806 1.00 42.19 ? 145 ASN A N 1 ATOM 1041 C CA . ASN A 1 145 ? -43.973 -2.767 94.824 1.00 40.50 ? 145 ASN A CA 1 ATOM 1042 C C . ASN A 1 145 ? -42.780 -1.996 94.268 1.00 38.13 ? 145 ASN A C 1 ATOM 1043 O O . ASN A 1 145 ? -41.657 -2.300 94.608 1.00 36.01 ? 145 ASN A O 1 ATOM 1044 C CB . ASN A 1 145 ? -44.242 -2.295 96.251 1.00 40.82 ? 145 ASN A CB 1 ATOM 1045 C CG . ASN A 1 145 ? -45.630 -2.653 96.743 1.00 40.87 ? 145 ASN A CG 1 ATOM 1046 O OD1 . ASN A 1 145 ? -46.350 -3.448 96.130 1.00 39.61 ? 145 ASN A OD1 1 ATOM 1047 N ND2 . ASN A 1 145 ? -46.018 -2.048 97.861 1.00 40.46 ? 145 ASN A ND2 1 ATOM 1048 N N . SER A 1 146 ? -43.016 -1.009 93.403 1.00 37.39 ? 146 SER A N 1 ATOM 1049 C CA . SER A 1 146 ? -41.892 -0.273 92.801 1.00 35.15 ? 146 SER A CA 1 ATOM 1050 C C . SER A 1 146 ? -42.338 1.141 92.440 1.00 34.49 ? 146 SER A C 1 ATOM 1051 O O . SER A 1 146 ? -43.351 1.638 92.953 1.00 33.05 ? 146 SER A O 1 ATOM 1052 C CB . SER A 1 146 ? -41.347 -1.027 91.570 1.00 36.02 ? 146 SER A CB 1 ATOM 1053 O OG . SER A 1 146 ? -40.059 -0.555 91.172 1.00 35.75 ? 146 SER A OG 1 ATOM 1054 N N . PHE A 1 147 ? -41.588 1.775 91.542 1.00 32.58 ? 147 PHE A N 1 ATOM 1055 C CA . PHE A 1 147 ? -41.846 3.161 91.172 1.00 31.31 ? 147 PHE A CA 1 ATOM 1056 C C . PHE A 1 147 ? -41.229 3.425 89.795 1.00 29.93 ? 147 PHE A C 1 ATOM 1057 O O . PHE A 1 147 ? -40.469 2.601 89.273 1.00 29.08 ? 147 PHE A O 1 ATOM 1058 C CB . PHE A 1 147 ? -41.222 4.078 92.225 1.00 30.86 ? 147 PHE A CB 1 ATOM 1059 C CG . PHE A 1 147 ? -41.793 5.466 92.260 1.00 30.98 ? 147 PHE A CG 1 ATOM 1060 C CD1 . PHE A 1 147 ? -43.129 5.681 92.581 1.00 30.94 ? 147 PHE A CD1 1 ATOM 1061 C CD2 . PHE A 1 147 ? -40.979 6.568 92.006 1.00 31.10 ? 147 PHE A CD2 1 ATOM 1062 C CE1 . PHE A 1 147 ? -43.649 6.965 92.628 1.00 31.29 ? 147 PHE A CE1 1 ATOM 1063 C CE2 . PHE A 1 147 ? -41.496 7.858 92.061 1.00 31.25 ? 147 PHE A CE2 1 ATOM 1064 C CZ . PHE A 1 147 ? -42.829 8.056 92.369 1.00 31.74 ? 147 PHE A CZ 1 ATOM 1065 N N . PHE A 1 148 ? -41.550 4.573 89.221 1.00 28.92 ? 148 PHE A N 1 ATOM 1066 C CA . PHE A 1 148 ? -40.879 5.020 87.997 1.00 29.26 ? 148 PHE A CA 1 ATOM 1067 C C . PHE A 1 148 ? -39.364 4.906 88.140 1.00 29.28 ? 148 PHE A C 1 ATOM 1068 O O . PHE A 1 148 ? -38.798 5.364 89.129 1.00 29.58 ? 148 PHE A O 1 ATOM 1069 C CB . PHE A 1 148 ? -41.236 6.482 87.729 1.00 29.75 ? 148 PHE A CB 1 ATOM 1070 C CG . PHE A 1 148 ? -42.708 6.718 87.518 1.00 29.49 ? 148 PHE A CG 1 ATOM 1071 C CD1 . PHE A 1 148 ? -43.325 6.340 86.335 1.00 30.45 ? 148 PHE A CD1 1 ATOM 1072 C CD2 . PHE A 1 148 ? -43.469 7.339 88.498 1.00 30.78 ? 148 PHE A CD2 1 ATOM 1073 C CE1 . PHE A 1 148 ? -44.684 6.564 86.132 1.00 30.25 ? 148 PHE A CE1 1 ATOM 1074 C CE2 . PHE A 1 148 ? -44.819 7.579 88.306 1.00 31.03 ? 148 PHE A CE2 1 ATOM 1075 C CZ . PHE A 1 148 ? -45.436 7.187 87.112 1.00 31.14 ? 148 PHE A CZ 1 ATOM 1076 N N . SER A 1 149 ? -38.703 4.308 87.153 1.00 28.79 ? 149 SER A N 1 ATOM 1077 C CA . SER A 1 149 ? -37.258 4.054 87.240 1.00 28.95 ? 149 SER A CA 1 ATOM 1078 C C . SER A 1 149 ? -36.416 5.319 87.335 1.00 28.61 ? 149 SER A C 1 ATOM 1079 O O . SER A 1 149 ? -35.366 5.313 87.984 1.00 26.97 ? 149 SER A O 1 ATOM 1080 C CB . SER A 1 149 ? -36.780 3.237 86.043 1.00 28.95 ? 149 SER A CB 1 ATOM 1081 O OG . SER A 1 149 ? -36.870 3.993 84.850 1.00 27.67 ? 149 SER A OG 1 ATOM 1082 N N . ARG A 1 150 ? -36.861 6.400 86.696 1.00 26.03 ? 150 ARG A N 1 ATOM 1083 C CA . ARG A 1 150 ? -36.030 7.590 86.626 1.00 26.48 ? 150 ARG A CA 1 ATOM 1084 C C . ARG A 1 150 ? -36.351 8.603 87.718 1.00 26.37 ? 150 ARG A C 1 ATOM 1085 O O . ARG A 1 150 ? -35.745 9.675 87.751 1.00 26.23 ? 150 ARG A O 1 ATOM 1086 C CB . ARG A 1 150 ? -36.124 8.247 85.236 1.00 25.79 ? 150 ARG A CB 1 ATOM 1087 C CG . ARG A 1 150 ? -35.907 7.268 84.088 1.00 25.58 ? 150 ARG A CG 1 ATOM 1088 C CD . ARG A 1 150 ? -34.583 6.555 84.215 1.00 26.15 ? 150 ARG A CD 1 ATOM 1089 N NE . ARG A 1 150 ? -34.168 5.971 82.949 1.00 25.67 ? 150 ARG A NE 1 ATOM 1090 C CZ . ARG A 1 150 ? -33.038 5.292 82.766 1.00 25.73 ? 150 ARG A CZ 1 ATOM 1091 N NH1 . ARG A 1 150 ? -32.206 5.078 83.783 1.00 25.90 ? 150 ARG A NH1 1 ATOM 1092 N NH2 . ARG A 1 150 ? -32.746 4.820 81.559 1.00 24.81 ? 150 ARG A NH2 1 ATOM 1093 N N . LEU A 1 151 ? -37.277 8.255 88.615 1.00 26.17 ? 151 LEU A N 1 ATOM 1094 C CA . LEU A 1 151 ? -37.677 9.154 89.687 1.00 26.37 ? 151 LEU A CA 1 ATOM 1095 C C . LEU A 1 151 ? -37.399 8.519 91.047 1.00 27.16 ? 151 LEU A C 1 ATOM 1096 O O . LEU A 1 151 ? -37.314 7.299 91.170 1.00 27.93 ? 151 LEU A O 1 ATOM 1097 C CB . LEU A 1 151 ? -39.145 9.517 89.559 1.00 25.79 ? 151 LEU A CB 1 ATOM 1098 C CG . LEU A 1 151 ? -39.453 10.299 88.259 1.00 25.84 ? 151 LEU A CG 1 ATOM 1099 C CD1 . LEU A 1 151 ? -40.956 10.423 88.076 1.00 24.55 ? 151 LEU A CD1 1 ATOM 1100 C CD2 . LEU A 1 151 ? -38.791 11.680 88.256 1.00 25.13 ? 151 LEU A CD2 1 ATOM 1101 N N . ASN A 1 152 ? -37.284 9.372 92.054 1.00 28.44 ? 152 ASN A N 1 ATOM 1102 C CA . ASN A 1 152 ? -36.869 8.957 93.411 1.00 28.20 ? 152 ASN A CA 1 ATOM 1103 C C . ASN A 1 152 ? -37.817 9.590 94.430 1.00 28.92 ? 152 ASN A C 1 ATOM 1104 O O . ASN A 1 152 ? -37.757 10.794 94.684 1.00 29.08 ? 152 ASN A O 1 ATOM 1105 C CB . ASN A 1 152 ? -35.433 9.406 93.637 1.00 28.09 ? 152 ASN A CB 1 ATOM 1106 C CG . ASN A 1 152 ? -34.820 8.845 94.918 1.00 29.91 ? 152 ASN A CG 1 ATOM 1107 O OD1 . ASN A 1 152 ? -35.505 8.228 95.754 1.00 29.13 ? 152 ASN A OD1 1 ATOM 1108 N ND2 . ASN A 1 152 ? -33.520 9.065 95.073 1.00 29.18 ? 152 ASN A ND2 1 ATOM 1109 N N . TRP A 1 153 ? -38.721 8.777 94.967 1.00 30.08 ? 153 TRP A N 1 ATOM 1110 C CA . TRP A 1 153 ? -39.694 9.223 95.959 1.00 30.68 ? 153 TRP A CA 1 ATOM 1111 C C . TRP A 1 153 ? -39.021 9.293 97.316 1.00 32.32 ? 153 TRP A C 1 ATOM 1112 O O . TRP A 1 153 ? -38.745 8.268 97.926 1.00 33.06 ? 153 TRP A O 1 ATOM 1113 C CB . TRP A 1 153 ? -40.843 8.244 96.009 1.00 30.45 ? 153 TRP A CB 1 ATOM 1114 C CG . TRP A 1 153 ? -42.076 8.717 96.745 1.00 30.02 ? 153 TRP A CG 1 ATOM 1115 C CD1 . TRP A 1 153 ? -42.242 9.876 97.515 1.00 30.08 ? 153 TRP A CD1 1 ATOM 1116 C CD2 . TRP A 1 153 ? -43.369 8.045 96.788 1.00 29.93 ? 153 TRP A CD2 1 ATOM 1117 N NE1 . TRP A 1 153 ? -43.525 9.958 97.994 1.00 29.76 ? 153 TRP A NE1 1 ATOM 1118 C CE2 . TRP A 1 153 ? -44.252 8.893 97.590 1.00 30.11 ? 153 TRP A CE2 1 ATOM 1119 C CE3 . TRP A 1 153 ? -43.877 6.880 96.237 1.00 31.05 ? 153 TRP A CE3 1 ATOM 1120 C CZ2 . TRP A 1 153 ? -45.573 8.557 97.826 1.00 30.65 ? 153 TRP A CZ2 1 ATOM 1121 C CZ3 . TRP A 1 153 ? -45.213 6.554 96.475 1.00 31.35 ? 153 TRP A CZ3 1 ATOM 1122 C CH2 . TRP A 1 153 ? -46.043 7.376 97.251 1.00 30.81 ? 153 TRP A CH2 1 ATOM 1123 N N . LEU A 1 154 ? -38.742 10.514 97.774 1.00 32.80 ? 154 LEU A N 1 ATOM 1124 C CA . LEU A 1 154 ? -38.082 10.750 99.059 1.00 32.90 ? 154 LEU A CA 1 ATOM 1125 C C . LEU A 1 154 ? -39.144 10.894 100.146 1.00 33.58 ? 154 LEU A C 1 ATOM 1126 O O . LEU A 1 154 ? -40.185 11.531 99.933 1.00 31.04 ? 154 LEU A O 1 ATOM 1127 C CB . LEU A 1 154 ? -37.247 12.029 99.002 1.00 33.33 ? 154 LEU A CB 1 ATOM 1128 C CG . LEU A 1 154 ? -36.244 12.163 97.849 1.00 33.49 ? 154 LEU A CG 1 ATOM 1129 C CD1 . LEU A 1 154 ? -35.612 13.553 97.797 1.00 34.30 ? 154 LEU A CD1 1 ATOM 1130 C CD2 . LEU A 1 154 ? -35.183 11.092 97.957 1.00 33.22 ? 154 LEU A CD2 1 ATOM 1131 N N . THR A 1 155 ? -38.880 10.312 101.313 1.00 33.82 ? 155 THR A N 1 ATOM 1132 C CA . THR A 1 155 ? -39.789 10.440 102.448 1.00 34.98 ? 155 THR A CA 1 ATOM 1133 C C . THR A 1 155 ? -38.953 10.677 103.704 1.00 35.73 ? 155 THR A C 1 ATOM 1134 O O . THR A 1 155 ? -37.724 10.691 103.642 1.00 34.37 ? 155 THR A O 1 ATOM 1135 C CB . THR A 1 155 ? -40.689 9.187 102.617 1.00 35.46 ? 155 THR A CB 1 ATOM 1136 O OG1 . THR A 1 155 ? -39.878 8.008 102.719 1.00 36.30 ? 155 THR A OG1 1 ATOM 1137 C CG2 . THR A 1 155 ? -41.667 9.067 101.439 1.00 36.13 ? 155 THR A CG2 1 ATOM 1138 N N . HIS A 1 156 ? -39.622 10.870 104.836 1.00 37.40 ? 156 HIS A N 1 ATOM 1139 C CA . HIS A 1 156 ? -38.912 11.186 106.079 1.00 38.83 ? 156 HIS A CA 1 ATOM 1140 C C . HIS A 1 156 ? -37.980 10.083 106.496 1.00 39.36 ? 156 HIS A C 1 ATOM 1141 O O . HIS A 1 156 ? -38.149 8.919 106.091 1.00 39.08 ? 156 HIS A O 1 ATOM 1142 C CB . HIS A 1 156 ? -39.902 11.516 107.198 1.00 40.02 ? 156 HIS A CB 1 ATOM 1143 C CG . HIS A 1 156 ? -40.645 10.315 107.742 1.00 40.68 ? 156 HIS A CG 1 ATOM 1144 N ND1 . HIS A 1 156 ? -40.039 9.357 108.472 1.00 41.38 ? 156 HIS A ND1 1 ATOM 1145 C CD2 . HIS A 1 156 ? -41.991 9.955 107.659 1.00 40.79 ? 156 HIS A CD2 1 ATOM 1146 C CE1 . HIS A 1 156 ? -40.945 8.427 108.829 1.00 41.58 ? 156 HIS A CE1 1 ATOM 1147 N NE2 . HIS A 1 156 ? -42.138 8.794 108.330 1.00 41.78 ? 156 HIS A NE2 1 ATOM 1148 N N . LEU A 1 157 ? -36.981 10.461 107.300 1.00 41.82 ? 157 LEU A N 1 ATOM 1149 C CA . LEU A 1 157 ? -36.060 9.531 107.950 1.00 42.50 ? 157 LEU A CA 1 ATOM 1150 C C . LEU A 1 157 ? -36.192 9.763 109.456 1.00 44.55 ? 157 LEU A C 1 ATOM 1151 O O . LEU A 1 157 ? -35.932 10.872 109.936 1.00 43.72 ? 157 LEU A O 1 ATOM 1152 C CB . LEU A 1 157 ? -34.627 9.813 107.511 1.00 42.40 ? 157 LEU A CB 1 ATOM 1153 C CG . LEU A 1 157 ? -33.534 8.957 108.149 1.00 41.60 ? 157 LEU A CG 1 ATOM 1154 C CD1 . LEU A 1 157 ? -33.675 7.505 107.709 1.00 41.20 ? 157 LEU A CD1 1 ATOM 1155 C CD2 . LEU A 1 157 ? -32.150 9.509 107.834 1.00 41.82 ? 157 LEU A CD2 1 ATOM 1156 N N . LYS A 1 158 ? -36.640 8.739 110.182 1.00 46.71 ? 158 LYS A N 1 ATOM 1157 C CA . LYS A 1 158 ? -36.858 8.844 111.635 1.00 48.67 ? 158 LYS A CA 1 ATOM 1158 C C . LYS A 1 158 ? -37.815 9.988 111.967 1.00 48.81 ? 158 LYS A C 1 ATOM 1159 O O . LYS A 1 158 ? -37.569 10.779 112.880 1.00 48.93 ? 158 LYS A O 1 ATOM 1160 C CB . LYS A 1 158 ? -35.528 9.059 112.371 1.00 50.95 ? 158 LYS A CB 1 ATOM 1161 C CG . LYS A 1 158 ? -34.431 8.061 112.037 1.00 53.19 ? 158 LYS A CG 1 ATOM 1162 C CD . LYS A 1 158 ? -34.880 6.623 112.255 1.00 56.17 ? 158 LYS A CD 1 ATOM 1163 C CE . LYS A 1 158 ? -33.765 5.773 112.853 1.00 58.15 ? 158 LYS A CE 1 ATOM 1164 N NZ . LYS A 1 158 ? -32.488 5.893 112.095 1.00 59.40 ? 158 LYS A NZ 1 ATOM 1165 N N . PHE A 1 159 ? -38.892 10.093 111.195 1.00 45.84 ? 159 PHE A N 1 ATOM 1166 C CA . PHE A 1 159 ? -39.889 11.147 111.370 1.00 45.36 ? 159 PHE A CA 1 ATOM 1167 C C . PHE A 1 159 ? -39.317 12.568 111.299 1.00 44.34 ? 159 PHE A C 1 ATOM 1168 O O . PHE A 1 159 ? -39.889 13.493 111.869 1.00 42.84 ? 159 PHE A O 1 ATOM 1169 C CB . PHE A 1 159 ? -40.680 10.927 112.671 1.00 47.70 ? 159 PHE A CB 1 ATOM 1170 C CG . PHE A 1 159 ? -41.169 9.518 112.833 1.00 49.97 ? 159 PHE A CG 1 ATOM 1171 C CD1 . PHE A 1 159 ? -42.287 9.076 112.141 1.00 50.35 ? 159 PHE A CD1 1 ATOM 1172 C CD2 . PHE A 1 159 ? -40.488 8.620 113.651 1.00 51.71 ? 159 PHE A CD2 1 ATOM 1173 C CE1 . PHE A 1 159 ? -42.729 7.767 112.266 1.00 52.28 ? 159 PHE A CE1 1 ATOM 1174 C CE2 . PHE A 1 159 ? -40.925 7.311 113.787 1.00 52.50 ? 159 PHE A CE2 1 ATOM 1175 C CZ . PHE A 1 159 ? -42.048 6.882 113.092 1.00 53.42 ? 159 PHE A CZ 1 ATOM 1176 N N . LYS A 1 160 ? -38.211 12.731 110.570 1.00 44.64 ? 160 LYS A N 1 ATOM 1177 C CA . LYS A 1 160 ? -37.664 14.045 110.228 1.00 44.64 ? 160 LYS A CA 1 ATOM 1178 C C . LYS A 1 160 ? -37.486 14.185 108.699 1.00 43.15 ? 160 LYS A C 1 ATOM 1179 O O . LYS A 1 160 ? -37.093 13.239 108.014 1.00 40.21 ? 160 LYS A O 1 ATOM 1180 C CB . LYS A 1 160 ? -36.313 14.268 110.904 1.00 47.91 ? 160 LYS A CB 1 ATOM 1181 C CG . LYS A 1 160 ? -36.394 14.608 112.391 1.00 51.78 ? 160 LYS A CG 1 ATOM 1182 C CD . LYS A 1 160 ? -35.020 14.990 112.935 1.00 54.36 ? 160 LYS A CD 1 ATOM 1183 C CE . LYS A 1 160 ? -34.992 15.005 114.460 1.00 56.69 ? 160 LYS A CE 1 ATOM 1184 N NZ . LYS A 1 160 ? -35.877 16.061 115.032 1.00 57.24 ? 160 LYS A NZ 1 ATOM 1185 N N . TYR A 1 161 ? -37.764 15.379 108.192 1.00 42.44 ? 161 TYR A N 1 ATOM 1186 C CA . TYR A 1 161 ? -37.518 15.713 106.792 1.00 41.58 ? 161 TYR A CA 1 ATOM 1187 C C . TYR A 1 161 ? -36.855 17.089 106.760 1.00 41.36 ? 161 TYR A C 1 ATOM 1188 O O . TYR A 1 161 ? -37.534 18.113 106.654 1.00 40.19 ? 161 TYR A O 1 ATOM 1189 C CB . TYR A 1 161 ? -38.836 15.688 106.013 1.00 41.98 ? 161 TYR A CB 1 ATOM 1190 C CG . TYR A 1 161 ? -38.693 15.653 104.494 1.00 40.41 ? 161 TYR A CG 1 ATOM 1191 C CD1 . TYR A 1 161 ? -38.129 16.719 103.795 1.00 40.55 ? 161 TYR A CD1 1 ATOM 1192 C CD2 . TYR A 1 161 ? -39.152 14.555 103.758 1.00 40.04 ? 161 TYR A CD2 1 ATOM 1193 C CE1 . TYR A 1 161 ? -38.013 16.691 102.402 1.00 39.89 ? 161 TYR A CE1 1 ATOM 1194 C CE2 . TYR A 1 161 ? -39.042 14.521 102.369 1.00 39.73 ? 161 TYR A CE2 1 ATOM 1195 C CZ . TYR A 1 161 ? -38.469 15.589 101.697 1.00 39.85 ? 161 TYR A CZ 1 ATOM 1196 O OH . TYR A 1 161 ? -38.364 15.564 100.315 1.00 39.10 ? 161 TYR A OH 1 ATOM 1197 N N . PRO A 1 162 ? -35.520 17.120 106.875 1.00 41.58 ? 162 PRO A N 1 ATOM 1198 C CA . PRO A 1 162 ? -34.819 18.397 106.902 1.00 42.88 ? 162 PRO A CA 1 ATOM 1199 C C . PRO A 1 162 ? -34.889 19.063 105.540 1.00 43.22 ? 162 PRO A C 1 ATOM 1200 O O . PRO A 1 162 ? -34.870 18.374 104.528 1.00 43.83 ? 162 PRO A O 1 ATOM 1201 C CB . PRO A 1 162 ? -33.377 18.009 107.238 1.00 43.38 ? 162 PRO A CB 1 ATOM 1202 C CG . PRO A 1 162 ? -33.231 16.618 106.744 1.00 43.99 ? 162 PRO A CG 1 ATOM 1203 C CD . PRO A 1 162 ? -34.590 15.979 106.820 1.00 43.80 ? 162 PRO A CD 1 ATOM 1204 N N . ALA A 1 163 ? -34.980 20.387 105.530 1.00 43.30 ? 163 ALA A N 1 ATOM 1205 C CA . ALA A 1 163 ? -35.139 21.149 104.304 1.00 44.05 ? 163 ALA A CA 1 ATOM 1206 C C . ALA A 1 163 ? -34.055 20.768 103.313 1.00 43.81 ? 163 ALA A C 1 ATOM 1207 O O . ALA A 1 163 ? -32.879 20.780 103.654 1.00 42.63 ? 163 ALA A O 1 ATOM 1208 C CB . ALA A 1 163 ? -35.076 22.641 104.598 1.00 45.84 ? 163 ALA A CB 1 ATOM 1209 N N . LEU A 1 164 ? -34.457 20.413 102.093 1.00 42.24 ? 164 LEU A N 1 ATOM 1210 C CA . LEU A 1 164 ? -33.500 20.086 101.046 1.00 41.57 ? 164 LEU A CA 1 ATOM 1211 C C . LEU A 1 164 ? -33.106 21.353 100.322 1.00 39.55 ? 164 LEU A C 1 ATOM 1212 O O . LEU A 1 164 ? -33.955 22.152 99.945 1.00 39.28 ? 164 LEU A O 1 ATOM 1213 C CB . LEU A 1 164 ? -34.091 19.083 100.055 1.00 41.34 ? 164 LEU A CB 1 ATOM 1214 C CG . LEU A 1 164 ? -34.483 17.739 100.664 1.00 42.82 ? 164 LEU A CG 1 ATOM 1215 C CD1 . LEU A 1 164 ? -35.268 16.919 99.651 1.00 42.49 ? 164 LEU A CD1 1 ATOM 1216 C CD2 . LEU A 1 164 ? -33.248 16.989 101.160 1.00 43.26 ? 164 LEU A CD2 1 ATOM 1217 N N . ASN A 1 165 ? -31.809 21.531 100.144 1.00 38.91 ? 165 ASN A N 1 ATOM 1218 C CA . ASN A 1 165 ? -31.271 22.636 99.386 1.00 40.89 ? 165 ASN A CA 1 ATOM 1219 C C . ASN A 1 165 ? -30.086 22.076 98.615 1.00 41.60 ? 165 ASN A C 1 ATOM 1220 O O . ASN A 1 165 ? -28.934 22.164 99.050 1.00 42.50 ? 165 ASN A O 1 ATOM 1221 C CB . ASN A 1 165 ? -30.885 23.795 100.310 1.00 42.38 ? 165 ASN A CB 1 ATOM 1222 C CG . ASN A 1 165 ? -30.335 24.986 99.550 1.00 44.07 ? 165 ASN A CG 1 ATOM 1223 O OD1 . ASN A 1 165 ? -30.978 25.512 98.636 1.00 44.71 ? 165 ASN A OD1 1 ATOM 1224 N ND2 . ASN A 1 165 ? -29.140 25.419 99.926 1.00 45.91 ? 165 ASN A ND2 1 ATOM 1225 N N . VAL A 1 166 ? -30.390 21.468 97.469 1.00 41.71 ? 166 VAL A N 1 ATOM 1226 C CA . VAL A 1 166 ? -29.447 20.582 96.786 1.00 40.14 ? 166 VAL A CA 1 ATOM 1227 C C . VAL A 1 166 ? -29.108 21.093 95.401 1.00 39.95 ? 166 VAL A C 1 ATOM 1228 O O . VAL A 1 166 ? -29.965 21.616 94.686 1.00 38.04 ? 166 VAL A O 1 ATOM 1229 C CB . VAL A 1 166 ? -30.010 19.155 96.696 1.00 40.24 ? 166 VAL A CB 1 ATOM 1230 C CG1 . VAL A 1 166 ? -29.044 18.237 95.972 1.00 41.13 ? 166 VAL A CG1 1 ATOM 1231 C CG2 . VAL A 1 166 ? -30.303 18.623 98.097 1.00 41.37 ? 166 VAL A CG2 1 ATOM 1232 N N . THR A 1 167 ? -27.850 20.903 95.028 1.00 39.54 ? 167 THR A N 1 ATOM 1233 C CA . THR A 1 167 ? -27.284 21.500 93.838 1.00 41.44 ? 167 THR A CA 1 ATOM 1234 C C . THR A 1 167 ? -26.752 20.419 92.879 1.00 40.51 ? 167 THR A C 1 ATOM 1235 O O . THR A 1 167 ? -26.286 19.353 93.311 1.00 42.51 ? 167 THR A O 1 ATOM 1236 C CB . THR A 1 167 ? -26.148 22.459 94.239 1.00 44.08 ? 167 THR A CB 1 ATOM 1237 O OG1 . THR A 1 167 ? -25.988 23.463 93.240 1.00 47.95 ? 167 THR A OG1 1 ATOM 1238 C CG2 . THR A 1 167 ? -24.829 21.714 94.434 1.00 45.16 ? 167 THR A CG2 1 ATOM 1239 N N . MET A 1 168 ? -26.829 20.694 91.581 1.00 37.93 ? 168 MET A N 1 ATOM 1240 C CA . MET A 1 168 ? -26.147 19.867 90.594 1.00 37.13 ? 168 MET A CA 1 ATOM 1241 C C . MET A 1 168 ? -25.688 20.734 89.421 1.00 37.84 ? 168 MET A C 1 ATOM 1242 O O . MET A 1 168 ? -26.511 21.160 88.595 1.00 36.96 ? 168 MET A O 1 ATOM 1243 C CB . MET A 1 168 ? -27.069 18.734 90.133 1.00 36.12 ? 168 MET A CB 1 ATOM 1244 C CG . MET A 1 168 ? -26.412 17.691 89.242 1.00 35.06 ? 168 MET A CG 1 ATOM 1245 S SD . MET A 1 168 ? -25.133 16.735 90.093 1.00 35.02 ? 168 MET A SD 1 ATOM 1246 C CE . MET A 1 168 ? -26.136 15.847 91.277 1.00 35.37 ? 168 MET A CE 1 ATOM 1247 N N . PRO A 1 169 ? -24.369 21.013 89.345 1.00 38.72 ? 169 PRO A N 1 ATOM 1248 C CA . PRO A 1 169 ? -23.837 21.823 88.252 1.00 37.62 ? 169 PRO A CA 1 ATOM 1249 C C . PRO A 1 169 ? -23.823 21.067 86.933 1.00 36.06 ? 169 PRO A C 1 ATOM 1250 O O . PRO A 1 169 ? -23.634 19.850 86.915 1.00 35.01 ? 169 PRO A O 1 ATOM 1251 C CB . PRO A 1 169 ? -22.400 22.117 88.695 1.00 39.04 ? 169 PRO A CB 1 ATOM 1252 C CG . PRO A 1 169 ? -22.043 20.956 89.548 1.00 40.03 ? 169 PRO A CG 1 ATOM 1253 C CD . PRO A 1 169 ? -23.302 20.573 90.269 1.00 39.38 ? 169 PRO A CD 1 ATOM 1254 N N . ASN A 1 170 ? -24.050 21.794 85.843 1.00 34.89 ? 170 ASN A N 1 ATOM 1255 C CA . ASN A 1 170 ? -23.842 21.268 84.511 1.00 34.71 ? 170 ASN A CA 1 ATOM 1256 C C . ASN A 1 170 ? -22.466 21.686 84.022 1.00 34.89 ? 170 ASN A C 1 ATOM 1257 O O . ASN A 1 170 ? -22.291 22.782 83.492 1.00 33.77 ? 170 ASN A O 1 ATOM 1258 C CB . ASN A 1 170 ? -24.928 21.757 83.533 1.00 34.01 ? 170 ASN A CB 1 ATOM 1259 C CG . ASN A 1 170 ? -24.764 21.179 82.146 1.00 34.23 ? 170 ASN A CG 1 ATOM 1260 O OD1 . ASN A 1 170 ? -23.774 20.502 81.853 1.00 33.27 ? 170 ASN A OD1 1 ATOM 1261 N ND2 . ASN A 1 170 ? -25.737 21.447 81.271 1.00 33.99 ? 170 ASN A ND2 1 ATOM 1262 N N . ASN A 1 171 ? -21.501 20.787 84.185 1.00 36.91 ? 171 ASN A N 1 ATOM 1263 C CA . ASN A 1 171 ? -20.141 21.023 83.697 1.00 39.43 ? 171 ASN A CA 1 ATOM 1264 C C . ASN A 1 171 ? -19.863 20.323 82.383 1.00 40.45 ? 171 ASN A C 1 ATOM 1265 O O . ASN A 1 171 ? -18.703 20.158 81.998 1.00 40.82 ? 171 ASN A O 1 ATOM 1266 C CB . ASN A 1 171 ? -19.128 20.630 84.774 1.00 40.05 ? 171 ASN A CB 1 ATOM 1267 C CG . ASN A 1 171 ? -19.294 21.460 86.021 1.00 41.03 ? 171 ASN A CG 1 ATOM 1268 O OD1 . ASN A 1 171 ? -19.445 22.687 85.937 1.00 41.32 ? 171 ASN A OD1 1 ATOM 1269 N ND2 . ASN A 1 171 ? -19.309 20.808 87.181 1.00 42.10 ? 171 ASN A ND2 1 ATOM 1270 N N . GLU A 1 172 ? -20.935 19.946 81.686 1.00 39.45 ? 172 GLU A N 1 ATOM 1271 C CA . GLU A 1 172 ? -20.850 19.322 80.369 1.00 40.11 ? 172 GLU A CA 1 ATOM 1272 C C . GLU A 1 172 ? -20.916 20.407 79.317 1.00 40.22 ? 172 GLU A C 1 ATOM 1273 O O . GLU A 1 172 ? -21.209 21.562 79.630 1.00 39.02 ? 172 GLU A O 1 ATOM 1274 C CB . GLU A 1 172 ? -22.024 18.360 80.143 1.00 40.47 ? 172 GLU A CB 1 ATOM 1275 C CG . GLU A 1 172 ? -22.181 17.293 81.209 1.00 42.21 ? 172 GLU A CG 1 ATOM 1276 C CD . GLU A 1 172 ? -20.966 16.383 81.296 1.00 44.15 ? 172 GLU A CD 1 ATOM 1277 O OE1 . GLU A 1 172 ? -20.282 16.201 80.270 1.00 46.28 ? 172 GLU A OE1 1 ATOM 1278 O OE2 . GLU A 1 172 ? -20.703 15.843 82.384 1.00 44.64 ? 172 GLU A OE2 1 ATOM 1279 N N . LYS A 1 173 ? -20.661 20.032 78.069 1.00 41.07 ? 173 LYS A N 1 ATOM 1280 C CA . LYS A 1 173 ? -20.812 20.967 76.951 1.00 43.09 ? 173 LYS A CA 1 ATOM 1281 C C . LYS A 1 173 ? -22.169 20.837 76.243 1.00 40.41 ? 173 LYS A C 1 ATOM 1282 O O . LYS A 1 173 ? -22.419 21.527 75.254 1.00 39.81 ? 173 LYS A O 1 ATOM 1283 C CB . LYS A 1 173 ? -19.637 20.861 75.958 1.00 47.76 ? 173 LYS A CB 1 ATOM 1284 C CG . LYS A 1 173 ? -19.429 19.514 75.278 1.00 51.49 ? 173 LYS A CG 1 ATOM 1285 C CD . LYS A 1 173 ? -18.078 19.481 74.560 1.00 55.56 ? 173 LYS A CD 1 ATOM 1286 C CE . LYS A 1 173 ? -17.799 18.139 73.887 1.00 57.43 ? 173 LYS A CE 1 ATOM 1287 N NZ . LYS A 1 173 ? -16.371 17.993 73.470 1.00 58.93 ? 173 LYS A NZ 1 ATOM 1288 N N . PHE A 1 174 ? -23.055 19.991 76.773 1.00 38.10 ? 174 PHE A N 1 ATOM 1289 C CA . PHE A 1 174 ? -24.433 19.859 76.253 1.00 35.73 ? 174 PHE A CA 1 ATOM 1290 C C . PHE A 1 174 ? -25.488 20.202 77.321 1.00 35.16 ? 174 PHE A C 1 ATOM 1291 O O . PHE A 1 174 ? -25.182 20.250 78.521 1.00 33.72 ? 174 PHE A O 1 ATOM 1292 C CB . PHE A 1 174 ? -24.682 18.443 75.732 1.00 36.28 ? 174 PHE A CB 1 ATOM 1293 C CG . PHE A 1 174 ? -24.282 17.366 76.696 1.00 37.27 ? 174 PHE A CG 1 ATOM 1294 C CD1 . PHE A 1 174 ? -25.121 16.999 77.739 1.00 36.23 ? 174 PHE A CD1 1 ATOM 1295 C CD2 . PHE A 1 174 ? -23.055 16.726 76.569 1.00 37.91 ? 174 PHE A CD2 1 ATOM 1296 C CE1 . PHE A 1 174 ? -24.746 16.016 78.631 1.00 37.06 ? 174 PHE A CE1 1 ATOM 1297 C CE2 . PHE A 1 174 ? -22.672 15.736 77.463 1.00 38.16 ? 174 PHE A CE2 1 ATOM 1298 C CZ . PHE A 1 174 ? -23.517 15.381 78.495 1.00 38.28 ? 174 PHE A CZ 1 ATOM 1299 N N . ASP A 1 175 ? -26.732 20.409 76.881 1.00 33.38 ? 175 ASP A N 1 ATOM 1300 C CA . ASP A 1 175 ? -27.847 20.705 77.790 1.00 32.60 ? 175 ASP A CA 1 ATOM 1301 C C . ASP A 1 175 ? -28.286 19.446 78.505 1.00 31.38 ? 175 ASP A C 1 ATOM 1302 O O . ASP A 1 175 ? -28.140 18.334 77.984 1.00 32.02 ? 175 ASP A O 1 ATOM 1303 C CB . ASP A 1 175 ? -29.057 21.286 77.042 1.00 33.89 ? 175 ASP A CB 1 ATOM 1304 C CG . ASP A 1 175 ? -28.798 22.671 76.445 1.00 35.70 ? 175 ASP A CG 1 ATOM 1305 O OD1 . ASP A 1 175 ? -27.777 23.301 76.766 1.00 36.33 ? 175 ASP A OD1 1 ATOM 1306 O OD2 . ASP A 1 175 ? -29.639 23.136 75.646 1.00 35.03 ? 175 ASP A OD2 1 ATOM 1307 N N . LYS A 1 176 ? -28.822 19.622 79.709 1.00 29.46 ? 176 LYS A N 1 ATOM 1308 C CA . LYS A 1 176 ? -29.372 18.526 80.472 1.00 28.17 ? 176 LYS A CA 1 ATOM 1309 C C . LYS A 1 176 ? -30.861 18.756 80.635 1.00 27.18 ? 176 LYS A C 1 ATOM 1310 O O . LYS A 1 176 ? -31.288 19.874 80.967 1.00 26.69 ? 176 LYS A O 1 ATOM 1311 C CB . LYS A 1 176 ? -28.728 18.478 81.859 1.00 28.95 ? 176 LYS A CB 1 ATOM 1312 C CG . LYS A 1 176 ? -27.244 18.164 81.895 1.00 29.63 ? 176 LYS A CG 1 ATOM 1313 C CD . LYS A 1 176 ? -26.787 18.179 83.350 1.00 30.96 ? 176 LYS A CD 1 ATOM 1314 C CE . LYS A 1 176 ? -25.326 17.805 83.560 1.00 31.43 ? 176 LYS A CE 1 ATOM 1315 N NZ . LYS A 1 176 ? -24.981 17.828 85.022 1.00 32.00 ? 176 LYS A NZ 1 ATOM 1316 N N . LEU A 1 177 ? -31.646 17.704 80.422 1.00 25.69 ? 177 LEU A N 1 ATOM 1317 C CA . LEU A 1 177 ? -33.092 17.751 80.636 1.00 24.37 ? 177 LEU A CA 1 ATOM 1318 C C . LEU A 1 177 ? -33.407 16.982 81.889 1.00 23.82 ? 177 LEU A C 1 ATOM 1319 O O . LEU A 1 177 ? -33.188 15.774 81.950 1.00 23.70 ? 177 LEU A O 1 ATOM 1320 C CB . LEU A 1 177 ? -33.877 17.156 79.434 1.00 23.81 ? 177 LEU A CB 1 ATOM 1321 C CG . LEU A 1 177 ? -35.387 16.921 79.611 1.00 23.57 ? 177 LEU A CG 1 ATOM 1322 C CD1 . LEU A 1 177 ? -36.078 18.260 79.815 1.00 23.49 ? 177 LEU A CD1 1 ATOM 1323 C CD2 . LEU A 1 177 ? -36.014 16.174 78.424 1.00 23.65 ? 177 LEU A CD2 1 ATOM 1324 N N . TYR A 1 178 ? -33.921 17.686 82.892 1.00 24.46 ? 178 TYR A N 1 ATOM 1325 C CA . TYR A 1 178 ? -34.327 17.073 84.159 1.00 25.02 ? 178 TYR A CA 1 ATOM 1326 C C . TYR A 1 178 ? -35.829 16.930 84.225 1.00 24.56 ? 178 TYR A C 1 ATOM 1327 O O . TYR A 1 178 ? -36.542 17.898 83.979 1.00 24.72 ? 178 TYR A O 1 ATOM 1328 C CB . TYR A 1 178 ? -33.861 17.923 85.355 1.00 25.28 ? 178 TYR A CB 1 ATOM 1329 C CG . TYR A 1 178 ? -32.377 17.829 85.617 1.00 25.65 ? 178 TYR A CG 1 ATOM 1330 C CD1 . TYR A 1 178 ? -31.854 16.781 86.365 1.00 26.68 ? 178 TYR A CD1 1 ATOM 1331 C CD2 . TYR A 1 178 ? -31.496 18.784 85.122 1.00 25.73 ? 178 TYR A CD2 1 ATOM 1332 C CE1 . TYR A 1 178 ? -30.489 16.684 86.617 1.00 27.28 ? 178 TYR A CE1 1 ATOM 1333 C CE2 . TYR A 1 178 ? -30.136 18.702 85.371 1.00 27.04 ? 178 TYR A CE2 1 ATOM 1334 C CZ . TYR A 1 178 ? -29.632 17.640 86.114 1.00 27.40 ? 178 TYR A CZ 1 ATOM 1335 O OH . TYR A 1 178 ? -28.271 17.550 86.373 1.00 28.52 ? 178 TYR A OH 1 ATOM 1336 N N . ILE A 1 179 ? -36.284 15.728 84.572 1.00 24.33 ? 179 ILE A N 1 ATOM 1337 C CA . ILE A 1 179 ? -37.694 15.435 84.814 1.00 24.49 ? 179 ILE A CA 1 ATOM 1338 C C . ILE A 1 179 ? -37.909 15.171 86.304 1.00 25.59 ? 179 ILE A C 1 ATOM 1339 O O . ILE A 1 179 ? -37.207 14.328 86.934 1.00 24.67 ? 179 ILE A O 1 ATOM 1340 C CB . ILE A 1 179 ? -38.142 14.181 84.028 1.00 24.71 ? 179 ILE A CB 1 ATOM 1341 C CG1 . ILE A 1 179 ? -37.794 14.293 82.538 1.00 24.02 ? 179 ILE A CG1 1 ATOM 1342 C CG2 . ILE A 1 179 ? -39.635 13.945 84.193 1.00 24.49 ? 179 ILE A CG2 1 ATOM 1343 C CD1 . ILE A 1 179 ? -38.454 15.464 81.809 1.00 23.03 ? 179 ILE A CD1 1 ATOM 1344 N N . TRP A 1 180 ? -38.885 15.867 86.876 1.00 25.82 ? 180 TRP A N 1 ATOM 1345 C CA . TRP A 1 180 ? -39.150 15.751 88.305 1.00 26.28 ? 180 TRP A CA 1 ATOM 1346 C C . TRP A 1 180 ? -40.605 15.929 88.591 1.00 26.58 ? 180 TRP A C 1 ATOM 1347 O O . TRP A 1 180 ? -41.398 16.174 87.676 1.00 26.96 ? 180 TRP A O 1 ATOM 1348 C CB . TRP A 1 180 ? -38.269 16.734 89.075 1.00 26.21 ? 180 TRP A CB 1 ATOM 1349 C CG . TRP A 1 180 ? -38.381 18.159 88.612 1.00 25.87 ? 180 TRP A CG 1 ATOM 1350 C CD1 . TRP A 1 180 ? -37.654 18.781 87.604 1.00 26.25 ? 180 TRP A CD1 1 ATOM 1351 C CD2 . TRP A 1 180 ? -39.280 19.191 89.131 1.00 25.91 ? 180 TRP A CD2 1 ATOM 1352 N NE1 . TRP A 1 180 ? -38.036 20.087 87.458 1.00 26.92 ? 180 TRP A NE1 1 ATOM 1353 C CE2 . TRP A 1 180 ? -39.008 20.401 88.350 1.00 26.59 ? 180 TRP A CE2 1 ATOM 1354 C CE3 . TRP A 1 180 ? -40.248 19.234 90.126 1.00 25.80 ? 180 TRP A CE3 1 ATOM 1355 C CZ2 . TRP A 1 180 ? -39.689 21.594 88.576 1.00 26.77 ? 180 TRP A CZ2 1 ATOM 1356 C CZ3 . TRP A 1 180 ? -40.924 20.437 90.346 1.00 26.44 ? 180 TRP A CZ3 1 ATOM 1357 C CH2 . TRP A 1 180 ? -40.661 21.586 89.580 1.00 26.32 ? 180 TRP A CH2 1 ATOM 1358 N N . GLY A 1 181 ? -41.000 15.780 89.852 1.00 27.10 ? 181 GLY A N 1 ATOM 1359 C CA . GLY A 1 181 ? -42.415 15.837 90.181 1.00 27.73 ? 181 GLY A CA 1 ATOM 1360 C C . GLY A 1 181 ? -42.766 16.236 91.596 1.00 29.10 ? 181 GLY A C 1 ATOM 1361 O O . GLY A 1 181 ? -41.893 16.325 92.466 1.00 29.42 ? 181 GLY A O 1 ATOM 1362 N N . VAL A 1 182 ? -44.061 16.455 91.808 1.00 29.51 ? 182 VAL A N 1 ATOM 1363 C CA . VAL A 1 182 ? -44.612 16.821 93.108 1.00 29.86 ? 182 VAL A CA 1 ATOM 1364 C C . VAL A 1 182 ? -45.681 15.800 93.450 1.00 30.10 ? 182 VAL A C 1 ATOM 1365 O O . VAL A 1 182 ? -46.518 15.475 92.615 1.00 28.67 ? 182 VAL A O 1 ATOM 1366 C CB . VAL A 1 182 ? -45.250 18.222 93.075 1.00 31.07 ? 182 VAL A CB 1 ATOM 1367 C CG1 . VAL A 1 182 ? -45.885 18.566 94.422 1.00 31.77 ? 182 VAL A CG1 1 ATOM 1368 C CG2 . VAL A 1 182 ? -44.194 19.245 92.706 1.00 32.98 ? 182 VAL A CG2 1 ATOM 1369 N N . HIS A 1 183 ? -45.646 15.302 94.677 1.00 30.91 ? 183 HIS A N 1 ATOM 1370 C CA . HIS A 1 183 ? -46.634 14.345 95.149 1.00 32.09 ? 183 HIS A CA 1 ATOM 1371 C C . HIS A 1 183 ? -47.735 15.060 95.887 1.00 33.18 ? 183 HIS A C 1 ATOM 1372 O O . HIS A 1 183 ? -47.467 15.797 96.858 1.00 31.63 ? 183 HIS A O 1 ATOM 1373 C CB . HIS A 1 183 ? -45.971 13.318 96.061 1.00 32.85 ? 183 HIS A CB 1 ATOM 1374 C CG . HIS A 1 183 ? -46.910 12.255 96.549 1.00 34.14 ? 183 HIS A CG 1 ATOM 1375 N ND1 . HIS A 1 183 ? -47.241 12.119 97.853 1.00 35.30 ? 183 HIS A ND1 1 ATOM 1376 C CD2 . HIS A 1 183 ? -47.621 11.272 95.856 1.00 35.46 ? 183 HIS A CD2 1 ATOM 1377 C CE1 . HIS A 1 183 ? -48.106 11.089 97.990 1.00 35.34 ? 183 HIS A CE1 1 ATOM 1378 N NE2 . HIS A 1 183 ? -48.338 10.571 96.767 1.00 35.47 ? 183 HIS A NE2 1 ATOM 1379 N N . HIS A 1 184 ? -48.970 14.853 95.417 1.00 32.54 ? 184 HIS A N 1 ATOM 1380 C CA . HIS A 1 184 ? -50.175 15.438 95.992 1.00 32.60 ? 184 HIS A CA 1 ATOM 1381 C C . HIS A 1 184 ? -50.869 14.367 96.799 1.00 33.77 ? 184 HIS A C 1 ATOM 1382 O O . HIS A 1 184 ? -51.583 13.519 96.246 1.00 33.62 ? 184 HIS A O 1 ATOM 1383 C CB . HIS A 1 184 ? -51.113 15.933 94.891 1.00 32.60 ? 184 HIS A CB 1 ATOM 1384 C CG . HIS A 1 184 ? -50.525 17.007 93.990 1.00 32.28 ? 184 HIS A CG 1 ATOM 1385 N ND1 . HIS A 1 184 ? -50.428 18.299 94.363 1.00 31.96 ? 184 HIS A ND1 1 ATOM 1386 C CD2 . HIS A 1 184 ? -50.059 16.944 92.666 1.00 32.00 ? 184 HIS A CD2 1 ATOM 1387 C CE1 . HIS A 1 184 ? -49.910 19.032 93.338 1.00 33.04 ? 184 HIS A CE1 1 ATOM 1388 N NE2 . HIS A 1 184 ? -49.690 18.202 92.301 1.00 31.36 ? 184 HIS A NE2 1 ATOM 1389 N N . PRO A 1 185 ? -50.663 14.358 98.130 1.00 34.19 ? 185 PRO A N 1 ATOM 1390 C CA . PRO A 1 185 ? -51.258 13.257 98.910 1.00 33.50 ? 185 PRO A CA 1 ATOM 1391 C C . PRO A 1 185 ? -52.790 13.325 99.058 1.00 32.90 ? 185 PRO A C 1 ATOM 1392 O O . PRO A 1 185 ? -53.375 14.404 99.050 1.00 33.53 ? 185 PRO A O 1 ATOM 1393 C CB . PRO A 1 185 ? -50.570 13.372 100.277 1.00 33.92 ? 185 PRO A CB 1 ATOM 1394 C CG . PRO A 1 185 ? -49.391 14.269 100.068 1.00 34.02 ? 185 PRO A CG 1 ATOM 1395 C CD . PRO A 1 185 ? -49.777 15.198 98.954 1.00 34.43 ? 185 PRO A CD 1 ATOM 1396 N N . GLY A 1 186 ? -53.418 12.163 99.187 1.00 33.90 ? 186 GLY A N 1 ATOM 1397 C CA . GLY A 1 186 ? -54.861 12.066 99.349 1.00 35.62 ? 186 GLY A CA 1 ATOM 1398 C C . GLY A 1 186 ? -55.374 12.788 100.583 1.00 37.39 ? 186 GLY A C 1 ATOM 1399 O O . GLY A 1 186 ? -56.376 13.494 100.510 1.00 37.56 ? 186 GLY A O 1 ATOM 1400 N N . THR A 1 187 ? -54.672 12.624 101.709 1.00 38.98 ? 187 THR A N 1 ATOM 1401 C CA . THR A 1 187 ? -55.103 13.187 103.002 1.00 41.00 ? 187 THR A CA 1 ATOM 1402 C C . THR A 1 187 ? -53.954 13.784 103.829 1.00 41.42 ? 187 THR A C 1 ATOM 1403 O O . THR A 1 187 ? -52.773 13.496 103.589 1.00 41.27 ? 187 THR A O 1 ATOM 1404 C CB . THR A 1 187 ? -55.766 12.100 103.879 1.00 41.49 ? 187 THR A CB 1 ATOM 1405 O OG1 . THR A 1 187 ? -54.775 11.148 104.289 1.00 40.54 ? 187 THR A OG1 1 ATOM 1406 C CG2 . THR A 1 187 ? -56.886 11.376 103.129 1.00 40.65 ? 187 THR A CG2 1 ATOM 1407 N N . ASP A 1 188 ? -54.317 14.594 104.822 1.00 42.72 ? 188 ASP A N 1 ATOM 1408 C CA . ASP A 1 188 ? -53.361 15.105 105.817 1.00 45.50 ? 188 ASP A CA 1 ATOM 1409 C C . ASP A 1 188 ? -52.596 13.971 106.500 1.00 44.53 ? 188 ASP A C 1 ATOM 1410 O O . ASP A 1 188 ? -51.405 14.095 106.795 1.00 43.24 ? 188 ASP A O 1 ATOM 1411 C CB . ASP A 1 188 ? -54.086 15.936 106.884 1.00 48.19 ? 188 ASP A CB 1 ATOM 1412 C CG . ASP A 1 188 ? -54.561 17.277 106.362 1.00 49.76 ? 188 ASP A CG 1 ATOM 1413 O OD1 . ASP A 1 188 ? -53.875 17.870 105.500 1.00 50.45 ? 188 ASP A OD1 1 ATOM 1414 O OD2 . ASP A 1 188 ? -55.623 17.743 106.829 1.00 53.59 ? 188 ASP A OD2 1 ATOM 1415 N N . ASN A 1 189 ? -53.287 12.861 106.734 1.00 44.78 ? 189 ASN A N 1 ATOM 1416 C CA . ASN A 1 189 ? -52.664 11.677 107.319 1.00 46.94 ? 189 ASN A CA 1 ATOM 1417 C C . ASN A 1 189 ? -51.503 11.164 106.462 1.00 45.15 ? 189 ASN A C 1 ATOM 1418 O O . ASN A 1 189 ? -50.443 10.822 106.990 1.00 43.20 ? 189 ASN A O 1 ATOM 1419 C CB . ASN A 1 189 ? -53.711 10.573 107.517 1.00 49.51 ? 189 ASN A CB 1 ATOM 1420 C CG . ASN A 1 189 ? -53.264 9.508 108.503 1.00 53.02 ? 189 ASN A CG 1 ATOM 1421 O OD1 . ASN A 1 189 ? -52.140 9.006 108.438 1.00 55.74 ? 189 ASN A OD1 1 ATOM 1422 N ND2 . ASN A 1 189 ? -54.154 9.148 109.419 1.00 56.24 ? 189 ASN A ND2 1 ATOM 1423 N N . ASP A 1 190 ? -51.705 11.117 105.141 1.00 43.20 ? 190 ASP A N 1 ATOM 1424 C CA . ASP A 1 190 ? -50.643 10.687 104.222 1.00 40.59 ? 190 ASP A CA 1 ATOM 1425 C C . ASP A 1 190 ? -49.490 11.678 104.236 1.00 37.81 ? 190 ASP A C 1 ATOM 1426 O O . ASP A 1 190 ? -48.333 11.283 104.180 1.00 36.05 ? 190 ASP A O 1 ATOM 1427 C CB . ASP A 1 190 ? -51.155 10.568 102.773 1.00 41.83 ? 190 ASP A CB 1 ATOM 1428 C CG . ASP A 1 190 ? -52.258 9.541 102.613 1.00 42.53 ? 190 ASP A CG 1 ATOM 1429 O OD1 . ASP A 1 190 ? -52.069 8.355 102.991 1.00 43.34 ? 190 ASP A OD1 1 ATOM 1430 O OD2 . ASP A 1 190 ? -53.315 9.931 102.080 1.00 43.10 ? 190 ASP A OD2 1 ATOM 1431 N N . GLN A 1 191 ? -49.813 12.970 104.279 1.00 37.15 ? 191 GLN A N 1 ATOM 1432 C CA . GLN A 1 191 ? -48.793 14.022 104.276 1.00 36.36 ? 191 GLN A CA 1 ATOM 1433 C C . GLN A 1 191 ? -47.839 13.806 105.441 1.00 36.72 ? 191 GLN A C 1 ATOM 1434 O O . GLN A 1 191 ? -46.612 13.814 105.284 1.00 36.50 ? 191 GLN A O 1 ATOM 1435 C CB . GLN A 1 191 ? -49.454 15.395 104.379 1.00 35.97 ? 191 GLN A CB 1 ATOM 1436 C CG . GLN A 1 191 ? -48.516 16.590 104.461 1.00 36.15 ? 191 GLN A CG 1 ATOM 1437 C CD . GLN A 1 191 ? -47.698 16.827 103.192 1.00 37.26 ? 191 GLN A CD 1 ATOM 1438 O OE1 . GLN A 1 191 ? -48.198 16.675 102.070 1.00 37.55 ? 191 GLN A OE1 1 ATOM 1439 N NE2 . GLN A 1 191 ? -46.449 17.240 103.367 1.00 34.78 ? 191 GLN A NE2 1 ATOM 1440 N N . ILE A 1 192 ? -48.415 13.592 106.613 1.00 37.49 ? 192 ILE A N 1 ATOM 1441 C CA . ILE A 1 192 ? -47.613 13.426 107.830 1.00 37.76 ? 192 ILE A CA 1 ATOM 1442 C C . ILE A 1 192 ? -46.901 12.088 107.795 1.00 36.41 ? 192 ILE A C 1 ATOM 1443 O O . ILE A 1 192 ? -45.711 12.018 108.073 1.00 38.86 ? 192 ILE A O 1 ATOM 1444 C CB . ILE A 1 192 ? -48.482 13.594 109.103 1.00 39.09 ? 192 ILE A CB 1 ATOM 1445 C CG1 . ILE A 1 192 ? -49.118 14.987 109.132 1.00 40.02 ? 192 ILE A CG1 1 ATOM 1446 C CG2 . ILE A 1 192 ? -47.657 13.384 110.366 1.00 39.45 ? 192 ILE A CG2 1 ATOM 1447 C CD1 . ILE A 1 192 ? -48.131 16.128 108.992 1.00 40.13 ? 192 ILE A CD1 1 ATOM 1448 N N . SER A 1 193 ? -47.594 11.021 107.407 1.00 37.39 ? 193 SER A N 1 ATOM 1449 C CA . SER A 1 193 ? -46.948 9.693 107.349 1.00 37.45 ? 193 SER A CA 1 ATOM 1450 C C . SER A 1 193 ? -45.770 9.647 106.373 1.00 37.10 ? 193 SER A C 1 ATOM 1451 O O . SER A 1 193 ? -44.808 8.907 106.579 1.00 36.39 ? 193 SER A O 1 ATOM 1452 C CB . SER A 1 193 ? -47.952 8.616 106.937 1.00 39.16 ? 193 SER A CB 1 ATOM 1453 O OG . SER A 1 193 ? -49.033 8.536 107.849 1.00 41.63 ? 193 SER A OG 1 ATOM 1454 N N . LEU A 1 194 ? -45.853 10.428 105.296 1.00 35.13 ? 194 LEU A N 1 ATOM 1455 C CA . LEU A 1 194 ? -44.816 10.404 104.280 1.00 34.98 ? 194 LEU A CA 1 ATOM 1456 C C . LEU A 1 194 ? -43.671 11.376 104.573 1.00 34.90 ? 194 LEU A C 1 ATOM 1457 O O . LEU A 1 194 ? -42.500 11.022 104.404 1.00 34.40 ? 194 LEU A O 1 ATOM 1458 C CB . LEU A 1 194 ? -45.427 10.689 102.897 1.00 34.76 ? 194 LEU A CB 1 ATOM 1459 C CG . LEU A 1 194 ? -46.330 9.585 102.335 1.00 35.16 ? 194 LEU A CG 1 ATOM 1460 C CD1 . LEU A 1 194 ? -47.250 10.109 101.229 1.00 35.52 ? 194 LEU A CD1 1 ATOM 1461 C CD2 . LEU A 1 194 ? -45.483 8.413 101.844 1.00 35.89 ? 194 LEU A CD2 1 ATOM 1462 N N . TYR A 1 195 ? -43.999 12.596 105.004 1.00 35.77 ? 195 TYR A N 1 ATOM 1463 C CA . TYR A 1 195 ? -43.007 13.692 105.029 1.00 37.29 ? 195 TYR A CA 1 ATOM 1464 C C . TYR A 1 195 ? -42.757 14.310 106.422 1.00 40.75 ? 195 TYR A C 1 ATOM 1465 O O . TYR A 1 195 ? -41.836 15.123 106.591 1.00 41.15 ? 195 TYR A O 1 ATOM 1466 C CB . TYR A 1 195 ? -43.400 14.769 104.005 1.00 36.72 ? 195 TYR A CB 1 ATOM 1467 C CG . TYR A 1 195 ? -43.764 14.154 102.661 1.00 35.49 ? 195 TYR A CG 1 ATOM 1468 C CD1 . TYR A 1 195 ? -42.806 13.479 101.908 1.00 35.18 ? 195 TYR A CD1 1 ATOM 1469 C CD2 . TYR A 1 195 ? -45.081 14.190 102.176 1.00 37.10 ? 195 TYR A CD2 1 ATOM 1470 C CE1 . TYR A 1 195 ? -43.128 12.894 100.690 1.00 35.36 ? 195 TYR A CE1 1 ATOM 1471 C CE2 . TYR A 1 195 ? -45.416 13.601 100.960 1.00 35.66 ? 195 TYR A CE2 1 ATOM 1472 C CZ . TYR A 1 195 ? -44.431 12.955 100.225 1.00 35.59 ? 195 TYR A CZ 1 ATOM 1473 O OH . TYR A 1 195 ? -44.737 12.352 99.022 1.00 36.45 ? 195 TYR A OH 1 ATOM 1474 N N . ALA A 1 196 ? -43.582 13.934 107.400 1.00 43.34 ? 196 ALA A N 1 ATOM 1475 C CA . ALA A 1 196 ? -43.361 14.292 108.807 1.00 46.32 ? 196 ALA A CA 1 ATOM 1476 C C . ALA A 1 196 ? -43.808 15.716 109.142 1.00 48.08 ? 196 ALA A C 1 ATOM 1477 O O . ALA A 1 196 ? -43.686 16.148 110.291 1.00 50.02 ? 196 ALA A O 1 ATOM 1478 C CB . ALA A 1 196 ? -41.896 14.096 109.184 1.00 44.92 ? 196 ALA A CB 1 ATOM 1479 N N . GLN A 1 197 ? -44.333 16.443 108.160 1.00 47.19 ? 197 GLN A N 1 ATOM 1480 C CA . GLN A 1 197 ? -44.762 17.820 108.395 1.00 48.18 ? 197 GLN A CA 1 ATOM 1481 C C . GLN A 1 197 ? -45.774 18.274 107.360 1.00 47.76 ? 197 GLN A C 1 ATOM 1482 O O . GLN A 1 197 ? -46.013 17.576 106.372 1.00 46.11 ? 197 GLN A O 1 ATOM 1483 C CB . GLN A 1 197 ? -43.553 18.762 108.423 1.00 49.13 ? 197 GLN A CB 1 ATOM 1484 C CG . GLN A 1 197 ? -42.700 18.746 107.157 1.00 50.05 ? 197 GLN A CG 1 ATOM 1485 C CD . GLN A 1 197 ? -41.221 18.955 107.436 1.00 52.36 ? 197 GLN A CD 1 ATOM 1486 O OE1 . GLN A 1 197 ? -40.809 19.178 108.583 1.00 51.74 ? 197 GLN A OE1 1 ATOM 1487 N NE2 . GLN A 1 197 ? -40.408 18.867 106.387 1.00 50.26 ? 197 GLN A NE2 1 ATOM 1488 N N . ALA A 1 198 ? -46.367 19.440 107.611 1.00 47.52 ? 198 ALA A N 1 ATOM 1489 C CA . ALA A 1 198 ? -47.360 20.042 106.718 1.00 49.48 ? 198 ALA A CA 1 ATOM 1490 C C . ALA A 1 198 ? -46.764 20.334 105.337 1.00 48.01 ? 198 ALA A C 1 ATOM 1491 O O . ALA A 1 198 ? -45.554 20.533 105.198 1.00 46.97 ? 198 ALA A O 1 ATOM 1492 C CB . ALA A 1 198 ? -47.918 21.322 107.335 1.00 49.72 ? 198 ALA A CB 1 ATOM 1493 N N . SER A 1 199 ? -47.618 20.368 104.317 1.00 48.47 ? 199 SER A N 1 ATOM 1494 C CA . SER A 1 199 ? -47.137 20.511 102.946 1.00 48.49 ? 199 SER A CA 1 ATOM 1495 C C . SER A 1 199 ? -46.563 21.904 102.744 1.00 50.59 ? 199 SER A C 1 ATOM 1496 O O . SER A 1 199 ? -47.080 22.891 103.281 1.00 50.83 ? 199 SER A O 1 ATOM 1497 C CB . SER A 1 199 ? -48.246 20.218 101.926 1.00 46.20 ? 199 SER A CB 1 ATOM 1498 O OG . SER A 1 199 ? -49.326 21.123 102.059 1.00 45.53 ? 199 SER A OG 1 ATOM 1499 N N . GLY A 1 200 ? -45.471 21.959 101.990 1.00 52.20 ? 200 GLY A N 1 ATOM 1500 C CA . GLY A 1 200 ? -44.784 23.206 101.662 1.00 52.72 ? 200 GLY A CA 1 ATOM 1501 C C . GLY A 1 200 ? -44.331 23.155 100.209 1.00 54.17 ? 200 GLY A C 1 ATOM 1502 O O . GLY A 1 200 ? -44.198 22.077 99.632 1.00 56.82 ? 200 GLY A O 1 ATOM 1503 N N . ARG A 1 201 ? -44.087 24.320 99.622 1.00 50.83 ? 201 ARG A N 1 ATOM 1504 C CA . ARG A 1 201 ? -43.848 24.416 98.177 1.00 49.36 ? 201 ARG A CA 1 ATOM 1505 C C . ARG A 1 201 ? -42.496 23.831 97.771 1.00 45.81 ? 201 ARG A C 1 ATOM 1506 O O . ARG A 1 201 ? -41.596 23.699 98.600 1.00 45.30 ? 201 ARG A O 1 ATOM 1507 C CB . ARG A 1 201 ? -43.950 25.874 97.738 1.00 50.38 ? 201 ARG A CB 1 ATOM 1508 C CG . ARG A 1 201 ? -42.813 26.732 98.263 1.00 52.17 ? 201 ARG A CG 1 ATOM 1509 C CD . ARG A 1 201 ? -43.224 28.165 98.563 1.00 53.93 ? 201 ARG A CD 1 ATOM 1510 N NE . ARG A 1 201 ? -42.122 28.823 99.256 1.00 56.51 ? 201 ARG A NE 1 ATOM 1511 C CZ . ARG A 1 201 ? -41.894 28.756 100.568 1.00 57.55 ? 201 ARG A CZ 1 ATOM 1512 N NH1 . ARG A 1 201 ? -42.718 28.091 101.379 1.00 58.36 ? 201 ARG A NH1 1 ATOM 1513 N NH2 . ARG A 1 201 ? -40.838 29.377 101.078 1.00 57.37 ? 201 ARG A NH2 1 ATOM 1514 N N . ILE A 1 202 ? -42.375 23.481 96.491 1.00 39.67 ? 202 ILE A N 1 ATOM 1515 C CA . ILE A 1 202 ? -41.119 22.997 95.913 1.00 37.07 ? 202 ILE A CA 1 ATOM 1516 C C . ILE A 1 202 ? -40.627 24.032 94.918 1.00 34.92 ? 202 ILE A C 1 ATOM 1517 O O . ILE A 1 202 ? -41.402 24.490 94.078 1.00 34.11 ? 202 ILE A O 1 ATOM 1518 C CB . ILE A 1 202 ? -41.319 21.650 95.185 1.00 37.07 ? 202 ILE A CB 1 ATOM 1519 C CG1 . ILE A 1 202 ? -41.685 20.560 96.196 1.00 38.16 ? 202 ILE A CG1 1 ATOM 1520 C CG2 . ILE A 1 202 ? -40.080 21.279 94.377 1.00 35.07 ? 202 ILE A CG2 1 ATOM 1521 C CD1 . ILE A 1 202 ? -42.138 19.263 95.568 1.00 39.78 ? 202 ILE A CD1 1 ATOM 1522 N N . THR A 1 203 ? -39.356 24.411 95.014 1.00 31.93 ? 203 THR A N 1 ATOM 1523 C CA . THR A 1 203 ? -38.762 25.347 94.059 1.00 32.30 ? 203 THR A CA 1 ATOM 1524 C C . THR A 1 203 ? -37.526 24.746 93.404 1.00 32.29 ? 203 THR A C 1 ATOM 1525 O O . THR A 1 203 ? -36.576 24.335 94.081 1.00 34.02 ? 203 THR A O 1 ATOM 1526 C CB . THR A 1 203 ? -38.444 26.724 94.694 1.00 32.52 ? 203 THR A CB 1 ATOM 1527 O OG1 . THR A 1 203 ? -39.665 27.318 95.146 1.00 31.59 ? 203 THR A OG1 1 ATOM 1528 C CG2 . THR A 1 203 ? -37.792 27.684 93.662 1.00 32.10 ? 203 THR A CG2 1 ATOM 1529 N N . VAL A 1 204 ? -37.569 24.682 92.075 1.00 31.43 ? 204 VAL A N 1 ATOM 1530 C CA . VAL A 1 204 ? -36.465 24.190 91.253 1.00 30.24 ? 204 VAL A CA 1 ATOM 1531 C C . VAL A 1 204 ? -36.005 25.325 90.352 1.00 29.76 ? 204 VAL A C 1 ATOM 1532 O O . VAL A 1 204 ? -36.794 25.888 89.575 1.00 29.16 ? 204 VAL A O 1 ATOM 1533 C CB . VAL A 1 204 ? -36.876 22.968 90.402 1.00 30.48 ? 204 VAL A CB 1 ATOM 1534 C CG1 . VAL A 1 204 ? -35.705 22.501 89.545 1.00 29.37 ? 204 VAL A CG1 1 ATOM 1535 C CG2 . VAL A 1 204 ? -37.349 21.840 91.303 1.00 30.51 ? 204 VAL A CG2 1 ATOM 1536 N N . SER A 1 205 ? -34.733 25.683 90.469 1.00 30.23 ? 205 SER A N 1 ATOM 1537 C CA . SER A 1 205 ? -34.229 26.872 89.812 1.00 30.61 ? 205 SER A CA 1 ATOM 1538 C C . SER A 1 205 ? -32.875 26.675 89.171 1.00 30.99 ? 205 SER A C 1 ATOM 1539 O O . SER A 1 205 ? -32.160 25.706 89.443 1.00 31.36 ? 205 SER A O 1 ATOM 1540 C CB . SER A 1 205 ? -34.144 28.035 90.823 1.00 31.84 ? 205 SER A CB 1 ATOM 1541 O OG . SER A 1 205 ? -33.323 27.694 91.938 1.00 32.38 ? 205 SER A OG 1 ATOM 1542 N N . THR A 1 206 ? -32.559 27.616 88.292 1.00 30.25 ? 206 THR A N 1 ATOM 1543 C CA . THR A 1 206 ? -31.245 27.773 87.715 1.00 30.40 ? 206 THR A CA 1 ATOM 1544 C C . THR A 1 206 ? -30.908 29.255 87.779 1.00 30.82 ? 206 THR A C 1 ATOM 1545 O O . THR A 1 206 ? -31.707 30.063 88.266 1.00 28.70 ? 206 THR A O 1 ATOM 1546 C CB . THR A 1 206 ? -31.219 27.320 86.240 1.00 30.71 ? 206 THR A CB 1 ATOM 1547 O OG1 . THR A 1 206 ? -31.997 28.223 85.435 1.00 29.71 ? 206 THR A OG1 1 ATOM 1548 C CG2 . THR A 1 206 ? -31.768 25.908 86.109 1.00 30.46 ? 206 THR A CG2 1 ATOM 1549 N N . LYS A 1 207 ? -29.739 29.615 87.262 1.00 31.49 ? 207 LYS A N 1 ATOM 1550 C CA . LYS A 1 207 ? -29.369 31.013 87.149 1.00 34.69 ? 207 LYS A CA 1 ATOM 1551 C C . LYS A 1 207 ? -30.364 31.795 86.287 1.00 36.16 ? 207 LYS A C 1 ATOM 1552 O O . LYS A 1 207 ? -30.574 32.978 86.521 1.00 36.36 ? 207 LYS A O 1 ATOM 1553 C CB . LYS A 1 207 ? -27.977 31.160 86.550 1.00 36.47 ? 207 LYS A CB 1 ATOM 1554 C CG . LYS A 1 207 ? -26.844 30.713 87.462 1.00 38.69 ? 207 LYS A CG 1 ATOM 1555 C CD . LYS A 1 207 ? -25.514 30.965 86.767 1.00 41.13 ? 207 LYS A CD 1 ATOM 1556 C CE . LYS A 1 207 ? -24.448 29.984 87.209 1.00 43.44 ? 207 LYS A CE 1 ATOM 1557 N NZ . LYS A 1 207 ? -23.212 30.205 86.416 1.00 45.07 ? 207 LYS A NZ 1 ATOM 1558 N N . ARG A 1 208 ? -30.970 31.137 85.298 1.00 37.07 ? 208 ARG A N 1 ATOM 1559 C CA . ARG A 1 208 ? -31.830 31.826 84.340 1.00 39.04 ? 208 ARG A CA 1 ATOM 1560 C C . ARG A 1 208 ? -33.321 31.531 84.487 1.00 36.90 ? 208 ARG A C 1 ATOM 1561 O O . ARG A 1 208 ? -34.126 32.152 83.813 1.00 36.58 ? 208 ARG A O 1 ATOM 1562 C CB . ARG A 1 208 ? -31.396 31.496 82.911 1.00 42.80 ? 208 ARG A CB 1 ATOM 1563 C CG . ARG A 1 208 ? -31.622 30.041 82.538 1.00 46.83 ? 208 ARG A CG 1 ATOM 1564 C CD . ARG A 1 208 ? -31.528 29.802 81.042 1.00 51.51 ? 208 ARG A CD 1 ATOM 1565 N NE . ARG A 1 208 ? -32.029 28.464 80.715 1.00 55.97 ? 208 ARG A NE 1 ATOM 1566 C CZ . ARG A 1 208 ? -32.205 27.993 79.481 1.00 58.66 ? 208 ARG A CZ 1 ATOM 1567 N NH1 . ARG A 1 208 ? -31.921 28.747 78.419 1.00 59.79 ? 208 ARG A NH1 1 ATOM 1568 N NH2 . ARG A 1 208 ? -32.661 26.754 79.310 1.00 58.74 ? 208 ARG A NH2 1 ATOM 1569 N N . SER A 1 209 ? -33.715 30.588 85.332 1.00 34.41 ? 209 SER A N 1 ATOM 1570 C CA . SER A 1 209 ? -35.136 30.258 85.424 1.00 34.35 ? 209 SER A CA 1 ATOM 1571 C C . SER A 1 209 ? -35.521 29.674 86.763 1.00 33.16 ? 209 SER A C 1 ATOM 1572 O O . SER A 1 209 ? -34.666 29.226 87.518 1.00 31.74 ? 209 SER A O 1 ATOM 1573 C CB . SER A 1 209 ? -35.507 29.271 84.314 1.00 35.68 ? 209 SER A CB 1 ATOM 1574 O OG . SER A 1 209 ? -34.776 28.072 84.486 1.00 35.78 ? 209 SER A OG 1 ATOM 1575 N N . GLN A 1 210 ? -36.821 29.683 87.049 1.00 32.12 ? 210 GLN A N 1 ATOM 1576 C CA . GLN A 1 210 ? -37.342 29.136 88.294 1.00 32.07 ? 210 GLN A CA 1 ATOM 1577 C C . GLN A 1 210 ? -38.748 28.604 88.085 1.00 31.75 ? 210 GLN A C 1 ATOM 1578 O O . GLN A 1 210 ? -39.495 29.109 87.244 1.00 32.00 ? 210 GLN A O 1 ATOM 1579 C CB . GLN A 1 210 ? -37.359 30.199 89.402 1.00 32.45 ? 210 GLN A CB 1 ATOM 1580 C CG . GLN A 1 210 ? -38.094 31.488 89.048 1.00 33.43 ? 210 GLN A CG 1 ATOM 1581 C CD . GLN A 1 210 ? -38.200 32.470 90.215 1.00 35.52 ? 210 GLN A CD 1 ATOM 1582 O OE1 . GLN A 1 210 ? -37.977 32.104 91.364 1.00 38.54 ? 210 GLN A OE1 1 ATOM 1583 N NE2 . GLN A 1 210 ? -38.568 33.713 89.920 1.00 34.39 ? 210 GLN A NE2 1 ATOM 1584 N N . GLN A 1 211 ? -39.085 27.568 88.839 1.00 32.18 ? 211 GLN A N 1 ATOM 1585 C CA . GLN A 1 211 ? -40.443 27.062 88.921 1.00 32.37 ? 211 GLN A CA 1 ATOM 1586 C C . GLN A 1 211 ? -40.735 26.693 90.355 1.00 30.45 ? 211 GLN A C 1 ATOM 1587 O O . GLN A 1 211 ? -39.986 25.939 90.965 1.00 29.98 ? 211 GLN A O 1 ATOM 1588 C CB . GLN A 1 211 ? -40.606 25.785 88.106 1.00 34.34 ? 211 GLN A CB 1 ATOM 1589 C CG . GLN A 1 211 ? -40.361 25.897 86.617 1.00 36.33 ? 211 GLN A CG 1 ATOM 1590 C CD . GLN A 1 211 ? -40.468 24.529 85.967 1.00 37.35 ? 211 GLN A CD 1 ATOM 1591 O OE1 . GLN A 1 211 ? -39.462 23.915 85.647 1.00 37.07 ? 211 GLN A OE1 1 ATOM 1592 N NE2 . GLN A 1 211 ? -41.703 24.032 85.814 1.00 39.77 ? 211 GLN A NE2 1 ATOM 1593 N N . THR A 1 212 ? -41.850 27.184 90.872 1.00 30.11 ? 212 THR A N 1 ATOM 1594 C CA . THR A 1 212 ? -42.327 26.785 92.184 1.00 30.67 ? 212 THR A CA 1 ATOM 1595 C C . THR A 1 212 ? -43.668 26.073 92.025 1.00 30.70 ? 212 THR A C 1 ATOM 1596 O O . THR A 1 212 ? -44.556 26.566 91.333 1.00 30.18 ? 212 THR A O 1 ATOM 1597 C CB . THR A 1 212 ? -42.480 28.004 93.107 1.00 31.05 ? 212 THR A CB 1 ATOM 1598 O OG1 . THR A 1 212 ? -41.202 28.615 93.298 1.00 30.38 ? 212 THR A OG1 1 ATOM 1599 C CG2 . THR A 1 212 ? -43.064 27.590 94.471 1.00 31.41 ? 212 THR A CG2 1 ATOM 1600 N N . VAL A 1 213 ? -43.800 24.917 92.665 1.00 32.02 ? 213 VAL A N 1 ATOM 1601 C CA . VAL A 1 213 ? -45.021 24.133 92.635 1.00 32.16 ? 213 VAL A CA 1 ATOM 1602 C C . VAL A 1 213 ? -45.489 23.813 94.058 1.00 33.81 ? 213 VAL A C 1 ATOM 1603 O O . VAL A 1 213 ? -44.689 23.390 94.898 1.00 35.86 ? 213 VAL A O 1 ATOM 1604 C CB . VAL A 1 213 ? -44.792 22.813 91.884 1.00 32.29 ? 213 VAL A CB 1 ATOM 1605 C CG1 . VAL A 1 213 ? -46.064 21.978 91.904 1.00 31.70 ? 213 VAL A CG1 1 ATOM 1606 C CG2 . VAL A 1 213 ? -44.339 23.088 90.447 1.00 31.85 ? 213 VAL A CG2 1 ATOM 1607 N N . ILE A 1 214 ? -46.786 24.015 94.306 1.00 35.36 ? 214 ILE A N 1 ATOM 1608 C CA . ILE A 1 214 ? -47.424 23.771 95.606 1.00 35.24 ? 214 ILE A CA 1 ATOM 1609 C C . ILE A 1 214 ? -48.092 22.398 95.624 1.00 35.50 ? 214 ILE A C 1 ATOM 1610 O O . ILE A 1 214 ? -48.986 22.153 94.828 1.00 34.61 ? 214 ILE A O 1 ATOM 1611 C CB . ILE A 1 214 ? -48.541 24.809 95.877 1.00 37.48 ? 214 ILE A CB 1 ATOM 1612 C CG1 . ILE A 1 214 ? -47.977 26.234 95.847 1.00 37.51 ? 214 ILE A CG1 1 ATOM 1613 C CG2 . ILE A 1 214 ? -49.239 24.532 97.210 1.00 37.28 ? 214 ILE A CG2 1 ATOM 1614 C CD1 . ILE A 1 214 ? -49.041 27.281 95.591 1.00 40.19 ? 214 ILE A CD1 1 ATOM 1615 N N . PRO A 1 215 ? -47.684 21.507 96.548 1.00 35.59 ? 215 PRO A N 1 ATOM 1616 C CA . PRO A 1 215 ? -48.424 20.262 96.729 1.00 35.77 ? 215 PRO A CA 1 ATOM 1617 C C . PRO A 1 215 ? -49.819 20.556 97.276 1.00 35.77 ? 215 PRO A C 1 ATOM 1618 O O . PRO A 1 215 ? -49.960 21.416 98.142 1.00 36.58 ? 215 PRO A O 1 ATOM 1619 C CB . PRO A 1 215 ? -47.595 19.490 97.761 1.00 36.08 ? 215 PRO A CB 1 ATOM 1620 C CG . PRO A 1 215 ? -46.284 20.185 97.832 1.00 35.59 ? 215 PRO A CG 1 ATOM 1621 C CD . PRO A 1 215 ? -46.542 21.605 97.466 1.00 35.71 ? 215 PRO A CD 1 ATOM 1622 N N . ASN A 1 216 ? -50.831 19.864 96.761 1.00 34.66 ? 216 ASN A N 1 ATOM 1623 C CA . ASN A 1 216 ? -52.222 20.111 97.134 1.00 34.61 ? 216 ASN A CA 1 ATOM 1624 C C . ASN A 1 216 ? -52.841 18.827 97.652 1.00 34.65 ? 216 ASN A C 1 ATOM 1625 O O . ASN A 1 216 ? -53.113 17.897 96.887 1.00 33.70 ? 216 ASN A O 1 ATOM 1626 C CB . ASN A 1 216 ? -53.021 20.637 95.941 1.00 35.59 ? 216 ASN A CB 1 ATOM 1627 C CG . ASN A 1 216 ? -52.481 21.953 95.406 1.00 36.37 ? 216 ASN A CG 1 ATOM 1628 O OD1 . ASN A 1 216 ? -52.254 22.107 94.194 1.00 37.73 ? 216 ASN A OD1 1 ATOM 1629 N ND2 . ASN A 1 216 ? -52.294 22.915 96.298 1.00 35.05 ? 216 ASN A ND2 1 ATOM 1630 N N . ILE A 1 217 ? -53.065 18.789 98.965 1.00 33.50 ? 217 ILE A N 1 ATOM 1631 C CA . ILE A 1 217 ? -53.655 17.636 99.633 1.00 33.44 ? 217 ILE A CA 1 ATOM 1632 C C . ILE A 1 217 ? -55.138 17.516 99.307 1.00 33.06 ? 217 ILE A C 1 ATOM 1633 O O . ILE A 1 217 ? -55.876 18.499 99.332 1.00 32.42 ? 217 ILE A O 1 ATOM 1634 C CB . ILE A 1 217 ? -53.450 17.734 101.175 1.00 33.86 ? 217 ILE A CB 1 ATOM 1635 C CG1 . ILE A 1 217 ? -51.952 17.684 101.513 1.00 34.82 ? 217 ILE A CG1 1 ATOM 1636 C CG2 . ILE A 1 217 ? -54.188 16.614 101.899 1.00 33.57 ? 217 ILE A CG2 1 ATOM 1637 C CD1 . ILE A 1 217 ? -51.591 18.319 102.855 1.00 35.73 ? 217 ILE A CD1 1 ATOM 1638 N N . GLY A 1 218 ? -55.587 16.301 99.015 1.00 34.28 ? 218 GLY A N 1 ATOM 1639 C CA . GLY A 1 218 ? -56.998 16.089 98.701 1.00 35.27 ? 218 GLY A CA 1 ATOM 1640 C C . GLY A 1 218 ? -57.214 14.768 97.997 1.00 37.04 ? 218 GLY A C 1 ATOM 1641 O O . GLY A 1 218 ? -56.301 14.229 97.352 1.00 36.94 ? 218 GLY A O 1 ATOM 1642 N N . SER A 1 219 ? -58.417 14.230 98.151 1.00 36.50 ? 219 SER A N 1 ATOM 1643 C CA . SER A 1 219 ? -58.809 13.001 97.474 1.00 37.70 ? 219 SER A CA 1 ATOM 1644 C C . SER A 1 219 ? -59.071 13.286 95.996 1.00 36.61 ? 219 SER A C 1 ATOM 1645 O O . SER A 1 219 ? -59.759 14.255 95.656 1.00 36.46 ? 219 SER A O 1 ATOM 1646 C CB . SER A 1 219 ? -60.073 12.402 98.111 1.00 38.88 ? 219 SER A CB 1 ATOM 1647 O OG . SER A 1 219 ? -59.780 11.843 99.385 1.00 39.77 ? 219 SER A OG 1 ATOM 1648 N N . ARG A 1 220 ? -58.477 12.461 95.135 1.00 34.07 ? 220 ARG A N 1 ATOM 1649 C CA . ARG A 1 220 ? -58.856 12.383 93.717 1.00 33.62 ? 220 ARG A CA 1 ATOM 1650 C C . ARG A 1 220 ? -59.432 10.980 93.536 1.00 33.39 ? 220 ARG A C 1 ATOM 1651 O O . ARG A 1 220 ? -59.162 10.086 94.365 1.00 33.04 ? 220 ARG A O 1 ATOM 1652 C CB . ARG A 1 220 ? -57.636 12.576 92.805 1.00 33.19 ? 220 ARG A CB 1 ATOM 1653 C CG . ARG A 1 220 ? -57.122 14.005 92.692 1.00 33.17 ? 220 ARG A CG 1 ATOM 1654 C CD . ARG A 1 220 ? -56.226 14.404 93.860 1.00 33.56 ? 220 ARG A CD 1 ATOM 1655 N NE . ARG A 1 220 ? -55.508 15.659 93.609 1.00 33.54 ? 220 ARG A NE 1 ATOM 1656 C CZ . ARG A 1 220 ? -54.822 16.354 94.524 1.00 33.63 ? 220 ARG A CZ 1 ATOM 1657 N NH1 . ARG A 1 220 ? -54.745 15.950 95.791 1.00 33.30 ? 220 ARG A NH1 1 ATOM 1658 N NH2 . ARG A 1 220 ? -54.198 17.471 94.164 1.00 34.39 ? 220 ARG A NH2 1 ATOM 1659 N N . PRO A 1 221 ? -60.240 10.766 92.487 1.00 33.04 ? 221 PRO A N 1 ATOM 1660 C CA . PRO A 1 221 ? -60.774 9.418 92.302 1.00 33.61 ? 221 PRO A CA 1 ATOM 1661 C C . PRO A 1 221 ? -59.666 8.371 92.265 1.00 33.72 ? 221 PRO A C 1 ATOM 1662 O O . PRO A 1 221 ? -58.634 8.574 91.635 1.00 33.53 ? 221 PRO A O 1 ATOM 1663 C CB . PRO A 1 221 ? -61.506 9.521 90.967 1.00 34.03 ? 221 PRO A CB 1 ATOM 1664 C CG . PRO A 1 221 ? -61.968 10.940 90.940 1.00 33.96 ? 221 PRO A CG 1 ATOM 1665 C CD . PRO A 1 221 ? -60.815 11.710 91.512 1.00 33.01 ? 221 PRO A CD 1 ATOM 1666 N N . ARG A 1 222 ? -59.862 7.273 92.975 1.00 33.83 ? 222 ARG A N 1 ATOM 1667 C CA . ARG A 1 222 ? -58.828 6.271 93.062 1.00 35.11 ? 222 ARG A CA 1 ATOM 1668 C C . ARG A 1 222 ? -58.540 5.654 91.710 1.00 35.01 ? 222 ARG A C 1 ATOM 1669 O O . ARG A 1 222 ? -59.450 5.395 90.926 1.00 34.31 ? 222 ARG A O 1 ATOM 1670 C CB . ARG A 1 222 ? -59.196 5.192 94.083 1.00 36.85 ? 222 ARG A CB 1 ATOM 1671 C CG . ARG A 1 222 ? -59.181 5.739 95.494 1.00 38.42 ? 222 ARG A CG 1 ATOM 1672 C CD . ARG A 1 222 ? -59.238 4.648 96.545 1.00 40.14 ? 222 ARG A CD 1 ATOM 1673 N NE . ARG A 1 222 ? -59.297 5.214 97.888 1.00 41.48 ? 222 ARG A NE 1 ATOM 1674 C CZ . ARG A 1 222 ? -59.239 4.490 99.007 1.00 45.08 ? 222 ARG A CZ 1 ATOM 1675 N NH1 . ARG A 1 222 ? -59.124 3.165 98.948 1.00 44.62 ? 222 ARG A NH1 1 ATOM 1676 N NH2 . ARG A 1 222 ? -59.301 5.089 100.190 1.00 45.67 ? 222 ARG A NH2 1 ATOM 1677 N N . VAL A 1 223 ? -57.249 5.465 91.451 1.00 34.32 ? 223 VAL A N 1 ATOM 1678 C CA . VAL A 1 223 ? -56.752 4.740 90.293 1.00 35.16 ? 223 VAL A CA 1 ATOM 1679 C C . VAL A 1 223 ? -55.717 3.755 90.836 1.00 33.78 ? 223 VAL A C 1 ATOM 1680 O O . VAL A 1 223 ? -54.751 4.161 91.477 1.00 32.36 ? 223 VAL A O 1 ATOM 1681 C CB . VAL A 1 223 ? -56.085 5.693 89.275 1.00 35.29 ? 223 VAL A CB 1 ATOM 1682 C CG1 . VAL A 1 223 ? -55.322 4.912 88.211 1.00 35.21 ? 223 VAL A CG1 1 ATOM 1683 C CG2 . VAL A 1 223 ? -57.122 6.616 88.635 1.00 36.62 ? 223 VAL A CG2 1 ATOM 1684 N N . ARG A 1 224 ? -55.920 2.469 90.584 1.00 34.73 ? 224 ARG A N 1 ATOM 1685 C CA . ARG A 1 224 ? -55.074 1.422 91.174 1.00 35.75 ? 224 ARG A CA 1 ATOM 1686 C C . ARG A 1 224 ? -55.005 1.613 92.695 1.00 35.69 ? 224 ARG A C 1 ATOM 1687 O O . ARG A 1 224 ? -53.950 1.449 93.337 1.00 35.87 ? 224 ARG A O 1 ATOM 1688 C CB . ARG A 1 224 ? -53.696 1.396 90.497 1.00 36.36 ? 224 ARG A CB 1 ATOM 1689 C CG . ARG A 1 224 ? -53.775 0.859 89.073 1.00 37.23 ? 224 ARG A CG 1 ATOM 1690 C CD . ARG A 1 224 ? -52.425 0.819 88.365 1.00 37.08 ? 224 ARG A CD 1 ATOM 1691 N NE . ARG A 1 224 ? -51.931 2.149 87.981 1.00 36.74 ? 224 ARG A NE 1 ATOM 1692 C CZ . ARG A 1 224 ? -52.398 2.878 86.966 1.00 34.76 ? 224 ARG A CZ 1 ATOM 1693 N NH1 . ARG A 1 224 ? -53.416 2.448 86.240 1.00 34.03 ? 224 ARG A NH1 1 ATOM 1694 N NH2 . ARG A 1 224 ? -51.865 4.068 86.702 1.00 33.58 ? 224 ARG A NH2 1 ATOM 1695 N N . ASP A 1 225 ? -56.175 1.957 93.237 1.00 36.68 ? 225 ASP A N 1 ATOM 1696 C CA . ASP A 1 225 ? -56.408 2.221 94.654 1.00 37.41 ? 225 ASP A CA 1 ATOM 1697 C C . ASP A 1 225 ? -55.605 3.388 95.233 1.00 36.71 ? 225 ASP A C 1 ATOM 1698 O O . ASP A 1 225 ? -55.392 3.449 96.459 1.00 34.29 ? 225 ASP A O 1 ATOM 1699 C CB . ASP A 1 225 ? -56.163 0.950 95.483 1.00 39.05 ? 225 ASP A CB 1 ATOM 1700 C CG . ASP A 1 225 ? -57.000 0.919 96.763 1.00 41.15 ? 225 ASP A CG 1 ATOM 1701 O OD1 . ASP A 1 225 ? -58.163 1.411 96.737 1.00 39.58 ? 225 ASP A OD1 1 ATOM 1702 O OD2 . ASP A 1 225 ? -56.486 0.403 97.784 1.00 42.80 ? 225 ASP A OD2 1 ATOM 1703 N N . ILE A 1 226 ? -55.193 4.327 94.369 1.00 33.29 ? 226 ILE A N 1 ATOM 1704 C CA . ILE A 1 226 ? -54.423 5.488 94.806 1.00 32.63 ? 226 ILE A CA 1 ATOM 1705 C C . ILE A 1 226 ? -55.244 6.760 94.594 1.00 33.32 ? 226 ILE A C 1 ATOM 1706 O O . ILE A 1 226 ? -55.614 7.091 93.449 1.00 32.55 ? 226 ILE A O 1 ATOM 1707 C CB . ILE A 1 226 ? -53.069 5.595 94.061 1.00 31.96 ? 226 ILE A CB 1 ATOM 1708 C CG1 . ILE A 1 226 ? -52.237 4.340 94.282 1.00 32.38 ? 226 ILE A CG1 1 ATOM 1709 C CG2 . ILE A 1 226 ? -52.289 6.821 94.496 1.00 30.77 ? 226 ILE A CG2 1 ATOM 1710 C CD1 . ILE A 1 226 ? -51.983 3.982 95.743 1.00 32.35 ? 226 ILE A CD1 1 ATOM 1711 N N . PRO A 1 227 ? -55.564 7.464 95.694 1.00 32.89 ? 227 PRO A N 1 ATOM 1712 C CA . PRO A 1 227 ? -56.264 8.741 95.613 1.00 32.88 ? 227 PRO A CA 1 ATOM 1713 C C . PRO A 1 227 ? -55.307 9.934 95.544 1.00 31.26 ? 227 PRO A C 1 ATOM 1714 O O . PRO A 1 227 ? -55.744 11.057 95.327 1.00 32.92 ? 227 PRO A O 1 ATOM 1715 C CB . PRO A 1 227 ? -57.078 8.765 96.916 1.00 33.95 ? 227 PRO A CB 1 ATOM 1716 C CG . PRO A 1 227 ? -56.218 8.035 97.886 1.00 34.15 ? 227 PRO A CG 1 ATOM 1717 C CD . PRO A 1 227 ? -55.448 6.999 97.097 1.00 34.23 ? 227 PRO A CD 1 ATOM 1718 N N . SER A 1 228 ? -54.016 9.690 95.696 1.00 31.36 ? 228 SER A N 1 ATOM 1719 C CA . SER A 1 228 ? -53.008 10.733 95.533 1.00 31.34 ? 228 SER A CA 1 ATOM 1720 C C . SER A 1 228 ? -52.680 10.883 94.041 1.00 30.28 ? 228 SER A C 1 ATOM 1721 O O . SER A 1 228 ? -53.130 10.074 93.217 1.00 30.09 ? 228 SER A O 1 ATOM 1722 C CB . SER A 1 228 ? -51.735 10.371 96.301 1.00 33.42 ? 228 SER A CB 1 ATOM 1723 O OG . SER A 1 228 ? -51.970 10.205 97.694 1.00 35.97 ? 228 SER A OG 1 ATOM 1724 N N . ARG A 1 229 ? -51.903 11.911 93.706 1.00 29.70 ? 229 ARG A N 1 ATOM 1725 C CA . ARG A 1 229 ? -51.424 12.136 92.333 1.00 29.63 ? 229 ARG A CA 1 ATOM 1726 C C . ARG A 1 229 ? -49.996 12.649 92.368 1.00 30.03 ? 229 ARG A C 1 ATOM 1727 O O . ARG A 1 229 ? -49.568 13.254 93.353 1.00 32.46 ? 229 ARG A O 1 ATOM 1728 C CB . ARG A 1 229 ? -52.285 13.182 91.613 1.00 29.68 ? 229 ARG A CB 1 ATOM 1729 C CG . ARG A 1 229 ? -53.723 12.767 91.346 1.00 30.71 ? 229 ARG A CG 1 ATOM 1730 C CD . ARG A 1 229 ? -53.810 11.615 90.351 1.00 31.09 ? 229 ARG A CD 1 ATOM 1731 N NE . ARG A 1 229 ? -55.201 11.367 89.965 1.00 31.37 ? 229 ARG A NE 1 ATOM 1732 C CZ . ARG A 1 229 ? -55.993 10.418 90.463 1.00 31.91 ? 229 ARG A CZ 1 ATOM 1733 N NH1 . ARG A 1 229 ? -55.559 9.563 91.397 1.00 32.93 ? 229 ARG A NH1 1 ATOM 1734 N NH2 . ARG A 1 229 ? -57.237 10.314 90.016 1.00 31.65 ? 229 ARG A NH2 1 ATOM 1735 N N . ILE A 1 230 ? -49.255 12.383 91.301 1.00 28.53 ? 230 ILE A N 1 ATOM 1736 C CA . ILE A 1 230 ? -47.977 13.041 91.068 1.00 27.48 ? 230 ILE A CA 1 ATOM 1737 C C . ILE A 1 230 ? -48.128 13.965 89.862 1.00 26.90 ? 230 ILE A C 1 ATOM 1738 O O . ILE A 1 230 ? -48.705 13.567 88.851 1.00 25.81 ? 230 ILE A O 1 ATOM 1739 C CB . ILE A 1 230 ? -46.856 12.031 90.813 1.00 27.82 ? 230 ILE A CB 1 ATOM 1740 C CG1 . ILE A 1 230 ? -46.647 11.174 92.082 1.00 28.82 ? 230 ILE A CG1 1 ATOM 1741 C CG2 . ILE A 1 230 ? -45.581 12.766 90.426 1.00 28.15 ? 230 ILE A CG2 1 ATOM 1742 C CD1 . ILE A 1 230 ? -45.630 10.062 91.946 1.00 28.80 ? 230 ILE A CD1 1 ATOM 1743 N N . SER A 1 231 ? -47.639 15.196 89.982 1.00 26.30 ? 231 SER A N 1 ATOM 1744 C CA . SER A 1 231 ? -47.617 16.119 88.845 1.00 26.06 ? 231 SER A CA 1 ATOM 1745 C C . SER A 1 231 ? -46.173 16.273 88.362 1.00 25.86 ? 231 SER A C 1 ATOM 1746 O O . SER A 1 231 ? -45.250 16.478 89.170 1.00 25.14 ? 231 SER A O 1 ATOM 1747 C CB . SER A 1 231 ? -48.237 17.464 89.224 1.00 25.75 ? 231 SER A CB 1 ATOM 1748 O OG . SER A 1 231 ? -49.648 17.348 89.375 1.00 26.01 ? 231 SER A OG 1 ATOM 1749 N N . ILE A 1 232 ? -45.977 16.166 87.047 1.00 25.06 ? 232 ILE A N 1 ATOM 1750 C CA . ILE A 1 232 ? -44.639 16.098 86.464 1.00 24.24 ? 232 ILE A CA 1 ATOM 1751 C C . ILE A 1 232 ? -44.213 17.429 85.836 1.00 25.47 ? 232 ILE A C 1 ATOM 1752 O O . ILE A 1 232 ? -45.002 18.086 85.134 1.00 25.31 ? 232 ILE A O 1 ATOM 1753 C CB . ILE A 1 232 ? -44.556 14.980 85.407 1.00 24.86 ? 232 ILE A CB 1 ATOM 1754 C CG1 . ILE A 1 232 ? -44.768 13.607 86.047 1.00 24.85 ? 232 ILE A CG1 1 ATOM 1755 C CG2 . ILE A 1 232 ? -43.216 15.001 84.677 1.00 24.28 ? 232 ILE A CG2 1 ATOM 1756 C CD1 . ILE A 1 232 ? -43.627 13.131 86.943 1.00 25.71 ? 232 ILE A CD1 1 ATOM 1757 N N . TYR A 1 233 ? -42.955 17.806 86.079 1.00 25.54 ? 233 TYR A N 1 ATOM 1758 C CA . TYR A 1 233 ? -42.381 19.066 85.615 1.00 25.70 ? 233 TYR A CA 1 ATOM 1759 C C . TYR A 1 233 ? -41.011 18.796 85.013 1.00 25.94 ? 233 TYR A C 1 ATOM 1760 O O . TYR A 1 233 ? -40.458 17.702 85.186 1.00 25.13 ? 233 TYR A O 1 ATOM 1761 C CB . TYR A 1 233 ? -42.265 20.063 86.780 1.00 26.00 ? 233 TYR A CB 1 ATOM 1762 C CG . TYR A 1 233 ? -43.616 20.448 87.298 1.00 26.41 ? 233 TYR A CG 1 ATOM 1763 C CD1 . TYR A 1 233 ? -44.254 19.683 88.281 1.00 26.71 ? 233 TYR A CD1 1 ATOM 1764 C CD2 . TYR A 1 233 ? -44.295 21.547 86.774 1.00 27.12 ? 233 TYR A CD2 1 ATOM 1765 C CE1 . TYR A 1 233 ? -45.512 20.009 88.723 1.00 26.73 ? 233 TYR A CE1 1 ATOM 1766 C CE2 . TYR A 1 233 ? -45.555 21.884 87.217 1.00 27.39 ? 233 TYR A CE2 1 ATOM 1767 C CZ . TYR A 1 233 ? -46.157 21.110 88.192 1.00 28.04 ? 233 TYR A CZ 1 ATOM 1768 O OH . TYR A 1 233 ? -47.410 21.440 88.635 1.00 29.76 ? 233 TYR A OH 1 ATOM 1769 N N . TRP A 1 234 ? -40.469 19.774 84.288 1.00 25.61 ? 234 TRP A N 1 ATOM 1770 C CA . TRP A 1 234 ? -39.147 19.591 83.677 1.00 26.14 ? 234 TRP A CA 1 ATOM 1771 C C . TRP A 1 234 ? -38.347 20.845 83.667 1.00 25.21 ? 234 TRP A C 1 ATOM 1772 O O . TRP A 1 234 ? -38.890 21.954 83.683 1.00 26.13 ? 234 TRP A O 1 ATOM 1773 C CB . TRP A 1 234 ? -39.269 18.999 82.268 1.00 27.06 ? 234 TRP A CB 1 ATOM 1774 C CG . TRP A 1 234 ? -39.789 19.929 81.204 1.00 28.69 ? 234 TRP A CG 1 ATOM 1775 C CD1 . TRP A 1 234 ? -39.048 20.738 80.343 1.00 30.31 ? 234 TRP A CD1 1 ATOM 1776 C CD2 . TRP A 1 234 ? -41.177 20.139 80.814 1.00 30.76 ? 234 TRP A CD2 1 ATOM 1777 N NE1 . TRP A 1 234 ? -39.863 21.415 79.496 1.00 31.00 ? 234 TRP A NE1 1 ATOM 1778 C CE2 . TRP A 1 234 ? -41.153 21.102 79.727 1.00 30.77 ? 234 TRP A CE2 1 ATOM 1779 C CE3 . TRP A 1 234 ? -42.390 19.643 81.246 1.00 32.19 ? 234 TRP A CE3 1 ATOM 1780 C CZ2 . TRP A 1 234 ? -42.297 21.538 79.119 1.00 32.76 ? 234 TRP A CZ2 1 ATOM 1781 C CZ3 . TRP A 1 234 ? -43.550 20.089 80.620 1.00 33.78 ? 234 TRP A CZ3 1 ATOM 1782 C CH2 . TRP A 1 234 ? -43.503 21.021 79.584 1.00 33.61 ? 234 TRP A CH2 1 ATOM 1783 N N . THR A 1 235 ? -37.038 20.683 83.638 1.00 25.23 ? 235 THR A N 1 ATOM 1784 C CA . THR A 1 235 ? -36.133 21.809 83.639 1.00 25.15 ? 235 THR A CA 1 ATOM 1785 C C . THR A 1 235 ? -34.960 21.489 82.735 1.00 25.61 ? 235 THR A C 1 ATOM 1786 O O . THR A 1 235 ? -34.383 20.399 82.819 1.00 25.64 ? 235 THR A O 1 ATOM 1787 C CB . THR A 1 235 ? -35.613 22.115 85.077 1.00 25.57 ? 235 THR A CB 1 ATOM 1788 O OG1 . THR A 1 235 ? -36.714 22.218 85.999 1.00 24.16 ? 235 THR A OG1 1 ATOM 1789 C CG2 . THR A 1 235 ? -34.822 23.422 85.087 1.00 26.02 ? 235 THR A CG2 1 ATOM 1790 N N . ILE A 1 236 ? -34.597 22.437 81.879 1.00 25.68 ? 236 ILE A N 1 ATOM 1791 C CA . ILE A 1 236 ? -33.410 22.294 81.039 1.00 27.44 ? 236 ILE A CA 1 ATOM 1792 C C . ILE A 1 236 ? -32.290 23.142 81.632 1.00 27.85 ? 236 ILE A C 1 ATOM 1793 O O . ILE A 1 236 ? -32.487 24.330 81.913 1.00 29.83 ? 236 ILE A O 1 ATOM 1794 C CB . ILE A 1 236 ? -33.703 22.700 79.570 1.00 27.81 ? 236 ILE A CB 1 ATOM 1795 C CG1 . ILE A 1 236 ? -34.661 21.677 78.932 1.00 29.10 ? 236 ILE A CG1 1 ATOM 1796 C CG2 . ILE A 1 236 ? -32.416 22.770 78.756 1.00 28.72 ? 236 ILE A CG2 1 ATOM 1797 C CD1 . ILE A 1 236 ? -35.260 22.120 77.601 1.00 28.69 ? 236 ILE A CD1 1 ATOM 1798 N N . VAL A 1 237 ? -31.126 22.545 81.845 1.00 28.53 ? 237 VAL A N 1 ATOM 1799 C CA . VAL A 1 237 ? -29.996 23.276 82.428 1.00 29.15 ? 237 VAL A CA 1 ATOM 1800 C C . VAL A 1 237 ? -28.868 23.404 81.409 1.00 30.60 ? 237 VAL A C 1 ATOM 1801 O O . VAL A 1 237 ? -28.342 22.406 80.914 1.00 31.39 ? 237 VAL A O 1 ATOM 1802 C CB . VAL A 1 237 ? -29.503 22.579 83.712 1.00 29.63 ? 237 VAL A CB 1 ATOM 1803 C CG1 . VAL A 1 237 ? -28.335 23.335 84.331 1.00 29.90 ? 237 VAL A CG1 1 ATOM 1804 C CG2 . VAL A 1 237 ? -30.656 22.427 84.702 1.00 28.01 ? 237 VAL A CG2 1 ATOM 1805 N N . LYS A 1 238 ? -28.492 24.640 81.098 1.00 32.68 ? 238 LYS A N 1 ATOM 1806 C CA . LYS A 1 238 ? -27.440 24.916 80.119 1.00 34.16 ? 238 LYS A CA 1 ATOM 1807 C C . LYS A 1 238 ? -26.038 24.640 80.689 1.00 34.72 ? 238 LYS A C 1 ATOM 1808 O O . LYS A 1 238 ? -25.846 24.638 81.912 1.00 33.86 ? 238 LYS A O 1 ATOM 1809 C CB . LYS A 1 238 ? -27.505 26.374 79.655 1.00 36.23 ? 238 LYS A CB 1 ATOM 1810 C CG . LYS A 1 238 ? -28.874 26.850 79.191 1.00 38.36 ? 238 LYS A CG 1 ATOM 1811 C CD . LYS A 1 238 ? -29.372 26.128 77.947 1.00 38.66 ? 238 LYS A CD 1 ATOM 1812 C CE . LYS A 1 238 ? -28.620 26.594 76.712 1.00 40.10 ? 238 LYS A CE 1 ATOM 1813 N NZ . LYS A 1 238 ? -29.221 26.067 75.460 1.00 40.31 ? 238 LYS A NZ 1 ATOM 1814 N N . PRO A 1 239 ? -25.046 24.419 79.803 1.00 34.87 ? 239 PRO A N 1 ATOM 1815 C CA . PRO A 1 239 ? -23.649 24.331 80.267 1.00 35.70 ? 239 PRO A CA 1 ATOM 1816 C C . PRO A 1 239 ? -23.263 25.573 81.053 1.00 35.65 ? 239 PRO A C 1 ATOM 1817 O O . PRO A 1 239 ? -23.643 26.677 80.676 1.00 36.04 ? 239 PRO A O 1 ATOM 1818 C CB . PRO A 1 239 ? -22.844 24.262 78.959 1.00 36.36 ? 239 PRO A CB 1 ATOM 1819 C CG . PRO A 1 239 ? -23.807 23.668 77.973 1.00 36.13 ? 239 PRO A CG 1 ATOM 1820 C CD . PRO A 1 239 ? -25.148 24.242 78.344 1.00 35.49 ? 239 PRO A CD 1 ATOM 1821 N N . GLY A 1 240 ? -22.544 25.391 82.155 1.00 37.65 ? 240 GLY A N 1 ATOM 1822 C CA . GLY A 1 240 ? -22.133 26.513 82.996 1.00 38.55 ? 240 GLY A CA 1 ATOM 1823 C C . GLY A 1 240 ? -23.179 26.916 84.022 1.00 38.88 ? 240 GLY A C 1 ATOM 1824 O O . GLY A 1 240 ? -22.892 27.715 84.910 1.00 40.20 ? 240 GLY A O 1 ATOM 1825 N N . ASP A 1 241 ? -24.392 26.372 83.908 1.00 37.14 ? 241 ASP A N 1 ATOM 1826 C CA . ASP A 1 241 ? -25.464 26.672 84.852 1.00 36.24 ? 241 ASP A CA 1 ATOM 1827 C C . ASP A 1 241 ? -25.577 25.559 85.902 1.00 36.46 ? 241 ASP A C 1 ATOM 1828 O O . ASP A 1 241 ? -24.824 24.576 85.881 1.00 36.11 ? 241 ASP A O 1 ATOM 1829 C CB . ASP A 1 241 ? -26.791 26.891 84.110 1.00 35.29 ? 241 ASP A CB 1 ATOM 1830 C CG . ASP A 1 241 ? -27.735 27.861 84.840 1.00 36.25 ? 241 ASP A CG 1 ATOM 1831 O OD1 . ASP A 1 241 ? -27.643 28.015 86.100 1.00 35.36 ? 241 ASP A OD1 1 ATOM 1832 O OD2 . ASP A 1 241 ? -28.577 28.474 84.146 1.00 35.14 ? 241 ASP A OD2 1 ATOM 1833 N N . ILE A 1 242 ? -26.496 25.745 86.841 1.00 35.18 ? 242 ILE A N 1 ATOM 1834 C CA . ILE A 1 242 ? -26.620 24.881 87.997 1.00 36.79 ? 242 ILE A CA 1 ATOM 1835 C C . ILE A 1 242 ? -28.092 24.647 88.284 1.00 35.71 ? 242 ILE A C 1 ATOM 1836 O O . ILE A 1 242 ? -28.879 25.586 88.256 1.00 36.58 ? 242 ILE A O 1 ATOM 1837 C CB . ILE A 1 242 ? -25.996 25.545 89.255 1.00 39.08 ? 242 ILE A CB 1 ATOM 1838 C CG1 . ILE A 1 242 ? -24.525 25.922 89.009 1.00 41.29 ? 242 ILE A CG1 1 ATOM 1839 C CG2 . ILE A 1 242 ? -26.116 24.621 90.450 1.00 39.61 ? 242 ILE A CG2 1 ATOM 1840 C CD1 . ILE A 1 242 ? -23.910 26.788 90.101 1.00 43.56 ? 242 ILE A CD1 1 ATOM 1841 N N . LEU A 1 243 ? -28.457 23.397 88.542 1.00 33.82 ? 243 LEU A N 1 ATOM 1842 C CA . LEU A 1 243 ? -29.775 23.067 89.034 1.00 32.73 ? 243 LEU A CA 1 ATOM 1843 C C . LEU A 1 243 ? -29.787 23.164 90.561 1.00 34.10 ? 243 LEU A C 1 ATOM 1844 O O . LEU A 1 243 ? -28.938 22.571 91.231 1.00 34.29 ? 243 LEU A O 1 ATOM 1845 C CB . LEU A 1 243 ? -30.143 21.646 88.625 1.00 31.67 ? 243 LEU A CB 1 ATOM 1846 C CG . LEU A 1 243 ? -31.558 21.200 88.968 1.00 31.12 ? 243 LEU A CG 1 ATOM 1847 C CD1 . LEU A 1 243 ? -32.569 21.894 88.063 1.00 29.88 ? 243 LEU A CD1 1 ATOM 1848 C CD2 . LEU A 1 243 ? -31.667 19.691 88.857 1.00 31.02 ? 243 LEU A CD2 1 ATOM 1849 N N . LEU A 1 244 ? -30.754 23.905 91.094 1.00 34.00 ? 244 LEU A N 1 ATOM 1850 C CA . LEU A 1 244 ? -30.974 24.004 92.534 1.00 34.59 ? 244 LEU A CA 1 ATOM 1851 C C . LEU A 1 244 ? -32.383 23.519 92.898 1.00 34.33 ? 244 LEU A C 1 ATOM 1852 O O . LEU A 1 244 ? -33.395 24.048 92.408 1.00 33.63 ? 244 LEU A O 1 ATOM 1853 C CB . LEU A 1 244 ? -30.758 25.447 93.001 1.00 35.58 ? 244 LEU A CB 1 ATOM 1854 C CG . LEU A 1 244 ? -30.467 25.653 94.492 1.00 36.23 ? 244 LEU A CG 1 ATOM 1855 C CD1 . LEU A 1 244 ? -29.870 27.037 94.738 1.00 35.94 ? 244 LEU A CD1 1 ATOM 1856 C CD2 . LEU A 1 244 ? -31.721 25.439 95.323 1.00 37.30 ? 244 LEU A CD2 1 ATOM 1857 N N . ILE A 1 245 ? -32.433 22.506 93.758 1.00 33.16 ? 245 ILE A N 1 ATOM 1858 C CA . ILE A 1 245 ? -33.677 21.918 94.219 1.00 33.23 ? 245 ILE A CA 1 ATOM 1859 C C . ILE A 1 245 ? -33.889 22.218 95.707 1.00 35.34 ? 245 ILE A C 1 ATOM 1860 O O . ILE A 1 245 ? -33.027 21.929 96.547 1.00 36.41 ? 245 ILE A O 1 ATOM 1861 C CB . ILE A 1 245 ? -33.705 20.398 93.982 1.00 32.49 ? 245 ILE A CB 1 ATOM 1862 C CG1 . ILE A 1 245 ? -33.542 20.080 92.486 1.00 32.15 ? 245 ILE A CG1 1 ATOM 1863 C CG2 . ILE A 1 245 ? -35.015 19.826 94.501 1.00 32.46 ? 245 ILE A CG2 1 ATOM 1864 C CD1 . ILE A 1 245 ? -33.514 18.601 92.156 1.00 31.11 ? 245 ILE A CD1 1 ATOM 1865 N N . ASN A 1 246 ? -35.050 22.785 96.021 1.00 36.21 ? 246 ASN A N 1 ATOM 1866 C CA . ASN A 1 246 ? -35.319 23.362 97.341 1.00 37.92 ? 246 ASN A CA 1 ATOM 1867 C C . ASN A 1 246 ? -36.716 22.900 97.761 1.00 38.44 ? 246 ASN A C 1 ATOM 1868 O O . ASN A 1 246 ? -37.721 23.279 97.133 1.00 38.16 ? 246 ASN A O 1 ATOM 1869 C CB . ASN A 1 246 ? -35.204 24.886 97.222 1.00 40.53 ? 246 ASN A CB 1 ATOM 1870 C CG . ASN A 1 246 ? -35.262 25.630 98.561 1.00 44.01 ? 246 ASN A CG 1 ATOM 1871 O OD1 . ASN A 1 246 ? -35.564 26.827 98.574 1.00 45.11 ? 246 ASN A OD1 1 ATOM 1872 N ND2 . ASN A 1 246 ? -34.970 24.957 99.671 1.00 45.16 ? 246 ASN A ND2 1 ATOM 1873 N N . SER A 1 247 ? -36.781 22.057 98.793 1.00 36.42 ? 247 SER A N 1 ATOM 1874 C CA . SER A 1 247 ? -38.036 21.428 99.203 1.00 37.21 ? 247 SER A CA 1 ATOM 1875 C C . SER A 1 247 ? -38.036 20.993 100.672 1.00 38.79 ? 247 SER A C 1 ATOM 1876 O O . SER A 1 247 ? -36.995 20.613 101.218 1.00 38.68 ? 247 SER A O 1 ATOM 1877 C CB . SER A 1 247 ? -38.297 20.194 98.347 1.00 35.98 ? 247 SER A CB 1 ATOM 1878 O OG . SER A 1 247 ? -39.453 19.498 98.774 1.00 36.19 ? 247 SER A OG 1 ATOM 1879 N N . THR A 1 248 ? -39.222 21.023 101.277 1.00 38.37 ? 248 THR A N 1 ATOM 1880 C CA . THR A 1 248 ? -39.431 20.526 102.633 1.00 40.64 ? 248 THR A CA 1 ATOM 1881 C C . THR A 1 248 ? -40.354 19.311 102.644 1.00 40.00 ? 248 THR A C 1 ATOM 1882 O O . THR A 1 248 ? -40.825 18.877 103.708 1.00 39.94 ? 248 THR A O 1 ATOM 1883 C CB . THR A 1 248 ? -40.045 21.620 103.517 1.00 42.28 ? 248 THR A CB 1 ATOM 1884 O OG1 . THR A 1 248 ? -41.277 22.063 102.933 1.00 41.44 ? 248 THR A OG1 1 ATOM 1885 C CG2 . THR A 1 248 ? -39.074 22.799 103.650 1.00 42.80 ? 248 THR A CG2 1 ATOM 1886 N N . GLY A 1 249 ? -40.601 18.749 101.462 1.00 37.22 ? 249 GLY A N 1 ATOM 1887 C CA . GLY A 1 249 ? -41.444 17.562 101.336 1.00 36.29 ? 249 GLY A CA 1 ATOM 1888 C C . GLY A 1 249 ? -42.127 17.492 99.985 1.00 34.46 ? 249 GLY A C 1 ATOM 1889 O O . GLY A 1 249 ? -42.114 18.460 99.237 1.00 34.61 ? 249 GLY A O 1 ATOM 1890 N N . ASN A 1 250 ? -42.707 16.331 99.696 1.00 33.12 ? 250 ASN A N 1 ATOM 1891 C CA . ASN A 1 250 ? -43.557 16.102 98.516 1.00 32.70 ? 250 ASN A CA 1 ATOM 1892 C C . ASN A 1 250 ? -42.788 16.050 97.189 1.00 32.18 ? 250 ASN A C 1 ATOM 1893 O O . ASN A 1 250 ? -43.401 16.033 96.113 1.00 31.72 ? 250 ASN A O 1 ATOM 1894 C CB . ASN A 1 250 ? -44.682 17.139 98.442 1.00 32.15 ? 250 ASN A CB 1 ATOM 1895 C CG . ASN A 1 250 ? -45.539 17.163 99.699 1.00 32.83 ? 250 ASN A CG 1 ATOM 1896 O OD1 . ASN A 1 250 ? -45.124 17.713 100.724 1.00 34.60 ? 250 ASN A OD1 1 ATOM 1897 N ND2 . ASN A 1 250 ? -46.734 16.568 99.630 1.00 29.89 ? 250 ASN A ND2 1 ATOM 1898 N N . LEU A 1 251 ? -41.462 16.018 97.282 1.00 30.77 ? 251 LEU A N 1 ATOM 1899 C CA . LEU A 1 251 ? -40.587 15.984 96.123 1.00 30.18 ? 251 LEU A CA 1 ATOM 1900 C C . LEU A 1 251 ? -40.447 14.577 95.559 1.00 30.29 ? 251 LEU A C 1 ATOM 1901 O O . LEU A 1 251 ? -40.086 13.634 96.273 1.00 29.73 ? 251 LEU A O 1 ATOM 1902 C CB . LEU A 1 251 ? -39.201 16.516 96.490 1.00 29.20 ? 251 LEU A CB 1 ATOM 1903 C CG . LEU A 1 251 ? -38.138 16.522 95.382 1.00 29.02 ? 251 LEU A CG 1 ATOM 1904 C CD1 . LEU A 1 251 ? -38.494 17.509 94.279 1.00 28.02 ? 251 LEU A CD1 1 ATOM 1905 C CD2 . LEU A 1 251 ? -36.767 16.842 95.968 1.00 27.86 ? 251 LEU A CD2 1 ATOM 1906 N N . ILE A 1 252 ? -40.721 14.459 94.257 1.00 28.58 ? 252 ILE A N 1 ATOM 1907 C CA . ILE A 1 252 ? -40.379 13.288 93.481 1.00 27.84 ? 252 ILE A CA 1 ATOM 1908 C C . ILE A 1 252 ? -39.151 13.702 92.685 1.00 27.75 ? 252 ILE A C 1 ATOM 1909 O O . ILE A 1 252 ? -39.230 14.453 91.681 1.00 27.14 ? 252 ILE A O 1 ATOM 1910 C CB . ILE A 1 252 ? -41.521 12.870 92.545 1.00 28.39 ? 252 ILE A CB 1 ATOM 1911 C CG1 . ILE A 1 252 ? -42.805 12.611 93.350 1.00 28.24 ? 252 ILE A CG1 1 ATOM 1912 C CG2 . ILE A 1 252 ? -41.141 11.612 91.754 1.00 27.53 ? 252 ILE A CG2 1 ATOM 1913 C CD1 . ILE A 1 252 ? -42.665 11.528 94.419 1.00 28.02 ? 252 ILE A CD1 1 ATOM 1914 N N . ALA A 1 253 ? -38.006 13.235 93.156 1.00 26.92 ? 253 ALA A N 1 ATOM 1915 C CA . ALA A 1 253 ? -36.738 13.756 92.716 1.00 27.80 ? 253 ALA A CA 1 ATOM 1916 C C . ALA A 1 253 ? -36.217 13.036 91.479 1.00 27.01 ? 253 ALA A C 1 ATOM 1917 O O . ALA A 1 253 ? -36.473 11.837 91.303 1.00 27.03 ? 253 ALA A O 1 ATOM 1918 C CB . ALA A 1 253 ? -35.709 13.661 93.841 1.00 27.58 ? 253 ALA A CB 1 ATOM 1919 N N . PRO A 1 254 ? -35.433 13.756 90.659 1.00 27.27 ? 254 PRO A N 1 ATOM 1920 C CA . PRO A 1 254 ? -34.751 13.169 89.513 1.00 27.78 ? 254 PRO A CA 1 ATOM 1921 C C . PRO A 1 254 ? -33.585 12.305 89.968 1.00 28.62 ? 254 PRO A C 1 ATOM 1922 O O . PRO A 1 254 ? -32.972 12.598 91.014 1.00 27.76 ? 254 PRO A O 1 ATOM 1923 C CB . PRO A 1 254 ? -34.231 14.386 88.755 1.00 28.09 ? 254 PRO A CB 1 ATOM 1924 C CG . PRO A 1 254 ? -33.988 15.403 89.815 1.00 28.39 ? 254 PRO A CG 1 ATOM 1925 C CD . PRO A 1 254 ? -35.069 15.174 90.842 1.00 27.53 ? 254 PRO A CD 1 ATOM 1926 N N . ARG A 1 255 ? -33.277 11.264 89.193 1.00 28.25 ? 255 ARG A N 1 ATOM 1927 C CA . ARG A 1 255 ? -32.117 10.412 89.460 1.00 28.55 ? 255 ARG A CA 1 ATOM 1928 C C . ARG A 1 255 ? -30.925 10.768 88.575 1.00 29.09 ? 255 ARG A C 1 ATOM 1929 O O . ARG A 1 255 ? -29.869 10.116 88.641 1.00 29.05 ? 255 ARG A O 1 ATOM 1930 C CB . ARG A 1 255 ? -32.480 8.947 89.273 1.00 28.60 ? 255 ARG A CB 1 ATOM 1931 C CG . ARG A 1 255 ? -33.430 8.404 90.322 1.00 28.42 ? 255 ARG A CG 1 ATOM 1932 C CD . ARG A 1 255 ? -33.556 6.893 90.187 1.00 29.20 ? 255 ARG A CD 1 ATOM 1933 N NE . ARG A 1 255 ? -34.629 6.413 91.049 1.00 30.35 ? 255 ARG A NE 1 ATOM 1934 C CZ . ARG A 1 255 ? -34.458 6.056 92.318 1.00 30.38 ? 255 ARG A CZ 1 ATOM 1935 N NH1 . ARG A 1 255 ? -33.242 6.077 92.862 1.00 30.34 ? 255 ARG A NH1 1 ATOM 1936 N NH2 . ARG A 1 255 ? -35.505 5.657 93.033 1.00 30.41 ? 255 ARG A NH2 1 ATOM 1937 N N . GLY A 1 256 ? -31.072 11.838 87.792 1.00 28.01 ? 256 GLY A N 1 ATOM 1938 C CA . GLY A 1 256 ? -30.109 12.190 86.752 1.00 28.22 ? 256 GLY A CA 1 ATOM 1939 C C . GLY A 1 256 ? -30.800 12.994 85.662 1.00 27.78 ? 256 GLY A C 1 ATOM 1940 O O . GLY A 1 256 ? -31.882 13.560 85.894 1.00 26.96 ? 256 GLY A O 1 ATOM 1941 N N . TYR A 1 257 ? -30.202 13.033 84.473 1.00 27.58 ? 257 TYR A N 1 ATOM 1942 C CA . TYR A 1 257 ? -30.770 13.818 83.373 1.00 27.84 ? 257 TYR A CA 1 ATOM 1943 C C . TYR A 1 257 ? -30.861 13.035 82.082 1.00 27.19 ? 257 TYR A C 1 ATOM 1944 O O . TYR A 1 257 ? -30.144 12.045 81.873 1.00 27.15 ? 257 TYR A O 1 ATOM 1945 C CB . TYR A 1 257 ? -29.929 15.054 83.096 1.00 28.37 ? 257 TYR A CB 1 ATOM 1946 C CG . TYR A 1 257 ? -28.516 14.728 82.703 1.00 29.13 ? 257 TYR A CG 1 ATOM 1947 C CD1 . TYR A 1 257 ? -28.175 14.500 81.374 1.00 29.26 ? 257 TYR A CD1 1 ATOM 1948 C CD2 . TYR A 1 257 ? -27.515 14.619 83.665 1.00 29.97 ? 257 TYR A CD2 1 ATOM 1949 C CE1 . TYR A 1 257 ? -26.882 14.196 81.012 1.00 29.61 ? 257 TYR A CE1 1 ATOM 1950 C CE2 . TYR A 1 257 ? -26.221 14.302 83.312 1.00 30.02 ? 257 TYR A CE2 1 ATOM 1951 C CZ . TYR A 1 257 ? -25.908 14.099 81.987 1.00 30.26 ? 257 TYR A CZ 1 ATOM 1952 O OH . TYR A 1 257 ? -24.632 13.788 81.609 1.00 30.04 ? 257 TYR A OH 1 ATOM 1953 N N . PHE A 1 258 ? -31.739 13.520 81.210 1.00 25.67 ? 258 PHE A N 1 ATOM 1954 C CA . PHE A 1 258 ? -31.800 13.057 79.844 1.00 25.92 ? 258 PHE A CA 1 ATOM 1955 C C . PHE A 1 258 ? -30.960 13.965 78.987 1.00 27.78 ? 258 PHE A C 1 ATOM 1956 O O . PHE A 1 258 ? -30.900 15.192 79.214 1.00 28.12 ? 258 PHE A O 1 ATOM 1957 C CB . PHE A 1 258 ? -33.251 13.046 79.343 1.00 24.19 ? 258 PHE A CB 1 ATOM 1958 C CG . PHE A 1 258 ? -34.104 12.044 80.043 1.00 23.21 ? 258 PHE A CG 1 ATOM 1959 C CD1 . PHE A 1 258 ? -34.764 12.381 81.208 1.00 23.80 ? 258 PHE A CD1 1 ATOM 1960 C CD2 . PHE A 1 258 ? -34.213 10.744 79.563 1.00 23.29 ? 258 PHE A CD2 1 ATOM 1961 C CE1 . PHE A 1 258 ? -35.579 11.467 81.853 1.00 23.06 ? 258 PHE A CE1 1 ATOM 1962 C CE2 . PHE A 1 258 ? -35.001 9.814 80.213 1.00 23.22 ? 258 PHE A CE2 1 ATOM 1963 C CZ . PHE A 1 258 ? -35.687 10.180 81.357 1.00 23.86 ? 258 PHE A CZ 1 ATOM 1964 N N . LYS A 1 259 ? -30.292 13.355 78.015 1.00 29.60 ? 259 LYS A N 1 ATOM 1965 C CA . LYS A 1 259 ? -29.685 14.108 76.959 1.00 33.24 ? 259 LYS A CA 1 ATOM 1966 C C . LYS A 1 259 ? -30.849 14.702 76.207 1.00 34.18 ? 259 LYS A C 1 ATOM 1967 O O . LYS A 1 259 ? -31.954 14.123 76.165 1.00 35.65 ? 259 LYS A O 1 ATOM 1968 C CB . LYS A 1 259 ? -28.871 13.204 76.037 1.00 37.35 ? 259 LYS A CB 1 ATOM 1969 C CG . LYS A 1 259 ? -27.702 12.502 76.713 1.00 40.58 ? 259 LYS A CG 1 ATOM 1970 C CD . LYS A 1 259 ? -26.366 13.128 76.361 1.00 43.64 ? 259 LYS A CD 1 ATOM 1971 C CE . LYS A 1 259 ? -25.233 12.133 76.553 1.00 46.16 ? 259 LYS A CE 1 ATOM 1972 N NZ . LYS A 1 259 ? -23.947 12.678 76.039 1.00 51.20 ? 259 LYS A NZ 1 ATOM 1973 N N . ILE A 1 260 ? -30.643 15.892 75.674 1.00 34.39 ? 260 ILE A N 1 ATOM 1974 C CA . ILE A 1 260 ? -31.584 16.453 74.752 1.00 32.44 ? 260 ILE A CA 1 ATOM 1975 C C . ILE A 1 260 ? -30.790 16.765 73.482 1.00 33.89 ? 260 ILE A C 1 ATOM 1976 O O . ILE A 1 260 ? -29.772 17.450 73.540 1.00 34.11 ? 260 ILE A O 1 ATOM 1977 C CB . ILE A 1 260 ? -32.361 17.633 75.379 1.00 33.64 ? 260 ILE A CB 1 ATOM 1978 C CG1 . ILE A 1 260 ? -33.366 18.201 74.378 1.00 34.07 ? 260 ILE A CG1 1 ATOM 1979 C CG2 . ILE A 1 260 ? -31.439 18.707 75.944 1.00 33.60 ? 260 ILE A CG2 1 ATOM 1980 C CD1 . ILE A 1 260 ? -34.500 18.970 75.029 1.00 33.16 ? 260 ILE A CD1 1 ATOM 1981 N N . ARG A 1 261 ? -31.222 16.197 72.352 1.00 32.51 ? 261 ARG A N 1 ATOM 1982 C CA . ARG A 1 261 ? -30.526 16.359 71.069 1.00 32.75 ? 261 ARG A CA 1 ATOM 1983 C C . ARG A 1 261 ? -31.409 17.148 70.106 1.00 30.78 ? 261 ARG A C 1 ATOM 1984 O O . ARG A 1 261 ? -32.589 17.343 70.359 1.00 28.03 ? 261 ARG A O 1 ATOM 1985 C CB . ARG A 1 261 ? -30.193 14.982 70.473 1.00 35.24 ? 261 ARG A CB 1 ATOM 1986 C CG . ARG A 1 261 ? -29.281 14.130 71.361 1.00 38.66 ? 261 ARG A CG 1 ATOM 1987 C CD . ARG A 1 261 ? -28.837 12.838 70.673 1.00 41.00 ? 261 ARG A CD 1 ATOM 1988 N NE . ARG A 1 261 ? -27.943 12.005 71.502 1.00 43.31 ? 261 ARG A NE 1 ATOM 1989 C CZ . ARG A 1 261 ? -26.632 12.210 71.682 1.00 46.52 ? 261 ARG A CZ 1 ATOM 1990 N NH1 . ARG A 1 261 ? -26.011 13.244 71.118 1.00 46.98 ? 261 ARG A NH1 1 ATOM 1991 N NH2 . ARG A 1 261 ? -25.927 11.383 72.452 1.00 47.59 ? 261 ARG A NH2 1 ATOM 1992 N N . SER A 1 262 ? -30.837 17.625 69.010 1.00 31.55 ? 262 SER A N 1 ATOM 1993 C CA . SER A 1 262 ? -31.653 18.191 67.939 1.00 31.69 ? 262 SER A CA 1 ATOM 1994 C C . SER A 1 262 ? -31.462 17.382 66.675 1.00 30.43 ? 262 SER A C 1 ATOM 1995 O O . SER A 1 262 ? -30.361 16.895 66.377 1.00 30.02 ? 262 SER A O 1 ATOM 1996 C CB . SER A 1 262 ? -31.337 19.666 67.705 1.00 34.86 ? 262 SER A CB 1 ATOM 1997 O OG . SER A 1 262 ? -30.085 19.835 67.096 1.00 36.91 ? 262 SER A OG 1 ATOM 1998 N N . GLY A 1 263 ? -32.551 17.204 65.946 1.00 28.13 ? 263 GLY A N 1 ATOM 1999 C CA . GLY A 1 263 ? -32.486 16.516 64.663 1.00 28.08 ? 263 GLY A CA 1 ATOM 2000 C C . GLY A 1 263 ? -33.881 16.331 64.122 1.00 26.16 ? 263 GLY A C 1 ATOM 2001 O O . GLY A 1 263 ? -34.768 17.121 64.421 1.00 26.15 ? 263 GLY A O 1 ATOM 2002 N N . LYS A 1 264 ? -34.061 15.247 63.381 1.00 25.14 ? 264 LYS A N 1 ATOM 2003 C CA . LYS A 1 264 ? -35.230 15.055 62.535 1.00 24.11 ? 264 LYS A CA 1 ATOM 2004 C C . LYS A 1 264 ? -36.243 14.075 63.127 1.00 20.78 ? 264 LYS A C 1 ATOM 2005 O O . LYS A 1 264 ? -37.074 13.534 62.424 1.00 18.86 ? 264 LYS A O 1 ATOM 2006 C CB . LYS A 1 264 ? -34.743 14.580 61.162 1.00 27.40 ? 264 LYS A CB 1 ATOM 2007 C CG . LYS A 1 264 ? -33.919 15.666 60.464 1.00 30.75 ? 264 LYS A CG 1 ATOM 2008 C CD . LYS A 1 264 ? -33.209 15.173 59.211 1.00 33.76 ? 264 LYS A CD 1 ATOM 2009 C CE . LYS A 1 264 ? -32.555 16.359 58.485 1.00 36.50 ? 264 LYS A CE 1 ATOM 2010 N NZ . LYS A 1 264 ? -32.111 15.988 57.112 1.00 38.78 ? 264 LYS A NZ 1 ATOM 2011 N N . SER A 1 265 ? -36.170 13.841 64.429 1.00 19.61 ? 265 SER A N 1 ATOM 2012 C CA . SER A 1 265 ? -37.017 12.822 65.042 1.00 19.10 ? 265 SER A CA 1 ATOM 2013 C C . SER A 1 265 ? -38.432 13.336 65.283 1.00 18.62 ? 265 SER A C 1 ATOM 2014 O O . SER A 1 265 ? -38.654 14.547 65.425 1.00 17.21 ? 265 SER A O 1 ATOM 2015 C CB . SER A 1 265 ? -36.380 12.312 66.337 1.00 19.76 ? 265 SER A CB 1 ATOM 2016 O OG . SER A 1 265 ? -35.159 11.649 66.055 1.00 19.69 ? 265 SER A OG 1 ATOM 2017 N N . SER A 1 266 ? -39.387 12.409 65.316 1.00 18.42 ? 266 SER A N 1 ATOM 2018 C CA . SER A 1 266 ? -40.764 12.755 65.610 1.00 17.99 ? 266 SER A CA 1 ATOM 2019 C C . SER A 1 266 ? -41.498 11.590 66.285 1.00 17.44 ? 266 SER A C 1 ATOM 2020 O O . SER A 1 266 ? -40.886 10.576 66.661 1.00 17.41 ? 266 SER A O 1 ATOM 2021 C CB . SER A 1 266 ? -41.507 13.175 64.330 1.00 18.10 ? 266 SER A CB 1 ATOM 2022 O OG . SER A 1 266 ? -42.763 13.772 64.659 1.00 18.53 ? 266 SER A OG 1 ATOM 2023 N N . ILE A 1 267 ? -42.810 11.761 66.426 1.00 16.79 ? 267 ILE A N 1 ATOM 2024 C CA . ILE A 1 267 ? -43.700 10.792 67.056 1.00 17.08 ? 267 ILE A CA 1 ATOM 2025 C C . ILE A 1 267 ? -44.989 10.743 66.255 1.00 17.70 ? 267 ILE A C 1 ATOM 2026 O O . ILE A 1 267 ? -45.441 11.796 65.734 1.00 16.26 ? 267 ILE A O 1 ATOM 2027 C CB . ILE A 1 267 ? -43.970 11.191 68.514 1.00 17.34 ? 267 ILE A CB 1 ATOM 2028 C CG1 . ILE A 1 267 ? -44.785 10.127 69.255 1.00 17.63 ? 267 ILE A CG1 1 ATOM 2029 C CG2 . ILE A 1 267 ? -44.638 12.561 68.624 1.00 17.05 ? 267 ILE A CG2 1 ATOM 2030 C CD1 . ILE A 1 267 ? -44.555 10.155 70.764 1.00 17.51 ? 267 ILE A CD1 1 ATOM 2031 N N . MET A 1 268 ? -45.571 9.552 66.124 1.00 17.63 ? 268 MET A N 1 ATOM 2032 C CA . MET A 1 268 ? -46.805 9.385 65.359 1.00 18.50 ? 268 MET A CA 1 ATOM 2033 C C . MET A 1 268 ? -47.745 8.416 66.087 1.00 18.90 ? 268 MET A C 1 ATOM 2034 O O . MET A 1 268 ? -47.289 7.425 66.678 1.00 19.42 ? 268 MET A O 1 ATOM 2035 C CB . MET A 1 268 ? -46.501 8.867 63.945 1.00 18.67 ? 268 MET A CB 1 ATOM 2036 C CG . MET A 1 268 ? -47.701 8.821 62.992 1.00 19.48 ? 268 MET A CG 1 ATOM 2037 S SD . MET A 1 268 ? -47.249 8.162 61.371 1.00 19.67 ? 268 MET A SD 1 ATOM 2038 C CE . MET A 1 268 ? -46.220 9.483 60.698 1.00 18.17 ? 268 MET A CE 1 ATOM 2039 N N . ARG A 1 269 ? -49.036 8.740 66.091 1.00 18.57 ? 269 ARG A N 1 ATOM 2040 C CA . ARG A 1 269 ? -50.073 7.837 66.618 1.00 19.44 ? 269 ARG A CA 1 ATOM 2041 C C . ARG A 1 269 ? -50.549 6.946 65.467 1.00 19.42 ? 269 ARG A C 1 ATOM 2042 O O . ARG A 1 269 ? -51.021 7.438 64.429 1.00 18.78 ? 269 ARG A O 1 ATOM 2043 C CB . ARG A 1 269 ? -51.265 8.616 67.193 1.00 20.24 ? 269 ARG A CB 1 ATOM 2044 C CG . ARG A 1 269 ? -50.880 9.562 68.315 1.00 21.04 ? 269 ARG A CG 1 ATOM 2045 C CD . ARG A 1 269 ? -52.085 10.114 69.066 1.00 22.14 ? 269 ARG A CD 1 ATOM 2046 N NE . ARG A 1 269 ? -51.669 11.026 70.135 1.00 22.38 ? 269 ARG A NE 1 ATOM 2047 C CZ . ARG A 1 269 ? -51.483 12.343 70.009 1.00 23.28 ? 269 ARG A CZ 1 ATOM 2048 N NH1 . ARG A 1 269 ? -51.688 12.975 68.864 1.00 23.55 ? 269 ARG A NH1 1 ATOM 2049 N NH2 . ARG A 1 269 ? -51.107 13.048 71.066 1.00 24.25 ? 269 ARG A NH2 1 ATOM 2050 N N . SER A 1 270 ? -50.422 5.642 65.637 1.00 19.10 ? 270 SER A N 1 ATOM 2051 C CA . SER A 1 270 ? -50.828 4.705 64.613 1.00 19.79 ? 270 SER A CA 1 ATOM 2052 C C . SER A 1 270 ? -51.015 3.329 65.221 1.00 21.30 ? 270 SER A C 1 ATOM 2053 O O . SER A 1 270 ? -50.293 2.960 66.150 1.00 20.61 ? 270 SER A O 1 ATOM 2054 C CB . SER A 1 270 ? -49.763 4.602 63.532 1.00 19.71 ? 270 SER A CB 1 ATOM 2055 O OG . SER A 1 270 ? -50.092 3.567 62.619 1.00 20.60 ? 270 SER A OG 1 ATOM 2056 N N . ASP A 1 271 ? -51.961 2.582 64.671 1.00 21.81 ? 271 ASP A N 1 ATOM 2057 C CA . ASP A 1 271 ? -52.101 1.175 64.991 1.00 23.76 ? 271 ASP A CA 1 ATOM 2058 C C . ASP A 1 271 ? -51.622 0.256 63.884 1.00 23.73 ? 271 ASP A C 1 ATOM 2059 O O . ASP A 1 271 ? -51.809 -0.966 63.969 1.00 23.87 ? 271 ASP A O 1 ATOM 2060 C CB . ASP A 1 271 ? -53.549 0.889 65.385 1.00 25.02 ? 271 ASP A CB 1 ATOM 2061 C CG . ASP A 1 271 ? -53.880 1.484 66.730 1.00 26.74 ? 271 ASP A CG 1 ATOM 2062 O OD1 . ASP A 1 271 ? -52.962 1.562 67.580 1.00 26.51 ? 271 ASP A OD1 1 ATOM 2063 O OD2 . ASP A 1 271 ? -55.034 1.891 66.940 1.00 29.51 ? 271 ASP A OD2 1 ATOM 2064 N N . ALA A 1 272 ? -50.946 0.808 62.878 1.00 22.63 ? 272 ALA A N 1 ATOM 2065 C CA . ALA A 1 272 ? -50.482 -0.009 61.763 1.00 23.20 ? 272 ALA A CA 1 ATOM 2066 C C . ALA A 1 272 ? -49.345 -0.918 62.229 1.00 23.54 ? 272 ALA A C 1 ATOM 2067 O O . ALA A 1 272 ? -48.488 -0.497 62.997 1.00 22.45 ? 272 ALA A O 1 ATOM 2068 C CB . ALA A 1 272 ? -50.058 0.841 60.565 1.00 22.84 ? 272 ALA A CB 1 ATOM 2069 N N . PRO A 1 273 ? -49.344 -2.182 61.774 1.00 25.06 ? 273 PRO A N 1 ATOM 2070 C CA . PRO A 1 273 ? -48.254 -3.072 62.183 1.00 26.01 ? 273 PRO A CA 1 ATOM 2071 C C . PRO A 1 273 ? -46.922 -2.652 61.552 1.00 25.65 ? 273 PRO A C 1 ATOM 2072 O O . PRO A 1 273 ? -46.906 -2.024 60.493 1.00 24.52 ? 273 PRO A O 1 ATOM 2073 C CB . PRO A 1 273 ? -48.705 -4.454 61.666 1.00 27.17 ? 273 PRO A CB 1 ATOM 2074 C CG . PRO A 1 273 ? -49.678 -4.179 60.577 1.00 27.35 ? 273 PRO A CG 1 ATOM 2075 C CD . PRO A 1 273 ? -50.295 -2.826 60.851 1.00 26.71 ? 273 PRO A CD 1 ATOM 2076 N N . ILE A 1 274 ? -45.821 -2.986 62.204 1.00 26.34 ? 274 ILE A N 1 ATOM 2077 C CA . ILE A 1 274 ? -44.501 -2.696 61.642 1.00 28.20 ? 274 ILE A CA 1 ATOM 2078 C C . ILE A 1 274 ? -44.056 -3.847 60.770 1.00 30.00 ? 274 ILE A C 1 ATOM 2079 O O . ILE A 1 274 ? -44.120 -4.995 61.183 1.00 31.10 ? 274 ILE A O 1 ATOM 2080 C CB . ILE A 1 274 ? -43.470 -2.398 62.729 1.00 29.35 ? 274 ILE A CB 1 ATOM 2081 C CG1 . ILE A 1 274 ? -43.956 -1.176 63.510 1.00 30.84 ? 274 ILE A CG1 1 ATOM 2082 C CG2 . ILE A 1 274 ? -42.107 -2.119 62.099 1.00 28.84 ? 274 ILE A CG2 1 ATOM 2083 C CD1 . ILE A 1 274 ? -43.005 -0.710 64.564 1.00 33.85 ? 274 ILE A CD1 1 ATOM 2084 N N . GLY A 1 275 ? -43.642 -3.543 59.544 1.00 29.95 ? 275 GLY A N 1 ATOM 2085 C CA . GLY A 1 275 ? -43.249 -4.590 58.601 1.00 30.06 ? 275 GLY A CA 1 ATOM 2086 C C . GLY A 1 275 ? -41.768 -4.552 58.291 1.00 30.66 ? 275 GLY A C 1 ATOM 2087 O O . GLY A 1 275 ? -41.101 -3.514 58.452 1.00 26.77 ? 275 GLY A O 1 ATOM 2088 N N . LYS A 1 276 ? -41.254 -5.681 57.810 1.00 31.01 ? 276 LYS A N 1 ATOM 2089 C CA . LYS A 1 276 ? -39.877 -5.746 57.354 1.00 32.53 ? 276 LYS A CA 1 ATOM 2090 C C . LYS A 1 276 ? -39.861 -5.374 55.887 1.00 31.14 ? 276 LYS A C 1 ATOM 2091 O O . LYS A 1 276 ? -39.973 -6.221 55.014 1.00 31.66 ? 276 LYS A O 1 ATOM 2092 C CB . LYS A 1 276 ? -39.278 -7.140 57.598 1.00 35.90 ? 276 LYS A CB 1 ATOM 2093 C CG . LYS A 1 276 ? -39.215 -7.491 59.081 1.00 39.25 ? 276 LYS A CG 1 ATOM 2094 C CD . LYS A 1 276 ? -38.251 -8.636 59.385 1.00 42.71 ? 276 LYS A CD 1 ATOM 2095 C CE . LYS A 1 276 ? -38.139 -8.880 60.888 1.00 45.25 ? 276 LYS A CE 1 ATOM 2096 N NZ . LYS A 1 276 ? -37.512 -7.744 61.641 1.00 48.36 ? 276 LYS A NZ 1 ATOM 2097 N N . CYS A 1 277 ? -39.751 -4.085 55.622 1.00 29.01 ? 277 CYS A N 1 ATOM 2098 C CA . CYS A 1 277 ? -39.797 -3.569 54.261 1.00 28.63 ? 277 CYS A CA 1 ATOM 2099 C C . CYS A 1 277 ? -39.163 -2.186 54.282 1.00 26.43 ? 277 CYS A C 1 ATOM 2100 O O . CYS A 1 277 ? -38.755 -1.705 55.352 1.00 25.78 ? 277 CYS A O 1 ATOM 2101 C CB . CYS A 1 277 ? -41.235 -3.528 53.692 1.00 30.18 ? 277 CYS A CB 1 ATOM 2102 S SG . CYS A 1 277 ? -42.493 -2.768 54.760 1.00 33.47 ? 277 CYS A SG 1 ATOM 2103 N N . ASN A 1 278 ? -39.051 -1.572 53.109 1.00 24.18 ? 278 ASN A N 1 ATOM 2104 C CA . ASN A 1 278 ? -38.337 -0.317 52.966 1.00 23.91 ? 278 ASN A CA 1 ATOM 2105 C C . ASN A 1 278 ? -39.216 0.714 52.266 1.00 23.55 ? 278 ASN A C 1 ATOM 2106 O O . ASN A 1 278 ? -39.598 0.507 51.139 1.00 22.12 ? 278 ASN A O 1 ATOM 2107 C CB . ASN A 1 278 ? -37.067 -0.558 52.163 1.00 24.59 ? 278 ASN A CB 1 ATOM 2108 C CG . ASN A 1 278 ? -36.101 0.600 52.245 1.00 25.02 ? 278 ASN A CG 1 ATOM 2109 O OD1 . ASN A 1 278 ? -36.458 1.742 51.943 1.00 25.93 ? 278 ASN A OD1 1 ATOM 2110 N ND2 . ASN A 1 278 ? -34.849 0.306 52.607 1.00 25.57 ? 278 ASN A ND2 1 ATOM 2111 N N . SER A 1 279 ? -39.533 1.806 52.943 1.00 22.68 ? 279 SER A N 1 ATOM 2112 C CA . SER A 1 279 ? -40.333 2.865 52.363 1.00 23.36 ? 279 SER A CA 1 ATOM 2113 C C . SER A 1 279 ? -40.013 4.216 53.007 1.00 22.42 ? 279 SER A C 1 ATOM 2114 O O . SER A 1 279 ? -39.931 4.327 54.228 1.00 22.08 ? 279 SER A O 1 ATOM 2115 C CB . SER A 1 279 ? -41.822 2.509 52.501 1.00 23.83 ? 279 SER A CB 1 ATOM 2116 O OG . SER A 1 279 ? -42.613 3.486 51.879 1.00 25.55 ? 279 SER A OG 1 ATOM 2117 N N . GLU A 1 280 ? -39.847 5.240 52.178 1.00 22.17 ? 280 GLU A N 1 ATOM 2118 C CA . GLU A 1 280 ? -39.427 6.558 52.654 1.00 22.86 ? 280 GLU A CA 1 ATOM 2119 C C . GLU A 1 280 ? -40.529 7.304 53.387 1.00 21.12 ? 280 GLU A C 1 ATOM 2120 O O . GLU A 1 280 ? -40.252 8.065 54.319 1.00 20.72 ? 280 GLU A O 1 ATOM 2121 C CB . GLU A 1 280 ? -38.945 7.430 51.487 1.00 25.24 ? 280 GLU A CB 1 ATOM 2122 C CG . GLU A 1 280 ? -37.681 6.940 50.804 1.00 28.00 ? 280 GLU A CG 1 ATOM 2123 C CD . GLU A 1 280 ? -36.434 7.198 51.610 1.00 31.23 ? 280 GLU A CD 1 ATOM 2124 O OE1 . GLU A 1 280 ? -36.454 8.119 52.475 1.00 32.11 ? 280 GLU A OE1 1 ATOM 2125 O OE2 . GLU A 1 280 ? -35.441 6.460 51.388 1.00 32.47 ? 280 GLU A OE2 1 ATOM 2126 N N . CYS A 1 281 ? -41.772 7.131 52.940 1.00 20.40 ? 281 CYS A N 1 ATOM 2127 C CA . CYS A 1 281 ? -42.903 7.914 53.465 1.00 19.62 ? 281 CYS A CA 1 ATOM 2128 C C . CYS A 1 281 ? -43.779 7.119 54.419 1.00 18.87 ? 281 CYS A C 1 ATOM 2129 O O . CYS A 1 281 ? -44.290 6.050 54.055 1.00 19.21 ? 281 CYS A O 1 ATOM 2130 C CB . CYS A 1 281 ? -43.770 8.401 52.323 1.00 20.14 ? 281 CYS A CB 1 ATOM 2131 S SG . CYS A 1 281 ? -45.135 9.410 52.905 1.00 20.33 ? 281 CYS A SG 1 ATOM 2132 N N . ILE A 1 282 ? -43.932 7.629 55.643 1.00 17.84 ? 282 ILE A N 1 ATOM 2133 C CA . ILE A 1 282 ? -44.762 6.981 56.656 1.00 17.90 ? 282 ILE A CA 1 ATOM 2134 C C . ILE A 1 282 ? -46.005 7.821 56.955 1.00 17.78 ? 282 ILE A C 1 ATOM 2135 O O . ILE A 1 282 ? -45.906 9.037 57.146 1.00 16.94 ? 282 ILE A O 1 ATOM 2136 C CB . ILE A 1 282 ? -43.974 6.782 57.964 1.00 17.98 ? 282 ILE A CB 1 ATOM 2137 C CG1 . ILE A 1 282 ? -42.684 5.985 57.705 1.00 18.88 ? 282 ILE A CG1 1 ATOM 2138 C CG2 . ILE A 1 282 ? -44.850 6.129 59.034 1.00 17.60 ? 282 ILE A CG2 1 ATOM 2139 C CD1 . ILE A 1 282 ? -41.764 5.870 58.925 1.00 19.43 ? 282 ILE A CD1 1 ATOM 2140 N N . THR A 1 283 ? -47.163 7.166 56.985 1.00 17.36 ? 283 THR A N 1 ATOM 2141 C CA . THR A 1 283 ? -48.416 7.765 57.430 1.00 17.66 ? 283 THR A CA 1 ATOM 2142 C C . THR A 1 283 ? -49.000 6.850 58.515 1.00 17.97 ? 283 THR A C 1 ATOM 2143 O O . THR A 1 283 ? -48.588 5.681 58.614 1.00 18.18 ? 283 THR A O 1 ATOM 2144 C CB . THR A 1 283 ? -49.468 7.906 56.281 1.00 17.70 ? 283 THR A CB 1 ATOM 2145 O OG1 . THR A 1 283 ? -50.138 6.654 56.052 1.00 17.45 ? 283 THR A OG1 1 ATOM 2146 C CG2 . THR A 1 283 ? -48.825 8.409 54.981 1.00 17.66 ? 283 THR A CG2 1 ATOM 2147 N N . PRO A 1 284 ? -49.954 7.355 59.317 1.00 18.05 ? 284 PRO A N 1 ATOM 2148 C CA . PRO A 1 284 ? -50.613 6.476 60.305 1.00 18.91 ? 284 PRO A CA 1 ATOM 2149 C C . PRO A 1 284 ? -51.329 5.266 59.711 1.00 20.35 ? 284 PRO A C 1 ATOM 2150 O O . PRO A 1 284 ? -51.572 4.286 60.423 1.00 20.35 ? 284 PRO A O 1 ATOM 2151 C CB . PRO A 1 284 ? -51.622 7.396 60.979 1.00 18.70 ? 284 PRO A CB 1 ATOM 2152 C CG . PRO A 1 284 ? -51.027 8.765 60.822 1.00 18.17 ? 284 PRO A CG 1 ATOM 2153 C CD . PRO A 1 284 ? -50.354 8.761 59.492 1.00 17.67 ? 284 PRO A CD 1 ATOM 2154 N N . ASN A 1 285 ? -51.671 5.328 58.426 1.00 21.03 ? 285 ASN A N 1 ATOM 2155 C CA . ASN A 1 285 ? -52.301 4.198 57.750 1.00 22.79 ? 285 ASN A CA 1 ATOM 2156 C C . ASN A 1 285 ? -51.298 3.161 57.283 1.00 22.59 ? 285 ASN A C 1 ATOM 2157 O O . ASN A 1 285 ? -51.695 2.132 56.788 1.00 24.33 ? 285 ASN A O 1 ATOM 2158 C CB . ASN A 1 285 ? -53.034 4.675 56.508 1.00 24.77 ? 285 ASN A CB 1 ATOM 2159 C CG . ASN A 1 285 ? -53.998 5.819 56.777 1.00 26.92 ? 285 ASN A CG 1 ATOM 2160 O OD1 . ASN A 1 285 ? -53.606 6.942 57.096 1.00 24.90 ? 285 ASN A OD1 1 ATOM 2161 N ND2 . ASN A 1 285 ? -55.252 5.547 56.608 1.00 32.19 ? 285 ASN A ND2 1 ATOM 2162 N N . GLY A 1 286 ? -50.006 3.437 57.417 1.00 21.30 ? 286 GLY A N 1 ATOM 2163 C CA . GLY A 1 286 ? -48.977 2.637 56.818 1.00 20.89 ? 286 GLY A CA 1 ATOM 2164 C C . GLY A 1 286 ? -48.069 3.467 55.942 1.00 21.02 ? 286 GLY A C 1 ATOM 2165 O O . GLY A 1 286 ? -48.370 4.630 55.632 1.00 20.24 ? 286 GLY A O 1 ATOM 2166 N N . SER A 1 287 ? -46.955 2.879 55.533 1.00 21.03 ? 287 SER A N 1 ATOM 2167 C CA . SER A 1 287 ? -46.068 3.545 54.584 1.00 20.87 ? 287 SER A CA 1 ATOM 2168 C C . SER A 1 287 ? -46.748 3.617 53.208 1.00 20.87 ? 287 SER A C 1 ATOM 2169 O O . SER A 1 287 ? -47.561 2.755 52.850 1.00 20.48 ? 287 SER A O 1 ATOM 2170 C CB . SER A 1 287 ? -44.733 2.806 54.478 1.00 21.00 ? 287 SER A CB 1 ATOM 2171 O OG . SER A 1 287 ? -44.080 2.694 55.745 1.00 21.13 ? 287 SER A OG 1 ATOM 2172 N N . ILE A 1 288 ? -46.447 4.663 52.452 1.00 20.64 ? 288 ILE A N 1 ATOM 2173 C CA . ILE A 1 288 ? -46.960 4.790 51.098 1.00 20.91 ? 288 ILE A CA 1 ATOM 2174 C C . ILE A 1 288 ? -45.812 5.043 50.146 1.00 21.13 ? 288 ILE A C 1 ATOM 2175 O O . ILE A 1 288 ? -44.789 5.628 50.515 1.00 21.36 ? 288 ILE A O 1 ATOM 2176 C CB . ILE A 1 288 ? -48.040 5.906 50.956 1.00 21.07 ? 288 ILE A CB 1 ATOM 2177 C CG1 . ILE A 1 288 ? -47.458 7.295 51.277 1.00 20.83 ? 288 ILE A CG1 1 ATOM 2178 C CG2 . ILE A 1 288 ? -49.223 5.612 51.873 1.00 21.12 ? 288 ILE A CG2 1 ATOM 2179 C CD1 . ILE A 1 288 ? -48.423 8.454 51.011 1.00 20.35 ? 288 ILE A CD1 1 ATOM 2180 N N . PRO A 1 289 ? -45.961 4.583 48.912 1.00 22.38 ? 289 PRO A N 1 ATOM 2181 C CA . PRO A 1 289 ? -45.020 4.942 47.883 1.00 23.11 ? 289 PRO A CA 1 ATOM 2182 C C . PRO A 1 289 ? -44.992 6.452 47.697 1.00 22.65 ? 289 PRO A C 1 ATOM 2183 O O . PRO A 1 289 ? -46.025 7.116 47.895 1.00 22.19 ? 289 PRO A O 1 ATOM 2184 C CB . PRO A 1 289 ? -45.585 4.271 46.619 1.00 23.87 ? 289 PRO A CB 1 ATOM 2185 C CG . PRO A 1 289 ? -46.602 3.309 47.079 1.00 24.75 ? 289 PRO A CG 1 ATOM 2186 C CD . PRO A 1 289 ? -47.021 3.677 48.450 1.00 23.26 ? 289 PRO A CD 1 ATOM 2187 N N . ASN A 1 290 ? -43.831 6.979 47.331 1.00 22.01 ? 290 ASN A N 1 ATOM 2188 C CA . ASN A 1 290 ? -43.670 8.415 47.135 1.00 22.79 ? 290 ASN A CA 1 ATOM 2189 C C . ASN A 1 290 ? -43.270 8.812 45.722 1.00 22.39 ? 290 ASN A C 1 ATOM 2190 O O . ASN A 1 290 ? -42.648 9.856 45.520 1.00 24.78 ? 290 ASN A O 1 ATOM 2191 C CB . ASN A 1 290 ? -42.666 8.986 48.140 1.00 22.68 ? 290 ASN A CB 1 ATOM 2192 C CG . ASN A 1 290 ? -41.263 8.478 47.936 1.00 23.58 ? 290 ASN A CG 1 ATOM 2193 O OD1 . ASN A 1 290 ? -41.008 7.589 47.108 1.00 23.98 ? 290 ASN A OD1 1 ATOM 2194 N ND2 . ASN A 1 290 ? -40.343 9.009 48.728 1.00 22.06 ? 290 ASN A ND2 1 ATOM 2195 N N . ASP A 1 291 ? -43.653 7.998 44.753 1.00 23.16 ? 291 ASP A N 1 ATOM 2196 C CA . ASP A 1 291 ? -43.441 8.327 43.365 1.00 23.57 ? 291 ASP A CA 1 ATOM 2197 C C . ASP A 1 291 ? -44.309 9.540 42.959 1.00 22.21 ? 291 ASP A C 1 ATOM 2198 O O . ASP A 1 291 ? -43.833 10.421 42.251 1.00 23.41 ? 291 ASP A O 1 ATOM 2199 C CB . ASP A 1 291 ? -43.654 7.106 42.434 1.00 25.20 ? 291 ASP A CB 1 ATOM 2200 C CG . ASP A 1 291 ? -44.987 6.396 42.641 1.00 28.10 ? 291 ASP A CG 1 ATOM 2201 O OD1 . ASP A 1 291 ? -45.171 5.742 43.683 1.00 30.90 ? 291 ASP A OD1 1 ATOM 2202 O OD2 . ASP A 1 291 ? -45.868 6.457 41.748 1.00 29.79 ? 291 ASP A OD2 1 ATOM 2203 N N . LYS A 1 292 ? -45.533 9.609 43.460 1.00 20.24 ? 292 LYS A N 1 ATOM 2204 C CA . LYS A 1 292 ? -46.499 10.622 43.011 1.00 19.01 ? 292 LYS A CA 1 ATOM 2205 C C . LYS A 1 292 ? -46.298 11.915 43.797 1.00 18.25 ? 292 LYS A C 1 ATOM 2206 O O . LYS A 1 292 ? -45.800 11.879 44.935 1.00 18.61 ? 292 LYS A O 1 ATOM 2207 C CB . LYS A 1 292 ? -47.923 10.083 43.161 1.00 19.07 ? 292 LYS A CB 1 ATOM 2208 C CG . LYS A 1 292 ? -48.194 8.795 42.368 1.00 19.49 ? 292 LYS A CG 1 ATOM 2209 C CD . LYS A 1 292 ? -49.605 8.254 42.570 1.00 19.94 ? 292 LYS A CD 1 ATOM 2210 C CE . LYS A 1 292 ? -49.853 6.965 41.775 1.00 21.63 ? 292 LYS A CE 1 ATOM 2211 N NZ . LYS A 1 292 ? -49.025 5.843 42.342 1.00 22.47 ? 292 LYS A NZ 1 ATOM 2212 N N . PRO A 1 293 ? -46.620 13.065 43.196 1.00 17.31 ? 293 PRO A N 1 ATOM 2213 C CA . PRO A 1 293 ? -46.376 14.340 43.906 1.00 16.65 ? 293 PRO A CA 1 ATOM 2214 C C . PRO A 1 293 ? -47.401 14.638 45.010 1.00 16.21 ? 293 PRO A C 1 ATOM 2215 O O . PRO A 1 293 ? -47.105 15.409 45.923 1.00 15.11 ? 293 PRO A O 1 ATOM 2216 C CB . PRO A 1 293 ? -46.441 15.379 42.795 1.00 16.77 ? 293 PRO A CB 1 ATOM 2217 C CG . PRO A 1 293 ? -47.311 14.758 41.739 1.00 17.29 ? 293 PRO A CG 1 ATOM 2218 C CD . PRO A 1 293 ? -46.995 13.283 41.789 1.00 17.32 ? 293 PRO A CD 1 ATOM 2219 N N . PHE A 1 294 ? -48.580 14.021 44.929 1.00 15.50 ? 294 PHE A N 1 ATOM 2220 C CA . PHE A 1 294 ? -49.660 14.261 45.858 1.00 15.32 ? 294 PHE A CA 1 ATOM 2221 C C . PHE A 1 294 ? -50.178 12.934 46.427 1.00 15.40 ? 294 PHE A C 1 ATOM 2222 O O . PHE A 1 294 ? -49.923 11.834 45.872 1.00 15.38 ? 294 PHE A O 1 ATOM 2223 C CB . PHE A 1 294 ? -50.819 15.052 45.180 1.00 15.50 ? 294 PHE A CB 1 ATOM 2224 C CG . PHE A 1 294 ? -50.363 16.291 44.467 1.00 15.12 ? 294 PHE A CG 1 ATOM 2225 C CD1 . PHE A 1 294 ? -49.841 17.349 45.176 1.00 15.22 ? 294 PHE A CD1 1 ATOM 2226 C CD2 . PHE A 1 294 ? -50.413 16.374 43.079 1.00 15.52 ? 294 PHE A CD2 1 ATOM 2227 C CE1 . PHE A 1 294 ? -49.372 18.491 44.535 1.00 15.22 ? 294 PHE A CE1 1 ATOM 2228 C CE2 . PHE A 1 294 ? -49.973 17.523 42.431 1.00 15.51 ? 294 PHE A CE2 1 ATOM 2229 C CZ . PHE A 1 294 ? -49.419 18.565 43.160 1.00 15.20 ? 294 PHE A CZ 1 ATOM 2230 N N . GLN A 1 295 ? -50.919 13.051 47.516 1.00 15.21 ? 295 GLN A N 1 ATOM 2231 C CA . GLN A 1 295 ? -51.527 11.915 48.180 1.00 15.46 ? 295 GLN A CA 1 ATOM 2232 C C . GLN A 1 295 ? -52.761 12.351 48.956 1.00 15.98 ? 295 GLN A C 1 ATOM 2233 O O . GLN A 1 295 ? -52.860 13.497 49.410 1.00 15.91 ? 295 GLN A O 1 ATOM 2234 C CB . GLN A 1 295 ? -50.509 11.192 49.103 1.00 15.51 ? 295 GLN A CB 1 ATOM 2235 C CG . GLN A 1 295 ? -49.869 12.032 50.199 1.00 15.24 ? 295 GLN A CG 1 ATOM 2236 C CD . GLN A 1 295 ? -50.577 11.987 51.541 1.00 15.11 ? 295 GLN A CD 1 ATOM 2237 O OE1 . GLN A 1 295 ? -51.534 11.230 51.749 1.00 15.52 ? 295 GLN A OE1 1 ATOM 2238 N NE2 . GLN A 1 295 ? -50.089 12.808 52.488 1.00 14.25 ? 295 GLN A NE2 1 ATOM 2239 N N . ASN A 1 296 ? -53.708 11.431 49.090 1.00 16.21 ? 296 ASN A N 1 ATOM 2240 C CA A ASN A 1 296 ? -54.899 11.694 49.890 0.50 16.94 ? 296 ASN A CA 1 ATOM 2241 C CA B ASN A 1 296 ? -54.945 11.644 49.817 0.50 16.18 ? 296 ASN A CA 1 ATOM 2242 C C . ASN A 1 296 ? -55.123 10.611 50.938 1.00 16.97 ? 296 ASN A C 1 ATOM 2243 O O . ASN A 1 296 ? -56.248 10.370 51.394 1.00 17.97 ? 296 ASN A O 1 ATOM 2244 C CB A ASN A 1 296 ? -56.120 11.863 48.997 0.50 17.72 ? 296 ASN A CB 1 ATOM 2245 C CB B ASN A 1 296 ? -56.091 11.539 48.819 0.50 15.95 ? 296 ASN A CB 1 ATOM 2246 C CG A ASN A 1 296 ? -56.756 10.555 48.627 0.50 18.87 ? 296 ASN A CG 1 ATOM 2247 C CG B ASN A 1 296 ? -57.430 11.934 49.401 0.50 15.61 ? 296 ASN A CG 1 ATOM 2248 O OD1 A ASN A 1 296 ? -56.068 9.537 48.445 0.50 19.59 ? 296 ASN A OD1 1 ATOM 2249 O OD1 B ASN A 1 296 ? -57.577 12.984 50.035 0.50 15.17 ? 296 ASN A OD1 1 ATOM 2250 N ND2 A ASN A 1 296 ? -58.081 10.559 48.545 0.50 19.11 ? 296 ASN A ND2 1 ATOM 2251 N ND2 B ASN A 1 296 ? -58.418 11.092 49.179 0.50 15.43 ? 296 ASN A ND2 1 ATOM 2252 N N . VAL A 1 297 ? -54.026 9.982 51.351 1.00 16.72 ? 297 VAL A N 1 ATOM 2253 C CA . VAL A 1 297 ? -54.063 8.950 52.379 1.00 16.96 ? 297 VAL A CA 1 ATOM 2254 C C . VAL A 1 297 ? -54.199 9.558 53.779 1.00 17.00 ? 297 VAL A C 1 ATOM 2255 O O . VAL A 1 297 ? -55.085 9.189 54.525 1.00 17.09 ? 297 VAL A O 1 ATOM 2256 C CB . VAL A 1 297 ? -52.811 8.033 52.303 1.00 16.95 ? 297 VAL A CB 1 ATOM 2257 C CG1 . VAL A 1 297 ? -52.761 7.039 53.469 1.00 17.23 ? 297 VAL A CG1 1 ATOM 2258 C CG2 . VAL A 1 297 ? -52.784 7.290 50.964 1.00 17.29 ? 297 VAL A CG2 1 ATOM 2259 N N . ASN A 1 298 ? -53.323 10.493 54.147 1.00 16.90 ? 298 ASN A N 1 ATOM 2260 C CA . ASN A 1 298 ? -53.387 11.082 55.474 1.00 16.57 ? 298 ASN A CA 1 ATOM 2261 C C . ASN A 1 298 ? -52.639 12.395 55.494 1.00 16.21 ? 298 ASN A C 1 ATOM 2262 O O . ASN A 1 298 ? -51.544 12.511 54.911 1.00 15.53 ? 298 ASN A O 1 ATOM 2263 C CB . ASN A 1 298 ? -52.778 10.122 56.509 1.00 16.72 ? 298 ASN A CB 1 ATOM 2264 C CG . ASN A 1 298 ? -53.345 10.325 57.914 1.00 17.18 ? 298 ASN A CG 1 ATOM 2265 O OD1 . ASN A 1 298 ? -53.240 11.426 58.498 1.00 17.06 ? 298 ASN A OD1 1 ATOM 2266 N ND2 . ASN A 1 298 ? -53.946 9.252 58.481 1.00 17.23 ? 298 ASN A ND2 1 ATOM 2267 N N . ARG A 1 299 ? -53.206 13.392 56.173 1.00 16.45 ? 299 ARG A N 1 ATOM 2268 C CA . ARG A 1 299 ? -52.487 14.653 56.352 1.00 16.95 ? 299 ARG A CA 1 ATOM 2269 C C . ARG A 1 299 ? -51.262 14.536 57.294 1.00 16.30 ? 299 ARG A C 1 ATOM 2270 O O . ARG A 1 299 ? -50.380 15.391 57.287 1.00 15.12 ? 299 ARG A O 1 ATOM 2271 C CB . ARG A 1 299 ? -53.437 15.741 56.838 1.00 18.90 ? 299 ARG A CB 1 ATOM 2272 C CG . ARG A 1 299 ? -53.974 15.534 58.234 1.00 21.32 ? 299 ARG A CG 1 ATOM 2273 C CD . ARG A 1 299 ? -54.951 16.651 58.604 1.00 24.38 ? 299 ARG A CD 1 ATOM 2274 N NE . ARG A 1 299 ? -56.145 16.660 57.768 1.00 25.33 ? 299 ARG A NE 1 ATOM 2275 C CZ . ARG A 1 299 ? -57.038 17.666 57.736 1.00 27.54 ? 299 ARG A CZ 1 ATOM 2276 N NH1 . ARG A 1 299 ? -56.899 18.779 58.481 1.00 27.63 ? 299 ARG A NH1 1 ATOM 2277 N NH2 . ARG A 1 299 ? -58.086 17.562 56.957 1.00 28.87 ? 299 ARG A NH2 1 ATOM 2278 N N . ILE A 1 300 ? -51.226 13.488 58.101 1.00 15.94 ? 300 ILE A N 1 ATOM 2279 C CA . ILE A 1 300 ? -50.088 13.211 58.969 1.00 16.01 ? 300 ILE A CA 1 ATOM 2280 C C . ILE A 1 300 ? -49.089 12.377 58.214 1.00 16.17 ? 300 ILE A C 1 ATOM 2281 O O . ILE A 1 300 ? -49.417 11.284 57.741 1.00 15.42 ? 300 ILE A O 1 ATOM 2282 C CB . ILE A 1 300 ? -50.511 12.470 60.243 1.00 16.23 ? 300 ILE A CB 1 ATOM 2283 C CG1 . ILE A 1 300 ? -51.534 13.310 61.028 1.00 16.29 ? 300 ILE A CG1 1 ATOM 2284 C CG2 . ILE A 1 300 ? -49.266 12.147 61.095 1.00 15.42 ? 300 ILE A CG2 1 ATOM 2285 C CD1 . ILE A 1 300 ? -52.305 12.527 62.112 1.00 16.82 ? 300 ILE A CD1 1 ATOM 2286 N N . THR A 1 301 ? -47.870 12.897 58.066 1.00 16.94 ? 301 THR A N 1 ATOM 2287 C CA . THR A 1 301 ? -46.813 12.183 57.347 1.00 17.02 ? 301 THR A CA 1 ATOM 2288 C C . THR A 1 301 ? -45.436 12.376 58.032 1.00 17.13 ? 301 THR A C 1 ATOM 2289 O O . THR A 1 301 ? -45.224 13.333 58.790 1.00 17.20 ? 301 THR A O 1 ATOM 2290 C CB . THR A 1 301 ? -46.699 12.631 55.862 1.00 17.92 ? 301 THR A CB 1 ATOM 2291 O OG1 . THR A 1 301 ? -46.063 13.901 55.777 1.00 19.09 ? 301 THR A OG1 1 ATOM 2292 C CG2 . THR A 1 301 ? -48.071 12.716 55.147 1.00 18.10 ? 301 THR A CG2 1 ATOM 2293 N N . TYR A 1 302 ? -44.516 11.469 57.737 1.00 16.67 ? 302 TYR A N 1 ATOM 2294 C CA . TYR A 1 302 ? -43.117 11.595 58.152 1.00 16.61 ? 302 TYR A CA 1 ATOM 2295 C C . TYR A 1 302 ? -42.246 11.088 57.026 1.00 16.44 ? 302 TYR A C 1 ATOM 2296 O O . TYR A 1 302 ? -42.496 10.018 56.499 1.00 17.33 ? 302 TYR A O 1 ATOM 2297 C CB . TYR A 1 302 ? -42.835 10.791 59.443 1.00 16.88 ? 302 TYR A CB 1 ATOM 2298 C CG . TYR A 1 302 ? -41.396 10.916 59.906 1.00 17.37 ? 302 TYR A CG 1 ATOM 2299 C CD1 . TYR A 1 302 ? -40.417 10.038 59.455 1.00 18.00 ? 302 TYR A CD1 1 ATOM 2300 C CD2 . TYR A 1 302 ? -41.008 11.927 60.793 1.00 17.67 ? 302 TYR A CD2 1 ATOM 2301 C CE1 . TYR A 1 302 ? -39.094 10.167 59.857 1.00 18.30 ? 302 TYR A CE1 1 ATOM 2302 C CE2 . TYR A 1 302 ? -39.679 12.051 61.201 1.00 18.05 ? 302 TYR A CE2 1 ATOM 2303 C CZ . TYR A 1 302 ? -38.742 11.154 60.744 1.00 17.82 ? 302 TYR A CZ 1 ATOM 2304 O OH . TYR A 1 302 ? -37.430 11.282 61.108 1.00 18.14 ? 302 TYR A OH 1 ATOM 2305 N N . GLY A 1 303 ? -41.226 11.847 56.652 1.00 16.44 ? 303 GLY A N 1 ATOM 2306 C CA . GLY A 1 303 ? -40.252 11.400 55.659 1.00 17.15 ? 303 GLY A CA 1 ATOM 2307 C C . GLY A 1 303 ? -40.492 12.070 54.314 1.00 17.94 ? 303 GLY A C 1 ATOM 2308 O O . GLY A 1 303 ? -41.199 13.090 54.242 1.00 18.25 ? 303 GLY A O 1 ATOM 2309 N N . ALA A 1 304 ? -39.904 11.513 53.261 1.00 18.76 ? 304 ALA A N 1 ATOM 2310 C CA . ALA A 1 304 ? -40.039 12.046 51.899 1.00 18.81 ? 304 ALA A CA 1 ATOM 2311 C C . ALA A 1 304 ? -41.399 11.630 51.351 1.00 19.00 ? 304 ALA A C 1 ATOM 2312 O O . ALA A 1 304 ? -41.573 10.503 50.884 1.00 19.49 ? 304 ALA A O 1 ATOM 2313 C CB . ALA A 1 304 ? -38.913 11.546 51.001 1.00 19.45 ? 304 ALA A CB 1 ATOM 2314 N N . CYS A 1 305 ? -42.365 12.539 51.446 1.00 18.38 ? 305 CYS A N 1 ATOM 2315 C CA . CYS A 1 305 ? -43.769 12.207 51.217 1.00 18.43 ? 305 CYS A CA 1 ATOM 2316 C C . CYS A 1 305 ? -44.431 13.088 50.167 1.00 17.41 ? 305 CYS A C 1 ATOM 2317 O O . CYS A 1 305 ? -44.144 14.276 50.097 1.00 17.40 ? 305 CYS A O 1 ATOM 2318 C CB . CYS A 1 305 ? -44.547 12.362 52.522 1.00 19.20 ? 305 CYS A CB 1 ATOM 2319 S SG . CYS A 1 305 ? -44.229 11.070 53.726 1.00 20.55 ? 305 CYS A SG 1 ATOM 2320 N N . PRO A 1 306 ? -45.328 12.511 49.351 1.00 16.61 ? 306 PRO A N 1 ATOM 2321 C CA . PRO A 1 306 ? -46.196 13.365 48.535 1.00 16.22 ? 306 PRO A CA 1 ATOM 2322 C C . PRO A 1 306 ? -47.002 14.333 49.417 1.00 15.63 ? 306 PRO A C 1 ATOM 2323 O O . PRO A 1 306 ? -47.274 14.045 50.589 1.00 14.97 ? 306 PRO A O 1 ATOM 2324 C CB . PRO A 1 306 ? -47.124 12.360 47.828 1.00 16.54 ? 306 PRO A CB 1 ATOM 2325 C CG . PRO A 1 306 ? -46.459 11.024 47.997 1.00 16.92 ? 306 PRO A CG 1 ATOM 2326 C CD . PRO A 1 306 ? -45.733 11.104 49.293 1.00 16.76 ? 306 PRO A CD 1 ATOM 2327 N N . ARG A 1 307 ? -47.390 15.472 48.848 1.00 15.76 ? 307 ARG A N 1 ATOM 2328 C CA . ARG A 1 307 ? -48.145 16.463 49.596 1.00 15.37 ? 307 ARG A CA 1 ATOM 2329 C C . ARG A 1 307 ? -49.612 16.028 49.663 1.00 14.86 ? 307 ARG A C 1 ATOM 2330 O O . ARG A 1 307 ? -50.189 15.564 48.651 1.00 14.20 ? 307 ARG A O 1 ATOM 2331 C CB . ARG A 1 307 ? -48.015 17.840 48.936 1.00 15.54 ? 307 ARG A CB 1 ATOM 2332 C CG . ARG A 1 307 ? -46.627 18.456 49.146 1.00 16.21 ? 307 ARG A CG 1 ATOM 2333 C CD . ARG A 1 307 ? -46.619 19.922 48.760 1.00 15.93 ? 307 ARG A CD 1 ATOM 2334 N NE . ARG A 1 307 ? -45.323 20.544 49.039 1.00 16.47 ? 307 ARG A NE 1 ATOM 2335 C CZ . ARG A 1 307 ? -44.939 21.026 50.214 1.00 16.78 ? 307 ARG A CZ 1 ATOM 2336 N NH1 . ARG A 1 307 ? -45.697 20.937 51.292 1.00 16.66 ? 307 ARG A NH1 1 ATOM 2337 N NH2 . ARG A 1 307 ? -43.751 21.590 50.311 1.00 18.24 ? 307 ARG A NH2 1 ATOM 2338 N N . TYR A 1 308 ? -50.207 16.226 50.833 1.00 14.28 ? 308 TYR A N 1 ATOM 2339 C CA . TYR A 1 308 ? -51.617 15.895 51.065 1.00 14.38 ? 308 TYR A CA 1 ATOM 2340 C C . TYR A 1 308 ? -52.549 16.857 50.342 1.00 14.42 ? 308 TYR A C 1 ATOM 2341 O O . TYR A 1 308 ? -52.403 18.089 50.450 1.00 14.64 ? 308 TYR A O 1 ATOM 2342 C CB . TYR A 1 308 ? -51.956 15.867 52.547 1.00 14.54 ? 308 TYR A CB 1 ATOM 2343 C CG . TYR A 1 308 ? -53.391 15.431 52.813 1.00 15.04 ? 308 TYR A CG 1 ATOM 2344 C CD1 . TYR A 1 308 ? -53.729 14.084 52.803 1.00 15.66 ? 308 TYR A CD1 1 ATOM 2345 C CD2 . TYR A 1 308 ? -54.407 16.366 52.970 1.00 15.73 ? 308 TYR A CD2 1 ATOM 2346 C CE1 . TYR A 1 308 ? -55.025 13.664 53.036 1.00 16.28 ? 308 TYR A CE1 1 ATOM 2347 C CE2 . TYR A 1 308 ? -55.717 15.965 53.178 1.00 16.33 ? 308 TYR A CE2 1 ATOM 2348 C CZ . TYR A 1 308 ? -56.009 14.597 53.203 1.00 16.64 ? 308 TYR A CZ 1 ATOM 2349 O OH . TYR A 1 308 ? -57.293 14.190 53.417 1.00 17.77 ? 308 TYR A OH 1 ATOM 2350 N N . VAL A 1 309 ? -53.498 16.295 49.594 1.00 14.33 ? 309 VAL A N 1 ATOM 2351 C CA . VAL A 1 309 ? -54.511 17.095 48.912 1.00 14.29 ? 309 VAL A CA 1 ATOM 2352 C C . VAL A 1 309 ? -55.879 16.472 49.173 1.00 15.61 ? 309 VAL A C 1 ATOM 2353 O O . VAL A 1 309 ? -55.973 15.296 49.557 1.00 15.12 ? 309 VAL A O 1 ATOM 2354 C CB . VAL A 1 309 ? -54.241 17.207 47.401 1.00 13.72 ? 309 VAL A CB 1 ATOM 2355 C CG1 . VAL A 1 309 ? -52.916 17.948 47.140 1.00 13.57 ? 309 VAL A CG1 1 ATOM 2356 C CG2 . VAL A 1 309 ? -54.235 15.842 46.715 1.00 13.53 ? 309 VAL A CG2 1 ATOM 2357 N N . LYS A 1 310 ? -56.931 17.244 48.930 1.00 17.00 ? 310 LYS A N 1 ATOM 2358 C CA . LYS A 1 310 ? -58.306 16.751 49.086 1.00 18.64 ? 310 LYS A CA 1 ATOM 2359 C C . LYS A 1 310 ? -58.797 15.842 47.948 1.00 18.86 ? 310 LYS A C 1 ATOM 2360 O O . LYS A 1 310 ? -59.677 15.011 48.170 1.00 17.75 ? 310 LYS A O 1 ATOM 2361 C CB . LYS A 1 310 ? -59.243 17.936 49.271 1.00 21.06 ? 310 LYS A CB 1 ATOM 2362 C CG . LYS A 1 310 ? -58.985 18.609 50.619 1.00 23.90 ? 310 LYS A CG 1 ATOM 2363 C CD . LYS A 1 310 ? -59.983 19.722 50.935 1.00 27.55 ? 310 LYS A CD 1 ATOM 2364 C CE . LYS A 1 310 ? -60.118 20.695 49.786 1.00 30.18 ? 310 LYS A CE 1 ATOM 2365 N NZ . LYS A 1 310 ? -60.888 21.919 50.189 1.00 34.81 ? 310 LYS A NZ 1 ATOM 2366 N N . GLN A 1 311 ? -58.242 16.003 46.749 1.00 17.34 ? 311 GLN A N 1 ATOM 2367 C CA . GLN A 1 311 ? -58.655 15.238 45.603 1.00 18.06 ? 311 GLN A CA 1 ATOM 2368 C C . GLN A 1 311 ? -58.264 13.776 45.790 1.00 19.52 ? 311 GLN A C 1 ATOM 2369 O O . GLN A 1 311 ? -57.184 13.467 46.290 1.00 18.35 ? 311 GLN A O 1 ATOM 2370 C CB . GLN A 1 311 ? -58.006 15.781 44.319 1.00 17.57 ? 311 GLN A CB 1 ATOM 2371 C CG . GLN A 1 311 ? -58.398 17.214 43.927 1.00 17.06 ? 311 GLN A CG 1 ATOM 2372 C CD . GLN A 1 311 ? -57.421 18.261 44.440 1.00 16.81 ? 311 GLN A CD 1 ATOM 2373 O OE1 . GLN A 1 311 ? -56.874 18.129 45.533 1.00 15.59 ? 311 GLN A OE1 1 ATOM 2374 N NE2 . GLN A 1 311 ? -57.195 19.303 43.638 1.00 15.88 ? 311 GLN A NE2 1 ATOM 2375 N N . ASN A 1 312 ? -59.131 12.870 45.358 1.00 20.60 ? 312 ASN A N 1 ATOM 2376 C CA . ASN A 1 312 ? -58.753 11.459 45.376 1.00 22.90 ? 312 ASN A CA 1 ATOM 2377 C C . ASN A 1 312 ? -58.144 10.951 44.067 1.00 21.58 ? 312 ASN A C 1 ATOM 2378 O O . ASN A 1 312 ? -57.599 9.843 44.039 1.00 21.85 ? 312 ASN A O 1 ATOM 2379 C CB . ASN A 1 312 ? -59.907 10.582 45.849 1.00 26.10 ? 312 ASN A CB 1 ATOM 2380 C CG . ASN A 1 312 ? -61.151 10.800 45.079 1.00 29.22 ? 312 ASN A CG 1 ATOM 2381 O OD1 . ASN A 1 312 ? -61.113 10.985 43.871 1.00 32.48 ? 312 ASN A OD1 1 ATOM 2382 N ND2 . ASN A 1 312 ? -62.294 10.772 45.776 1.00 35.85 ? 312 ASN A ND2 1 ATOM 2383 N N . THR A 1 313 ? -58.179 11.786 43.026 1.00 19.44 ? 313 THR A N 1 ATOM 2384 C CA . THR A 1 313 ? -57.538 11.499 41.757 1.00 19.28 ? 313 THR A CA 1 ATOM 2385 C C . THR A 1 313 ? -57.214 12.785 41.009 1.00 18.61 ? 313 THR A C 1 ATOM 2386 O O . THR A 1 313 ? -57.985 13.735 41.038 1.00 18.50 ? 313 THR A O 1 ATOM 2387 C CB . THR A 1 313 ? -58.439 10.585 40.861 1.00 20.31 ? 313 THR A CB 1 ATOM 2388 O OG1 . THR A 1 313 ? -57.789 10.374 39.611 1.00 20.47 ? 313 THR A OG1 1 ATOM 2389 C CG2 . THR A 1 313 ? -59.809 11.215 40.608 1.00 20.42 ? 313 THR A CG2 1 ATOM 2390 N N . LEU A 1 314 ? -56.044 12.822 40.377 1.00 18.26 ? 314 LEU A N 1 ATOM 2391 C CA . LEU A 1 314 ? -55.703 13.856 39.439 1.00 18.19 ? 314 LEU A CA 1 ATOM 2392 C C . LEU A 1 314 ? -54.917 13.220 38.314 1.00 18.51 ? 314 LEU A C 1 ATOM 2393 O O . LEU A 1 314 ? -53.785 12.780 38.532 1.00 18.09 ? 314 LEU A O 1 ATOM 2394 C CB . LEU A 1 314 ? -54.843 14.923 40.120 1.00 17.88 ? 314 LEU A CB 1 ATOM 2395 C CG . LEU A 1 314 ? -55.524 15.906 41.050 1.00 17.94 ? 314 LEU A CG 1 ATOM 2396 C CD1 . LEU A 1 314 ? -54.469 16.684 41.825 1.00 17.64 ? 314 LEU A CD1 1 ATOM 2397 C CD2 . LEU A 1 314 ? -56.442 16.857 40.259 1.00 18.12 ? 314 LEU A CD2 1 ATOM 2398 N N . LYS A 1 315 ? -55.485 13.182 37.117 1.00 18.12 ? 315 LYS A N 1 ATOM 2399 C CA . LYS A 1 315 ? -54.842 12.471 36.021 1.00 19.34 ? 315 LYS A CA 1 ATOM 2400 C C . LYS A 1 315 ? -54.037 13.398 35.121 1.00 18.09 ? 315 LYS A C 1 ATOM 2401 O O . LYS A 1 315 ? -54.576 14.351 34.590 1.00 17.33 ? 315 LYS A O 1 ATOM 2402 C CB . LYS A 1 315 ? -55.904 11.760 35.177 1.00 21.67 ? 315 LYS A CB 1 ATOM 2403 C CG . LYS A 1 315 ? -56.660 10.719 35.970 1.00 24.79 ? 315 LYS A CG 1 ATOM 2404 C CD . LYS A 1 315 ? -55.774 9.532 36.284 1.00 27.23 ? 315 LYS A CD 1 ATOM 2405 C CE . LYS A 1 315 ? -55.786 8.538 35.124 1.00 31.11 ? 315 LYS A CE 1 ATOM 2406 N NZ . LYS A 1 315 ? -54.576 7.655 35.143 1.00 35.24 ? 315 LYS A NZ 1 ATOM 2407 N N . LEU A 1 316 ? -52.761 13.086 34.944 1.00 17.37 ? 316 LEU A N 1 ATOM 2408 C CA . LEU A 1 316 ? -51.882 13.846 34.065 1.00 17.31 ? 316 LEU A CA 1 ATOM 2409 C C . LEU A 1 316 ? -51.859 13.143 32.720 1.00 17.16 ? 316 LEU A C 1 ATOM 2410 O O . LEU A 1 316 ? -51.500 11.976 32.651 1.00 17.07 ? 316 LEU A O 1 ATOM 2411 C CB . LEU A 1 316 ? -50.473 13.843 34.619 1.00 17.35 ? 316 LEU A CB 1 ATOM 2412 C CG . LEU A 1 316 ? -49.434 14.635 33.834 1.00 17.56 ? 316 LEU A CG 1 ATOM 2413 C CD1 . LEU A 1 316 ? -49.583 16.118 34.157 1.00 17.33 ? 316 LEU A CD1 1 ATOM 2414 C CD2 . LEU A 1 316 ? -48.023 14.147 34.172 1.00 17.87 ? 316 LEU A CD2 1 ATOM 2415 N N . ALA A 1 317 ? -52.245 13.857 31.678 1.00 17.46 ? 317 ALA A N 1 ATOM 2416 C CA . ALA A 1 317 ? -52.138 13.372 30.312 1.00 17.87 ? 317 ALA A CA 1 ATOM 2417 C C . ALA A 1 317 ? -50.697 12.996 29.962 1.00 18.47 ? 317 ALA A C 1 ATOM 2418 O O . ALA A 1 317 ? -49.762 13.755 30.250 1.00 18.17 ? 317 ALA A O 1 ATOM 2419 C CB . ALA A 1 317 ? -52.675 14.430 29.349 1.00 17.91 ? 317 ALA A CB 1 ATOM 2420 N N . THR A 1 318 ? -50.524 11.805 29.378 1.00 18.54 ? 318 THR A N 1 ATOM 2421 C CA . THR A 1 318 ? -49.225 11.376 28.882 1.00 19.26 ? 318 THR A CA 1 ATOM 2422 C C . THR A 1 318 ? -49.312 11.011 27.393 1.00 20.35 ? 318 THR A C 1 ATOM 2423 O O . THR A 1 318 ? -48.487 10.262 26.865 1.00 22.10 ? 318 THR A O 1 ATOM 2424 C CB . THR A 1 318 ? -48.687 10.188 29.695 1.00 19.10 ? 318 THR A CB 1 ATOM 2425 O OG1 . THR A 1 318 ? -49.609 9.105 29.617 1.00 19.59 ? 318 THR A OG1 1 ATOM 2426 C CG2 . THR A 1 318 ? -48.440 10.587 31.192 1.00 19.34 ? 318 THR A CG2 1 ATOM 2427 N N . GLY A 1 319 ? -50.311 11.557 26.719 1.00 20.19 ? 319 GLY A N 1 ATOM 2428 C CA . GLY A 1 319 ? -50.490 11.338 25.297 1.00 20.44 ? 319 GLY A CA 1 ATOM 2429 C C . GLY A 1 319 ? -51.376 12.419 24.738 1.00 20.13 ? 319 GLY A C 1 ATOM 2430 O O . GLY A 1 319 ? -51.918 13.246 25.489 1.00 19.40 ? 319 GLY A O 1 ATOM 2431 N N . MET A 1 320 ? -51.520 12.427 23.419 1.00 19.76 ? 320 MET A N 1 ATOM 2432 C CA . MET A 1 320 ? -52.298 13.440 22.729 1.00 19.67 ? 320 MET A CA 1 ATOM 2433 C C . MET A 1 320 ? -53.794 13.181 22.833 1.00 20.44 ? 320 MET A C 1 ATOM 2434 O O . MET A 1 320 ? -54.228 12.135 23.334 1.00 20.94 ? 320 MET A O 1 ATOM 2435 C CB . MET A 1 320 ? -51.911 13.467 21.249 1.00 19.93 ? 320 MET A CB 1 ATOM 2436 C CG . MET A 1 320 ? -52.279 12.209 20.478 1.00 20.17 ? 320 MET A CG 1 ATOM 2437 S SD . MET A 1 320 ? -51.794 12.328 18.755 1.00 21.04 ? 320 MET A SD 1 ATOM 2438 C CE . MET A 1 320 ? -50.041 12.016 18.888 1.00 20.29 ? 320 MET A CE 1 ATOM 2439 N N . ARG A 1 321 ? -54.585 14.106 22.311 1.00 20.64 ? 321 ARG A N 1 ATOM 2440 C CA . ARG A 1 321 ? -56.019 13.885 22.194 1.00 22.51 ? 321 ARG A CA 1 ATOM 2441 C C . ARG A 1 321 ? -56.298 12.575 21.440 1.00 22.90 ? 321 ARG A C 1 ATOM 2442 O O . ARG A 1 321 ? -55.633 12.264 20.438 1.00 21.18 ? 321 ARG A O 1 ATOM 2443 C CB . ARG A 1 321 ? -56.703 15.039 21.477 1.00 23.59 ? 321 ARG A CB 1 ATOM 2444 C CG . ARG A 1 321 ? -56.218 15.249 20.049 1.00 26.19 ? 321 ARG A CG 1 ATOM 2445 C CD . ARG A 1 321 ? -56.928 16.400 19.344 1.00 28.75 ? 321 ARG A CD 1 ATOM 2446 N NE . ARG A 1 321 ? -56.524 17.708 19.855 1.00 28.77 ? 321 ARG A NE 1 ATOM 2447 C CZ . ARG A 1 321 ? -57.287 18.529 20.565 1.00 29.03 ? 321 ARG A CZ 1 ATOM 2448 N NH1 . ARG A 1 321 ? -58.522 18.211 20.922 1.00 30.62 ? 321 ARG A NH1 1 ATOM 2449 N NH2 . ARG A 1 321 ? -56.797 19.700 20.930 1.00 31.04 ? 321 ARG A NH2 1 ATOM 2450 N N . ASN A 1 322 ? -57.271 11.823 21.936 1.00 22.81 ? 322 ASN A N 1 ATOM 2451 C CA . ASN A 1 322 ? -57.683 10.574 21.314 1.00 24.85 ? 322 ASN A CA 1 ATOM 2452 C C . ASN A 1 322 ? -58.929 10.817 20.462 1.00 25.65 ? 322 ASN A C 1 ATOM 2453 O O . ASN A 1 322 ? -59.956 11.259 20.966 1.00 25.23 ? 322 ASN A O 1 ATOM 2454 C CB . ASN A 1 322 ? -57.964 9.509 22.371 1.00 25.32 ? 322 ASN A CB 1 ATOM 2455 C CG . ASN A 1 322 ? -57.937 8.106 21.799 1.00 25.53 ? 322 ASN A CG 1 ATOM 2456 O OD1 . ASN A 1 322 ? -57.085 7.771 20.963 1.00 25.00 ? 322 ASN A OD1 1 ATOM 2457 N ND2 . ASN A 1 322 ? -58.880 7.270 22.247 1.00 25.98 ? 322 ASN A ND2 1 ATOM 2458 N N . VAL A 1 323 ? -58.809 10.581 19.159 1.00 26.55 ? 323 VAL A N 1 ATOM 2459 C CA . VAL A 1 323 ? -59.834 10.976 18.203 1.00 27.71 ? 323 VAL A CA 1 ATOM 2460 C C . VAL A 1 323 ? -60.212 9.731 17.381 1.00 30.03 ? 323 VAL A C 1 ATOM 2461 O O . VAL A 1 323 ? -59.359 9.127 16.740 1.00 28.95 ? 323 VAL A O 1 ATOM 2462 C CB . VAL A 1 323 ? -59.339 12.135 17.282 1.00 28.26 ? 323 VAL A CB 1 ATOM 2463 C CG1 . VAL A 1 323 ? -60.439 12.633 16.347 1.00 28.34 ? 323 VAL A CG1 1 ATOM 2464 C CG2 . VAL A 1 323 ? -58.835 13.306 18.112 1.00 27.65 ? 323 VAL A CG2 1 ATOM 2465 N N . PRO A 1 324 ? -61.492 9.336 17.410 1.00 33.89 ? 324 PRO A N 1 ATOM 2466 C CA . PRO A 1 324 ? -61.906 8.161 16.610 1.00 35.55 ? 324 PRO A CA 1 ATOM 2467 C C . PRO A 1 324 ? -61.579 8.306 15.132 1.00 36.31 ? 324 PRO A C 1 ATOM 2468 O O . PRO A 1 324 ? -61.532 9.427 14.604 1.00 36.99 ? 324 PRO A O 1 ATOM 2469 C CB . PRO A 1 324 ? -63.426 8.113 16.798 1.00 36.10 ? 324 PRO A CB 1 ATOM 2470 C CG . PRO A 1 324 ? -63.822 9.488 17.196 1.00 36.19 ? 324 PRO A CG 1 ATOM 2471 C CD . PRO A 1 324 ? -62.653 10.089 17.932 1.00 34.78 ? 324 PRO A CD 1 ATOM 2472 N N . GLU A 1 325 ? -61.328 7.183 14.478 1.00 39.19 ? 325 GLU A N 1 ATOM 2473 C CA . GLU A 1 325 ? -61.143 7.176 13.034 1.00 42.08 ? 325 GLU A CA 1 ATOM 2474 C C . GLU A 1 325 ? -62.499 7.270 12.339 1.00 47.28 ? 325 GLU A C 1 ATOM 2475 O O . GLU A 1 325 ? -63.390 6.482 12.627 1.00 46.64 ? 325 GLU A O 1 ATOM 2476 C CB . GLU A 1 325 ? -60.412 5.908 12.596 1.00 41.63 ? 325 GLU A CB 1 ATOM 2477 C CG . GLU A 1 325 ? -59.973 5.969 11.136 1.00 41.15 ? 325 GLU A CG 1 ATOM 2478 C CD . GLU A 1 325 ? -58.677 5.238 10.869 1.00 40.25 ? 325 GLU A CD 1 ATOM 2479 O OE1 . GLU A 1 325 ? -58.231 4.443 11.740 1.00 38.60 ? 325 GLU A OE1 1 ATOM 2480 O OE2 . GLU A 1 325 ? -58.107 5.466 9.775 1.00 38.60 ? 325 GLU A OE2 1 ATOM 2481 N N . LYS A 1 326 ? -62.659 8.240 11.440 1.00 52.37 ? 326 LYS A N 1 ATOM 2482 C CA . LYS A 1 326 ? -63.928 8.393 10.723 1.00 59.40 ? 326 LYS A CA 1 ATOM 2483 C C . LYS A 1 326 ? -64.132 7.201 9.773 1.00 63.38 ? 326 LYS A C 1 ATOM 2484 O O . LYS A 1 326 ? -63.183 6.717 9.143 1.00 60.48 ? 326 LYS A O 1 ATOM 2485 C CB . LYS A 1 326 ? -64.011 9.742 9.987 1.00 59.54 ? 326 LYS A CB 1 ATOM 2486 C CG . LYS A 1 326 ? -63.087 9.877 8.784 1.00 62.40 ? 326 LYS A CG 1 ATOM 2487 C CD . LYS A 1 326 ? -63.220 11.243 8.113 1.00 62.66 ? 326 LYS A CD 1 ATOM 2488 C CE . LYS A 1 326 ? -62.242 11.405 6.951 1.00 62.11 ? 326 LYS A CE 1 ATOM 2489 N NZ . LYS A 1 326 ? -62.242 10.232 6.023 1.00 60.34 ? 326 LYS A NZ 1 ATOM 2490 N N . GLN A 1 327 ? -65.376 6.741 9.692 1.00 69.93 ? 327 GLN A N 1 ATOM 2491 C CA . GLN A 1 327 ? -65.705 5.454 9.075 1.00 76.14 ? 327 GLN A CA 1 ATOM 2492 C C . GLN A 1 327 ? -65.658 5.517 7.543 1.00 77.74 ? 327 GLN A C 1 ATOM 2493 O O . GLN A 1 327 ? -66.024 6.529 6.944 1.00 77.01 ? 327 GLN A O 1 ATOM 2494 C CB . GLN A 1 327 ? -67.090 4.997 9.548 1.00 78.79 ? 327 GLN A CB 1 ATOM 2495 C CG . GLN A 1 327 ? -67.279 3.489 9.602 1.00 81.11 ? 327 GLN A CG 1 ATOM 2496 C CD . GLN A 1 327 ? -68.715 3.097 9.903 1.00 82.01 ? 327 GLN A CD 1 ATOM 2497 O OE1 . GLN A 1 327 ? -68.982 2.357 10.848 1.00 83.51 ? 327 GLN A OE1 1 ATOM 2498 N NE2 . GLN A 1 327 ? -69.648 3.600 9.100 1.00 80.78 ? 327 GLN A NE2 1 ATOM 2499 N N . THR A 1 328 ? -65.210 4.425 6.924 1.00 82.74 ? 328 THR A N 1 ATOM 2500 C CA . THR A 1 328 ? -65.040 4.355 5.468 1.00 84.04 ? 328 THR A CA 1 ATOM 2501 C C . THR A 1 328 ? -65.469 2.989 4.926 1.00 83.85 ? 328 THR A C 1 ATOM 2502 O O . THR A 1 328 ? -66.617 2.806 4.520 1.00 82.15 ? 328 THR A O 1 ATOM 2503 C CB . THR A 1 328 ? -63.573 4.628 5.067 1.00 84.55 ? 328 THR A CB 1 ATOM 2504 O OG1 . THR A 1 328 ? -63.477 4.788 3.646 1.00 83.54 ? 328 THR A OG1 1 ATOM 2505 C CG2 . THR A 1 328 ? -62.653 3.484 5.522 1.00 83.38 ? 328 THR A CG2 1 ATOM 2506 N N . ALA A 1 334 ? -61.196 6.396 0.323 1.00 48.79 ? 334 ALA A N 1 ATOM 2507 C CA . ALA A 1 334 ? -60.206 7.463 0.235 1.00 45.72 ? 334 ALA A CA 1 ATOM 2508 C C . ALA A 1 334 ? -59.494 7.631 1.585 1.00 44.48 ? 334 ALA A C 1 ATOM 2509 O O . ALA A 1 334 ? -60.145 7.845 2.617 1.00 45.57 ? 334 ALA A O 1 ATOM 2510 C CB . ALA A 1 334 ? -60.874 8.764 -0.189 1.00 47.43 ? 334 ALA A CB 1 ATOM 2511 N N . ILE A 1 335 ? -58.164 7.505 1.589 1.00 38.67 ? 335 ILE A N 1 ATOM 2512 C CA . ILE A 1 335 ? -57.389 7.817 2.791 1.00 33.77 ? 335 ILE A CA 1 ATOM 2513 C C . ILE A 1 335 ? -57.658 9.266 3.228 1.00 31.47 ? 335 ILE A C 1 ATOM 2514 O O . ILE A 1 335 ? -58.118 10.081 2.450 1.00 30.08 ? 335 ILE A O 1 ATOM 2515 C CB . ILE A 1 335 ? -55.880 7.563 2.606 1.00 32.72 ? 335 ILE A CB 1 ATOM 2516 C CG1 . ILE A 1 335 ? -55.320 8.329 1.402 1.00 32.47 ? 335 ILE A CG1 1 ATOM 2517 C CG2 . ILE A 1 335 ? -55.609 6.073 2.468 1.00 33.71 ? 335 ILE A CG2 1 ATOM 2518 C CD1 . ILE A 1 335 ? -53.810 8.418 1.395 1.00 30.09 ? 335 ILE A CD1 1 ATOM 2519 N N . ALA A 1 336 ? -57.392 9.571 4.487 1.00 29.14 ? 336 ALA A N 1 ATOM 2520 C CA . ALA A 1 336 ? -57.707 10.888 5.020 1.00 28.71 ? 336 ALA A CA 1 ATOM 2521 C C . ALA A 1 336 ? -56.724 11.204 6.133 1.00 27.17 ? 336 ALA A C 1 ATOM 2522 O O . ALA A 1 336 ? -56.168 10.299 6.744 1.00 26.87 ? 336 ALA A O 1 ATOM 2523 C CB . ALA A 1 336 ? -59.145 10.938 5.523 1.00 29.61 ? 336 ALA A CB 1 ATOM 2524 N N . GLY A 1 337 ? -56.477 12.487 6.347 1.00 26.11 ? 337 GLY A N 1 ATOM 2525 C CA . GLY A 1 337 ? -55.467 12.939 7.289 1.00 25.84 ? 337 GLY A CA 1 ATOM 2526 C C . GLY A 1 337 ? -56.066 13.334 8.620 1.00 25.41 ? 337 GLY A C 1 ATOM 2527 O O . GLY A 1 337 ? -57.190 12.964 8.933 1.00 25.16 ? 337 GLY A O 1 ATOM 2528 N N . PHE A 1 338 ? -55.316 14.124 9.377 1.00 25.27 ? 338 PHE A N 1 ATOM 2529 C CA . PHE A 1 338 ? -55.636 14.380 10.784 1.00 26.40 ? 338 PHE A CA 1 ATOM 2530 C C . PHE A 1 338 ? -56.860 15.261 11.063 1.00 27.23 ? 338 PHE A C 1 ATOM 2531 O O . PHE A 1 338 ? -57.292 15.335 12.203 1.00 28.21 ? 338 PHE A O 1 ATOM 2532 C CB . PHE A 1 338 ? -54.436 14.969 11.517 1.00 25.14 ? 338 PHE A CB 1 ATOM 2533 C CG . PHE A 1 338 ? -54.065 16.353 11.066 1.00 25.62 ? 338 PHE A CG 1 ATOM 2534 C CD1 . PHE A 1 338 ? -53.234 16.541 9.981 1.00 25.52 ? 338 PHE A CD1 1 ATOM 2535 C CD2 . PHE A 1 338 ? -54.541 17.475 11.741 1.00 26.98 ? 338 PHE A CD2 1 ATOM 2536 C CE1 . PHE A 1 338 ? -52.881 17.811 9.561 1.00 26.53 ? 338 PHE A CE1 1 ATOM 2537 C CE2 . PHE A 1 338 ? -54.193 18.750 11.328 1.00 27.09 ? 338 PHE A CE2 1 ATOM 2538 C CZ . PHE A 1 338 ? -53.364 18.921 10.233 1.00 26.95 ? 338 PHE A CZ 1 ATOM 2539 N N . ILE A 1 339 ? -57.404 15.944 10.070 1.00 28.83 ? 339 ILE A N 1 ATOM 2540 C CA . ILE A 1 339 ? -58.530 16.837 10.328 1.00 31.17 ? 339 ILE A CA 1 ATOM 2541 C C . ILE A 1 339 ? -59.727 16.004 10.858 1.00 33.50 ? 339 ILE A C 1 ATOM 2542 O O . ILE A 1 339 ? -60.280 15.182 10.152 1.00 33.94 ? 339 ILE A O 1 ATOM 2543 C CB . ILE A 1 339 ? -58.912 17.657 9.075 1.00 31.53 ? 339 ILE A CB 1 ATOM 2544 C CG1 . ILE A 1 339 ? -57.734 18.507 8.594 1.00 30.99 ? 339 ILE A CG1 1 ATOM 2545 C CG2 . ILE A 1 339 ? -60.124 18.539 9.367 1.00 32.35 ? 339 ILE A CG2 1 ATOM 2546 C CD1 . ILE A 1 339 ? -57.295 19.582 9.561 1.00 31.33 ? 339 ILE A CD1 1 ATOM 2547 N N . GLU A 1 340 ? -60.049 16.179 12.137 1.00 37.60 ? 340 GLU A N 1 ATOM 2548 C CA . GLU A 1 340 ? -61.133 15.436 12.821 1.00 40.96 ? 340 GLU A CA 1 ATOM 2549 C C . GLU A 1 340 ? -61.073 13.914 12.648 1.00 37.85 ? 340 GLU A C 1 ATOM 2550 O O . GLU A 1 340 ? -62.091 13.270 12.435 1.00 38.41 ? 340 GLU A O 1 ATOM 2551 C CB . GLU A 1 340 ? -62.505 15.945 12.347 1.00 44.83 ? 340 GLU A CB 1 ATOM 2552 C CG . GLU A 1 340 ? -62.695 17.449 12.458 1.00 49.43 ? 340 GLU A CG 1 ATOM 2553 C CD . GLU A 1 340 ? -62.605 17.964 13.880 1.00 54.22 ? 340 GLU A CD 1 ATOM 2554 O OE1 . GLU A 1 340 ? -62.816 17.174 14.829 1.00 59.37 ? 340 GLU A OE1 1 ATOM 2555 O OE2 . GLU A 1 340 ? -62.330 19.174 14.050 1.00 59.37 ? 340 GLU A OE2 1 ATOM 2556 N N . ASN A 1 341 ? -59.883 13.340 12.780 1.00 36.31 ? 341 ASN A N 1 ATOM 2557 C CA . ASN A 1 341 ? -59.653 11.953 12.401 1.00 33.13 ? 341 ASN A CA 1 ATOM 2558 C C . ASN A 1 341 ? -58.294 11.423 12.893 1.00 31.55 ? 341 ASN A C 1 ATOM 2559 O O . ASN A 1 341 ? -57.262 11.944 12.487 1.00 34.78 ? 341 ASN A O 1 ATOM 2560 C CB . ASN A 1 341 ? -59.685 11.879 10.880 1.00 33.88 ? 341 ASN A CB 1 ATOM 2561 C CG . ASN A 1 341 ? -59.512 10.462 10.358 1.00 33.43 ? 341 ASN A CG 1 ATOM 2562 O OD1 . ASN A 1 341 ? -60.199 9.548 10.813 1.00 33.93 ? 341 ASN A OD1 1 ATOM 2563 N ND2 . ASN A 1 341 ? -58.574 10.272 9.428 1.00 31.71 ? 341 ASN A ND2 1 ATOM 2564 N N . GLY A 1 342 ? -58.294 10.420 13.762 1.00 27.97 ? 342 GLY A N 1 ATOM 2565 C CA . GLY A 1 342 ? -57.068 9.725 14.161 1.00 27.87 ? 342 GLY A CA 1 ATOM 2566 C C . GLY A 1 342 ? -56.940 8.356 13.488 1.00 28.29 ? 342 GLY A C 1 ATOM 2567 O O . GLY A 1 342 ? -57.899 7.844 12.914 1.00 28.72 ? 342 GLY A O 1 ATOM 2568 N N . TRP A 1 343 ? -55.754 7.771 13.562 1.00 27.17 ? 343 TRP A N 1 ATOM 2569 C CA . TRP A 1 343 ? -55.454 6.519 12.882 1.00 28.26 ? 343 TRP A CA 1 ATOM 2570 C C . TRP A 1 343 ? -55.212 5.443 13.891 1.00 29.88 ? 343 TRP A C 1 ATOM 2571 O O . TRP A 1 343 ? -54.126 5.350 14.478 1.00 28.21 ? 343 TRP A O 1 ATOM 2572 C CB . TRP A 1 343 ? -54.216 6.665 12.012 1.00 26.46 ? 343 TRP A CB 1 ATOM 2573 C CG . TRP A 1 343 ? -54.334 7.576 10.815 1.00 24.68 ? 343 TRP A CG 1 ATOM 2574 C CD1 . TRP A 1 343 ? -55.486 8.065 10.200 1.00 24.14 ? 343 TRP A CD1 1 ATOM 2575 C CD2 . TRP A 1 343 ? -53.231 8.103 10.030 1.00 24.05 ? 343 TRP A CD2 1 ATOM 2576 N NE1 . TRP A 1 343 ? -55.173 8.838 9.108 1.00 23.51 ? 343 TRP A NE1 1 ATOM 2577 C CE2 . TRP A 1 343 ? -53.828 8.913 8.963 1.00 23.59 ? 343 TRP A CE2 1 ATOM 2578 C CE3 . TRP A 1 343 ? -51.851 8.010 10.110 1.00 24.42 ? 343 TRP A CE3 1 ATOM 2579 C CZ2 . TRP A 1 343 ? -53.055 9.570 8.031 1.00 23.18 ? 343 TRP A CZ2 1 ATOM 2580 C CZ3 . TRP A 1 343 ? -51.083 8.681 9.156 1.00 23.97 ? 343 TRP A CZ3 1 ATOM 2581 C CH2 . TRP A 1 343 ? -51.675 9.436 8.142 1.00 23.52 ? 343 TRP A CH2 1 ATOM 2582 N N . GLU A 1 344 ? -56.216 4.602 14.109 1.00 33.39 ? 344 GLU A N 1 ATOM 2583 C CA . GLU A 1 344 ? -56.067 3.505 15.064 1.00 36.83 ? 344 GLU A CA 1 ATOM 2584 C C . GLU A 1 344 ? -55.054 2.470 14.598 1.00 36.43 ? 344 GLU A C 1 ATOM 2585 O O . GLU A 1 344 ? -54.363 1.869 15.406 1.00 36.08 ? 344 GLU A O 1 ATOM 2586 C CB . GLU A 1 344 ? -57.424 2.879 15.382 1.00 40.44 ? 344 GLU A CB 1 ATOM 2587 C CG . GLU A 1 344 ? -58.308 3.867 16.130 1.00 43.76 ? 344 GLU A CG 1 ATOM 2588 C CD . GLU A 1 344 ? -59.640 3.298 16.566 1.00 48.28 ? 344 GLU A CD 1 ATOM 2589 O OE1 . GLU A 1 344 ? -59.664 2.140 17.046 1.00 51.02 ? 344 GLU A OE1 1 ATOM 2590 O OE2 . GLU A 1 344 ? -60.656 4.026 16.425 1.00 50.80 ? 344 GLU A OE2 1 ATOM 2591 N N . GLY A 1 345 ? -54.919 2.311 13.291 1.00 36.92 ? 345 GLY A N 1 ATOM 2592 C CA . GLY A 1 345 ? -53.943 1.381 12.746 1.00 36.56 ? 345 GLY A CA 1 ATOM 2593 C C . GLY A 1 345 ? -52.503 1.838 12.759 1.00 37.07 ? 345 GLY A C 1 ATOM 2594 O O . GLY A 1 345 ? -51.638 1.109 12.302 1.00 35.99 ? 345 GLY A O 1 ATOM 2595 N N . MET A 1 346 ? -52.211 3.047 13.244 1.00 37.14 ? 346 MET A N 1 ATOM 2596 C CA . MET A 1 346 ? -50.815 3.434 13.365 1.00 37.64 ? 346 MET A CA 1 ATOM 2597 C C . MET A 1 346 ? -50.296 3.122 14.746 1.00 37.98 ? 346 MET A C 1 ATOM 2598 O O . MET A 1 346 ? -50.559 3.855 15.709 1.00 37.69 ? 346 MET A O 1 ATOM 2599 C CB . MET A 1 346 ? -50.565 4.894 13.061 1.00 39.08 ? 346 MET A CB 1 ATOM 2600 C CG . MET A 1 346 ? -49.070 5.171 13.130 1.00 41.27 ? 346 MET A CG 1 ATOM 2601 S SD . MET A 1 346 ? -48.636 6.476 12.021 1.00 45.57 ? 346 MET A SD 1 ATOM 2602 C CE . MET A 1 346 ? -49.515 7.737 12.938 1.00 41.89 ? 346 MET A CE 1 ATOM 2603 N N . VAL A 1 347 ? -49.500 2.068 14.808 1.00 37.83 ? 347 VAL A N 1 ATOM 2604 C CA . VAL A 1 347 ? -49.069 1.486 16.061 1.00 39.48 ? 347 VAL A CA 1 ATOM 2605 C C . VAL A 1 347 ? -47.557 1.578 16.290 1.00 39.43 ? 347 VAL A C 1 ATOM 2606 O O . VAL A 1 347 ? -47.091 1.285 17.388 1.00 42.13 ? 347 VAL A O 1 ATOM 2607 C CB . VAL A 1 347 ? -49.540 0.018 16.149 1.00 42.07 ? 347 VAL A CB 1 ATOM 2608 C CG1 . VAL A 1 347 ? -51.061 -0.036 16.242 1.00 42.03 ? 347 VAL A CG1 1 ATOM 2609 C CG2 . VAL A 1 347 ? -49.047 -0.793 14.954 1.00 40.75 ? 347 VAL A CG2 1 ATOM 2610 N N . ASP A 1 348 ? -46.784 1.993 15.287 1.00 38.48 ? 348 ASP A N 1 ATOM 2611 C CA . ASP A 1 348 ? -45.332 2.115 15.465 1.00 37.66 ? 348 ASP A CA 1 ATOM 2612 C C . ASP A 1 348 ? -44.846 3.561 15.549 1.00 35.09 ? 348 ASP A C 1 ATOM 2613 O O . ASP A 1 348 ? -43.653 3.835 15.435 1.00 35.46 ? 348 ASP A O 1 ATOM 2614 C CB . ASP A 1 348 ? -44.582 1.348 14.364 1.00 41.12 ? 348 ASP A CB 1 ATOM 2615 C CG . ASP A 1 348 ? -44.770 1.948 12.983 1.00 43.43 ? 348 ASP A CG 1 ATOM 2616 O OD1 . ASP A 1 348 ? -45.741 2.712 12.766 1.00 45.86 ? 348 ASP A OD1 1 ATOM 2617 O OD2 . ASP A 1 348 ? -43.944 1.633 12.098 1.00 47.54 ? 348 ASP A OD2 1 ATOM 2618 N N . GLY A 1 349 ? -45.764 4.487 15.771 1.00 32.37 ? 349 GLY A N 1 ATOM 2619 C CA . GLY A 1 349 ? -45.403 5.888 15.916 1.00 29.99 ? 349 GLY A CA 1 ATOM 2620 C C . GLY A 1 349 ? -46.620 6.699 16.295 1.00 28.14 ? 349 GLY A C 1 ATOM 2621 O O . GLY A 1 349 ? -47.751 6.229 16.186 1.00 27.81 ? 349 GLY A O 1 ATOM 2622 N N . TRP A 1 350 ? -46.400 7.929 16.735 1.00 25.68 ? 350 TRP A N 1 ATOM 2623 C CA . TRP A 1 350 ? -47.509 8.801 17.116 1.00 24.48 ? 350 TRP A CA 1 ATOM 2624 C C . TRP A 1 350 ? -48.021 9.638 15.991 1.00 23.06 ? 350 TRP A C 1 ATOM 2625 O O . TRP A 1 350 ? -49.176 10.038 16.008 1.00 21.90 ? 350 TRP A O 1 ATOM 2626 C CB . TRP A 1 350 ? -47.070 9.721 18.234 1.00 24.23 ? 350 TRP A CB 1 ATOM 2627 C CG . TRP A 1 350 ? -47.018 9.049 19.572 1.00 24.73 ? 350 TRP A CG 1 ATOM 2628 C CD1 . TRP A 1 350 ? -46.934 7.682 19.859 1.00 25.52 ? 350 TRP A CD1 1 ATOM 2629 C CD2 . TRP A 1 350 ? -47.020 9.719 20.857 1.00 23.59 ? 350 TRP A CD2 1 ATOM 2630 N NE1 . TRP A 1 350 ? -46.915 7.476 21.207 1.00 25.66 ? 350 TRP A NE1 1 ATOM 2631 C CE2 . TRP A 1 350 ? -46.937 8.670 21.867 1.00 24.98 ? 350 TRP A CE2 1 ATOM 2632 C CE3 . TRP A 1 350 ? -47.074 11.041 21.256 1.00 23.71 ? 350 TRP A CE3 1 ATOM 2633 C CZ2 . TRP A 1 350 ? -46.945 8.957 23.221 1.00 24.44 ? 350 TRP A CZ2 1 ATOM 2634 C CZ3 . TRP A 1 350 ? -47.055 11.329 22.629 1.00 23.84 ? 350 TRP A CZ3 1 ATOM 2635 C CH2 . TRP A 1 350 ? -46.989 10.312 23.584 1.00 23.94 ? 350 TRP A CH2 1 ATOM 2636 N N . TYR A 1 351 ? -47.143 9.946 15.038 1.00 23.02 ? 351 TYR A N 1 ATOM 2637 C CA . TYR A 1 351 ? -47.483 10.724 13.851 1.00 22.30 ? 351 TYR A CA 1 ATOM 2638 C C . TYR A 1 351 ? -46.910 10.023 12.639 1.00 23.02 ? 351 TYR A C 1 ATOM 2639 O O . TYR A 1 351 ? -45.931 9.287 12.753 1.00 23.09 ? 351 TYR A O 1 ATOM 2640 C CB . TYR A 1 351 ? -46.860 12.113 13.902 1.00 22.47 ? 351 TYR A CB 1 ATOM 2641 C CG . TYR A 1 351 ? -47.132 12.867 15.192 1.00 22.46 ? 351 TYR A CG 1 ATOM 2642 C CD1 . TYR A 1 351 ? -46.277 12.746 16.296 1.00 22.78 ? 351 TYR A CD1 1 ATOM 2643 C CD2 . TYR A 1 351 ? -48.251 13.676 15.313 1.00 22.30 ? 351 TYR A CD2 1 ATOM 2644 C CE1 . TYR A 1 351 ? -46.532 13.431 17.484 1.00 22.31 ? 351 TYR A CE1 1 ATOM 2645 C CE2 . TYR A 1 351 ? -48.516 14.366 16.496 1.00 22.29 ? 351 TYR A CE2 1 ATOM 2646 C CZ . TYR A 1 351 ? -47.652 14.236 17.576 1.00 22.37 ? 351 TYR A CZ 1 ATOM 2647 O OH . TYR A 1 351 ? -47.911 14.916 18.752 1.00 22.24 ? 351 TYR A OH 1 ATOM 2648 N N . GLY A 1 352 ? -47.470 10.297 11.476 1.00 22.97 ? 352 GLY A N 1 ATOM 2649 C CA . GLY A 1 352 ? -46.928 9.708 10.250 1.00 23.79 ? 352 GLY A CA 1 ATOM 2650 C C . GLY A 1 352 ? -47.676 10.085 9.001 1.00 23.78 ? 352 GLY A C 1 ATOM 2651 O O . GLY A 1 352 ? -48.429 11.067 8.970 1.00 22.82 ? 352 GLY A O 1 ATOM 2652 N N . PHE A 1 353 ? -47.439 9.275 7.971 1.00 23.64 ? 353 PHE A N 1 ATOM 2653 C CA . PHE A 1 353 ? -47.822 9.558 6.607 1.00 23.67 ? 353 PHE A CA 1 ATOM 2654 C C . PHE A 1 353 ? -48.606 8.372 6.083 1.00 23.53 ? 353 PHE A C 1 ATOM 2655 O O . PHE A 1 353 ? -48.237 7.227 6.369 1.00 24.12 ? 353 PHE A O 1 ATOM 2656 C CB . PHE A 1 353 ? -46.590 9.663 5.729 1.00 24.47 ? 353 PHE A CB 1 ATOM 2657 C CG . PHE A 1 353 ? -45.689 10.811 6.042 1.00 25.64 ? 353 PHE A CG 1 ATOM 2658 C CD1 . PHE A 1 353 ? -45.892 12.050 5.448 1.00 25.57 ? 353 PHE A CD1 1 ATOM 2659 C CD2 . PHE A 1 353 ? -44.589 10.648 6.877 1.00 26.87 ? 353 PHE A CD2 1 ATOM 2660 C CE1 . PHE A 1 353 ? -45.033 13.096 5.695 1.00 26.76 ? 353 PHE A CE1 1 ATOM 2661 C CE2 . PHE A 1 353 ? -43.733 11.711 7.136 1.00 26.59 ? 353 PHE A CE2 1 ATOM 2662 C CZ . PHE A 1 353 ? -43.949 12.932 6.535 1.00 26.58 ? 353 PHE A CZ 1 ATOM 2663 N N . ARG A 1 354 ? -49.676 8.644 5.350 1.00 23.16 ? 354 ARG A N 1 ATOM 2664 C CA . ARG A 1 354 ? -50.368 7.634 4.538 1.00 24.27 ? 354 ARG A CA 1 ATOM 2665 C C . ARG A 1 354 ? -50.407 8.134 3.115 1.00 24.49 ? 354 ARG A C 1 ATOM 2666 O O . ARG A 1 354 ? -50.614 9.311 2.874 1.00 24.06 ? 354 ARG A O 1 ATOM 2667 C CB . ARG A 1 354 ? -51.795 7.378 5.014 1.00 24.81 ? 354 ARG A CB 1 ATOM 2668 C CG . ARG A 1 354 ? -51.882 6.354 6.122 1.00 25.61 ? 354 ARG A CG 1 ATOM 2669 C CD . ARG A 1 354 ? -53.304 6.118 6.578 1.00 26.48 ? 354 ARG A CD 1 ATOM 2670 N NE . ARG A 1 354 ? -53.303 5.247 7.744 1.00 27.44 ? 354 ARG A NE 1 ATOM 2671 C CZ . ARG A 1 354 ? -54.375 4.909 8.454 1.00 28.23 ? 354 ARG A CZ 1 ATOM 2672 N NH1 . ARG A 1 354 ? -55.578 5.370 8.149 1.00 29.06 ? 354 ARG A NH1 1 ATOM 2673 N NH2 . ARG A 1 354 ? -54.228 4.103 9.490 1.00 29.21 ? 354 ARG A NH2 1 ATOM 2674 N N . HIS A 1 355 ? -50.242 7.235 2.150 1.00 24.89 ? 355 HIS A N 1 ATOM 2675 C CA . HIS A 1 355 ? -50.162 7.668 0.769 1.00 24.41 ? 355 HIS A CA 1 ATOM 2676 C C . HIS A 1 355 ? -50.966 6.765 -0.090 1.00 25.28 ? 355 HIS A C 1 ATOM 2677 O O . HIS A 1 355 ? -51.250 5.623 0.286 1.00 24.16 ? 355 HIS A O 1 ATOM 2678 C CB . HIS A 1 355 ? -48.702 7.744 0.299 1.00 24.91 ? 355 HIS A CB 1 ATOM 2679 C CG . HIS A 1 355 ? -48.015 6.396 0.203 1.00 25.88 ? 355 HIS A CG 1 ATOM 2680 N ND1 . HIS A 1 355 ? -47.236 5.910 1.185 1.00 26.09 ? 355 HIS A ND1 1 ATOM 2681 C CD2 . HIS A 1 355 ? -48.032 5.421 -0.813 1.00 26.48 ? 355 HIS A CD2 1 ATOM 2682 C CE1 . HIS A 1 355 ? -46.778 4.687 0.830 1.00 27.53 ? 355 HIS A CE1 1 ATOM 2683 N NE2 . HIS A 1 355 ? -47.264 4.393 -0.395 1.00 26.59 ? 355 HIS A NE2 1 ATOM 2684 N N . GLN A 1 356 ? -51.380 7.306 -1.228 1.00 26.12 ? 356 GLN A N 1 ATOM 2685 C CA . GLN A 1 356 ? -51.924 6.525 -2.328 1.00 27.38 ? 356 GLN A CA 1 ATOM 2686 C C . GLN A 1 356 ? -51.224 6.940 -3.611 1.00 26.94 ? 356 GLN A C 1 ATOM 2687 O O . GLN A 1 356 ? -51.204 8.127 -3.975 1.00 25.04 ? 356 GLN A O 1 ATOM 2688 C CB . GLN A 1 356 ? -53.421 6.736 -2.476 1.00 30.39 ? 356 GLN A CB 1 ATOM 2689 C CG . GLN A 1 356 ? -54.016 5.886 -3.597 1.00 33.84 ? 356 GLN A CG 1 ATOM 2690 C CD . GLN A 1 356 ? -55.523 5.917 -3.619 1.00 37.97 ? 356 GLN A CD 1 ATOM 2691 O OE1 . GLN A 1 356 ? -56.136 6.922 -3.271 1.00 44.28 ? 356 GLN A OE1 1 ATOM 2692 N NE2 . GLN A 1 356 ? -56.133 4.813 -4.048 1.00 41.89 ? 356 GLN A NE2 1 ATOM 2693 N N . ASN A 1 357 ? -50.636 5.963 -4.300 1.00 26.82 ? 357 ASN A N 1 ATOM 2694 C CA . ASN A 1 357 ? -49.954 6.228 -5.555 1.00 27.01 ? 357 ASN A CA 1 ATOM 2695 C C . ASN A 1 357 ? -50.150 5.041 -6.503 1.00 29.09 ? 357 ASN A C 1 ATOM 2696 O O . ASN A 1 357 ? -51.027 4.206 -6.256 1.00 26.78 ? 357 ASN A O 1 ATOM 2697 C CB . ASN A 1 357 ? -48.474 6.548 -5.295 1.00 27.31 ? 357 ASN A CB 1 ATOM 2698 C CG . ASN A 1 357 ? -47.684 5.366 -4.748 1.00 27.29 ? 357 ASN A CG 1 ATOM 2699 O OD1 . ASN A 1 357 ? -48.177 4.226 -4.704 1.00 27.68 ? 357 ASN A OD1 1 ATOM 2700 N ND2 . ASN A 1 357 ? -46.439 5.624 -4.357 1.00 26.30 ? 357 ASN A ND2 1 ATOM 2701 N N . SER A 1 358 ? -49.357 5.020 -7.582 1.00 31.48 ? 358 SER A N 1 ATOM 2702 C CA . SER A 1 358 ? -49.339 3.956 -8.598 1.00 34.99 ? 358 SER A CA 1 ATOM 2703 C C . SER A 1 358 ? -49.124 2.564 -8.037 1.00 35.19 ? 358 SER A C 1 ATOM 2704 O O . SER A 1 358 ? -49.594 1.585 -8.614 1.00 37.54 ? 358 SER A O 1 ATOM 2705 C CB . SER A 1 358 ? -48.208 4.233 -9.625 1.00 37.29 ? 358 SER A CB 1 ATOM 2706 O OG . SER A 1 358 ? -47.020 4.727 -8.969 1.00 40.55 ? 358 SER A OG 1 ATOM 2707 N N . GLU A 1 359 ? -48.390 2.479 -6.932 1.00 34.61 ? 359 GLU A N 1 ATOM 2708 C CA . GLU A 1 359 ? -47.973 1.207 -6.355 1.00 34.24 ? 359 GLU A CA 1 ATOM 2709 C C . GLU A 1 359 ? -48.825 0.740 -5.166 1.00 33.05 ? 359 GLU A C 1 ATOM 2710 O O . GLU A 1 359 ? -48.538 -0.325 -4.586 1.00 32.97 ? 359 GLU A O 1 ATOM 2711 C CB . GLU A 1 359 ? -46.515 1.312 -5.922 1.00 34.68 ? 359 GLU A CB 1 ATOM 2712 C CG . GLU A 1 359 ? -45.591 1.796 -7.032 1.00 36.07 ? 359 GLU A CG 1 ATOM 2713 C CD . GLU A 1 359 ? -44.132 1.608 -6.690 1.00 37.70 ? 359 GLU A CD 1 ATOM 2714 O OE1 . GLU A 1 359 ? -43.650 0.461 -6.770 1.00 40.60 ? 359 GLU A OE1 1 ATOM 2715 O OE2 . GLU A 1 359 ? -43.455 2.588 -6.314 1.00 38.04 ? 359 GLU A OE2 1 ATOM 2716 N N . GLY A 1 360 ? -49.843 1.524 -4.796 1.00 29.42 ? 360 GLY A N 1 ATOM 2717 C CA . GLY A 1 360 ? -50.785 1.119 -3.751 1.00 28.73 ? 360 GLY A CA 1 ATOM 2718 C C . GLY A 1 360 ? -51.015 2.182 -2.681 1.00 28.29 ? 360 GLY A C 1 ATOM 2719 O O . GLY A 1 360 ? -50.882 3.378 -2.950 1.00 25.47 ? 360 GLY A O 1 ATOM 2720 N N . ILE A 1 361 ? -51.389 1.716 -1.491 1.00 28.91 ? 361 ILE A N 1 ATOM 2721 C CA . ILE A 1 361 ? -51.708 2.566 -0.349 1.00 30.62 ? 361 ILE A CA 1 ATOM 2722 C C . ILE A 1 361 ? -50.862 2.128 0.821 1.00 30.63 ? 361 ILE A C 1 ATOM 2723 O O . ILE A 1 361 ? -50.910 0.953 1.209 1.00 31.32 ? 361 ILE A O 1 ATOM 2724 C CB . ILE A 1 361 ? -53.191 2.451 0.038 1.00 32.26 ? 361 ILE A CB 1 ATOM 2725 C CG1 . ILE A 1 361 ? -54.066 3.011 -1.075 1.00 34.39 ? 361 ILE A CG1 1 ATOM 2726 C CG2 . ILE A 1 361 ? -53.463 3.218 1.338 1.00 34.59 ? 361 ILE A CG2 1 ATOM 2727 C CD1 . ILE A 1 361 ? -55.505 2.533 -1.028 1.00 36.25 ? 361 ILE A CD1 1 ATOM 2728 N N . GLY A 1 362 ? -50.079 3.055 1.373 1.00 29.50 ? 362 GLY A N 1 ATOM 2729 C CA . GLY A 1 362 ? -49.124 2.717 2.413 1.00 29.50 ? 362 GLY A CA 1 ATOM 2730 C C . GLY A 1 362 ? -49.141 3.690 3.584 1.00 29.27 ? 362 GLY A C 1 ATOM 2731 O O . GLY A 1 362 ? -49.777 4.748 3.521 1.00 27.03 ? 362 GLY A O 1 ATOM 2732 N N . GLN A 1 363 ? -48.438 3.295 4.639 1.00 29.26 ? 363 GLN A N 1 ATOM 2733 C CA . GLN A 1 363 ? -48.336 4.050 5.878 1.00 29.37 ? 363 GLN A CA 1 ATOM 2734 C C . GLN A 1 363 ? -46.905 3.964 6.363 1.00 28.97 ? 363 GLN A C 1 ATOM 2735 O O . GLN A 1 363 ? -46.270 2.920 6.214 1.00 28.74 ? 363 GLN A O 1 ATOM 2736 C CB . GLN A 1 363 ? -49.273 3.432 6.911 1.00 30.71 ? 363 GLN A CB 1 ATOM 2737 C CG . GLN A 1 363 ? -49.363 4.149 8.249 1.00 32.29 ? 363 GLN A CG 1 ATOM 2738 C CD . GLN A 1 363 ? -50.333 3.437 9.170 1.00 33.69 ? 363 GLN A CD 1 ATOM 2739 O OE1 . GLN A 1 363 ? -51.530 3.741 9.181 1.00 35.87 ? 363 GLN A OE1 1 ATOM 2740 N NE2 . GLN A 1 363 ? -49.839 2.433 9.895 1.00 35.03 ? 363 GLN A NE2 1 ATOM 2741 N N . ALA A 1 364 ? -46.407 5.048 6.963 1.00 26.79 ? 364 ALA A N 1 ATOM 2742 C CA . ALA A 1 364 ? -45.127 5.055 7.643 1.00 26.70 ? 364 ALA A CA 1 ATOM 2743 C C . ALA A 1 364 ? -45.170 6.078 8.793 1.00 26.55 ? 364 ALA A C 1 ATOM 2744 O O . ALA A 1 364 ? -45.759 7.163 8.654 1.00 24.25 ? 364 ALA A O 1 ATOM 2745 C CB . ALA A 1 364 ? -44.017 5.425 6.680 1.00 26.86 ? 364 ALA A CB 1 ATOM 2746 N N . ALA A 1 365 ? -44.519 5.723 9.889 1.00 28.05 ? 365 ALA A N 1 ATOM 2747 C CA . ALA A 1 365 ? -44.424 6.565 11.064 1.00 28.19 ? 365 ALA A CA 1 ATOM 2748 C C . ALA A 1 365 ? -43.367 7.609 10.830 1.00 28.76 ? 365 ALA A C 1 ATOM 2749 O O . ALA A 1 365 ? -42.390 7.355 10.132 1.00 29.01 ? 365 ALA A O 1 ATOM 2750 C CB . ALA A 1 365 ? -44.070 5.721 12.284 1.00 29.73 ? 365 ALA A CB 1 ATOM 2751 N N . ASP A 1 366 ? -43.550 8.787 11.418 1.00 27.87 ? 366 ASP A N 1 ATOM 2752 C CA . ASP A 1 366 ? -42.504 9.803 11.437 1.00 29.18 ? 366 ASP A CA 1 ATOM 2753 C C . ASP A 1 366 ? -41.835 9.788 12.813 1.00 30.66 ? 366 ASP A C 1 ATOM 2754 O O . ASP A 1 366 ? -42.463 10.137 13.826 1.00 29.76 ? 366 ASP A O 1 ATOM 2755 C CB . ASP A 1 366 ? -43.100 11.180 11.123 1.00 29.44 ? 366 ASP A CB 1 ATOM 2756 C CG . ASP A 1 366 ? -42.052 12.274 11.039 1.00 31.84 ? 366 ASP A CG 1 ATOM 2757 O OD1 . ASP A 1 366 ? -41.300 12.324 10.036 1.00 33.76 ? 366 ASP A OD1 1 ATOM 2758 O OD2 . ASP A 1 366 ? -41.970 13.098 11.977 1.00 31.58 ? 366 ASP A OD2 1 ATOM 2759 N N . LEU A 1 367 ? -40.569 9.382 12.843 1.00 31.93 ? 367 LEU A N 1 ATOM 2760 C CA . LEU A 1 367 ? -39.821 9.210 14.089 1.00 34.04 ? 367 LEU A CA 1 ATOM 2761 C C . LEU A 1 367 ? -39.621 10.542 14.798 1.00 33.35 ? 367 LEU A C 1 ATOM 2762 O O . LEU A 1 367 ? -39.787 10.622 16.016 1.00 32.93 ? 367 LEU A O 1 ATOM 2763 C CB . LEU A 1 367 ? -38.443 8.590 13.807 1.00 37.70 ? 367 LEU A CB 1 ATOM 2764 C CG . LEU A 1 367 ? -37.509 8.207 14.977 1.00 40.19 ? 367 LEU A CG 1 ATOM 2765 C CD1 . LEU A 1 367 ? -36.422 7.250 14.481 1.00 43.20 ? 367 LEU A CD1 1 ATOM 2766 C CD2 . LEU A 1 367 ? -36.852 9.411 15.650 1.00 42.12 ? 367 LEU A CD2 1 ATOM 2767 N N . LYS A 1 368 ? -39.266 11.577 14.041 1.00 33.43 ? 368 LYS A N 1 ATOM 2768 C CA . LYS A 1 368 ? -38.830 12.836 14.631 1.00 35.76 ? 368 LYS A CA 1 ATOM 2769 C C . LYS A 1 368 ? -39.924 13.468 15.488 1.00 33.23 ? 368 LYS A C 1 ATOM 2770 O O . LYS A 1 368 ? -39.692 13.830 16.657 1.00 31.12 ? 368 LYS A O 1 ATOM 2771 C CB . LYS A 1 368 ? -38.406 13.826 13.547 1.00 39.18 ? 368 LYS A CB 1 ATOM 2772 C CG . LYS A 1 368 ? -37.815 15.127 14.092 1.00 42.90 ? 368 LYS A CG 1 ATOM 2773 C CD . LYS A 1 368 ? -38.395 16.348 13.384 1.00 45.71 ? 368 LYS A CD 1 ATOM 2774 C CE . LYS A 1 368 ? -37.916 17.654 14.011 1.00 48.71 ? 368 LYS A CE 1 ATOM 2775 N NZ . LYS A 1 368 ? -36.525 18.008 13.615 1.00 50.10 ? 368 LYS A NZ 1 ATOM 2776 N N . SER A 1 369 ? -41.103 13.603 14.898 1.00 30.65 ? 369 SER A N 1 ATOM 2777 C CA . SER A 1 369 ? -42.258 14.189 15.575 1.00 29.22 ? 369 SER A CA 1 ATOM 2778 C C . SER A 1 369 ? -42.707 13.328 16.755 1.00 27.87 ? 369 SER A C 1 ATOM 2779 O O . SER A 1 369 ? -42.997 13.841 17.844 1.00 26.68 ? 369 SER A O 1 ATOM 2780 C CB . SER A 1 369 ? -43.400 14.387 14.579 1.00 28.96 ? 369 SER A CB 1 ATOM 2781 O OG . SER A 1 369 ? -43.735 13.170 13.935 1.00 29.61 ? 369 SER A OG 1 ATOM 2782 N N . THR A 1 370 ? -42.748 12.017 16.552 1.00 27.99 ? 370 THR A N 1 ATOM 2783 C CA . THR A 1 370 ? -43.092 11.081 17.621 1.00 27.60 ? 370 THR A CA 1 ATOM 2784 C C . THR A 1 370 ? -42.143 11.231 18.814 1.00 28.17 ? 370 THR A C 1 ATOM 2785 O O . THR A 1 370 ? -42.576 11.314 19.961 1.00 26.58 ? 370 THR A O 1 ATOM 2786 C CB . THR A 1 370 ? -43.029 9.628 17.130 1.00 28.35 ? 370 THR A CB 1 ATOM 2787 O OG1 . THR A 1 370 ? -43.963 9.452 16.063 1.00 26.90 ? 370 THR A OG1 1 ATOM 2788 C CG2 . THR A 1 370 ? -43.340 8.653 18.283 1.00 28.22 ? 370 THR A CG2 1 ATOM 2789 N N . GLN A 1 371 ? -40.842 11.272 18.536 1.00 29.34 ? 371 GLN A N 1 ATOM 2790 C CA . GLN A 1 371 ? -39.850 11.355 19.598 1.00 30.96 ? 371 GLN A CA 1 ATOM 2791 C C . GLN A 1 371 ? -39.886 12.717 20.333 1.00 29.35 ? 371 GLN A C 1 ATOM 2792 O O . GLN A 1 371 ? -39.702 12.778 21.542 1.00 28.80 ? 371 GLN A O 1 ATOM 2793 C CB . GLN A 1 371 ? -38.458 11.056 19.033 1.00 34.75 ? 371 GLN A CB 1 ATOM 2794 C CG . GLN A 1 371 ? -37.442 10.633 20.082 1.00 39.03 ? 371 GLN A CG 1 ATOM 2795 C CD . GLN A 1 371 ? -37.944 9.506 20.975 1.00 41.79 ? 371 GLN A CD 1 ATOM 2796 O OE1 . GLN A 1 371 ? -38.363 8.443 20.495 1.00 44.51 ? 371 GLN A OE1 1 ATOM 2797 N NE2 . GLN A 1 371 ? -37.921 9.743 22.286 1.00 43.57 ? 371 GLN A NE2 1 ATOM 2798 N N . ALA A 1 372 ? -40.115 13.798 19.597 1.00 28.88 ? 372 ALA A N 1 ATOM 2799 C CA . ALA A 1 372 ? -40.216 15.142 20.182 1.00 28.36 ? 372 ALA A CA 1 ATOM 2800 C C . ALA A 1 372 ? -41.368 15.220 21.187 1.00 26.96 ? 372 ALA A C 1 ATOM 2801 O O . ALA A 1 372 ? -41.228 15.801 22.269 1.00 25.74 ? 372 ALA A O 1 ATOM 2802 C CB . ALA A 1 372 ? -40.404 16.176 19.077 1.00 28.71 ? 372 ALA A CB 1 ATOM 2803 N N . ALA A 1 373 ? -42.510 14.637 20.837 1.00 26.45 ? 373 ALA A N 1 ATOM 2804 C CA . ALA A 1 373 ? -43.662 14.572 21.746 1.00 25.73 ? 373 ALA A CA 1 ATOM 2805 C C . ALA A 1 373 ? -43.353 13.702 22.964 1.00 26.39 ? 373 ALA A C 1 ATOM 2806 O O . ALA A 1 373 ? -43.593 14.103 24.104 1.00 27.06 ? 373 ALA A O 1 ATOM 2807 C CB . ALA A 1 373 ? -44.901 14.049 21.027 1.00 25.31 ? 373 ALA A CB 1 ATOM 2808 N N . ILE A 1 374 ? -42.808 12.519 22.731 1.00 27.55 ? 374 ILE A N 1 ATOM 2809 C CA . ILE A 1 374 ? -42.502 11.603 23.822 1.00 29.39 ? 374 ILE A CA 1 ATOM 2810 C C . ILE A 1 374 ? -41.474 12.219 24.781 1.00 30.22 ? 374 ILE A C 1 ATOM 2811 O O . ILE A 1 374 ? -41.657 12.165 26.005 1.00 28.85 ? 374 ILE A O 1 ATOM 2812 C CB . ILE A 1 374 ? -42.045 10.222 23.298 1.00 30.40 ? 374 ILE A CB 1 ATOM 2813 C CG1 . ILE A 1 374 ? -43.242 9.504 22.679 1.00 30.94 ? 374 ILE A CG1 1 ATOM 2814 C CG2 . ILE A 1 374 ? -41.426 9.381 24.412 1.00 30.17 ? 374 ILE A CG2 1 ATOM 2815 C CD1 . ILE A 1 374 ? -42.916 8.199 21.976 1.00 31.69 ? 374 ILE A CD1 1 ATOM 2816 N N . ASN A 1 375 ? -40.435 12.845 24.226 1.00 31.36 ? 375 ASN A N 1 ATOM 2817 C CA . ASN A 1 375 ? -39.382 13.453 25.038 1.00 33.31 ? 375 ASN A CA 1 ATOM 2818 C C . ASN A 1 375 ? -39.913 14.513 25.983 1.00 31.92 ? 375 ASN A C 1 ATOM 2819 O O . ASN A 1 375 ? -39.533 14.548 27.155 1.00 30.04 ? 375 ASN A O 1 ATOM 2820 C CB . ASN A 1 375 ? -38.276 14.058 24.161 1.00 35.62 ? 375 ASN A CB 1 ATOM 2821 C CG . ASN A 1 375 ? -37.392 13.003 23.529 1.00 37.81 ? 375 ASN A CG 1 ATOM 2822 O OD1 . ASN A 1 375 ? -37.346 11.854 23.987 1.00 39.86 ? 375 ASN A OD1 1 ATOM 2823 N ND2 . ASN A 1 375 ? -36.696 13.379 22.457 1.00 38.35 ? 375 ASN A ND2 1 ATOM 2824 N N . GLN A 1 376 ? -40.800 15.362 25.473 1.00 30.55 ? 376 GLN A N 1 ATOM 2825 C CA . GLN A 1 376 ? -41.381 16.435 26.264 1.00 29.91 ? 376 GLN A CA 1 ATOM 2826 C C . GLN A 1 376 ? -42.280 15.908 27.367 1.00 28.48 ? 376 GLN A C 1 ATOM 2827 O O . GLN A 1 376 ? -42.283 16.442 28.460 1.00 27.97 ? 376 GLN A O 1 ATOM 2828 C CB . GLN A 1 376 ? -42.162 17.380 25.379 1.00 29.79 ? 376 GLN A CB 1 ATOM 2829 C CG . GLN A 1 376 ? -41.262 18.206 24.476 1.00 31.61 ? 376 GLN A CG 1 ATOM 2830 C CD . GLN A 1 376 ? -42.052 19.083 23.547 1.00 31.40 ? 376 GLN A CD 1 ATOM 2831 O OE1 . GLN A 1 376 ? -42.622 20.074 23.961 1.00 32.47 ? 376 GLN A OE1 1 ATOM 2832 N NE2 . GLN A 1 376 ? -42.097 18.712 22.277 1.00 35.63 ? 376 GLN A NE2 1 ATOM 2833 N N . ILE A 1 377 ? -43.060 14.876 27.068 1.00 26.94 ? 377 ILE A N 1 ATOM 2834 C CA . ILE A 1 377 ? -43.933 14.284 28.064 1.00 26.43 ? 377 ILE A CA 1 ATOM 2835 C C . ILE A 1 377 ? -43.068 13.607 29.136 1.00 26.95 ? 377 ILE A C 1 ATOM 2836 O O . ILE A 1 377 ? -43.338 13.729 30.336 1.00 27.56 ? 377 ILE A O 1 ATOM 2837 C CB . ILE A 1 377 ? -44.950 13.329 27.420 1.00 25.41 ? 377 ILE A CB 1 ATOM 2838 C CG1 . ILE A 1 377 ? -46.017 14.143 26.659 1.00 25.38 ? 377 ILE A CG1 1 ATOM 2839 C CG2 . ILE A 1 377 ? -45.596 12.423 28.460 1.00 25.15 ? 377 ILE A CG2 1 ATOM 2840 C CD1 . ILE A 1 377 ? -46.851 13.320 25.694 1.00 23.83 ? 377 ILE A CD1 1 ATOM 2841 N N . ASN A 1 378 ? -41.998 12.950 28.717 1.00 27.42 ? 378 ASN A N 1 ATOM 2842 C CA . ASN A 1 378 ? -41.086 12.342 29.679 1.00 30.53 ? 378 ASN A CA 1 ATOM 2843 C C . ASN A 1 378 ? -40.421 13.389 30.557 1.00 30.72 ? 378 ASN A C 1 ATOM 2844 O O . ASN A 1 378 ? -40.220 13.154 31.738 1.00 33.18 ? 378 ASN A O 1 ATOM 2845 C CB . ASN A 1 378 ? -40.055 11.442 28.995 1.00 31.40 ? 378 ASN A CB 1 ATOM 2846 C CG . ASN A 1 378 ? -40.641 10.105 28.592 1.00 32.65 ? 378 ASN A CG 1 ATOM 2847 O OD1 . ASN A 1 378 ? -41.626 9.650 29.170 1.00 33.37 ? 378 ASN A OD1 1 ATOM 2848 N ND2 . ASN A 1 378 ? -40.040 9.470 27.606 1.00 33.35 ? 378 ASN A ND2 1 ATOM 2849 N N . GLY A 1 379 ? -40.121 14.551 29.984 1.00 30.60 ? 379 GLY A N 1 ATOM 2850 C CA . GLY A 1 379 ? -39.590 15.660 30.743 1.00 32.41 ? 379 GLY A CA 1 ATOM 2851 C C . GLY A 1 379 ? -40.498 16.104 31.870 1.00 31.80 ? 379 GLY A C 1 ATOM 2852 O O . GLY A 1 379 ? -40.039 16.343 33.001 1.00 29.49 ? 379 GLY A O 1 ATOM 2853 N N . LYS A 1 380 ? -41.793 16.245 31.589 1.00 30.93 ? 380 LYS A N 1 ATOM 2854 C CA . LYS A 1 380 ? -42.697 16.666 32.663 1.00 30.66 ? 380 LYS A CA 1 ATOM 2855 C C . LYS A 1 380 ? -42.954 15.560 33.655 1.00 29.26 ? 380 LYS A C 1 ATOM 2856 O O . LYS A 1 380 ? -43.110 15.823 34.834 1.00 29.70 ? 380 LYS A O 1 ATOM 2857 C CB . LYS A 1 380 ? -43.984 17.345 32.160 1.00 32.36 ? 380 LYS A CB 1 ATOM 2858 C CG . LYS A 1 380 ? -44.901 16.550 31.305 1.00 32.63 ? 380 LYS A CG 1 ATOM 2859 C CD . LYS A 1 380 ? -46.142 17.364 30.940 1.00 31.22 ? 380 LYS A CD 1 ATOM 2860 C CE . LYS A 1 380 ? -45.830 18.486 29.962 1.00 30.58 ? 380 LYS A CE 1 ATOM 2861 N NZ . LYS A 1 380 ? -47.027 19.314 29.691 1.00 27.93 ? 380 LYS A NZ 1 ATOM 2862 N N . LEU A 1 381 ? -42.935 14.316 33.207 1.00 28.86 ? 381 LEU A N 1 ATOM 2863 C CA . LEU A 1 381 ? -42.971 13.212 34.141 1.00 29.86 ? 381 LEU A CA 1 ATOM 2864 C C . LEU A 1 381 ? -41.766 13.268 35.092 1.00 31.62 ? 381 LEU A C 1 ATOM 2865 O O . LEU A 1 381 ? -41.924 13.101 36.302 1.00 32.27 ? 381 LEU A O 1 ATOM 2866 C CB . LEU A 1 381 ? -43.009 11.869 33.413 1.00 29.63 ? 381 LEU A CB 1 ATOM 2867 C CG . LEU A 1 381 ? -44.362 11.500 32.792 1.00 28.93 ? 381 LEU A CG 1 ATOM 2868 C CD1 . LEU A 1 381 ? -44.195 10.261 31.928 1.00 27.97 ? 381 LEU A CD1 1 ATOM 2869 C CD2 . LEU A 1 381 ? -45.428 11.279 33.856 1.00 27.52 ? 381 LEU A CD2 1 ATOM 2870 N N . ASN A 1 382 ? -40.578 13.530 34.546 1.00 32.36 ? 382 ASN A N 1 ATOM 2871 C CA A ASN A 1 382 ? -39.372 13.584 35.359 0.50 33.30 ? 382 ASN A CA 1 ATOM 2872 C CA B ASN A 1 382 ? -39.365 13.598 35.358 0.50 33.38 ? 382 ASN A CA 1 ATOM 2873 C C . ASN A 1 382 ? -39.431 14.691 36.430 1.00 33.47 ? 382 ASN A C 1 ATOM 2874 O O . ASN A 1 382 ? -38.877 14.529 37.508 1.00 33.76 ? 382 ASN A O 1 ATOM 2875 C CB A ASN A 1 382 ? -38.132 13.713 34.471 0.50 34.20 ? 382 ASN A CB 1 ATOM 2876 C CB B ASN A 1 382 ? -38.124 13.801 34.495 0.50 34.43 ? 382 ASN A CB 1 ATOM 2877 C CG A ASN A 1 382 ? -37.879 12.464 33.639 0.50 35.03 ? 382 ASN A CG 1 ATOM 2878 C CG B ASN A 1 382 ? -36.843 13.788 35.315 0.50 35.60 ? 382 ASN A CG 1 ATOM 2879 O OD1 A ASN A 1 382 ? -38.579 11.462 33.777 0.50 35.52 ? 382 ASN A OD1 1 ATOM 2880 O OD1 B ASN A 1 382 ? -36.541 12.807 35.988 0.50 36.90 ? 382 ASN A OD1 1 ATOM 2881 N ND2 A ASN A 1 382 ? -36.888 12.525 32.759 0.50 35.40 ? 382 ASN A ND2 1 ATOM 2882 N ND2 B ASN A 1 382 ? -36.104 14.890 35.285 0.50 35.71 ? 382 ASN A ND2 1 ATOM 2883 N N . ARG A 1 383 ? -40.121 15.798 36.142 1.00 33.21 ? 383 ARG A N 1 ATOM 2884 C CA . ARG A 1 383 ? -40.298 16.883 37.122 1.00 34.69 ? 383 ARG A CA 1 ATOM 2885 C C . ARG A 1 383 ? -41.284 16.570 38.251 1.00 33.07 ? 383 ARG A C 1 ATOM 2886 O O . ARG A 1 383 ? -41.190 17.139 39.332 1.00 32.74 ? 383 ARG A O 1 ATOM 2887 C CB . ARG A 1 383 ? -40.818 18.144 36.433 1.00 38.14 ? 383 ARG A CB 1 ATOM 2888 C CG . ARG A 1 383 ? -39.832 18.787 35.486 1.00 42.44 ? 383 ARG A CG 1 ATOM 2889 C CD . ARG A 1 383 ? -40.285 20.183 35.053 1.00 44.84 ? 383 ARG A CD 1 ATOM 2890 N NE . ARG A 1 383 ? -41.179 20.175 33.896 1.00 47.24 ? 383 ARG A NE 1 ATOM 2891 C CZ . ARG A 1 383 ? -40.819 19.865 32.644 1.00 48.97 ? 383 ARG A CZ 1 ATOM 2892 N NH1 . ARG A 1 383 ? -39.573 19.497 32.353 1.00 51.32 ? 383 ARG A NH1 1 ATOM 2893 N NH2 . ARG A 1 383 ? -41.721 19.910 31.667 1.00 49.52 ? 383 ARG A NH2 1 ATOM 2894 N N . LEU A 1 384 ? -42.251 15.706 37.973 1.00 30.47 ? 384 LEU A N 1 ATOM 2895 C CA . LEU A 1 384 ? -43.376 15.453 38.879 1.00 30.05 ? 384 LEU A CA 1 ATOM 2896 C C . LEU A 1 384 ? -43.304 14.126 39.626 1.00 30.07 ? 384 LEU A C 1 ATOM 2897 O O . LEU A 1 384 ? -43.973 13.971 40.656 1.00 30.11 ? 384 LEU A O 1 ATOM 2898 C CB . LEU A 1 384 ? -44.676 15.459 38.078 1.00 28.93 ? 384 LEU A CB 1 ATOM 2899 C CG . LEU A 1 384 ? -45.126 16.811 37.531 1.00 28.99 ? 384 LEU A CG 1 ATOM 2900 C CD1 . LEU A 1 384 ? -46.245 16.652 36.490 1.00 29.16 ? 384 LEU A CD1 1 ATOM 2901 C CD2 . LEU A 1 384 ? -45.557 17.693 38.685 1.00 29.09 ? 384 LEU A CD2 1 ATOM 2902 N N . ILE A 1 385 ? -42.557 13.164 39.079 1.00 29.22 ? 385 ILE A N 1 ATOM 2903 C CA . ILE A 1 385 ? -42.516 11.802 39.601 1.00 29.75 ? 385 ILE A CA 1 ATOM 2904 C C . ILE A 1 385 ? -41.196 11.561 40.326 1.00 31.23 ? 385 ILE A C 1 ATOM 2905 O O . ILE A 1 385 ? -40.115 11.877 39.806 1.00 31.58 ? 385 ILE A O 1 ATOM 2906 C CB . ILE A 1 385 ? -42.700 10.756 38.473 1.00 30.08 ? 385 ILE A CB 1 ATOM 2907 C CG1 . ILE A 1 385 ? -44.039 10.963 37.763 1.00 30.10 ? 385 ILE A CG1 1 ATOM 2908 C CG2 . ILE A 1 385 ? -42.657 9.326 39.020 1.00 30.59 ? 385 ILE A CG2 1 ATOM 2909 C CD1 . ILE A 1 385 ? -45.233 10.986 38.697 1.00 29.58 ? 385 ILE A CD1 1 ATOM 2910 N N . GLY A 1 386 ? -41.298 11.036 41.543 1.00 31.73 ? 386 GLY A N 1 ATOM 2911 C CA . GLY A 1 386 ? -40.139 10.726 42.368 1.00 33.02 ? 386 GLY A CA 1 ATOM 2912 C C . GLY A 1 386 ? -39.362 11.936 42.839 1.00 33.92 ? 386 GLY A C 1 ATOM 2913 O O . GLY A 1 386 ? -38.135 11.862 42.968 1.00 35.36 ? 386 GLY A O 1 ATOM 2914 N N . LYS A 1 387 ? -40.065 13.036 43.121 1.00 32.78 ? 387 LYS A N 1 ATOM 2915 C CA . LYS A 1 387 ? -39.420 14.309 43.468 1.00 33.26 ? 387 LYS A CA 1 ATOM 2916 C C . LYS A 1 387 ? -39.913 14.905 44.786 1.00 32.38 ? 387 LYS A C 1 ATOM 2917 O O . LYS A 1 387 ? -39.813 16.107 45.012 1.00 33.38 ? 387 LYS A O 1 ATOM 2918 C CB . LYS A 1 387 ? -39.620 15.312 42.337 1.00 34.04 ? 387 LYS A CB 1 ATOM 2919 C CG . LYS A 1 387 ? -38.990 14.882 41.023 1.00 35.78 ? 387 LYS A CG 1 ATOM 2920 C CD . LYS A 1 387 ? -37.470 14.837 41.120 1.00 38.50 ? 387 LYS A CD 1 ATOM 2921 C CE . LYS A 1 387 ? -36.830 14.578 39.767 1.00 39.87 ? 387 LYS A CE 1 ATOM 2922 N NZ . LYS A 1 387 ? -37.274 13.274 39.196 1.00 40.89 ? 387 LYS A NZ 1 ATOM 2923 N N . THR A 1 388 ? -40.421 14.055 45.671 1.00 31.30 ? 388 THR A N 1 ATOM 2924 C CA . THR A 1 388 ? -41.006 14.522 46.919 1.00 30.04 ? 388 THR A CA 1 ATOM 2925 C C . THR A 1 388 ? -39.903 15.032 47.856 1.00 31.42 ? 388 THR A C 1 ATOM 2926 O O . THR A 1 388 ? -38.717 14.654 47.737 1.00 29.13 ? 388 THR A O 1 ATOM 2927 C CB . THR A 1 388 ? -41.819 13.416 47.630 1.00 29.13 ? 388 THR A CB 1 ATOM 2928 O OG1 . THR A 1 388 ? -40.929 12.373 48.071 1.00 29.51 ? 388 THR A OG1 1 ATOM 2929 C CG2 . THR A 1 388 ? -42.917 12.844 46.676 1.00 28.17 ? 388 THR A CG2 1 ATOM 2930 N N . ASN A 1 389 ? -40.318 15.904 48.768 1.00 31.00 ? 389 ASN A N 1 ATOM 2931 C CA A ASN A 1 389 ? -39.427 16.508 49.744 0.50 32.71 ? 389 ASN A CA 1 ATOM 2932 C CA B ASN A 1 389 ? -39.393 16.472 49.744 0.50 32.96 ? 389 ASN A CA 1 ATOM 2933 C C . ASN A 1 389 ? -39.762 15.985 51.136 1.00 31.68 ? 389 ASN A C 1 ATOM 2934 O O . ASN A 1 389 ? -40.920 15.652 51.404 1.00 30.66 ? 389 ASN A O 1 ATOM 2935 C CB A ASN A 1 389 ? -39.589 18.024 49.680 0.50 33.78 ? 389 ASN A CB 1 ATOM 2936 C CB B ASN A 1 389 ? -39.341 18.012 49.665 0.50 34.83 ? 389 ASN A CB 1 ATOM 2937 C CG A ASN A 1 389 ? -39.065 18.598 48.376 0.50 34.65 ? 389 ASN A CG 1 ATOM 2938 C CG B ASN A 1 389 ? -40.647 18.689 50.054 0.50 34.47 ? 389 ASN A CG 1 ATOM 2939 O OD1 A ASN A 1 389 ? -38.164 18.030 47.758 0.50 35.19 ? 389 ASN A OD1 1 ATOM 2940 O OD1 B ASN A 1 389 ? -41.684 18.046 50.205 0.50 37.44 ? 389 ASN A OD1 1 ATOM 2941 N ND2 A ASN A 1 389 ? -39.625 19.718 47.955 0.50 34.08 ? 389 ASN A ND2 1 ATOM 2942 N ND2 B ASN A 1 389 ? -40.594 20.017 50.221 0.50 34.63 ? 389 ASN A ND2 1 ATOM 2943 N N . GLU A 1 390 ? -38.759 15.929 52.005 1.00 29.71 ? 390 GLU A N 1 ATOM 2944 C CA . GLU A 1 390 ? -38.931 15.434 53.349 1.00 27.57 ? 390 GLU A CA 1 ATOM 2945 C C . GLU A 1 390 ? -39.452 16.468 54.352 1.00 25.09 ? 390 GLU A C 1 ATOM 2946 O O . GLU A 1 390 ? -38.963 17.599 54.400 1.00 24.22 ? 390 GLU A O 1 ATOM 2947 C CB . GLU A 1 390 ? -37.583 14.931 53.864 1.00 29.71 ? 390 GLU A CB 1 ATOM 2948 C CG . GLU A 1 390 ? -37.039 13.696 53.179 1.00 32.48 ? 390 GLU A CG 1 ATOM 2949 C CD . GLU A 1 390 ? -35.774 13.227 53.858 1.00 34.46 ? 390 GLU A CD 1 ATOM 2950 O OE1 . GLU A 1 390 ? -34.798 13.968 53.741 1.00 34.64 ? 390 GLU A OE1 1 ATOM 2951 O OE2 . GLU A 1 390 ? -35.785 12.165 54.552 1.00 37.37 ? 390 GLU A OE2 1 ATOM 2952 N N . LYS A 1 391 ? -40.369 16.041 55.217 1.00 22.46 ? 391 LYS A N 1 ATOM 2953 C CA . LYS A 1 391 ? -40.721 16.779 56.420 1.00 21.32 ? 391 LYS A CA 1 ATOM 2954 C C . LYS A 1 391 ? -40.679 15.821 57.618 1.00 21.18 ? 391 LYS A C 1 ATOM 2955 O O . LYS A 1 391 ? -40.913 14.618 57.468 1.00 20.68 ? 391 LYS A O 1 ATOM 2956 C CB . LYS A 1 391 ? -42.108 17.394 56.312 1.00 21.28 ? 391 LYS A CB 1 ATOM 2957 C CG . LYS A 1 391 ? -42.280 18.374 55.157 1.00 21.38 ? 391 LYS A CG 1 ATOM 2958 C CD . LYS A 1 391 ? -41.541 19.679 55.367 1.00 21.31 ? 391 LYS A CD 1 ATOM 2959 C CE . LYS A 1 391 ? -41.869 20.677 54.252 1.00 20.93 ? 391 LYS A CE 1 ATOM 2960 N NZ . LYS A 1 391 ? -40.882 21.777 54.155 1.00 19.63 ? 391 LYS A NZ 1 ATOM 2961 N N . PHE A 1 392 ? -40.415 16.369 58.796 1.00 20.20 ? 392 PHE A N 1 ATOM 2962 C CA . PHE A 1 392 ? -40.144 15.557 59.974 1.00 21.03 ? 392 PHE A CA 1 ATOM 2963 C C . PHE A 1 392 ? -41.125 15.916 61.084 1.00 20.12 ? 392 PHE A C 1 ATOM 2964 O O . PHE A 1 392 ? -42.315 15.698 60.908 1.00 19.95 ? 392 PHE A O 1 ATOM 2965 C CB . PHE A 1 392 ? -38.656 15.674 60.339 1.00 21.78 ? 392 PHE A CB 1 ATOM 2966 C CG . PHE A 1 392 ? -37.740 15.280 59.202 1.00 22.42 ? 392 PHE A CG 1 ATOM 2967 C CD1 . PHE A 1 392 ? -37.695 13.983 58.775 1.00 23.18 ? 392 PHE A CD1 1 ATOM 2968 C CD2 . PHE A 1 392 ? -37.004 16.235 58.507 1.00 23.58 ? 392 PHE A CD2 1 ATOM 2969 C CE1 . PHE A 1 392 ? -36.906 13.595 57.700 1.00 23.93 ? 392 PHE A CE1 1 ATOM 2970 C CE2 . PHE A 1 392 ? -36.202 15.868 57.426 1.00 24.56 ? 392 PHE A CE2 1 ATOM 2971 C CZ . PHE A 1 392 ? -36.139 14.546 57.034 1.00 24.84 ? 392 PHE A CZ 1 ATOM 2972 N N . HIS A 1 393 ? -40.667 16.511 62.185 1.00 20.29 ? 393 HIS A N 1 ATOM 2973 C CA . HIS A 1 393 ? -41.579 16.888 63.249 1.00 19.73 ? 393 HIS A CA 1 ATOM 2974 C C . HIS A 1 393 ? -42.340 18.133 62.869 1.00 19.52 ? 393 HIS A C 1 ATOM 2975 O O . HIS A 1 393 ? -41.752 19.148 62.463 1.00 18.82 ? 393 HIS A O 1 ATOM 2976 C CB . HIS A 1 393 ? -40.825 17.085 64.533 1.00 20.47 ? 393 HIS A CB 1 ATOM 2977 C CG . HIS A 1 393 ? -41.704 17.094 65.747 1.00 20.68 ? 393 HIS A CG 1 ATOM 2978 N ND1 . HIS A 1 393 ? -42.571 16.096 66.020 1.00 21.09 ? 393 HIS A ND1 1 ATOM 2979 C CD2 . HIS A 1 393 ? -41.861 18.030 66.746 1.00 20.65 ? 393 HIS A CD2 1 ATOM 2980 C CE1 . HIS A 1 393 ? -43.230 16.391 67.145 1.00 20.47 ? 393 HIS A CE1 1 ATOM 2981 N NE2 . HIS A 1 393 ? -42.789 17.556 67.595 1.00 20.13 ? 393 HIS A NE2 1 ATOM 2982 N N . GLN A 1 394 ? -43.655 18.068 63.018 1.00 18.37 ? 394 GLN A N 1 ATOM 2983 C CA A GLN A 1 394 ? -44.547 19.120 62.534 0.50 18.58 ? 394 GLN A CA 1 ATOM 2984 C CA B GLN A 1 394 ? -44.527 19.147 62.551 0.50 18.64 ? 394 GLN A CA 1 ATOM 2985 C C . GLN A 1 394 ? -45.467 19.557 63.680 1.00 18.39 ? 394 GLN A C 1 ATOM 2986 O O . GLN A 1 394 ? -44.999 19.842 64.762 1.00 21.34 ? 394 GLN A O 1 ATOM 2987 C CB A GLN A 1 394 ? -45.304 18.596 61.305 0.50 18.16 ? 394 GLN A CB 1 ATOM 2988 C CB B GLN A 1 394 ? -45.234 18.711 61.266 0.50 18.31 ? 394 GLN A CB 1 ATOM 2989 C CG A GLN A 1 394 ? -44.383 18.186 60.159 0.50 18.45 ? 394 GLN A CG 1 ATOM 2990 C CG B GLN A 1 394 ? -44.270 18.591 60.095 0.50 18.67 ? 394 GLN A CG 1 ATOM 2991 C CD A GLN A 1 394 ? -45.056 17.302 59.123 0.50 18.36 ? 394 GLN A CD 1 ATOM 2992 C CD B GLN A 1 394 ? -44.964 18.394 58.757 0.50 18.55 ? 394 GLN A CD 1 ATOM 2993 O OE1 A GLN A 1 394 ? -46.095 17.665 58.581 0.50 18.25 ? 394 GLN A OE1 1 ATOM 2994 O OE1 B GLN A 1 394 ? -45.933 17.647 58.656 0.50 18.65 ? 394 GLN A OE1 1 ATOM 2995 N NE2 A GLN A 1 394 ? -44.462 16.134 58.842 0.50 17.98 ? 394 GLN A NE2 1 ATOM 2996 N NE2 B GLN A 1 394 ? -44.470 19.083 57.719 0.50 18.47 ? 394 GLN A NE2 1 ATOM 2997 N N . ILE A 1 395 ? -46.768 19.628 63.454 1.00 17.11 ? 395 ILE A N 1 ATOM 2998 C CA . ILE A 1 395 ? -47.704 19.910 64.509 1.00 16.69 ? 395 ILE A CA 1 ATOM 2999 C C . ILE A 1 395 ? -48.635 18.725 64.541 1.00 16.46 ? 395 ILE A C 1 ATOM 3000 O O . ILE A 1 395 ? -48.681 17.941 63.578 1.00 16.13 ? 395 ILE A O 1 ATOM 3001 C CB . ILE A 1 395 ? -48.533 21.204 64.271 1.00 16.22 ? 395 ILE A CB 1 ATOM 3002 C CG1 . ILE A 1 395 ? -49.318 21.123 62.971 1.00 16.01 ? 395 ILE A CG1 1 ATOM 3003 C CG2 . ILE A 1 395 ? -47.613 22.425 64.285 1.00 16.38 ? 395 ILE A CG2 1 ATOM 3004 C CD1 . ILE A 1 395 ? -50.351 22.232 62.793 1.00 15.53 ? 395 ILE A CD1 1 ATOM 3005 N N . GLU A 1 396 ? -49.369 18.591 65.637 1.00 16.75 ? 396 GLU A N 1 ATOM 3006 C CA . GLU A 1 396 ? -50.391 17.556 65.737 1.00 17.20 ? 396 GLU A CA 1 ATOM 3007 C C . GLU A 1 396 ? -51.622 17.962 64.914 1.00 17.03 ? 396 GLU A C 1 ATOM 3008 O O . GLU A 1 396 ? -51.920 19.149 64.755 1.00 16.04 ? 396 GLU A O 1 ATOM 3009 C CB . GLU A 1 396 ? -50.764 17.332 67.190 1.00 18.20 ? 396 GLU A CB 1 ATOM 3010 C CG . GLU A 1 396 ? -49.579 16.844 68.055 1.00 18.68 ? 396 GLU A CG 1 ATOM 3011 C CD . GLU A 1 396 ? -49.022 15.488 67.669 1.00 20.28 ? 396 GLU A CD 1 ATOM 3012 O OE1 . GLU A 1 396 ? -49.758 14.656 67.061 1.00 22.05 ? 396 GLU A OE1 1 ATOM 3013 O OE2 . GLU A 1 396 ? -47.829 15.229 67.987 1.00 20.94 ? 396 GLU A OE2 1 ATOM 3014 N N . LYS A 1 397 ? -52.326 16.969 64.391 1.00 16.68 ? 397 LYS A N 1 ATOM 3015 C CA . LYS A 1 397 ? -53.406 17.210 63.461 1.00 17.07 ? 397 LYS A CA 1 ATOM 3016 C C . LYS A 1 397 ? -54.698 16.449 63.809 1.00 18.65 ? 397 LYS A C 1 ATOM 3017 O O . LYS A 1 397 ? -55.720 16.598 63.113 1.00 19.57 ? 397 LYS A O 1 ATOM 3018 C CB . LYS A 1 397 ? -52.922 16.864 62.055 1.00 16.40 ? 397 LYS A CB 1 ATOM 3019 C CG . LYS A 1 397 ? -51.702 17.713 61.629 1.00 15.89 ? 397 LYS A CG 1 ATOM 3020 C CD . LYS A 1 397 ? -51.135 17.323 60.281 1.00 15.89 ? 397 LYS A CD 1 ATOM 3021 C CE . LYS A 1 397 ? -49.856 18.102 59.959 1.00 15.92 ? 397 LYS A CE 1 ATOM 3022 N NZ . LYS A 1 397 ? -49.406 17.844 58.559 1.00 15.66 ? 397 LYS A NZ 1 ATOM 3023 N N . GLU A 1 398 ? -54.645 15.642 64.858 1.00 19.29 ? 398 GLU A N 1 ATOM 3024 C CA . GLU A 1 398 ? -55.826 14.973 65.439 1.00 21.00 ? 398 GLU A CA 1 ATOM 3025 C C . GLU A 1 398 ? -55.729 15.159 66.945 1.00 21.13 ? 398 GLU A C 1 ATOM 3026 O O . GLU A 1 398 ? -54.608 15.170 67.497 1.00 20.12 ? 398 GLU A O 1 ATOM 3027 C CB . GLU A 1 398 ? -55.841 13.476 65.108 1.00 23.29 ? 398 GLU A CB 1 ATOM 3028 C CG . GLU A 1 398 ? -56.024 13.161 63.628 1.00 25.48 ? 398 GLU A CG 1 ATOM 3029 C CD . GLU A 1 398 ? -56.157 11.668 63.342 1.00 28.75 ? 398 GLU A CD 1 ATOM 3030 O OE1 . GLU A 1 398 ? -56.391 10.878 64.283 1.00 31.44 ? 398 GLU A OE1 1 ATOM 3031 O OE2 . GLU A 1 398 ? -56.051 11.269 62.165 1.00 31.36 ? 398 GLU A OE2 1 ATOM 3032 N N . PHE A 1 399 ? -56.881 15.303 67.609 1.00 20.72 ? 399 PHE A N 1 ATOM 3033 C CA . PHE A 1 399 ? -56.929 15.652 69.042 1.00 21.32 ? 399 PHE A CA 1 ATOM 3034 C C . PHE A 1 399 ? -57.979 14.806 69.777 1.00 23.47 ? 399 PHE A C 1 ATOM 3035 O O . PHE A 1 399 ? -59.101 14.699 69.299 1.00 23.70 ? 399 PHE A O 1 ATOM 3036 C CB . PHE A 1 399 ? -57.253 17.146 69.183 1.00 20.80 ? 399 PHE A CB 1 ATOM 3037 C CG . PHE A 1 399 ? -56.301 18.016 68.426 1.00 19.41 ? 399 PHE A CG 1 ATOM 3038 C CD1 . PHE A 1 399 ? -56.525 18.311 67.100 1.00 19.38 ? 399 PHE A CD1 1 ATOM 3039 C CD2 . PHE A 1 399 ? -55.132 18.462 69.028 1.00 19.58 ? 399 PHE A CD2 1 ATOM 3040 C CE1 . PHE A 1 399 ? -55.601 19.073 66.391 1.00 19.38 ? 399 PHE A CE1 1 ATOM 3041 C CE2 . PHE A 1 399 ? -54.216 19.238 68.331 1.00 19.01 ? 399 PHE A CE2 1 ATOM 3042 C CZ . PHE A 1 399 ? -54.449 19.532 67.015 1.00 18.95 ? 399 PHE A CZ 1 ATOM 3043 N N . SER A 1 400 ? -57.600 14.208 70.906 1.00 25.06 ? 400 SER A N 1 ATOM 3044 C CA . SER A 1 400 ? -58.521 13.383 71.711 1.00 27.45 ? 400 SER A CA 1 ATOM 3045 C C . SER A 1 400 ? -59.349 14.190 72.727 1.00 28.83 ? 400 SER A C 1 ATOM 3046 O O . SER A 1 400 ? -60.348 13.689 73.255 1.00 29.55 ? 400 SER A O 1 ATOM 3047 C CB . SER A 1 400 ? -57.746 12.294 72.452 1.00 27.80 ? 400 SER A CB 1 ATOM 3048 O OG . SER A 1 400 ? -56.711 12.878 73.225 1.00 29.00 ? 400 SER A OG 1 ATOM 3049 N N . GLU A 1 401 ? -58.935 15.420 73.015 1.00 28.96 ? 401 GLU A N 1 ATOM 3050 C CA . GLU A 1 401 ? -59.655 16.269 73.968 1.00 30.56 ? 401 GLU A CA 1 ATOM 3051 C C . GLU A 1 401 ? -59.970 17.619 73.341 1.00 28.08 ? 401 GLU A C 1 ATOM 3052 O O . GLU A 1 401 ? -59.264 18.082 72.462 1.00 26.67 ? 401 GLU A O 1 ATOM 3053 C CB . GLU A 1 401 ? -58.841 16.505 75.238 1.00 33.53 ? 401 GLU A CB 1 ATOM 3054 C CG . GLU A 1 401 ? -58.716 15.295 76.141 1.00 38.27 ? 401 GLU A CG 1 ATOM 3055 C CD . GLU A 1 401 ? -57.674 14.328 75.658 1.00 40.23 ? 401 GLU A CD 1 ATOM 3056 O OE1 . GLU A 1 401 ? -56.586 14.808 75.288 1.00 48.28 ? 401 GLU A OE1 1 ATOM 3057 O OE2 . GLU A 1 401 ? -57.945 13.100 75.635 1.00 44.77 ? 401 GLU A OE2 1 ATOM 3058 N N . VAL A 1 402 ? -61.038 18.226 73.832 1.00 26.48 ? 402 VAL A N 1 ATOM 3059 C CA . VAL A 1 402 ? -61.445 19.574 73.493 1.00 25.93 ? 402 VAL A CA 1 ATOM 3060 C C . VAL A 1 402 ? -60.570 20.567 74.262 1.00 24.13 ? 402 VAL A C 1 ATOM 3061 O O . VAL A 1 402 ? -60.382 20.415 75.472 1.00 23.17 ? 402 VAL A O 1 ATOM 3062 C CB . VAL A 1 402 ? -62.941 19.742 73.868 1.00 26.89 ? 402 VAL A CB 1 ATOM 3063 C CG1 . VAL A 1 402 ? -63.342 21.201 73.964 1.00 27.42 ? 402 VAL A CG1 1 ATOM 3064 C CG2 . VAL A 1 402 ? -63.803 19.009 72.849 1.00 28.09 ? 402 VAL A CG2 1 ATOM 3065 N N . GLU A 1 403 ? -60.047 21.589 73.584 1.00 23.08 ? 403 GLU A N 1 ATOM 3066 C CA . GLU A 1 403 ? -59.126 22.547 74.233 1.00 22.70 ? 403 GLU A CA 1 ATOM 3067 C C . GLU A 1 403 ? -59.399 24.034 73.967 1.00 22.46 ? 403 GLU A C 1 ATOM 3068 O O . GLU A 1 403 ? -58.988 24.875 74.747 1.00 23.14 ? 403 GLU A O 1 ATOM 3069 C CB . GLU A 1 403 ? -57.675 22.261 73.833 1.00 22.51 ? 403 GLU A CB 1 ATOM 3070 C CG . GLU A 1 403 ? -57.169 20.870 74.160 1.00 22.80 ? 403 GLU A CG 1 ATOM 3071 C CD . GLU A 1 403 ? -55.787 20.635 73.601 1.00 23.48 ? 403 GLU A CD 1 ATOM 3072 O OE1 . GLU A 1 403 ? -55.636 20.470 72.362 1.00 24.03 ? 403 GLU A OE1 1 ATOM 3073 O OE2 . GLU A 1 403 ? -54.839 20.629 74.391 1.00 24.38 ? 403 GLU A OE2 1 ATOM 3074 N N . GLY A 1 404 ? -60.022 24.358 72.845 1.00 21.22 ? 404 GLY A N 1 ATOM 3075 C CA . GLY A 1 404 ? -60.313 25.728 72.499 1.00 21.19 ? 404 GLY A CA 1 ATOM 3076 C C . GLY A 1 404 ? -59.206 26.360 71.645 1.00 20.47 ? 404 GLY A C 1 ATOM 3077 O O . GLY A 1 404 ? -58.767 25.784 70.654 1.00 19.28 ? 404 GLY A O 1 ATOM 3078 N N . ARG A 1 405 ? -58.763 27.534 72.074 1.00 20.22 ? 405 ARG A N 1 ATOM 3079 C CA . ARG A 1 405 ? -58.010 28.468 71.256 1.00 19.72 ? 405 ARG A CA 1 ATOM 3080 C C . ARG A 1 405 ? -56.796 27.896 70.513 1.00 18.89 ? 405 ARG A C 1 ATOM 3081 O O . ARG A 1 405 ? -56.670 28.090 69.307 1.00 17.94 ? 405 ARG A O 1 ATOM 3082 C CB . ARG A 1 405 ? -57.556 29.619 72.136 1.00 20.24 ? 405 ARG A CB 1 ATOM 3083 C CG . ARG A 1 405 ? -57.035 30.809 71.361 1.00 20.49 ? 405 ARG A CG 1 ATOM 3084 C CD . ARG A 1 405 ? -56.724 31.954 72.314 1.00 21.32 ? 405 ARG A CD 1 ATOM 3085 N NE . ARG A 1 405 ? -56.222 33.111 71.589 1.00 21.27 ? 405 ARG A NE 1 ATOM 3086 C CZ . ARG A 1 405 ? -56.055 34.319 72.110 1.00 21.19 ? 405 ARG A CZ 1 ATOM 3087 N NH1 . ARG A 1 405 ? -56.303 34.555 73.394 1.00 21.24 ? 405 ARG A NH1 1 ATOM 3088 N NH2 . ARG A 1 405 ? -55.624 35.294 71.335 1.00 21.22 ? 405 ARG A NH2 1 ATOM 3089 N N . ILE A 1 406 ? -55.897 27.238 71.225 1.00 18.35 ? 406 ILE A N 1 ATOM 3090 C CA . ILE A 1 406 ? -54.685 26.742 70.591 1.00 18.62 ? 406 ILE A CA 1 ATOM 3091 C C . ILE A 1 406 ? -55.021 25.666 69.565 1.00 17.74 ? 406 ILE A C 1 ATOM 3092 O O . ILE A 1 406 ? -54.451 25.644 68.475 1.00 16.46 ? 406 ILE A O 1 ATOM 3093 C CB . ILE A 1 406 ? -53.641 26.221 71.610 1.00 19.84 ? 406 ILE A CB 1 ATOM 3094 C CG1 . ILE A 1 406 ? -52.363 25.761 70.902 1.00 19.60 ? 406 ILE A CG1 1 ATOM 3095 C CG2 . ILE A 1 406 ? -54.176 25.048 72.423 1.00 21.26 ? 406 ILE A CG2 1 ATOM 3096 C CD1 . ILE A 1 406 ? -51.512 26.909 70.408 1.00 21.38 ? 406 ILE A CD1 1 ATOM 3097 N N . GLN A 1 407 ? -55.949 24.774 69.915 1.00 17.33 ? 407 GLN A N 1 ATOM 3098 C CA . GLN A 1 407 ? -56.356 23.727 69.008 1.00 17.25 ? 407 GLN A CA 1 ATOM 3099 C C . GLN A 1 407 ? -57.082 24.274 67.784 1.00 16.80 ? 407 GLN A C 1 ATOM 3100 O O . GLN A 1 407 ? -56.876 23.766 66.680 1.00 16.09 ? 407 GLN A O 1 ATOM 3101 C CB . GLN A 1 407 ? -57.217 22.676 69.744 1.00 17.63 ? 407 GLN A CB 1 ATOM 3102 C CG . GLN A 1 407 ? -57.506 21.444 68.910 1.00 18.17 ? 407 GLN A CG 1 ATOM 3103 C CD . GLN A 1 407 ? -58.431 20.460 69.623 1.00 18.46 ? 407 GLN A CD 1 ATOM 3104 O OE1 . GLN A 1 407 ? -59.435 20.072 69.077 1.00 19.63 ? 407 GLN A OE1 1 ATOM 3105 N NE2 . GLN A 1 407 ? -58.099 20.091 70.852 1.00 18.62 ? 407 GLN A NE2 1 ATOM 3106 N N . ASP A 1 408 ? -57.917 25.296 67.978 1.00 16.78 ? 408 ASP A N 1 ATOM 3107 C CA . ASP A 1 408 ? -58.590 25.979 66.863 1.00 16.98 ? 408 ASP A CA 1 ATOM 3108 C C . ASP A 1 408 ? -57.528 26.469 65.853 1.00 16.68 ? 408 ASP A C 1 ATOM 3109 O O . ASP A 1 408 ? -57.678 26.285 64.653 1.00 16.09 ? 408 ASP A O 1 ATOM 3110 C CB . ASP A 1 408 ? -59.351 27.208 67.324 1.00 18.00 ? 408 ASP A CB 1 ATOM 3111 C CG . ASP A 1 408 ? -60.558 26.893 68.232 1.00 18.57 ? 408 ASP A CG 1 ATOM 3112 O OD1 . ASP A 1 408 ? -61.130 25.775 68.165 1.00 18.84 ? 408 ASP A OD1 1 ATOM 3113 O OD2 . ASP A 1 408 ? -60.937 27.811 68.970 1.00 18.15 ? 408 ASP A OD2 1 ATOM 3114 N N . LEU A 1 409 ? -56.479 27.104 66.376 1.00 16.17 ? 409 LEU A N 1 ATOM 3115 C CA . LEU A 1 409 ? -55.391 27.628 65.550 1.00 15.72 ? 409 LEU A CA 1 ATOM 3116 C C . LEU A 1 409 ? -54.623 26.516 64.835 1.00 15.42 ? 409 LEU A C 1 ATOM 3117 O O . LEU A 1 409 ? -54.399 26.595 63.619 1.00 14.74 ? 409 LEU A O 1 ATOM 3118 C CB . LEU A 1 409 ? -54.449 28.484 66.385 1.00 15.57 ? 409 LEU A CB 1 ATOM 3119 C CG . LEU A 1 409 ? -53.346 29.278 65.665 1.00 15.67 ? 409 LEU A CG 1 ATOM 3120 C CD1 . LEU A 1 409 ? -53.917 30.140 64.549 1.00 15.64 ? 409 LEU A CD1 1 ATOM 3121 C CD2 . LEU A 1 409 ? -52.580 30.128 66.668 1.00 15.83 ? 409 LEU A CD2 1 ATOM 3122 N N . GLU A 1 410 ? -54.241 25.463 65.567 1.00 15.61 ? 410 GLU A N 1 ATOM 3123 C CA . GLU A 1 410 ? -53.587 24.304 64.938 1.00 16.02 ? 410 GLU A CA 1 ATOM 3124 C C . GLU A 1 410 ? -54.418 23.722 63.777 1.00 16.02 ? 410 GLU A C 1 ATOM 3125 O O . GLU A 1 410 ? -53.889 23.466 62.668 1.00 15.22 ? 410 GLU A O 1 ATOM 3126 C CB . GLU A 1 410 ? -53.266 23.205 65.973 1.00 16.54 ? 410 GLU A CB 1 ATOM 3127 C CG . GLU A 1 410 ? -52.144 23.574 66.905 1.00 17.26 ? 410 GLU A CG 1 ATOM 3128 C CD . GLU A 1 410 ? -52.112 22.816 68.226 1.00 18.83 ? 410 GLU A CD 1 ATOM 3129 O OE1 . GLU A 1 410 ? -53.166 22.298 68.677 1.00 20.29 ? 410 GLU A OE1 1 ATOM 3130 O OE2 . GLU A 1 410 ? -51.012 22.772 68.847 1.00 19.59 ? 410 GLU A OE2 1 ATOM 3131 N N . LYS A 1 411 ? -55.707 23.502 64.014 1.00 15.72 ? 411 LYS A N 1 ATOM 3132 C CA . LYS A 1 411 ? -56.595 23.017 62.967 1.00 16.37 ? 411 LYS A CA 1 ATOM 3133 C C . LYS A 1 411 ? -56.733 23.979 61.786 1.00 15.51 ? 411 LYS A C 1 ATOM 3134 O O . LYS A 1 411 ? -56.765 23.544 60.642 1.00 15.01 ? 411 LYS A O 1 ATOM 3135 C CB . LYS A 1 411 ? -57.997 22.722 63.520 1.00 17.83 ? 411 LYS A CB 1 ATOM 3136 C CG . LYS A 1 411 ? -58.033 21.506 64.446 1.00 19.52 ? 411 LYS A CG 1 ATOM 3137 C CD . LYS A 1 411 ? -59.451 21.307 65.010 1.00 21.01 ? 411 LYS A CD 1 ATOM 3138 C CE . LYS A 1 411 ? -59.569 19.974 65.718 1.00 23.30 ? 411 LYS A CE 1 ATOM 3139 N NZ . LYS A 1 411 ? -60.962 19.654 66.182 1.00 24.58 ? 411 LYS A NZ 1 ATOM 3140 N N . TYR A 1 412 ? -56.856 25.277 62.062 1.00 15.10 ? 412 TYR A N 1 ATOM 3141 C CA . TYR A 1 412 ? -57.031 26.252 60.982 1.00 14.94 ? 412 TYR A CA 1 ATOM 3142 C C . TYR A 1 412 ? -55.765 26.368 60.113 1.00 14.08 ? 412 TYR A C 1 ATOM 3143 O O . TYR A 1 412 ? -55.845 26.509 58.892 1.00 13.71 ? 412 TYR A O 1 ATOM 3144 C CB . TYR A 1 412 ? -57.352 27.616 61.590 1.00 15.34 ? 412 TYR A CB 1 ATOM 3145 C CG . TYR A 1 412 ? -57.737 28.708 60.625 1.00 15.57 ? 412 TYR A CG 1 ATOM 3146 C CD1 . TYR A 1 412 ? -58.993 28.737 60.033 1.00 15.78 ? 412 TYR A CD1 1 ATOM 3147 C CD2 . TYR A 1 412 ? -56.853 29.760 60.343 1.00 15.71 ? 412 TYR A CD2 1 ATOM 3148 C CE1 . TYR A 1 412 ? -59.371 29.777 59.199 1.00 16.26 ? 412 TYR A CE1 1 ATOM 3149 C CE2 . TYR A 1 412 ? -57.218 30.781 59.484 1.00 15.88 ? 412 TYR A CE2 1 ATOM 3150 C CZ . TYR A 1 412 ? -58.482 30.797 58.931 1.00 16.10 ? 412 TYR A CZ 1 ATOM 3151 O OH . TYR A 1 412 ? -58.880 31.805 58.097 1.00 16.46 ? 412 TYR A OH 1 ATOM 3152 N N . VAL A 1 413 ? -54.602 26.282 60.746 1.00 14.02 ? 413 VAL A N 1 ATOM 3153 C CA . VAL A 1 413 ? -53.328 26.315 60.021 1.00 13.89 ? 413 VAL A CA 1 ATOM 3154 C C . VAL A 1 413 ? -53.258 25.156 59.022 1.00 13.75 ? 413 VAL A C 1 ATOM 3155 O O . VAL A 1 413 ? -52.913 25.343 57.839 1.00 13.05 ? 413 VAL A O 1 ATOM 3156 C CB . VAL A 1 413 ? -52.138 26.285 61.005 1.00 13.91 ? 413 VAL A CB 1 ATOM 3157 C CG1 . VAL A 1 413 ? -50.840 25.980 60.281 1.00 14.11 ? 413 VAL A CG1 1 ATOM 3158 C CG2 . VAL A 1 413 ? -52.035 27.635 61.730 1.00 14.41 ? 413 VAL A CG2 1 ATOM 3159 N N . GLU A 1 414 ? -53.653 23.967 59.481 1.00 14.02 ? 414 GLU A N 1 ATOM 3160 C CA . GLU A 1 414 ? -53.577 22.771 58.638 1.00 14.57 ? 414 GLU A CA 1 ATOM 3161 C C . GLU A 1 414 ? -54.641 22.801 57.544 1.00 14.64 ? 414 GLU A C 1 ATOM 3162 O O . GLU A 1 414 ? -54.334 22.521 56.389 1.00 14.15 ? 414 GLU A O 1 ATOM 3163 C CB . GLU A 1 414 ? -53.697 21.505 59.490 1.00 15.04 ? 414 GLU A CB 1 ATOM 3164 C CG . GLU A 1 414 ? -53.466 20.201 58.735 1.00 15.61 ? 414 GLU A CG 1 ATOM 3165 C CD . GLU A 1 414 ? -52.056 20.045 58.193 1.00 15.53 ? 414 GLU A CD 1 ATOM 3166 O OE1 . GLU A 1 414 ? -51.184 20.892 58.472 1.00 16.72 ? 414 GLU A OE1 1 ATOM 3167 O OE2 . GLU A 1 414 ? -51.804 19.043 57.513 1.00 15.68 ? 414 GLU A OE2 1 ATOM 3168 N N . ASP A 1 415 ? -55.872 23.159 57.894 1.00 15.45 ? 415 ASP A N 1 ATOM 3169 C CA . ASP A 1 415 ? -56.945 23.319 56.897 1.00 16.29 ? 415 ASP A CA 1 ATOM 3170 C C . ASP A 1 415 ? -56.533 24.309 55.794 1.00 15.60 ? 415 ASP A C 1 ATOM 3171 O O . ASP A 1 415 ? -56.748 24.056 54.606 1.00 15.11 ? 415 ASP A O 1 ATOM 3172 C CB . ASP A 1 415 ? -58.241 23.809 57.540 1.00 18.08 ? 415 ASP A CB 1 ATOM 3173 C CG . ASP A 1 415 ? -59.457 23.605 56.629 1.00 20.10 ? 415 ASP A CG 1 ATOM 3174 O OD1 . ASP A 1 415 ? -59.661 22.511 56.054 1.00 22.45 ? 415 ASP A OD1 1 ATOM 3175 O OD2 . ASP A 1 415 ? -60.190 24.564 56.447 1.00 22.82 ? 415 ASP A OD2 1 ATOM 3176 N N . THR A 1 416 ? -55.963 25.437 56.215 1.00 14.69 ? 416 THR A N 1 ATOM 3177 C CA . THR A 1 416 ? -55.496 26.480 55.309 1.00 14.44 ? 416 THR A CA 1 ATOM 3178 C C . THR A 1 416 ? -54.456 25.936 54.333 1.00 13.54 ? 416 THR A C 1 ATOM 3179 O O . THR A 1 416 ? -54.567 26.111 53.114 1.00 12.76 ? 416 THR A O 1 ATOM 3180 C CB . THR A 1 416 ? -54.929 27.663 56.123 1.00 14.42 ? 416 THR A CB 1 ATOM 3181 O OG1 . THR A 1 416 ? -55.998 28.249 56.897 1.00 14.66 ? 416 THR A OG1 1 ATOM 3182 C CG2 . THR A 1 416 ? -54.294 28.725 55.207 1.00 14.39 ? 416 THR A CG2 1 ATOM 3183 N N . LYS A 1 417 ? -53.460 25.250 54.891 1.00 13.01 ? 417 LYS A N 1 ATOM 3184 C CA . LYS A 1 417 ? -52.401 24.641 54.106 1.00 12.86 ? 417 LYS A CA 1 ATOM 3185 C C . LYS A 1 417 ? -52.940 23.648 53.087 1.00 12.47 ? 417 LYS A C 1 ATOM 3186 O O . LYS A 1 417 ? -52.589 23.719 51.937 1.00 11.82 ? 417 LYS A O 1 ATOM 3187 C CB . LYS A 1 417 ? -51.377 23.954 55.015 1.00 12.87 ? 417 LYS A CB 1 ATOM 3188 C CG . LYS A 1 417 ? -50.312 23.180 54.266 1.00 13.13 ? 417 LYS A CG 1 ATOM 3189 C CD . LYS A 1 417 ? -49.288 22.545 55.209 1.00 13.53 ? 417 LYS A CD 1 ATOM 3190 C CE . LYS A 1 417 ? -48.317 21.618 54.490 1.00 13.81 ? 417 LYS A CE 1 ATOM 3191 N NZ . LYS A 1 417 ? -47.434 20.882 55.483 1.00 14.54 ? 417 LYS A NZ 1 ATOM 3192 N N . ILE A 1 418 ? -53.844 22.774 53.509 1.00 12.46 ? 418 ILE A N 1 ATOM 3193 C CA . ILE A 1 418 ? -54.352 21.741 52.606 1.00 12.37 ? 418 ILE A CA 1 ATOM 3194 C C . ILE A 1 418 ? -55.170 22.351 51.462 1.00 12.23 ? 418 ILE A C 1 ATOM 3195 O O . ILE A 1 418 ? -55.029 21.934 50.326 1.00 11.78 ? 418 ILE A O 1 ATOM 3196 C CB . ILE A 1 418 ? -55.171 20.712 53.387 1.00 12.75 ? 418 ILE A CB 1 ATOM 3197 C CG1 . ILE A 1 418 ? -54.239 19.969 54.367 1.00 12.79 ? 418 ILE A CG1 1 ATOM 3198 C CG2 . ILE A 1 418 ? -55.918 19.777 52.442 1.00 12.61 ? 418 ILE A CG2 1 ATOM 3199 C CD1 . ILE A 1 418 ? -54.987 19.131 55.422 1.00 13.43 ? 418 ILE A CD1 1 ATOM 3200 N N . ASP A 1 419 ? -55.990 23.352 51.758 1.00 12.48 ? 419 ASP A N 1 ATOM 3201 C CA . ASP A 1 419 ? -56.774 23.993 50.707 1.00 12.66 ? 419 ASP A CA 1 ATOM 3202 C C . ASP A 1 419 ? -55.859 24.662 49.672 1.00 12.16 ? 419 ASP A C 1 ATOM 3203 O O . ASP A 1 419 ? -56.137 24.621 48.478 1.00 12.21 ? 419 ASP A O 1 ATOM 3204 C CB . ASP A 1 419 ? -57.744 25.016 51.298 1.00 13.47 ? 419 ASP A CB 1 ATOM 3205 C CG . ASP A 1 419 ? -59.023 24.376 51.897 1.00 14.65 ? 419 ASP A CG 1 ATOM 3206 O OD1 . ASP A 1 419 ? -59.238 23.134 51.755 1.00 15.18 ? 419 ASP A OD1 1 ATOM 3207 O OD2 . ASP A 1 419 ? -59.818 25.146 52.479 1.00 15.87 ? 419 ASP A OD2 1 ATOM 3208 N N . LEU A 1 420 ? -54.783 25.287 50.132 1.00 11.94 ? 420 LEU A N 1 ATOM 3209 C CA . LEU A 1 420 ? -53.851 25.961 49.215 1.00 11.91 ? 420 LEU A CA 1 ATOM 3210 C C . LEU A 1 420 ? -53.107 24.981 48.321 1.00 11.76 ? 420 LEU A C 1 ATOM 3211 O O . LEU A 1 420 ? -53.015 25.206 47.113 1.00 11.86 ? 420 LEU A O 1 ATOM 3212 C CB . LEU A 1 420 ? -52.908 26.878 49.963 1.00 11.86 ? 420 LEU A CB 1 ATOM 3213 C CG . LEU A 1 420 ? -53.592 28.182 50.399 1.00 12.09 ? 420 LEU A CG 1 ATOM 3214 C CD1 . LEU A 1 420 ? -52.849 28.840 51.562 1.00 12.23 ? 420 LEU A CD1 1 ATOM 3215 C CD2 . LEU A 1 420 ? -53.709 29.141 49.208 1.00 12.37 ? 420 LEU A CD2 1 ATOM 3216 N N . TRP A 1 421 ? -52.631 23.875 48.898 1.00 11.82 ? 421 TRP A N 1 ATOM 3217 C CA . TRP A 1 421 ? -52.023 22.796 48.089 1.00 11.75 ? 421 TRP A CA 1 ATOM 3218 C C . TRP A 1 421 ? -52.986 22.105 47.147 1.00 11.85 ? 421 TRP A C 1 ATOM 3219 O O . TRP A 1 421 ? -52.597 21.781 46.036 1.00 11.69 ? 421 TRP A O 1 ATOM 3220 C CB . TRP A 1 421 ? -51.284 21.798 48.995 1.00 11.50 ? 421 TRP A CB 1 ATOM 3221 C CG . TRP A 1 421 ? -49.935 22.347 49.329 1.00 11.47 ? 421 TRP A CG 1 ATOM 3222 C CD1 . TRP A 1 421 ? -49.468 22.807 50.561 1.00 11.66 ? 421 TRP A CD1 1 ATOM 3223 C CD2 . TRP A 1 421 ? -48.871 22.650 48.373 1.00 11.58 ? 421 TRP A CD2 1 ATOM 3224 N NE1 . TRP A 1 421 ? -48.189 23.301 50.436 1.00 11.80 ? 421 TRP A NE1 1 ATOM 3225 C CE2 . TRP A 1 421 ? -47.780 23.235 49.138 1.00 11.96 ? 421 TRP A CE2 1 ATOM 3226 C CE3 . TRP A 1 421 ? -48.711 22.454 47.004 1.00 11.70 ? 421 TRP A CE3 1 ATOM 3227 C CZ2 . TRP A 1 421 ? -46.592 23.630 48.541 1.00 12.06 ? 421 TRP A CZ2 1 ATOM 3228 C CZ3 . TRP A 1 421 ? -47.504 22.850 46.416 1.00 12.06 ? 421 TRP A CZ3 1 ATOM 3229 C CH2 . TRP A 1 421 ? -46.485 23.433 47.170 1.00 12.26 ? 421 TRP A CH2 1 ATOM 3230 N N . SER A 1 422 ? -54.223 21.867 47.580 1.00 11.97 ? 422 SER A N 1 ATOM 3231 C CA . SER A 1 422 ? -55.238 21.258 46.736 1.00 12.30 ? 422 SER A CA 1 ATOM 3232 C C . SER A 1 422 ? -55.528 22.153 45.519 1.00 12.43 ? 422 SER A C 1 ATOM 3233 O O . SER A 1 422 ? -55.638 21.662 44.392 1.00 12.19 ? 422 SER A O 1 ATOM 3234 C CB . SER A 1 422 ? -56.530 20.980 47.525 1.00 12.64 ? 422 SER A CB 1 ATOM 3235 O OG . SER A 1 422 ? -56.294 20.076 48.620 1.00 12.94 ? 422 SER A OG 1 ATOM 3236 N N . TYR A 1 423 ? -55.576 23.458 45.758 1.00 12.51 ? 423 TYR A N 1 ATOM 3237 C CA . TYR A 1 423 ? -55.710 24.447 44.678 1.00 12.86 ? 423 TYR A CA 1 ATOM 3238 C C . TYR A 1 423 ? -54.506 24.374 43.728 1.00 12.54 ? 423 TYR A C 1 ATOM 3239 O O . TYR A 1 423 ? -54.682 24.247 42.519 1.00 12.24 ? 423 TYR A O 1 ATOM 3240 C CB . TYR A 1 423 ? -55.895 25.880 45.235 1.00 13.18 ? 423 TYR A CB 1 ATOM 3241 C CG . TYR A 1 423 ? -55.950 26.877 44.122 1.00 13.87 ? 423 TYR A CG 1 ATOM 3242 C CD1 . TYR A 1 423 ? -57.143 27.102 43.456 1.00 14.39 ? 423 TYR A CD1 1 ATOM 3243 C CD2 . TYR A 1 423 ? -54.797 27.521 43.646 1.00 13.93 ? 423 TYR A CD2 1 ATOM 3244 C CE1 . TYR A 1 423 ? -57.208 27.959 42.380 1.00 15.28 ? 423 TYR A CE1 1 ATOM 3245 C CE2 . TYR A 1 423 ? -54.852 28.385 42.557 1.00 14.40 ? 423 TYR A CE2 1 ATOM 3246 C CZ . TYR A 1 423 ? -56.077 28.617 41.935 1.00 15.28 ? 423 TYR A CZ 1 ATOM 3247 O OH . TYR A 1 423 ? -56.235 29.452 40.839 1.00 16.00 ? 423 TYR A OH 1 ATOM 3248 N N . ASN A 1 424 ? -53.288 24.423 44.278 1.00 12.33 ? 424 ASN A N 1 ATOM 3249 C CA . ASN A 1 424 ? -52.081 24.319 43.441 1.00 12.45 ? 424 ASN A CA 1 ATOM 3250 C C . ASN A 1 424 ? -52.085 23.055 42.591 1.00 12.50 ? 424 ASN A C 1 ATOM 3251 O O . ASN A 1 424 ? -51.789 23.117 41.399 1.00 12.60 ? 424 ASN A O 1 ATOM 3252 C CB . ASN A 1 424 ? -50.801 24.326 44.268 1.00 12.55 ? 424 ASN A CB 1 ATOM 3253 C CG . ASN A 1 424 ? -50.513 25.657 44.909 1.00 12.87 ? 424 ASN A CG 1 ATOM 3254 O OD1 . ASN A 1 424 ? -51.008 26.706 44.463 1.00 13.09 ? 424 ASN A OD1 1 ATOM 3255 N ND2 . ASN A 1 424 ? -49.662 25.634 45.943 1.00 12.80 ? 424 ASN A ND2 1 ATOM 3256 N N . ALA A 1 425 ? -52.465 21.930 43.190 1.00 12.54 ? 425 ALA A N 1 ATOM 3257 C CA . ALA A 1 425 ? -52.528 20.649 42.460 1.00 13.02 ? 425 ALA A CA 1 ATOM 3258 C C . ALA A 1 425 ? -53.517 20.693 41.312 1.00 13.56 ? 425 ALA A C 1 ATOM 3259 O O . ALA A 1 425 ? -53.197 20.270 40.186 1.00 13.64 ? 425 ALA A O 1 ATOM 3260 C CB . ALA A 1 425 ? -52.892 19.491 43.406 1.00 12.82 ? 425 ALA A CB 1 ATOM 3261 N N . GLU A 1 426 ? -54.724 21.183 41.597 1.00 14.01 ? 426 GLU A N 1 ATOM 3262 C CA . GLU A 1 426 ? -55.771 21.315 40.579 1.00 15.31 ? 426 GLU A CA 1 ATOM 3263 C C . GLU A 1 426 ? -55.306 22.181 39.387 1.00 14.57 ? 426 GLU A C 1 ATOM 3264 O O . GLU A 1 426 ? -55.413 21.769 38.238 1.00 14.32 ? 426 GLU A O 1 ATOM 3265 C CB . GLU A 1 426 ? -57.042 21.890 41.184 1.00 16.53 ? 426 GLU A CB 1 ATOM 3266 C CG . GLU A 1 426 ? -58.273 21.717 40.294 1.00 18.15 ? 426 GLU A CG 1 ATOM 3267 C CD . GLU A 1 426 ? -58.788 20.289 40.235 1.00 19.31 ? 426 GLU A CD 1 ATOM 3268 O OE1 . GLU A 1 426 ? -58.778 19.605 41.275 1.00 20.13 ? 426 GLU A OE1 1 ATOM 3269 O OE2 . GLU A 1 426 ? -59.211 19.847 39.142 1.00 21.03 ? 426 GLU A OE2 1 ATOM 3270 N N . LEU A 1 427 ? -54.763 23.353 39.676 1.00 14.46 ? 427 LEU A N 1 ATOM 3271 C CA . LEU A 1 427 ? -54.251 24.248 38.624 1.00 14.42 ? 427 LEU A CA 1 ATOM 3272 C C . LEU A 1 427 ? -53.071 23.635 37.851 1.00 14.16 ? 427 LEU A C 1 ATOM 3273 O O . LEU A 1 427 ? -53.032 23.697 36.626 1.00 13.86 ? 427 LEU A O 1 ATOM 3274 C CB . LEU A 1 427 ? -53.846 25.597 39.219 1.00 14.64 ? 427 LEU A CB 1 ATOM 3275 C CG . LEU A 1 427 ? -53.375 26.644 38.217 1.00 15.05 ? 427 LEU A CG 1 ATOM 3276 C CD1 . LEU A 1 427 ? -54.452 26.977 37.177 1.00 15.07 ? 427 LEU A CD1 1 ATOM 3277 C CD2 . LEU A 1 427 ? -52.933 27.903 38.976 1.00 15.63 ? 427 LEU A CD2 1 ATOM 3278 N N . LEU A 1 428 ? -52.132 23.041 38.570 1.00 14.17 ? 428 LEU A N 1 ATOM 3279 C CA . LEU A 1 428 ? -50.928 22.473 37.964 1.00 14.80 ? 428 LEU A CA 1 ATOM 3280 C C . LEU A 1 428 ? -51.291 21.426 36.914 1.00 14.98 ? 428 LEU A C 1 ATOM 3281 O O . LEU A 1 428 ? -50.791 21.447 35.771 1.00 14.83 ? 428 LEU A O 1 ATOM 3282 C CB . LEU A 1 428 ? -50.008 21.867 39.034 1.00 15.15 ? 428 LEU A CB 1 ATOM 3283 C CG . LEU A 1 428 ? -48.675 21.282 38.528 1.00 15.57 ? 428 LEU A CG 1 ATOM 3284 C CD1 . LEU A 1 428 ? -47.856 22.277 37.684 1.00 16.71 ? 428 LEU A CD1 1 ATOM 3285 C CD2 . LEU A 1 428 ? -47.852 20.789 39.709 1.00 16.08 ? 428 LEU A CD2 1 ATOM 3286 N N . VAL A 1 429 ? -52.185 20.519 37.280 1.00 15.53 ? 429 VAL A N 1 ATOM 3287 C CA . VAL A 1 429 ? -52.555 19.454 36.369 1.00 16.11 ? 429 VAL A CA 1 ATOM 3288 C C . VAL A 1 429 ? -53.370 19.960 35.168 1.00 16.39 ? 429 VAL A C 1 ATOM 3289 O O . VAL A 1 429 ? -53.138 19.509 34.027 1.00 16.07 ? 429 VAL A O 1 ATOM 3290 C CB . VAL A 1 429 ? -53.243 18.306 37.117 1.00 16.88 ? 429 VAL A CB 1 ATOM 3291 C CG1 . VAL A 1 429 ? -53.719 17.236 36.146 1.00 18.56 ? 429 VAL A CG1 1 ATOM 3292 C CG2 . VAL A 1 429 ? -52.252 17.715 38.114 1.00 17.45 ? 429 VAL A CG2 1 ATOM 3293 N N . ALA A 1 430 ? -54.278 20.918 35.393 1.00 16.16 ? 430 ALA A N 1 ATOM 3294 C CA . ALA A 1 430 ? -55.006 21.544 34.287 1.00 16.46 ? 430 ALA A CA 1 ATOM 3295 C C . ALA A 1 430 ? -54.048 22.267 33.308 1.00 16.61 ? 430 ALA A C 1 ATOM 3296 O O . ALA A 1 430 ? -54.195 22.144 32.075 1.00 16.08 ? 430 ALA A O 1 ATOM 3297 C CB . ALA A 1 430 ? -56.077 22.518 34.806 1.00 16.40 ? 430 ALA A CB 1 ATOM 3298 N N . LEU A 1 431 ? -53.093 23.018 33.851 1.00 16.20 ? 431 LEU A N 1 ATOM 3299 C CA . LEU A 1 431 ? -52.077 23.702 33.037 1.00 16.45 ? 431 LEU A CA 1 ATOM 3300 C C . LEU A 1 431 ? -51.161 22.731 32.274 1.00 16.29 ? 431 LEU A C 1 ATOM 3301 O O . LEU A 1 431 ? -50.914 22.911 31.082 1.00 16.48 ? 431 LEU A O 1 ATOM 3302 C CB . LEU A 1 431 ? -51.210 24.642 33.892 1.00 16.26 ? 431 LEU A CB 1 ATOM 3303 C CG . LEU A 1 431 ? -51.866 25.920 34.430 1.00 16.92 ? 431 LEU A CG 1 ATOM 3304 C CD1 . LEU A 1 431 ? -50.858 26.637 35.325 1.00 17.06 ? 431 LEU A CD1 1 ATOM 3305 C CD2 . LEU A 1 431 ? -52.363 26.821 33.287 1.00 17.24 ? 431 LEU A CD2 1 ATOM 3306 N N . GLU A 1 432 ? -50.637 21.736 32.973 1.00 16.91 ? 432 GLU A N 1 ATOM 3307 C CA . GLU A 1 432 ? -49.800 20.730 32.349 1.00 17.85 ? 432 GLU A CA 1 ATOM 3308 C C . GLU A 1 432 ? -50.551 19.990 31.241 1.00 17.23 ? 432 GLU A C 1 ATOM 3309 O O . GLU A 1 432 ? -49.992 19.791 30.154 1.00 17.15 ? 432 GLU A O 1 ATOM 3310 C CB . GLU A 1 432 ? -49.223 19.759 33.380 1.00 19.00 ? 432 GLU A CB 1 ATOM 3311 C CG . GLU A 1 432 ? -48.179 20.392 34.276 1.00 20.96 ? 432 GLU A CG 1 ATOM 3312 C CD . GLU A 1 432 ? -46.809 20.539 33.633 1.00 23.49 ? 432 GLU A CD 1 ATOM 3313 O OE1 . GLU A 1 432 ? -46.639 20.316 32.416 1.00 24.99 ? 432 GLU A OE1 1 ATOM 3314 O OE2 . GLU A 1 432 ? -45.888 20.912 34.364 1.00 28.55 ? 432 GLU A OE2 1 ATOM 3315 N N . ASN A 1 433 ? -51.804 19.624 31.487 1.00 16.22 ? 433 ASN A N 1 ATOM 3316 C CA . ASN A 1 433 ? -52.587 18.895 30.487 1.00 16.07 ? 433 ASN A CA 1 ATOM 3317 C C . ASN A 1 433 ? -52.908 19.752 29.268 1.00 16.73 ? 433 ASN A C 1 ATOM 3318 O O . ASN A 1 433 ? -52.799 19.286 28.129 1.00 16.40 ? 433 ASN A O 1 ATOM 3319 C CB . ASN A 1 433 ? -53.865 18.347 31.092 1.00 15.64 ? 433 ASN A CB 1 ATOM 3320 C CG . ASN A 1 433 ? -53.622 17.195 32.055 1.00 15.17 ? 433 ASN A CG 1 ATOM 3321 O OD1 . ASN A 1 433 ? -52.514 16.671 32.145 1.00 15.72 ? 433 ASN A OD1 1 ATOM 3322 N ND2 . ASN A 1 433 ? -54.666 16.796 32.790 1.00 14.41 ? 433 ASN A ND2 1 ATOM 3323 N N . GLN A 1 434 ? -53.218 21.023 29.490 1.00 16.66 ? 434 GLN A N 1 ATOM 3324 C CA . GLN A 1 434 ? -53.379 21.933 28.377 1.00 17.63 ? 434 GLN A CA 1 ATOM 3325 C C . GLN A 1 434 ? -52.100 22.023 27.538 1.00 17.80 ? 434 GLN A C 1 ATOM 3326 O O . GLN A 1 434 ? -52.165 21.993 26.308 1.00 16.82 ? 434 GLN A O 1 ATOM 3327 C CB . GLN A 1 434 ? -53.785 23.324 28.851 1.00 19.14 ? 434 GLN A CB 1 ATOM 3328 C CG . GLN A 1 434 ? -54.127 24.259 27.687 1.00 20.61 ? 434 GLN A CG 1 ATOM 3329 C CD . GLN A 1 434 ? -55.334 23.769 26.924 1.00 22.08 ? 434 GLN A CD 1 ATOM 3330 O OE1 . GLN A 1 434 ? -56.417 23.618 27.512 1.00 23.23 ? 434 GLN A OE1 1 ATOM 3331 N NE2 . GLN A 1 434 ? -55.156 23.443 25.613 1.00 23.86 ? 434 GLN A NE2 1 ATOM 3332 N N . HIS A 1 435 ? -50.960 22.097 28.212 1.00 17.74 ? 435 HIS A N 1 ATOM 3333 C CA . HIS A 1 435 ? -49.660 22.168 27.535 1.00 19.22 ? 435 HIS A CA 1 ATOM 3334 C C . HIS A 1 435 ? -49.344 20.903 26.751 1.00 18.71 ? 435 HIS A C 1 ATOM 3335 O O . HIS A 1 435 ? -48.845 20.974 25.628 1.00 19.33 ? 435 HIS A O 1 ATOM 3336 C CB . HIS A 1 435 ? -48.564 22.495 28.538 1.00 20.04 ? 435 HIS A CB 1 ATOM 3337 C CG . HIS A 1 435 ? -47.182 22.595 27.927 1.00 21.90 ? 435 HIS A CG 1 ATOM 3338 N ND1 . HIS A 1 435 ? -46.302 21.567 27.964 1.00 22.61 ? 435 HIS A ND1 1 ATOM 3339 C CD2 . HIS A 1 435 ? -46.540 23.645 27.285 1.00 23.70 ? 435 HIS A CD2 1 ATOM 3340 C CE1 . HIS A 1 435 ? -45.158 21.938 27.367 1.00 24.37 ? 435 HIS A CE1 1 ATOM 3341 N NE2 . HIS A 1 435 ? -45.300 23.221 26.953 1.00 24.65 ? 435 HIS A NE2 1 ATOM 3342 N N . THR A 1 436 ? -49.694 19.757 27.303 1.00 18.07 ? 436 THR A N 1 ATOM 3343 C CA . THR A 1 436 ? -49.527 18.477 26.608 1.00 17.87 ? 436 THR A CA 1 ATOM 3344 C C . THR A 1 436 ? -50.394 18.392 25.354 1.00 18.27 ? 436 THR A C 1 ATOM 3345 O O . THR A 1 436 ? -49.900 17.968 24.297 1.00 18.27 ? 436 THR A O 1 ATOM 3346 C CB . THR A 1 436 ? -49.792 17.304 27.558 1.00 17.88 ? 436 THR A CB 1 ATOM 3347 O OG1 . THR A 1 436 ? -48.791 17.322 28.582 1.00 17.79 ? 436 THR A OG1 1 ATOM 3348 C CG2 . THR A 1 436 ? -49.765 15.915 26.799 1.00 17.35 ? 436 THR A CG2 1 ATOM 3349 N N . ILE A 1 437 ? -51.660 18.805 25.447 1.00 17.72 ? 437 ILE A N 1 ATOM 3350 C CA . ILE A 1 437 ? -52.512 18.858 24.286 1.00 19.40 ? 437 ILE A CA 1 ATOM 3351 C C . ILE A 1 437 ? -51.898 19.833 23.259 1.00 19.90 ? 437 ILE A C 1 ATOM 3352 O O . ILE A 1 437 ? -51.858 19.538 22.053 1.00 18.34 ? 437 ILE A O 1 ATOM 3353 C CB . ILE A 1 437 ? -53.946 19.286 24.653 1.00 19.64 ? 437 ILE A CB 1 ATOM 3354 C CG1 . ILE A 1 437 ? -54.614 18.250 25.571 1.00 20.46 ? 437 ILE A CG1 1 ATOM 3355 C CG2 . ILE A 1 437 ? -54.789 19.524 23.420 1.00 20.11 ? 437 ILE A CG2 1 ATOM 3356 C CD1 . ILE A 1 437 ? -54.765 16.878 24.974 1.00 20.96 ? 437 ILE A CD1 1 ATOM 3357 N N . ASP A 1 438 ? -51.437 20.998 23.727 1.00 19.69 ? 438 ASP A N 1 ATOM 3358 C CA . ASP A 1 438 ? -50.864 21.981 22.808 1.00 20.54 ? 438 ASP A CA 1 ATOM 3359 C C . ASP A 1 438 ? -49.576 21.496 22.127 1.00 19.96 ? 438 ASP A C 1 ATOM 3360 O O . ASP A 1 438 ? -49.441 21.670 20.943 1.00 20.52 ? 438 ASP A O 1 ATOM 3361 C CB . ASP A 1 438 ? -50.597 23.325 23.494 1.00 22.50 ? 438 ASP A CB 1 ATOM 3362 C CG . ASP A 1 438 ? -51.859 24.035 23.927 1.00 22.97 ? 438 ASP A CG 1 ATOM 3363 O OD1 . ASP A 1 438 ? -52.957 23.662 23.497 1.00 25.12 ? 438 ASP A OD1 1 ATOM 3364 O OD2 . ASP A 1 438 ? -51.723 24.996 24.717 1.00 24.85 ? 438 ASP A OD2 1 ATOM 3365 N N . LEU A 1 439 ? -48.654 20.885 22.850 1.00 19.73 ? 439 LEU A N 1 ATOM 3366 C CA . LEU A 1 439 ? -47.397 20.422 22.262 1.00 20.31 ? 439 LEU A CA 1 ATOM 3367 C C . LEU A 1 439 ? -47.612 19.228 21.290 1.00 20.53 ? 439 LEU A C 1 ATOM 3368 O O . LEU A 1 439 ? -46.920 19.124 20.288 1.00 21.46 ? 439 LEU A O 1 ATOM 3369 C CB . LEU A 1 439 ? -46.371 20.040 23.331 1.00 20.75 ? 439 LEU A CB 1 ATOM 3370 C CG . LEU A 1 439 ? -46.403 18.697 24.087 1.00 20.66 ? 439 LEU A CG 1 ATOM 3371 C CD1 . LEU A 1 439 ? -45.673 17.570 23.340 1.00 20.72 ? 439 LEU A CD1 1 ATOM 3372 C CD2 . LEU A 1 439 ? -45.810 18.841 25.493 1.00 21.34 ? 439 LEU A CD2 1 ATOM 3373 N N . THR A 1 440 ? -48.582 18.368 21.582 1.00 19.75 ? 440 THR A N 1 ATOM 3374 C CA . THR A 1 440 ? -48.870 17.222 20.702 1.00 20.27 ? 440 THR A CA 1 ATOM 3375 C C . THR A 1 440 ? -49.614 17.671 19.455 1.00 20.98 ? 440 THR A C 1 ATOM 3376 O O . THR A 1 440 ? -49.295 17.197 18.334 1.00 22.40 ? 440 THR A O 1 ATOM 3377 C CB . THR A 1 440 ? -49.595 16.076 21.425 1.00 18.85 ? 440 THR A CB 1 ATOM 3378 O OG1 . THR A 1 440 ? -50.752 16.565 22.099 1.00 18.41 ? 440 THR A OG1 1 ATOM 3379 C CG2 . THR A 1 440 ? -48.672 15.380 22.416 1.00 19.67 ? 440 THR A CG2 1 ATOM 3380 N N . ASP A 1 441 ? -50.580 18.586 19.615 1.00 20.69 ? 441 ASP A N 1 ATOM 3381 C CA . ASP A 1 441 ? -51.209 19.235 18.460 1.00 21.47 ? 441 ASP A CA 1 ATOM 3382 C C . ASP A 1 441 ? -50.113 19.923 17.614 1.00 22.51 ? 441 ASP A C 1 ATOM 3383 O O . ASP A 1 441 ? -50.116 19.831 16.374 1.00 21.21 ? 441 ASP A O 1 ATOM 3384 C CB . ASP A 1 441 ? -52.259 20.290 18.859 1.00 21.93 ? 441 ASP A CB 1 ATOM 3385 C CG . ASP A 1 441 ? -53.578 19.696 19.375 1.00 23.10 ? 441 ASP A CG 1 ATOM 3386 O OD1 . ASP A 1 441 ? -53.797 18.474 19.315 1.00 23.66 ? 441 ASP A OD1 1 ATOM 3387 O OD2 . ASP A 1 441 ? -54.434 20.481 19.843 1.00 23.31 ? 441 ASP A OD2 1 ATOM 3388 N N . SER A 1 442 ? -49.192 20.620 18.281 1.00 23.03 ? 442 SER A N 1 ATOM 3389 C CA . SER A 1 442 ? -48.145 21.357 17.563 1.00 24.18 ? 442 SER A CA 1 ATOM 3390 C C . SER A 1 442 ? -47.244 20.438 16.715 1.00 23.84 ? 442 SER A C 1 ATOM 3391 O O . SER A 1 442 ? -46.932 20.786 15.577 1.00 23.72 ? 442 SER A O 1 ATOM 3392 C CB . SER A 1 442 ? -47.300 22.212 18.516 1.00 24.91 ? 442 SER A CB 1 ATOM 3393 O OG . SER A 1 442 ? -46.243 22.849 17.793 1.00 25.97 ? 442 SER A OG 1 ATOM 3394 N N . GLU A 1 443 ? -46.821 19.294 17.243 1.00 24.03 ? 443 GLU A N 1 ATOM 3395 C CA . GLU A 1 443 ? -46.019 18.365 16.424 1.00 24.69 ? 443 GLU A CA 1 ATOM 3396 C C . GLU A 1 443 ? -46.782 17.955 15.154 1.00 24.64 ? 443 GLU A C 1 ATOM 3397 O O . GLU A 1 443 ? -46.194 17.889 14.081 1.00 25.17 ? 443 GLU A O 1 ATOM 3398 C CB . GLU A 1 443 ? -45.554 17.140 17.214 1.00 25.52 ? 443 GLU A CB 1 ATOM 3399 C CG . GLU A 1 443 ? -44.529 17.424 18.316 1.00 27.00 ? 443 GLU A CG 1 ATOM 3400 C CD . GLU A 1 443 ? -43.296 18.151 17.799 1.00 28.33 ? 443 GLU A CD 1 ATOM 3401 O OE1 . GLU A 1 443 ? -42.816 17.842 16.685 1.00 29.24 ? 443 GLU A OE1 1 ATOM 3402 O OE2 . GLU A 1 443 ? -42.803 19.043 18.494 1.00 29.36 ? 443 GLU A OE2 1 ATOM 3403 N N . MET A 1 444 ? -48.091 17.725 15.252 1.00 24.39 ? 444 MET A N 1 ATOM 3404 C CA . MET A 1 444 ? -48.895 17.386 14.065 1.00 23.89 ? 444 MET A CA 1 ATOM 3405 C C . MET A 1 444 ? -48.888 18.534 13.054 1.00 25.02 ? 444 MET A C 1 ATOM 3406 O O . MET A 1 444 ? -48.644 18.323 11.845 1.00 21.81 ? 444 MET A O 1 ATOM 3407 C CB . MET A 1 444 ? -50.335 17.056 14.451 1.00 23.53 ? 444 MET A CB 1 ATOM 3408 C CG . MET A 1 444 ? -51.227 16.610 13.290 1.00 23.96 ? 444 MET A CG 1 ATOM 3409 S SD . MET A 1 444 ? -50.868 14.906 12.754 1.00 23.64 ? 444 MET A SD 1 ATOM 3410 C CE . MET A 1 444 ? -49.521 15.173 11.607 1.00 25.63 ? 444 MET A CE 1 ATOM 3411 N N . ASN A 1 445 ? -49.136 19.750 13.549 1.00 24.51 ? 445 ASN A N 1 ATOM 3412 C CA . ASN A 1 445 ? -49.193 20.928 12.693 1.00 25.93 ? 445 ASN A CA 1 ATOM 3413 C C . ASN A 1 445 ? -47.859 21.236 12.025 1.00 25.44 ? 445 ASN A C 1 ATOM 3414 O O . ASN A 1 445 ? -47.828 21.610 10.850 1.00 26.07 ? 445 ASN A O 1 ATOM 3415 C CB . ASN A 1 445 ? -49.657 22.162 13.490 1.00 28.11 ? 445 ASN A CB 1 ATOM 3416 C CG . ASN A 1 445 ? -51.092 22.049 13.954 1.00 30.58 ? 445 ASN A CG 1 ATOM 3417 O OD1 . ASN A 1 445 ? -51.923 21.430 13.290 1.00 32.70 ? 445 ASN A OD1 1 ATOM 3418 N ND2 . ASN A 1 445 ? -51.401 22.680 15.081 1.00 31.86 ? 445 ASN A ND2 1 ATOM 3419 N N . LYS A 1 446 ? -46.771 21.048 12.756 1.00 25.59 ? 446 LYS A N 1 ATOM 3420 C CA . LYS A 1 446 ? -45.444 21.319 12.217 1.00 28.40 ? 446 LYS A CA 1 ATOM 3421 C C . LYS A 1 446 ? -45.104 20.296 11.128 1.00 27.91 ? 446 LYS A C 1 ATOM 3422 O O . LYS A 1 446 ? -44.491 20.648 10.127 1.00 27.79 ? 446 LYS A O 1 ATOM 3423 C CB . LYS A 1 446 ? -44.376 21.306 13.308 1.00 29.91 ? 446 LYS A CB 1 ATOM 3424 C CG . LYS A 1 446 ? -44.439 22.516 14.242 1.00 32.18 ? 446 LYS A CG 1 ATOM 3425 C CD . LYS A 1 446 ? -43.294 22.549 15.255 1.00 33.53 ? 446 LYS A CD 1 ATOM 3426 C CE . LYS A 1 446 ? -43.247 21.319 16.150 1.00 33.99 ? 446 LYS A CE 1 ATOM 3427 N NZ . LYS A 1 446 ? -42.164 21.430 17.185 1.00 36.23 ? 446 LYS A NZ 1 ATOM 3428 N N . LEU A 1 447 ? -45.521 19.050 11.321 1.00 27.08 ? 447 LEU A N 1 ATOM 3429 C CA . LEU A 1 447 ? -45.258 17.996 10.329 1.00 27.18 ? 447 LEU A CA 1 ATOM 3430 C C . LEU A 1 447 ? -45.970 18.356 9.034 1.00 26.48 ? 447 LEU A C 1 ATOM 3431 O O . LEU A 1 447 ? -45.389 18.258 7.952 1.00 27.01 ? 447 LEU A O 1 ATOM 3432 C CB . LEU A 1 447 ? -45.712 16.629 10.850 1.00 27.84 ? 447 LEU A CB 1 ATOM 3433 C CG . LEU A 1 447 ? -45.354 15.401 9.989 1.00 28.75 ? 447 LEU A CG 1 ATOM 3434 C CD1 . LEU A 1 447 ? -43.858 15.330 9.683 1.00 29.99 ? 447 LEU A CD1 1 ATOM 3435 C CD2 . LEU A 1 447 ? -45.848 14.133 10.659 1.00 29.51 ? 447 LEU A CD2 1 ATOM 3436 N N . PHE A 1 448 ? -47.217 18.807 9.147 1.00 24.77 ? 448 PHE A N 1 ATOM 3437 C CA . PHE A 1 448 ? -47.999 19.194 7.989 1.00 25.15 ? 448 PHE A CA 1 ATOM 3438 C C . PHE A 1 448 ? -47.358 20.391 7.288 1.00 26.31 ? 448 PHE A C 1 ATOM 3439 O O . PHE A 1 448 ? -47.251 20.414 6.054 1.00 23.88 ? 448 PHE A O 1 ATOM 3440 C CB . PHE A 1 448 ? -49.455 19.486 8.396 1.00 24.38 ? 448 PHE A CB 1 ATOM 3441 C CG . PHE A 1 448 ? -50.346 19.807 7.246 1.00 24.36 ? 448 PHE A CG 1 ATOM 3442 C CD1 . PHE A 1 448 ? -50.948 18.805 6.520 1.00 24.23 ? 448 PHE A CD1 1 ATOM 3443 C CD2 . PHE A 1 448 ? -50.547 21.121 6.856 1.00 25.55 ? 448 PHE A CD2 1 ATOM 3444 C CE1 . PHE A 1 448 ? -51.766 19.105 5.448 1.00 24.99 ? 448 PHE A CE1 1 ATOM 3445 C CE2 . PHE A 1 448 ? -51.366 21.430 5.787 1.00 25.63 ? 448 PHE A CE2 1 ATOM 3446 C CZ . PHE A 1 448 ? -51.977 20.419 5.079 1.00 25.16 ? 448 PHE A CZ 1 ATOM 3447 N N . GLU A 1 449 ? -46.927 21.384 8.067 1.00 26.73 ? 449 GLU A N 1 ATOM 3448 C CA . GLU A 1 449 ? -46.326 22.585 7.465 1.00 29.75 ? 449 GLU A CA 1 ATOM 3449 C C . GLU A 1 449 ? -45.017 22.290 6.751 1.00 28.76 ? 449 GLU A C 1 ATOM 3450 O O . GLU A 1 449 ? -44.836 22.768 5.652 1.00 28.60 ? 449 GLU A O 1 ATOM 3451 C CB . GLU A 1 449 ? -46.106 23.704 8.502 1.00 32.81 ? 449 GLU A CB 1 ATOM 3452 C CG . GLU A 1 449 ? -47.384 24.432 8.877 1.00 36.74 ? 449 GLU A CG 1 ATOM 3453 C CD . GLU A 1 449 ? -48.107 25.045 7.681 1.00 40.61 ? 449 GLU A CD 1 ATOM 3454 O OE1 . GLU A 1 449 ? -47.467 25.831 6.922 1.00 43.50 ? 449 GLU A OE1 1 ATOM 3455 O OE2 . GLU A 1 449 ? -49.311 24.723 7.495 1.00 41.04 ? 449 GLU A OE2 1 ATOM 3456 N N . ARG A 1 450 ? -44.134 21.513 7.377 1.00 30.17 ? 450 ARG A N 1 ATOM 3457 C CA . ARG A 1 450 ? -42.872 21.073 6.780 1.00 32.55 ? 450 ARG A CA 1 ATOM 3458 C C . ARG A 1 450 ? -43.115 20.406 5.419 1.00 30.42 ? 450 ARG A C 1 ATOM 3459 O O . ARG A 1 450 ? -42.398 20.656 4.445 1.00 29.64 ? 450 ARG A O 1 ATOM 3460 C CB . ARG A 1 450 ? -42.157 20.048 7.685 1.00 36.33 ? 450 ARG A CB 1 ATOM 3461 C CG . ARG A 1 450 ? -41.593 20.589 8.995 1.00 43.34 ? 450 ARG A CG 1 ATOM 3462 C CD . ARG A 1 450 ? -40.460 19.726 9.566 1.00 46.96 ? 450 ARG A CD 1 ATOM 3463 N NE . ARG A 1 450 ? -40.839 18.371 10.008 1.00 49.08 ? 450 ARG A NE 1 ATOM 3464 C CZ . ARG A 1 450 ? -41.436 18.065 11.173 1.00 49.62 ? 450 ARG A CZ 1 ATOM 3465 N NH1 . ARG A 1 450 ? -41.787 19.009 12.032 1.00 48.57 ? 450 ARG A NH1 1 ATOM 3466 N NH2 . ARG A 1 450 ? -41.701 16.794 11.471 1.00 49.48 ? 450 ARG A NH2 1 ATOM 3467 N N . THR A 1 451 ? -44.128 19.550 5.371 1.00 27.10 ? 451 THR A N 1 ATOM 3468 C CA . THR A 1 451 ? -44.468 18.808 4.155 1.00 24.89 ? 451 THR A CA 1 ATOM 3469 C C . THR A 1 451 ? -44.986 19.755 3.096 1.00 24.40 ? 451 THR A C 1 ATOM 3470 O O . THR A 1 451 ? -44.557 19.694 1.960 1.00 24.47 ? 451 THR A O 1 ATOM 3471 C CB . THR A 1 451 ? -45.502 17.713 4.472 1.00 23.20 ? 451 THR A CB 1 ATOM 3472 O OG1 . THR A 1 451 ? -44.972 16.855 5.492 1.00 22.76 ? 451 THR A OG1 1 ATOM 3473 C CG2 . THR A 1 451 ? -45.859 16.891 3.237 1.00 21.82 ? 451 THR A CG2 1 ATOM 3474 N N . LYS A 1 452 ? -45.885 20.655 3.476 1.00 25.44 ? 452 LYS A N 1 ATOM 3475 C CA . LYS A 1 452 ? -46.389 21.659 2.570 1.00 27.51 ? 452 LYS A CA 1 ATOM 3476 C C . LYS A 1 452 ? -45.230 22.417 1.912 1.00 29.42 ? 452 LYS A C 1 ATOM 3477 O O . LYS A 1 452 ? -45.244 22.687 0.691 1.00 27.84 ? 452 LYS A O 1 ATOM 3478 C CB . LYS A 1 452 ? -47.309 22.645 3.318 1.00 29.95 ? 452 LYS A CB 1 ATOM 3479 C CG . LYS A 1 452 ? -47.904 23.745 2.450 1.00 32.16 ? 452 LYS A CG 1 ATOM 3480 C CD . LYS A 1 452 ? -48.615 24.804 3.282 1.00 35.33 ? 452 LYS A CD 1 ATOM 3481 C CE . LYS A 1 452 ? -48.764 26.121 2.527 1.00 38.76 ? 452 LYS A CE 1 ATOM 3482 N NZ . LYS A 1 452 ? -47.637 27.105 2.738 1.00 41.36 ? 452 LYS A NZ 1 ATOM 3483 N N . LYS A 1 453 ? -44.240 22.773 2.719 1.00 30.60 ? 453 LYS A N 1 ATOM 3484 C CA . LYS A 1 453 ? -43.149 23.608 2.221 1.00 32.58 ? 453 LYS A CA 1 ATOM 3485 C C . LYS A 1 453 ? -42.284 22.837 1.215 1.00 30.03 ? 453 LYS A C 1 ATOM 3486 O O . LYS A 1 453 ? -41.909 23.402 0.187 1.00 30.35 ? 453 LYS A O 1 ATOM 3487 C CB . LYS A 1 453 ? -42.287 24.178 3.357 1.00 34.65 ? 453 LYS A CB 1 ATOM 3488 C CG . LYS A 1 453 ? -43.018 24.963 4.441 1.00 37.14 ? 453 LYS A CG 1 ATOM 3489 C CD . LYS A 1 453 ? -43.671 26.263 3.971 1.00 38.39 ? 453 LYS A CD 1 ATOM 3490 C CE . LYS A 1 453 ? -44.433 26.965 5.106 1.00 40.54 ? 453 LYS A CE 1 ATOM 3491 N NZ . LYS A 1 453 ? -43.751 28.124 5.745 1.00 39.46 ? 453 LYS A NZ 1 ATOM 3492 N N . GLN A 1 454 ? -41.986 21.564 1.490 1.00 29.03 ? 454 GLN A N 1 ATOM 3493 C CA . GLN A 1 454 ? -41.244 20.723 0.549 1.00 29.01 ? 454 GLN A CA 1 ATOM 3494 C C . GLN A 1 454 ? -41.912 20.690 -0.814 1.00 26.69 ? 454 GLN A C 1 ATOM 3495 O O . GLN A 1 454 ? -41.230 20.729 -1.848 1.00 25.93 ? 454 GLN A O 1 ATOM 3496 C CB . GLN A 1 454 ? -41.131 19.261 1.024 1.00 29.94 ? 454 GLN A CB 1 ATOM 3497 C CG . GLN A 1 454 ? -40.056 18.978 2.042 1.00 33.39 ? 454 GLN A CG 1 ATOM 3498 C CD . GLN A 1 454 ? -39.938 17.500 2.336 1.00 33.79 ? 454 GLN A CD 1 ATOM 3499 O OE1 . GLN A 1 454 ? -39.137 16.809 1.729 1.00 33.98 ? 454 GLN A OE1 1 ATOM 3500 N NE2 . GLN A 1 454 ? -40.736 17.014 3.272 1.00 33.10 ? 454 GLN A NE2 1 ATOM 3501 N N . LEU A 1 455 ? -43.242 20.583 -0.812 1.00 24.08 ? 455 LEU A N 1 ATOM 3502 C CA . LEU A 1 455 ? -43.996 20.300 -2.041 1.00 22.98 ? 455 LEU A CA 1 ATOM 3503 C C . LEU A 1 455 ? -44.098 21.500 -2.970 1.00 23.09 ? 455 LEU A C 1 ATOM 3504 O O . LEU A 1 455 ? -44.268 21.333 -4.166 1.00 22.20 ? 455 LEU A O 1 ATOM 3505 C CB . LEU A 1 455 ? -45.383 19.740 -1.692 1.00 22.29 ? 455 LEU A CB 1 ATOM 3506 C CG . LEU A 1 455 ? -45.344 18.346 -1.063 1.00 21.50 ? 455 LEU A CG 1 ATOM 3507 C CD1 . LEU A 1 455 ? -46.701 17.915 -0.515 1.00 20.42 ? 455 LEU A CD1 1 ATOM 3508 C CD2 . LEU A 1 455 ? -44.844 17.304 -2.065 1.00 22.25 ? 455 LEU A CD2 1 ATOM 3509 N N . ARG A 1 456 ? -43.976 22.709 -2.417 1.00 24.16 ? 456 ARG A N 1 ATOM 3510 C CA . ARG A 1 456 ? -43.926 23.939 -3.201 1.00 25.77 ? 456 ARG A CA 1 ATOM 3511 C C . ARG A 1 456 ? -45.150 24.009 -4.108 1.00 25.02 ? 456 ARG A C 1 ATOM 3512 O O . ARG A 1 456 ? -46.255 23.848 -3.629 1.00 25.00 ? 456 ARG A O 1 ATOM 3513 C CB . ARG A 1 456 ? -42.615 24.038 -4.002 1.00 27.34 ? 456 ARG A CB 1 ATOM 3514 C CG . ARG A 1 456 ? -41.393 24.355 -3.172 1.00 28.62 ? 456 ARG A CG 1 ATOM 3515 C CD . ARG A 1 456 ? -41.333 25.836 -2.808 1.00 29.35 ? 456 ARG A CD 1 ATOM 3516 N NE . ARG A 1 456 ? -41.029 26.727 -3.933 1.00 29.71 ? 456 ARG A NE 1 ATOM 3517 C CZ . ARG A 1 456 ? -39.822 27.183 -4.270 1.00 30.16 ? 456 ARG A CZ 1 ATOM 3518 N NH1 . ARG A 1 456 ? -38.720 26.814 -3.614 1.00 30.38 ? 456 ARG A NH1 1 ATOM 3519 N NH2 . ARG A 1 456 ? -39.707 28.013 -5.292 1.00 31.41 ? 456 ARG A NH2 1 ATOM 3520 N N . GLU A 1 457 ? -44.959 24.167 -5.414 1.00 25.58 ? 457 GLU A N 1 ATOM 3521 C CA . GLU A 1 457 ? -46.084 24.324 -6.334 1.00 25.68 ? 457 GLU A CA 1 ATOM 3522 C C . GLU A 1 457 ? -46.534 22.987 -6.919 1.00 24.99 ? 457 GLU A C 1 ATOM 3523 O O . GLU A 1 457 ? -47.303 22.962 -7.884 1.00 26.08 ? 457 GLU A O 1 ATOM 3524 C CB . GLU A 1 457 ? -45.708 25.291 -7.457 1.00 27.66 ? 457 GLU A CB 1 ATOM 3525 C CG . GLU A 1 457 ? -45.399 26.698 -6.964 1.00 29.23 ? 457 GLU A CG 1 ATOM 3526 C CD . GLU A 1 457 ? -46.540 27.289 -6.166 1.00 30.36 ? 457 GLU A CD 1 ATOM 3527 O OE1 . GLU A 1 457 ? -47.688 27.116 -6.594 1.00 32.52 ? 457 GLU A OE1 1 ATOM 3528 O OE2 . GLU A 1 457 ? -46.310 27.937 -5.127 1.00 32.08 ? 457 GLU A OE2 1 ATOM 3529 N N . ASN A 1 458 ? -46.085 21.876 -6.332 1.00 23.64 ? 458 ASN A N 1 ATOM 3530 C CA . ASN A 1 458 ? -46.353 20.563 -6.914 1.00 22.76 ? 458 ASN A CA 1 ATOM 3531 C C . ASN A 1 458 ? -47.545 19.862 -6.303 1.00 21.80 ? 458 ASN A C 1 ATOM 3532 O O . ASN A 1 458 ? -47.917 18.771 -6.748 1.00 21.27 ? 458 ASN A O 1 ATOM 3533 C CB . ASN A 1 458 ? -45.129 19.672 -6.798 1.00 23.36 ? 458 ASN A CB 1 ATOM 3534 C CG . ASN A 1 458 ? -43.942 20.227 -7.547 1.00 23.69 ? 458 ASN A CG 1 ATOM 3535 O OD1 . ASN A 1 458 ? -44.061 21.229 -8.264 1.00 23.50 ? 458 ASN A OD1 1 ATOM 3536 N ND2 . ASN A 1 458 ? -42.791 19.582 -7.386 1.00 23.79 ? 458 ASN A ND2 1 ATOM 3537 N N . ALA A 1 459 ? -48.140 20.479 -5.288 1.00 20.68 ? 459 ALA A N 1 ATOM 3538 C CA . ALA A 1 459 ? -49.271 19.882 -4.583 1.00 21.65 ? 459 ALA A CA 1 ATOM 3539 C C . ALA A 1 459 ? -50.259 20.931 -4.129 1.00 22.44 ? 459 ALA A C 1 ATOM 3540 O O . ALA A 1 459 ? -49.926 22.118 -4.039 1.00 24.48 ? 459 ALA A O 1 ATOM 3541 C CB . ALA A 1 459 ? -48.792 19.081 -3.377 1.00 20.70 ? 459 ALA A CB 1 ATOM 3542 N N . GLU A 1 460 ? -51.475 20.493 -3.840 1.00 22.55 ? 460 GLU A N 1 ATOM 3543 C CA . GLU A 1 460 ? -52.483 21.362 -3.229 1.00 23.24 ? 460 GLU A CA 1 ATOM 3544 C C . GLU A 1 460 ? -53.056 20.704 -1.978 1.00 23.94 ? 460 GLU A C 1 ATOM 3545 O O . GLU A 1 460 ? -53.182 19.469 -1.884 1.00 22.22 ? 460 GLU A O 1 ATOM 3546 C CB . GLU A 1 460 ? -53.619 21.693 -4.206 1.00 23.53 ? 460 GLU A CB 1 ATOM 3547 C CG . GLU A 1 460 ? -53.172 22.550 -5.381 1.00 23.62 ? 460 GLU A CG 1 ATOM 3548 C CD . GLU A 1 460 ? -54.243 22.785 -6.423 1.00 24.00 ? 460 GLU A CD 1 ATOM 3549 O OE1 . GLU A 1 460 ? -55.440 22.591 -6.145 1.00 24.26 ? 460 GLU A OE1 1 ATOM 3550 O OE2 . GLU A 1 460 ? -53.867 23.184 -7.543 1.00 23.77 ? 460 GLU A OE2 1 ATOM 3551 N N . ASP A 1 461 ? -53.387 21.557 -1.015 1.00 24.53 ? 461 ASP A N 1 ATOM 3552 C CA . ASP A 1 461 ? -53.986 21.152 0.249 1.00 24.96 ? 461 ASP A CA 1 ATOM 3553 C C . ASP A 1 461 ? -55.468 20.790 0.054 1.00 26.05 ? 461 ASP A C 1 ATOM 3554 O O . ASP A 1 461 ? -56.273 21.651 -0.303 1.00 25.65 ? 461 ASP A O 1 ATOM 3555 C CB . ASP A 1 461 ? -53.846 22.323 1.230 1.00 26.03 ? 461 ASP A CB 1 ATOM 3556 C CG . ASP A 1 461 ? -54.288 21.981 2.643 1.00 27.02 ? 461 ASP A CG 1 ATOM 3557 O OD1 . ASP A 1 461 ? -55.043 21.007 2.846 1.00 25.30 ? 461 ASP A OD1 1 ATOM 3558 O OD2 . ASP A 1 461 ? -53.875 22.736 3.558 1.00 29.49 ? 461 ASP A OD2 1 ATOM 3559 N N . MET A 1 462 ? -55.818 19.531 0.302 1.00 25.04 ? 462 MET A N 1 ATOM 3560 C CA . MET A 1 462 ? -57.182 19.025 0.082 1.00 27.36 ? 462 MET A CA 1 ATOM 3561 C C . MET A 1 462 ? -58.128 19.325 1.248 1.00 28.75 ? 462 MET A C 1 ATOM 3562 O O . MET A 1 462 ? -59.320 18.988 1.191 1.00 31.17 ? 462 MET A O 1 ATOM 3563 C CB . MET A 1 462 ? -57.166 17.505 -0.149 1.00 27.69 ? 462 MET A CB 1 ATOM 3564 C CG . MET A 1 462 ? -56.501 17.044 -1.440 1.00 29.33 ? 462 MET A CG 1 ATOM 3565 S SD . MET A 1 462 ? -56.065 15.278 -1.462 1.00 31.55 ? 462 MET A SD 1 ATOM 3566 C CE . MET A 1 462 ? -57.665 14.519 -1.178 1.00 33.22 ? 462 MET A CE 1 ATOM 3567 N N . GLY A 1 463 ? -57.619 19.916 2.324 1.00 27.31 ? 463 GLY A N 1 ATOM 3568 C CA . GLY A 1 463 ? -58.497 20.379 3.407 1.00 28.94 ? 463 GLY A CA 1 ATOM 3569 C C . GLY A 1 463 ? -58.745 19.371 4.508 1.00 29.01 ? 463 GLY A C 1 ATOM 3570 O O . GLY A 1 463 ? -59.348 19.705 5.531 1.00 30.94 ? 463 GLY A O 1 ATOM 3571 N N . ASN A 1 464 ? -58.272 18.144 4.310 1.00 28.24 ? 464 ASN A N 1 ATOM 3572 C CA . ASN A 1 464 ? -58.526 17.033 5.226 1.00 28.04 ? 464 ASN A CA 1 ATOM 3573 C C . ASN A 1 464 ? -57.233 16.502 5.856 1.00 26.53 ? 464 ASN A C 1 ATOM 3574 O O . ASN A 1 464 ? -57.191 15.377 6.336 1.00 27.15 ? 464 ASN A O 1 ATOM 3575 C CB . ASN A 1 464 ? -59.238 15.904 4.478 1.00 29.29 ? 464 ASN A CB 1 ATOM 3576 C CG . ASN A 1 464 ? -58.398 15.323 3.357 1.00 29.45 ? 464 ASN A CG 1 ATOM 3577 O OD1 . ASN A 1 464 ? -57.409 15.921 2.928 1.00 28.29 ? 464 ASN A OD1 1 ATOM 3578 N ND2 . ASN A 1 464 ? -58.793 14.149 2.867 1.00 30.93 ? 464 ASN A ND2 1 ATOM 3579 N N . GLY A 1 465 ? -56.193 17.327 5.855 1.00 24.95 ? 465 GLY A N 1 ATOM 3580 C CA . GLY A 1 465 ? -54.869 16.906 6.277 1.00 23.71 ? 465 GLY A CA 1 ATOM 3581 C C . GLY A 1 465 ? -54.078 16.156 5.220 1.00 22.29 ? 465 GLY A C 1 ATOM 3582 O O . GLY A 1 465 ? -53.062 15.546 5.544 1.00 21.84 ? 465 GLY A O 1 ATOM 3583 N N . CYS A 1 466 ? -54.536 16.193 3.974 1.00 21.98 ? 466 CYS A N 1 ATOM 3584 C CA . CYS A 1 466 ? -53.821 15.566 2.856 1.00 23.34 ? 466 CYS A CA 1 ATOM 3585 C C . CYS A 1 466 ? -53.502 16.550 1.750 1.00 22.80 ? 466 CYS A C 1 ATOM 3586 O O . CYS A 1 466 ? -54.184 17.570 1.564 1.00 23.99 ? 466 CYS A O 1 ATOM 3587 C CB . CYS A 1 466 ? -54.625 14.407 2.227 1.00 25.53 ? 466 CYS A CB 1 ATOM 3588 S SG . CYS A 1 466 ? -55.414 13.258 3.356 1.00 27.83 ? 466 CYS A SG 1 ATOM 3589 N N . PHE A 1 467 ? -52.471 16.200 0.994 1.00 21.99 ? 467 PHE A N 1 ATOM 3590 C CA . PHE A 1 467 ? -52.070 16.896 -0.205 1.00 21.38 ? 467 PHE A CA 1 ATOM 3591 C C . PHE A 1 467 ? -52.408 16.047 -1.446 1.00 22.82 ? 467 PHE A C 1 ATOM 3592 O O . PHE A 1 467 ? -52.182 14.832 -1.459 1.00 22.47 ? 467 PHE A O 1 ATOM 3593 C CB . PHE A 1 467 ? -50.560 17.100 -0.179 1.00 20.82 ? 467 PHE A CB 1 ATOM 3594 C CG . PHE A 1 467 ? -50.081 17.945 0.959 1.00 21.11 ? 467 PHE A CG 1 ATOM 3595 C CD1 . PHE A 1 467 ? -50.197 19.313 0.899 1.00 21.55 ? 467 PHE A CD1 1 ATOM 3596 C CD2 . PHE A 1 467 ? -49.530 17.356 2.096 1.00 21.11 ? 467 PHE A CD2 1 ATOM 3597 C CE1 . PHE A 1 467 ? -49.765 20.106 1.964 1.00 22.16 ? 467 PHE A CE1 1 ATOM 3598 C CE2 . PHE A 1 467 ? -49.101 18.127 3.149 1.00 22.19 ? 467 PHE A CE2 1 ATOM 3599 C CZ . PHE A 1 467 ? -49.216 19.511 3.088 1.00 22.05 ? 467 PHE A CZ 1 ATOM 3600 N N . LYS A 1 468 ? -52.951 16.700 -2.460 1.00 23.63 ? 468 LYS A N 1 ATOM 3601 C CA . LYS A 1 468 ? -53.010 16.137 -3.804 1.00 24.14 ? 468 LYS A CA 1 ATOM 3602 C C . LYS A 1 468 ? -51.713 16.522 -4.475 1.00 23.14 ? 468 LYS A C 1 ATOM 3603 O O . LYS A 1 468 ? -51.420 17.703 -4.650 1.00 21.79 ? 468 LYS A O 1 ATOM 3604 C CB . LYS A 1 468 ? -54.195 16.681 -4.584 1.00 25.96 ? 468 LYS A CB 1 ATOM 3605 C CG . LYS A 1 468 ? -54.283 16.144 -6.012 1.00 28.81 ? 468 LYS A CG 1 ATOM 3606 C CD . LYS A 1 468 ? -55.614 16.508 -6.668 1.00 31.87 ? 468 LYS A CD 1 ATOM 3607 C CE . LYS A 1 468 ? -55.663 16.074 -8.134 1.00 33.94 ? 468 LYS A CE 1 ATOM 3608 N NZ . LYS A 1 468 ? -56.984 16.392 -8.757 1.00 36.33 ? 468 LYS A NZ 1 ATOM 3609 N N . ILE A 1 469 ? -50.899 15.518 -4.779 1.00 22.44 ? 469 ILE A N 1 ATOM 3610 C CA . ILE A 1 469 ? -49.629 15.734 -5.434 1.00 21.99 ? 469 ILE A CA 1 ATOM 3611 C C . ILE A 1 469 ? -49.892 15.544 -6.934 1.00 23.30 ? 469 ILE A C 1 ATOM 3612 O O . ILE A 1 469 ? -50.362 14.486 -7.357 1.00 23.92 ? 469 ILE A O 1 ATOM 3613 C CB . ILE A 1 469 ? -48.562 14.741 -4.936 1.00 22.29 ? 469 ILE A CB 1 ATOM 3614 C CG1 . ILE A 1 469 ? -48.272 14.956 -3.443 1.00 21.49 ? 469 ILE A CG1 1 ATOM 3615 C CG2 . ILE A 1 469 ? -47.267 14.861 -5.738 1.00 21.98 ? 469 ILE A CG2 1 ATOM 3616 C CD1 . ILE A 1 469 ? -47.288 13.948 -2.884 1.00 22.65 ? 469 ILE A CD1 1 ATOM 3617 N N . TYR A 1 470 ? -49.570 16.563 -7.725 1.00 24.23 ? 470 TYR A N 1 ATOM 3618 C CA . TYR A 1 470 ? -49.992 16.616 -9.130 1.00 25.78 ? 470 TYR A CA 1 ATOM 3619 C C . TYR A 1 470 ? -48.967 16.002 -10.095 1.00 26.12 ? 470 TYR A C 1 ATOM 3620 O O . TYR A 1 470 ? -48.785 16.481 -11.209 1.00 27.22 ? 470 TYR A O 1 ATOM 3621 C CB . TYR A 1 470 ? -50.345 18.055 -9.514 1.00 25.67 ? 470 TYR A CB 1 ATOM 3622 C CG . TYR A 1 470 ? -51.710 18.513 -9.054 1.00 26.63 ? 470 TYR A CG 1 ATOM 3623 C CD1 . TYR A 1 470 ? -51.910 19.015 -7.767 1.00 26.40 ? 470 TYR A CD1 1 ATOM 3624 C CD2 . TYR A 1 470 ? -52.799 18.487 -9.923 1.00 27.78 ? 470 TYR A CD2 1 ATOM 3625 C CE1 . TYR A 1 470 ? -53.165 19.455 -7.354 1.00 27.36 ? 470 TYR A CE1 1 ATOM 3626 C CE2 . TYR A 1 470 ? -54.055 18.916 -9.517 1.00 29.03 ? 470 TYR A CE2 1 ATOM 3627 C CZ . TYR A 1 470 ? -54.234 19.405 -8.231 1.00 28.21 ? 470 TYR A CZ 1 ATOM 3628 O OH . TYR A 1 470 ? -55.474 19.840 -7.848 1.00 28.95 ? 470 TYR A OH 1 ATOM 3629 N N . HIS A 1 471 ? -48.299 14.939 -9.659 1.00 26.85 ? 471 HIS A N 1 ATOM 3630 C CA . HIS A 1 471 ? -47.395 14.207 -10.517 1.00 27.06 ? 471 HIS A CA 1 ATOM 3631 C C . HIS A 1 471 ? -47.320 12.779 -10.078 1.00 27.75 ? 471 HIS A C 1 ATOM 3632 O O . HIS A 1 471 ? -47.703 12.439 -8.961 1.00 27.30 ? 471 HIS A O 1 ATOM 3633 C CB . HIS A 1 471 ? -46.012 14.864 -10.551 1.00 27.00 ? 471 HIS A CB 1 ATOM 3634 C CG . HIS A 1 471 ? -45.303 14.908 -9.219 1.00 26.13 ? 471 HIS A CG 1 ATOM 3635 N ND1 . HIS A 1 471 ? -44.605 13.858 -8.735 1.00 26.17 ? 471 HIS A ND1 1 ATOM 3636 C CD2 . HIS A 1 471 ? -45.164 15.937 -8.294 1.00 25.06 ? 471 HIS A CD2 1 ATOM 3637 C CE1 . HIS A 1 471 ? -44.074 14.187 -7.548 1.00 25.87 ? 471 HIS A CE1 1 ATOM 3638 N NE2 . HIS A 1 471 ? -44.411 15.465 -7.278 1.00 24.35 ? 471 HIS A NE2 1 ATOM 3639 N N . LYS A 1 472 ? -46.817 11.925 -10.949 1.00 27.28 ? 472 LYS A N 1 ATOM 3640 C CA . LYS A 1 472 ? -46.596 10.548 -10.584 1.00 30.03 ? 472 LYS A CA 1 ATOM 3641 C C . LYS A 1 472 ? -45.576 10.530 -9.467 1.00 28.51 ? 472 LYS A C 1 ATOM 3642 O O . LYS A 1 472 ? -44.509 11.133 -9.579 1.00 28.03 ? 472 LYS A O 1 ATOM 3643 C CB . LYS A 1 472 ? -46.086 9.757 -11.790 1.00 32.77 ? 472 LYS A CB 1 ATOM 3644 C CG . LYS A 1 472 ? -45.821 8.299 -11.500 1.00 37.06 ? 472 LYS A CG 1 ATOM 3645 C CD . LYS A 1 472 ? -45.636 7.520 -12.802 1.00 40.61 ? 472 LYS A CD 1 ATOM 3646 C CE . LYS A 1 472 ? -45.762 6.019 -12.592 1.00 45.24 ? 472 LYS A CE 1 ATOM 3647 N NZ . LYS A 1 472 ? -44.497 5.428 -12.080 1.00 49.30 ? 472 LYS A NZ 1 ATOM 3648 N N . CYS A 1 473 ? -45.905 9.866 -8.375 1.00 28.67 ? 473 CYS A N 1 ATOM 3649 C CA . CYS A 1 473 ? -45.022 9.887 -7.215 1.00 28.87 ? 473 CYS A CA 1 ATOM 3650 C C . CYS A 1 473 ? -45.021 8.492 -6.644 1.00 29.66 ? 473 CYS A C 1 ATOM 3651 O O . CYS A 1 473 ? -45.860 8.151 -5.821 1.00 30.18 ? 473 CYS A O 1 ATOM 3652 C CB . CYS A 1 473 ? -45.437 10.992 -6.203 1.00 29.26 ? 473 CYS A CB 1 ATOM 3653 S SG . CYS A 1 473 ? -44.286 11.308 -4.819 1.00 31.16 ? 473 CYS A SG 1 ATOM 3654 N N . ASP A 1 474 ? -44.070 7.684 -7.118 1.00 29.25 ? 474 ASP A N 1 ATOM 3655 C CA . ASP A 1 474 ? -43.941 6.289 -6.726 1.00 30.11 ? 474 ASP A CA 1 ATOM 3656 C C . ASP A 1 474 ? -43.398 6.135 -5.292 1.00 30.01 ? 474 ASP A C 1 ATOM 3657 O O . ASP A 1 474 ? -43.193 7.126 -4.578 1.00 27.16 ? 474 ASP A O 1 ATOM 3658 C CB . ASP A 1 474 ? -43.065 5.534 -7.752 1.00 31.71 ? 474 ASP A CB 1 ATOM 3659 C CG . ASP A 1 474 ? -41.586 5.961 -7.734 1.00 32.30 ? 474 ASP A CG 1 ATOM 3660 O OD1 . ASP A 1 474 ? -41.127 6.710 -6.835 1.00 29.84 ? 474 ASP A OD1 1 ATOM 3661 O OD2 . ASP A 1 474 ? -40.860 5.522 -8.650 1.00 33.72 ? 474 ASP A OD2 1 ATOM 3662 N N . ASN A 1 475 ? -43.157 4.898 -4.869 1.00 29.68 ? 475 ASN A N 1 ATOM 3663 C CA . ASN A 1 475 ? -42.797 4.657 -3.475 1.00 30.20 ? 475 ASN A CA 1 ATOM 3664 C C . ASN A 1 475 ? -41.519 5.365 -3.044 1.00 29.47 ? 475 ASN A C 1 ATOM 3665 O O . ASN A 1 475 ? -41.436 5.885 -1.925 1.00 28.25 ? 475 ASN A O 1 ATOM 3666 C CB . ASN A 1 475 ? -42.695 3.164 -3.185 1.00 31.66 ? 475 ASN A CB 1 ATOM 3667 C CG . ASN A 1 475 ? -44.050 2.495 -3.105 1.00 32.64 ? 475 ASN A CG 1 ATOM 3668 O OD1 . ASN A 1 475 ? -45.091 3.158 -3.096 1.00 31.90 ? 475 ASN A OD1 1 ATOM 3669 N ND2 . ASN A 1 475 ? -44.047 1.173 -3.063 1.00 34.06 ? 475 ASN A ND2 1 ATOM 3670 N N . ALA A 1 476 ? -40.541 5.392 -3.940 1.00 29.72 ? 476 ALA A N 1 ATOM 3671 C CA . ALA A 1 476 ? -39.301 6.100 -3.698 1.00 30.44 ? 476 ALA A CA 1 ATOM 3672 C C . ALA A 1 476 ? -39.535 7.610 -3.601 1.00 28.48 ? 476 ALA A C 1 ATOM 3673 O O . ALA A 1 476 ? -38.919 8.273 -2.777 1.00 29.68 ? 476 ALA A O 1 ATOM 3674 C CB . ALA A 1 476 ? -38.277 5.780 -4.782 1.00 30.88 ? 476 ALA A CB 1 ATOM 3675 N N . CYS A 1 477 ? -40.428 8.135 -4.426 1.00 27.65 ? 477 CYS A N 1 ATOM 3676 C CA . CYS A 1 477 ? -40.752 9.565 -4.411 1.00 27.92 ? 477 CYS A CA 1 ATOM 3677 C C . CYS A 1 477 ? -41.393 9.938 -3.080 1.00 25.96 ? 477 CYS A C 1 ATOM 3678 O O . CYS A 1 477 ? -40.988 10.910 -2.447 1.00 25.96 ? 477 CYS A O 1 ATOM 3679 C CB . CYS A 1 477 ? -41.672 9.910 -5.581 1.00 29.19 ? 477 CYS A CB 1 ATOM 3680 S SG . CYS A 1 477 ? -42.363 11.582 -5.636 1.00 29.95 ? 477 CYS A SG 1 ATOM 3681 N N . ILE A 1 478 ? -42.372 9.155 -2.655 1.00 25.25 ? 478 ILE A N 1 ATOM 3682 C CA . ILE A 1 478 ? -43.047 9.400 -1.386 1.00 25.97 ? 478 ILE A CA 1 ATOM 3683 C C . ILE A 1 478 ? -42.021 9.333 -0.261 1.00 26.81 ? 478 ILE A C 1 ATOM 3684 O O . ILE A 1 478 ? -42.005 10.199 0.625 1.00 26.26 ? 478 ILE A O 1 ATOM 3685 C CB . ILE A 1 478 ? -44.186 8.394 -1.129 1.00 25.90 ? 478 ILE A CB 1 ATOM 3686 C CG1 . ILE A 1 478 ? -45.318 8.558 -2.159 1.00 25.50 ? 478 ILE A CG1 1 ATOM 3687 C CG2 . ILE A 1 478 ? -44.706 8.513 0.307 1.00 26.03 ? 478 ILE A CG2 1 ATOM 3688 C CD1 . ILE A 1 478 ? -46.107 9.861 -2.081 1.00 25.00 ? 478 ILE A CD1 1 ATOM 3689 N N . GLY A 1 479 ? -41.148 8.326 -0.318 1.00 27.12 ? 479 GLY A N 1 ATOM 3690 C CA . GLY A 1 479 ? -40.053 8.186 0.621 1.00 27.67 ? 479 GLY A CA 1 ATOM 3691 C C . GLY A 1 479 ? -39.156 9.409 0.693 1.00 27.49 ? 479 GLY A C 1 ATOM 3692 O O . GLY A 1 479 ? -38.718 9.785 1.776 1.00 28.41 ? 479 GLY A O 1 ATOM 3693 N N . SER A 1 480 ? -38.879 10.026 -0.450 1.00 27.22 ? 480 SER A N 1 ATOM 3694 C CA . SER A 1 480 ? -38.057 11.241 -0.491 1.00 28.05 ? 480 SER A CA 1 ATOM 3695 C C . SER A 1 480 ? -38.732 12.398 0.262 1.00 28.06 ? 480 SER A C 1 ATOM 3696 O O . SER A 1 480 ? -38.048 13.212 0.887 1.00 28.15 ? 480 SER A O 1 ATOM 3697 C CB . SER A 1 480 ? -37.726 11.651 -1.926 1.00 29.22 ? 480 SER A CB 1 ATOM 3698 O OG . SER A 1 480 ? -38.847 12.212 -2.605 1.00 28.68 ? 480 SER A OG 1 ATOM 3699 N N . ILE A 1 481 ? -40.065 12.450 0.209 1.00 26.98 ? 481 ILE A N 1 ATOM 3700 C CA . ILE A 1 481 ? -40.833 13.469 0.933 1.00 26.77 ? 481 ILE A CA 1 ATOM 3701 C C . ILE A 1 481 ? -40.752 13.182 2.421 1.00 28.52 ? 481 ILE A C 1 ATOM 3702 O O . ILE A 1 481 ? -40.425 14.065 3.219 1.00 29.49 ? 481 ILE A O 1 ATOM 3703 C CB . ILE A 1 481 ? -42.299 13.532 0.484 1.00 25.38 ? 481 ILE A CB 1 ATOM 3704 C CG1 . ILE A 1 481 ? -42.368 13.863 -1.001 1.00 25.00 ? 481 ILE A CG1 1 ATOM 3705 C CG2 . ILE A 1 481 ? -43.065 14.596 1.283 1.00 25.00 ? 481 ILE A CG2 1 ATOM 3706 C CD1 . ILE A 1 481 ? -43.732 13.637 -1.608 1.00 25.10 ? 481 ILE A CD1 1 ATOM 3707 N N . ARG A 1 482 ? -41.004 11.938 2.802 1.00 29.45 ? 482 ARG A N 1 ATOM 3708 C CA . ARG A 1 482 ? -40.923 11.559 4.211 1.00 30.38 ? 482 ARG A CA 1 ATOM 3709 C C . ARG A 1 482 ? -39.531 11.771 4.817 1.00 33.52 ? 482 ARG A C 1 ATOM 3710 O O . ARG A 1 482 ? -39.411 12.158 5.994 1.00 33.47 ? 482 ARG A O 1 ATOM 3711 C CB . ARG A 1 482 ? -41.342 10.109 4.386 1.00 30.64 ? 482 ARG A CB 1 ATOM 3712 C CG . ARG A 1 482 ? -42.769 9.820 4.003 1.00 30.06 ? 482 ARG A CG 1 ATOM 3713 C CD . ARG A 1 482 ? -43.202 8.450 4.479 1.00 31.03 ? 482 ARG A CD 1 ATOM 3714 N NE . ARG A 1 482 ? -42.274 7.444 4.001 1.00 32.15 ? 482 ARG A NE 1 ATOM 3715 C CZ . ARG A 1 482 ? -42.582 6.376 3.270 1.00 33.56 ? 482 ARG A CZ 1 ATOM 3716 N NH1 . ARG A 1 482 ? -43.837 6.063 2.950 1.00 32.81 ? 482 ARG A NH1 1 ATOM 3717 N NH2 . ARG A 1 482 ? -41.590 5.578 2.882 1.00 35.19 ? 482 ARG A NH2 1 ATOM 3718 N N . ASN A 1 483 ? -38.494 11.517 4.018 1.00 35.82 ? 483 ASN A N 1 ATOM 3719 C CA . ASN A 1 483 ? -37.091 11.680 4.418 1.00 39.28 ? 483 ASN A CA 1 ATOM 3720 C C . ASN A 1 483 ? -36.573 13.101 4.331 1.00 39.04 ? 483 ASN A C 1 ATOM 3721 O O . ASN A 1 483 ? -35.464 13.373 4.778 1.00 39.20 ? 483 ASN A O 1 ATOM 3722 C CB . ASN A 1 483 ? -36.168 10.861 3.510 1.00 43.53 ? 483 ASN A CB 1 ATOM 3723 C CG . ASN A 1 483 ? -36.238 9.382 3.776 1.00 47.71 ? 483 ASN A CG 1 ATOM 3724 O OD1 . ASN A 1 483 ? -37.044 8.914 4.588 1.00 52.32 ? 483 ASN A OD1 1 ATOM 3725 N ND2 . ASN A 1 483 ? -35.379 8.626 3.091 1.00 49.93 ? 483 ASN A ND2 1 ATOM 3726 N N . GLY A 1 484 ? -37.329 13.985 3.692 1.00 37.38 ? 484 GLY A N 1 ATOM 3727 C CA . GLY A 1 484 ? -36.914 15.366 3.550 1.00 37.45 ? 484 GLY A CA 1 ATOM 3728 C C . GLY A 1 484 ? -35.892 15.616 2.467 1.00 38.18 ? 484 GLY A C 1 ATOM 3729 O O . GLY A 1 484 ? -35.158 16.596 2.551 1.00 40.43 ? 484 GLY A O 1 ATOM 3730 N N . THR A 1 485 ? -35.843 14.753 1.446 1.00 37.53 ? 485 THR A N 1 ATOM 3731 C CA . THR A 1 485 ? -34.912 14.904 0.315 1.00 37.71 ? 485 THR A CA 1 ATOM 3732 C C . THR A 1 485 ? -35.607 15.136 -1.043 1.00 35.52 ? 485 THR A C 1 ATOM 3733 O O . THR A 1 485 ? -34.964 15.159 -2.077 1.00 37.71 ? 485 THR A O 1 ATOM 3734 C CB . THR A 1 485 ? -33.985 13.682 0.185 1.00 39.21 ? 485 THR A CB 1 ATOM 3735 O OG1 . THR A 1 485 ? -34.757 12.497 -0.081 1.00 37.63 ? 485 THR A OG1 1 ATOM 3736 C CG2 . THR A 1 485 ? -33.171 13.498 1.466 1.00 40.09 ? 485 THR A CG2 1 ATOM 3737 N N . TYR A 1 486 ? -36.916 15.331 -1.019 1.00 33.74 ? 486 TYR A N 1 ATOM 3738 C CA . TYR A 1 486 ? -37.705 15.573 -2.220 1.00 31.61 ? 486 TYR A CA 1 ATOM 3739 C C . TYR A 1 486 ? -37.248 16.847 -2.914 1.00 32.10 ? 486 TYR A C 1 ATOM 3740 O O . TYR A 1 486 ? -37.116 17.882 -2.276 1.00 31.28 ? 486 TYR A O 1 ATOM 3741 C CB . TYR A 1 486 ? -39.161 15.676 -1.806 1.00 29.91 ? 486 TYR A CB 1 ATOM 3742 C CG . TYR A 1 486 ? -40.140 16.072 -2.874 1.00 28.06 ? 486 TYR A CG 1 ATOM 3743 C CD1 . TYR A 1 486 ? -40.715 15.120 -3.700 1.00 26.60 ? 486 TYR A CD1 1 ATOM 3744 C CD2 . TYR A 1 486 ? -40.543 17.399 -3.007 1.00 26.38 ? 486 TYR A CD2 1 ATOM 3745 C CE1 . TYR A 1 486 ? -41.654 15.487 -4.653 1.00 26.52 ? 486 TYR A CE1 1 ATOM 3746 C CE2 . TYR A 1 486 ? -41.478 17.772 -3.946 1.00 25.79 ? 486 TYR A CE2 1 ATOM 3747 C CZ . TYR A 1 486 ? -42.027 16.820 -4.770 1.00 25.60 ? 486 TYR A CZ 1 ATOM 3748 O OH . TYR A 1 486 ? -42.938 17.213 -5.696 1.00 23.94 ? 486 TYR A OH 1 ATOM 3749 N N . ASP A 1 487 ? -36.974 16.751 -4.211 1.00 32.26 ? 487 ASP A N 1 ATOM 3750 C CA . ASP A 1 487 ? -36.540 17.893 -5.001 1.00 33.73 ? 487 ASP A CA 1 ATOM 3751 C C . ASP A 1 487 ? -37.711 18.343 -5.864 1.00 31.81 ? 487 ASP A C 1 ATOM 3752 O O . ASP A 1 487 ? -38.004 17.733 -6.896 1.00 30.85 ? 487 ASP A O 1 ATOM 3753 C CB . ASP A 1 487 ? -35.342 17.511 -5.872 1.00 37.43 ? 487 ASP A CB 1 ATOM 3754 C CG . ASP A 1 487 ? -34.722 18.709 -6.594 1.00 40.00 ? 487 ASP A CG 1 ATOM 3755 O OD1 . ASP A 1 487 ? -35.352 19.794 -6.636 1.00 40.30 ? 487 ASP A OD1 1 ATOM 3756 O OD2 . ASP A 1 487 ? -33.589 18.559 -7.108 1.00 43.75 ? 487 ASP A OD2 1 ATOM 3757 N N . HIS A 1 488 ? -38.369 19.421 -5.449 1.00 28.38 ? 488 HIS A N 1 ATOM 3758 C CA . HIS A 1 488 ? -39.566 19.888 -6.144 1.00 28.36 ? 488 HIS A CA 1 ATOM 3759 C C . HIS A 1 488 ? -39.289 20.288 -7.572 1.00 28.60 ? 488 HIS A C 1 ATOM 3760 O O . HIS A 1 488 ? -40.164 20.181 -8.423 1.00 28.23 ? 488 HIS A O 1 ATOM 3761 C CB . HIS A 1 488 ? -40.204 21.056 -5.390 1.00 27.40 ? 488 HIS A CB 1 ATOM 3762 C CG . HIS A 1 488 ? -39.518 22.371 -5.626 1.00 27.59 ? 488 HIS A CG 1 ATOM 3763 N ND1 . HIS A 1 488 ? -40.045 23.328 -6.416 1.00 28.05 ? 488 HIS A ND1 1 ATOM 3764 C CD2 . HIS A 1 488 ? -38.287 22.856 -5.178 1.00 28.19 ? 488 HIS A CD2 1 ATOM 3765 C CE1 . HIS A 1 488 ? -39.199 24.385 -6.458 1.00 29.25 ? 488 HIS A CE1 1 ATOM 3766 N NE2 . HIS A 1 488 ? -38.129 24.099 -5.692 1.00 28.28 ? 488 HIS A NE2 1 ATOM 3767 N N . ASP A 1 489 ? -38.077 20.750 -7.855 1.00 29.77 ? 489 ASP A N 1 ATOM 3768 C CA . ASP A 1 489 ? -37.733 21.178 -9.219 1.00 32.90 ? 489 ASP A CA 1 ATOM 3769 C C . ASP A 1 489 ? -37.850 20.064 -10.250 1.00 31.87 ? 489 ASP A C 1 ATOM 3770 O O . ASP A 1 489 ? -38.258 20.310 -11.382 1.00 31.97 ? 489 ASP A O 1 ATOM 3771 C CB . ASP A 1 489 ? -36.323 21.772 -9.263 1.00 35.41 ? 489 ASP A CB 1 ATOM 3772 C CG . ASP A 1 489 ? -36.308 23.225 -8.882 1.00 38.40 ? 489 ASP A CG 1 ATOM 3773 O OD1 . ASP A 1 489 ? -37.149 23.988 -9.408 1.00 42.00 ? 489 ASP A OD1 1 ATOM 3774 O OD2 . ASP A 1 489 ? -35.456 23.616 -8.065 1.00 42.39 ? 489 ASP A OD2 1 ATOM 3775 N N . VAL A 1 490 ? -37.494 18.853 -9.839 1.00 32.62 ? 490 VAL A N 1 ATOM 3776 C CA . VAL A 1 490 ? -37.553 17.660 -10.687 1.00 34.71 ? 490 VAL A CA 1 ATOM 3777 C C . VAL A 1 490 ? -38.950 17.429 -11.268 1.00 33.31 ? 490 VAL A C 1 ATOM 3778 O O . VAL A 1 490 ? -39.084 16.985 -12.411 1.00 32.12 ? 490 VAL A O 1 ATOM 3779 C CB . VAL A 1 490 ? -37.119 16.406 -9.878 1.00 36.18 ? 490 VAL A CB 1 ATOM 3780 C CG1 . VAL A 1 490 ? -37.384 15.121 -10.643 1.00 40.00 ? 490 VAL A CG1 1 ATOM 3781 C CG2 . VAL A 1 490 ? -35.649 16.503 -9.496 1.00 39.01 ? 490 VAL A CG2 1 ATOM 3782 N N . TYR A 1 491 ? -39.983 17.732 -10.483 1.00 30.39 ? 491 TYR A N 1 ATOM 3783 C CA . TYR A 1 491 ? -41.377 17.423 -10.864 1.00 29.70 ? 491 TYR A CA 1 ATOM 3784 C C . TYR A 1 491 ? -42.219 18.627 -11.258 1.00 28.04 ? 491 TYR A C 1 ATOM 3785 O O . TYR A 1 491 ? -43.373 18.469 -11.629 1.00 28.17 ? 491 TYR A O 1 ATOM 3786 C CB . TYR A 1 491 ? -42.085 16.717 -9.705 1.00 28.60 ? 491 TYR A CB 1 ATOM 3787 C CG . TYR A 1 491 ? -41.376 15.488 -9.222 1.00 29.09 ? 491 TYR A CG 1 ATOM 3788 C CD1 . TYR A 1 491 ? -41.514 14.275 -9.891 1.00 29.88 ? 491 TYR A CD1 1 ATOM 3789 C CD2 . TYR A 1 491 ? -40.557 15.530 -8.101 1.00 29.82 ? 491 TYR A CD2 1 ATOM 3790 C CE1 . TYR A 1 491 ? -40.871 13.128 -9.441 1.00 30.87 ? 491 TYR A CE1 1 ATOM 3791 C CE2 . TYR A 1 491 ? -39.902 14.394 -7.650 1.00 30.12 ? 491 TYR A CE2 1 ATOM 3792 C CZ . TYR A 1 491 ? -40.067 13.198 -8.318 1.00 31.41 ? 491 TYR A CZ 1 ATOM 3793 O OH . TYR A 1 491 ? -39.407 12.073 -7.864 1.00 33.95 ? 491 TYR A OH 1 ATOM 3794 N N . ARG A 1 492 ? -41.656 19.827 -11.171 1.00 28.43 ? 492 ARG A N 1 ATOM 3795 C CA . ARG A 1 492 ? -42.463 21.042 -11.245 1.00 27.59 ? 492 ARG A CA 1 ATOM 3796 C C . ARG A 1 492 ? -43.154 21.229 -12.597 1.00 28.63 ? 492 ARG A C 1 ATOM 3797 O O . ARG A 1 492 ? -44.332 21.600 -12.651 1.00 28.64 ? 492 ARG A O 1 ATOM 3798 C CB . ARG A 1 492 ? -41.588 22.245 -10.920 1.00 27.96 ? 492 ARG A CB 1 ATOM 3799 C CG . ARG A 1 492 ? -42.299 23.576 -10.926 1.00 27.61 ? 492 ARG A CG 1 ATOM 3800 C CD . ARG A 1 492 ? -41.319 24.633 -10.472 1.00 28.63 ? 492 ARG A CD 1 ATOM 3801 N NE . ARG A 1 492 ? -41.846 25.979 -10.585 1.00 28.43 ? 492 ARG A NE 1 ATOM 3802 C CZ . ARG A 1 492 ? -42.235 26.744 -9.568 1.00 28.67 ? 492 ARG A CZ 1 ATOM 3803 N NH1 . ARG A 1 492 ? -42.172 26.318 -8.304 1.00 28.05 ? 492 ARG A NH1 1 ATOM 3804 N NH2 . ARG A 1 492 ? -42.685 27.965 -9.820 1.00 29.17 ? 492 ARG A NH2 1 ATOM 3805 N N . ASP A 1 493 ? -42.437 20.971 -13.690 1.00 30.22 ? 493 ASP A N 1 ATOM 3806 C CA . ASP A 1 493 ? -43.043 21.083 -15.022 1.00 31.83 ? 493 ASP A CA 1 ATOM 3807 C C . ASP A 1 493 ? -44.249 20.153 -15.134 1.00 30.21 ? 493 ASP A C 1 ATOM 3808 O O . ASP A 1 493 ? -45.327 20.573 -15.565 1.00 29.04 ? 493 ASP A O 1 ATOM 3809 C CB . ASP A 1 493 ? -42.026 20.771 -16.129 1.00 35.35 ? 493 ASP A CB 1 ATOM 3810 C CG . ASP A 1 493 ? -41.001 21.883 -16.318 1.00 38.77 ? 493 ASP A CG 1 ATOM 3811 O OD1 . ASP A 1 493 ? -41.256 23.022 -15.877 1.00 39.37 ? 493 ASP A OD1 1 ATOM 3812 O OD2 . ASP A 1 493 ? -39.942 21.621 -16.929 1.00 43.04 ? 493 ASP A OD2 1 ATOM 3813 N N . GLU A 1 494 ? -44.067 18.900 -14.735 1.00 29.34 ? 494 GLU A N 1 ATOM 3814 C CA . GLU A 1 494 ? -45.158 17.918 -14.757 1.00 30.11 ? 494 GLU A CA 1 ATOM 3815 C C . GLU A 1 494 ? -46.308 18.400 -13.882 1.00 29.42 ? 494 GLU A C 1 ATOM 3816 O O . GLU A 1 494 ? -47.470 18.419 -14.320 1.00 28.36 ? 494 GLU A O 1 ATOM 3817 C CB . GLU A 1 494 ? -44.670 16.535 -14.301 1.00 31.08 ? 494 GLU A CB 1 ATOM 3818 C CG . GLU A 1 494 ? -45.762 15.455 -14.227 1.00 31.91 ? 494 GLU A CG 1 ATOM 3819 C CD . GLU A 1 494 ? -45.254 14.105 -13.727 1.00 32.32 ? 494 GLU A CD 1 ATOM 3820 O OE1 . GLU A 1 494 ? -44.049 13.974 -13.434 1.00 33.27 ? 494 GLU A OE1 1 ATOM 3821 O OE2 . GLU A 1 494 ? -46.072 13.163 -13.587 1.00 32.85 ? 494 GLU A OE2 1 ATOM 3822 N N . ALA A 1 495 ? -45.992 18.827 -12.656 1.00 27.90 ? 495 ALA A N 1 ATOM 3823 C CA . ALA A 1 495 ? -47.049 19.225 -11.721 1.00 27.92 ? 495 ALA A CA 1 ATOM 3824 C C . ALA A 1 495 ? -47.815 20.448 -12.211 1.00 28.00 ? 495 ALA A C 1 ATOM 3825 O O . ALA A 1 495 ? -49.035 20.477 -12.150 1.00 28.18 ? 495 ALA A O 1 ATOM 3826 C CB . ALA A 1 495 ? -46.473 19.466 -10.319 1.00 28.15 ? 495 ALA A CB 1 ATOM 3827 N N . LEU A 1 496 ? -47.109 21.457 -12.705 1.00 28.89 ? 496 LEU A N 1 ATOM 3828 C CA . LEU A 1 496 ? -47.778 22.698 -13.132 1.00 30.30 ? 496 LEU A CA 1 ATOM 3829 C C . LEU A 1 496 ? -48.714 22.467 -14.313 1.00 32.47 ? 496 LEU A C 1 ATOM 3830 O O . LEU A 1 496 ? -49.806 23.046 -14.365 1.00 33.52 ? 496 LEU A O 1 ATOM 3831 C CB . LEU A 1 496 ? -46.766 23.795 -13.465 1.00 31.38 ? 496 LEU A CB 1 ATOM 3832 C CG . LEU A 1 496 ? -46.011 24.402 -12.276 1.00 31.65 ? 496 LEU A CG 1 ATOM 3833 C CD1 . LEU A 1 496 ? -44.982 25.410 -12.785 1.00 33.09 ? 496 LEU A CD1 1 ATOM 3834 C CD2 . LEU A 1 496 ? -46.965 25.031 -11.270 1.00 31.87 ? 496 LEU A CD2 1 ATOM 3835 N N . ASN A 1 497 ? -48.289 21.624 -15.253 1.00 33.08 ? 497 ASN A N 1 ATOM 3836 C CA A ASN A 1 497 ? -49.145 21.254 -16.378 0.50 33.96 ? 497 ASN A CA 1 ATOM 3837 C CA B ASN A 1 497 ? -49.140 21.262 -16.374 0.50 34.73 ? 497 ASN A CA 1 ATOM 3838 C C . ASN A 1 497 ? -50.416 20.583 -15.885 1.00 34.09 ? 497 ASN A C 1 ATOM 3839 O O . ASN A 1 497 ? -51.507 20.886 -16.368 1.00 34.73 ? 497 ASN A O 1 ATOM 3840 C CB A ASN A 1 497 ? -48.427 20.323 -17.365 0.50 34.78 ? 497 ASN A CB 1 ATOM 3841 C CB B ASN A 1 497 ? -48.396 20.357 -17.365 0.50 36.64 ? 497 ASN A CB 1 ATOM 3842 C CG A ASN A 1 497 ? -49.377 19.733 -18.399 0.50 35.72 ? 497 ASN A CG 1 ATOM 3843 C CG B ASN A 1 497 ? -48.437 20.898 -18.772 0.50 38.97 ? 497 ASN A CG 1 ATOM 3844 O OD1 A ASN A 1 497 ? -49.508 18.517 -18.518 0.50 36.28 ? 497 ASN A OD1 1 ATOM 3845 O OD1 B ASN A 1 497 ? -49.156 20.384 -19.636 0.50 42.42 ? 497 ASN A OD1 1 ATOM 3846 N ND2 A ASN A 1 497 ? -50.071 20.605 -19.132 0.50 37.29 ? 497 ASN A ND2 1 ATOM 3847 N ND2 B ASN A 1 497 ? -47.679 21.960 -19.010 0.50 39.10 ? 497 ASN A ND2 1 ATOM 3848 N N . ASN A 1 498 ? -50.277 19.679 -14.914 1.00 32.42 ? 498 ASN A N 1 ATOM 3849 C CA . ASN A 1 498 ? -51.433 18.982 -14.358 1.00 33.09 ? 498 ASN A CA 1 ATOM 3850 C C . ASN A 1 498 ? -52.357 19.882 -13.536 1.00 33.01 ? 498 ASN A C 1 ATOM 3851 O O . ASN A 1 498 ? -53.571 19.741 -13.604 1.00 33.85 ? 498 ASN A O 1 ATOM 3852 C CB . ASN A 1 498 ? -50.991 17.785 -13.514 1.00 32.89 ? 498 ASN A CB 1 ATOM 3853 C CG . ASN A 1 498 ? -50.559 16.612 -14.360 1.00 34.64 ? 498 ASN A CG 1 ATOM 3854 O OD1 . ASN A 1 498 ? -50.978 16.490 -15.510 1.00 36.80 ? 498 ASN A OD1 1 ATOM 3855 N ND2 . ASN A 1 498 ? -49.724 15.739 -13.799 1.00 33.82 ? 498 ASN A ND2 1 ATOM 3856 N N . ARG A 1 499 ? -51.779 20.795 -12.757 1.00 32.11 ? 499 ARG A N 1 ATOM 3857 C CA . ARG A 1 499 ? -52.572 21.704 -11.916 1.00 33.88 ? 499 ARG A CA 1 ATOM 3858 C C . ARG A 1 499 ? -53.361 22.714 -12.706 1.00 37.33 ? 499 ARG A C 1 ATOM 3859 O O . ARG A 1 499 ? -54.552 22.922 -12.461 1.00 36.66 ? 499 ARG A O 1 ATOM 3860 C CB . ARG A 1 499 ? -51.670 22.483 -10.965 1.00 32.65 ? 499 ARG A CB 1 ATOM 3861 C CG . ARG A 1 499 ? -51.215 21.685 -9.778 1.00 30.74 ? 499 ARG A CG 1 ATOM 3862 C CD . ARG A 1 499 ? -50.321 22.517 -8.894 1.00 29.93 ? 499 ARG A CD 1 ATOM 3863 N NE . ARG A 1 499 ? -51.078 23.516 -8.146 1.00 29.07 ? 499 ARG A NE 1 ATOM 3864 C CZ . ARG A 1 499 ? -50.554 24.626 -7.634 1.00 30.65 ? 499 ARG A CZ 1 ATOM 3865 N NH1 . ARG A 1 499 ? -49.259 24.902 -7.772 1.00 30.20 ? 499 ARG A NH1 1 ATOM 3866 N NH2 . ARG A 1 499 ? -51.332 25.471 -6.970 1.00 31.85 ? 499 ARG A NH2 1 ATOM 3867 N N . PHE A 1 500 ? -52.679 23.366 -13.641 1.00 41.70 ? 500 PHE A N 1 ATOM 3868 C CA . PHE A 1 500 ? -53.259 24.487 -14.358 1.00 46.31 ? 500 PHE A CA 1 ATOM 3869 C C . PHE A 1 500 ? -53.619 24.119 -15.783 1.00 53.50 ? 500 PHE A C 1 ATOM 3870 O O . PHE A 1 500 ? -53.531 24.958 -16.672 1.00 56.73 ? 500 PHE A O 1 ATOM 3871 C CB . PHE A 1 500 ? -52.314 25.695 -14.309 1.00 46.46 ? 500 PHE A CB 1 ATOM 3872 C CG . PHE A 1 500 ? -51.915 26.086 -12.914 1.00 45.27 ? 500 PHE A CG 1 ATOM 3873 C CD1 . PHE A 1 500 ? -52.867 26.214 -11.917 1.00 45.40 ? 500 PHE A CD1 1 ATOM 3874 C CD2 . PHE A 1 500 ? -50.590 26.326 -12.598 1.00 46.49 ? 500 PHE A CD2 1 ATOM 3875 C CE1 . PHE A 1 500 ? -52.509 26.563 -10.623 1.00 46.88 ? 500 PHE A CE1 1 ATOM 3876 C CE2 . PHE A 1 500 ? -50.221 26.673 -11.302 1.00 46.24 ? 500 PHE A CE2 1 ATOM 3877 C CZ . PHE A 1 500 ? -51.181 26.799 -10.317 1.00 45.84 ? 500 PHE A CZ 1 ATOM 3878 N N . GLN A 1 501 ? -54.037 22.864 -15.981 1.00 59.43 ? 501 GLN A N 1 ATOM 3879 C CA . GLN A 1 501 ? -54.678 22.432 -17.226 1.00 65.98 ? 501 GLN A CA 1 ATOM 3880 C C . GLN A 1 501 ? -56.107 22.953 -17.246 1.00 72.75 ? 501 GLN A C 1 ATOM 3881 O O . GLN A 1 501 ? -56.716 23.134 -16.188 1.00 76.62 ? 501 GLN A O 1 ATOM 3882 C CB . GLN A 1 501 ? -54.698 20.898 -17.344 1.00 66.58 ? 501 GLN A CB 1 ATOM 3883 C CG . GLN A 1 501 ? -55.533 20.182 -16.283 1.00 67.48 ? 501 GLN A CG 1 ATOM 3884 C CD . GLN A 1 501 ? -55.525 18.671 -16.432 1.00 69.30 ? 501 GLN A CD 1 ATOM 3885 O OE1 . GLN A 1 501 ? -56.057 18.130 -17.403 1.00 71.22 ? 501 GLN A OE1 1 ATOM 3886 N NE2 . GLN A 1 501 ? -54.940 17.976 -15.454 1.00 67.16 ? 501 GLN A NE2 1 ATOM 3887 N N . ILE A 1 502 ? -56.643 23.185 -18.442 1.00 79.40 ? 502 ILE A N 1 ATOM 3888 C CA . ILE A 1 502 ? -58.038 23.610 -18.595 1.00 82.38 ? 502 ILE A CA 1 ATOM 3889 C C . ILE A 1 502 ? -58.891 22.414 -19.047 1.00 86.06 ? 502 ILE A C 1 ATOM 3890 O O . ILE A 1 502 ? -58.647 21.831 -20.107 1.00 89.50 ? 502 ILE A O 1 ATOM 3891 C CB . ILE A 1 502 ? -58.170 24.825 -19.555 1.00 83.18 ? 502 ILE A CB 1 ATOM 3892 C CG1 . ILE A 1 502 ? -59.624 25.309 -19.622 1.00 84.95 ? 502 ILE A CG1 1 ATOM 3893 C CG2 . ILE A 1 502 ? -57.635 24.501 -20.947 1.00 84.26 ? 502 ILE A CG2 1 ATOM 3894 C CD1 . ILE A 1 502 ? -59.778 26.729 -20.127 1.00 85.33 ? 502 ILE A CD1 1 ATOM 3895 N N . LYS A 1 503 ? -59.867 22.039 -18.218 1.00 85.84 ? 503 LYS A N 1 ATOM 3896 C CA . LYS A 1 503 ? -60.784 20.942 -18.530 1.00 87.18 ? 503 LYS A CA 1 ATOM 3897 C C . LYS A 1 503 ? -62.080 21.497 -19.111 1.00 89.59 ? 503 LYS A C 1 ATOM 3898 O O . LYS A 1 503 ? -62.552 21.045 -20.153 1.00 92.86 ? 503 LYS A O 1 ATOM 3899 C CB . LYS A 1 503 ? -61.098 20.119 -17.279 1.00 86.58 ? 503 LYS A CB 1 ATOM 3900 C CG . LYS A 1 503 ? -59.887 19.778 -16.424 1.00 84.75 ? 503 LYS A CG 1 ATOM 3901 C CD . LYS A 1 503 ? -60.219 18.666 -15.444 1.00 84.05 ? 503 LYS A CD 1 ATOM 3902 C CE . LYS A 1 503 ? -59.267 18.649 -14.260 1.00 82.16 ? 503 LYS A CE 1 ATOM 3903 N NZ . LYS A 1 503 ? -59.582 17.526 -13.337 1.00 81.05 ? 503 LYS A NZ 1 HETATM 3904 C C1 . NAG B 2 . ? -49.048 5.344 29.742 1.00 47.44 ? 1504 NAG A C1 1 HETATM 3905 C C2 . NAG B 2 . ? -48.275 4.068 29.413 1.00 54.71 ? 1504 NAG A C2 1 HETATM 3906 C C3 . NAG B 2 . ? -47.423 3.585 30.574 1.00 57.61 ? 1504 NAG A C3 1 HETATM 3907 C C4 . NAG B 2 . ? -46.481 4.714 30.977 1.00 57.30 ? 1504 NAG A C4 1 HETATM 3908 C C5 . NAG B 2 . ? -47.318 5.919 31.421 1.00 58.00 ? 1504 NAG A C5 1 HETATM 3909 C C6 . NAG B 2 . ? -46.435 7.116 31.759 1.00 56.74 ? 1504 NAG A C6 1 HETATM 3910 C C7 . NAG B 2 . ? -49.219 2.605 27.707 1.00 59.01 ? 1504 NAG A C7 1 HETATM 3911 C C8 . NAG B 2 . ? -50.166 1.483 27.401 1.00 60.10 ? 1504 NAG A C8 1 HETATM 3912 N N2 . NAG B 2 . ? -49.158 2.997 28.978 1.00 56.28 ? 1504 NAG A N2 1 HETATM 3913 O O3 . NAG B 2 . ? -46.708 2.436 30.167 1.00 58.83 ? 1504 NAG A O3 1 HETATM 3914 O O4 . NAG B 2 . ? -45.631 4.288 32.028 1.00 58.53 ? 1504 NAG A O4 1 HETATM 3915 O O5 . NAG B 2 . ? -48.247 6.326 30.424 1.00 51.06 ? 1504 NAG A O5 1 HETATM 3916 O O6 . NAG B 2 . ? -45.729 7.499 30.598 1.00 58.49 ? 1504 NAG A O6 1 HETATM 3917 O O7 . NAG B 2 . ? -48.557 3.118 26.807 1.00 58.12 ? 1504 NAG A O7 1 HETATM 3918 C C1 . NAG C 2 . ? -49.364 -5.230 76.374 1.00 44.34 ? 1505 NAG A C1 1 HETATM 3919 C C2 . NAG C 2 . ? -48.544 -6.512 76.404 1.00 50.06 ? 1505 NAG A C2 1 HETATM 3920 C C3 . NAG C 2 . ? -49.439 -7.729 76.167 1.00 52.48 ? 1505 NAG A C3 1 HETATM 3921 C C4 . NAG C 2 . ? -50.633 -7.689 77.111 1.00 54.75 ? 1505 NAG A C4 1 HETATM 3922 C C5 . NAG C 2 . ? -51.358 -6.363 76.871 1.00 52.02 ? 1505 NAG A C5 1 HETATM 3923 C C6 . NAG C 2 . ? -52.667 -6.209 77.634 1.00 51.18 ? 1505 NAG A C6 1 HETATM 3924 C C7 . NAG C 2 . ? -46.243 -6.223 75.629 1.00 52.14 ? 1505 NAG A C7 1 HETATM 3925 C C8 . NAG C 2 . ? -45.304 -6.221 74.458 1.00 55.19 ? 1505 NAG A C8 1 HETATM 3926 N N2 . NAG C 2 . ? -47.521 -6.468 75.370 1.00 49.92 ? 1505 NAG A N2 1 HETATM 3927 O O3 . NAG C 2 . ? -48.693 -8.912 76.329 1.00 55.84 ? 1505 NAG A O3 1 HETATM 3928 O O4 . NAG C 2 . ? -51.465 -8.806 76.870 1.00 59.21 ? 1505 NAG A O4 1 HETATM 3929 O O5 . NAG C 2 . ? -50.462 -5.333 77.255 1.00 46.07 ? 1505 NAG A O5 1 HETATM 3930 O O6 . NAG C 2 . ? -52.408 -6.221 79.016 1.00 51.57 ? 1505 NAG A O6 1 HETATM 3931 O O7 . NAG C 2 . ? -45.824 -6.003 76.761 1.00 56.97 ? 1505 NAG A O7 1 HETATM 3932 C C1 . NAG D 2 . ? -32.277 3.005 95.358 1.00 58.91 ? 1506 NAG A C1 1 HETATM 3933 C C2 . NAG D 2 . ? -31.631 1.707 94.840 1.00 68.79 ? 1506 NAG A C2 1 HETATM 3934 C C3 . NAG D 2 . ? -30.106 1.572 95.075 1.00 69.79 ? 1506 NAG A C3 1 HETATM 3935 C C4 . NAG D 2 . ? -29.539 2.377 96.253 1.00 68.25 ? 1506 NAG A C4 1 HETATM 3936 C C5 . NAG D 2 . ? -30.647 3.099 97.011 1.00 66.87 ? 1506 NAG A C5 1 HETATM 3937 C C6 . NAG D 2 . ? -30.124 4.055 98.077 1.00 65.34 ? 1506 NAG A C6 1 HETATM 3938 C C7 . NAG D 2 . ? -33.374 -0.058 94.770 1.00 79.05 ? 1506 NAG A C7 1 HETATM 3939 C C8 . NAG D 2 . ? -33.963 -1.250 95.473 1.00 78.08 ? 1506 NAG A C8 1 HETATM 3940 N N2 . NAG D 2 . ? -32.333 0.539 95.375 1.00 74.54 ? 1506 NAG A N2 1 HETATM 3941 O O3 . NAG D 2 . ? -29.405 1.945 93.907 1.00 71.32 ? 1506 NAG A O3 1 HETATM 3942 O O4 . NAG D 2 . ? -28.805 1.535 97.117 1.00 69.83 ? 1506 NAG A O4 1 HETATM 3943 O O5 . NAG D 2 . ? -31.369 3.830 96.045 1.00 66.26 ? 1506 NAG A O5 1 HETATM 3944 O O6 . NAG D 2 . ? -30.764 3.765 99.300 1.00 62.90 ? 1506 NAG A O6 1 HETATM 3945 O O7 . NAG D 2 . ? -33.861 0.311 93.700 1.00 83.89 ? 1506 NAG A O7 1 HETATM 3946 C C1 . NAG E 2 . ? -28.476 26.522 99.293 1.00 39.59 ? 1507 NAG A C1 1 HETATM 3947 C C2 . NAG E 2 . ? -27.977 27.622 100.221 1.00 42.73 ? 1507 NAG A C2 1 HETATM 3948 C C3 . NAG E 2 . ? -27.197 28.671 99.442 1.00 43.35 ? 1507 NAG A C3 1 HETATM 3949 C C4 . NAG E 2 . ? -26.111 28.028 98.599 1.00 41.92 ? 1507 NAG A C4 1 HETATM 3950 C C5 . NAG E 2 . ? -26.761 26.953 97.731 1.00 42.62 ? 1507 NAG A C5 1 HETATM 3951 C C6 . NAG E 2 . ? -25.769 26.234 96.830 1.00 43.46 ? 1507 NAG A C6 1 HETATM 3952 C C7 . NAG E 2 . ? -29.256 28.288 102.209 1.00 49.41 ? 1507 NAG A C7 1 HETATM 3953 C C8 . NAG E 2 . ? -30.460 29.020 102.729 1.00 47.80 ? 1507 NAG A C8 1 HETATM 3954 N N2 . NAG E 2 . ? -29.093 28.275 100.881 1.00 47.42 ? 1507 NAG A N2 1 HETATM 3955 O O3 . NAG E 2 . ? -26.628 29.631 100.303 1.00 45.91 ? 1507 NAG A O3 1 HETATM 3956 O O4 . NAG E 2 . ? -25.599 29.046 97.780 1.00 41.25 ? 1507 NAG A O4 1 HETATM 3957 O O5 . NAG E 2 . ? -27.399 25.991 98.551 1.00 41.06 ? 1507 NAG A O5 1 HETATM 3958 O O6 . NAG E 2 . ? -24.965 25.391 97.618 1.00 47.28 ? 1507 NAG A O6 1 HETATM 3959 O O7 . NAG E 2 . ? -28.480 27.736 102.991 1.00 50.18 ? 1507 NAG A O7 1 HETATM 3960 C C1 . NAG F 2 . ? -24.195 29.320 97.929 1.00 46.25 ? 1508 NAG A C1 1 HETATM 3961 C C2 . NAG F 2 . ? -23.762 30.047 96.663 1.00 43.99 ? 1508 NAG A C2 1 HETATM 3962 C C3 . NAG F 2 . ? -22.311 30.514 96.720 1.00 46.92 ? 1508 NAG A C3 1 HETATM 3963 C C4 . NAG F 2 . ? -21.968 31.213 98.036 1.00 53.02 ? 1508 NAG A C4 1 HETATM 3964 C C5 . NAG F 2 . ? -22.492 30.373 99.202 1.00 52.66 ? 1508 NAG A C5 1 HETATM 3965 C C6 . NAG F 2 . ? -22.213 31.070 100.530 1.00 54.95 ? 1508 NAG A C6 1 HETATM 3966 C C7 . NAG F 2 . ? -24.941 29.320 94.613 1.00 41.83 ? 1508 NAG A C7 1 HETATM 3967 C C8 . NAG F 2 . ? -24.916 28.345 93.467 1.00 39.54 ? 1508 NAG A C8 1 HETATM 3968 N N2 . NAG F 2 . ? -23.935 29.203 95.488 1.00 43.89 ? 1508 NAG A N2 1 HETATM 3969 O O3 . NAG F 2 . ? -22.120 31.402 95.648 1.00 41.97 ? 1508 NAG A O3 1 HETATM 3970 O O4 . NAG F 2 . ? -20.558 31.400 98.162 1.00 61.55 ? 1508 NAG A O4 1 HETATM 3971 O O5 . NAG F 2 . ? -23.887 30.124 99.063 1.00 48.16 ? 1508 NAG A O5 1 HETATM 3972 O O6 . NAG F 2 . ? -23.042 30.527 101.534 1.00 54.81 ? 1508 NAG A O6 1 HETATM 3973 O O7 . NAG F 2 . ? -25.848 30.155 94.707 1.00 40.00 ? 1508 NAG A O7 1 HETATM 3974 C C1 . MAN G 3 . ? -20.063 32.759 98.038 1.00 69.38 ? 1509 MAN A C1 1 HETATM 3975 C C2 . MAN G 3 . ? -19.241 32.941 96.759 1.00 73.79 ? 1509 MAN A C2 1 HETATM 3976 C C3 . MAN G 3 . ? -19.006 34.435 96.514 1.00 77.04 ? 1509 MAN A C3 1 HETATM 3977 C C4 . MAN G 3 . ? -18.857 35.177 97.838 1.00 76.47 ? 1509 MAN A C4 1 HETATM 3978 C C5 . MAN G 3 . ? -18.296 34.223 98.897 1.00 75.51 ? 1509 MAN A C5 1 HETATM 3979 C C6 . MAN G 3 . ? -17.979 34.932 100.213 1.00 75.82 ? 1509 MAN A C6 1 HETATM 3980 O O2 . MAN G 3 . ? -19.867 32.344 95.619 1.00 73.07 ? 1509 MAN A O2 1 HETATM 3981 O O3 . MAN G 3 . ? -20.082 35.025 95.768 1.00 78.17 ? 1509 MAN A O3 1 HETATM 3982 O O4 . MAN G 3 . ? -18.013 36.314 97.626 1.00 78.52 ? 1509 MAN A O4 1 HETATM 3983 O O5 . MAN G 3 . ? -19.221 33.141 99.142 1.00 73.54 ? 1509 MAN A O5 1 HETATM 3984 O O6 . MAN G 3 . ? -17.217 34.047 101.043 1.00 74.23 ? 1509 MAN A O6 1 HETATM 3985 C C1 . NAG H 2 . ? -56.244 6.578 56.750 1.00 37.55 ? 1510 NAG A C1 1 HETATM 3986 C C2 . NAG H 2 . ? -57.387 6.236 55.772 1.00 42.40 ? 1510 NAG A C2 1 HETATM 3987 C C3 . NAG H 2 . ? -58.522 7.252 55.884 1.00 46.27 ? 1510 NAG A C3 1 HETATM 3988 C C4 . NAG H 2 . ? -58.862 7.524 57.345 1.00 49.16 ? 1510 NAG A C4 1 HETATM 3989 C C5 . NAG H 2 . ? -57.589 7.878 58.133 1.00 49.58 ? 1510 NAG A C5 1 HETATM 3990 C C6 . NAG H 2 . ? -57.860 8.206 59.597 1.00 49.43 ? 1510 NAG A C6 1 HETATM 3991 C C7 . NAG H 2 . ? -56.632 4.970 53.783 1.00 42.47 ? 1510 NAG A C7 1 HETATM 3992 C C8 . NAG H 2 . ? -56.214 4.969 52.335 1.00 40.59 ? 1510 NAG A C8 1 HETATM 3993 N N2 . NAG H 2 . ? -56.957 6.147 54.364 1.00 40.18 ? 1510 NAG A N2 1 HETATM 3994 O O3 . NAG H 2 . ? -59.662 6.805 55.170 1.00 49.87 ? 1510 NAG A O3 1 HETATM 3995 O O4 . NAG H 2 . ? -59.763 8.611 57.359 1.00 52.76 ? 1510 NAG A O4 1 HETATM 3996 O O5 . NAG H 2 . ? -56.677 6.788 58.070 1.00 42.84 ? 1510 NAG A O5 1 HETATM 3997 O O6 . NAG H 2 . ? -58.327 7.044 60.229 1.00 52.56 ? 1510 NAG A O6 1 HETATM 3998 O O7 . NAG H 2 . ? -56.623 3.893 54.392 1.00 42.76 ? 1510 NAG A O7 1 HETATM 3999 C C1 . NAG I 2 . ? -35.027 25.654 100.947 1.00 45.78 ? 1511 NAG A C1 1 HETATM 4000 C C2 . NAG I 2 . ? -36.362 25.525 101.681 1.00 47.33 ? 1511 NAG A C2 1 HETATM 4001 C C3 . NAG I 2 . ? -36.358 26.355 102.964 1.00 50.37 ? 1511 NAG A C3 1 HETATM 4002 C C4 . NAG I 2 . ? -35.118 26.056 103.793 1.00 50.23 ? 1511 NAG A C4 1 HETATM 4003 C C5 . NAG I 2 . ? -33.863 26.154 102.929 1.00 49.47 ? 1511 NAG A C5 1 HETATM 4004 C C6 . NAG I 2 . ? -32.612 25.746 103.686 1.00 48.72 ? 1511 NAG A C6 1 HETATM 4005 C C7 . NAG I 2 . ? -38.453 25.328 100.416 1.00 50.16 ? 1511 NAG A C7 1 HETATM 4006 C C8 . NAG I 2 . ? -39.435 26.063 99.553 1.00 51.99 ? 1511 NAG A C8 1 HETATM 4007 N N2 . NAG I 2 . ? -37.419 26.044 100.840 1.00 47.91 ? 1511 NAG A N2 1 HETATM 4008 O O3 . NAG I 2 . ? -37.544 26.122 103.702 1.00 46.77 ? 1511 NAG A O3 1 HETATM 4009 O O4 . NAG I 2 . ? -35.037 26.981 104.861 1.00 58.56 ? 1511 NAG A O4 1 HETATM 4010 O O5 . NAG I 2 . ? -33.964 25.298 101.802 1.00 46.98 ? 1511 NAG A O5 1 HETATM 4011 O O6 . NAG I 2 . ? -31.529 25.923 102.801 1.00 47.74 ? 1511 NAG A O6 1 HETATM 4012 O O7 . NAG I 2 . ? -38.623 24.141 100.685 1.00 52.35 ? 1511 NAG A O7 1 HETATM 4013 C C1 . NAG J 2 . ? -35.218 26.339 106.146 1.00 59.05 ? 1512 NAG A C1 1 HETATM 4014 C C2 . NAG J 2 . ? -34.776 27.341 107.213 1.00 57.83 ? 1512 NAG A C2 1 HETATM 4015 C C3 . NAG J 2 . ? -35.083 26.812 108.614 1.00 60.07 ? 1512 NAG A C3 1 HETATM 4016 C C4 . NAG J 2 . ? -36.547 26.388 108.698 1.00 62.21 ? 1512 NAG A C4 1 HETATM 4017 C C5 . NAG J 2 . ? -36.807 25.333 107.616 1.00 63.85 ? 1512 NAG A C5 1 HETATM 4018 C C6 . NAG J 2 . ? -38.213 24.727 107.658 1.00 62.88 ? 1512 NAG A C6 1 HETATM 4019 C C7 . NAG J 2 . ? -32.898 28.885 106.760 1.00 53.55 ? 1512 NAG A C7 1 HETATM 4020 C C8 . NAG J 2 . ? -31.412 29.050 106.641 1.00 52.01 ? 1512 NAG A C8 1 HETATM 4021 N N2 . NAG J 2 . ? -33.358 27.662 107.056 1.00 56.39 ? 1512 NAG A N2 1 HETATM 4022 O O3 . NAG J 2 . ? -34.816 27.806 109.575 1.00 56.36 ? 1512 NAG A O3 1 HETATM 4023 O O4 . NAG J 2 . ? -36.834 25.907 109.997 1.00 65.97 ? 1512 NAG A O4 1 HETATM 4024 O O5 . NAG J 2 . ? -36.566 25.923 106.348 1.00 60.55 ? 1512 NAG A O5 1 HETATM 4025 O O6 . NAG J 2 . ? -39.193 25.682 107.311 1.00 61.88 ? 1512 NAG A O6 1 HETATM 4026 O O7 . NAG J 2 . ? -33.619 29.866 106.587 1.00 54.48 ? 1512 NAG A O7 1 HETATM 4027 N N1 . EPE K 4 . ? -35.441 -0.055 88.996 1.00 70.98 ? 1513 EPE A N1 1 HETATM 4028 C C2 . EPE K 4 . ? -35.513 -0.696 90.314 1.00 67.82 ? 1513 EPE A C2 1 HETATM 4029 C C3 . EPE K 4 . ? -36.538 0.096 91.105 1.00 65.59 ? 1513 EPE A C3 1 HETATM 4030 N N4 . EPE K 4 . ? -36.264 1.563 91.134 1.00 60.59 ? 1513 EPE A N4 1 HETATM 4031 C C5 . EPE K 4 . ? -35.199 2.101 90.238 1.00 62.43 ? 1513 EPE A C5 1 HETATM 4032 C C6 . EPE K 4 . ? -34.657 1.178 89.142 1.00 66.70 ? 1513 EPE A C6 1 HETATM 4033 C C7 . EPE K 4 . ? -37.526 2.341 91.001 1.00 53.31 ? 1513 EPE A C7 1 HETATM 4034 C C8 . EPE K 4 . ? -37.631 3.343 92.136 1.00 48.37 ? 1513 EPE A C8 1 HETATM 4035 O O8 . EPE K 4 . ? -37.810 4.668 91.626 1.00 34.92 ? 1513 EPE A O8 1 HETATM 4036 C C9 . EPE K 4 . ? -34.814 -0.961 88.024 1.00 77.16 ? 1513 EPE A C9 1 HETATM 4037 C C10 . EPE K 4 . ? -35.312 -0.648 86.620 1.00 80.52 ? 1513 EPE A C10 1 HETATM 4038 S S . EPE K 4 . ? -34.327 -1.401 85.511 1.00 89.92 ? 1513 EPE A S 1 HETATM 4039 O O1S . EPE K 4 . ? -35.024 -1.520 84.259 1.00 92.70 ? 1513 EPE A O1S 1 HETATM 4040 O O2S . EPE K 4 . ? -33.973 -2.716 85.981 1.00 90.21 ? 1513 EPE A O2S 1 HETATM 4041 O O3S . EPE K 4 . ? -32.971 -0.510 85.283 1.00 87.78 ? 1513 EPE A O3S 1 HETATM 4042 N N1 . EPE L 4 . ? -25.349 4.898 79.711 1.00 59.99 ? 1514 EPE A N1 1 HETATM 4043 C C2 . EPE L 4 . ? -26.470 5.658 79.107 1.00 58.38 ? 1514 EPE A C2 1 HETATM 4044 C C3 . EPE L 4 . ? -26.813 5.140 77.710 1.00 56.27 ? 1514 EPE A C3 1 HETATM 4045 N N4 . EPE L 4 . ? -25.684 5.273 76.757 1.00 57.64 ? 1514 EPE A N4 1 HETATM 4046 C C5 . EPE L 4 . ? -24.367 5.413 77.445 1.00 57.73 ? 1514 EPE A C5 1 HETATM 4047 C C6 . EPE L 4 . ? -24.251 4.611 78.744 1.00 58.38 ? 1514 EPE A C6 1 HETATM 4048 C C7 . EPE L 4 . ? -25.701 4.184 75.744 1.00 53.02 ? 1514 EPE A C7 1 HETATM 4049 C C8 . EPE L 4 . ? -26.322 4.600 74.417 1.00 50.62 ? 1514 EPE A C8 1 HETATM 4050 O O8 . EPE L 4 . ? -27.721 4.854 74.581 1.00 49.33 ? 1514 EPE A O8 1 HETATM 4051 C C9 . EPE L 4 . ? -24.845 5.570 80.937 1.00 60.33 ? 1514 EPE A C9 1 HETATM 4052 C C10 . EPE L 4 . ? -25.847 5.401 82.076 1.00 60.95 ? 1514 EPE A C10 1 HETATM 4053 S S . EPE L 4 . ? -25.226 5.747 83.601 1.00 64.34 ? 1514 EPE A S 1 HETATM 4054 O O1S . EPE L 4 . ? -24.058 6.590 83.562 1.00 60.69 ? 1514 EPE A O1S 1 HETATM 4055 O O2S . EPE L 4 . ? -24.898 4.501 84.239 1.00 61.94 ? 1514 EPE A O2S 1 HETATM 4056 O O3S . EPE L 4 . ? -26.403 6.510 84.424 1.00 53.81 ? 1514 EPE A O3S 1 HETATM 4057 C C1 . SIA M 5 . ? -48.680 2.097 98.131 1.00 38.23 ? 1515 SIA A C1 1 HETATM 4058 C C2 . SIA M 5 . ? -48.824 2.308 99.633 1.00 38.04 ? 1515 SIA A C2 1 HETATM 4059 C C3 . SIA M 5 . ? -47.618 1.749 100.385 1.00 39.12 ? 1515 SIA A C3 1 HETATM 4060 C C4 . SIA M 5 . ? -46.381 2.576 100.065 1.00 38.50 ? 1515 SIA A C4 1 HETATM 4061 C C5 . SIA M 5 . ? -46.591 4.046 100.404 1.00 39.36 ? 1515 SIA A C5 1 HETATM 4062 C C6 . SIA M 5 . ? -47.840 4.543 99.686 1.00 37.66 ? 1515 SIA A C6 1 HETATM 4063 C C7 . SIA M 5 . ? -48.313 5.940 100.042 1.00 39.01 ? 1515 SIA A C7 1 HETATM 4064 C C8 . SIA M 5 . ? -49.626 6.219 99.280 1.00 39.19 ? 1515 SIA A C8 1 HETATM 4065 C C9 . SIA M 5 . ? -50.005 7.691 99.216 1.00 39.05 ? 1515 SIA A C9 1 HETATM 4066 C C10 . SIA M 5 . ? -44.472 5.279 100.514 1.00 40.12 ? 1515 SIA A C10 1 HETATM 4067 C C11 . SIA M 5 . ? -43.347 5.864 99.724 1.00 38.02 ? 1515 SIA A C11 1 HETATM 4068 N N5 . SIA M 5 . ? -45.430 4.690 99.804 1.00 37.37 ? 1515 SIA A N5 1 HETATM 4069 O O1A . SIA M 5 . ? -48.858 3.052 97.331 1.00 36.92 ? 1515 SIA A O1A 1 HETATM 4070 O O1B . SIA M 5 . ? -48.406 0.948 97.743 1.00 38.96 ? 1515 SIA A O1B 1 HETATM 4071 O O4 . SIA M 5 . ? -45.232 2.052 100.733 1.00 42.18 ? 1515 SIA A O4 1 HETATM 4072 O O6 . SIA M 5 . ? -48.956 3.691 99.963 1.00 38.12 ? 1515 SIA A O6 1 HETATM 4073 O O7 . SIA M 5 . ? -48.500 6.022 101.460 1.00 40.41 ? 1515 SIA A O7 1 HETATM 4074 O O8 . SIA M 5 . ? -49.544 5.709 97.938 1.00 38.34 ? 1515 SIA A O8 1 HETATM 4075 O O9 . SIA M 5 . ? -51.316 7.784 98.624 1.00 41.57 ? 1515 SIA A O9 1 HETATM 4076 O O10 . SIA M 5 . ? -44.514 5.362 101.730 1.00 41.11 ? 1515 SIA A O10 1 HETATM 4077 C C1 . GAL N 6 . ? -53.281 2.837 102.291 1.00 43.60 ? 1516 GAL A C1 1 HETATM 4078 C C2 . GAL N 6 . ? -54.662 2.960 101.663 1.00 42.82 ? 1516 GAL A C2 1 HETATM 4079 C C3 . GAL N 6 . ? -54.834 1.871 100.604 1.00 41.53 ? 1516 GAL A C3 1 HETATM 4080 C C4 . GAL N 6 . ? -53.699 1.948 99.582 1.00 42.05 ? 1516 GAL A C4 1 HETATM 4081 C C5 . GAL N 6 . ? -52.369 1.843 100.318 1.00 40.36 ? 1516 GAL A C5 1 HETATM 4082 C C6 . GAL N 6 . ? -51.186 1.900 99.363 1.00 39.50 ? 1516 GAL A C6 1 HETATM 4083 O O2 . GAL N 6 . ? -55.663 2.877 102.689 1.00 43.93 ? 1516 GAL A O2 1 HETATM 4084 O O3 . GAL N 6 . ? -56.071 2.027 99.921 1.00 39.54 ? 1516 GAL A O3 1 HETATM 4085 O O4 . GAL N 6 . ? -53.772 3.190 98.844 1.00 40.44 ? 1516 GAL A O4 1 HETATM 4086 O O5 . GAL N 6 . ? -52.273 2.915 101.263 1.00 41.98 ? 1516 GAL A O5 1 HETATM 4087 O O6 . GAL N 6 . ? -49.990 1.628 100.099 1.00 38.76 ? 1516 GAL A O6 1 HETATM 4088 C C1 . NAG O 2 . ? -50.421 4.754 106.262 1.00 46.60 ? 1517 NAG A C1 1 HETATM 4089 C C2 . NAG O 2 . ? -49.773 4.364 104.929 1.00 46.44 ? 1517 NAG A C2 1 HETATM 4090 C C3 . NAG O 2 . ? -50.800 4.473 103.798 1.00 45.92 ? 1517 NAG A C3 1 HETATM 4091 C C4 . NAG O 2 . ? -52.037 3.654 104.171 1.00 45.87 ? 1517 NAG A C4 1 HETATM 4092 C C5 . NAG O 2 . ? -52.545 3.968 105.592 1.00 47.57 ? 1517 NAG A C5 1 HETATM 4093 C C6 . NAG O 2 . ? -53.665 3.018 106.011 1.00 48.45 ? 1517 NAG A C6 1 HETATM 4094 C C7 . NAG O 2 . ? -47.400 4.947 104.691 1.00 46.26 ? 1517 NAG A C7 1 HETATM 4095 C C8 . NAG O 2 . ? -46.399 6.051 104.495 1.00 44.69 ? 1517 NAG A C8 1 HETATM 4096 N N2 . NAG O 2 . ? -48.685 5.323 104.729 1.00 43.81 ? 1517 NAG A N2 1 HETATM 4097 O O1 . NAG O 2 . ? -49.461 4.668 107.314 1.00 49.68 ? 1517 NAG A O1 1 HETATM 4098 O O3 . NAG O 2 . ? -50.258 3.979 102.559 1.00 44.70 ? 1517 NAG A O3 1 HETATM 4099 O O4 . NAG O 2 . ? -53.106 3.887 103.249 1.00 43.19 ? 1517 NAG A O4 1 HETATM 4100 O O5 . NAG O 2 . ? -51.479 3.847 106.532 1.00 45.32 ? 1517 NAG A O5 1 HETATM 4101 O O6 . NAG O 2 . ? -53.227 1.657 105.841 1.00 49.31 ? 1517 NAG A O6 1 HETATM 4102 O O7 . NAG O 2 . ? -47.038 3.784 104.794 1.00 45.02 ? 1517 NAG A O7 1 HETATM 4103 C C . TAM P 7 . ? -42.684 21.882 40.301 1.00 64.05 ? 1518 TAM A C 1 HETATM 4104 C C1 . TAM P 7 . ? -42.945 23.206 39.577 1.00 62.77 ? 1518 TAM A C1 1 HETATM 4105 C C2 . TAM P 7 . ? -43.933 21.434 41.059 1.00 64.18 ? 1518 TAM A C2 1 HETATM 4106 C C3 . TAM P 7 . ? -41.456 22.037 41.209 1.00 64.10 ? 1518 TAM A C3 1 HETATM 4107 C C4 . TAM P 7 . ? -43.836 23.108 38.341 1.00 62.68 ? 1518 TAM A C4 1 HETATM 4108 C C5 . TAM P 7 . ? -43.789 20.122 41.830 1.00 64.25 ? 1518 TAM A C5 1 HETATM 4109 C C6 . TAM P 7 . ? -41.755 22.743 42.529 1.00 63.92 ? 1518 TAM A C6 1 HETATM 4110 N N . TAM P 7 . ? -42.379 20.851 39.313 1.00 64.67 ? 1518 TAM A N 1 HETATM 4111 O O4 . TAM P 7 . ? -43.181 23.737 37.230 1.00 65.97 ? 1518 TAM A O4 1 HETATM 4112 O O5 . TAM P 7 . ? -44.693 20.108 42.943 1.00 63.41 ? 1518 TAM A O5 1 HETATM 4113 O O6 . TAM P 7 . ? -40.555 23.321 43.048 1.00 67.37 ? 1518 TAM A O6 1 HETATM 4114 O O . HOH Q 8 . ? -55.551 12.344 -11.294 1.00 64.13 ? 2001 HOH A O 1 HETATM 4115 O O . HOH Q 8 . ? -48.618 13.203 -14.138 1.00 36.19 ? 2002 HOH A O 1 HETATM 4116 O O . HOH Q 8 . ? -51.761 12.023 -17.068 1.00 58.22 ? 2003 HOH A O 1 HETATM 4117 O O . HOH Q 8 . ? -52.704 7.687 -7.040 1.00 48.03 ? 2004 HOH A O 1 HETATM 4118 O O . HOH Q 8 . ? -48.305 8.032 -8.529 1.00 28.76 ? 2005 HOH A O 1 HETATM 4119 O O . HOH Q 8 . ? -54.385 9.264 -5.060 1.00 44.62 ? 2006 HOH A O 1 HETATM 4120 O O . HOH Q 8 . ? -57.166 10.706 -2.272 1.00 42.95 ? 2007 HOH A O 1 HETATM 4121 O O . HOH Q 8 . ? -55.443 13.387 -4.542 1.00 50.38 ? 2008 HOH A O 1 HETATM 4122 O O . HOH Q 8 . ? -58.895 16.437 15.908 1.00 32.49 ? 2009 HOH A O 1 HETATM 4123 O O . HOH Q 8 . ? -64.459 5.091 18.743 1.00 58.90 ? 2010 HOH A O 1 HETATM 4124 O O . HOH Q 8 . ? -54.846 11.088 11.648 1.00 23.56 ? 2011 HOH A O 1 HETATM 4125 O O . HOH Q 8 . ? -56.093 10.519 18.387 1.00 20.42 ? 2012 HOH A O 1 HETATM 4126 O O . HOH Q 8 . ? -56.687 15.216 14.908 1.00 42.79 ? 2013 HOH A O 1 HETATM 4127 O O . HOH Q 8 . ? -61.953 16.793 36.871 1.00 45.89 ? 2014 HOH A O 1 HETATM 4128 O O . HOH Q 8 . ? -57.382 17.150 36.914 1.00 37.99 ? 2015 HOH A O 1 HETATM 4129 O O . HOH Q 8 . ? -49.363 4.014 18.205 1.00 40.36 ? 2016 HOH A O 1 HETATM 4130 O O . HOH Q 8 . ? -50.289 10.028 22.273 1.00 21.37 ? 2017 HOH A O 1 HETATM 4131 O O . HOH Q 8 . ? -53.027 2.622 18.159 1.00 52.04 ? 2018 HOH A O 1 HETATM 4132 O O . HOH Q 8 . ? -61.994 4.536 21.376 1.00 60.54 ? 2019 HOH A O 1 HETATM 4133 O O . HOH Q 8 . ? -63.628 16.426 24.098 1.00 51.56 ? 2020 HOH A O 1 HETATM 4134 O O . HOH Q 8 . ? -61.272 5.186 24.086 1.00 42.00 ? 2021 HOH A O 1 HETATM 4135 O O . HOH Q 8 . ? -52.959 2.043 28.157 1.00 61.96 ? 2022 HOH A O 1 HETATM 4136 O O . HOH Q 8 . ? -44.185 6.881 26.106 1.00 54.72 ? 2023 HOH A O 1 HETATM 4137 O O . HOH Q 8 . ? -55.696 5.266 28.180 1.00 39.64 ? 2024 HOH A O 1 HETATM 4138 O O . HOH Q 8 . ? -61.364 7.922 31.646 1.00 32.89 ? 2025 HOH A O 1 HETATM 4139 O O . HOH Q 8 . ? -62.025 15.219 33.632 1.00 41.66 ? 2026 HOH A O 1 HETATM 4140 O O . HOH Q 8 . ? -57.089 15.586 34.771 1.00 15.91 ? 2027 HOH A O 1 HETATM 4141 O O . HOH Q 8 . ? -37.129 -1.561 63.682 1.00 35.02 ? 2028 HOH A O 1 HETATM 4142 O O . HOH Q 8 . ? -61.321 22.970 33.024 1.00 36.76 ? 2029 HOH A O 1 HETATM 4143 O O . HOH Q 8 . ? -58.056 20.681 25.826 1.00 24.54 ? 2030 HOH A O 1 HETATM 4144 O O . HOH Q 8 . ? -30.187 8.704 66.184 1.00 24.08 ? 2031 HOH A O 1 HETATM 4145 O O . HOH Q 8 . ? -65.836 24.293 28.188 1.00 50.80 ? 2032 HOH A O 1 HETATM 4146 O O . HOH Q 8 . ? -40.626 -2.827 65.959 1.00 49.52 ? 2033 HOH A O 1 HETATM 4147 O O . HOH Q 8 . ? -38.745 -0.932 73.418 1.00 65.73 ? 2034 HOH A O 1 HETATM 4148 O O . HOH Q 8 . ? -38.745 -0.932 73.418 1.00 65.73 ? 2035 HOH A O 1 HETATM 4149 O O . HOH Q 8 . ? -48.313 -4.330 65.695 1.00 42.22 ? 2036 HOH A O 1 HETATM 4150 O O . HOH Q 8 . ? -59.749 20.644 22.791 1.00 53.84 ? 2037 HOH A O 1 HETATM 4151 O O . HOH Q 8 . ? -65.353 21.861 29.443 1.00 51.15 ? 2038 HOH A O 1 HETATM 4152 O O . HOH Q 8 . ? -65.219 19.037 28.664 1.00 44.11 ? 2039 HOH A O 1 HETATM 4153 O O . HOH Q 8 . ? -67.592 23.825 33.415 1.00 35.30 ? 2040 HOH A O 1 HETATM 4154 O O . HOH Q 8 . ? -62.535 13.951 24.069 1.00 28.49 ? 2041 HOH A O 1 HETATM 4155 O O . HOH Q 8 . ? -60.251 13.554 22.282 1.00 32.95 ? 2042 HOH A O 1 HETATM 4156 O O . HOH Q 8 . ? -51.744 4.037 25.409 1.00 52.74 ? 2043 HOH A O 1 HETATM 4157 O O . HOH Q 8 . ? -50.102 6.949 24.308 1.00 41.05 ? 2044 HOH A O 1 HETATM 4158 O O . HOH Q 8 . ? -29.156 9.831 62.469 1.00 40.78 ? 2045 HOH A O 1 HETATM 4159 O O . HOH Q 8 . ? -50.977 4.826 32.029 1.00 48.48 ? 2046 HOH A O 1 HETATM 4160 O O . HOH Q 8 . ? -48.268 7.570 26.528 1.00 39.10 ? 2047 HOH A O 1 HETATM 4161 O O . HOH Q 8 . ? -49.573 5.292 34.186 1.00 53.41 ? 2048 HOH A O 1 HETATM 4162 O O . HOH Q 8 . ? -50.947 -2.003 68.353 1.00 44.49 ? 2049 HOH A O 1 HETATM 4163 O O . HOH Q 8 . ? -51.632 5.715 36.808 1.00 27.23 ? 2050 HOH A O 1 HETATM 4164 O O . HOH Q 8 . ? -48.304 7.916 38.237 1.00 33.16 ? 2051 HOH A O 1 HETATM 4165 O O . HOH Q 8 . ? -56.277 6.654 39.110 1.00 35.85 ? 2052 HOH A O 1 HETATM 4166 O O . HOH Q 8 . ? -55.677 8.195 43.288 1.00 20.20 ? 2053 HOH A O 1 HETATM 4167 O O . HOH Q 8 . ? -53.618 7.448 85.602 1.00 45.94 ? 2054 HOH A O 1 HETATM 4168 O O . HOH Q 8 . ? -52.827 5.349 44.268 1.00 29.34 ? 2055 HOH A O 1 HETATM 4169 O O . HOH Q 8 . ? -49.387 2.713 44.517 1.00 36.55 ? 2056 HOH A O 1 HETATM 4170 O O . HOH Q 8 . ? -47.001 3.790 43.556 1.00 43.22 ? 2057 HOH A O 1 HETATM 4171 O O . HOH Q 8 . ? -46.820 8.006 45.463 1.00 24.11 ? 2058 HOH A O 1 HETATM 4172 O O . HOH Q 8 . ? -45.322 23.181 84.026 1.00 42.95 ? 2059 HOH A O 1 HETATM 4173 O O . HOH Q 8 . ? -52.687 17.341 75.204 1.00 33.98 ? 2060 HOH A O 1 HETATM 4174 O O . HOH Q 8 . ? -56.930 7.062 50.165 1.00 50.25 ? 2061 HOH A O 1 HETATM 4175 O O . HOH Q 8 . ? -56.695 3.607 45.734 1.00 53.60 ? 2062 HOH A O 1 HETATM 4176 O O . HOH Q 8 . ? -50.886 15.151 74.105 1.00 27.97 ? 2063 HOH A O 1 HETATM 4177 O O . HOH Q 8 . ? -51.781 17.856 70.857 1.00 20.89 ? 2064 HOH A O 1 HETATM 4178 O O . HOH Q 8 . ? -49.995 1.102 48.340 1.00 40.45 ? 2065 HOH A O 1 HETATM 4179 O O . HOH Q 8 . ? -38.378 20.980 70.654 1.00 21.99 ? 2066 HOH A O 1 HETATM 4180 O O . HOH Q 8 . ? -55.009 1.310 50.766 1.00 42.52 ? 2067 HOH A O 1 HETATM 4181 O O . HOH Q 8 . ? -54.643 -1.130 49.422 1.00 59.28 ? 2068 HOH A O 1 HETATM 4182 O O . HOH Q 8 . ? -34.168 20.988 68.782 1.00 62.76 ? 2069 HOH A O 1 HETATM 4183 O O . HOH Q 8 . ? -34.168 20.988 68.782 1.00 62.76 ? 2070 HOH A O 1 HETATM 4184 O O . HOH Q 8 . ? -48.163 1.235 50.635 1.00 38.90 ? 2071 HOH A O 1 HETATM 4185 O O . HOH Q 8 . ? -52.980 -0.245 59.256 1.00 53.70 ? 2072 HOH A O 1 HETATM 4186 O O . HOH Q 8 . ? -41.587 3.218 56.214 1.00 21.56 ? 2073 HOH A O 1 HETATM 4187 O O . HOH Q 8 . ? -38.550 3.196 58.488 1.00 20.01 ? 2074 HOH A O 1 HETATM 4188 O O . HOH Q 8 . ? -36.472 0.591 62.386 1.00 17.17 ? 2075 HOH A O 1 HETATM 4189 O O . HOH Q 8 . ? -36.130 -4.381 56.898 1.00 36.62 ? 2076 HOH A O 1 HETATM 4190 O O . HOH Q 8 . ? -39.437 -4.934 61.999 1.00 33.24 ? 2077 HOH A O 1 HETATM 4191 O O . HOH Q 8 . ? -35.688 -5.362 60.382 1.00 43.19 ? 2078 HOH A O 1 HETATM 4192 O O . HOH Q 8 . ? -35.688 -3.513 61.952 1.00 54.94 ? 2079 HOH A O 1 HETATM 4193 O O . HOH Q 8 . ? -32.000 3.667 59.961 1.00 20.71 ? 2080 HOH A O 1 HETATM 4194 O O . HOH Q 8 . ? -34.220 8.697 58.805 1.00 26.14 ? 2081 HOH A O 1 HETATM 4195 O O . HOH Q 8 . ? -37.657 9.979 53.772 1.00 20.42 ? 2082 HOH A O 1 HETATM 4196 O O . HOH Q 8 . ? -32.275 7.583 64.627 1.00 22.38 ? 2083 HOH A O 1 HETATM 4197 O O . HOH Q 8 . ? -29.852 6.059 66.501 1.00 24.54 ? 2084 HOH A O 1 HETATM 4198 O O . HOH Q 8 . ? -33.431 0.238 66.087 1.00 19.88 ? 2085 HOH A O 1 HETATM 4199 O O . HOH Q 8 . ? -34.824 2.169 68.903 1.00 31.71 ? 2086 HOH A O 1 HETATM 4200 O O . HOH Q 8 . ? -36.048 0.621 67.206 1.00 35.99 ? 2087 HOH A O 1 HETATM 4201 O O . HOH Q 8 . ? -39.580 -1.046 68.213 1.00 27.18 ? 2088 HOH A O 1 HETATM 4202 O O . HOH Q 8 . ? -40.947 -2.112 70.796 1.00 31.72 ? 2089 HOH A O 1 HETATM 4203 O O . HOH Q 8 . ? -47.073 -3.373 68.210 1.00 37.25 ? 2090 HOH A O 1 HETATM 4204 O O . HOH Q 8 . ? -43.114 -3.799 66.632 1.00 33.12 ? 2091 HOH A O 1 HETATM 4205 O O . HOH Q 8 . ? -47.569 2.794 72.239 1.00 22.47 ? 2092 HOH A O 1 HETATM 4206 O O . HOH Q 8 . ? -42.462 -4.675 69.046 1.00 44.78 ? 2093 HOH A O 1 HETATM 4207 O O . HOH Q 8 . ? -46.804 -4.323 70.852 1.00 51.91 ? 2094 HOH A O 1 HETATM 4208 O O . HOH Q 8 . ? -45.016 -2.380 76.032 1.00 38.14 ? 2095 HOH A O 1 HETATM 4209 O O . HOH Q 8 . ? -48.517 3.942 78.302 1.00 33.91 ? 2096 HOH A O 1 HETATM 4210 O O . HOH Q 8 . ? -47.200 -4.062 78.555 1.00 47.48 ? 2097 HOH A O 1 HETATM 4211 O O . HOH Q 8 . ? -48.507 8.980 79.083 1.00 26.58 ? 2098 HOH A O 1 HETATM 4212 O O . HOH Q 8 . ? -46.353 10.465 75.329 1.00 18.83 ? 2099 HOH A O 1 HETATM 4213 O O . HOH Q 8 . ? -19.672 25.706 79.785 1.00 48.05 ? 2100 HOH A O 1 HETATM 4214 O O . HOH Q 8 . ? -19.667 16.148 75.510 1.00 57.49 ? 2101 HOH A O 1 HETATM 4215 O O . HOH Q 8 . ? -47.039 5.228 84.026 1.00 28.08 ? 2102 HOH A O 1 HETATM 4216 O O . HOH Q 8 . ? -32.005 21.250 72.459 1.00 29.78 ? 2103 HOH A O 1 HETATM 4217 O O . HOH Q 8 . ? -38.203 3.209 80.391 1.00 20.97 ? 2104 HOH A O 1 HETATM 4218 O O . HOH Q 8 . ? -36.429 6.459 80.825 1.00 24.91 ? 2105 HOH A O 1 HETATM 4219 O O . HOH Q 8 . ? -45.877 -1.401 84.254 1.00 37.83 ? 2106 HOH A O 1 HETATM 4220 O O . HOH Q 8 . ? -40.296 -4.398 81.431 1.00 53.19 ? 2107 HOH A O 1 HETATM 4221 O O . HOH Q 8 . ? -44.298 -4.220 78.224 1.00 48.19 ? 2108 HOH A O 1 HETATM 4222 O O . HOH Q 8 . ? -40.149 -2.747 78.187 1.00 45.30 ? 2109 HOH A O 1 HETATM 4223 O O . HOH Q 8 . ? -33.682 -2.046 80.142 1.00 35.08 ? 2110 HOH A O 1 HETATM 4224 O O . HOH Q 8 . ? -37.286 2.242 82.940 1.00 30.13 ? 2111 HOH A O 1 HETATM 4225 O O . HOH Q 8 . ? -35.596 -3.975 75.035 1.00 31.06 ? 2112 HOH A O 1 HETATM 4226 O O . HOH Q 8 . ? -32.983 2.042 86.004 1.00 40.70 ? 2113 HOH A O 1 HETATM 4227 O O . HOH Q 8 . ? -34.033 6.047 79.389 1.00 25.58 ? 2114 HOH A O 1 HETATM 4228 O O . HOH Q 8 . ? -28.922 4.696 72.375 1.00 25.71 ? 2115 HOH A O 1 HETATM 4229 O O . HOH Q 8 . ? -29.589 4.610 81.866 1.00 32.02 ? 2116 HOH A O 1 HETATM 4230 O O . HOH Q 8 . ? -36.906 -1.412 68.668 1.00 33.28 ? 2117 HOH A O 1 HETATM 4231 O O . HOH Q 8 . ? -32.182 0.463 69.792 1.00 25.06 ? 2118 HOH A O 1 HETATM 4232 O O . HOH Q 8 . ? -25.460 7.450 72.377 1.00 32.87 ? 2119 HOH A O 1 HETATM 4233 O O . HOH Q 8 . ? -32.395 10.094 67.446 1.00 28.41 ? 2120 HOH A O 1 HETATM 4234 O O . HOH Q 8 . ? -31.611 9.486 61.376 1.00 26.76 ? 2121 HOH A O 1 HETATM 4235 O O . HOH Q 8 . ? -33.276 11.319 64.205 1.00 36.81 ? 2122 HOH A O 1 HETATM 4236 O O . HOH Q 8 . ? -31.971 6.252 60.554 1.00 24.91 ? 2123 HOH A O 1 HETATM 4237 O O . HOH Q 8 . ? -52.155 5.897 69.199 1.00 37.27 ? 2124 HOH A O 1 HETATM 4238 O O . HOH Q 8 . ? -50.888 8.940 72.070 1.00 33.43 ? 2125 HOH A O 1 HETATM 4239 O O . HOH Q 8 . ? -47.545 24.610 85.150 1.00 46.53 ? 2126 HOH A O 1 HETATM 4240 O O . HOH Q 8 . ? -51.505 5.863 73.002 1.00 38.13 ? 2127 HOH A O 1 HETATM 4241 O O . HOH Q 8 . ? -53.082 -0.358 69.496 1.00 26.60 ? 2128 HOH A O 1 HETATM 4242 O O . HOH Q 8 . ? -54.619 4.716 75.025 1.00 46.31 ? 2129 HOH A O 1 HETATM 4243 O O . HOH Q 8 . ? -55.887 0.734 76.821 1.00 53.34 ? 2130 HOH A O 1 HETATM 4244 O O . HOH Q 8 . ? -50.896 -6.104 73.338 1.00 65.23 ? 2131 HOH A O 1 HETATM 4245 O O . HOH Q 8 . ? -50.948 5.258 78.461 1.00 44.31 ? 2132 HOH A O 1 HETATM 4246 O O . HOH Q 8 . ? -52.495 6.001 75.601 1.00 45.04 ? 2133 HOH A O 1 HETATM 4247 O O . HOH Q 8 . ? -53.558 4.545 81.315 1.00 41.78 ? 2134 HOH A O 1 HETATM 4248 O O . HOH Q 8 . ? -48.795 -1.694 88.526 1.00 43.01 ? 2135 HOH A O 1 HETATM 4249 O O . HOH Q 8 . ? -49.036 5.576 85.956 1.00 33.27 ? 2136 HOH A O 1 HETATM 4250 O O . HOH Q 8 . ? -51.313 7.521 85.321 1.00 35.16 ? 2137 HOH A O 1 HETATM 4251 O O . HOH Q 8 . ? -51.194 9.812 83.065 1.00 51.36 ? 2138 HOH A O 1 HETATM 4252 O O . HOH Q 8 . ? -54.556 6.143 63.412 1.00 52.90 ? 2139 HOH A O 1 HETATM 4253 O O . HOH Q 8 . ? -54.708 14.186 87.042 1.00 36.24 ? 2140 HOH A O 1 HETATM 4254 O O . HOH Q 8 . ? -51.416 14.741 81.887 1.00 25.21 ? 2141 HOH A O 1 HETATM 4255 O O . HOH Q 8 . ? -51.788 19.253 79.558 1.00 35.09 ? 2142 HOH A O 1 HETATM 4256 O O . HOH Q 8 . ? -52.428 18.034 82.420 1.00 48.17 ? 2143 HOH A O 1 HETATM 4257 O O . HOH Q 8 . ? -45.117 20.369 83.558 1.00 32.14 ? 2144 HOH A O 1 HETATM 4258 O O . HOH Q 8 . ? -50.700 23.320 79.317 1.00 68.65 ? 2145 HOH A O 1 HETATM 4259 O O . HOH Q 8 . ? -50.489 21.825 75.833 1.00 23.05 ? 2146 HOH A O 1 HETATM 4260 O O . HOH Q 8 . ? -47.343 25.224 75.776 1.00 47.16 ? 2147 HOH A O 1 HETATM 4261 O O . HOH Q 8 . ? -42.711 2.042 48.172 1.00 39.61 ? 2148 HOH A O 1 HETATM 4262 O O . HOH Q 8 . ? -51.044 19.056 76.864 1.00 24.16 ? 2149 HOH A O 1 HETATM 4263 O O . HOH Q 8 . ? -50.186 10.321 74.815 1.00 49.45 ? 2150 HOH A O 1 HETATM 4264 O O . HOH Q 8 . ? -47.276 16.290 71.616 1.00 18.10 ? 2151 HOH A O 1 HETATM 4265 O O . HOH Q 8 . ? -48.300 0.991 40.532 1.00 53.15 ? 2152 HOH A O 1 HETATM 4266 O O . HOH Q 8 . ? -50.021 15.887 71.604 1.00 17.46 ? 2153 HOH A O 1 HETATM 4267 O O . HOH Q 8 . ? -48.495 12.328 67.333 1.00 18.76 ? 2154 HOH A O 1 HETATM 4268 O O . HOH Q 8 . ? -45.992 16.796 69.122 1.00 19.68 ? 2155 HOH A O 1 HETATM 4269 O O . HOH Q 8 . ? -60.510 22.571 60.446 1.00 37.69 ? 2156 HOH A O 1 HETATM 4270 O O . HOH Q 8 . ? -36.667 19.173 71.573 1.00 20.90 ? 2157 HOH A O 1 HETATM 4271 O O . HOH Q 8 . ? -37.368 16.980 65.083 1.00 20.16 ? 2158 HOH A O 1 HETATM 4272 O O . HOH Q 8 . ? -33.834 14.297 66.337 1.00 26.10 ? 2159 HOH A O 1 HETATM 4273 O O . HOH Q 8 . ? -34.819 18.414 67.125 1.00 35.44 ? 2160 HOH A O 1 HETATM 4274 O O . HOH Q 8 . ? -31.761 12.762 67.644 1.00 40.68 ? 2161 HOH A O 1 HETATM 4275 O O . HOH Q 8 . ? -34.393 13.571 74.823 1.00 29.25 ? 2162 HOH A O 1 HETATM 4276 O O . HOH Q 8 . ? -61.691 16.519 43.357 1.00 46.54 ? 2163 HOH A O 1 HETATM 4277 O O . HOH Q 8 . ? -25.462 8.656 76.203 1.00 38.19 ? 2164 HOH A O 1 HETATM 4278 O O . HOH Q 8 . ? -58.142 4.783 5.030 1.00 43.48 ? 2165 HOH A O 1 HETATM 4279 O O . HOH Q 8 . ? -32.399 5.672 86.584 1.00 32.73 ? 2166 HOH A O 1 HETATM 4280 O O . HOH Q 8 . ? -28.996 8.112 90.018 1.00 41.96 ? 2167 HOH A O 1 HETATM 4281 O O . HOH Q 8 . ? -26.522 7.821 91.107 1.00 48.34 ? 2168 HOH A O 1 HETATM 4282 O O . HOH Q 8 . ? -29.278 10.462 92.576 1.00 45.91 ? 2169 HOH A O 1 HETATM 4283 O O . HOH Q 8 . ? -24.426 8.689 89.964 1.00 49.57 ? 2170 HOH A O 1 HETATM 4284 O O . HOH Q 8 . ? -23.043 13.069 89.921 1.00 41.61 ? 2171 HOH A O 1 HETATM 4285 O O . HOH Q 8 . ? -27.931 10.091 94.769 1.00 58.89 ? 2172 HOH A O 1 HETATM 4286 O O . HOH Q 8 . ? -26.317 17.165 95.388 1.00 44.24 ? 2173 HOH A O 1 HETATM 4287 O O . HOH Q 8 . ? -32.106 11.066 93.032 1.00 29.98 ? 2174 HOH A O 1 HETATM 4288 O O . HOH Q 8 . ? -39.231 6.883 100.517 1.00 35.17 ? 2175 HOH A O 1 HETATM 4289 O O . HOH Q 8 . ? -33.042 5.723 101.865 1.00 48.32 ? 2176 HOH A O 1 HETATM 4290 O O . HOH Q 8 . ? -33.618 0.680 97.881 1.00 56.82 ? 2177 HOH A O 1 HETATM 4291 O O . HOH Q 8 . ? -38.472 5.923 94.353 1.00 32.70 ? 2178 HOH A O 1 HETATM 4292 O O . HOH Q 8 . ? -42.623 2.870 99.920 1.00 45.79 ? 2179 HOH A O 1 HETATM 4293 O O . HOH Q 8 . ? -44.146 -0.253 98.951 1.00 38.77 ? 2180 HOH A O 1 HETATM 4294 O O . HOH Q 8 . ? -40.477 -2.641 97.278 1.00 56.14 ? 2181 HOH A O 1 HETATM 4295 O O . HOH Q 8 . ? -52.485 -0.736 94.284 1.00 45.41 ? 2182 HOH A O 1 HETATM 4296 O O . HOH Q 8 . ? -52.510 -1.840 91.473 1.00 63.92 ? 2183 HOH A O 1 HETATM 4297 O O . HOH Q 8 . ? -48.982 -1.533 98.949 1.00 50.18 ? 2184 HOH A O 1 HETATM 4298 O O . HOH Q 8 . ? -44.839 -6.999 88.315 1.00 53.49 ? 2185 HOH A O 1 HETATM 4299 O O . HOH Q 8 . ? -36.061 18.866 61.250 1.00 49.09 ? 2186 HOH A O 1 HETATM 4300 O O . HOH Q 8 . ? -38.460 22.497 62.295 1.00 39.90 ? 2187 HOH A O 1 HETATM 4301 O O . HOH Q 8 . ? -63.310 20.115 69.075 1.00 37.30 ? 2188 HOH A O 1 HETATM 4302 O O . HOH Q 8 . ? -52.927 12.016 78.695 1.00 63.02 ? 2189 HOH A O 1 HETATM 4303 O O . HOH Q 8 . ? -57.054 21.918 78.031 1.00 58.49 ? 2190 HOH A O 1 HETATM 4304 O O . HOH Q 8 . ? -44.006 -5.808 97.319 1.00 46.44 ? 2191 HOH A O 1 HETATM 4305 O O . HOH Q 8 . ? -35.824 12.078 86.194 1.00 31.40 ? 2192 HOH A O 1 HETATM 4306 O O . HOH Q 8 . ? -53.160 27.038 29.625 1.00 36.59 ? 2193 HOH A O 1 HETATM 4307 O O . HOH Q 8 . ? -49.054 26.838 31.085 0.33 14.25 ? 2194 HOH A O 1 HETATM 4308 O O . HOH Q 8 . ? -40.263 13.993 98.992 1.00 30.77 ? 2195 HOH A O 1 HETATM 4309 O O . HOH Q 8 . ? -40.196 7.214 105.391 1.00 37.44 ? 2196 HOH A O 1 HETATM 4310 O O . HOH Q 8 . ? -53.638 27.974 27.130 1.00 35.27 ? 2197 HOH A O 1 HETATM 4311 O O . HOH Q 8 . ? -42.887 7.236 105.521 1.00 42.06 ? 2198 HOH A O 1 HETATM 4312 O O . HOH Q 8 . ? -37.115 6.100 109.138 1.00 47.62 ? 2199 HOH A O 1 HETATM 4313 O O . HOH Q 8 . ? -52.615 22.437 9.605 1.00 48.55 ? 2200 HOH A O 1 HETATM 4314 O O . HOH Q 8 . ? -38.639 19.705 5.312 1.00 50.06 ? 2201 HOH A O 1 HETATM 4315 O O . HOH Q 8 . ? -38.857 17.228 109.775 1.00 47.52 ? 2202 HOH A O 1 HETATM 4316 O O . HOH Q 8 . ? -37.463 21.622 0.688 1.00 31.20 ? 2203 HOH A O 1 HETATM 4317 O O . HOH Q 8 . ? -29.905 19.893 101.601 1.00 47.54 ? 2204 HOH A O 1 HETATM 4318 O O . HOH Q 8 . ? -27.416 21.170 101.318 1.00 52.57 ? 2205 HOH A O 1 HETATM 4319 O O . HOH Q 8 . ? -26.496 23.157 98.334 1.00 50.51 ? 2206 HOH A O 1 HETATM 4320 O O . HOH Q 8 . ? -25.475 20.203 97.221 1.00 49.60 ? 2207 HOH A O 1 HETATM 4321 O O . HOH Q 8 . ? -23.501 18.443 93.711 1.00 56.51 ? 2208 HOH A O 1 HETATM 4322 O O . HOH Q 8 . ? -26.721 19.716 86.160 1.00 29.67 ? 2209 HOH A O 1 HETATM 4323 O O . HOH Q 8 . ? -22.143 17.883 84.945 1.00 36.33 ? 2210 HOH A O 1 HETATM 4324 O O . HOH Q 8 . ? -22.309 17.708 87.970 1.00 43.71 ? 2211 HOH A O 1 HETATM 4325 O O . HOH Q 8 . ? -19.848 23.292 81.074 1.00 48.50 ? 2212 HOH A O 1 HETATM 4326 O O . HOH Q 8 . ? -21.854 24.717 86.222 1.00 46.63 ? 2213 HOH A O 1 HETATM 4327 O O . HOH Q 8 . ? -18.938 22.741 89.372 1.00 57.10 ? 2214 HOH A O 1 HETATM 4328 O O . HOH Q 8 . ? -19.559 17.393 78.052 1.00 39.94 ? 2215 HOH A O 1 HETATM 4329 O O . HOH Q 8 . ? -33.546 14.486 -7.229 1.00 52.75 ? 2216 HOH A O 1 HETATM 4330 O O . HOH Q 8 . ? -41.725 17.207 -17.187 1.00 48.25 ? 2217 HOH A O 1 HETATM 4331 O O . HOH Q 8 . ? -27.178 20.365 74.070 1.00 43.36 ? 2218 HOH A O 1 HETATM 4332 O O . HOH Q 8 . ? -27.990 16.922 75.697 1.00 31.72 ? 2219 HOH A O 1 HETATM 4333 O O . HOH Q 8 . ? -32.157 22.641 75.021 1.00 33.50 ? 2220 HOH A O 1 HETATM 4334 O O . HOH Q 8 . ? -34.421 13.552 84.743 1.00 24.61 ? 2221 HOH A O 1 HETATM 4335 O O . HOH Q 8 . ? -49.028 20.456 90.551 1.00 34.82 ? 2222 HOH A O 1 HETATM 4336 O O . HOH Q 8 . ? -49.431 7.825 103.306 1.00 42.37 ? 2223 HOH A O 1 HETATM 4337 O O . HOH Q 8 . ? -55.801 8.940 101.423 1.00 47.02 ? 2224 HOH A O 1 HETATM 4338 O O . HOH Q 8 . ? -45.983 21.413 109.901 1.00 56.72 ? 2225 HOH A O 1 HETATM 4339 O O . HOH Q 8 . ? -50.135 20.338 105.194 1.00 42.28 ? 2226 HOH A O 1 HETATM 4340 O O . HOH Q 8 . ? -48.721 22.804 100.152 1.00 45.56 ? 2227 HOH A O 1 HETATM 4341 O O . HOH Q 8 . ? -52.130 21.134 100.547 1.00 47.00 ? 2228 HOH A O 1 HETATM 4342 O O . HOH Q 8 . ? -43.876 20.176 101.102 1.00 38.70 ? 2229 HOH A O 1 HETATM 4343 O O . HOH Q 8 . ? -46.620 24.443 99.609 1.00 50.89 ? 2230 HOH A O 1 HETATM 4344 O O . HOH Q 8 . ? -41.559 21.102 99.585 1.00 50.02 ? 2231 HOH A O 1 HETATM 4345 O O . HOH Q 8 . ? -41.342 23.929 101.469 1.00 48.02 ? 2232 HOH A O 1 HETATM 4346 O O . HOH Q 8 . ? -34.684 26.567 93.713 1.00 41.42 ? 2233 HOH A O 1 HETATM 4347 O O . HOH Q 8 . ? -37.313 24.801 86.920 1.00 44.36 ? 2234 HOH A O 1 HETATM 4348 O O . HOH Q 8 . ? -32.911 26.849 82.948 1.00 38.88 ? 2235 HOH A O 1 HETATM 4349 O O . HOH Q 8 . ? -36.850 32.580 83.261 1.00 46.53 ? 2236 HOH A O 1 HETATM 4350 O O . HOH Q 8 . ? -34.204 30.845 79.641 1.00 58.66 ? 2237 HOH A O 1 HETATM 4351 O O . HOH Q 8 . ? -29.917 26.830 82.587 1.00 38.88 ? 2238 HOH A O 1 HETATM 4352 O O . HOH Q 8 . ? -31.664 27.048 75.556 1.00 59.49 ? 2239 HOH A O 1 HETATM 4353 O O . HOH Q 8 . ? -36.598 26.488 84.661 1.00 39.56 ? 2240 HOH A O 1 HETATM 4354 O O . HOH Q 8 . ? -38.344 31.420 85.132 1.00 33.37 ? 2241 HOH A O 1 HETATM 4355 O O . HOH Q 8 . ? -39.257 28.205 84.127 1.00 50.95 ? 2242 HOH A O 1 HETATM 4356 O O . HOH Q 8 . ? -41.026 31.258 92.079 1.00 31.91 ? 2243 HOH A O 1 HETATM 4357 O O . HOH Q 8 . ? -44.062 24.992 86.372 1.00 53.80 ? 2244 HOH A O 1 HETATM 4358 O O . HOH Q 8 . ? -42.371 22.061 83.774 1.00 25.05 ? 2245 HOH A O 1 HETATM 4359 O O . HOH Q 8 . ? -43.117 29.393 89.607 1.00 40.41 ? 2246 HOH A O 1 HETATM 4360 O O . HOH Q 8 . ? -45.577 26.434 88.718 1.00 43.09 ? 2247 HOH A O 1 HETATM 4361 O O . HOH Q 8 . ? -48.386 25.183 92.066 1.00 31.48 ? 2248 HOH A O 1 HETATM 4362 O O . HOH Q 8 . ? -49.691 22.562 92.295 1.00 31.00 ? 2249 HOH A O 1 HETATM 4363 O O . HOH Q 8 . ? -52.032 23.451 98.994 1.00 43.95 ? 2250 HOH A O 1 HETATM 4364 O O . HOH Q 8 . ? -56.104 20.387 97.460 1.00 48.17 ? 2251 HOH A O 1 HETATM 4365 O O . HOH Q 8 . ? -59.163 16.636 96.166 1.00 38.85 ? 2252 HOH A O 1 HETATM 4366 O O . HOH Q 8 . ? -58.261 9.992 99.997 1.00 47.89 ? 2253 HOH A O 1 HETATM 4367 O O . HOH Q 8 . ? -61.985 5.622 91.102 1.00 36.28 ? 2254 HOH A O 1 HETATM 4368 O O . HOH Q 8 . ? -58.827 2.189 92.146 1.00 42.69 ? 2255 HOH A O 1 HETATM 4369 O O . HOH Q 8 . ? -59.835 7.846 98.643 1.00 39.96 ? 2256 HOH A O 1 HETATM 4370 O O . HOH Q 8 . ? -58.005 1.456 88.840 1.00 40.99 ? 2257 HOH A O 1 HETATM 4371 O O . HOH Q 8 . ? -53.988 4.819 84.640 1.00 40.82 ? 2258 HOH A O 1 HETATM 4372 O O . HOH Q 8 . ? -56.250 -1.699 92.482 1.00 45.56 ? 2259 HOH A O 1 HETATM 4373 O O . HOH Q 8 . ? -56.606 13.438 88.814 1.00 38.00 ? 2260 HOH A O 1 HETATM 4374 O O . HOH Q 8 . ? -48.645 23.422 87.486 1.00 41.91 ? 2261 HOH A O 1 HETATM 4375 O O . HOH Q 8 . ? -40.427 23.506 81.849 1.00 38.75 ? 2262 HOH A O 1 HETATM 4376 O O . HOH Q 8 . ? -39.146 23.480 77.970 1.00 37.31 ? 2263 HOH A O 1 HETATM 4377 O O . HOH Q 8 . ? -36.387 25.305 81.722 1.00 38.01 ? 2264 HOH A O 1 HETATM 4378 O O . HOH Q 8 . ? -20.011 27.703 85.667 1.00 50.74 ? 2265 HOH A O 1 HETATM 4379 O O . HOH Q 8 . ? -27.649 30.217 82.193 1.00 43.92 ? 2266 HOH A O 1 HETATM 4380 O O . HOH Q 8 . ? -30.659 7.073 92.029 1.00 40.79 ? 2267 HOH A O 1 HETATM 4381 O O . HOH Q 8 . ? -29.617 20.001 72.547 1.00 44.92 ? 2268 HOH A O 1 HETATM 4382 O O . HOH Q 8 . ? -34.060 19.539 71.076 1.00 30.54 ? 2269 HOH A O 1 HETATM 4383 O O . HOH Q 8 . ? -27.863 17.432 68.857 1.00 42.97 ? 2270 HOH A O 1 HETATM 4384 O O . HOH Q 8 . ? -28.539 19.956 69.681 1.00 61.97 ? 2271 HOH A O 1 HETATM 4385 O O . HOH Q 8 . ? -35.316 20.373 64.919 1.00 50.87 ? 2272 HOH A O 1 HETATM 4386 O O . HOH Q 8 . ? -31.547 18.791 61.667 1.00 61.56 ? 2273 HOH A O 1 HETATM 4387 O O . HOH Q 8 . ? -31.790 13.623 62.880 1.00 32.05 ? 2274 HOH A O 1 HETATM 4388 O O . HOH Q 8 . ? -45.223 15.697 63.605 1.00 20.74 ? 2275 HOH A O 1 HETATM 4389 O O . HOH Q 8 . ? -44.392 13.831 61.454 1.00 31.68 ? 2276 HOH A O 1 HETATM 4390 O O . HOH Q 8 . ? -46.224 14.390 65.853 1.00 24.79 ? 2277 HOH A O 1 HETATM 4391 O O . HOH Q 8 . ? -46.070 12.127 63.105 1.00 30.91 ? 2278 HOH A O 1 HETATM 4392 O O . HOH Q 8 . ? -49.878 11.177 64.837 1.00 19.06 ? 2279 HOH A O 1 HETATM 4393 O O . HOH Q 8 . ? -53.245 8.822 63.671 1.00 28.75 ? 2280 HOH A O 1 HETATM 4394 O O . HOH Q 8 . ? -52.328 11.822 65.904 1.00 21.06 ? 2281 HOH A O 1 HETATM 4395 O O . HOH Q 8 . ? -52.876 15.592 69.570 1.00 18.54 ? 2282 HOH A O 1 HETATM 4396 O O . HOH Q 8 . ? -54.527 14.204 71.156 1.00 30.77 ? 2283 HOH A O 1 HETATM 4397 O O . HOH Q 8 . ? -51.524 12.485 73.786 1.00 33.81 ? 2284 HOH A O 1 HETATM 4398 O O . HOH Q 8 . ? -54.028 12.157 72.983 1.00 36.46 ? 2285 HOH A O 1 HETATM 4399 O O . HOH Q 8 . ? -53.818 5.383 66.451 1.00 54.95 ? 2286 HOH A O 1 HETATM 4400 O O . HOH Q 8 . ? -53.473 3.434 62.332 1.00 31.99 ? 2287 HOH A O 1 HETATM 4401 O O . HOH Q 8 . ? -53.770 -2.691 63.444 1.00 47.08 ? 2288 HOH A O 1 HETATM 4402 O O . HOH Q 8 . ? -50.689 -2.717 65.904 1.00 46.26 ? 2289 HOH A O 1 HETATM 4403 O O . HOH Q 8 . ? -46.141 -4.590 64.450 1.00 33.77 ? 2290 HOH A O 1 HETATM 4404 O O . HOH Q 8 . ? -46.086 -6.915 59.957 1.00 47.48 ? 2291 HOH A O 1 HETATM 4405 O O . HOH Q 8 . ? -41.590 -6.324 61.670 1.00 48.94 ? 2292 HOH A O 1 HETATM 4406 O O . HOH Q 8 . ? -42.830 -8.104 57.448 1.00 43.53 ? 2293 HOH A O 1 HETATM 4407 O O . HOH Q 8 . ? -36.117 -6.164 63.310 1.00 47.32 ? 2294 HOH A O 1 HETATM 4408 O O . HOH Q 8 . ? -39.356 -3.231 50.681 1.00 35.07 ? 2295 HOH A O 1 HETATM 4409 O O . HOH Q 8 . ? -42.233 -0.840 50.411 1.00 45.56 ? 2296 HOH A O 1 HETATM 4410 O O . HOH Q 8 . ? -35.106 3.924 50.892 1.00 25.19 ? 2297 HOH A O 1 HETATM 4411 O O . HOH Q 8 . ? -44.768 2.190 50.724 1.00 34.87 ? 2298 HOH A O 1 HETATM 4412 O O . HOH Q 8 . ? -42.249 5.975 50.234 1.00 24.86 ? 2299 HOH A O 1 HETATM 4413 O O . HOH Q 8 . ? -39.672 4.662 49.310 1.00 25.19 ? 2300 HOH A O 1 HETATM 4414 O O . HOH Q 8 . ? -54.074 1.369 55.228 1.00 53.27 ? 2301 HOH A O 1 HETATM 4415 O O . HOH Q 8 . ? -55.849 2.790 57.167 1.00 44.39 ? 2302 HOH A O 1 HETATM 4416 O O . HOH Q 8 . ? -41.794 4.691 46.842 1.00 36.40 ? 2303 HOH A O 1 HETATM 4417 O O . HOH Q 8 . ? -40.296 11.096 45.794 1.00 31.34 ? 2304 HOH A O 1 HETATM 4418 O O . HOH Q 8 . ? -38.835 5.920 47.396 1.00 42.79 ? 2305 HOH A O 1 HETATM 4419 O O . HOH Q 8 . ? -40.041 7.578 44.210 1.00 50.89 ? 2306 HOH A O 1 HETATM 4420 O O . HOH Q 8 . ? -37.444 9.164 48.162 1.00 38.65 ? 2307 HOH A O 1 HETATM 4421 O O . HOH Q 8 . ? -43.019 13.313 42.979 1.00 25.47 ? 2308 HOH A O 1 HETATM 4422 O O . HOH Q 8 . ? -42.834 4.081 43.891 1.00 39.80 ? 2309 HOH A O 1 HETATM 4423 O O . HOH Q 8 . ? -45.961 7.341 39.328 1.00 29.91 ? 2310 HOH A O 1 HETATM 4424 O O . HOH Q 8 . ? -49.527 3.909 40.722 1.00 43.49 ? 2311 HOH A O 1 HETATM 4425 O O . HOH Q 8 . ? -44.656 16.585 46.254 1.00 23.78 ? 2312 HOH A O 1 HETATM 4426 O O . HOH Q 8 . ? -57.967 8.148 52.425 1.00 36.93 ? 2313 HOH A O 1 HETATM 4427 O O . HOH Q 8 . ? -58.038 11.663 53.034 1.00 32.53 ? 2314 HOH A O 1 HETATM 4428 O O . HOH Q 8 . ? -58.631 8.129 48.389 1.00 49.69 ? 2315 HOH A O 1 HETATM 4429 O O . HOH Q 8 . ? -60.313 14.174 50.705 1.00 37.37 ? 2316 HOH A O 1 HETATM 4430 O O . HOH Q 8 . ? -55.343 12.465 59.998 1.00 23.52 ? 2317 HOH A O 1 HETATM 4431 O O . HOH Q 8 . ? -55.960 12.970 56.972 1.00 22.06 ? 2318 HOH A O 1 HETATM 4432 O O . HOH Q 8 . ? -54.704 9.252 61.396 1.00 25.24 ? 2319 HOH A O 1 HETATM 4433 O O . HOH Q 8 . ? -49.199 17.070 55.546 1.00 19.99 ? 2320 HOH A O 1 HETATM 4434 O O . HOH Q 8 . ? -47.659 15.528 59.628 1.00 18.60 ? 2321 HOH A O 1 HETATM 4435 O O . HOH Q 8 . ? -56.573 15.021 60.634 1.00 40.81 ? 2322 HOH A O 1 HETATM 4436 O O . HOH Q 8 . ? -58.016 14.982 56.099 1.00 45.71 ? 2323 HOH A O 1 HETATM 4437 O O . HOH Q 8 . ? -57.865 21.088 60.364 1.00 23.61 ? 2324 HOH A O 1 HETATM 4438 O O . HOH Q 8 . ? -59.165 20.102 57.211 1.00 50.79 ? 2325 HOH A O 1 HETATM 4439 O O . HOH Q 8 . ? -55.734 19.129 61.608 1.00 21.37 ? 2326 HOH A O 1 HETATM 4440 O O . HOH Q 8 . ? -58.968 16.885 54.440 1.00 48.25 ? 2327 HOH A O 1 HETATM 4441 O O . HOH Q 8 . ? -46.352 15.406 52.847 1.00 26.83 ? 2328 HOH A O 1 HETATM 4442 O O . HOH Q 8 . ? -43.379 14.245 55.532 1.00 18.47 ? 2329 HOH A O 1 HETATM 4443 O O . HOH Q 8 . ? -46.671 16.515 56.228 1.00 22.33 ? 2330 HOH A O 1 HETATM 4444 O O . HOH Q 8 . ? -34.906 11.245 59.380 1.00 29.69 ? 2331 HOH A O 1 HETATM 4445 O O . HOH Q 8 . ? -43.070 15.521 52.871 1.00 29.58 ? 2332 HOH A O 1 HETATM 4446 O O . HOH Q 8 . ? -43.219 16.430 48.716 1.00 29.41 ? 2333 HOH A O 1 HETATM 4447 O O . HOH Q 8 . ? -43.096 21.573 47.286 1.00 41.56 ? 2334 HOH A O 1 HETATM 4448 O O . HOH Q 8 . ? -48.270 19.608 51.829 1.00 17.03 ? 2335 HOH A O 1 HETATM 4449 O O . HOH Q 8 . ? -44.305 18.210 52.284 1.00 32.26 ? 2336 HOH A O 1 HETATM 4450 O O . HOH Q 8 . ? -48.440 17.027 52.962 1.00 18.10 ? 2337 HOH A O 1 HETATM 4451 O O . HOH Q 8 . ? -50.995 19.915 52.109 1.00 15.28 ? 2338 HOH A O 1 HETATM 4452 O O . HOH Q 8 . ? -61.863 18.057 46.264 1.00 55.88 ? 2339 HOH A O 1 HETATM 4453 O O . HOH Q 8 . ? -61.417 13.997 43.872 1.00 41.42 ? 2340 HOH A O 1 HETATM 4454 O O . HOH Q 8 . ? -59.313 7.032 44.735 1.00 64.34 ? 2341 HOH A O 1 HETATM 4455 O O . HOH Q 8 . ? -59.570 14.907 39.392 1.00 41.06 ? 2342 HOH A O 1 HETATM 4456 O O . HOH Q 8 . ? -59.339 9.318 37.663 1.00 41.87 ? 2343 HOH A O 1 HETATM 4457 O O . HOH Q 8 . ? -58.271 13.937 36.856 1.00 27.96 ? 2344 HOH A O 1 HETATM 4458 O O . HOH Q 8 . ? -49.925 16.393 30.862 1.00 16.93 ? 2345 HOH A O 1 HETATM 4459 O O . HOH Q 8 . ? -44.697 9.420 26.821 1.00 53.47 ? 2346 HOH A O 1 HETATM 4460 O O . HOH Q 8 . ? -52.278 15.623 17.710 1.00 35.68 ? 2347 HOH A O 1 HETATM 4461 O O . HOH Q 8 . ? -53.387 16.640 21.189 1.00 21.80 ? 2348 HOH A O 1 HETATM 4462 O O . HOH Q 8 . ? -60.268 16.023 20.726 1.00 30.44 ? 2349 HOH A O 1 HETATM 4463 O O . HOH Q 8 . ? -61.927 6.877 19.494 1.00 56.00 ? 2350 HOH A O 1 HETATM 4464 O O . HOH Q 8 . ? -63.188 11.424 14.286 1.00 37.68 ? 2351 HOH A O 1 HETATM 4465 O O . HOH Q 8 . ? -56.337 3.049 10.948 1.00 34.39 ? 2352 HOH A O 1 HETATM 4466 O O . HOH Q 8 . ? -58.547 7.745 8.287 1.00 30.70 ? 2353 HOH A O 1 HETATM 4467 O O . HOH Q 8 . ? -61.120 7.820 7.126 1.00 47.16 ? 2354 HOH A O 1 HETATM 4468 O O . HOH Q 8 . ? -60.782 6.069 4.969 1.00 62.63 ? 2355 HOH A O 1 HETATM 4469 O O . HOH Q 8 . ? -59.022 4.754 -0.028 1.00 65.72 ? 2356 HOH A O 1 HETATM 4470 O O . HOH Q 8 . ? -58.012 11.764 0.289 1.00 46.42 ? 2357 HOH A O 1 HETATM 4471 O O . HOH Q 8 . ? -56.687 7.061 6.049 1.00 31.16 ? 2358 HOH A O 1 HETATM 4472 O O . HOH Q 8 . ? -59.787 14.013 7.816 1.00 34.82 ? 2359 HOH A O 1 HETATM 4473 O O . HOH Q 8 . ? -47.814 1.268 12.395 1.00 42.69 ? 2360 HOH A O 1 HETATM 4474 O O . HOH Q 8 . ? -43.344 3.160 9.853 1.00 36.01 ? 2361 HOH A O 1 HETATM 4475 O O . HOH Q 8 . ? -44.243 4.836 19.395 1.00 60.63 ? 2362 HOH A O 1 HETATM 4476 O O . HOH Q 8 . ? -43.204 4.862 22.038 1.00 55.27 ? 2363 HOH A O 1 HETATM 4477 O O . HOH Q 8 . ? -46.500 6.944 3.635 1.00 28.46 ? 2364 HOH A O 1 HETATM 4478 O O . HOH Q 8 . ? -53.329 2.133 5.168 1.00 59.75 ? 2365 HOH A O 1 HETATM 4479 O O . HOH Q 8 . ? -47.555 2.513 -2.504 1.00 26.25 ? 2366 HOH A O 1 HETATM 4480 O O . HOH Q 8 . ? -52.808 -0.409 -6.990 1.00 51.01 ? 2367 HOH A O 1 HETATM 4481 O O . HOH Q 8 . ? -46.206 -0.551 -3.057 1.00 41.21 ? 2368 HOH A O 1 HETATM 4482 O O . HOH Q 8 . ? -40.319 3.377 -6.045 1.00 38.71 ? 2369 HOH A O 1 HETATM 4483 O O . HOH Q 8 . ? -48.057 -0.525 0.649 0.50 33.69 ? 2370 HOH A O 1 HETATM 4484 O O . HOH Q 8 . ? -41.721 8.268 7.604 1.00 31.95 ? 2371 HOH A O 1 HETATM 4485 O O . HOH Q 8 . ? -39.219 8.868 10.329 1.00 34.39 ? 2372 HOH A O 1 HETATM 4486 O O . HOH Q 8 . ? -40.509 10.780 8.285 1.00 37.69 ? 2373 HOH A O 1 HETATM 4487 O O . HOH Q 8 . ? -38.347 11.644 11.262 1.00 35.43 ? 2374 HOH A O 1 HETATM 4488 O O . HOH Q 8 . ? -39.822 5.730 13.573 1.00 52.99 ? 2375 HOH A O 1 HETATM 4489 O O . HOH Q 8 . ? -37.265 14.349 17.633 1.00 34.72 ? 2376 HOH A O 1 HETATM 4490 O O . HOH Q 8 . ? -37.685 18.842 11.258 1.00 53.92 ? 2377 HOH A O 1 HETATM 4491 O O . HOH Q 8 . ? -37.047 14.081 28.231 1.00 44.30 ? 2378 HOH A O 1 HETATM 4492 O O . HOH Q 8 . ? -37.734 10.576 26.356 1.00 50.90 ? 2379 HOH A O 1 HETATM 4493 O O . HOH Q 8 . ? -43.351 21.839 22.326 1.00 39.14 ? 2380 HOH A O 1 HETATM 4494 O O . HOH Q 8 . ? -44.369 20.181 20.328 1.00 30.02 ? 2381 HOH A O 1 HETATM 4495 O O . HOH Q 8 . ? -42.551 17.363 42.064 1.00 40.24 ? 2382 HOH A O 1 HETATM 4496 O O . HOH Q 8 . ? -38.995 18.409 40.073 1.00 38.24 ? 2383 HOH A O 1 HETATM 4497 O O . HOH Q 8 . ? -43.509 21.434 33.015 1.00 51.49 ? 2384 HOH A O 1 HETATM 4498 O O . HOH Q 8 . ? -43.746 20.277 35.866 1.00 48.99 ? 2385 HOH A O 1 HETATM 4499 O O . HOH Q 8 . ? -38.063 9.533 45.271 1.00 46.67 ? 2386 HOH A O 1 HETATM 4500 O O . HOH Q 8 . ? -36.063 12.209 44.862 1.00 48.40 ? 2387 HOH A O 1 HETATM 4501 O O . HOH Q 8 . ? -42.880 15.687 44.212 1.00 28.89 ? 2388 HOH A O 1 HETATM 4502 O O . HOH Q 8 . ? -37.091 17.286 44.951 1.00 54.15 ? 2389 HOH A O 1 HETATM 4503 O O . HOH Q 8 . ? -41.090 19.701 46.062 1.00 53.23 ? 2390 HOH A O 1 HETATM 4504 O O . HOH Q 8 . ? -39.199 19.940 52.727 1.00 41.06 ? 2391 HOH A O 1 HETATM 4505 O O . HOH Q 8 . ? -37.506 19.222 56.130 1.00 45.25 ? 2392 HOH A O 1 HETATM 4506 O O . HOH Q 8 . ? -34.202 11.275 56.622 1.00 32.84 ? 2393 HOH A O 1 HETATM 4507 O O . HOH Q 8 . ? -39.988 19.129 59.139 1.00 28.47 ? 2394 HOH A O 1 HETATM 4508 O O . HOH Q 8 . ? -38.093 18.016 62.798 1.00 24.22 ? 2395 HOH A O 1 HETATM 4509 O O . HOH Q 8 . ? -42.309 20.816 65.184 1.00 36.51 ? 2396 HOH A O 1 HETATM 4510 O O . HOH Q 8 . ? -39.389 19.944 61.694 1.00 36.31 ? 2397 HOH A O 1 HETATM 4511 O O . HOH Q 8 . ? -39.799 20.968 64.064 1.00 43.97 ? 2398 HOH A O 1 HETATM 4512 O O . HOH Q 8 . ? -45.954 18.834 54.516 1.00 25.51 ? 2399 HOH A O 1 HETATM 4513 O O . HOH Q 8 . ? -42.219 20.848 59.014 1.00 34.50 ? 2400 HOH A O 1 HETATM 4514 O O . HOH Q 8 . ? -48.610 15.532 62.492 1.00 29.54 ? 2401 HOH A O 1 HETATM 4515 O O . HOH Q 8 . ? -48.451 20.381 67.879 1.00 20.67 ? 2402 HOH A O 1 HETATM 4516 O O . HOH Q 8 . ? -53.647 20.564 62.952 1.00 13.92 ? 2403 HOH A O 1 HETATM 4517 O O . HOH Q 8 . ? -51.401 14.373 64.989 1.00 22.92 ? 2404 HOH A O 1 HETATM 4518 O O . HOH Q 8 . ? -48.289 13.446 64.000 1.00 30.46 ? 2405 HOH A O 1 HETATM 4519 O O . HOH Q 8 . ? -58.281 17.351 63.647 1.00 35.53 ? 2406 HOH A O 1 HETATM 4520 O O . HOH Q 8 . ? -55.326 11.889 68.804 1.00 39.36 ? 2407 HOH A O 1 HETATM 4521 O O . HOH Q 8 . ? -54.216 10.605 65.413 1.00 39.75 ? 2408 HOH A O 1 HETATM 4522 O O . HOH Q 8 . ? -59.217 15.708 65.784 1.00 23.24 ? 2409 HOH A O 1 HETATM 4523 O O . HOH Q 8 . ? -61.534 16.031 70.812 1.00 46.95 ? 2410 HOH A O 1 HETATM 4524 O O . HOH Q 8 . ? -57.923 11.688 68.410 1.00 49.04 ? 2411 HOH A O 1 HETATM 4525 O O . HOH Q 8 . ? -56.174 16.543 72.766 1.00 36.21 ? 2412 HOH A O 1 HETATM 4526 O O . HOH Q 8 . ? -61.277 11.298 72.220 1.00 52.08 ? 2413 HOH A O 1 HETATM 4527 O O . HOH Q 8 . ? -63.184 14.815 73.077 1.00 53.25 ? 2414 HOH A O 1 HETATM 4528 O O . HOH Q 8 . ? -61.354 18.406 69.892 1.00 29.28 ? 2415 HOH A O 1 HETATM 4529 O O . HOH Q 8 . ? -54.579 12.966 76.465 1.00 62.19 ? 2416 HOH A O 1 HETATM 4530 O O . HOH Q 8 . ? -62.797 16.608 75.725 1.00 31.70 ? 2417 HOH A O 1 HETATM 4531 O O . HOH Q 8 . ? -61.002 22.408 71.058 1.00 20.33 ? 2418 HOH A O 1 HETATM 4532 O O . HOH Q 8 . ? -56.371 26.601 74.044 1.00 24.09 ? 2419 HOH A O 1 HETATM 4533 O O . HOH Q 8 . ? -58.112 24.912 77.082 1.00 42.50 ? 2420 HOH A O 1 HETATM 4534 O O . HOH Q 8 . ? -53.774 18.224 72.717 1.00 24.08 ? 2421 HOH A O 1 HETATM 4535 O O . HOH Q 8 . ? -60.489 23.078 68.418 1.00 24.99 ? 2422 HOH A O 1 HETATM 4536 O O . HOH Q 8 . ? -60.245 26.078 63.485 1.00 19.96 ? 2423 HOH A O 1 HETATM 4537 O O . HOH Q 8 . ? -63.397 25.187 69.539 1.00 25.52 ? 2424 HOH A O 1 HETATM 4538 O O . HOH Q 8 . ? -61.479 30.138 67.825 1.00 24.49 ? 2425 HOH A O 1 HETATM 4539 O O . HOH Q 8 . ? -50.594 19.954 69.532 1.00 20.48 ? 2426 HOH A O 1 HETATM 4540 O O . HOH Q 8 . ? -48.577 22.912 67.797 1.00 16.29 ? 2427 HOH A O 1 HETATM 4541 O O . HOH Q 8 . ? -61.102 17.254 67.184 1.00 33.27 ? 2428 HOH A O 1 HETATM 4542 O O . HOH Q 8 . ? -62.160 21.783 66.798 1.00 35.54 ? 2429 HOH A O 1 HETATM 4543 O O . HOH Q 8 . ? -60.268 25.204 60.785 1.00 23.30 ? 2430 HOH A O 1 HETATM 4544 O O . HOH Q 8 . ? -50.742 19.188 54.853 1.00 17.71 ? 2431 HOH A O 1 HETATM 4545 O O . HOH Q 8 . ? -59.274 21.488 54.027 1.00 36.96 ? 2432 HOH A O 1 HETATM 4546 O O . HOH Q 8 . ? -60.226 26.446 57.583 1.00 31.35 ? 2433 HOH A O 1 HETATM 4547 O O . HOH Q 8 . ? -58.614 27.856 56.154 1.00 17.05 ? 2434 HOH A O 1 HETATM 4548 O O . HOH Q 8 . ? -58.761 24.378 47.587 1.00 24.35 ? 2435 HOH A O 1 HETATM 4549 O O . HOH Q 8 . ? -59.027 27.454 53.500 1.00 13.12 ? 2436 HOH A O 1 HETATM 4550 O O . HOH Q 8 . ? -52.230 28.000 46.471 1.00 14.08 ? 2437 HOH A O 1 HETATM 4551 O O . HOH Q 8 . ? -46.736 24.580 52.486 1.00 10.84 ? 2438 HOH A O 1 HETATM 4552 O O . HOH Q 8 . ? -54.080 30.960 40.406 1.00 12.16 ? 2439 HOH A O 1 HETATM 4553 O O . HOH Q 8 . ? -50.944 27.599 41.892 1.00 13.57 ? 2440 HOH A O 1 HETATM 4554 O O . HOH Q 8 . ? -57.213 19.881 37.313 1.00 23.62 ? 2441 HOH A O 1 HETATM 4555 O O . HOH Q 8 . ? -60.700 17.789 41.270 1.00 34.79 ? 2442 HOH A O 1 HETATM 4556 O O . HOH Q 8 . ? -59.706 17.375 38.498 1.00 43.04 ? 2443 HOH A O 1 HETATM 4557 O O . HOH Q 8 . ? -50.915 25.411 29.739 1.00 23.81 ? 2444 HOH A O 1 HETATM 4558 O O . HOH Q 8 . ? -57.356 22.103 23.718 1.00 39.36 ? 2445 HOH A O 1 HETATM 4559 O O . HOH Q 8 . ? -53.550 26.672 25.020 1.00 42.25 ? 2446 HOH A O 1 HETATM 4560 O O . HOH Q 8 . ? -50.216 25.363 27.236 1.00 29.57 ? 2447 HOH A O 1 HETATM 4561 O O . HOH Q 8 . ? -47.347 23.112 24.324 1.00 43.47 ? 2448 HOH A O 1 HETATM 4562 O O . HOH Q 8 . ? -50.604 23.706 19.557 1.00 36.22 ? 2449 HOH A O 1 HETATM 4563 O O . HOH Q 8 . ? -54.140 22.616 21.459 1.00 46.90 ? 2450 HOH A O 1 HETATM 4564 O O . HOH Q 8 . ? -49.592 26.822 23.566 1.00 46.57 ? 2451 HOH A O 1 HETATM 4565 O O . HOH Q 8 . ? -53.261 19.523 15.147 1.00 37.37 ? 2452 HOH A O 1 HETATM 4566 O O . HOH Q 8 . ? -47.263 24.529 15.816 1.00 45.71 ? 2453 HOH A O 1 HETATM 4567 O O . HOH Q 8 . ? -43.388 17.859 14.052 1.00 28.05 ? 2454 HOH A O 1 HETATM 4568 O O . HOH Q 8 . ? -40.263 18.213 16.012 1.00 37.93 ? 2455 HOH A O 1 HETATM 4569 O O . HOH Q 8 . ? -40.343 20.114 19.319 1.00 51.91 ? 2456 HOH A O 1 HETATM 4570 O O . HOH Q 8 . ? -49.970 23.033 9.927 1.00 49.96 ? 2457 HOH A O 1 HETATM 4571 O O . HOH Q 8 . ? -47.001 24.410 12.997 1.00 44.36 ? 2458 HOH A O 1 HETATM 4572 O O . HOH Q 8 . ? -53.881 22.359 12.090 1.00 49.92 ? 2459 HOH A O 1 HETATM 4573 O O . HOH Q 8 . ? -50.134 24.053 16.694 1.00 50.21 ? 2460 HOH A O 1 HETATM 4574 O O . HOH Q 8 . ? -43.146 23.125 10.467 1.00 42.77 ? 2461 HOH A O 1 HETATM 4575 O O . HOH Q 8 . ? -51.576 25.213 6.043 1.00 42.99 ? 2462 HOH A O 1 HETATM 4576 O O . HOH Q 8 . ? -40.152 21.998 4.654 1.00 35.63 ? 2463 HOH A O 1 HETATM 4577 O O . HOH Q 8 . ? -41.093 21.711 11.941 1.00 59.69 ? 2464 HOH A O 1 HETATM 4578 O O . HOH Q 8 . ? -42.353 16.155 5.396 1.00 37.17 ? 2465 HOH A O 1 HETATM 4579 O O . HOH Q 8 . ? -47.014 23.264 -1.184 1.00 32.83 ? 2466 HOH A O 1 HETATM 4580 O O . HOH Q 8 . ? -45.667 27.138 0.693 1.00 48.50 ? 2467 HOH A O 1 HETATM 4581 O O . HOH Q 8 . ? -40.132 25.503 0.372 1.00 45.02 ? 2468 HOH A O 1 HETATM 4582 O O . HOH Q 8 . ? -41.733 29.938 7.622 1.00 39.20 ? 2469 HOH A O 1 HETATM 4583 O O . HOH Q 8 . ? -38.845 22.074 -1.587 1.00 35.11 ? 2470 HOH A O 1 HETATM 4584 O O . HOH Q 8 . ? -37.033 18.057 0.468 1.00 43.77 ? 2471 HOH A O 1 HETATM 4585 O O . HOH Q 8 . ? -49.040 24.759 -3.952 1.00 34.68 ? 2472 HOH A O 1 HETATM 4586 O O . HOH Q 8 . ? -44.413 27.181 -3.647 1.00 37.13 ? 2473 HOH A O 1 HETATM 4587 O O . HOH Q 8 . ? -38.277 24.894 -1.605 1.00 27.99 ? 2474 HOH A O 1 HETATM 4588 O O . HOH Q 8 . ? -36.220 28.429 -4.849 1.00 40.47 ? 2475 HOH A O 1 HETATM 4589 O O . HOH Q 8 . ? -42.744 23.502 -7.305 1.00 25.08 ? 2476 HOH A O 1 HETATM 4590 O O . HOH Q 8 . ? -49.768 22.667 -0.951 1.00 32.54 ? 2477 HOH A O 1 HETATM 4591 O O . HOH Q 8 . ? -53.386 24.399 -1.625 1.00 32.81 ? 2478 HOH A O 1 HETATM 4592 O O . HOH Q 8 . ? -55.880 20.016 5.357 1.00 25.21 ? 2479 HOH A O 1 HETATM 4593 O O . HOH Q 8 . ? -52.343 24.715 2.948 1.00 37.07 ? 2480 HOH A O 1 HETATM 4594 O O . HOH Q 8 . ? -60.398 22.269 6.436 1.00 39.03 ? 2481 HOH A O 1 HETATM 4595 O O . HOH Q 8 . ? -57.365 19.734 -9.817 1.00 42.97 ? 2482 HOH A O 1 HETATM 4596 O O . HOH Q 8 . ? -43.195 11.763 -11.970 1.00 31.43 ? 2483 HOH A O 1 HETATM 4597 O O . HOH Q 8 . ? -42.463 8.966 -9.191 1.00 24.23 ? 2484 HOH A O 1 HETATM 4598 O O . HOH Q 8 . ? -42.703 3.725 -10.437 1.00 52.91 ? 2485 HOH A O 1 HETATM 4599 O O . HOH Q 8 . ? -38.866 7.880 -7.639 1.00 36.91 ? 2486 HOH A O 1 HETATM 4600 O O . HOH Q 8 . ? -38.656 4.015 -8.112 1.00 51.70 ? 2487 HOH A O 1 HETATM 4601 O O . HOH Q 8 . ? -42.796 4.947 0.328 1.00 46.17 ? 2488 HOH A O 1 HETATM 4602 O O . HOH Q 8 . ? -43.595 2.318 0.362 1.00 43.01 ? 2489 HOH A O 1 HETATM 4603 O O . HOH Q 8 . ? -41.597 -0.097 -3.228 1.00 46.63 ? 2490 HOH A O 1 HETATM 4604 O O . HOH Q 8 . ? -37.611 9.403 -5.822 1.00 40.70 ? 2491 HOH A O 1 HETATM 4605 O O . HOH Q 8 . ? -36.300 7.498 -1.441 1.00 46.25 ? 2492 HOH A O 1 HETATM 4606 O O . HOH Q 8 . ? -38.351 6.642 3.468 1.00 58.20 ? 2493 HOH A O 1 HETATM 4607 O O . HOH Q 8 . ? -38.064 12.206 -5.224 1.00 34.35 ? 2494 HOH A O 1 HETATM 4608 O O . HOH Q 8 . ? -40.464 14.805 6.210 1.00 46.04 ? 2495 HOH A O 1 HETATM 4609 O O . HOH Q 8 . ? -40.351 6.564 6.074 1.00 43.30 ? 2496 HOH A O 1 HETATM 4610 O O . HOH Q 8 . ? -34.908 8.779 0.607 1.00 55.94 ? 2497 HOH A O 1 HETATM 4611 O O . HOH Q 8 . ? -32.696 8.503 2.451 1.00 71.73 ? 2498 HOH A O 1 HETATM 4612 O O . HOH Q 8 . ? -37.231 20.457 -2.990 1.00 32.81 ? 2499 HOH A O 1 HETATM 4613 O O . HOH Q 8 . ? -36.411 14.366 -5.561 1.00 41.73 ? 2500 HOH A O 1 HETATM 4614 O O . HOH Q 8 . ? -39.618 20.007 -13.814 1.00 33.83 ? 2501 HOH A O 1 HETATM 4615 O O . HOH Q 8 . ? -38.197 23.253 -12.504 1.00 46.89 ? 2502 HOH A O 1 HETATM 4616 O O . HOH Q 8 . ? -41.531 15.072 -13.747 1.00 37.35 ? 2503 HOH A O 1 HETATM 4617 O O . HOH Q 8 . ? -41.371 17.776 -14.478 1.00 32.38 ? 2504 HOH A O 1 HETATM 4618 O O . HOH Q 8 . ? -37.101 16.968 -14.545 1.00 48.20 ? 2505 HOH A O 1 HETATM 4619 O O . HOH Q 8 . ? -39.920 9.801 -9.340 1.00 39.08 ? 2506 HOH A O 1 HETATM 4620 O O . HOH Q 8 . ? -41.508 26.678 -13.341 1.00 32.33 ? 2507 HOH A O 1 HETATM 4621 O O . HOH Q 8 . ? -40.039 24.379 -13.877 1.00 49.18 ? 2508 HOH A O 1 HETATM 4622 O O . HOH Q 8 . ? -48.016 16.735 -16.688 1.00 36.39 ? 2509 HOH A O 1 HETATM 4623 O O . HOH Q 8 . ? -45.117 11.145 -15.359 1.00 47.55 ? 2510 HOH A O 1 HETATM 4624 O O . HOH Q 8 . ? -49.465 25.084 -17.237 1.00 62.20 ? 2511 HOH A O 1 HETATM 4625 O O . HOH Q 8 . ? -56.401 20.295 -12.349 1.00 47.93 ? 2512 HOH A O 1 HETATM 4626 O O . HOH Q 8 . ? -52.190 24.626 -19.028 1.00 55.52 ? 2513 HOH A O 1 HETATM 4627 O O . HOH Q 8 . ? -45.228 6.254 35.030 1.00 58.10 ? 2514 HOH A O 1 HETATM 4628 O O . HOH Q 8 . ? -48.667 -1.724 27.630 1.00 58.45 ? 2515 HOH A O 1 HETATM 4629 O O . HOH Q 8 . ? -53.831 -9.683 77.433 1.00 62.03 ? 2516 HOH A O 1 HETATM 4630 O O . HOH Q 8 . ? -27.983 30.445 96.323 1.00 33.22 ? 2517 HOH A O 1 HETATM 4631 O O . HOH Q 8 . ? -14.533 34.216 100.726 1.00 59.56 ? 2518 HOH A O 1 HETATM 4632 O O . HOH Q 8 . ? -15.785 37.725 96.902 1.00 60.23 ? 2519 HOH A O 1 HETATM 4633 O O . HOH Q 8 . ? -42.337 3.289 35.152 1.00 64.18 ? 2520 HOH A O 1 HETATM 4634 O O . HOH Q 8 . ? -58.546 3.056 56.742 1.00 54.77 ? 2521 HOH A O 1 HETATM 4635 O O . HOH Q 8 . ? -35.444 30.274 104.620 1.00 45.47 ? 2522 HOH A O 1 HETATM 4636 O O . HOH Q 8 . ? -30.922 26.267 106.880 1.00 53.84 ? 2523 HOH A O 1 HETATM 4637 O O . HOH Q 8 . ? -33.577 32.481 107.289 1.00 39.74 ? 2524 HOH A O 1 HETATM 4638 O O . HOH Q 8 . ? -53.257 5.880 99.352 1.00 39.15 ? 2525 HOH A O 1 HETATM 4639 O O . HOH Q 8 . ? -42.635 5.445 103.568 1.00 43.14 ? 2526 HOH A O 1 HETATM 4640 O O . HOH Q 8 . ? -50.383 0.553 102.811 1.00 47.33 ? 2527 HOH A O 1 HETATM 4641 O O . HOH Q 8 . ? -40.210 24.792 44.945 1.00 57.25 ? 2528 HOH A O 1 HETATM 4642 O O . HOH Q 8 . ? -48.236 -2.766 30.148 1.00 64.96 ? 2529 HOH A O 1 HETATM 4643 O O . HOH Q 8 . ? -14.292 28.738 94.185 1.00 68.51 ? 2530 HOH A O 1 HETATM 4644 O O . HOH Q 8 . ? -50.564 29.193 101.809 0.33 56.12 ? 2531 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 ? 0.9373 0.7798 0.7607 -0.0477 -0.0909 -0.0517 8 ASN A N 2 C CA . ASN A 8 ? 0.9154 0.7606 0.7343 -0.0479 -0.0915 -0.0524 8 ASN A CA 3 C C . ASN A 8 ? 0.8555 0.7095 0.6804 -0.0414 -0.0866 -0.0519 8 ASN A C 4 O O . ASN A 8 ? 0.8711 0.7373 0.7015 -0.0418 -0.0861 -0.0486 8 ASN A O 5 C CB . ASN A 8 ? 0.9501 0.8036 0.7694 -0.0549 -0.0959 -0.0491 8 ASN A CB 6 C CG . ASN A 8 ? 0.9936 0.8461 0.8052 -0.0567 -0.0980 -0.0505 8 ASN A CG 7 O OD1 . ASN A 8 ? 1.0195 0.8831 0.8346 -0.0556 -0.0971 -0.0484 8 ASN A OD1 8 N ND2 . ASN A 8 ? 1.0242 0.8627 0.8245 -0.0592 -0.1008 -0.0541 8 ASN A ND2 9 N N . SER A 9 ? 0.7691 0.6168 0.5926 -0.0355 -0.0829 -0.0550 9 SER A N 10 C CA . SER A 9 ? 0.6936 0.5480 0.5222 -0.0295 -0.0779 -0.0549 9 SER A CA 11 C C . SER A 9 ? 0.6121 0.4754 0.4512 -0.0276 -0.0749 -0.0518 9 SER A C 12 O O . SER A 9 ? 0.5677 0.4363 0.4110 -0.0231 -0.0707 -0.0515 9 SER A O 13 C CB . SER A 9 ? 0.7095 0.5708 0.5366 -0.0296 -0.0780 -0.0539 9 SER A CB 14 O OG . SER A 9 ? 0.7161 0.5898 0.5501 -0.0319 -0.0787 -0.0494 9 SER A OG 15 N N . THR A 10 ? 0.5650 0.4296 0.4081 -0.0311 -0.0770 -0.0497 10 THR A N 16 C CA . THR A 10 ? 0.5248 0.3968 0.3774 -0.0295 -0.0744 -0.0470 10 THR A CA 17 C C . THR A 10 ? 0.4987 0.3648 0.3521 -0.0314 -0.0758 -0.0472 10 THR A C 18 O O . THR A 10 ? 0.5036 0.3601 0.3502 -0.0345 -0.0792 -0.0491 10 THR A O 19 C CB . THR A 10 ? 0.5273 0.4119 0.3860 -0.0320 -0.0752 -0.0423 10 THR A CB 20 O OG1 . THR A 10 ? 0.5625 0.4471 0.4187 -0.0384 -0.0802 -0.0409 10 THR A OG1 21 C CG2 . THR A 10 ? 0.5521 0.4433 0.4104 -0.0295 -0.0734 -0.0416 10 THR A CG2 22 N N . ALA A 11 ? 0.4468 0.3182 0.3081 -0.0295 -0.0733 -0.0453 11 ALA A N 23 C CA . ALA A 11 ? 0.4352 0.3029 0.2987 -0.0311 -0.0744 -0.0449 11 ALA A CA 24 C C . ALA A 11 ? 0.4094 0.2881 0.2823 -0.0318 -0.0733 -0.0407 11 ALA A C 25 O O . ALA A 11 ? 0.3937 0.2815 0.2711 -0.0297 -0.0708 -0.0388 11 ALA A O 26 C CB . ALA A 11 ? 0.4299 0.2902 0.2923 -0.0262 -0.0714 -0.0481 11 ALA A CB 27 N N . THR A 12 ? 0.4000 0.2775 0.2753 -0.0347 -0.0752 -0.0393 12 THR A N 28 C CA . THR A 12 ? 0.3860 0.2729 0.2700 -0.0350 -0.0741 -0.0355 12 THR A CA 29 C C . THR A 12 ? 0.3757 0.2581 0.2624 -0.0326 -0.0721 -0.0366 12 THR A C 30 O O . THR A 12 ? 0.3906 0.2631 0.2726 -0.0337 -0.0739 -0.0388 12 THR A O 31 C CB . THR A 12 ? 0.3890 0.2804 0.2739 -0.0414 -0.0784 -0.0322 12 THR A CB 32 O OG1 . THR A 12 ? 0.4017 0.2975 0.2836 -0.0437 -0.0804 -0.0314 12 THR A OG1 33 C CG2 . THR A 12 ? 0.3808 0.2831 0.2748 -0.0415 -0.0772 -0.0279 12 THR A CG2 34 N N . LEU A 13 ? 0.3567 0.2459 0.2504 -0.0292 -0.0684 -0.0351 13 LEU A N 35 C CA . LEU A 13 ? 0.3568 0.2438 0.2542 -0.0272 -0.0666 -0.0356 13 LEU A CA 36 C C . LEU A 13 ? 0.3624 0.2589 0.2677 -0.0282 -0.0659 -0.0315 13 LEU A C 37 O O . LEU A 13 ? 0.3536 0.2580 0.2628 -0.0261 -0.0632 -0.0297 13 LEU A O 38 C CB . LEU A 13 ? 0.3466 0.2318 0.2441 -0.0216 -0.0623 -0.0383 13 LEU A CB 39 C CG . LEU A 13 ? 0.3427 0.2262 0.2438 -0.0190 -0.0601 -0.0390 13 LEU A CG 40 C CD1 . LEU A 13 ? 0.3554 0.2290 0.2519 -0.0202 -0.0627 -0.0409 13 LEU A CD1 41 C CD2 . LEU A 13 ? 0.3392 0.2236 0.2410 -0.0141 -0.0556 -0.0411 13 LEU A CD2 42 N N . CYS A 14 ? 0.3757 0.2706 0.2824 -0.0313 -0.0683 -0.0301 14 CYS A N 43 C CA . CYS A 14 ? 0.3761 0.2792 0.2898 -0.0325 -0.0680 -0.0263 14 CYS A CA 44 C C . CYS A 14 ? 0.3679 0.2690 0.2853 -0.0298 -0.0656 -0.0269 14 CYS A C 45 O O . CYS A 14 ? 0.3559 0.2482 0.2700 -0.0291 -0.0661 -0.0295 14 CYS A O 46 C CB . CYS A 14 ? 0.3945 0.2983 0.3074 -0.0386 -0.0726 -0.0238 14 CYS A CB 47 S SG . CYS A 14 ? 0.4272 0.3355 0.3363 -0.0428 -0.0759 -0.0224 14 CYS A SG 48 N N . LEU A 15 ? 0.3567 0.2658 0.2805 -0.0279 -0.0629 -0.0245 15 LEU A N 49 C CA . LEU A 15 ? 0.3499 0.2589 0.2779 -0.0261 -0.0610 -0.0243 15 LEU A CA 50 C C . LEU A 15 ? 0.3431 0.2568 0.2753 -0.0295 -0.0630 -0.0206 15 LEU A C 51 O O . LEU A 15 ? 0.3457 0.2670 0.2799 -0.0315 -0.0641 -0.0174 15 LEU A O 52 C CB . LEU A 15 ? 0.3678 0.2816 0.2993 -0.0218 -0.0563 -0.0243 15 LEU A CB 53 C CG . LEU A 15 ? 0.3873 0.2955 0.3150 -0.0185 -0.0541 -0.0283 15 LEU A CG 54 C CD1 . LEU A 15 ? 0.4120 0.3203 0.3355 -0.0185 -0.0545 -0.0291 15 LEU A CD1 55 C CD2 . LEU A 15 ? 0.4375 0.3481 0.3684 -0.0150 -0.0499 -0.0289 15 LEU A CD2 56 N N . GLY A 16 ? 0.3279 0.2376 0.2613 -0.0299 -0.0635 -0.0209 16 GLY A N 57 C CA . GLY A 16 ? 0.3286 0.2416 0.2652 -0.0334 -0.0658 -0.0177 16 GLY A CA 58 C C . GLY A 16 ? 0.3266 0.2372 0.2662 -0.0320 -0.0646 -0.0178 16 GLY A C 59 O O . GLY A 16 ? 0.3048 0.2110 0.2437 -0.0283 -0.0622 -0.0206 16 GLY A O 60 N N . HIS A 17 ? 0.3201 0.2340 0.2628 -0.0351 -0.0665 -0.0147 17 HIS A N 61 C CA . HIS A 17 ? 0.3222 0.2342 0.2676 -0.0344 -0.0658 -0.0144 17 HIS A CA 62 C C . HIS A 17 ? 0.3270 0.2364 0.2713 -0.0394 -0.0697 -0.0124 17 HIS A C 63 O O . HIS A 17 ? 0.3449 0.2574 0.2881 -0.0438 -0.0725 -0.0103 17 HIS A O 64 C CB . HIS A 17 ? 0.3113 0.2325 0.2634 -0.0319 -0.0627 -0.0120 17 HIS A CB 65 C CG . HIS A 17 ? 0.3132 0.2442 0.2688 -0.0345 -0.0637 -0.0077 17 HIS A CG 66 N ND1 . HIS A 17 ? 0.3048 0.2381 0.2620 -0.0386 -0.0665 -0.0047 17 HIS A ND1 67 C CD2 . HIS A 17 ? 0.3120 0.2512 0.2696 -0.0331 -0.0621 -0.0058 17 HIS A CD2 68 C CE1 . HIS A 17 ? 0.3085 0.2520 0.2687 -0.0398 -0.0668 -0.0011 17 HIS A CE1 69 N NE2 . HIS A 17 ? 0.3113 0.2582 0.2716 -0.0361 -0.0640 -0.0017 17 HIS A NE2 70 N N . HIS A 18 ? 0.3340 0.2379 0.2782 -0.0390 -0.0699 -0.0130 18 HIS A N 71 C CA . HIS A 18 ? 0.3478 0.2476 0.2900 -0.0438 -0.0734 -0.0113 18 HIS A CA 72 C C . HIS A 18 ? 0.3540 0.2639 0.3018 -0.0471 -0.0744 -0.0066 18 HIS A C 73 O O . HIS A 18 ? 0.3372 0.2571 0.2906 -0.0450 -0.0719 -0.0047 18 HIS A O 74 C CB . HIS A 18 ? 0.3520 0.2425 0.2920 -0.0419 -0.0732 -0.0131 18 HIS A CB 75 C CG . HIS A 18 ? 0.3469 0.2430 0.2935 -0.0391 -0.0706 -0.0116 18 HIS A CG 76 N ND1 . HIS A 18 ? 0.3617 0.2522 0.3077 -0.0385 -0.0710 -0.0119 18 HIS A ND1 77 C CD2 . HIS A 18 ? 0.3370 0.2438 0.2905 -0.0369 -0.0677 -0.0098 18 HIS A CD2 78 C CE1 . HIS A 18 ? 0.3588 0.2565 0.3113 -0.0361 -0.0684 -0.0103 18 HIS A CE1 79 N NE2 . HIS A 18 ? 0.3283 0.2357 0.2852 -0.0352 -0.0664 -0.0091 18 HIS A NE2 80 N N . ALA A 19 ? 0.3700 0.2768 0.3154 -0.0525 -0.0780 -0.0048 19 ALA A N 81 C CA . ALA A 19 ? 0.3878 0.3035 0.3379 -0.0565 -0.0794 -0.0003 19 ALA A CA 82 C C . ALA A 19 ? 0.4178 0.3246 0.3640 -0.0608 -0.0825 0.0001 19 ALA A C 83 O O . ALA A 19 ? 0.4509 0.3453 0.3897 -0.0616 -0.0842 -0.0028 19 ALA A O 84 C CB . ALA A 19 ? 0.3826 0.3068 0.3330 -0.0604 -0.0814 0.0022 19 ALA A CB 85 N N . VAL A 20 ? 0.4338 0.3463 0.3843 -0.0631 -0.0830 0.0037 20 VAL A N 86 C CA . VAL A 20 ? 0.4573 0.3614 0.4042 -0.0669 -0.0856 0.0044 20 VAL A CA 87 C C . VAL A 20 ? 0.4835 0.3949 0.4319 -0.0741 -0.0888 0.0089 20 VAL A C 88 O O . VAL A 20 ? 0.4819 0.4070 0.4361 -0.0745 -0.0881 0.0119 20 VAL A O 89 C CB . VAL A 20 ? 0.4587 0.3612 0.4090 -0.0628 -0.0832 0.0042 20 VAL A CB 90 C CG1 . VAL A 20 ? 0.4576 0.3535 0.4063 -0.0561 -0.0802 -0.0001 20 VAL A CG1 91 C CG2 . VAL A 20 ? 0.4262 0.3428 0.3854 -0.0617 -0.0811 0.0080 20 VAL A CG2 92 N N . PRO A 21 ? 0.5365 0.4389 0.4790 -0.0798 -0.0923 0.0094 21 PRO A N 93 C CA . PRO A 21 ? 0.5572 0.4674 0.5011 -0.0873 -0.0954 0.0139 21 PRO A CA 94 C C . PRO A 21 ? 0.5692 0.4896 0.5208 -0.0870 -0.0941 0.0179 21 PRO A C 95 O O . PRO A 21 ? 0.6155 0.5483 0.5714 -0.0910 -0.0953 0.0222 21 PRO A O 96 C CB . PRO A 21 ? 0.5667 0.4622 0.5008 -0.0935 -0.0994 0.0128 21 PRO A CB 97 C CG . PRO A 21 ? 0.5737 0.4548 0.5034 -0.0882 -0.0978 0.0089 21 PRO A CG 98 C CD . PRO A 21 ? 0.5530 0.4380 0.4869 -0.0800 -0.0937 0.0061 21 PRO A CD 99 N N . ASN A 22 ? 0.5608 0.4767 0.5142 -0.0821 -0.0917 0.0167 22 ASN A N 100 C CA . ASN A 22 ? 0.5709 0.4947 0.5307 -0.0817 -0.0905 0.0203 22 ASN A CA 101 C C . ASN A 22 ? 0.5163 0.4477 0.4832 -0.0740 -0.0859 0.0198 22 ASN A C 102 O O . ASN A 22 ? 0.5150 0.4412 0.4826 -0.0699 -0.0839 0.0182 22 ASN A O 103 C CB . ASN A 22 ? 0.6079 0.5196 0.5633 -0.0836 -0.0919 0.0199 22 ASN A CB 104 C CG . ASN A 22 ? 0.6663 0.5647 0.6172 -0.0777 -0.0902 0.0151 22 ASN A CG 105 O OD1 . ASN A 22 ? 0.7104 0.6054 0.6590 -0.0743 -0.0890 0.0116 22 ASN A OD1 106 N ND2 . ASN A 22 ? 0.6764 0.5677 0.6262 -0.0764 -0.0898 0.0151 22 ASN A ND2 107 N N . GLY A 23 ? 0.4822 0.4258 0.4539 -0.0722 -0.0842 0.0212 23 GLY A N 108 C CA . GLY A 23 ? 0.4673 0.4174 0.4447 -0.0651 -0.0798 0.0208 23 GLY A CA 109 C C . GLY A 23 ? 0.4508 0.4094 0.4342 -0.0646 -0.0786 0.0245 23 GLY A C 110 O O . GLY A 23 ? 0.4350 0.3962 0.4188 -0.0698 -0.0811 0.0278 23 GLY A O 111 N N . THR A 24 ? 0.4091 0.3720 0.3967 -0.0585 -0.0747 0.0240 24 THR A N 112 C CA . THR A 24 ? 0.4009 0.3716 0.3940 -0.0571 -0.0730 0.0272 24 THR A CA 113 C C . THR A 24 ? 0.3494 0.3315 0.3469 -0.0529 -0.0698 0.0289 24 THR A C 114 O O . THR A 24 ? 0.3365 0.3171 0.3331 -0.0489 -0.0676 0.0262 24 THR A O 115 C CB . THR A 24 ? 0.4339 0.3975 0.4272 -0.0535 -0.0711 0.0250 24 THR A CB 116 O OG1 . THR A 24 ? 0.4874 0.4384 0.4754 -0.0557 -0.0734 0.0225 24 THR A OG1 117 C CG2 . THR A 24 ? 0.4428 0.4130 0.4406 -0.0536 -0.0704 0.0286 24 THR A CG2 118 N N . ILE A 25 ? 0.3091 0.3019 0.3111 -0.0535 -0.0694 0.0333 25 ILE A N 119 C CA . ILE A 25 ? 0.3083 0.3119 0.3137 -0.0493 -0.0665 0.0354 25 ILE A CA 120 C C . ILE A 25 ? 0.2756 0.2780 0.2830 -0.0436 -0.0626 0.0342 25 ILE A C 121 O O . ILE A 25 ? 0.2672 0.2676 0.2760 -0.0440 -0.0626 0.0348 25 ILE A O 122 C CB . ILE A 25 ? 0.3179 0.3347 0.3269 -0.0522 -0.0677 0.0411 25 ILE A CB 123 C CG1 . ILE A 25 ? 0.3452 0.3645 0.3522 -0.0583 -0.0717 0.0425 25 ILE A CG1 124 C CG2 . ILE A 25 ? 0.3113 0.3387 0.3233 -0.0467 -0.0642 0.0433 25 ILE A CG2 125 C CD1 . ILE A 25 ? 0.3678 0.3878 0.3726 -0.0566 -0.0713 0.0407 25 ILE A CD1 126 N N . VAL A 26 ? 0.2674 0.2704 0.2743 -0.0386 -0.0594 0.0324 26 VAL A N 127 C CA . VAL A 26 ? 0.2497 0.2521 0.2578 -0.0334 -0.0555 0.0314 26 VAL A CA 128 C C . VAL A 26 ? 0.2491 0.2596 0.2580 -0.0293 -0.0526 0.0334 26 VAL A C 129 O O . VAL A 26 ? 0.2448 0.2611 0.2533 -0.0300 -0.0534 0.0351 26 VAL A O 130 C CB . VAL A 26 ? 0.2381 0.2299 0.2434 -0.0310 -0.0540 0.0262 26 VAL A CB 131 C CG1 . VAL A 26 ? 0.2371 0.2202 0.2408 -0.0342 -0.0567 0.0242 26 VAL A CG1 132 C CG2 . VAL A 26 ? 0.2282 0.2182 0.2305 -0.0294 -0.0531 0.0238 26 VAL A CG2 133 N N . LYS A 27 ? 0.2557 0.2664 0.2653 -0.0251 -0.0492 0.0332 27 LYS A N 134 C CA . LYS A 27 ? 0.2692 0.2856 0.2784 -0.0204 -0.0459 0.0348 27 LYS A CA 135 C C . LYS A 27 ? 0.2655 0.2744 0.2711 -0.0167 -0.0428 0.0307 27 LYS A C 136 O O . LYS A 27 ? 0.2422 0.2439 0.2471 -0.0164 -0.0420 0.0275 27 LYS A O 137 C CB . LYS A 27 ? 0.2994 0.3215 0.3110 -0.0184 -0.0442 0.0380 27 LYS A CB 138 C CG . LYS A 27 ? 0.3374 0.3640 0.3475 -0.0129 -0.0404 0.0397 27 LYS A CG 139 C CD . LYS A 27 ? 0.3734 0.4055 0.3857 -0.0110 -0.0389 0.0429 27 LYS A CD 140 C CE . LYS A 27 ? 0.4032 0.4352 0.4122 -0.0050 -0.0345 0.0431 27 LYS A CE 141 N NZ . LYS A 27 ? 0.4232 0.4612 0.4340 -0.0029 -0.0331 0.0466 27 LYS A NZ 142 N N . THR A 28 ? 0.2657 0.2768 0.2689 -0.0139 -0.0411 0.0310 28 THR A N 143 C CA . THR A 28 ? 0.2814 0.2861 0.2807 -0.0103 -0.0377 0.0277 28 THR A CA 144 C C . THR A 28 ? 0.3001 0.3095 0.2977 -0.0055 -0.0343 0.0304 28 THR A C 145 O O . THR A 28 ? 0.3122 0.3298 0.3120 -0.0047 -0.0345 0.0345 28 THR A O 146 C CB . THR A 28 ? 0.2795 0.2803 0.2761 -0.0111 -0.0386 0.0251 28 THR A CB 147 O OG1 . THR A 28 ? 0.2977 0.3060 0.2942 -0.0107 -0.0394 0.0282 28 THR A OG1 148 C CG2 . THR A 28 ? 0.2835 0.2794 0.2809 -0.0155 -0.0420 0.0227 28 THR A CG2 149 N N . ILE A 29 ? 0.3149 0.3187 0.3081 -0.0022 -0.0311 0.0280 29 ILE A N 150 C CA . ILE A 29 ? 0.3358 0.3422 0.3257 0.0026 -0.0278 0.0302 29 ILE A CA 151 C C . ILE A 29 ? 0.3400 0.3535 0.3295 0.0036 -0.0287 0.0330 29 ILE A C 152 O O . ILE A 29 ? 0.3696 0.3901 0.3588 0.0068 -0.0274 0.0368 29 ILE A O 153 C CB . ILE A 29 ? 0.3526 0.3501 0.3368 0.0054 -0.0242 0.0268 29 ILE A CB 154 C CG1 . ILE A 29 ? 0.3711 0.3625 0.3557 0.0041 -0.0234 0.0240 29 ILE A CG1 155 C CG2 . ILE A 29 ? 0.3728 0.3718 0.3524 0.0107 -0.0207 0.0293 29 ILE A CG2 156 C CD1 . ILE A 29 ? 0.3988 0.3932 0.3844 0.0058 -0.0221 0.0265 29 ILE A CD1 157 N N . THR A 30 ? 0.3495 0.3615 0.3389 0.0009 -0.0310 0.0313 30 THR A N 158 C CA . THR A 30 ? 0.3609 0.3797 0.3499 0.0014 -0.0321 0.0337 30 THR A CA 159 C C . THR A 30 ? 0.3801 0.4098 0.3740 -0.0015 -0.0355 0.0378 30 THR A C 160 O O . THR A 30 ? 0.3587 0.3976 0.3528 0.0003 -0.0355 0.0416 30 THR A O 161 C CB . THR A 30 ? 0.3622 0.3752 0.3491 -0.0007 -0.0335 0.0301 30 THR A CB 162 O OG1 . THR A 30 ? 0.3481 0.3518 0.3305 0.0018 -0.0303 0.0265 30 THR A OG1 163 C CG2 . THR A 30 ? 0.3801 0.4000 0.3661 -0.0003 -0.0348 0.0324 30 THR A CG2 164 N N . ASN A 31 ? 0.3764 0.4051 0.3739 -0.0064 -0.0384 0.0372 31 ASN A N 165 C CA . ASN A 31 ? 0.3863 0.4242 0.3880 -0.0107 -0.0422 0.0408 31 ASN A CA 166 C C . ASN A 31 ? 0.3753 0.4148 0.3805 -0.0125 -0.0429 0.0423 31 ASN A C 167 O O . ASN A 31 ? 0.3510 0.3821 0.3563 -0.0140 -0.0430 0.0392 31 ASN A O 168 C CB . ASN A 31 ? 0.4140 0.4476 0.4155 -0.0161 -0.0460 0.0383 31 ASN A CB 169 C CG . ASN A 31 ? 0.4397 0.4741 0.4383 -0.0154 -0.0462 0.0376 31 ASN A CG 170 O OD1 . ASN A 31 ? 0.4924 0.5369 0.4918 -0.0151 -0.0470 0.0413 31 ASN A OD1 171 N ND2 . ASN A 31 ? 0.4316 0.4560 0.4268 -0.0152 -0.0456 0.0331 31 ASN A ND2 172 N N . ASP A 32 ? 0.3735 0.4242 0.3819 -0.0125 -0.0434 0.0472 32 ASP A N 173 C CA . ASP A 32 ? 0.3841 0.4374 0.3961 -0.0152 -0.0447 0.0491 32 ASP A CA 174 C C . ASP A 32 ? 0.3581 0.4074 0.3716 -0.0221 -0.0490 0.0478 32 ASP A C 175 O O . ASP A 32 ? 0.3344 0.3796 0.3494 -0.0242 -0.0497 0.0471 32 ASP A O 176 C CB . ASP A 32 ? 0.4417 0.5091 0.4567 -0.0141 -0.0447 0.0550 32 ASP A CB 177 C CG . ASP A 32 ? 0.5105 0.5805 0.5236 -0.0068 -0.0402 0.0565 32 ASP A CG 178 O OD1 . ASP A 32 ? 0.5669 0.6272 0.5772 -0.0038 -0.0374 0.0533 32 ASP A OD1 179 O OD2 . ASP A 32 ? 0.5811 0.6626 0.5950 -0.0040 -0.0394 0.0610 32 ASP A OD2 180 N N . GLN A 33 ? 0.3398 0.3897 0.3523 -0.0255 -0.0517 0.0473 33 GLN A N 181 C CA . GLN A 33 ? 0.3510 0.3958 0.3635 -0.0321 -0.0558 0.0458 33 GLN A CA 182 C C . GLN A 33 ? 0.3348 0.3727 0.3435 -0.0329 -0.0567 0.0421 33 GLN A C 183 O O . GLN A 33 ? 0.3518 0.3958 0.3597 -0.0322 -0.0569 0.0435 33 GLN A O 184 C CB . GLN A 33 ? 0.3873 0.4430 0.4026 -0.0374 -0.0592 0.0506 33 GLN A CB 185 C CG . GLN A 33 ? 0.4231 0.4839 0.4420 -0.0381 -0.0591 0.0539 33 GLN A CG 186 C CD . GLN A 33 ? 0.4717 0.5428 0.4933 -0.0443 -0.0627 0.0585 33 GLN A CD 187 O OE1 . GLN A 33 ? 0.5183 0.5934 0.5391 -0.0483 -0.0655 0.0595 33 GLN A OE1 188 N NE2 . GLN A 33 ? 0.5197 0.5953 0.5444 -0.0452 -0.0627 0.0615 33 GLN A NE2 189 N N . ILE A 34 ? 0.3004 0.3261 0.3068 -0.0339 -0.0571 0.0376 34 ILE A N 190 C CA . ILE A 34 ? 0.2973 0.3160 0.3000 -0.0352 -0.0584 0.0340 34 ILE A CA 191 C C . ILE A 34 ? 0.2864 0.2951 0.2874 -0.0395 -0.0612 0.0313 34 ILE A C 192 O O . ILE A 34 ? 0.2660 0.2693 0.2677 -0.0388 -0.0604 0.0300 34 ILE A O 193 C CB . ILE A 34 ? 0.2981 0.3112 0.2981 -0.0297 -0.0547 0.0305 34 ILE A CB 194 C CG1 . ILE A 34 ? 0.3188 0.3254 0.3149 -0.0312 -0.0562 0.0271 34 ILE A CG1 195 C CG2 . ILE A 34 ? 0.2981 0.3036 0.2981 -0.0271 -0.0523 0.0277 34 ILE A CG2 196 C CD1 . ILE A 34 ? 0.3248 0.3281 0.3182 -0.0263 -0.0528 0.0245 34 ILE A CD1 197 N N . GLU A 35 ? 0.2846 0.2909 0.2830 -0.0440 -0.0646 0.0306 35 GLU A N 198 C CA . GLU A 35 ? 0.2958 0.2916 0.2913 -0.0480 -0.0673 0.0281 35 GLU A CA 199 C C . GLU A 35 ? 0.2789 0.2632 0.2707 -0.0450 -0.0659 0.0227 35 GLU A C 200 O O . GLU A 35 ? 0.2826 0.2662 0.2722 -0.0432 -0.0650 0.0209 35 GLU A O 201 C CB . GLU A 35 ? 0.3245 0.3219 0.3180 -0.0548 -0.0718 0.0298 35 GLU A CB 202 C CG . GLU A 35 ? 0.3542 0.3408 0.3442 -0.0595 -0.0749 0.0281 35 GLU A CG 203 C CD . GLU A 35 ? 0.3957 0.3821 0.3823 -0.0664 -0.0792 0.0292 35 GLU A CD 204 O OE1 . GLU A 35 ? 0.4488 0.4468 0.4380 -0.0697 -0.0808 0.0335 35 GLU A OE1 205 O OE2 . GLU A 35 ? 0.4126 0.3876 0.3935 -0.0684 -0.0811 0.0257 35 GLU A OE2 206 N N . VAL A 36 ? 0.2694 0.2454 0.2605 -0.0445 -0.0656 0.0205 36 VAL A N 207 C CA . VAL A 36 ? 0.2732 0.2386 0.2609 -0.0420 -0.0645 0.0156 36 VAL A CA 208 C C . VAL A 36 ? 0.2833 0.2386 0.2670 -0.0457 -0.0677 0.0139 36 VAL A C 209 O O . VAL A 36 ? 0.2953 0.2513 0.2792 -0.0502 -0.0705 0.0165 36 VAL A O 210 C CB . VAL A 36 ? 0.2605 0.2251 0.2505 -0.0370 -0.0608 0.0142 36 VAL A CB 211 C CG1 . VAL A 36 ? 0.2485 0.2205 0.2404 -0.0331 -0.0574 0.0152 36 VAL A CG1 212 C CG2 . VAL A 36 ? 0.2520 0.2177 0.2449 -0.0379 -0.0611 0.0163 36 VAL A CG2 213 N N . THR A 37 ? 0.2900 0.2356 0.2697 -0.0437 -0.0673 0.0096 37 THR A N 214 C CA . THR A 37 ? 0.3065 0.2411 0.2810 -0.0465 -0.0702 0.0076 37 THR A CA 215 C C . THR A 37 ? 0.3180 0.2486 0.2933 -0.0464 -0.0704 0.0081 37 THR A C 216 O O . THR A 37 ? 0.3119 0.2352 0.2833 -0.0500 -0.0733 0.0083 37 THR A O 217 C CB . THR A 37 ? 0.3090 0.2348 0.2786 -0.0437 -0.0694 0.0029 37 THR A CB 218 O OG1 . THR A 37 ? 0.3069 0.2322 0.2785 -0.0383 -0.0659 0.0007 37 THR A OG1 219 C CG2 . THR A 37 ? 0.2944 0.2237 0.2625 -0.0441 -0.0695 0.0025 37 THR A CG2 220 N N . ASN A 38 ? 0.3148 0.2500 0.2946 -0.0426 -0.0673 0.0086 38 ASN A N 221 C CA . ASN A 38 ? 0.3284 0.2601 0.3092 -0.0419 -0.0672 0.0088 38 ASN A CA 222 C C . ASN A 38 ? 0.3058 0.2456 0.2923 -0.0384 -0.0639 0.0102 38 ASN A C 223 O O . ASN A 38 ? 0.2744 0.2193 0.2627 -0.0354 -0.0612 0.0095 38 ASN A O 224 C CB . ASN A 38 ? 0.3681 0.2891 0.3444 -0.0391 -0.0669 0.0047 38 ASN A CB 225 C CG . ASN A 38 ? 0.4110 0.3264 0.3865 -0.0389 -0.0676 0.0049 38 ASN A CG 226 O OD1 . ASN A 38 ? 0.4233 0.3397 0.3997 -0.0424 -0.0695 0.0080 38 ASN A OD1 227 N ND2 . ASN A 38 ? 0.5305 0.4403 0.5042 -0.0346 -0.0660 0.0018 38 ASN A ND2 228 N N . ALA A 39 ? 0.2926 0.2331 0.2813 -0.0389 -0.0641 0.0121 39 ALA A N 229 C CA . ALA A 39 ? 0.2910 0.2383 0.2845 -0.0358 -0.0612 0.0134 39 ALA A CA 230 C C . ALA A 39 ? 0.3011 0.2442 0.2949 -0.0353 -0.0615 0.0135 39 ALA A C 231 O O . ALA A 39 ? 0.2919 0.2276 0.2823 -0.0378 -0.0642 0.0133 39 ALA A O 232 C CB . ALA A 39 ? 0.2787 0.2364 0.2760 -0.0377 -0.0612 0.0178 39 ALA A CB 233 N N . THR A 40 ? 0.2851 0.2323 0.2823 -0.0321 -0.0587 0.0136 40 THR A N 234 C CA . THR A 40 ? 0.2915 0.2364 0.2896 -0.0314 -0.0588 0.0141 40 THR A CA 235 C C . THR A 40 ? 0.2732 0.2267 0.2760 -0.0308 -0.0572 0.0173 40 THR A C 236 O O . THR A 40 ? 0.2650 0.2251 0.2700 -0.0291 -0.0549 0.0179 40 THR A O 237 C CB . THR A 40 ? 0.2974 0.2365 0.2936 -0.0274 -0.0573 0.0102 40 THR A CB 238 O OG1 . THR A 40 ? 0.3309 0.2659 0.3266 -0.0273 -0.0583 0.0107 40 THR A OG1 239 C CG2 . THR A 40 ? 0.3011 0.2457 0.3001 -0.0237 -0.0536 0.0088 40 THR A CG2 240 N N . GLU A 41 ? 0.2710 0.2241 0.2749 -0.0323 -0.0584 0.0195 41 GLU A N 241 C CA . GLU A 41 ? 0.2640 0.2249 0.2719 -0.0321 -0.0573 0.0229 41 GLU A CA 242 C C . GLU A 41 ? 0.2487 0.2108 0.2583 -0.0278 -0.0542 0.0212 41 GLU A C 243 O O . GLU A 41 ? 0.2512 0.2076 0.2594 -0.0261 -0.0541 0.0188 41 GLU A O 244 C CB . GLU A 41 ? 0.2806 0.2400 0.2884 -0.0357 -0.0600 0.0259 41 GLU A CB 245 C CG . GLU A 41 ? 0.2749 0.2421 0.2868 -0.0358 -0.0591 0.0297 41 GLU A CG 246 C CD . GLU A 41 ? 0.2728 0.2502 0.2877 -0.0359 -0.0579 0.0324 41 GLU A CD 247 O OE1 . GLU A 41 ? 0.2802 0.2605 0.2949 -0.0397 -0.0600 0.0347 41 GLU A OE1 248 O OE2 . GLU A 41 ? 0.2433 0.2258 0.2604 -0.0323 -0.0548 0.0324 41 GLU A OE2 249 N N . LEU A 42 ? 0.2243 0.1936 0.2366 -0.0259 -0.0516 0.0224 42 LEU A N 250 C CA . LEU A 42 ? 0.2169 0.1876 0.2303 -0.0224 -0.0487 0.0210 42 LEU A CA 251 C C . LEU A 42 ? 0.2057 0.1811 0.2219 -0.0222 -0.0481 0.0241 42 LEU A C 252 O O . LEU A 42 ? 0.1968 0.1732 0.2136 -0.0196 -0.0459 0.0230 42 LEU A O 253 C CB . LEU A 42 ? 0.2178 0.1916 0.2309 -0.0199 -0.0457 0.0197 42 LEU A CB 254 C CG . LEU A 42 ? 0.2248 0.1942 0.2351 -0.0194 -0.0455 0.0162 42 LEU A CG 255 C CD1 . LEU A 42 ? 0.2232 0.1951 0.2328 -0.0169 -0.0423 0.0150 42 LEU A CD1 256 C CD2 . LEU A 42 ? 0.2271 0.1899 0.2357 -0.0186 -0.0462 0.0128 42 LEU A CD2 257 N N . VAL A 43 ? 0.2016 0.1802 0.2192 -0.0250 -0.0501 0.0278 43 VAL A N 258 C CA . VAL A 43 ? 0.2023 0.1852 0.2224 -0.0251 -0.0498 0.0310 43 VAL A CA 259 C C . VAL A 43 ? 0.2177 0.1958 0.2372 -0.0276 -0.0526 0.0319 43 VAL A C 260 O O . VAL A 43 ? 0.2152 0.1916 0.2337 -0.0314 -0.0554 0.0335 43 VAL A O 261 C CB . VAL A 43 ? 0.1963 0.1880 0.2187 -0.0263 -0.0496 0.0353 43 VAL A CB 262 C CG1 . VAL A 43 ? 0.1955 0.1918 0.2203 -0.0262 -0.0492 0.0385 43 VAL A CG1 263 C CG2 . VAL A 43 ? 0.1912 0.1871 0.2134 -0.0233 -0.0467 0.0346 43 VAL A CG2 264 N N . GLN A 44 ? 0.2245 0.2004 0.2443 -0.0257 -0.0518 0.0309 44 GLN A N 265 C CA . GLN A 44 ? 0.2404 0.2119 0.2594 -0.0274 -0.0541 0.0322 44 GLN A CA 266 C C . GLN A 44 ? 0.2555 0.2332 0.2769 -0.0299 -0.0548 0.0370 44 GLN A C 267 O O . GLN A 44 ? 0.2352 0.2195 0.2592 -0.0280 -0.0527 0.0386 44 GLN A O 268 C CB . GLN A 44 ? 0.2403 0.2089 0.2590 -0.0241 -0.0528 0.0300 44 GLN A CB 269 C CG . GLN A 44 ? 0.2474 0.2102 0.2644 -0.0251 -0.0550 0.0309 44 GLN A CG 270 C CD . GLN A 44 ? 0.2594 0.2130 0.2721 -0.0268 -0.0575 0.0293 44 GLN A CD 271 O OE1 . GLN A 44 ? 0.2782 0.2286 0.2890 -0.0253 -0.0570 0.0260 44 GLN A OE1 272 N NE2 . GLN A 44 ? 0.2656 0.2143 0.2760 -0.0299 -0.0602 0.0316 44 GLN A NE2 273 N N . SER A 45 ? 0.2632 0.2388 0.2835 -0.0343 -0.0578 0.0394 45 SER A N 274 C CA . SER A 45 ? 0.3032 0.2857 0.3259 -0.0372 -0.0587 0.0442 45 SER A CA 275 C C . SER A 45 ? 0.3300 0.3077 0.3513 -0.0401 -0.0610 0.0463 45 SER A C 276 O O . SER A 45 ? 0.3510 0.3345 0.3743 -0.0427 -0.0617 0.0505 45 SER A O 277 C CB . SER A 45 ? 0.3140 0.3018 0.3373 -0.0408 -0.0600 0.0466 45 SER A CB 278 O OG . SER A 45 ? 0.3550 0.3348 0.3745 -0.0442 -0.0628 0.0451 45 SER A OG 279 N N . SER A 46 ? 0.3515 0.3191 0.3692 -0.0393 -0.0620 0.0436 46 SER A N 280 C CA . SER A 46 ? 0.3940 0.3559 0.4094 -0.0414 -0.0641 0.0455 46 SER A CA 281 C C . SER A 46 ? 0.4034 0.3613 0.4183 -0.0369 -0.0627 0.0433 46 SER A C 282 O O . SER A 46 ? 0.3633 0.3201 0.3781 -0.0328 -0.0608 0.0396 46 SER A O 283 C CB . SER A 46 ? 0.4140 0.3656 0.4239 -0.0452 -0.0672 0.0447 46 SER A CB 284 O OG . SER A 46 ? 0.4319 0.3757 0.4386 -0.0418 -0.0667 0.0401 46 SER A OG 285 N N . SER A 47 ? 0.4317 0.3878 0.4460 -0.0378 -0.0636 0.0458 47 SER A N 286 C CA . SER A 47 ? 0.4414 0.3923 0.4541 -0.0341 -0.0631 0.0443 47 SER A CA 287 C C . SER A 47 ? 0.4971 0.4374 0.5044 -0.0369 -0.0660 0.0456 47 SER A C 288 O O . SER A 47 ? 0.4709 0.4107 0.4771 -0.0421 -0.0680 0.0488 47 SER A O 289 C CB . SER A 47 ? 0.4502 0.4093 0.4671 -0.0321 -0.0611 0.0464 47 SER A CB 290 O OG . SER A 47 ? 0.4478 0.4020 0.4629 -0.0291 -0.0610 0.0455 47 SER A OG 291 N N . THR A 48 ? 0.5406 0.4728 0.5444 -0.0333 -0.0660 0.0433 48 THR A N 292 C CA . THR A 48 ? 0.5867 0.5083 0.5848 -0.0346 -0.0682 0.0446 48 THR A CA 293 C C . THR A 48 ? 0.5823 0.5077 0.5821 -0.0371 -0.0687 0.0491 48 THR A C 294 O O . THR A 48 ? 0.6187 0.5367 0.6140 -0.0409 -0.0711 0.0516 48 THR A O 295 C CB . THR A 48 ? 0.6059 0.5217 0.6013 -0.0286 -0.0673 0.0417 48 THR A CB 296 O OG1 . THR A 48 ? 0.6816 0.5954 0.6760 -0.0255 -0.0664 0.0374 48 THR A OG1 297 C CG2 . THR A 48 ? 0.6503 0.5534 0.6385 -0.0292 -0.0695 0.0428 48 THR A CG2 298 N N . GLY A 49 ? 0.5428 0.4793 0.5487 -0.0349 -0.0664 0.0501 49 GLY A N 299 C CA . GLY A 49 ? 0.5137 0.4552 0.5217 -0.0367 -0.0665 0.0542 49 GLY A CA 300 C C . GLY A 49 ? 0.4837 0.4230 0.4910 -0.0323 -0.0656 0.0538 49 GLY A C 301 O O . GLY A 49 ? 0.5052 0.4493 0.5147 -0.0329 -0.0652 0.0570 49 GLY A O 302 N N . GLY A 50 ? 0.4114 0.3441 0.4157 -0.0278 -0.0652 0.0501 50 GLY A N 303 C CA . GLY A 50 ? 0.3657 0.2981 0.3698 -0.0228 -0.0640 0.0494 50 GLY A CA 304 C C . GLY A 50 ? 0.3260 0.2652 0.3337 -0.0178 -0.0614 0.0459 50 GLY A C 305 O O . GLY A 50 ? 0.2994 0.2391 0.3075 -0.0171 -0.0607 0.0428 50 GLY A O 306 N N . ILE A 51 ? 0.2999 0.2445 0.3100 -0.0147 -0.0600 0.0463 51 ILE A N 307 C CA . ILE A 51 ? 0.2939 0.2444 0.3066 -0.0101 -0.0576 0.0431 51 ILE A CA 308 C C . ILE A 51 ? 0.3060 0.2497 0.3146 -0.0058 -0.0581 0.0406 51 ILE A C 309 O O . ILE A 51 ? 0.3145 0.2544 0.3206 -0.0040 -0.0589 0.0422 51 ILE A O 310 C CB . ILE A 51 ? 0.2824 0.2421 0.2991 -0.0090 -0.0559 0.0447 51 ILE A CB 311 C CG1 . ILE A 51 ? 0.2850 0.2522 0.3055 -0.0122 -0.0550 0.0467 51 ILE A CG1 312 C CG2 . ILE A 51 ? 0.2903 0.2552 0.3086 -0.0046 -0.0538 0.0414 51 ILE A CG2 313 C CD1 . ILE A 51 ? 0.2775 0.2525 0.3010 -0.0115 -0.0535 0.0490 51 ILE A CD1 314 N N . CYS A 52 ? 0.2986 0.2409 0.3063 -0.0038 -0.0575 0.0369 52 CYS A N 315 C CA . CYS A 52 ? 0.3186 0.2557 0.3226 0.0008 -0.0576 0.0344 52 CYS A CA 316 C C . CYS A 52 ? 0.3054 0.2500 0.3120 0.0051 -0.0559 0.0336 52 CYS A C 317 O O . CYS A 52 ? 0.2782 0.2323 0.2893 0.0050 -0.0540 0.0326 52 CYS A O 318 C CB . CYS A 52 ? 0.3409 0.2761 0.3439 0.0015 -0.0572 0.0308 52 CYS A CB 319 S SG . CYS A 52 ? 0.3726 0.2969 0.3709 -0.0029 -0.0596 0.0314 52 CYS A SG 320 N N . ASP A 53 ? 0.3064 0.2465 0.3094 0.0087 -0.0567 0.0342 53 ASP A N 321 C CA . ASP A 53 ? 0.3111 0.2585 0.3162 0.0128 -0.0554 0.0338 53 ASP A CA 322 C C . ASP A 53 ? 0.2986 0.2513 0.3048 0.0166 -0.0538 0.0300 53 ASP A C 323 O O . ASP A 53 ? 0.3096 0.2697 0.3176 0.0198 -0.0527 0.0295 53 ASP A O 324 C CB . ASP A 53 ? 0.3266 0.2675 0.3272 0.0158 -0.0567 0.0360 53 ASP A CB 325 C CG . ASP A 53 ? 0.3449 0.2754 0.3390 0.0195 -0.0577 0.0344 53 ASP A CG 326 O OD1 . ASP A 53 ? 0.3506 0.2794 0.3438 0.0201 -0.0574 0.0315 53 ASP A OD1 327 O OD2 . ASP A 53 ? 0.3855 0.3090 0.3749 0.0220 -0.0588 0.0363 53 ASP A OD2 328 N N . SER A 54 ? 0.2946 0.2438 0.2993 0.0163 -0.0538 0.0275 54 SER A N 329 C CA . SER A 54 ? 0.2848 0.2394 0.2907 0.0193 -0.0523 0.0239 54 SER A CA 330 C C . SER A 54 ? 0.2802 0.2375 0.2887 0.0156 -0.0513 0.0221 54 SER A C 331 O O . SER A 54 ? 0.2755 0.2272 0.2830 0.0119 -0.0524 0.0232 54 SER A O 332 C CB . SER A 54 ? 0.3031 0.2496 0.3034 0.0236 -0.0531 0.0225 54 SER A CB 333 O OG . SER A 54 ? 0.3060 0.2480 0.3028 0.0270 -0.0542 0.0245 54 SER A OG 334 N N . PRO A 55 ? 0.2662 0.2320 0.2776 0.0165 -0.0494 0.0194 55 PRO A N 335 C CA . PRO A 55 ? 0.2699 0.2435 0.2826 0.0203 -0.0481 0.0179 55 PRO A CA 336 C C . PRO A 55 ? 0.2656 0.2486 0.2821 0.0192 -0.0469 0.0190 55 PRO A C 337 O O . PRO A 55 ? 0.2692 0.2601 0.2870 0.0216 -0.0458 0.0176 55 PRO A O 338 C CB . PRO A 55 ? 0.2696 0.2465 0.2829 0.0204 -0.0467 0.0145 55 PRO A CB 339 C CG . PRO A 55 ? 0.2633 0.2394 0.2783 0.0155 -0.0463 0.0147 55 PRO A CG 340 C CD . PRO A 55 ? 0.2636 0.2316 0.2769 0.0133 -0.0483 0.0177 55 PRO A CD 341 N N . HIS A 56 ? 0.2466 0.2293 0.2647 0.0154 -0.0470 0.0212 56 HIS A N 342 C CA . HIS A 56 ? 0.2416 0.2321 0.2626 0.0143 -0.0459 0.0223 56 HIS A CA 343 C C . HIS A 56 ? 0.2442 0.2338 0.2643 0.0162 -0.0470 0.0251 56 HIS A C 344 O O . HIS A 56 ? 0.2496 0.2311 0.2672 0.0165 -0.0488 0.0272 56 HIS A O 345 C CB . HIS A 56 ? 0.2376 0.2285 0.2603 0.0100 -0.0452 0.0236 56 HIS A CB 346 C CG . HIS A 56 ? 0.2353 0.2258 0.2582 0.0081 -0.0442 0.0212 56 HIS A CG 347 N ND1 . HIS A 56 ? 0.2360 0.2321 0.2597 0.0082 -0.0424 0.0183 56 HIS A ND1 348 C CD2 . HIS A 56 ? 0.2336 0.2186 0.2557 0.0058 -0.0449 0.0215 56 HIS A CD2 349 C CE1 . HIS A 56 ? 0.2384 0.2321 0.2617 0.0063 -0.0419 0.0169 56 HIS A CE1 350 N NE2 . HIS A 56 ? 0.2347 0.2220 0.2572 0.0050 -0.0434 0.0188 56 HIS A NE2 351 N N . GLN A 57 ? 0.2372 0.2348 0.2592 0.0173 -0.0460 0.0253 57 GLN A N 352 C CA . GLN A 57 ? 0.2396 0.2374 0.2611 0.0191 -0.0469 0.0280 57 GLN A CA 353 C C . GLN A 57 ? 0.2331 0.2294 0.2556 0.0157 -0.0472 0.0311 57 GLN A C 354 O O . GLN A 57 ? 0.2176 0.2197 0.2423 0.0134 -0.0459 0.0312 57 GLN A O 355 C CB . GLN A 57 ? 0.2385 0.2461 0.2615 0.0213 -0.0459 0.0272 57 GLN A CB 356 C CG . GLN A 57 ? 0.2413 0.2491 0.2636 0.0235 -0.0469 0.0302 57 GLN A CG 357 C CD . GLN A 57 ? 0.2381 0.2559 0.2616 0.0259 -0.0461 0.0295 57 GLN A CD 358 O OE1 . GLN A 57 ? 0.2429 0.2685 0.2684 0.0242 -0.0447 0.0274 57 GLN A OE1 359 N NE2 . GLN A 57 ? 0.2313 0.2489 0.2534 0.0296 -0.0471 0.0314 57 GLN A NE2 360 N N . ILE A 58 ? 0.2481 0.2365 0.2685 0.0153 -0.0490 0.0338 58 ILE A N 361 C CA . ILE A 58 ? 0.2519 0.2388 0.2730 0.0119 -0.0494 0.0371 58 ILE A CA 362 C C . ILE A 58 ? 0.2715 0.2603 0.2924 0.0134 -0.0499 0.0399 58 ILE A C 363 O O . ILE A 58 ? 0.2806 0.2665 0.2991 0.0169 -0.0508 0.0403 58 ILE A O 364 C CB . ILE A 58 ? 0.2680 0.2450 0.2865 0.0098 -0.0513 0.0387 58 ILE A CB 365 C CG1 . ILE A 58 ? 0.2742 0.2486 0.2924 0.0085 -0.0511 0.0360 58 ILE A CG1 366 C CG2 . ILE A 58 ? 0.2717 0.2488 0.2914 0.0059 -0.0518 0.0425 58 ILE A CG2 367 C CD1 . ILE A 58 ? 0.2799 0.2608 0.3014 0.0062 -0.0492 0.0345 58 ILE A CD1 368 N N . LEU A 59 ? 0.2635 0.2573 0.2867 0.0112 -0.0491 0.0419 59 LEU A N 369 C CA . LEU A 59 ? 0.2738 0.2688 0.2968 0.0121 -0.0496 0.0450 59 LEU A CA 370 C C . LEU A 59 ? 0.2676 0.2599 0.2909 0.0083 -0.0502 0.0486 59 LEU A C 371 O O . LEU A 59 ? 0.2636 0.2605 0.2893 0.0058 -0.0490 0.0489 59 LEU A O 372 C CB . LEU A 59 ? 0.2691 0.2735 0.2941 0.0132 -0.0480 0.0443 59 LEU A CB 373 C CG . LEU A 59 ? 0.2805 0.2871 0.3052 0.0146 -0.0484 0.0473 59 LEU A CG 374 C CD1 . LEU A 59 ? 0.3033 0.3028 0.3248 0.0173 -0.0503 0.0491 59 LEU A CD1 375 C CD2 . LEU A 59 ? 0.2669 0.2827 0.2929 0.0163 -0.0471 0.0457 59 LEU A CD2 376 N N . ASP A 60 ? 0.2684 0.2532 0.2890 0.0079 -0.0521 0.0512 60 ASP A N 377 C CA . ASP A 60 ? 0.2764 0.2588 0.2971 0.0039 -0.0530 0.0551 60 ASP A CA 378 C C . ASP A 60 ? 0.2841 0.2716 0.3059 0.0042 -0.0525 0.0580 60 ASP A C 379 O O . ASP A 60 ? 0.2910 0.2765 0.3108 0.0068 -0.0532 0.0592 60 ASP A O 380 C CB . ASP A 60 ? 0.2938 0.2651 0.3100 0.0029 -0.0553 0.0567 60 ASP A CB 381 C CG . ASP A 60 ? 0.2939 0.2628 0.3100 -0.0020 -0.0564 0.0606 60 ASP A CG 382 O OD1 . ASP A 60 ? 0.2921 0.2684 0.3116 -0.0040 -0.0554 0.0627 60 ASP A OD1 383 O OD2 . ASP A 60 ? 0.3061 0.2657 0.3183 -0.0040 -0.0583 0.0615 60 ASP A OD2 384 N N . GLY A 61 ? 0.2761 0.2702 0.3009 0.0019 -0.0512 0.0594 61 GLY A N 385 C CA . GLY A 61 ? 0.2904 0.2901 0.3164 0.0023 -0.0505 0.0621 61 GLY A CA 386 C C . GLY A 61 ? 0.3087 0.3041 0.3330 0.0006 -0.0521 0.0666 61 GLY A C 387 O O . GLY A 61 ? 0.3140 0.3126 0.3383 0.0017 -0.0518 0.0688 61 GLY A O 388 N N . GLU A 62 ? 0.3227 0.3108 0.3450 -0.0022 -0.0538 0.0680 62 GLU A N 389 C CA . GLU A 62 ? 0.3577 0.3410 0.3777 -0.0047 -0.0555 0.0723 62 GLU A CA 390 C C . GLU A 62 ? 0.3530 0.3442 0.3759 -0.0067 -0.0545 0.0760 62 GLU A C 391 O O . GLU A 62 ? 0.3388 0.3355 0.3646 -0.0091 -0.0535 0.0764 62 GLU A O 392 C CB . GLU A 62 ? 0.3952 0.3716 0.4110 -0.0014 -0.0567 0.0726 62 GLU A CB 393 C CG . GLU A 62 ? 0.4367 0.4061 0.4496 0.0011 -0.0574 0.0688 62 GLU A CG 394 C CD . GLU A 62 ? 0.4982 0.4588 0.5057 0.0044 -0.0587 0.0694 62 GLU A CD 395 O OE1 . GLU A 62 ? 0.5335 0.4977 0.5410 0.0089 -0.0580 0.0686 62 GLU A OE1 396 O OE2 . GLU A 62 ? 0.5594 0.5092 0.5621 0.0025 -0.0605 0.0705 62 GLU A OE2 397 N N . ASN A 63 ? 0.3552 0.3474 0.3772 -0.0056 -0.0546 0.0787 63 ASN A N 398 C CA . ASN A 63 ? 0.3692 0.3693 0.3938 -0.0073 -0.0536 0.0822 63 ASN A CA 399 C C . ASN A 63 ? 0.3417 0.3512 0.3692 -0.0044 -0.0511 0.0804 63 ASN A C 400 O O . ASN A 63 ? 0.3240 0.3402 0.3532 -0.0051 -0.0499 0.0830 63 ASN A O 401 C CB . ASN A 63 ? 0.4232 0.4206 0.4454 -0.0075 -0.0547 0.0862 63 ASN A CB 402 C CG . ASN A 63 ? 0.4711 0.4601 0.4901 -0.0119 -0.0569 0.0893 63 ASN A CG 403 O OD1 . ASN A 63 ? 0.4732 0.4625 0.4934 -0.0160 -0.0574 0.0901 63 ASN A OD1 404 N ND2 . ASN A 63 ? 0.5419 0.5233 0.5566 -0.0110 -0.0584 0.0910 63 ASN A ND2 405 N N . CYS A 64 ? 0.3335 0.3433 0.3611 -0.0014 -0.0503 0.0759 64 CYS A N 406 C CA . CYS A 64 ? 0.3168 0.3342 0.3459 0.0011 -0.0482 0.0737 64 CYS A CA 407 C C . CYS A 64 ? 0.3025 0.3231 0.3333 0.0005 -0.0465 0.0706 64 CYS A C 408 O O . CYS A 64 ? 0.2783 0.2951 0.3089 0.0003 -0.0470 0.0678 64 CYS A O 409 C CB . CYS A 64 ? 0.3523 0.3688 0.3800 0.0049 -0.0484 0.0709 64 CYS A CB 410 S SG . CYS A 64 ? 0.3895 0.4030 0.4146 0.0068 -0.0499 0.0743 64 CYS A SG 411 N N . THR A 65 ? 0.2780 0.3054 0.3101 0.0006 -0.0445 0.0711 65 THR A N 412 C CA . THR A 65 ? 0.2705 0.3007 0.3030 0.0010 -0.0426 0.0678 65 THR A CA 413 C C . THR A 65 ? 0.2646 0.2957 0.2960 0.0036 -0.0420 0.0639 65 THR A C 414 O O . THR A 65 ? 0.2661 0.2975 0.2968 0.0054 -0.0428 0.0643 65 THR A O 415 C CB . THR A 65 ? 0.2672 0.3036 0.3002 0.0009 -0.0405 0.0696 65 THR A CB 416 O OG1 . THR A 65 ? 0.2582 0.2981 0.2903 0.0026 -0.0399 0.0708 65 THR A OG1 417 C CG2 . THR A 65 ? 0.2773 0.3149 0.3118 -0.0016 -0.0409 0.0740 65 THR A CG2 418 N N . LEU A 66 ? 0.2473 0.2792 0.2786 0.0037 -0.0407 0.0602 66 LEU A N 419 C CA . LEU A 66 ? 0.2408 0.2747 0.2709 0.0056 -0.0400 0.0564 66 LEU A CA 420 C C . LEU A 66 ? 0.2468 0.2859 0.2760 0.0067 -0.0389 0.0573 66 LEU A C 421 O O . LEU A 66 ? 0.2363 0.2773 0.2648 0.0084 -0.0394 0.0562 66 LEU A O 422 C CB . LEU A 66 ? 0.2310 0.2649 0.2606 0.0048 -0.0385 0.0527 66 LEU A CB 423 C CG . LEU A 66 ? 0.2267 0.2632 0.2549 0.0059 -0.0376 0.0487 66 LEU A CG 424 C CD1 . LEU A 66 ? 0.2295 0.2656 0.2582 0.0077 -0.0394 0.0479 66 LEU A CD1 425 C CD2 . LEU A 66 ? 0.2140 0.2494 0.2414 0.0047 -0.0362 0.0453 66 LEU A CD2 426 N N . ILE A 67 ? 0.2554 0.2971 0.2841 0.0060 -0.0373 0.0592 67 ILE A N 427 C CA . ILE A 67 ? 0.2604 0.3066 0.2874 0.0071 -0.0361 0.0598 67 ILE A CA 428 C C . ILE A 67 ? 0.2676 0.3147 0.2953 0.0082 -0.0376 0.0629 67 ILE A C 429 O O . ILE A 67 ? 0.2746 0.3247 0.3012 0.0096 -0.0376 0.0621 67 ILE A O 430 C CB . ILE A 67 ? 0.2758 0.3242 0.3017 0.0067 -0.0339 0.0615 67 ILE A CB 431 C CG1 . ILE A 67 ? 0.2805 0.3277 0.3045 0.0062 -0.0321 0.0582 67 ILE A CG1 432 C CG2 . ILE A 67 ? 0.2739 0.3264 0.2978 0.0080 -0.0328 0.0628 67 ILE A CG2 433 C CD1 . ILE A 67 ? 0.2833 0.3306 0.3050 0.0064 -0.0315 0.0537 67 ILE A CD1 434 N N . ASP A 68 ? 0.2733 0.3176 0.3025 0.0073 -0.0392 0.0663 68 ASP A N 435 C CA . ASP A 68 ? 0.2826 0.3265 0.3117 0.0084 -0.0407 0.0692 68 ASP A CA 436 C C . ASP A 68 ? 0.2805 0.3228 0.3091 0.0104 -0.0421 0.0669 68 ASP A C 437 O O . ASP A 68 ? 0.2780 0.3225 0.3056 0.0123 -0.0425 0.0677 68 ASP A O 438 C CB . ASP A 68 ? 0.2876 0.3280 0.3177 0.0065 -0.0422 0.0734 68 ASP A CB 439 C CG . ASP A 68 ? 0.2988 0.3435 0.3296 0.0053 -0.0410 0.0771 68 ASP A CG 440 O OD1 . ASP A 68 ? 0.3252 0.3748 0.3551 0.0065 -0.0392 0.0769 68 ASP A OD1 441 O OD2 . ASP A 68 ? 0.3218 0.3649 0.3535 0.0030 -0.0419 0.0805 68 ASP A OD2 442 N N . ALA A 69 ? 0.2746 0.3133 0.3034 0.0103 -0.0427 0.0640 69 ALA A N 443 C CA . ALA A 69 ? 0.2757 0.3136 0.3038 0.0126 -0.0437 0.0615 69 ALA A CA 444 C C . ALA A 69 ? 0.2699 0.3144 0.2975 0.0139 -0.0424 0.0586 69 ALA A C 445 O O . ALA A 69 ? 0.2681 0.3150 0.2951 0.0163 -0.0432 0.0580 69 ALA A O 446 C CB . ALA A 69 ? 0.2797 0.3126 0.3080 0.0122 -0.0444 0.0591 69 ALA A CB 447 N N . LEU A 70 ? 0.2598 0.3073 0.2871 0.0123 -0.0406 0.0569 70 LEU A N 448 C CA . LEU A 70 ? 0.2567 0.3097 0.2825 0.0126 -0.0393 0.0542 70 LEU A CA 449 C C . LEU A 70 ? 0.2746 0.3321 0.2995 0.0138 -0.0393 0.0564 70 LEU A C 450 O O . LEU A 70 ? 0.2785 0.3403 0.3026 0.0151 -0.0396 0.0551 70 LEU A O 451 C CB . LEU A 70 ? 0.2527 0.3059 0.2773 0.0105 -0.0372 0.0523 70 LEU A CB 452 C CG . LEU A 70 ? 0.2502 0.3077 0.2721 0.0098 -0.0356 0.0493 70 LEU A CG 453 C CD1 . LEU A 70 ? 0.2486 0.3075 0.2703 0.0095 -0.0359 0.0453 70 LEU A CD1 454 C CD2 . LEU A 70 ? 0.2446 0.3006 0.2641 0.0083 -0.0334 0.0491 70 LEU A CD2 455 N N . LEU A 71 ? 0.2837 0.3405 0.3084 0.0132 -0.0388 0.0598 71 LEU A N 456 C CA . LEU A 71 ? 0.2948 0.3555 0.3184 0.0142 -0.0385 0.0622 71 LEU A CA 457 C C . LEU A 71 ? 0.3006 0.3612 0.3249 0.0163 -0.0405 0.0643 71 LEU A C 458 O O . LEU A 71 ? 0.3049 0.3698 0.3281 0.0179 -0.0407 0.0647 71 LEU A O 459 C CB . LEU A 71 ? 0.2993 0.3596 0.3228 0.0132 -0.0375 0.0656 71 LEU A CB 460 C CG . LEU A 71 ? 0.3064 0.3666 0.3287 0.0117 -0.0353 0.0641 71 LEU A CG 461 C CD1 . LEU A 71 ? 0.3149 0.3758 0.3372 0.0114 -0.0343 0.0681 71 LEU A CD1 462 C CD2 . LEU A 71 ? 0.3034 0.3666 0.3223 0.0117 -0.0337 0.0606 71 LEU A CD2 463 N N . GLY A 72 ? 0.2962 0.3512 0.3216 0.0165 -0.0420 0.0657 72 GLY A N 464 C CA . GLY A 72 ? 0.3082 0.3613 0.3333 0.0189 -0.0439 0.0677 72 GLY A CA 465 C C . GLY A 72 ? 0.3288 0.3789 0.3537 0.0184 -0.0446 0.0726 72 GLY A C 466 O O . GLY A 72 ? 0.3224 0.3734 0.3461 0.0203 -0.0454 0.0749 72 GLY A O 467 N N . ASP A 73 ? 0.3350 0.3818 0.3608 0.0157 -0.0443 0.0743 73 ASP A N 468 C CA . ASP A 73 ? 0.3510 0.3941 0.3766 0.0143 -0.0453 0.0790 73 ASP A CA 469 C C . ASP A 73 ? 0.3628 0.3993 0.3866 0.0160 -0.0474 0.0800 73 ASP A C 470 O O . ASP A 73 ? 0.3578 0.3903 0.3812 0.0168 -0.0482 0.0773 73 ASP A O 471 C CB . ASP A 73 ? 0.3600 0.4009 0.3871 0.0110 -0.0449 0.0797 73 ASP A CB 472 C CG . ASP A 73 ? 0.3841 0.4221 0.4112 0.0086 -0.0459 0.0847 73 ASP A CG 473 O OD1 . ASP A 73 ? 0.4469 0.4795 0.4723 0.0089 -0.0476 0.0866 73 ASP A OD1 474 O OD2 . ASP A 73 ? 0.3758 0.4168 0.4043 0.0063 -0.0448 0.0866 73 ASP A OD2 475 N N . PRO A 74 ? 0.4005 0.4357 0.4227 0.0169 -0.0483 0.0837 74 PRO A N 476 C CA . PRO A 74 ? 0.4059 0.4343 0.4252 0.0193 -0.0502 0.0848 74 PRO A CA 477 C C . PRO A 74 ? 0.4172 0.4364 0.4352 0.0181 -0.0516 0.0841 74 PRO A C 478 O O . PRO A 74 ? 0.4381 0.4531 0.4540 0.0211 -0.0525 0.0822 74 PRO A O 479 C CB . PRO A 74 ? 0.4324 0.4598 0.4503 0.0186 -0.0507 0.0898 74 PRO A CB 480 C CG . PRO A 74 ? 0.4256 0.4623 0.4455 0.0182 -0.0489 0.0902 74 PRO A CG 481 C CD . PRO A 74 ? 0.4168 0.4571 0.4393 0.0163 -0.0474 0.0870 74 PRO A CD 482 N N . GLN A 75 ? 0.4217 0.4381 0.4407 0.0139 -0.0516 0.0854 75 GLN A N 483 C CA . GLN A 75 ? 0.4351 0.4425 0.4525 0.0123 -0.0530 0.0847 75 GLN A CA 484 C C . GLN A 75 ? 0.4064 0.4141 0.4248 0.0137 -0.0525 0.0798 75 GLN A C 485 O O . GLN A 75 ? 0.4108 0.4108 0.4272 0.0135 -0.0537 0.0786 75 GLN A O 486 C CB . GLN A 75 ? 0.4591 0.4645 0.4774 0.0071 -0.0533 0.0876 75 GLN A CB 487 C CG . GLN A 75 ? 0.4747 0.4878 0.4970 0.0049 -0.0515 0.0865 75 GLN A CG 488 C CD . GLN A 75 ? 0.5103 0.5234 0.5336 0.0001 -0.0518 0.0902 75 GLN A CD 489 O OE1 . GLN A 75 ? 0.5495 0.5556 0.5704 -0.0023 -0.0536 0.0930 75 GLN A OE1 490 N NE2 . GLN A 75 ? 0.4877 0.5087 0.5142 -0.0010 -0.0500 0.0904 75 GLN A NE2 491 N N . CYS A 76 ? 0.3685 0.3847 0.3895 0.0152 -0.0509 0.0769 76 CYS A N 492 C CA . CYS A 76 ? 0.3603 0.3780 0.3823 0.0163 -0.0503 0.0722 76 CYS A CA 493 C C . CYS A 76 ? 0.3476 0.3681 0.3686 0.0208 -0.0504 0.0697 76 CYS A C 494 O O . CYS A 76 ? 0.3276 0.3510 0.3496 0.0218 -0.0498 0.0659 76 CYS A O 495 C CB . CYS A 76 ? 0.3564 0.3813 0.3813 0.0142 -0.0483 0.0705 76 CYS A CB 496 S SG . CYS A 76 ? 0.3665 0.3911 0.3929 0.0097 -0.0478 0.0739 76 CYS A SG 497 N N . ASP A 77 ? 0.3436 0.3635 0.3625 0.0236 -0.0512 0.0721 77 ASP A N 498 C CA . ASP A 77 ? 0.3462 0.3705 0.3643 0.0282 -0.0513 0.0702 77 ASP A CA 499 C C . ASP A 77 ? 0.3317 0.3522 0.3487 0.0306 -0.0519 0.0671 77 ASP A C 500 O O . ASP A 77 ? 0.3253 0.3521 0.3431 0.0333 -0.0514 0.0642 77 ASP A O 501 C CB . ASP A 77 ? 0.3687 0.3912 0.3840 0.0312 -0.0523 0.0737 77 ASP A CB 502 C CG . ASP A 77 ? 0.3881 0.4173 0.4047 0.0301 -0.0515 0.0760 77 ASP A CG 503 O OD1 . ASP A 77 ? 0.3841 0.4203 0.4034 0.0278 -0.0500 0.0745 77 ASP A OD1 504 O OD2 . ASP A 77 ? 0.4029 0.4301 0.4172 0.0317 -0.0523 0.0794 77 ASP A OD2 505 N N . GLY A 78 ? 0.3266 0.3370 0.3414 0.0294 -0.0529 0.0678 78 GLY A N 506 C CA . GLY A 78 ? 0.3367 0.3421 0.3498 0.0316 -0.0535 0.0651 78 GLY A CA 507 C C . GLY A 78 ? 0.3214 0.3326 0.3377 0.0304 -0.0522 0.0608 78 GLY A C 508 O O . GLY A 78 ? 0.3261 0.3365 0.3415 0.0331 -0.0523 0.0581 78 GLY A O 509 N N . PHE A 79 ? 0.3172 0.3343 0.3368 0.0267 -0.0509 0.0603 79 PHE A N 510 C CA . PHE A 79 ? 0.3215 0.3432 0.3436 0.0250 -0.0496 0.0565 79 PHE A CA 511 C C . PHE A 79 ? 0.2994 0.3312 0.3229 0.0269 -0.0485 0.0539 79 PHE A C 512 O O . PHE A 79 ? 0.2743 0.3098 0.2993 0.0256 -0.0475 0.0505 79 PHE A O 513 C CB . PHE A 79 ? 0.3445 0.3671 0.3687 0.0204 -0.0486 0.0572 79 PHE A CB 514 C CG . PHE A 79 ? 0.3778 0.3920 0.4012 0.0177 -0.0495 0.0590 79 PHE A CG 515 C CD1 . PHE A 79 ? 0.3910 0.4012 0.4133 0.0162 -0.0505 0.0632 79 PHE A CD1 516 C CD2 . PHE A 79 ? 0.4134 0.4241 0.4371 0.0161 -0.0495 0.0567 79 PHE A CD2 517 C CE1 . PHE A 79 ? 0.3967 0.3999 0.4182 0.0130 -0.0515 0.0650 79 PHE A CE1 518 C CE2 . PHE A 79 ? 0.4296 0.4330 0.4525 0.0132 -0.0505 0.0584 79 PHE A CE2 519 C CZ . PHE A 79 ? 0.4028 0.4027 0.4246 0.0115 -0.0515 0.0626 79 PHE A CZ 520 N N . GLN A 80 ? 0.2835 0.3200 0.3065 0.0295 -0.0488 0.0554 80 GLN A N 521 C CA . GLN A 80 ? 0.2714 0.3184 0.2955 0.0305 -0.0479 0.0532 80 GLN A CA 522 C C . GLN A 80 ? 0.2662 0.3163 0.2909 0.0318 -0.0476 0.0493 80 GLN A C 523 O O . GLN A 80 ? 0.2654 0.3116 0.2887 0.0351 -0.0485 0.0491 80 GLN A O 524 C CB . GLN A 80 ? 0.2869 0.3381 0.3099 0.0340 -0.0486 0.0554 80 GLN A CB 525 C CG . GLN A 80 ? 0.2919 0.3435 0.3148 0.0323 -0.0484 0.0586 80 GLN A CG 526 C CD . GLN A 80 ? 0.3157 0.3738 0.3378 0.0354 -0.0488 0.0601 80 GLN A CD 527 O OE1 . GLN A 80 ? 0.3098 0.3723 0.3314 0.0391 -0.0493 0.0589 80 GLN A OE1 528 N NE2 . GLN A 80 ? 0.3260 0.3855 0.3479 0.0341 -0.0485 0.0628 80 GLN A NE2 529 N N . ASN A 81 ? 0.2536 0.3106 0.2799 0.0292 -0.0462 0.0465 81 ASN A N 530 C CA . ASN A 81 ? 0.2628 0.3250 0.2897 0.0297 -0.0457 0.0428 81 ASN A CA 531 C C . ASN A 81 ? 0.2594 0.3155 0.2863 0.0294 -0.0457 0.0409 81 ASN A C 532 O O . ASN A 81 ? 0.2655 0.3260 0.2930 0.0299 -0.0453 0.0379 81 ASN A O 533 C CB . ASN A 81 ? 0.2786 0.3481 0.3052 0.0342 -0.0465 0.0428 81 ASN A CB 534 C CG . ASN A 81 ? 0.2910 0.3684 0.3177 0.0341 -0.0463 0.0440 81 ASN A CG 535 O OD1 . ASN A 81 ? 0.2768 0.3599 0.3040 0.0305 -0.0452 0.0424 81 ASN A OD1 536 N ND2 . ASN A 81 ? 0.2778 0.3549 0.3033 0.0379 -0.0474 0.0470 81 ASN A ND2 537 N N . LYS A 82 ? 0.2592 0.3057 0.2855 0.0282 -0.0463 0.0425 82 LYS A N 538 C CA . LYS A 82 ? 0.2680 0.3080 0.2939 0.0279 -0.0464 0.0408 82 LYS A CA 539 C C . LYS A 82 ? 0.2487 0.2911 0.2760 0.0240 -0.0449 0.0379 82 LYS A C 540 O O . LYS A 82 ? 0.2361 0.2819 0.2642 0.0210 -0.0438 0.0379 82 LYS A O 541 C CB . LYS A 82 ? 0.2918 0.3211 0.3164 0.0269 -0.0475 0.0435 82 LYS A CB 542 C CG . LYS A 82 ? 0.3280 0.3520 0.3498 0.0308 -0.0491 0.0461 82 LYS A CG 543 C CD . LYS A 82 ? 0.3519 0.3653 0.3717 0.0289 -0.0503 0.0491 82 LYS A CD 544 C CE . LYS A 82 ? 0.3803 0.3855 0.3988 0.0277 -0.0508 0.0477 82 LYS A CE 545 N NZ . LYS A 82 ? 0.4065 0.4074 0.4221 0.0320 -0.0516 0.0460 82 LYS A NZ 546 N N . LYS A 83 ? 0.2467 0.2864 0.2739 0.0242 -0.0449 0.0355 83 LYS A N 547 C CA . LYS A 83 ? 0.2432 0.2834 0.2712 0.0208 -0.0435 0.0328 83 LYS A CA 548 C C . LYS A 83 ? 0.2413 0.2722 0.2688 0.0195 -0.0440 0.0332 83 LYS A C 549 O O . LYS A 83 ? 0.2434 0.2674 0.2696 0.0213 -0.0455 0.0350 83 LYS A O 550 C CB . LYS A 83 ? 0.2544 0.3010 0.2828 0.0219 -0.0429 0.0293 83 LYS A CB 551 C CG . LYS A 83 ? 0.2584 0.3152 0.2872 0.0230 -0.0426 0.0289 83 LYS A CG 552 C CD . LYS A 83 ? 0.2629 0.3272 0.2923 0.0225 -0.0416 0.0255 83 LYS A CD 553 C CE . LYS A 83 ? 0.2778 0.3528 0.3076 0.0248 -0.0419 0.0253 83 LYS A CE 554 N NZ . LYS A 83 ? 0.2807 0.3557 0.3103 0.0306 -0.0433 0.0269 83 LYS A NZ 555 N N . TRP A 84 ? 0.2290 0.2595 0.2571 0.0163 -0.0428 0.0314 84 TRP A N 556 C CA . TRP A 84 ? 0.2239 0.2467 0.2517 0.0148 -0.0433 0.0316 84 TRP A CA 557 C C . TRP A 84 ? 0.2171 0.2412 0.2452 0.0125 -0.0418 0.0286 84 TRP A C 558 O O . TRP A 84 ? 0.2147 0.2446 0.2430 0.0110 -0.0402 0.0270 84 TRP A O 559 C CB . TRP A 84 ? 0.2227 0.2415 0.2506 0.0126 -0.0436 0.0349 84 TRP A CB 560 C CG . TRP A 84 ? 0.2236 0.2474 0.2523 0.0102 -0.0419 0.0352 84 TRP A CG 561 C CD1 . TRP A 84 ? 0.2199 0.2437 0.2488 0.0075 -0.0405 0.0343 84 TRP A CD1 562 C CD2 . TRP A 84 ? 0.2234 0.2528 0.2522 0.0107 -0.0414 0.0366 84 TRP A CD2 563 N NE1 . TRP A 84 ? 0.2166 0.2446 0.2451 0.0065 -0.0390 0.0350 84 TRP A NE1 564 C CE2 . TRP A 84 ? 0.2245 0.2561 0.2531 0.0082 -0.0396 0.0363 84 TRP A CE2 565 C CE3 . TRP A 84 ? 0.2307 0.2630 0.2594 0.0131 -0.0422 0.0379 84 TRP A CE3 566 C CZ2 . TRP A 84 ? 0.2199 0.2562 0.2479 0.0079 -0.0386 0.0372 84 TRP A CZ2 567 C CZ3 . TRP A 84 ? 0.2298 0.2674 0.2584 0.0126 -0.0414 0.0389 84 TRP A CZ3 568 C CH2 . TRP A 84 ? 0.2286 0.2680 0.2567 0.0100 -0.0396 0.0385 84 TRP A CH2 569 N N . ASP A 85 ? 0.2184 0.2365 0.2460 0.0120 -0.0423 0.0278 85 ASP A N 570 C CA . ASP A 85 ? 0.2091 0.2263 0.2368 0.0093 -0.0410 0.0259 85 ASP A CA 571 C C . ASP A 85 ? 0.2083 0.2224 0.2363 0.0068 -0.0409 0.0286 85 ASP A C 572 O O . ASP A 85 ? 0.2119 0.2281 0.2399 0.0047 -0.0393 0.0280 85 ASP A O 573 C CB . ASP A 85 ? 0.2137 0.2264 0.2406 0.0100 -0.0416 0.0239 85 ASP A CB 574 C CG . ASP A 85 ? 0.2195 0.2364 0.2461 0.0125 -0.0413 0.0212 85 ASP A CG 575 O OD1 . ASP A 85 ? 0.2188 0.2432 0.2461 0.0123 -0.0401 0.0199 85 ASP A OD1 576 O OD2 . ASP A 85 ? 0.2286 0.2415 0.2542 0.0146 -0.0422 0.0203 85 ASP A OD2 577 N N . LEU A 86 ? 0.2068 0.2160 0.2347 0.0069 -0.0426 0.0315 86 LEU A N 578 C CA . LEU A 86 ? 0.1986 0.2059 0.2271 0.0044 -0.0427 0.0344 86 LEU A CA 579 C C . LEU A 86 ? 0.2024 0.2089 0.2309 0.0049 -0.0440 0.0381 86 LEU A C 580 O O . LEU A 86 ? 0.2078 0.2095 0.2351 0.0061 -0.0458 0.0392 86 LEU A O 581 C CB . LEU A 86 ? 0.1998 0.2012 0.2278 0.0027 -0.0436 0.0345 86 LEU A CB 582 C CG . LEU A 86 ? 0.1961 0.1974 0.2250 0.0000 -0.0435 0.0373 86 LEU A CG 583 C CD1 . LEU A 86 ? 0.1892 0.1956 0.2187 -0.0006 -0.0410 0.0363 86 LEU A CD1 584 C CD2 . LEU A 86 ? 0.1988 0.1944 0.2271 -0.0017 -0.0449 0.0377 86 LEU A CD2 585 N N . PHE A 87 ? 0.2097 0.2206 0.2391 0.0041 -0.0430 0.0400 87 PHE A N 586 C CA . PHE A 87 ? 0.2148 0.2257 0.2444 0.0040 -0.0439 0.0439 87 PHE A CA 587 C C . PHE A 87 ? 0.2171 0.2251 0.2472 0.0012 -0.0445 0.0467 87 PHE A C 588 O O . PHE A 87 ? 0.2084 0.2187 0.2393 -0.0002 -0.0432 0.0466 87 PHE A O 589 C CB . PHE A 87 ? 0.2159 0.2333 0.2460 0.0045 -0.0424 0.0445 87 PHE A CB 590 C CG . PHE A 87 ? 0.2275 0.2453 0.2576 0.0051 -0.0433 0.0481 87 PHE A CG 591 C CD1 . PHE A 87 ? 0.2245 0.2413 0.2552 0.0031 -0.0438 0.0519 87 PHE A CD1 592 C CD2 . PHE A 87 ? 0.2344 0.2544 0.2639 0.0076 -0.0438 0.0480 87 PHE A CD2 593 C CE1 . PHE A 87 ? 0.2365 0.2537 0.2671 0.0034 -0.0446 0.0554 87 PHE A CE1 594 C CE2 . PHE A 87 ? 0.2336 0.2537 0.2629 0.0082 -0.0447 0.0515 87 PHE A CE2 595 C CZ . PHE A 87 ? 0.2345 0.2530 0.2642 0.0060 -0.0450 0.0552 87 PHE A CZ 596 N N . VAL A 88 ? 0.2269 0.2300 0.2562 0.0005 -0.0466 0.0494 88 VAL A N 597 C CA . VAL A 88 ? 0.2345 0.2352 0.2642 -0.0027 -0.0475 0.0523 88 VAL A CA 598 C C . VAL A 88 ? 0.2438 0.2471 0.2741 -0.0037 -0.0478 0.0567 88 VAL A C 599 O O . VAL A 88 ? 0.2541 0.2547 0.2831 -0.0029 -0.0490 0.0583 88 VAL A O 600 C CB . VAL A 88 ? 0.2430 0.2353 0.2706 -0.0038 -0.0497 0.0521 88 VAL A CB 601 C CG1 . VAL A 88 ? 0.2483 0.2389 0.2761 -0.0079 -0.0508 0.0554 88 VAL A CG1 602 C CG2 . VAL A 88 ? 0.2443 0.2345 0.2712 -0.0026 -0.0493 0.0478 88 VAL A CG2 603 N N . GLU A 89 ? 0.2540 0.2627 0.2861 -0.0052 -0.0464 0.0585 89 GLU A N 604 C CA . GLU A 89 ? 0.2657 0.2782 0.2987 -0.0061 -0.0463 0.0628 89 GLU A CA 605 C C . GLU A 89 ? 0.2723 0.2832 0.3057 -0.0098 -0.0478 0.0663 89 GLU A C 606 O O . GLU A 89 ? 0.2638 0.2755 0.2980 -0.0116 -0.0476 0.0660 89 GLU A O 607 C CB . GLU A 89 ? 0.2738 0.2939 0.3080 -0.0052 -0.0437 0.0630 89 GLU A CB 608 C CG . GLU A 89 ? 0.2785 0.3015 0.3120 -0.0023 -0.0424 0.0612 89 GLU A CG 609 C CD . GLU A 89 ? 0.2765 0.3056 0.3100 -0.0015 -0.0399 0.0616 89 GLU A CD 610 O OE1 . GLU A 89 ? 0.2579 0.2891 0.2918 -0.0023 -0.0386 0.0623 89 GLU A OE1 611 O OE2 . GLU A 89 ? 0.2710 0.3027 0.3036 0.0002 -0.0391 0.0611 89 GLU A OE2 612 N N . ARG A 90 ? 0.2716 0.2806 0.3043 -0.0112 -0.0494 0.0699 90 ARG A N 613 C CA . ARG A 90 ? 0.2868 0.2934 0.3191 -0.0154 -0.0513 0.0735 90 ARG A CA 614 C C . ARG A 90 ? 0.3014 0.3161 0.3361 -0.0171 -0.0503 0.0777 90 ARG A C 615 O O . ARG A 90 ? 0.2886 0.3084 0.3240 -0.0150 -0.0489 0.0788 90 ARG A O 616 C CB . ARG A 90 ? 0.2891 0.2878 0.3182 -0.0161 -0.0536 0.0751 90 ARG A CB 617 C CG . ARG A 90 ? 0.2925 0.2830 0.3186 -0.0134 -0.0545 0.0714 90 ARG A CG 618 C CD . ARG A 90 ? 0.2839 0.2715 0.3099 -0.0141 -0.0546 0.0681 90 ARG A CD 619 N NE . ARG A 90 ? 0.2763 0.2543 0.2984 -0.0126 -0.0561 0.0655 90 ARG A NE 620 C CZ . ARG A 90 ? 0.2801 0.2528 0.3006 -0.0140 -0.0570 0.0635 90 ARG A CZ 621 N NH1 . ARG A 90 ? 0.2749 0.2513 0.2977 -0.0170 -0.0567 0.0636 90 ARG A NH1 622 N NH2 . ARG A 90 ? 0.2910 0.2547 0.3075 -0.0122 -0.0583 0.0613 90 ARG A NH2 623 N N . SER A 91 ? 0.3149 0.3313 0.3505 -0.0211 -0.0512 0.0803 91 SER A N 624 C CA . SER A 91 ? 0.3322 0.3575 0.3702 -0.0226 -0.0503 0.0847 91 SER A CA 625 C C . SER A 91 ? 0.3464 0.3719 0.3837 -0.0237 -0.0512 0.0887 91 SER A C 626 O O . SER A 91 ? 0.3630 0.3964 0.4021 -0.0232 -0.0498 0.0917 91 SER A O 627 C CB . SER A 91 ? 0.3367 0.3648 0.3760 -0.0268 -0.0512 0.0870 91 SER A CB 628 O OG . SER A 91 ? 0.3489 0.3701 0.3860 -0.0313 -0.0542 0.0887 91 SER A OG 629 N N . LYS A 92 ? 0.3679 0.3845 0.4022 -0.0249 -0.0534 0.0888 92 LYS A N 630 C CA . LYS A 92 ? 0.3999 0.4152 0.4328 -0.0261 -0.0544 0.0926 92 LYS A CA 631 C C . LYS A 92 ? 0.3735 0.3913 0.4065 -0.0214 -0.0527 0.0917 92 LYS A C 632 O O . LYS A 92 ? 0.3581 0.3760 0.3901 -0.0217 -0.0532 0.0948 92 LYS A O 633 C CB . LYS A 92 ? 0.4326 0.4357 0.4609 -0.0282 -0.0572 0.0926 92 LYS A CB 634 C CG . LYS A 92 ? 0.4804 0.4763 0.5061 -0.0236 -0.0572 0.0884 92 LYS A CG 635 C CD . LYS A 92 ? 0.5323 0.5154 0.5529 -0.0250 -0.0596 0.0874 92 LYS A CD 636 C CE . LYS A 92 ? 0.5687 0.5463 0.5870 -0.0195 -0.0593 0.0834 92 LYS A CE 637 N NZ . LYS A 92 ? 0.5934 0.5581 0.6055 -0.0197 -0.0615 0.0836 92 LYS A NZ 638 N N . ALA A 93 ? 0.3487 0.3683 0.3825 -0.0173 -0.0509 0.0874 93 ALA A N 639 C CA . ALA A 93 ? 0.3502 0.3716 0.3836 -0.0131 -0.0497 0.0861 93 ALA A CA 640 C C . ALA A 93 ? 0.3564 0.3861 0.3913 -0.0129 -0.0482 0.0898 93 ALA A C 641 O O . ALA A 93 ? 0.3697 0.4060 0.4067 -0.0141 -0.0470 0.0916 93 ALA A O 642 C CB . ALA A 93 ? 0.3334 0.3561 0.3673 -0.0096 -0.0480 0.0810 93 ALA A CB 643 N N . TYR A 94 ? 0.3543 0.3837 0.3880 -0.0109 -0.0483 0.0908 94 TYR A N 644 C CA . TYR A 94 ? 0.3725 0.4095 0.4073 -0.0104 -0.0469 0.0943 94 TYR A CA 645 C C . TYR A 94 ? 0.3659 0.4034 0.3994 -0.0064 -0.0461 0.0927 94 TYR A C 646 O O . TYR A 94 ? 0.3435 0.3751 0.3751 -0.0048 -0.0473 0.0906 94 TYR A O 647 C CB . TYR A 94 ? 0.3944 0.4309 0.4289 -0.0143 -0.0485 0.0998 94 TYR A CB 648 C CG . TYR A 94 ? 0.4100 0.4375 0.4412 -0.0148 -0.0508 0.1005 94 TYR A CG 649 C CD1 . TYR A 94 ? 0.4271 0.4454 0.4561 -0.0174 -0.0530 0.0997 94 TYR A CD1 650 C CD2 . TYR A 94 ? 0.4289 0.4565 0.4586 -0.0126 -0.0507 0.1021 94 TYR A CD2 651 C CE1 . TYR A 94 ? 0.4423 0.4512 0.4671 -0.0174 -0.0549 0.1005 94 TYR A CE1 652 C CE2 . TYR A 94 ? 0.4392 0.4581 0.4653 -0.0126 -0.0526 0.1029 94 TYR A CE2 653 C CZ . TYR A 94 ? 0.4546 0.4638 0.4780 -0.0149 -0.0547 0.1021 94 TYR A CZ 654 O OH . TYR A 94 ? 0.4499 0.4492 0.4686 -0.0145 -0.0566 0.1030 94 TYR A OH 655 N N . SER A 95 ? 0.3594 0.4043 0.3936 -0.0046 -0.0441 0.0937 95 SER A N 656 C CA . SER A 95 ? 0.3619 0.4083 0.3947 -0.0012 -0.0433 0.0926 95 SER A CA 657 C C . SER A 95 ? 0.3745 0.4208 0.4064 -0.0018 -0.0444 0.0970 95 SER A C 658 O O . SER A 95 ? 0.3819 0.4308 0.4148 -0.0045 -0.0445 0.1013 95 SER A O 659 C CB . SER A 95 ? 0.3598 0.4134 0.3929 0.0008 -0.0406 0.0914 95 SER A CB 660 O OG . SER A 95 ? 0.3432 0.3960 0.3763 0.0014 -0.0395 0.0872 95 SER A OG 661 N N . ASN A 96 ? 0.3868 0.4305 0.4169 0.0006 -0.0451 0.0960 96 ASN A N 662 C CA . ASN A 96 ? 0.4049 0.4474 0.4335 0.0004 -0.0462 0.1000 96 ASN A CA 663 C C . ASN A 96 ? 0.3833 0.4290 0.4107 0.0042 -0.0454 0.0991 96 ASN A C 664 O O . ASN A 96 ? 0.3809 0.4228 0.4061 0.0057 -0.0467 0.0999 96 ASN A O 665 C CB . ASN A 96 ? 0.4287 0.4614 0.4551 -0.0010 -0.0487 0.1008 96 ASN A CB 666 C CG . ASN A 96 ? 0.4520 0.4824 0.4766 -0.0032 -0.0500 0.1061 96 ASN A CG 667 O OD1 . ASN A 96 ? 0.4704 0.5069 0.4964 -0.0050 -0.0491 0.1097 96 ASN A OD1 668 N ND2 . ASN A 96 ? 0.4549 0.4761 0.4759 -0.0030 -0.0520 0.1066 96 ASN A ND2 669 N N . CYS A 97 ? 0.3719 0.4244 0.4000 0.0059 -0.0432 0.0974 97 CYS A N 670 C CA . CYS A 97 ? 0.3700 0.4263 0.3968 0.0091 -0.0424 0.0961 97 CYS A CA 671 C C . CYS A 97 ? 0.3478 0.4113 0.3748 0.0094 -0.0401 0.0976 97 CYS A C 672 O O . CYS A 97 ? 0.3372 0.4030 0.3654 0.0073 -0.0395 0.1010 97 CYS A O 673 C CB . CYS A 97 ? 0.3799 0.4350 0.4062 0.0111 -0.0423 0.0907 97 CYS A CB 674 S SG . CYS A 97 ? 0.3874 0.4465 0.4118 0.0147 -0.0420 0.0884 97 CYS A SG 675 N N . TYR A 98 ? 0.3468 0.4143 0.3723 0.0118 -0.0387 0.0951 98 TYR A N 676 C CA . TYR A 98 ? 0.3514 0.4248 0.3760 0.0126 -0.0364 0.0964 98 TYR A CA 677 C C . TYR A 98 ? 0.3434 0.4179 0.3687 0.0116 -0.0347 0.0953 98 TYR A C 678 O O . TYR A 98 ? 0.3270 0.3986 0.3524 0.0113 -0.0347 0.0914 98 TYR A O 679 C CB . TYR A 98 ? 0.3545 0.4309 0.3764 0.0151 -0.0354 0.0937 98 TYR A CB 680 C CG . TYR A 98 ? 0.3582 0.4399 0.3783 0.0163 -0.0338 0.0965 98 TYR A CG 681 C CD1 . TYR A 98 ? 0.3621 0.4452 0.3819 0.0170 -0.0348 0.1001 98 TYR A CD1 682 C CD2 . TYR A 98 ? 0.3587 0.4435 0.3768 0.0171 -0.0313 0.0956 98 TYR A CD2 683 C CE1 . TYR A 98 ? 0.3634 0.4514 0.3814 0.0182 -0.0333 0.1027 98 TYR A CE1 684 C CE2 . TYR A 98 ? 0.3685 0.4578 0.3844 0.0186 -0.0297 0.0981 98 TYR A CE2 685 C CZ . TYR A 98 ? 0.3691 0.4603 0.3852 0.0191 -0.0307 0.1016 98 TYR A CZ 686 O OH . TYR A 98 ? 0.3651 0.4609 0.3789 0.0206 -0.0291 0.1041 98 TYR A OH 687 N N . PRO A 99 ? 0.3443 0.4231 0.3700 0.0111 -0.0333 0.0990 99 PRO A N 688 C CA . PRO A 99 ? 0.3420 0.4223 0.3682 0.0107 -0.0316 0.0983 99 PRO A CA 689 C C . PRO A 99 ? 0.3377 0.4178 0.3607 0.0129 -0.0296 0.0936 99 PRO A C 690 O O . PRO A 99 ? 0.3253 0.4075 0.3453 0.0149 -0.0284 0.0929 99 PRO A O 691 C CB . PRO A 99 ? 0.3530 0.4394 0.3798 0.0106 -0.0304 0.1035 99 PRO A CB 692 C CG . PRO A 99 ? 0.3543 0.4425 0.3802 0.0114 -0.0309 0.1063 99 PRO A CG 693 C CD . PRO A 99 ? 0.3604 0.4430 0.3865 0.0108 -0.0334 0.1044 99 PRO A CD 694 N N . TYR A 100 ? 0.3310 0.4082 0.3543 0.0122 -0.0293 0.0904 100 TYR A N 695 C CA . TYR A 100 ? 0.3197 0.3954 0.3394 0.0136 -0.0275 0.0858 100 TYR A CA 696 C C . TYR A 100 ? 0.3329 0.4076 0.3526 0.0134 -0.0261 0.0846 100 TYR A C 697 O O . TYR A 100 ? 0.3150 0.3898 0.3379 0.0118 -0.0270 0.0868 100 TYR A O 698 C CB . TYR A 100 ? 0.3254 0.3975 0.3449 0.0132 -0.0291 0.0815 100 TYR A CB 699 C CG . TYR A 100 ? 0.3270 0.3950 0.3493 0.0115 -0.0307 0.0798 100 TYR A CG 700 C CD1 . TYR A 100 ? 0.3290 0.3950 0.3542 0.0102 -0.0331 0.0820 100 TYR A CD1 701 C CD2 . TYR A 100 ? 0.3289 0.3943 0.3501 0.0111 -0.0297 0.0760 100 TYR A CD2 702 C CE1 . TYR A 100 ? 0.3420 0.4036 0.3691 0.0087 -0.0345 0.0803 100 TYR A CE1 703 C CE2 . TYR A 100 ? 0.3226 0.3844 0.3462 0.0096 -0.0311 0.0745 100 TYR A CE2 704 C CZ . TYR A 100 ? 0.3384 0.3982 0.3649 0.0085 -0.0335 0.0766 100 TYR A CZ 705 O OH . TYR A 100 ? 0.3263 0.3818 0.3546 0.0071 -0.0350 0.0750 100 TYR A OH 706 N N . ASP A 101 ? 0.3397 0.4131 0.3550 0.0148 -0.0239 0.0812 101 ASP A N 707 C CA . ASP A 101 ? 0.3390 0.4099 0.3532 0.0148 -0.0226 0.0790 101 ASP A CA 708 C C . ASP A 101 ? 0.3348 0.4013 0.3451 0.0147 -0.0221 0.0735 101 ASP A C 709 O O . ASP A 101 ? 0.3202 0.3867 0.3283 0.0150 -0.0224 0.0717 101 ASP A O 710 C CB . ASP A 101 ? 0.3687 0.4425 0.3803 0.0170 -0.0199 0.0814 101 ASP A CB 711 C CG . ASP A 101 ? 0.4000 0.4749 0.4061 0.0195 -0.0178 0.0812 101 ASP A CG 712 O OD1 . ASP A 101 ? 0.4136 0.4849 0.4155 0.0196 -0.0174 0.0771 101 ASP A OD1 713 O OD2 . ASP A 101 ? 0.4799 0.5595 0.4858 0.0212 -0.0167 0.0853 101 ASP A OD2 714 N N . VAL A 102 ? 0.3089 0.3721 0.3185 0.0142 -0.0214 0.0709 102 VAL A N 715 C CA . VAL A 102 ? 0.3084 0.3673 0.3141 0.0138 -0.0206 0.0658 102 VAL A CA 716 C C . VAL A 102 ? 0.3246 0.3810 0.3258 0.0151 -0.0179 0.0648 102 VAL A C 717 O O . VAL A 102 ? 0.3191 0.3747 0.3225 0.0148 -0.0178 0.0654 102 VAL A O 718 C CB . VAL A 102 ? 0.3081 0.3644 0.3173 0.0116 -0.0228 0.0632 102 VAL A CB 719 C CG1 . VAL A 102 ? 0.2957 0.3488 0.3010 0.0107 -0.0221 0.0580 102 VAL A CG1 720 C CG2 . VAL A 102 ? 0.2970 0.3553 0.3108 0.0109 -0.0255 0.0650 102 VAL A CG2 721 N N . PRO A 103 ? 0.3247 0.3795 0.3191 0.0166 -0.0156 0.0635 103 PRO A N 722 C CA . PRO A 103 ? 0.3509 0.4016 0.3399 0.0181 -0.0129 0.0620 103 PRO A CA 723 C C . PRO A 103 ? 0.3517 0.3978 0.3408 0.0158 -0.0135 0.0579 103 PRO A C 724 O O . PRO A 103 ? 0.3937 0.4386 0.3830 0.0136 -0.0149 0.0548 103 PRO A O 725 C CB . PRO A 103 ? 0.3522 0.4003 0.3328 0.0193 -0.0108 0.0602 103 PRO A CB 726 C CG . PRO A 103 ? 0.3487 0.4019 0.3316 0.0197 -0.0119 0.0629 103 PRO A CG 727 C CD . PRO A 103 ? 0.3411 0.3975 0.3321 0.0174 -0.0152 0.0637 103 PRO A CD 728 N N . ASP A 104 ? 0.3751 0.4192 0.3643 0.0164 -0.0126 0.0580 104 ASP A N 729 C CA . ASP A 104 ? 0.3602 0.4006 0.3506 0.0142 -0.0135 0.0546 104 ASP A CA 730 C C . ASP A 104 ? 0.3078 0.3504 0.3054 0.0117 -0.0167 0.0543 104 ASP A C 731 O O . ASP A 104 ? 0.2909 0.3313 0.2887 0.0097 -0.0177 0.0506 104 ASP A O 732 C CB . ASP A 104 ? 0.3937 0.4280 0.3767 0.0133 -0.0119 0.0498 104 ASP A CB 733 C CG . ASP A 104 ? 0.4429 0.4723 0.4247 0.0122 -0.0113 0.0470 104 ASP A CG 734 O OD1 . ASP A 104 ? 0.4284 0.4589 0.4145 0.0127 -0.0118 0.0487 104 ASP A OD1 735 O OD2 . ASP A 104 ? 0.4814 0.5060 0.4575 0.0106 -0.0104 0.0430 104 ASP A OD2 736 N N . TYR A 105 ? 0.2846 0.3317 0.2877 0.0120 -0.0183 0.0583 105 TYR A N 737 C CA . TYR A 105 ? 0.2689 0.3170 0.2783 0.0101 -0.0212 0.0589 105 TYR A CA 738 C C . TYR A 105 ? 0.2567 0.3012 0.2673 0.0086 -0.0218 0.0559 105 TYR A C 739 O O . TYR A 105 ? 0.2465 0.2898 0.2590 0.0071 -0.0236 0.0536 105 TYR A O 740 C CB . TYR A 105 ? 0.2725 0.3246 0.2863 0.0103 -0.0222 0.0639 105 TYR A CB 741 C CG . TYR A 105 ? 0.2844 0.3367 0.3037 0.0083 -0.0253 0.0651 105 TYR A CG 742 C CD1 . TYR A 105 ? 0.2906 0.3408 0.3128 0.0067 -0.0265 0.0646 105 TYR A CD1 743 C CD2 . TYR A 105 ? 0.2899 0.3441 0.3110 0.0081 -0.0269 0.0669 105 TYR A CD2 744 C CE1 . TYR A 105 ? 0.2918 0.3408 0.3178 0.0049 -0.0293 0.0657 105 TYR A CE1 745 C CE2 . TYR A 105 ? 0.3070 0.3601 0.3320 0.0065 -0.0296 0.0681 105 TYR A CE2 746 C CZ . TYR A 105 ? 0.2978 0.3480 0.3251 0.0049 -0.0308 0.0674 105 TYR A CZ 747 O OH . TYR A 105 ? 0.3236 0.3715 0.3536 0.0034 -0.0334 0.0686 105 TYR A OH 748 N N . ALA A 106 ? 0.2501 0.2931 0.2593 0.0092 -0.0203 0.0560 106 ALA A N 749 C CA . ALA A 106 ? 0.2449 0.2845 0.2553 0.0078 -0.0210 0.0535 106 ALA A CA 750 C C . ALA A 106 ? 0.2443 0.2802 0.2517 0.0067 -0.0207 0.0486 106 ALA A C 751 O O . ALA A 106 ? 0.2455 0.2799 0.2554 0.0051 -0.0222 0.0465 106 ALA A O 752 C CB . ALA A 106 ? 0.2393 0.2782 0.2482 0.0090 -0.0192 0.0546 106 ALA A CB 753 N N . SER A 107 ? 0.2480 0.2824 0.2496 0.0072 -0.0187 0.0468 107 SER A N 754 C CA . SER A 107 ? 0.2519 0.2835 0.2503 0.0055 -0.0185 0.0422 107 SER A CA 755 C C . SER A 107 ? 0.2413 0.2759 0.2431 0.0042 -0.0208 0.0412 107 SER A C 756 O O . SER A 107 ? 0.2469 0.2806 0.2492 0.0026 -0.0216 0.0381 107 SER A O 757 C CB . SER A 107 ? 0.2608 0.2892 0.2511 0.0059 -0.0159 0.0404 107 SER A CB 758 O OG . SER A 107 ? 0.2676 0.2917 0.2537 0.0070 -0.0137 0.0402 107 SER A OG 759 N N . LEU A 108 ? 0.2468 0.2852 0.2506 0.0051 -0.0218 0.0439 108 LEU A N 760 C CA . LEU A 108 ? 0.2371 0.2786 0.2437 0.0044 -0.0239 0.0431 108 LEU A CA 761 C C . LEU A 108 ? 0.2302 0.2716 0.2424 0.0041 -0.0263 0.0436 108 LEU A C 762 O O . LEU A 108 ? 0.2285 0.2703 0.2421 0.0033 -0.0276 0.0412 108 LEU A O 763 C CB . LEU A 108 ? 0.2435 0.2887 0.2503 0.0056 -0.0243 0.0461 108 LEU A CB 764 C CG . LEU A 108 ? 0.2392 0.2879 0.2488 0.0056 -0.0265 0.0460 108 LEU A CG 765 C CD1 . LEU A 108 ? 0.2500 0.2996 0.2567 0.0041 -0.0263 0.0418 108 LEU A CD1 766 C CD2 . LEU A 108 ? 0.2360 0.2880 0.2457 0.0069 -0.0268 0.0493 108 LEU A CD2 767 N N . ARG A 109 ? 0.2231 0.2638 0.2381 0.0046 -0.0267 0.0468 109 ARG A N 768 C CA . ARG A 109 ? 0.2161 0.2553 0.2353 0.0040 -0.0288 0.0472 109 ARG A CA 769 C C . ARG A 109 ? 0.2103 0.2466 0.2289 0.0029 -0.0286 0.0433 109 ARG A C 770 O O . ARG A 109 ? 0.1999 0.2356 0.2206 0.0026 -0.0302 0.0418 109 ARG A O 771 C CB . ARG A 109 ? 0.2119 0.2510 0.2333 0.0040 -0.0290 0.0511 109 ARG A CB 772 C CG . ARG A 109 ? 0.2127 0.2495 0.2377 0.0029 -0.0312 0.0518 109 ARG A CG 773 C CD . ARG A 109 ? 0.2127 0.2506 0.2397 0.0024 -0.0315 0.0561 109 ARG A CD 774 N NE . ARG A 109 ? 0.2062 0.2414 0.2359 0.0007 -0.0335 0.0568 109 ARG A NE 775 C CZ . ARG A 109 ? 0.2080 0.2408 0.2377 0.0000 -0.0334 0.0551 109 ARG A CZ 776 N NH1 . ARG A 109 ? 0.2058 0.2384 0.2331 0.0006 -0.0312 0.0526 109 ARG A NH1 777 N NH2 . ARG A 109 ? 0.1959 0.2261 0.2277 -0.0016 -0.0354 0.0559 109 ARG A NH2 778 N N . SER A 110 ? 0.2082 0.2424 0.2233 0.0026 -0.0264 0.0417 110 SER A N 779 C CA . SER A 110 ? 0.2139 0.2452 0.2279 0.0015 -0.0259 0.0382 110 SER A CA 780 C C . SER A 110 ? 0.2147 0.2470 0.2273 0.0005 -0.0261 0.0346 110 SER A C 781 O O . SER A 110 ? 0.2037 0.2353 0.2179 -0.0001 -0.0271 0.0323 110 SER A O 782 C CB . SER A 110 ? 0.2198 0.2482 0.2293 0.0016 -0.0234 0.0375 110 SER A CB 783 O OG . SER A 110 ? 0.2307 0.2560 0.2388 0.0003 -0.0229 0.0339 110 SER A OG 784 N N . LEU A 111 ? 0.2144 0.2487 0.2237 0.0004 -0.0252 0.0340 111 LEU A N 785 C CA . LEU A 111 ? 0.2247 0.2609 0.2324 -0.0009 -0.0253 0.0305 111 LEU A CA 786 C C . LEU A 111 ? 0.2129 0.2531 0.2251 -0.0002 -0.0278 0.0309 111 LEU A C 787 O O . LEU A 111 ? 0.2141 0.2557 0.2269 -0.0009 -0.0284 0.0282 111 LEU A O 788 C CB . LEU A 111 ? 0.2337 0.2706 0.2358 -0.0018 -0.0237 0.0295 111 LEU A CB 789 C CG . LEU A 111 ? 0.2393 0.2799 0.2415 -0.0007 -0.0241 0.0318 111 LEU A CG 790 C CD1 . LEU A 111 ? 0.2499 0.2958 0.2539 -0.0013 -0.0258 0.0303 111 LEU A CD1 791 C CD2 . LEU A 111 ? 0.2547 0.2928 0.2500 -0.0012 -0.0217 0.0313 111 LEU A CD2 792 N N . VAL A 112 ? 0.2131 0.2547 0.2281 0.0014 -0.0291 0.0343 112 VAL A N 793 C CA . VAL A 112 ? 0.2181 0.2623 0.2368 0.0027 -0.0314 0.0349 112 VAL A CA 794 C C . VAL A 112 ? 0.2125 0.2534 0.2341 0.0030 -0.0326 0.0344 112 VAL A C 795 O O . VAL A 112 ? 0.2066 0.2488 0.2294 0.0036 -0.0337 0.0326 112 VAL A O 796 C CB . VAL A 112 ? 0.2205 0.2663 0.2408 0.0043 -0.0325 0.0388 112 VAL A CB 797 C CG1 . VAL A 112 ? 0.2123 0.2597 0.2354 0.0060 -0.0347 0.0394 112 VAL A CG1 798 C CG2 . VAL A 112 ? 0.2264 0.2758 0.2437 0.0041 -0.0313 0.0390 112 VAL A CG2 799 N N . ALA A 113 ? 0.2104 0.2473 0.2325 0.0026 -0.0323 0.0359 113 ALA A N 800 C CA . ALA A 113 ? 0.2047 0.2378 0.2288 0.0025 -0.0334 0.0355 113 ALA A CA 801 C C . ALA A 113 ? 0.2027 0.2355 0.2259 0.0018 -0.0329 0.0315 113 ALA A C 802 O O . ALA A 113 ? 0.1972 0.2291 0.2220 0.0025 -0.0343 0.0305 113 ALA A O 803 C CB . ALA A 113 ? 0.1945 0.2245 0.2188 0.0017 -0.0329 0.0376 113 ALA A CB 804 N N . SER A 114 ? 0.2048 0.2380 0.2249 0.0003 -0.0309 0.0293 114 SER A N 805 C CA . SER A 114 ? 0.2190 0.2520 0.2375 -0.0009 -0.0300 0.0256 114 SER A CA 806 C C . SER A 114 ? 0.2215 0.2596 0.2403 -0.0008 -0.0307 0.0235 114 SER A C 807 O O . SER A 114 ? 0.2332 0.2720 0.2526 -0.0011 -0.0309 0.0210 114 SER A O 808 C CB . SER A 114 ? 0.2250 0.2560 0.2390 -0.0026 -0.0275 0.0242 114 SER A CB 809 O OG . SER A 114 ? 0.2539 0.2845 0.2660 -0.0043 -0.0267 0.0206 114 SER A OG 810 N N . SER A 115 ? 0.2240 0.2662 0.2424 -0.0003 -0.0309 0.0246 115 SER A N 811 C CA . SER A 115 ? 0.2312 0.2795 0.2503 0.0001 -0.0318 0.0232 115 SER A CA 812 C C . SER A 115 ? 0.2232 0.2721 0.2460 0.0029 -0.0339 0.0241 115 SER A C 813 O O . SER A 115 ? 0.2383 0.2911 0.2618 0.0035 -0.0344 0.0220 115 SER A O 814 C CB . SER A 115 ? 0.2374 0.2896 0.2551 0.0001 -0.0317 0.0246 115 SER A CB 815 O OG . SER A 115 ? 0.2506 0.3095 0.2696 0.0012 -0.0329 0.0241 115 SER A OG 816 N N . GLY A 116 ? 0.2119 0.2568 0.2364 0.0046 -0.0351 0.0271 116 GLY A N 817 C CA . GLY A 116 ? 0.2122 0.2549 0.2389 0.0071 -0.0369 0.0278 116 GLY A CA 818 C C . GLY A 116 ? 0.2208 0.2675 0.2483 0.0099 -0.0383 0.0289 116 GLY A C 819 O O . GLY A 116 ? 0.2101 0.2556 0.2384 0.0124 -0.0396 0.0286 116 GLY A O 820 N N . THR A 117 ? 0.2231 0.2744 0.2501 0.0099 -0.0381 0.0301 117 THR A N 821 C CA . THR A 117 ? 0.2304 0.2863 0.2580 0.0128 -0.0393 0.0313 117 THR A CA 822 C C . THR A 117 ? 0.2331 0.2904 0.2602 0.0129 -0.0394 0.0341 117 THR A C 823 O O . THR A 117 ? 0.2415 0.2997 0.2672 0.0105 -0.0381 0.0341 117 THR A O 824 C CB . THR A 117 ? 0.2268 0.2911 0.2543 0.0130 -0.0390 0.0284 117 THR A CB 825 O OG1 . THR A 117 ? 0.2320 0.3011 0.2601 0.0163 -0.0403 0.0299 117 THR A OG1 826 C CG2 . THR A 117 ? 0.2215 0.2902 0.2469 0.0093 -0.0373 0.0265 117 THR A CG2 827 N N . LEU A 118 ? 0.2330 0.2901 0.2608 0.0159 -0.0409 0.0366 118 LEU A N 828 C CA . LEU A 118 ? 0.2403 0.2998 0.2676 0.0165 -0.0411 0.0394 118 LEU A CA 829 C C . LEU A 118 ? 0.2465 0.3142 0.2737 0.0186 -0.0417 0.0388 118 LEU A C 830 O O . LEU A 118 ? 0.2578 0.3277 0.2847 0.0201 -0.0422 0.0412 118 LEU A O 831 C CB . LEU A 118 ? 0.2441 0.2971 0.2717 0.0181 -0.0425 0.0431 118 LEU A CB 832 C CG . LEU A 118 ? 0.2430 0.2901 0.2709 0.0155 -0.0420 0.0447 118 LEU A CG 833 C CD1 . LEU A 118 ? 0.2543 0.2946 0.2822 0.0165 -0.0436 0.0480 118 LEU A CD1 834 C CD2 . LEU A 118 ? 0.2499 0.3001 0.2771 0.0137 -0.0406 0.0459 118 LEU A CD2 835 N N . GLU A 119 ? 0.2582 0.3310 0.2856 0.0188 -0.0415 0.0357 119 GLU A N 836 C CA . GLU A 119 ? 0.2673 0.3495 0.2948 0.0207 -0.0420 0.0352 119 GLU A CA 837 C C . GLU A 119 ? 0.2621 0.3492 0.2883 0.0187 -0.0414 0.0359 119 GLU A C 838 O O . GLU A 119 ? 0.2469 0.3341 0.2715 0.0149 -0.0399 0.0342 119 GLU A O 839 C CB . GLU A 119 ? 0.2740 0.3625 0.3019 0.0199 -0.0415 0.0317 119 GLU A CB 840 C CG . GLU A 119 ? 0.2965 0.3822 0.3254 0.0228 -0.0422 0.0309 119 GLU A CG 841 C CD . GLU A 119 ? 0.3234 0.4142 0.3526 0.0207 -0.0412 0.0272 119 GLU A CD 842 O OE1 . GLU A 119 ? 0.3051 0.3913 0.3337 0.0171 -0.0401 0.0255 119 GLU A OE1 843 O OE2 . GLU A 119 ? 0.3276 0.4275 0.3575 0.0225 -0.0416 0.0263 119 GLU A OE2 844 N N . PHE A 120 ? 0.2643 0.3554 0.2905 0.0216 -0.0424 0.0382 120 PHE A N 845 C CA . PHE A 120 ? 0.2704 0.3658 0.2953 0.0203 -0.0421 0.0393 120 PHE A CA 846 C C . PHE A 120 ? 0.2948 0.4008 0.3197 0.0224 -0.0429 0.0390 120 PHE A C 847 O O . PHE A 120 ? 0.2811 0.3888 0.3072 0.0267 -0.0442 0.0404 120 PHE A O 848 C CB . PHE A 120 ? 0.2692 0.3586 0.2939 0.0217 -0.0425 0.0432 120 PHE A CB 849 C CG . PHE A 120 ? 0.2749 0.3678 0.2979 0.0205 -0.0420 0.0445 120 PHE A CG 850 C CD1 . PHE A 120 ? 0.2798 0.3702 0.3009 0.0170 -0.0404 0.0439 120 PHE A CD1 851 C CD2 . PHE A 120 ? 0.2785 0.3772 0.3013 0.0231 -0.0430 0.0464 120 PHE A CD2 852 C CE1 . PHE A 120 ? 0.2829 0.3761 0.3019 0.0161 -0.0398 0.0451 120 PHE A CE1 853 C CE2 . PHE A 120 ? 0.2795 0.3816 0.3004 0.0220 -0.0426 0.0475 120 PHE A CE2 854 C CZ . PHE A 120 ? 0.2880 0.3872 0.3069 0.0184 -0.0409 0.0468 120 PHE A CZ 855 N N . ASN A 121 ? 0.3116 0.4246 0.3349 0.0193 -0.0422 0.0374 121 ASN A N 856 C CA . ASN A 121 ? 0.3404 0.4647 0.3637 0.0205 -0.0431 0.0372 121 ASN A CA 857 C C . ASN A 121 ? 0.3399 0.4663 0.3613 0.0199 -0.0431 0.0391 121 ASN A C 858 O O . ASN A 121 ? 0.3272 0.4518 0.3459 0.0159 -0.0419 0.0381 121 ASN A O 859 C CB . ASN A 121 ? 0.3779 0.5100 0.4006 0.0169 -0.0425 0.0335 121 ASN A CB 860 C CG . ASN A 121 ? 0.4286 0.5626 0.4536 0.0187 -0.0428 0.0319 121 ASN A CG 861 O OD1 . ASN A 121 ? 0.4937 0.6227 0.5204 0.0230 -0.0435 0.0334 121 ASN A OD1 862 N ND2 . ASN A 121 ? 0.4796 0.6206 0.5041 0.0154 -0.0423 0.0288 121 ASN A ND2 863 N N . ASN A 122 ? 0.3569 0.4866 0.3791 0.0241 -0.0444 0.0419 122 ASN A N 864 C CA . ASN A 122 ? 0.3674 0.5002 0.3877 0.0240 -0.0446 0.0439 122 ASN A CA 865 C C . ASN A 122 ? 0.3498 0.4929 0.3682 0.0206 -0.0444 0.0416 122 ASN A C 866 O O . ASN A 122 ? 0.3343 0.4858 0.3537 0.0203 -0.0449 0.0395 122 ASN A O 867 C CB . ASN A 122 ? 0.3991 0.5332 0.4206 0.0296 -0.0461 0.0475 122 ASN A CB 868 C CG . ASN A 122 ? 0.4247 0.5473 0.4466 0.0317 -0.0462 0.0504 122 ASN A CG 869 O OD1 . ASN A 122 ? 0.4441 0.5615 0.4649 0.0299 -0.0455 0.0521 122 ASN A OD1 870 N ND2 . ASN A 122 ? 0.4560 0.5745 0.4793 0.0352 -0.0470 0.0511 122 ASN A ND2 871 N N . GLU A 123 ? 0.3454 0.4879 0.3607 0.0178 -0.0437 0.0419 123 GLU A N 872 C CA . GLU A 123 ? 0.3491 0.5008 0.3616 0.0144 -0.0437 0.0400 123 GLU A CA 873 C C . GLU A 123 ? 0.3606 0.5149 0.3714 0.0158 -0.0442 0.0426 123 GLU A C 874 O O . GLU A 123 ? 0.3429 0.4900 0.3536 0.0177 -0.0439 0.0454 123 GLU A O 875 C CB . GLU A 123 ? 0.3456 0.4937 0.3542 0.0084 -0.0421 0.0366 123 GLU A CB 876 C CG . GLU A 123 ? 0.3398 0.4868 0.3496 0.0063 -0.0416 0.0336 123 GLU A CG 877 C CD . GLU A 123 ? 0.3311 0.4724 0.3363 0.0006 -0.0398 0.0306 123 GLU A CD 878 O OE1 . GLU A 123 ? 0.3370 0.4692 0.3396 0.0001 -0.0385 0.0315 123 GLU A OE1 879 O OE2 . GLU A 123 ? 0.3248 0.4705 0.3286 -0.0031 -0.0396 0.0275 123 GLU A OE2 880 N N . SER A 124 ? 0.3957 0.5611 0.4051 0.0147 -0.0451 0.0418 124 SER A N 881 C CA . SER A 124 ? 0.4253 0.5950 0.4329 0.0161 -0.0458 0.0442 124 SER A CA 882 C C . SER A 124 ? 0.4255 0.5928 0.4277 0.0109 -0.0445 0.0425 124 SER A C 883 O O . SER A 124 ? 0.4254 0.5998 0.4245 0.0068 -0.0447 0.0399 124 SER A O 884 C CB . SER A 124 ? 0.4509 0.6349 0.4598 0.0178 -0.0475 0.0443 124 SER A CB 885 O OG . SER A 124 ? 0.4929 0.6792 0.5061 0.0231 -0.0485 0.0457 124 SER A OG 886 N N . PHE A 125 ? 0.4191 0.5763 0.4196 0.0111 -0.0433 0.0440 125 PHE A N 887 C CA . PHE A 125 ? 0.4459 0.5997 0.4405 0.0072 -0.0419 0.0428 125 PHE A CA 888 C C . PHE A 125 ? 0.4762 0.6363 0.4691 0.0087 -0.0428 0.0450 125 PHE A C 889 O O . PHE A 125 ? 0.4797 0.6422 0.4760 0.0134 -0.0440 0.0484 125 PHE A O 890 C CB . PHE A 125 ? 0.4449 0.5866 0.4384 0.0075 -0.0401 0.0440 125 PHE A CB 891 C CG . PHE A 125 ? 0.4250 0.5600 0.4187 0.0052 -0.0389 0.0415 125 PHE A CG 892 C CD1 . PHE A 125 ? 0.4221 0.5542 0.4210 0.0077 -0.0393 0.0423 125 PHE A CD1 893 C CD2 . PHE A 125 ? 0.4287 0.5595 0.4166 0.0005 -0.0373 0.0384 125 PHE A CD2 894 C CE1 . PHE A 125 ? 0.4105 0.5366 0.4094 0.0056 -0.0382 0.0400 125 PHE A CE1 895 C CE2 . PHE A 125 ? 0.4390 0.5634 0.4267 -0.0013 -0.0361 0.0362 125 PHE A CE2 896 C CZ . PHE A 125 ? 0.4186 0.5411 0.4121 0.0011 -0.0366 0.0370 125 PHE A CZ 897 N N . ASN A 126 ? 0.4878 0.6500 0.4748 0.0046 -0.0424 0.0431 126 ASN A N 898 C CA . ASN A 126 ? 0.5239 0.6917 0.5086 0.0056 -0.0431 0.0450 126 ASN A CA 899 C C . ASN A 126 ? 0.5091 0.6681 0.4910 0.0070 -0.0417 0.0474 126 ASN A C 900 O O . ASN A 126 ? 0.5040 0.6579 0.4797 0.0037 -0.0401 0.0457 126 ASN A O 901 C CB . ASN A 126 ? 0.5623 0.7374 0.5416 0.0004 -0.0436 0.0418 126 ASN A CB 902 C CG . ASN A 126 ? 0.6038 0.7858 0.5807 0.0013 -0.0446 0.0436 126 ASN A CG 903 O OD1 . ASN A 126 ? 0.5997 0.7787 0.5774 0.0053 -0.0444 0.0471 126 ASN A OD1 904 N ND2 . ASN A 126 ? 0.6426 0.8343 0.6163 -0.0025 -0.0457 0.0414 126 ASN A ND2 905 N N . TRP A 127 ? 0.4896 0.6467 0.4758 0.0120 -0.0421 0.0514 127 TRP A N 906 C CA . TRP A 127 ? 0.5077 0.6584 0.4919 0.0136 -0.0409 0.0543 127 TRP A CA 907 C C . TRP A 127 ? 0.5238 0.6810 0.5067 0.0158 -0.0420 0.0569 127 TRP A C 908 O O . TRP A 127 ? 0.5319 0.6876 0.5172 0.0197 -0.0423 0.0609 127 TRP A O 909 C CB . TRP A 127 ? 0.4867 0.6303 0.4757 0.0170 -0.0406 0.0574 127 TRP A CB 910 C CG . TRP A 127 ? 0.4655 0.6029 0.4564 0.0154 -0.0397 0.0552 127 TRP A CG 911 C CD1 . TRP A 127 ? 0.4611 0.5971 0.4573 0.0175 -0.0406 0.0558 127 TRP A CD1 912 C CD2 . TRP A 127 ? 0.4565 0.5879 0.4434 0.0116 -0.0378 0.0520 127 TRP A CD2 913 N NE1 . TRP A 127 ? 0.4478 0.5779 0.4441 0.0151 -0.0394 0.0533 127 TRP A NE1 914 C CE2 . TRP A 127 ? 0.4341 0.5612 0.4249 0.0116 -0.0377 0.0510 127 TRP A CE2 915 C CE3 . TRP A 127 ? 0.4627 0.5912 0.4428 0.0085 -0.0361 0.0500 127 TRP A CE3 916 C CZ2 . TRP A 127 ? 0.4375 0.5584 0.4259 0.0087 -0.0361 0.0483 127 TRP A CZ2 917 C CZ3 . TRP A 127 ? 0.4591 0.5804 0.4362 0.0056 -0.0344 0.0472 127 TRP A CZ3 918 C CH2 . TRP A 127 ? 0.4453 0.5632 0.4267 0.0057 -0.0344 0.0464 127 TRP A CH2 919 N N . THR A 128 ? 0.5562 0.7206 0.5351 0.0130 -0.0426 0.0546 128 THR A N 920 C CA . THR A 128 ? 0.5613 0.7323 0.5382 0.0146 -0.0436 0.0568 128 THR A CA 921 C C . THR A 128 ? 0.5509 0.7153 0.5224 0.0141 -0.0418 0.0579 128 THR A C 922 O O . THR A 128 ? 0.5670 0.7258 0.5330 0.0105 -0.0402 0.0552 128 THR A O 923 C CB . THR A 128 ? 0.5986 0.7804 0.5728 0.0114 -0.0450 0.0540 128 THR A CB 924 O OG1 . THR A 128 ? 0.6389 0.8174 0.6076 0.0055 -0.0438 0.0497 128 THR A OG1 925 C CG2 . THR A 128 ? 0.5772 0.7681 0.5573 0.0134 -0.0469 0.0540 128 THR A CG2 926 N N . GLY A 129 ? 0.5564 0.7212 0.5293 0.0181 -0.0421 0.0621 129 GLY A N 927 C CA . GLY A 129 ? 0.5465 0.7066 0.5146 0.0184 -0.0405 0.0638 129 GLY A CA 928 C C . GLY A 129 ? 0.5358 0.6876 0.5066 0.0211 -0.0390 0.0671 129 GLY A C 929 O O . GLY A 129 ? 0.5237 0.6722 0.4912 0.0219 -0.0376 0.0691 129 GLY A O 930 N N . VAL A 130 ? 0.5134 0.6622 0.4900 0.0223 -0.0394 0.0677 130 VAL A N 931 C CA . VAL A 130 ? 0.4803 0.6218 0.4599 0.0243 -0.0383 0.0710 130 VAL A CA 932 C C . VAL A 130 ? 0.4586 0.6009 0.4446 0.0276 -0.0400 0.0739 130 VAL A C 933 O O . VAL A 130 ? 0.4341 0.5817 0.4223 0.0284 -0.0418 0.0729 130 VAL A O 934 C CB . VAL A 130 ? 0.4830 0.6171 0.4621 0.0220 -0.0365 0.0685 130 VAL A CB 935 C CG1 . VAL A 130 ? 0.4825 0.6139 0.4542 0.0192 -0.0346 0.0658 130 VAL A CG1 936 C CG2 . VAL A 130 ? 0.4709 0.6059 0.4534 0.0206 -0.0376 0.0655 130 VAL A CG2 937 N N . THR A 131 ? 0.4473 0.5842 0.4356 0.0294 -0.0394 0.0777 131 THR A N 938 C CA . THR A 131 ? 0.4533 0.5881 0.4466 0.0321 -0.0408 0.0807 131 THR A CA 939 C C . THR A 131 ? 0.4539 0.5830 0.4501 0.0306 -0.0405 0.0787 131 THR A C 940 O O . THR A 131 ? 0.4148 0.5393 0.4099 0.0285 -0.0387 0.0777 131 THR A O 941 C CB . THR A 131 ? 0.4752 0.6066 0.4690 0.0339 -0.0404 0.0858 131 THR A CB 942 O OG1 . THR A 131 ? 0.4838 0.6203 0.4746 0.0353 -0.0405 0.0877 131 THR A OG1 943 C CG2 . THR A 131 ? 0.4883 0.6163 0.4862 0.0362 -0.0418 0.0889 131 THR A CG2 944 N N . GLN A 132 ? 0.4491 0.5786 0.4487 0.0320 -0.0421 0.0783 132 GLN A N 945 C CA . GLN A 132 ? 0.4426 0.5669 0.4450 0.0309 -0.0420 0.0765 132 GLN A CA 946 C C . GLN A 132 ? 0.4495 0.5674 0.4548 0.0328 -0.0426 0.0803 132 GLN A C 947 O O . GLN A 132 ? 0.4381 0.5557 0.4432 0.0350 -0.0432 0.0843 132 GLN A O 948 C CB . GLN A 132 ? 0.4361 0.5650 0.4397 0.0313 -0.0433 0.0732 132 GLN A CB 949 C CG . GLN A 132 ? 0.4315 0.5677 0.4321 0.0289 -0.0430 0.0696 132 GLN A CG 950 C CD . GLN A 132 ? 0.4423 0.5834 0.4444 0.0286 -0.0441 0.0663 132 GLN A CD 951 O OE1 . GLN A 132 ? 0.4306 0.5677 0.4353 0.0283 -0.0441 0.0649 132 GLN A OE1 952 N NE2 . GLN A 132 ? 0.4121 0.5626 0.4127 0.0285 -0.0450 0.0649 132 GLN A NE2 953 N N . ASN A 133 ? 0.4434 0.5559 0.4510 0.0317 -0.0425 0.0790 133 ASN A N 954 C CA . ASN A 133 ? 0.4437 0.5496 0.4537 0.0330 -0.0434 0.0819 133 ASN A CA 955 C C . ASN A 133 ? 0.4191 0.5207 0.4291 0.0326 -0.0428 0.0863 133 ASN A C 956 O O . ASN A 133 ? 0.4069 0.5047 0.4175 0.0342 -0.0440 0.0899 133 ASN A O 957 C CB . ASN A 133 ? 0.4796 0.5869 0.4901 0.0367 -0.0454 0.0830 133 ASN A CB 958 C CG . ASN A 133 ? 0.5408 0.6517 0.5522 0.0373 -0.0461 0.0790 133 ASN A CG 959 O OD1 . ASN A 133 ? 0.5174 0.6297 0.5291 0.0346 -0.0452 0.0752 133 ASN A OD1 960 N ND2 . ASN A 133 ? 0.6376 0.7500 0.6493 0.0411 -0.0477 0.0799 133 ASN A ND2 961 N N . GLY A 134 ? 0.4087 0.5107 0.4175 0.0305 -0.0410 0.0863 134 GLY A N 962 C CA . GLY A 134 ? 0.4112 0.5100 0.4205 0.0298 -0.0403 0.0906 134 GLY A CA 963 C C . GLY A 134 ? 0.4381 0.5301 0.4500 0.0288 -0.0410 0.0920 134 GLY A C 964 O O . GLY A 134 ? 0.4352 0.5247 0.4485 0.0279 -0.0412 0.0889 134 GLY A O 965 N N . THR A 135 ? 0.4394 0.5284 0.4517 0.0288 -0.0415 0.0968 135 THR A N 966 C CA . THR A 135 ? 0.4285 0.5108 0.4428 0.0273 -0.0424 0.0986 135 THR A CA 967 C C . THR A 135 ? 0.4301 0.5117 0.4450 0.0251 -0.0414 0.1028 135 THR A C 968 O O . THR A 135 ? 0.4244 0.5107 0.4382 0.0253 -0.0400 0.1044 135 THR A O 969 C CB . THR A 135 ? 0.4461 0.5239 0.4596 0.0293 -0.0445 0.1004 135 THR A CB 970 O OG1 . THR A 135 ? 0.4375 0.5167 0.4493 0.0307 -0.0448 0.1046 135 THR A OG1 971 C CG2 . THR A 135 ? 0.4278 0.5076 0.4410 0.0320 -0.0454 0.0965 135 THR A CG2 972 N N . SER A 136 ? 0.4278 0.5036 0.4442 0.0230 -0.0422 0.1045 136 SER A N 973 C CA . SER A 136 ? 0.4207 0.4964 0.4381 0.0204 -0.0416 0.1086 136 SER A CA 974 C C . SER A 136 ? 0.4278 0.4962 0.4456 0.0182 -0.0434 0.1115 136 SER A C 975 O O . SER A 136 ? 0.4139 0.4764 0.4316 0.0183 -0.0448 0.1093 136 SER A O 976 C CB . SER A 136 ? 0.4128 0.4910 0.4316 0.0188 -0.0397 0.1066 136 SER A CB 977 O OG . SER A 136 ? 0.4043 0.4830 0.4246 0.0162 -0.0392 0.1105 136 SER A OG 978 N N . SER A 137 ? 0.4246 0.4933 0.4425 0.0160 -0.0433 0.1165 137 SER A N 979 C CA . SER A 137 ? 0.4353 0.4972 0.4530 0.0129 -0.0449 0.1198 137 SER A CA 980 C C . SER A 137 ? 0.4350 0.4954 0.4551 0.0098 -0.0448 0.1185 137 SER A C 981 O O . SER A 137 ? 0.4393 0.4929 0.4590 0.0070 -0.0464 0.1198 137 SER A O 982 C CB . SER A 137 ? 0.4393 0.5033 0.4564 0.0109 -0.0448 0.1258 137 SER A CB 983 O OG . SER A 137 ? 0.4183 0.4907 0.4375 0.0101 -0.0426 0.1269 137 SER A OG 984 N N . ALA A 138 ? 0.4316 0.4979 0.4536 0.0101 -0.0429 0.1160 138 ALA A N 985 C CA . ALA A 138 ? 0.4167 0.4821 0.4409 0.0079 -0.0425 0.1140 138 ALA A CA 986 C C . ALA A 138 ? 0.4235 0.4829 0.4475 0.0088 -0.0437 0.1092 138 ALA A C 987 O O . ALA A 138 ? 0.4383 0.4953 0.4637 0.0069 -0.0438 0.1076 138 ALA A O 988 C CB . ALA A 138 ? 0.3974 0.4702 0.4227 0.0088 -0.0399 0.1127 138 ALA A CB 989 N N . CYS A 139 ? 0.4215 0.4791 0.4436 0.0119 -0.0444 0.1071 139 CYS A N 990 C CA . CYS A 139 ? 0.4384 0.4917 0.4602 0.0133 -0.0453 0.1026 139 CYS A CA 991 C C . CYS A 139 ? 0.4462 0.4939 0.4655 0.0156 -0.0472 0.1031 139 CYS A C 992 O O . CYS A 139 ? 0.4511 0.5011 0.4695 0.0190 -0.0472 0.1007 139 CYS A O 993 C CB . CYS A 139 ? 0.4196 0.4784 0.4419 0.0154 -0.0437 0.0979 139 CYS A CB 994 S SG . CYS A 139 ? 0.4324 0.4875 0.4550 0.0166 -0.0445 0.0923 139 CYS A SG 995 N N . LYS A 140 ? 0.4735 0.5138 0.4912 0.0137 -0.0488 0.1062 140 LYS A N 996 C CA . LYS A 140 ? 0.5156 0.5494 0.5298 0.0160 -0.0505 0.1073 140 LYS A CA 997 C C . LYS A 140 ? 0.5235 0.5515 0.5366 0.0182 -0.0516 0.1034 140 LYS A C 998 O O . LYS A 140 ? 0.4996 0.5245 0.5139 0.0161 -0.0517 0.1013 140 LYS A O 999 C CB . LYS A 140 ? 0.5681 0.5951 0.5799 0.0130 -0.0518 0.1125 140 LYS A CB 1000 C CG . LYS A 140 ? 0.5955 0.6286 0.6079 0.0116 -0.0508 0.1169 140 LYS A CG 1001 C CD . LYS A 140 ? 0.6327 0.6589 0.6413 0.0102 -0.0523 0.1219 140 LYS A CD 1002 C CE . LYS A 140 ? 0.6546 0.6868 0.6643 0.0074 -0.0514 0.1267 140 LYS A CE 1003 N NZ . LYS A 140 ? 0.6760 0.7118 0.6889 0.0026 -0.0507 0.1278 140 LYS A NZ 1004 N N . ARG A 141 ? 0.5083 0.5355 0.5191 0.0226 -0.0522 0.1025 141 ARG A N 1005 C CA . ARG A 141 ? 0.5433 0.5652 0.5522 0.0256 -0.0532 0.0994 141 ARG A CA 1006 C C . ARG A 141 ? 0.6014 0.6159 0.6054 0.0287 -0.0547 0.1022 141 ARG A C 1007 O O . ARG A 141 ? 0.5626 0.5812 0.5655 0.0315 -0.0546 0.1038 141 ARG A O 1008 C CB . ARG A 141 ? 0.5337 0.5643 0.5449 0.0288 -0.0522 0.0950 141 ARG A CB 1009 C CG . ARG A 141 ? 0.5320 0.5593 0.5420 0.0321 -0.0530 0.0916 141 ARG A CG 1010 C CD . ARG A 141 ? 0.5146 0.5516 0.5271 0.0341 -0.0520 0.0872 141 ARG A CD 1011 N NE . ARG A 141 ? 0.5029 0.5421 0.5184 0.0310 -0.0509 0.0839 141 ARG A NE 1012 C CZ . ARG A 141 ? 0.4962 0.5422 0.5142 0.0285 -0.0493 0.0827 141 ARG A CZ 1013 N NH1 . ARG A 141 ? 0.4831 0.5350 0.5012 0.0285 -0.0486 0.0845 141 ARG A NH1 1014 N NH2 . ARG A 141 ? 0.4814 0.5279 0.5014 0.0262 -0.0485 0.0796 141 ARG A NH2 1015 N N . ARG A 142 ? 0.6421 0.6452 0.6425 0.0282 -0.0561 0.1027 142 ARG A N 1016 C CA . ARG A 142 ? 0.7042 0.6976 0.6984 0.0307 -0.0575 0.1057 142 ARG A CA 1017 C C . ARG A 142 ? 0.7000 0.6945 0.6931 0.0290 -0.0575 0.1106 142 ARG A C 1018 O O . ARG A 142 ? 0.7006 0.6963 0.6912 0.0329 -0.0576 0.1123 142 ARG A O 1019 C CB . ARG A 142 ? 0.7389 0.7338 0.7311 0.0376 -0.0577 0.1035 142 ARG A CB 1020 C CG . ARG A 142 ? 0.7887 0.7816 0.7813 0.0396 -0.0579 0.0990 142 ARG A CG 1021 C CD . ARG A 142 ? 0.8312 0.8286 0.8227 0.0465 -0.0578 0.0969 142 ARG A CD 1022 N NE . ARG A 142 ? 0.8591 0.8711 0.8556 0.0473 -0.0566 0.0950 142 ARG A NE 1023 C CZ . ARG A 142 ? 0.8770 0.8973 0.8779 0.0466 -0.0556 0.0909 142 ARG A CZ 1024 N NH1 . ARG A 142 ? 0.8548 0.8712 0.8565 0.0452 -0.0557 0.0880 142 ARG A NH1 1025 N NH2 . ARG A 142 ? 0.8926 0.9251 0.8968 0.0470 -0.0546 0.0896 142 ARG A NH2 1026 N N . SER A 143 ? 0.7076 0.7026 0.7027 0.0232 -0.0572 0.1129 143 SER A N 1027 C CA . SER A 143 ? 0.7167 0.7131 0.7111 0.0205 -0.0571 0.1180 143 SER A CA 1028 C C . SER A 143 ? 0.6832 0.6915 0.6805 0.0227 -0.0556 0.1186 143 SER A C 1029 O O . SER A 143 ? 0.7174 0.7281 0.7146 0.0204 -0.0553 0.1227 143 SER A O 1030 C CB . SER A 143 ? 0.7466 0.7306 0.7339 0.0209 -0.0587 0.1218 143 SER A CB 1031 O OG . SER A 143 ? 0.7915 0.7642 0.7757 0.0172 -0.0600 0.1220 143 SER A OG 1032 N N . ASN A 144 ? 0.6291 0.6448 0.6286 0.0269 -0.0548 0.1148 144 ASN A N 1033 C CA . ASN A 144 ? 0.6009 0.6276 0.6025 0.0289 -0.0535 0.1149 144 ASN A CA 1034 C C . ASN A 144 ? 0.5787 0.6145 0.5852 0.0264 -0.0518 0.1124 144 ASN A C 1035 O O . ASN A 144 ? 0.5492 0.5844 0.5579 0.0250 -0.0516 0.1091 144 ASN A O 1036 C CB . ASN A 144 ? 0.6120 0.6421 0.6125 0.0347 -0.0538 0.1122 144 ASN A CB 1037 C CG . ASN A 144 ? 0.6659 0.6874 0.6610 0.0384 -0.0553 0.1144 144 ASN A CG 1038 O OD1 . ASN A 144 ? 0.7164 0.7378 0.7100 0.0431 -0.0558 0.1120 144 ASN A OD1 1039 N ND2 . ASN A 144 ? 0.6353 0.6494 0.6268 0.0364 -0.0560 0.1192 144 ASN A ND2 1040 N N . ASN A 145 ? 0.5171 0.5610 0.5249 0.0262 -0.0505 0.1141 145 ASN A N 1041 C CA . ASN A 145 ? 0.4916 0.5441 0.5030 0.0248 -0.0487 0.1116 145 ASN A CA 1042 C C . ASN A 145 ? 0.4601 0.5158 0.4725 0.0273 -0.0484 0.1061 145 ASN A C 1043 O O . ASN A 145 ? 0.4335 0.4903 0.4444 0.0309 -0.0491 0.1049 145 ASN A O 1044 C CB . ASN A 145 ? 0.4932 0.5534 0.5044 0.0256 -0.0474 0.1138 145 ASN A CB 1045 C CG . ASN A 145 ? 0.4938 0.5537 0.5051 0.0224 -0.0470 0.1190 145 ASN A CG 1046 O OD1 . ASN A 145 ? 0.4802 0.5334 0.4911 0.0194 -0.0480 0.1214 145 ASN A OD1 1047 N ND2 . ASN A 145 ? 0.4861 0.5533 0.4976 0.0227 -0.0456 0.1206 145 ASN A ND2 1048 N N . SER A 146 ? 0.4494 0.5069 0.4642 0.0252 -0.0474 0.1029 146 SER A N 1049 C CA . SER A 146 ? 0.4197 0.4802 0.4354 0.0270 -0.0471 0.0977 146 SER A CA 1050 C C . SER A 146 ? 0.4092 0.4741 0.4269 0.0247 -0.0453 0.0950 146 SER A C 1051 O O . SER A 146 ? 0.3899 0.4576 0.4080 0.0229 -0.0440 0.0971 146 SER A O 1052 C CB . SER A 146 ? 0.4334 0.4865 0.4486 0.0277 -0.0486 0.0959 146 SER A CB 1053 O OG . SER A 146 ? 0.4286 0.4852 0.4442 0.0302 -0.0486 0.0915 146 SER A OG 1054 N N . PHE A 147 ? 0.3846 0.4501 0.4031 0.0249 -0.0450 0.0904 147 PHE A N 1055 C CA . PHE A 147 ? 0.3669 0.4360 0.3865 0.0231 -0.0432 0.0874 147 PHE A CA 1056 C C . PHE A 147 ? 0.3500 0.4164 0.3706 0.0227 -0.0435 0.0832 147 PHE A C 1057 O O . PHE A 147 ? 0.3404 0.4036 0.3609 0.0244 -0.0451 0.0824 147 PHE A O 1058 C CB . PHE A 147 ? 0.3593 0.4357 0.3773 0.0243 -0.0421 0.0858 147 PHE A CB 1059 C CG . PHE A 147 ? 0.3601 0.4393 0.3776 0.0225 -0.0399 0.0841 147 PHE A CG 1060 C CD1 . PHE A 147 ? 0.3596 0.4387 0.3772 0.0212 -0.0387 0.0872 147 PHE A CD1 1061 C CD2 . PHE A 147 ? 0.3611 0.4432 0.3774 0.0222 -0.0390 0.0795 147 PHE A CD2 1062 C CE1 . PHE A 147 ? 0.3636 0.4450 0.3800 0.0202 -0.0365 0.0857 147 PHE A CE1 1063 C CE2 . PHE A 147 ? 0.3631 0.4465 0.3778 0.0208 -0.0369 0.0779 147 PHE A CE2 1064 C CZ . PHE A 147 ? 0.3694 0.4523 0.3840 0.0201 -0.0356 0.0810 147 PHE A CZ 1065 N N . PHE A 148 ? 0.3365 0.4043 0.3578 0.0208 -0.0420 0.0806 148 PHE A N 1066 C CA . PHE A 148 ? 0.3411 0.4074 0.3631 0.0204 -0.0420 0.0763 148 PHE A CA 1067 C C . PHE A 148 ? 0.3404 0.4101 0.3617 0.0228 -0.0429 0.0736 148 PHE A C 1068 O O . PHE A 148 ? 0.3427 0.4182 0.3627 0.0237 -0.0424 0.0730 148 PHE A O 1069 C CB . PHE A 148 ? 0.3467 0.4153 0.3683 0.0185 -0.0399 0.0737 148 PHE A CB 1070 C CG . PHE A 148 ? 0.3438 0.4105 0.3662 0.0165 -0.0389 0.0762 148 PHE A CG 1071 C CD1 . PHE A 148 ? 0.3570 0.4188 0.3811 0.0149 -0.0395 0.0766 148 PHE A CD1 1072 C CD2 . PHE A 148 ? 0.3594 0.4295 0.3804 0.0164 -0.0373 0.0783 148 PHE A CD2 1073 C CE1 . PHE A 148 ? 0.3543 0.4155 0.3793 0.0131 -0.0386 0.0791 148 PHE A CE1 1074 C CE2 . PHE A 148 ? 0.3625 0.4320 0.3842 0.0150 -0.0362 0.0808 148 PHE A CE2 1075 C CZ . PHE A 148 ? 0.3645 0.4300 0.3884 0.0133 -0.0369 0.0813 148 PHE A CZ 1076 N N . SER A 149 ? 0.3351 0.4015 0.3571 0.0238 -0.0441 0.0719 149 SER A N 1077 C CA . SER A 149 ? 0.3360 0.4063 0.3575 0.0266 -0.0449 0.0698 149 SER A CA 1078 C C . SER A 149 ? 0.3295 0.4069 0.3507 0.0257 -0.0438 0.0658 149 SER A C 1079 O O . SER A 149 ? 0.3068 0.3904 0.3273 0.0276 -0.0443 0.0650 149 SER A O 1080 C CB . SER A 149 ? 0.3375 0.4026 0.3596 0.0281 -0.0462 0.0687 149 SER A CB 1081 O OG . SER A 149 ? 0.3215 0.3851 0.3447 0.0258 -0.0454 0.0654 149 SER A OG 1082 N N . ARG A 150 ? 0.2969 0.3735 0.3183 0.0228 -0.0424 0.0635 150 ARG A N 1083 C CA . ARG A 150 ? 0.3012 0.3831 0.3215 0.0214 -0.0414 0.0595 150 ARG A CA 1084 C C . ARG A 150 ? 0.2995 0.3850 0.3173 0.0199 -0.0399 0.0595 150 ARG A C 1085 O O . ARG A 150 ? 0.2972 0.3862 0.3129 0.0181 -0.0390 0.0563 150 ARG A O 1086 C CB . ARG A 150 ? 0.2935 0.3720 0.3144 0.0193 -0.0406 0.0563 150 ARG A CB 1087 C CG . ARG A 150 ? 0.2915 0.3656 0.3145 0.0207 -0.0419 0.0562 150 ARG A CG 1088 C CD . ARG A 150 ? 0.2973 0.3756 0.3206 0.0238 -0.0433 0.0555 150 ARG A CD 1089 N NE . ARG A 150 ? 0.2921 0.3668 0.3164 0.0250 -0.0441 0.0541 150 ARG A NE 1090 C CZ . ARG A 150 ? 0.2918 0.3694 0.3163 0.0283 -0.0452 0.0533 150 ARG A CZ 1091 N NH1 . ARG A 150 ? 0.2918 0.3764 0.3157 0.0306 -0.0458 0.0540 150 ARG A NH1 1092 N NH2 . ARG A 150 ? 0.2813 0.3549 0.3064 0.0295 -0.0458 0.0520 150 ARG A NH2 1093 N N . LEU A 151 ? 0.2975 0.3818 0.3148 0.0205 -0.0397 0.0633 151 LEU A N 1094 C CA . LEU A 151 ? 0.3001 0.3872 0.3145 0.0195 -0.0382 0.0637 151 LEU A CA 1095 C C . LEU A 151 ? 0.3089 0.4003 0.3226 0.0216 -0.0391 0.0664 151 LEU A C 1096 O O . LEU A 151 ? 0.3184 0.4088 0.3339 0.0238 -0.0406 0.0691 151 LEU A O 1097 C CB . LEU A 151 ? 0.2942 0.3770 0.3084 0.0183 -0.0368 0.0657 151 LEU A CB 1098 C CG . LEU A 151 ? 0.2961 0.3750 0.3105 0.0162 -0.0357 0.0629 151 LEU A CG 1099 C CD1 . LEU A 151 ? 0.2808 0.3562 0.2956 0.0156 -0.0345 0.0656 151 LEU A CD1 1100 C CD2 . LEU A 151 ? 0.2877 0.3686 0.2985 0.0145 -0.0342 0.0587 151 LEU A CD2 1101 N N . ASN A 152 ? 0.3249 0.4203 0.3354 0.0209 -0.0380 0.0658 152 ASN A N 1102 C CA . ASN A 152 ? 0.3205 0.4211 0.3298 0.0227 -0.0388 0.0678 152 ASN A CA 1103 C C . ASN A 152 ? 0.3306 0.4311 0.3369 0.0221 -0.0371 0.0697 152 ASN A C 1104 O O . ASN A 152 ? 0.3335 0.4350 0.3361 0.0203 -0.0356 0.0671 152 ASN A O 1105 C CB . ASN A 152 ? 0.3174 0.4245 0.3251 0.0224 -0.0394 0.0644 152 ASN A CB 1106 C CG . ASN A 152 ? 0.3387 0.4520 0.3456 0.0246 -0.0405 0.0664 152 ASN A CG 1107 O OD1 . ASN A 152 ? 0.3292 0.4415 0.3360 0.0263 -0.0407 0.0702 152 ASN A OD1 1108 N ND2 . ASN A 152 ? 0.3274 0.4476 0.3336 0.0246 -0.0414 0.0638 152 ASN A ND2 1109 N N . TRP A 153 ? 0.3455 0.4444 0.3529 0.0236 -0.0374 0.0741 153 TRP A N 1110 C CA . TRP A 153 ? 0.3538 0.4532 0.3587 0.0235 -0.0358 0.0766 153 TRP A CA 1111 C C . TRP A 153 ? 0.3735 0.4786 0.3756 0.0247 -0.0361 0.0769 153 TRP A C 1112 O O . TRP A 153 ? 0.3819 0.4890 0.3853 0.0267 -0.0376 0.0796 153 TRP A O 1113 C CB . TRP A 153 ? 0.3510 0.4474 0.3585 0.0243 -0.0361 0.0814 153 TRP A CB 1114 C CG . TRP A 153 ? 0.3460 0.4427 0.3516 0.0242 -0.0342 0.0842 153 TRP A CG 1115 C CD1 . TRP A 153 ? 0.3475 0.4465 0.3488 0.0241 -0.0322 0.0830 153 TRP A CD1 1116 C CD2 . TRP A 153 ? 0.3448 0.4397 0.3525 0.0241 -0.0340 0.0889 153 TRP A CD2 1117 N NE1 . TRP A 153 ? 0.3436 0.4425 0.3444 0.0245 -0.0308 0.0866 153 TRP A NE1 1118 C CE2 . TRP A 153 ? 0.3473 0.4444 0.3521 0.0244 -0.0317 0.0903 153 TRP A CE2 1119 C CE3 . TRP A 153 ? 0.3588 0.4505 0.3701 0.0237 -0.0354 0.0920 153 TRP A CE3 1120 C CZ2 . TRP A 153 ? 0.3536 0.4511 0.3598 0.0244 -0.0309 0.0948 153 TRP A CZ2 1121 C CZ3 . TRP A 153 ? 0.3624 0.4539 0.3746 0.0231 -0.0347 0.0965 153 TRP A CZ3 1122 C CH2 . TRP A 153 ? 0.3551 0.4501 0.3652 0.0234 -0.0325 0.0979 153 TRP A CH2 1123 N N . LEU A 154 ? 0.3805 0.4876 0.3782 0.0233 -0.0348 0.0740 154 LEU A N 1124 C CA . LEU A 154 ? 0.3810 0.4936 0.3752 0.0239 -0.0350 0.0738 154 LEU A CA 1125 C C . LEU A 154 ? 0.3906 0.5029 0.3822 0.0249 -0.0336 0.0772 154 LEU A C 1126 O O . LEU A 154 ? 0.3602 0.4688 0.3503 0.0243 -0.0316 0.0776 154 LEU A O 1127 C CB . LEU A 154 ? 0.3874 0.5017 0.3772 0.0213 -0.0343 0.0689 154 LEU A CB 1128 C CG . LEU A 154 ? 0.3886 0.5033 0.3802 0.0197 -0.0353 0.0651 154 LEU A CG 1129 C CD1 . LEU A 154 ? 0.4005 0.5159 0.3869 0.0163 -0.0343 0.0605 154 LEU A CD1 1130 C CD2 . LEU A 154 ? 0.3821 0.5026 0.3772 0.0216 -0.0377 0.0658 154 LEU A CD2 1131 N N . THR A 155 ? 0.3924 0.5090 0.3833 0.0267 -0.0345 0.0797 155 THR A N 1132 C CA . THR A 155 ? 0.4078 0.5250 0.3960 0.0278 -0.0331 0.0829 155 THR A CA 1133 C C . THR A 155 ? 0.4168 0.5397 0.4010 0.0283 -0.0336 0.0822 155 THR A C 1134 O O . THR A 155 ? 0.3984 0.5250 0.3824 0.0277 -0.0351 0.0795 155 THR A O 1135 C CB . THR A 155 ? 0.4130 0.5291 0.4051 0.0296 -0.0337 0.0883 155 THR A CB 1136 O OG1 . THR A 155 ? 0.4220 0.5401 0.4168 0.0311 -0.0361 0.0897 155 THR A OG1 1137 C CG2 . THR A 155 ? 0.4222 0.5330 0.4176 0.0285 -0.0331 0.0892 155 THR A CG2 1138 N N . HIS A 156 ? 0.4387 0.5626 0.4196 0.0294 -0.0324 0.0847 156 HIS A N 1139 C CA . HIS A 156 ? 0.4566 0.5857 0.4330 0.0297 -0.0328 0.0840 156 HIS A CA 1140 C C . HIS A 156 ? 0.4606 0.5949 0.4398 0.0314 -0.0353 0.0855 156 HIS A C 1141 O O . HIS A 156 ? 0.4558 0.5890 0.4399 0.0330 -0.0365 0.0884 156 HIS A O 1142 C CB . HIS A 156 ? 0.4731 0.6020 0.4454 0.0310 -0.0309 0.0868 156 HIS A CB 1143 C CG . HIS A 156 ? 0.4799 0.6099 0.4557 0.0335 -0.0314 0.0925 156 HIS A CG 1144 N ND1 . HIS A 156 ? 0.4869 0.6213 0.4641 0.0352 -0.0333 0.0948 156 HIS A ND1 1145 C CD2 . HIS A 156 ? 0.4814 0.6089 0.4593 0.0344 -0.0301 0.0966 156 HIS A CD2 1146 C CE1 . HIS A 156 ? 0.4887 0.6225 0.4685 0.0368 -0.0332 0.0999 156 HIS A CE1 1147 N NE2 . HIS A 156 ? 0.4923 0.6222 0.4727 0.0361 -0.0313 0.1010 156 HIS A NE2 1148 N N . LEU A 157 ? 0.4910 0.6310 0.4667 0.0310 -0.0361 0.0835 157 LEU A N 1149 C CA . LEU A 157 ? 0.4970 0.6434 0.4742 0.0331 -0.0383 0.0851 157 LEU A CA 1150 C C . LEU A 157 ? 0.5234 0.6734 0.4958 0.0340 -0.0378 0.0868 157 LEU A C 1151 O O . LEU A 157 ? 0.5143 0.6656 0.4811 0.0318 -0.0369 0.0838 157 LEU A O 1152 C CB . LEU A 157 ? 0.4941 0.6455 0.4714 0.0315 -0.0398 0.0810 157 LEU A CB 1153 C CG . LEU A 157 ? 0.4807 0.6403 0.4593 0.0339 -0.0421 0.0823 157 LEU A CG 1154 C CD1 . LEU A 157 ? 0.4746 0.6322 0.4586 0.0375 -0.0433 0.0859 157 LEU A CD1 1155 C CD2 . LEU A 157 ? 0.4816 0.6478 0.4594 0.0317 -0.0433 0.0779 157 LEU A CD2 1156 N N . LYS A 158 ? 0.5498 0.7009 0.5239 0.0369 -0.0383 0.0916 158 LYS A N 1157 C CA . LYS A 158 ? 0.5749 0.7294 0.5447 0.0381 -0.0378 0.0938 158 LYS A CA 1158 C C . LYS A 158 ? 0.5796 0.7304 0.5444 0.0367 -0.0351 0.0930 158 LYS A C 1159 O O . LYS A 158 ? 0.5824 0.7356 0.5412 0.0360 -0.0345 0.0914 158 LYS A O 1160 C CB . LYS A 158 ? 0.6022 0.7645 0.5691 0.0379 -0.0394 0.0916 158 LYS A CB 1161 C CG . LYS A 158 ? 0.6275 0.7947 0.5987 0.0397 -0.0419 0.0919 158 LYS A CG 1162 C CD . LYS A 158 ? 0.6646 0.8302 0.6394 0.0435 -0.0427 0.0973 158 LYS A CD 1163 C CE . LYS A 158 ? 0.6870 0.8599 0.6623 0.0465 -0.0450 0.0986 158 LYS A CE 1164 N NZ . LYS A 158 ? 0.7006 0.8784 0.6778 0.0459 -0.0465 0.0949 158 LYS A NZ 1165 N N . PHE A 159 ? 0.5433 0.6881 0.5101 0.0364 -0.0335 0.0939 159 PHE A N 1166 C CA . PHE A 159 ? 0.5401 0.6811 0.5023 0.0358 -0.0308 0.0934 159 PHE A CA 1167 C C . PHE A 159 ? 0.5298 0.6694 0.4855 0.0331 -0.0299 0.0880 159 PHE A C 1168 O O . PHE A 159 ? 0.5137 0.6509 0.4631 0.0331 -0.0278 0.0874 159 PHE A O 1169 C CB . PHE A 159 ? 0.5699 0.7129 0.5295 0.0381 -0.0297 0.0977 159 PHE A CB 1170 C CG . PHE A 159 ? 0.5965 0.7406 0.5615 0.0402 -0.0307 0.1031 159 PHE A CG 1171 C CD1 . PHE A 159 ? 0.6011 0.7416 0.5703 0.0403 -0.0298 0.1061 159 PHE A CD1 1172 C CD2 . PHE A 159 ? 0.6166 0.7655 0.5824 0.0418 -0.0327 0.1053 159 PHE A CD2 1173 C CE1 . PHE A 159 ? 0.6240 0.7648 0.5976 0.0416 -0.0309 0.1111 159 PHE A CE1 1174 C CE2 . PHE A 159 ? 0.6253 0.7741 0.5953 0.0436 -0.0336 0.1103 159 PHE A CE2 1175 C CZ . PHE A 159 ? 0.6372 0.7817 0.6109 0.0433 -0.0327 0.1132 159 PHE A CZ 1176 N N . LYS A 160 ? 0.5328 0.6736 0.4897 0.0309 -0.0314 0.0841 160 LYS A N 1177 C CA . LYS A 160 ? 0.5354 0.6738 0.4866 0.0276 -0.0307 0.0788 160 LYS A CA 1178 C C . LYS A 160 ? 0.5165 0.6512 0.4715 0.0257 -0.0308 0.0761 160 LYS A C 1179 O O . LYS A 160 ? 0.4763 0.6132 0.4381 0.0263 -0.0326 0.0770 160 LYS A O 1180 C CB . LYS A 160 ? 0.5758 0.7207 0.5236 0.0258 -0.0325 0.0761 160 LYS A CB 1181 C CG . LYS A 160 ? 0.6263 0.7736 0.5674 0.0265 -0.0319 0.0771 160 LYS A CG 1182 C CD . LYS A 160 ? 0.6581 0.8118 0.5953 0.0238 -0.0338 0.0738 160 LYS A CD 1183 C CE . LYS A 160 ? 0.6881 0.8457 0.6200 0.0250 -0.0339 0.0756 160 LYS A CE 1184 N NZ . LYS A 160 ? 0.7001 0.8510 0.6235 0.0247 -0.0311 0.0748 160 LYS A NZ 1185 N N . TYR A 161 ? 0.5111 0.6399 0.4612 0.0235 -0.0289 0.0728 161 TYR A N 1186 C CA . TYR A 161 ? 0.5007 0.6259 0.4531 0.0213 -0.0289 0.0697 161 TYR A CA 1187 C C . TYR A 161 ? 0.5015 0.6241 0.4458 0.0174 -0.0282 0.0645 161 TYR A C 1188 O O . TYR A 161 ? 0.4910 0.6066 0.4292 0.0168 -0.0258 0.0630 161 TYR A O 1189 C CB . TYR A 161 ? 0.5070 0.6260 0.4620 0.0228 -0.0271 0.0717 161 TYR A CB 1190 C CG . TYR A 161 ? 0.4866 0.6025 0.4461 0.0213 -0.0274 0.0697 161 TYR A CG 1191 C CD1 . TYR A 161 ? 0.4908 0.6033 0.4463 0.0181 -0.0269 0.0648 161 TYR A CD1 1192 C CD2 . TYR A 161 ? 0.4793 0.5952 0.4468 0.0229 -0.0284 0.0726 161 TYR A CD2 1193 C CE1 . TYR A 161 ? 0.4820 0.5917 0.4415 0.0168 -0.0271 0.0630 161 TYR A CE1 1194 C CE2 . TYR A 161 ? 0.4751 0.5879 0.4463 0.0216 -0.0287 0.0708 161 TYR A CE2 1195 C CZ . TYR A 161 ? 0.4788 0.5888 0.4463 0.0187 -0.0280 0.0660 161 TYR A CZ 1196 O OH . TYR A 161 ? 0.4691 0.5761 0.4403 0.0175 -0.0283 0.0642 161 TYR A OH 1197 N N . PRO A 162 ? 0.5025 0.6309 0.4463 0.0149 -0.0302 0.0618 162 PRO A N 1198 C CA . PRO A 162 ? 0.5224 0.6488 0.4580 0.0104 -0.0297 0.0570 162 PRO A CA 1199 C C . PRO A 162 ? 0.5289 0.6488 0.4643 0.0080 -0.0287 0.0538 162 PRO A C 1200 O O . PRO A 162 ? 0.5337 0.6545 0.4769 0.0089 -0.0295 0.0546 162 PRO A O 1201 C CB . PRO A 162 ? 0.5248 0.6611 0.4622 0.0085 -0.0325 0.0556 162 PRO A CB 1202 C CG . PRO A 162 ? 0.5274 0.6689 0.4750 0.0116 -0.0343 0.0587 162 PRO A CG 1203 C CD . PRO A 162 ? 0.5255 0.6623 0.4763 0.0158 -0.0330 0.0631 162 PRO A CD 1204 N N . ALA A 163 ? 0.5354 0.6482 0.4616 0.0051 -0.0269 0.0504 163 ALA A N 1205 C CA . ALA A 163 ? 0.5479 0.6533 0.4725 0.0029 -0.0255 0.0475 163 ALA A CA 1206 C C . ALA A 163 ? 0.5411 0.6517 0.4718 0.0003 -0.0277 0.0454 163 ALA A C 1207 O O . ALA A 163 ? 0.5240 0.6416 0.4538 -0.0026 -0.0295 0.0436 163 ALA A O 1208 C CB . ALA A 163 ? 0.5773 0.6748 0.4893 -0.0004 -0.0237 0.0437 163 ALA A CB 1209 N N . LEU A 164 ? 0.5200 0.6279 0.4569 0.0014 -0.0274 0.0459 164 LEU A N 1210 C CA . LEU A 164 ? 0.5082 0.6203 0.4507 -0.0006 -0.0291 0.0439 164 LEU A CA 1211 C C . LEU A 164 ? 0.4868 0.5931 0.4227 -0.0054 -0.0280 0.0393 164 LEU A C 1212 O O . LEU A 164 ? 0.4882 0.5850 0.4192 -0.0054 -0.0256 0.0385 164 LEU A O 1213 C CB . LEU A 164 ? 0.5024 0.6139 0.4543 0.0026 -0.0294 0.0466 164 LEU A CB 1214 C CG . LEU A 164 ? 0.5174 0.6338 0.4758 0.0071 -0.0306 0.0513 164 LEU A CG 1215 C CD1 . LEU A 164 ? 0.5119 0.6250 0.4775 0.0097 -0.0305 0.0538 164 LEU A CD1 1216 C CD2 . LEU A 164 ? 0.5185 0.6450 0.4800 0.0071 -0.0332 0.0515 164 LEU A CD2 1217 N N . ASN A 165 ? 0.4768 0.5892 0.4124 -0.0095 -0.0297 0.0364 165 ASN A N 1218 C CA . ASN A 165 ? 0.5052 0.6133 0.4352 -0.0147 -0.0290 0.0320 165 ASN A CA 1219 C C . ASN A 165 ? 0.5088 0.6261 0.4457 -0.0165 -0.0312 0.0308 165 ASN A C 1220 O O . ASN A 165 ? 0.5177 0.6435 0.4534 -0.0199 -0.0329 0.0292 165 ASN A O 1221 C CB . ASN A 165 ? 0.5289 0.6341 0.4470 -0.0191 -0.0283 0.0292 165 ASN A CB 1222 C CG . ASN A 165 ? 0.5546 0.6541 0.4656 -0.0251 -0.0276 0.0247 165 ASN A CG 1223 O OD1 . ASN A 165 ? 0.5664 0.6565 0.4756 -0.0250 -0.0256 0.0237 165 ASN A OD1 1224 N ND2 . ASN A 165 ? 0.5774 0.6828 0.4842 -0.0307 -0.0291 0.0220 165 ASN A ND2 1225 N N . VAL A 166 ? 0.5080 0.6241 0.4524 -0.0141 -0.0312 0.0317 166 VAL A N 1226 C CA . VAL A 166 ? 0.4822 0.6076 0.4350 -0.0137 -0.0334 0.0318 166 VAL A CA 1227 C C . VAL A 166 ? 0.4807 0.6031 0.4340 -0.0168 -0.0329 0.0288 166 VAL A C 1228 O O . VAL A 166 ? 0.4606 0.5729 0.4118 -0.0167 -0.0310 0.0281 166 VAL A O 1229 C CB . VAL A 166 ? 0.4798 0.6073 0.4416 -0.0076 -0.0342 0.0361 166 VAL A CB 1230 C CG1 . VAL A 166 ? 0.4857 0.6218 0.4552 -0.0065 -0.0363 0.0361 166 VAL A CG1 1231 C CG2 . VAL A 166 ? 0.4932 0.6241 0.4544 -0.0047 -0.0348 0.0392 166 VAL A CG2 1232 N N . THR A 167 ? 0.4713 0.6031 0.4276 -0.0192 -0.0346 0.0271 167 THR A N 1233 C CA . THR A 167 ? 0.4960 0.6267 0.4518 -0.0231 -0.0343 0.0238 167 THR A CA 1234 C C . THR A 167 ? 0.4785 0.6163 0.4440 -0.0202 -0.0358 0.0248 167 THR A C 1235 O O . THR A 167 ? 0.4989 0.6459 0.4701 -0.0167 -0.0377 0.0271 167 THR A O 1236 C CB . THR A 167 ? 0.5300 0.6659 0.4789 -0.0298 -0.0349 0.0205 167 THR A CB 1237 O OG1 . THR A 167 ? 0.5826 0.7122 0.5271 -0.0347 -0.0337 0.0170 167 THR A OG1 1238 C CG2 . THR A 167 ? 0.5365 0.6881 0.4911 -0.0300 -0.0375 0.0208 167 THR A CG2 1239 N N . MET A 168 ? 0.4470 0.5801 0.4139 -0.0214 -0.0350 0.0231 168 MET A N 1240 C CA . MET A 168 ? 0.4320 0.5719 0.4066 -0.0196 -0.0363 0.0232 168 MET A CA 1241 C C . MET A 168 ? 0.4426 0.5802 0.4150 -0.0243 -0.0355 0.0196 168 MET A C 1242 O O . MET A 168 ? 0.4353 0.5624 0.4063 -0.0244 -0.0338 0.0189 168 MET A O 1243 C CB . MET A 168 ? 0.4185 0.5539 0.3998 -0.0134 -0.0363 0.0264 168 MET A CB 1244 C CG . MET A 168 ? 0.4004 0.5422 0.3894 -0.0104 -0.0378 0.0270 168 MET A CG 1245 S SD . MET A 168 ? 0.3934 0.5507 0.3861 -0.0079 -0.0403 0.0286 168 MET A SD 1246 C CE . MET A 168 ? 0.3988 0.5526 0.3924 -0.0028 -0.0406 0.0330 168 MET A CE 1247 N N . PRO A 169 ? 0.4504 0.5982 0.4224 -0.0283 -0.0366 0.0174 169 PRO A N 1248 C CA . PRO A 169 ? 0.4376 0.5843 0.4075 -0.0333 -0.0359 0.0141 169 PRO A CA 1249 C C . PRO A 169 ? 0.4151 0.5623 0.3925 -0.0298 -0.0361 0.0146 169 PRO A C 1250 O O . PRO A 169 ? 0.3973 0.5509 0.3818 -0.0245 -0.0375 0.0170 169 PRO A O 1251 C CB . PRO A 169 ? 0.4516 0.6117 0.4199 -0.0380 -0.0375 0.0125 169 PRO A CB 1252 C CG . PRO A 169 ? 0.4586 0.6295 0.4327 -0.0331 -0.0394 0.0155 169 PRO A CG 1253 C CD . PRO A 169 ? 0.4536 0.6153 0.4271 -0.0285 -0.0387 0.0182 169 PRO A CD 1254 N N . ASN A 170 ? 0.4035 0.5432 0.3786 -0.0326 -0.0347 0.0123 170 ASN A N 1255 C CA . ASN A 170 ? 0.3989 0.5398 0.3800 -0.0306 -0.0348 0.0120 170 ASN A CA 1256 C C . ASN A 170 ? 0.3979 0.5490 0.3788 -0.0354 -0.0355 0.0094 170 ASN A C 1257 O O . ASN A 170 ? 0.3868 0.5337 0.3622 -0.0411 -0.0343 0.0066 170 ASN A O 1258 C CB . ASN A 170 ? 0.3952 0.5223 0.3744 -0.0305 -0.0328 0.0113 170 ASN A CB 1259 C CG . ASN A 170 ? 0.3958 0.5236 0.3810 -0.0283 -0.0330 0.0110 170 ASN A CG 1260 O OD1 . ASN A 170 ? 0.3784 0.5169 0.3687 -0.0271 -0.0345 0.0111 170 ASN A OD1 1261 N ND2 . ASN A 170 ? 0.3967 0.5133 0.3812 -0.0276 -0.0315 0.0108 170 ASN A ND2 1262 N N . ASN A 171 ? 0.4169 0.5817 0.4036 -0.0329 -0.0374 0.0106 171 ASN A N 1263 C CA . ASN A 171 ? 0.4443 0.6214 0.4322 -0.0366 -0.0382 0.0087 171 ASN A CA 1264 C C . ASN A 171 ? 0.4542 0.6339 0.4486 -0.0331 -0.0383 0.0088 171 ASN A C 1265 O O . ASN A 171 ? 0.4538 0.6461 0.4510 -0.0340 -0.0392 0.0081 171 ASN A O 1266 C CB . ASN A 171 ? 0.4467 0.6390 0.4358 -0.0366 -0.0401 0.0098 171 ASN A CB 1267 C CG . ASN A 171 ? 0.4624 0.6524 0.4441 -0.0412 -0.0400 0.0092 171 ASN A CG 1268 O OD1 . ASN A 171 ? 0.4711 0.6536 0.4452 -0.0477 -0.0387 0.0066 171 ASN A OD1 1269 N ND2 . ASN A 171 ? 0.4737 0.6689 0.4568 -0.0377 -0.0412 0.0117 171 ASN A ND2 1270 N N . GLU A 172 ? 0.4449 0.6127 0.4411 -0.0291 -0.0373 0.0097 172 GLU A N 1271 C CA . GLU A 172 ? 0.4516 0.6192 0.4532 -0.0257 -0.0373 0.0096 172 GLU A CA 1272 C C . GLU A 172 ? 0.4564 0.6175 0.4542 -0.0311 -0.0356 0.0066 172 GLU A C 1273 O O . GLU A 172 ? 0.4456 0.6003 0.4364 -0.0366 -0.0345 0.0049 172 GLU A O 1274 C CB . GLU A 172 ? 0.4582 0.6158 0.4633 -0.0192 -0.0371 0.0122 172 GLU A CB 1275 C CG . GLU A 172 ? 0.4783 0.6394 0.4862 -0.0139 -0.0385 0.0154 172 GLU A CG 1276 C CD . GLU A 172 ? 0.4965 0.6718 0.5091 -0.0104 -0.0402 0.0164 172 GLU A CD 1277 O OE1 . GLU A 172 ? 0.5210 0.7011 0.5363 -0.0098 -0.0403 0.0153 172 GLU A OE1 1278 O OE2 . GLU A 172 ? 0.5003 0.6821 0.5136 -0.0080 -0.0414 0.0185 172 GLU A OE2 1279 N N . LYS A 173 ? 0.4655 0.6275 0.4673 -0.0292 -0.0355 0.0060 173 LYS A N 1280 C CA . LYS A 173 ? 0.4946 0.6495 0.4931 -0.0336 -0.0339 0.0034 173 LYS A CA 1281 C C . LYS A 173 ? 0.4654 0.6055 0.4642 -0.0305 -0.0327 0.0040 173 LYS A C 1282 O O . LYS A 173 ? 0.4610 0.5942 0.4574 -0.0332 -0.0313 0.0021 173 LYS A O 1283 C CB . LYS A 173 ? 0.5491 0.7146 0.5509 -0.0347 -0.0343 0.0020 173 LYS A CB 1284 C CG . LYS A 173 ? 0.5923 0.7625 0.6016 -0.0274 -0.0352 0.0037 173 LYS A CG 1285 C CD . LYS A 173 ? 0.6384 0.8221 0.6503 -0.0286 -0.0356 0.0024 173 LYS A CD 1286 C CE . LYS A 173 ? 0.6584 0.8466 0.6768 -0.0209 -0.0365 0.0040 173 LYS A CE 1287 N NZ . LYS A 173 ? 0.6711 0.8756 0.6923 -0.0211 -0.0370 0.0034 173 LYS A NZ 1288 N N . PHE A 174 ? 0.4369 0.5723 0.4382 -0.0252 -0.0332 0.0067 174 PHE A N 1289 C CA . PHE A 174 ? 0.4113 0.5334 0.4128 -0.0226 -0.0322 0.0077 174 PHE A CA 1290 C C . PHE A 174 ? 0.4080 0.5224 0.4055 -0.0226 -0.0316 0.0092 174 PHE A C 1291 O O . PHE A 174 ? 0.3886 0.5081 0.3844 -0.0234 -0.0322 0.0099 174 PHE A O 1292 C CB . PHE A 174 ? 0.4160 0.5381 0.4241 -0.0160 -0.0334 0.0100 174 PHE A CB 1293 C CG . PHE A 174 ? 0.4247 0.5548 0.4363 -0.0118 -0.0351 0.0125 174 PHE A CG 1294 C CD1 . PHE A 174 ? 0.4131 0.5390 0.4242 -0.0096 -0.0354 0.0151 174 PHE A CD1 1295 C CD2 . PHE A 174 ? 0.4277 0.5697 0.4428 -0.0099 -0.0364 0.0125 174 PHE A CD2 1296 C CE1 . PHE A 174 ? 0.4204 0.5533 0.4343 -0.0057 -0.0370 0.0174 174 PHE A CE1 1297 C CE2 . PHE A 174 ? 0.4276 0.5767 0.4454 -0.0055 -0.0379 0.0149 174 PHE A CE2 1298 C CZ . PHE A 174 ? 0.4310 0.5752 0.4481 -0.0035 -0.0382 0.0174 174 PHE A CZ 1299 N N . ASP A 175 ? 0.3897 0.4924 0.3859 -0.0215 -0.0303 0.0098 175 ASP A N 1300 C CA . ASP A 175 ? 0.3835 0.4788 0.3761 -0.0209 -0.0294 0.0114 175 ASP A CA 1301 C C . ASP A 175 ? 0.3656 0.4632 0.3632 -0.0156 -0.0309 0.0149 175 ASP A C 1302 O O . ASP A 175 ? 0.3710 0.4712 0.3744 -0.0119 -0.0321 0.0162 175 ASP A O 1303 C CB . ASP A 175 ? 0.4048 0.4881 0.3947 -0.0209 -0.0276 0.0112 175 ASP A CB 1304 C CG . ASP A 175 ? 0.4315 0.5101 0.4148 -0.0261 -0.0258 0.0079 175 ASP A CG 1305 O OD1 . ASP A 175 ? 0.4388 0.5227 0.4186 -0.0305 -0.0259 0.0058 175 ASP A OD1 1306 O OD2 . ASP A 175 ? 0.4267 0.4963 0.4080 -0.0260 -0.0244 0.0076 175 ASP A OD2 1307 N N . LYS A 176 ? 0.3429 0.4388 0.3375 -0.0154 -0.0306 0.0165 176 LYS A N 1308 C CA . LYS A 176 ? 0.3249 0.4218 0.3233 -0.0108 -0.0317 0.0200 176 LYS A CA 1309 C C . LYS A 176 ? 0.3163 0.4035 0.3127 -0.0096 -0.0304 0.0219 176 LYS A C 1310 O O . LYS A 176 ? 0.3139 0.3960 0.3042 -0.0122 -0.0286 0.0207 176 LYS A O 1311 C CB . LYS A 176 ? 0.3328 0.4374 0.3296 -0.0113 -0.0326 0.0207 176 LYS A CB 1312 C CG . LYS A 176 ? 0.3368 0.4531 0.3359 -0.0120 -0.0341 0.0195 176 LYS A CG 1313 C CD . LYS A 176 ? 0.3520 0.4753 0.3490 -0.0126 -0.0350 0.0204 176 LYS A CD 1314 C CE . LYS A 176 ? 0.3527 0.4894 0.3521 -0.0128 -0.0366 0.0197 176 LYS A CE 1315 N NZ . LYS A 176 ? 0.3585 0.5017 0.3556 -0.0133 -0.0375 0.0208 176 LYS A NZ 1316 N N . LEU A 177 ? 0.2967 0.3813 0.2979 -0.0056 -0.0311 0.0248 177 LEU A N 1317 C CA . LEU A 177 ? 0.2827 0.3600 0.2830 -0.0041 -0.0300 0.0272 177 LEU A CA 1318 C C . LEU A 177 ? 0.2743 0.3545 0.2760 -0.0015 -0.0310 0.0305 177 LEU A C 1319 O O . LEU A 177 ? 0.2702 0.3536 0.2766 0.0013 -0.0327 0.0325 177 LEU A O 1320 C CB . LEU A 177 ? 0.2761 0.3480 0.2804 -0.0022 -0.0302 0.0283 177 LEU A CB 1321 C CG . LEU A 177 ? 0.2749 0.3411 0.2796 -0.0003 -0.0295 0.0315 177 LEU A CG 1322 C CD1 . LEU A 177 ? 0.2775 0.3387 0.2762 -0.0021 -0.0271 0.0306 177 LEU A CD1 1323 C CD2 . LEU A 177 ? 0.2757 0.3379 0.2847 0.0011 -0.0302 0.0326 177 LEU A CD2 1324 N N . TYR A 178 ? 0.2846 0.3630 0.2816 -0.0023 -0.0297 0.0311 178 TYR A N 1325 C CA . TYR A 178 ? 0.2907 0.3716 0.2884 0.0000 -0.0304 0.0344 178 TYR A CA 1326 C C . TYR A 178 ? 0.2868 0.3617 0.2847 0.0019 -0.0293 0.0375 178 TYR A C 1327 O O . TYR A 178 ? 0.2919 0.3614 0.2859 0.0008 -0.0274 0.0367 178 TYR A O 1328 C CB . TYR A 178 ? 0.2950 0.3787 0.2868 -0.0020 -0.0297 0.0332 178 TYR A CB 1329 C CG . TYR A 178 ? 0.2967 0.3889 0.2889 -0.0036 -0.0312 0.0312 178 TYR A CG 1330 C CD1 . TYR A 178 ? 0.3062 0.4056 0.3020 -0.0011 -0.0331 0.0333 178 TYR A CD1 1331 C CD2 . TYR A 178 ? 0.2985 0.3918 0.2871 -0.0077 -0.0307 0.0274 178 TYR A CD2 1332 C CE1 . TYR A 178 ? 0.3106 0.4190 0.3069 -0.0022 -0.0344 0.0318 178 TYR A CE1 1333 C CE2 . TYR A 178 ? 0.3118 0.4144 0.3010 -0.0094 -0.0320 0.0258 178 TYR A CE2 1334 C CZ . TYR A 178 ? 0.3123 0.4229 0.3055 -0.0065 -0.0339 0.0280 178 TYR A CZ 1335 O OH . TYR A 178 ? 0.3229 0.4438 0.3168 -0.0078 -0.0353 0.0266 178 TYR A OH 1336 N N . ILE A 179 ? 0.2818 0.3580 0.2843 0.0048 -0.0307 0.0411 179 ILE A N 1337 C CA . ILE A 179 ? 0.2849 0.3573 0.2881 0.0065 -0.0300 0.0446 179 ILE A CA 1338 C C . ILE A 179 ? 0.2981 0.3738 0.3001 0.0079 -0.0301 0.0474 179 ILE A C 1339 O O . ILE A 179 ? 0.2842 0.3648 0.2883 0.0092 -0.0319 0.0484 179 ILE A O 1340 C CB . ILE A 179 ? 0.2864 0.3571 0.2954 0.0082 -0.0315 0.0470 179 ILE A CB 1341 C CG1 . ILE A 179 ? 0.2780 0.3459 0.2885 0.0071 -0.0317 0.0443 179 ILE A CG1 1342 C CG2 . ILE A 179 ? 0.2844 0.3518 0.2942 0.0093 -0.0308 0.0507 179 ILE A CG2 1343 C CD1 . ILE A 179 ? 0.2681 0.3312 0.2757 0.0054 -0.0296 0.0425 179 ILE A CD1 1344 N N . TRP A 180 ? 0.3032 0.3763 0.3015 0.0081 -0.0283 0.0487 180 TRP A N 1345 C CA . TRP A 180 ? 0.3087 0.3846 0.3051 0.0094 -0.0281 0.0512 180 TRP A CA 1346 C C . TRP A 180 ? 0.3138 0.3868 0.3092 0.0109 -0.0265 0.0543 180 TRP A C 1347 O O . TRP A 180 ? 0.3197 0.3888 0.3159 0.0108 -0.0256 0.0545 180 TRP A O 1348 C CB . TRP A 180 ? 0.3091 0.3871 0.2995 0.0076 -0.0274 0.0482 180 TRP A CB 1349 C CG . TRP A 180 ? 0.3086 0.3814 0.2929 0.0054 -0.0252 0.0449 180 TRP A CG 1350 C CD1 . TRP A 180 ? 0.3144 0.3854 0.2974 0.0028 -0.0251 0.0410 180 TRP A CD1 1351 C CD2 . TRP A 180 ? 0.3128 0.3810 0.2906 0.0058 -0.0227 0.0453 180 TRP A CD2 1352 N NE1 . TRP A 180 ? 0.3273 0.3922 0.3033 0.0013 -0.0227 0.0390 180 TRP A NE1 1353 C CE2 . TRP A 180 ? 0.3251 0.3878 0.2974 0.0033 -0.0212 0.0414 180 TRP A CE2 1354 C CE3 . TRP A 180 ? 0.3122 0.3801 0.2878 0.0081 -0.0215 0.0484 180 TRP A CE3 1355 C CZ2 . TRP A 180 ? 0.3320 0.3885 0.2965 0.0034 -0.0185 0.0406 180 TRP A CZ2 1356 C CZ3 . TRP A 180 ? 0.3247 0.3870 0.2927 0.0084 -0.0189 0.0476 180 TRP A CZ3 1357 C CH2 . TRP A 180 ? 0.3270 0.3834 0.2894 0.0062 -0.0174 0.0438 180 TRP A CH2 1358 N N . GLY A 181 ? 0.3201 0.3956 0.3139 0.0123 -0.0262 0.0570 181 GLY A N 1359 C CA . GLY A 181 ? 0.3286 0.4027 0.3221 0.0140 -0.0247 0.0606 181 GLY A CA 1360 C C . GLY A 181 ? 0.3468 0.4228 0.3358 0.0153 -0.0234 0.0623 181 GLY A C 1361 O O . GLY A 181 ? 0.3508 0.4296 0.3373 0.0149 -0.0240 0.0611 181 GLY A O 1362 N N . VAL A 182 ? 0.3527 0.4277 0.3408 0.0170 -0.0217 0.0653 182 VAL A N 1363 C CA . VAL A 182 ? 0.3580 0.4347 0.3418 0.0188 -0.0202 0.0675 182 VAL A CA 1364 C C . VAL A 182 ? 0.3582 0.4382 0.3469 0.0205 -0.0207 0.0729 182 VAL A C 1365 O O . VAL A 182 ? 0.3392 0.4184 0.3317 0.0205 -0.0206 0.0749 182 VAL A O 1366 C CB . VAL A 182 ? 0.3771 0.4494 0.3537 0.0197 -0.0171 0.0661 182 VAL A CB 1367 C CG1 . VAL A 182 ? 0.3870 0.4609 0.3589 0.0221 -0.0154 0.0686 182 VAL A CG1 1368 C CG2 . VAL A 182 ? 0.4046 0.4726 0.3756 0.0174 -0.0167 0.0607 182 VAL A CG2 1369 N N . HIS A 183 ? 0.3673 0.4512 0.3557 0.0216 -0.0212 0.0755 183 HIS A N 1370 C CA . HIS A 183 ? 0.3798 0.4670 0.3722 0.0229 -0.0216 0.0808 183 HIS A CA 1371 C C . HIS A 183 ? 0.3945 0.4830 0.3829 0.0251 -0.0189 0.0833 183 HIS A C 1372 O O . HIS A 183 ? 0.3769 0.4655 0.3592 0.0262 -0.0176 0.0821 183 HIS A O 1373 C CB . HIS A 183 ? 0.3876 0.4784 0.3820 0.0231 -0.0237 0.0825 183 HIS A CB 1374 C CG . HIS A 183 ? 0.4017 0.4955 0.3999 0.0239 -0.0243 0.0881 183 HIS A CG 1375 N ND1 . HIS A 183 ? 0.4158 0.5132 0.4120 0.0255 -0.0237 0.0912 183 HIS A ND1 1376 C CD2 . HIS A 183 ? 0.4167 0.5101 0.4203 0.0230 -0.0254 0.0914 183 HIS A CD2 1377 C CE1 . HIS A 183 ? 0.4143 0.5137 0.4146 0.0254 -0.0244 0.0961 183 HIS A CE1 1378 N NE2 . HIS A 183 ? 0.4154 0.5122 0.4200 0.0237 -0.0255 0.0962 183 HIS A NE2 1379 N N . HIS A 184 ? 0.3851 0.4747 0.3764 0.0257 -0.0181 0.0867 184 HIS A N 1380 C CA . HIS A 184 ? 0.3862 0.4780 0.3745 0.0283 -0.0154 0.0897 184 HIS A CA 1381 C C . HIS A 184 ? 0.3977 0.4952 0.3899 0.0288 -0.0162 0.0952 184 HIS A C 1382 O O . HIS A 184 ? 0.3933 0.4929 0.3912 0.0276 -0.0173 0.0986 184 HIS A O 1383 C CB . HIS A 184 ? 0.3863 0.4768 0.3755 0.0287 -0.0140 0.0901 184 HIS A CB 1384 C CG . HIS A 184 ? 0.3857 0.4700 0.3707 0.0282 -0.0130 0.0848 184 HIS A CG 1385 N ND1 . HIS A 184 ? 0.3855 0.4662 0.3624 0.0300 -0.0105 0.0822 184 HIS A ND1 1386 C CD2 . HIS A 184 ? 0.3824 0.4631 0.3702 0.0259 -0.0142 0.0819 184 HIS A CD2 1387 C CE1 . HIS A 184 ? 0.4019 0.4768 0.3764 0.0287 -0.0101 0.0779 184 HIS A CE1 1388 N NE2 . HIS A 184 ? 0.3781 0.4536 0.3597 0.0263 -0.0124 0.0778 184 HIS A NE2 1389 N N . PRO A 185 ? 0.4033 0.5033 0.3924 0.0302 -0.0159 0.0964 185 PRO A N 1390 C CA . PRO A 185 ? 0.3915 0.4968 0.3843 0.0304 -0.0168 0.1018 185 PRO A CA 1391 C C . PRO A 185 ? 0.3821 0.4920 0.3758 0.0319 -0.0148 0.1067 185 PRO A C 1392 O O . PRO A 185 ? 0.3914 0.5013 0.3809 0.0343 -0.0121 0.1061 185 PRO A O 1393 C CB . PRO A 185 ? 0.3978 0.5044 0.3863 0.0317 -0.0167 0.1013 185 PRO A CB 1394 C CG . PRO A 185 ? 0.4022 0.5042 0.3859 0.0312 -0.0166 0.0953 185 PRO A CG 1395 C CD . PRO A 185 ? 0.4093 0.5073 0.3915 0.0311 -0.0150 0.0928 185 PRO A CD 1396 N N . GLY A 186 ? 0.3915 0.5056 0.3906 0.0306 -0.0162 0.1116 186 GLY A N 1397 C CA . GLY A 186 ? 0.4107 0.5308 0.4116 0.0315 -0.0147 0.1168 186 GLY A CA 1398 C C . GLY A 186 ? 0.4335 0.5577 0.4292 0.0351 -0.0120 0.1186 186 GLY A C 1399 O O . GLY A 186 ? 0.4351 0.5626 0.4291 0.0375 -0.0094 0.1204 186 GLY A O 1400 N N . THR A 187 ? 0.4547 0.5788 0.4475 0.0359 -0.0124 0.1182 187 THR A N 1401 C CA . THR A 187 ? 0.4807 0.6085 0.4683 0.0394 -0.0100 0.1202 187 THR A CA 1402 C C . THR A 187 ? 0.4894 0.6134 0.4706 0.0406 -0.0098 0.1159 187 THR A C 1403 O O . THR A 187 ? 0.4886 0.6086 0.4705 0.0385 -0.0121 0.1124 187 THR A O 1404 C CB . THR A 187 ? 0.4835 0.6181 0.4747 0.0389 -0.0107 0.1263 187 THR A CB 1405 O OG1 . THR A 187 ? 0.4716 0.6041 0.4644 0.0369 -0.0135 0.1258 187 THR A OG1 1406 C CG2 . THR A 187 ? 0.4692 0.6082 0.4668 0.0367 -0.0112 0.1309 187 THR A CG2 1407 N N . ASP A 188 ? 0.5076 0.6331 0.4823 0.0440 -0.0072 0.1165 188 ASP A N 1408 C CA . ASP A 188 ? 0.5459 0.6687 0.5139 0.0450 -0.0070 0.1133 188 ASP A CA 1409 C C . ASP A 188 ? 0.5318 0.6568 0.5032 0.0431 -0.0098 0.1146 188 ASP A C 1410 O O . ASP A 188 ? 0.5173 0.6394 0.4860 0.0422 -0.0112 0.1108 188 ASP A O 1411 C CB . ASP A 188 ? 0.5817 0.7067 0.5426 0.0492 -0.0038 0.1151 188 ASP A CB 1412 C CG . ASP A 188 ? 0.6050 0.7258 0.5597 0.0518 -0.0007 0.1126 188 ASP A CG 1413 O OD1 . ASP A 188 ? 0.6166 0.7307 0.5693 0.0503 -0.0011 0.1077 188 ASP A OD1 1414 O OD2 . ASP A 188 ? 0.6534 0.7776 0.6049 0.0557 0.0020 0.1157 188 ASP A OD2 1415 N N . ASN A 189 ? 0.5313 0.6615 0.5083 0.0425 -0.0108 0.1200 189 ASN A N 1416 C CA . ASN A 189 ? 0.5571 0.6890 0.5374 0.0409 -0.0134 0.1218 189 ASN A CA 1417 C C . ASN A 189 ? 0.5349 0.6620 0.5183 0.0381 -0.0163 0.1182 189 ASN A C 1418 O O . ASN A 189 ? 0.5108 0.6373 0.4932 0.0379 -0.0180 0.1166 189 ASN A O 1419 C CB . ASN A 189 ? 0.5860 0.7232 0.5716 0.0401 -0.0139 0.1284 189 ASN A CB 1420 C CG . ASN A 189 ? 0.6296 0.7687 0.6162 0.0396 -0.0158 0.1312 189 ASN A CG 1421 O OD1 . ASN A 189 ? 0.6648 0.8007 0.6522 0.0385 -0.0181 0.1287 189 ASN A OD1 1422 N ND2 . ASN A 189 ? 0.6684 0.8133 0.6551 0.0407 -0.0147 0.1365 189 ASN A ND2 1423 N N . ASP A 190 ? 0.5098 0.6343 0.4971 0.0363 -0.0168 0.1171 190 ASP A N 1424 C CA . ASP A 190 ? 0.4773 0.5973 0.4674 0.0340 -0.0194 0.1135 190 ASP A CA 1425 C C . ASP A 190 ? 0.4449 0.5616 0.4300 0.0343 -0.0191 0.1076 190 ASP A C 1426 O O . ASP A 190 ? 0.4228 0.5381 0.4086 0.0333 -0.0212 0.1051 190 ASP A O 1427 C CB . ASP A 190 ? 0.4923 0.6099 0.4869 0.0321 -0.0197 0.1133 190 ASP A CB 1428 C CG . ASP A 190 ? 0.4985 0.6192 0.4982 0.0307 -0.0203 0.1190 190 ASP A CG 1429 O OD1 . ASP A 190 ? 0.5078 0.6289 0.5100 0.0295 -0.0224 0.1219 190 ASP A OD1 1430 O OD2 . ASP A 190 ? 0.5047 0.6272 0.5054 0.0308 -0.0188 0.1207 190 ASP A OD2 1431 N N . GLN A 191 ? 0.4388 0.5541 0.4184 0.0358 -0.0165 0.1054 191 GLN A N 1432 C CA . GLN A 191 ? 0.4321 0.5434 0.4057 0.0355 -0.0161 0.0997 191 GLN A CA 1433 C C . GLN A 191 ? 0.4369 0.5504 0.4077 0.0358 -0.0172 0.0990 191 GLN A C 1434 O O . GLN A 191 ? 0.4346 0.5469 0.4049 0.0341 -0.0190 0.0952 191 GLN A O 1435 C CB . GLN A 191 ? 0.4303 0.5392 0.3970 0.0376 -0.0127 0.0983 191 GLN A CB 1436 C CG . GLN A 191 ? 0.4370 0.5408 0.3958 0.0371 -0.0120 0.0926 191 GLN A CG 1437 C CD . GLN A 191 ? 0.4519 0.5513 0.4123 0.0342 -0.0132 0.0881 191 GLN A CD 1438 O OE1 . GLN A 191 ? 0.4546 0.5527 0.4194 0.0337 -0.0132 0.0885 191 GLN A OE1 1439 N NE2 . GLN A 191 ? 0.4224 0.5199 0.3790 0.0323 -0.0142 0.0837 191 GLN A NE2 1440 N N . ILE A 192 ? 0.4459 0.5633 0.4150 0.0378 -0.0163 0.1027 192 ILE A N 1441 C CA . ILE A 192 ? 0.4496 0.5696 0.4154 0.0383 -0.0173 0.1025 192 ILE A CA 1442 C C . ILE A 192 ? 0.4297 0.5519 0.4015 0.0371 -0.0204 0.1039 192 ILE A C 1443 O O . ILE A 192 ? 0.4611 0.5838 0.4316 0.0364 -0.0221 0.1012 192 ILE A O 1444 C CB . ILE A 192 ? 0.4666 0.5901 0.4286 0.0411 -0.0152 0.1062 192 ILE A CB 1445 C CG1 . ILE A 192 ? 0.4817 0.6021 0.4365 0.0430 -0.0119 0.1045 192 ILE A CG1 1446 C CG2 . ILE A 192 ? 0.4713 0.5976 0.4299 0.0417 -0.0163 0.1061 192 ILE A CG2 1447 C CD1 . ILE A 192 ? 0.4874 0.6023 0.4350 0.0418 -0.0116 0.0983 192 ILE A CD1 1448 N N . SER A 193 ? 0.4398 0.5631 0.4178 0.0368 -0.0213 0.1082 193 SER A N 1449 C CA . SER A 193 ? 0.4387 0.5627 0.4215 0.0360 -0.0242 0.1098 193 SER A CA 1450 C C . SER A 193 ? 0.4346 0.5557 0.4191 0.0344 -0.0261 0.1052 193 SER A C 1451 O O . SER A 193 ? 0.4249 0.5470 0.4107 0.0345 -0.0283 0.1049 193 SER A O 1452 C CB . SER A 193 ? 0.4584 0.5825 0.4467 0.0353 -0.0248 0.1148 193 SER A CB 1453 O OG . SER A 193 ? 0.4888 0.6167 0.4760 0.0366 -0.0231 0.1195 193 SER A OG 1454 N N . LEU A 194 ? 0.4109 0.5285 0.3953 0.0331 -0.0252 0.1019 194 LEU A N 1455 C CA . LEU A 194 ? 0.4092 0.5242 0.3955 0.0315 -0.0269 0.0977 194 LEU A CA 1456 C C . LEU A 194 ? 0.4097 0.5252 0.3910 0.0310 -0.0268 0.0927 194 LEU A C 1457 O O . LEU A 194 ? 0.4026 0.5194 0.3850 0.0303 -0.0288 0.0904 194 LEU A O 1458 C CB . LEU A 194 ? 0.4069 0.5179 0.3959 0.0301 -0.0261 0.0967 194 LEU A CB 1459 C CG . LEU A 194 ? 0.4103 0.5205 0.4049 0.0296 -0.0270 0.1010 194 LEU A CG 1460 C CD1 . LEU A 194 ? 0.4153 0.5228 0.4113 0.0286 -0.0256 0.1007 194 LEU A CD1 1461 C CD2 . LEU A 194 ? 0.4188 0.5274 0.4173 0.0290 -0.0298 0.1009 194 LEU A CD2 1462 N N . TYR A 195 ? 0.4231 0.5377 0.3983 0.0312 -0.0244 0.0910 195 TYR A N 1463 C CA . TYR A 195 ? 0.4446 0.5579 0.4141 0.0297 -0.0241 0.0856 195 TYR A CA 1464 C C . TYR A 195 ? 0.4901 0.6057 0.4525 0.0305 -0.0233 0.0852 195 TYR A C 1465 O O . TYR A 195 ? 0.4970 0.6121 0.4542 0.0287 -0.0234 0.0809 195 TYR A O 1466 C CB . TYR A 195 ? 0.4400 0.5477 0.4071 0.0285 -0.0222 0.0825 195 TYR A CB 1467 C CG . TYR A 195 ? 0.4229 0.5286 0.3968 0.0278 -0.0230 0.0833 195 TYR A CG 1468 C CD1 . TYR A 195 ? 0.4172 0.5234 0.3957 0.0264 -0.0254 0.0816 195 TYR A CD1 1469 C CD2 . TYR A 195 ? 0.4433 0.5471 0.4190 0.0288 -0.0214 0.0861 195 TYR A CD2 1470 C CE1 . TYR A 195 ? 0.4184 0.5223 0.4026 0.0258 -0.0262 0.0823 195 TYR A CE1 1471 C CE2 . TYR A 195 ? 0.4237 0.5258 0.4054 0.0279 -0.0223 0.0868 195 TYR A CE2 1472 C CZ . TYR A 195 ? 0.4216 0.5232 0.4073 0.0263 -0.0247 0.0848 195 TYR A CZ 1473 O OH . TYR A 195 ? 0.4314 0.5308 0.4225 0.0254 -0.0256 0.0855 195 TYR A OH 1474 N N . ALA A 196 ? 0.5223 0.6402 0.4842 0.0328 -0.0224 0.0895 196 ALA A N 1475 C CA . ALA A 196 ? 0.5611 0.6818 0.5169 0.0339 -0.0219 0.0898 196 ALA A CA 1476 C C . ALA A 196 ? 0.5878 0.7043 0.5347 0.0343 -0.0190 0.0875 196 ALA A C 1477 O O . ALA A 196 ? 0.6140 0.7318 0.5546 0.0351 -0.0183 0.0874 196 ALA A O 1478 C CB . ALA A 196 ? 0.5424 0.6667 0.4975 0.0324 -0.0243 0.0871 196 ALA A CB 1479 N N . GLN A 197 ? 0.5786 0.6898 0.5245 0.0338 -0.0173 0.0857 197 GLN A N 1480 C CA . GLN A 197 ? 0.5960 0.7019 0.5325 0.0346 -0.0144 0.0834 197 GLN A CA 1481 C C . GLN A 197 ? 0.5919 0.6934 0.5293 0.0356 -0.0123 0.0838 197 GLN A C 1482 O O . GLN A 197 ? 0.5681 0.6705 0.5133 0.0349 -0.0134 0.0852 197 GLN A O 1483 C CB . GLN A 197 ? 0.6115 0.7141 0.5409 0.0315 -0.0149 0.0777 197 GLN A CB 1484 C CG . GLN A 197 ? 0.6224 0.7234 0.5558 0.0282 -0.0166 0.0741 197 GLN A CG 1485 C CD . GLN A 197 ? 0.6519 0.7550 0.5824 0.0248 -0.0186 0.0701 197 GLN A CD 1486 O OE1 . GLN A 197 ? 0.6452 0.7505 0.5702 0.0246 -0.0188 0.0698 197 GLN A OE1 1487 N NE2 . GLN A 197 ? 0.6241 0.7271 0.5584 0.0220 -0.0202 0.0672 197 GLN A NE2 1488 N N . ALA A 198 ? 0.5934 0.6900 0.5221 0.0373 -0.0093 0.0827 198 ALA A N 1489 C CA . ALA A 198 ? 0.6199 0.7121 0.5478 0.0390 -0.0069 0.0830 198 ALA A CA 1490 C C . ALA A 198 ? 0.6022 0.6899 0.5321 0.0359 -0.0078 0.0790 198 ALA A C 1491 O O . ALA A 198 ? 0.5901 0.6763 0.5183 0.0326 -0.0095 0.0749 198 ALA A O 1492 C CB . ALA A 198 ? 0.6286 0.7154 0.5450 0.0418 -0.0035 0.0819 198 ALA A CB 1493 N N . SER A 199 ? 0.6073 0.6935 0.5407 0.0370 -0.0067 0.0803 199 SER A N 1494 C CA . SER A 199 ? 0.6078 0.6903 0.5442 0.0342 -0.0077 0.0770 199 SER A CA 1495 C C . SER A 199 ? 0.6406 0.7149 0.5668 0.0328 -0.0062 0.0717 199 SER A C 1496 O O . SER A 199 ? 0.6482 0.7178 0.5651 0.0352 -0.0034 0.0713 199 SER A O 1497 C CB . SER A 199 ? 0.5766 0.6597 0.5190 0.0357 -0.0069 0.0799 199 SER A CB 1498 O OG . SER A 199 ? 0.5711 0.6514 0.5072 0.0393 -0.0035 0.0811 199 SER A OG 1499 N N . GLY A 200 ? 0.6611 0.7335 0.5887 0.0289 -0.0080 0.0677 200 GLY A N 1500 C CA . GLY A 200 ? 0.6733 0.7379 0.5917 0.0265 -0.0070 0.0624 200 GLY A CA 1501 C C . GLY A 200 ? 0.6908 0.7534 0.6140 0.0237 -0.0081 0.0599 200 GLY A C 1502 O O . GLY A 200 ? 0.7191 0.7870 0.6525 0.0230 -0.0103 0.0616 200 GLY A O 1503 N N . ARG A 201 ? 0.6538 0.7082 0.5692 0.0220 -0.0066 0.0559 201 ARG A N 1504 C CA . ARG A 201 ? 0.6349 0.6864 0.5539 0.0199 -0.0071 0.0537 201 ARG A CA 1505 C C . ARG A 201 ? 0.5866 0.6425 0.5113 0.0156 -0.0102 0.0512 201 ARG A C 1506 O O . ARG A 201 ? 0.5796 0.6390 0.5025 0.0136 -0.0117 0.0500 201 ARG A O 1507 C CB . ARG A 201 ? 0.6551 0.6960 0.5631 0.0194 -0.0044 0.0502 201 ARG A CB 1508 C CG . ARG A 201 ? 0.6825 0.7189 0.5807 0.0153 -0.0046 0.0456 201 ARG A CG 1509 C CD . ARG A 201 ? 0.7134 0.7386 0.5971 0.0165 -0.0013 0.0436 201 ARG A CD 1510 N NE . ARG A 201 ? 0.7502 0.7721 0.6248 0.0120 -0.0020 0.0396 201 ARG A NE 1511 C CZ . ARG A 201 ? 0.7638 0.7884 0.6344 0.0122 -0.0024 0.0402 201 ARG A CZ 1512 N NH1 . ARG A 201 ? 0.7709 0.8010 0.6454 0.0168 -0.0020 0.0446 201 ARG A NH1 1513 N NH2 . ARG A 201 ? 0.7652 0.7870 0.6275 0.0074 -0.0032 0.0364 201 ARG A NH2 1514 N N . ILE A 202 ? 0.5067 0.5626 0.4378 0.0144 -0.0111 0.0505 202 ILE A N 1515 C CA . ILE A 202 ? 0.4708 0.5306 0.4071 0.0106 -0.0138 0.0480 202 ILE A CA 1516 C C . ILE A 202 ? 0.4476 0.5005 0.3786 0.0075 -0.0129 0.0435 202 ILE A C 1517 O O . ILE A 202 ? 0.4396 0.4869 0.3695 0.0088 -0.0111 0.0436 202 ILE A O 1518 C CB . ILE A 202 ? 0.4650 0.5303 0.4132 0.0118 -0.0158 0.0508 202 ILE A CB 1519 C CG1 . ILE A 202 ? 0.4750 0.5468 0.4280 0.0144 -0.0170 0.0553 202 ILE A CG1 1520 C CG2 . ILE A 202 ? 0.4373 0.5053 0.3899 0.0085 -0.0181 0.0480 202 ILE A CG2 1521 C CD1 . ILE A 202 ? 0.4909 0.5664 0.4540 0.0158 -0.0186 0.0587 202 ILE A CD1 1522 N N . THR A 203 ? 0.4012 0.4535 0.3584 0.0081 -0.0186 0.0318 203 THR A N 1523 C CA . THR A 203 ? 0.4078 0.4571 0.3624 0.0062 -0.0173 0.0279 203 THR A CA 1524 C C . THR A 203 ? 0.4055 0.4574 0.3640 0.0049 -0.0193 0.0254 203 THR A C 1525 O O . THR A 203 ? 0.4257 0.4817 0.3852 0.0045 -0.0209 0.0246 203 THR A O 1526 C CB . THR A 203 ? 0.4138 0.4608 0.3609 0.0049 -0.0151 0.0256 203 THR A CB 1527 O OG1 . THR A 203 ? 0.4043 0.4484 0.3476 0.0065 -0.0131 0.0277 203 THR A OG1 1528 C CG2 . THR A 203 ? 0.4107 0.4542 0.3548 0.0025 -0.0139 0.0215 203 THR A CG2 1529 N N . VAL A 204 ? 0.3946 0.4443 0.3553 0.0044 -0.0193 0.0243 204 VAL A N 1530 C CA . VAL A 204 ? 0.3775 0.4294 0.3418 0.0033 -0.0209 0.0216 204 VAL A CA 1531 C C . VAL A 204 ? 0.3737 0.4226 0.3344 0.0010 -0.0190 0.0180 204 VAL A C 1532 O O . VAL A 204 ? 0.3682 0.4125 0.3271 0.0010 -0.0173 0.0182 204 VAL A O 1533 C CB . VAL A 204 ? 0.3785 0.4306 0.3490 0.0048 -0.0227 0.0235 204 VAL A CB 1534 C CG1 . VAL A 204 ? 0.3625 0.4170 0.3364 0.0039 -0.0243 0.0205 204 VAL A CG1 1535 C CG2 . VAL A 204 ? 0.3769 0.4315 0.3507 0.0068 -0.0247 0.0273 204 VAL A CG2 1536 N N . SER A 205 ? 0.3792 0.4307 0.3385 -0.0010 -0.0192 0.0147 205 SER A N 1537 C CA . SER A 205 ? 0.3865 0.4351 0.3412 -0.0038 -0.0173 0.0112 205 SER A CA 1538 C C . SER A 205 ? 0.3893 0.4418 0.3464 -0.0058 -0.0184 0.0078 205 SER A C 1539 O O . SER A 205 ? 0.3905 0.4486 0.3521 -0.0049 -0.0207 0.0078 205 SER A O 1540 C CB . SER A 205 ? 0.4051 0.4519 0.3526 -0.0052 -0.0156 0.0102 205 SER A CB 1541 O OG . SER A 205 ? 0.4100 0.4622 0.3580 -0.0054 -0.0170 0.0099 205 SER A OG 1542 N N . THR A 206 ? 0.3820 0.4315 0.3357 -0.0083 -0.0168 0.0050 206 THR A N 1543 C CA . THR A 206 ? 0.3825 0.4355 0.3368 -0.0109 -0.0172 0.0013 206 THR A CA 1544 C C . THR A 206 ? 0.3915 0.4409 0.3383 -0.0144 -0.0149 -0.0012 206 THR A C 1545 O O . THR A 206 ? 0.3683 0.4123 0.3096 -0.0142 -0.0132 -0.0001 206 THR A O 1546 C CB . THR A 206 ? 0.3853 0.4378 0.3436 -0.0108 -0.0176 0.0005 206 THR A CB 1547 O OG1 . THR A 206 ? 0.3763 0.4219 0.3306 -0.0117 -0.0154 0.0003 206 THR A OG1 1548 C CG2 . THR A 206 ? 0.3793 0.4335 0.3443 -0.0074 -0.0197 0.0034 206 THR A CG2 1549 N N . LYS A 207 ? 0.3993 0.4515 0.3454 -0.0175 -0.0148 -0.0047 207 LYS A N 1550 C CA . LYS A 207 ? 0.4437 0.4919 0.3824 -0.0213 -0.0127 -0.0074 207 LYS A CA 1551 C C . LYS A 207 ? 0.4665 0.5060 0.4011 -0.0214 -0.0106 -0.0069 207 LYS A C 1552 O O . LYS A 207 ? 0.4735 0.5072 0.4007 -0.0232 -0.0086 -0.0078 207 LYS A O 1553 C CB . LYS A 207 ? 0.4642 0.5174 0.4038 -0.0249 -0.0131 -0.0110 207 LYS A CB 1554 C CG . LYS A 207 ? 0.4888 0.5505 0.4306 -0.0256 -0.0149 -0.0122 207 LYS A CG 1555 C CD . LYS A 207 ? 0.5178 0.5847 0.4602 -0.0293 -0.0150 -0.0159 207 LYS A CD 1556 C CE . LYS A 207 ? 0.5416 0.6189 0.4899 -0.0284 -0.0174 -0.0166 207 LYS A CE 1557 N NZ . LYS A 207 ? 0.5601 0.6428 0.5093 -0.0318 -0.0174 -0.0202 207 LYS A NZ 1558 N N . ARG A 208 ? 0.4769 0.5154 0.4161 -0.0193 -0.0110 -0.0055 208 ARG A N 1559 C CA . ARG A 208 ? 0.5055 0.5365 0.4413 -0.0194 -0.0092 -0.0053 208 ARG A CA 1560 C C . ARG A 208 ? 0.4794 0.5064 0.4161 -0.0156 -0.0089 -0.0016 208 ARG A C 1561 O O . ARG A 208 ? 0.4785 0.4993 0.4119 -0.0153 -0.0073 -0.0011 208 ARG A O 1562 C CB . ARG A 208 ? 0.5515 0.5836 0.4909 -0.0204 -0.0096 -0.0070 208 ARG A CB 1563 C CG . ARG A 208 ? 0.5982 0.6348 0.5460 -0.0173 -0.0117 -0.0051 208 ARG A CG 1564 C CD . ARG A 208 ? 0.6569 0.6928 0.6075 -0.0178 -0.0118 -0.0063 208 ARG A CD 1565 N NE . ARG A 208 ? 0.7103 0.7484 0.6679 -0.0145 -0.0137 -0.0040 208 ARG A NE 1566 C CZ . ARG A 208 ? 0.7434 0.7808 0.7043 -0.0140 -0.0142 -0.0043 208 ARG A CZ 1567 N NH1 . ARG A 208 ? 0.7596 0.7942 0.7176 -0.0165 -0.0127 -0.0066 208 ARG A NH1 1568 N NH2 . ARG A 208 ? 0.7419 0.7811 0.7088 -0.0111 -0.0161 -0.0021 208 ARG A NH2 1569 N N . SER A 209 ? 0.4452 0.4760 0.3861 -0.0128 -0.0104 0.0011 209 SER A N 1570 C CA . SER A 209 ? 0.4449 0.4728 0.3871 -0.0094 -0.0102 0.0047 209 SER A CA 1571 C C . SER A 209 ? 0.4284 0.4594 0.3721 -0.0072 -0.0112 0.0074 209 SER A C 1572 O O . SER A 209 ? 0.4081 0.4443 0.3536 -0.0077 -0.0126 0.0068 209 SER A O 1573 C CB . SER A 209 ? 0.4594 0.4882 0.4080 -0.0079 -0.0115 0.0058 209 SER A CB 1574 O OG . SER A 209 ? 0.4564 0.4917 0.4113 -0.0074 -0.0139 0.0058 209 SER A OG 1575 N N . GLN A 210 ? 0.4164 0.4445 0.3594 -0.0046 -0.0104 0.0106 210 GLN A N 1576 C CA . GLN A 210 ? 0.4144 0.4452 0.3586 -0.0024 -0.0112 0.0135 210 GLN A CA 1577 C C . GLN A 210 ? 0.4099 0.4394 0.3569 0.0004 -0.0112 0.0173 210 GLN A C 1578 O O . GLN A 210 ? 0.4151 0.4402 0.3604 0.0008 -0.0098 0.0175 210 GLN A O 1579 C CB . GLN A 210 ? 0.4225 0.4510 0.3595 -0.0029 -0.0095 0.0130 210 GLN A CB 1580 C CG . GLN A 210 ? 0.4396 0.4609 0.3697 -0.0029 -0.0068 0.0125 210 GLN A CG 1581 C CD . GLN A 210 ? 0.4694 0.4880 0.3921 -0.0030 -0.0052 0.0121 210 GLN A CD 1582 O OE1 . GLN A 210 ? 0.5061 0.5286 0.4293 -0.0025 -0.0060 0.0131 210 GLN A OE1 1583 N NE2 . GLN A 210 ? 0.4599 0.4715 0.3753 -0.0035 -0.0029 0.0109 210 GLN A NE2 1584 N N . GLN A 211 ? 0.4125 0.4461 0.3638 0.0023 -0.0128 0.0202 211 GLN A N 1585 C CA . GLN A 211 ? 0.4143 0.4475 0.3680 0.0048 -0.0128 0.0241 211 GLN A CA 1586 C C . GLN A 211 ? 0.3890 0.4254 0.3425 0.0062 -0.0133 0.0267 211 GLN A C 1587 O O . GLN A 211 ? 0.3807 0.4212 0.3370 0.0059 -0.0152 0.0267 211 GLN A O 1588 C CB . GLN A 211 ? 0.4362 0.4715 0.3970 0.0055 -0.0150 0.0256 211 GLN A CB 1589 C CG . GLN A 211 ? 0.4618 0.4947 0.4238 0.0043 -0.0149 0.0234 211 GLN A CG 1590 C CD . GLN A 211 ? 0.4717 0.5067 0.4406 0.0051 -0.0173 0.0249 211 GLN A CD 1591 O OE1 . GLN A 211 ? 0.4663 0.5038 0.4383 0.0043 -0.0190 0.0231 211 GLN A OE1 1592 N NE2 . GLN A 211 ? 0.5018 0.5361 0.4730 0.0067 -0.0176 0.0283 211 GLN A NE2 1593 N N . THR A 212 ? 0.3863 0.4209 0.3368 0.0079 -0.0117 0.0290 212 THR A N 1594 C CA . THR A 212 ? 0.3924 0.4301 0.3429 0.0094 -0.0120 0.0319 212 THR A CA 1595 C C . THR A 212 ? 0.3911 0.4299 0.3454 0.0114 -0.0123 0.0360 212 THR A C 1596 O O . THR A 212 ? 0.3858 0.4217 0.3389 0.0123 -0.0108 0.0366 212 THR A O 1597 C CB . THR A 212 ? 0.4003 0.4358 0.3434 0.0097 -0.0097 0.0311 212 THR A CB 1598 O OG1 . THR A 212 ? 0.3933 0.4281 0.3329 0.0074 -0.0096 0.0274 212 THR A OG1 1599 C CG2 . THR A 212 ? 0.4037 0.4426 0.3468 0.0115 -0.0099 0.0344 212 THR A CG2 1600 N N . VAL A 213 ? 0.4050 0.4478 0.3636 0.0121 -0.0143 0.0389 213 VAL A N 1601 C CA . VAL A 213 ? 0.4050 0.4494 0.3673 0.0136 -0.0148 0.0430 213 VAL A CA 1602 C C . VAL A 213 ? 0.4249 0.4729 0.3866 0.0148 -0.0149 0.0461 213 VAL A C 1603 O O . VAL A 213 ? 0.4500 0.5004 0.4120 0.0143 -0.0163 0.0459 213 VAL A O 1604 C CB . VAL A 213 ? 0.4039 0.4498 0.3729 0.0130 -0.0176 0.0439 213 VAL A CB 1605 C CG1 . VAL A 213 ? 0.3948 0.4423 0.3673 0.0141 -0.0183 0.0483 213 VAL A CG1 1606 C CG2 . VAL A 213 ? 0.3992 0.4419 0.3689 0.0119 -0.0175 0.0408 213 VAL A CG2 1607 N N . ILE A 214 ? 0.4447 0.4931 0.4055 0.0164 -0.0135 0.0491 214 ILE A N 1608 C CA . ILE A 214 ? 0.4423 0.4942 0.4023 0.0176 -0.0132 0.0524 214 ILE A CA 1609 C C . ILE A 214 ? 0.4426 0.4978 0.4084 0.0177 -0.0153 0.0565 214 ILE A C 1610 O O . ILE A 214 ? 0.4305 0.4855 0.3989 0.0180 -0.0152 0.0582 214 ILE A O 1611 C CB . ILE A 214 ? 0.4725 0.5236 0.4279 0.0195 -0.0103 0.0534 214 ILE A CB 1612 C CG1 . ILE A 214 ? 0.4765 0.5232 0.4252 0.0194 -0.0081 0.0494 214 ILE A CG1 1613 C CG2 . ILE A 214 ? 0.4688 0.5241 0.4235 0.0208 -0.0099 0.0569 214 ILE A CG2 1614 C CD1 . ILE A 214 ? 0.5128 0.5569 0.4572 0.0214 -0.0054 0.0498 214 ILE A CD1 1615 N N . PRO A 215 ? 0.4421 0.5003 0.4097 0.0174 -0.0172 0.0581 215 PRO A N 1616 C CA . PRO A 215 ? 0.4420 0.5030 0.4141 0.0174 -0.0190 0.0624 215 PRO A CA 1617 C C . PRO A 215 ? 0.4415 0.5050 0.4123 0.0187 -0.0171 0.0659 215 PRO A C 1618 O O . PRO A 215 ? 0.4531 0.5174 0.4192 0.0198 -0.0151 0.0656 215 PRO A O 1619 C CB . PRO A 215 ? 0.4450 0.5081 0.4177 0.0170 -0.0211 0.0631 215 PRO A CB 1620 C CG . PRO A 215 ? 0.4403 0.5019 0.4101 0.0165 -0.0208 0.0587 215 PRO A CG 1621 C CD . PRO A 215 ? 0.4441 0.5032 0.4094 0.0169 -0.0178 0.0563 215 PRO A CD 1622 N N . ASN A 216 ? 0.4258 0.4907 0.4004 0.0185 -0.0178 0.0691 216 ASN A N 1623 C CA . ASN A 216 ? 0.4243 0.4923 0.3982 0.0197 -0.0160 0.0724 216 ASN A CA 1624 C C . ASN A 216 ? 0.4224 0.4941 0.4001 0.0188 -0.0179 0.0770 216 ASN A C 1625 O O . ASN A 216 ? 0.4089 0.4803 0.3910 0.0175 -0.0198 0.0786 216 ASN A O 1626 C CB . ASN A 216 ? 0.4370 0.5035 0.4115 0.0203 -0.0146 0.0720 216 ASN A CB 1627 C CG . ASN A 216 ? 0.4498 0.5120 0.4199 0.0211 -0.0126 0.0676 216 ASN A CG 1628 O OD1 . ASN A 216 ? 0.4677 0.5267 0.4390 0.0205 -0.0129 0.0654 216 ASN A OD1 1629 N ND2 . ASN A 216 ? 0.4350 0.4970 0.3997 0.0223 -0.0106 0.0663 216 ASN A ND2 1630 N N . ILE A 217 ? 0.4073 0.4825 0.3830 0.0194 -0.0173 0.0793 217 ILE A N 1631 C CA . ILE A 217 ? 0.4043 0.4832 0.3828 0.0185 -0.0190 0.0839 217 ILE A CA 1632 C C . ILE A 217 ? 0.3977 0.4800 0.3782 0.0186 -0.0180 0.0874 217 ILE A C 1633 O O . ILE A 217 ? 0.3898 0.4739 0.3678 0.0203 -0.0153 0.0872 217 ILE A O 1634 C CB . ILE A 217 ? 0.4098 0.4916 0.3850 0.0192 -0.0184 0.0851 217 ILE A CB 1635 C CG1 . ILE A 217 ? 0.4233 0.5024 0.3970 0.0188 -0.0199 0.0819 217 ILE A CG1 1636 C CG2 . ILE A 217 ? 0.4039 0.4898 0.3815 0.0181 -0.0198 0.0902 217 ILE A CG2 1637 C CD1 . ILE A 217 ? 0.4359 0.5168 0.4048 0.0199 -0.0185 0.0813 217 ILE A CD1 1638 N N . GLY A 218 ? 0.4113 0.4948 0.3962 0.0167 -0.0202 0.0906 218 GLY A N 1639 C CA . GLY A 218 ? 0.4218 0.5091 0.4089 0.0163 -0.0196 0.0942 218 GLY A CA 1640 C C . GLY A 218 ? 0.4430 0.5293 0.4349 0.0137 -0.0225 0.0965 218 GLY A C 1641 O O . GLY A 218 ? 0.4428 0.5243 0.4363 0.0128 -0.0248 0.0944 218 GLY A O 1642 N N . SER A 219 ? 0.4339 0.5248 0.4279 0.0126 -0.0226 0.1009 219 SER A N 1643 C CA . SER A 219 ? 0.4480 0.5381 0.4463 0.0099 -0.0253 0.1034 219 SER A CA 1644 C C . SER A 219 ? 0.4342 0.5220 0.4345 0.0098 -0.0252 0.1015 219 SER A C 1645 O O . SER A 219 ? 0.4318 0.5221 0.4313 0.0114 -0.0227 0.1009 219 SER A O 1646 C CB . SER A 219 ? 0.4604 0.5567 0.4601 0.0084 -0.0252 0.1088 219 SER A CB 1647 O OG . SER A 219 ? 0.4718 0.5693 0.4700 0.0078 -0.0261 0.1111 219 SER A OG 1648 N N . ARG A 220 ? 0.4029 0.4857 0.4056 0.0081 -0.0279 0.1003 220 ARG A N 1649 C CA . ARG A 220 ? 0.3970 0.4779 0.4024 0.0073 -0.0284 0.0994 220 ARG A CA 1650 C C . ARG A 220 ? 0.3929 0.4740 0.4016 0.0042 -0.0312 0.1033 220 ARG A C 1651 O O . ARG A 220 ? 0.3887 0.4694 0.3973 0.0029 -0.0331 0.1056 220 ARG A O 1652 C CB . ARG A 220 ? 0.3937 0.4683 0.3989 0.0079 -0.0293 0.0946 220 ARG A CB 1653 C CG . ARG A 220 ? 0.3949 0.4684 0.3968 0.0104 -0.0266 0.0905 220 ARG A CG 1654 C CD . ARG A 220 ? 0.4010 0.4745 0.3996 0.0117 -0.0259 0.0891 220 ARG A CD 1655 N NE . ARG A 220 ? 0.4026 0.4737 0.3979 0.0136 -0.0238 0.0846 220 ARG A NE 1656 C CZ . ARG A 220 ? 0.4050 0.4761 0.3966 0.0149 -0.0225 0.0828 220 ARG A CZ 1657 N NH1 . ARG A 220 ? 0.4002 0.4740 0.3908 0.0149 -0.0229 0.0850 220 ARG A NH1 1658 N NH2 . ARG A 220 ? 0.4165 0.4849 0.4050 0.0162 -0.0208 0.0787 220 ARG A NH2 1659 N N . PRO A 221 ? 0.3874 0.4690 0.3987 0.0028 -0.0317 0.1043 221 PRO A N 1660 C CA . PRO A 221 ? 0.3938 0.4752 0.4079 -0.0004 -0.0345 0.1079 221 PRO A CA 1661 C C . PRO A 221 ? 0.3973 0.4720 0.4116 -0.0016 -0.0377 0.1069 221 PRO A C 1662 O O . PRO A 221 ? 0.3967 0.4664 0.4106 -0.0003 -0.0382 0.1028 221 PRO A O 1663 C CB . PRO A 221 ? 0.3983 0.4799 0.4148 -0.0013 -0.0345 0.1076 221 PRO A CB 1664 C CG . PRO A 221 ? 0.3964 0.4822 0.4114 0.0014 -0.0310 0.1062 221 PRO A CG 1665 C CD . PRO A 221 ? 0.3865 0.4695 0.3982 0.0041 -0.0297 0.1026 221 PRO A CD 1666 N N . ARG A 222 ? 0.3986 0.4733 0.4132 -0.0038 -0.0398 0.1106 222 ARG A N 1667 C CA . ARG A 222 ? 0.4172 0.4855 0.4314 -0.0044 -0.0428 0.1098 222 ARG A CA 1668 C C . ARG A 222 ? 0.4172 0.4796 0.4333 -0.0056 -0.0451 0.1080 222 ARG A C 1669 O O . ARG A 222 ? 0.4073 0.4706 0.4254 -0.0076 -0.0455 0.1096 222 ARG A O 1670 C CB . ARG A 222 ? 0.4391 0.5083 0.4528 -0.0067 -0.0447 0.1146 222 ARG A CB 1671 C CG . ARG A 222 ? 0.4581 0.5321 0.4694 -0.0052 -0.0427 0.1158 222 ARG A CG 1672 C CD . ARG A 222 ? 0.4804 0.5541 0.4907 -0.0072 -0.0448 0.1199 222 ARG A CD 1673 N NE . ARG A 222 ? 0.4964 0.5753 0.5044 -0.0058 -0.0427 0.1212 222 ARG A NE 1674 C CZ . ARG A 222 ? 0.5424 0.6216 0.5487 -0.0069 -0.0440 0.1244 222 ARG A CZ 1675 N NH1 . ARG A 222 ? 0.5381 0.6123 0.5447 -0.0094 -0.0474 0.1268 222 ARG A NH1 1676 N NH2 . ARG A 222 ? 0.5489 0.6331 0.5530 -0.0055 -0.0419 0.1253 222 ARG A NH2 1677 N N . VAL A 223 ? 0.4106 0.4674 0.4260 -0.0042 -0.0465 0.1044 223 VAL A N 1678 C CA . VAL A 223 ? 0.4229 0.4733 0.4396 -0.0049 -0.0491 0.1024 223 VAL A CA 1679 C C . VAL A 223 ? 0.4075 0.4529 0.4230 -0.0046 -0.0519 0.1023 223 VAL A C 1680 O O . VAL A 223 ? 0.3900 0.4355 0.4039 -0.0023 -0.0513 0.1001 223 VAL A O 1681 C CB . VAL A 223 ? 0.4250 0.4738 0.4420 -0.0028 -0.0476 0.0973 223 VAL A CB 1682 C CG1 . VAL A 223 ? 0.4258 0.4679 0.4438 -0.0031 -0.0503 0.0947 223 VAL A CG1 1683 C CG2 . VAL A 223 ? 0.4401 0.4932 0.4580 -0.0029 -0.0451 0.0974 223 VAL A CG2 1684 N N . ARG A 224 ? 0.4208 0.4617 0.4368 -0.0069 -0.0550 0.1046 224 ARG A N 1685 C CA . ARG A 224 ? 0.4360 0.4719 0.4505 -0.0066 -0.0579 0.1052 224 ARG A CA 1686 C C . ARG A 224 ? 0.4345 0.4743 0.4470 -0.0059 -0.0569 0.1074 224 ARG A C 1687 O O . ARG A 224 ? 0.4380 0.4759 0.4488 -0.0039 -0.0578 0.1061 224 ARG A O 1688 C CB . ARG A 224 ? 0.4454 0.4761 0.4597 -0.0041 -0.0590 0.1003 224 ARG A CB 1689 C CG . ARG A 224 ? 0.4577 0.4833 0.4735 -0.0052 -0.0608 0.0988 224 ARG A CG 1690 C CD . ARG A 224 ? 0.4573 0.4783 0.4730 -0.0026 -0.0618 0.0939 224 ARG A CD 1691 N NE . ARG A 224 ? 0.4516 0.4762 0.4679 -0.0005 -0.0589 0.0897 224 ARG A NE 1692 C CZ . ARG A 224 ? 0.4256 0.4515 0.4433 -0.0009 -0.0571 0.0880 224 ARG A CZ 1693 N NH1 . ARG A 224 ? 0.4163 0.4412 0.4353 -0.0034 -0.0579 0.0901 224 ARG A NH1 1694 N NH2 . ARG A 224 ? 0.4098 0.4383 0.4274 0.0009 -0.0546 0.0843 224 ARG A NH2 1695 N N . ASP A 225 ? 0.4450 0.4908 0.4577 -0.0075 -0.0551 0.1110 225 ASP A N 1696 C CA . ASP A 225 ? 0.4532 0.5040 0.4641 -0.0072 -0.0537 0.1137 225 ASP A CA 1697 C C . ASP A 225 ? 0.4437 0.4976 0.4532 -0.0039 -0.0512 0.1103 225 ASP A C 1698 O O . ASP A 225 ? 0.4130 0.4693 0.4205 -0.0032 -0.0507 0.1118 225 ASP A O 1699 C CB . ASP A 225 ? 0.4758 0.5228 0.4850 -0.0086 -0.0567 0.1169 225 ASP A CB 1700 C CG . ASP A 225 ? 0.5009 0.5536 0.5088 -0.0101 -0.0557 0.1216 225 ASP A CG 1701 O OD1 . ASP A 225 ? 0.4787 0.5374 0.4878 -0.0115 -0.0535 0.1238 225 ASP A OD1 1702 O OD2 . ASP A 225 ? 0.5230 0.5743 0.5287 -0.0097 -0.0570 0.1231 225 ASP A OD2 1703 N N . ILE A 226 ? 0.4002 0.4539 0.4104 -0.0021 -0.0495 0.1059 226 ILE A N 1704 C CA . ILE A 226 ? 0.3916 0.4477 0.4002 0.0007 -0.0471 0.1025 226 ILE A CA 1705 C C . ILE A 226 ? 0.3986 0.4598 0.4073 0.0013 -0.0436 0.1019 226 ILE A C 1706 O O . ILE A 226 ? 0.3886 0.4491 0.3989 0.0010 -0.0430 0.1004 226 ILE A O 1707 C CB . ILE A 226 ? 0.3847 0.4361 0.3934 0.0025 -0.0481 0.0974 226 ILE A CB 1708 C CG1 . ILE A 226 ? 0.3918 0.4382 0.4003 0.0025 -0.0516 0.0979 226 ILE A CG1 1709 C CG2 . ILE A 226 ? 0.3694 0.4233 0.3762 0.0050 -0.0456 0.0939 226 ILE A CG2 1710 C CD1 . ILE A 226 ? 0.3916 0.4395 0.3978 0.0029 -0.0523 0.1004 226 ILE A CD1 1711 N N . PRO A 227 ? 0.3922 0.4585 0.3988 0.0022 -0.0413 0.1032 227 PRO A N 1712 C CA . PRO A 227 ? 0.3908 0.4618 0.3967 0.0034 -0.0378 0.1025 227 PRO A CA 1713 C C . PRO A 227 ? 0.3713 0.4414 0.3750 0.0061 -0.0358 0.0976 227 PRO A C 1714 O O . PRO A 227 ? 0.3919 0.4644 0.3945 0.0073 -0.0330 0.0962 227 PRO A O 1715 C CB . PRO A 227 ? 0.4028 0.4796 0.4074 0.0031 -0.0366 0.1066 227 PRO A CB 1716 C CG . PRO A 227 ? 0.4065 0.4812 0.4096 0.0030 -0.0386 0.1073 227 PRO A CG 1717 C CD . PRO A 227 ? 0.4092 0.4774 0.4139 0.0021 -0.0419 0.1061 227 PRO A CD 1718 N N . SER A 228 ? 0.3740 0.4405 0.3769 0.0068 -0.0373 0.0949 228 SER A N 1719 C CA . SER A 228 ? 0.3748 0.4401 0.3757 0.0088 -0.0358 0.0901 228 SER A CA 1720 C C . SER A 228 ? 0.3620 0.4235 0.3648 0.0087 -0.0362 0.0867 228 SER A C 1721 O O . SER A 228 ? 0.3594 0.4189 0.3648 0.0072 -0.0379 0.0881 228 SER A O 1722 C CB . SER A 228 ? 0.4021 0.4659 0.4017 0.0096 -0.0374 0.0887 228 SER A CB 1723 O OG . SER A 228 ? 0.4340 0.5010 0.4316 0.0097 -0.0372 0.0917 228 SER A OG 1724 N N . ARG A 229 ? 0.3556 0.4160 0.3566 0.0101 -0.0345 0.0824 229 ARG A N 1725 C CA . ARG A 229 ? 0.3555 0.4123 0.3577 0.0101 -0.0348 0.0788 229 ARG A CA 1726 C C . ARG A 229 ? 0.3616 0.4169 0.3622 0.0112 -0.0346 0.0743 229 ARG A C 1727 O O . ARG A 229 ? 0.3928 0.4499 0.3905 0.0121 -0.0334 0.0736 229 ARG A O 1728 C CB . ARG A 229 ? 0.3560 0.4138 0.3576 0.0105 -0.0321 0.0781 229 ARG A CB 1729 C CG . ARG A 229 ? 0.3676 0.4277 0.3713 0.0093 -0.0321 0.0821 229 ARG A CG 1730 C CD . ARG A 229 ? 0.3723 0.4292 0.3795 0.0076 -0.0349 0.0829 229 ARG A CD 1731 N NE . ARG A 229 ? 0.3744 0.4338 0.3835 0.0063 -0.0348 0.0864 229 ARG A NE 1732 C CZ . ARG A 229 ? 0.3801 0.4415 0.3908 0.0046 -0.0362 0.0908 229 ARG A CZ 1733 N NH1 . ARG A 229 ? 0.3933 0.4542 0.4037 0.0040 -0.0381 0.0926 229 ARG A NH1 1734 N NH2 . ARG A 229 ? 0.3753 0.4395 0.3877 0.0033 -0.0358 0.0935 229 ARG A NH2 1735 N N . ILE A 230 ? 0.3433 0.3951 0.3454 0.0110 -0.0359 0.0714 230 ILE A N 1736 C CA . ILE A 230 ? 0.3309 0.3816 0.3316 0.0118 -0.0354 0.0667 230 ILE A CA 1737 C C . ILE A 230 ? 0.3242 0.3733 0.3245 0.0117 -0.0335 0.0639 230 ILE A C 1738 O O . ILE A 230 ? 0.3102 0.3575 0.3128 0.0110 -0.0342 0.0646 230 ILE A O 1739 C CB . ILE A 230 ? 0.3352 0.3838 0.3378 0.0119 -0.0384 0.0652 230 ILE A CB 1740 C CG1 . ILE A 230 ? 0.3475 0.3975 0.3500 0.0123 -0.0402 0.0679 230 ILE A CG1 1741 C CG2 . ILE A 230 ? 0.3399 0.3881 0.3413 0.0125 -0.0376 0.0602 230 ILE A CG2 1742 C CD1 . ILE A 230 ? 0.3474 0.3952 0.3515 0.0128 -0.0434 0.0670 230 ILE A CD1 1743 N N . SER A 231 ? 0.3175 0.3669 0.3146 0.0123 -0.0312 0.0608 231 SER A N 1744 C CA . SER A 231 ? 0.3155 0.3628 0.3116 0.0122 -0.0294 0.0578 231 SER A CA 1745 C C . SER A 231 ? 0.3136 0.3593 0.3094 0.0120 -0.0301 0.0534 231 SER A C 1746 O O . SER A 231 ? 0.3046 0.3518 0.2987 0.0122 -0.0301 0.0518 231 SER A O 1747 C CB . SER A 231 ? 0.3127 0.3609 0.3048 0.0129 -0.0262 0.0577 231 SER A CB 1748 O OG . SER A 231 ? 0.3151 0.3650 0.3079 0.0131 -0.0256 0.0616 231 SER A OG 1749 N N . ILE A 232 ? 0.3037 0.3469 0.3013 0.0114 -0.0306 0.0513 232 ILE A N 1750 C CA . ILE A 232 ? 0.2935 0.3358 0.2917 0.0112 -0.0315 0.0474 232 ILE A CA 1751 C C . ILE A 232 ? 0.3105 0.3515 0.3055 0.0107 -0.0290 0.0436 232 ILE A C 1752 O O . ILE A 232 ? 0.3095 0.3487 0.3034 0.0105 -0.0274 0.0437 232 ILE A O 1753 C CB . ILE A 232 ? 0.3007 0.3409 0.3027 0.0109 -0.0339 0.0473 232 ILE A CB 1754 C CG1 . ILE A 232 ? 0.2996 0.3403 0.3042 0.0113 -0.0367 0.0507 232 ILE A CG1 1755 C CG2 . ILE A 232 ? 0.2935 0.3330 0.2960 0.0109 -0.0346 0.0430 232 ILE A CG2 1756 C CD1 . ILE A 232 ? 0.3100 0.3523 0.3144 0.0121 -0.0383 0.0498 232 ILE A CD1 1757 N N . TYR A 233 ? 0.3117 0.3536 0.3052 0.0104 -0.0289 0.0403 233 TYR A N 1758 C CA . TYR A 233 ? 0.3151 0.3559 0.3052 0.0095 -0.0267 0.0366 233 TYR A CA 1759 C C . TYR A 233 ? 0.3174 0.3589 0.3090 0.0089 -0.0280 0.0329 233 TYR A C 1760 O O . TYR A 233 ? 0.3057 0.3488 0.3004 0.0095 -0.0304 0.0333 233 TYR A O 1761 C CB . TYR A 233 ? 0.3201 0.3620 0.3055 0.0095 -0.0248 0.0363 233 TYR A CB 1762 C CG . TYR A 233 ? 0.3261 0.3676 0.3097 0.0104 -0.0232 0.0396 233 TYR A CG 1763 C CD1 . TYR A 233 ? 0.3286 0.3724 0.3138 0.0113 -0.0243 0.0434 233 TYR A CD1 1764 C CD2 . TYR A 233 ? 0.3371 0.3759 0.3174 0.0104 -0.0208 0.0390 233 TYR A CD2 1765 C CE1 . TYR A 233 ? 0.3291 0.3733 0.3129 0.0122 -0.0229 0.0465 233 TYR A CE1 1766 C CE2 . TYR A 233 ? 0.3410 0.3799 0.3198 0.0116 -0.0194 0.0420 233 TYR A CE2 1767 C CZ . TYR A 233 ? 0.3476 0.3894 0.3282 0.0124 -0.0204 0.0457 233 TYR A CZ 1768 O OH . TYR A 233 ? 0.3696 0.4123 0.3489 0.0136 -0.0189 0.0487 233 TYR A OH 1769 N N . TRP A 234 ? 0.3146 0.3547 0.3036 0.0077 -0.0263 0.0294 234 TRP A N 1770 C CA . TRP A 234 ? 0.3204 0.3618 0.3108 0.0069 -0.0273 0.0258 234 TRP A CA 1771 C C . TRP A 234 ? 0.3100 0.3516 0.2962 0.0053 -0.0252 0.0223 234 TRP A C 1772 O O . TRP A 234 ? 0.3239 0.3628 0.3058 0.0046 -0.0228 0.0222 234 TRP A O 1773 C CB . TRP A 234 ? 0.3317 0.3712 0.3253 0.0069 -0.0283 0.0251 234 TRP A CB 1774 C CG . TRP A 234 ? 0.3542 0.3902 0.3455 0.0059 -0.0262 0.0240 234 TRP A CG 1775 C CD1 . TRP A 234 ? 0.3758 0.4109 0.3650 0.0044 -0.0248 0.0202 234 TRP A CD1 1776 C CD2 . TRP A 234 ? 0.3815 0.4146 0.3724 0.0063 -0.0252 0.0266 234 TRP A CD2 1777 N NE1 . TRP A 234 ? 0.3864 0.4178 0.3737 0.0039 -0.0232 0.0204 234 TRP A NE1 1778 C CE2 . TRP A 234 ? 0.3836 0.4138 0.3718 0.0051 -0.0233 0.0241 234 TRP A CE2 1779 C CE3 . TRP A 234 ? 0.3992 0.4321 0.3914 0.0074 -0.0257 0.0306 234 TRP A CE3 1780 C CZ2 . TRP A 234 ? 0.4101 0.4373 0.3972 0.0054 -0.0221 0.0256 234 TRP A CZ2 1781 C CZ3 . TRP A 234 ? 0.4206 0.4509 0.4118 0.0075 -0.0244 0.0321 234 TRP A CZ3 1782 C CH2 . TRP A 234 ? 0.4202 0.4478 0.4090 0.0067 -0.0226 0.0296 234 TRP A CH2 1783 N N . THR A 235 ? 0.3090 0.3536 0.2960 0.0046 -0.0261 0.0194 235 THR A N 1784 C CA . THR A 235 ? 0.3090 0.3543 0.2921 0.0026 -0.0244 0.0159 235 THR A CA 1785 C C . THR A 235 ? 0.3132 0.3609 0.2987 0.0017 -0.0254 0.0125 235 THR A C 1786 O O . THR A 235 ? 0.3111 0.3622 0.3008 0.0031 -0.0278 0.0126 235 THR A O 1787 C CB . THR A 235 ? 0.3141 0.3626 0.2948 0.0024 -0.0243 0.0159 235 THR A CB 1788 O OG1 . THR A 235 ? 0.2974 0.3442 0.2763 0.0036 -0.0237 0.0193 235 THR A OG1 1789 C CG2 . THR A 235 ? 0.3215 0.3698 0.2972 -0.0001 -0.0223 0.0124 235 THR A CG2 1790 N N . ILE A 236 ? 0.3156 0.3617 0.2984 -0.0003 -0.0236 0.0096 236 ILE A N 1791 C CA . ILE A 236 ? 0.3362 0.3853 0.3208 -0.0014 -0.0242 0.0061 236 ILE A CA 1792 C C . ILE A 236 ? 0.3414 0.3938 0.3226 -0.0037 -0.0233 0.0032 236 ILE A C 1793 O O . ILE A 236 ? 0.3692 0.4188 0.3451 -0.0055 -0.0211 0.0026 236 ILE A O 1794 C CB . ILE A 236 ? 0.3425 0.3878 0.3265 -0.0025 -0.0230 0.0047 236 ILE A CB 1795 C CG1 . ILE A 236 ? 0.3582 0.4011 0.3462 -0.0003 -0.0245 0.0073 236 ILE A CG1 1796 C CG2 . ILE A 236 ? 0.3525 0.4012 0.3374 -0.0042 -0.0232 0.0007 236 ILE A CG2 1797 C CD1 . ILE A 236 ? 0.3548 0.3933 0.3418 -0.0012 -0.0232 0.0067 236 ILE A CD1 1798 N N . VAL A 237 ? 0.3472 0.4055 0.3313 -0.0035 -0.0249 0.0014 237 VAL A N 1799 C CA . VAL A 237 ? 0.3545 0.4170 0.3358 -0.0058 -0.0243 -0.0012 237 VAL A CA 1800 C C . VAL A 237 ? 0.3714 0.4374 0.3538 -0.0076 -0.0242 -0.0050 237 VAL A C 1801 O O . VAL A 237 ? 0.3785 0.4482 0.3658 -0.0059 -0.0260 -0.0057 237 VAL A O 1802 C CB . VAL A 237 ? 0.3583 0.4259 0.3415 -0.0041 -0.0262 -0.0001 237 VAL A CB 1803 C CG1 . VAL A 237 ? 0.3610 0.4334 0.3414 -0.0067 -0.0256 -0.0030 237 VAL A CG1 1804 C CG2 . VAL A 237 ? 0.3392 0.4035 0.3213 -0.0024 -0.0262 0.0037 237 VAL A CG2 1805 N N . LYS A 238 ? 0.3997 0.4644 0.3774 -0.0111 -0.0220 -0.0075 238 LYS A N 1806 C CA . LYS A 238 ? 0.4172 0.4852 0.3952 -0.0135 -0.0216 -0.0111 238 LYS A CA 1807 C C . LYS A 238 ? 0.4207 0.4975 0.4007 -0.0141 -0.0228 -0.0134 238 LYS A C 1808 O O . LYS A 238 ? 0.4093 0.4886 0.3884 -0.0138 -0.0234 -0.0125 238 LYS A O 1809 C CB . LYS A 238 ? 0.4471 0.5105 0.4188 -0.0173 -0.0188 -0.0129 238 LYS A CB 1810 C CG . LYS A 238 ? 0.4780 0.5327 0.4467 -0.0168 -0.0173 -0.0108 238 LYS A CG 1811 C CD . LYS A 238 ? 0.4810 0.5340 0.4537 -0.0150 -0.0179 -0.0102 238 LYS A CD 1812 C CE . LYS A 238 ? 0.4993 0.5530 0.4711 -0.0177 -0.0169 -0.0135 238 LYS A CE 1813 N NZ . LYS A 238 ? 0.5020 0.5528 0.4766 -0.0163 -0.0173 -0.0129 238 LYS A NZ 1814 N N . PRO A 239 ? 0.4202 0.5020 0.4027 -0.0150 -0.0232 -0.0163 239 PRO A N 1815 C CA . PRO A 239 ? 0.4272 0.5181 0.4111 -0.0161 -0.0241 -0.0188 239 PRO A CA 1816 C C . PRO A 239 ? 0.4283 0.5195 0.4064 -0.0200 -0.0225 -0.0201 239 PRO A C 1817 O O . PRO A 239 ? 0.4370 0.5224 0.4098 -0.0231 -0.0202 -0.0207 239 PRO A O 1818 C CB . PRO A 239 ? 0.4337 0.5283 0.4196 -0.0173 -0.0239 -0.0220 239 PRO A CB 1819 C CG . PRO A 239 ? 0.4319 0.5206 0.4201 -0.0149 -0.0241 -0.0203 239 PRO A CG 1820 C CD . PRO A 239 ? 0.4280 0.5080 0.4122 -0.0150 -0.0228 -0.0175 239 PRO A CD 1821 N N . GLY A 240 ? 0.4514 0.5488 0.4301 -0.0199 -0.0237 -0.0204 240 GLY A N 1822 C CA . GLY A 240 ? 0.4645 0.5625 0.4376 -0.0237 -0.0224 -0.0216 240 GLY A CA 1823 C C . GLY A 240 ? 0.4722 0.5636 0.4413 -0.0230 -0.0217 -0.0187 240 GLY A C 1824 O O . GLY A 240 ? 0.4903 0.5821 0.4548 -0.0255 -0.0210 -0.0194 240 GLY A O 1825 N N . ASP A 241 ? 0.4517 0.5372 0.4223 -0.0196 -0.0220 -0.0156 241 ASP A N 1826 C CA . ASP A 241 ? 0.4433 0.5230 0.4105 -0.0185 -0.0214 -0.0127 241 ASP A CA 1827 C C . ASP A 241 ? 0.4435 0.5270 0.4148 -0.0148 -0.0237 -0.0101 241 ASP A C 1828 O O . ASP A 241 ? 0.4351 0.5251 0.4115 -0.0130 -0.0258 -0.0106 241 ASP A O 1829 C CB . ASP A 241 ? 0.4346 0.5057 0.4004 -0.0175 -0.0200 -0.0107 241 ASP A CB 1830 C CG . ASP A 241 ? 0.4512 0.5154 0.4107 -0.0182 -0.0181 -0.0091 241 ASP A CG 1831 O OD1 . ASP A 241 ? 0.4401 0.5059 0.3974 -0.0181 -0.0184 -0.0083 241 ASP A OD1 1832 O OD2 . ASP A 241 ? 0.4404 0.4977 0.3968 -0.0186 -0.0164 -0.0086 241 ASP A OD2 1833 N N . ILE A 242 ? 0.4296 0.5088 0.3981 -0.0137 -0.0233 -0.0073 242 ILE A N 1834 C CA . ILE A 242 ? 0.4482 0.5305 0.4192 -0.0108 -0.0252 -0.0048 242 ILE A CA 1835 C C . ILE A 242 ? 0.4367 0.5127 0.4072 -0.0084 -0.0248 -0.0009 242 ILE A C 1836 O O . ILE A 242 ? 0.4514 0.5214 0.4171 -0.0096 -0.0226 -0.0004 242 ILE A O 1837 C CB . ILE A 242 ? 0.4774 0.5630 0.4443 -0.0128 -0.0249 -0.0057 242 ILE A CB 1838 C CG1 . ILE A 242 ? 0.5033 0.5956 0.4700 -0.0159 -0.0251 -0.0097 242 ILE A CG1 1839 C CG2 . ILE A 242 ? 0.4823 0.5711 0.4517 -0.0097 -0.0270 -0.0030 242 ILE A CG2 1840 C CD1 . ILE A 242 ? 0.5328 0.6275 0.4945 -0.0187 -0.0245 -0.0111 242 ILE A CD1 1841 N N . LEU A 243 ? 0.4106 0.4881 0.3860 -0.0049 -0.0269 0.0017 243 LEU A N 1842 C CA . LEU A 243 ? 0.3984 0.4714 0.3736 -0.0027 -0.0269 0.0056 243 LEU A CA 1843 C C . LEU A 243 ? 0.4160 0.4909 0.3887 -0.0023 -0.0272 0.0072 243 LEU A C 1844 O O . LEU A 243 ? 0.4157 0.4963 0.3905 -0.0015 -0.0291 0.0069 243 LEU A O 1845 C CB . LEU A 243 ? 0.3829 0.4562 0.3640 0.0003 -0.0292 0.0079 243 LEU A CB 1846 C CG . LEU A 243 ? 0.3774 0.4462 0.3589 0.0024 -0.0292 0.0122 243 LEU A CG 1847 C CD1 . LEU A 243 ? 0.3643 0.4271 0.3438 0.0015 -0.0271 0.0125 243 LEU A CD1 1848 C CD2 . LEU A 243 ? 0.3738 0.4440 0.3608 0.0052 -0.0320 0.0144 243 LEU A CD2 1849 N N . LEU A 244 ? 0.4178 0.4880 0.3861 -0.0025 -0.0253 0.0089 244 LEU A N 1850 C CA . LEU A 244 ? 0.4257 0.4970 0.3914 -0.0019 -0.0254 0.0108 244 LEU A CA 1851 C C . LEU A 244 ? 0.4234 0.4912 0.3898 0.0006 -0.0254 0.0151 244 LEU A C 1852 O O . LEU A 244 ? 0.4169 0.4795 0.3813 0.0006 -0.0235 0.0161 244 LEU A O 1853 C CB . LEU A 244 ? 0.4412 0.5106 0.3998 -0.0047 -0.0231 0.0086 244 LEU A CB 1854 C CG . LEU A 244 ? 0.4496 0.5218 0.4051 -0.0048 -0.0234 0.0092 244 LEU A CG 1855 C CD1 . LEU A 244 ? 0.4485 0.5195 0.3974 -0.0083 -0.0215 0.0059 244 LEU A CD1 1856 C CD2 . LEU A 244 ? 0.4644 0.5337 0.4189 -0.0024 -0.0230 0.0131 244 LEU A CD2 1857 N N . ILE A 245 ? 0.4065 0.4774 0.3758 0.0027 -0.0274 0.0177 245 ILE A N 1858 C CA . ILE A 245 ? 0.4077 0.4764 0.3781 0.0049 -0.0277 0.0220 245 ILE A CA 1859 C C . ILE A 245 ? 0.4354 0.5053 0.4021 0.0052 -0.0273 0.0237 245 ILE A C 1860 O O . ILE A 245 ? 0.4473 0.5217 0.4141 0.0053 -0.0287 0.0231 245 ILE A O 1861 C CB . ILE A 245 ? 0.3959 0.4663 0.3723 0.0072 -0.0305 0.0242 245 ILE A CB 1862 C CG1 . ILE A 245 ? 0.3909 0.4598 0.3707 0.0070 -0.0309 0.0225 245 ILE A CG1 1863 C CG2 . ILE A 245 ? 0.3960 0.4642 0.3731 0.0089 -0.0307 0.0287 245 ILE A CG2 1864 C CD1 . ILE A 245 ? 0.3756 0.4454 0.3609 0.0091 -0.0338 0.0243 245 ILE A CD1 1865 N N . ASN A 246 ? 0.4487 0.5149 0.4121 0.0056 -0.0253 0.0257 246 ASN A N 1866 C CA . ASN A 246 ? 0.4718 0.5384 0.4305 0.0057 -0.0242 0.0268 246 ASN A CA 1867 C C . ASN A 246 ? 0.4787 0.5437 0.4381 0.0078 -0.0239 0.0312 246 ASN A C 1868 O O . ASN A 246 ? 0.4766 0.5378 0.4354 0.0082 -0.0223 0.0322 246 ASN A O 1869 C CB . ASN A 246 ? 0.5081 0.5713 0.4604 0.0036 -0.0215 0.0238 246 ASN A CB 1870 C CG . ASN A 246 ? 0.5541 0.6175 0.5005 0.0033 -0.0203 0.0240 246 ASN A CG 1871 O OD1 . ASN A 246 ? 0.5713 0.6306 0.5119 0.0023 -0.0179 0.0226 246 ASN A OD1 1872 N ND2 . ASN A 246 ? 0.5668 0.6345 0.5143 0.0043 -0.0220 0.0256 246 ASN A ND2 1873 N N . SER A 247 ? 0.4515 0.5197 0.4125 0.0092 -0.0256 0.0340 247 SER A N 1874 C CA . SER A 247 ? 0.4612 0.5288 0.4237 0.0110 -0.0257 0.0385 247 SER A CA 1875 C C . SER A 247 ? 0.4805 0.5515 0.4419 0.0119 -0.0267 0.0410 247 SER A C 1876 O O . SER A 247 ? 0.4778 0.5521 0.4397 0.0118 -0.0285 0.0399 247 SER A O 1877 C CB . SER A 247 ? 0.4437 0.5110 0.4122 0.0119 -0.0278 0.0404 247 SER A CB 1878 O OG . SER A 247 ? 0.4460 0.5131 0.4160 0.0132 -0.0282 0.0448 247 SER A OG 1879 N N . THR A 248 ? 0.4759 0.5461 0.4358 0.0130 -0.0255 0.0444 248 THR A N 1880 C CA . THR A 248 ? 0.5039 0.5771 0.4629 0.0140 -0.0264 0.0474 248 THR A CA 1881 C C . THR A 248 ? 0.4943 0.5679 0.4575 0.0152 -0.0279 0.0520 248 THR A C 1882 O O . THR A 248 ? 0.4931 0.5687 0.4556 0.0160 -0.0283 0.0553 248 THR A O 1883 C CB . THR A 248 ? 0.5269 0.5994 0.4799 0.0142 -0.0237 0.0477 248 THR A CB 1884 O OG1 . THR A 248 ? 0.5175 0.5871 0.4699 0.0148 -0.0215 0.0491 248 THR A OG1 1885 C CG2 . THR A 248 ? 0.5354 0.6071 0.4834 0.0126 -0.0224 0.0433 248 THR A CG2 1886 N N . GLY A 249 ? 0.4584 0.5299 0.4258 0.0152 -0.0287 0.0522 249 GLY A N 1887 C CA . GLY A 249 ? 0.4453 0.5167 0.4167 0.0159 -0.0303 0.0564 249 GLY A CA 1888 C C . GLY A 249 ? 0.4222 0.4906 0.3964 0.0156 -0.0298 0.0564 249 GLY A C 1889 O O . GLY A 249 ? 0.4254 0.4917 0.3979 0.0151 -0.0279 0.0536 249 GLY A O 1890 N N . ASN A 250 ? 0.4041 0.4720 0.3822 0.0159 -0.0317 0.0597 250 ASN A N 1891 C CA . ASN A 250 ? 0.3986 0.4640 0.3795 0.0156 -0.0314 0.0606 250 ASN A CA 1892 C C . ASN A 250 ? 0.3920 0.4551 0.3753 0.0151 -0.0323 0.0571 250 ASN A C 1893 O O . ASN A 250 ? 0.3864 0.4471 0.3716 0.0148 -0.0318 0.0572 250 ASN A O 1894 C CB . ASN A 250 ? 0.3927 0.4576 0.3710 0.0157 -0.0283 0.0613 250 ASN A CB 1895 C CG . ASN A 250 ? 0.4011 0.4687 0.3772 0.0163 -0.0274 0.0650 250 ASN A CG 1896 O OD1 . ASN A 250 ? 0.4243 0.4935 0.3967 0.0167 -0.0265 0.0642 250 ASN A OD1 1897 N ND2 . ASN A 250 ? 0.3630 0.4312 0.3412 0.0163 -0.0275 0.0689 250 ASN A ND2 1898 N N . LEU A 251 ? 0.3739 0.4380 0.3571 0.0151 -0.0334 0.0540 251 LEU A N 1899 C CA . LEU A 251 ? 0.3662 0.4289 0.3514 0.0147 -0.0342 0.0504 251 LEU A CA 1900 C C . LEU A 251 ? 0.3665 0.4281 0.3562 0.0153 -0.0372 0.0518 251 LEU A C 1901 O O . LEU A 251 ? 0.3586 0.4216 0.3494 0.0162 -0.0396 0.0535 251 LEU A O 1902 C CB . LEU A 251 ? 0.3536 0.4188 0.3369 0.0144 -0.0343 0.0467 251 LEU A CB 1903 C CG . LEU A 251 ? 0.3508 0.4156 0.3360 0.0139 -0.0350 0.0427 251 LEU A CG 1904 C CD1 . LEU A 251 ? 0.3394 0.4014 0.3235 0.0127 -0.0326 0.0404 251 LEU A CD1 1905 C CD2 . LEU A 251 ? 0.3354 0.4040 0.3192 0.0136 -0.0355 0.0396 251 LEU A CD2 1906 N N . ILE A 252 ? 0.3450 0.4039 0.3370 0.0149 -0.0372 0.0508 252 ILE A N 1907 C CA . ILE A 252 ? 0.3348 0.3921 0.3307 0.0154 -0.0399 0.0509 252 ILE A CA 1908 C C . ILE A 252 ? 0.3334 0.3912 0.3296 0.0153 -0.0399 0.0461 252 ILE A C 1909 O O . ILE A 252 ? 0.3263 0.3825 0.3222 0.0144 -0.0382 0.0437 252 ILE A O 1910 C CB . ILE A 252 ? 0.3422 0.3961 0.3402 0.0149 -0.0400 0.0530 252 ILE A CB 1911 C CG1 . ILE A 252 ? 0.3403 0.3946 0.3377 0.0147 -0.0396 0.0578 252 ILE A CG1 1912 C CG2 . ILE A 252 ? 0.3309 0.3825 0.3324 0.0155 -0.0430 0.0529 252 ILE A CG2 1913 C CD1 . ILE A 252 ? 0.3372 0.3924 0.3350 0.0154 -0.0421 0.0608 252 ILE A CD1 1914 N N . ALA A 253 ? 0.3219 0.3822 0.3187 0.0162 -0.0417 0.0447 253 ALA A N 1915 C CA . ALA A 253 ? 0.3324 0.3948 0.3289 0.0160 -0.0415 0.0401 253 ALA A CA 1916 C C . ALA A 253 ? 0.3217 0.3828 0.3217 0.0166 -0.0432 0.0382 253 ALA A C 1917 O O . ALA A 253 ? 0.3217 0.3808 0.3243 0.0179 -0.0456 0.0404 253 ALA A O 1918 C CB . ALA A 253 ? 0.3285 0.3953 0.3240 0.0167 -0.0426 0.0394 253 ALA A CB 1919 N N . PRO A 254 ? 0.3247 0.3869 0.3245 0.0157 -0.0420 0.0341 254 PRO A N 1920 C CA . PRO A 254 ? 0.3303 0.3920 0.3330 0.0164 -0.0435 0.0316 254 PRO A CA 1921 C C . PRO A 254 ? 0.3392 0.4045 0.3437 0.0183 -0.0461 0.0307 254 PRO A C 1922 O O . PRO A 254 ? 0.3275 0.3968 0.3304 0.0185 -0.0462 0.0303 254 PRO A O 1923 C CB . PRO A 254 ? 0.3344 0.3972 0.3356 0.0145 -0.0411 0.0276 254 PRO A CB 1924 C CG . PRO A 254 ? 0.3385 0.4041 0.3360 0.0134 -0.0394 0.0270 254 PRO A CG 1925 C CD . PRO A 254 ? 0.3286 0.3926 0.3249 0.0139 -0.0394 0.0314 254 PRO A CD 1926 N N . ARG A 255 ? 0.3339 0.3978 0.3414 0.0200 -0.0484 0.0303 255 ARG A N 1927 C CA . ARG A 255 ? 0.3361 0.4032 0.3453 0.0223 -0.0510 0.0290 255 ARG A CA 1928 C C . ARG A 255 ? 0.3414 0.4121 0.3517 0.0223 -0.0507 0.0243 255 ARG A C 1929 O O . ARG A 255 ? 0.3392 0.4133 0.3512 0.0244 -0.0527 0.0227 255 ARG A O 1930 C CB . ARG A 255 ? 0.3374 0.4004 0.3487 0.0246 -0.0539 0.0317 255 ARG A CB 1931 C CG . ARG A 255 ? 0.3363 0.3967 0.3465 0.0248 -0.0548 0.0365 255 ARG A CG 1932 C CD . ARG A 255 ? 0.3471 0.4035 0.3589 0.0270 -0.0581 0.0387 255 ARG A CD 1933 N NE . ARG A 255 ? 0.3630 0.4163 0.3736 0.0266 -0.0588 0.0436 255 ARG A NE 1934 C CZ . ARG A 255 ? 0.3633 0.4183 0.3725 0.0276 -0.0600 0.0458 255 ARG A CZ 1935 N NH1 . ARG A 255 ? 0.3613 0.4210 0.3704 0.0293 -0.0609 0.0437 255 ARG A NH1 1936 N NH2 . ARG A 255 ? 0.3649 0.4172 0.3730 0.0268 -0.0603 0.0503 255 ARG A NH2 1937 N N . GLY A 256 ? 0.3282 0.3985 0.3375 0.0199 -0.0480 0.0220 256 GLY A N 1938 C CA . GLY A 256 ? 0.3296 0.4026 0.3400 0.0194 -0.0475 0.0177 256 GLY A CA 1939 C C . GLY A 256 ? 0.3255 0.3949 0.3350 0.0171 -0.0451 0.0168 256 GLY A C 1940 O O . GLY A 256 ? 0.3170 0.3828 0.3243 0.0157 -0.0434 0.0190 256 GLY A O 1941 N N . TYR A 257 ? 0.3222 0.3923 0.3331 0.0169 -0.0449 0.0136 257 TYR A N 1942 C CA . TYR A 257 ? 0.3270 0.3937 0.3369 0.0147 -0.0427 0.0124 257 TYR A CA 1943 C C . TYR A 257 ? 0.3189 0.3828 0.3315 0.0159 -0.0438 0.0117 257 TYR A C 1944 O O . TYR A 257 ? 0.3168 0.3825 0.3320 0.0183 -0.0461 0.0108 257 TYR A O 1945 C CB . TYR A 257 ? 0.3332 0.4037 0.3410 0.0122 -0.0404 0.0086 257 TYR A CB 1946 C CG . TYR A 257 ? 0.3401 0.4163 0.3500 0.0131 -0.0415 0.0051 257 TYR A CG 1947 C CD1 . TYR A 257 ? 0.3413 0.4172 0.3531 0.0133 -0.0416 0.0027 257 TYR A CD1 1948 C CD2 . TYR A 257 ? 0.3487 0.4310 0.3588 0.0138 -0.0426 0.0042 257 TYR A CD2 1949 C CE1 . TYR A 257 ? 0.3431 0.4250 0.3569 0.0142 -0.0426 -0.0005 257 TYR A CE1 1950 C CE2 . TYR A 257 ? 0.3466 0.4350 0.3589 0.0148 -0.0436 0.0010 257 TYR A CE2 1951 C CZ . TYR A 257 ? 0.3490 0.4373 0.3631 0.0151 -0.0436 -0.0013 257 TYR A CZ 1952 O OH . TYR A 257 ? 0.3434 0.4382 0.3597 0.0162 -0.0446 -0.0045 257 TYR A OH 1953 N N . PHE A 258 ? 0.3013 0.3608 0.3130 0.0143 -0.0422 0.0120 258 PHE A N 1954 C CA . PHE A 258 ? 0.3047 0.3617 0.3184 0.0147 -0.0428 0.0107 258 PHE A CA 1955 C C . PHE A 258 ? 0.3275 0.3874 0.3403 0.0129 -0.0409 0.0065 258 PHE A C 1956 O O . PHE A 258 ? 0.3325 0.3935 0.3424 0.0104 -0.0385 0.0055 258 PHE A O 1957 C CB . PHE A 258 ? 0.2849 0.3358 0.2982 0.0140 -0.0422 0.0135 258 PHE A CB 1958 C CG . PHE A 258 ? 0.2731 0.3211 0.2874 0.0155 -0.0442 0.0177 258 PHE A CG 1959 C CD1 . PHE A 258 ? 0.2812 0.3292 0.2937 0.0149 -0.0435 0.0206 258 PHE A CD1 1960 C CD2 . PHE A 258 ? 0.2743 0.3195 0.2911 0.0174 -0.0468 0.0186 258 PHE A CD2 1961 C CE1 . PHE A 258 ? 0.2723 0.3178 0.2857 0.0160 -0.0452 0.0246 258 PHE A CE1 1962 C CE2 . PHE A 258 ? 0.2742 0.3164 0.2916 0.0184 -0.0487 0.0226 258 PHE A CE2 1963 C CZ . PHE A 258 ? 0.2827 0.3253 0.2985 0.0176 -0.0479 0.0256 258 PHE A CZ 1964 N N . LYS A 259 ? 0.3494 0.4104 0.3645 0.0141 -0.0421 0.0041 259 LYS A N 1965 C CA . LYS A 259 ? 0.3952 0.4580 0.4097 0.0123 -0.0403 0.0005 259 LYS A CA 1966 C C . LYS A 259 ? 0.4096 0.4666 0.4224 0.0104 -0.0386 0.0016 259 LYS A C 1967 O O . LYS A 259 ? 0.4296 0.4817 0.4431 0.0113 -0.0395 0.0048 259 LYS A O 1968 C CB . LYS A 259 ? 0.4456 0.5103 0.4630 0.0144 -0.0421 -0.0019 259 LYS A CB 1969 C CG . LYS A 259 ? 0.4839 0.5546 0.5032 0.0169 -0.0441 -0.0031 259 LYS A CG 1970 C CD . LYS A 259 ? 0.5202 0.5982 0.5396 0.0158 -0.0430 -0.0074 259 LYS A CD 1971 C CE . LYS A 259 ? 0.5493 0.6329 0.5716 0.0192 -0.0454 -0.0089 259 LYS A CE 1972 N NZ . LYS A 259 ? 0.6103 0.7017 0.6331 0.0181 -0.0443 -0.0132 259 LYS A NZ 1973 N N . ILE A 260 ? 0.4130 0.4705 0.4232 0.0077 -0.0361 -0.0005 260 ILE A N 1974 C CA . ILE A 260 ? 0.3905 0.4428 0.3990 0.0061 -0.0344 0.0000 260 ILE A CA 1975 C C . ILE A 260 ? 0.4083 0.4624 0.4170 0.0050 -0.0336 -0.0038 260 ILE A C 1976 O O . ILE A 260 ? 0.4100 0.4686 0.4174 0.0034 -0.0324 -0.0067 260 ILE A O 1977 C CB . ILE A 260 ? 0.4079 0.4577 0.4124 0.0041 -0.0321 0.0015 260 ILE A CB 1978 C CG1 . ILE A 260 ? 0.4157 0.4601 0.4185 0.0028 -0.0305 0.0021 260 ILE A CG1 1979 C CG2 . ILE A 260 ? 0.4071 0.4608 0.4086 0.0020 -0.0304 -0.0008 260 ILE A CG2 1980 C CD1 . ILE A 260 ? 0.4063 0.4473 0.4060 0.0021 -0.0289 0.0049 260 ILE A CD1 1981 N N . ARG A 261 ? 0.3913 0.4420 0.4016 0.0058 -0.0343 -0.0039 261 ARG A N 1982 C CA . ARG A 261 ? 0.3937 0.4460 0.4043 0.0049 -0.0337 -0.0074 261 ARG A CA 1983 C C . ARG A 261 ? 0.3714 0.4185 0.3795 0.0028 -0.0318 -0.0071 261 ARG A C 1984 O O . ARG A 261 ? 0.3385 0.3810 0.3453 0.0027 -0.0313 -0.0041 261 ARG A O 1985 C CB . ARG A 261 ? 0.4239 0.4766 0.4383 0.0079 -0.0363 -0.0080 261 ARG A CB 1986 C CG . ARG A 261 ? 0.4648 0.5224 0.4815 0.0104 -0.0384 -0.0083 261 ARG A CG 1987 C CD . ARG A 261 ? 0.4933 0.5513 0.5132 0.0135 -0.0409 -0.0095 261 ARG A CD 1988 N NE . ARG A 261 ? 0.5203 0.5828 0.5422 0.0164 -0.0430 -0.0098 261 ARG A NE 1989 C CZ . ARG A 261 ? 0.5582 0.6282 0.5808 0.0167 -0.0428 -0.0129 261 ARG A CZ 1990 N NH1 . ARG A 261 ? 0.5632 0.6371 0.5845 0.0139 -0.0405 -0.0159 261 ARG A NH1 1991 N NH2 . ARG A 261 ? 0.5699 0.6438 0.5944 0.0197 -0.0449 -0.0129 261 ARG A NH2 1992 N N . SER A 262 ? 0.3810 0.4292 0.3883 0.0013 -0.0305 -0.0102 262 SER A N 1993 C CA . SER A 262 ? 0.3853 0.4284 0.3904 -0.0001 -0.0291 -0.0100 262 SER A CA 1994 C C . SER A 262 ? 0.3686 0.4112 0.3762 0.0009 -0.0303 -0.0116 262 SER A C 1995 O O . SER A 262 ? 0.3611 0.4085 0.3708 0.0018 -0.0312 -0.0143 262 SER A O 1996 C CB . SER A 262 ? 0.4268 0.4700 0.4275 -0.0035 -0.0262 -0.0119 262 SER A CB 1997 O OG . SER A 262 ? 0.4510 0.4991 0.4520 -0.0047 -0.0257 -0.0157 262 SER A OG 1998 N N . GLY A 263 ? 0.3413 0.3785 0.3487 0.0011 -0.0305 -0.0098 263 GLY A N 1999 C CA . GLY A 263 ? 0.3405 0.3765 0.3497 0.0020 -0.0315 -0.0113 263 GLY A CA 2000 C C . GLY A 263 ? 0.3183 0.3482 0.3272 0.0021 -0.0319 -0.0085 263 GLY A C 2001 O O . GLY A 263 ? 0.3200 0.3470 0.3266 0.0008 -0.0304 -0.0064 263 GLY A O 2002 N N . LYS A 264 ? 0.3052 0.3333 0.3166 0.0038 -0.0339 -0.0085 264 LYS A N 2003 C CA . LYS A 264 ? 0.2940 0.3167 0.3051 0.0035 -0.0343 -0.0068 264 LYS A CA 2004 C C . LYS A 264 ? 0.2523 0.2719 0.2654 0.0051 -0.0365 -0.0030 264 LYS A C 2005 O O . LYS A 264 ? 0.2290 0.2447 0.2428 0.0053 -0.0376 -0.0016 264 LYS A O 2006 C CB . LYS A 264 ? 0.3354 0.3580 0.3474 0.0039 -0.0349 -0.0096 264 LYS A CB 2007 C CG . LYS A 264 ? 0.3778 0.4031 0.3873 0.0018 -0.0324 -0.0130 264 LYS A CG 2008 C CD . LYS A 264 ? 0.4152 0.4417 0.4257 0.0023 -0.0329 -0.0163 264 LYS A CD 2009 C CE . LYS A 264 ? 0.4502 0.4788 0.4577 -0.0002 -0.0302 -0.0192 264 LYS A CE 2010 N NZ . LYS A 264 ? 0.4788 0.5078 0.4867 0.0000 -0.0305 -0.0220 264 LYS A NZ 2011 N N . SER A 265 ? 0.2365 0.2578 0.2504 0.0060 -0.0372 -0.0012 265 SER A N 2012 C CA . SER A 265 ? 0.2304 0.2491 0.2461 0.0074 -0.0395 0.0023 265 SER A CA 2013 C C . SER A 265 ? 0.2257 0.2414 0.2402 0.0061 -0.0385 0.0058 265 SER A C 2014 O O . SER A 265 ? 0.2086 0.2248 0.2205 0.0046 -0.0361 0.0058 265 SER A O 2015 C CB . SER A 265 ? 0.2373 0.2590 0.2543 0.0090 -0.0407 0.0029 265 SER A CB 2016 O OG . SER A 265 ? 0.2350 0.2594 0.2535 0.0107 -0.0420 -0.0001 265 SER A OG 2017 N N . SER A 266 ? 0.2238 0.2363 0.2398 0.0067 -0.0406 0.0088 266 SER A N 2018 C CA . SER A 266 ? 0.2192 0.2298 0.2346 0.0057 -0.0399 0.0125 266 SER A CA 2019 C C . SER A 266 ? 0.2121 0.2210 0.2295 0.0066 -0.0425 0.0161 266 SER A C 2020 O O . SER A 266 ? 0.2111 0.2201 0.2301 0.0080 -0.0446 0.0158 266 SER A O 2021 C CB . SER A 266 ? 0.2218 0.2296 0.2361 0.0045 -0.0391 0.0122 266 SER A CB 2022 O OG . SER A 266 ? 0.2280 0.2349 0.2412 0.0036 -0.0379 0.0155 266 SER A OG 2023 N N . ILE A 267 ? 0.2044 0.2118 0.2215 0.0056 -0.0422 0.0195 267 ILE A N 2024 C CA . ILE A 267 ? 0.2080 0.2139 0.2267 0.0058 -0.0443 0.0234 267 ILE A CA 2025 C C . ILE A 267 ? 0.2166 0.2202 0.2355 0.0045 -0.0445 0.0255 267 ILE A C 2026 O O . ILE A 267 ? 0.1988 0.2028 0.2161 0.0036 -0.0423 0.0251 267 ILE A O 2027 C CB . ILE A 267 ? 0.2106 0.2192 0.2288 0.0059 -0.0433 0.0260 267 ILE A CB 2028 C CG1 . ILE A 267 ? 0.2141 0.2216 0.2339 0.0060 -0.0456 0.0300 267 ILE A CG1 2029 C CG2 . ILE A 267 ? 0.2073 0.2173 0.2233 0.0050 -0.0404 0.0267 267 ILE A CG2 2030 C CD1 . ILE A 267 ? 0.2118 0.2219 0.2314 0.0067 -0.0454 0.0317 267 ILE A CD1 2031 N N . MET A 268 ? 0.2161 0.2171 0.2367 0.0043 -0.0471 0.0277 268 MET A N 2032 C CA . MET A 268 ? 0.2276 0.2265 0.2486 0.0028 -0.0477 0.0298 268 MET A CA 2033 C C . MET A 268 ? 0.2325 0.2305 0.2548 0.0021 -0.0498 0.0341 268 MET A C 2034 O O . MET A 268 ? 0.2394 0.2360 0.2625 0.0029 -0.0519 0.0346 268 MET A O 2035 C CB . MET A 268 ? 0.2308 0.2265 0.2519 0.0027 -0.0490 0.0272 268 MET A CB 2036 C CG . MET A 268 ? 0.2417 0.2355 0.2629 0.0010 -0.0494 0.0288 268 MET A CG 2037 S SD . MET A 268 ? 0.2454 0.2352 0.2665 0.0010 -0.0510 0.0255 268 MET A SD 2038 C CE . MET A 268 ? 0.2263 0.2183 0.2456 0.0016 -0.0480 0.0210 268 MET A CE 2039 N N . ARG A 269 ? 0.2280 0.2271 0.2505 0.0008 -0.0492 0.0373 269 ARG A N 2040 C CA . ARG A 269 ? 0.2387 0.2372 0.2625 -0.0004 -0.0511 0.0415 269 ARG A CA 2041 C C . ARG A 269 ? 0.2395 0.2342 0.2640 -0.0017 -0.0535 0.0416 269 ARG A C 2042 O O . ARG A 269 ? 0.2316 0.2261 0.2558 -0.0025 -0.0527 0.0408 269 ARG A O 2043 C CB . ARG A 269 ? 0.2476 0.2499 0.2713 -0.0012 -0.0493 0.0449 269 ARG A CB 2044 C CG . ARG A 269 ? 0.2570 0.2629 0.2795 0.0000 -0.0469 0.0449 269 ARG A CG 2045 C CD . ARG A 269 ? 0.2697 0.2793 0.2922 -0.0003 -0.0454 0.0487 269 ARG A CD 2046 N NE . ARG A 269 ? 0.2722 0.2847 0.2931 0.0009 -0.0431 0.0483 269 ARG A NE 2047 C CZ . ARG A 269 ? 0.2840 0.2977 0.3026 0.0018 -0.0403 0.0464 269 ARG A CZ 2048 N NH1 . ARG A 269 ? 0.2881 0.3007 0.3058 0.0016 -0.0393 0.0447 269 ARG A NH1 2049 N NH2 . ARG A 269 ? 0.2961 0.3121 0.3131 0.0028 -0.0385 0.0463 269 ARG A NH2 2050 N N . SER A 270 ? 0.2364 0.2276 0.2615 -0.0020 -0.0564 0.0426 270 SER A N 2051 C CA . SER A 270 ? 0.2465 0.2333 0.2719 -0.0034 -0.0589 0.0427 270 SER A CA 2052 C C . SER A 270 ? 0.2668 0.2501 0.2924 -0.0041 -0.0621 0.0453 270 SER A C 2053 O O . SER A 270 ? 0.2582 0.2412 0.2836 -0.0027 -0.0627 0.0453 270 SER A O 2054 C CB . SER A 270 ? 0.2467 0.2306 0.2714 -0.0020 -0.0593 0.0380 270 SER A CB 2055 O OG . SER A 270 ? 0.2597 0.2387 0.2842 -0.0032 -0.0620 0.0380 270 SER A OG 2056 N N . ASP A 271 ? 0.2740 0.2546 0.2999 -0.0064 -0.0641 0.0474 271 ASP A N 2057 C CA . ASP A 271 ? 0.3005 0.2762 0.3260 -0.0075 -0.0674 0.0495 271 ASP A CA 2058 C C . ASP A 271 ? 0.3026 0.2718 0.3270 -0.0073 -0.0699 0.0468 271 ASP A C 2059 O O . ASP A 271 ? 0.3065 0.2704 0.3300 -0.0084 -0.0730 0.0484 271 ASP A O 2060 C CB . ASP A 271 ? 0.3157 0.2930 0.3420 -0.0107 -0.0682 0.0544 271 ASP A CB 2061 C CG . ASP A 271 ? 0.3354 0.3182 0.3624 -0.0105 -0.0663 0.0573 271 ASP A CG 2062 O OD1 . ASP A 271 ? 0.3324 0.3156 0.3590 -0.0083 -0.0658 0.0563 271 ASP A OD1 2063 O OD2 . ASP A 271 ? 0.3687 0.3558 0.3967 -0.0123 -0.0654 0.0605 271 ASP A OD2 2064 N N . ALA A 272 ? 0.2888 0.2579 0.3128 -0.0058 -0.0687 0.0427 272 ALA A N 2065 C CA . ALA A 272 ? 0.2984 0.2616 0.3212 -0.0054 -0.0709 0.0399 272 ALA A CA 2066 C C . ALA A 272 ? 0.3045 0.2636 0.3262 -0.0029 -0.0728 0.0382 272 ALA A C 2067 O O . ALA A 272 ? 0.2895 0.2517 0.3116 -0.0006 -0.0714 0.0371 272 ALA A O 2068 C CB . ALA A 272 ? 0.2935 0.2582 0.3162 -0.0046 -0.0690 0.0360 272 ALA A CB 2069 N N . PRO A 273 ? 0.3266 0.2787 0.3468 -0.0033 -0.0760 0.0382 273 PRO A N 2070 C CA . PRO A 273 ? 0.3405 0.2883 0.3593 -0.0004 -0.0780 0.0365 273 PRO A CA 2071 C C . PRO A 273 ? 0.3355 0.2846 0.3543 0.0029 -0.0767 0.0313 273 PRO A C 2072 O O . PRO A 273 ? 0.3206 0.2712 0.3396 0.0026 -0.0753 0.0288 273 PRO A O 2073 C CB . PRO A 273 ? 0.3587 0.2980 0.3753 -0.0019 -0.0817 0.0376 273 PRO A CB 2074 C CG . PRO A 273 ? 0.3609 0.3002 0.3777 -0.0049 -0.0814 0.0379 273 PRO A CG 2075 C CD . PRO A 273 ? 0.3493 0.2969 0.3686 -0.0061 -0.0781 0.0394 273 PRO A CD 2076 N N . ILE A 274 ? 0.3445 0.2933 0.3628 0.0060 -0.0772 0.0298 274 ILE A N 2077 C CA . ILE A 274 ? 0.3675 0.3179 0.3858 0.0093 -0.0763 0.0249 274 ILE A CA 2078 C C . ILE A 274 ? 0.3934 0.3367 0.4096 0.0109 -0.0791 0.0225 274 ILE A C 2079 O O . ILE A 274 ? 0.4099 0.3472 0.4244 0.0114 -0.0820 0.0242 274 ILE A O 2080 C CB . ILE A 274 ? 0.3803 0.3351 0.3994 0.0121 -0.0753 0.0241 274 ILE A CB 2081 C CG1 . ILE A 274 ? 0.3964 0.3581 0.4172 0.0104 -0.0723 0.0262 274 ILE A CG1 2082 C CG2 . ILE A 274 ? 0.3732 0.3303 0.3923 0.0153 -0.0743 0.0190 274 ILE A CG2 2083 C CD1 . ILE A 274 ? 0.4326 0.3992 0.4541 0.0126 -0.0709 0.0253 274 ILE A CD1 2084 N N . GLY A 275 ? 0.3928 0.3363 0.4088 0.0116 -0.0783 0.0188 275 GLY A N 2085 C CA . GLY A 275 ? 0.3972 0.3338 0.4109 0.0132 -0.0808 0.0163 275 GLY A CA 2086 C C . GLY A 275 ? 0.4042 0.3428 0.4177 0.0174 -0.0802 0.0115 275 GLY A C 2087 O O . GLY A 275 ? 0.3518 0.2978 0.3672 0.0184 -0.0774 0.0096 275 GLY A O 2088 N N . LYS A 276 ? 0.4115 0.3437 0.4228 0.0199 -0.0829 0.0096 276 LYS A N 2089 C CA . LYS A 276 ? 0.4303 0.3643 0.4412 0.0241 -0.0826 0.0048 276 LYS A CA 2090 C C . LYS A 276 ? 0.4127 0.3470 0.4233 0.0235 -0.0815 0.0016 276 LYS A C 2091 O O . LYS A 276 ? 0.4223 0.3498 0.4305 0.0239 -0.0836 0.0003 276 LYS A O 2092 C CB . LYS A 276 ? 0.4762 0.4032 0.4846 0.0277 -0.0860 0.0042 276 LYS A CB 2093 C CG . LYS A 276 ? 0.5185 0.4454 0.5271 0.0286 -0.0870 0.0074 276 LYS A CG 2094 C CD . LYS A 276 ? 0.5647 0.4868 0.5710 0.0334 -0.0898 0.0058 276 LYS A CD 2095 C CE . LYS A 276 ? 0.5965 0.5194 0.6031 0.0343 -0.0906 0.0089 276 LYS A CE 2096 N NZ . LYS A 276 ? 0.6313 0.5648 0.6412 0.0349 -0.0876 0.0083 276 LYS A NZ 2097 N N . CYS A 277 ? 0.3826 0.3243 0.3952 0.0222 -0.0781 0.0004 277 CYS A N 2098 C CA . CYS A 277 ? 0.3776 0.3202 0.3899 0.0212 -0.0768 -0.0023 277 CYS A CA 2099 C C . CYS A 277 ? 0.3460 0.2977 0.3603 0.0212 -0.0730 -0.0043 277 CYS A C 2100 O O . CYS A 277 ? 0.3356 0.2922 0.3514 0.0218 -0.0718 -0.0034 277 CYS A O 2101 C CB . CYS A 277 ? 0.3987 0.3376 0.4103 0.0170 -0.0773 0.0004 277 CYS A CB 2102 S SG . CYS A 277 ? 0.4385 0.3808 0.4521 0.0131 -0.0759 0.0057 277 CYS A SG 2103 N N . ASN A 278 ? 0.3170 0.2705 0.3310 0.0204 -0.0713 -0.0071 278 ASN A N 2104 C CA . ASN A 278 ? 0.3105 0.2720 0.3258 0.0204 -0.0679 -0.0095 278 ASN A CA 2105 C C . ASN A 278 ? 0.3056 0.2684 0.3208 0.0168 -0.0658 -0.0086 278 ASN A C 2106 O O . ASN A 278 ? 0.2890 0.2485 0.3029 0.0159 -0.0664 -0.0097 278 ASN A O 2107 C CB . ASN A 278 ? 0.3188 0.2820 0.3335 0.0235 -0.0678 -0.0144 278 ASN A CB 2108 C CG . ASN A 278 ? 0.3209 0.2926 0.3369 0.0239 -0.0646 -0.0169 278 ASN A CG 2109 O OD1 . ASN A 278 ? 0.3312 0.3063 0.3475 0.0211 -0.0620 -0.0167 278 ASN A OD1 2110 N ND2 . ASN A 278 ? 0.3265 0.3019 0.3431 0.0273 -0.0647 -0.0195 278 ASN A ND2 2111 N N . SER A 279 ? 0.2925 0.2601 0.3089 0.0149 -0.0634 -0.0067 279 SER A N 2112 C CA . SER A 279 ? 0.3008 0.2699 0.3169 0.0119 -0.0612 -0.0059 279 SER A CA 2113 C C . SER A 279 ? 0.2864 0.2620 0.3033 0.0111 -0.0580 -0.0058 279 SER A C 2114 O O . SER A 279 ? 0.2810 0.2588 0.2990 0.0115 -0.0578 -0.0039 279 SER A O 2115 C CB . SER A 279 ? 0.3082 0.2730 0.3242 0.0094 -0.0628 -0.0016 279 SER A CB 2116 O OG . SER A 279 ? 0.3296 0.2959 0.3453 0.0068 -0.0609 -0.0008 279 SER A OG 2117 N N . GLU A 280 ? 0.2825 0.2609 0.2986 0.0098 -0.0555 -0.0079 280 GLU A N 2118 C CA . GLU A 280 ? 0.2895 0.2735 0.3056 0.0090 -0.0524 -0.0084 280 GLU A CA 2119 C C . GLU A 280 ? 0.2673 0.2517 0.2835 0.0069 -0.0512 -0.0045 280 GLU A C 2120 O O . GLU A 280 ? 0.2608 0.2489 0.2772 0.0067 -0.0495 -0.0039 280 GLU A O 2121 C CB . GLU A 280 ? 0.3194 0.3056 0.3340 0.0081 -0.0501 -0.0117 280 GLU A CB 2122 C CG . GLU A 280 ? 0.3538 0.3415 0.3683 0.0102 -0.0505 -0.0160 280 GLU A CG 2123 C CD . GLU A 280 ? 0.3925 0.3859 0.4080 0.0118 -0.0494 -0.0179 280 GLU A CD 2124 O OE1 . GLU A 280 ? 0.4026 0.3992 0.4182 0.0105 -0.0475 -0.0166 280 GLU A OE1 2125 O OE2 . GLU A 280 ? 0.4076 0.4022 0.4236 0.0144 -0.0505 -0.0208 280 GLU A OE2 2126 N N . CYS A 281 ? 0.2594 0.2402 0.2752 0.0052 -0.0521 -0.0019 281 CYS A N 2127 C CA . CYS A 281 ? 0.2494 0.2309 0.2651 0.0033 -0.0509 0.0016 281 CYS A CA 2128 C C . CYS A 281 ? 0.2401 0.2196 0.2572 0.0031 -0.0530 0.0056 281 CYS A C 2129 O O . CYS A 281 ? 0.2457 0.2210 0.2631 0.0029 -0.0556 0.0067 281 CYS A O 2130 C CB . CYS A 281 ? 0.2570 0.2368 0.2714 0.0015 -0.0502 0.0019 281 CYS A CB 2131 S SG . CYS A 281 ? 0.2591 0.2403 0.2732 -0.0003 -0.0486 0.0061 281 CYS A SG 2132 N N . ILE A 282 ? 0.2259 0.2082 0.2436 0.0031 -0.0518 0.0079 282 ILE A N 2133 C CA . ILE A 282 ? 0.2267 0.2078 0.2456 0.0027 -0.0535 0.0119 282 ILE A CA 2134 C C . ILE A 282 ? 0.2246 0.2074 0.2434 0.0009 -0.0520 0.0153 282 ILE A C 2135 O O . ILE A 282 ? 0.2132 0.1991 0.2311 0.0007 -0.0493 0.0149 282 ILE A O 2136 C CB . ILE A 282 ? 0.2266 0.2100 0.2464 0.0043 -0.0536 0.0121 282 ILE A CB 2137 C CG1 . ILE A 282 ? 0.2382 0.2207 0.2582 0.0066 -0.0551 0.0086 282 ILE A CG1 2138 C CG2 . ILE A 282 ? 0.2218 0.2040 0.2427 0.0038 -0.0553 0.0165 282 ILE A CG2 2139 C CD1 . ILE A 282 ? 0.2440 0.2294 0.2647 0.0085 -0.0551 0.0083 282 ILE A CD1 2140 N N . THR A 283 ? 0.2198 0.2004 0.2394 -0.0003 -0.0539 0.0187 283 THR A N 2141 C CA . THR A 283 ? 0.2228 0.2054 0.2426 -0.0018 -0.0529 0.0225 283 THR A CA 2142 C C . THR A 283 ? 0.2265 0.2085 0.2478 -0.0022 -0.0549 0.0262 283 THR A C 2143 O O . THR A 283 ? 0.2300 0.2088 0.2517 -0.0017 -0.0574 0.0259 283 THR A O 2144 C CB . THR A 283 ? 0.2238 0.2052 0.2432 -0.0035 -0.0531 0.0233 283 THR A CB 2145 O OG1 . THR A 283 ? 0.2215 0.1995 0.2418 -0.0047 -0.0562 0.0253 283 THR A OG1 2146 C CG2 . THR A 283 ? 0.2242 0.2046 0.2419 -0.0032 -0.0520 0.0194 283 THR A CG2 2147 N N . PRO A 284 ? 0.2263 0.2113 0.2481 -0.0031 -0.0538 0.0298 284 PRO A N 2148 C CA . PRO A 284 ? 0.2368 0.2215 0.2600 -0.0038 -0.0558 0.0337 284 PRO A CA 2149 C C . PRO A 284 ? 0.2562 0.2369 0.2799 -0.0056 -0.0589 0.0353 284 PRO A C 2150 O O . PRO A 284 ? 0.2566 0.2356 0.2809 -0.0062 -0.0611 0.0377 284 PRO A O 2151 C CB . PRO A 284 ? 0.2326 0.2217 0.2560 -0.0045 -0.0537 0.0369 284 PRO A CB 2152 C CG . PRO A 284 ? 0.2257 0.2172 0.2475 -0.0033 -0.0506 0.0342 284 PRO A CG 2153 C CD . PRO A 284 ? 0.2204 0.2093 0.2414 -0.0031 -0.0507 0.0303 284 PRO A CD 2154 N N . ASN A 285 ? 0.2656 0.2446 0.2887 -0.0066 -0.0592 0.0340 285 ASN A N 2155 C CA . ASN A 285 ? 0.2893 0.2641 0.3125 -0.0084 -0.0622 0.0351 285 ASN A CA 2156 C C . ASN A 285 ? 0.2888 0.2582 0.3111 -0.0073 -0.0645 0.0321 285 ASN A C 2157 O O . ASN A 285 ? 0.3124 0.2774 0.3343 -0.0087 -0.0672 0.0328 285 ASN A O 2158 C CB . ASN A 285 ? 0.3144 0.2896 0.3371 -0.0098 -0.0617 0.0348 285 ASN A CB 2159 C CG . ASN A 285 ? 0.3396 0.3202 0.3629 -0.0104 -0.0593 0.0372 285 ASN A CG 2160 O OD1 . ASN A 285 ? 0.3131 0.2969 0.3359 -0.0089 -0.0565 0.0361 285 ASN A OD1 2161 N ND2 . ASN A 285 ? 0.4057 0.3874 0.4299 -0.0126 -0.0604 0.0405 285 ASN A ND2 2162 N N . GLY A 286 ? 0.2725 0.2423 0.2943 -0.0048 -0.0634 0.0287 286 GLY A N 2163 C CA . GLY A 286 ? 0.2691 0.2346 0.2899 -0.0032 -0.0650 0.0253 286 GLY A CA 2164 C C . GLY A 286 ? 0.2704 0.2376 0.2904 -0.0017 -0.0629 0.0209 286 GLY A C 2165 O O . GLY A 286 ? 0.2593 0.2301 0.2793 -0.0024 -0.0603 0.0207 286 GLY A O 2166 N N . SER A 287 ? 0.2716 0.2362 0.2909 0.0002 -0.0639 0.0174 287 SER A N 2167 C CA . SER A 287 ? 0.2694 0.2356 0.2879 0.0014 -0.0621 0.0131 287 SER A CA 2168 C C . SER A 287 ? 0.2704 0.2344 0.2879 -0.0003 -0.0624 0.0125 287 SER A C 2169 O O . SER A 287 ? 0.2669 0.2268 0.2841 -0.0017 -0.0648 0.0143 287 SER A O 2170 C CB . SER A 287 ? 0.2718 0.2362 0.2898 0.0041 -0.0633 0.0096 287 SER A CB 2171 O OG . SER A 287 ? 0.2723 0.2389 0.2913 0.0058 -0.0633 0.0101 287 SER A OG 2172 N N . ILE A 288 ? 0.2669 0.2336 0.2836 -0.0003 -0.0599 0.0101 288 ILE A N 2173 C CA . ILE A 288 ? 0.2713 0.2362 0.2868 -0.0017 -0.0600 0.0091 288 ILE A CA 2174 C C . ILE A 288 ? 0.2744 0.2396 0.2887 -0.0002 -0.0590 0.0043 288 ILE A C 2175 O O . ILE A 288 ? 0.2762 0.2447 0.2905 0.0012 -0.0571 0.0021 288 ILE A O 2176 C CB . ILE A 288 ? 0.2724 0.2402 0.2878 -0.0036 -0.0580 0.0115 288 ILE A CB 2177 C CG1 . ILE A 288 ? 0.2679 0.2403 0.2829 -0.0029 -0.0545 0.0101 288 ILE A CG1 2178 C CG2 . ILE A 288 ? 0.2724 0.2406 0.2893 -0.0051 -0.0591 0.0163 288 ILE A CG2 2179 C CD1 . ILE A 288 ? 0.2615 0.2361 0.2756 -0.0044 -0.0525 0.0120 288 ILE A CD1 2180 N N . PRO A 289 ? 0.2918 0.2536 0.3048 -0.0007 -0.0602 0.0027 289 PRO A N 2181 C CA . PRO A 289 ? 0.3013 0.2638 0.3129 0.0002 -0.0590 -0.0015 289 PRO A CA 2182 C C . PRO A 289 ? 0.2942 0.2612 0.3052 -0.0006 -0.0555 -0.0020 289 PRO A C 2183 O O . PRO A 289 ? 0.2879 0.2560 0.2990 -0.0023 -0.0546 0.0009 289 PRO A O 2184 C CB . PRO A 289 ? 0.3129 0.2708 0.3230 -0.0007 -0.0610 -0.0022 289 PRO A CB 2185 C CG . PRO A 289 ? 0.3251 0.2793 0.3360 -0.0020 -0.0638 0.0013 289 PRO A CG 2186 C CD . PRO A 289 ? 0.3045 0.2617 0.3172 -0.0024 -0.0630 0.0048 289 PRO A CD 2187 N N . ASN A 290 ? 0.2855 0.2550 0.2956 0.0005 -0.0537 -0.0057 290 ASN A N 2188 C CA . ASN A 290 ? 0.2946 0.2678 0.3035 -0.0004 -0.0504 -0.0065 290 ASN A CA 2189 C C . ASN A 290 ? 0.2903 0.2633 0.2971 -0.0008 -0.0493 -0.0098 290 ASN A C 2190 O O . ASN A 290 ? 0.3200 0.2960 0.3255 -0.0012 -0.0466 -0.0117 290 ASN A O 2191 C CB . ASN A 290 ? 0.2915 0.2689 0.3010 0.0006 -0.0485 -0.0076 290 ASN A CB 2192 C CG . ASN A 290 ? 0.3025 0.2813 0.3122 0.0026 -0.0488 -0.0115 290 ASN A CG 2193 O OD1 . ASN A 290 ? 0.3085 0.2846 0.3179 0.0036 -0.0506 -0.0135 290 ASN A OD1 2194 N ND2 . ASN A 290 ? 0.2816 0.2646 0.2918 0.0034 -0.0472 -0.0127 290 ASN A ND2 2195 N N . ASP A 291 ? 0.3014 0.2706 0.3076 -0.0010 -0.0514 -0.0104 291 ASP A N 2196 C CA . ASP A 291 ? 0.3076 0.2762 0.3116 -0.0016 -0.0506 -0.0131 291 ASP A CA 2197 C C . ASP A 291 ? 0.2906 0.2601 0.2930 -0.0037 -0.0486 -0.0114 291 ASP A C 2198 O O . ASP A 291 ? 0.3060 0.2770 0.3063 -0.0042 -0.0464 -0.0136 291 ASP A O 2199 C CB . ASP A 291 ? 0.3299 0.2939 0.3334 -0.0012 -0.0535 -0.0142 291 ASP A CB 2200 C CG . ASP A 291 ? 0.3676 0.3279 0.3719 -0.0025 -0.0560 -0.0105 291 ASP A CG 2201 O OD1 . ASP A 291 ? 0.4029 0.3623 0.4089 -0.0020 -0.0576 -0.0083 291 ASP A OD1 2202 O OD2 . ASP A 291 ? 0.3901 0.3484 0.3932 -0.0042 -0.0566 -0.0096 291 ASP A OD2 2203 N N . LYS A 292 ? 0.2657 0.2344 0.2690 -0.0048 -0.0492 -0.0074 292 LYS A N 2204 C CA . LYS A 292 ? 0.2505 0.2196 0.2522 -0.0064 -0.0478 -0.0055 292 LYS A CA 2205 C C . LYS A 292 ? 0.2399 0.2123 0.2409 -0.0065 -0.0448 -0.0048 292 LYS A C 2206 O O . LYS A 292 ? 0.2435 0.2177 0.2459 -0.0055 -0.0444 -0.0044 292 LYS A O 2207 C CB . LYS A 292 ? 0.2513 0.2187 0.2543 -0.0075 -0.0499 -0.0016 292 LYS A CB 2208 C CG . LYS A 292 ? 0.2579 0.2214 0.2611 -0.0078 -0.0531 -0.0022 292 LYS A CG 2209 C CD . LYS A 292 ? 0.2636 0.2258 0.2681 -0.0094 -0.0553 0.0017 292 LYS A CD 2210 C CE . LYS A 292 ? 0.2866 0.2443 0.2908 -0.0100 -0.0585 0.0010 292 LYS A CE 2211 N NZ . LYS A 292 ? 0.2977 0.2530 0.3028 -0.0085 -0.0603 -0.0002 292 LYS A NZ 2212 N N . PRO A 293 ? 0.2288 0.2016 0.2272 -0.0074 -0.0427 -0.0048 293 PRO A N 2213 C CA . PRO A 293 ? 0.2202 0.1953 0.2171 -0.0075 -0.0398 -0.0043 293 PRO A CA 2214 C C . PRO A 293 ? 0.2139 0.1898 0.2119 -0.0074 -0.0397 -0.0002 293 PRO A C 2215 O O . PRO A 293 ? 0.1996 0.1774 0.1970 -0.0071 -0.0378 0.0002 293 PRO A O 2216 C CB . PRO A 293 ? 0.2231 0.1974 0.2163 -0.0086 -0.0378 -0.0056 293 PRO A CB 2217 C CG . PRO A 293 ? 0.2306 0.2025 0.2238 -0.0091 -0.0399 -0.0049 293 PRO A CG 2218 C CD . PRO A 293 ? 0.2303 0.2013 0.2264 -0.0084 -0.0427 -0.0058 293 PRO A CD 2219 N N . PHE A 294 ? 0.2047 0.1797 0.2043 -0.0078 -0.0417 0.0026 294 PHE A N 2220 C CA . PHE A 294 ? 0.2017 0.1779 0.2024 -0.0078 -0.0417 0.0067 294 PHE A CA 2221 C C . PHE A 294 ? 0.2017 0.1776 0.2058 -0.0078 -0.0447 0.0089 294 PHE A C 2222 O O . PHE A 294 ? 0.2018 0.1755 0.2069 -0.0080 -0.0470 0.0076 294 PHE A O 2223 C CB . PHE A 294 ? 0.2046 0.1807 0.2034 -0.0084 -0.0409 0.0087 294 PHE A CB 2224 C CG . PHE A 294 ? 0.2013 0.1768 0.1961 -0.0085 -0.0383 0.0065 294 PHE A CG 2225 C CD1 . PHE A 294 ? 0.2029 0.1794 0.1958 -0.0080 -0.0357 0.0061 294 PHE A CD1 2226 C CD2 . PHE A 294 ? 0.2077 0.1814 0.2006 -0.0093 -0.0385 0.0049 294 PHE A CD2 2227 C CE1 . PHE A 294 ? 0.2046 0.1800 0.1934 -0.0084 -0.0333 0.0041 294 PHE A CE1 2228 C CE2 . PHE A 294 ? 0.2091 0.1819 0.1980 -0.0095 -0.0361 0.0029 294 PHE A CE2 2229 C CZ . PHE A 294 ? 0.2058 0.1793 0.1925 -0.0092 -0.0335 0.0025 294 PHE A CZ 2230 N N . GLN A 295 ? 0.1982 0.1760 0.2037 -0.0077 -0.0446 0.0124 295 GLN A N 2231 C CA . GLN A 295 ? 0.2003 0.1780 0.2088 -0.0081 -0.0472 0.0151 295 GLN A CA 2232 C C . GLN A 295 ? 0.2057 0.1862 0.2151 -0.0083 -0.0467 0.0194 295 GLN A C 2233 O O . GLN A 295 ? 0.2047 0.1872 0.2126 -0.0076 -0.0442 0.0200 295 GLN A O 2234 C CB . GLN A 295 ? 0.2006 0.1780 0.2106 -0.0071 -0.0479 0.0140 295 GLN A CB 2235 C CG . GLN A 295 ? 0.1964 0.1765 0.2060 -0.0060 -0.0455 0.0137 295 GLN A CG 2236 C CD . GLN A 295 ? 0.1934 0.1757 0.2047 -0.0058 -0.0457 0.0175 295 GLN A CD 2237 O OE1 . GLN A 295 ? 0.1981 0.1802 0.2112 -0.0066 -0.0477 0.0205 295 GLN A OE1 2238 N NE2 . GLN A 295 ? 0.1821 0.1665 0.1926 -0.0049 -0.0435 0.0174 295 GLN A NE2 2239 N N . ASN A 296 ? 0.2079 0.1884 0.2194 -0.0095 -0.0491 0.0223 296 ASN A N 2240 C CA A ASN A 296 ? 0.2156 0.1994 0.2284 -0.0098 -0.0489 0.0265 296 ASN A CA 2241 C CA B ASN A 296 ? 0.2060 0.1897 0.2188 -0.0099 -0.0491 0.0266 296 ASN A CA 2242 C C . ASN A 296 ? 0.2150 0.1991 0.2305 -0.0103 -0.0510 0.0290 296 ASN A C 2243 O O . ASN A 296 ? 0.2263 0.2129 0.2434 -0.0113 -0.0519 0.0328 296 ASN A O 2244 C CB A ASN A 296 ? 0.2252 0.2100 0.2378 -0.0109 -0.0495 0.0284 296 ASN A CB 2245 C CB B ASN A 296 ? 0.2031 0.1871 0.2159 -0.0113 -0.0503 0.0282 296 ASN A CB 2246 C CG A ASN A 296 ? 0.2396 0.2230 0.2541 -0.0129 -0.0529 0.0299 296 ASN A CG 2247 C CG B ASN A 296 ? 0.1970 0.1852 0.2109 -0.0116 -0.0499 0.0325 296 ASN A CG 2248 O OD1 A ASN A 296 ? 0.2499 0.2297 0.2647 -0.0134 -0.0548 0.0281 296 ASN A OD1 2249 O OD1 B ASN A 296 ? 0.1907 0.1817 0.2038 -0.0101 -0.0474 0.0334 296 ASN A OD1 2250 N ND2 A ASN A 296 ? 0.2413 0.2276 0.2568 -0.0141 -0.0536 0.0333 296 ASN A ND2 2251 N ND2 B ASN A 296 ? 0.1938 0.1828 0.2096 -0.0134 -0.0523 0.0350 296 ASN A ND2 2252 N N . VAL A 297 ? 0.2124 0.1944 0.2283 -0.0096 -0.0517 0.0269 297 VAL A N 2253 C CA . VAL A 297 ? 0.2150 0.1965 0.2329 -0.0100 -0.0536 0.0290 297 VAL A CA 2254 C C . VAL A 297 ? 0.2140 0.1993 0.2326 -0.0090 -0.0519 0.0312 297 VAL A C 2255 O O . VAL A 297 ? 0.2139 0.2011 0.2341 -0.0099 -0.0528 0.0349 297 VAL A O 2256 C CB . VAL A 297 ? 0.2161 0.1938 0.2339 -0.0091 -0.0552 0.0258 297 VAL A CB 2257 C CG1 . VAL A 297 ? 0.2193 0.1963 0.2388 -0.0092 -0.0570 0.0279 297 VAL A CG1 2258 C CG2 . VAL A 297 ? 0.2220 0.1957 0.2390 -0.0101 -0.0572 0.0238 297 VAL A CG2 2259 N N . ASN A 298 ? 0.2128 0.1993 0.2300 -0.0074 -0.0493 0.0291 298 ASN A N 2260 C CA . ASN A 298 ? 0.2075 0.1971 0.2249 -0.0065 -0.0476 0.0310 298 ASN A CA 2261 C C . ASN A 298 ? 0.2034 0.1939 0.2184 -0.0051 -0.0445 0.0285 298 ASN A C 2262 O O . ASN A 298 ? 0.1958 0.1845 0.2096 -0.0047 -0.0441 0.0247 298 ASN A O 2263 C CB . ASN A 298 ? 0.2091 0.1980 0.2281 -0.0061 -0.0492 0.0314 298 ASN A CB 2264 C CG . ASN A 298 ? 0.2135 0.2058 0.2335 -0.0059 -0.0485 0.0349 298 ASN A CG 2265 O OD1 . ASN A 298 ? 0.2115 0.2064 0.2303 -0.0048 -0.0459 0.0349 298 ASN A OD1 2266 N ND2 . ASN A 298 ? 0.2135 0.2056 0.2354 -0.0070 -0.0509 0.0380 298 ASN A ND2 2267 N N . ARG A 299 ? 0.2058 0.1992 0.2198 -0.0045 -0.0424 0.0304 299 ARG A N 2268 C CA . ARG A 299 ? 0.2129 0.2067 0.2241 -0.0034 -0.0394 0.0282 299 ARG A CA 2269 C C . ARG A 299 ? 0.2047 0.1987 0.2160 -0.0026 -0.0390 0.0264 299 ARG A C 2270 O O . ARG A 299 ? 0.1905 0.1843 0.1995 -0.0021 -0.0370 0.0237 299 ARG A O 2271 C CB . ARG A 299 ? 0.2373 0.2336 0.2470 -0.0027 -0.0373 0.0308 299 ARG A CB 2272 C CG . ARG A 299 ? 0.2665 0.2658 0.2778 -0.0022 -0.0374 0.0341 299 ARG A CG 2273 C CD . ARG A 299 ? 0.3050 0.3067 0.3145 -0.0012 -0.0352 0.0365 299 ARG A CD 2274 N NE . ARG A 299 ? 0.3165 0.3193 0.3265 -0.0016 -0.0359 0.0385 299 ARG A NE 2275 C CZ . ARG A 299 ? 0.3446 0.3492 0.3527 -0.0004 -0.0341 0.0401 299 ARG A CZ 2276 N NH1 . ARG A 299 ? 0.3465 0.3516 0.3517 0.0012 -0.0315 0.0400 299 ARG A NH1 2277 N NH2 . ARG A 299 ? 0.3606 0.3665 0.3695 -0.0009 -0.0349 0.0419 299 ARG A NH2 2278 N N . ILE A 300 ? 0.1990 0.1935 0.2129 -0.0027 -0.0410 0.0280 300 ILE A N 2279 C CA . ILE A 300 ? 0.1997 0.1945 0.2139 -0.0018 -0.0411 0.0264 300 ILE A CA 2280 C C . ILE A 300 ? 0.2023 0.1946 0.2172 -0.0018 -0.0428 0.0232 300 ILE A C 2281 O O . ILE A 300 ? 0.1930 0.1833 0.2096 -0.0024 -0.0453 0.0239 300 ILE A O 2282 C CB . ILE A 300 ? 0.2013 0.1976 0.2177 -0.0017 -0.0425 0.0297 300 ILE A CB 2283 C CG1 . ILE A 300 ? 0.2013 0.2006 0.2170 -0.0015 -0.0407 0.0330 300 ILE A CG1 2284 C CG2 . ILE A 300 ? 0.1908 0.1875 0.2075 -0.0007 -0.0427 0.0279 300 ILE A CG2 2285 C CD1 . ILE A 300 ? 0.2066 0.2078 0.2245 -0.0019 -0.0422 0.0370 300 ILE A CD1 2286 N N . THR A 301 ? 0.2124 0.2051 0.2259 -0.0011 -0.0414 0.0196 301 THR A N 2287 C CA . THR A 301 ? 0.2138 0.2049 0.2278 -0.0007 -0.0427 0.0162 301 THR A CA 2288 C C . THR A 301 ? 0.2147 0.2077 0.2284 0.0002 -0.0418 0.0135 301 THR A C 2289 O O . THR A 301 ? 0.2152 0.2106 0.2276 0.0003 -0.0396 0.0136 301 THR A O 2290 C CB . THR A 301 ? 0.2263 0.2158 0.2386 -0.0014 -0.0419 0.0135 301 THR A CB 2291 O OG1 . THR A 301 ? 0.2415 0.2325 0.2512 -0.0015 -0.0390 0.0113 301 THR A OG1 2292 C CG2 . THR A 301 ? 0.2292 0.2173 0.2412 -0.0025 -0.0423 0.0160 301 THR A CG2 2293 N N . TYR A 302 ? 0.2088 0.2010 0.2236 0.0011 -0.0435 0.0111 302 TYR A N 2294 C CA . TYR A 302 ? 0.2072 0.2019 0.2220 0.0022 -0.0428 0.0081 302 TYR A CA 2295 C C . TYR A 302 ? 0.2053 0.1991 0.2201 0.0028 -0.0437 0.0044 302 TYR A C 2296 O O . TYR A 302 ? 0.2172 0.2080 0.2331 0.0033 -0.0461 0.0047 302 TYR A O 2297 C CB . TYR A 302 ? 0.2097 0.2054 0.2263 0.0035 -0.0444 0.0097 302 TYR A CB 2298 C CG . TYR A 302 ? 0.2147 0.2136 0.2314 0.0048 -0.0438 0.0067 302 TYR A CG 2299 C CD1 . TYR A 302 ? 0.2225 0.2212 0.2402 0.0063 -0.0455 0.0039 302 TYR A CD1 2300 C CD2 . TYR A 302 ? 0.2178 0.2201 0.2333 0.0045 -0.0416 0.0065 302 TYR A CD2 2301 C CE1 . TYR A 302 ? 0.2250 0.2275 0.2428 0.0075 -0.0449 0.0011 302 TYR A CE1 2302 C CE2 . TYR A 302 ? 0.2214 0.2272 0.2369 0.0054 -0.0411 0.0037 302 TYR A CE2 2303 C CZ . TYR A 302 ? 0.2179 0.2241 0.2348 0.0069 -0.0428 0.0011 302 TYR A CZ 2304 O OH . TYR A 302 ? 0.2205 0.2308 0.2376 0.0078 -0.0423 -0.0016 302 TYR A OH 2305 N N . GLY A 303 ? 0.2049 0.2011 0.2183 0.0027 -0.0417 0.0010 303 GLY A N 2306 C CA . GLY A 303 ? 0.2139 0.2102 0.2274 0.0035 -0.0423 -0.0027 303 GLY A CA 2307 C C . GLY A 303 ? 0.2250 0.2200 0.2365 0.0020 -0.0409 -0.0042 303 GLY A C 2308 O O . GLY A 303 ? 0.2297 0.2243 0.2393 0.0005 -0.0390 -0.0028 303 GLY A O 2309 N N . ALA A 304 ? 0.2357 0.2299 0.2472 0.0026 -0.0418 -0.0072 304 ALA A N 2310 C CA . ALA A 304 ? 0.2374 0.2303 0.2469 0.0013 -0.0407 -0.0089 304 ALA A CA 2311 C C . ALA A 304 ? 0.2412 0.2299 0.2507 0.0006 -0.0421 -0.0062 304 ALA A C 2312 O O . ALA A 304 ? 0.2479 0.2339 0.2586 0.0014 -0.0446 -0.0063 304 ALA A O 2313 C CB . ALA A 304 ? 0.2451 0.2392 0.2547 0.0023 -0.0411 -0.0130 304 ALA A CB 2314 N N . CYS A 305 ? 0.2340 0.2221 0.2422 -0.0008 -0.0407 -0.0038 305 CYS A N 2315 C CA . CYS A 305 ? 0.2354 0.2206 0.2440 -0.0015 -0.0420 -0.0005 305 CYS A CA 2316 C C . CYS A 305 ? 0.2237 0.2077 0.2299 -0.0030 -0.0406 -0.0004 305 CYS A C 2317 O O . CYS A 305 ? 0.2240 0.2093 0.2278 -0.0036 -0.0380 -0.0015 305 CYS A O 2318 C CB . CYS A 305 ? 0.2446 0.2307 0.2542 -0.0015 -0.0420 0.0033 305 CYS A CB 2319 S SG . CYS A 305 ? 0.2606 0.2469 0.2732 0.0000 -0.0445 0.0046 305 CYS A SG 2320 N N . PRO A 306 ? 0.2144 0.1957 0.2209 -0.0035 -0.0423 0.0007 306 PRO A N 2321 C CA . PRO A 306 ? 0.2105 0.1908 0.2148 -0.0048 -0.0411 0.0016 306 PRO A CA 2322 C C . PRO A 306 ? 0.2028 0.1846 0.2064 -0.0050 -0.0394 0.0048 306 PRO A C 2323 O O . PRO A 306 ? 0.1934 0.1765 0.1988 -0.0045 -0.0399 0.0071 306 PRO A O 2324 C CB . PRO A 306 ? 0.2150 0.1926 0.2205 -0.0053 -0.0438 0.0031 306 PRO A CB 2325 C CG . PRO A 306 ? 0.2196 0.1960 0.2272 -0.0043 -0.0463 0.0018 306 PRO A CG 2326 C CD . PRO A 306 ? 0.2163 0.1952 0.2250 -0.0031 -0.0455 0.0018 306 PRO A CD 2327 N N . ARG A 307 ? 0.2055 0.1870 0.2062 -0.0057 -0.0373 0.0048 307 ARG A N 2328 C CA . ARG A 307 ? 0.2006 0.1832 0.2001 -0.0056 -0.0356 0.0075 307 ARG A CA 2329 C C . ARG A 307 ? 0.1936 0.1761 0.1948 -0.0057 -0.0372 0.0114 307 ARG A C 2330 O O . ARG A 307 ? 0.1857 0.1667 0.1871 -0.0064 -0.0387 0.0117 307 ARG A O 2331 C CB . ARG A 307 ? 0.2045 0.1861 0.1996 -0.0061 -0.0329 0.0061 307 ARG A CB 2332 C CG . ARG A 307 ? 0.2135 0.1958 0.2066 -0.0064 -0.0309 0.0028 307 ARG A CG 2333 C CD . ARG A 307 ? 0.2119 0.1929 0.2002 -0.0071 -0.0281 0.0021 307 ARG A CD 2334 N NE . ARG A 307 ? 0.2191 0.2010 0.2054 -0.0078 -0.0263 -0.0007 307 ARG A NE 2335 C CZ . ARG A 307 ? 0.2227 0.2060 0.2085 -0.0076 -0.0250 -0.0004 307 ARG A CZ 2336 N NH1 . ARG A 307 ? 0.2205 0.2045 0.2077 -0.0065 -0.0254 0.0026 307 ARG A NH1 2337 N NH2 . ARG A 307 ? 0.2416 0.2259 0.2253 -0.0086 -0.0234 -0.0033 307 ARG A NH2 2338 N N . TYR A 308 ? 0.1853 0.1697 0.1874 -0.0051 -0.0368 0.0145 308 TYR A N 2339 C CA . TYR A 308 ? 0.1857 0.1711 0.1895 -0.0053 -0.0381 0.0184 308 TYR A CA 2340 C C . TYR A 308 ? 0.1871 0.1723 0.1884 -0.0053 -0.0368 0.0196 308 TYR A C 2341 O O . TYR A 308 ? 0.1909 0.1761 0.1890 -0.0047 -0.0342 0.0191 308 TYR A O 2342 C CB . TYR A 308 ? 0.1864 0.1743 0.1918 -0.0046 -0.0379 0.0213 308 TYR A CB 2343 C CG . TYR A 308 ? 0.1914 0.1811 0.1989 -0.0049 -0.0393 0.0255 308 TYR A CG 2344 C CD1 . TYR A 308 ? 0.1984 0.1877 0.2089 -0.0059 -0.0422 0.0268 308 TYR A CD1 2345 C CD2 . TYR A 308 ? 0.1999 0.1915 0.2060 -0.0043 -0.0377 0.0279 308 TYR A CD2 2346 C CE1 . TYR A 308 ? 0.2049 0.1962 0.2174 -0.0067 -0.0436 0.0307 308 TYR A CE1 2347 C CE2 . TYR A 308 ? 0.2059 0.2001 0.2142 -0.0047 -0.0390 0.0318 308 TYR A CE2 2348 C CZ . TYR A 308 ? 0.2088 0.2030 0.2204 -0.0061 -0.0419 0.0331 308 TYR A CZ 2349 O OH . TYR A 308 ? 0.2214 0.2184 0.2350 -0.0069 -0.0432 0.0369 308 TYR A OH 2350 N N . VAL A 309 ? 0.1856 0.1707 0.1881 -0.0061 -0.0386 0.0213 309 VAL A N 2351 C CA . VAL A 309 ? 0.1855 0.1711 0.1861 -0.0060 -0.0378 0.0228 309 VAL A CA 2352 C C . VAL A 309 ? 0.2005 0.1887 0.2040 -0.0064 -0.0396 0.0268 309 VAL A C 2353 O O . VAL A 309 ? 0.1930 0.1816 0.1997 -0.0073 -0.0419 0.0279 309 VAL A O 2354 C CB . VAL A 309 ? 0.1800 0.1628 0.1785 -0.0067 -0.0379 0.0202 309 VAL A CB 2355 C CG1 . VAL A 309 ? 0.1798 0.1606 0.1751 -0.0065 -0.0358 0.0163 309 VAL A CG1 2356 C CG2 . VAL A 309 ? 0.1771 0.1587 0.1781 -0.0080 -0.0409 0.0195 309 VAL A CG2 2357 N N . LYS A 310 ? 0.2179 0.2078 0.2200 -0.0058 -0.0387 0.0290 310 LYS A N 2358 C CA . LYS A 310 ? 0.2366 0.2300 0.2415 -0.0063 -0.0403 0.0329 310 LYS A CA 2359 C C . LYS A 310 ? 0.2393 0.2318 0.2455 -0.0081 -0.0430 0.0330 310 LYS A C 2360 O O . LYS A 310 ? 0.2234 0.2184 0.2326 -0.0093 -0.0451 0.0358 310 LYS A O 2361 C CB . LYS A 310 ? 0.2671 0.2631 0.2699 -0.0045 -0.0383 0.0352 310 LYS A CB 2362 C CG . LYS A 310 ? 0.3028 0.3001 0.3048 -0.0029 -0.0362 0.0360 310 LYS A CG 2363 C CD . LYS A 310 ? 0.3488 0.3489 0.3488 -0.0008 -0.0343 0.0385 310 LYS A CD 2364 C CE . LYS A 310 ? 0.3844 0.3820 0.3803 0.0000 -0.0330 0.0372 310 LYS A CE 2365 N NZ . LYS A 310 ? 0.4434 0.4427 0.4364 0.0026 -0.0308 0.0392 310 LYS A NZ 2366 N N . GLN A 311 ? 0.2218 0.2111 0.2258 -0.0085 -0.0429 0.0299 311 GLN A N 2367 C CA . GLN A 311 ? 0.2310 0.2192 0.2357 -0.0102 -0.0453 0.0297 311 GLN A CA 2368 C C . GLN A 311 ? 0.2492 0.2357 0.2566 -0.0117 -0.0481 0.0291 311 GLN A C 2369 O O . GLN A 311 ? 0.2350 0.2195 0.2427 -0.0113 -0.0478 0.0270 311 GLN A O 2370 C CB . GLN A 311 ? 0.2272 0.2120 0.2284 -0.0101 -0.0444 0.0262 311 GLN A CB 2371 C CG . GLN A 311 ? 0.2217 0.2071 0.2193 -0.0086 -0.0419 0.0265 311 GLN A CG 2372 C CD . GLN A 311 ? 0.2200 0.2038 0.2147 -0.0072 -0.0389 0.0245 311 GLN A CD 2373 O OE1 . GLN A 311 ? 0.2040 0.1883 0.1999 -0.0068 -0.0384 0.0245 311 GLN A OE1 2374 N NE2 . GLN A 311 ? 0.2104 0.1920 0.2009 -0.0067 -0.0371 0.0229 311 GLN A NE2 2375 N N . ASN A 312 ? 0.2621 0.2492 0.2715 -0.0135 -0.0507 0.0310 312 ASN A N 2376 C CA . ASN A 312 ? 0.2915 0.2757 0.3027 -0.0151 -0.0535 0.0303 312 ASN A CA 2377 C C . ASN A 312 ? 0.2768 0.2566 0.2864 -0.0159 -0.0548 0.0268 312 ASN A C 2378 O O . ASN A 312 ? 0.2811 0.2576 0.2914 -0.0167 -0.0569 0.0254 312 ASN A O 2379 C CB . ASN A 312 ? 0.3303 0.3169 0.3443 -0.0170 -0.0559 0.0342 312 ASN A CB 2380 C CG . ASN A 312 ? 0.3688 0.3583 0.3829 -0.0182 -0.0567 0.0364 312 ASN A CG 2381 O OD1 . ASN A 312 ? 0.4113 0.3990 0.4235 -0.0184 -0.0569 0.0345 312 ASN A OD1 2382 N ND2 . ASN A 312 ? 0.4504 0.4449 0.4667 -0.0188 -0.0571 0.0405 312 ASN A ND2 2383 N N . THR A 313 ? 0.2506 0.2302 0.2576 -0.0155 -0.0535 0.0253 313 THR A N 2384 C CA . THR A 313 ? 0.2505 0.2262 0.2555 -0.0160 -0.0543 0.0217 313 THR A CA 2385 C C . THR A 313 ? 0.2431 0.2188 0.2448 -0.0148 -0.0516 0.0198 313 THR A C 2386 O O . THR A 313 ? 0.2412 0.2196 0.2419 -0.0142 -0.0501 0.0218 313 THR A O 2387 C CB . THR A 313 ? 0.2637 0.2385 0.2693 -0.0182 -0.0573 0.0228 313 THR A CB 2388 O OG1 . THR A 313 ? 0.2677 0.2388 0.2710 -0.0185 -0.0578 0.0192 313 THR A OG1 2389 C CG2 . THR A 313 ? 0.2637 0.2426 0.2694 -0.0187 -0.0571 0.0261 313 THR A CG2 2390 N N . LEU A 314 ? 0.2405 0.2131 0.2401 -0.0144 -0.0509 0.0158 314 LEU A N 2391 C CA . LEU A 314 ? 0.2410 0.2129 0.2372 -0.0139 -0.0488 0.0136 314 LEU A CA 2392 C C . LEU A 314 ? 0.2466 0.2151 0.2414 -0.0145 -0.0499 0.0099 314 LEU A C 2393 O O . LEU A 314 ? 0.2417 0.2087 0.2368 -0.0140 -0.0498 0.0072 314 LEU A O 2394 C CB . LEU A 314 ? 0.2375 0.2099 0.2319 -0.0124 -0.0456 0.0124 314 LEU A CB 2395 C CG . LEU A 314 ? 0.2374 0.2126 0.2317 -0.0113 -0.0438 0.0154 314 LEU A CG 2396 C CD1 . LEU A 314 ? 0.2341 0.2091 0.2269 -0.0102 -0.0411 0.0137 314 LEU A CD1 2397 C CD2 . LEU A 314 ? 0.2403 0.2161 0.2319 -0.0111 -0.0429 0.0168 314 LEU A CD2 2398 N N . LYS A 315 ? 0.2425 0.2100 0.2358 -0.0155 -0.0509 0.0097 315 LYS A N 2399 C CA . LYS A 315 ? 0.2595 0.2238 0.2515 -0.0162 -0.0523 0.0063 315 LYS A CA 2400 C C . LYS A 315 ? 0.2453 0.2085 0.2335 -0.0157 -0.0499 0.0031 315 LYS A C 2401 O O . LYS A 315 ? 0.2361 0.2002 0.2221 -0.0157 -0.0486 0.0041 315 LYS A O 2402 C CB . LYS A 315 ? 0.2891 0.2526 0.2814 -0.0179 -0.0551 0.0078 315 LYS A CB 2403 C CG . LYS A 315 ? 0.3273 0.2914 0.3230 -0.0189 -0.0577 0.0107 315 LYS A CG 2404 C CD . LYS A 315 ? 0.3590 0.3198 0.3558 -0.0189 -0.0594 0.0086 315 LYS A CD 2405 C CE . LYS A 315 ? 0.4099 0.3668 0.4054 -0.0202 -0.0620 0.0066 315 LYS A CE 2406 N NZ . LYS A 315 ? 0.4635 0.4166 0.4587 -0.0192 -0.0628 0.0032 315 LYS A NZ 2407 N N . LEU A 316 ? 0.2369 0.1985 0.2245 -0.0152 -0.0494 -0.0005 316 LEU A N 2408 C CA . LEU A 316 ? 0.2375 0.1984 0.2216 -0.0150 -0.0473 -0.0038 316 LEU A CA 2409 C C . LEU A 316 ? 0.2369 0.1953 0.2196 -0.0158 -0.0491 -0.0060 316 LEU A C 2410 O O . LEU A 316 ? 0.2359 0.1926 0.2201 -0.0158 -0.0512 -0.0074 316 LEU A O 2411 C CB . LEU A 316 ? 0.2377 0.1990 0.2222 -0.0140 -0.0458 -0.0067 316 LEU A CB 2412 C CG . LEU A 316 ? 0.2417 0.2029 0.2227 -0.0141 -0.0434 -0.0102 316 LEU A CG 2413 C CD1 . LEU A 316 ? 0.2392 0.2015 0.2177 -0.0141 -0.0404 -0.0089 316 LEU A CD1 2414 C CD2 . LEU A 316 ? 0.2450 0.2069 0.2270 -0.0132 -0.0430 -0.0136 316 LEU A CD2 2415 N N . ALA A 317 ? 0.2418 0.1999 0.2215 -0.0165 -0.0483 -0.0061 317 ALA A N 2416 C CA . ALA A 317 ? 0.2485 0.2043 0.2261 -0.0173 -0.0496 -0.0085 317 ALA A CA 2417 C C . ALA A 317 ? 0.2567 0.2114 0.2334 -0.0166 -0.0489 -0.0130 317 ALA A C 2418 O O . ALA A 317 ? 0.2529 0.2090 0.2284 -0.0160 -0.0463 -0.0147 317 ALA A O 2419 C CB . ALA A 317 ? 0.2502 0.2061 0.2241 -0.0179 -0.0483 -0.0080 317 ALA A CB 2420 N N . THR A 318 ? 0.2582 0.2107 0.2353 -0.0168 -0.0514 -0.0149 318 THR A N 2421 C CA . THR A 318 ? 0.2680 0.2196 0.2440 -0.0159 -0.0510 -0.0192 318 THR A CA 2422 C C . THR A 318 ? 0.2835 0.2327 0.2566 -0.0167 -0.0522 -0.0214 318 THR A C 2423 O O . THR A 318 ? 0.3065 0.2542 0.2789 -0.0160 -0.0529 -0.0249 318 THR A O 2424 C CB . THR A 318 ? 0.2654 0.2159 0.2443 -0.0147 -0.0528 -0.0201 318 THR A CB 2425 O OG1 . THR A 318 ? 0.2721 0.2198 0.2523 -0.0155 -0.0561 -0.0183 318 THR A OG1 2426 C CG2 . THR A 318 ? 0.2666 0.2198 0.2482 -0.0138 -0.0514 -0.0183 318 THR A CG2 2427 N N . GLY A 319 ? 0.2822 0.2312 0.2535 -0.0180 -0.0523 -0.0195 319 GLY A N 2428 C CA . GLY A 319 ? 0.2871 0.2341 0.2554 -0.0189 -0.0533 -0.0212 319 GLY A CA 2429 C C . GLY A 319 ? 0.2836 0.2315 0.2495 -0.0199 -0.0523 -0.0190 319 GLY A C 2430 O O . GLY A 319 ? 0.2734 0.2233 0.2401 -0.0198 -0.0510 -0.0160 319 GLY A O 2431 N N . MET A 320 ? 0.2805 0.2270 0.2432 -0.0208 -0.0528 -0.0205 320 MET A N 2432 C CA . MET A 320 ? 0.2801 0.2272 0.2399 -0.0216 -0.0519 -0.0187 320 MET A CA 2433 C C . MET A 320 ? 0.2891 0.2366 0.2506 -0.0225 -0.0543 -0.0148 320 MET A C 2434 O O . MET A 320 ? 0.2946 0.2415 0.2592 -0.0229 -0.0568 -0.0136 320 MET A O 2435 C CB . MET A 320 ? 0.2853 0.2307 0.2410 -0.0223 -0.0517 -0.0218 320 MET A CB 2436 C CG . MET A 320 ? 0.2891 0.2321 0.2449 -0.0230 -0.0551 -0.0229 320 MET A CG 2437 S SD . MET A 320 ? 0.3024 0.2437 0.2531 -0.0236 -0.0546 -0.0266 320 MET A SD 2438 C CE . MET A 320 ? 0.2929 0.2344 0.2435 -0.0222 -0.0528 -0.0313 320 MET A CE 2439 N N . ARG A 321 ? 0.2921 0.2406 0.2513 -0.0229 -0.0536 -0.0127 321 ARG A N 2440 C CA . ARG A 321 ? 0.3151 0.2647 0.2754 -0.0238 -0.0559 -0.0092 321 ARG A CA 2441 C C . ARG A 321 ? 0.3207 0.2681 0.2813 -0.0252 -0.0593 -0.0105 321 ARG A C 2442 O O . ARG A 321 ? 0.3006 0.2456 0.2585 -0.0255 -0.0595 -0.0139 321 ARG A O 2443 C CB . ARG A 321 ? 0.3295 0.2801 0.2864 -0.0238 -0.0547 -0.0076 321 ARG A CB 2444 C CG . ARG A 321 ? 0.3648 0.3132 0.3171 -0.0244 -0.0542 -0.0106 321 ARG A CG 2445 C CD . ARG A 321 ? 0.3981 0.3473 0.3467 -0.0243 -0.0532 -0.0088 321 ARG A CD 2446 N NE . ARG A 321 ? 0.3990 0.3485 0.3456 -0.0231 -0.0498 -0.0082 321 ARG A NE 2447 C CZ . ARG A 321 ? 0.4015 0.3528 0.3486 -0.0220 -0.0489 -0.0047 321 ARG A CZ 2448 N NH1 . ARG A 321 ? 0.4199 0.3737 0.3698 -0.0219 -0.0510 -0.0013 321 ARG A NH1 2449 N NH2 . ARG A 321 ? 0.4281 0.3786 0.3724 -0.0210 -0.0458 -0.0047 321 ARG A NH2 2450 N N . ASN A 322 ? 0.3182 0.2664 0.2820 -0.0262 -0.0619 -0.0077 322 ASN A N 2451 C CA . ASN A 322 ? 0.3447 0.2906 0.3087 -0.0279 -0.0654 -0.0083 322 ASN A CA 2452 C C . ASN A 322 ? 0.3547 0.3022 0.3173 -0.0294 -0.0670 -0.0060 322 ASN A C 2453 O O . ASN A 322 ? 0.3476 0.2987 0.3121 -0.0296 -0.0671 -0.0022 322 ASN A O 2454 C CB . ASN A 322 ? 0.3495 0.2950 0.3175 -0.0285 -0.0676 -0.0067 322 ASN A CB 2455 C CG . ASN A 322 ? 0.3537 0.2950 0.3212 -0.0300 -0.0710 -0.0086 322 ASN A CG 2456 O OD1 . ASN A 322 ? 0.3490 0.2870 0.3137 -0.0296 -0.0709 -0.0125 322 ASN A OD1 2457 N ND2 . ASN A 322 ? 0.3586 0.3000 0.3285 -0.0318 -0.0739 -0.0058 322 ASN A ND2 2458 N N . VAL A 323 ? 0.3681 0.3133 0.3273 -0.0302 -0.0679 -0.0085 323 VAL A N 2459 C CA . VAL A 323 ? 0.3829 0.3297 0.3400 -0.0314 -0.0690 -0.0068 323 VAL A CA 2460 C C . VAL A 323 ? 0.4135 0.3576 0.3699 -0.0336 -0.0726 -0.0080 323 VAL A C 2461 O O . VAL A 323 ? 0.4019 0.3420 0.3560 -0.0336 -0.0730 -0.0118 323 VAL A O 2462 C CB . VAL A 323 ? 0.3914 0.3381 0.3441 -0.0303 -0.0663 -0.0086 323 VAL A CB 2463 C CG1 . VAL A 323 ? 0.3925 0.3411 0.3429 -0.0312 -0.0673 -0.0065 323 VAL A CG1 2464 C CG2 . VAL A 323 ? 0.3831 0.3314 0.3359 -0.0283 -0.0627 -0.0078 323 VAL A CG2 2465 N N . PRO A 324 ? 0.4610 0.4073 0.4191 -0.0355 -0.0753 -0.0047 324 PRO A N 2466 C CA . PRO A 324 ? 0.4834 0.4268 0.4404 -0.0380 -0.0790 -0.0057 324 PRO A CA 2467 C C . PRO A 324 ? 0.4954 0.4364 0.4476 -0.0382 -0.0790 -0.0089 324 PRO A C 2468 O O . PRO A 324 ? 0.5042 0.4472 0.4540 -0.0370 -0.0767 -0.0088 324 PRO A O 2469 C CB . PRO A 324 ? 0.4881 0.4360 0.4474 -0.0400 -0.0812 -0.0012 324 PRO A CB 2470 C CG . PRO A 324 ? 0.4872 0.4402 0.4473 -0.0381 -0.0785 0.0014 324 PRO A CG 2471 C CD . PRO A 324 ? 0.4698 0.4216 0.4301 -0.0354 -0.0750 -0.0001 324 PRO A CD 2472 N N . GLU A 325 ? 0.5340 0.4705 0.4844 -0.0396 -0.0815 -0.0116 325 GLU A N 2473 C CA . GLU A 325 ? 0.5730 0.5072 0.5187 -0.0402 -0.0820 -0.0144 325 GLU A CA 2474 C C . GLU A 325 ? 0.6380 0.5751 0.5830 -0.0424 -0.0843 -0.0117 325 GLU A C 2475 O O . GLU A 325 ? 0.6291 0.5666 0.5762 -0.0447 -0.0873 -0.0094 325 GLU A O 2476 C CB . GLU A 325 ? 0.5699 0.4980 0.5137 -0.0407 -0.0839 -0.0184 325 GLU A CB 2477 C CG . GLU A 325 ? 0.5664 0.4920 0.5051 -0.0407 -0.0838 -0.0220 325 GLU A CG 2478 C CD . GLU A 325 ? 0.5574 0.4778 0.4939 -0.0393 -0.0835 -0.0269 325 GLU A CD 2479 O OE1 . GLU A 325 ? 0.5366 0.4545 0.4754 -0.0387 -0.0842 -0.0275 325 GLU A OE1 2480 O OE2 . GLU A 325 ? 0.5383 0.4574 0.4707 -0.0387 -0.0825 -0.0301 325 GLU A OE2 2481 N N . LYS A 326 ? 0.6756 0.6650 0.6492 -0.0709 -0.0687 0.0076 326 LYS A N 2482 C CA . LYS A 326 ? 0.7601 0.7616 0.7351 -0.0744 -0.0698 0.0098 326 LYS A CA 2483 C C . LYS A 326 ? 0.8161 0.8094 0.7825 -0.0815 -0.0730 0.0100 326 LYS A C 2484 O O . LYS A 326 ? 0.7862 0.7647 0.7469 -0.0802 -0.0736 0.0078 326 LYS A O 2485 C CB . LYS A 326 ? 0.7577 0.7663 0.7381 -0.0676 -0.0679 0.0094 326 LYS A CB 2486 C CG . LYS A 326 ? 0.7988 0.7960 0.7761 -0.0649 -0.0676 0.0070 326 LYS A CG 2487 C CD . LYS A 326 ? 0.7994 0.8016 0.7795 -0.0588 -0.0657 0.0067 326 LYS A CD 2488 C CE . LYS A 326 ? 0.7974 0.7883 0.7739 -0.0570 -0.0650 0.0041 326 LYS A CE 2489 N NZ . LYS A 326 ? 0.7789 0.7634 0.7503 -0.0622 -0.0678 0.0038 326 LYS A NZ 2490 N N . GLN A 327 ? 0.8962 0.8997 0.8610 -0.0891 -0.0749 0.0125 327 GLN A N 2491 C CA . GLN A 327 ? 0.9812 0.9761 0.9354 -0.0983 -0.0781 0.0131 327 GLN A CA 2492 C C . GLN A 327 ? 1.0031 0.9950 0.9555 -0.0975 -0.0791 0.0123 327 GLN A C 2493 O O . GLN A 327 ? 0.9873 0.9913 0.9471 -0.0928 -0.0779 0.0124 327 GLN A O 2494 C CB . GLN A 327 ? 1.0104 1.0198 0.9633 -0.1082 -0.0796 0.0159 327 GLN A CB 2495 C CG . GLN A 327 ? 1.0492 1.0450 0.9876 -0.1197 -0.0826 0.0167 327 GLN A CG 2496 C CD . GLN A 327 ? 1.0554 1.0682 0.9922 -0.1313 -0.0839 0.0193 327 GLN A CD 2497 O OE1 . GLN A 327 ? 1.0780 1.0873 1.0076 -0.1392 -0.0846 0.0205 327 GLN A OE1 2498 N NE2 . GLN A 327 ? 1.0313 1.0636 0.9744 -0.1324 -0.0842 0.0202 327 GLN A NE2 2499 N N . THR A 328 ? 1.0759 1.0506 1.0171 -0.1018 -0.0814 0.0114 328 THR A N 2500 C CA . THR A 328 ? 1.0952 1.0644 1.0333 -0.1012 -0.0825 0.0103 328 THR A CA 2501 C C . THR A 328 ? 1.1012 1.0593 1.0254 -0.1113 -0.0861 0.0112 328 THR A C 2502 O O . THR A 328 ? 1.0761 1.0455 0.9995 -0.1191 -0.0876 0.0133 328 THR A O 2503 C CB . THR A 328 ? 1.1063 1.0620 1.0442 -0.0923 -0.0810 0.0070 328 THR A CB 2504 O OG1 . THR A 328 ? 1.0947 1.0481 1.0314 -0.0912 -0.0815 0.0061 328 THR A OG1 2505 C CG2 . THR A 328 ? 1.1018 1.0378 1.0284 -0.0928 -0.0825 0.0053 328 THR A CG2 2506 N N . ALA A 334 ? 0.6580 0.5987 0.5970 -0.0755 -0.0776 -0.0010 334 ALA A N 2507 C CA . ALA A 334 ? 0.6173 0.5587 0.5612 -0.0688 -0.0742 -0.0035 334 ALA A CA 2508 C C . ALA A 334 ? 0.6002 0.5421 0.5475 -0.0656 -0.0723 -0.0047 334 ALA A C 2509 O O . ALA A 334 ? 0.6102 0.5595 0.5618 -0.0666 -0.0721 -0.0025 334 ALA A O 2510 C CB . ALA A 334 ? 0.6337 0.5852 0.5830 -0.0668 -0.0725 -0.0021 334 ALA A CB 2511 N N . ILE A 335 ? 0.5295 0.4647 0.4750 -0.0617 -0.0710 -0.0084 335 ILE A N 2512 C CA . ILE A 335 ? 0.4654 0.4027 0.4148 -0.0581 -0.0689 -0.0100 335 ILE A CA 2513 C C . ILE A 335 ? 0.4306 0.3775 0.3875 -0.0564 -0.0657 -0.0089 335 ILE A C 2514 O O . ILE A 335 ? 0.4117 0.3616 0.3695 -0.0564 -0.0648 -0.0079 335 ILE A O 2515 C CB . ILE A 335 ? 0.4548 0.3869 0.4014 -0.0538 -0.0678 -0.0146 335 ILE A CB 2516 C CG1 . ILE A 335 ? 0.4511 0.3845 0.3981 -0.0526 -0.0656 -0.0169 335 ILE A CG1 2517 C CG2 . ILE A 335 ? 0.4743 0.3951 0.4112 -0.0538 -0.0713 -0.0157 335 ILE A CG2 2518 C CD1 . ILE A 335 ? 0.4207 0.3550 0.3674 -0.0486 -0.0635 -0.0218 335 ILE A CD1 2519 N N . ALA A 336 ? 0.3986 0.3490 0.3595 -0.0545 -0.0642 -0.0090 336 ALA A N 2520 C CA . ALA A 336 ? 0.3890 0.3466 0.3551 -0.0526 -0.0615 -0.0078 336 ALA A CA 2521 C C . ALA A 336 ? 0.3684 0.3266 0.3371 -0.0500 -0.0592 -0.0099 336 ALA A C 2522 O O . ALA A 336 ? 0.3660 0.3213 0.3335 -0.0495 -0.0603 -0.0113 336 ALA A O 2523 C CB . ALA A 336 ? 0.3971 0.3621 0.3658 -0.0545 -0.0630 -0.0037 336 ALA A CB 2524 N N . GLY A 337 ? 0.3534 0.3145 0.3241 -0.0480 -0.0560 -0.0104 337 GLY A N 2525 C CA . GLY A 337 ? 0.3489 0.3111 0.3215 -0.0462 -0.0535 -0.0129 337 GLY A CA 2526 C C . GLY A 337 ? 0.3407 0.3074 0.3172 -0.0451 -0.0529 -0.0104 337 GLY A C 2527 O O . GLY A 337 ? 0.3360 0.3058 0.3140 -0.0460 -0.0550 -0.0072 337 GLY A O 2528 N N . PHE A 338 ? 0.3382 0.3060 0.3157 -0.0437 -0.0501 -0.0122 338 PHE A N 2529 C CA . PHE A 338 ? 0.3501 0.3216 0.3311 -0.0424 -0.0495 -0.0105 338 PHE A CA 2530 C C . PHE A 338 ? 0.3595 0.3341 0.3410 -0.0409 -0.0492 -0.0070 338 PHE A C 2531 O O . PHE A 338 ? 0.3695 0.3482 0.3540 -0.0398 -0.0491 -0.0053 338 PHE A O 2532 C CB . PHE A 338 ? 0.3339 0.3058 0.3154 -0.0415 -0.0466 -0.0137 338 PHE A CB 2533 C CG . PHE A 338 ? 0.3423 0.3114 0.3194 -0.0420 -0.0434 -0.0148 338 PHE A CG 2534 C CD1 . PHE A 338 ? 0.3432 0.3098 0.3164 -0.0441 -0.0422 -0.0179 338 PHE A CD1 2535 C CD2 . PHE A 338 ? 0.3605 0.3286 0.3359 -0.0407 -0.0416 -0.0130 338 PHE A CD2 2536 C CE1 . PHE A 338 ? 0.3596 0.3218 0.3264 -0.0459 -0.0392 -0.0190 338 PHE A CE1 2537 C CE2 . PHE A 338 ? 0.3664 0.3285 0.3344 -0.0416 -0.0388 -0.0140 338 PHE A CE2 2538 C CZ . PHE A 338 ? 0.3673 0.3259 0.3305 -0.0447 -0.0376 -0.0170 338 PHE A CZ 2539 N N . ILE A 339 ? 0.3814 0.3545 0.3593 -0.0403 -0.0490 -0.0060 339 ILE A N 2540 C CA . ILE A 339 ? 0.4103 0.3868 0.3872 -0.0371 -0.0489 -0.0030 339 ILE A CA 2541 C C . ILE A 339 ? 0.4348 0.4209 0.4169 -0.0377 -0.0516 0.0000 339 ILE A C 2542 O O . ILE A 339 ? 0.4394 0.4280 0.4219 -0.0404 -0.0541 0.0010 339 ILE A O 2543 C CB . ILE A 339 ? 0.4184 0.3905 0.3888 -0.0354 -0.0487 -0.0027 339 ILE A CB 2544 C CG1 . ILE A 339 ? 0.4173 0.3793 0.3809 -0.0364 -0.0457 -0.0057 339 ILE A CG1 2545 C CG2 . ILE A 339 ? 0.4281 0.4044 0.3963 -0.0303 -0.0490 0.0001 339 ILE A CG2 2546 C CD1 . ILE A 339 ? 0.4241 0.3822 0.3839 -0.0348 -0.0428 -0.0063 339 ILE A CD1 2547 N N . GLU A 340 ? 0.4840 0.4752 0.4693 -0.0362 -0.0511 0.0013 340 GLU A N 2548 C CA . GLU A 340 ? 0.5217 0.5232 0.5114 -0.0378 -0.0532 0.0040 340 GLU A CA 2549 C C . GLU A 340 ? 0.4824 0.4829 0.4729 -0.0437 -0.0558 0.0040 340 GLU A C 2550 O O . GLU A 340 ? 0.4869 0.4944 0.4780 -0.0470 -0.0581 0.0061 340 GLU A O 2551 C CB . GLU A 340 ? 0.5676 0.5788 0.5569 -0.0352 -0.0544 0.0065 340 GLU A CB 2552 C CG . GLU A 340 ? 0.6276 0.6377 0.6129 -0.0280 -0.0524 0.0067 340 GLU A CG 2553 C CD . GLU A 340 ? 0.6871 0.6989 0.6740 -0.0251 -0.0506 0.0070 340 GLU A CD 2554 O OE1 . GLU A 340 ? 0.7481 0.7669 0.7406 -0.0281 -0.0513 0.0079 340 GLU A OE1 2555 O OE2 . GLU A 340 ? 0.7564 0.7615 0.7376 -0.0200 -0.0485 0.0064 340 GLU A OE2 2556 N N . ASN A 341 ? 0.4660 0.4579 0.4553 -0.0449 -0.0555 0.0014 341 ASN A N 2557 C CA . ASN A 341 ? 0.4285 0.4150 0.4150 -0.0491 -0.0581 0.0008 341 ASN A CA 2558 C C . ASN A 341 ? 0.4117 0.3902 0.3966 -0.0480 -0.0577 -0.0023 341 ASN A C 2559 O O . ASN A 341 ? 0.4538 0.4291 0.4383 -0.0455 -0.0558 -0.0053 341 ASN A O 2560 C CB . ASN A 341 ? 0.4402 0.4235 0.4235 -0.0500 -0.0591 0.0001 341 ASN A CB 2561 C CG . ASN A 341 ? 0.4385 0.4146 0.4169 -0.0541 -0.0620 -0.0004 341 ASN A CG 2562 O OD1 . ASN A 341 ? 0.4453 0.4220 0.4217 -0.0584 -0.0643 0.0015 341 ASN A OD1 2563 N ND2 . ASN A 341 ? 0.4204 0.3889 0.3954 -0.0530 -0.0619 -0.0033 341 ASN A ND2 2564 N N . GLY A 342 ? 0.3678 0.3437 0.3510 -0.0499 -0.0594 -0.0019 342 GLY A N 2565 C CA . GLY A 342 ? 0.3704 0.3383 0.3502 -0.0479 -0.0598 -0.0050 342 GLY A CA 2566 C C . GLY A 342 ? 0.3817 0.3397 0.3533 -0.0501 -0.0632 -0.0058 342 GLY A C 2567 O O . GLY A 342 ? 0.3885 0.3455 0.3569 -0.0548 -0.0653 -0.0033 342 GLY A O 2568 N N . TRP A 343 ? 0.3714 0.3222 0.3387 -0.0465 -0.0638 -0.0093 343 TRP A N 2569 C CA . TRP A 343 ? 0.3924 0.3317 0.3497 -0.0467 -0.0670 -0.0107 343 TRP A CA 2570 C C . TRP A 343 ? 0.4189 0.3484 0.3680 -0.0458 -0.0695 -0.0110 343 TRP A C 2571 O O . TRP A 343 ? 0.3985 0.3266 0.3467 -0.0399 -0.0691 -0.0143 343 TRP A O 2572 C CB . TRP A 343 ? 0.3700 0.3085 0.3266 -0.0417 -0.0661 -0.0152 343 TRP A CB 2573 C CG . TRP A 343 ? 0.3439 0.2884 0.3053 -0.0429 -0.0641 -0.0153 343 TRP A CG 2574 C CD1 . TRP A 343 ? 0.3350 0.2830 0.2989 -0.0473 -0.0639 -0.0119 343 TRP A CD1 2575 C CD2 . TRP A 343 ? 0.3344 0.2821 0.2972 -0.0397 -0.0620 -0.0193 343 TRP A CD2 2576 N NE1 . TRP A 343 ? 0.3254 0.2764 0.2914 -0.0465 -0.0620 -0.0133 343 TRP A NE1 2577 C CE2 . TRP A 343 ? 0.3267 0.2775 0.2921 -0.0427 -0.0606 -0.0177 343 TRP A CE2 2578 C CE3 . TRP A 343 ? 0.3387 0.2883 0.3007 -0.0348 -0.0611 -0.0241 343 TRP A CE3 2579 C CZ2 . TRP A 343 ? 0.3203 0.2739 0.2864 -0.0417 -0.0584 -0.0207 343 TRP A CZ2 2580 C CZ3 . TRP A 343 ? 0.3306 0.2856 0.2944 -0.0342 -0.0587 -0.0273 343 TRP A CZ3 2581 C CH2 . TRP A 343 ? 0.3241 0.2800 0.2894 -0.0380 -0.0573 -0.0255 343 TRP A CH2 2582 N N . GLU A 344 ? 0.4681 0.3907 0.4099 -0.0518 -0.0721 -0.0078 344 GLU A N 2583 C CA . GLU A 344 ? 0.5195 0.4295 0.4502 -0.0519 -0.0748 -0.0078 344 GLU A CA 2584 C C . GLU A 344 ? 0.5240 0.4186 0.4416 -0.0464 -0.0776 -0.0114 344 GLU A C 2585 O O . GLU A 344 ? 0.5250 0.4109 0.4350 -0.0416 -0.0791 -0.0134 344 GLU A O 2586 C CB . GLU A 344 ? 0.5685 0.4749 0.4929 -0.0614 -0.0768 -0.0034 344 GLU A CB 2587 C CG . GLU A 344 ? 0.6009 0.5240 0.5378 -0.0646 -0.0741 -0.0005 344 GLU A CG 2588 C CD . GLU A 344 ? 0.6596 0.5833 0.5914 -0.0745 -0.0757 0.0034 344 GLU A CD 2589 O OE1 . GLU A 344 ? 0.7041 0.6126 0.6217 -0.0782 -0.0785 0.0038 344 GLU A OE1 2590 O OE2 . GLU A 344 ? 0.6832 0.6227 0.6241 -0.0783 -0.0742 0.0059 344 GLU A OE2 2591 N N . GLY A 345 ? 0.5319 0.4238 0.4468 -0.0462 -0.0783 -0.0126 345 GLY A N 2592 C CA . GLY A 345 ? 0.5362 0.4145 0.4384 -0.0399 -0.0810 -0.0164 345 GLY A CA 2593 C C . GLY A 345 ? 0.5382 0.4242 0.4460 -0.0299 -0.0792 -0.0215 345 GLY A C 2594 O O . GLY A 345 ? 0.5308 0.4081 0.4285 -0.0232 -0.0813 -0.0252 345 GLY A O 2595 N N . MET A 346 ? 0.5285 0.4312 0.4512 -0.0287 -0.0753 -0.0221 346 MET A N 2596 C CA . MET A 346 ? 0.5307 0.4419 0.4576 -0.0205 -0.0736 -0.0272 346 MET A CA 2597 C C . MET A 346 ? 0.5364 0.4459 0.4606 -0.0156 -0.0743 -0.0286 346 MET A C 2598 O O . MET A 346 ? 0.5271 0.4448 0.4601 -0.0179 -0.0720 -0.0268 346 MET A O 2599 C CB . MET A 346 ? 0.5381 0.4668 0.4797 -0.0218 -0.0690 -0.0280 346 MET A CB 2600 C CG . MET A 346 ? 0.5617 0.5001 0.5060 -0.0146 -0.0674 -0.0338 346 MET A CG 2601 S SD . MET A 346 ? 0.6082 0.5609 0.5623 -0.0172 -0.0631 -0.0358 346 MET A SD 2602 C CE . MET A 346 ? 0.5561 0.5152 0.5203 -0.0232 -0.0599 -0.0314 346 MET A CE 2603 N N . VAL A 347 ? 0.5423 0.4411 0.4537 -0.0080 -0.0775 -0.0320 347 VAL A N 2604 C CA . VAL A 347 ? 0.5678 0.4602 0.4720 -0.0025 -0.0795 -0.0332 347 VAL A CA 2605 C C . VAL A 347 ? 0.5632 0.4658 0.4689 0.0084 -0.0790 -0.0395 347 VAL A C 2606 O O . VAL A 347 ? 0.5992 0.5001 0.5012 0.0138 -0.0801 -0.0410 347 VAL A O 2607 C CB . VAL A 347 ? 0.6159 0.4832 0.4991 -0.0025 -0.0845 -0.0316 347 VAL A CB 2608 C CG1 . VAL A 347 ? 0.6180 0.4786 0.5003 -0.0148 -0.0847 -0.0254 347 VAL A CG1 2609 C CG2 . VAL A 347 ? 0.6069 0.4638 0.4775 0.0026 -0.0873 -0.0346 347 VAL A CG2 2610 N N . ASP A 348 ? 0.5455 0.4599 0.4565 0.0116 -0.0773 -0.0433 348 ASP A N 2611 C CA . ASP A 348 ? 0.5297 0.4580 0.4429 0.0214 -0.0766 -0.0498 348 ASP A CA 2612 C C . ASP A 348 ? 0.4835 0.4354 0.4142 0.0179 -0.0714 -0.0514 348 ASP A C 2613 O O . ASP A 348 ? 0.4818 0.4494 0.4161 0.0236 -0.0700 -0.0569 348 ASP A O 2614 C CB . ASP A 348 ? 0.5781 0.5031 0.4811 0.0293 -0.0790 -0.0543 348 ASP A CB 2615 C CG . ASP A 348 ? 0.6026 0.5348 0.5126 0.0234 -0.0766 -0.0540 348 ASP A CG 2616 O OD1 . ASP A 348 ? 0.6300 0.5634 0.5489 0.0131 -0.0741 -0.0493 348 ASP A OD1 2617 O OD2 . ASP A 348 ? 0.6546 0.5913 0.5605 0.0298 -0.0772 -0.0586 348 ASP A OD2 2618 N N . GLY A 349 ? 0.4450 0.3994 0.3854 0.0084 -0.0685 -0.0467 349 GLY A N 2619 C CA . GLY A 349 ? 0.4043 0.3768 0.3583 0.0043 -0.0637 -0.0476 349 GLY A CA 2620 C C . GLY A 349 ? 0.3794 0.3496 0.3402 -0.0044 -0.0616 -0.0418 349 GLY A C 2621 O O . GLY A 349 ? 0.3808 0.3384 0.3373 -0.0081 -0.0636 -0.0372 349 GLY A O 2622 N N . TRP A 350 ? 0.3409 0.3234 0.3112 -0.0078 -0.0577 -0.0420 350 TRP A N 2623 C CA . TRP A 350 ? 0.3243 0.3053 0.3003 -0.0146 -0.0556 -0.0368 350 TRP A CA 2624 C C . TRP A 350 ? 0.3049 0.2873 0.2839 -0.0203 -0.0534 -0.0351 350 TRP A C 2625 O O . TRP A 350 ? 0.2909 0.2691 0.2718 -0.0247 -0.0530 -0.0304 350 TRP A O 2626 C CB . TRP A 350 ? 0.3159 0.3063 0.2981 -0.0151 -0.0527 -0.0377 350 TRP A CB 2627 C CG . TRP A 350 ? 0.3242 0.3111 0.3042 -0.0110 -0.0548 -0.0374 350 TRP A CG 2628 C CD1 . TRP A 350 ? 0.3406 0.3175 0.3117 -0.0055 -0.0590 -0.0381 350 TRP A CD1 2629 C CD2 . TRP A 350 ? 0.3065 0.2982 0.2914 -0.0119 -0.0529 -0.0365 350 TRP A CD2 2630 N NE1 . TRP A 350 ? 0.3431 0.3183 0.3135 -0.0033 -0.0598 -0.0374 350 TRP A NE1 2631 C CE2 . TRP A 350 ? 0.3282 0.3132 0.3076 -0.0069 -0.0562 -0.0366 350 TRP A CE2 2632 C CE3 . TRP A 350 ? 0.3033 0.3025 0.2948 -0.0162 -0.0491 -0.0356 350 TRP A CE3 2633 C CZ2 . TRP A 350 ? 0.3197 0.3068 0.3018 -0.0064 -0.0554 -0.0357 350 TRP A CZ2 2634 C CZ3 . TRP A 350 ? 0.3034 0.3046 0.2974 -0.0156 -0.0484 -0.0349 350 TRP A CZ3 2635 C CH2 . TRP A 350 ? 0.3077 0.3039 0.2979 -0.0108 -0.0514 -0.0349 350 TRP A CH2 2636 N N . TYR A 351 ? 0.3020 0.2914 0.2813 -0.0199 -0.0518 -0.0391 351 TYR A N 2637 C CA . TYR A 351 ? 0.2924 0.2822 0.2727 -0.0249 -0.0498 -0.0381 351 TYR A CA 2638 C C . TYR A 351 ? 0.3031 0.2926 0.2790 -0.0225 -0.0512 -0.0414 351 TYR A C 2639 O O . TYR A 351 ? 0.3035 0.2971 0.2766 -0.0166 -0.0526 -0.0457 351 TYR A O 2640 C CB . TYR A 351 ? 0.2899 0.2895 0.2742 -0.0288 -0.0453 -0.0401 351 TYR A CB 2641 C CG . TYR A 351 ? 0.2881 0.2891 0.2759 -0.0303 -0.0435 -0.0380 351 TYR A CG 2642 C CD1 . TYR A 351 ? 0.2891 0.2974 0.2787 -0.0273 -0.0432 -0.0410 351 TYR A CD1 2643 C CD2 . TYR A 351 ? 0.2877 0.2830 0.2763 -0.0339 -0.0424 -0.0333 351 TYR A CD2 2644 C CE1 . TYR A 351 ? 0.2819 0.2911 0.2744 -0.0287 -0.0416 -0.0391 351 TYR A CE1 2645 C CE2 . TYR A 351 ? 0.2866 0.2827 0.2776 -0.0346 -0.0409 -0.0315 351 TYR A CE2 2646 C CZ . TYR A 351 ? 0.2847 0.2873 0.2777 -0.0324 -0.0405 -0.0343 351 TYR A CZ 2647 O OH . TYR A 351 ? 0.2824 0.2852 0.2773 -0.0331 -0.0389 -0.0324 351 TYR A OH 2648 N N . GLY A 352 ? 0.3041 0.2896 0.2789 -0.0263 -0.0508 -0.0396 352 GLY A N 2649 C CA . GLY A 352 ? 0.3160 0.3013 0.2864 -0.0243 -0.0519 -0.0427 352 GLY A CA 2650 C C . GLY A 352 ? 0.3181 0.2982 0.2873 -0.0290 -0.0515 -0.0402 352 GLY A C 2651 O O . GLY A 352 ? 0.3053 0.2842 0.2773 -0.0338 -0.0495 -0.0368 352 GLY A O 2652 N N . PHE A 353 ? 0.3191 0.2956 0.2832 -0.0268 -0.0535 -0.0420 353 PHE A N 2653 C CA . PHE A 353 ? 0.3212 0.2945 0.2835 -0.0304 -0.0530 -0.0411 353 PHE A CA 2654 C C . PHE A 353 ? 0.3256 0.2866 0.2817 -0.0292 -0.0573 -0.0386 353 PHE A C 2655 O O . PHE A 353 ? 0.3365 0.2927 0.2869 -0.0239 -0.0603 -0.0404 353 PHE A O 2656 C CB . PHE A 353 ? 0.3289 0.3110 0.2898 -0.0291 -0.0513 -0.0467 353 PHE A CB 2657 C CG . PHE A 353 ? 0.3379 0.3331 0.3031 -0.0320 -0.0469 -0.0499 353 PHE A CG 2658 C CD1 . PHE A 353 ? 0.3367 0.3324 0.3023 -0.0389 -0.0435 -0.0488 353 PHE A CD1 2659 C CD2 . PHE A 353 ? 0.3489 0.3557 0.3160 -0.0281 -0.0462 -0.0543 353 PHE A CD2 2660 C CE1 . PHE A 353 ? 0.3480 0.3538 0.3148 -0.0430 -0.0394 -0.0519 353 PHE A CE1 2661 C CE2 . PHE A 353 ? 0.3401 0.3599 0.3102 -0.0322 -0.0421 -0.0575 353 PHE A CE2 2662 C CZ . PHE A 353 ? 0.3405 0.3592 0.3099 -0.0403 -0.0386 -0.0563 353 PHE A CZ 2663 N N . ARG A 354 ? 0.3229 0.2783 0.2787 -0.0339 -0.0576 -0.0347 354 ARG A N 2664 C CA . ARG A 354 ? 0.3428 0.2875 0.2919 -0.0344 -0.0612 -0.0328 354 ARG A CA 2665 C C . ARG A 354 ? 0.3455 0.2909 0.2941 -0.0371 -0.0600 -0.0332 354 ARG A C 2666 O O . ARG A 354 ? 0.3370 0.2871 0.2899 -0.0405 -0.0570 -0.0322 354 ARG A O 2667 C CB . ARG A 354 ? 0.3517 0.2901 0.3006 -0.0383 -0.0634 -0.0272 354 ARG A CB 2668 C CG . ARG A 354 ? 0.3654 0.2974 0.3099 -0.0362 -0.0662 -0.0266 354 ARG A CG 2669 C CD . ARG A 354 ? 0.3781 0.3060 0.3221 -0.0415 -0.0680 -0.0213 354 ARG A CD 2670 N NE . ARG A 354 ? 0.3940 0.3155 0.3330 -0.0401 -0.0702 -0.0208 354 ARG A NE 2671 C CZ . ARG A 354 ? 0.4055 0.3239 0.3429 -0.0448 -0.0718 -0.0168 354 ARG A CZ 2672 N NH1 . ARG A 354 ? 0.4130 0.3364 0.3546 -0.0507 -0.0715 -0.0129 354 ARG A NH1 2673 N NH2 . ARG A 354 ? 0.4225 0.3335 0.3536 -0.0435 -0.0737 -0.0168 354 ARG A NH2 2674 N N . HIS A 355 ? 0.3550 0.2939 0.2967 -0.0355 -0.0624 -0.0347 355 HIS A N 2675 C CA . HIS A 355 ? 0.3490 0.2887 0.2897 -0.0377 -0.0611 -0.0356 355 HIS A CA 2676 C C . HIS A 355 ? 0.3660 0.2946 0.2998 -0.0391 -0.0647 -0.0333 355 HIS A C 2677 O O . HIS A 355 ? 0.3569 0.2764 0.2843 -0.0376 -0.0682 -0.0323 355 HIS A O 2678 C CB . HIS A 355 ? 0.3529 0.3006 0.2927 -0.0341 -0.0591 -0.0416 355 HIS A CB 2679 C CG . HIS A 355 ? 0.3692 0.3126 0.3015 -0.0273 -0.0622 -0.0451 355 HIS A CG 2680 N ND1 . HIS A 355 ? 0.3709 0.3179 0.3023 -0.0213 -0.0629 -0.0480 355 HIS A ND1 2681 C CD2 . HIS A 355 ? 0.3828 0.3169 0.3062 -0.0249 -0.0652 -0.0460 355 HIS A CD2 2682 C CE1 . HIS A 355 ? 0.3948 0.3347 0.3165 -0.0146 -0.0663 -0.0508 355 HIS A CE1 2683 N NE2 . HIS A 355 ? 0.3874 0.3189 0.3039 -0.0171 -0.0676 -0.0495 355 HIS A NE2 2684 N N . GLN A 356 ? 0.3767 0.3050 0.3107 -0.0427 -0.0638 -0.0322 356 GLN A N 2685 C CA . GLN A 356 ? 0.3981 0.3171 0.3251 -0.0441 -0.0668 -0.0310 356 GLN A CA 2686 C C . GLN A 356 ? 0.3920 0.3137 0.3177 -0.0439 -0.0648 -0.0342 356 GLN A C 2687 O O . GLN A 356 ? 0.3645 0.2921 0.2945 -0.0466 -0.0616 -0.0341 356 GLN A O 2688 C CB . GLN A 356 ? 0.4366 0.3531 0.3649 -0.0496 -0.0682 -0.0256 356 GLN A CB 2689 C CG . GLN A 356 ? 0.4860 0.3933 0.4065 -0.0520 -0.0715 -0.0243 356 GLN A CG 2690 C CD . GLN A 356 ? 0.5381 0.4451 0.4595 -0.0575 -0.0734 -0.0193 356 GLN A CD 2691 O OE1 . GLN A 356 ? 0.6129 0.5280 0.5414 -0.0590 -0.0716 -0.0170 356 GLN A OE1 2692 N NE2 . GLN A 356 ? 0.5936 0.4913 0.5067 -0.0607 -0.0771 -0.0177 356 GLN A NE2 2693 N N . ASN A 357 ? 0.3948 0.3111 0.3130 -0.0404 -0.0668 -0.0371 357 ASN A N 2694 C CA . ASN A 357 ? 0.3970 0.3161 0.3132 -0.0400 -0.0652 -0.0404 357 ASN A CA 2695 C C . ASN A 357 ? 0.4306 0.3379 0.3368 -0.0385 -0.0690 -0.0406 357 ASN A C 2696 O O . ASN A 357 ? 0.4066 0.3031 0.3075 -0.0398 -0.0726 -0.0373 357 ASN A O 2697 C CB . ASN A 357 ? 0.3958 0.3271 0.3146 -0.0359 -0.0621 -0.0462 357 ASN A CB 2698 C CG . ASN A 357 ? 0.3978 0.3277 0.3111 -0.0279 -0.0647 -0.0497 357 ASN A CG 2699 O OD1 . ASN A 357 ? 0.4100 0.3265 0.3150 -0.0256 -0.0689 -0.0481 357 ASN A OD1 2700 N ND2 . ASN A 357 ? 0.3799 0.3232 0.2961 -0.0238 -0.0622 -0.0549 357 ASN A ND2 2701 N N . SER A 358 ? 0.4611 0.3708 0.3641 -0.0365 -0.0679 -0.0444 358 SER A N 2702 C CA . SER A 358 ? 0.5127 0.4116 0.4051 -0.0341 -0.0711 -0.0455 358 SER A CA 2703 C C . SER A 358 ? 0.5222 0.4102 0.4045 -0.0279 -0.0752 -0.0467 358 SER A C 2704 O O . SER A 358 ? 0.5605 0.4339 0.4318 -0.0279 -0.0789 -0.0454 358 SER A O 2705 C CB . SER A 358 ? 0.5393 0.4466 0.4310 -0.0314 -0.0686 -0.0508 358 SER A CB 2706 O OG . SER A 358 ? 0.5737 0.4962 0.4709 -0.0278 -0.0653 -0.0554 358 SER A OG 2707 N N . GLU A 359 ? 0.5121 0.4063 0.3964 -0.0226 -0.0746 -0.0492 359 GLU A N 2708 C CA . GLU A 359 ? 0.5147 0.3985 0.3876 -0.0148 -0.0784 -0.0512 359 GLU A CA 2709 C C . GLU A 359 ? 0.5040 0.3774 0.3741 -0.0171 -0.0809 -0.0470 359 GLU A C 2710 O O . GLU A 359 ? 0.5108 0.3727 0.3692 -0.0110 -0.0843 -0.0483 359 GLU A O 2711 C CB . GLU A 359 ? 0.5147 0.4128 0.3900 -0.0060 -0.0764 -0.0575 359 GLU A CB 2712 C CG . GLU A 359 ? 0.5269 0.4384 0.4051 -0.0043 -0.0735 -0.0623 359 GLU A CG 2713 C CD . GLU A 359 ? 0.5429 0.4689 0.4206 0.0054 -0.0725 -0.0692 359 GLU A CD 2714 O OE1 . GLU A 359 ? 0.5865 0.5043 0.4517 0.0153 -0.0761 -0.0723 359 GLU A OE1 2715 O OE2 . GLU A 359 ? 0.5370 0.4827 0.4256 0.0037 -0.0683 -0.0717 359 GLU A OE2 2716 N N . GLY A 360 ? 0.4536 0.3308 0.3332 -0.0255 -0.0795 -0.0422 360 GLY A N 2717 C CA . GLY A 360 ? 0.4484 0.3173 0.3258 -0.0293 -0.0817 -0.0378 360 GLY A CA 2718 C C . GLY A 360 ? 0.4338 0.3159 0.3249 -0.0321 -0.0785 -0.0360 360 GLY A C 2719 O O . GLY A 360 ? 0.3901 0.2853 0.2921 -0.0342 -0.0747 -0.0363 360 GLY A O 2720 N N . ILE A 361 ? 0.4444 0.3211 0.3329 -0.0324 -0.0803 -0.0339 361 ILE A N 2721 C CA . ILE A 361 ? 0.4588 0.3459 0.3586 -0.0349 -0.0779 -0.0318 361 ILE A CA 2722 C C . ILE A 361 ? 0.4600 0.3466 0.3571 -0.0281 -0.0784 -0.0346 361 ILE A C 2723 O O . ILE A 361 ? 0.4779 0.3498 0.3622 -0.0257 -0.0821 -0.0345 361 ILE A O 2724 C CB . ILE A 361 ? 0.4812 0.3636 0.3808 -0.0429 -0.0795 -0.0260 361 ILE A CB 2725 C CG1 . ILE A 361 ? 0.5057 0.3916 0.4091 -0.0489 -0.0789 -0.0234 361 ILE A CG1 2726 C CG2 . ILE A 361 ? 0.5040 0.3964 0.4138 -0.0441 -0.0773 -0.0242 361 ILE A CG2 2727 C CD1 . ILE A 361 ? 0.5324 0.4129 0.4318 -0.0568 -0.0817 -0.0185 361 ILE A CD1 2728 N N . GLY A 362 ? 0.4372 0.3386 0.3448 -0.0253 -0.0747 -0.0371 362 GLY A N 2729 C CA . GLY A 362 ? 0.4370 0.3409 0.3430 -0.0180 -0.0750 -0.0405 362 GLY A CA 2730 C C . GLY A 362 ? 0.4262 0.3420 0.3438 -0.0198 -0.0719 -0.0395 362 GLY A C 2731 O O . GLY A 362 ? 0.3924 0.3153 0.3194 -0.0260 -0.0692 -0.0365 362 GLY A O 2732 N N . GLN A 363 ? 0.4265 0.3432 0.3420 -0.0137 -0.0727 -0.0419 363 GLN A N 2733 C CA . GLN A 363 ? 0.4215 0.3482 0.3463 -0.0144 -0.0702 -0.0414 363 GLN A CA 2734 C C . GLN A 363 ? 0.4130 0.3496 0.3380 -0.0059 -0.0695 -0.0473 363 GLN A C 2735 O O . GLN A 363 ? 0.4158 0.3459 0.3302 0.0018 -0.0725 -0.0507 363 GLN A O 2736 C CB . GLN A 363 ? 0.4438 0.3588 0.3639 -0.0167 -0.0729 -0.0371 363 GLN A CB 2737 C CG . GLN A 363 ? 0.4581 0.3815 0.3871 -0.0179 -0.0707 -0.0357 363 GLN A CG 2738 C CD . GLN A 363 ? 0.4819 0.3932 0.4048 -0.0209 -0.0735 -0.0315 363 GLN A CD 2739 O OE1 . GLN A 363 ? 0.5087 0.4193 0.4350 -0.0283 -0.0733 -0.0268 363 GLN A OE1 2740 N NE2 . GLN A 363 ? 0.5056 0.4071 0.4181 -0.0150 -0.0765 -0.0334 363 GLN A NE2 2741 N N . ALA A 364 ? 0.3766 0.3288 0.3124 -0.0072 -0.0656 -0.0487 364 ALA A N 2742 C CA . ALA A 364 ? 0.3709 0.3354 0.3082 -0.0002 -0.0647 -0.0541 364 ALA A CA 2743 C C . ALA A 364 ? 0.3623 0.3366 0.3096 -0.0040 -0.0616 -0.0528 364 ALA A C 2744 O O . ALA A 364 ? 0.3298 0.3073 0.2843 -0.0118 -0.0585 -0.0497 364 ALA A O 2745 C CB . ALA A 364 ? 0.3673 0.3465 0.3067 0.0017 -0.0624 -0.0597 364 ALA A CB 2746 N N . ALA A 365 ? 0.3803 0.3585 0.3266 0.0020 -0.0625 -0.0553 365 ALA A N 2747 C CA . ALA A 365 ? 0.3763 0.3636 0.3309 -0.0004 -0.0599 -0.0546 365 ALA A CA 2748 C C . ALA A 365 ? 0.3745 0.3817 0.3364 -0.0022 -0.0556 -0.0592 365 ALA A C 2749 O O . ALA A 365 ? 0.3752 0.3920 0.3350 0.0019 -0.0555 -0.0644 365 ALA A O 2750 C CB . ALA A 365 ? 0.3988 0.3825 0.3483 0.0072 -0.0628 -0.0560 365 ALA A CB 2751 N N . ASP A 366 ? 0.3587 0.3721 0.3281 -0.0087 -0.0520 -0.0574 366 ASP A N 2752 C CA . ASP A 366 ? 0.3674 0.3991 0.3420 -0.0118 -0.0479 -0.0618 366 ASP A CA 2753 C C . ASP A 366 ? 0.3821 0.4232 0.3594 -0.0078 -0.0478 -0.0643 366 ASP A C 2754 O O . ASP A 366 ? 0.3718 0.4072 0.3517 -0.0101 -0.0475 -0.0605 366 ASP A O 2755 C CB . ASP A 366 ? 0.3700 0.4002 0.3481 -0.0219 -0.0440 -0.0585 366 ASP A CB 2756 C CG . ASP A 366 ? 0.3941 0.4406 0.3748 -0.0273 -0.0395 -0.0629 366 ASP A CG 2757 O OD1 . ASP A 366 ? 0.4159 0.4716 0.3950 -0.0284 -0.0382 -0.0670 366 ASP A OD1 2758 O OD2 . ASP A 366 ? 0.3887 0.4389 0.3722 -0.0310 -0.0372 -0.0623 366 ASP A OD2 2759 N N . LEU A 367 ? 0.3935 0.4497 0.3700 -0.0014 -0.0481 -0.0707 367 LEU A N 2760 C CA . LEU A 367 ? 0.4162 0.4829 0.3943 0.0040 -0.0487 -0.0739 367 LEU A CA 2761 C C . LEU A 367 ? 0.4016 0.4788 0.3867 -0.0043 -0.0443 -0.0737 367 LEU A C 2762 O O . LEU A 367 ? 0.3961 0.4716 0.3832 -0.0032 -0.0446 -0.0721 367 LEU A O 2763 C CB . LEU A 367 ? 0.4573 0.5419 0.4331 0.0129 -0.0498 -0.0817 367 LEU A CB 2764 C CG . LEU A 367 ? 0.4844 0.5823 0.4603 0.0215 -0.0512 -0.0862 367 LEU A CG 2765 C CD1 . LEU A 367 ? 0.5203 0.6306 0.4906 0.0336 -0.0538 -0.0932 367 LEU A CD1 2766 C CD2 . LEU A 367 ? 0.4994 0.6171 0.4836 0.0142 -0.0467 -0.0886 367 LEU A CD2 2767 N N . LYS A 368 ? 0.3987 0.4855 0.3860 -0.0129 -0.0402 -0.0753 368 LYS A N 2768 C CA . LYS A 368 ? 0.4233 0.5210 0.4142 -0.0213 -0.0358 -0.0764 368 LYS A CA 2769 C C . LYS A 368 ? 0.3958 0.4784 0.3880 -0.0258 -0.0352 -0.0700 368 LYS A C 2770 O O . LYS A 368 ? 0.3667 0.4541 0.3615 -0.0262 -0.0343 -0.0703 368 LYS A O 2771 C CB . LYS A 368 ? 0.4644 0.5701 0.4542 -0.0311 -0.0317 -0.0786 368 LYS A CB 2772 C CG . LYS A 368 ? 0.5074 0.6242 0.4980 -0.0410 -0.0271 -0.0805 368 LYS A CG 2773 C CD . LYS A 368 ? 0.5486 0.6537 0.5345 -0.0526 -0.0236 -0.0771 368 LYS A CD 2774 C CE . LYS A 368 ? 0.5854 0.6963 0.5688 -0.0629 -0.0194 -0.0783 368 LYS A CE 2775 N NZ . LYS A 368 ? 0.5955 0.7299 0.5779 -0.0691 -0.0163 -0.0855 368 LYS A NZ 2776 N N . SER A 369 ? 0.3696 0.4350 0.3599 -0.0287 -0.0357 -0.0645 369 SER A N 2777 C CA . SER A 369 ? 0.3559 0.4075 0.3468 -0.0321 -0.0352 -0.0584 369 SER A CA 2778 C C . SER A 369 ? 0.3402 0.3860 0.3327 -0.0253 -0.0385 -0.0561 369 SER A C 2779 O O . SER A 369 ? 0.3249 0.3691 0.3195 -0.0269 -0.0375 -0.0539 369 SER A O 2780 C CB . SER A 369 ? 0.3582 0.3954 0.3465 -0.0354 -0.0355 -0.0536 369 SER A CB 2781 O OG . SER A 369 ? 0.3690 0.4003 0.3557 -0.0298 -0.0393 -0.0531 369 SER A OG 2782 N N . THR A 370 ? 0.3439 0.3855 0.3339 -0.0179 -0.0425 -0.0567 370 THR A N 2783 C CA . THR A 370 ? 0.3418 0.3762 0.3305 -0.0116 -0.0460 -0.0549 370 THR A CA 2784 C C . THR A 370 ? 0.3441 0.3908 0.3354 -0.0085 -0.0452 -0.0586 370 THR A C 2785 O O . THR A 370 ? 0.3249 0.3671 0.3177 -0.0082 -0.0456 -0.0559 370 THR A O 2786 C CB . THR A 370 ? 0.3560 0.3832 0.3380 -0.0038 -0.0505 -0.0562 370 THR A CB 2787 O OG1 . THR A 370 ? 0.3425 0.3579 0.3218 -0.0071 -0.0513 -0.0526 370 THR A OG1 2788 C CG2 . THR A 370 ? 0.3591 0.3764 0.3368 0.0022 -0.0541 -0.0545 370 THR A CG2 2789 N N . GLN A 371 ? 0.3529 0.4168 0.3449 -0.0062 -0.0442 -0.0650 371 GLN A N 2790 C CA . GLN A 371 ? 0.3677 0.4463 0.3621 -0.0028 -0.0437 -0.0693 371 GLN A CA 2791 C C . GLN A 371 ? 0.3442 0.4276 0.3432 -0.0117 -0.0395 -0.0679 371 GLN A C 2792 O O . GLN A 371 ? 0.3356 0.4221 0.3364 -0.0098 -0.0397 -0.0681 371 GLN A O 2793 C CB . GLN A 371 ? 0.4092 0.5080 0.4030 0.0017 -0.0436 -0.0769 371 GLN A CB 2794 C CG . GLN A 371 ? 0.4583 0.5719 0.4527 0.0097 -0.0450 -0.0819 371 GLN A CG 2795 C CD . GLN A 371 ? 0.5002 0.5981 0.4895 0.0194 -0.0498 -0.0794 371 GLN A CD 2796 O OE1 . GLN A 371 ? 0.5418 0.6253 0.5238 0.0258 -0.0535 -0.0782 371 GLN A OE1 2797 N NE2 . GLN A 371 ? 0.5215 0.6208 0.5131 0.0197 -0.0496 -0.0786 371 GLN A NE2 2798 N N . ALA A 372 ? 0.3384 0.4210 0.3377 -0.0211 -0.0359 -0.0666 372 ALA A N 2799 C CA . ALA A 372 ? 0.3313 0.4144 0.3316 -0.0298 -0.0320 -0.0650 372 ALA A CA 2800 C C . ALA A 372 ? 0.3183 0.3863 0.3194 -0.0290 -0.0331 -0.0589 372 ALA A C 2801 O O . ALA A 372 ? 0.3016 0.3722 0.3040 -0.0309 -0.0316 -0.0587 372 ALA A O 2802 C CB . ALA A 372 ? 0.3380 0.4177 0.3350 -0.0392 -0.0287 -0.0641 372 ALA A CB 2803 N N . ALA A 373 ? 0.3172 0.3702 0.3172 -0.0264 -0.0356 -0.0541 373 ALA A N 2804 C CA . ALA A 373 ? 0.3120 0.3526 0.3127 -0.0254 -0.0368 -0.0485 373 ALA A CA 2805 C C . ALA A 373 ? 0.3193 0.3621 0.3211 -0.0186 -0.0395 -0.0496 373 ALA A C 2806 O O . ALA A 373 ? 0.3277 0.3692 0.3312 -0.0194 -0.0387 -0.0477 373 ALA A O 2807 C CB . ALA A 373 ? 0.3118 0.3389 0.3108 -0.0249 -0.0391 -0.0437 373 ALA A CB 2808 N N . ILE A 374 ? 0.3340 0.3791 0.3334 -0.0116 -0.0427 -0.0527 374 ILE A N 2809 C CA . ILE A 374 ? 0.3580 0.4028 0.3558 -0.0040 -0.0457 -0.0539 374 ILE A CA 2810 C C . ILE A 374 ? 0.3623 0.4222 0.3636 -0.0040 -0.0436 -0.0579 374 ILE A C 2811 O O . ILE A 374 ? 0.3457 0.4029 0.3476 -0.0022 -0.0442 -0.0564 374 ILE A O 2812 C CB . ILE A 374 ? 0.3736 0.4161 0.3651 0.0046 -0.0498 -0.0570 374 ILE A CB 2813 C CG1 . ILE A 374 ? 0.3882 0.4124 0.3747 0.0039 -0.0524 -0.0521 374 ILE A CG1 2814 C CG2 . ILE A 374 ? 0.3713 0.4155 0.3592 0.0135 -0.0528 -0.0597 374 ILE A CG2 2815 C CD1 . ILE A 374 ? 0.4027 0.4207 0.3805 0.0114 -0.0565 -0.0546 374 ILE A CD1 2816 N N . ASN A 375 ? 0.3707 0.4469 0.3740 -0.0070 -0.0409 -0.0629 375 ASN A N 2817 C CA . ASN A 375 ? 0.3886 0.4819 0.3949 -0.0082 -0.0387 -0.0673 375 ASN A CA 2818 C C . ASN A 375 ? 0.3721 0.4602 0.3803 -0.0150 -0.0360 -0.0636 375 ASN A C 2819 O O . ASN A 375 ? 0.3460 0.4396 0.3557 -0.0129 -0.0362 -0.0648 375 ASN A O 2820 C CB . ASN A 375 ? 0.4112 0.5234 0.4184 -0.0130 -0.0358 -0.0731 375 ASN A CB 2821 C CG . ASN A 375 ? 0.4356 0.5597 0.4413 -0.0042 -0.0385 -0.0787 375 ASN A CG 2822 O OD1 . ASN A 375 ? 0.4638 0.5839 0.4667 0.0065 -0.0427 -0.0794 375 ASN A OD1 2823 N ND2 . ASN A 375 ? 0.4379 0.5754 0.4438 -0.0085 -0.0363 -0.0827 375 ASN A ND2 2824 N N . GLN A 376 ? 0.3587 0.4359 0.3661 -0.0224 -0.0337 -0.0592 376 GLN A N 2825 C CA . GLN A 376 ? 0.3529 0.4232 0.3602 -0.0282 -0.0311 -0.0555 376 GLN A CA 2826 C C . GLN A 376 ? 0.3380 0.3975 0.3465 -0.0234 -0.0335 -0.0510 376 GLN A C 2827 O O . GLN A 376 ? 0.3311 0.3910 0.3404 -0.0247 -0.0322 -0.0502 376 GLN A O 2828 C CB . GLN A 376 ? 0.3560 0.4158 0.3601 -0.0353 -0.0286 -0.0520 376 GLN A CB 2829 C CG . GLN A 376 ? 0.3769 0.4460 0.3779 -0.0427 -0.0253 -0.0561 376 GLN A CG 2830 C CD . GLN A 376 ? 0.3805 0.4365 0.3760 -0.0488 -0.0234 -0.0526 376 GLN A CD 2831 O OE1 . GLN A 376 ? 0.3987 0.4447 0.3901 -0.0528 -0.0214 -0.0495 376 GLN A OE1 2832 N NE2 . GLN A 376 ? 0.4345 0.4899 0.4291 -0.0487 -0.0241 -0.0533 376 GLN A NE2 2833 N N . ILE A 377 ? 0.3222 0.3716 0.3298 -0.0185 -0.0368 -0.0482 377 ILE A N 2834 C CA . ILE A 377 ? 0.3191 0.3583 0.3266 -0.0149 -0.0392 -0.0440 377 ILE A CA 2835 C C . ILE A 377 ? 0.3235 0.3695 0.3309 -0.0087 -0.0411 -0.0475 377 ILE A C 2836 O O . ILE A 377 ? 0.3318 0.3751 0.3400 -0.0080 -0.0411 -0.0456 377 ILE A O 2837 C CB . ILE A 377 ? 0.3111 0.3380 0.3159 -0.0129 -0.0422 -0.0403 377 ILE A CB 2838 C CG1 . ILE A 377 ? 0.3128 0.3333 0.3182 -0.0188 -0.0403 -0.0360 377 ILE A CG1 2839 C CG2 . ILE A 377 ? 0.3117 0.3295 0.3143 -0.0091 -0.0453 -0.0374 377 ILE A CG2 2840 C CD1 . ILE A 377 ? 0.2969 0.3086 0.2997 -0.0183 -0.0428 -0.0334 377 ILE A CD1 2841 N N . ASN A 378 ? 0.3266 0.3823 0.3326 -0.0036 -0.0427 -0.0529 378 ASN A N 2842 C CA . ASN A 378 ? 0.3637 0.4275 0.3688 0.0035 -0.0447 -0.0569 378 ASN A CA 2843 C C . ASN A 378 ? 0.3604 0.4370 0.3697 -0.0004 -0.0415 -0.0591 378 ASN A C 2844 O O . ASN A 378 ? 0.3912 0.4689 0.4004 0.0034 -0.0427 -0.0595 378 ASN A O 2845 C CB . ASN A 378 ? 0.3726 0.4459 0.3745 0.0112 -0.0473 -0.0628 378 ASN A CB 2846 C CG . ASN A 378 ? 0.3963 0.4533 0.3906 0.0178 -0.0517 -0.0608 378 ASN A CG 2847 O OD1 . ASN A 378 ? 0.4121 0.4527 0.4030 0.0179 -0.0536 -0.0559 378 ASN A OD1 2848 N ND2 . ASN A 378 ? 0.4050 0.4663 0.3956 0.0229 -0.0535 -0.0647 378 ASN A ND2 2849 N N . GLY A 379 ? 0.3554 0.4400 0.3670 -0.0088 -0.0375 -0.0603 379 GLY A N 2850 C CA . GLY A 379 ? 0.3747 0.4687 0.3881 -0.0147 -0.0341 -0.0619 379 GLY A CA 2851 C C . GLY A 379 ? 0.3709 0.4527 0.3846 -0.0165 -0.0335 -0.0567 379 GLY A C 2852 O O . GLY A 379 ? 0.3393 0.4271 0.3540 -0.0159 -0.0330 -0.0582 379 GLY A O 2853 N N . LYS A 380 ? 0.3656 0.4313 0.3782 -0.0184 -0.0335 -0.0508 380 LYS A N 2854 C CA . LYS A 380 ? 0.3654 0.4210 0.3781 -0.0195 -0.0329 -0.0460 380 LYS A CA 2855 C C . LYS A 380 ? 0.3492 0.4004 0.3621 -0.0122 -0.0364 -0.0448 380 LYS A C 2856 O O . LYS A 380 ? 0.3549 0.4047 0.3686 -0.0120 -0.0360 -0.0434 380 LYS A O 2857 C CB . LYS A 380 ? 0.3919 0.4346 0.4031 -0.0238 -0.0314 -0.0405 380 LYS A CB 2858 C CG . LYS A 380 ? 0.3982 0.4323 0.4090 -0.0215 -0.0338 -0.0374 380 LYS A CG 2859 C CD . LYS A 380 ? 0.3842 0.4085 0.3936 -0.0253 -0.0321 -0.0323 380 LYS A CD 2860 C CE . LYS A 380 ? 0.3769 0.4019 0.3830 -0.0310 -0.0290 -0.0337 380 LYS A CE 2861 N NZ . LYS A 380 ? 0.3479 0.3625 0.3508 -0.0329 -0.0277 -0.0290 380 LYS A NZ 2862 N N . LEU A 381 ? 0.3456 0.3941 0.3566 -0.0063 -0.0400 -0.0456 381 LEU A N 2863 C CA . LEU A 381 ? 0.3610 0.4044 0.3692 0.0006 -0.0436 -0.0453 381 LEU A CA 2864 C C . LEU A 381 ? 0.3786 0.4348 0.3877 0.0044 -0.0436 -0.0503 381 LEU A C 2865 O O . LEU A 381 ? 0.3883 0.4409 0.3967 0.0067 -0.0445 -0.0489 381 LEU A O 2866 C CB . LEU A 381 ? 0.3621 0.3987 0.3648 0.0065 -0.0476 -0.0461 381 LEU A CB 2867 C CG . LEU A 381 ? 0.3591 0.3808 0.3594 0.0035 -0.0486 -0.0406 381 LEU A CG 2868 C CD1 . LEU A 381 ? 0.3512 0.3667 0.3446 0.0086 -0.0523 -0.0422 381 LEU A CD1 2869 C CD2 . LEU A 381 ? 0.3455 0.3560 0.3441 0.0023 -0.0495 -0.0355 381 LEU A CD2 2870 N N . ASN A 382 ? 0.3820 0.4545 0.3928 0.0045 -0.0426 -0.0561 382 ASN A N 2871 C CA A ASN A 382 ? 0.3882 0.4766 0.4001 0.0080 -0.0427 -0.0614 382 ASN A CA 2872 C CA B ASN A 382 ? 0.3892 0.4778 0.4012 0.0079 -0.0426 -0.0615 382 ASN A CA 2873 C C . ASN A 382 ? 0.3887 0.4794 0.4036 0.0018 -0.0395 -0.0600 382 ASN A C 2874 O O . ASN A 382 ? 0.3902 0.4873 0.4052 0.0057 -0.0405 -0.0622 382 ASN A O 2875 C CB A ASN A 382 ? 0.3926 0.5009 0.4060 0.0081 -0.0418 -0.0681 382 ASN A CB 2876 C CB B ASN A 382 ? 0.3952 0.5039 0.4088 0.0075 -0.0415 -0.0681 382 ASN A CB 2877 C CG A ASN A 382 ? 0.4048 0.5122 0.4140 0.0171 -0.0456 -0.0706 382 ASN A CG 2878 C CG B ASN A 382 ? 0.4029 0.5316 0.4179 0.0116 -0.0419 -0.0742 382 ASN A CG 2879 O OD1 A ASN A 382 ? 0.4183 0.5089 0.4223 0.0231 -0.0492 -0.0674 382 ASN A OD1 2880 O OD1 B ASN A 382 ? 0.4205 0.5490 0.4324 0.0218 -0.0457 -0.0760 382 ASN A OD1 2881 N ND2 A ASN A 382 ? 0.4032 0.5282 0.4136 0.0176 -0.0449 -0.0762 382 ASN A ND2 2882 N ND2 B ASN A 382 ? 0.3977 0.5431 0.4160 0.0032 -0.0380 -0.0775 382 ASN A ND2 2883 N N . ARG A 383 ? 0.3872 0.4715 0.4031 -0.0070 -0.0359 -0.0563 383 ARG A N 2884 C CA . ARG A 383 ? 0.4062 0.4892 0.4226 -0.0127 -0.0330 -0.0544 383 ARG A CA 2885 C C . ARG A 383 ? 0.3903 0.4599 0.4063 -0.0095 -0.0344 -0.0494 383 ARG A C 2886 O O . ARG A 383 ? 0.3857 0.4563 0.4020 -0.0112 -0.0331 -0.0490 383 ARG A O 2887 C CB . ARG A 383 ? 0.4525 0.5294 0.4672 -0.0220 -0.0291 -0.0518 383 ARG A CB 2888 C CG . ARG A 383 ? 0.5031 0.5926 0.5166 -0.0284 -0.0266 -0.0566 383 ARG A CG 2889 C CD . ARG A 383 ? 0.5382 0.6187 0.5465 -0.0381 -0.0226 -0.0541 383 ARG A CD 2890 N NE . ARG A 383 ? 0.5731 0.6420 0.5797 -0.0387 -0.0227 -0.0506 383 ARG A NE 2891 C CZ . ARG A 383 ? 0.5932 0.6674 0.5999 -0.0395 -0.0230 -0.0530 383 ARG A CZ 2892 N NH1 . ARG A 383 ? 0.6164 0.7083 0.6250 -0.0392 -0.0232 -0.0591 383 ARG A NH1 2893 N NH2 . ARG A 383 ? 0.6046 0.6672 0.6095 -0.0402 -0.0231 -0.0495 383 ARG A NH2 2894 N N . LEU A 384 ? 0.3620 0.4190 0.3767 -0.0059 -0.0370 -0.0455 384 LEU A N 2895 C CA . LEU A 384 ? 0.3612 0.4053 0.3750 -0.0047 -0.0380 -0.0402 384 LEU A CA 2896 C C . LEU A 384 ? 0.3641 0.4037 0.3747 0.0028 -0.0421 -0.0405 384 LEU A C 2897 O O . LEU A 384 ? 0.3675 0.3992 0.3770 0.0034 -0.0427 -0.0371 384 LEU A O 2898 C CB . LEU A 384 ? 0.3509 0.3839 0.3642 -0.0075 -0.0378 -0.0351 384 LEU A CB 2899 C CG . LEU A 384 ? 0.3518 0.3838 0.3659 -0.0141 -0.0340 -0.0331 384 LEU A CG 2900 C CD1 . LEU A 384 ? 0.3568 0.3807 0.3704 -0.0155 -0.0345 -0.0293 384 LEU A CD1 2901 C CD2 . LEU A 384 ? 0.3540 0.3830 0.3680 -0.0161 -0.0319 -0.0306 384 LEU A CD2 2902 N N . ILE A 385 ? 0.3531 0.3963 0.3607 0.0087 -0.0451 -0.0445 385 ILE A N 2903 C CA . ILE A 385 ? 0.3648 0.3997 0.3657 0.0167 -0.0496 -0.0449 385 ILE A CA 2904 C C . ILE A 385 ? 0.3798 0.4269 0.3797 0.0236 -0.0510 -0.0507 385 ILE A C 2905 O O . ILE A 385 ? 0.3778 0.4414 0.3806 0.0245 -0.0501 -0.0561 385 ILE A O 2906 C CB . ILE A 385 ? 0.3736 0.4005 0.3686 0.0200 -0.0526 -0.0451 385 ILE A CB 2907 C CG1 . ILE A 385 ? 0.3770 0.3933 0.3731 0.0131 -0.0514 -0.0394 385 ILE A CG1 2908 C CG2 . ILE A 385 ? 0.3878 0.4022 0.3720 0.0284 -0.0576 -0.0455 385 ILE A CG2 2909 C CD1 . ILE A 385 ? 0.3744 0.3798 0.3697 0.0096 -0.0512 -0.0337 385 ILE A CD1 2910 N N . GLY A 386 ? 0.3900 0.4301 0.3856 0.0279 -0.0532 -0.0497 386 GLY A N 2911 C CA . GLY A 386 ? 0.4035 0.4539 0.3970 0.0356 -0.0551 -0.0550 386 GLY A CA 2912 C C . GLY A 386 ? 0.4059 0.4751 0.4075 0.0312 -0.0514 -0.0580 386 GLY A C 2913 O O . GLY A 386 ? 0.4184 0.5044 0.4205 0.0363 -0.0523 -0.0641 386 GLY A O 2914 N N . LYS A 387 ? 0.3908 0.4572 0.3974 0.0220 -0.0475 -0.0539 387 LYS A N 2915 C CA . LYS A 387 ? 0.3902 0.4712 0.4022 0.0158 -0.0437 -0.0563 387 LYS A CA 2916 C C . LYS A 387 ? 0.3807 0.4558 0.3935 0.0128 -0.0421 -0.0529 387 LYS A C 2917 O O . LYS A 387 ? 0.3908 0.4710 0.4063 0.0055 -0.0384 -0.0527 387 LYS A O 2918 C CB . LYS A 387 ? 0.3980 0.4818 0.4132 0.0068 -0.0399 -0.0555 387 LYS A CB 2919 C CG . LYS A 387 ? 0.4172 0.5099 0.4324 0.0088 -0.0408 -0.0595 387 LYS A CG 2920 C CD . LYS A 387 ? 0.4436 0.5590 0.4601 0.0120 -0.0413 -0.0671 387 LYS A CD 2921 C CE . LYS A 387 ? 0.4571 0.5837 0.4739 0.0129 -0.0415 -0.0713 387 LYS A CE 2922 N NZ . LYS A 387 ? 0.4757 0.5900 0.4879 0.0217 -0.0457 -0.0700 387 LYS A NZ 2923 N N . THR A 388 ? 0.3723 0.4357 0.3811 0.0184 -0.0450 -0.0503 388 THR A N 2924 C CA . THR A 388 ? 0.3586 0.4151 0.3676 0.0159 -0.0437 -0.0467 388 THR A CA 2925 C C . THR A 388 ? 0.3707 0.4415 0.3814 0.0167 -0.0429 -0.0512 388 THR A C 2926 O O . THR A 388 ? 0.3369 0.4221 0.3475 0.0217 -0.0446 -0.0571 388 THR A O 2927 C CB . THR A 388 ? 0.3545 0.3947 0.3575 0.0209 -0.0470 -0.0430 388 THR A CB 2928 O OG1 . THR A 388 ? 0.3604 0.4028 0.3577 0.0303 -0.0511 -0.0472 388 THR A OG1 2929 C CG2 . THR A 388 ? 0.3475 0.3746 0.3480 0.0192 -0.0480 -0.0388 388 THR A CG2 2930 N N . ASN A 389 ? 0.3661 0.4335 0.3781 0.0118 -0.0402 -0.0484 389 ASN A N 2931 C CA A ASN A 389 ? 0.3834 0.4626 0.3966 0.0109 -0.0391 -0.0518 389 ASN A CA 2932 C CA B ASN A 389 ? 0.3865 0.4660 0.3997 0.0112 -0.0392 -0.0520 389 ASN A CA 2933 C C . ASN A 389 ? 0.3743 0.4448 0.3846 0.0159 -0.0412 -0.0496 389 ASN A C 2934 O O . ASN A 389 ? 0.3673 0.4220 0.3756 0.0160 -0.0417 -0.0442 389 ASN A O 2935 C CB A ASN A 389 ? 0.3960 0.4764 0.4108 0.0007 -0.0343 -0.0504 389 ASN A CB 2936 C CB B ASN A 389 ? 0.4082 0.4918 0.4231 0.0009 -0.0344 -0.0516 389 ASN A CB 2937 C CG A ASN A 389 ? 0.4036 0.4934 0.4195 -0.0049 -0.0322 -0.0534 389 ASN A CG 2938 C CG B ASN A 389 ? 0.4094 0.4768 0.4231 -0.0033 -0.0321 -0.0451 389 ASN A CG 2939 O OD1 A ASN A 389 ? 0.4057 0.5086 0.4228 -0.0016 -0.0339 -0.0583 389 ASN A OD1 2940 O OD1 B ASN A 389 ? 0.4516 0.5064 0.4645 0.0000 -0.0337 -0.0406 389 ASN A OD1 2941 N ND2 A ASN A 389 ? 0.3992 0.4819 0.4135 -0.0131 -0.0285 -0.0505 389 ASN A ND2 2942 N ND2 B ASN A 389 ? 0.4119 0.4797 0.4242 -0.0109 -0.0283 -0.0448 389 ASN A ND2 2943 N N . GLU A 390 ? 0.3456 0.4275 0.3557 0.0195 -0.0423 -0.0540 390 GLU A N 2944 C CA . GLU A 390 ? 0.3221 0.3967 0.3287 0.0246 -0.0444 -0.0526 390 GLU A CA 2945 C C . GLU A 390 ? 0.2917 0.3616 0.2997 0.0183 -0.0411 -0.0491 390 GLU A C 2946 O O . GLU A 390 ? 0.2766 0.3562 0.2871 0.0117 -0.0378 -0.0510 390 GLU A O 2947 C CB . GLU A 390 ? 0.3445 0.4345 0.3497 0.0323 -0.0473 -0.0592 390 GLU A CB 2948 C CG . GLU A 390 ? 0.3801 0.4728 0.3811 0.0422 -0.0516 -0.0629 390 GLU A CG 2949 C CD . GLU A 390 ? 0.4007 0.5090 0.3994 0.0514 -0.0547 -0.0694 390 GLU A CD 2950 O OE1 . GLU A 390 ? 0.3938 0.5243 0.3979 0.0480 -0.0527 -0.0743 390 GLU A OE1 2951 O OE2 . GLU A 390 ? 0.4438 0.5418 0.4343 0.0614 -0.0591 -0.0695 390 GLU A OE2 2952 N N . LYS A 391 ? 0.2645 0.3195 0.2693 0.0204 -0.0421 -0.0445 391 LYS A N 2953 C CA . LYS A 391 ? 0.2513 0.3026 0.2562 0.0172 -0.0400 -0.0420 391 LYS A CA 2954 C C . LYS A 391 ? 0.2532 0.2982 0.2533 0.0244 -0.0434 -0.0419 391 LYS A C 2955 O O . LYS A 391 ? 0.2514 0.2877 0.2464 0.0303 -0.0470 -0.0413 391 LYS A O 2956 C CB . LYS A 391 ? 0.2547 0.2935 0.2603 0.0115 -0.0371 -0.0357 391 LYS A CB 2957 C CG . LYS A 391 ? 0.2542 0.2956 0.2623 0.0049 -0.0338 -0.0353 391 LYS A CG 2958 C CD . LYS A 391 ? 0.2505 0.3004 0.2588 -0.0010 -0.0305 -0.0380 391 LYS A CD 2959 C CE . LYS A 391 ? 0.2464 0.2943 0.2542 -0.0078 -0.0272 -0.0369 391 LYS A CE 2960 N NZ . LYS A 391 ? 0.2276 0.2847 0.2333 -0.0146 -0.0245 -0.0408 391 LYS A NZ 2961 N N . PHE A 392 ? 0.2398 0.2876 0.2400 0.0235 -0.0423 -0.0423 392 PHE A N 2962 C CA . PHE A 392 ? 0.2533 0.2973 0.2484 0.0305 -0.0456 -0.0431 392 PHE A CA 2963 C C . PHE A 392 ? 0.2462 0.2782 0.2399 0.0275 -0.0439 -0.0379 392 PHE A C 2964 O O . PHE A 392 ? 0.2486 0.2681 0.2411 0.0252 -0.0433 -0.0328 392 PHE A O 2965 C CB . PHE A 392 ? 0.2563 0.3186 0.2525 0.0343 -0.0469 -0.0499 392 PHE A CB 2966 C CG . PHE A 392 ? 0.2594 0.3353 0.2569 0.0378 -0.0486 -0.0552 392 PHE A CG 2967 C CD1 . PHE A 392 ? 0.2730 0.3427 0.2648 0.0466 -0.0529 -0.0562 392 PHE A CD1 2968 C CD2 . PHE A 392 ? 0.2663 0.3598 0.2695 0.0314 -0.0456 -0.0589 392 PHE A CD2 2969 C CE1 . PHE A 392 ? 0.2783 0.3601 0.2708 0.0506 -0.0545 -0.0610 392 PHE A CE1 2970 C CE2 . PHE A 392 ? 0.2738 0.3810 0.2784 0.0343 -0.0470 -0.0638 392 PHE A CE2 2971 C CZ . PHE A 392 ? 0.2805 0.3827 0.2803 0.0446 -0.0515 -0.0649 392 PHE A CZ 2972 N N . HIS A 393 ? 0.2466 0.2836 0.2407 0.0268 -0.0428 -0.0392 393 HIS A N 2973 C CA . HIS A 393 ? 0.2435 0.2699 0.2361 0.0242 -0.0411 -0.0345 393 HIS A CA 2974 C C . HIS A 393 ? 0.2403 0.2649 0.2364 0.0164 -0.0365 -0.0311 393 HIS A C 2975 O O . HIS A 393 ? 0.2276 0.2611 0.2262 0.0117 -0.0339 -0.0335 393 HIS A O 2976 C CB . HIS A 393 ? 0.2517 0.2832 0.2426 0.0266 -0.0417 -0.0371 393 HIS A CB 2977 C CG . HIS A 393 ? 0.2595 0.2787 0.2472 0.0262 -0.0411 -0.0325 393 HIS A CG 2978 N ND1 . HIS A 393 ? 0.2711 0.2766 0.2537 0.0289 -0.0432 -0.0289 393 HIS A ND1 2979 C CD2 . HIS A 393 ? 0.2592 0.2780 0.2473 0.0227 -0.0383 -0.0311 393 HIS A CD2 2980 C CE1 . HIS A 393 ? 0.2661 0.2645 0.2469 0.0272 -0.0417 -0.0254 393 HIS A CE1 2981 N NE2 . HIS A 393 ? 0.2581 0.2644 0.2424 0.0241 -0.0389 -0.0268 393 HIS A NE2 2982 N N . GLN A 394 ? 0.2299 0.2429 0.2251 0.0149 -0.0354 -0.0255 394 GLN A N 2983 C CA A GLN A 394 ? 0.2328 0.2429 0.2300 0.0093 -0.0316 -0.0220 394 GLN A CA 2984 C CA B GLN A 394 ? 0.2335 0.2438 0.2307 0.0093 -0.0316 -0.0221 394 GLN A CA 2985 C C . GLN A 394 ? 0.2336 0.2363 0.2289 0.0085 -0.0298 -0.0178 394 GLN A C 2986 O O . GLN A 394 ? 0.2712 0.2748 0.2647 0.0093 -0.0296 -0.0190 394 GLN A O 2987 C CB A GLN A 394 ? 0.2282 0.2348 0.2268 0.0088 -0.0322 -0.0198 394 GLN A CB 2988 C CB B GLN A 394 ? 0.2298 0.2371 0.2286 0.0085 -0.0320 -0.0200 394 GLN A CB 2989 C CG A GLN A 394 ? 0.2290 0.2429 0.2291 0.0099 -0.0339 -0.0240 394 GLN A CG 2990 C CG B GLN A 394 ? 0.2309 0.2467 0.2317 0.0085 -0.0329 -0.0245 394 GLN A CG 2991 C CD A GLN A 394 ? 0.2296 0.2384 0.2295 0.0107 -0.0357 -0.0221 394 GLN A CD 2992 C CD B GLN A 394 ? 0.2297 0.2428 0.2321 0.0069 -0.0327 -0.0224 394 GLN A CD 2993 O OE1 A GLN A 394 ? 0.2290 0.2338 0.2303 0.0074 -0.0338 -0.0183 394 GLN A OE1 2994 O OE1 B GLN A 394 ? 0.2339 0.2394 0.2351 0.0078 -0.0340 -0.0189 394 GLN A OE1 2995 N NE2 A GLN A 394 ? 0.2257 0.2345 0.2228 0.0156 -0.0395 -0.0248 394 GLN A NE2 2996 N NE2 B GLN A 394 ? 0.2259 0.2454 0.2303 0.0036 -0.0310 -0.0248 394 GLN A NE2 2997 N N . ILE A 395 ? 0.2192 0.2159 0.2147 0.0071 -0.0284 -0.0131 395 ILE A N 2998 C CA . ILE A 395 ? 0.2164 0.2078 0.2100 0.0070 -0.0269 -0.0093 395 ILE A CA 2999 C C . ILE A 395 ? 0.2154 0.2018 0.2079 0.0078 -0.0290 -0.0061 395 ILE A C 3000 O O . ILE A 395 ? 0.2113 0.1973 0.2042 0.0078 -0.0310 -0.0064 395 ILE A O 3001 C CB . ILE A 395 ? 0.2107 0.2009 0.2043 0.0047 -0.0231 -0.0065 395 ILE A CB 3002 C CG1 . ILE A 395 ? 0.2072 0.1979 0.2030 0.0036 -0.0228 -0.0046 395 ILE A CG1 3003 C CG2 . ILE A 395 ? 0.2130 0.2049 0.2044 0.0026 -0.0210 -0.0095 395 ILE A CG2 3004 C CD1 . ILE A 395 ? 0.2022 0.1911 0.1965 0.0032 -0.0196 -0.0014 395 ILE A CD1 3005 N N . GLU A 396 ? 0.2211 0.2037 0.2113 0.0079 -0.0285 -0.0031 396 GLU A N 3006 C CA . GLU A 396 ? 0.2294 0.2072 0.2169 0.0067 -0.0300 0.0002 396 GLU A CA 3007 C C . GLU A 396 ? 0.2249 0.2064 0.2158 0.0039 -0.0278 0.0036 396 GLU A C 3008 O O . GLU A 396 ? 0.2102 0.1956 0.2036 0.0040 -0.0248 0.0043 396 GLU A O 3009 C CB . GLU A 396 ? 0.2447 0.2184 0.2283 0.0069 -0.0299 0.0021 396 GLU A CB 3010 C CG . GLU A 396 ? 0.2535 0.2233 0.2329 0.0104 -0.0325 -0.0012 396 GLU A CG 3011 C CD . GLU A 396 ? 0.2775 0.2413 0.2514 0.0127 -0.0369 -0.0032 396 GLU A CD 3012 O OE1 . GLU A 396 ? 0.3027 0.2614 0.2734 0.0103 -0.0381 -0.0010 396 GLU A OE1 3013 O OE2 . GLU A 396 ? 0.2866 0.2506 0.2582 0.0172 -0.0392 -0.0073 396 GLU A OE2 3014 N N . LYS A 397 ? 0.2217 0.2011 0.2109 0.0015 -0.0295 0.0055 397 LYS A N 3015 C CA . LYS A 397 ? 0.2238 0.2084 0.2162 -0.0010 -0.0280 0.0082 397 LYS A CA 3016 C C . LYS A 397 ? 0.2445 0.2296 0.2343 -0.0050 -0.0282 0.0120 397 LYS A C 3017 O O . LYS A 397 ? 0.2530 0.2448 0.2455 -0.0074 -0.0270 0.0143 397 LYS A O 3018 C CB . LYS A 397 ? 0.2148 0.1993 0.2088 -0.0012 -0.0296 0.0062 397 LYS A CB 3019 C CG . LYS A 397 ? 0.2067 0.1934 0.2034 0.0014 -0.0288 0.0023 397 LYS A CG 3020 C CD . LYS A 397 ? 0.2061 0.1934 0.2040 0.0013 -0.0305 0.0000 397 LYS A CD 3021 C CE . LYS A 397 ? 0.2046 0.1956 0.2045 0.0028 -0.0297 -0.0043 397 LYS A CE 3022 N NZ . LYS A 397 ? 0.2000 0.1932 0.2015 0.0024 -0.0308 -0.0065 397 LYS A NZ 3023 N N . GLU A 398 ? 0.2569 0.2353 0.2406 -0.0061 -0.0298 0.0125 398 GLU A N 3024 C CA . GLU A 398 ? 0.2799 0.2586 0.2593 -0.0113 -0.0297 0.0160 398 GLU A CA 3025 C C . GLU A 398 ? 0.2834 0.2596 0.2599 -0.0100 -0.0289 0.0165 398 GLU A C 3026 O O . GLU A 398 ? 0.2735 0.2430 0.2479 -0.0060 -0.0302 0.0138 398 GLU A O 3027 C CB . GLU A 398 ? 0.3153 0.2836 0.2859 -0.0155 -0.0333 0.0163 398 GLU A CB 3028 C CG . GLU A 398 ? 0.3419 0.3118 0.3141 -0.0175 -0.0343 0.0161 398 GLU A CG 3029 C CD . GLU A 398 ? 0.3913 0.3488 0.3521 -0.0224 -0.0378 0.0166 398 GLU A CD 3030 O OE1 . GLU A 398 ? 0.4318 0.3802 0.3825 -0.0258 -0.0391 0.0179 398 GLU A OE1 3031 O OE2 . GLU A 398 ? 0.4251 0.3808 0.3855 -0.0232 -0.0394 0.0159 398 GLU A OE2 3032 N N . PHE A 399 ? 0.2759 0.2588 0.2523 -0.0133 -0.0268 0.0196 399 PHE A N 3033 C CA . PHE A 399 ? 0.2843 0.2667 0.2588 -0.0119 -0.0254 0.0203 399 PHE A CA 3034 C C . PHE A 399 ? 0.3136 0.2962 0.2817 -0.0187 -0.0254 0.0233 399 PHE A C 3035 O O . PHE A 399 ? 0.3126 0.3053 0.2825 -0.0234 -0.0242 0.0256 399 PHE A O 3036 C CB . PHE A 399 ? 0.2720 0.2648 0.2535 -0.0075 -0.0217 0.0207 399 PHE A CB 3037 C CG . PHE A 399 ? 0.2533 0.2450 0.2389 -0.0027 -0.0214 0.0179 399 PHE A CG 3038 C CD1 . PHE A 399 ? 0.2500 0.2465 0.2396 -0.0026 -0.0211 0.0177 399 PHE A CD1 3039 C CD2 . PHE A 399 ? 0.2579 0.2434 0.2424 0.0008 -0.0217 0.0152 399 PHE A CD2 3040 C CE1 . PHE A 399 ? 0.2499 0.2444 0.2419 0.0006 -0.0208 0.0150 399 PHE A CE1 3041 C CE2 . PHE A 399 ? 0.2499 0.2350 0.2371 0.0036 -0.0213 0.0123 399 PHE A CE2 3042 C CZ . PHE A 399 ? 0.2467 0.2358 0.2372 0.0032 -0.0209 0.0123 399 PHE A CZ 3043 N N . SER A 400 ? 0.3398 0.3120 0.3000 -0.0194 -0.0268 0.0232 400 SER A N 3044 C CA . SER A 400 ? 0.3734 0.3440 0.3254 -0.0269 -0.0268 0.0259 400 SER A CA 3045 C C . SER A 400 ? 0.3856 0.3684 0.3414 -0.0268 -0.0232 0.0279 400 SER A C 3046 O O . SER A 400 ? 0.3947 0.3821 0.3459 -0.0339 -0.0223 0.0304 400 SER A O 3047 C CB . SER A 400 ? 0.3886 0.3399 0.3277 -0.0276 -0.0303 0.0249 400 SER A CB 3048 O OG . SER A 400 ? 0.4046 0.3518 0.3455 -0.0201 -0.0304 0.0226 400 SER A OG 3049 N N . GLU A 401 ? 0.3831 0.3710 0.3462 -0.0193 -0.0211 0.0267 401 GLU A N 3050 C CA . GLU A 401 ? 0.3989 0.3973 0.3647 -0.0176 -0.0178 0.0283 401 GLU A CA 3051 C C . GLU A 401 ? 0.3605 0.3712 0.3350 -0.0115 -0.0150 0.0280 401 GLU A C 3052 O O . GLU A 401 ? 0.3425 0.3501 0.3205 -0.0076 -0.0156 0.0261 401 GLU A O 3053 C CB . GLU A 401 ? 0.4410 0.4299 0.4032 -0.0138 -0.0179 0.0271 401 GLU A CB 3054 C CG . GLU A 401 ? 0.5085 0.4853 0.4601 -0.0190 -0.0202 0.0277 401 GLU A CG 3055 C CD . GLU A 401 ? 0.5406 0.5017 0.4859 -0.0190 -0.0244 0.0256 401 GLU A CD 3056 O OE1 . GLU A 401 ? 0.6424 0.6003 0.5917 -0.0126 -0.0254 0.0227 401 GLU A OE1 3057 O OE2 . GLU A 401 ? 0.6046 0.5564 0.5398 -0.0254 -0.0267 0.0266 401 GLU A OE2 3058 N N . VAL A 402 ? 0.3350 0.3594 0.3116 -0.0107 -0.0121 0.0299 402 VAL A N 3059 C CA . VAL A 402 ? 0.3229 0.3576 0.3047 -0.0034 -0.0094 0.0298 402 VAL A CA 3060 C C . VAL A 402 ? 0.3036 0.3291 0.2838 0.0034 -0.0085 0.0283 402 VAL A C 3061 O O . VAL A 402 ? 0.2943 0.3152 0.2708 0.0028 -0.0083 0.0285 402 VAL A O 3062 C CB . VAL A 402 ? 0.3282 0.3820 0.3112 -0.0044 -0.0069 0.0322 402 VAL A CB 3063 C CG1 . VAL A 402 ? 0.3315 0.3936 0.3165 0.0053 -0.0042 0.0320 402 VAL A CG1 3064 C CG2 . VAL A 402 ? 0.3387 0.4042 0.3241 -0.0107 -0.0076 0.0334 402 VAL A CG2 3065 N N . GLU A 403 ? 0.2909 0.3132 0.2726 0.0092 -0.0079 0.0266 403 GLU A N 3066 C CA . GLU A 403 ? 0.2906 0.3027 0.2691 0.0142 -0.0071 0.0249 403 GLU A CA 3067 C C . GLU A 403 ? 0.2877 0.3012 0.2642 0.0216 -0.0047 0.0247 403 GLU A C 3068 O O . GLU A 403 ? 0.3002 0.3068 0.2721 0.0254 -0.0035 0.0239 403 GLU A O 3069 C CB . GLU A 403 ? 0.2923 0.2923 0.2706 0.0128 -0.0095 0.0220 403 GLU A CB 3070 C CG . GLU A 403 ? 0.2982 0.2925 0.2753 0.0076 -0.0124 0.0216 403 GLU A CG 3071 C CD . GLU A 403 ? 0.3096 0.2953 0.2869 0.0078 -0.0149 0.0183 403 GLU A CD 3072 O OE1 . GLU A 403 ? 0.3152 0.3022 0.2954 0.0069 -0.0158 0.0174 403 GLU A OE1 3073 O OE2 . GLU A 403 ? 0.3242 0.3031 0.2988 0.0089 -0.0158 0.0164 403 GLU A OE2 3074 N N . GLY A 404 ? 0.2690 0.2896 0.2476 0.0236 -0.0042 0.0252 404 GLY A N 3075 C CA . GLY A 404 ? 0.2703 0.2901 0.2445 0.0313 -0.0023 0.0249 404 GLY A CA 3076 C C . GLY A 404 ? 0.2666 0.2731 0.2377 0.0318 -0.0029 0.0225 404 GLY A C 3077 O O . GLY A 404 ? 0.2504 0.2563 0.2257 0.0278 -0.0046 0.0216 404 GLY A O 3078 N N . ARG A 405 ? 0.2698 0.2657 0.2327 0.0363 -0.0015 0.0215 405 ARG A N 3079 C CA . ARG A 405 ? 0.2696 0.2534 0.2260 0.0375 -0.0013 0.0195 405 ARG A CA 3080 C C . ARG A 405 ? 0.2594 0.2384 0.2199 0.0308 -0.0032 0.0171 405 ARG A C 3081 O O . ARG A 405 ? 0.2477 0.2254 0.2082 0.0303 -0.0035 0.0163 405 ARG A O 3082 C CB . ARG A 405 ? 0.2842 0.2551 0.2294 0.0409 0.0002 0.0187 405 ARG A CB 3083 C CG . ARG A 405 ? 0.2957 0.2526 0.2299 0.0426 0.0009 0.0171 405 ARG A CG 3084 C CD . ARG A 405 ? 0.3155 0.2583 0.2361 0.0457 0.0025 0.0165 405 ARG A CD 3085 N NE . ARG A 405 ? 0.3249 0.2515 0.2316 0.0462 0.0032 0.0150 405 ARG A NE 3086 C CZ . ARG A 405 ? 0.3348 0.2451 0.2249 0.0494 0.0047 0.0145 405 ARG A CZ 3087 N NH1 . ARG A 405 ? 0.3373 0.2460 0.2236 0.0528 0.0055 0.0154 405 ARG A NH1 3088 N NH2 . ARG A 405 ? 0.3453 0.2396 0.2213 0.0486 0.0051 0.0132 405 ARG A NH2 3089 N N . ILE A 406 ? 0.2523 0.2290 0.2156 0.0264 -0.0044 0.0158 406 ILE A N 3090 C CA . ILE A 406 ? 0.2558 0.2294 0.2222 0.0214 -0.0063 0.0130 406 ILE A CA 3091 C C . ILE A 406 ? 0.2394 0.2208 0.2136 0.0189 -0.0082 0.0135 406 ILE A C 3092 O O . ILE A 406 ? 0.2233 0.2033 0.1988 0.0169 -0.0090 0.0117 406 ILE A O 3093 C CB . ILE A 406 ? 0.2719 0.2426 0.2391 0.0185 -0.0076 0.0110 406 ILE A CB 3094 C CG1 . ILE A 406 ? 0.2682 0.2382 0.2382 0.0145 -0.0097 0.0075 406 ILE A CG1 3095 C CG2 . ILE A 406 ? 0.2866 0.2628 0.2582 0.0178 -0.0089 0.0129 406 ILE A CG2 3096 C CD1 . ILE A 406 ? 0.2949 0.2585 0.2588 0.0130 -0.0084 0.0049 406 ILE A CD1 3097 N N . GLN A 407 ? 0.2302 0.2196 0.2087 0.0184 -0.0087 0.0160 407 GLN A N 3098 C CA . GLN A 407 ? 0.2251 0.2209 0.2092 0.0153 -0.0105 0.0167 407 GLN A CA 3099 C C . GLN A 407 ? 0.2177 0.2181 0.2024 0.0174 -0.0095 0.0176 407 GLN A C 3100 O O . GLN A 407 ? 0.2072 0.2087 0.1953 0.0149 -0.0110 0.0169 407 GLN A O 3101 C CB . GLN A 407 ? 0.2272 0.2295 0.2132 0.0127 -0.0112 0.0192 407 GLN A CB 3102 C CG . GLN A 407 ? 0.2316 0.2377 0.2210 0.0079 -0.0134 0.0198 407 GLN A CG 3103 C CD . GLN A 407 ? 0.2336 0.2453 0.2225 0.0038 -0.0138 0.0224 407 GLN A CD 3104 O OE1 . GLN A 407 ? 0.2445 0.2656 0.2354 0.0011 -0.0136 0.0242 407 GLN A OE1 3105 N NE2 . GLN A 407 ? 0.2385 0.2449 0.2240 0.0028 -0.0142 0.0223 407 GLN A NE2 3106 N N . ASP A 408 ? 0.2179 0.2208 0.1987 0.0228 -0.0073 0.0191 408 ASP A N 3107 C CA . ASP A 408 ? 0.2199 0.2260 0.1992 0.0266 -0.0065 0.0197 408 ASP A CA 3108 C C . ASP A 408 ? 0.2205 0.2161 0.1969 0.0253 -0.0069 0.0171 408 ASP A C 3109 O O . ASP A 408 ? 0.2113 0.2096 0.1903 0.0243 -0.0077 0.0170 408 ASP A O 3110 C CB . ASP A 408 ? 0.2353 0.2413 0.2072 0.0345 -0.0042 0.0207 408 ASP A CB 3111 C CG . ASP A 408 ? 0.2372 0.2568 0.2115 0.0368 -0.0033 0.0231 408 ASP A CG 3112 O OD1 . ASP A 408 ? 0.2341 0.2659 0.2159 0.0321 -0.0043 0.0244 408 ASP A OD1 3113 O OD2 . ASP A 408 ? 0.2347 0.2526 0.2023 0.0433 -0.0016 0.0236 408 ASP A OD2 3114 N N . LEU A 409 ? 0.2196 0.2041 0.1903 0.0246 -0.0063 0.0150 409 LEU A N 3115 C CA . LEU A 409 ? 0.2184 0.1938 0.1852 0.0220 -0.0064 0.0123 409 LEU A CA 3116 C C . LEU A 409 ? 0.2105 0.1897 0.1853 0.0165 -0.0087 0.0104 409 LEU A C 3117 O O . LEU A 409 ? 0.2021 0.1806 0.1773 0.0150 -0.0091 0.0094 409 LEU A O 3118 C CB . LEU A 409 ? 0.2229 0.1873 0.1813 0.0212 -0.0053 0.0103 409 LEU A CB 3119 C CG . LEU A 409 ? 0.2299 0.1844 0.1810 0.0174 -0.0048 0.0073 409 LEU A CG 3120 C CD1 . LEU A 409 ? 0.2340 0.1826 0.1775 0.0203 -0.0037 0.0081 409 LEU A CD1 3121 C CD2 . LEU A 409 ? 0.2384 0.1829 0.1800 0.0160 -0.0035 0.0057 409 LEU A CD2 3122 N N . GLU A 410 ? 0.2101 0.1927 0.1901 0.0139 -0.0104 0.0100 410 GLU A N 3123 C CA . GLU A 410 ? 0.2123 0.1978 0.1983 0.0102 -0.0130 0.0083 410 GLU A CA 3124 C C . GLU A 410 ? 0.2090 0.2003 0.1994 0.0097 -0.0139 0.0100 410 GLU A C 3125 O O . GLU A 410 ? 0.1983 0.1894 0.1905 0.0077 -0.0150 0.0082 410 GLU A O 3126 C CB . GLU A 410 ? 0.2178 0.2043 0.2062 0.0089 -0.0149 0.0081 410 GLU A CB 3127 C CG . GLU A 410 ? 0.2295 0.2115 0.2148 0.0088 -0.0149 0.0055 410 GLU A CG 3128 C CD . GLU A 410 ? 0.2496 0.2310 0.2347 0.0092 -0.0161 0.0061 410 GLU A CD 3129 O OE1 . GLU A 410 ? 0.2670 0.2507 0.2529 0.0095 -0.0161 0.0092 410 GLU A OE1 3130 O OE2 . GLU A 410 ? 0.2604 0.2397 0.2442 0.0090 -0.0171 0.0032 410 GLU A OE2 3131 N N . LYS A 411 ? 0.2026 0.2002 0.1943 0.0111 -0.0133 0.0132 411 LYS A N 3132 C CA . LYS A 411 ? 0.2073 0.2120 0.2026 0.0102 -0.0140 0.0149 411 LYS A CA 3133 C C . LYS A 411 ? 0.1974 0.2010 0.1907 0.0127 -0.0129 0.0144 411 LYS A C 3134 O O . LYS A 411 ? 0.1894 0.1952 0.1857 0.0108 -0.0141 0.0141 411 LYS A O 3135 C CB . LYS A 411 ? 0.2220 0.2366 0.2187 0.0109 -0.0133 0.0181 411 LYS A CB 3136 C CG . LYS A 411 ? 0.2427 0.2582 0.2406 0.0066 -0.0149 0.0190 411 LYS A CG 3137 C CD . LYS A 411 ? 0.2574 0.2846 0.2561 0.0061 -0.0138 0.0221 411 LYS A CD 3138 C CE . LYS A 411 ? 0.2869 0.3136 0.2848 0.0000 -0.0155 0.0231 411 LYS A CE 3139 N NZ . LYS A 411 ? 0.2985 0.3385 0.2968 -0.0027 -0.0144 0.0259 411 LYS A NZ 3140 N N . TYR A 412 ? 0.1959 0.1948 0.1826 0.0172 -0.0107 0.0145 412 TYR A N 3141 C CA . TYR A 412 ? 0.1969 0.1920 0.1785 0.0202 -0.0097 0.0142 412 TYR A CA 3142 C C . TYR A 412 ? 0.1892 0.1763 0.1694 0.0161 -0.0103 0.0111 412 TYR A C 3143 O O . TYR A 412 ? 0.1848 0.1715 0.1646 0.0158 -0.0105 0.0108 412 TYR A O 3144 C CB . TYR A 412 ? 0.2077 0.1957 0.1790 0.0262 -0.0075 0.0147 412 TYR A CB 3145 C CG . TYR A 412 ? 0.2157 0.1975 0.1781 0.0310 -0.0065 0.0148 412 TYR A CG 3146 C CD1 . TYR A 412 ? 0.2148 0.2061 0.1784 0.0362 -0.0066 0.0168 412 TYR A CD1 3147 C CD2 . TYR A 412 ? 0.2265 0.1926 0.1776 0.0302 -0.0055 0.0127 412 TYR A CD2 3148 C CE1 . TYR A 412 ? 0.2266 0.2110 0.1802 0.0420 -0.0060 0.0168 412 TYR A CE1 3149 C CE2 . TYR A 412 ? 0.2353 0.1927 0.1753 0.0347 -0.0047 0.0129 412 TYR A CE2 3150 C CZ . TYR A 412 ? 0.2348 0.2008 0.1758 0.0414 -0.0051 0.0149 412 TYR A CZ 3151 O OH . TYR A 412 ? 0.2466 0.2033 0.1753 0.0472 -0.0046 0.0150 412 TYR A OH 3152 N N . VAL A 413 ? 0.1903 0.1726 0.1698 0.0128 -0.0105 0.0087 413 VAL A N 3153 C CA . VAL A 413 ? 0.1902 0.1685 0.1691 0.0083 -0.0111 0.0053 413 VAL A CA 3154 C C . VAL A 413 ? 0.1834 0.1685 0.1705 0.0059 -0.0133 0.0048 413 VAL A C 3155 O O . VAL A 413 ? 0.1752 0.1589 0.1615 0.0041 -0.0134 0.0034 413 VAL A O 3156 C CB . VAL A 413 ? 0.1915 0.1674 0.1695 0.0056 -0.0112 0.0026 413 VAL A CB 3157 C CG1 . VAL A 413 ? 0.1929 0.1703 0.1728 0.0009 -0.0123 -0.0012 413 VAL A CG1 3158 C CG2 . VAL A 413 ? 0.2046 0.1710 0.1719 0.0067 -0.0088 0.0025 413 VAL A CG2 3159 N N . GLU A 414 ? 0.1827 0.1738 0.1759 0.0056 -0.0151 0.0062 414 GLU A N 3160 C CA . GLU A 414 ? 0.1865 0.1817 0.1852 0.0032 -0.0176 0.0057 414 GLU A CA 3161 C C . GLU A 414 ? 0.1857 0.1847 0.1858 0.0039 -0.0174 0.0080 414 GLU A C 3162 O O . GLU A 414 ? 0.1788 0.1781 0.1806 0.0021 -0.0184 0.0067 414 GLU A O 3163 C CB . GLU A 414 ? 0.1910 0.1881 0.1923 0.0022 -0.0197 0.0066 414 GLU A CB 3164 C CG . GLU A 414 ? 0.1971 0.1949 0.2010 0.0000 -0.0226 0.0058 414 GLU A CG 3165 C CD . GLU A 414 ? 0.1967 0.1926 0.2007 -0.0003 -0.0240 0.0015 414 GLU A CD 3166 O OE1 . GLU A 414 ? 0.2125 0.2076 0.2150 0.0000 -0.0226 -0.0009 414 GLU A OE1 3167 O OE2 . GLU A 414 ? 0.1984 0.1941 0.2033 -0.0011 -0.0264 0.0005 414 GLU A OE2 3168 N N . ASP A 415 ? 0.1948 0.1980 0.1942 0.0067 -0.0162 0.0110 415 ASP A N 3169 C CA . ASP A 415 ? 0.2031 0.2121 0.2035 0.0083 -0.0160 0.0130 415 ASP A CA 3170 C C . ASP A 415 ? 0.1981 0.2008 0.1939 0.0097 -0.0150 0.0114 415 ASP A C 3171 O O . ASP A 415 ? 0.1904 0.1955 0.1882 0.0087 -0.0159 0.0114 415 ASP A O 3172 C CB . ASP A 415 ? 0.2240 0.2400 0.2229 0.0126 -0.0145 0.0158 415 ASP A CB 3173 C CG . ASP A 415 ? 0.2450 0.2718 0.2468 0.0136 -0.0149 0.0178 415 ASP A CG 3174 O OD1 . ASP A 415 ? 0.2714 0.3034 0.2781 0.0089 -0.0167 0.0183 415 ASP A OD1 3175 O OD2 . ASP A 415 ? 0.2799 0.3093 0.2777 0.0195 -0.0135 0.0188 415 ASP A OD2 3176 N N . THR A 416 ? 0.1919 0.1859 0.1803 0.0115 -0.0132 0.0101 416 THR A N 3177 C CA . THR A 416 ? 0.1943 0.1793 0.1750 0.0118 -0.0120 0.0085 416 THR A CA 3178 C C . THR A 416 ? 0.1820 0.1664 0.1661 0.0064 -0.0133 0.0057 416 THR A C 3179 O O . THR A 416 ? 0.1728 0.1561 0.1557 0.0060 -0.0134 0.0055 416 THR A O 3180 C CB . THR A 416 ? 0.2012 0.1750 0.1714 0.0128 -0.0100 0.0074 416 THR A CB 3181 O OG1 . THR A 416 ? 0.2058 0.1797 0.1715 0.0192 -0.0089 0.0099 416 THR A OG1 3182 C CG2 . THR A 416 ? 0.2084 0.1703 0.1679 0.0110 -0.0088 0.0054 416 THR A CG2 3183 N N . LYS A 417 ? 0.1734 0.1593 0.1616 0.0029 -0.0143 0.0035 417 LYS A N 3184 C CA . LYS A 417 ? 0.1698 0.1573 0.1615 -0.0011 -0.0157 0.0004 417 LYS A CA 3185 C C . LYS A 417 ? 0.1610 0.1540 0.1587 -0.0014 -0.0176 0.0015 417 LYS A C 3186 O O . LYS A 417 ? 0.1531 0.1455 0.1505 -0.0032 -0.0178 0.0000 417 LYS A O 3187 C CB . LYS A 417 ? 0.1680 0.1580 0.1628 -0.0029 -0.0169 -0.0019 417 LYS A CB 3188 C CG . LYS A 417 ? 0.1687 0.1627 0.1673 -0.0055 -0.0188 -0.0055 417 LYS A CG 3189 C CD . LYS A 417 ? 0.1720 0.1692 0.1725 -0.0056 -0.0202 -0.0083 417 LYS A CD 3190 C CE . LYS A 417 ? 0.1727 0.1753 0.1765 -0.0062 -0.0226 -0.0119 417 LYS A CE 3191 N NZ . LYS A 417 ? 0.1805 0.1865 0.1854 -0.0043 -0.0247 -0.0145 417 LYS A NZ 3192 N N . ILE A 418 ? 0.1577 0.1558 0.1598 -0.0003 -0.0190 0.0042 418 ILE A N 3193 C CA . ILE A 418 ? 0.1536 0.1562 0.1602 -0.0017 -0.0210 0.0052 418 ILE A CA 3194 C C . ILE A 418 ? 0.1518 0.1557 0.1572 -0.0004 -0.0202 0.0067 418 ILE A C 3195 O O . ILE A 418 ? 0.1452 0.1498 0.1524 -0.0022 -0.0213 0.0059 418 ILE A O 3196 C CB . ILE A 418 ? 0.1560 0.1629 0.1653 -0.0023 -0.0225 0.0077 418 ILE A CB 3197 C CG1 . ILE A 418 ? 0.1577 0.1612 0.1667 -0.0033 -0.0239 0.0059 418 ILE A CG1 3198 C CG2 . ILE A 418 ? 0.1521 0.1631 0.1639 -0.0047 -0.0243 0.0093 418 ILE A CG2 3199 C CD1 . ILE A 418 ? 0.1654 0.1705 0.1744 -0.0042 -0.0249 0.0084 418 ILE A CD1 3200 N N . ASP A 419 ? 0.1562 0.1601 0.1577 0.0033 -0.0183 0.0086 419 ASP A N 3201 C CA . ASP A 419 ? 0.1592 0.1639 0.1580 0.0060 -0.0176 0.0099 419 ASP A CA 3202 C C . ASP A 419 ? 0.1573 0.1534 0.1511 0.0045 -0.0170 0.0072 419 ASP A C 3203 O O . ASP A 419 ? 0.1576 0.1546 0.1516 0.0043 -0.0176 0.0074 419 ASP A O 3204 C CB . ASP A 419 ? 0.1710 0.1763 0.1643 0.0121 -0.0159 0.0120 419 ASP A CB 3205 C CG . ASP A 419 ? 0.1798 0.1983 0.1785 0.0137 -0.0165 0.0149 419 ASP A CG 3206 O OD1 . ASP A 419 ? 0.1817 0.2075 0.1873 0.0090 -0.0183 0.0155 419 ASP A OD1 3207 O OD2 . ASP A 419 ? 0.1956 0.2169 0.1903 0.0194 -0.0151 0.0163 419 ASP A OD2 3208 N N . LEU A 420 ? 0.1587 0.1471 0.1475 0.0028 -0.0157 0.0048 420 LEU A N 3209 C CA . LEU A 420 ? 0.1630 0.1437 0.1457 -0.0002 -0.0148 0.0020 420 LEU A CA 3210 C C . LEU A 420 ? 0.1572 0.1427 0.1466 -0.0045 -0.0165 -0.0001 420 LEU A C 3211 O O . LEU A 420 ? 0.1599 0.1433 0.1471 -0.0058 -0.0165 -0.0009 420 LEU A O 3212 C CB . LEU A 420 ? 0.1678 0.1402 0.1424 -0.0022 -0.0130 0.0000 420 LEU A CB 3213 C CG . LEU A 420 ? 0.1781 0.1404 0.1408 0.0022 -0.0110 0.0017 420 LEU A CG 3214 C CD1 . LEU A 420 ? 0.1844 0.1398 0.1404 0.0004 -0.0095 0.0003 420 LEU A CD1 3215 C CD2 . LEU A 420 ? 0.1888 0.1408 0.1403 0.0026 -0.0101 0.0015 420 LEU A CD2 3216 N N . TRP A 421 ? 0.1537 0.1451 0.1503 -0.0059 -0.0183 -0.0011 421 TRP A N 3217 C CA . TRP A 421 ? 0.1495 0.1453 0.1515 -0.0084 -0.0204 -0.0032 421 TRP A CA 3218 C C . TRP A 421 ? 0.1486 0.1475 0.1541 -0.0077 -0.0220 -0.0009 421 TRP A C 3219 O O . TRP A 421 ? 0.1461 0.1455 0.1526 -0.0095 -0.0229 -0.0025 421 TRP A O 3220 C CB . TRP A 421 ? 0.1439 0.1431 0.1499 -0.0087 -0.0222 -0.0050 421 TRP A CB 3221 C CG . TRP A 421 ? 0.1444 0.1435 0.1478 -0.0107 -0.0211 -0.0090 421 TRP A CG 3222 C CD1 . TRP A 421 ? 0.1479 0.1461 0.1490 -0.0107 -0.0201 -0.0098 421 TRP A CD1 3223 C CD2 . TRP A 421 ? 0.1457 0.1466 0.1475 -0.0141 -0.0206 -0.0128 421 TRP A CD2 3224 N NE1 . TRP A 421 ? 0.1498 0.1500 0.1484 -0.0141 -0.0191 -0.0141 421 TRP A NE1 3225 C CE2 . TRP A 421 ? 0.1510 0.1534 0.1498 -0.0164 -0.0193 -0.0161 421 TRP A CE2 3226 C CE3 . TRP A 421 ? 0.1465 0.1488 0.1491 -0.0157 -0.0211 -0.0140 421 TRP A CE3 3227 C CZ2 . TRP A 421 ? 0.1516 0.1582 0.1483 -0.0209 -0.0183 -0.0205 421 TRP A CZ2 3228 C CZ3 . TRP A 421 ? 0.1507 0.1564 0.1512 -0.0196 -0.0201 -0.0184 421 TRP A CZ3 3229 C CH2 . TRP A 421 ? 0.1533 0.1617 0.1508 -0.0225 -0.0187 -0.0215 421 TRP A CH2 3230 N N . SER A 422 ? 0.1484 0.1505 0.1556 -0.0056 -0.0224 0.0026 422 SER A N 3231 C CA . SER A 422 ? 0.1502 0.1569 0.1603 -0.0058 -0.0237 0.0049 422 SER A CA 3232 C C . SER A 422 ? 0.1536 0.1583 0.1602 -0.0046 -0.0226 0.0050 422 SER A C 3233 O O . SER A 422 ? 0.1494 0.1556 0.1579 -0.0062 -0.0239 0.0048 422 SER A O 3234 C CB . SER A 422 ? 0.1517 0.1649 0.1636 -0.0044 -0.0239 0.0084 422 SER A CB 3235 O OG . SER A 422 ? 0.1548 0.1683 0.1685 -0.0061 -0.0251 0.0085 422 SER A OG 3236 N N . TYR A 423 ? 0.1586 0.1579 0.1585 -0.0018 -0.0204 0.0051 423 TYR A N 3237 C CA . TYR A 423 ? 0.1673 0.1608 0.1604 -0.0003 -0.0193 0.0048 423 TYR A CA 3238 C C . TYR A 423 ? 0.1650 0.1542 0.1571 -0.0050 -0.0193 0.0015 423 TYR A C 3239 O O . TYR A 423 ? 0.1610 0.1505 0.1533 -0.0057 -0.0200 0.0014 423 TYR A O 3240 C CB . TYR A 423 ? 0.1778 0.1627 0.1603 0.0036 -0.0170 0.0053 423 TYR A CB 3241 C CG . TYR A 423 ? 0.1929 0.1685 0.1654 0.0050 -0.0160 0.0049 423 TYR A CG 3242 C CD1 . TYR A 423 ? 0.1992 0.1777 0.1698 0.0103 -0.0167 0.0071 423 TYR A CD1 3243 C CD2 . TYR A 423 ? 0.1998 0.1648 0.1644 0.0003 -0.0147 0.0019 423 TYR A CD2 3244 C CE1 . TYR A 423 ? 0.2170 0.1859 0.1774 0.0121 -0.0162 0.0067 423 TYR A CE1 3245 C CE2 . TYR A 423 ? 0.2128 0.1676 0.1665 0.0008 -0.0140 0.0016 423 TYR A CE2 3246 C CZ . TYR A 423 ? 0.2245 0.1802 0.1757 0.0072 -0.0148 0.0041 423 TYR A CZ 3247 O OH . TYR A 423 ? 0.2413 0.1860 0.1806 0.0088 -0.0144 0.0039 423 TYR A OH 3248 N N . ASN A 424 ? 0.1633 0.1502 0.1547 -0.0082 -0.0186 -0.0014 424 ASN A N 3249 C CA . ASN A 424 ? 0.1653 0.1515 0.1562 -0.0129 -0.0186 -0.0051 424 ASN A CA 3250 C C . ASN A 424 ? 0.1612 0.1539 0.1598 -0.0138 -0.0211 -0.0055 424 ASN A C 3251 O O . ASN A 424 ? 0.1632 0.1550 0.1605 -0.0158 -0.0211 -0.0069 424 ASN A O 3252 C CB . ASN A 424 ? 0.1660 0.1536 0.1570 -0.0159 -0.0180 -0.0085 424 ASN A CB 3253 C CG . ASN A 424 ? 0.1761 0.1554 0.1572 -0.0171 -0.0154 -0.0090 424 ASN A CG 3254 O OD1 . ASN A 424 ? 0.1853 0.1551 0.1568 -0.0164 -0.0138 -0.0076 424 ASN A OD1 3255 N ND2 . ASN A 424 ? 0.1743 0.1560 0.1561 -0.0190 -0.0150 -0.0111 424 ASN A ND2 3256 N N . ALA A 425 ? 0.1578 0.1558 0.1628 -0.0124 -0.0232 -0.0041 425 ALA A N 3257 C CA . ALA A 425 ? 0.1609 0.1626 0.1708 -0.0133 -0.0259 -0.0043 425 ALA A CA 3258 C C . ALA A 425 ? 0.1678 0.1698 0.1775 -0.0130 -0.0263 -0.0020 425 ALA A C 3259 O O . ALA A 425 ? 0.1686 0.1707 0.1790 -0.0147 -0.0273 -0.0034 425 ALA A O 3260 C CB . ALA A 425 ? 0.1565 0.1606 0.1698 -0.0125 -0.0281 -0.0028 425 ALA A CB 3261 N N . GLU A 426 ? 0.1734 0.1766 0.1821 -0.0106 -0.0255 0.0013 426 GLU A N 3262 C CA . GLU A 426 ? 0.1892 0.1947 0.1976 -0.0094 -0.0260 0.0035 426 GLU A CA 3263 C C . GLU A 426 ? 0.1836 0.1831 0.1867 -0.0098 -0.0247 0.0017 426 GLU A C 3264 O O . GLU A 426 ? 0.1797 0.1802 0.1840 -0.0112 -0.0259 0.0015 426 GLU A O 3265 C CB . GLU A 426 ? 0.2037 0.2133 0.2109 -0.0054 -0.0251 0.0067 426 GLU A CB 3266 C CG . GLU A 426 ? 0.2215 0.2380 0.2300 -0.0041 -0.0262 0.0091 426 GLU A CG 3267 C CD . GLU A 426 ? 0.2316 0.2559 0.2462 -0.0081 -0.0286 0.0104 426 GLU A CD 3268 O OE1 . GLU A 426 ? 0.2405 0.2668 0.2574 -0.0100 -0.0292 0.0110 426 GLU A OE1 3269 O OE2 . GLU A 426 ? 0.2519 0.2793 0.2678 -0.0098 -0.0300 0.0109 426 GLU A OE2 3270 N N . LEU A 427 ? 0.1871 0.1793 0.1830 -0.0092 -0.0224 0.0004 427 LEU A N 3271 C CA . LEU A 427 ? 0.1918 0.1760 0.1799 -0.0108 -0.0211 -0.0013 427 LEU A CA 3272 C C . LEU A 427 ? 0.1870 0.1728 0.1781 -0.0158 -0.0216 -0.0048 427 LEU A C 3273 O O . LEU A 427 ? 0.1844 0.1684 0.1735 -0.0172 -0.0218 -0.0054 427 LEU A O 3274 C CB . LEU A 427 ? 0.2015 0.1757 0.1789 -0.0105 -0.0185 -0.0021 427 LEU A CB 3275 C CG . LEU A 427 ? 0.2143 0.1773 0.1799 -0.0129 -0.0168 -0.0038 427 LEU A CG 3276 C CD1 . LEU A 427 ? 0.2171 0.1769 0.1783 -0.0086 -0.0175 -0.0015 427 LEU A CD1 3277 C CD2 . LEU A 427 ? 0.2299 0.1810 0.1827 -0.0138 -0.0144 -0.0046 427 LEU A CD2 3278 N N . LEU A 428 ? 0.1843 0.1742 0.1797 -0.0179 -0.0220 -0.0072 428 LEU A N 3279 C CA . LEU A 428 ? 0.1903 0.1838 0.1882 -0.0214 -0.0226 -0.0111 428 LEU A CA 3280 C C . LEU A 428 ? 0.1899 0.1867 0.1925 -0.0210 -0.0250 -0.0106 428 LEU A C 3281 O O . LEU A 428 ? 0.1885 0.1851 0.1898 -0.0233 -0.0249 -0.0126 428 LEU A O 3282 C CB . LEU A 428 ? 0.1916 0.1905 0.1935 -0.0216 -0.0233 -0.0136 428 LEU A CB 3283 C CG . LEU A 428 ? 0.1940 0.1993 0.1982 -0.0239 -0.0240 -0.0183 428 LEU A CG 3284 C CD1 . LEU A 428 ? 0.2107 0.2150 0.2089 -0.0289 -0.0215 -0.0214 428 LEU A CD1 3285 C CD2 . LEU A 428 ? 0.1977 0.2086 0.2047 -0.0227 -0.0248 -0.0207 428 LEU A CD2 3286 N N . VAL A 429 ? 0.1944 0.1939 0.2017 -0.0187 -0.0272 -0.0077 429 VAL A N 3287 C CA . VAL A 429 ? 0.2000 0.2014 0.2104 -0.0190 -0.0296 -0.0071 429 VAL A CA 3288 C C . VAL A 429 ? 0.2049 0.2046 0.2130 -0.0191 -0.0292 -0.0052 429 VAL A C 3289 O O . VAL A 429 ? 0.2007 0.2004 0.2092 -0.0206 -0.0303 -0.0065 429 VAL A O 3290 C CB . VAL A 429 ? 0.2080 0.2116 0.2217 -0.0182 -0.0321 -0.0047 429 VAL A CB 3291 C CG1 . VAL A 429 ? 0.2290 0.2327 0.2435 -0.0195 -0.0347 -0.0038 429 VAL A CG1 3292 C CG2 . VAL A 429 ? 0.2150 0.2187 0.2293 -0.0175 -0.0329 -0.0073 429 VAL A CG2 3293 N N . ALA A 430 ? 0.2037 0.2018 0.2086 -0.0169 -0.0278 -0.0026 430 ALA A N 3294 C CA . ALA A 430 ? 0.2094 0.2053 0.2105 -0.0157 -0.0275 -0.0012 430 ALA A CA 3295 C C . ALA A 430 ? 0.2156 0.2047 0.2106 -0.0182 -0.0259 -0.0042 430 ALA A C 3296 O O . ALA A 430 ? 0.2095 0.1978 0.2036 -0.0191 -0.0266 -0.0043 430 ALA A O 3297 C CB . ALA A 430 ? 0.2104 0.2055 0.2072 -0.0111 -0.0263 0.0016 430 ALA A CB 3298 N N . LEU A 431 ? 0.2134 0.1982 0.2037 -0.0201 -0.0238 -0.0065 431 LEU A N 3299 C CA . LEU A 431 ? 0.2207 0.1999 0.2042 -0.0243 -0.0220 -0.0098 431 LEU A CA 3300 C C . LEU A 431 ? 0.2147 0.2003 0.2038 -0.0276 -0.0232 -0.0130 431 LEU A C 3301 O O . LEU A 431 ? 0.2189 0.2023 0.2047 -0.0300 -0.0228 -0.0142 431 LEU A O 3302 C CB . LEU A 431 ? 0.2222 0.1967 0.1989 -0.0271 -0.0194 -0.0119 431 LEU A CB 3303 C CG . LEU A 431 ? 0.2376 0.2014 0.2036 -0.0244 -0.0177 -0.0096 431 LEU A CG 3304 C CD1 . LEU A 431 ? 0.2428 0.2025 0.2025 -0.0285 -0.0154 -0.0121 431 LEU A CD1 3305 C CD2 . LEU A 431 ? 0.2493 0.2019 0.2038 -0.0237 -0.0170 -0.0086 431 LEU A CD2 3306 N N . GLU A 432 ? 0.2177 0.2106 0.2139 -0.0272 -0.0246 -0.0144 432 GLU A N 3307 C CA . GLU A 432 ? 0.2261 0.2251 0.2267 -0.0284 -0.0262 -0.0176 432 GLU A CA 3308 C C . GLU A 432 ? 0.2178 0.2162 0.2205 -0.0273 -0.0284 -0.0157 432 GLU A C 3309 O O . GLU A 432 ? 0.2167 0.2161 0.2186 -0.0292 -0.0286 -0.0181 432 GLU A O 3310 C CB . GLU A 432 ? 0.2371 0.2420 0.2428 -0.0264 -0.0279 -0.0192 432 GLU A CB 3311 C CG . GLU A 432 ? 0.2613 0.2695 0.2654 -0.0281 -0.0259 -0.0223 432 GLU A CG 3312 C CD . GLU A 432 ? 0.2915 0.3064 0.2943 -0.0317 -0.0248 -0.0275 432 GLU A CD 3313 O OE1 . GLU A 432 ? 0.3103 0.3263 0.3127 -0.0330 -0.0252 -0.0288 432 GLU A OE1 3314 O OE2 . GLU A 432 ? 0.3541 0.3744 0.3561 -0.0336 -0.0235 -0.0306 432 GLU A OE2 3315 N N . ASN A 433 ? 0.2046 0.2020 0.2094 -0.0248 -0.0299 -0.0117 433 ASN A N 3316 C CA . ASN A 433 ? 0.2022 0.1997 0.2085 -0.0246 -0.0321 -0.0098 433 ASN A CA 3317 C C . ASN A 433 ? 0.2133 0.2071 0.2151 -0.0255 -0.0308 -0.0093 433 ASN A C 3318 O O . ASN A 433 ? 0.2091 0.2028 0.2110 -0.0268 -0.0319 -0.0102 433 ASN A O 3319 C CB . ASN A 433 ? 0.1951 0.1948 0.2042 -0.0230 -0.0338 -0.0058 433 ASN A CB 3320 C CG . ASN A 433 ? 0.1877 0.1889 0.1996 -0.0229 -0.0358 -0.0061 433 ASN A CG 3321 O OD1 . ASN A 433 ? 0.1948 0.1956 0.2066 -0.0227 -0.0364 -0.0094 433 ASN A OD1 3322 N ND2 . ASN A 433 ? 0.1769 0.1801 0.1902 -0.0227 -0.0368 -0.0027 433 ASN A ND2 3323 N N . GLN A 434 ? 0.2158 0.2051 0.2120 -0.0246 -0.0286 -0.0082 434 GLN A N 3324 C CA . GLN A 434 ? 0.2326 0.2155 0.2215 -0.0252 -0.0273 -0.0082 434 GLN A CA 3325 C C . GLN A 434 ? 0.2362 0.2177 0.2224 -0.0298 -0.0262 -0.0123 434 GLN A C 3326 O O . GLN A 434 ? 0.2251 0.2046 0.2091 -0.0311 -0.0266 -0.0127 434 GLN A O 3327 C CB . GLN A 434 ? 0.2574 0.2325 0.2373 -0.0230 -0.0252 -0.0068 434 GLN A CB 3328 C CG . GLN A 434 ? 0.2824 0.2484 0.2522 -0.0225 -0.0244 -0.0064 434 GLN A CG 3329 C CD . GLN A 434 ? 0.2983 0.2688 0.2716 -0.0189 -0.0267 -0.0036 434 GLN A CD 3330 O OE1 . GLN A 434 ? 0.3099 0.2860 0.2866 -0.0144 -0.0279 -0.0007 434 GLN A OE1 3331 N NE2 . GLN A 434 ? 0.3212 0.2909 0.2943 -0.0213 -0.0275 -0.0046 434 GLN A NE2 3332 N N . HIS A 435 ? 0.2345 0.2185 0.2210 -0.0325 -0.0249 -0.0155 435 HIS A N 3333 C CA . HIS A 435 ? 0.2530 0.2394 0.2375 -0.0373 -0.0236 -0.0200 435 HIS A CA 3334 C C . HIS A 435 ? 0.2422 0.2355 0.2331 -0.0367 -0.0260 -0.0217 435 HIS A C 3335 O O . HIS A 435 ? 0.2508 0.2443 0.2392 -0.0396 -0.0254 -0.0240 435 HIS A O 3336 C CB . HIS A 435 ? 0.2623 0.2528 0.2461 -0.0400 -0.0218 -0.0232 435 HIS A CB 3337 C CG . HIS A 435 ? 0.2845 0.2812 0.2664 -0.0455 -0.0203 -0.0284 435 HIS A CG 3338 N ND1 . HIS A 435 ? 0.2870 0.2958 0.2761 -0.0445 -0.0218 -0.0319 435 HIS A ND1 3339 C CD2 . HIS A 435 ? 0.3118 0.3045 0.2840 -0.0523 -0.0174 -0.0307 435 HIS A CD2 3340 C CE1 . HIS A 435 ? 0.3083 0.3234 0.2941 -0.0501 -0.0198 -0.0365 435 HIS A CE1 3341 N NE2 . HIS A 435 ? 0.3187 0.3237 0.2940 -0.0558 -0.0170 -0.0357 435 HIS A NE2 3342 N N . THR A 436 ? 0.2304 0.2278 0.2282 -0.0330 -0.0287 -0.0205 436 THR A N 3343 C CA . THR A 436 ? 0.2255 0.2263 0.2269 -0.0317 -0.0315 -0.0217 436 THR A CA 3344 C C . THR A 436 ? 0.2325 0.2291 0.2325 -0.0321 -0.0324 -0.0193 436 THR A C 3345 O O . THR A 436 ? 0.2323 0.2300 0.2317 -0.0331 -0.0331 -0.0216 436 THR A O 3346 C CB . THR A 436 ? 0.2237 0.2262 0.2294 -0.0282 -0.0343 -0.0205 436 THR A CB 3347 O OG1 . THR A 436 ? 0.2205 0.2279 0.2274 -0.0274 -0.0336 -0.0235 436 THR A OG1 3348 C CG2 . THR A 436 ? 0.2169 0.2190 0.2232 -0.0266 -0.0376 -0.0213 436 THR A CG2 3349 N N . ILE A 437 ? 0.2272 0.2198 0.2263 -0.0309 -0.0326 -0.0151 437 ILE A N 3350 C CA . ILE A 437 ? 0.2500 0.2397 0.2472 -0.0310 -0.0334 -0.0130 437 ILE A CA 3351 C C . ILE A 437 ? 0.2600 0.2454 0.2507 -0.0338 -0.0311 -0.0152 437 ILE A C 3352 O O . ILE A 437 ? 0.2408 0.2253 0.2305 -0.0350 -0.0319 -0.0160 437 ILE A O 3353 C CB . ILE A 437 ? 0.2535 0.2423 0.2503 -0.0284 -0.0338 -0.0085 437 ILE A CB 3354 C CG1 . ILE A 437 ? 0.2604 0.2542 0.2629 -0.0273 -0.0360 -0.0062 437 ILE A CG1 3355 C CG2 . ILE A 437 ? 0.2611 0.2479 0.2550 -0.0280 -0.0345 -0.0067 437 ILE A CG2 3356 C CD1 . ILE A 437 ? 0.2654 0.2605 0.2702 -0.0287 -0.0390 -0.0061 437 ILE A CD1 3357 N N . ASP A 438 ? 0.2604 0.2420 0.2454 -0.0354 -0.0282 -0.0163 438 ASP A N 3358 C CA . ASP A 438 ? 0.2762 0.2517 0.2523 -0.0393 -0.0258 -0.0184 438 ASP A CA 3359 C C . ASP A 438 ? 0.2663 0.2479 0.2440 -0.0434 -0.0254 -0.0230 438 ASP A C 3360 O O . ASP A 438 ? 0.2757 0.2545 0.2492 -0.0458 -0.0250 -0.0240 438 ASP A O 3361 C CB . ASP A 438 ? 0.3066 0.2747 0.2735 -0.0413 -0.0229 -0.0186 438 ASP A CB 3362 C CG . ASP A 438 ? 0.3168 0.2772 0.2788 -0.0364 -0.0231 -0.0144 438 ASP A CG 3363 O OD1 . ASP A 438 ? 0.3427 0.3041 0.3075 -0.0322 -0.0252 -0.0115 438 ASP A OD1 3364 O OD2 . ASP A 438 ? 0.3453 0.2990 0.2997 -0.0368 -0.0211 -0.0144 438 ASP A OD2 3365 N N . LEU A 439 ? 0.2586 0.2492 0.2418 -0.0436 -0.0256 -0.0260 439 LEU A N 3366 C CA . LEU A 439 ? 0.2625 0.2618 0.2472 -0.0463 -0.0252 -0.0310 439 LEU A CA 3367 C C . LEU A 439 ? 0.2632 0.2647 0.2520 -0.0434 -0.0282 -0.0310 439 LEU A C 3368 O O . LEU A 439 ? 0.2744 0.2794 0.2616 -0.0458 -0.0277 -0.0341 439 LEU A O 3369 C CB . LEU A 439 ? 0.2631 0.2728 0.2522 -0.0457 -0.0251 -0.0344 439 LEU A CB 3370 C CG . LEU A 439 ? 0.2577 0.2728 0.2543 -0.0395 -0.0284 -0.0344 439 LEU A CG 3371 C CD1 . LEU A 439 ? 0.2551 0.2777 0.2542 -0.0370 -0.0305 -0.0380 439 LEU A CD1 3372 C CD2 . LEU A 439 ? 0.2638 0.2846 0.2624 -0.0388 -0.0276 -0.0359 439 LEU A CD2 3373 N N . THR A 440 ? 0.2527 0.2518 0.2458 -0.0390 -0.0311 -0.0275 440 THR A N 3374 C CA . THR A 440 ? 0.2588 0.2576 0.2538 -0.0369 -0.0341 -0.0272 440 THR A CA 3375 C C . THR A 440 ? 0.2710 0.2636 0.2623 -0.0388 -0.0339 -0.0251 440 THR A C 3376 O O . THR A 440 ? 0.2891 0.2824 0.2795 -0.0394 -0.0347 -0.0269 440 THR A O 3377 C CB . THR A 440 ? 0.2400 0.2375 0.2386 -0.0330 -0.0375 -0.0245 440 THR A CB 3378 O OG1 . THR A 440 ? 0.2354 0.2294 0.2346 -0.0328 -0.0372 -0.0201 440 THR A OG1 3379 C CG2 . THR A 440 ? 0.2480 0.2507 0.2487 -0.0301 -0.0384 -0.0276 440 THR A CG2 3380 N N . ASP A 441 ? 0.2702 0.2571 0.2587 -0.0390 -0.0329 -0.0215 441 ASP A N 3381 C CA . ASP A 441 ? 0.2840 0.2645 0.2670 -0.0402 -0.0324 -0.0198 441 ASP A CA 3382 C C . ASP A 441 ? 0.2996 0.2789 0.2766 -0.0448 -0.0297 -0.0237 441 ASP A C 3383 O O . ASP A 441 ? 0.2848 0.2619 0.2591 -0.0462 -0.0300 -0.0243 441 ASP A O 3384 C CB . ASP A 441 ? 0.2934 0.2677 0.2720 -0.0384 -0.0315 -0.0161 441 ASP A CB 3385 C CG . ASP A 441 ? 0.3056 0.2828 0.2893 -0.0344 -0.0340 -0.0120 441 ASP A CG 3386 O OD1 . ASP A 441 ? 0.3092 0.2909 0.2987 -0.0341 -0.0366 -0.0115 441 ASP A OD1 3387 O OD2 . ASP A 441 ? 0.3100 0.2848 0.2908 -0.0317 -0.0335 -0.0092 441 ASP A OD2 3388 N N . SER A 442 ? 0.3066 0.2875 0.2807 -0.0478 -0.0270 -0.0264 442 SER A N 3389 C CA . SER A 442 ? 0.3236 0.3043 0.2906 -0.0540 -0.0241 -0.0302 442 SER A CA 3390 C C . SER A 442 ? 0.3147 0.3051 0.2859 -0.0550 -0.0249 -0.0342 442 SER A C 3391 O O . SER A 442 ? 0.3158 0.3040 0.2815 -0.0589 -0.0237 -0.0359 442 SER A O 3392 C CB . SER A 442 ? 0.3337 0.3160 0.2967 -0.0582 -0.0212 -0.0326 442 SER A CB 3393 O OG . SER A 442 ? 0.3492 0.3328 0.3047 -0.0658 -0.0183 -0.0367 442 SER A OG 3394 N N . GLU A 443 ? 0.3111 0.3112 0.2905 -0.0511 -0.0270 -0.0360 443 GLU A N 3395 C CA . GLU A 443 ? 0.3158 0.3243 0.2978 -0.0502 -0.0282 -0.0399 443 GLU A CA 3396 C C . GLU A 443 ? 0.3180 0.3195 0.2984 -0.0493 -0.0300 -0.0377 443 GLU A C 3397 O O . GLU A 443 ? 0.3245 0.3291 0.3026 -0.0516 -0.0294 -0.0405 443 GLU A O 3398 C CB . GLU A 443 ? 0.3213 0.3383 0.3097 -0.0444 -0.0308 -0.0418 443 GLU A CB 3399 C CG . GLU A 443 ? 0.3360 0.3635 0.3262 -0.0451 -0.0291 -0.0454 443 GLU A CG 3400 C CD . GLU A 443 ? 0.3505 0.3883 0.3374 -0.0513 -0.0257 -0.0506 443 GLU A CD 3401 O OE1 . GLU A 443 ? 0.3608 0.4036 0.3466 -0.0521 -0.0258 -0.0534 443 GLU A OE1 3402 O OE2 . GLU A 443 ? 0.3631 0.4045 0.3479 -0.0561 -0.0230 -0.0520 443 GLU A OE2 3403 N N . MET A 444 ? 0.3173 0.3106 0.2988 -0.0464 -0.0322 -0.0327 444 MET A N 3404 C CA . MET A 444 ? 0.3134 0.3008 0.2933 -0.0459 -0.0340 -0.0304 444 MET A CA 3405 C C . MET A 444 ? 0.3322 0.3138 0.3045 -0.0504 -0.0314 -0.0306 444 MET A C 3406 O O . MET A 444 ? 0.2925 0.2736 0.2624 -0.0520 -0.0316 -0.0321 444 MET A O 3407 C CB . MET A 444 ? 0.3098 0.2921 0.2920 -0.0429 -0.0365 -0.0252 444 MET A CB 3408 C CG . MET A 444 ? 0.3172 0.2951 0.2981 -0.0426 -0.0387 -0.0228 444 MET A CG 3409 S SD . MET A 444 ? 0.3118 0.2915 0.2948 -0.0407 -0.0423 -0.0247 444 MET A SD 3410 C CE . MET A 444 ? 0.3369 0.3201 0.3166 -0.0429 -0.0401 -0.0300 444 MET A CE 3411 N N . ASN A 445 ? 0.3296 0.3053 0.2964 -0.0524 -0.0291 -0.0291 445 ASN A N 3412 C CA . ASN A 445 ? 0.3541 0.3205 0.3103 -0.0565 -0.0268 -0.0290 445 ASN A CA 3413 C C . ASN A 445 ? 0.3482 0.3186 0.2997 -0.0630 -0.0240 -0.0340 445 ASN A C 3414 O O . ASN A 445 ? 0.3604 0.3252 0.3049 -0.0662 -0.0232 -0.0345 445 ASN A O 3415 C CB . ASN A 445 ? 0.3874 0.3445 0.3360 -0.0567 -0.0250 -0.0266 445 ASN A CB 3416 C CG . ASN A 445 ? 0.4188 0.3726 0.3703 -0.0503 -0.0274 -0.0217 445 ASN A CG 3417 O OD1 . ASN A 445 ? 0.4444 0.3987 0.3992 -0.0473 -0.0300 -0.0195 445 ASN A OD1 3418 N ND2 . ASN A 445 ? 0.4367 0.3876 0.3862 -0.0484 -0.0265 -0.0201 445 ASN A ND2 3419 N N . LYS A 446 ? 0.3451 0.3265 0.3005 -0.0650 -0.0227 -0.0377 446 LYS A N 3420 C CA . LYS A 446 ? 0.3793 0.3688 0.3310 -0.0716 -0.0200 -0.0431 446 LYS A CA 3421 C C . LYS A 446 ? 0.3690 0.3661 0.3251 -0.0698 -0.0217 -0.0454 446 LYS A C 3422 O O . LYS A 446 ? 0.3689 0.3675 0.3193 -0.0753 -0.0197 -0.0483 446 LYS A O 3423 C CB . LYS A 446 ? 0.3927 0.3953 0.3482 -0.0734 -0.0185 -0.0469 446 LYS A CB 3424 C CG . LYS A 446 ? 0.4265 0.4214 0.3746 -0.0777 -0.0159 -0.0456 446 LYS A CG 3425 C CD . LYS A 446 ? 0.4378 0.4470 0.3891 -0.0807 -0.0142 -0.0498 446 LYS A CD 3426 C CE . LYS A 446 ? 0.4356 0.4561 0.3998 -0.0722 -0.0173 -0.0502 446 LYS A CE 3427 N NZ . LYS A 446 ? 0.4583 0.4929 0.4252 -0.0745 -0.0157 -0.0543 446 LYS A NZ 3428 N N . LEU A 447 ? 0.3545 0.3549 0.3192 -0.0624 -0.0253 -0.0442 447 LEU A N 3429 C CA . LEU A 447 ? 0.3532 0.3585 0.3207 -0.0596 -0.0274 -0.0462 447 LEU A CA 3430 C C . LEU A 447 ? 0.3500 0.3445 0.3116 -0.0620 -0.0275 -0.0438 447 LEU A C 3431 O O . LEU A 447 ? 0.3565 0.3543 0.3153 -0.0645 -0.0267 -0.0468 447 LEU A O 3432 C CB . LEU A 447 ? 0.3590 0.3653 0.3334 -0.0517 -0.0316 -0.0447 447 LEU A CB 3433 C CG . LEU A 447 ? 0.3689 0.3790 0.3444 -0.0477 -0.0342 -0.0471 447 LEU A CG 3434 C CD1 . LEU A 447 ? 0.3796 0.4046 0.3550 -0.0486 -0.0324 -0.0538 447 LEU A CD1 3435 C CD2 . LEU A 447 ? 0.3784 0.3854 0.3572 -0.0407 -0.0383 -0.0452 447 LEU A CD2 3436 N N . PHE A 448 ? 0.3332 0.3155 0.2924 -0.0608 -0.0284 -0.0387 448 PHE A N 3437 C CA . PHE A 448 ? 0.3435 0.3154 0.2966 -0.0619 -0.0287 -0.0361 448 PHE A CA 3438 C C . PHE A 448 ? 0.3633 0.3306 0.3055 -0.0693 -0.0250 -0.0384 448 PHE A C 3439 O O . PHE A 448 ? 0.3350 0.2995 0.2726 -0.0717 -0.0247 -0.0394 448 PHE A O 3440 C CB . PHE A 448 ? 0.3369 0.2995 0.2896 -0.0582 -0.0305 -0.0305 448 PHE A CB 3441 C CG . PHE A 448 ? 0.3419 0.2951 0.2886 -0.0579 -0.0315 -0.0279 448 PHE A CG 3442 C CD1 . PHE A 448 ? 0.3384 0.2928 0.2894 -0.0552 -0.0346 -0.0265 448 PHE A CD1 3443 C CD2 . PHE A 448 ? 0.3645 0.3067 0.2996 -0.0606 -0.0293 -0.0270 448 PHE A CD2 3444 C CE1 . PHE A 448 ? 0.3523 0.2992 0.2979 -0.0549 -0.0356 -0.0242 448 PHE A CE1 3445 C CE2 . PHE A 448 ? 0.3706 0.3039 0.2992 -0.0594 -0.0304 -0.0247 448 PHE A CE2 3446 C CZ . PHE A 448 ? 0.3614 0.2982 0.2962 -0.0565 -0.0335 -0.0234 448 PHE A CZ 3447 N N . GLU A 449 ? 0.4092 0.3073 0.2988 -0.0362 0.0305 -0.0561 449 GLU A N 3448 C CA . GLU A 449 ? 0.4508 0.3410 0.3385 -0.0425 0.0356 -0.0604 449 GLU A CA 3449 C C . GLU A 449 ? 0.4271 0.3371 0.3286 -0.0476 0.0253 -0.0619 449 GLU A C 3450 O O . GLU A 449 ? 0.4209 0.3331 0.3326 -0.0461 0.0288 -0.0606 449 GLU A O 3451 C CB . GLU A 449 ? 0.5065 0.3719 0.3683 -0.0527 0.0424 -0.0679 449 GLU A CB 3452 C CG . GLU A 449 ? 0.5696 0.4091 0.4171 -0.0456 0.0592 -0.0655 449 GLU A CG 3453 C CD . GLU A 449 ? 0.6149 0.4520 0.4759 -0.0363 0.0704 -0.0588 449 GLU A CD 3454 O OE1 . GLU A 449 ? 0.6514 0.4859 0.5155 -0.0412 0.0726 -0.0617 449 GLU A OE1 3455 O OE2 . GLU A 449 ? 0.6164 0.4564 0.4862 -0.0243 0.0765 -0.0496 449 GLU A OE2 3456 N N . ARG A 450 ? 0.4398 0.3646 0.3420 -0.0525 0.0136 -0.0630 450 ARG A N 3457 C CA . ARG A 450 ? 0.4572 0.4043 0.3750 -0.0552 0.0045 -0.0616 450 ARG A CA 3458 C C . ARG A 450 ? 0.4211 0.3781 0.3565 -0.0438 0.0053 -0.0561 450 ARG A C 3459 O O . ARG A 450 ? 0.4047 0.3700 0.3512 -0.0441 0.0057 -0.0550 450 ARG A O 3460 C CB . ARG A 450 ? 0.4994 0.4635 0.4175 -0.0574 -0.0071 -0.0599 450 ARG A CB 3461 C CG . ARG A 450 ? 0.5954 0.5553 0.4957 -0.0712 -0.0120 -0.0648 450 ARG A CG 3462 C CD . ARG A 450 ? 0.6302 0.6163 0.5376 -0.0748 -0.0254 -0.0605 450 ARG A CD 3463 N NE . ARG A 450 ? 0.6535 0.6477 0.5633 -0.0639 -0.0293 -0.0550 450 ARG A NE 3464 C CZ . ARG A 450 ? 0.6695 0.6538 0.5619 -0.0638 -0.0301 -0.0561 450 ARG A CZ 3465 N NH1 . ARG A 450 ? 0.6711 0.6345 0.5397 -0.0732 -0.0266 -0.0630 450 ARG A NH1 3466 N NH2 . ARG A 450 ? 0.6634 0.6562 0.5604 -0.0536 -0.0331 -0.0501 450 ARG A NH2 3467 N N . THR A 451 ? 0.3793 0.3344 0.3156 -0.0347 0.0057 -0.0524 451 THR A N 3468 C CA . THR A 451 ? 0.3456 0.3066 0.2934 -0.0257 0.0051 -0.0478 451 THR A CA 3469 C C . THR A 451 ? 0.3411 0.2942 0.2915 -0.0238 0.0132 -0.0469 451 THR A C 3470 O O . THR A 451 ? 0.3375 0.2964 0.2958 -0.0210 0.0131 -0.0454 451 THR A O 3471 C CB . THR A 451 ? 0.3253 0.2844 0.2716 -0.0196 0.0028 -0.0440 451 THR A CB 3472 O OG1 . THR A 451 ? 0.3185 0.2844 0.2616 -0.0206 -0.0037 -0.0440 451 THR A OG1 3473 C CG2 . THR A 451 ? 0.3044 0.2665 0.2581 -0.0130 0.0009 -0.0400 451 THR A CG2 3474 N N . LYS A 452 ? 0.3614 0.3005 0.3044 -0.0244 0.0215 -0.0471 452 LYS A N 3475 C CA . LYS A 452 ? 0.3894 0.3209 0.3347 -0.0217 0.0307 -0.0447 452 LYS A CA 3476 C C . LYS A 452 ? 0.4119 0.3453 0.3606 -0.0267 0.0323 -0.0480 452 LYS A C 3477 O O . LYS A 452 ? 0.3887 0.3244 0.3445 -0.0225 0.0355 -0.0448 452 LYS A O 3478 C CB . LYS A 452 ? 0.4299 0.3435 0.3644 -0.0216 0.0420 -0.0442 452 LYS A CB 3479 C CG . LYS A 452 ? 0.4601 0.3649 0.3969 -0.0170 0.0537 -0.0397 452 LYS A CG 3480 C CD . LYS A 452 ? 0.5122 0.3950 0.4352 -0.0163 0.0678 -0.0393 452 LYS A CD 3481 C CE . LYS A 452 ? 0.5600 0.4302 0.4823 -0.0137 0.0812 -0.0366 452 LYS A CE 3482 N NZ . LYS A 452 ? 0.6020 0.4568 0.5125 -0.0246 0.0852 -0.0459 452 LYS A NZ 3483 N N . LYS A 453 ? 0.4289 0.3617 0.3720 -0.0365 0.0298 -0.0536 453 LYS A N 3484 C CA . LYS A 453 ? 0.4519 0.3866 0.3991 -0.0436 0.0318 -0.0560 453 LYS A CA 3485 C C . LYS A 453 ? 0.4079 0.3623 0.3705 -0.0394 0.0259 -0.0523 453 LYS A C 3486 O O . LYS A 453 ? 0.4095 0.3647 0.3788 -0.0382 0.0310 -0.0506 453 LYS A O 3487 C CB . LYS A 453 ? 0.4829 0.4136 0.4200 -0.0581 0.0289 -0.0622 453 LYS A CB 3488 C CG . LYS A 453 ? 0.5300 0.4356 0.4454 -0.0631 0.0361 -0.0670 453 LYS A CG 3489 C CD . LYS A 453 ? 0.5562 0.4381 0.4639 -0.0615 0.0516 -0.0673 453 LYS A CD 3490 C CE . LYS A 453 ? 0.6013 0.4544 0.4843 -0.0644 0.0613 -0.0713 453 LYS A CE 3491 N NZ . LYS A 453 ? 0.6021 0.4325 0.4647 -0.0803 0.0658 -0.0798 453 LYS A NZ 3492 N N . GLN A 454 ? 0.3893 0.3574 0.3562 -0.0359 0.0169 -0.0505 454 GLN A N 3493 C CA . GLN A 454 ? 0.3803 0.3629 0.3587 -0.0293 0.0137 -0.0462 454 GLN A CA 3494 C C . GLN A 454 ? 0.3528 0.3289 0.3321 -0.0204 0.0189 -0.0433 454 GLN A C 3495 O O . GLN A 454 ? 0.3394 0.3208 0.3251 -0.0169 0.0215 -0.0408 454 GLN A O 3496 C CB . GLN A 454 ? 0.3887 0.3807 0.3679 -0.0241 0.0058 -0.0438 454 GLN A CB 3497 C CG . GLN A 454 ? 0.4259 0.4333 0.4092 -0.0302 -0.0010 -0.0430 454 GLN A CG 3498 C CD . GLN A 454 ? 0.4278 0.4434 0.4126 -0.0223 -0.0065 -0.0388 454 GLN A CD 3499 O OE1 . GLN A 454 ? 0.4235 0.4501 0.4173 -0.0155 -0.0065 -0.0336 454 GLN A OE1 3500 N NE2 . GLN A 454 ? 0.4244 0.4332 0.3998 -0.0222 -0.0096 -0.0403 454 GLN A NE2 3501 N N . LEU A 455 ? 0.3254 0.2913 0.2980 -0.0166 0.0202 -0.0426 455 LEU A N 3502 C CA . LEU A 455 ? 0.3129 0.2753 0.2848 -0.0091 0.0217 -0.0387 455 LEU A CA 3503 C C . LEU A 455 ? 0.3155 0.2728 0.2890 -0.0082 0.0303 -0.0369 455 LEU A C 3504 O O . LEU A 455 ? 0.3044 0.2616 0.2775 -0.0026 0.0312 -0.0336 455 LEU A O 3505 C CB . LEU A 455 ? 0.3072 0.2650 0.2746 -0.0068 0.0189 -0.0364 455 LEU A CB 3506 C CG . LEU A 455 ? 0.2967 0.2581 0.2620 -0.0060 0.0108 -0.0369 455 LEU A CG 3507 C CD1 . LEU A 455 ? 0.2851 0.2427 0.2478 -0.0056 0.0087 -0.0340 455 LEU A CD1 3508 C CD2 . LEU A 455 ? 0.3064 0.2690 0.2699 -0.0011 0.0072 -0.0359 455 LEU A CD2 3509 N N . ARG A 456 ? 0.3314 0.2822 0.3043 -0.0140 0.0370 -0.0392 456 ARG A N 3510 C CA . ARG A 456 ? 0.3536 0.2975 0.3277 -0.0137 0.0468 -0.0374 456 ARG A CA 3511 C C . ARG A 456 ? 0.3457 0.2864 0.3185 -0.0052 0.0500 -0.0308 456 ARG A C 3512 O O . ARG A 456 ? 0.3471 0.2852 0.3175 -0.0031 0.0495 -0.0281 456 ARG A O 3513 C CB . ARG A 456 ? 0.3685 0.3204 0.3499 -0.0146 0.0476 -0.0373 456 ARG A CB 3514 C CG . ARG A 456 ? 0.3813 0.3388 0.3670 -0.0251 0.0459 -0.0414 456 ARG A CG 3515 C CD . ARG A 456 ? 0.3966 0.3402 0.3781 -0.0340 0.0547 -0.0443 456 ARG A CD 3516 N NE . ARG A 456 ? 0.4010 0.3406 0.3871 -0.0321 0.0643 -0.0409 456 ARG A NE 3517 C CZ . ARG A 456 ? 0.4013 0.3480 0.3964 -0.0384 0.0663 -0.0404 456 ARG A CZ 3518 N NH1 . ARG A 456 ? 0.3966 0.3582 0.3993 -0.0474 0.0584 -0.0419 456 ARG A NH1 3519 N NH2 . ARG A 456 ? 0.4181 0.3589 0.4162 -0.0354 0.0764 -0.0367 456 ARG A NH2 3520 N N . GLU A 457 ? 0.3514 0.2943 0.3262 -0.0003 0.0525 -0.0270 457 GLU A N 3521 C CA . GLU A 457 ? 0.3534 0.2957 0.3266 0.0066 0.0545 -0.0194 457 GLU A CA 3522 C C . GLU A 457 ? 0.3438 0.2927 0.3130 0.0097 0.0436 -0.0174 457 GLU A C 3523 O O . GLU A 457 ? 0.3579 0.3086 0.3244 0.0139 0.0423 -0.0109 457 GLU A O 3524 C CB . GLU A 457 ? 0.3791 0.3182 0.3533 0.0101 0.0635 -0.0158 457 GLU A CB 3525 C CG . GLU A 457 ? 0.4022 0.3303 0.3780 0.0063 0.0758 -0.0171 457 GLU A CG 3526 C CD . GLU A 457 ? 0.4203 0.3395 0.3934 0.0075 0.0820 -0.0141 457 GLU A CD 3527 O OE1 . GLU A 457 ? 0.4456 0.3698 0.4200 0.0147 0.0813 -0.0056 457 GLU A OE1 3528 O OE2 . GLU A 457 ? 0.4476 0.3545 0.4166 0.0013 0.0881 -0.0192 457 GLU A OE2 3529 N N . ASN A 458 ? 0.3264 0.2778 0.2939 0.0070 0.0356 -0.0224 458 ASN A N 3530 C CA . ASN A 458 ? 0.3173 0.2697 0.2775 0.0090 0.0265 -0.0218 458 ASN A CA 3531 C C . ASN A 458 ? 0.3050 0.2589 0.2643 0.0068 0.0194 -0.0194 458 ASN A C 3532 O O . ASN A 458 ? 0.3014 0.2538 0.2529 0.0063 0.0113 -0.0188 458 ASN A O 3533 C CB . ASN A 458 ? 0.3256 0.2782 0.2836 0.0093 0.0239 -0.0268 458 ASN A CB 3534 C CG . ASN A 458 ? 0.3286 0.2822 0.2892 0.0121 0.0309 -0.0270 458 ASN A CG 3535 O OD1 . ASN A 458 ? 0.3264 0.2783 0.2881 0.0136 0.0374 -0.0240 458 ASN A OD1 3536 N ND2 . ASN A 458 ? 0.3280 0.2851 0.2906 0.0135 0.0305 -0.0290 458 ASN A ND2 3537 N N . ALA A 459 ? 0.2882 0.2433 0.2539 0.0052 0.0232 -0.0178 459 ALA A N 3538 C CA . ALA A 459 ? 0.2990 0.2570 0.2664 0.0037 0.0182 -0.0141 459 ALA A CA 3539 C C . ALA A 459 ? 0.3064 0.2655 0.2805 0.0058 0.0264 -0.0072 459 ALA A C 3540 O O . ALA A 459 ? 0.3338 0.2872 0.3088 0.0074 0.0368 -0.0078 459 ALA A O 3541 C CB . ALA A 459 ? 0.2879 0.2445 0.2539 0.0007 0.0143 -0.0202 459 ALA A CB 3542 N N . GLU A 460 ? 0.3042 0.2696 0.2828 0.0059 0.0229 0.0002 460 GLU A N 3543 C CA . GLU A 460 ? 0.3101 0.2768 0.2960 0.0098 0.0324 0.0088 460 GLU A CA 3544 C C . GLU A 460 ? 0.3181 0.2855 0.3058 0.0081 0.0306 0.0096 460 GLU A C 3545 O O . GLU A 460 ? 0.2951 0.2670 0.2822 0.0040 0.0197 0.0084 460 GLU A O 3546 C CB . GLU A 460 ? 0.3069 0.2859 0.3013 0.0136 0.0324 0.0228 460 GLU A CB 3547 C CG . GLU A 460 ? 0.3091 0.2866 0.3014 0.0171 0.0370 0.0240 460 GLU A CG 3548 C CD . GLU A 460 ? 0.3066 0.2989 0.3062 0.0206 0.0349 0.0389 460 GLU A CD 3549 O OE1 . GLU A 460 ? 0.3020 0.3074 0.3122 0.0214 0.0329 0.0508 460 GLU A OE1 3550 O OE2 . GLU A 460 ? 0.3052 0.2974 0.3004 0.0225 0.0352 0.0398 460 GLU A OE2 3551 N N . ASP A 461 ? 0.3281 0.2880 0.3159 0.0116 0.0426 0.0117 461 ASP A N 3552 C CA . ASP A 461 ? 0.3341 0.2923 0.3220 0.0118 0.0445 0.0137 461 ASP A CA 3553 C C . ASP A 461 ? 0.3379 0.3117 0.3400 0.0149 0.0430 0.0293 461 ASP A C 3554 O O . ASP A 461 ? 0.3282 0.3073 0.3388 0.0214 0.0522 0.0412 461 ASP A O 3555 C CB . ASP A 461 ? 0.3565 0.2971 0.3353 0.0149 0.0601 0.0109 461 ASP A CB 3556 C CG . ASP A 461 ? 0.3729 0.3071 0.3464 0.0155 0.0637 0.0112 461 ASP A CG 3557 O OD1 . ASP A 461 ? 0.3442 0.2906 0.3265 0.0157 0.0571 0.0180 461 ASP A OD1 3558 O OD2 . ASP A 461 ? 0.4155 0.3306 0.3742 0.0151 0.0737 0.0046 461 ASP A OD2 3559 N N . MET A 462 ? 0.3213 0.3032 0.3267 0.0102 0.0319 0.0304 462 MET A N 3560 C CA . MET A 462 ? 0.3397 0.3394 0.3603 0.0099 0.0275 0.0457 462 MET A CA 3561 C C . MET A 462 ? 0.3544 0.3553 0.3826 0.0160 0.0392 0.0559 462 MET A C 3562 O O . MET A 462 ? 0.3738 0.3923 0.4182 0.0164 0.0374 0.0712 462 MET A O 3563 C CB . MET A 462 ? 0.3428 0.3473 0.3620 0.0006 0.0112 0.0425 462 MET A CB 3564 C CG . MET A 462 ? 0.3667 0.3699 0.3775 -0.0049 -0.0001 0.0357 462 MET A CG 3565 S SD . MET A 462 ? 0.4012 0.3966 0.4006 -0.0144 -0.0146 0.0268 462 MET A SD 3566 C CE . MET A 462 ? 0.4123 0.4234 0.4265 -0.0207 -0.0211 0.0419 462 MET A CE 3567 N N . GLY A 463 ? 0.3464 0.3288 0.3623 0.0200 0.0510 0.0481 463 GLY A N 3568 C CA . GLY A 463 ? 0.3674 0.3459 0.3860 0.0278 0.0658 0.0579 463 GLY A CA 3569 C C . GLY A 463 ? 0.3691 0.3470 0.3861 0.0253 0.0625 0.0574 463 GLY A C 3570 O O . GLY A 463 ? 0.3964 0.3674 0.4116 0.0322 0.0758 0.0639 463 GLY A O 3571 N N . ASN A 464 ? 0.3580 0.3408 0.3739 0.0165 0.0464 0.0500 464 ASN A N 3572 C CA . ASN A 464 ? 0.3553 0.3389 0.3711 0.0136 0.0419 0.0506 464 ASN A CA 3573 C C . ASN A 464 ? 0.3473 0.3161 0.3445 0.0095 0.0364 0.0339 464 ASN A C 3574 O O . ASN A 464 ? 0.3553 0.3249 0.3513 0.0059 0.0292 0.0325 464 ASN A O 3575 C CB . ASN A 464 ? 0.3597 0.3619 0.3911 0.0063 0.0280 0.0593 464 ASN A CB 3576 C CG . ASN A 464 ? 0.3642 0.3655 0.3890 -0.0015 0.0136 0.0490 464 ASN A CG 3577 O OD1 . ASN A 464 ? 0.3561 0.3483 0.3704 -0.0003 0.0147 0.0386 464 ASN A OD1 3578 N ND2 . ASN A 464 ? 0.3789 0.3877 0.4085 -0.0102 0.0007 0.0521 464 ASN A ND2 3579 N N . GLY A 465 ? 0.3360 0.2921 0.3195 0.0099 0.0401 0.0226 465 GLY A N 3580 C CA . GLY A 465 ? 0.3282 0.2755 0.2971 0.0054 0.0334 0.0087 465 GLY A CA 3581 C C . GLY A 465 ? 0.3072 0.2610 0.2786 0.0004 0.0204 0.0028 465 GLY A C 3582 O O . GLY A 465 ? 0.3054 0.2559 0.2685 -0.0021 0.0143 -0.0055 465 GLY A O 3583 N N . CYS A 466 ? 0.2969 0.2596 0.2784 -0.0002 0.0168 0.0082 466 CYS A N 3584 C CA . CYS A 466 ? 0.3140 0.2787 0.2938 -0.0042 0.0064 0.0028 466 CYS A CA 3585 C C . CYS A 466 ? 0.3065 0.2722 0.2874 -0.0029 0.0091 0.0018 466 CYS A C 3586 O O . CYS A 466 ? 0.3186 0.2871 0.3056 0.0006 0.0173 0.0089 466 CYS A O 3587 C CB . CYS A 466 ? 0.3374 0.3092 0.3233 -0.0088 -0.0033 0.0093 466 CYS A CB 3588 S SG . CYS A 466 ? 0.3651 0.3378 0.3544 -0.0109 -0.0055 0.0150 466 CYS A SG 3589 N N . PHE A 467 ? 0.2990 0.2622 0.2739 -0.0049 0.0032 -0.0057 467 PHE A N 3590 C CA . PHE A 467 ? 0.2912 0.2551 0.2659 -0.0039 0.0044 -0.0067 467 PHE A CA 3591 C C . PHE A 467 ? 0.3089 0.2759 0.2821 -0.0068 -0.0051 -0.0039 467 PHE A C 3592 O O . PHE A 467 ? 0.3082 0.2707 0.2749 -0.0100 -0.0125 -0.0071 467 PHE A O 3593 C CB . PHE A 467 ? 0.2882 0.2465 0.2561 -0.0039 0.0055 -0.0167 467 PHE A CB 3594 C CG . PHE A 467 ? 0.2943 0.2478 0.2596 -0.0042 0.0128 -0.0209 467 PHE A CG 3595 C CD1 . PHE A 467 ? 0.3014 0.2503 0.2670 -0.0030 0.0227 -0.0200 467 PHE A CD1 3596 C CD2 . PHE A 467 ? 0.2966 0.2485 0.2569 -0.0062 0.0099 -0.0255 467 PHE A CD2 3597 C CE1 . PHE A 467 ? 0.3147 0.2541 0.2729 -0.0053 0.0295 -0.0250 467 PHE A CE1 3598 C CE2 . PHE A 467 ? 0.3142 0.2604 0.2682 -0.0085 0.0153 -0.0298 467 PHE A CE2 3599 C CZ . PHE A 467 ? 0.3159 0.2542 0.2675 -0.0088 0.0250 -0.0302 467 PHE A CZ 3600 N N . LYS A 468 ? 0.3160 0.2888 0.2931 -0.0060 -0.0043 0.0024 468 LYS A N 3601 C CA . LYS A 468 ? 0.3247 0.2975 0.2950 -0.0093 -0.0129 0.0032 468 LYS A CA 3602 C C . LYS A 468 ? 0.3175 0.2823 0.2792 -0.0060 -0.0093 -0.0048 468 LYS A C 3603 O O . LYS A 468 ? 0.2985 0.2650 0.2644 -0.0019 -0.0009 -0.0041 468 LYS A O 3604 C CB . LYS A 468 ? 0.3407 0.3263 0.3192 -0.0100 -0.0145 0.0155 468 LYS A CB 3605 C CG . LYS A 468 ? 0.3809 0.3654 0.3481 -0.0150 -0.0246 0.0162 468 LYS A CG 3606 C CD . LYS A 468 ? 0.4105 0.4127 0.3877 -0.0177 -0.0293 0.0311 468 LYS A CD 3607 C CE . LYS A 468 ? 0.4426 0.4424 0.4044 -0.0238 -0.0401 0.0314 468 LYS A CE 3608 N NZ . LYS A 468 ? 0.4621 0.4835 0.4347 -0.0279 -0.0470 0.0478 468 LYS A NZ 3609 N N . ILE A 469 ? 0.3160 0.2710 0.2656 -0.0072 -0.0140 -0.0119 469 ILE A N 3610 C CA . ILE A 469 ? 0.3146 0.2633 0.2572 -0.0033 -0.0100 -0.0180 469 ILE A CA 3611 C C . ILE A 469 ? 0.3369 0.2808 0.2676 -0.0043 -0.0142 -0.0158 469 ILE A C 3612 O O . ILE A 469 ? 0.3513 0.2877 0.2699 -0.0092 -0.0225 -0.0157 469 ILE A O 3613 C CB . ILE A 469 ? 0.3232 0.2642 0.2594 -0.0018 -0.0107 -0.0248 469 ILE A CB 3614 C CG1 . ILE A 469 ? 0.3078 0.2547 0.2538 -0.0017 -0.0078 -0.0264 469 ILE A CG1 3615 C CG2 . ILE A 469 ? 0.3229 0.2590 0.2531 0.0032 -0.0058 -0.0285 469 ILE A CG2 3616 C CD1 . ILE A 469 ? 0.3252 0.2684 0.2670 0.0003 -0.0090 -0.0305 469 ILE A CD1 3617 N N . TYR A 470 ? 0.3474 0.2937 0.2792 -0.0003 -0.0084 -0.0142 470 TYR A N 3618 C CA . TYR A 470 ? 0.3715 0.3156 0.2921 -0.0011 -0.0122 -0.0102 470 TYR A CA 3619 C C . TYR A 470 ? 0.3876 0.3160 0.2887 0.0015 -0.0113 -0.0164 470 TYR A C 3620 O O . TYR A 470 ? 0.4053 0.3310 0.2979 0.0044 -0.0088 -0.0146 470 TYR A O 3621 C CB . TYR A 470 ? 0.3630 0.3178 0.2945 0.0027 -0.0054 -0.0030 470 TYR A CB 3622 C CG . TYR A 470 ? 0.3657 0.3348 0.3113 0.0008 -0.0071 0.0072 470 TYR A CG 3623 C CD1 . TYR A 470 ? 0.3565 0.3301 0.3164 0.0024 -0.0005 0.0081 470 TYR A CD1 3624 C CD2 . TYR A 470 ? 0.3776 0.3561 0.3217 -0.0022 -0.0147 0.0173 470 TYR A CD2 3625 C CE1 . TYR A 470 ? 0.3602 0.3461 0.3332 0.0029 0.0006 0.0193 470 TYR A CE1 3626 C CE2 . TYR A 470 ? 0.3823 0.3777 0.3428 -0.0026 -0.0152 0.0297 470 TYR A CE2 3627 C CZ . TYR A 470 ? 0.3660 0.3645 0.3414 0.0009 -0.0063 0.0310 470 TYR A CZ 3628 O OH . TYR A 470 ? 0.3646 0.3790 0.3562 0.0025 -0.0044 0.0449 470 TYR A OH 3629 N N . HIS A 471 ? 0.4031 0.3205 0.2963 0.0019 -0.0120 -0.0227 471 HIS A N 3630 C CA . HIS A 471 ? 0.4186 0.3181 0.2914 0.0059 -0.0094 -0.0274 471 HIS A CA 3631 C C . HIS A 471 ? 0.4363 0.3212 0.2967 0.0036 -0.0133 -0.0316 471 HIS A C 3632 O O . HIS A 471 ? 0.4248 0.3161 0.2963 0.0003 -0.0167 -0.0313 471 HIS A O 3633 C CB . HIS A 471 ? 0.4139 0.3169 0.2950 0.0147 0.0019 -0.0289 471 HIS A CB 3634 C CG . HIS A 471 ? 0.3933 0.3067 0.2925 0.0163 0.0053 -0.0306 471 HIS A CG 3635 N ND1 . HIS A 471 ? 0.3975 0.3043 0.2924 0.0194 0.0060 -0.0332 471 HIS A ND1 3636 C CD2 . HIS A 471 ? 0.3678 0.2968 0.2875 0.0150 0.0084 -0.0297 471 HIS A CD2 3637 C CE1 . HIS A 471 ? 0.3829 0.3040 0.2961 0.0194 0.0078 -0.0332 471 HIS A CE1 3638 N NE2 . HIS A 471 ? 0.3550 0.2882 0.2819 0.0159 0.0090 -0.0319 471 HIS A NE2 3639 N N . LYS A 472 ? 0.4461 0.3087 0.2814 0.0062 -0.0115 -0.0351 472 LYS A N 3640 C CA . LYS A 472 ? 0.4922 0.3359 0.3129 0.0059 -0.0122 -0.0390 472 LYS A CA 3641 C C . LYS A 472 ? 0.4630 0.3174 0.3027 0.0141 -0.0047 -0.0390 472 LYS A C 3642 O O . LYS A 472 ? 0.4510 0.3137 0.3003 0.0225 0.0039 -0.0379 472 LYS A O 3643 C CB . LYS A 472 ? 0.5481 0.3615 0.3352 0.0096 -0.0078 -0.0428 472 LYS A CB 3644 C CG . LYS A 472 ? 0.6176 0.4052 0.3851 0.0106 -0.0057 -0.0466 472 LYS A CG 3645 C CD . LYS A 472 ? 0.6885 0.4393 0.4149 0.0113 -0.0023 -0.0509 472 LYS A CD 3646 C CE . LYS A 472 ? 0.7665 0.4852 0.4672 0.0081 -0.0022 -0.0551 472 LYS A CE 3647 N NZ . LYS A 472 ? 0.8197 0.5304 0.5230 0.0238 0.0126 -0.0540 472 LYS A NZ 3648 N N . CYS A 473 ? 0.4623 0.3185 0.3084 0.0109 -0.0086 -0.0392 473 CYS A N 3649 C CA . CYS A 473 ? 0.4542 0.3239 0.3187 0.0173 -0.0036 -0.0381 473 CYS A CA 3650 C C . CYS A 473 ? 0.4729 0.3272 0.3266 0.0180 -0.0042 -0.0390 473 CYS A C 3651 O O . CYS A 473 ? 0.4770 0.3341 0.3355 0.0113 -0.0107 -0.0384 473 CYS A O 3652 C CB . CYS A 473 ? 0.4423 0.3372 0.3320 0.0130 -0.0065 -0.0360 473 CYS A CB 3653 S SG . CYS A 473 ? 0.4530 0.3672 0.3637 0.0180 -0.0021 -0.0348 473 CYS A SG 3654 N N . ASP A 474 ? 0.4788 0.3152 0.3171 0.0273 0.0040 -0.0394 474 ASP A N 3655 C CA . ASP A 474 ? 0.5014 0.3174 0.3253 0.0304 0.0065 -0.0396 474 ASP A CA 3656 C C . ASP A 474 ? 0.4864 0.3218 0.3319 0.0356 0.0080 -0.0353 474 ASP A C 3657 O O . ASP A 474 ? 0.4329 0.2964 0.3026 0.0346 0.0057 -0.0333 474 ASP A O 3658 C CB . ASP A 474 ? 0.5394 0.3274 0.3378 0.0409 0.0179 -0.0402 474 ASP A CB 3659 C CG . ASP A 474 ? 0.5362 0.3405 0.3503 0.0555 0.0295 -0.0345 474 ASP A CG 3660 O OD1 . ASP A 474 ? 0.4844 0.3209 0.3283 0.0567 0.0280 -0.0305 474 ASP A OD1 3661 O OD2 . ASP A 474 ? 0.5673 0.3510 0.3626 0.0657 0.0407 -0.0336 474 ASP A OD2 3662 N N . ASN A 475 ? 0.4913 0.3101 0.3261 0.0408 0.0121 -0.0338 475 ASN A N 3663 C CA . ASN A 475 ? 0.4859 0.3226 0.3388 0.0447 0.0120 -0.0289 475 ASN A CA 3664 C C . ASN A 475 ? 0.4595 0.3249 0.3351 0.0537 0.0166 -0.0232 475 ASN A C 3665 O O . ASN A 475 ? 0.4290 0.3195 0.3246 0.0509 0.0116 -0.0209 475 ASN A O 3666 C CB . ASN A 475 ? 0.5184 0.3301 0.3544 0.0506 0.0175 -0.0269 475 ASN A CB 3667 C CG . ASN A 475 ? 0.5427 0.3337 0.3636 0.0381 0.0100 -0.0311 475 ASN A CG 3668 O OD1 . ASN A 475 ? 0.5277 0.3287 0.3554 0.0256 0.0001 -0.0339 475 ASN A OD1 3669 N ND2 . ASN A 475 ? 0.5773 0.3389 0.3779 0.0413 0.0156 -0.0306 475 ASN A ND2 3670 N N . ALA A 476 ? 0.4656 0.3267 0.3369 0.0635 0.0260 -0.0207 476 ALA A N 3671 C CA . ALA A 476 ? 0.4574 0.3474 0.3517 0.0706 0.0303 -0.0139 476 ALA A CA 3672 C C . ALA A 476 ? 0.4189 0.3324 0.3308 0.0603 0.0231 -0.0171 476 ALA A C 3673 O O . ALA A 476 ? 0.4176 0.3588 0.3512 0.0588 0.0205 -0.0133 476 ALA A O 3674 C CB . ALA A 476 ? 0.4697 0.3484 0.3552 0.0841 0.0438 -0.0092 476 ALA A CB 3675 N N . CYS A 477 ? 0.4160 0.3173 0.3173 0.0527 0.0199 -0.0236 477 CYS A N 3676 C CA . CYS A 477 ? 0.4088 0.3277 0.3242 0.0441 0.0152 -0.0261 477 CYS A CA 3677 C C . CYS A 477 ? 0.3752 0.3084 0.3027 0.0354 0.0069 -0.0273 477 CYS A C 3678 O O . CYS A 477 ? 0.3629 0.3165 0.3069 0.0317 0.0054 -0.0265 477 CYS A O 3679 C CB . CYS A 477 ? 0.4355 0.3379 0.3356 0.0391 0.0136 -0.0308 477 CYS A CB 3680 S SG . CYS A 477 ? 0.4352 0.3537 0.3491 0.0296 0.0093 -0.0327 477 CYS A SG 3681 N N . ILE A 478 ? 0.3737 0.2943 0.2914 0.0319 0.0022 -0.0291 478 ILE A N 3682 C CA . ILE A 478 ? 0.3762 0.3074 0.3029 0.0251 -0.0039 -0.0294 478 ILE A CA 3683 C C . ILE A 478 ? 0.3767 0.3261 0.3158 0.0289 -0.0035 -0.0254 478 ILE A C 3684 O O . ILE A 478 ? 0.3608 0.3261 0.3107 0.0231 -0.0069 -0.0260 478 ILE A O 3685 C CB . ILE A 478 ? 0.3847 0.2996 0.2997 0.0215 -0.0080 -0.0302 478 ILE A CB 3686 C CG1 . ILE A 478 ? 0.3874 0.2893 0.2921 0.0146 -0.0113 -0.0328 478 ILE A CG1 3687 C CG2 . ILE A 478 ? 0.3795 0.3055 0.3038 0.0173 -0.0122 -0.0289 478 ILE A CG2 3688 C CD1 . ILE A 478 ? 0.3727 0.2882 0.2890 0.0079 -0.0142 -0.0329 478 ILE A CD1 3689 N N . GLY A 479 ? 0.3825 0.3290 0.3188 0.0386 0.0010 -0.0206 479 GLY A N 3690 C CA . GLY A 479 ? 0.3782 0.3456 0.3276 0.0434 0.0013 -0.0139 479 GLY A CA 3691 C C . GLY A 479 ? 0.3619 0.3539 0.3284 0.0398 0.0005 -0.0123 479 GLY A C 3692 O O . GLY A 479 ? 0.3632 0.3754 0.3406 0.0354 -0.0045 -0.0098 479 GLY A O 3693 N N . SER A 480 ? 0.3591 0.3485 0.3265 0.0407 0.0052 -0.0137 480 SER A N 3694 C CA . SER A 480 ? 0.3572 0.3679 0.3407 0.0359 0.0052 -0.0122 480 SER A CA 3695 C C . SER A 480 ? 0.3548 0.3704 0.3409 0.0224 -0.0013 -0.0186 480 SER A C 3696 O O . SER A 480 ? 0.3458 0.3801 0.3435 0.0153 -0.0043 -0.0173 480 SER A O 3697 C CB . SER A 480 ? 0.3747 0.3786 0.3568 0.0402 0.0129 -0.0122 480 SER A CB 3698 O OG . SER A 480 ? 0.3773 0.3641 0.3481 0.0347 0.0122 -0.0197 480 SER A OG 3699 N N . ILE A 481 ? 0.3508 0.3490 0.3253 0.0187 -0.0030 -0.0246 481 ILE A N 3700 C CA . ILE A 481 ? 0.3480 0.3466 0.3223 0.0085 -0.0064 -0.0295 481 ILE A CA 3701 C C . ILE A 481 ? 0.3672 0.3743 0.3420 0.0051 -0.0119 -0.0285 481 ILE A C 3702 O O . ILE A 481 ? 0.3752 0.3920 0.3532 -0.0031 -0.0145 -0.0302 481 ILE A O 3703 C CB . ILE A 481 ? 0.3394 0.3206 0.3040 0.0070 -0.0060 -0.0330 481 ILE A CB 3704 C CG1 . ILE A 481 ? 0.3379 0.3116 0.3000 0.0097 -0.0016 -0.0335 481 ILE A CG1 3705 C CG2 . ILE A 481 ? 0.3347 0.3156 0.2994 -0.0009 -0.0066 -0.0362 481 ILE A CG2 3706 C CD1 . ILE A 481 ? 0.3473 0.3066 0.2997 0.0088 -0.0030 -0.0345 481 ILE A CD1 3707 N N . ARG A 482 ? 0.3824 0.3847 0.3519 0.0110 -0.0134 -0.0257 482 ARG A N 3708 C CA . ARG A 482 ? 0.3917 0.4020 0.3605 0.0092 -0.0183 -0.0236 482 ARG A CA 3709 C C . ARG A 482 ? 0.4200 0.4541 0.3994 0.0077 -0.0218 -0.0185 482 ARG A C 3710 O O . ARG A 482 ? 0.4169 0.4601 0.3946 0.0003 -0.0274 -0.0190 482 ARG A O 3711 C CB . ARG A 482 ? 0.4007 0.4007 0.3626 0.0170 -0.0179 -0.0201 482 ARG A CB 3712 C CG . ARG A 482 ? 0.4033 0.3829 0.3556 0.0156 -0.0169 -0.0237 482 ARG A CG 3713 C CD . ARG A 482 ? 0.4215 0.3909 0.3666 0.0204 -0.0172 -0.0203 482 ARG A CD 3714 N NE . ARG A 482 ? 0.4368 0.4039 0.3806 0.0301 -0.0135 -0.0155 482 ARG A NE 3715 C CZ . ARG A 482 ? 0.4653 0.4116 0.3980 0.0351 -0.0097 -0.0150 482 ARG A CZ 3716 N NH1 . ARG A 482 ? 0.4652 0.3932 0.3883 0.0295 -0.0113 -0.0186 482 ARG A NH1 3717 N NH2 . ARG A 482 ? 0.4876 0.4311 0.4184 0.0457 -0.0038 -0.0099 482 ARG A NH2 3718 N N . ASN A 483 ? 0.4424 0.4867 0.4318 0.0143 -0.0184 -0.0128 483 ASN A N 3719 C CA . ASN A 483 ? 0.4720 0.5441 0.4764 0.0134 -0.0215 -0.0048 483 ASN A CA 3720 C C . ASN A 483 ? 0.4622 0.5462 0.4748 0.0011 -0.0237 -0.0078 483 ASN A C 3721 O O . ASN A 483 ? 0.4514 0.5607 0.4769 -0.0036 -0.0284 -0.0012 483 ASN A O 3722 C CB . ASN A 483 ? 0.5205 0.5990 0.5342 0.0272 -0.0143 0.0046 483 ASN A CB 3723 C CG . ASN A 483 ? 0.5779 0.6492 0.5856 0.0399 -0.0115 0.0108 483 ASN A CG 3724 O OD1 . ASN A 483 ? 0.6431 0.7044 0.6402 0.0383 -0.0152 0.0078 483 ASN A OD1 3725 N ND2 . ASN A 483 ? 0.6028 0.6777 0.6166 0.0536 -0.0032 0.0204 483 ASN A ND2 3726 N N . GLY A 484 ? 0.4491 0.5159 0.4551 -0.0038 -0.0200 -0.0163 484 GLY A N 3727 C CA . GLY A 484 ? 0.4462 0.5189 0.4576 -0.0155 -0.0202 -0.0196 484 GLY A CA 3728 C C . GLY A 484 ? 0.4461 0.5315 0.4729 -0.0120 -0.0151 -0.0137 484 GLY A C 3729 O O . GLY A 484 ? 0.4670 0.5657 0.5033 -0.0226 -0.0169 -0.0130 484 GLY A O 3730 N N . THR A 485 ? 0.4395 0.5189 0.4673 0.0022 -0.0081 -0.0094 485 THR A N 3731 C CA . THR A 485 ? 0.4346 0.5230 0.4750 0.0084 -0.0007 -0.0030 485 THR A CA 3732 C C . THR A 485 ? 0.4182 0.4832 0.4481 0.0139 0.0077 -0.0081 485 THR A C 3733 O O . THR A 485 ? 0.4431 0.5105 0.4790 0.0211 0.0154 -0.0031 485 THR A O 3734 C CB . THR A 485 ? 0.4460 0.5481 0.4956 0.0227 0.0028 0.0091 485 THR A CB 3735 O OG1 . THR A 485 ? 0.4395 0.5181 0.4720 0.0342 0.0065 0.0071 485 THR A OG1 3736 C CG2 . THR A 485 ? 0.4429 0.5742 0.5060 0.0176 -0.0060 0.0171 485 THR A CG2 3737 N N . TYR A 486 ? 0.4078 0.4517 0.4223 0.0104 0.0061 -0.0169 486 TYR A N 3738 C CA . TYR A 486 ? 0.3910 0.4149 0.3948 0.0141 0.0118 -0.0210 486 TYR A CA 3739 C C . TYR A 486 ? 0.3930 0.4215 0.4051 0.0095 0.0170 -0.0209 486 TYR A C 3740 O O . TYR A 486 ? 0.3782 0.4138 0.3964 -0.0017 0.0147 -0.0233 486 TYR A O 3741 C CB . TYR A 486 ? 0.3790 0.3870 0.3701 0.0092 0.0079 -0.0278 486 TYR A CB 3742 C CG . TYR A 486 ? 0.3644 0.3557 0.3457 0.0105 0.0114 -0.0308 486 TYR A CG 3743 C CD1 . TYR A 486 ? 0.3553 0.3318 0.3236 0.0173 0.0120 -0.0306 486 TYR A CD1 3744 C CD2 . TYR A 486 ? 0.3431 0.3325 0.3265 0.0040 0.0141 -0.0334 486 TYR A CD2 3745 C CE1 . TYR A 486 ? 0.3615 0.3255 0.3206 0.0170 0.0132 -0.0323 486 TYR A CE1 3746 C CE2 . TYR A 486 ? 0.3423 0.3195 0.3181 0.0058 0.0170 -0.0341 486 TYR A CE2 3747 C CZ . TYR A 486 ? 0.3472 0.3138 0.3117 0.0119 0.0156 -0.0332 486 TYR A CZ 3748 O OH . TYR A 486 ? 0.3316 0.2893 0.2887 0.0124 0.0168 -0.0326 486 TYR A OH 3749 N N . ASP A 487 ? 0.3977 0.4201 0.4078 0.0180 0.0248 -0.0180 487 ASP A N 3750 C CA . ASP A 487 ? 0.4128 0.4382 0.4303 0.0154 0.0313 -0.0168 487 ASP A CA 3751 C C . ASP A 487 ? 0.4003 0.4050 0.4030 0.0163 0.0341 -0.0218 487 ASP A C 3752 O O . ASP A 487 ? 0.3968 0.3884 0.3869 0.0254 0.0376 -0.0210 487 ASP A O 3753 C CB . ASP A 487 ? 0.4537 0.4884 0.4800 0.0256 0.0394 -0.0081 487 ASP A CB 3754 C CG . ASP A 487 ? 0.4802 0.5217 0.5179 0.0222 0.0467 -0.0052 487 ASP A CG 3755 O OD1 . ASP A 487 ? 0.4878 0.5211 0.5222 0.0136 0.0466 -0.0107 487 ASP A OD1 3756 O OD2 . ASP A 487 ? 0.5189 0.5738 0.5693 0.0288 0.0536 0.0037 487 ASP A OD2 3757 N N . HIS A 488 ? 0.3581 0.3593 0.3609 0.0071 0.0329 -0.0261 488 HIS A N 3758 C CA . HIS A 488 ? 0.3669 0.3522 0.3582 0.0084 0.0352 -0.0285 488 HIS A CA 3759 C C . HIS A 488 ? 0.3722 0.3528 0.3614 0.0147 0.0433 -0.0251 488 HIS A C 3760 O O . HIS A 488 ? 0.3758 0.3443 0.3523 0.0191 0.0440 -0.0250 488 HIS A O 3761 C CB . HIS A 488 ? 0.3554 0.3373 0.3482 -0.0009 0.0356 -0.0319 488 HIS A CB 3762 C CG . HIS A 488 ? 0.3543 0.3384 0.3555 -0.0065 0.0430 -0.0312 488 HIS A CG 3763 N ND1 . HIS A 488 ? 0.3646 0.3385 0.3624 -0.0050 0.0506 -0.0301 488 HIS A ND1 3764 C CD2 . HIS A 488 ? 0.3536 0.3503 0.3672 -0.0144 0.0436 -0.0304 488 HIS A CD2 3765 C CE1 . HIS A 488 ? 0.3761 0.3526 0.3826 -0.0115 0.0569 -0.0295 488 HIS A CE1 3766 N NE2 . HIS A 488 ? 0.3556 0.3466 0.3720 -0.0184 0.0519 -0.0298 488 HIS A NE2 3767 N N . ASP A 489 ? 0.3794 0.3706 0.3809 0.0146 0.0493 -0.0213 489 ASP A N 3768 C CA . ASP A 489 ? 0.4211 0.4078 0.4208 0.0214 0.0587 -0.0172 489 ASP A CA 3769 C C . ASP A 489 ? 0.4174 0.3928 0.4007 0.0333 0.0604 -0.0154 489 ASP A C 3770 O O . ASP A 489 ? 0.4266 0.3902 0.3976 0.0383 0.0650 -0.0143 489 ASP A O 3771 C CB . ASP A 489 ? 0.4414 0.4441 0.4600 0.0190 0.0651 -0.0118 489 ASP A CB 3772 C CG . ASP A 489 ? 0.4756 0.4799 0.5033 0.0072 0.0676 -0.0135 489 ASP A CG 3773 O OD1 . ASP A 489 ? 0.5289 0.5190 0.5477 0.0076 0.0720 -0.0152 489 ASP A OD1 3774 O OD2 . ASP A 489 ? 0.5164 0.5352 0.5591 -0.0029 0.0655 -0.0126 489 ASP A OD2 3775 N N . VAL A 490 ? 0.4271 0.4042 0.4080 0.0376 0.0570 -0.0149 490 VAL A N 3776 C CA . VAL A 490 ? 0.4655 0.4266 0.4266 0.0483 0.0594 -0.0142 490 VAL A CA 3777 C C . VAL A 490 ? 0.4620 0.4033 0.4003 0.0471 0.0541 -0.0190 490 VAL A C 3778 O O . VAL A 490 ? 0.4593 0.3838 0.3770 0.0537 0.0577 -0.0185 490 VAL A O 3779 C CB . VAL A 490 ? 0.4825 0.4470 0.4448 0.0520 0.0563 -0.0131 490 VAL A CB 3780 C CG1 . VAL A 490 ? 0.5477 0.4881 0.4838 0.0614 0.0588 -0.0141 490 VAL A CG1 3781 C CG2 . VAL A 490 ? 0.5033 0.4904 0.4885 0.0551 0.0619 -0.0051 490 VAL A CG2 3782 N N . TYR A 491 ? 0.4232 0.3670 0.3644 0.0383 0.0455 -0.0226 491 TYR A N 3783 C CA . TYR A 491 ? 0.4246 0.3552 0.3484 0.0356 0.0385 -0.0250 491 TYR A CA 3784 C C . TYR A 491 ? 0.4020 0.3349 0.3285 0.0320 0.0389 -0.0233 491 TYR A C 3785 O O . TYR A 491 ? 0.4095 0.3361 0.3247 0.0297 0.0328 -0.0228 491 TYR A O 3786 C CB . TYR A 491 ? 0.4099 0.3417 0.3350 0.0300 0.0292 -0.0280 491 TYR A CB 3787 C CG . TYR A 491 ? 0.4180 0.3470 0.3402 0.0341 0.0289 -0.0287 491 TYR A CG 3788 C CD1 . TYR A 491 ? 0.4419 0.3513 0.3418 0.0387 0.0285 -0.0299 491 TYR A CD1 3789 C CD2 . TYR A 491 ? 0.4160 0.3608 0.3560 0.0333 0.0293 -0.0277 491 TYR A CD2 3790 C CE1 . TYR A 491 ? 0.4575 0.3616 0.3536 0.0442 0.0303 -0.0295 491 TYR A CE1 3791 C CE2 . TYR A 491 ? 0.4205 0.3647 0.3591 0.0387 0.0297 -0.0262 491 TYR A CE2 3792 C CZ . TYR A 491 ? 0.4509 0.3742 0.3682 0.0450 0.0311 -0.0268 491 TYR A CZ 3793 O OH . TYR A 491 ? 0.4846 0.4052 0.3999 0.0520 0.0337 -0.0242 491 TYR A OH 3794 N N . ARG A 492 ? 0.3988 0.3409 0.3405 0.0311 0.0462 -0.0213 492 ARG A N 3795 C CA . ARG A 492 ? 0.3860 0.3297 0.3325 0.0279 0.0482 -0.0191 492 ARG A CA 3796 C C . ARG A 492 ? 0.4066 0.3425 0.3387 0.0323 0.0492 -0.0148 492 ARG A C 3797 O O . ARG A 492 ? 0.4070 0.3438 0.3374 0.0303 0.0455 -0.0117 492 ARG A O 3798 C CB . ARG A 492 ? 0.3829 0.3338 0.3456 0.0252 0.0571 -0.0183 492 ARG A CB 3799 C CG . ARG A 492 ? 0.3778 0.3265 0.3446 0.0227 0.0625 -0.0158 492 ARG A CG 3800 C CD . ARG A 492 ? 0.3851 0.3372 0.3654 0.0173 0.0707 -0.0166 492 ARG A CD 3801 N NE . ARG A 492 ? 0.3842 0.3294 0.3663 0.0160 0.0792 -0.0139 492 ARG A NE 3802 C CZ . ARG A 492 ? 0.3880 0.3281 0.3731 0.0093 0.0817 -0.0164 492 ARG A CZ 3803 N NH1 . ARG A 492 ? 0.3787 0.3213 0.3654 0.0023 0.0751 -0.0220 492 ARG A NH1 3804 N NH2 . ARG A 492 ? 0.3977 0.3282 0.3823 0.0102 0.0922 -0.0127 492 ARG A NH2 3805 N N . ASP A 493 ? 0.4325 0.3617 0.3538 0.0389 0.0543 -0.0135 493 ASP A N 3806 C CA . ASP A 493 ? 0.4620 0.3824 0.3651 0.0429 0.0544 -0.0095 493 ASP A CA 3807 C C . ASP A 493 ? 0.4490 0.3633 0.3355 0.0387 0.0416 -0.0105 493 ASP A C 3808 O O . ASP A 493 ? 0.4344 0.3518 0.3171 0.0366 0.0370 -0.0055 493 ASP A O 3809 C CB . ASP A 493 ? 0.5144 0.4247 0.4039 0.0512 0.0626 -0.0086 493 ASP A CB 3810 C CG . ASP A 493 ? 0.5496 0.4674 0.4558 0.0548 0.0757 -0.0047 493 ASP A CG 3811 O OD1 . ASP A 493 ? 0.5489 0.4754 0.4715 0.0507 0.0785 -0.0026 493 ASP A OD1 3812 O OD2 . ASP A 493 ? 0.6064 0.5201 0.5086 0.0620 0.0843 -0.0030 493 ASP A OD2 3813 N N . GLU A 494 ? 0.4435 0.3502 0.3211 0.0372 0.0361 -0.0157 494 GLU A N 3814 C CA . GLU A 494 ? 0.4610 0.3604 0.3226 0.0310 0.0235 -0.0172 494 GLU A CA 3815 C C . GLU A 494 ? 0.4415 0.3559 0.3203 0.0242 0.0168 -0.0138 494 GLU A C 3816 O O . GLU A 494 ? 0.4292 0.3465 0.3017 0.0198 0.0087 -0.0089 494 GLU A O 3817 C CB . GLU A 494 ? 0.4809 0.3678 0.3321 0.0309 0.0212 -0.0232 494 GLU A CB 3818 C CG . GLU A 494 ? 0.5003 0.3772 0.3349 0.0225 0.0084 -0.0253 494 GLU A CG 3819 C CD . GLU A 494 ? 0.5141 0.3758 0.3379 0.0234 0.0082 -0.0308 494 GLU A CD 3820 O OE1 . GLU A 494 ? 0.5241 0.3853 0.3544 0.0316 0.0178 -0.0320 494 GLU A OE1 3821 O OE2 . GLU A 494 ? 0.5288 0.3800 0.3390 0.0156 -0.0013 -0.0329 494 GLU A OE2 3822 N N . ALA A 495 ? 0.4119 0.3364 0.3118 0.0234 0.0205 -0.0154 495 ALA A N 3823 C CA . ALA A 495 ? 0.4036 0.3393 0.3177 0.0185 0.0164 -0.0123 495 ALA A CA 3824 C C . ALA A 495 ? 0.3997 0.3434 0.3206 0.0202 0.0202 -0.0039 495 ALA A C 3825 O O . ALA A 495 ? 0.3985 0.3498 0.3223 0.0173 0.0142 0.0026 495 ALA A O 3826 C CB . ALA A 495 ? 0.3993 0.3404 0.3297 0.0172 0.0205 -0.0164 495 ALA A CB 3827 N N . LEU A 496 ? 0.4100 0.3530 0.3347 0.0253 0.0308 -0.0025 496 LEU A N 3828 C CA . LEU A 496 ? 0.4235 0.3725 0.3550 0.0285 0.0369 0.0063 496 LEU A CA 3829 C C . LEU A 496 ? 0.4543 0.4062 0.3730 0.0292 0.0294 0.0143 496 LEU A C 3830 O O . LEU A 496 ? 0.4615 0.4241 0.3878 0.0298 0.0285 0.0243 496 LEU A O 3831 C CB . LEU A 496 ? 0.4366 0.3820 0.3734 0.0331 0.0505 0.0061 496 LEU A CB 3832 C CG . LEU A 496 ? 0.4356 0.3802 0.3867 0.0299 0.0582 0.0006 496 LEU A CG 3833 C CD1 . LEU A 496 ? 0.4537 0.3945 0.4090 0.0326 0.0706 0.0012 496 LEU A CD1 3834 C CD2 . LEU A 496 ? 0.4345 0.3814 0.3949 0.0278 0.0604 0.0036 496 LEU A CD2 3835 N N . ASN A 497 ? 0.4722 0.4141 0.3704 0.0291 0.0243 0.0106 497 ASN A N 3836 C CA A ASN A 497 ? 0.4892 0.4313 0.3696 0.0269 0.0145 0.0168 497 ASN A CA 3837 C CA B ASN A 497 ? 0.4989 0.4410 0.3794 0.0270 0.0146 0.0168 497 ASN A CA 3838 C C . ASN A 497 ? 0.4868 0.4385 0.3700 0.0183 0.0008 0.0206 497 ASN A C 3839 O O . ASN A 497 ? 0.4900 0.4548 0.3748 0.0163 -0.0056 0.0317 497 ASN A O 3840 C CB A ASN A 497 ? 0.5154 0.4386 0.3672 0.0273 0.0120 0.0102 497 ASN A CB 3841 C CB B ASN A 497 ? 0.5389 0.4621 0.3911 0.0276 0.0125 0.0102 497 ASN A CB 3842 C CG A ASN A 497 ? 0.5364 0.4565 0.3642 0.0212 -0.0013 0.0146 497 ASN A CG 3843 C CG B ASN A 497 ? 0.5747 0.4949 0.4109 0.0323 0.0150 0.0166 497 ASN A CG 3844 O OD1 A ASN A 497 ? 0.5549 0.4613 0.3620 0.0140 -0.0110 0.0086 497 ASN A OD1 3845 O OD1 B ASN A 497 ? 0.6269 0.5436 0.4413 0.0274 0.0038 0.0198 497 ASN A OD1 3846 N ND2 A ASN A 497 ? 0.5515 0.4840 0.3812 0.0232 -0.0021 0.0259 497 ASN A ND2 3847 N ND2 B ASN A 497 ? 0.5726 0.4941 0.4188 0.0410 0.0292 0.0190 497 ASN A ND2 3848 N N . ASN A 498 ? 0.4663 0.4135 0.3518 0.0133 -0.0034 0.0129 498 ASN A N 3849 C CA . ASN A 498 ? 0.4706 0.4263 0.3603 0.0046 -0.0155 0.0166 498 ASN A CA 3850 C C . ASN A 498 ? 0.4541 0.4299 0.3701 0.0063 -0.0120 0.0269 498 ASN A C 3851 O O . ASN A 498 ? 0.4579 0.4483 0.3797 0.0013 -0.0210 0.0372 498 ASN A O 3852 C CB . ASN A 498 ? 0.4736 0.4175 0.3583 0.0001 -0.0192 0.0062 498 ASN A CB 3853 C CG . ASN A 498 ? 0.5130 0.4354 0.3677 -0.0034 -0.0253 -0.0010 498 ASN A CG 3854 O OD1 . ASN A 498 ? 0.5482 0.4661 0.3837 -0.0069 -0.0319 0.0022 498 ASN A OD1 3855 N ND2 . ASN A 498 ? 0.5095 0.4174 0.3580 -0.0024 -0.0226 -0.0104 498 ASN A ND2 3856 N N . ARG A 499 ? 0.4378 0.4135 0.3688 0.0129 0.0013 0.0247 499 ARG A N 3857 C CA . ARG A 499 ? 0.4489 0.4373 0.4009 0.0161 0.0082 0.0337 499 ARG A CA 3858 C C . ARG A 499 ? 0.4862 0.4873 0.4446 0.0217 0.0121 0.0484 499 ARG A C 3859 O O . ARG A 499 ? 0.4679 0.4853 0.4395 0.0220 0.0101 0.0614 499 ARG A O 3860 C CB . ARG A 499 ? 0.4336 0.4132 0.3937 0.0204 0.0222 0.0264 499 ARG A CB 3861 C CG . ARG A 499 ? 0.4111 0.3848 0.3719 0.0157 0.0193 0.0163 499 ARG A CG 3862 C CD . ARG A 499 ? 0.4015 0.3675 0.3682 0.0177 0.0313 0.0097 499 ARG A CD 3863 N NE . ARG A 499 ? 0.3864 0.3543 0.3636 0.0207 0.0409 0.0165 499 ARG A NE 3864 C CZ . ARG A 499 ? 0.4089 0.3672 0.3883 0.0226 0.0539 0.0137 499 ARG A CZ 3865 N NH1 . ARG A 499 ? 0.4072 0.3573 0.3826 0.0205 0.0576 0.0050 499 ARG A NH1 3866 N NH2 . ARG A 499 ? 0.4231 0.3788 0.4082 0.0262 0.0642 0.0203 499 ARG A NH2 3867 N N . PHE A 500 ? 0.5464 0.5410 0.4968 0.0271 0.0189 0.0479 500 PHE A N 3868 C CA . PHE A 500 ? 0.5993 0.6040 0.5561 0.0346 0.0260 0.0622 500 PHE A CA 3869 C C . PHE A 500 ? 0.6934 0.7044 0.6349 0.0326 0.0147 0.0689 500 PHE A C 3870 O O . PHE A 500 ? 0.7347 0.7473 0.6733 0.0397 0.0214 0.0763 500 PHE A O 3871 C CB . PHE A 500 ? 0.6042 0.5967 0.5643 0.0425 0.0441 0.0589 500 PHE A CB 3872 C CG . PHE A 500 ? 0.5887 0.5721 0.5592 0.0421 0.0543 0.0514 500 PHE A CG 3873 C CD1 . PHE A 500 ? 0.5839 0.5742 0.5668 0.0425 0.0561 0.0577 500 PHE A CD1 3874 C CD2 . PHE A 500 ? 0.6102 0.5786 0.5774 0.0408 0.0619 0.0390 500 PHE A CD2 3875 C CE1 . PHE A 500 ? 0.6049 0.5838 0.5924 0.0416 0.0654 0.0501 500 PHE A CE1 3876 C CE2 . PHE A 500 ? 0.6077 0.5675 0.5814 0.0382 0.0693 0.0319 500 PHE A CE2 3877 C CZ . PHE A 500 ? 0.5989 0.5621 0.5806 0.0386 0.0712 0.0367 500 PHE A CZ 3878 N N . GLN A 501 ? 0.7717 0.7847 0.7013 0.0223 -0.0023 0.0663 501 GLN A N 3879 C CA . GLN A 501 ? 0.8576 0.8782 0.7709 0.0169 -0.0165 0.0742 501 GLN A CA 3880 C C . GLN A 501 ? 0.9271 0.9768 0.8600 0.0174 -0.0208 0.0948 501 GLN A C 3881 O O . GLN A 501 ? 0.9647 1.0260 0.9202 0.0187 -0.0171 0.1005 501 GLN A O 3882 C CB . GLN A 501 ? 0.8759 0.8855 0.7681 0.0035 -0.0331 0.0643 501 GLN A CB 3883 C CG . GLN A 501 ? 0.8788 0.8991 0.7857 -0.0051 -0.0418 0.0661 501 GLN A CG 3884 C CD . GLN A 501 ? 0.9146 0.9200 0.7984 -0.0188 -0.0569 0.0561 501 GLN A CD 3885 O OE1 . GLN A 501 ? 0.9453 0.9511 0.8094 -0.0287 -0.0713 0.0599 501 GLN A OE1 3886 N NE2 . GLN A 501 ? 0.8920 0.8830 0.7765 -0.0200 -0.0538 0.0438 501 GLN A NE2 3887 N N . ILE A 502 ? 1.0102 1.0722 0.9343 0.0171 -0.0284 0.1071 502 ILE A N 3888 C CA . ILE A 502 ? 1.0306 1.1252 0.9741 0.0173 -0.0345 0.1300 502 ILE A CA 3889 C C . ILE A 502 ? 1.0769 1.1838 1.0089 -0.0001 -0.0592 0.1339 502 ILE A C 3890 O O . ILE A 502 ? 1.1342 1.2301 1.0362 -0.0084 -0.0714 0.1284 502 ILE A O 3891 C CB . ILE A 502 ? 1.0363 1.1418 0.9820 0.0296 -0.0256 0.1453 502 ILE A CB 3892 C CG1 . ILE A 502 ? 1.0380 1.1811 1.0084 0.0320 -0.0301 0.1721 502 ILE A CG1 3893 C CG2 . ILE A 502 ? 1.0651 1.1581 0.9779 0.0256 -0.0343 0.1399 502 ILE A CG2 3894 C CD1 . ILE A 502 ? 1.0355 1.1892 1.0174 0.0491 -0.0139 0.1894 502 ILE A CD1 3895 N N . LYS A 503 ? 1.0602 1.1873 1.0141 -0.0064 -0.0660 0.1429 503 LYS A N 3896 C CA . LYS A 503 ? 1.0744 1.2160 1.0218 -0.0252 -0.0897 0.1486 503 LYS A CA 3897 C C . LYS A 503 ? 1.0849 1.2674 1.0515 -0.0256 -0.0984 0.1765 503 LYS A C 3898 O O . LYS A 503 ? 1.1288 1.3216 1.0779 -0.0385 -0.1177 0.1832 503 LYS A O 3899 C CB . LYS A 503 ? 1.0622 1.2035 1.0237 -0.0331 -0.0927 0.1434 503 LYS A CB 3900 C CG . LYS A 503 ? 1.0535 1.1610 1.0054 -0.0288 -0.0805 0.1201 503 LYS A CG 3901 C CD . LYS A 503 ? 1.0439 1.1487 1.0009 -0.0403 -0.0885 0.1143 503 LYS A CD 3902 C CE . LYS A 503 ? 1.0260 1.1089 0.9866 -0.0320 -0.0732 0.0984 503 LYS A CE 3903 N NZ . LYS A 503 ? 1.0120 1.0914 0.9758 -0.0427 -0.0807 0.0933 503 LYS A NZ # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'NAG A 1506 WRONG CHIRALITY AT 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 1504 1504 NAG NAG A . C 2 NAG 1 1505 1505 NAG NAG A . D 2 NAG 1 1506 1506 NAG NAG A . E 2 NAG 1 1507 1507 NAG NAG A . F 2 NAG 2 1508 1508 NAG NAG A . G 3 MAN 3 1509 1509 MAN MAN A . H 2 NAG 1 1510 1510 NAG NAG A . I 2 NAG 1 1511 1511 NAG NAG A . J 2 NAG 2 1512 1512 NAG NAG A . K 4 EPE 1 1513 1513 EPE EPE A . L 4 EPE 1 1514 1514 EPE EPE A . M 5 SIA 1 1515 1515 SIA SIA A . N 6 GAL 2 1516 1516 GAL GAL A . O 2 NAG 3 1517 1517 NAG NAG A . P 7 TAM 1 1518 1518 TAM TAM A . Q 8 HOH 1 2001 2001 HOH HOH A . Q 8 HOH 2 2002 2002 HOH HOH A . Q 8 HOH 3 2003 2003 HOH HOH A . Q 8 HOH 4 2004 2004 HOH HOH A . Q 8 HOH 5 2005 2005 HOH HOH A . Q 8 HOH 6 2006 2006 HOH HOH A . Q 8 HOH 7 2007 2007 HOH HOH A . Q 8 HOH 8 2008 2008 HOH HOH A . Q 8 HOH 9 2009 2009 HOH HOH A . Q 8 HOH 10 2010 2010 HOH HOH A . Q 8 HOH 11 2011 2011 HOH HOH A . Q 8 HOH 12 2012 2012 HOH HOH A . Q 8 HOH 13 2013 2013 HOH HOH A . Q 8 HOH 14 2014 2014 HOH HOH A . Q 8 HOH 15 2015 2015 HOH HOH A . Q 8 HOH 16 2016 2016 HOH HOH A . Q 8 HOH 17 2017 2017 HOH HOH A . Q 8 HOH 18 2018 2018 HOH HOH A . Q 8 HOH 19 2019 2019 HOH HOH A . Q 8 HOH 20 2020 2020 HOH HOH A . Q 8 HOH 21 2021 2021 HOH HOH A . Q 8 HOH 22 2022 2022 HOH HOH A . Q 8 HOH 23 2023 2023 HOH HOH A . Q 8 HOH 24 2024 2024 HOH HOH A . Q 8 HOH 25 2025 2025 HOH HOH A . Q 8 HOH 26 2026 2026 HOH HOH A . Q 8 HOH 27 2027 2027 HOH HOH A . Q 8 HOH 28 2028 2028 HOH HOH A . Q 8 HOH 29 2029 2029 HOH HOH A . Q 8 HOH 30 2030 2030 HOH HOH A . Q 8 HOH 31 2031 2031 HOH HOH A . Q 8 HOH 32 2032 2032 HOH HOH A . Q 8 HOH 33 2033 2033 HOH HOH A . Q 8 HOH 34 2034 2034 HOH HOH A . Q 8 HOH 35 2035 2035 HOH HOH A . Q 8 HOH 36 2036 2036 HOH HOH A . Q 8 HOH 37 2037 2037 HOH HOH A . Q 8 HOH 38 2038 2038 HOH HOH A . Q 8 HOH 39 2039 2039 HOH HOH A . Q 8 HOH 40 2040 2040 HOH HOH A . Q 8 HOH 41 2041 2041 HOH HOH A . Q 8 HOH 42 2042 2042 HOH HOH A . Q 8 HOH 43 2043 2043 HOH HOH A . Q 8 HOH 44 2044 2044 HOH HOH A . Q 8 HOH 45 2045 2045 HOH HOH A . Q 8 HOH 46 2046 2046 HOH HOH A . Q 8 HOH 47 2047 2047 HOH HOH A . Q 8 HOH 48 2048 2048 HOH HOH A . Q 8 HOH 49 2049 2049 HOH HOH A . Q 8 HOH 50 2050 2050 HOH HOH A . Q 8 HOH 51 2051 2051 HOH HOH A . Q 8 HOH 52 2052 2052 HOH HOH A . Q 8 HOH 53 2053 2053 HOH HOH A . Q 8 HOH 54 2054 2054 HOH HOH A . Q 8 HOH 55 2055 2055 HOH HOH A . Q 8 HOH 56 2056 2056 HOH HOH A . Q 8 HOH 57 2057 2057 HOH HOH A . Q 8 HOH 58 2058 2058 HOH HOH A . Q 8 HOH 59 2059 2059 HOH HOH A . Q 8 HOH 60 2060 2060 HOH HOH A . Q 8 HOH 61 2061 2061 HOH HOH A . Q 8 HOH 62 2062 2062 HOH HOH A . Q 8 HOH 63 2063 2063 HOH HOH A . Q 8 HOH 64 2064 2064 HOH HOH A . Q 8 HOH 65 2065 2065 HOH HOH A . Q 8 HOH 66 2066 2066 HOH HOH A . Q 8 HOH 67 2067 2067 HOH HOH A . Q 8 HOH 68 2068 2068 HOH HOH A . Q 8 HOH 69 2069 2069 HOH HOH A . Q 8 HOH 70 2070 2070 HOH HOH A . Q 8 HOH 71 2071 2071 HOH HOH A . Q 8 HOH 72 2072 2072 HOH HOH A . Q 8 HOH 73 2073 2073 HOH HOH A . Q 8 HOH 74 2074 2074 HOH HOH A . Q 8 HOH 75 2075 2075 HOH HOH A . Q 8 HOH 76 2076 2076 HOH HOH A . Q 8 HOH 77 2077 2077 HOH HOH A . Q 8 HOH 78 2078 2078 HOH HOH A . Q 8 HOH 79 2079 2079 HOH HOH A . Q 8 HOH 80 2080 2080 HOH HOH A . Q 8 HOH 81 2081 2081 HOH HOH A . Q 8 HOH 82 2082 2082 HOH HOH A . Q 8 HOH 83 2083 2083 HOH HOH A . Q 8 HOH 84 2084 2084 HOH HOH A . Q 8 HOH 85 2085 2085 HOH HOH A . Q 8 HOH 86 2086 2086 HOH HOH A . Q 8 HOH 87 2087 2087 HOH HOH A . Q 8 HOH 88 2088 2088 HOH HOH A . Q 8 HOH 89 2089 2089 HOH HOH A . Q 8 HOH 90 2090 2090 HOH HOH A . Q 8 HOH 91 2091 2091 HOH HOH A . Q 8 HOH 92 2092 2092 HOH HOH A . Q 8 HOH 93 2093 2093 HOH HOH A . Q 8 HOH 94 2094 2094 HOH HOH A . Q 8 HOH 95 2095 2095 HOH HOH A . Q 8 HOH 96 2096 2096 HOH HOH A . Q 8 HOH 97 2097 2097 HOH HOH A . Q 8 HOH 98 2098 2098 HOH HOH A . Q 8 HOH 99 2099 2099 HOH HOH A . Q 8 HOH 100 2100 2100 HOH HOH A . Q 8 HOH 101 2101 2101 HOH HOH A . Q 8 HOH 102 2102 2102 HOH HOH A . Q 8 HOH 103 2103 2103 HOH HOH A . Q 8 HOH 104 2104 2104 HOH HOH A . Q 8 HOH 105 2105 2105 HOH HOH A . Q 8 HOH 106 2106 2106 HOH HOH A . Q 8 HOH 107 2107 2107 HOH HOH A . Q 8 HOH 108 2108 2108 HOH HOH A . Q 8 HOH 109 2109 2109 HOH HOH A . Q 8 HOH 110 2110 2110 HOH HOH A . Q 8 HOH 111 2111 2111 HOH HOH A . Q 8 HOH 112 2112 2112 HOH HOH A . Q 8 HOH 113 2113 2113 HOH HOH A . Q 8 HOH 114 2114 2114 HOH HOH A . Q 8 HOH 115 2115 2115 HOH HOH A . Q 8 HOH 116 2116 2116 HOH HOH A . Q 8 HOH 117 2117 2117 HOH HOH A . Q 8 HOH 118 2118 2118 HOH HOH A . Q 8 HOH 119 2119 2119 HOH HOH A . Q 8 HOH 120 2120 2120 HOH HOH A . Q 8 HOH 121 2121 2121 HOH HOH A . Q 8 HOH 122 2122 2122 HOH HOH A . Q 8 HOH 123 2123 2123 HOH HOH A . Q 8 HOH 124 2124 2124 HOH HOH A . Q 8 HOH 125 2125 2125 HOH HOH A . Q 8 HOH 126 2126 2126 HOH HOH A . Q 8 HOH 127 2127 2127 HOH HOH A . Q 8 HOH 128 2128 2128 HOH HOH A . Q 8 HOH 129 2129 2129 HOH HOH A . Q 8 HOH 130 2130 2130 HOH HOH A . Q 8 HOH 131 2131 2131 HOH HOH A . Q 8 HOH 132 2132 2132 HOH HOH A . Q 8 HOH 133 2133 2133 HOH HOH A . Q 8 HOH 134 2134 2134 HOH HOH A . Q 8 HOH 135 2135 2135 HOH HOH A . Q 8 HOH 136 2136 2136 HOH HOH A . Q 8 HOH 137 2137 2137 HOH HOH A . Q 8 HOH 138 2138 2138 HOH HOH A . Q 8 HOH 139 2139 2139 HOH HOH A . Q 8 HOH 140 2140 2140 HOH HOH A . Q 8 HOH 141 2141 2141 HOH HOH A . Q 8 HOH 142 2142 2142 HOH HOH A . Q 8 HOH 143 2143 2143 HOH HOH A . Q 8 HOH 144 2144 2144 HOH HOH A . Q 8 HOH 145 2145 2145 HOH HOH A . Q 8 HOH 146 2146 2146 HOH HOH A . Q 8 HOH 147 2147 2147 HOH HOH A . Q 8 HOH 148 2148 2148 HOH HOH A . Q 8 HOH 149 2149 2149 HOH HOH A . Q 8 HOH 150 2150 2150 HOH HOH A . Q 8 HOH 151 2151 2151 HOH HOH A . Q 8 HOH 152 2152 2152 HOH HOH A . Q 8 HOH 153 2153 2153 HOH HOH A . Q 8 HOH 154 2154 2154 HOH HOH A . Q 8 HOH 155 2155 2155 HOH HOH A . Q 8 HOH 156 2156 2156 HOH HOH A . Q 8 HOH 157 2157 2157 HOH HOH A . Q 8 HOH 158 2158 2158 HOH HOH A . Q 8 HOH 159 2159 2159 HOH HOH A . Q 8 HOH 160 2160 2160 HOH HOH A . Q 8 HOH 161 2161 2161 HOH HOH A . Q 8 HOH 162 2162 2162 HOH HOH A . Q 8 HOH 163 2163 2163 HOH HOH A . Q 8 HOH 164 2164 2164 HOH HOH A . Q 8 HOH 165 2165 2165 HOH HOH A . Q 8 HOH 166 2166 2166 HOH HOH A . Q 8 HOH 167 2167 2167 HOH HOH A . Q 8 HOH 168 2168 2168 HOH HOH A . Q 8 HOH 169 2169 2169 HOH HOH A . Q 8 HOH 170 2170 2170 HOH HOH A . Q 8 HOH 171 2171 2171 HOH HOH A . Q 8 HOH 172 2172 2172 HOH HOH A . Q 8 HOH 173 2173 2173 HOH HOH A . Q 8 HOH 174 2174 2174 HOH HOH A . Q 8 HOH 175 2175 2175 HOH HOH A . Q 8 HOH 176 2176 2176 HOH HOH A . Q 8 HOH 177 2177 2177 HOH HOH A . Q 8 HOH 178 2178 2178 HOH HOH A . Q 8 HOH 179 2179 2179 HOH HOH A . Q 8 HOH 180 2180 2180 HOH HOH A . Q 8 HOH 181 2181 2181 HOH HOH A . Q 8 HOH 182 2182 2182 HOH HOH A . Q 8 HOH 183 2183 2183 HOH HOH A . Q 8 HOH 184 2184 2184 HOH HOH A . Q 8 HOH 185 2185 2185 HOH HOH A . Q 8 HOH 186 2186 2186 HOH HOH A . Q 8 HOH 187 2187 2187 HOH HOH A . Q 8 HOH 188 2188 2188 HOH HOH A . Q 8 HOH 189 2189 2189 HOH HOH A . Q 8 HOH 190 2190 2190 HOH HOH A . Q 8 HOH 191 2191 2191 HOH HOH A . Q 8 HOH 192 2192 2192 HOH HOH A . Q 8 HOH 193 2193 2193 HOH HOH A . Q 8 HOH 194 2194 2194 HOH HOH A . Q 8 HOH 195 2195 2195 HOH HOH A . Q 8 HOH 196 2196 2196 HOH HOH A . Q 8 HOH 197 2197 2197 HOH HOH A . Q 8 HOH 198 2198 2198 HOH HOH A . Q 8 HOH 199 2199 2199 HOH HOH A . Q 8 HOH 200 2200 2200 HOH HOH A . Q 8 HOH 201 2201 2201 HOH HOH A . Q 8 HOH 202 2202 2202 HOH HOH A . Q 8 HOH 203 2203 2203 HOH HOH A . Q 8 HOH 204 2204 2204 HOH HOH A . Q 8 HOH 205 2205 2205 HOH HOH A . Q 8 HOH 206 2206 2206 HOH HOH A . Q 8 HOH 207 2207 2207 HOH HOH A . Q 8 HOH 208 2208 2208 HOH HOH A . Q 8 HOH 209 2209 2209 HOH HOH A . Q 8 HOH 210 2210 2210 HOH HOH A . Q 8 HOH 211 2211 2211 HOH HOH A . Q 8 HOH 212 2212 2212 HOH HOH A . Q 8 HOH 213 2213 2213 HOH HOH A . Q 8 HOH 214 2214 2214 HOH HOH A . Q 8 HOH 215 2215 2215 HOH HOH A . Q 8 HOH 216 2216 2216 HOH HOH A . Q 8 HOH 217 2217 2217 HOH HOH A . Q 8 HOH 218 2218 2218 HOH HOH A . Q 8 HOH 219 2219 2219 HOH HOH A . Q 8 HOH 220 2220 2220 HOH HOH A . Q 8 HOH 221 2221 2221 HOH HOH A . Q 8 HOH 222 2222 2222 HOH HOH A . Q 8 HOH 223 2223 2223 HOH HOH A . Q 8 HOH 224 2224 2224 HOH HOH A . Q 8 HOH 225 2225 2225 HOH HOH A . Q 8 HOH 226 2226 2226 HOH HOH A . Q 8 HOH 227 2227 2227 HOH HOH A . Q 8 HOH 228 2228 2228 HOH HOH A . Q 8 HOH 229 2229 2229 HOH HOH A . Q 8 HOH 230 2230 2230 HOH HOH A . Q 8 HOH 231 2231 2231 HOH HOH A . Q 8 HOH 232 2232 2232 HOH HOH A . Q 8 HOH 233 2233 2233 HOH HOH A . Q 8 HOH 234 2234 2234 HOH HOH A . Q 8 HOH 235 2235 2235 HOH HOH A . Q 8 HOH 236 2236 2236 HOH HOH A . Q 8 HOH 237 2237 2237 HOH HOH A . Q 8 HOH 238 2238 2238 HOH HOH A . Q 8 HOH 239 2239 2239 HOH HOH A . Q 8 HOH 240 2240 2240 HOH HOH A . Q 8 HOH 241 2241 2241 HOH HOH A . Q 8 HOH 242 2242 2242 HOH HOH A . Q 8 HOH 243 2243 2243 HOH HOH A . Q 8 HOH 244 2244 2244 HOH HOH A . Q 8 HOH 245 2245 2245 HOH HOH A . Q 8 HOH 246 2246 2246 HOH HOH A . Q 8 HOH 247 2247 2247 HOH HOH A . Q 8 HOH 248 2248 2248 HOH HOH A . Q 8 HOH 249 2249 2249 HOH HOH A . Q 8 HOH 250 2250 2250 HOH HOH A . Q 8 HOH 251 2251 2251 HOH HOH A . Q 8 HOH 252 2252 2252 HOH HOH A . Q 8 HOH 253 2253 2253 HOH HOH A . Q 8 HOH 254 2254 2254 HOH HOH A . Q 8 HOH 255 2255 2255 HOH HOH A . Q 8 HOH 256 2256 2256 HOH HOH A . Q 8 HOH 257 2257 2257 HOH HOH A . Q 8 HOH 258 2258 2258 HOH HOH A . Q 8 HOH 259 2259 2259 HOH HOH A . Q 8 HOH 260 2260 2260 HOH HOH A . Q 8 HOH 261 2261 2261 HOH HOH A . Q 8 HOH 262 2262 2262 HOH HOH A . Q 8 HOH 263 2263 2263 HOH HOH A . Q 8 HOH 264 2264 2264 HOH HOH A . Q 8 HOH 265 2265 2265 HOH HOH A . Q 8 HOH 266 2266 2266 HOH HOH A . Q 8 HOH 267 2267 2267 HOH HOH A . Q 8 HOH 268 2268 2268 HOH HOH A . Q 8 HOH 269 2269 2269 HOH HOH A . Q 8 HOH 270 2270 2270 HOH HOH A . Q 8 HOH 271 2271 2271 HOH HOH A . Q 8 HOH 272 2272 2272 HOH HOH A . Q 8 HOH 273 2273 2273 HOH HOH A . Q 8 HOH 274 2274 2274 HOH HOH A . Q 8 HOH 275 2275 2275 HOH HOH A . Q 8 HOH 276 2276 2276 HOH HOH A . Q 8 HOH 277 2277 2277 HOH HOH A . Q 8 HOH 278 2278 2278 HOH HOH A . Q 8 HOH 279 2279 2279 HOH HOH A . Q 8 HOH 280 2280 2280 HOH HOH A . Q 8 HOH 281 2281 2281 HOH HOH A . Q 8 HOH 282 2282 2282 HOH HOH A . Q 8 HOH 283 2283 2283 HOH HOH A . Q 8 HOH 284 2284 2284 HOH HOH A . Q 8 HOH 285 2285 2285 HOH HOH A . Q 8 HOH 286 2286 2286 HOH HOH A . Q 8 HOH 287 2287 2287 HOH HOH A . Q 8 HOH 288 2288 2288 HOH HOH A . Q 8 HOH 289 2289 2289 HOH HOH A . Q 8 HOH 290 2290 2290 HOH HOH A . Q 8 HOH 291 2291 2291 HOH HOH A . Q 8 HOH 292 2292 2292 HOH HOH A . Q 8 HOH 293 2293 2293 HOH HOH A . Q 8 HOH 294 2294 2294 HOH HOH A . Q 8 HOH 295 2295 2295 HOH HOH A . Q 8 HOH 296 2296 2296 HOH HOH A . Q 8 HOH 297 2297 2297 HOH HOH A . Q 8 HOH 298 2298 2298 HOH HOH A . Q 8 HOH 299 2299 2299 HOH HOH A . Q 8 HOH 300 2300 2300 HOH HOH A . Q 8 HOH 301 2301 2301 HOH HOH A . Q 8 HOH 302 2302 2302 HOH HOH A . Q 8 HOH 303 2303 2303 HOH HOH A . Q 8 HOH 304 2304 2304 HOH HOH A . Q 8 HOH 305 2305 2305 HOH HOH A . Q 8 HOH 306 2306 2306 HOH HOH A . Q 8 HOH 307 2307 2307 HOH HOH A . Q 8 HOH 308 2308 2308 HOH HOH A . Q 8 HOH 309 2309 2309 HOH HOH A . Q 8 HOH 310 2310 2310 HOH HOH A . Q 8 HOH 311 2311 2311 HOH HOH A . Q 8 HOH 312 2312 2312 HOH HOH A . Q 8 HOH 313 2313 2313 HOH HOH A . Q 8 HOH 314 2314 2314 HOH HOH A . Q 8 HOH 315 2315 2315 HOH HOH A . Q 8 HOH 316 2316 2316 HOH HOH A . Q 8 HOH 317 2317 2317 HOH HOH A . Q 8 HOH 318 2318 2318 HOH HOH A . Q 8 HOH 319 2319 2319 HOH HOH A . Q 8 HOH 320 2320 2320 HOH HOH A . Q 8 HOH 321 2321 2321 HOH HOH A . Q 8 HOH 322 2322 2322 HOH HOH A . Q 8 HOH 323 2323 2323 HOH HOH A . Q 8 HOH 324 2324 2324 HOH HOH A . Q 8 HOH 325 2325 2325 HOH HOH A . Q 8 HOH 326 2326 2326 HOH HOH A . Q 8 HOH 327 2327 2327 HOH HOH A . Q 8 HOH 328 2328 2328 HOH HOH A . Q 8 HOH 329 2329 2329 HOH HOH A . Q 8 HOH 330 2330 2330 HOH HOH A . Q 8 HOH 331 2331 2331 HOH HOH A . Q 8 HOH 332 2332 2332 HOH HOH A . Q 8 HOH 333 2333 2333 HOH HOH A . Q 8 HOH 334 2334 2334 HOH HOH A . Q 8 HOH 335 2335 2335 HOH HOH A . Q 8 HOH 336 2336 2336 HOH HOH A . Q 8 HOH 337 2337 2337 HOH HOH A . Q 8 HOH 338 2338 2338 HOH HOH A . Q 8 HOH 339 2339 2339 HOH HOH A . Q 8 HOH 340 2340 2340 HOH HOH A . Q 8 HOH 341 2341 2341 HOH HOH A . Q 8 HOH 342 2342 2342 HOH HOH A . Q 8 HOH 343 2343 2343 HOH HOH A . Q 8 HOH 344 2344 2344 HOH HOH A . Q 8 HOH 345 2345 2345 HOH HOH A . Q 8 HOH 346 2346 2346 HOH HOH A . Q 8 HOH 347 2347 2347 HOH HOH A . Q 8 HOH 348 2348 2348 HOH HOH A . Q 8 HOH 349 2349 2349 HOH HOH A . Q 8 HOH 350 2350 2350 HOH HOH A . Q 8 HOH 351 2351 2351 HOH HOH A . Q 8 HOH 352 2352 2352 HOH HOH A . Q 8 HOH 353 2353 2353 HOH HOH A . Q 8 HOH 354 2354 2354 HOH HOH A . Q 8 HOH 355 2355 2355 HOH HOH A . Q 8 HOH 356 2356 2356 HOH HOH A . Q 8 HOH 357 2357 2357 HOH HOH A . Q 8 HOH 358 2358 2358 HOH HOH A . Q 8 HOH 359 2359 2359 HOH HOH A . Q 8 HOH 360 2360 2360 HOH HOH A . Q 8 HOH 361 2361 2361 HOH HOH A . Q 8 HOH 362 2362 2362 HOH HOH A . Q 8 HOH 363 2363 2363 HOH HOH A . Q 8 HOH 364 2364 2364 HOH HOH A . Q 8 HOH 365 2365 2365 HOH HOH A . Q 8 HOH 366 2366 2366 HOH HOH A . Q 8 HOH 367 2367 2367 HOH HOH A . Q 8 HOH 368 2368 2368 HOH HOH A . Q 8 HOH 369 2369 2369 HOH HOH A . Q 8 HOH 370 2370 2370 HOH HOH A . Q 8 HOH 371 2371 2371 HOH HOH A . Q 8 HOH 372 2372 2372 HOH HOH A . Q 8 HOH 373 2373 2373 HOH HOH A . Q 8 HOH 374 2374 2374 HOH HOH A . Q 8 HOH 375 2375 2375 HOH HOH A . Q 8 HOH 376 2376 2376 HOH HOH A . Q 8 HOH 377 2377 2377 HOH HOH A . Q 8 HOH 378 2378 2378 HOH HOH A . Q 8 HOH 379 2379 2379 HOH HOH A . Q 8 HOH 380 2380 2380 HOH HOH A . Q 8 HOH 381 2381 2381 HOH HOH A . Q 8 HOH 382 2382 2382 HOH HOH A . Q 8 HOH 383 2383 2383 HOH HOH A . Q 8 HOH 384 2384 2384 HOH HOH A . Q 8 HOH 385 2385 2385 HOH HOH A . Q 8 HOH 386 2386 2386 HOH HOH A . Q 8 HOH 387 2387 2387 HOH HOH A . Q 8 HOH 388 2388 2388 HOH HOH A . Q 8 HOH 389 2389 2389 HOH HOH A . Q 8 HOH 390 2390 2390 HOH HOH A . Q 8 HOH 391 2391 2391 HOH HOH A . Q 8 HOH 392 2392 2392 HOH HOH A . Q 8 HOH 393 2393 2393 HOH HOH A . Q 8 HOH 394 2394 2394 HOH HOH A . Q 8 HOH 395 2395 2395 HOH HOH A . Q 8 HOH 396 2396 2396 HOH HOH A . Q 8 HOH 397 2397 2397 HOH HOH A . Q 8 HOH 398 2398 2398 HOH HOH A . Q 8 HOH 399 2399 2399 HOH HOH A . Q 8 HOH 400 2400 2400 HOH HOH A . Q 8 HOH 401 2401 2401 HOH HOH A . Q 8 HOH 402 2402 2402 HOH HOH A . Q 8 HOH 403 2403 2403 HOH HOH A . Q 8 HOH 404 2404 2404 HOH HOH A . Q 8 HOH 405 2405 2405 HOH HOH A . Q 8 HOH 406 2406 2406 HOH HOH A . Q 8 HOH 407 2407 2407 HOH HOH A . Q 8 HOH 408 2408 2408 HOH HOH A . Q 8 HOH 409 2409 2409 HOH HOH A . Q 8 HOH 410 2410 2410 HOH HOH A . Q 8 HOH 411 2411 2411 HOH HOH A . Q 8 HOH 412 2412 2412 HOH HOH A . Q 8 HOH 413 2413 2413 HOH HOH A . Q 8 HOH 414 2414 2414 HOH HOH A . Q 8 HOH 415 2415 2415 HOH HOH A . Q 8 HOH 416 2416 2416 HOH HOH A . Q 8 HOH 417 2417 2417 HOH HOH A . Q 8 HOH 418 2418 2418 HOH HOH A . Q 8 HOH 419 2419 2419 HOH HOH A . Q 8 HOH 420 2420 2420 HOH HOH A . Q 8 HOH 421 2421 2421 HOH HOH A . Q 8 HOH 422 2422 2422 HOH HOH A . Q 8 HOH 423 2423 2423 HOH HOH A . Q 8 HOH 424 2424 2424 HOH HOH A . Q 8 HOH 425 2425 2425 HOH HOH A . Q 8 HOH 426 2426 2426 HOH HOH A . Q 8 HOH 427 2427 2427 HOH HOH A . Q 8 HOH 428 2428 2428 HOH HOH A . Q 8 HOH 429 2429 2429 HOH HOH A . Q 8 HOH 430 2430 2430 HOH HOH A . Q 8 HOH 431 2431 2431 HOH HOH A . Q 8 HOH 432 2432 2432 HOH HOH A . Q 8 HOH 433 2433 2433 HOH HOH A . Q 8 HOH 434 2434 2434 HOH HOH A . Q 8 HOH 435 2435 2435 HOH HOH A . Q 8 HOH 436 2436 2436 HOH HOH A . Q 8 HOH 437 2437 2437 HOH HOH A . Q 8 HOH 438 2438 2438 HOH HOH A . Q 8 HOH 439 2439 2439 HOH HOH A . Q 8 HOH 440 2440 2440 HOH HOH A . Q 8 HOH 441 2441 2441 HOH HOH A . Q 8 HOH 442 2442 2442 HOH HOH A . Q 8 HOH 443 2443 2443 HOH HOH A . Q 8 HOH 444 2444 2444 HOH HOH A . Q 8 HOH 445 2445 2445 HOH HOH A . Q 8 HOH 446 2446 2446 HOH HOH A . Q 8 HOH 447 2447 2447 HOH HOH A . Q 8 HOH 448 2448 2448 HOH HOH A . Q 8 HOH 449 2449 2449 HOH HOH A . Q 8 HOH 450 2450 2450 HOH HOH A . Q 8 HOH 451 2451 2451 HOH HOH A . Q 8 HOH 452 2452 2452 HOH HOH A . Q 8 HOH 453 2453 2453 HOH HOH A . Q 8 HOH 454 2454 2454 HOH HOH A . Q 8 HOH 455 2455 2455 HOH HOH A . Q 8 HOH 456 2456 2456 HOH HOH A . Q 8 HOH 457 2457 2457 HOH HOH A . Q 8 HOH 458 2458 2458 HOH HOH A . Q 8 HOH 459 2459 2459 HOH HOH A . Q 8 HOH 460 2460 2460 HOH HOH A . Q 8 HOH 461 2461 2461 HOH HOH A . Q 8 HOH 462 2462 2462 HOH HOH A . Q 8 HOH 463 2463 2463 HOH HOH A . Q 8 HOH 464 2464 2464 HOH HOH A . Q 8 HOH 465 2465 2465 HOH HOH A . Q 8 HOH 466 2466 2466 HOH HOH A . Q 8 HOH 467 2467 2467 HOH HOH A . Q 8 HOH 468 2468 2468 HOH HOH A . Q 8 HOH 469 2469 2469 HOH HOH A . Q 8 HOH 470 2470 2470 HOH HOH A . Q 8 HOH 471 2471 2471 HOH HOH A . Q 8 HOH 472 2472 2472 HOH HOH A . Q 8 HOH 473 2473 2473 HOH HOH A . Q 8 HOH 474 2474 2474 HOH HOH A . Q 8 HOH 475 2475 2475 HOH HOH A . Q 8 HOH 476 2476 2476 HOH HOH A . Q 8 HOH 477 2477 2477 HOH HOH A . Q 8 HOH 478 2478 2478 HOH HOH A . Q 8 HOH 479 2479 2479 HOH HOH A . Q 8 HOH 480 2480 2480 HOH HOH A . Q 8 HOH 481 2481 2481 HOH HOH A . Q 8 HOH 482 2482 2482 HOH HOH A . Q 8 HOH 483 2483 2483 HOH HOH A . Q 8 HOH 484 2484 2484 HOH HOH A . Q 8 HOH 485 2485 2485 HOH HOH A . Q 8 HOH 486 2486 2486 HOH HOH A . Q 8 HOH 487 2487 2487 HOH HOH A . Q 8 HOH 488 2488 2488 HOH HOH A . Q 8 HOH 489 2489 2489 HOH HOH A . Q 8 HOH 490 2490 2490 HOH HOH A . Q 8 HOH 491 2491 2491 HOH HOH A . Q 8 HOH 492 2492 2492 HOH HOH A . Q 8 HOH 493 2493 2493 HOH HOH A . Q 8 HOH 494 2494 2494 HOH HOH A . Q 8 HOH 495 2495 2495 HOH HOH A . Q 8 HOH 496 2496 2496 HOH HOH A . Q 8 HOH 497 2497 2497 HOH HOH A . Q 8 HOH 498 2498 2498 HOH HOH A . Q 8 HOH 499 2499 2499 HOH HOH A . Q 8 HOH 500 2500 2500 HOH HOH A . Q 8 HOH 501 2501 2501 HOH HOH A . Q 8 HOH 502 2502 2502 HOH HOH A . Q 8 HOH 503 2503 2503 HOH HOH A . Q 8 HOH 504 2504 2504 HOH HOH A . Q 8 HOH 505 2505 2505 HOH HOH A . Q 8 HOH 506 2506 2506 HOH HOH A . Q 8 HOH 507 2507 2507 HOH HOH A . Q 8 HOH 508 2508 2508 HOH HOH A . Q 8 HOH 509 2509 2509 HOH HOH A . Q 8 HOH 510 2510 2510 HOH HOH A . Q 8 HOH 511 2511 2511 HOH HOH A . Q 8 HOH 512 2512 2512 HOH HOH A . Q 8 HOH 513 2513 2513 HOH HOH A . Q 8 HOH 514 2514 2514 HOH HOH A . Q 8 HOH 515 2515 2515 HOH HOH A . Q 8 HOH 516 2516 2516 HOH HOH A . Q 8 HOH 517 2517 2517 HOH HOH A . Q 8 HOH 518 2518 2518 HOH HOH A . Q 8 HOH 519 2519 2519 HOH HOH A . Q 8 HOH 520 2520 2520 HOH HOH A . Q 8 HOH 521 2521 2521 HOH HOH A . Q 8 HOH 522 2522 2522 HOH HOH A . Q 8 HOH 523 2523 2523 HOH HOH A . Q 8 HOH 524 2524 2524 HOH HOH A . Q 8 HOH 525 2525 2525 HOH HOH A . Q 8 HOH 526 2526 2526 HOH HOH A . Q 8 HOH 527 2527 2527 HOH HOH A . Q 8 HOH 528 2528 2528 HOH HOH A . Q 8 HOH 529 2529 2529 HOH HOH A . Q 8 HOH 530 2530 2530 HOH HOH A . Q 8 HOH 531 2531 2531 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' # _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 # 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)' 28080 ? 1 MORE 143.8 ? 1 'SSA (A^2)' 60060 ? # 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_565 -y,x-y+1,z -0.5000000000 -0.8660254038 0.0000000000 -50.5650000000 0.8660254038 -0.5000000000 0.0000000000 87.5811490847 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 3_455 -x+y-1,-x,z -0.5000000000 0.8660254038 0.0000000000 -101.1300000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # _pdbx_struct_special_symmetry.id 1 _pdbx_struct_special_symmetry.PDB_model_num 1 _pdbx_struct_special_symmetry.auth_asym_id A _pdbx_struct_special_symmetry.auth_comp_id HOH _pdbx_struct_special_symmetry.auth_seq_id 2531 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id Q _pdbx_struct_special_symmetry.label_comp_id HOH _pdbx_struct_special_symmetry.label_seq_id . # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 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 -42.7405 9.7399 74.5415 0.0507 0.0870 0.0795 0.0054 -0.0377 0.0519 0.1143 0.1071 0.7234 -0.0232 -0.0328 -0.1257 0.0178 -0.0881 -0.0816 0.0120 0.0554 0.0143 0.0514 0.0195 -0.0732 'X-RAY DIFFRACTION' 2 ? refined -44.7413 13.7962 68.9092 0.0546 0.0661 0.0682 0.0047 -0.0378 0.0264 0.1166 0.0928 0.4477 0.0050 0.0424 -0.0114 0.0323 -0.0473 -0.0802 0.0019 0.0559 0.0047 0.0211 0.0192 -0.0882 'X-RAY DIFFRACTION' 3 ? refined -50.0516 16.0178 32.6579 0.0621 0.0665 0.0736 -0.0207 -0.0371 -0.0173 0.0185 0.1514 1.7646 0.0165 0.1109 0.2167 0.0266 0.0087 -0.0287 -0.0178 0.0856 0.0048 0.0364 0.0837 -0.1123 'X-RAY DIFFRACTION' 4 ? refined -46.2903 17.9787 -4.7904 0.0843 0.0378 0.0408 0.0039 0.0108 -0.0289 0.9967 1.8579 2.2519 0.0432 -0.8637 -1.3627 0.1414 0.0464 0.0851 -0.1136 0.0111 -0.0252 0.0562 0.0249 -0.1525 # 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 202 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 203 ? ? A 325 ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 326 ? ? 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 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O A HOH 2034 ? ? O A HOH 2035 ? ? 0.00 2 1 O A HOH 2069 ? ? O A HOH 2070 ? ? 0.00 # _pdbx_validate_rmsd_bond.id 1 _pdbx_validate_rmsd_bond.PDB_model_num 1 _pdbx_validate_rmsd_bond.auth_atom_id_1 CG _pdbx_validate_rmsd_bond.auth_asym_id_1 A _pdbx_validate_rmsd_bond.auth_comp_id_1 HIS _pdbx_validate_rmsd_bond.auth_seq_id_1 355 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 ? _pdbx_validate_rmsd_bond.auth_atom_id_2 CD2 _pdbx_validate_rmsd_bond.auth_asym_id_2 A _pdbx_validate_rmsd_bond.auth_comp_id_2 HIS _pdbx_validate_rmsd_bond.auth_seq_id_2 355 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 ? _pdbx_validate_rmsd_bond.bond_value 1.408 _pdbx_validate_rmsd_bond.bond_target_value 1.354 _pdbx_validate_rmsd_bond.bond_deviation 0.054 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.009 _pdbx_validate_rmsd_bond.linker_flag N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 22 ? ? -116.87 73.54 2 1 GLU A 62 ? ? 54.44 -118.99 3 1 ASN A 96 ? ? -140.04 45.87 4 1 CYS A 97 ? ? -143.51 -155.23 5 1 TRP A 127 ? ? -100.43 53.13 6 1 SER A 143 ? ? 64.11 -7.17 7 1 ALA A 196 ? ? 80.06 0.27 8 1 ASN A 341 ? ? -168.69 116.92 9 1 PHE A 392 ? ? -123.22 -112.83 10 1 GLN A 394 ? ? -128.01 -130.60 11 1 GLN A 394 ? ? -129.27 -129.08 12 1 ARG A 456 ? ? 54.67 -124.95 13 1 TYR A 470 ? ? -91.52 35.91 # _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 1506 _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 2530 ? . 6.79 2 1 O ? A HOH 2531 ? 7.35 . # 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 'O-SIALIC ACID' SIA 6 BETA-D-GALACTOSE GAL 7 'TRIS(HYDROXYETHYL)AMINOMETHANE' TAM 8 water HOH #