data_3FW9 # _entry.id 3FW9 # _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 3FW9 RCSB RCSB051120 WWPDB D_1000051120 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3d2d . unspecified PDB 3d2h . unspecified PDB 3d2j . unspecified PDB 3fw7 . unspecified PDB 3fw8 . unspecified # _pdbx_database_status.entry_id 3FW9 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.recvd_initial_deposition_date 2009-01-17 _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Winkler, A.' 1 'Macheroux, P.' 2 'Gruber, K.' 3 # loop_ _citation.id _citation.title _citation.journal_abbrev _citation.journal_volume _citation.page_first _citation.page_last _citation.year _citation.journal_id_ASTM _citation.country _citation.journal_id_ISSN _citation.journal_id_CSD _citation.book_publisher _citation.pdbx_database_id_PubMed _citation.pdbx_database_id_DOI primary 'Structural roles of biocovalent flaninylation in berberine bridge enzyme' 'to be published' ? ? ? ? ? ? ? 0353 ? ? ? 1 'A concerted mechanism for berberine bridge enzyme.' 'Nat. Chem. Biol.' 4 739 741 2008 ? US 1552-4450 ? ? ? ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Winkler, A.' 1 primary 'Motz, K.' 2 primary 'Riedl, S.' 3 primary 'Puhl, M.' 4 primary 'Macheroux, P.' 5 primary 'Gruber, K.' 6 1 'Winkler, A.' 7 1 'Lyskowski, A.' 8 1 'Riedl, S.' 9 1 'Puhl, M.' 10 1 'Kutchan, T.M.' 11 1 'Macheroux, P.' 12 1 'Gruber, K.' 13 # _cell.length_a 68.720 _cell.length_b 68.720 _cell.length_c 247.170 _cell.angle_alpha 90.000 _cell.angle_beta 90.000 _cell.angle_gamma 90.000 _cell.entry_id 3FW9 _cell.pdbx_unique_axis ? _cell.Z_PDB 8 _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.space_group_name_H-M 'P 41 21 2' _symmetry.entry_id 3FW9 _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.Int_Tables_number 92 _symmetry.cell_setting ? _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'Reticuline oxidase' 55364.676 1 1.21.3.3 ? ? ? 2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550 1 ? ? ? ? 3 non-polymer syn '(13aS)-3,10-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquino[3,2-a]isoquinoline-2,9-diol' 327.374 1 ? ? ? ? 4 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 3 ? ? ? ? 6 non-polymer syn 'MAGNESIUM ION' 24.305 1 ? ? ? ? 7 water nat water 18.015 603 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'Berberine bridge-forming enzyme, BBE, Tetrahydroprotoberberine synthase' # _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 ;DLLSCLTFNGVRNHTVFSADSDSDFNRFLHLSIQNPLFQNSLISKPSAIILPGSKEELSNTIRCIRKGSWTIRLRSGGHS YEGLSYTSDTPFILIDLMNLNRVSIDLESETAWVESGSTLGELYYAITESSSKLGFTAGWCPTVGTGGHISGGGFGMMSR KYGLAADNVVDAILIDANGAILDRQAMGEDVFWAIRGGGGGVWGAIYAWKIKLLPVPEKVTVFRVTKNVAIDEATSLLHK WQFVAEELEEDFTLSVLGGADEKQVWLTMLGFHFGLKTVAKSTFDLLFPELGLVEEDYLEMSWGESFAYLAGLETVSQLN NRFLKFDERAFKTKVDLTKEPLPSKAFYGLLERLSKEPNGFIALNGFGGQMSKISSDFTPFPHRSGTRLMVEYIVAWNQS EQKKKTEFLDWLEKVYEFMKPFVSKNPRLGYVNHIDLDLGGIDWGNKTVVNNAIEISRSWGESYFLSNYERLIRAKTLID PNNVFNHPQSIPPMA ; _entity_poly.pdbx_seq_one_letter_code_can ;DLLSCLTFNGVRNHTVFSADSDSDFNRFLHLSIQNPLFQNSLISKPSAIILPGSKEELSNTIRCIRKGSWTIRLRSGGHS YEGLSYTSDTPFILIDLMNLNRVSIDLESETAWVESGSTLGELYYAITESSSKLGFTAGWCPTVGTGGHISGGGFGMMSR KYGLAADNVVDAILIDANGAILDRQAMGEDVFWAIRGGGGGVWGAIYAWKIKLLPVPEKVTVFRVTKNVAIDEATSLLHK WQFVAEELEEDFTLSVLGGADEKQVWLTMLGFHFGLKTVAKSTFDLLFPELGLVEEDYLEMSWGESFAYLAGLETVSQLN NRFLKFDERAFKTKVDLTKEPLPSKAFYGLLERLSKEPNGFIALNGFGGQMSKISSDFTPFPHRSGTRLMVEYIVAWNQS EQKKKTEFLDWLEKVYEFMKPFVSKNPRLGYVNHIDLDLGGIDWGNKTVVNNAIEISRSWGESYFLSNYERLIRAKTLID PNNVFNHPQSIPPMA ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ASP n 1 2 LEU n 1 3 LEU n 1 4 SER n 1 5 CYS n 1 6 LEU n 1 7 THR n 1 8 PHE n 1 9 ASN n 1 10 GLY n 1 11 VAL n 1 12 ARG n 1 13 ASN n 1 14 HIS n 1 15 THR n 1 16 VAL n 1 17 PHE n 1 18 SER n 1 19 ALA n 1 20 ASP n 1 21 SER n 1 22 ASP n 1 23 SER n 1 24 ASP n 1 25 PHE n 1 26 ASN n 1 27 ARG n 1 28 PHE n 1 29 LEU n 1 30 HIS n 1 31 LEU n 1 32 SER n 1 33 ILE n 1 34 GLN n 1 35 ASN n 1 36 PRO n 1 37 LEU n 1 38 PHE n 1 39 GLN n 1 40 ASN n 1 41 SER n 1 42 LEU n 1 43 ILE n 1 44 SER n 1 45 LYS n 1 46 PRO n 1 47 SER n 1 48 ALA n 1 49 ILE n 1 50 ILE n 1 51 LEU n 1 52 PRO n 1 53 GLY n 1 54 SER n 1 55 LYS n 1 56 GLU n 1 57 GLU n 1 58 LEU n 1 59 SER n 1 60 ASN n 1 61 THR n 1 62 ILE n 1 63 ARG n 1 64 CYS n 1 65 ILE n 1 66 ARG n 1 67 LYS n 1 68 GLY n 1 69 SER n 1 70 TRP n 1 71 THR n 1 72 ILE n 1 73 ARG n 1 74 LEU n 1 75 ARG n 1 76 SER n 1 77 GLY n 1 78 GLY n 1 79 HIS n 1 80 SER n 1 81 TYR n 1 82 GLU n 1 83 GLY n 1 84 LEU n 1 85 SER n 1 86 TYR n 1 87 THR n 1 88 SER n 1 89 ASP n 1 90 THR n 1 91 PRO n 1 92 PHE n 1 93 ILE n 1 94 LEU n 1 95 ILE n 1 96 ASP n 1 97 LEU n 1 98 MET n 1 99 ASN n 1 100 LEU n 1 101 ASN n 1 102 ARG n 1 103 VAL n 1 104 SER n 1 105 ILE n 1 106 ASP n 1 107 LEU n 1 108 GLU n 1 109 SER n 1 110 GLU n 1 111 THR n 1 112 ALA n 1 113 TRP n 1 114 VAL n 1 115 GLU n 1 116 SER n 1 117 GLY n 1 118 SER n 1 119 THR n 1 120 LEU n 1 121 GLY n 1 122 GLU n 1 123 LEU n 1 124 TYR n 1 125 TYR n 1 126 ALA n 1 127 ILE n 1 128 THR n 1 129 GLU n 1 130 SER n 1 131 SER n 1 132 SER n 1 133 LYS n 1 134 LEU n 1 135 GLY n 1 136 PHE n 1 137 THR n 1 138 ALA n 1 139 GLY n 1 140 TRP n 1 141 CYS n 1 142 PRO n 1 143 THR n 1 144 VAL n 1 145 GLY n 1 146 THR n 1 147 GLY n 1 148 GLY n 1 149 HIS n 1 150 ILE n 1 151 SER n 1 152 GLY n 1 153 GLY n 1 154 GLY n 1 155 PHE n 1 156 GLY n 1 157 MET n 1 158 MET n 1 159 SER n 1 160 ARG n 1 161 LYS n 1 162 TYR n 1 163 GLY n 1 164 LEU n 1 165 ALA n 1 166 ALA n 1 167 ASP n 1 168 ASN n 1 169 VAL n 1 170 VAL n 1 171 ASP n 1 172 ALA n 1 173 ILE n 1 174 LEU n 1 175 ILE n 1 176 ASP n 1 177 ALA n 1 178 ASN n 1 179 GLY n 1 180 ALA n 1 181 ILE n 1 182 LEU n 1 183 ASP n 1 184 ARG n 1 185 GLN n 1 186 ALA n 1 187 MET n 1 188 GLY n 1 189 GLU n 1 190 ASP n 1 191 VAL n 1 192 PHE n 1 193 TRP n 1 194 ALA n 1 195 ILE n 1 196 ARG n 1 197 GLY n 1 198 GLY n 1 199 GLY n 1 200 GLY n 1 201 GLY n 1 202 VAL n 1 203 TRP n 1 204 GLY n 1 205 ALA n 1 206 ILE n 1 207 TYR n 1 208 ALA n 1 209 TRP n 1 210 LYS n 1 211 ILE n 1 212 LYS n 1 213 LEU n 1 214 LEU n 1 215 PRO n 1 216 VAL n 1 217 PRO n 1 218 GLU n 1 219 LYS n 1 220 VAL n 1 221 THR n 1 222 VAL n 1 223 PHE n 1 224 ARG n 1 225 VAL n 1 226 THR n 1 227 LYS n 1 228 ASN n 1 229 VAL n 1 230 ALA n 1 231 ILE n 1 232 ASP n 1 233 GLU n 1 234 ALA n 1 235 THR n 1 236 SER n 1 237 LEU n 1 238 LEU n 1 239 HIS n 1 240 LYS n 1 241 TRP n 1 242 GLN n 1 243 PHE n 1 244 VAL n 1 245 ALA n 1 246 GLU n 1 247 GLU n 1 248 LEU n 1 249 GLU n 1 250 GLU n 1 251 ASP n 1 252 PHE n 1 253 THR n 1 254 LEU n 1 255 SER n 1 256 VAL n 1 257 LEU n 1 258 GLY n 1 259 GLY n 1 260 ALA n 1 261 ASP n 1 262 GLU n 1 263 LYS n 1 264 GLN n 1 265 VAL n 1 266 TRP n 1 267 LEU n 1 268 THR n 1 269 MET n 1 270 LEU n 1 271 GLY n 1 272 PHE n 1 273 HIS n 1 274 PHE n 1 275 GLY n 1 276 LEU n 1 277 LYS n 1 278 THR n 1 279 VAL n 1 280 ALA n 1 281 LYS n 1 282 SER n 1 283 THR n 1 284 PHE n 1 285 ASP n 1 286 LEU n 1 287 LEU n 1 288 PHE n 1 289 PRO n 1 290 GLU n 1 291 LEU n 1 292 GLY n 1 293 LEU n 1 294 VAL n 1 295 GLU n 1 296 GLU n 1 297 ASP n 1 298 TYR n 1 299 LEU n 1 300 GLU n 1 301 MET n 1 302 SER n 1 303 TRP n 1 304 GLY n 1 305 GLU n 1 306 SER n 1 307 PHE n 1 308 ALA n 1 309 TYR n 1 310 LEU n 1 311 ALA n 1 312 GLY n 1 313 LEU n 1 314 GLU n 1 315 THR n 1 316 VAL n 1 317 SER n 1 318 GLN n 1 319 LEU n 1 320 ASN n 1 321 ASN n 1 322 ARG n 1 323 PHE n 1 324 LEU n 1 325 LYS n 1 326 PHE n 1 327 ASP n 1 328 GLU n 1 329 ARG n 1 330 ALA n 1 331 PHE n 1 332 LYS n 1 333 THR n 1 334 LYS n 1 335 VAL n 1 336 ASP n 1 337 LEU n 1 338 THR n 1 339 LYS n 1 340 GLU n 1 341 PRO n 1 342 LEU n 1 343 PRO n 1 344 SER n 1 345 LYS n 1 346 ALA n 1 347 PHE n 1 348 TYR n 1 349 GLY n 1 350 LEU n 1 351 LEU n 1 352 GLU n 1 353 ARG n 1 354 LEU n 1 355 SER n 1 356 LYS n 1 357 GLU n 1 358 PRO n 1 359 ASN n 1 360 GLY n 1 361 PHE n 1 362 ILE n 1 363 ALA n 1 364 LEU n 1 365 ASN n 1 366 GLY n 1 367 PHE n 1 368 GLY n 1 369 GLY n 1 370 GLN n 1 371 MET n 1 372 SER n 1 373 LYS n 1 374 ILE n 1 375 SER n 1 376 SER n 1 377 ASP n 1 378 PHE n 1 379 THR n 1 380 PRO n 1 381 PHE n 1 382 PRO n 1 383 HIS n 1 384 ARG n 1 385 SER n 1 386 GLY n 1 387 THR n 1 388 ARG n 1 389 LEU n 1 390 MET n 1 391 VAL n 1 392 GLU n 1 393 TYR n 1 394 ILE n 1 395 VAL n 1 396 ALA n 1 397 TRP n 1 398 ASN n 1 399 GLN n 1 400 SER n 1 401 GLU n 1 402 GLN n 1 403 LYS n 1 404 LYS n 1 405 LYS n 1 406 THR n 1 407 GLU n 1 408 PHE n 1 409 LEU n 1 410 ASP n 1 411 TRP n 1 412 LEU n 1 413 GLU n 1 414 LYS n 1 415 VAL n 1 416 TYR n 1 417 GLU n 1 418 PHE n 1 419 MET n 1 420 LYS n 1 421 PRO n 1 422 PHE n 1 423 VAL n 1 424 SER n 1 425 LYS n 1 426 ASN n 1 427 PRO n 1 428 ARG n 1 429 LEU n 1 430 GLY n 1 431 TYR n 1 432 VAL n 1 433 ASN n 1 434 HIS n 1 435 ILE n 1 436 ASP n 1 437 LEU n 1 438 ASP n 1 439 LEU n 1 440 GLY n 1 441 GLY n 1 442 ILE n 1 443 ASP n 1 444 TRP n 1 445 GLY n 1 446 ASN n 1 447 LYS n 1 448 THR n 1 449 VAL n 1 450 VAL n 1 451 ASN n 1 452 ASN n 1 453 ALA n 1 454 ILE n 1 455 GLU n 1 456 ILE n 1 457 SER n 1 458 ARG n 1 459 SER n 1 460 TRP n 1 461 GLY n 1 462 GLU n 1 463 SER n 1 464 TYR n 1 465 PHE n 1 466 LEU n 1 467 SER n 1 468 ASN n 1 469 TYR n 1 470 GLU n 1 471 ARG n 1 472 LEU n 1 473 ILE n 1 474 ARG n 1 475 ALA n 1 476 LYS n 1 477 THR n 1 478 LEU n 1 479 ILE n 1 480 ASP n 1 481 PRO n 1 482 ASN n 1 483 ASN n 1 484 VAL n 1 485 PHE n 1 486 ASN n 1 487 HIS n 1 488 PRO n 1 489 GLN n 1 490 SER n 1 491 ILE n 1 492 PRO n 1 493 PRO n 1 494 MET n 1 495 ALA 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 'California poppy' _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene BBE1 _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Eschscholzia californica' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 3467 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Pichia pastoris' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 4922 _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 KM71H _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type PLASMID _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name PPICZA _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code RETO_ESCCA _struct_ref.pdbx_db_accession P30986 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;DLLSCLTFNGVRNHTVFSADSDSDFNRFLHLSIQNPLFQNSLISKPSAIILPGSKEELSNTIRCIRKGSWTIRLRSGGHS YEGLSYTSDTPFILIDLMNLNRVSIDLESETAWVESGSTLGELYYAITESSSKLGFTAGWCPTVGTGGHISGGGFGMMSR KYGLAADNVVDAILIDANGAILDRQAMGEDVFWAIRGGGGGVWGAIYAWKIKLLPVPEKVTVFRVTKNVAIDEATSLLHK WQFVAEELEEDFTLSVLGGADEKQVWLTMLGFHFGLKTVAKSTFDLLFPELGLVEEDYLEMSWGESFAYLAGLETVSQLN NRFLKFDERAFKTKVDLTKEPLPSKAFYGLLERLSKEPNGFIALNGFGGQMSKISSDFTPFPHRSGTRLMVEYIVAWNQS EQKKKTEFLDWLEKVYEFMKPFVSKNPRLGYVNHIDLDLGGIDWGNKTVVNNAIEISRSWGESYFLSNYERLIRAKTLID PNNVFNHPQSIPPMA ; _struct_ref.pdbx_align_begin 26 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 3FW9 _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 495 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P30986 _struct_ref_seq.db_align_beg 26 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 520 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 26 _struct_ref_seq.pdbx_auth_seq_align_end 520 # 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 FAD non-polymer . 'FLAVIN-ADENINE DINUCLEOTIDE' ? 'C27 H33 N9 O15 P2' 785.550 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 MG non-polymer . 'MAGNESIUM ION' ? 'Mg 2' 24.305 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 SLX non-polymer . '(13aS)-3,10-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquino[3,2-a]isoquinoline-2,9-diol' '(S)-scoulerine' 'C19 H21 N O4' 327.374 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.crystals_number 1 _exptl.entry_id 3FW9 _exptl.method 'X-RAY DIFFRACTION' # _exptl_crystal.id 1 _exptl_crystal.density_Matthews 2.64 _exptl_crystal.density_meas ? _exptl_crystal.density_percent_sol 53.33 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION' _exptl_crystal_grow.pH 8.5 _exptl_crystal_grow.temp 298 _exptl_crystal_grow.pdbx_details '0.2 M MAGNESIUMCHLORIDE, 30% PEG-4000, 0.1 M TRIS/HCL, pH 8.5, vapor diffusion, temperature 298K' _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'MARMOSAIC 225 mm CCD' _diffrn_detector.pdbx_collection_date 2008-07-01 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.monochromator ? _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.9794 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SLS BEAMLINE X06SA' _diffrn_source.pdbx_wavelength_list 0.9794 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_site SLS _diffrn_source.pdbx_synchrotron_beamline X06SA # _reflns.entry_id 3FW9 _reflns.B_iso_Wilson_estimate 13.980 _reflns.observed_criterion_sigma_F 0 _reflns.observed_criterion_sigma_I 0 _reflns.d_resolution_high 1.489 _reflns.d_resolution_low 45.9 _reflns.number_all 95974 _reflns.number_obs 95974 _reflns.percent_possible_obs 97.6 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.085 _reflns.pdbx_netI_over_sigmaI 10.9 _reflns.pdbx_redundancy 9.2 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.49 _reflns_shell.d_res_low 1.58 _reflns_shell.percent_possible_obs ? _reflns_shell.percent_possible_all 86.2 _reflns_shell.Rmerge_I_obs ? _reflns_shell.meanI_over_sigI_obs 2.4 _reflns_shell.pdbx_Rsym_value 0.600 _reflns_shell.pdbx_redundancy 7.4 _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 3FW9 _refine.ls_d_res_high 1.489 _refine.ls_d_res_low 45.9 _refine.pdbx_ls_sigma_F 2.00 _refine.ls_percent_reflns_obs 97.940 _refine.ls_number_reflns_obs 95974 _refine.ls_R_factor_obs 0.173 _refine.ls_R_factor_R_work 0.172 _refine.ls_R_factor_R_free 0.195 _refine.ls_percent_reflns_R_free 5.000 _refine.ls_number_reflns_R_free 4798 _refine.B_iso_mean 27.113 _refine.solvent_model_param_bsol 64.046 _refine.solvent_model_param_ksol 0.356 _refine.aniso_B[1][1] -6.555 _refine.aniso_B[2][2] -6.555 _refine.aniso_B[3][3] -10.956 _refine.aniso_B[1][2] -0.000 _refine.aniso_B[1][3] -0.000 _refine.aniso_B[2][3] -0.000 _refine.overall_SU_ML 0.170 _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.pdbx_solvent_vdw_probe_radii 1.110 _refine.pdbx_solvent_shrinkage_radii 0.900 _refine.pdbx_method_to_determine_struct ? _refine.pdbx_stereochemistry_target_values 'Engh & Huber' _refine.overall_FOM_work_R_set 0.900 _refine.B_iso_max 94.74 _refine.B_iso_min 14.14 _refine.occupancy_max 1.00 _refine.occupancy_min 0.24 _refine.pdbx_ls_sigma_I ? _refine.ls_number_reflns_all 95974 _refine.ls_R_factor_all 0.173 _refine.ls_redundancy_reflns_obs ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.pdbx_starting_model 3d2j _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.pdbx_R_Free_selection_details random _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_isotropic_thermal_model ? _refine.details ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.pdbx_solvent_ion_probe_radii ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.overall_SU_B ? _refine.pdbx_overall_ESU_R_Free ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.pdbx_overall_ESU_R ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.pdbx_overall_phase_error ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3907 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 131 _refine_hist.number_atoms_solvent 603 _refine_hist.number_atoms_total 4641 _refine_hist.d_res_high 1.489 _refine_hist.d_res_low 45.9 # loop_ _refine_ls_restr.type _refine_ls_restr.number _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function f_bond_d 4294 0.024 ? ? 'X-RAY DIFFRACTION' ? f_angle_d 5855 1.029 ? ? 'X-RAY DIFFRACTION' ? f_chiral_restr 640 0.067 ? ? 'X-RAY DIFFRACTION' ? f_plane_restr 735 0.005 ? ? 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 1564 18.257 ? ? 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.percent_reflns_obs _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_all _refine_ls_shell.R_factor_R_work _refine_ls_shell.R_factor_R_free _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.number_reflns_all _refine_ls_shell.number_reflns_obs _refine_ls_shell.redundancy_reflns_obs _refine_ls_shell.pdbx_refine_id 1.489 1.506 30 38.000 1161 . 0.309 0.305 . 60 . 1221 . . 'X-RAY DIFFRACTION' 1.506 1.524 30 100.000 3094 . 0.220 0.254 . 152 . 3246 . . 'X-RAY DIFFRACTION' 1.524 1.543 30 100.000 3018 . 0.216 0.241 . 162 . 3180 . . 'X-RAY DIFFRACTION' 1.543 1.562 30 100.000 3079 . 0.209 0.256 . 158 . 3237 . . 'X-RAY DIFFRACTION' 1.562 1.583 30 100.000 3033 . 0.204 0.220 . 153 . 3186 . . 'X-RAY DIFFRACTION' 1.583 1.604 30 100.000 3061 . 0.197 0.219 . 149 . 3210 . . 'X-RAY DIFFRACTION' 1.604 1.627 30 100.000 3040 . 0.190 0.247 . 174 . 3214 . . 'X-RAY DIFFRACTION' 1.627 1.651 30 100.000 3070 . 0.182 0.231 . 146 . 3216 . . 'X-RAY DIFFRACTION' 1.651 1.677 30 100.000 3080 . 0.178 0.195 . 163 . 3243 . . 'X-RAY DIFFRACTION' 1.677 1.705 30 100.000 3064 . 0.173 0.212 . 152 . 3216 . . 'X-RAY DIFFRACTION' 1.705 1.734 30 100.000 3078 . 0.171 0.216 . 138 . 3216 . . 'X-RAY DIFFRACTION' 1.734 1.766 30 100.000 3078 . 0.170 0.206 . 168 . 3246 . . 'X-RAY DIFFRACTION' 1.766 1.800 30 100.000 3055 . 0.173 0.202 . 157 . 3212 . . 'X-RAY DIFFRACTION' 1.800 1.836 30 100.000 3055 . 0.170 0.189 . 158 . 3213 . . 'X-RAY DIFFRACTION' 1.836 1.876 30 100.000 3085 . 0.169 0.201 . 168 . 3253 . . 'X-RAY DIFFRACTION' 1.876 1.920 30 100.000 3093 . 0.169 0.197 . 148 . 3241 . . 'X-RAY DIFFRACTION' 1.920 1.968 30 100.000 3099 . 0.167 0.201 . 166 . 3265 . . 'X-RAY DIFFRACTION' 1.968 2.021 30 100.000 3119 . 0.165 0.201 . 150 . 3269 . . 'X-RAY DIFFRACTION' 2.021 2.081 30 100.000 3068 . 0.165 0.172 . 155 . 3223 . . 'X-RAY DIFFRACTION' 2.081 2.148 30 100.000 3056 . 0.160 0.186 . 197 . 3253 . . 'X-RAY DIFFRACTION' 2.148 2.225 30 100.000 3067 . 0.160 0.204 . 200 . 3267 . . 'X-RAY DIFFRACTION' 2.225 2.314 30 100.000 3093 . 0.157 0.179 . 180 . 3273 . . 'X-RAY DIFFRACTION' 2.314 2.419 30 100.000 3091 . 0.159 0.203 . 172 . 3263 . . 'X-RAY DIFFRACTION' 2.419 2.546 30 100.000 3143 . 0.163 0.188 . 160 . 3303 . . 'X-RAY DIFFRACTION' 2.546 2.706 30 100.000 3092 . 0.172 0.199 . 180 . 3272 . . 'X-RAY DIFFRACTION' 2.706 2.915 30 100.000 3162 . 0.176 0.195 . 157 . 3319 . . 'X-RAY DIFFRACTION' 2.915 3.208 30 100.000 3168 . 0.172 0.203 . 166 . 3334 . . 'X-RAY DIFFRACTION' 3.208 3.672 30 100.000 3210 . 0.158 0.164 . 150 . 3360 . . 'X-RAY DIFFRACTION' 3.672 4.626 30 100.000 3246 . 0.137 0.151 . 185 . 3431 . . 'X-RAY DIFFRACTION' 4.626 45.970 30 99.000 3418 . 0.168 0.168 . 174 . 3592 . . 'X-RAY DIFFRACTION' # _struct.entry_id 3FW9 _struct.title 'Structure of berberine bridge enzyme in complex with (S)-scoulerine' _struct.pdbx_descriptor 'Reticuline oxidase (E.C.1.21.3.3)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3FW9 _struct_keywords.text ;BI-COVALENT FLAVINYLATION, N-GLYCOSYLATION, ALAKLOID BIOSYNTHESIS, OXIDOREDUCTASE, Alkaloid metabolism, Cytoplasmic vesicle, FAD, Flavoprotein, Glycoprotein ; _struct_keywords.pdbx_keywords FLAVOPROTEIN # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 5 ? F N N 5 ? G N N 5 ? H N N 6 ? I N N 7 ? # _struct_biol.id 1 _struct_biol.details 'biological unit is the same as asymmetric unit.' # 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 ASP A 1 ? ASN A 9 ? ASP A 26 ASN A 34 1 ? 9 HELX_P HELX_P2 2 SER A 23 ? SER A 32 ? SER A 48 SER A 57 1 ? 10 HELX_P HELX_P3 3 ASN A 35 ? GLN A 39 ? ASN A 60 GLN A 64 5 ? 5 HELX_P HELX_P4 4 SER A 54 ? LYS A 67 ? SER A 79 LYS A 92 1 ? 14 HELX_P HELX_P5 5 THR A 119 ? SER A 131 ? THR A 144 SER A 156 1 ? 13 HELX_P HELX_P6 6 GLY A 145 ? GLY A 152 ? GLY A 170 GLY A 177 1 ? 8 HELX_P HELX_P7 7 MET A 158 ? GLY A 163 ? MET A 183 GLY A 188 1 ? 6 HELX_P HELX_P8 8 LEU A 164 ? ASP A 167 ? LEU A 189 ASP A 192 5 ? 4 HELX_P HELX_P9 9 ASP A 183 ? GLY A 188 ? ASP A 208 GLY A 213 1 ? 6 HELX_P HELX_P10 10 GLY A 188 ? ARG A 196 ? GLY A 213 ARG A 221 1 ? 9 HELX_P HELX_P11 11 ALA A 230 ? LEU A 248 ? ALA A 255 LEU A 273 1 ? 19 HELX_P HELX_P12 12 LEU A 276 ? PHE A 288 ? LEU A 301 PHE A 313 1 ? 13 HELX_P HELX_P13 13 PRO A 289 ? GLY A 292 ? PRO A 314 GLY A 317 5 ? 4 HELX_P HELX_P14 14 VAL A 294 ? TYR A 298 ? VAL A 319 TYR A 323 5 ? 5 HELX_P HELX_P15 15 SER A 302 ? ALA A 311 ? SER A 327 ALA A 336 1 ? 10 HELX_P HELX_P16 16 THR A 315 ? ASN A 321 ? THR A 340 ASN A 346 5 ? 7 HELX_P HELX_P17 17 PRO A 343 ? GLU A 357 ? PRO A 368 GLU A 382 1 ? 15 HELX_P HELX_P18 18 GLY A 368 ? LYS A 373 ? GLY A 393 LYS A 398 5 ? 6 HELX_P HELX_P19 19 ASN A 398 ? LYS A 403 ? ASN A 423 LYS A 428 5 ? 6 HELX_P HELX_P20 20 LYS A 404 ? LYS A 420 ? LYS A 429 LYS A 445 1 ? 17 HELX_P HELX_P21 21 PRO A 421 ? VAL A 423 ? PRO A 446 VAL A 448 5 ? 3 HELX_P HELX_P22 22 TYR A 431 ? ILE A 435 ? TYR A 456 ILE A 460 5 ? 5 HELX_P HELX_P23 23 ASP A 436 ? GLY A 440 ? ASP A 461 GLY A 465 5 ? 5 HELX_P HELX_P24 24 ASN A 446 ? ASN A 452 ? ASN A 471 ASN A 477 1 ? 7 HELX_P HELX_P25 25 ASN A 452 ? LEU A 466 ? ASN A 477 LEU A 491 1 ? 15 HELX_P HELX_P26 26 ASN A 468 ? ASP A 480 ? ASN A 493 ASP A 505 1 ? 13 # _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 5 SG ? ? ? 1_555 A CYS 64 SG ? ? A CYS 30 A CYS 89 1_555 ? ? ? ? ? ? ? 2.036 ? covale1 covale ? ? A ASN 13 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 38 A NAG 521 1_555 ? ? ? ? ? ? ? 1.443 ? metalc1 metalc ? ? A ASP 20 OD1 ? ? ? 1_555 H MG . MG ? ? A ASP 45 A MG 524 1_555 ? ? ? ? ? ? ? 2.393 ? metalc2 metalc ? ? A ASP 22 OD1 ? ? ? 1_555 H MG . MG ? ? A ASP 47 A MG 524 1_555 ? ? ? ? ? ? ? 2.121 ? covale2 covale ? ? A ASN 446 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 471 A NAG 523 1_555 ? ? ? ? ? ? ? 1.441 ? covale3 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 521 A NAG 522 1_555 ? ? ? ? ? ? ? 1.440 ? covale4 covale ? ? F NAG . O4 ? ? ? 1_555 D MAN . C1 ? ? A NAG 522 A MAN 3 1_555 ? ? ? ? ? ? ? 1.443 ? metalc3 metalc ? ? H MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 524 A HOH 4 1_555 ? ? ? ? ? ? ? 2.215 ? metalc4 metalc ? ? H MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 524 A HOH 5 1_555 ? ? ? ? ? ? ? 2.032 ? metalc5 metalc ? ? H MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 524 A HOH 578 1_555 ? ? ? ? ? ? ? 2.169 ? metalc6 metalc ? ? H MG . MG ? ? ? 1_555 I HOH . O ? ? A MG 524 A HOH 576 1_555 ? ? ? ? ? ? ? 2.003 ? covale5 covale ? ? A HIS 79 ND1 ? ? ? 1_555 B FAD . C8M ? ? A HIS 104 A FAD 1 1_555 ? ? ? ? ? ? ? 1.643 ? covale6 covale ? ? A CYS 141 SG ? ? ? 1_555 B FAD . C6 ? ? A CYS 166 A FAD 1 1_555 ? ? ? ? ? ? ? 1.790 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id ASN _struct_mon_prot_cis.label_seq_id 426 _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 ASN _struct_mon_prot_cis.auth_seq_id 451 _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_2 427 _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_2 452 _struct_mon_prot_cis.pdbx_auth_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle 0.08 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 4 ? B ? 5 ? C ? 2 ? D ? 7 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? parallel A 3 4 ? parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel B 4 5 ? anti-parallel C 1 2 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel D 4 5 ? anti-parallel D 5 6 ? anti-parallel D 6 7 ? 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 A 1 HIS A 14 ? VAL A 16 ? HIS A 39 VAL A 41 A 2 ALA A 48 ? ILE A 50 ? ALA A 73 ILE A 75 A 3 PHE A 92 ? ASP A 96 ? PHE A 117 ASP A 121 A 4 THR A 71 ? ARG A 75 ? THR A 96 ARG A 100 B 1 VAL A 103 ? ASP A 106 ? VAL A 128 ASP A 131 B 2 THR A 111 ? GLU A 115 ? THR A 136 GLU A 140 B 3 ALA A 205 ? LYS A 212 ? ALA A 230 LYS A 237 B 4 VAL A 169 ? ILE A 175 ? VAL A 194 ILE A 200 B 5 ILE A 181 ? LEU A 182 ? ILE A 206 LEU A 207 C 1 LEU A 134 ? GLY A 135 ? LEU A 159 GLY A 160 C 2 LEU A 214 ? PRO A 215 ? LEU A 239 PRO A 240 D 1 LEU A 299 ? MET A 301 ? LEU A 324 MET A 326 D 2 VAL A 220 ? VAL A 229 ? VAL A 245 VAL A 254 D 3 GLN A 264 ? HIS A 273 ? GLN A 289 HIS A 298 D 4 PHE A 252 ? ASP A 261 ? PHE A 277 ASP A 286 D 5 GLY A 360 ? GLY A 366 ? GLY A 385 GLY A 391 D 6 LEU A 389 ? TRP A 397 ? LEU A 414 TRP A 422 D 7 ALA A 330 ? LEU A 337 ? ALA A 355 LEU A 362 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N THR A 15 ? N THR A 40 O ILE A 49 ? O ILE A 74 A 2 3 N ILE A 50 ? N ILE A 75 O LEU A 94 ? O LEU A 119 A 3 4 O ILE A 95 ? O ILE A 120 N ARG A 73 ? N ARG A 98 B 1 2 N SER A 104 ? N SER A 129 O TRP A 113 ? O TRP A 138 B 2 3 N VAL A 114 ? N VAL A 139 O TRP A 209 ? O TRP A 234 B 3 4 O TYR A 207 ? O TYR A 232 N ILE A 173 ? N ILE A 198 B 4 5 N LEU A 174 ? N LEU A 199 O LEU A 182 ? O LEU A 207 C 1 2 N GLY A 135 ? N GLY A 160 O LEU A 214 ? O LEU A 239 D 1 2 O MET A 301 ? O MET A 326 N VAL A 220 ? N VAL A 245 D 2 3 N VAL A 225 ? N VAL A 250 O MET A 269 ? O MET A 294 D 3 4 O THR A 268 ? O THR A 293 N LEU A 257 ? N LEU A 282 D 4 5 N VAL A 256 ? N VAL A 281 O LEU A 364 ? O LEU A 389 D 5 6 N ASN A 365 ? N ASN A 390 O MET A 390 ? O MET A 415 D 6 7 O VAL A 391 ? O VAL A 416 N ASP A 336 ? N ASP A 361 # 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 ? ? ? ? 33 'BINDING SITE FOR RESIDUE FAD A 1' AC2 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE SLX A 2' AC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 521' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 522' AC5 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE MAN A 3' AC6 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 523' AC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MG A 524' # 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 33 HOH I . ? HOH A 10 . ? 1_555 ? 2 AC1 33 HOH I . ? HOH A 17 . ? 1_555 ? 3 AC1 33 LEU A 74 ? LEU A 99 . ? 1_555 ? 4 AC1 33 ARG A 75 ? ARG A 100 . ? 1_555 ? 5 AC1 33 SER A 76 ? SER A 101 . ? 1_555 ? 6 AC1 33 GLY A 77 ? GLY A 102 . ? 1_555 ? 7 AC1 33 GLY A 78 ? GLY A 103 . ? 1_555 ? 8 AC1 33 HIS A 79 ? HIS A 104 . ? 1_555 ? 9 AC1 33 SER A 80 ? SER A 105 . ? 1_555 ? 10 AC1 33 TYR A 81 ? TYR A 106 . ? 1_555 ? 11 AC1 33 SER A 85 ? SER A 110 . ? 1_555 ? 12 AC1 33 LEU A 97 ? LEU A 122 . ? 1_555 ? 13 AC1 33 SER A 116 ? SER A 141 . ? 1_555 ? 14 AC1 33 GLY A 139 ? GLY A 164 . ? 1_555 ? 15 AC1 33 TRP A 140 ? TRP A 165 . ? 1_555 ? 16 AC1 33 CYS A 141 ? CYS A 166 . ? 1_555 ? 17 AC1 33 VAL A 144 ? VAL A 169 . ? 1_555 ? 18 AC1 33 GLY A 145 ? GLY A 170 . ? 1_555 ? 19 AC1 33 GLY A 147 ? GLY A 172 . ? 1_555 ? 20 AC1 33 GLY A 148 ? GLY A 173 . ? 1_555 ? 21 AC1 33 HIS A 149 ? HIS A 174 . ? 1_555 ? 22 AC1 33 PHE A 155 ? PHE A 180 . ? 1_555 ? 23 AC1 33 GLY A 200 ? GLY A 225 . ? 1_555 ? 24 AC1 33 GLY A 201 ? GLY A 226 . ? 1_555 ? 25 AC1 33 GLY A 204 ? GLY A 229 . ? 1_555 ? 26 AC1 33 ILE A 206 ? ILE A 231 . ? 1_555 ? 27 AC1 33 TYR A 431 ? TYR A 456 . ? 1_555 ? 28 AC1 33 ASN A 433 ? ASN A 458 . ? 1_555 ? 29 AC1 33 HOH I . ? HOH A 619 . ? 1_555 ? 30 AC1 33 HOH I . ? HOH A 624 . ? 1_555 ? 31 AC1 33 HOH I . ? HOH A 646 . ? 1_555 ? 32 AC1 33 HOH I . ? HOH A 831 . ? 1_555 ? 33 AC1 33 HOH I . ? HOH A 1083 . ? 1_555 ? 34 AC2 9 TYR A 81 ? TYR A 106 . ? 1_555 ? 35 AC2 9 TRP A 140 ? TRP A 165 . ? 1_555 ? 36 AC2 9 MET A 157 ? MET A 182 . ? 1_555 ? 37 AC2 9 LEU A 257 ? LEU A 282 . ? 1_555 ? 38 AC2 9 ASP A 327 ? ASP A 352 . ? 1_555 ? 39 AC2 9 PHE A 331 ? PHE A 356 . ? 1_555 ? 40 AC2 9 ASN A 365 ? ASN A 390 . ? 1_555 ? 41 AC2 9 GLU A 392 ? GLU A 417 . ? 1_555 ? 42 AC2 9 HOH I . ? HOH A 831 . ? 1_555 ? 43 AC3 6 ASN A 13 ? ASN A 38 . ? 1_555 ? 44 AC3 6 LEU A 51 ? LEU A 76 . ? 1_555 ? 45 AC3 6 ASN A 99 ? ASN A 124 . ? 1_555 ? 46 AC3 6 LYS A 403 ? LYS A 428 . ? 6_544 ? 47 AC3 6 NAG F . ? NAG A 522 . ? 1_555 ? 48 AC3 6 HOH I . ? HOH A 1086 . ? 1_555 ? 49 AC4 5 MAN D . ? MAN A 3 . ? 1_555 ? 50 AC4 5 ARG A 27 ? ARG A 52 . ? 1_555 ? 51 AC4 5 LEU A 31 ? LEU A 56 . ? 1_555 ? 52 AC4 5 NAG E . ? NAG A 521 . ? 1_555 ? 53 AC4 5 HOH I . ? HOH A 1068 . ? 1_555 ? 54 AC5 1 NAG F . ? NAG A 522 . ? 1_555 ? 55 AC6 7 PRO A 289 ? PRO A 314 . ? 4_444 ? 56 AC6 7 ASN A 446 ? ASN A 471 . ? 1_555 ? 57 AC6 7 VAL A 449 ? VAL A 474 . ? 1_555 ? 58 AC6 7 HOH I . ? HOH A 612 . ? 1_555 ? 59 AC6 7 HOH I . ? HOH A 714 . ? 1_555 ? 60 AC6 7 HOH I . ? HOH A 830 . ? 1_555 ? 61 AC6 7 HOH I . ? HOH A 1053 . ? 1_555 ? 62 AC7 6 HOH I . ? HOH A 4 . ? 1_555 ? 63 AC7 6 HOH I . ? HOH A 5 . ? 1_555 ? 64 AC7 6 ASP A 20 ? ASP A 45 . ? 1_555 ? 65 AC7 6 ASP A 22 ? ASP A 47 . ? 1_555 ? 66 AC7 6 HOH I . ? HOH A 576 . ? 1_555 ? 67 AC7 6 HOH I . ? HOH A 578 . ? 1_555 ? # _atom_sites.entry_id 3FW9 _atom_sites.fract_transf_matrix[1][1] 0.014552 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.014552 _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] 0.004046 _atom_sites.fract_transf_vector[1] 0.000000 _atom_sites.fract_transf_vector[2] 0.000000 _atom_sites.fract_transf_vector[3] 0.000000 # loop_ _atom_type.symbol C MG N O P 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 . ASP A 1 1 ? -14.305 3.637 -48.468 1.00 71.39 ? 26 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? -14.594 2.599 -47.486 1.00 64.01 ? 26 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? -14.358 3.112 -46.067 1.00 58.76 ? 26 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? -13.497 3.962 -45.835 1.00 49.35 ? 26 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? -13.735 1.360 -47.749 1.00 71.85 ? 26 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? -14.210 0.145 -46.974 1.00 83.29 ? 26 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? -15.432 0.023 -46.745 1.00 85.61 ? 26 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? -13.363 -0.691 -46.597 1.00 87.71 ? 26 ASP A OD2 1 ATOM 9 N N . LEU A 1 2 ? -15.133 2.598 -45.120 1.00 50.61 ? 27 LEU A N 1 ATOM 10 C CA . LEU A 1 2 ? -14.965 2.969 -43.721 1.00 43.35 ? 27 LEU A CA 1 ATOM 11 C C . LEU A 1 2 ? -13.560 2.610 -43.248 1.00 46.25 ? 27 LEU A C 1 ATOM 12 O O . LEU A 1 2 ? -12.898 3.397 -42.567 1.00 39.50 ? 27 LEU A O 1 ATOM 13 C CB . LEU A 1 2 ? -16.017 2.271 -42.857 1.00 39.93 ? 27 LEU A CB 1 ATOM 14 C CG . LEU A 1 2 ? -15.901 2.429 -41.340 1.00 35.93 ? 27 LEU A CG 1 ATOM 15 C CD1 . LEU A 1 2 ? -15.908 3.896 -40.944 1.00 35.75 ? 27 LEU A CD1 1 ATOM 16 C CD2 . LEU A 1 2 ? -17.027 1.679 -40.642 1.00 44.74 ? 27 LEU A CD2 1 ATOM 17 N N . LEU A 1 3 ? -13.107 1.418 -43.625 1.00 56.33 ? 28 LEU A N 1 ATOM 18 C CA . LEU A 1 3 ? -11.794 0.925 -43.226 1.00 61.62 ? 28 LEU A CA 1 ATOM 19 C C . LEU A 1 3 ? -10.670 1.838 -43.704 1.00 60.54 ? 28 LEU A C 1 ATOM 20 O O . LEU A 1 3 ? -9.730 2.117 -42.960 1.00 56.33 ? 28 LEU A O 1 ATOM 21 C CB . LEU A 1 3 ? -11.575 -0.491 -43.757 1.00 67.41 ? 28 LEU A CB 1 ATOM 22 C CG . LEU A 1 3 ? -12.634 -1.525 -43.370 1.00 74.57 ? 28 LEU A CG 1 ATOM 23 C CD1 . LEU A 1 3 ? -12.312 -2.878 -43.987 1.00 78.71 ? 28 LEU A CD1 1 ATOM 24 C CD2 . LEU A 1 3 ? -12.756 -1.635 -41.857 1.00 74.67 ? 28 LEU A CD2 1 ATOM 25 N N . SER A 1 4 ? -10.767 2.301 -44.946 1.00 60.51 ? 29 SER A N 1 ATOM 26 C CA . SER A 1 4 ? -9.738 3.166 -45.510 1.00 63.28 ? 29 SER A CA 1 ATOM 27 C C . SER A 1 4 ? -9.658 4.486 -44.751 1.00 54.60 ? 29 SER A C 1 ATOM 28 O O . SER A 1 4 ? -8.575 5.045 -44.577 1.00 48.67 ? 29 SER A O 1 ATOM 29 C CB . SER A 1 4 ? -9.981 3.414 -47.002 1.00 71.31 ? 29 SER A CB 1 ATOM 30 O OG . SER A 1 4 ? -11.104 4.251 -47.212 1.00 77.34 ? 29 SER A OG 1 ATOM 31 N N . CYS A 1 5 ? -10.805 4.984 -44.297 1.00 40.54 ? 30 CYS A N 1 ATOM 32 C CA . CYS A 1 5 ? -10.821 6.199 -43.497 1.00 38.42 ? 30 CYS A CA 1 ATOM 33 C C . CYS A 1 5 ? -10.166 5.914 -42.149 1.00 39.60 ? 30 CYS A C 1 ATOM 34 O O . CYS A 1 5 ? -9.312 6.674 -41.691 1.00 36.33 ? 30 CYS A O 1 ATOM 35 C CB . CYS A 1 5 ? -12.251 6.717 -43.301 1.00 35.37 ? 30 CYS A CB 1 ATOM 36 S SG . CYS A 1 5 ? -12.349 8.286 -42.405 1.00 41.67 ? 30 CYS A SG 1 ATOM 37 N N . LEU A 1 6 ? -10.561 4.807 -41.527 1.00 37.09 ? 31 LEU A N 1 ATOM 38 C CA . LEU A 1 6 ? -10.023 4.425 -40.224 1.00 34.37 ? 31 LEU A CA 1 ATOM 39 C C . LEU A 1 6 ? -8.505 4.280 -40.278 1.00 38.50 ? 31 LEU A C 1 ATOM 40 O O . LEU A 1 6 ? -7.797 4.698 -39.366 1.00 38.25 ? 31 LEU A O 1 ATOM 41 C CB . LEU A 1 6 ? -10.670 3.126 -39.734 1.00 34.65 ? 31 LEU A CB 1 ATOM 42 C CG . LEU A 1 6 ? -12.134 3.243 -39.306 1.00 32.19 ? 31 LEU A CG 1 ATOM 43 C CD1 . LEU A 1 6 ? -12.756 1.876 -39.063 1.00 34.77 ? 31 LEU A CD1 1 ATOM 44 C CD2 . LEU A 1 6 ? -12.232 4.105 -38.059 1.00 27.38 ? 31 LEU A CD2 1 ATOM 45 N N . THR A 1 7 ? -8.010 3.698 -41.364 1.00 45.89 ? 32 THR A N 1 ATOM 46 C CA . THR A 1 7 ? -6.576 3.483 -41.530 1.00 46.58 ? 32 THR A CA 1 ATOM 47 C C . THR A 1 7 ? -5.821 4.786 -41.781 1.00 42.51 ? 32 THR A C 1 ATOM 48 O O . THR A 1 7 ? -4.760 5.016 -41.201 1.00 53.75 ? 32 THR A O 1 ATOM 49 C CB . THR A 1 7 ? -6.293 2.478 -42.657 1.00 56.67 ? 32 THR A CB 1 ATOM 50 O OG1 . THR A 1 7 ? -6.759 1.183 -42.258 1.00 52.08 ? 32 THR A OG1 1 ATOM 51 C CG2 . THR A 1 7 ? -4.801 2.408 -42.948 1.00 61.62 ? 32 THR A CG2 1 ATOM 52 N N . PHE A 1 8 ? -6.372 5.639 -42.639 1.00 43.65 ? 33 PHE A N 1 ATOM 53 C CA . PHE A 1 8 ? -5.781 6.945 -42.907 1.00 54.40 ? 33 PHE A CA 1 ATOM 54 C C . PHE A 1 8 ? -5.651 7.759 -41.622 1.00 50.77 ? 33 PHE A C 1 ATOM 55 O O . PHE A 1 8 ? -4.799 8.643 -41.518 1.00 49.32 ? 33 PHE A O 1 ATOM 56 C CB . PHE A 1 8 ? -6.617 7.710 -43.940 1.00 62.93 ? 33 PHE A CB 1 ATOM 57 C CG . PHE A 1 8 ? -6.130 9.111 -44.205 1.00 72.09 ? 33 PHE A CG 1 ATOM 58 C CD1 . PHE A 1 8 ? -5.110 9.347 -45.113 1.00 74.16 ? 33 PHE A CD1 1 ATOM 59 C CD2 . PHE A 1 8 ? -6.701 10.193 -43.553 1.00 76.13 ? 33 PHE A CD2 1 ATOM 60 C CE1 . PHE A 1 8 ? -4.665 10.633 -45.360 1.00 78.89 ? 33 PHE A CE1 1 ATOM 61 C CE2 . PHE A 1 8 ? -6.260 11.481 -43.795 1.00 78.89 ? 33 PHE A CE2 1 ATOM 62 C CZ . PHE A 1 8 ? -5.241 11.702 -44.700 1.00 79.47 ? 33 PHE A CZ 1 ATOM 63 N N . ASN A 1 9 ? -6.497 7.455 -40.641 1.00 37.48 ? 34 ASN A N 1 ATOM 64 C CA . ASN A 1 9 ? -6.497 8.197 -39.384 1.00 43.05 ? 34 ASN A CA 1 ATOM 65 C C . ASN A 1 9 ? -5.900 7.435 -38.202 1.00 43.54 ? 34 ASN A C 1 ATOM 66 O O . ASN A 1 9 ? -6.001 7.880 -37.060 1.00 47.47 ? 34 ASN A O 1 ATOM 67 C CB . ASN A 1 9 ? -7.905 8.691 -39.040 1.00 45.46 ? 34 ASN A CB 1 ATOM 68 C CG . ASN A 1 9 ? -8.374 9.798 -39.964 1.00 56.08 ? 34 ASN A CG 1 ATOM 69 O OD1 . ASN A 1 9 ? -8.600 9.575 -41.152 1.00 53.69 ? 34 ASN A OD1 1 ATOM 70 N ND2 . ASN A 1 9 ? -8.529 10.999 -39.418 1.00 57.13 ? 34 ASN A ND2 1 ATOM 71 N N . GLY A 1 10 ? -5.289 6.288 -38.476 1.00 40.50 ? 35 GLY A N 1 ATOM 72 C CA . GLY A 1 10 ? -4.543 5.569 -37.457 1.00 41.21 ? 35 GLY A CA 1 ATOM 73 C C . GLY A 1 10 ? -5.365 4.735 -36.491 1.00 43.82 ? 35 GLY A C 1 ATOM 74 O O . GLY A 1 10 ? -4.949 4.504 -35.354 1.00 43.08 ? 35 GLY A O 1 ATOM 75 N N . VAL A 1 11 ? -6.532 4.284 -36.937 1.00 33.19 ? 36 VAL A N 1 ATOM 76 C CA . VAL A 1 11 ? -7.348 3.365 -36.151 1.00 33.41 ? 36 VAL A CA 1 ATOM 77 C C . VAL A 1 11 ? -7.258 1.981 -36.780 1.00 36.73 ? 36 VAL A C 1 ATOM 78 O O . VAL A 1 11 ? -7.815 1.744 -37.852 1.00 40.55 ? 36 VAL A O 1 ATOM 79 C CB . VAL A 1 11 ? -8.817 3.816 -36.107 1.00 31.42 ? 36 VAL A CB 1 ATOM 80 C CG1 . VAL A 1 11 ? -9.623 2.913 -35.187 1.00 34.91 ? 36 VAL A CG1 1 ATOM 81 C CG2 . VAL A 1 11 ? -8.910 5.261 -35.654 1.00 32.05 ? 36 VAL A CG2 1 ATOM 82 N N . ARG A 1 12 ? -6.553 1.070 -36.118 1.00 35.01 ? 37 ARG A N 1 ATOM 83 C CA . ARG A 1 12 ? -6.221 -0.216 -36.723 1.00 35.91 ? 37 ARG A CA 1 ATOM 84 C C . ARG A 1 12 ? -7.008 -1.387 -36.148 1.00 33.68 ? 37 ARG A C 1 ATOM 85 O O . ARG A 1 12 ? -7.119 -2.436 -36.782 1.00 34.05 ? 37 ARG A O 1 ATOM 86 C CB . ARG A 1 12 ? -4.721 -0.493 -36.587 1.00 48.65 ? 37 ARG A CB 1 ATOM 87 C CG . ARG A 1 12 ? -3.836 0.676 -36.982 1.00 61.67 ? 37 ARG A CG 1 ATOM 88 C CD . ARG A 1 12 ? -2.369 0.355 -36.762 1.00 75.25 ? 37 ARG A CD 1 ATOM 89 N NE . ARG A 1 12 ? -1.551 1.564 -36.720 1.00 86.33 ? 37 ARG A NE 1 ATOM 90 C CZ . ARG A 1 12 ? -1.288 2.247 -35.611 1.00 90.20 ? 37 ARG A CZ 1 ATOM 91 N NH1 . ARG A 1 12 ? -0.535 3.337 -35.665 1.00 93.34 ? 37 ARG A NH1 1 ATOM 92 N NH2 . ARG A 1 12 ? -1.778 1.840 -34.447 1.00 86.38 ? 37 ARG A NH2 1 ATOM 93 N N . ASN A 1 13 ? -7.545 -1.221 -34.944 1.00 29.00 ? 38 ASN A N 1 ATOM 94 C CA . ASN A 1 13 ? -8.253 -2.319 -34.307 1.00 28.20 ? 38 ASN A CA 1 ATOM 95 C C . ASN A 1 13 ? -9.707 -2.367 -34.741 1.00 26.51 ? 38 ASN A C 1 ATOM 96 O O . ASN A 1 13 ? -10.591 -1.790 -34.099 1.00 25.85 ? 38 ASN A O 1 ATOM 97 C CB . ASN A 1 13 ? -8.136 -2.247 -32.781 1.00 29.83 ? 38 ASN A CB 1 ATOM 98 C CG . ASN A 1 13 ? -8.319 -3.604 -32.120 1.00 34.74 ? 38 ASN A CG 1 ATOM 99 O OD1 . ASN A 1 13 ? -9.099 -4.433 -32.590 1.00 37.39 ? 38 ASN A OD1 1 ATOM 100 N ND2 . ASN A 1 13 ? -7.597 -3.836 -31.022 1.00 32.26 ? 38 ASN A ND2 1 ATOM 101 N N . HIS A 1 14 ? -9.948 -3.051 -35.851 1.00 28.92 ? 39 HIS A N 1 ATOM 102 C CA . HIS A 1 14 ? -11.295 -3.202 -36.367 1.00 32.37 ? 39 HIS A CA 1 ATOM 103 C C . HIS A 1 14 ? -11.468 -4.556 -37.040 1.00 36.42 ? 39 HIS A C 1 ATOM 104 O O . HIS A 1 14 ? -10.506 -5.148 -37.538 1.00 36.15 ? 39 HIS A O 1 ATOM 105 C CB . HIS A 1 14 ? -11.626 -2.073 -37.341 1.00 32.85 ? 39 HIS A CB 1 ATOM 106 C CG . HIS A 1 14 ? -10.549 -1.809 -38.343 1.00 31.98 ? 39 HIS A CG 1 ATOM 107 N ND1 . HIS A 1 14 ? -10.315 -2.638 -39.420 1.00 36.84 ? 39 HIS A ND1 1 ATOM 108 C CD2 . HIS A 1 14 ? -9.642 -0.808 -38.434 1.00 43.73 ? 39 HIS A CD2 1 ATOM 109 C CE1 . HIS A 1 14 ? -9.308 -2.159 -40.129 1.00 41.65 ? 39 HIS A CE1 1 ATOM 110 N NE2 . HIS A 1 14 ? -8.882 -1.049 -39.553 1.00 41.51 ? 39 HIS A NE2 1 ATOM 111 N N . THR A 1 15 ? -12.706 -5.038 -37.041 1.00 30.90 ? 40 THR A N 1 ATOM 112 C CA A THR A 1 15 ? -13.033 -6.330 -37.628 0.24 28.42 ? 40 THR A CA 1 ATOM 113 C CA B THR A 1 15 ? -13.035 -6.333 -37.617 0.76 27.53 ? 40 THR A CA 1 ATOM 114 C C . THR A 1 15 ? -14.380 -6.254 -38.334 1.00 27.16 ? 40 THR A C 1 ATOM 115 O O . THR A 1 15 ? -15.383 -5.870 -37.740 1.00 26.64 ? 40 THR A O 1 ATOM 116 C CB A THR A 1 15 ? -13.091 -7.441 -36.560 0.24 29.40 ? 40 THR A CB 1 ATOM 117 C CB B THR A 1 15 ? -13.104 -7.413 -36.521 0.76 28.70 ? 40 THR A CB 1 ATOM 118 O OG1 A THR A 1 15 ? -14.223 -7.234 -35.708 0.24 26.07 ? 40 THR A OG1 1 ATOM 119 O OG1 B THR A 1 15 ? -11.840 -7.491 -35.847 0.76 35.52 ? 40 THR A OG1 1 ATOM 120 C CG2 A THR A 1 15 ? -11.825 -7.444 -35.716 0.24 32.56 ? 40 THR A CG2 1 ATOM 121 C CG2 B THR A 1 15 ? -13.433 -8.764 -37.120 0.76 28.50 ? 40 THR A CG2 1 ATOM 122 N N . VAL A 1 16 ? -14.406 -6.618 -39.612 1.00 27.79 ? 41 VAL A N 1 ATOM 123 C CA . VAL A 1 16 ? -15.654 -6.584 -40.363 1.00 27.87 ? 41 VAL A CA 1 ATOM 124 C C . VAL A 1 16 ? -16.485 -7.833 -40.101 1.00 26.92 ? 41 VAL A C 1 ATOM 125 O O . VAL A 1 16 ? -15.953 -8.875 -39.707 1.00 28.60 ? 41 VAL A O 1 ATOM 126 C CB . VAL A 1 16 ? -15.423 -6.454 -41.882 1.00 33.69 ? 41 VAL A CB 1 ATOM 127 C CG1 . VAL A 1 16 ? -14.652 -5.180 -42.196 1.00 39.70 ? 41 VAL A CG1 1 ATOM 128 C CG2 . VAL A 1 16 ? -14.703 -7.683 -42.413 1.00 33.71 ? 41 VAL A CG2 1 ATOM 129 N N . PHE A 1 17 ? -17.789 -7.717 -40.331 1.00 27.61 ? 42 PHE A N 1 ATOM 130 C CA . PHE A 1 17 ? -18.700 -8.840 -40.182 1.00 29.55 ? 42 PHE A CA 1 ATOM 131 C C . PHE A 1 17 ? -18.171 -10.080 -40.890 1.00 32.33 ? 42 PHE A C 1 ATOM 132 O O . PHE A 1 17 ? -17.630 -9.998 -41.995 1.00 33.75 ? 42 PHE A O 1 ATOM 133 C CB . PHE A 1 17 ? -20.084 -8.484 -40.730 1.00 31.05 ? 42 PHE A CB 1 ATOM 134 C CG . PHE A 1 17 ? -21.021 -9.653 -40.797 1.00 34.18 ? 42 PHE A CG 1 ATOM 135 C CD1 . PHE A 1 17 ? -21.884 -9.928 -39.750 1.00 35.27 ? 42 PHE A CD1 1 ATOM 136 C CD2 . PHE A 1 17 ? -21.031 -10.487 -41.905 1.00 41.34 ? 42 PHE A CD2 1 ATOM 137 C CE1 . PHE A 1 17 ? -22.744 -11.008 -39.807 1.00 40.38 ? 42 PHE A CE1 1 ATOM 138 C CE2 . PHE A 1 17 ? -21.888 -11.569 -41.968 1.00 43.62 ? 42 PHE A CE2 1 ATOM 139 C CZ . PHE A 1 17 ? -22.746 -11.831 -40.918 1.00 41.78 ? 42 PHE A CZ 1 ATOM 140 N N . SER A 1 18 ? -18.334 -11.228 -40.244 1.00 31.80 ? 43 SER A N 1 ATOM 141 C CA . SER A 1 18 ? -17.987 -12.508 -40.847 1.00 31.21 ? 43 SER A CA 1 ATOM 142 C C . SER A 1 18 ? -19.074 -13.535 -40.556 1.00 38.47 ? 43 SER A C 1 ATOM 143 O O . SER A 1 18 ? -19.602 -13.589 -39.446 1.00 36.35 ? 43 SER A O 1 ATOM 144 C CB . SER A 1 18 ? -16.647 -13.008 -40.308 1.00 32.88 ? 43 SER A CB 1 ATOM 145 O OG . SER A 1 18 ? -16.367 -14.314 -40.788 1.00 35.93 ? 43 SER A OG 1 ATOM 146 N N . ALA A 1 19 ? -19.399 -14.351 -41.554 1.00 45.92 ? 44 ALA A N 1 ATOM 147 C CA . ALA A 1 19 ? -20.389 -15.410 -41.389 1.00 60.59 ? 44 ALA A CA 1 ATOM 148 C C . ALA A 1 19 ? -19.799 -16.612 -40.653 1.00 59.57 ? 44 ALA A C 1 ATOM 149 O O . ALA A 1 19 ? -20.530 -17.453 -40.131 1.00 59.03 ? 44 ALA A O 1 ATOM 150 C CB . ALA A 1 19 ? -20.948 -15.831 -42.740 1.00 63.49 ? 44 ALA A CB 1 ATOM 151 N N . ASP A 1 20 ? -18.471 -16.690 -40.623 1.00 52.11 ? 45 ASP A N 1 ATOM 152 C CA . ASP A 1 20 ? -17.778 -17.745 -39.894 1.00 45.12 ? 45 ASP A CA 1 ATOM 153 C C . ASP A 1 20 ? -18.254 -17.755 -38.445 1.00 53.41 ? 45 ASP A C 1 ATOM 154 O O . ASP A 1 20 ? -18.056 -16.784 -37.713 1.00 43.27 ? 45 ASP A O 1 ATOM 155 C CB . ASP A 1 20 ? -16.264 -17.526 -39.967 1.00 37.76 ? 45 ASP A CB 1 ATOM 156 C CG . ASP A 1 20 ? -15.472 -18.614 -39.261 1.00 33.79 ? 45 ASP A CG 1 ATOM 157 O OD1 . ASP A 1 20 ? -16.053 -19.670 -38.934 1.00 43.03 ? 45 ASP A OD1 1 ATOM 158 O OD2 . ASP A 1 20 ? -14.263 -18.409 -39.036 1.00 31.81 ? 45 ASP A OD2 1 ATOM 159 N N . SER A 1 21 ? -18.883 -18.855 -38.041 1.00 60.43 ? 46 SER A N 1 ATOM 160 C CA . SER A 1 21 ? -19.507 -18.956 -36.723 1.00 67.80 ? 46 SER A CA 1 ATOM 161 C C . SER A 1 21 ? -18.561 -18.612 -35.573 1.00 59.32 ? 46 SER A C 1 ATOM 162 O O . SER A 1 21 ? -18.954 -17.943 -34.620 1.00 56.42 ? 46 SER A O 1 ATOM 163 C CB . SER A 1 21 ? -20.103 -20.351 -36.514 1.00 80.25 ? 46 SER A CB 1 ATOM 164 O OG . SER A 1 21 ? -19.089 -21.339 -36.465 1.00 88.91 ? 46 SER A OG 1 ATOM 165 N N . ASP A 1 22 ? -17.319 -19.076 -35.656 1.00 45.97 ? 47 ASP A N 1 ATOM 166 C CA . ASP A 1 22 ? -16.337 -18.769 -34.621 1.00 49.64 ? 47 ASP A CA 1 ATOM 167 C C . ASP A 1 22 ? -15.241 -17.842 -35.138 1.00 40.46 ? 47 ASP A C 1 ATOM 168 O O . ASP A 1 22 ? -14.080 -17.941 -34.737 1.00 36.59 ? 47 ASP A O 1 ATOM 169 C CB . ASP A 1 22 ? -15.743 -20.045 -34.013 1.00 56.79 ? 47 ASP A CB 1 ATOM 170 C CG . ASP A 1 22 ? -15.221 -21.002 -35.059 1.00 64.46 ? 47 ASP A CG 1 ATOM 171 O OD1 . ASP A 1 22 ? -15.351 -20.696 -36.261 1.00 59.56 ? 47 ASP A OD1 1 ATOM 172 O OD2 . ASP A 1 22 ? -14.683 -22.063 -34.680 1.00 72.61 ? 47 ASP A OD2 1 ATOM 173 N N . SER A 1 23 ? -15.628 -16.936 -36.029 1.00 35.55 ? 48 SER A N 1 ATOM 174 C CA . SER A 1 23 ? -14.743 -15.877 -36.492 1.00 33.41 ? 48 SER A CA 1 ATOM 175 C C . SER A 1 23 ? -14.351 -14.983 -35.331 1.00 36.23 ? 48 SER A C 1 ATOM 176 O O . SER A 1 23 ? -15.027 -14.958 -34.300 1.00 31.29 ? 48 SER A O 1 ATOM 177 C CB . SER A 1 23 ? -15.446 -15.031 -37.557 1.00 29.98 ? 48 SER A CB 1 ATOM 178 O OG . SER A 1 23 ? -16.595 -14.390 -37.017 1.00 31.00 ? 48 SER A OG 1 ATOM 179 N N . ASP A 1 24 ? -13.263 -14.243 -35.501 1.00 30.32 ? 49 ASP A N 1 ATOM 180 C CA . ASP A 1 24 ? -12.869 -13.237 -34.522 1.00 27.37 ? 49 ASP A CA 1 ATOM 181 C C . ASP A 1 24 ? -13.978 -12.197 -34.329 1.00 27.97 ? 49 ASP A C 1 ATOM 182 O O . ASP A 1 24 ? -14.239 -11.748 -33.214 1.00 29.61 ? 49 ASP A O 1 ATOM 183 C CB . ASP A 1 24 ? -11.579 -12.547 -34.960 1.00 30.51 ? 49 ASP A CB 1 ATOM 184 C CG . ASP A 1 24 ? -10.410 -13.510 -35.073 1.00 44.04 ? 49 ASP A CG 1 ATOM 185 O OD1 . ASP A 1 24 ? -10.367 -14.496 -34.305 1.00 45.24 ? 49 ASP A OD1 1 ATOM 186 O OD2 . ASP A 1 24 ? -9.531 -13.280 -35.929 1.00 39.03 ? 49 ASP A OD2 1 ATOM 187 N N . PHE A 1 25 ? -14.624 -11.815 -35.424 1.00 26.25 ? 50 PHE A N 1 ATOM 188 C CA . PHE A 1 25 ? -15.745 -10.887 -35.366 1.00 26.86 ? 50 PHE A CA 1 ATOM 189 C C . PHE A 1 25 ? -16.783 -11.354 -34.350 1.00 26.59 ? 50 PHE A C 1 ATOM 190 O O . PHE A 1 25 ? -17.209 -10.592 -33.480 1.00 23.76 ? 50 PHE A O 1 ATOM 191 C CB . PHE A 1 25 ? -16.383 -10.753 -36.747 1.00 24.58 ? 50 PHE A CB 1 ATOM 192 C CG . PHE A 1 25 ? -17.701 -10.033 -36.741 1.00 25.48 ? 50 PHE A CG 1 ATOM 193 C CD1 . PHE A 1 25 ? -17.750 -8.647 -36.760 1.00 25.74 ? 50 PHE A CD1 1 ATOM 194 C CD2 . PHE A 1 25 ? -18.893 -10.741 -36.720 1.00 30.20 ? 50 PHE A CD2 1 ATOM 195 C CE1 . PHE A 1 25 ? -18.967 -7.980 -36.758 1.00 24.58 ? 50 PHE A CE1 1 ATOM 196 C CE2 . PHE A 1 25 ? -20.112 -10.081 -36.717 1.00 30.66 ? 50 PHE A CE2 1 ATOM 197 C CZ . PHE A 1 25 ? -20.149 -8.698 -36.736 1.00 26.56 ? 50 PHE A CZ 1 ATOM 198 N N . ASN A 1 26 ? -17.195 -12.611 -34.466 1.00 27.27 ? 51 ASN A N 1 ATOM 199 C CA A ASN A 1 26 ? -18.187 -13.183 -33.562 0.45 29.42 ? 51 ASN A CA 1 ATOM 200 C CA B ASN A 1 26 ? -18.200 -13.138 -33.556 0.55 28.46 ? 51 ASN A CA 1 ATOM 201 C C . ASN A 1 26 ? -17.680 -13.216 -32.125 1.00 28.65 ? 51 ASN A C 1 ATOM 202 O O . ASN A 1 26 ? -18.433 -12.979 -31.177 1.00 28.58 ? 51 ASN A O 1 ATOM 203 C CB A ASN A 1 26 ? -18.559 -14.597 -34.010 0.45 31.28 ? 51 ASN A CB 1 ATOM 204 C CB B ASN A 1 26 ? -18.726 -14.491 -34.041 0.55 31.95 ? 51 ASN A CB 1 ATOM 205 C CG A ASN A 1 26 ? -19.839 -15.091 -33.369 0.45 34.28 ? 51 ASN A CG 1 ATOM 206 C CG B ASN A 1 26 ? -19.814 -14.345 -35.093 0.55 29.68 ? 51 ASN A CG 1 ATOM 207 O OD1 A ASN A 1 26 ? -20.880 -14.443 -33.459 0.45 44.93 ? 51 ASN A OD1 1 ATOM 208 O OD1 B ASN A 1 26 ? -20.673 -13.466 -34.997 0.55 30.03 ? 51 ASN A OD1 1 ATOM 209 N ND2 A ASN A 1 26 ? -19.769 -16.248 -32.723 0.45 39.36 ? 51 ASN A ND2 1 ATOM 210 N ND2 B ASN A 1 26 ? -19.786 -15.211 -36.099 0.55 36.67 ? 51 ASN A ND2 1 ATOM 211 N N . ARG A 1 27 ? -16.397 -13.520 -31.973 1.00 25.67 ? 52 ARG A N 1 ATOM 212 C CA . ARG A 1 27 ? -15.786 -13.576 -30.654 1.00 25.04 ? 52 ARG A CA 1 ATOM 213 C C . ARG A 1 27 ? -15.887 -12.216 -29.973 1.00 28.12 ? 52 ARG A C 1 ATOM 214 O O . ARG A 1 27 ? -16.322 -12.120 -28.822 1.00 26.33 ? 52 ARG A O 1 ATOM 215 C CB . ARG A 1 27 ? -14.328 -14.031 -30.749 1.00 29.05 ? 52 ARG A CB 1 ATOM 216 C CG . ARG A 1 27 ? -13.656 -14.235 -29.405 1.00 31.96 ? 52 ARG A CG 1 ATOM 217 C CD . ARG A 1 27 ? -12.357 -15.018 -29.552 1.00 41.46 ? 52 ARG A CD 1 ATOM 218 N NE . ARG A 1 27 ? -11.423 -14.369 -30.468 1.00 48.15 ? 52 ARG A NE 1 ATOM 219 C CZ . ARG A 1 27 ? -10.571 -13.412 -30.112 1.00 51.08 ? 52 ARG A CZ 1 ATOM 220 N NH1 . ARG A 1 27 ? -10.535 -12.985 -28.855 1.00 44.59 ? 52 ARG A NH1 1 ATOM 221 N NH2 . ARG A 1 27 ? -9.756 -12.880 -31.014 1.00 49.79 ? 52 ARG A NH2 1 ATOM 222 N N . PHE A 1 28 ? -15.500 -11.162 -30.688 1.00 24.27 ? 53 PHE A N 1 ATOM 223 C CA . PHE A 1 28 ? -15.586 -9.809 -30.136 1.00 27.22 ? 53 PHE A CA 1 ATOM 224 C C . PHE A 1 28 ? -17.032 -9.394 -29.878 1.00 22.18 ? 53 PHE A C 1 ATOM 225 O O . PHE A 1 28 ? -17.334 -8.776 -28.855 1.00 22.82 ? 53 PHE A O 1 ATOM 226 C CB . PHE A 1 28 ? -14.926 -8.784 -31.058 1.00 26.96 ? 53 PHE A CB 1 ATOM 227 C CG . PHE A 1 28 ? -13.438 -8.933 -31.166 1.00 31.86 ? 53 PHE A CG 1 ATOM 228 C CD1 . PHE A 1 28 ? -12.657 -9.094 -30.035 1.00 38.65 ? 53 PHE A CD1 1 ATOM 229 C CD2 . PHE A 1 28 ? -12.820 -8.885 -32.401 1.00 33.11 ? 53 PHE A CD2 1 ATOM 230 C CE1 . PHE A 1 28 ? -11.279 -9.226 -30.138 1.00 33.60 ? 53 PHE A CE1 1 ATOM 231 C CE2 . PHE A 1 28 ? -11.449 -9.010 -32.511 1.00 34.76 ? 53 PHE A CE2 1 ATOM 232 C CZ . PHE A 1 28 ? -10.681 -9.180 -31.376 1.00 33.86 ? 53 PHE A CZ 1 ATOM 233 N N . LEU A 1 29 ? -17.924 -9.723 -30.805 1.00 22.09 ? 54 LEU A N 1 ATOM 234 C CA . LEU A 1 29 ? -19.331 -9.379 -30.634 1.00 23.08 ? 54 LEU A CA 1 ATOM 235 C C . LEU A 1 29 ? -19.864 -9.935 -29.318 1.00 23.24 ? 54 LEU A C 1 ATOM 236 O O . LEU A 1 29 ? -20.454 -9.208 -28.526 1.00 22.95 ? 54 LEU A O 1 ATOM 237 C CB . LEU A 1 29 ? -20.175 -9.896 -31.803 1.00 22.33 ? 54 LEU A CB 1 ATOM 238 C CG . LEU A 1 29 ? -21.687 -9.677 -31.689 1.00 23.84 ? 54 LEU A CG 1 ATOM 239 C CD1 . LEU A 1 29 ? -22.004 -8.198 -31.536 1.00 24.52 ? 54 LEU A CD1 1 ATOM 240 C CD2 . LEU A 1 29 ? -22.404 -10.257 -32.895 1.00 24.27 ? 54 LEU A CD2 1 ATOM 241 N N . HIS A 1 30 ? -19.644 -11.225 -29.083 1.00 24.60 ? 55 HIS A N 1 ATOM 242 C CA . HIS A 1 30 ? -20.271 -11.908 -27.952 1.00 23.62 ? 55 HIS A CA 1 ATOM 243 C C . HIS A 1 30 ? -19.567 -11.680 -26.622 1.00 25.78 ? 55 HIS A C 1 ATOM 244 O O . HIS A 1 30 ? -20.146 -11.897 -25.557 1.00 26.68 ? 55 HIS A O 1 ATOM 245 C CB . HIS A 1 30 ? -20.415 -13.400 -28.249 1.00 28.45 ? 55 HIS A CB 1 ATOM 246 C CG . HIS A 1 30 ? -21.400 -13.689 -29.337 1.00 33.48 ? 55 HIS A CG 1 ATOM 247 N ND1 . HIS A 1 30 ? -22.746 -13.858 -29.095 1.00 38.90 ? 55 HIS A ND1 1 ATOM 248 C CD2 . HIS A 1 30 ? -21.240 -13.808 -30.676 1.00 40.43 ? 55 HIS A CD2 1 ATOM 249 C CE1 . HIS A 1 30 ? -23.371 -14.084 -30.237 1.00 42.39 ? 55 HIS A CE1 1 ATOM 250 N NE2 . HIS A 1 30 ? -22.480 -14.056 -31.212 1.00 34.97 ? 55 HIS A NE2 1 ATOM 251 N N . LEU A 1 31 ? -18.324 -11.219 -26.697 1.00 23.69 ? 56 LEU A N 1 ATOM 252 C CA . LEU A 1 31 ? -17.481 -11.043 -25.525 1.00 24.56 ? 56 LEU A CA 1 ATOM 253 C C . LEU A 1 31 ? -18.172 -10.214 -24.443 1.00 25.69 ? 56 LEU A C 1 ATOM 254 O O . LEU A 1 31 ? -18.068 -10.523 -23.255 1.00 27.34 ? 56 LEU A O 1 ATOM 255 C CB . LEU A 1 31 ? -16.167 -10.379 -25.936 1.00 34.79 ? 56 LEU A CB 1 ATOM 256 C CG . LEU A 1 31 ? -14.987 -10.452 -24.970 1.00 39.11 ? 56 LEU A CG 1 ATOM 257 C CD1 . LEU A 1 31 ? -14.698 -11.890 -24.577 1.00 33.15 ? 56 LEU A CD1 1 ATOM 258 C CD2 . LEU A 1 31 ? -13.765 -9.809 -25.602 1.00 37.26 ? 56 LEU A CD2 1 ATOM 259 N N . SER A 1 32 ? -18.882 -9.167 -24.857 1.00 22.36 ? 57 SER A N 1 ATOM 260 C CA . SER A 1 32 ? -19.532 -8.273 -23.904 1.00 24.56 ? 57 SER A CA 1 ATOM 261 C C . SER A 1 32 ? -21.046 -8.209 -24.067 1.00 23.93 ? 57 SER A C 1 ATOM 262 O O . SER A 1 32 ? -21.663 -7.181 -23.782 1.00 25.26 ? 57 SER A O 1 ATOM 263 C CB . SER A 1 32 ? -18.938 -6.865 -23.984 1.00 24.52 ? 57 SER A CB 1 ATOM 264 O OG . SER A 1 32 ? -17.597 -6.872 -23.528 1.00 34.26 ? 57 SER A OG 1 ATOM 265 N N . ILE A 1 33 ? -21.652 -9.295 -24.531 1.00 20.22 ? 58 ILE A N 1 ATOM 266 C CA . ILE A 1 33 ? -23.108 -9.390 -24.482 1.00 21.29 ? 58 ILE A CA 1 ATOM 267 C C . ILE A 1 33 ? -23.475 -9.960 -23.121 1.00 25.82 ? 58 ILE A C 1 ATOM 268 O O . ILE A 1 33 ? -23.200 -11.129 -22.834 1.00 28.30 ? 58 ILE A O 1 ATOM 269 C CB . ILE A 1 33 ? -23.675 -10.266 -25.608 1.00 22.90 ? 58 ILE A CB 1 ATOM 270 C CG1 . ILE A 1 33 ? -23.492 -9.562 -26.954 1.00 20.31 ? 58 ILE A CG1 1 ATOM 271 C CG2 . ILE A 1 33 ? -25.156 -10.552 -25.368 1.00 21.88 ? 58 ILE A CG2 1 ATOM 272 C CD1 . ILE A 1 33 ? -23.996 -10.363 -28.133 1.00 22.83 ? 58 ILE A CD1 1 ATOM 273 N N . GLN A 1 34 ? -24.071 -9.128 -22.272 1.00 20.64 ? 59 GLN A N 1 ATOM 274 C CA . GLN A 1 34 ? -24.341 -9.535 -20.894 1.00 19.52 ? 59 GLN A CA 1 ATOM 275 C C . GLN A 1 34 ? -25.779 -9.978 -20.657 1.00 26.94 ? 59 GLN A C 1 ATOM 276 O O . GLN A 1 34 ? -26.149 -10.338 -19.543 1.00 31.38 ? 59 GLN A O 1 ATOM 277 C CB . GLN A 1 34 ? -23.943 -8.423 -19.916 1.00 18.85 ? 59 GLN A CB 1 ATOM 278 C CG . GLN A 1 34 ? -22.469 -8.059 -19.980 1.00 23.13 ? 59 GLN A CG 1 ATOM 279 C CD . GLN A 1 34 ? -21.571 -9.106 -19.344 1.00 29.12 ? 59 GLN A CD 1 ATOM 280 O OE1 . GLN A 1 34 ? -21.972 -10.252 -19.144 1.00 33.13 ? 59 GLN A OE1 1 ATOM 281 N NE2 . GLN A 1 34 ? -20.343 -8.715 -19.028 1.00 37.55 ? 59 GLN A NE2 1 ATOM 282 N N . ASN A 1 35 ? -26.589 -9.950 -21.707 1.00 23.31 ? 60 ASN A N 1 ATOM 283 C CA . ASN A 1 35 ? -27.917 -10.541 -21.647 1.00 19.75 ? 60 ASN A CA 1 ATOM 284 C C . ASN A 1 35 ? -28.107 -11.487 -22.823 1.00 22.10 ? 60 ASN A C 1 ATOM 285 O O . ASN A 1 35 ? -28.360 -11.039 -23.940 1.00 26.76 ? 60 ASN A O 1 ATOM 286 C CB . ASN A 1 35 ? -29.014 -9.477 -21.641 1.00 22.05 ? 60 ASN A CB 1 ATOM 287 C CG . ASN A 1 35 ? -30.386 -10.071 -21.364 1.00 19.41 ? 60 ASN A CG 1 ATOM 288 O OD1 . ASN A 1 35 ? -30.541 -11.290 -21.334 1.00 22.05 ? 60 ASN A OD1 1 ATOM 289 N ND2 . ASN A 1 35 ? -31.384 -9.211 -21.165 1.00 22.64 ? 60 ASN A ND2 1 ATOM 290 N N . PRO A 1 36 ? -27.974 -12.800 -22.574 1.00 24.16 ? 61 PRO A N 1 ATOM 291 C CA . PRO A 1 36 ? -28.099 -13.843 -23.598 1.00 24.50 ? 61 PRO A CA 1 ATOM 292 C C . PRO A 1 36 ? -29.397 -13.759 -24.402 1.00 24.99 ? 61 PRO A C 1 ATOM 293 O O . PRO A 1 36 ? -29.471 -14.344 -25.482 1.00 27.38 ? 61 PRO A O 1 ATOM 294 C CB . PRO A 1 36 ? -28.066 -15.137 -22.780 1.00 26.21 ? 61 PRO A CB 1 ATOM 295 C CG . PRO A 1 36 ? -27.252 -14.795 -21.589 1.00 28.80 ? 61 PRO A CG 1 ATOM 296 C CD . PRO A 1 36 ? -27.581 -13.361 -21.267 1.00 24.65 ? 61 PRO A CD 1 ATOM 297 N N . LEU A 1 37 ? -30.398 -13.051 -23.886 1.00 25.38 ? 62 LEU A N 1 ATOM 298 C CA . LEU A 1 37 ? -31.649 -12.850 -24.614 1.00 23.85 ? 62 LEU A CA 1 ATOM 299 C C . LEU A 1 37 ? -31.400 -12.263 -26.006 1.00 24.95 ? 62 LEU A C 1 ATOM 300 O O . LEU A 1 37 ? -32.195 -12.465 -26.925 1.00 28.77 ? 62 LEU A O 1 ATOM 301 C CB . LEU A 1 37 ? -32.586 -11.924 -23.824 1.00 24.45 ? 62 LEU A CB 1 ATOM 302 C CG . LEU A 1 37 ? -33.964 -11.649 -24.436 1.00 25.63 ? 62 LEU A CG 1 ATOM 303 C CD1 . LEU A 1 37 ? -34.703 -12.951 -24.694 1.00 30.92 ? 62 LEU A CD1 1 ATOM 304 C CD2 . LEU A 1 37 ? -34.791 -10.712 -23.547 1.00 25.51 ? 62 LEU A CD2 1 ATOM 305 N N . PHE A 1 38 ? -30.295 -11.539 -26.157 1.00 25.40 ? 63 PHE A N 1 ATOM 306 C CA . PHE A 1 38 ? -29.989 -10.865 -27.418 1.00 27.12 ? 63 PHE A CA 1 ATOM 307 C C . PHE A 1 38 ? -28.757 -11.445 -28.108 1.00 27.48 ? 63 PHE A C 1 ATOM 308 O O . PHE A 1 38 ? -28.034 -10.735 -28.810 1.00 29.84 ? 63 PHE A O 1 ATOM 309 C CB . PHE A 1 38 ? -29.815 -9.362 -27.184 1.00 24.54 ? 63 PHE A CB 1 ATOM 310 C CG . PHE A 1 38 ? -30.996 -8.725 -26.528 1.00 25.43 ? 63 PHE A CG 1 ATOM 311 C CD1 . PHE A 1 38 ? -32.127 -8.407 -27.267 1.00 24.13 ? 63 PHE A CD1 1 ATOM 312 C CD2 . PHE A 1 38 ? -30.994 -8.467 -25.168 1.00 25.91 ? 63 PHE A CD2 1 ATOM 313 C CE1 . PHE A 1 38 ? -33.227 -7.831 -26.660 1.00 32.54 ? 63 PHE A CE1 1 ATOM 314 C CE2 . PHE A 1 38 ? -32.090 -7.893 -24.559 1.00 26.28 ? 63 PHE A CE2 1 ATOM 315 C CZ . PHE A 1 38 ? -33.205 -7.572 -25.300 1.00 27.40 ? 63 PHE A CZ 1 ATOM 316 N N . GLN A 1 39 ? -28.528 -12.738 -27.920 1.00 30.90 ? 64 GLN A N 1 ATOM 317 C CA . GLN A 1 39 ? -27.323 -13.371 -28.444 1.00 35.18 ? 64 GLN A CA 1 ATOM 318 C C . GLN A 1 39 ? -27.577 -14.240 -29.679 1.00 50.31 ? 64 GLN A C 1 ATOM 319 O O . GLN A 1 39 ? -26.650 -14.543 -30.432 1.00 54.48 ? 64 GLN A O 1 ATOM 320 C CB . GLN A 1 39 ? -26.655 -14.193 -27.342 1.00 37.89 ? 64 GLN A CB 1 ATOM 321 C CG . GLN A 1 39 ? -25.160 -14.352 -27.501 1.00 56.02 ? 64 GLN A CG 1 ATOM 322 C CD . GLN A 1 39 ? -24.437 -14.359 -26.169 1.00 59.83 ? 64 GLN A CD 1 ATOM 323 O OE1 . GLN A 1 39 ? -25.047 -14.567 -25.119 1.00 67.30 ? 64 GLN A OE1 1 ATOM 324 N NE2 . GLN A 1 39 ? -23.131 -14.123 -26.203 1.00 47.30 ? 64 GLN A NE2 1 ATOM 325 N N . ASN A 1 40 ? -28.833 -14.619 -29.892 1.00 46.85 ? 65 ASN A N 1 ATOM 326 C CA . ASN A 1 40 ? -29.183 -15.594 -30.929 1.00 52.53 ? 65 ASN A CA 1 ATOM 327 C C . ASN A 1 40 ? -29.000 -15.121 -32.376 1.00 50.36 ? 65 ASN A C 1 ATOM 328 O O . ASN A 1 40 ? -28.828 -13.931 -32.644 1.00 46.79 ? 65 ASN A O 1 ATOM 329 C CB . ASN A 1 40 ? -30.607 -16.115 -30.715 1.00 51.41 ? 65 ASN A CB 1 ATOM 330 C CG . ASN A 1 40 ? -31.661 -15.097 -31.087 1.00 49.07 ? 65 ASN A CG 1 ATOM 331 O OD1 . ASN A 1 40 ? -31.877 -14.814 -32.264 1.00 44.77 ? 65 ASN A OD1 1 ATOM 332 N ND2 . ASN A 1 40 ? -32.333 -14.545 -30.083 1.00 53.22 ? 65 ASN A ND2 1 ATOM 333 N N . SER A 1 41 ? -29.059 -16.074 -33.302 1.00 55.86 ? 66 SER A N 1 ATOM 334 C CA . SER A 1 41 ? -28.744 -15.831 -34.708 1.00 57.60 ? 66 SER A CA 1 ATOM 335 C C . SER A 1 41 ? -29.758 -14.956 -35.447 1.00 53.83 ? 66 SER A C 1 ATOM 336 O O . SER A 1 41 ? -29.474 -14.465 -36.538 1.00 63.20 ? 66 SER A O 1 ATOM 337 C CB . SER A 1 41 ? -28.581 -17.162 -35.446 1.00 61.81 ? 66 SER A CB 1 ATOM 338 O OG . SER A 1 41 ? -29.769 -17.933 -35.373 1.00 62.06 ? 66 SER A OG 1 ATOM 339 N N . LEU A 1 42 ? -30.937 -14.768 -34.864 1.00 45.76 ? 67 LEU A N 1 ATOM 340 C CA . LEU A 1 42 ? -31.974 -13.958 -35.502 1.00 51.04 ? 67 LEU A CA 1 ATOM 341 C C . LEU A 1 42 ? -31.858 -12.467 -35.164 1.00 50.52 ? 67 LEU A C 1 ATOM 342 O O . LEU A 1 42 ? -32.605 -11.644 -35.694 1.00 61.41 ? 67 LEU A O 1 ATOM 343 C CB . LEU A 1 42 ? -33.364 -14.477 -35.131 1.00 62.49 ? 67 LEU A CB 1 ATOM 344 C CG . LEU A 1 42 ? -33.757 -15.829 -35.732 1.00 69.77 ? 67 LEU A CG 1 ATOM 345 C CD1 . LEU A 1 42 ? -35.071 -16.321 -35.144 1.00 73.44 ? 67 LEU A CD1 1 ATOM 346 C CD2 . LEU A 1 42 ? -33.845 -15.733 -37.248 1.00 70.67 ? 67 LEU A CD2 1 ATOM 347 N N . ILE A 1 43 ? -30.920 -12.131 -34.286 1.00 37.28 ? 68 ILE A N 1 ATOM 348 C CA . ILE A 1 43 ? -30.708 -10.747 -33.864 1.00 31.55 ? 68 ILE A CA 1 ATOM 349 C C . ILE A 1 43 ? -29.839 -9.987 -34.866 1.00 35.66 ? 68 ILE A C 1 ATOM 350 O O . ILE A 1 43 ? -28.959 -10.570 -35.497 1.00 36.24 ? 68 ILE A O 1 ATOM 351 C CB . ILE A 1 43 ? -30.023 -10.691 -32.479 1.00 37.44 ? 68 ILE A CB 1 ATOM 352 C CG1 . ILE A 1 43 ? -30.832 -11.476 -31.443 1.00 41.67 ? 68 ILE A CG1 1 ATOM 353 C CG2 . ILE A 1 43 ? -29.823 -9.249 -32.029 1.00 37.29 ? 68 ILE A CG2 1 ATOM 354 C CD1 . ILE A 1 43 ? -32.123 -10.802 -31.031 1.00 43.19 ? 68 ILE A CD1 1 ATOM 355 N N . SER A 1 44 ? -30.091 -8.687 -35.004 1.00 36.58 ? 69 SER A N 1 ATOM 356 C CA . SER A 1 44 ? -29.268 -7.817 -35.844 1.00 41.25 ? 69 SER A CA 1 ATOM 357 C C . SER A 1 44 ? -27.798 -7.917 -35.444 1.00 28.51 ? 69 SER A C 1 ATOM 358 O O . SER A 1 44 ? -27.493 -8.051 -34.264 1.00 29.83 ? 69 SER A O 1 ATOM 359 C CB . SER A 1 44 ? -29.741 -6.363 -35.720 1.00 31.87 ? 69 SER A CB 1 ATOM 360 O OG . SER A 1 44 ? -29.605 -5.878 -34.383 1.00 25.97 ? 69 SER A OG 1 ATOM 361 N N . LYS A 1 45 ? -26.897 -7.861 -36.425 1.00 29.07 ? 70 LYS A N 1 ATOM 362 C CA . LYS A 1 45 ? -25.453 -7.898 -36.156 1.00 26.44 ? 70 LYS A CA 1 ATOM 363 C C . LYS A 1 45 ? -24.723 -6.703 -36.780 1.00 26.19 ? 70 LYS A C 1 ATOM 364 O O . LYS A 1 45 ? -25.093 -6.234 -37.857 1.00 27.01 ? 70 LYS A O 1 ATOM 365 C CB . LYS A 1 45 ? -24.832 -9.203 -36.662 1.00 33.51 ? 70 LYS A CB 1 ATOM 366 C CG . LYS A 1 45 ? -25.610 -10.460 -36.299 1.00 41.16 ? 70 LYS A CG 1 ATOM 367 C CD . LYS A 1 45 ? -25.465 -10.824 -34.830 1.00 39.06 ? 70 LYS A CD 1 ATOM 368 C CE . LYS A 1 45 ? -26.261 -12.086 -34.500 1.00 40.98 ? 70 LYS A CE 1 ATOM 369 N NZ . LYS A 1 45 ? -26.220 -12.430 -33.046 1.00 44.28 ? 70 LYS A NZ 1 ATOM 370 N N . PRO A 1 46 ? -23.673 -6.210 -36.108 1.00 23.15 ? 71 PRO A N 1 ATOM 371 C CA . PRO A 1 46 ? -22.936 -5.055 -36.638 1.00 23.72 ? 71 PRO A CA 1 ATOM 372 C C . PRO A 1 46 ? -22.245 -5.373 -37.958 1.00 26.17 ? 71 PRO A C 1 ATOM 373 O O . PRO A 1 46 ? -21.851 -6.517 -38.188 1.00 26.95 ? 71 PRO A O 1 ATOM 374 C CB . PRO A 1 46 ? -21.860 -4.777 -35.575 1.00 23.21 ? 71 PRO A CB 1 ATOM 375 C CG . PRO A 1 46 ? -22.080 -5.730 -34.468 1.00 27.37 ? 71 PRO A CG 1 ATOM 376 C CD . PRO A 1 46 ? -23.100 -6.745 -34.860 1.00 23.60 ? 71 PRO A CD 1 ATOM 377 N N . SER A 1 47 ? -22.082 -4.363 -38.808 1.00 23.67 ? 72 SER A N 1 ATOM 378 C CA . SER A 1 47 ? -21.339 -4.531 -40.054 1.00 24.94 ? 72 SER A CA 1 ATOM 379 C C . SER A 1 47 ? -19.833 -4.545 -39.810 1.00 24.60 ? 72 SER A C 1 ATOM 380 O O . SER A 1 47 ? -19.066 -5.088 -40.608 1.00 26.74 ? 72 SER A O 1 ATOM 381 C CB . SER A 1 47 ? -21.705 -3.428 -41.042 1.00 29.93 ? 72 SER A CB 1 ATOM 382 O OG . SER A 1 47 ? -23.099 -3.439 -41.289 1.00 32.38 ? 72 SER A OG 1 ATOM 383 N N . ALA A 1 48 ? -19.413 -3.939 -38.703 1.00 24.02 ? 73 ALA A N 1 ATOM 384 C CA . ALA A 1 48 ? -18.023 -3.979 -38.276 1.00 22.89 ? 73 ALA A CA 1 ATOM 385 C C . ALA A 1 48 ? -17.959 -3.630 -36.803 1.00 21.19 ? 73 ALA A C 1 ATOM 386 O O . ALA A 1 48 ? -18.881 -3.013 -36.267 1.00 21.75 ? 73 ALA A O 1 ATOM 387 C CB . ALA A 1 48 ? -17.171 -3.009 -39.087 1.00 26.80 ? 73 ALA A CB 1 ATOM 388 N N . ILE A 1 49 ? -16.874 -4.039 -36.158 1.00 21.20 ? 74 ILE A N 1 ATOM 389 C CA . ILE A 1 49 ? -16.635 -3.725 -34.757 1.00 23.12 ? 74 ILE A CA 1 ATOM 390 C C . ILE A 1 49 ? -15.300 -3.000 -34.668 1.00 23.71 ? 74 ILE A C 1 ATOM 391 O O . ILE A 1 49 ? -14.289 -3.483 -35.180 1.00 23.98 ? 74 ILE A O 1 ATOM 392 C CB . ILE A 1 49 ? -16.604 -5.005 -33.902 1.00 22.34 ? 74 ILE A CB 1 ATOM 393 C CG1 . ILE A 1 49 ? -17.935 -5.755 -34.038 1.00 25.91 ? 74 ILE A CG1 1 ATOM 394 C CG2 . ILE A 1 49 ? -16.298 -4.678 -32.437 1.00 22.97 ? 74 ILE A CG2 1 ATOM 395 C CD1 . ILE A 1 49 ? -17.994 -7.066 -33.287 1.00 26.34 ? 74 ILE A CD1 1 ATOM 396 N N . ILE A 1 50 ? -15.310 -1.827 -34.039 1.00 23.09 ? 75 ILE A N 1 ATOM 397 C CA . ILE A 1 50 ? -14.111 -1.010 -33.885 1.00 24.21 ? 75 ILE A CA 1 ATOM 398 C C . ILE A 1 50 ? -13.758 -0.935 -32.409 1.00 20.92 ? 75 ILE A C 1 ATOM 399 O O . ILE A 1 50 ? -14.639 -0.696 -31.579 1.00 21.30 ? 75 ILE A O 1 ATOM 400 C CB . ILE A 1 50 ? -14.336 0.435 -34.387 1.00 25.02 ? 75 ILE A CB 1 ATOM 401 C CG1 . ILE A 1 50 ? -15.147 0.451 -35.688 1.00 29.87 ? 75 ILE A CG1 1 ATOM 402 C CG2 . ILE A 1 50 ? -13.009 1.162 -34.542 1.00 27.40 ? 75 ILE A CG2 1 ATOM 403 C CD1 . ILE A 1 50 ? -14.587 -0.421 -36.773 1.00 32.86 ? 75 ILE A CD1 1 ATOM 404 N N . LEU A 1 51 ? -12.482 -1.134 -32.088 1.00 22.36 ? 76 LEU A N 1 ATOM 405 C CA . LEU A 1 51 ? -11.997 -1.055 -30.711 1.00 23.60 ? 76 LEU A CA 1 ATOM 406 C C . LEU A 1 51 ? -10.955 0.053 -30.570 1.00 24.42 ? 76 LEU A C 1 ATOM 407 O O . LEU A 1 51 ? -9.751 -0.216 -30.602 1.00 28.26 ? 76 LEU A O 1 ATOM 408 C CB . LEU A 1 51 ? -11.374 -2.385 -30.286 1.00 28.12 ? 76 LEU A CB 1 ATOM 409 C CG . LEU A 1 51 ? -12.273 -3.497 -29.753 1.00 36.95 ? 76 LEU A CG 1 ATOM 410 C CD1 . LEU A 1 51 ? -13.313 -3.894 -30.774 1.00 36.06 ? 76 LEU A CD1 1 ATOM 411 C CD2 . LEU A 1 51 ? -11.417 -4.690 -29.368 1.00 43.82 ? 76 LEU A CD2 1 ATOM 412 N N . PRO A 1 52 ? -11.411 1.304 -30.414 1.00 23.05 ? 77 PRO A N 1 ATOM 413 C CA . PRO A 1 52 ? -10.478 2.432 -30.276 1.00 22.81 ? 77 PRO A CA 1 ATOM 414 C C . PRO A 1 52 ? -9.625 2.311 -29.016 1.00 27.32 ? 77 PRO A C 1 ATOM 415 O O . PRO A 1 52 ? -10.132 1.907 -27.970 1.00 25.55 ? 77 PRO A O 1 ATOM 416 C CB . PRO A 1 52 ? -11.396 3.652 -30.187 1.00 24.69 ? 77 PRO A CB 1 ATOM 417 C CG . PRO A 1 52 ? -12.748 3.112 -29.818 1.00 26.41 ? 77 PRO A CG 1 ATOM 418 C CD . PRO A 1 52 ? -12.824 1.715 -30.332 1.00 25.57 ? 77 PRO A CD 1 ATOM 419 N N . GLY A 1 53 ? -8.344 2.653 -29.122 1.00 27.91 ? 78 GLY A N 1 ATOM 420 C CA . GLY A 1 53 ? -7.425 2.513 -28.005 1.00 31.35 ? 78 GLY A CA 1 ATOM 421 C C . GLY A 1 53 ? -7.049 3.819 -27.329 1.00 29.49 ? 78 GLY A C 1 ATOM 422 O O . GLY A 1 53 ? -6.243 3.834 -26.399 1.00 32.07 ? 78 GLY A O 1 ATOM 423 N N . SER A 1 54 ? -7.624 4.919 -27.798 1.00 25.85 ? 79 SER A N 1 ATOM 424 C CA . SER A 1 54 ? -7.331 6.228 -27.226 1.00 27.67 ? 79 SER A CA 1 ATOM 425 C C . SER A 1 54 ? -8.448 7.201 -27.551 1.00 28.88 ? 79 SER A C 1 ATOM 426 O O . SER A 1 54 ? -9.301 6.918 -28.393 1.00 28.27 ? 79 SER A O 1 ATOM 427 C CB . SER A 1 54 ? -6.008 6.765 -27.774 1.00 32.54 ? 79 SER A CB 1 ATOM 428 O OG . SER A 1 54 ? -6.146 7.133 -29.137 1.00 31.70 ? 79 SER A OG 1 ATOM 429 N N . LYS A 1 55 ? -8.448 8.351 -26.885 1.00 29.77 ? 80 LYS A N 1 ATOM 430 C CA . LYS A 1 55 ? -9.478 9.351 -27.137 1.00 32.32 ? 80 LYS A CA 1 ATOM 431 C C . LYS A 1 55 ? -9.372 9.879 -28.562 1.00 29.13 ? 80 LYS A C 1 ATOM 432 O O . LYS A 1 55 ? -10.379 10.203 -29.190 1.00 29.34 ? 80 LYS A O 1 ATOM 433 C CB . LYS A 1 55 ? -9.403 10.495 -26.125 1.00 35.60 ? 80 LYS A CB 1 ATOM 434 C CG . LYS A 1 55 ? -8.145 11.328 -26.207 1.00 39.31 ? 80 LYS A CG 1 ATOM 435 C CD . LYS A 1 55 ? -8.156 12.420 -25.149 1.00 44.85 ? 80 LYS A CD 1 ATOM 436 C CE . LYS A 1 55 ? -6.881 13.240 -25.187 1.00 49.14 ? 80 LYS A CE 1 ATOM 437 N NZ . LYS A 1 55 ? -6.917 14.342 -24.190 1.00 57.76 ? 80 LYS A NZ 1 ATOM 438 N N . GLU A 1 56 ? -8.147 9.959 -29.071 1.00 30.99 ? 81 GLU A N 1 ATOM 439 C CA . GLU A 1 56 ? -7.931 10.382 -30.447 1.00 31.72 ? 81 GLU A CA 1 ATOM 440 C C . GLU A 1 56 ? -8.519 9.372 -31.428 1.00 27.77 ? 81 GLU A C 1 ATOM 441 O O . GLU A 1 56 ? -9.145 9.751 -32.417 1.00 27.27 ? 81 GLU A O 1 ATOM 442 C CB . GLU A 1 56 ? -6.438 10.588 -30.727 1.00 33.72 ? 81 GLU A CB 1 ATOM 443 C CG . GLU A 1 56 ? -5.858 11.843 -30.096 1.00 37.59 ? 81 GLU A CG 1 ATOM 444 C CD . GLU A 1 56 ? -5.594 11.692 -28.613 1.00 45.06 ? 81 GLU A CD 1 ATOM 445 O OE1 . GLU A 1 56 ? -5.525 10.542 -28.127 1.00 39.05 ? 81 GLU A OE1 1 ATOM 446 O OE2 . GLU A 1 56 ? -5.449 12.729 -27.931 1.00 53.68 ? 81 GLU A OE2 1 ATOM 447 N N . GLU A 1 57 ? -8.315 8.087 -31.156 1.00 27.80 ? 82 GLU A N 1 ATOM 448 C CA . GLU A 1 57 ? -8.890 7.041 -32.000 1.00 28.48 ? 82 GLU A CA 1 ATOM 449 C C . GLU A 1 57 ? -10.415 7.046 -31.924 1.00 24.33 ? 82 GLU A C 1 ATOM 450 O O . GLU A 1 57 ? -11.098 6.787 -32.916 1.00 24.75 ? 82 GLU A O 1 ATOM 451 C CB . GLU A 1 57 ? -8.341 5.661 -31.632 1.00 26.82 ? 82 GLU A CB 1 ATOM 452 C CG . GLU A 1 57 ? -6.900 5.434 -32.081 1.00 27.37 ? 82 GLU A CG 1 ATOM 453 C CD . GLU A 1 57 ? -6.431 4.006 -31.863 1.00 34.95 ? 82 GLU A CD 1 ATOM 454 O OE1 . GLU A 1 57 ? -7.286 3.107 -31.737 1.00 30.32 ? 82 GLU A OE1 1 ATOM 455 O OE2 . GLU A 1 57 ? -5.201 3.780 -31.825 1.00 39.10 ? 82 GLU A OE2 1 ATOM 456 N N . LEU A 1 58 ? -10.953 7.337 -30.744 1.00 23.45 ? 83 LEU A N 1 ATOM 457 C CA . LEU A 1 58 ? -12.401 7.408 -30.594 1.00 23.49 ? 83 LEU A CA 1 ATOM 458 C C . LEU A 1 58 ? -12.960 8.556 -31.437 1.00 25.48 ? 83 LEU A C 1 ATOM 459 O O . LEU A 1 58 ? -13.957 8.397 -32.143 1.00 24.50 ? 83 LEU A O 1 ATOM 460 C CB . LEU A 1 58 ? -12.783 7.561 -29.115 1.00 20.49 ? 83 LEU A CB 1 ATOM 461 C CG . LEU A 1 58 ? -14.271 7.647 -28.744 1.00 20.64 ? 83 LEU A CG 1 ATOM 462 C CD1 . LEU A 1 58 ? -15.107 6.556 -29.416 1.00 22.64 ? 83 LEU A CD1 1 ATOM 463 C CD2 . LEU A 1 58 ? -14.463 7.605 -27.215 1.00 20.50 ? 83 LEU A CD2 1 ATOM 464 N N . SER A 1 59 ? -12.298 9.707 -31.367 1.00 27.14 ? 84 SER A N 1 ATOM 465 C CA . SER A 1 59 ? -12.691 10.876 -32.147 1.00 28.38 ? 84 SER A CA 1 ATOM 466 C C . SER A 1 59 ? -12.682 10.599 -33.649 1.00 28.34 ? 84 SER A C 1 ATOM 467 O O . SER A 1 59 ? -13.636 10.915 -34.361 1.00 27.43 ? 84 SER A O 1 ATOM 468 C CB . SER A 1 59 ? -11.761 12.049 -31.832 1.00 29.10 ? 84 SER A CB 1 ATOM 469 O OG . SER A 1 59 ? -11.928 13.093 -32.772 1.00 32.41 ? 84 SER A OG 1 ATOM 470 N N . ASN A 1 60 ? -11.596 10.006 -34.126 1.00 28.15 ? 85 ASN A N 1 ATOM 471 C CA . ASN A 1 60 ? -11.454 9.726 -35.549 1.00 27.30 ? 85 ASN A CA 1 ATOM 472 C C . ASN A 1 60 ? -12.388 8.611 -36.014 1.00 28.28 ? 85 ASN A C 1 ATOM 473 O O . ASN A 1 60 ? -12.837 8.606 -37.159 1.00 30.18 ? 85 ASN A O 1 ATOM 474 C CB . ASN A 1 60 ? -9.997 9.415 -35.892 1.00 33.16 ? 85 ASN A CB 1 ATOM 475 C CG . ASN A 1 60 ? -9.104 10.640 -35.786 1.00 37.24 ? 85 ASN A CG 1 ATOM 476 O OD1 . ASN A 1 60 ? -9.507 11.748 -36.148 1.00 45.87 ? 85 ASN A OD1 1 ATOM 477 N ND2 . ASN A 1 60 ? -7.892 10.449 -35.282 1.00 34.65 ? 85 ASN A ND2 1 ATOM 478 N N . THR A 1 61 ? -12.692 7.673 -35.125 1.00 29.12 ? 86 THR A N 1 ATOM 479 C CA . THR A 1 61 ? -13.630 6.610 -35.464 1.00 26.43 ? 86 THR A CA 1 ATOM 480 C C . THR A 1 61 ? -15.001 7.204 -35.768 1.00 27.90 ? 86 THR A C 1 ATOM 481 O O . THR A 1 61 ? -15.632 6.872 -36.772 1.00 26.36 ? 86 THR A O 1 ATOM 482 C CB . THR A 1 61 ? -13.743 5.567 -34.335 1.00 24.10 ? 86 THR A CB 1 ATOM 483 O OG1 . THR A 1 61 ? -12.517 4.831 -34.249 1.00 26.17 ? 86 THR A OG1 1 ATOM 484 C CG2 . THR A 1 61 ? -14.880 4.595 -34.618 1.00 25.60 ? 86 THR A CG2 1 ATOM 485 N N . ILE A 1 62 ? -15.454 8.097 -34.897 1.00 25.68 ? 87 ILE A N 1 ATOM 486 C CA . ILE A 1 62 ? -16.723 8.779 -35.101 1.00 27.25 ? 87 ILE A CA 1 ATOM 487 C C . ILE A 1 62 ? -16.696 9.603 -36.390 1.00 30.21 ? 87 ILE A C 1 ATOM 488 O O . ILE A 1 62 ? -17.616 9.525 -37.200 1.00 28.97 ? 87 ILE A O 1 ATOM 489 C CB . ILE A 1 62 ? -17.073 9.648 -33.883 1.00 26.78 ? 87 ILE A CB 1 ATOM 490 C CG1 . ILE A 1 62 ? -17.325 8.737 -32.679 1.00 27.69 ? 87 ILE A CG1 1 ATOM 491 C CG2 . ILE A 1 62 ? -18.285 10.526 -34.174 1.00 26.98 ? 87 ILE A CG2 1 ATOM 492 C CD1 . ILE A 1 62 ? -17.328 9.450 -31.350 1.00 25.60 ? 87 ILE A CD1 1 ATOM 493 N N . ARG A 1 63 ? -15.629 10.370 -36.585 1.00 29.18 ? 88 ARG A N 1 ATOM 494 C CA . ARG A 1 63 ? -15.499 11.188 -37.790 1.00 32.47 ? 88 ARG A CA 1 ATOM 495 C C . ARG A 1 63 ? -15.612 10.355 -39.068 1.00 37.36 ? 88 ARG A C 1 ATOM 496 O O . ARG A 1 63 ? -16.259 10.769 -40.032 1.00 34.54 ? 88 ARG A O 1 ATOM 497 C CB . ARG A 1 63 ? -14.190 11.983 -37.768 1.00 27.47 ? 88 ARG A CB 1 ATOM 498 C CG . ARG A 1 63 ? -14.148 13.052 -36.680 1.00 32.61 ? 88 ARG A CG 1 ATOM 499 C CD . ARG A 1 63 ? -12.818 13.788 -36.641 1.00 29.86 ? 88 ARG A CD 1 ATOM 500 N NE . ARG A 1 63 ? -12.561 14.515 -37.879 1.00 33.34 ? 88 ARG A NE 1 ATOM 501 C CZ . ARG A 1 63 ? -11.629 14.175 -38.762 1.00 42.82 ? 88 ARG A CZ 1 ATOM 502 N NH1 . ARG A 1 63 ? -10.850 13.124 -38.538 1.00 43.92 ? 88 ARG A NH1 1 ATOM 503 N NH2 . ARG A 1 63 ? -11.469 14.891 -39.868 1.00 42.87 ? 88 ARG A NH2 1 ATOM 504 N N . CYS A 1 64 ? -14.992 9.180 -39.071 1.00 32.00 ? 89 CYS A N 1 ATOM 505 C CA . CYS A 1 64 ? -15.032 8.304 -40.242 1.00 31.29 ? 89 CYS A CA 1 ATOM 506 C C . CYS A 1 64 ? -16.411 7.703 -40.485 1.00 34.42 ? 89 CYS A C 1 ATOM 507 O O . CYS A 1 64 ? -16.906 7.692 -41.614 1.00 31.12 ? 89 CYS A O 1 ATOM 508 C CB . CYS A 1 64 ? -13.994 7.188 -40.122 1.00 33.47 ? 89 CYS A CB 1 ATOM 509 S SG . CYS A 1 64 ? -12.309 7.735 -40.445 1.00 34.54 ? 89 CYS A SG 1 ATOM 510 N N . ILE A 1 65 ? -17.026 7.193 -39.424 1.00 28.18 ? 90 ILE A N 1 ATOM 511 C CA . ILE A 1 65 ? -18.339 6.579 -39.540 1.00 29.72 ? 90 ILE A CA 1 ATOM 512 C C . ILE A 1 65 ? -19.339 7.558 -40.146 1.00 35.25 ? 90 ILE A C 1 ATOM 513 O O . ILE A 1 65 ? -20.217 7.171 -40.917 1.00 35.70 ? 90 ILE A O 1 ATOM 514 C CB . ILE A 1 65 ? -18.843 6.080 -38.174 1.00 25.91 ? 90 ILE A CB 1 ATOM 515 C CG1 . ILE A 1 65 ? -17.982 4.904 -37.702 1.00 26.67 ? 90 ILE A CG1 1 ATOM 516 C CG2 . ILE A 1 65 ? -20.313 5.683 -38.260 1.00 28.84 ? 90 ILE A CG2 1 ATOM 517 C CD1 . ILE A 1 65 ? -18.220 4.506 -36.255 1.00 23.87 ? 90 ILE A CD1 1 ATOM 518 N N . ARG A 1 66 ? -19.185 8.834 -39.813 1.00 32.81 ? 91 ARG A N 1 ATOM 519 C CA . ARG A 1 66 ? -20.106 9.853 -40.305 1.00 39.95 ? 91 ARG A CA 1 ATOM 520 C C . ARG A 1 66 ? -19.998 10.104 -41.808 1.00 40.46 ? 91 ARG A C 1 ATOM 521 O O . ARG A 1 66 ? -20.974 10.502 -42.446 1.00 43.89 ? 91 ARG A O 1 ATOM 522 C CB . ARG A 1 66 ? -19.920 11.152 -39.532 1.00 46.55 ? 91 ARG A CB 1 ATOM 523 C CG . ARG A 1 66 ? -20.315 11.026 -38.080 1.00 44.85 ? 91 ARG A CG 1 ATOM 524 C CD . ARG A 1 66 ? -20.808 12.344 -37.558 1.00 50.43 ? 91 ARG A CD 1 ATOM 525 N NE . ARG A 1 66 ? -21.906 12.874 -38.360 1.00 38.99 ? 91 ARG A NE 1 ATOM 526 C CZ . ARG A 1 66 ? -22.372 14.112 -38.235 1.00 35.71 ? 91 ARG A CZ 1 ATOM 527 N NH1 . ARG A 1 66 ? -23.375 14.531 -38.993 1.00 35.19 ? 91 ARG A NH1 1 ATOM 528 N NH2 . ARG A 1 66 ? -21.825 14.931 -37.345 1.00 37.46 ? 91 ARG A NH2 1 ATOM 529 N N . LYS A 1 67 ? -18.817 9.874 -42.369 1.00 35.14 ? 92 LYS A N 1 ATOM 530 C CA . LYS A 1 67 ? -18.621 10.016 -43.809 1.00 38.22 ? 92 LYS A CA 1 ATOM 531 C C . LYS A 1 67 ? -19.434 8.970 -44.565 1.00 42.00 ? 92 LYS A C 1 ATOM 532 O O . LYS A 1 67 ? -19.583 9.044 -45.787 1.00 42.08 ? 92 LYS A O 1 ATOM 533 C CB . LYS A 1 67 ? -17.138 9.901 -44.165 1.00 41.59 ? 92 LYS A CB 1 ATOM 534 C CG . LYS A 1 67 ? -16.306 11.096 -43.733 1.00 46.81 ? 92 LYS A CG 1 ATOM 535 C CD . LYS A 1 67 ? -14.830 10.868 -44.007 1.00 58.57 ? 92 LYS A CD 1 ATOM 536 C CE . LYS A 1 67 ? -14.022 12.131 -43.752 1.00 67.29 ? 92 LYS A CE 1 ATOM 537 N NZ . LYS A 1 67 ? -14.230 12.658 -42.374 1.00 70.26 ? 92 LYS A NZ 1 ATOM 538 N N . GLY A 1 68 ? -19.955 7.995 -43.828 1.00 40.95 ? 93 GLY A N 1 ATOM 539 C CA . GLY A 1 68 ? -20.798 6.967 -44.407 1.00 33.89 ? 93 GLY A CA 1 ATOM 540 C C . GLY A 1 68 ? -22.239 7.081 -43.954 1.00 36.58 ? 93 GLY A C 1 ATOM 541 O O . GLY A 1 68 ? -22.649 8.091 -43.379 1.00 46.88 ? 93 GLY A O 1 ATOM 542 N N . SER A 1 69 ? -23.017 6.040 -44.219 1.00 35.96 ? 94 SER A N 1 ATOM 543 C CA . SER A 1 69 ? -24.389 5.981 -43.743 1.00 45.75 ? 94 SER A CA 1 ATOM 544 C C . SER A 1 69 ? -24.507 4.811 -42.783 1.00 50.56 ? 94 SER A C 1 ATOM 545 O O . SER A 1 69 ? -24.932 3.717 -43.155 1.00 55.02 ? 94 SER A O 1 ATOM 546 C CB . SER A 1 69 ? -25.378 5.841 -44.903 1.00 54.24 ? 94 SER A CB 1 ATOM 547 O OG . SER A 1 69 ? -25.202 4.613 -45.586 1.00 67.79 ? 94 SER A OG 1 ATOM 548 N N . TRP A 1 70 ? -24.100 5.052 -41.544 1.00 36.96 ? 95 TRP A N 1 ATOM 549 C CA . TRP A 1 70 ? -24.117 4.031 -40.513 1.00 32.70 ? 95 TRP A CA 1 ATOM 550 C C . TRP A 1 70 ? -24.805 4.567 -39.277 1.00 28.09 ? 95 TRP A C 1 ATOM 551 O O . TRP A 1 70 ? -24.773 5.766 -39.012 1.00 36.72 ? 95 TRP A O 1 ATOM 552 C CB . TRP A 1 70 ? -22.690 3.657 -40.120 1.00 33.04 ? 95 TRP A CB 1 ATOM 553 C CG . TRP A 1 70 ? -21.868 3.109 -41.222 1.00 35.46 ? 95 TRP A CG 1 ATOM 554 C CD1 . TRP A 1 70 ? -20.862 3.743 -41.891 1.00 33.47 ? 95 TRP A CD1 1 ATOM 555 C CD2 . TRP A 1 70 ? -21.967 1.801 -41.787 1.00 32.74 ? 95 TRP A CD2 1 ATOM 556 N NE1 . TRP A 1 70 ? -20.328 2.908 -42.840 1.00 40.11 ? 95 TRP A NE1 1 ATOM 557 C CE2 . TRP A 1 70 ? -20.991 1.709 -42.797 1.00 35.17 ? 95 TRP A CE2 1 ATOM 558 C CE3 . TRP A 1 70 ? -22.788 0.698 -41.538 1.00 33.16 ? 95 TRP A CE3 1 ATOM 559 C CZ2 . TRP A 1 70 ? -20.813 0.559 -43.556 1.00 32.75 ? 95 TRP A CZ2 1 ATOM 560 C CZ3 . TRP A 1 70 ? -22.612 -0.441 -42.293 1.00 38.44 ? 95 TRP A CZ3 1 ATOM 561 C CH2 . TRP A 1 70 ? -21.632 -0.503 -43.291 1.00 41.77 ? 95 TRP A CH2 1 ATOM 562 N N . THR A 1 71 ? -25.411 3.672 -38.508 1.00 24.78 ? 96 THR A N 1 ATOM 563 C CA . THR A 1 71 ? -25.856 4.023 -37.172 1.00 22.50 ? 96 THR A CA 1 ATOM 564 C C . THR A 1 71 ? -24.739 3.664 -36.205 1.00 23.50 ? 96 THR A C 1 ATOM 565 O O . THR A 1 71 ? -24.184 2.572 -36.271 1.00 25.22 ? 96 THR A O 1 ATOM 566 C CB . THR A 1 71 ? -27.139 3.277 -36.800 1.00 21.05 ? 96 THR A CB 1 ATOM 567 O OG1 . THR A 1 71 ? -28.184 3.668 -37.703 1.00 28.69 ? 96 THR A OG1 1 ATOM 568 C CG2 . THR A 1 71 ? -27.557 3.604 -35.383 1.00 22.93 ? 96 THR A CG2 1 ATOM 569 N N . ILE A 1 72 ? -24.387 4.595 -35.326 1.00 20.47 ? 97 ILE A N 1 ATOM 570 C CA . ILE A 1 72 ? -23.350 4.337 -34.335 1.00 20.24 ? 97 ILE A CA 1 ATOM 571 C C . ILE A 1 72 ? -23.924 3.605 -33.124 1.00 19.38 ? 97 ILE A C 1 ATOM 572 O O . ILE A 1 72 ? -24.981 3.969 -32.614 1.00 20.46 ? 97 ILE A O 1 ATOM 573 C CB . ILE A 1 72 ? -22.679 5.651 -33.884 1.00 18.80 ? 97 ILE A CB 1 ATOM 574 C CG1 . ILE A 1 72 ? -21.817 6.207 -35.019 1.00 24.18 ? 97 ILE A CG1 1 ATOM 575 C CG2 . ILE A 1 72 ? -21.842 5.427 -32.630 1.00 21.86 ? 97 ILE A CG2 1 ATOM 576 C CD1 . ILE A 1 72 ? -21.219 7.574 -34.741 1.00 25.31 ? 97 ILE A CD1 1 ATOM 577 N N . ARG A 1 73 ? -23.232 2.561 -32.676 1.00 18.18 ? 98 ARG A N 1 ATOM 578 C CA . ARG A 1 73 ? -23.576 1.904 -31.416 1.00 18.81 ? 98 ARG A CA 1 ATOM 579 C C . ARG A 1 73 ? -22.353 1.843 -30.516 1.00 20.05 ? 98 ARG A C 1 ATOM 580 O O . ARG A 1 73 ? -21.318 1.301 -30.909 1.00 23.99 ? 98 ARG A O 1 ATOM 581 C CB . ARG A 1 73 ? -24.123 0.496 -31.664 1.00 19.59 ? 98 ARG A CB 1 ATOM 582 C CG . ARG A 1 73 ? -25.564 0.481 -32.183 1.00 17.58 ? 98 ARG A CG 1 ATOM 583 C CD . ARG A 1 73 ? -26.504 0.855 -31.048 1.00 18.21 ? 98 ARG A CD 1 ATOM 584 N NE . ARG A 1 73 ? -27.905 0.982 -31.450 1.00 18.94 ? 98 ARG A NE 1 ATOM 585 C CZ . ARG A 1 73 ? -28.482 2.123 -31.817 1.00 18.66 ? 98 ARG A CZ 1 ATOM 586 N NH1 . ARG A 1 73 ? -27.773 3.245 -31.884 1.00 20.65 ? 98 ARG A NH1 1 ATOM 587 N NH2 . ARG A 1 73 ? -29.776 2.135 -32.133 1.00 20.86 ? 98 ARG A NH2 1 ATOM 588 N N . LEU A 1 74 ? -22.476 2.421 -29.322 1.00 16.85 ? 99 LEU A N 1 ATOM 589 C CA . LEU A 1 74 ? -21.405 2.428 -28.332 1.00 17.55 ? 99 LEU A CA 1 ATOM 590 C C . LEU A 1 74 ? -21.632 1.339 -27.300 1.00 16.97 ? 99 LEU A C 1 ATOM 591 O O . LEU A 1 74 ? -22.737 1.190 -26.781 1.00 18.44 ? 99 LEU A O 1 ATOM 592 C CB . LEU A 1 74 ? -21.366 3.781 -27.607 1.00 17.36 ? 99 LEU A CB 1 ATOM 593 C CG . LEU A 1 74 ? -21.249 5.013 -28.504 1.00 19.91 ? 99 LEU A CG 1 ATOM 594 C CD1 . LEU A 1 74 ? -21.448 6.279 -27.689 1.00 20.04 ? 99 LEU A CD1 1 ATOM 595 C CD2 . LEU A 1 74 ? -19.899 5.031 -29.190 1.00 23.96 ? 99 LEU A CD2 1 ATOM 596 N N . ARG A 1 75 ? -20.582 0.588 -26.987 1.00 17.54 ? 100 ARG A N 1 ATOM 597 C CA . ARG A 1 75 ? -20.679 -0.408 -25.924 1.00 15.75 ? 100 ARG A CA 1 ATOM 598 C C . ARG A 1 75 ? -19.521 -0.297 -24.950 1.00 15.59 ? 100 ARG A C 1 ATOM 599 O O . ARG A 1 75 ? -18.359 -0.259 -25.339 1.00 17.41 ? 100 ARG A O 1 ATOM 600 C CB . ARG A 1 75 ? -20.771 -1.826 -26.505 1.00 17.34 ? 100 ARG A CB 1 ATOM 601 C CG . ARG A 1 75 ? -21.032 -2.907 -25.452 1.00 17.58 ? 100 ARG A CG 1 ATOM 602 C CD . ARG A 1 75 ? -21.303 -4.265 -26.103 1.00 16.56 ? 100 ARG A CD 1 ATOM 603 N NE . ARG A 1 75 ? -20.111 -4.843 -26.726 1.00 19.03 ? 100 ARG A NE 1 ATOM 604 C CZ . ARG A 1 75 ? -20.116 -6.006 -27.373 1.00 21.48 ? 100 ARG A CZ 1 ATOM 605 N NH1 . ARG A 1 75 ? -18.996 -6.477 -27.905 1.00 22.14 ? 100 ARG A NH1 1 ATOM 606 N NH2 . ARG A 1 75 ? -21.246 -6.698 -27.488 1.00 19.97 ? 100 ARG A NH2 1 ATOM 607 N N . SER A 1 76 ? -19.869 -0.235 -23.667 1.00 15.16 ? 101 SER A N 1 ATOM 608 C CA A SER A 1 76 ? -18.888 -0.210 -22.593 0.68 17.12 ? 101 SER A CA 1 ATOM 609 C CA B SER A 1 76 ? -18.873 -0.227 -22.610 0.32 16.86 ? 101 SER A CA 1 ATOM 610 C C . SER A 1 76 ? -18.887 -1.579 -21.916 1.00 15.87 ? 101 SER A C 1 ATOM 611 O O . SER A 1 76 ? -18.067 -2.436 -22.227 1.00 20.01 ? 101 SER A O 1 ATOM 612 C CB A SER A 1 76 ? -19.239 0.901 -21.596 0.68 14.27 ? 101 SER A CB 1 ATOM 613 C CB B SER A 1 76 ? -19.132 0.912 -21.626 0.32 15.96 ? 101 SER A CB 1 ATOM 614 O OG A SER A 1 76 ? -18.454 0.817 -20.415 0.68 15.60 ? 101 SER A OG 1 ATOM 615 O OG B SER A 1 76 ? -18.745 2.149 -22.195 0.32 15.31 ? 101 SER A OG 1 ATOM 616 N N . GLY A 1 77 ? -19.832 -1.790 -21.005 1.00 14.81 ? 102 GLY A N 1 ATOM 617 C CA . GLY A 1 77 ? -19.946 -3.072 -20.329 1.00 15.69 ? 102 GLY A CA 1 ATOM 618 C C . GLY A 1 77 ? -20.939 -4.055 -20.942 1.00 16.60 ? 102 GLY A C 1 ATOM 619 O O . GLY A 1 77 ? -20.938 -5.238 -20.593 1.00 17.70 ? 102 GLY A O 1 ATOM 620 N N . GLY A 1 78 ? -21.800 -3.573 -21.836 1.00 15.57 ? 103 GLY A N 1 ATOM 621 C CA . GLY A 1 78 ? -22.752 -4.437 -22.518 1.00 15.09 ? 103 GLY A CA 1 ATOM 622 C C . GLY A 1 78 ? -23.924 -4.912 -21.675 1.00 16.97 ? 103 GLY A C 1 ATOM 623 O O . GLY A 1 78 ? -24.586 -5.894 -22.025 1.00 18.42 ? 103 GLY A O 1 ATOM 624 N N . HIS A 1 79 ? -24.198 -4.208 -20.578 1.00 16.06 ? 104 HIS A N 1 ATOM 625 C CA . HIS A 1 79 ? -25.262 -4.622 -19.670 1.00 15.94 ? 104 HIS A CA 1 ATOM 626 C C . HIS A 1 79 ? -26.663 -4.118 -20.009 1.00 16.86 ? 104 HIS A C 1 ATOM 627 O O . HIS A 1 79 ? -27.615 -4.451 -19.310 1.00 17.13 ? 104 HIS A O 1 ATOM 628 C CB . HIS A 1 79 ? -24.910 -4.267 -18.217 1.00 15.38 ? 104 HIS A CB 1 ATOM 629 C CG . HIS A 1 79 ? -24.186 -5.358 -17.495 1.00 17.17 ? 104 HIS A CG 1 ATOM 630 N ND1 . HIS A 1 79 ? -24.836 -6.299 -16.725 1.00 19.12 ? 104 HIS A ND1 1 ATOM 631 C CD2 . HIS A 1 79 ? -22.870 -5.672 -17.443 1.00 18.57 ? 104 HIS A CD2 1 ATOM 632 C CE1 . HIS A 1 79 ? -23.949 -7.142 -16.224 1.00 19.42 ? 104 HIS A CE1 1 ATOM 633 N NE2 . HIS A 1 79 ? -22.749 -6.785 -16.645 1.00 19.67 ? 104 HIS A NE2 1 ATOM 634 N N . SER A 1 80 ? -26.795 -3.342 -21.080 1.00 15.47 ? 105 SER A N 1 ATOM 635 C CA . SER A 1 80 ? -28.114 -2.838 -21.471 1.00 15.57 ? 105 SER A CA 1 ATOM 636 C C . SER A 1 80 ? -29.175 -3.924 -21.347 1.00 17.35 ? 105 SER A C 1 ATOM 637 O O . SER A 1 80 ? -29.053 -4.987 -21.958 1.00 17.11 ? 105 SER A O 1 ATOM 638 C CB . SER A 1 80 ? -28.105 -2.342 -22.916 1.00 15.49 ? 105 SER A CB 1 ATOM 639 O OG . SER A 1 80 ? -29.424 -1.991 -23.316 1.00 17.86 ? 105 SER A OG 1 ATOM 640 N N . TYR A 1 81 ? -30.236 -3.648 -20.594 1.00 15.92 ? 106 TYR A N 1 ATOM 641 C CA . TYR A 1 81 ? -31.284 -4.637 -20.394 1.00 16.98 ? 106 TYR A CA 1 ATOM 642 C C . TYR A 1 81 ? -31.972 -4.995 -21.709 1.00 18.19 ? 106 TYR A C 1 ATOM 643 O O . TYR A 1 81 ? -32.564 -6.068 -21.835 1.00 23.97 ? 106 TYR A O 1 ATOM 644 C CB . TYR A 1 81 ? -32.324 -4.124 -19.397 1.00 21.23 ? 106 TYR A CB 1 ATOM 645 C CG . TYR A 1 81 ? -31.836 -4.022 -17.966 1.00 21.23 ? 106 TYR A CG 1 ATOM 646 C CD1 . TYR A 1 81 ? -30.702 -4.709 -17.535 1.00 19.90 ? 106 TYR A CD1 1 ATOM 647 C CD2 . TYR A 1 81 ? -32.538 -3.273 -17.038 1.00 23.07 ? 106 TYR A CD2 1 ATOM 648 C CE1 . TYR A 1 81 ? -30.266 -4.623 -16.217 1.00 21.14 ? 106 TYR A CE1 1 ATOM 649 C CE2 . TYR A 1 81 ? -32.115 -3.188 -15.723 1.00 21.76 ? 106 TYR A CE2 1 ATOM 650 C CZ . TYR A 1 81 ? -30.980 -3.860 -15.321 1.00 24.18 ? 106 TYR A CZ 1 ATOM 651 O OH . TYR A 1 81 ? -30.567 -3.777 -14.011 1.00 27.76 ? 106 TYR A OH 1 ATOM 652 N N . GLU A 1 82 ? -31.890 -4.087 -22.680 1.00 17.05 ? 107 GLU A N 1 ATOM 653 C CA . GLU A 1 82 ? -32.568 -4.265 -23.962 1.00 17.87 ? 107 GLU A CA 1 ATOM 654 C C . GLU A 1 82 ? -31.572 -4.405 -25.110 1.00 19.41 ? 107 GLU A C 1 ATOM 655 O O . GLU A 1 82 ? -31.947 -4.297 -26.282 1.00 19.95 ? 107 GLU A O 1 ATOM 656 C CB . GLU A 1 82 ? -33.510 -3.085 -24.233 1.00 20.52 ? 107 GLU A CB 1 ATOM 657 C CG . GLU A 1 82 ? -34.653 -2.919 -23.220 1.00 22.46 ? 107 GLU A CG 1 ATOM 658 C CD . GLU A 1 82 ? -35.831 -3.855 -23.472 1.00 25.49 ? 107 GLU A CD 1 ATOM 659 O OE1 . GLU A 1 82 ? -35.660 -4.877 -24.171 1.00 25.50 ? 107 GLU A OE1 1 ATOM 660 O OE2 . GLU A 1 82 ? -36.940 -3.567 -22.963 1.00 25.63 ? 107 GLU A OE2 1 ATOM 661 N N . GLY A 1 83 ? -30.309 -4.650 -24.772 1.00 18.55 ? 108 GLY A N 1 ATOM 662 C CA . GLY A 1 83 ? -29.275 -4.891 -25.766 1.00 21.19 ? 108 GLY A CA 1 ATOM 663 C C . GLY A 1 83 ? -29.008 -3.717 -26.691 1.00 17.83 ? 108 GLY A C 1 ATOM 664 O O . GLY A 1 83 ? -28.536 -3.907 -27.814 1.00 19.56 ? 108 GLY A O 1 ATOM 665 N N . LEU A 1 84 ? -29.276 -2.501 -26.220 1.00 17.74 ? 109 LEU A N 1 ATOM 666 C CA . LEU A 1 84 ? -29.220 -1.327 -27.088 1.00 19.70 ? 109 LEU A CA 1 ATOM 667 C C . LEU A 1 84 ? -27.807 -0.854 -27.423 1.00 19.04 ? 109 LEU A C 1 ATOM 668 O O . LEU A 1 84 ? -27.632 0.045 -28.239 1.00 19.34 ? 109 LEU A O 1 ATOM 669 C CB . LEU A 1 84 ? -30.046 -0.176 -26.509 1.00 17.97 ? 109 LEU A CB 1 ATOM 670 C CG . LEU A 1 84 ? -31.538 -0.466 -26.398 1.00 23.65 ? 109 LEU A CG 1 ATOM 671 C CD1 . LEU A 1 84 ? -32.279 0.763 -25.895 1.00 26.19 ? 109 LEU A CD1 1 ATOM 672 C CD2 . LEU A 1 84 ? -32.094 -0.922 -27.740 1.00 27.55 ? 109 LEU A CD2 1 ATOM 673 N N . SER A 1 85 ? -26.800 -1.456 -26.800 1.00 16.30 ? 110 SER A N 1 ATOM 674 C CA . SER A 1 85 ? -25.422 -1.125 -27.130 1.00 16.50 ? 110 SER A CA 1 ATOM 675 C C . SER A 1 85 ? -24.860 -1.961 -28.287 1.00 17.01 ? 110 SER A C 1 ATOM 676 O O . SER A 1 85 ? -23.767 -1.676 -28.765 1.00 20.13 ? 110 SER A O 1 ATOM 677 C CB . SER A 1 85 ? -24.532 -1.278 -25.899 1.00 16.94 ? 110 SER A CB 1 ATOM 678 O OG . SER A 1 85 ? -24.757 -2.537 -25.303 1.00 17.47 ? 110 SER A OG 1 ATOM 679 N N . TYR A 1 86 ? -25.592 -2.982 -28.737 1.00 16.54 ? 111 TYR A N 1 ATOM 680 C CA . TYR A 1 86 ? -25.059 -3.875 -29.775 1.00 18.48 ? 111 TYR A CA 1 ATOM 681 C C . TYR A 1 86 ? -26.126 -4.417 -30.728 1.00 21.47 ? 111 TYR A C 1 ATOM 682 O O . TYR A 1 86 ? -25.905 -5.420 -31.412 1.00 20.84 ? 111 TYR A O 1 ATOM 683 C CB . TYR A 1 86 ? -24.257 -5.028 -29.142 1.00 21.23 ? 111 TYR A CB 1 ATOM 684 C CG . TYR A 1 86 ? -25.023 -5.761 -28.070 1.00 19.92 ? 111 TYR A CG 1 ATOM 685 C CD1 . TYR A 1 86 ? -25.844 -6.842 -28.390 1.00 21.44 ? 111 TYR A CD1 1 ATOM 686 C CD2 . TYR A 1 86 ? -24.947 -5.362 -26.737 1.00 17.42 ? 111 TYR A CD2 1 ATOM 687 C CE1 . TYR A 1 86 ? -26.568 -7.509 -27.417 1.00 19.50 ? 111 TYR A CE1 1 ATOM 688 C CE2 . TYR A 1 86 ? -25.670 -6.024 -25.752 1.00 20.62 ? 111 TYR A CE2 1 ATOM 689 C CZ . TYR A 1 86 ? -26.477 -7.098 -26.102 1.00 20.45 ? 111 TYR A CZ 1 ATOM 690 O OH . TYR A 1 86 ? -27.194 -7.759 -25.132 1.00 20.70 ? 111 TYR A OH 1 ATOM 691 N N . THR A 1 87 ? -27.277 -3.752 -30.770 1.00 18.86 ? 112 THR A N 1 ATOM 692 C CA . THR A 1 87 ? -28.329 -4.078 -31.730 1.00 18.69 ? 112 THR A CA 1 ATOM 693 C C . THR A 1 87 ? -28.875 -2.799 -32.340 1.00 18.80 ? 112 THR A C 1 ATOM 694 O O . THR A 1 87 ? -28.788 -1.728 -31.735 1.00 21.82 ? 112 THR A O 1 ATOM 695 C CB . THR A 1 87 ? -29.492 -4.867 -31.088 1.00 19.65 ? 112 THR A CB 1 ATOM 696 O OG1 . THR A 1 87 ? -30.131 -4.068 -30.081 1.00 22.89 ? 112 THR A OG1 1 ATOM 697 C CG2 . THR A 1 87 ? -28.998 -6.167 -30.474 1.00 21.65 ? 112 THR A CG2 1 ATOM 698 N N . SER A 1 88 ? -29.440 -2.929 -33.538 1.00 22.21 ? 113 SER A N 1 ATOM 699 C CA . SER A 1 88 ? -30.028 -1.805 -34.265 1.00 23.40 ? 113 SER A CA 1 ATOM 700 C C . SER A 1 88 ? -30.817 -2.329 -35.461 1.00 26.14 ? 113 SER A C 1 ATOM 701 O O . SER A 1 88 ? -30.413 -3.297 -36.104 1.00 28.01 ? 113 SER A O 1 ATOM 702 C CB . SER A 1 88 ? -28.937 -0.842 -34.741 1.00 25.88 ? 113 SER A CB 1 ATOM 703 O OG . SER A 1 88 ? -29.465 0.155 -35.606 1.00 25.20 ? 113 SER A OG 1 ATOM 704 N N . ASP A 1 89 ? -31.945 -1.689 -35.755 1.00 29.00 ? 114 ASP A N 1 ATOM 705 C CA . ASP A 1 89 ? -32.755 -2.091 -36.901 1.00 35.83 ? 114 ASP A CA 1 ATOM 706 C C . ASP A 1 89 ? -32.165 -1.581 -38.213 1.00 39.59 ? 114 ASP A C 1 ATOM 707 O O . ASP A 1 89 ? -32.520 -2.054 -39.290 1.00 48.05 ? 114 ASP A O 1 ATOM 708 C CB . ASP A 1 89 ? -34.200 -1.622 -36.733 1.00 42.50 ? 114 ASP A CB 1 ATOM 709 C CG . ASP A 1 89 ? -34.997 -2.521 -35.809 1.00 61.47 ? 114 ASP A CG 1 ATOM 710 O OD1 . ASP A 1 89 ? -34.515 -3.634 -35.501 1.00 52.42 ? 114 ASP A OD1 1 ATOM 711 O OD2 . ASP A 1 89 ? -36.106 -2.121 -35.395 1.00 74.39 ? 114 ASP A OD2 1 ATOM 712 N N . THR A 1 90 ? -31.260 -0.616 -38.111 1.00 24.82 ? 115 THR A N 1 ATOM 713 C CA . THR A 1 90 ? -30.555 -0.095 -39.271 1.00 26.16 ? 115 THR A CA 1 ATOM 714 C C . THR A 1 90 ? -29.101 -0.563 -39.229 1.00 26.51 ? 115 THR A C 1 ATOM 715 O O . THR A 1 90 ? -28.559 -0.796 -38.150 1.00 26.84 ? 115 THR A O 1 ATOM 716 C CB . THR A 1 90 ? -30.603 1.443 -39.300 1.00 26.45 ? 115 THR A CB 1 ATOM 717 O OG1 . THR A 1 90 ? -30.023 1.959 -38.096 1.00 28.59 ? 115 THR A OG1 1 ATOM 718 C CG2 . THR A 1 90 ? -32.047 1.928 -39.393 1.00 30.21 ? 115 THR A CG2 1 ATOM 719 N N . PRO A 1 91 ? -28.466 -0.714 -40.402 1.00 23.88 ? 116 PRO A N 1 ATOM 720 C CA . PRO A 1 91 ? -27.061 -1.129 -40.451 1.00 28.14 ? 116 PRO A CA 1 ATOM 721 C C . PRO A 1 91 ? -26.234 -0.286 -39.493 1.00 25.91 ? 116 PRO A C 1 ATOM 722 O O . PRO A 1 91 ? -26.370 0.939 -39.476 1.00 25.44 ? 116 PRO A O 1 ATOM 723 C CB . PRO A 1 91 ? -26.670 -0.832 -41.897 1.00 32.17 ? 116 PRO A CB 1 ATOM 724 C CG . PRO A 1 91 ? -27.941 -1.028 -42.655 1.00 28.44 ? 116 PRO A CG 1 ATOM 725 C CD . PRO A 1 91 ? -29.039 -0.540 -41.749 1.00 27.85 ? 116 PRO A CD 1 ATOM 726 N N . PHE A 1 92 ? -25.390 -0.931 -38.695 1.00 22.84 ? 117 PHE A N 1 ATOM 727 C CA . PHE A 1 92 ? -24.696 -0.205 -37.643 1.00 22.70 ? 117 PHE A CA 1 ATOM 728 C C . PHE A 1 92 ? -23.252 -0.633 -37.469 1.00 23.49 ? 117 PHE A C 1 ATOM 729 O O . PHE A 1 92 ? -22.852 -1.722 -37.887 1.00 23.97 ? 117 PHE A O 1 ATOM 730 C CB . PHE A 1 92 ? -25.466 -0.291 -36.317 1.00 22.81 ? 117 PHE A CB 1 ATOM 731 C CG . PHE A 1 92 ? -25.554 -1.681 -35.732 1.00 19.69 ? 117 PHE A CG 1 ATOM 732 C CD1 . PHE A 1 92 ? -24.827 -2.010 -34.594 1.00 20.97 ? 117 PHE A CD1 1 ATOM 733 C CD2 . PHE A 1 92 ? -26.391 -2.638 -36.282 1.00 23.29 ? 117 PHE A CD2 1 ATOM 734 C CE1 . PHE A 1 92 ? -24.919 -3.285 -34.031 1.00 21.46 ? 117 PHE A CE1 1 ATOM 735 C CE2 . PHE A 1 92 ? -26.481 -3.911 -35.730 1.00 24.57 ? 117 PHE A CE2 1 ATOM 736 C CZ . PHE A 1 92 ? -25.745 -4.230 -34.596 1.00 23.65 ? 117 PHE A CZ 1 ATOM 737 N N . ILE A 1 93 ? -22.471 0.260 -36.873 1.00 23.38 ? 118 ILE A N 1 ATOM 738 C CA . ILE A 1 93 ? -21.088 -0.009 -36.536 1.00 20.37 ? 118 ILE A CA 1 ATOM 739 C C . ILE A 1 93 ? -21.008 -0.046 -35.021 1.00 19.63 ? 118 ILE A C 1 ATOM 740 O O . ILE A 1 93 ? -21.471 0.869 -34.344 1.00 21.58 ? 118 ILE A O 1 ATOM 741 C CB . ILE A 1 93 ? -20.145 1.089 -37.079 1.00 21.48 ? 118 ILE A CB 1 ATOM 742 C CG1 . ILE A 1 93 ? -20.252 1.198 -38.603 1.00 23.83 ? 118 ILE A CG1 1 ATOM 743 C CG2 . ILE A 1 93 ? -18.703 0.811 -36.675 1.00 24.86 ? 118 ILE A CG2 1 ATOM 744 C CD1 . ILE A 1 93 ? -19.842 -0.062 -39.352 1.00 28.54 ? 118 ILE A CD1 1 ATOM 745 N N . LEU A 1 94 ? -20.446 -1.123 -34.492 1.00 19.82 ? 119 LEU A N 1 ATOM 746 C CA . LEU A 1 94 ? -20.290 -1.261 -33.054 1.00 19.01 ? 119 LEU A CA 1 ATOM 747 C C . LEU A 1 94 ? -18.927 -0.731 -32.623 1.00 19.26 ? 119 LEU A C 1 ATOM 748 O O . LEU A 1 94 ? -17.880 -1.240 -33.046 1.00 21.04 ? 119 LEU A O 1 ATOM 749 C CB . LEU A 1 94 ? -20.463 -2.721 -32.645 1.00 18.49 ? 119 LEU A CB 1 ATOM 750 C CG . LEU A 1 94 ? -20.113 -3.055 -31.195 1.00 22.09 ? 119 LEU A CG 1 ATOM 751 C CD1 . LEU A 1 94 ? -20.990 -2.248 -30.250 1.00 25.12 ? 119 LEU A CD1 1 ATOM 752 C CD2 . LEU A 1 94 ? -20.250 -4.555 -30.945 1.00 22.93 ? 119 LEU A CD2 1 ATOM 753 N N . ILE A 1 95 ? -18.948 0.315 -31.803 1.00 19.57 ? 120 ILE A N 1 ATOM 754 C CA . ILE A 1 95 ? -17.734 0.846 -31.211 1.00 18.37 ? 120 ILE A CA 1 ATOM 755 C C . ILE A 1 95 ? -17.644 0.291 -29.806 1.00 19.01 ? 120 ILE A C 1 ATOM 756 O O . ILE A 1 95 ? -18.356 0.731 -28.901 1.00 19.11 ? 120 ILE A O 1 ATOM 757 C CB . ILE A 1 95 ? -17.726 2.376 -31.169 1.00 18.89 ? 120 ILE A CB 1 ATOM 758 C CG1 . ILE A 1 95 ? -17.978 2.943 -32.567 1.00 22.14 ? 120 ILE A CG1 1 ATOM 759 C CG2 . ILE A 1 95 ? -16.388 2.883 -30.625 1.00 20.71 ? 120 ILE A CG2 1 ATOM 760 C CD1 . ILE A 1 95 ? -18.063 4.454 -32.597 1.00 22.13 ? 120 ILE A CD1 1 ATOM 761 N N . ASP A 1 96 ? -16.788 -0.709 -29.644 1.00 19.41 ? 121 ASP A N 1 ATOM 762 C CA . ASP A 1 96 ? -16.586 -1.360 -28.361 1.00 19.61 ? 121 ASP A CA 1 ATOM 763 C C . ASP A 1 96 ? -15.437 -0.690 -27.620 1.00 19.96 ? 121 ASP A C 1 ATOM 764 O O . ASP A 1 96 ? -14.329 -0.571 -28.146 1.00 21.51 ? 121 ASP A O 1 ATOM 765 C CB . ASP A 1 96 ? -16.295 -2.845 -28.587 1.00 23.47 ? 121 ASP A CB 1 ATOM 766 C CG . ASP A 1 96 ? -16.363 -3.650 -27.310 1.00 36.13 ? 121 ASP A CG 1 ATOM 767 O OD1 . ASP A 1 96 ? -15.706 -3.257 -26.328 1.00 25.03 ? 121 ASP A OD1 1 ATOM 768 O OD2 . ASP A 1 96 ? -17.072 -4.676 -27.287 1.00 45.04 ? 121 ASP A OD2 1 ATOM 769 N N . LEU A 1 97 ? -15.708 -0.262 -26.391 1.00 17.86 ? 122 LEU A N 1 ATOM 770 C CA . LEU A 1 97 ? -14.772 0.555 -25.619 1.00 17.58 ? 122 LEU A CA 1 ATOM 771 C C . LEU A 1 97 ? -13.914 -0.240 -24.632 1.00 18.83 ? 122 LEU A C 1 ATOM 772 O O . LEU A 1 97 ? -13.258 0.352 -23.771 1.00 19.63 ? 122 LEU A O 1 ATOM 773 C CB . LEU A 1 97 ? -15.551 1.641 -24.866 1.00 17.18 ? 122 LEU A CB 1 ATOM 774 C CG . LEU A 1 97 ? -16.426 2.503 -25.774 1.00 19.27 ? 122 LEU A CG 1 ATOM 775 C CD1 . LEU A 1 97 ? -17.358 3.391 -24.949 1.00 22.83 ? 122 LEU A CD1 1 ATOM 776 C CD2 . LEU A 1 97 ? -15.570 3.344 -26.719 1.00 25.91 ? 122 LEU A CD2 1 ATOM 777 N N . MET A 1 98 ? -13.893 -1.566 -24.762 1.00 20.05 ? 123 MET A N 1 ATOM 778 C CA . MET A 1 98 ? -13.187 -2.413 -23.787 1.00 21.19 ? 123 MET A CA 1 ATOM 779 C C . MET A 1 98 ? -11.704 -2.098 -23.607 1.00 24.20 ? 123 MET A C 1 ATOM 780 O O . MET A 1 98 ? -11.149 -2.356 -22.541 1.00 24.59 ? 123 MET A O 1 ATOM 781 C CB . MET A 1 98 ? -13.351 -3.898 -24.107 1.00 22.47 ? 123 MET A CB 1 ATOM 782 C CG . MET A 1 98 ? -12.805 -4.320 -25.462 1.00 24.82 ? 123 MET A CG 1 ATOM 783 S SD . MET A 1 98 ? -12.732 -6.118 -25.623 1.00 30.55 ? 123 MET A SD 1 ATOM 784 C CE . MET A 1 98 ? -13.337 -6.344 -27.293 1.00 65.02 ? 123 MET A CE 1 ATOM 785 N N . ASN A 1 99 ? -11.056 -1.562 -24.638 1.00 19.77 ? 124 ASN A N 1 ATOM 786 C CA . ASN A 1 99 ? -9.648 -1.194 -24.522 1.00 22.48 ? 124 ASN A CA 1 ATOM 787 C C . ASN A 1 99 ? -9.421 0.126 -23.797 1.00 23.12 ? 124 ASN A C 1 ATOM 788 O O . ASN A 1 99 ? -8.287 0.457 -23.432 1.00 27.15 ? 124 ASN A O 1 ATOM 789 C CB . ASN A 1 99 ? -8.987 -1.161 -25.896 1.00 24.75 ? 124 ASN A CB 1 ATOM 790 C CG . ASN A 1 99 ? -8.818 -2.540 -26.483 1.00 28.84 ? 124 ASN A CG 1 ATOM 791 O OD1 . ASN A 1 99 ? -8.886 -3.541 -25.769 1.00 31.74 ? 124 ASN A OD1 1 ATOM 792 N ND2 . ASN A 1 99 ? -8.609 -2.607 -27.792 1.00 30.05 ? 124 ASN A ND2 1 ATOM 793 N N . LEU A 1 100 ? -10.498 0.877 -23.596 1.00 19.60 ? 125 LEU A N 1 ATOM 794 C CA . LEU A 1 100 ? -10.439 2.121 -22.839 1.00 21.08 ? 125 LEU A CA 1 ATOM 795 C C . LEU A 1 100 ? -10.846 1.845 -21.396 1.00 20.23 ? 125 LEU A C 1 ATOM 796 O O . LEU A 1 100 ? -11.911 2.282 -20.941 1.00 19.23 ? 125 LEU A O 1 ATOM 797 C CB . LEU A 1 100 ? -11.361 3.167 -23.466 1.00 22.07 ? 125 LEU A CB 1 ATOM 798 C CG . LEU A 1 100 ? -11.048 3.482 -24.933 1.00 23.42 ? 125 LEU A CG 1 ATOM 799 C CD1 . LEU A 1 100 ? -12.013 4.512 -25.485 1.00 26.80 ? 125 LEU A CD1 1 ATOM 800 C CD2 . LEU A 1 100 ? -9.615 3.968 -25.065 1.00 25.09 ? 125 LEU A CD2 1 ATOM 801 N N . ASN A 1 101 ? -10.003 1.101 -20.683 1.00 20.93 ? 126 ASN A N 1 ATOM 802 C CA . ASN A 1 101 ? -10.336 0.703 -19.316 1.00 24.23 ? 126 ASN A CA 1 ATOM 803 C C . ASN A 1 101 ? -9.310 1.145 -18.285 1.00 24.29 ? 126 ASN A C 1 ATOM 804 O O . ASN A 1 101 ? -9.161 0.515 -17.237 1.00 23.99 ? 126 ASN A O 1 ATOM 805 C CB . ASN A 1 101 ? -10.596 -0.808 -19.221 1.00 28.24 ? 126 ASN A CB 1 ATOM 806 C CG . ASN A 1 101 ? -9.339 -1.636 -19.401 1.00 30.44 ? 126 ASN A CG 1 ATOM 807 O OD1 . ASN A 1 101 ? -8.350 -1.179 -19.976 1.00 27.81 ? 126 ASN A OD1 1 ATOM 808 N ND2 . ASN A 1 101 ? -9.376 -2.873 -18.911 1.00 31.92 ? 126 ASN A ND2 1 ATOM 809 N N . ARG A 1 102 ? -8.625 2.243 -18.583 1.00 21.44 ? 127 ARG A N 1 ATOM 810 C CA . ARG A 1 102 ? -7.638 2.809 -17.668 1.00 22.80 ? 127 ARG A CA 1 ATOM 811 C C . ARG A 1 102 ? -8.280 3.650 -16.575 1.00 20.66 ? 127 ARG A C 1 ATOM 812 O O . ARG A 1 102 ? -9.121 4.510 -16.840 1.00 21.95 ? 127 ARG A O 1 ATOM 813 C CB . ARG A 1 102 ? -6.637 3.669 -18.430 1.00 26.58 ? 127 ARG A CB 1 ATOM 814 C CG . ARG A 1 102 ? -5.744 2.887 -19.378 1.00 47.26 ? 127 ARG A CG 1 ATOM 815 C CD . ARG A 1 102 ? -5.016 3.820 -20.330 1.00 53.31 ? 127 ARG A CD 1 ATOM 816 N NE . ARG A 1 102 ? -4.481 3.109 -21.488 1.00 54.66 ? 127 ARG A NE 1 ATOM 817 C CZ . ARG A 1 102 ? -5.228 2.635 -22.480 1.00 54.04 ? 127 ARG A CZ 1 ATOM 818 N NH1 . ARG A 1 102 ? -6.547 2.784 -22.450 1.00 38.96 ? 127 ARG A NH1 1 ATOM 819 N NH2 . ARG A 1 102 ? -4.660 2.003 -23.498 1.00 53.08 ? 127 ARG A NH2 1 ATOM 820 N N . VAL A 1 103 ? -7.861 3.399 -15.341 1.00 19.42 ? 128 VAL A N 1 ATOM 821 C CA . VAL A 1 103 ? -8.296 4.186 -14.199 1.00 19.02 ? 128 VAL A CA 1 ATOM 822 C C . VAL A 1 103 ? -7.066 4.901 -13.665 1.00 20.34 ? 128 VAL A C 1 ATOM 823 O O . VAL A 1 103 ? -6.041 4.268 -13.405 1.00 24.24 ? 128 VAL A O 1 ATOM 824 C CB . VAL A 1 103 ? -8.899 3.305 -13.096 1.00 19.55 ? 128 VAL A CB 1 ATOM 825 C CG1 . VAL A 1 103 ? -9.244 4.152 -11.873 1.00 20.33 ? 128 VAL A CG1 1 ATOM 826 C CG2 . VAL A 1 103 ? -10.129 2.560 -13.603 1.00 21.29 ? 128 VAL A CG2 1 ATOM 827 N N . SER A 1 104 ? -7.153 6.222 -13.538 1.00 19.45 ? 129 SER A N 1 ATOM 828 C CA A SER A 1 104 ? -6.041 7.013 -13.019 0.44 19.72 ? 129 SER A CA 1 ATOM 829 C CA B SER A 1 104 ? -6.042 7.016 -13.027 0.56 19.49 ? 129 SER A CA 1 ATOM 830 C C . SER A 1 104 ? -6.450 7.714 -11.734 1.00 20.09 ? 129 SER A C 1 ATOM 831 O O . SER A 1 104 ? -7.227 8.672 -11.752 1.00 20.84 ? 129 SER A O 1 ATOM 832 C CB A SER A 1 104 ? -5.564 8.041 -14.045 0.44 20.42 ? 129 SER A CB 1 ATOM 833 C CB B SER A 1 104 ? -5.599 8.041 -14.069 0.56 20.01 ? 129 SER A CB 1 ATOM 834 O OG A SER A 1 104 ? -4.552 8.867 -13.490 0.44 23.44 ? 129 SER A OG 1 ATOM 835 O OG B SER A 1 104 ? -5.353 7.411 -15.314 0.56 24.97 ? 129 SER A OG 1 ATOM 836 N N . ILE A 1 105 ? -5.927 7.223 -10.617 1.00 17.96 ? 130 ILE A N 1 ATOM 837 C CA . ILE A 1 105 ? -6.262 7.769 -9.309 1.00 19.07 ? 130 ILE A CA 1 ATOM 838 C C . ILE A 1 105 ? -5.285 8.854 -8.900 1.00 19.19 ? 130 ILE A C 1 ATOM 839 O O . ILE A 1 105 ? -4.069 8.664 -8.970 1.00 20.68 ? 130 ILE A O 1 ATOM 840 C CB . ILE A 1 105 ? -6.265 6.665 -8.257 1.00 21.08 ? 130 ILE A CB 1 ATOM 841 C CG1 . ILE A 1 105 ? -7.397 5.681 -8.560 1.00 28.89 ? 130 ILE A CG1 1 ATOM 842 C CG2 . ILE A 1 105 ? -6.428 7.251 -6.849 1.00 20.86 ? 130 ILE A CG2 1 ATOM 843 C CD1 . ILE A 1 105 ? -7.288 4.408 -7.806 1.00 28.47 ? 130 ILE A CD1 1 ATOM 844 N N . ASP A 1 106 ? -5.818 10.002 -8.495 1.00 19.16 ? 131 ASP A N 1 ATOM 845 C CA . ASP A 1 106 ? -4.988 11.086 -7.982 1.00 20.52 ? 131 ASP A CA 1 ATOM 846 C C . ASP A 1 106 ? -5.232 11.193 -6.485 1.00 19.68 ? 131 ASP A C 1 ATOM 847 O O . ASP A 1 106 ? -6.257 11.734 -6.057 1.00 19.23 ? 131 ASP A O 1 ATOM 848 C CB . ASP A 1 106 ? -5.335 12.409 -8.677 1.00 21.14 ? 131 ASP A CB 1 ATOM 849 C CG . ASP A 1 106 ? -4.445 13.570 -8.227 1.00 26.93 ? 131 ASP A CG 1 ATOM 850 O OD1 . ASP A 1 106 ? -3.821 13.481 -7.151 1.00 25.75 ? 131 ASP A OD1 1 ATOM 851 O OD2 . ASP A 1 106 ? -4.377 14.585 -8.952 1.00 32.84 ? 131 ASP A OD2 1 ATOM 852 N N . LEU A 1 107 ? -4.302 10.659 -5.699 1.00 19.51 ? 132 LEU A N 1 ATOM 853 C CA . LEU A 1 107 ? -4.449 10.658 -4.247 1.00 17.18 ? 132 LEU A CA 1 ATOM 854 C C . LEU A 1 107 ? -4.269 12.044 -3.635 1.00 20.47 ? 132 LEU A C 1 ATOM 855 O O . LEU A 1 107 ? -4.717 12.283 -2.516 1.00 22.98 ? 132 LEU A O 1 ATOM 856 C CB . LEU A 1 107 ? -3.483 9.672 -3.592 1.00 18.90 ? 132 LEU A CB 1 ATOM 857 C CG . LEU A 1 107 ? -3.790 8.199 -3.867 1.00 18.39 ? 132 LEU A CG 1 ATOM 858 C CD1 . LEU A 1 107 ? -2.660 7.325 -3.343 1.00 24.22 ? 132 LEU A CD1 1 ATOM 859 C CD2 . LEU A 1 107 ? -5.129 7.803 -3.252 1.00 20.58 ? 132 LEU A CD2 1 ATOM 860 N N . GLU A 1 108 ? -3.626 12.954 -4.364 1.00 18.98 ? 133 GLU A N 1 ATOM 861 C CA . GLU A 1 108 ? -3.428 14.313 -3.851 1.00 20.42 ? 133 GLU A CA 1 ATOM 862 C C . GLU A 1 108 ? -4.703 15.152 -3.911 1.00 19.57 ? 133 GLU A C 1 ATOM 863 O O . GLU A 1 108 ? -4.928 16.011 -3.053 1.00 21.26 ? 133 GLU A O 1 ATOM 864 C CB . GLU A 1 108 ? -2.285 15.017 -4.583 1.00 21.26 ? 133 GLU A CB 1 ATOM 865 C CG . GLU A 1 108 ? -0.954 14.292 -4.452 1.00 26.71 ? 133 GLU A CG 1 ATOM 866 C CD . GLU A 1 108 ? -0.711 13.780 -3.047 1.00 54.74 ? 133 GLU A CD 1 ATOM 867 O OE1 . GLU A 1 108 ? -0.797 12.550 -2.837 1.00 61.91 ? 133 GLU A OE1 1 ATOM 868 O OE2 . GLU A 1 108 ? -0.447 14.607 -2.149 1.00 65.20 ? 133 GLU A OE2 1 ATOM 869 N N . SER A 1 109 ? -5.535 14.904 -4.915 1.00 17.10 ? 134 SER A N 1 ATOM 870 C CA . SER A 1 109 ? -6.822 15.579 -5.004 1.00 18.03 ? 134 SER A CA 1 ATOM 871 C C . SER A 1 109 ? -7.986 14.691 -4.573 1.00 17.72 ? 134 SER A C 1 ATOM 872 O O . SER A 1 109 ? -9.110 15.169 -4.401 1.00 19.36 ? 134 SER A O 1 ATOM 873 C CB . SER A 1 109 ? -7.060 16.077 -6.429 1.00 21.02 ? 134 SER A CB 1 ATOM 874 O OG . SER A 1 109 ? -7.022 14.992 -7.338 1.00 23.54 ? 134 SER A OG 1 ATOM 875 N N . GLU A 1 110 ? -7.715 13.396 -4.405 1.00 17.87 ? 135 GLU A N 1 ATOM 876 C CA . GLU A 1 110 ? -8.764 12.410 -4.134 1.00 17.93 ? 135 GLU A CA 1 ATOM 877 C C . GLU A 1 110 ? -9.868 12.470 -5.197 1.00 16.93 ? 135 GLU A C 1 ATOM 878 O O . GLU A 1 110 ? -11.067 12.594 -4.909 1.00 18.16 ? 135 GLU A O 1 ATOM 879 C CB . GLU A 1 110 ? -9.264 12.512 -2.682 1.00 20.01 ? 135 GLU A CB 1 ATOM 880 C CG . GLU A 1 110 ? -8.148 12.136 -1.708 1.00 19.35 ? 135 GLU A CG 1 ATOM 881 C CD . GLU A 1 110 ? -8.531 12.181 -0.240 1.00 18.30 ? 135 GLU A CD 1 ATOM 882 O OE1 . GLU A 1 110 ? -9.556 12.799 0.109 1.00 22.37 ? 135 GLU A OE1 1 ATOM 883 O OE2 . GLU A 1 110 ? -7.768 11.597 0.563 1.00 23.89 ? 135 GLU A OE2 1 ATOM 884 N N . THR A 1 111 ? -9.414 12.389 -6.444 1.00 17.40 ? 136 THR A N 1 ATOM 885 C CA . THR A 1 111 ? -10.280 12.267 -7.609 1.00 18.79 ? 136 THR A CA 1 ATOM 886 C C . THR A 1 111 ? -9.707 11.153 -8.476 1.00 20.72 ? 136 THR A C 1 ATOM 887 O O . THR A 1 111 ? -8.597 10.678 -8.228 1.00 19.31 ? 136 THR A O 1 ATOM 888 C CB . THR A 1 111 ? -10.293 13.567 -8.441 1.00 16.13 ? 136 THR A CB 1 ATOM 889 O OG1 . THR A 1 111 ? -8.948 13.902 -8.819 1.00 19.02 ? 136 THR A OG1 1 ATOM 890 C CG2 . THR A 1 111 ? -10.897 14.715 -7.640 1.00 18.80 ? 136 THR A CG2 1 ATOM 891 N N . ALA A 1 112 ? -10.454 10.738 -9.493 1.00 17.65 ? 137 ALA A N 1 ATOM 892 C CA . ALA A 1 112 ? -9.943 9.769 -10.457 1.00 17.34 ? 137 ALA A CA 1 ATOM 893 C C . ALA A 1 112 ? -10.487 10.088 -11.829 1.00 17.45 ? 137 ALA A C 1 ATOM 894 O O . ALA A 1 112 ? -11.629 10.520 -11.964 1.00 19.02 ? 137 ALA A O 1 ATOM 895 C CB . ALA A 1 112 ? -10.342 8.352 -10.062 1.00 20.40 ? 137 ALA A CB 1 ATOM 896 N N . TRP A 1 113 ? -9.661 9.884 -12.846 1.00 17.24 ? 138 TRP A N 1 ATOM 897 C CA . TRP A 1 113 ? -10.133 9.863 -14.226 1.00 17.18 ? 138 TRP A CA 1 ATOM 898 C C . TRP A 1 113 ? -10.339 8.408 -14.623 1.00 17.90 ? 138 TRP A C 1 ATOM 899 O O . TRP A 1 113 ? -9.440 7.577 -14.469 1.00 21.06 ? 138 TRP A O 1 ATOM 900 C CB . TRP A 1 113 ? -9.129 10.524 -15.161 1.00 18.77 ? 138 TRP A CB 1 ATOM 901 C CG . TRP A 1 113 ? -9.270 12.012 -15.275 1.00 16.91 ? 138 TRP A CG 1 ATOM 902 C CD1 . TRP A 1 113 ? -8.472 12.958 -14.695 1.00 19.12 ? 138 TRP A CD1 1 ATOM 903 C CD2 . TRP A 1 113 ? -10.252 12.732 -16.038 1.00 17.67 ? 138 TRP A CD2 1 ATOM 904 N NE1 . TRP A 1 113 ? -8.898 14.217 -15.043 1.00 20.42 ? 138 TRP A NE1 1 ATOM 905 C CE2 . TRP A 1 113 ? -9.987 14.108 -15.868 1.00 18.87 ? 138 TRP A CE2 1 ATOM 906 C CE3 . TRP A 1 113 ? -11.328 12.346 -16.848 1.00 20.09 ? 138 TRP A CE3 1 ATOM 907 C CZ2 . TRP A 1 113 ? -10.761 15.101 -16.474 1.00 21.59 ? 138 TRP A CZ2 1 ATOM 908 C CZ3 . TRP A 1 113 ? -12.094 13.329 -17.450 1.00 20.14 ? 138 TRP A CZ3 1 ATOM 909 C CH2 . TRP A 1 113 ? -11.808 14.693 -17.262 1.00 21.58 ? 138 TRP A CH2 1 ATOM 910 N N . VAL A 1 114 ? -11.528 8.110 -15.133 1.00 16.48 ? 139 VAL A N 1 ATOM 911 C CA . VAL A 1 114 ? -11.939 6.743 -15.408 1.00 17.92 ? 139 VAL A CA 1 ATOM 912 C C . VAL A 1 114 ? -12.363 6.628 -16.863 1.00 17.48 ? 139 VAL A C 1 ATOM 913 O O . VAL A 1 114 ? -13.399 7.165 -17.250 1.00 17.02 ? 139 VAL A O 1 ATOM 914 C CB . VAL A 1 114 ? -13.133 6.350 -14.511 1.00 18.96 ? 139 VAL A CB 1 ATOM 915 C CG1 . VAL A 1 114 ? -13.513 4.896 -14.725 1.00 19.17 ? 139 VAL A CG1 1 ATOM 916 C CG2 . VAL A 1 114 ? -12.801 6.603 -13.041 1.00 19.64 ? 139 VAL A CG2 1 ATOM 917 N N . GLU A 1 115 ? -11.558 5.961 -17.685 1.00 18.41 ? 140 GLU A N 1 ATOM 918 C CA . GLU A 1 115 ? -11.967 5.724 -19.070 1.00 18.01 ? 140 GLU A CA 1 ATOM 919 C C . GLU A 1 115 ? -13.274 4.938 -19.081 1.00 18.09 ? 140 GLU A C 1 ATOM 920 O O . GLU A 1 115 ? -13.509 4.079 -18.230 1.00 17.40 ? 140 GLU A O 1 ATOM 921 C CB . GLU A 1 115 ? -10.878 4.995 -19.858 1.00 18.25 ? 140 GLU A CB 1 ATOM 922 C CG . GLU A 1 115 ? -9.678 5.879 -20.191 1.00 19.69 ? 140 GLU A CG 1 ATOM 923 C CD . GLU A 1 115 ? -8.637 5.169 -21.043 1.00 20.26 ? 140 GLU A CD 1 ATOM 924 O OE1 . GLU A 1 115 ? -8.548 3.920 -20.982 1.00 22.44 ? 140 GLU A OE1 1 ATOM 925 O OE2 . GLU A 1 115 ? -7.916 5.869 -21.782 1.00 26.97 ? 140 GLU A OE2 1 ATOM 926 N N . SER A 1 116 ? -14.124 5.240 -20.054 1.00 16.76 ? 141 SER A N 1 ATOM 927 C CA . SER A 1 116 ? -15.514 4.779 -20.037 1.00 18.47 ? 141 SER A CA 1 ATOM 928 C C . SER A 1 116 ? -15.723 3.295 -20.329 1.00 18.52 ? 141 SER A C 1 ATOM 929 O O . SER A 1 116 ? -16.833 2.791 -20.160 1.00 18.71 ? 141 SER A O 1 ATOM 930 C CB . SER A 1 116 ? -16.343 5.600 -21.021 1.00 19.60 ? 141 SER A CB 1 ATOM 931 O OG . SER A 1 116 ? -15.856 5.399 -22.338 1.00 18.14 ? 141 SER A OG 1 ATOM 932 N N . GLY A 1 117 ? -14.680 2.598 -20.775 1.00 17.11 ? 142 GLY A N 1 ATOM 933 C CA . GLY A 1 117 ? -14.757 1.158 -20.925 1.00 16.63 ? 142 GLY A CA 1 ATOM 934 C C . GLY A 1 117 ? -14.501 0.417 -19.618 1.00 17.36 ? 142 GLY A C 1 ATOM 935 O O . GLY A 1 117 ? -14.713 -0.791 -19.533 1.00 19.87 ? 142 GLY A O 1 ATOM 936 N N . SER A 1 118 ? -14.042 1.140 -18.596 1.00 18.44 ? 143 SER A N 1 ATOM 937 C CA . SER A 1 118 ? -13.795 0.538 -17.287 1.00 17.49 ? 143 SER A CA 1 ATOM 938 C C . SER A 1 118 ? -15.092 0.034 -16.670 1.00 17.50 ? 143 SER A C 1 ATOM 939 O O . SER A 1 118 ? -16.112 0.730 -16.708 1.00 19.23 ? 143 SER A O 1 ATOM 940 C CB . SER A 1 118 ? -13.177 1.561 -16.325 1.00 18.47 ? 143 SER A CB 1 ATOM 941 O OG . SER A 1 118 ? -12.010 2.173 -16.858 1.00 20.28 ? 143 SER A OG 1 ATOM 942 N N . THR A 1 119 ? -15.062 -1.159 -16.083 1.00 17.07 ? 144 THR A N 1 ATOM 943 C CA . THR A 1 119 ? -16.228 -1.658 -15.348 1.00 16.10 ? 144 THR A CA 1 ATOM 944 C C . THR A 1 119 ? -16.233 -1.122 -13.919 1.00 16.77 ? 144 THR A C 1 ATOM 945 O O . THR A 1 119 ? -15.215 -0.607 -13.438 1.00 17.13 ? 144 THR A O 1 ATOM 946 C CB . THR A 1 119 ? -16.242 -3.186 -15.263 1.00 16.56 ? 144 THR A CB 1 ATOM 947 O OG1 . THR A 1 119 ? -15.096 -3.630 -14.526 1.00 17.81 ? 144 THR A OG1 1 ATOM 948 C CG2 . THR A 1 119 ? -16.225 -3.802 -16.660 1.00 17.87 ? 144 THR A CG2 1 ATOM 949 N N . LEU A 1 120 ? -17.376 -1.245 -13.246 1.00 15.58 ? 145 LEU A N 1 ATOM 950 C CA . LEU A 1 120 ? -17.464 -0.887 -11.831 1.00 15.77 ? 145 LEU A CA 1 ATOM 951 C C . LEU A 1 120 ? -16.439 -1.665 -11.010 1.00 15.28 ? 145 LEU A C 1 ATOM 952 O O . LEU A 1 120 ? -15.767 -1.087 -10.147 1.00 16.24 ? 145 LEU A O 1 ATOM 953 C CB . LEU A 1 120 ? -18.871 -1.133 -11.276 1.00 16.39 ? 145 LEU A CB 1 ATOM 954 C CG . LEU A 1 120 ? -20.015 -0.393 -11.989 1.00 17.40 ? 145 LEU A CG 1 ATOM 955 C CD1 . LEU A 1 120 ? -21.338 -0.565 -11.238 1.00 16.95 ? 145 LEU A CD1 1 ATOM 956 C CD2 . LEU A 1 120 ? -19.684 1.083 -12.169 1.00 18.68 ? 145 LEU A CD2 1 ATOM 957 N N . GLY A 1 121 ? -16.319 -2.964 -11.273 1.00 15.69 ? 146 GLY A N 1 ATOM 958 C CA . GLY A 1 121 ? -15.365 -3.792 -10.553 1.00 15.90 ? 146 GLY A CA 1 ATOM 959 C C . GLY A 1 121 ? -13.941 -3.302 -10.733 1.00 17.05 ? 146 GLY A C 1 ATOM 960 O O . GLY A 1 121 ? -13.178 -3.214 -9.775 1.00 16.97 ? 146 GLY A O 1 ATOM 961 N N . GLU A 1 122 ? -13.571 -2.992 -11.971 1.00 17.21 ? 147 GLU A N 1 ATOM 962 C CA . GLU A 1 122 ? -12.223 -2.483 -12.247 1.00 17.63 ? 147 GLU A CA 1 ATOM 963 C C . GLU A 1 122 ? -11.964 -1.181 -11.486 1.00 17.59 ? 147 GLU A C 1 ATOM 964 O O . GLU A 1 122 ? -10.886 -0.972 -10.918 1.00 18.43 ? 147 GLU A O 1 ATOM 965 C CB . GLU A 1 122 ? -12.021 -2.272 -13.754 1.00 16.81 ? 147 GLU A CB 1 ATOM 966 C CG . GLU A 1 122 ? -11.850 -3.568 -14.550 1.00 17.21 ? 147 GLU A CG 1 ATOM 967 C CD . GLU A 1 122 ? -11.917 -3.351 -16.053 1.00 19.59 ? 147 GLU A CD 1 ATOM 968 O OE1 . GLU A 1 122 ? -12.448 -2.317 -16.495 1.00 21.30 ? 147 GLU A OE1 1 ATOM 969 O OE2 . GLU A 1 122 ? -11.444 -4.230 -16.801 1.00 22.64 ? 147 GLU A OE2 1 ATOM 970 N N . LEU A 1 123 ? -12.964 -0.306 -11.475 1.00 17.65 ? 148 LEU A N 1 ATOM 971 C CA . LEU A 1 123 ? -12.880 0.946 -10.730 1.00 16.14 ? 148 LEU A CA 1 ATOM 972 C C . LEU A 1 123 ? -12.722 0.708 -9.224 1.00 16.35 ? 148 LEU A C 1 ATOM 973 O O . LEU A 1 123 ? -11.833 1.277 -8.588 1.00 17.33 ? 148 LEU A O 1 ATOM 974 C CB . LEU A 1 123 ? -14.124 1.799 -11.001 1.00 17.55 ? 148 LEU A CB 1 ATOM 975 C CG . LEU A 1 123 ? -14.225 3.092 -10.185 1.00 16.22 ? 148 LEU A CG 1 ATOM 976 C CD1 . LEU A 1 123 ? -12.994 3.983 -10.372 1.00 20.53 ? 148 LEU A CD1 1 ATOM 977 C CD2 . LEU A 1 123 ? -15.499 3.852 -10.541 1.00 20.08 ? 148 LEU A CD2 1 ATOM 978 N N . TYR A 1 124 ? -13.591 -0.128 -8.659 1.00 15.51 ? 149 TYR A N 1 ATOM 979 C CA . TYR A 1 124 ? -13.533 -0.429 -7.231 1.00 16.31 ? 149 TYR A CA 1 ATOM 980 C C . TYR A 1 124 ? -12.171 -1.039 -6.857 1.00 18.18 ? 149 TYR A C 1 ATOM 981 O O . TYR A 1 124 ? -11.576 -0.700 -5.825 1.00 18.40 ? 149 TYR A O 1 ATOM 982 C CB . TYR A 1 124 ? -14.655 -1.392 -6.837 1.00 16.70 ? 149 TYR A CB 1 ATOM 983 C CG . TYR A 1 124 ? -16.078 -0.878 -7.013 1.00 16.93 ? 149 TYR A CG 1 ATOM 984 C CD1 . TYR A 1 124 ? -16.375 0.480 -6.951 1.00 17.51 ? 149 TYR A CD1 1 ATOM 985 C CD2 . TYR A 1 124 ? -17.132 -1.770 -7.208 1.00 17.01 ? 149 TYR A CD2 1 ATOM 986 C CE1 . TYR A 1 124 ? -17.690 0.937 -7.097 1.00 17.52 ? 149 TYR A CE1 1 ATOM 987 C CE2 . TYR A 1 124 ? -18.438 -1.325 -7.361 1.00 16.21 ? 149 TYR A CE2 1 ATOM 988 C CZ . TYR A 1 124 ? -18.711 0.026 -7.305 1.00 17.47 ? 149 TYR A CZ 1 ATOM 989 O OH . TYR A 1 124 ? -20.014 0.451 -7.445 1.00 19.85 ? 149 TYR A OH 1 ATOM 990 N N . TYR A 1 125 ? -11.685 -1.951 -7.696 1.00 17.30 ? 150 TYR A N 1 ATOM 991 C CA . TYR A 1 125 ? -10.402 -2.596 -7.454 1.00 17.56 ? 150 TYR A CA 1 ATOM 992 C C . TYR A 1 125 ? -9.283 -1.561 -7.439 1.00 17.47 ? 150 TYR A C 1 ATOM 993 O O . TYR A 1 125 ? -8.446 -1.562 -6.544 1.00 17.76 ? 150 TYR A O 1 ATOM 994 C CB . TYR A 1 125 ? -10.131 -3.657 -8.525 1.00 17.36 ? 150 TYR A CB 1 ATOM 995 C CG . TYR A 1 125 ? -8.810 -4.370 -8.352 1.00 17.81 ? 150 TYR A CG 1 ATOM 996 C CD1 . TYR A 1 125 ? -8.683 -5.446 -7.480 1.00 20.24 ? 150 TYR A CD1 1 ATOM 997 C CD2 . TYR A 1 125 ? -7.684 -3.966 -9.059 1.00 20.74 ? 150 TYR A CD2 1 ATOM 998 C CE1 . TYR A 1 125 ? -7.470 -6.103 -7.320 1.00 22.30 ? 150 TYR A CE1 1 ATOM 999 C CE2 . TYR A 1 125 ? -6.472 -4.619 -8.914 1.00 22.57 ? 150 TYR A CE2 1 ATOM 1000 C CZ . TYR A 1 125 ? -6.369 -5.683 -8.038 1.00 22.67 ? 150 TYR A CZ 1 ATOM 1001 O OH . TYR A 1 125 ? -5.167 -6.339 -7.880 1.00 25.40 ? 150 TYR A OH 1 ATOM 1002 N N . ALA A 1 126 ? -9.282 -0.675 -8.431 1.00 18.03 ? 151 ALA A N 1 ATOM 1003 C CA . ALA A 1 126 ? -8.253 0.353 -8.523 1.00 17.40 ? 151 ALA A CA 1 ATOM 1004 C C . ALA A 1 126 ? -8.258 1.264 -7.291 1.00 15.65 ? 151 ALA A C 1 ATOM 1005 O O . ALA A 1 126 ? -7.195 1.612 -6.763 1.00 18.06 ? 151 ALA A O 1 ATOM 1006 C CB . ALA A 1 126 ? -8.430 1.171 -9.807 1.00 18.48 ? 151 ALA A CB 1 ATOM 1007 N N . ILE A 1 127 ? -9.447 1.650 -6.835 1.00 15.87 ? 152 ILE A N 1 ATOM 1008 C CA . ILE A 1 127 ? -9.554 2.510 -5.658 1.00 16.51 ? 152 ILE A CA 1 ATOM 1009 C C . ILE A 1 127 ? -9.012 1.803 -4.419 1.00 19.08 ? 152 ILE A C 1 ATOM 1010 O O . ILE A 1 127 ? -8.183 2.350 -3.686 1.00 18.41 ? 152 ILE A O 1 ATOM 1011 C CB . ILE A 1 127 ? -11.011 2.949 -5.410 1.00 14.98 ? 152 ILE A CB 1 ATOM 1012 C CG1 . ILE A 1 127 ? -11.497 3.847 -6.554 1.00 16.53 ? 152 ILE A CG1 1 ATOM 1013 C CG2 . ILE A 1 127 ? -11.126 3.663 -4.070 1.00 17.53 ? 152 ILE A CG2 1 ATOM 1014 C CD1 . ILE A 1 127 ? -12.995 4.073 -6.569 1.00 17.06 ? 152 ILE A CD1 1 ATOM 1015 N N . THR A 1 128 ? -9.461 0.575 -4.193 1.00 18.89 ? 153 THR A N 1 ATOM 1016 C CA A THR A 1 128 ? -9.029 -0.237 -3.054 0.43 19.99 ? 153 THR A CA 1 ATOM 1017 C CA B THR A 1 128 ? -9.023 -0.135 -3.002 0.57 18.91 ? 153 THR A CA 1 ATOM 1018 C C . THR A 1 128 ? -7.515 -0.426 -3.014 1.00 21.64 ? 153 THR A C 1 ATOM 1019 O O . THR A 1 128 ? -6.886 -0.441 -1.951 1.00 22.30 ? 153 THR A O 1 ATOM 1020 C CB A THR A 1 128 ? -9.683 -1.633 -3.119 0.43 16.84 ? 153 THR A CB 1 ATOM 1021 C CB B THR A 1 128 ? -9.859 -1.406 -2.749 0.57 19.79 ? 153 THR A CB 1 ATOM 1022 O OG1 A THR A 1 128 ? -11.107 -1.497 -3.044 0.43 19.76 ? 153 THR A OG1 1 ATOM 1023 O OG1 B THR A 1 128 ? -9.589 -1.900 -1.431 0.57 22.29 ? 153 THR A OG1 1 ATOM 1024 C CG2 A THR A 1 128 ? -9.189 -2.521 -1.982 0.43 20.31 ? 153 THR A CG2 1 ATOM 1025 C CG2 B THR A 1 128 ? -9.542 -2.472 -3.780 0.57 18.81 ? 153 THR A CG2 1 ATOM 1026 N N . GLU A 1 129 ? -6.925 -0.610 -4.192 1.00 19.46 ? 154 GLU A N 1 ATOM 1027 C CA . GLU A 1 129 ? -5.478 -0.787 -4.287 1.00 21.39 ? 154 GLU A CA 1 ATOM 1028 C C . GLU A 1 129 ? -4.725 0.486 -3.888 1.00 23.39 ? 154 GLU A C 1 ATOM 1029 O O . GLU A 1 129 ? -3.630 0.416 -3.331 1.00 26.51 ? 154 GLU A O 1 ATOM 1030 C CB . GLU A 1 129 ? -5.081 -1.208 -5.702 1.00 23.38 ? 154 GLU A CB 1 ATOM 1031 C CG . GLU A 1 129 ? -5.344 -2.677 -6.001 1.00 30.90 ? 154 GLU A CG 1 ATOM 1032 C CD . GLU A 1 129 ? -4.377 -3.591 -5.274 1.00 43.90 ? 154 GLU A CD 1 ATOM 1033 O OE1 . GLU A 1 129 ? -3.164 -3.534 -5.570 1.00 47.71 ? 154 GLU A OE1 1 ATOM 1034 O OE2 . GLU A 1 129 ? -4.828 -4.366 -4.406 1.00 42.08 ? 154 GLU A OE2 1 ATOM 1035 N N . SER A 1 130 ? -5.325 1.642 -4.160 1.00 18.02 ? 155 SER A N 1 ATOM 1036 C CA . SER A 1 130 ? -4.671 2.930 -3.926 1.00 17.48 ? 155 SER A CA 1 ATOM 1037 C C . SER A 1 130 ? -4.789 3.414 -2.487 1.00 21.66 ? 155 SER A C 1 ATOM 1038 O O . SER A 1 130 ? -3.919 4.135 -1.996 1.00 21.46 ? 155 SER A O 1 ATOM 1039 C CB . SER A 1 130 ? -5.244 4.006 -4.853 1.00 20.86 ? 155 SER A CB 1 ATOM 1040 O OG . SER A 1 130 ? -6.517 4.443 -4.402 1.00 25.24 ? 155 SER A OG 1 ATOM 1041 N N . SER A 1 131 ? -5.873 3.037 -1.815 1.00 21.11 ? 156 SER A N 1 ATOM 1042 C CA . SER A 1 131 ? -6.162 3.601 -0.506 1.00 18.06 ? 156 SER A CA 1 ATOM 1043 C C . SER A 1 131 ? -7.142 2.747 0.280 1.00 18.79 ? 156 SER A C 1 ATOM 1044 O O . SER A 1 131 ? -8.042 2.131 -0.293 1.00 23.65 ? 156 SER A O 1 ATOM 1045 C CB . SER A 1 131 ? -6.752 5.002 -0.662 1.00 22.65 ? 156 SER A CB 1 ATOM 1046 O OG . SER A 1 131 ? -7.194 5.493 0.592 1.00 23.09 ? 156 SER A OG 1 ATOM 1047 N N . SER A 1 132 ? -6.970 2.744 1.598 1.00 20.86 ? 157 SER A N 1 ATOM 1048 C CA . SER A 1 132 ? -7.866 2.030 2.495 1.00 23.75 ? 157 SER A CA 1 ATOM 1049 C C . SER A 1 132 ? -8.969 2.936 3.040 1.00 18.97 ? 157 SER A C 1 ATOM 1050 O O . SER A 1 132 ? -9.838 2.476 3.781 1.00 21.66 ? 157 SER A O 1 ATOM 1051 C CB . SER A 1 132 ? -7.075 1.435 3.662 1.00 25.89 ? 157 SER A CB 1 ATOM 1052 O OG . SER A 1 132 ? -6.404 2.449 4.385 1.00 29.20 ? 157 SER A OG 1 ATOM 1053 N N . LYS A 1 133 ? -8.938 4.217 2.674 1.00 17.19 ? 158 LYS A N 1 ATOM 1054 C CA . LYS A 1 133 ? -9.878 5.193 3.228 1.00 19.76 ? 158 LYS A CA 1 ATOM 1055 C C . LYS A 1 133 ? -10.710 5.914 2.169 1.00 17.25 ? 158 LYS A C 1 ATOM 1056 O O . LYS A 1 133 ? -11.358 6.927 2.462 1.00 18.69 ? 158 LYS A O 1 ATOM 1057 C CB . LYS A 1 133 ? -9.146 6.235 4.080 1.00 21.86 ? 158 LYS A CB 1 ATOM 1058 C CG . LYS A 1 133 ? -8.514 5.693 5.348 1.00 28.22 ? 158 LYS A CG 1 ATOM 1059 C CD . LYS A 1 133 ? -7.854 6.818 6.137 1.00 34.24 ? 158 LYS A CD 1 ATOM 1060 C CE . LYS A 1 133 ? -7.221 6.296 7.420 1.00 47.69 ? 158 LYS A CE 1 ATOM 1061 N NZ . LYS A 1 133 ? -6.626 7.394 8.236 1.00 54.73 ? 158 LYS A NZ 1 ATOM 1062 N N . LEU A 1 134 ? -10.695 5.391 0.947 1.00 16.52 ? 159 LEU A N 1 ATOM 1063 C CA . LEU A 1 134 ? -11.469 5.974 -0.145 1.00 16.13 ? 159 LEU A CA 1 ATOM 1064 C C . LEU A 1 134 ? -12.330 4.921 -0.822 1.00 16.47 ? 159 LEU A C 1 ATOM 1065 O O . LEU A 1 134 ? -11.937 3.754 -0.928 1.00 17.31 ? 159 LEU A O 1 ATOM 1066 C CB . LEU A 1 134 ? -10.543 6.604 -1.187 1.00 16.08 ? 159 LEU A CB 1 ATOM 1067 C CG . LEU A 1 134 ? -9.732 7.815 -0.713 1.00 17.45 ? 159 LEU A CG 1 ATOM 1068 C CD1 . LEU A 1 134 ? -8.662 8.169 -1.743 1.00 20.40 ? 159 LEU A CD1 1 ATOM 1069 C CD2 . LEU A 1 134 ? -10.639 9.009 -0.456 1.00 19.12 ? 159 LEU A CD2 1 ATOM 1070 N N . GLY A 1 135 ? -13.497 5.351 -1.289 1.00 15.15 ? 160 GLY A N 1 ATOM 1071 C CA . GLY A 1 135 ? -14.400 4.489 -2.034 1.00 16.46 ? 160 GLY A CA 1 ATOM 1072 C C . GLY A 1 135 ? -15.163 5.298 -3.061 1.00 15.12 ? 160 GLY A C 1 ATOM 1073 O O . GLY A 1 135 ? -14.839 6.459 -3.315 1.00 15.46 ? 160 GLY A O 1 ATOM 1074 N N . PHE A 1 136 ? -16.174 4.688 -3.666 1.00 17.10 ? 161 PHE A N 1 ATOM 1075 C CA . PHE A 1 136 ? -17.018 5.403 -4.611 1.00 16.65 ? 161 PHE A CA 1 ATOM 1076 C C . PHE A 1 136 ? -18.406 4.791 -4.639 1.00 16.02 ? 161 PHE A C 1 ATOM 1077 O O . PHE A 1 136 ? -18.569 3.580 -4.454 1.00 19.67 ? 161 PHE A O 1 ATOM 1078 C CB . PHE A 1 136 ? -16.415 5.406 -6.020 1.00 17.64 ? 161 PHE A CB 1 ATOM 1079 C CG . PHE A 1 136 ? -17.110 6.344 -6.956 1.00 16.06 ? 161 PHE A CG 1 ATOM 1080 C CD1 . PHE A 1 136 ? -17.055 7.716 -6.744 1.00 15.87 ? 161 PHE A CD1 1 ATOM 1081 C CD2 . PHE A 1 136 ? -17.853 5.865 -8.024 1.00 16.83 ? 161 PHE A CD2 1 ATOM 1082 C CE1 . PHE A 1 136 ? -17.707 8.597 -7.596 1.00 16.73 ? 161 PHE A CE1 1 ATOM 1083 C CE2 . PHE A 1 136 ? -18.511 6.748 -8.881 1.00 16.69 ? 161 PHE A CE2 1 ATOM 1084 C CZ . PHE A 1 136 ? -18.437 8.114 -8.659 1.00 17.05 ? 161 PHE A CZ 1 ATOM 1085 N N . THR A 1 137 ? -19.406 5.637 -4.873 1.00 16.07 ? 162 THR A N 1 ATOM 1086 C CA . THR A 1 137 ? -20.785 5.183 -4.889 1.00 18.55 ? 162 THR A CA 1 ATOM 1087 C C . THR A 1 137 ? -21.218 4.859 -6.309 1.00 15.88 ? 162 THR A C 1 ATOM 1088 O O . THR A 1 137 ? -21.305 5.730 -7.165 1.00 16.34 ? 162 THR A O 1 ATOM 1089 C CB . THR A 1 137 ? -21.748 6.214 -4.238 1.00 16.14 ? 162 THR A CB 1 ATOM 1090 O OG1 . THR A 1 137 ? -23.091 5.713 -4.293 1.00 17.31 ? 162 THR A OG1 1 ATOM 1091 C CG2 . THR A 1 137 ? -21.669 7.587 -4.928 1.00 16.76 ? 162 THR A CG2 1 ATOM 1092 N N . ALA A 1 138 ? -21.449 3.577 -6.557 1.00 15.31 ? 163 ALA A N 1 ATOM 1093 C CA . ALA A 1 138 ? -22.032 3.137 -7.811 1.00 15.81 ? 163 ALA A CA 1 ATOM 1094 C C . ALA A 1 138 ? -22.722 1.800 -7.579 1.00 17.81 ? 163 ALA A C 1 ATOM 1095 O O . ALA A 1 138 ? -22.941 1.391 -6.438 1.00 17.08 ? 163 ALA A O 1 ATOM 1096 C CB . ALA A 1 138 ? -20.970 3.030 -8.910 1.00 16.80 ? 163 ALA A CB 1 ATOM 1097 N N . GLY A 1 139 ? -23.054 1.118 -8.667 1.00 15.12 ? 164 GLY A N 1 ATOM 1098 C CA . GLY A 1 139 ? -23.867 -0.077 -8.602 1.00 16.29 ? 164 GLY A CA 1 ATOM 1099 C C . GLY A 1 139 ? -23.234 -1.295 -7.972 1.00 16.22 ? 164 GLY A C 1 ATOM 1100 O O . GLY A 1 139 ? -22.040 -1.336 -7.674 1.00 19.15 ? 164 GLY A O 1 ATOM 1101 N N . TRP A 1 140 ? -24.070 -2.313 -7.818 1.00 18.10 ? 165 TRP A N 1 ATOM 1102 C CA . TRP A 1 140 ? -23.763 -3.527 -7.080 1.00 20.94 ? 165 TRP A CA 1 ATOM 1103 C C . TRP A 1 140 ? -23.111 -4.584 -7.989 1.00 22.99 ? 165 TRP A C 1 ATOM 1104 O O . TRP A 1 140 ? -22.242 -5.340 -7.546 1.00 23.29 ? 165 TRP A O 1 ATOM 1105 C CB . TRP A 1 140 ? -25.085 -4.005 -6.459 1.00 21.97 ? 165 TRP A CB 1 ATOM 1106 C CG . TRP A 1 140 ? -25.117 -5.288 -5.695 1.00 23.84 ? 165 TRP A CG 1 ATOM 1107 C CD1 . TRP A 1 140 ? -24.879 -5.462 -4.359 1.00 24.49 ? 165 TRP A CD1 1 ATOM 1108 C CD2 . TRP A 1 140 ? -25.494 -6.571 -6.206 1.00 22.63 ? 165 TRP A CD2 1 ATOM 1109 N NE1 . TRP A 1 140 ? -25.056 -6.784 -4.018 1.00 22.65 ? 165 TRP A NE1 1 ATOM 1110 C CE2 . TRP A 1 140 ? -25.433 -7.485 -5.134 1.00 26.61 ? 165 TRP A CE2 1 ATOM 1111 C CE3 . TRP A 1 140 ? -25.862 -7.038 -7.473 1.00 25.06 ? 165 TRP A CE3 1 ATOM 1112 C CZ2 . TRP A 1 140 ? -25.724 -8.843 -5.290 1.00 27.27 ? 165 TRP A CZ2 1 ATOM 1113 C CZ3 . TRP A 1 140 ? -26.152 -8.383 -7.627 1.00 25.74 ? 165 TRP A CZ3 1 ATOM 1114 C CH2 . TRP A 1 140 ? -26.078 -9.271 -6.542 1.00 27.17 ? 165 TRP A CH2 1 ATOM 1115 N N . CYS A 1 141 ? -23.510 -4.622 -9.263 1.00 19.70 ? 166 CYS A N 1 ATOM 1116 C CA . CYS A 1 141 ? -22.974 -5.613 -10.206 1.00 20.41 ? 166 CYS A CA 1 ATOM 1117 C C . CYS A 1 141 ? -21.593 -5.202 -10.734 1.00 17.50 ? 166 CYS A C 1 ATOM 1118 O O . CYS A 1 141 ? -21.459 -4.164 -11.372 1.00 20.05 ? 166 CYS A O 1 ATOM 1119 C CB . CYS A 1 141 ? -23.931 -5.792 -11.396 1.00 20.42 ? 166 CYS A CB 1 ATOM 1120 S SG . CYS A 1 141 ? -25.645 -6.309 -11.037 1.00 21.55 ? 166 CYS A SG 1 ATOM 1121 N N . PRO A 1 142 ? -20.559 -6.027 -10.493 1.00 19.07 ? 167 PRO A N 1 ATOM 1122 C CA . PRO A 1 142 ? -19.191 -5.603 -10.822 1.00 19.41 ? 167 PRO A CA 1 ATOM 1123 C C . PRO A 1 142 ? -18.836 -5.544 -12.309 1.00 19.97 ? 167 PRO A C 1 ATOM 1124 O O . PRO A 1 142 ? -17.858 -4.871 -12.638 1.00 21.18 ? 167 PRO A O 1 ATOM 1125 C CB . PRO A 1 142 ? -18.323 -6.659 -10.122 1.00 23.50 ? 167 PRO A CB 1 ATOM 1126 C CG . PRO A 1 142 ? -19.226 -7.863 -10.040 1.00 31.20 ? 167 PRO A CG 1 ATOM 1127 C CD . PRO A 1 142 ? -20.564 -7.270 -9.703 1.00 24.08 ? 167 PRO A CD 1 ATOM 1128 N N . THR A 1 143 ? -19.579 -6.223 -13.181 1.00 19.71 ? 168 THR A N 1 ATOM 1129 C CA . THR A 1 143 ? -19.219 -6.227 -14.599 1.00 18.57 ? 168 THR A CA 1 ATOM 1130 C C . THR A 1 143 ? -19.922 -5.143 -15.413 1.00 16.74 ? 168 THR A C 1 ATOM 1131 O O . THR A 1 143 ? -19.707 -5.028 -16.619 1.00 18.72 ? 168 THR A O 1 ATOM 1132 C CB . THR A 1 143 ? -19.423 -7.615 -15.260 1.00 17.80 ? 168 THR A CB 1 ATOM 1133 O OG1 . THR A 1 143 ? -20.803 -7.998 -15.188 1.00 20.79 ? 168 THR A OG1 1 ATOM 1134 C CG2 . THR A 1 143 ? -18.557 -8.661 -14.567 1.00 19.08 ? 168 THR A CG2 1 ATOM 1135 N N . VAL A 1 144 ? -20.755 -4.344 -14.754 1.00 16.63 ? 169 VAL A N 1 ATOM 1136 C CA . VAL A 1 144 ? -21.397 -3.207 -15.409 1.00 16.28 ? 169 VAL A CA 1 ATOM 1137 C C . VAL A 1 144 ? -20.341 -2.183 -15.843 1.00 17.14 ? 169 VAL A C 1 ATOM 1138 O O . VAL A 1 144 ? -19.372 -1.945 -15.129 1.00 16.32 ? 169 VAL A O 1 ATOM 1139 C CB . VAL A 1 144 ? -22.423 -2.560 -14.455 1.00 15.59 ? 169 VAL A CB 1 ATOM 1140 C CG1 . VAL A 1 144 ? -22.778 -1.142 -14.894 1.00 17.41 ? 169 VAL A CG1 1 ATOM 1141 C CG2 . VAL A 1 144 ? -23.661 -3.438 -14.343 1.00 15.62 ? 169 VAL A CG2 1 ATOM 1142 N N . GLY A 1 145 ? -20.514 -1.591 -17.019 1.00 16.57 ? 170 GLY A N 1 ATOM 1143 C CA . GLY A 1 145 ? -19.574 -0.598 -17.516 1.00 16.73 ? 170 GLY A CA 1 ATOM 1144 C C . GLY A 1 145 ? -19.865 0.800 -16.999 1.00 15.29 ? 170 GLY A C 1 ATOM 1145 O O . GLY A 1 145 ? -21.033 1.183 -16.856 1.00 16.09 ? 170 GLY A O 1 ATOM 1146 N N . THR A 1 146 ? -18.816 1.571 -16.719 1.00 14.21 ? 171 THR A N 1 ATOM 1147 C CA . THR A 1 146 ? -19.013 2.952 -16.276 1.00 15.14 ? 171 THR A CA 1 ATOM 1148 C C . THR A 1 146 ? -19.637 3.803 -17.376 1.00 17.53 ? 171 THR A C 1 ATOM 1149 O O . THR A 1 146 ? -20.328 4.780 -17.093 1.00 17.44 ? 171 THR A O 1 ATOM 1150 C CB . THR A 1 146 ? -17.703 3.632 -15.812 1.00 17.37 ? 171 THR A CB 1 ATOM 1151 O OG1 . THR A 1 146 ? -16.722 3.549 -16.850 1.00 17.77 ? 171 THR A OG1 1 ATOM 1152 C CG2 . THR A 1 146 ? -17.168 2.986 -14.537 1.00 18.01 ? 171 THR A CG2 1 ATOM 1153 N N . GLY A 1 147 ? -19.405 3.424 -18.631 1.00 18.42 ? 172 GLY A N 1 ATOM 1154 C CA . GLY A 1 147 ? -19.929 4.189 -19.754 1.00 18.45 ? 172 GLY A CA 1 ATOM 1155 C C . GLY A 1 147 ? -21.441 4.324 -19.716 1.00 17.24 ? 172 GLY A C 1 ATOM 1156 O O . GLY A 1 147 ? -21.973 5.436 -19.712 1.00 20.07 ? 172 GLY A O 1 ATOM 1157 N N . GLY A 1 148 ? -22.141 3.199 -19.682 1.00 15.69 ? 173 GLY A N 1 ATOM 1158 C CA . GLY A 1 148 ? -23.590 3.236 -19.606 1.00 14.14 ? 173 GLY A CA 1 ATOM 1159 C C . GLY A 1 148 ? -24.100 3.621 -18.223 1.00 15.22 ? 173 GLY A C 1 ATOM 1160 O O . GLY A 1 148 ? -25.053 4.385 -18.083 1.00 16.27 ? 173 GLY A O 1 ATOM 1161 N N . HIS A 1 149 ? -23.452 3.088 -17.193 1.00 14.75 ? 174 HIS A N 1 ATOM 1162 C CA . HIS A 1 149 ? -23.960 3.180 -15.824 1.00 15.30 ? 174 HIS A CA 1 ATOM 1163 C C . HIS A 1 149 ? -23.968 4.612 -15.317 1.00 15.12 ? 174 HIS A C 1 ATOM 1164 O O . HIS A 1 149 ? -24.981 5.107 -14.827 1.00 15.27 ? 174 HIS A O 1 ATOM 1165 C CB . HIS A 1 149 ? -23.083 2.306 -14.927 1.00 16.51 ? 174 HIS A CB 1 ATOM 1166 C CG . HIS A 1 149 ? -23.505 2.244 -13.487 1.00 16.29 ? 174 HIS A CG 1 ATOM 1167 N ND1 . HIS A 1 149 ? -24.594 1.520 -13.057 1.00 15.72 ? 174 HIS A ND1 1 ATOM 1168 C CD2 . HIS A 1 149 ? -22.924 2.750 -12.372 1.00 17.06 ? 174 HIS A CD2 1 ATOM 1169 C CE1 . HIS A 1 149 ? -24.679 1.599 -11.737 1.00 16.19 ? 174 HIS A CE1 1 ATOM 1170 N NE2 . HIS A 1 149 ? -23.678 2.338 -11.298 1.00 16.15 ? 174 HIS A NE2 1 ATOM 1171 N N . ILE A 1 150 ? -22.826 5.278 -15.417 1.00 14.73 ? 175 ILE A N 1 ATOM 1172 C CA . ILE A 1 150 ? -22.758 6.648 -14.947 1.00 14.21 ? 175 ILE A CA 1 ATOM 1173 C C . ILE A 1 150 ? -23.602 7.573 -15.832 1.00 15.04 ? 175 ILE A C 1 ATOM 1174 O O . ILE A 1 150 ? -24.211 8.520 -15.345 1.00 15.86 ? 175 ILE A O 1 ATOM 1175 C CB . ILE A 1 150 ? -21.298 7.129 -14.791 1.00 14.47 ? 175 ILE A CB 1 ATOM 1176 C CG1 . ILE A 1 150 ? -20.551 6.187 -13.841 1.00 15.41 ? 175 ILE A CG1 1 ATOM 1177 C CG2 . ILE A 1 150 ? -21.259 8.575 -14.294 1.00 16.41 ? 175 ILE A CG2 1 ATOM 1178 C CD1 . ILE A 1 150 ? -19.149 6.661 -13.472 1.00 18.47 ? 175 ILE A CD1 1 ATOM 1179 N N . SER A 1 151 ? -23.670 7.272 -17.127 1.00 14.40 ? 176 SER A N 1 ATOM 1180 C CA . SER A 1 151 ? -24.512 8.044 -18.038 1.00 16.15 ? 176 SER A CA 1 ATOM 1181 C C . SER A 1 151 ? -25.981 8.053 -17.628 1.00 14.57 ? 176 SER A C 1 ATOM 1182 O O . SER A 1 151 ? -26.699 9.012 -17.921 1.00 15.23 ? 176 SER A O 1 ATOM 1183 C CB . SER A 1 151 ? -24.407 7.504 -19.463 1.00 16.51 ? 176 SER A CB 1 ATOM 1184 O OG . SER A 1 151 ? -23.130 7.761 -20.007 1.00 16.37 ? 176 SER A OG 1 ATOM 1185 N N . GLY A 1 152 ? -26.417 6.985 -16.964 1.00 14.20 ? 177 GLY A N 1 ATOM 1186 C CA . GLY A 1 152 ? -27.806 6.837 -16.559 1.00 14.92 ? 177 GLY A CA 1 ATOM 1187 C C . GLY A 1 152 ? -28.071 7.096 -15.086 1.00 14.67 ? 177 GLY A C 1 ATOM 1188 O O . GLY A 1 152 ? -29.209 6.947 -14.631 1.00 16.88 ? 177 GLY A O 1 ATOM 1189 N N . GLY A 1 153 ? -27.040 7.497 -14.344 1.00 15.30 ? 178 GLY A N 1 ATOM 1190 C CA . GLY A 1 153 ? -27.191 7.763 -12.916 1.00 15.72 ? 178 GLY A CA 1 ATOM 1191 C C . GLY A 1 153 ? -26.271 6.894 -12.075 1.00 14.26 ? 178 GLY A C 1 ATOM 1192 O O . GLY A 1 153 ? -25.134 7.279 -11.786 1.00 15.25 ? 178 GLY A O 1 ATOM 1193 N N . GLY A 1 154 ? -26.757 5.720 -11.689 1.00 14.30 ? 179 GLY A N 1 ATOM 1194 C CA . GLY A 1 154 ? -25.922 4.722 -11.045 1.00 15.23 ? 179 GLY A CA 1 ATOM 1195 C C . GLY A 1 154 ? -26.157 4.628 -9.552 1.00 15.23 ? 179 GLY A C 1 ATOM 1196 O O . GLY A 1 154 ? -25.541 5.358 -8.764 1.00 15.99 ? 179 GLY A O 1 ATOM 1197 N N . PHE A 1 155 ? -27.041 3.711 -9.168 1.00 15.11 ? 180 PHE A N 1 ATOM 1198 C CA . PHE A 1 155 ? -27.481 3.566 -7.781 1.00 16.14 ? 180 PHE A CA 1 ATOM 1199 C C . PHE A 1 155 ? -26.877 2.319 -7.153 1.00 18.18 ? 180 PHE A C 1 ATOM 1200 O O . PHE A 1 155 ? -26.796 1.268 -7.785 1.00 19.47 ? 180 PHE A O 1 ATOM 1201 C CB . PHE A 1 155 ? -29.016 3.475 -7.729 1.00 18.26 ? 180 PHE A CB 1 ATOM 1202 C CG . PHE A 1 155 ? -29.576 3.395 -6.331 1.00 17.55 ? 180 PHE A CG 1 ATOM 1203 C CD1 . PHE A 1 155 ? -30.016 4.541 -5.692 1.00 18.52 ? 180 PHE A CD1 1 ATOM 1204 C CD2 . PHE A 1 155 ? -29.663 2.180 -5.662 1.00 20.83 ? 180 PHE A CD2 1 ATOM 1205 C CE1 . PHE A 1 155 ? -30.541 4.483 -4.407 1.00 23.06 ? 180 PHE A CE1 1 ATOM 1206 C CE2 . PHE A 1 155 ? -30.185 2.112 -4.366 1.00 21.15 ? 180 PHE A CE2 1 ATOM 1207 C CZ . PHE A 1 155 ? -30.620 3.268 -3.742 1.00 22.61 ? 180 PHE A CZ 1 ATOM 1208 N N . GLY A 1 156 ? -26.455 2.424 -5.901 1.00 16.08 ? 181 GLY A N 1 ATOM 1209 C CA . GLY A 1 156 ? -25.882 1.279 -5.224 1.00 18.28 ? 181 GLY A CA 1 ATOM 1210 C C . GLY A 1 156 ? -25.975 1.351 -3.713 1.00 16.97 ? 181 GLY A C 1 ATOM 1211 O O . GLY A 1 156 ? -26.707 2.174 -3.158 1.00 18.65 ? 181 GLY A O 1 ATOM 1212 N N . MET A 1 157 ? -25.205 0.494 -3.053 1.00 18.23 ? 182 MET A N 1 ATOM 1213 C CA . MET A 1 157 ? -25.326 0.286 -1.613 1.00 18.23 ? 182 MET A CA 1 ATOM 1214 C C . MET A 1 157 ? -24.880 1.473 -0.767 1.00 19.58 ? 182 MET A C 1 ATOM 1215 O O . MET A 1 157 ? -25.150 1.503 0.433 1.00 21.59 ? 182 MET A O 1 ATOM 1216 C CB . MET A 1 157 ? -24.551 -0.960 -1.189 1.00 21.31 ? 182 MET A CB 1 ATOM 1217 C CG . MET A 1 157 ? -25.180 -2.274 -1.646 1.00 26.03 ? 182 MET A CG 1 ATOM 1218 S SD . MET A 1 157 ? -26.758 -2.670 -0.850 1.00 26.23 ? 182 MET A SD 1 ATOM 1219 C CE . MET A 1 157 ? -26.273 -2.952 0.853 1.00 22.45 ? 182 MET A CE 1 ATOM 1220 N N . MET A 1 158 ? -24.195 2.435 -1.376 1.00 17.71 ? 183 MET A N 1 ATOM 1221 C CA . MET A 1 158 ? -23.803 3.640 -0.652 1.00 17.00 ? 183 MET A CA 1 ATOM 1222 C C . MET A 1 158 ? -24.557 4.881 -1.125 1.00 15.64 ? 183 MET A C 1 ATOM 1223 O O . MET A 1 158 ? -24.215 5.998 -0.748 1.00 16.94 ? 183 MET A O 1 ATOM 1224 C CB . MET A 1 158 ? -22.288 3.870 -0.729 1.00 20.91 ? 183 MET A CB 1 ATOM 1225 C CG . MET A 1 158 ? -21.469 2.848 0.059 1.00 20.97 ? 183 MET A CG 1 ATOM 1226 S SD . MET A 1 158 ? -19.741 3.341 0.238 1.00 24.56 ? 183 MET A SD 1 ATOM 1227 C CE . MET A 1 158 ? -19.333 3.778 -1.450 1.00 25.45 ? 183 MET A CE 1 ATOM 1228 N N . SER A 1 159 ? -25.601 4.693 -1.923 1.00 16.38 ? 184 SER A N 1 ATOM 1229 C CA . SER A 1 159 ? -26.335 5.848 -2.443 1.00 17.01 ? 184 SER A CA 1 ATOM 1230 C C . SER A 1 159 ? -27.114 6.625 -1.373 1.00 16.07 ? 184 SER A C 1 ATOM 1231 O O . SER A 1 159 ? -27.362 7.818 -1.534 1.00 17.81 ? 184 SER A O 1 ATOM 1232 C CB . SER A 1 159 ? -27.252 5.443 -3.598 1.00 17.17 ? 184 SER A CB 1 ATOM 1233 O OG . SER A 1 159 ? -26.479 5.164 -4.752 1.00 16.82 ? 184 SER A OG 1 ATOM 1234 N N . ARG A 1 160 ? -27.493 5.969 -0.285 1.00 16.72 ? 185 ARG A N 1 ATOM 1235 C CA A ARG A 1 160 ? -28.191 6.679 0.783 0.40 17.48 ? 185 ARG A CA 1 ATOM 1236 C CA B ARG A 1 160 ? -28.184 6.653 0.806 0.60 17.25 ? 185 ARG A CA 1 ATOM 1237 C C . ARG A 1 160 ? -27.229 7.592 1.537 1.00 17.51 ? 185 ARG A C 1 ATOM 1238 O O . ARG A 1 160 ? -27.662 8.517 2.226 1.00 18.91 ? 185 ARG A O 1 ATOM 1239 C CB A ARG A 1 160 ? -28.902 5.709 1.729 0.40 18.20 ? 185 ARG A CB 1 ATOM 1240 C CB B ARG A 1 160 ? -28.800 5.644 1.777 0.60 16.70 ? 185 ARG A CB 1 ATOM 1241 C CG A ARG A 1 160 ? -29.883 4.787 1.008 0.40 16.51 ? 185 ARG A CG 1 ATOM 1242 C CG B ARG A 1 160 ? -29.776 4.672 1.102 0.60 20.49 ? 185 ARG A CG 1 ATOM 1243 C CD A ARG A 1 160 ? -30.867 4.095 1.945 0.40 24.67 ? 185 ARG A CD 1 ATOM 1244 C CD B ARG A 1 160 ? -30.535 3.791 2.093 0.60 14.94 ? 185 ARG A CD 1 ATOM 1245 N NE A ARG A 1 160 ? -30.421 4.070 3.334 0.40 23.07 ? 185 ARG A NE 1 ATOM 1246 N NE B ARG A 1 160 ? -31.561 4.555 2.805 0.60 15.64 ? 185 ARG A NE 1 ATOM 1247 C CZ A ARG A 1 160 ? -30.955 4.812 4.298 0.40 19.27 ? 185 ARG A CZ 1 ATOM 1248 C CZ B ARG A 1 160 ? -31.398 5.072 4.017 0.60 19.93 ? 185 ARG A CZ 1 ATOM 1249 N NH1 A ARG A 1 160 ? -30.485 4.730 5.534 0.40 16.60 ? 185 ARG A NH1 1 ATOM 1250 N NH1 B ARG A 1 160 ? -32.377 5.771 4.577 0.60 16.62 ? 185 ARG A NH1 1 ATOM 1251 N NH2 A ARG A 1 160 ? -31.959 5.639 4.026 0.40 20.57 ? 185 ARG A NH2 1 ATOM 1252 N NH2 B ARG A 1 160 ? -30.257 4.891 4.667 0.60 17.56 ? 185 ARG A NH2 1 ATOM 1253 N N . LYS A 1 161 ? -25.927 7.344 1.378 1.00 16.33 ? 186 LYS A N 1 ATOM 1254 C CA . LYS A 1 161 ? -24.885 8.173 1.989 1.00 19.54 ? 186 LYS A CA 1 ATOM 1255 C C . LYS A 1 161 ? -24.366 9.235 1.017 1.00 18.13 ? 186 LYS A C 1 ATOM 1256 O O . LYS A 1 161 ? -24.129 10.381 1.407 1.00 20.56 ? 186 LYS A O 1 ATOM 1257 C CB . LYS A 1 161 ? -23.719 7.294 2.462 1.00 19.31 ? 186 LYS A CB 1 ATOM 1258 C CG . LYS A 1 161 ? -22.519 8.054 3.016 1.00 25.62 ? 186 LYS A CG 1 ATOM 1259 C CD . LYS A 1 161 ? -22.786 8.543 4.417 1.00 26.04 ? 186 LYS A CD 1 ATOM 1260 C CE . LYS A 1 161 ? -21.530 9.129 5.045 1.00 26.61 ? 186 LYS A CE 1 ATOM 1261 N NZ . LYS A 1 161 ? -21.832 9.659 6.403 1.00 26.57 ? 186 LYS A NZ 1 ATOM 1262 N N . TYR A 1 162 ? -24.203 8.856 -0.252 1.00 16.59 ? 187 TYR A N 1 ATOM 1263 C CA . TYR A 1 162 ? -23.495 9.705 -1.206 1.00 16.98 ? 187 TYR A CA 1 ATOM 1264 C C . TYR A 1 162 ? -24.224 9.964 -2.526 1.00 16.41 ? 187 TYR A C 1 ATOM 1265 O O . TYR A 1 162 ? -23.688 10.646 -3.405 1.00 17.96 ? 187 TYR A O 1 ATOM 1266 C CB . TYR A 1 162 ? -22.119 9.106 -1.520 1.00 16.90 ? 187 TYR A CB 1 ATOM 1267 C CG . TYR A 1 162 ? -21.115 9.136 -0.380 1.00 16.04 ? 187 TYR A CG 1 ATOM 1268 C CD1 . TYR A 1 162 ? -20.785 10.330 0.258 1.00 16.83 ? 187 TYR A CD1 1 ATOM 1269 C CD2 . TYR A 1 162 ? -20.465 7.976 0.028 1.00 16.52 ? 187 TYR A CD2 1 ATOM 1270 C CE1 . TYR A 1 162 ? -19.855 10.359 1.294 1.00 17.78 ? 187 TYR A CE1 1 ATOM 1271 C CE2 . TYR A 1 162 ? -19.529 7.999 1.067 1.00 17.06 ? 187 TYR A CE2 1 ATOM 1272 C CZ . TYR A 1 162 ? -19.234 9.197 1.693 1.00 18.43 ? 187 TYR A CZ 1 ATOM 1273 O OH . TYR A 1 162 ? -18.303 9.238 2.714 1.00 20.31 ? 187 TYR A OH 1 ATOM 1274 N N . GLY A 1 163 ? -25.425 9.423 -2.672 1.00 16.38 ? 188 GLY A N 1 ATOM 1275 C CA . GLY A 1 163 ? -26.181 9.604 -3.901 1.00 17.86 ? 188 GLY A CA 1 ATOM 1276 C C . GLY A 1 163 ? -25.714 8.693 -5.022 1.00 14.85 ? 188 GLY A C 1 ATOM 1277 O O . GLY A 1 163 ? -25.104 7.655 -4.784 1.00 16.75 ? 188 GLY A O 1 ATOM 1278 N N . LEU A 1 164 ? -26.015 9.088 -6.255 1.00 15.58 ? 189 LEU A N 1 ATOM 1279 C CA . LEU A 1 164 ? -25.665 8.291 -7.430 1.00 15.40 ? 189 LEU A CA 1 ATOM 1280 C C . LEU A 1 164 ? -24.215 8.510 -7.858 1.00 15.40 ? 189 LEU A C 1 ATOM 1281 O O . LEU A 1 164 ? -23.597 9.515 -7.512 1.00 16.78 ? 189 LEU A O 1 ATOM 1282 C CB . LEU A 1 164 ? -26.574 8.666 -8.599 1.00 15.08 ? 189 LEU A CB 1 ATOM 1283 C CG . LEU A 1 164 ? -28.079 8.585 -8.332 1.00 17.19 ? 189 LEU A CG 1 ATOM 1284 C CD1 . LEU A 1 164 ? -28.848 9.065 -9.552 1.00 16.83 ? 189 LEU A CD1 1 ATOM 1285 C CD2 . LEU A 1 164 ? -28.474 7.168 -7.959 1.00 18.07 ? 189 LEU A CD2 1 ATOM 1286 N N . ALA A 1 165 ? -23.684 7.574 -8.644 1.00 14.53 ? 190 ALA A N 1 ATOM 1287 C CA . ALA A 1 165 ? -22.381 7.777 -9.256 1.00 14.91 ? 190 ALA A CA 1 ATOM 1288 C C . ALA A 1 165 ? -22.347 9.129 -9.959 1.00 17.02 ? 190 ALA A C 1 ATOM 1289 O O . ALA A 1 165 ? -21.410 9.910 -9.794 1.00 16.63 ? 190 ALA A O 1 ATOM 1290 C CB . ALA A 1 165 ? -22.086 6.664 -10.242 1.00 15.75 ? 190 ALA A CB 1 ATOM 1291 N N . ALA A 1 166 ? -23.392 9.416 -10.729 1.00 15.64 ? 191 ALA A N 1 ATOM 1292 C CA . ALA A 1 166 ? -23.439 10.652 -11.507 1.00 15.82 ? 191 ALA A CA 1 ATOM 1293 C C . ALA A 1 166 ? -23.446 11.918 -10.653 1.00 15.43 ? 191 ALA A C 1 ATOM 1294 O O . ALA A 1 166 ? -23.050 12.986 -11.132 1.00 17.32 ? 191 ALA A O 1 ATOM 1295 C CB . ALA A 1 166 ? -24.640 10.640 -12.462 1.00 17.95 ? 191 ALA A CB 1 ATOM 1296 N N . ASP A 1 167 ? -23.899 11.799 -9.405 1.00 15.50 ? 192 ASP A N 1 ATOM 1297 C CA . ASP A 1 167 ? -23.935 12.928 -8.475 1.00 16.32 ? 192 ASP A CA 1 ATOM 1298 C C . ASP A 1 167 ? -22.534 13.300 -7.986 1.00 17.70 ? 192 ASP A C 1 ATOM 1299 O O . ASP A 1 167 ? -22.355 14.321 -7.319 1.00 21.50 ? 192 ASP A O 1 ATOM 1300 C CB . ASP A 1 167 ? -24.815 12.595 -7.265 1.00 16.88 ? 192 ASP A CB 1 ATOM 1301 C CG . ASP A 1 167 ? -26.284 12.433 -7.626 1.00 17.55 ? 192 ASP A CG 1 ATOM 1302 O OD1 . ASP A 1 167 ? -26.742 13.061 -8.609 1.00 19.80 ? 192 ASP A OD1 1 ATOM 1303 O OD2 . ASP A 1 167 ? -26.988 11.684 -6.911 1.00 17.62 ? 192 ASP A OD2 1 ATOM 1304 N N . ASN A 1 168 ? -21.549 12.468 -8.315 1.00 15.54 ? 193 ASN A N 1 ATOM 1305 C CA . ASN A 1 168 ? -20.189 12.667 -7.835 1.00 16.06 ? 193 ASN A CA 1 ATOM 1306 C C . ASN A 1 168 ? -19.184 12.791 -8.979 1.00 16.10 ? 193 ASN A C 1 ATOM 1307 O O . ASN A 1 168 ? -17.989 12.557 -8.799 1.00 18.47 ? 193 ASN A O 1 ATOM 1308 C CB . ASN A 1 168 ? -19.817 11.533 -6.886 1.00 15.87 ? 193 ASN A CB 1 ATOM 1309 C CG . ASN A 1 168 ? -20.657 11.549 -5.616 1.00 17.65 ? 193 ASN A CG 1 ATOM 1310 O OD1 . ASN A 1 168 ? -20.318 12.229 -4.649 1.00 18.48 ? 193 ASN A OD1 1 ATOM 1311 N ND2 . ASN A 1 168 ? -21.758 10.806 -5.617 1.00 16.72 ? 193 ASN A ND2 1 ATOM 1312 N N . VAL A 1 169 ? -19.696 13.163 -10.151 1.00 16.01 ? 194 VAL A N 1 ATOM 1313 C CA . VAL A 1 169 ? -18.870 13.447 -11.322 1.00 15.85 ? 194 VAL A CA 1 ATOM 1314 C C . VAL A 1 169 ? -18.572 14.949 -11.377 1.00 16.10 ? 194 VAL A C 1 ATOM 1315 O O . VAL A 1 169 ? -19.487 15.771 -11.280 1.00 18.39 ? 194 VAL A O 1 ATOM 1316 C CB . VAL A 1 169 ? -19.610 13.026 -12.599 1.00 17.36 ? 194 VAL A CB 1 ATOM 1317 C CG1 . VAL A 1 169 ? -18.939 13.601 -13.845 1.00 18.17 ? 194 VAL A CG1 1 ATOM 1318 C CG2 . VAL A 1 169 ? -19.712 11.506 -12.675 1.00 18.19 ? 194 VAL A CG2 1 ATOM 1319 N N . VAL A 1 170 ? -17.297 15.307 -11.529 1.00 16.31 ? 195 VAL A N 1 ATOM 1320 C CA . VAL A 1 170 ? -16.892 16.720 -11.480 1.00 17.25 ? 195 VAL A CA 1 ATOM 1321 C C . VAL A 1 170 ? -16.343 17.238 -12.813 1.00 19.91 ? 195 VAL A C 1 ATOM 1322 O O . VAL A 1 170 ? -16.207 18.448 -13.011 1.00 19.35 ? 195 VAL A O 1 ATOM 1323 C CB . VAL A 1 170 ? -15.883 16.997 -10.337 1.00 18.49 ? 195 VAL A CB 1 ATOM 1324 C CG1 . VAL A 1 170 ? -16.543 16.725 -8.980 1.00 20.23 ? 195 VAL A CG1 1 ATOM 1325 C CG2 . VAL A 1 170 ? -14.622 16.153 -10.507 1.00 21.43 ? 195 VAL A CG2 1 ATOM 1326 N N . ASP A 1 171 ? -16.030 16.318 -13.721 1.00 18.35 ? 196 ASP A N 1 ATOM 1327 C CA . ASP A 1 171 ? -15.604 16.668 -15.075 1.00 17.57 ? 196 ASP A CA 1 ATOM 1328 C C . ASP A 1 171 ? -15.818 15.419 -15.917 1.00 16.98 ? 196 ASP A C 1 ATOM 1329 O O . ASP A 1 171 ? -16.131 14.350 -15.389 1.00 17.35 ? 196 ASP A O 1 ATOM 1330 C CB . ASP A 1 171 ? -14.122 17.097 -15.092 1.00 19.01 ? 196 ASP A CB 1 ATOM 1331 C CG . ASP A 1 171 ? -13.773 18.038 -16.253 1.00 23.42 ? 196 ASP A CG 1 ATOM 1332 O OD1 . ASP A 1 171 ? -14.470 18.042 -17.293 1.00 19.31 ? 196 ASP A OD1 1 ATOM 1333 O OD2 . ASP A 1 171 ? -12.776 18.785 -16.117 1.00 24.18 ? 196 ASP A OD2 1 ATOM 1334 N N . ALA A 1 172 ? -15.669 15.561 -17.229 1.00 18.30 ? 197 ALA A N 1 ATOM 1335 C CA . ALA A 1 172 ? -15.793 14.440 -18.150 1.00 16.59 ? 197 ALA A CA 1 ATOM 1336 C C . ALA A 1 172 ? -15.204 14.866 -19.477 1.00 17.22 ? 197 ALA A C 1 ATOM 1337 O O . ALA A 1 172 ? -15.104 16.060 -19.756 1.00 19.70 ? 197 ALA A O 1 ATOM 1338 C CB . ALA A 1 172 ? -17.258 14.035 -18.328 1.00 19.10 ? 197 ALA A CB 1 ATOM 1339 N N . ILE A 1 173 ? -14.787 13.894 -20.279 1.00 18.71 ? 198 ILE A N 1 ATOM 1340 C CA . ILE A 1 173 ? -14.407 14.172 -21.656 1.00 18.08 ? 198 ILE A CA 1 ATOM 1341 C C . ILE A 1 173 ? -15.455 13.543 -22.555 1.00 18.64 ? 198 ILE A C 1 ATOM 1342 O O . ILE A 1 173 ? -15.649 12.327 -22.536 1.00 18.74 ? 198 ILE A O 1 ATOM 1343 C CB . ILE A 1 173 ? -13.015 13.609 -22.008 1.00 19.30 ? 198 ILE A CB 1 ATOM 1344 C CG1 . ILE A 1 173 ? -11.938 14.252 -21.131 1.00 25.06 ? 198 ILE A CG1 1 ATOM 1345 C CG2 . ILE A 1 173 ? -12.704 13.831 -23.493 1.00 18.72 ? 198 ILE A CG2 1 ATOM 1346 C CD1 . ILE A 1 173 ? -11.725 15.723 -21.408 1.00 30.56 ? 198 ILE A CD1 1 ATOM 1347 N N . LEU A 1 174 ? -16.141 14.380 -23.330 1.00 18.99 ? 199 LEU A N 1 ATOM 1348 C CA . LEU A 1 174 ? -17.187 13.920 -24.235 1.00 17.40 ? 199 LEU A CA 1 ATOM 1349 C C . LEU A 1 174 ? -16.718 14.115 -25.668 1.00 20.75 ? 199 LEU A C 1 ATOM 1350 O O . LEU A 1 174 ? -16.272 15.203 -26.029 1.00 23.21 ? 199 LEU A O 1 ATOM 1351 C CB . LEU A 1 174 ? -18.477 14.711 -24.003 1.00 19.37 ? 199 LEU A CB 1 ATOM 1352 C CG . LEU A 1 174 ? -19.654 14.433 -24.945 1.00 21.90 ? 199 LEU A CG 1 ATOM 1353 C CD1 . LEU A 1 174 ? -20.233 13.050 -24.704 1.00 20.90 ? 199 LEU A CD1 1 ATOM 1354 C CD2 . LEU A 1 174 ? -20.733 15.484 -24.756 1.00 24.51 ? 199 LEU A CD2 1 ATOM 1355 N N . ILE A 1 175 ? -16.809 13.061 -26.475 1.00 18.45 ? 200 ILE A N 1 ATOM 1356 C CA . ILE A 1 175 ? -16.495 13.157 -27.900 1.00 18.02 ? 200 ILE A CA 1 ATOM 1357 C C . ILE A 1 175 ? -17.808 13.343 -28.639 1.00 20.69 ? 200 ILE A C 1 ATOM 1358 O O . ILE A 1 175 ? -18.688 12.478 -28.573 1.00 19.75 ? 200 ILE A O 1 ATOM 1359 C CB . ILE A 1 175 ? -15.785 11.892 -28.429 1.00 20.12 ? 200 ILE A CB 1 ATOM 1360 C CG1 . ILE A 1 175 ? -14.621 11.489 -27.519 1.00 23.28 ? 200 ILE A CG1 1 ATOM 1361 C CG2 . ILE A 1 175 ? -15.319 12.096 -29.879 1.00 20.16 ? 200 ILE A CG2 1 ATOM 1362 C CD1 . ILE A 1 175 ? -13.580 12.550 -27.336 1.00 26.98 ? 200 ILE A CD1 1 ATOM 1363 N N . ASP A 1 176 ? -17.957 14.475 -29.323 1.00 20.10 ? 201 ASP A N 1 ATOM 1364 C CA . ASP A 1 176 ? -19.249 14.806 -29.927 1.00 18.39 ? 201 ASP A CA 1 ATOM 1365 C C . ASP A 1 176 ? -19.415 14.272 -31.344 1.00 22.79 ? 201 ASP A C 1 ATOM 1366 O O . ASP A 1 176 ? -18.549 13.566 -31.851 1.00 21.56 ? 201 ASP A O 1 ATOM 1367 C CB . ASP A 1 176 ? -19.562 16.309 -29.829 1.00 20.60 ? 201 ASP A CB 1 ATOM 1368 C CG . ASP A 1 176 ? -18.909 17.142 -30.924 1.00 25.18 ? 201 ASP A CG 1 ATOM 1369 O OD1 . ASP A 1 176 ? -18.114 16.609 -31.724 1.00 23.55 ? 201 ASP A OD1 1 ATOM 1370 O OD2 . ASP A 1 176 ? -19.207 18.353 -30.969 1.00 26.93 ? 201 ASP A OD2 1 ATOM 1371 N N . ALA A 1 177 ? -20.550 14.591 -31.955 1.00 24.02 ? 202 ALA A N 1 ATOM 1372 C CA . ALA A 1 177 ? -20.892 14.064 -33.272 1.00 23.18 ? 202 ALA A CA 1 ATOM 1373 C C . ALA A 1 177 ? -19.856 14.387 -34.344 1.00 25.37 ? 202 ALA A C 1 ATOM 1374 O O . ALA A 1 177 ? -19.769 13.685 -35.348 1.00 26.44 ? 202 ALA A O 1 ATOM 1375 C CB . ALA A 1 177 ? -22.252 14.564 -33.700 1.00 24.34 ? 202 ALA A CB 1 ATOM 1376 N N . ASN A 1 178 ? -19.087 15.452 -34.140 1.00 26.43 ? 203 ASN A N 1 ATOM 1377 C CA . ASN A 1 178 ? -18.054 15.834 -35.106 1.00 28.96 ? 203 ASN A CA 1 ATOM 1378 C C . ASN A 1 178 ? -16.649 15.395 -34.696 1.00 28.29 ? 203 ASN A C 1 ATOM 1379 O O . ASN A 1 178 ? -15.668 15.729 -35.361 1.00 30.00 ? 203 ASN A O 1 ATOM 1380 C CB . ASN A 1 178 ? -18.075 17.344 -35.352 1.00 30.25 ? 203 ASN A CB 1 ATOM 1381 C CG . ASN A 1 178 ? -19.408 17.826 -35.898 1.00 39.80 ? 203 ASN A CG 1 ATOM 1382 O OD1 . ASN A 1 178 ? -19.974 17.221 -36.808 1.00 43.38 ? 203 ASN A OD1 1 ATOM 1383 N ND2 . ASN A 1 178 ? -19.914 18.920 -35.343 1.00 36.39 ? 203 ASN A ND2 1 ATOM 1384 N N . GLY A 1 179 ? -16.552 14.651 -33.600 1.00 23.92 ? 204 GLY A N 1 ATOM 1385 C CA . GLY A 1 179 ? -15.263 14.197 -33.109 1.00 21.94 ? 204 GLY A CA 1 ATOM 1386 C C . GLY A 1 179 ? -14.550 15.197 -32.212 1.00 20.71 ? 204 GLY A C 1 ATOM 1387 O O . GLY A 1 179 ? -13.388 14.999 -31.865 1.00 25.73 ? 204 GLY A O 1 ATOM 1388 N N . ALA A 1 180 ? -15.240 16.268 -31.836 1.00 23.73 ? 205 ALA A N 1 ATOM 1389 C CA . ALA A 1 180 ? -14.647 17.258 -30.941 1.00 24.97 ? 205 ALA A CA 1 ATOM 1390 C C . ALA A 1 180 ? -14.373 16.613 -29.591 1.00 26.65 ? 205 ALA A C 1 ATOM 1391 O O . ALA A 1 180 ? -15.134 15.758 -29.139 1.00 27.25 ? 205 ALA A O 1 ATOM 1392 C CB . ALA A 1 180 ? -15.564 18.449 -30.781 1.00 24.97 ? 205 ALA A CB 1 ATOM 1393 N N . ILE A 1 181 ? -13.282 17.016 -28.955 1.00 22.25 ? 206 ILE A N 1 ATOM 1394 C CA . ILE A 1 181 ? -12.925 16.480 -27.649 1.00 22.13 ? 206 ILE A CA 1 ATOM 1395 C C . ILE A 1 181 ? -13.235 17.539 -26.594 1.00 21.62 ? 206 ILE A C 1 ATOM 1396 O O . ILE A 1 181 ? -12.514 18.524 -26.467 1.00 20.48 ? 206 ILE A O 1 ATOM 1397 C CB . ILE A 1 181 ? -11.442 16.088 -27.608 1.00 22.80 ? 206 ILE A CB 1 ATOM 1398 C CG1 . ILE A 1 181 ? -11.134 15.084 -28.728 1.00 22.43 ? 206 ILE A CG1 1 ATOM 1399 C CG2 . ILE A 1 181 ? -11.071 15.524 -26.239 1.00 22.50 ? 206 ILE A CG2 1 ATOM 1400 C CD1 . ILE A 1 181 ? -9.677 14.713 -28.842 1.00 28.50 ? 206 ILE A CD1 1 ATOM 1401 N N . LEU A 1 182 ? -14.314 17.331 -25.845 1.00 19.80 ? 207 LEU A N 1 ATOM 1402 C CA . LEU A 1 182 ? -14.880 18.377 -24.991 1.00 22.17 ? 207 LEU A CA 1 ATOM 1403 C C . LEU A 1 182 ? -14.833 18.023 -23.509 1.00 20.06 ? 207 LEU A C 1 ATOM 1404 O O . LEU A 1 182 ? -15.404 17.014 -23.095 1.00 18.61 ? 207 LEU A O 1 ATOM 1405 C CB . LEU A 1 182 ? -16.343 18.623 -25.379 1.00 22.46 ? 207 LEU A CB 1 ATOM 1406 C CG . LEU A 1 182 ? -16.633 18.826 -26.868 1.00 20.87 ? 207 LEU A CG 1 ATOM 1407 C CD1 . LEU A 1 182 ? -18.131 18.778 -27.122 1.00 25.14 ? 207 LEU A CD1 1 ATOM 1408 C CD2 . LEU A 1 182 ? -16.023 20.134 -27.366 1.00 22.58 ? 207 LEU A CD2 1 ATOM 1409 N N . ASP A 1 183 ? -14.178 18.860 -22.709 1.00 19.31 ? 208 ASP A N 1 ATOM 1410 C CA . ASP A 1 183 ? -14.275 18.727 -21.258 1.00 18.28 ? 208 ASP A CA 1 ATOM 1411 C C . ASP A 1 183 ? -15.481 19.511 -20.735 1.00 19.23 ? 208 ASP A C 1 ATOM 1412 O O . ASP A 1 183 ? -16.268 20.046 -21.518 1.00 19.61 ? 208 ASP A O 1 ATOM 1413 C CB . ASP A 1 183 ? -12.973 19.123 -20.543 1.00 18.75 ? 208 ASP A CB 1 ATOM 1414 C CG . ASP A 1 183 ? -12.578 20.573 -20.777 1.00 20.59 ? 208 ASP A CG 1 ATOM 1415 O OD1 . ASP A 1 183 ? -13.431 21.394 -21.182 1.00 21.55 ? 208 ASP A OD1 1 ATOM 1416 O OD2 . ASP A 1 183 ? -11.394 20.895 -20.530 1.00 27.29 ? 208 ASP A OD2 1 ATOM 1417 N N . ARG A 1 184 ? -15.638 19.558 -19.416 1.00 19.20 ? 209 ARG A N 1 ATOM 1418 C CA . ARG A 1 184 ? -16.796 20.214 -18.821 1.00 20.07 ? 209 ARG A CA 1 ATOM 1419 C C . ARG A 1 184 ? -16.908 21.665 -19.291 1.00 22.85 ? 209 ARG A C 1 ATOM 1420 O O . ARG A 1 184 ? -17.985 22.124 -19.668 1.00 20.81 ? 209 ARG A O 1 ATOM 1421 C CB . ARG A 1 184 ? -16.716 20.146 -17.296 1.00 19.85 ? 209 ARG A CB 1 ATOM 1422 C CG . ARG A 1 184 ? -17.760 20.989 -16.584 1.00 22.17 ? 209 ARG A CG 1 ATOM 1423 C CD . ARG A 1 184 ? -17.693 20.774 -15.080 1.00 21.03 ? 209 ARG A CD 1 ATOM 1424 N NE . ARG A 1 184 ? -18.779 21.463 -14.393 1.00 22.68 ? 209 ARG A NE 1 ATOM 1425 C CZ . ARG A 1 184 ? -19.038 21.338 -13.094 1.00 20.89 ? 209 ARG A CZ 1 ATOM 1426 N NH1 . ARG A 1 184 ? -18.282 20.557 -12.330 1.00 23.12 ? 209 ARG A NH1 1 ATOM 1427 N NH2 . ARG A 1 184 ? -20.061 21.997 -12.561 1.00 24.90 ? 209 ARG A NH2 1 ATOM 1428 N N . GLN A 1 185 ? -15.789 22.382 -19.285 1.00 20.57 ? 210 GLN A N 1 ATOM 1429 C CA . GLN A 1 185 ? -15.800 23.785 -19.694 1.00 22.91 ? 210 GLN A CA 1 ATOM 1430 C C . GLN A 1 185 ? -16.199 23.961 -21.159 1.00 26.73 ? 210 GLN A C 1 ATOM 1431 O O . GLN A 1 185 ? -16.900 24.914 -21.508 1.00 30.77 ? 210 GLN A O 1 ATOM 1432 C CB . GLN A 1 185 ? -14.440 24.441 -19.425 1.00 22.70 ? 210 GLN A CB 1 ATOM 1433 C CG . GLN A 1 185 ? -14.050 24.446 -17.953 1.00 27.17 ? 210 GLN A CG 1 ATOM 1434 C CD . GLN A 1 185 ? -15.153 24.991 -17.062 1.00 45.34 ? 210 GLN A CD 1 ATOM 1435 O OE1 . GLN A 1 185 ? -15.719 26.050 -17.334 1.00 48.24 ? 210 GLN A OE1 1 ATOM 1436 N NE2 . GLN A 1 185 ? -15.461 24.270 -15.989 1.00 44.99 ? 210 GLN A NE2 1 ATOM 1437 N N . ALA A 1 186 ? -15.760 23.040 -22.014 1.00 21.50 ? 211 ALA A N 1 ATOM 1438 C CA . ALA A 1 186 ? -16.055 23.123 -23.442 1.00 21.79 ? 211 ALA A CA 1 ATOM 1439 C C . ALA A 1 186 ? -17.505 22.781 -23.775 1.00 24.09 ? 211 ALA A C 1 ATOM 1440 O O . ALA A 1 186 ? -18.127 23.442 -24.613 1.00 25.85 ? 211 ALA A O 1 ATOM 1441 C CB . ALA A 1 186 ? -15.114 22.225 -24.233 1.00 22.93 ? 211 ALA A CB 1 ATOM 1442 N N . MET A 1 187 ? -18.043 21.745 -23.135 1.00 20.15 ? 212 MET A N 1 ATOM 1443 C CA . MET A 1 187 ? -19.397 21.307 -23.458 1.00 22.04 ? 212 MET A CA 1 ATOM 1444 C C . MET A 1 187 ? -20.462 22.226 -22.858 1.00 21.86 ? 212 MET A C 1 ATOM 1445 O O . MET A 1 187 ? -21.581 22.298 -23.363 1.00 23.66 ? 212 MET A O 1 ATOM 1446 C CB . MET A 1 187 ? -19.626 19.848 -23.033 1.00 22.27 ? 212 MET A CB 1 ATOM 1447 C CG . MET A 1 187 ? -19.715 19.632 -21.528 1.00 19.96 ? 212 MET A CG 1 ATOM 1448 S SD . MET A 1 187 ? -19.915 17.887 -21.058 1.00 20.22 ? 212 MET A SD 1 ATOM 1449 C CE . MET A 1 187 ? -18.214 17.313 -21.133 1.00 20.02 ? 212 MET A CE 1 ATOM 1450 N N . GLY A 1 188 ? -20.114 22.920 -21.781 1.00 21.08 ? 213 GLY A N 1 ATOM 1451 C CA . GLY A 1 188 ? -21.044 23.839 -21.146 1.00 21.90 ? 213 GLY A CA 1 ATOM 1452 C C . GLY A 1 188 ? -21.860 23.170 -20.058 1.00 22.95 ? 213 GLY A C 1 ATOM 1453 O O . GLY A 1 188 ? -21.952 21.940 -20.001 1.00 20.78 ? 213 GLY A O 1 ATOM 1454 N N . GLU A 1 189 ? -22.469 23.974 -19.194 1.00 22.71 ? 214 GLU A N 1 ATOM 1455 C CA . GLU A 1 189 ? -23.133 23.420 -18.014 1.00 22.63 ? 214 GLU A CA 1 ATOM 1456 C C . GLU A 1 189 ? -24.405 22.615 -18.317 1.00 22.94 ? 214 GLU A C 1 ATOM 1457 O O . GLU A 1 189 ? -24.708 21.655 -17.609 1.00 23.70 ? 214 GLU A O 1 ATOM 1458 C CB . GLU A 1 189 ? -23.390 24.504 -16.963 1.00 26.26 ? 214 GLU A CB 1 ATOM 1459 C CG . GLU A 1 189 ? -22.125 24.944 -16.234 1.00 26.91 ? 214 GLU A CG 1 ATOM 1460 C CD . GLU A 1 189 ? -21.432 23.800 -15.508 1.00 31.89 ? 214 GLU A CD 1 ATOM 1461 O OE1 . GLU A 1 189 ? -21.999 23.277 -14.527 1.00 28.64 ? 214 GLU A OE1 1 ATOM 1462 O OE2 . GLU A 1 189 ? -20.309 23.433 -15.908 1.00 32.41 ? 214 GLU A OE2 1 ATOM 1463 N N . ASP A 1 190 ? -25.139 22.984 -19.364 1.00 19.33 ? 215 ASP A N 1 ATOM 1464 C CA . ASP A 1 190 ? -26.333 22.223 -19.742 1.00 21.91 ? 215 ASP A CA 1 ATOM 1465 C C . ASP A 1 190 ? -25.975 20.805 -20.198 1.00 20.57 ? 215 ASP A C 1 ATOM 1466 O O . ASP A 1 190 ? -26.608 19.828 -19.795 1.00 20.75 ? 215 ASP A O 1 ATOM 1467 C CB . ASP A 1 190 ? -27.127 22.941 -20.837 1.00 25.78 ? 215 ASP A CB 1 ATOM 1468 C CG . ASP A 1 190 ? -28.055 24.014 -20.287 1.00 34.40 ? 215 ASP A CG 1 ATOM 1469 O OD1 . ASP A 1 190 ? -28.406 23.961 -19.089 1.00 27.76 ? 215 ASP A OD1 1 ATOM 1470 O OD2 . ASP A 1 190 ? -28.439 24.914 -21.063 1.00 38.11 ? 215 ASP A OD2 1 ATOM 1471 N N . VAL A 1 191 ? -24.961 20.691 -21.048 1.00 20.12 ? 216 VAL A N 1 ATOM 1472 C CA . VAL A 1 191 ? -24.542 19.381 -21.527 1.00 20.03 ? 216 VAL A CA 1 ATOM 1473 C C . VAL A 1 191 ? -23.870 18.563 -20.423 1.00 19.01 ? 216 VAL A C 1 ATOM 1474 O O . VAL A 1 191 ? -24.100 17.359 -20.311 1.00 18.63 ? 216 VAL A O 1 ATOM 1475 C CB . VAL A 1 191 ? -23.640 19.491 -22.775 1.00 18.57 ? 216 VAL A CB 1 ATOM 1476 C CG1 . VAL A 1 191 ? -23.216 18.104 -23.247 1.00 19.33 ? 216 VAL A CG1 1 ATOM 1477 C CG2 . VAL A 1 191 ? -24.379 20.229 -23.882 1.00 20.95 ? 216 VAL A CG2 1 ATOM 1478 N N . PHE A 1 192 ? -23.069 19.221 -19.587 1.00 19.20 ? 217 PHE A N 1 ATOM 1479 C CA . PHE A 1 192 ? -22.414 18.523 -18.484 1.00 17.46 ? 217 PHE A CA 1 ATOM 1480 C C . PHE A 1 192 ? -23.444 18.005 -17.478 1.00 19.28 ? 217 PHE A C 1 ATOM 1481 O O . PHE A 1 192 ? -23.251 16.958 -16.857 1.00 17.02 ? 217 PHE A O 1 ATOM 1482 C CB . PHE A 1 192 ? -21.365 19.404 -17.792 1.00 18.20 ? 217 PHE A CB 1 ATOM 1483 C CG . PHE A 1 192 ? -20.684 18.716 -16.648 1.00 17.57 ? 217 PHE A CG 1 ATOM 1484 C CD1 . PHE A 1 192 ? -19.781 17.686 -16.884 1.00 18.40 ? 217 PHE A CD1 1 ATOM 1485 C CD2 . PHE A 1 192 ? -20.965 19.074 -15.336 1.00 17.29 ? 217 PHE A CD2 1 ATOM 1486 C CE1 . PHE A 1 192 ? -19.164 17.023 -15.831 1.00 18.17 ? 217 PHE A CE1 1 ATOM 1487 C CE2 . PHE A 1 192 ? -20.351 18.419 -14.283 1.00 19.76 ? 217 PHE A CE2 1 ATOM 1488 C CZ . PHE A 1 192 ? -19.455 17.394 -14.526 1.00 18.59 ? 217 PHE A CZ 1 ATOM 1489 N N . TRP A 1 193 ? -24.538 18.746 -17.325 1.00 18.97 ? 218 TRP A N 1 ATOM 1490 C CA . TRP A 1 193 ? -25.681 18.285 -16.541 1.00 18.85 ? 218 TRP A CA 1 ATOM 1491 C C . TRP A 1 193 ? -26.335 17.076 -17.214 1.00 18.29 ? 218 TRP A C 1 ATOM 1492 O O . TRP A 1 193 ? -26.545 16.041 -16.581 1.00 17.98 ? 218 TRP A O 1 ATOM 1493 C CB . TRP A 1 193 ? -26.680 19.435 -16.378 1.00 19.61 ? 218 TRP A CB 1 ATOM 1494 C CG . TRP A 1 193 ? -27.975 19.078 -15.693 1.00 18.30 ? 218 TRP A CG 1 ATOM 1495 C CD1 . TRP A 1 193 ? -28.213 19.041 -14.344 1.00 21.09 ? 218 TRP A CD1 1 ATOM 1496 C CD2 . TRP A 1 193 ? -29.214 18.746 -16.327 1.00 18.55 ? 218 TRP A CD2 1 ATOM 1497 N NE1 . TRP A 1 193 ? -29.523 18.694 -14.105 1.00 18.71 ? 218 TRP A NE1 1 ATOM 1498 C CE2 . TRP A 1 193 ? -30.158 18.506 -15.305 1.00 19.29 ? 218 TRP A CE2 1 ATOM 1499 C CE3 . TRP A 1 193 ? -29.619 18.624 -17.661 1.00 19.68 ? 218 TRP A CE3 1 ATOM 1500 C CZ2 . TRP A 1 193 ? -31.480 18.154 -15.576 1.00 19.25 ? 218 TRP A CZ2 1 ATOM 1501 C CZ3 . TRP A 1 193 ? -30.938 18.273 -17.929 1.00 21.07 ? 218 TRP A CZ3 1 ATOM 1502 C CH2 . TRP A 1 193 ? -31.849 18.038 -16.887 1.00 18.05 ? 218 TRP A CH2 1 ATOM 1503 N N . ALA A 1 194 ? -26.632 17.199 -18.507 1.00 17.37 ? 219 ALA A N 1 ATOM 1504 C CA . ALA A 1 194 ? -27.337 16.146 -19.233 1.00 18.12 ? 219 ALA A CA 1 ATOM 1505 C C . ALA A 1 194 ? -26.626 14.795 -19.203 1.00 16.28 ? 219 ALA A C 1 ATOM 1506 O O . ALA A 1 194 ? -27.272 13.753 -19.084 1.00 16.55 ? 219 ALA A O 1 ATOM 1507 C CB . ALA A 1 194 ? -27.590 16.571 -20.684 1.00 19.39 ? 219 ALA A CB 1 ATOM 1508 N N . ILE A 1 195 ? -25.300 14.794 -19.328 1.00 17.67 ? 220 ILE A N 1 ATOM 1509 C CA . ILE A 1 195 ? -24.585 13.520 -19.393 1.00 15.77 ? 220 ILE A CA 1 ATOM 1510 C C . ILE A 1 195 ? -24.540 12.794 -18.048 1.00 15.91 ? 220 ILE A C 1 ATOM 1511 O O . ILE A 1 195 ? -24.270 11.595 -18.001 1.00 17.38 ? 220 ILE A O 1 ATOM 1512 C CB . ILE A 1 195 ? -23.152 13.656 -19.954 1.00 15.83 ? 220 ILE A CB 1 ATOM 1513 C CG1 . ILE A 1 195 ? -22.277 14.514 -19.034 1.00 16.88 ? 220 ILE A CG1 1 ATOM 1514 C CG2 . ILE A 1 195 ? -23.179 14.223 -21.366 1.00 18.44 ? 220 ILE A CG2 1 ATOM 1515 C CD1 . ILE A 1 195 ? -20.786 14.512 -19.435 1.00 18.55 ? 220 ILE A CD1 1 ATOM 1516 N N . ARG A 1 196 ? -24.820 13.518 -16.968 1.00 16.06 ? 221 ARG A N 1 ATOM 1517 C CA . ARG A 1 196 ? -24.766 12.935 -15.629 1.00 17.09 ? 221 ARG A CA 1 ATOM 1518 C C . ARG A 1 196 ? -26.097 12.307 -15.228 1.00 15.96 ? 221 ARG A C 1 ATOM 1519 O O . ARG A 1 196 ? -26.639 12.614 -14.165 1.00 15.97 ? 221 ARG A O 1 ATOM 1520 C CB . ARG A 1 196 ? -24.360 13.990 -14.595 1.00 16.78 ? 221 ARG A CB 1 ATOM 1521 C CG . ARG A 1 196 ? -22.885 14.405 -14.640 1.00 19.18 ? 221 ARG A CG 1 ATOM 1522 C CD . ARG A 1 196 ? -22.594 15.473 -13.583 1.00 16.23 ? 221 ARG A CD 1 ATOM 1523 N NE . ARG A 1 196 ? -23.173 16.763 -13.947 1.00 19.80 ? 221 ARG A NE 1 ATOM 1524 C CZ . ARG A 1 196 ? -23.467 17.719 -13.073 1.00 23.01 ? 221 ARG A CZ 1 ATOM 1525 N NH1 . ARG A 1 196 ? -23.265 17.515 -11.776 1.00 22.78 ? 221 ARG A NH1 1 ATOM 1526 N NH2 . ARG A 1 196 ? -23.986 18.869 -13.493 1.00 22.90 ? 221 ARG A NH2 1 ATOM 1527 N N . GLY A 1 197 ? -26.630 11.431 -16.079 1.00 16.77 ? 222 GLY A N 1 ATOM 1528 C CA . GLY A 1 197 ? -27.882 10.756 -15.768 1.00 17.51 ? 222 GLY A CA 1 ATOM 1529 C C . GLY A 1 197 ? -28.921 10.788 -16.873 1.00 15.30 ? 222 GLY A C 1 ATOM 1530 O O . GLY A 1 197 ? -29.948 10.121 -16.775 1.00 15.58 ? 222 GLY A O 1 ATOM 1531 N N . GLY A 1 198 ? -28.650 11.548 -17.930 1.00 14.98 ? 223 GLY A N 1 ATOM 1532 C CA . GLY A 1 198 ? -29.600 11.699 -19.022 1.00 15.87 ? 223 GLY A CA 1 ATOM 1533 C C . GLY A 1 198 ? -29.695 10.511 -19.959 1.00 16.84 ? 223 GLY A C 1 ATOM 1534 O O . GLY A 1 198 ? -30.499 10.526 -20.896 1.00 17.20 ? 223 GLY A O 1 ATOM 1535 N N . GLY A 1 199 ? -28.879 9.490 -19.710 1.00 15.75 ? 224 GLY A N 1 ATOM 1536 C CA . GLY A 1 199 ? -28.920 8.262 -20.483 1.00 15.38 ? 224 GLY A CA 1 ATOM 1537 C C . GLY A 1 199 ? -27.770 8.131 -21.458 1.00 14.95 ? 224 GLY A C 1 ATOM 1538 O O . GLY A 1 199 ? -27.366 9.102 -22.105 1.00 16.55 ? 224 GLY A O 1 ATOM 1539 N N . GLY A 1 200 ? -27.243 6.916 -21.580 1.00 15.89 ? 225 GLY A N 1 ATOM 1540 C CA . GLY A 1 200 ? -26.189 6.657 -22.545 1.00 15.01 ? 225 GLY A CA 1 ATOM 1541 C C . GLY A 1 200 ? -26.692 6.579 -23.973 1.00 16.27 ? 225 GLY A C 1 ATOM 1542 O O . GLY A 1 200 ? -27.888 6.387 -24.225 1.00 17.42 ? 225 GLY A O 1 ATOM 1543 N N . GLY A 1 201 ? -25.766 6.754 -24.912 1.00 15.24 ? 226 GLY A N 1 ATOM 1544 C CA . GLY A 1 201 ? -26.086 6.640 -26.327 1.00 15.50 ? 226 GLY A CA 1 ATOM 1545 C C . GLY A 1 201 ? -26.871 7.801 -26.916 1.00 16.79 ? 226 GLY A C 1 ATOM 1546 O O . GLY A 1 201 ? -27.528 7.642 -27.951 1.00 17.17 ? 226 GLY A O 1 ATOM 1547 N N . VAL A 1 202 ? -26.793 8.969 -26.282 1.00 16.82 ? 227 VAL A N 1 ATOM 1548 C CA . VAL A 1 202 ? -27.650 10.095 -26.645 1.00 17.00 ? 227 VAL A CA 1 ATOM 1549 C C . VAL A 1 202 ? -26.899 11.404 -26.911 1.00 17.52 ? 227 VAL A C 1 ATOM 1550 O O . VAL A 1 202 ? -27.335 12.216 -27.735 1.00 18.32 ? 227 VAL A O 1 ATOM 1551 C CB . VAL A 1 202 ? -28.696 10.357 -25.533 1.00 18.06 ? 227 VAL A CB 1 ATOM 1552 C CG1 . VAL A 1 202 ? -29.543 11.581 -25.857 1.00 19.17 ? 227 VAL A CG1 1 ATOM 1553 C CG2 . VAL A 1 202 ? -29.568 9.123 -25.320 1.00 18.35 ? 227 VAL A CG2 1 ATOM 1554 N N . TRP A 1 203 ? -25.776 11.612 -26.224 1.00 17.13 ? 228 TRP A N 1 ATOM 1555 C CA . TRP A 1 203 ? -25.115 12.922 -26.211 1.00 17.02 ? 228 TRP A CA 1 ATOM 1556 C C . TRP A 1 203 ? -23.827 12.971 -27.020 1.00 18.39 ? 228 TRP A C 1 ATOM 1557 O O . TRP A 1 203 ? -23.339 14.053 -27.367 1.00 20.17 ? 228 TRP A O 1 ATOM 1558 C CB . TRP A 1 203 ? -24.826 13.337 -24.761 1.00 22.05 ? 228 TRP A CB 1 ATOM 1559 C CG . TRP A 1 203 ? -25.986 13.017 -23.894 1.00 20.21 ? 228 TRP A CG 1 ATOM 1560 C CD1 . TRP A 1 203 ? -26.132 11.927 -23.084 1.00 17.79 ? 228 TRP A CD1 1 ATOM 1561 C CD2 . TRP A 1 203 ? -27.207 13.755 -23.802 1.00 18.26 ? 228 TRP A CD2 1 ATOM 1562 N NE1 . TRP A 1 203 ? -27.367 11.956 -22.473 1.00 17.39 ? 228 TRP A NE1 1 ATOM 1563 C CE2 . TRP A 1 203 ? -28.047 13.067 -22.902 1.00 17.65 ? 228 TRP A CE2 1 ATOM 1564 C CE3 . TRP A 1 203 ? -27.671 14.943 -24.385 1.00 18.84 ? 228 TRP A CE3 1 ATOM 1565 C CZ2 . TRP A 1 203 ? -29.328 13.527 -22.569 1.00 18.06 ? 228 TRP A CZ2 1 ATOM 1566 C CZ3 . TRP A 1 203 ? -28.938 15.395 -24.052 1.00 19.99 ? 228 TRP A CZ3 1 ATOM 1567 C CH2 . TRP A 1 203 ? -29.750 14.688 -23.151 1.00 18.14 ? 228 TRP A CH2 1 ATOM 1568 N N . GLY A 1 204 ? -23.295 11.791 -27.326 1.00 19.02 ? 229 GLY A N 1 ATOM 1569 C CA . GLY A 1 204 ? -21.945 11.650 -27.833 1.00 17.85 ? 229 GLY A CA 1 ATOM 1570 C C . GLY A 1 204 ? -21.317 10.466 -27.129 1.00 17.99 ? 229 GLY A C 1 ATOM 1571 O O . GLY A 1 204 ? -21.999 9.741 -26.401 1.00 18.49 ? 229 GLY A O 1 ATOM 1572 N N . ALA A 1 205 ? -20.022 10.268 -27.328 1.00 16.53 ? 230 ALA A N 1 ATOM 1573 C CA . ALA A 1 205 ? -19.335 9.163 -26.674 1.00 16.37 ? 230 ALA A CA 1 ATOM 1574 C C . ALA A 1 205 ? -18.521 9.696 -25.503 1.00 18.04 ? 230 ALA A C 1 ATOM 1575 O O . ALA A 1 205 ? -17.596 10.488 -25.691 1.00 18.42 ? 230 ALA A O 1 ATOM 1576 C CB . ALA A 1 205 ? -18.433 8.437 -27.673 1.00 18.53 ? 230 ALA A CB 1 ATOM 1577 N N . ILE A 1 206 ? -18.866 9.281 -24.289 1.00 14.81 ? 231 ILE A N 1 ATOM 1578 C CA . ILE A 1 206 ? -18.040 9.647 -23.149 1.00 16.67 ? 231 ILE A CA 1 ATOM 1579 C C . ILE A 1 206 ? -16.715 8.907 -23.289 1.00 17.06 ? 231 ILE A C 1 ATOM 1580 O O . ILE A 1 206 ? -16.699 7.678 -23.418 1.00 17.94 ? 231 ILE A O 1 ATOM 1581 C CB . ILE A 1 206 ? -18.694 9.259 -21.811 1.00 15.65 ? 231 ILE A CB 1 ATOM 1582 C CG1 . ILE A 1 206 ? -20.025 9.991 -21.629 1.00 17.54 ? 231 ILE A CG1 1 ATOM 1583 C CG2 . ILE A 1 206 ? -17.723 9.540 -20.657 1.00 16.56 ? 231 ILE A CG2 1 ATOM 1584 C CD1 . ILE A 1 206 ? -19.872 11.452 -21.279 1.00 19.24 ? 231 ILE A CD1 1 ATOM 1585 N N . TYR A 1 207 ? -15.610 9.652 -23.302 1.00 16.05 ? 232 TYR A N 1 ATOM 1586 C CA . TYR A 1 207 ? -14.286 9.035 -23.283 1.00 15.40 ? 232 TYR A CA 1 ATOM 1587 C C . TYR A 1 207 ? -13.874 8.666 -21.852 1.00 16.79 ? 232 TYR A C 1 ATOM 1588 O O . TYR A 1 207 ? -13.407 7.553 -21.599 1.00 18.66 ? 232 TYR A O 1 ATOM 1589 C CB . TYR A 1 207 ? -13.219 9.927 -23.951 1.00 19.48 ? 232 TYR A CB 1 ATOM 1590 C CG . TYR A 1 207 ? -11.824 9.535 -23.508 1.00 20.63 ? 232 TYR A CG 1 ATOM 1591 C CD1 . TYR A 1 207 ? -11.295 8.292 -23.836 1.00 23.11 ? 232 TYR A CD1 1 ATOM 1592 C CD2 . TYR A 1 207 ? -11.064 10.380 -22.711 1.00 21.82 ? 232 TYR A CD2 1 ATOM 1593 C CE1 . TYR A 1 207 ? -10.035 7.912 -23.404 1.00 26.60 ? 232 TYR A CE1 1 ATOM 1594 C CE2 . TYR A 1 207 ? -9.802 10.008 -22.275 1.00 22.82 ? 232 TYR A CE2 1 ATOM 1595 C CZ . TYR A 1 207 ? -9.295 8.775 -22.627 1.00 26.10 ? 232 TYR A CZ 1 ATOM 1596 O OH . TYR A 1 207 ? -8.045 8.397 -22.190 1.00 29.72 ? 232 TYR A OH 1 ATOM 1597 N N . ALA A 1 208 ? -14.055 9.599 -20.923 1.00 17.75 ? 233 ALA A N 1 ATOM 1598 C CA . ALA A 1 208 ? -13.658 9.382 -19.535 1.00 17.18 ? 233 ALA A CA 1 ATOM 1599 C C . ALA A 1 208 ? -14.480 10.239 -18.589 1.00 18.41 ? 233 ALA A C 1 ATOM 1600 O O . ALA A 1 208 ? -14.972 11.300 -18.966 1.00 18.39 ? 233 ALA A O 1 ATOM 1601 C CB . ALA A 1 208 ? -12.152 9.665 -19.347 1.00 19.87 ? 233 ALA A CB 1 ATOM 1602 N N . TRP A 1 209 ? -14.637 9.750 -17.361 1.00 16.60 ? 234 TRP A N 1 ATOM 1603 C CA . TRP A 1 209 ? -15.316 10.466 -16.294 1.00 16.79 ? 234 TRP A CA 1 ATOM 1604 C C . TRP A 1 209 ? -14.278 10.916 -15.282 1.00 17.50 ? 234 TRP A C 1 ATOM 1605 O O . TRP A 1 209 ? -13.381 10.148 -14.952 1.00 18.40 ? 234 TRP A O 1 ATOM 1606 C CB . TRP A 1 209 ? -16.268 9.522 -15.557 1.00 15.27 ? 234 TRP A CB 1 ATOM 1607 C CG . TRP A 1 209 ? -17.407 8.956 -16.363 1.00 15.46 ? 234 TRP A CG 1 ATOM 1608 C CD1 . TRP A 1 209 ? -17.531 7.675 -16.819 1.00 20.25 ? 234 TRP A CD1 1 ATOM 1609 C CD2 . TRP A 1 209 ? -18.597 9.642 -16.762 1.00 15.63 ? 234 TRP A CD2 1 ATOM 1610 N NE1 . TRP A 1 209 ? -18.722 7.523 -17.487 1.00 17.73 ? 234 TRP A NE1 1 ATOM 1611 C CE2 . TRP A 1 209 ? -19.397 8.715 -17.470 1.00 16.02 ? 234 TRP A CE2 1 ATOM 1612 C CE3 . TRP A 1 209 ? -19.065 10.954 -16.596 1.00 17.15 ? 234 TRP A CE3 1 ATOM 1613 C CZ2 . TRP A 1 209 ? -20.642 9.057 -18.011 1.00 18.24 ? 234 TRP A CZ2 1 ATOM 1614 C CZ3 . TRP A 1 209 ? -20.308 11.289 -17.134 1.00 19.93 ? 234 TRP A CZ3 1 ATOM 1615 C CH2 . TRP A 1 209 ? -21.079 10.341 -17.828 1.00 16.97 ? 234 TRP A CH2 1 ATOM 1616 N N . LYS A 1 210 ? -14.403 12.136 -14.770 1.00 16.71 ? 235 LYS A N 1 ATOM 1617 C CA . LYS A 1 210 ? -13.620 12.518 -13.595 1.00 16.15 ? 235 LYS A CA 1 ATOM 1618 C C . LYS A 1 210 ? -14.526 12.511 -12.370 1.00 14.98 ? 235 LYS A C 1 ATOM 1619 O O . LYS A 1 210 ? -15.511 13.252 -12.303 1.00 17.15 ? 235 LYS A O 1 ATOM 1620 C CB . LYS A 1 210 ? -12.943 13.879 -13.771 1.00 17.06 ? 235 LYS A CB 1 ATOM 1621 C CG . LYS A 1 210 ? -12.002 14.237 -12.624 1.00 17.46 ? 235 LYS A CG 1 ATOM 1622 C CD . LYS A 1 210 ? -11.414 15.637 -12.782 1.00 17.10 ? 235 LYS A CD 1 ATOM 1623 C CE . LYS A 1 210 ? -10.492 15.952 -11.608 1.00 21.25 ? 235 LYS A CE 1 ATOM 1624 N NZ . LYS A 1 210 ? -9.922 17.321 -11.733 1.00 26.02 ? 235 LYS A NZ 1 ATOM 1625 N N . ILE A 1 211 ? -14.200 11.652 -11.413 1.00 16.03 ? 236 ILE A N 1 ATOM 1626 C CA . ILE A 1 211 ? -15.045 11.463 -10.245 1.00 18.48 ? 236 ILE A CA 1 ATOM 1627 C C . ILE A 1 211 ? -14.341 11.915 -8.985 1.00 16.47 ? 236 ILE A C 1 ATOM 1628 O O . ILE A 1 211 ? -13.114 11.871 -8.895 1.00 17.30 ? 236 ILE A O 1 ATOM 1629 C CB . ILE A 1 211 ? -15.468 9.985 -10.079 1.00 16.67 ? 236 ILE A CB 1 ATOM 1630 C CG1 . ILE A 1 211 ? -14.244 9.079 -9.937 1.00 16.56 ? 236 ILE A CG1 1 ATOM 1631 C CG2 . ILE A 1 211 ? -16.306 9.534 -11.272 1.00 19.43 ? 236 ILE A CG2 1 ATOM 1632 C CD1 . ILE A 1 211 ? -14.591 7.613 -9.703 1.00 18.48 ? 236 ILE A CD1 1 ATOM 1633 N N . LYS A 1 212 ? -15.132 12.353 -8.012 1.00 17.04 ? 237 LYS A N 1 ATOM 1634 C CA . LYS A 1 212 ? -14.611 12.645 -6.691 1.00 17.40 ? 237 LYS A CA 1 ATOM 1635 C C . LYS A 1 212 ? -14.661 11.373 -5.867 1.00 17.48 ? 237 LYS A C 1 ATOM 1636 O O . LYS A 1 212 ? -15.715 10.742 -5.749 1.00 19.01 ? 237 LYS A O 1 ATOM 1637 C CB . LYS A 1 212 ? -15.433 13.738 -6.013 1.00 19.39 ? 237 LYS A CB 1 ATOM 1638 C CG . LYS A 1 212 ? -14.881 14.170 -4.656 1.00 20.39 ? 237 LYS A CG 1 ATOM 1639 C CD . LYS A 1 212 ? -13.551 14.904 -4.787 1.00 21.15 ? 237 LYS A CD 1 ATOM 1640 C CE . LYS A 1 212 ? -12.870 15.046 -3.428 1.00 27.00 ? 237 LYS A CE 1 ATOM 1641 N NZ . LYS A 1 212 ? -11.606 15.806 -3.545 1.00 39.27 ? 237 LYS A NZ 1 ATOM 1642 N N . LEU A 1 213 ? -13.514 10.991 -5.321 1.00 15.76 ? 238 LEU A N 1 ATOM 1643 C CA . LEU A 1 213 ? -13.435 9.831 -4.449 1.00 17.61 ? 238 LEU A CA 1 ATOM 1644 C C . LEU A 1 213 ? -13.939 10.218 -3.064 1.00 18.24 ? 238 LEU A C 1 ATOM 1645 O O . LEU A 1 213 ? -13.772 11.360 -2.626 1.00 18.87 ? 238 LEU A O 1 ATOM 1646 C CB . LEU A 1 213 ? -12.005 9.289 -4.401 1.00 17.04 ? 238 LEU A CB 1 ATOM 1647 C CG . LEU A 1 213 ? -11.478 8.781 -5.756 1.00 17.68 ? 238 LEU A CG 1 ATOM 1648 C CD1 . LEU A 1 213 ? -10.040 8.264 -5.631 1.00 21.09 ? 238 LEU A CD1 1 ATOM 1649 C CD2 . LEU A 1 213 ? -12.391 7.713 -6.382 1.00 19.50 ? 238 LEU A CD2 1 ATOM 1650 N N . LEU A 1 214 ? -14.577 9.270 -2.388 1.00 17.89 ? 239 LEU A N 1 ATOM 1651 C CA . LEU A 1 214 ? -15.340 9.583 -1.186 1.00 17.81 ? 239 LEU A CA 1 ATOM 1652 C C . LEU A 1 214 ? -14.793 8.852 0.032 1.00 16.78 ? 239 LEU A C 1 ATOM 1653 O O . LEU A 1 214 ? -14.322 7.721 -0.066 1.00 18.56 ? 239 LEU A O 1 ATOM 1654 C CB . LEU A 1 214 ? -16.816 9.231 -1.410 1.00 17.86 ? 239 LEU A CB 1 ATOM 1655 C CG . LEU A 1 214 ? -17.454 9.869 -2.652 1.00 19.34 ? 239 LEU A CG 1 ATOM 1656 C CD1 . LEU A 1 214 ? -18.763 9.185 -3.037 1.00 20.14 ? 239 LEU A CD1 1 ATOM 1657 C CD2 . LEU A 1 214 ? -17.669 11.362 -2.420 1.00 24.85 ? 239 LEU A CD2 1 ATOM 1658 N N . PRO A 1 215 ? -14.864 9.491 1.202 1.00 16.76 ? 240 PRO A N 1 ATOM 1659 C CA . PRO A 1 215 ? -14.286 8.842 2.383 1.00 17.32 ? 240 PRO A CA 1 ATOM 1660 C C . PRO A 1 215 ? -15.046 7.583 2.801 1.00 19.39 ? 240 PRO A C 1 ATOM 1661 O O . PRO A 1 215 ? -16.276 7.526 2.739 1.00 18.77 ? 240 PRO A O 1 ATOM 1662 C CB . PRO A 1 215 ? -14.414 9.908 3.481 1.00 20.90 ? 240 PRO A CB 1 ATOM 1663 C CG . PRO A 1 215 ? -14.786 11.178 2.786 1.00 23.25 ? 240 PRO A CG 1 ATOM 1664 C CD . PRO A 1 215 ? -15.460 10.801 1.510 1.00 22.35 ? 240 PRO A CD 1 ATOM 1665 N N . VAL A 1 216 ? -14.292 6.574 3.213 1.00 17.61 ? 241 VAL A N 1 ATOM 1666 C CA . VAL A 1 216 ? -14.851 5.397 3.856 1.00 17.65 ? 241 VAL A CA 1 ATOM 1667 C C . VAL A 1 216 ? -13.944 5.056 5.030 1.00 18.31 ? 241 VAL A C 1 ATOM 1668 O O . VAL A 1 216 ? -12.736 5.320 4.983 1.00 17.99 ? 241 VAL A O 1 ATOM 1669 C CB . VAL A 1 216 ? -14.924 4.189 2.894 1.00 18.08 ? 241 VAL A CB 1 ATOM 1670 C CG1 . VAL A 1 216 ? -15.931 4.442 1.778 1.00 19.50 ? 241 VAL A CG1 1 ATOM 1671 C CG2 . VAL A 1 216 ? -13.551 3.874 2.312 1.00 16.89 ? 241 VAL A CG2 1 ATOM 1672 N N . PRO A 1 217 ? -14.514 4.493 6.104 1.00 17.50 ? 242 PRO A N 1 ATOM 1673 C CA . PRO A 1 217 ? -13.673 4.045 7.221 1.00 20.38 ? 242 PRO A CA 1 ATOM 1674 C C . PRO A 1 217 ? -12.809 2.862 6.783 1.00 15.87 ? 242 PRO A C 1 ATOM 1675 O O . PRO A 1 217 ? -13.157 2.184 5.818 1.00 18.09 ? 242 PRO A O 1 ATOM 1676 C CB . PRO A 1 217 ? -14.692 3.574 8.274 1.00 23.33 ? 242 PRO A CB 1 ATOM 1677 C CG . PRO A 1 217 ? -16.043 4.013 7.773 1.00 24.09 ? 242 PRO A CG 1 ATOM 1678 C CD . PRO A 1 217 ? -15.937 4.173 6.296 1.00 18.95 ? 242 PRO A CD 1 ATOM 1679 N N . GLU A 1 218 ? -11.705 2.613 7.480 1.00 20.45 ? 243 GLU A N 1 ATOM 1680 C CA . GLU A 1 218 ? -10.847 1.491 7.116 1.00 19.52 ? 243 GLU A CA 1 ATOM 1681 C C . GLU A 1 218 ? -11.541 0.141 7.301 1.00 20.02 ? 243 GLU A C 1 ATOM 1682 O O . GLU A 1 218 ? -11.225 -0.830 6.610 1.00 23.00 ? 243 GLU A O 1 ATOM 1683 C CB . GLU A 1 218 ? -9.516 1.561 7.867 1.00 24.95 ? 243 GLU A CB 1 ATOM 1684 C CG . GLU A 1 218 ? -8.654 2.720 7.389 1.00 28.10 ? 243 GLU A CG 1 ATOM 1685 C CD . GLU A 1 218 ? -7.249 2.681 7.939 1.00 47.85 ? 243 GLU A CD 1 ATOM 1686 O OE1 . GLU A 1 218 ? -7.098 2.530 9.168 1.00 49.17 ? 243 GLU A OE1 1 ATOM 1687 O OE2 . GLU A 1 218 ? -6.296 2.814 7.141 1.00 50.55 ? 243 GLU A OE2 1 ATOM 1688 N N . LYS A 1 219 ? -12.501 0.086 8.220 1.00 19.71 ? 244 LYS A N 1 ATOM 1689 C CA . LYS A 1 219 ? -13.350 -1.088 8.363 1.00 20.40 ? 244 LYS A CA 1 ATOM 1690 C C . LYS A 1 219 ? -14.816 -0.672 8.338 1.00 20.41 ? 244 LYS A C 1 ATOM 1691 O O . LYS A 1 219 ? -15.239 0.195 9.100 1.00 21.90 ? 244 LYS A O 1 ATOM 1692 C CB . LYS A 1 219 ? -13.051 -1.836 9.664 1.00 23.70 ? 244 LYS A CB 1 ATOM 1693 C CG . LYS A 1 219 ? -11.628 -2.375 9.764 1.00 28.85 ? 244 LYS A CG 1 ATOM 1694 C CD . LYS A 1 219 ? -11.298 -3.332 8.617 1.00 37.58 ? 244 LYS A CD 1 ATOM 1695 C CE . LYS A 1 219 ? -9.849 -3.801 8.700 1.00 43.44 ? 244 LYS A CE 1 ATOM 1696 N NZ . LYS A 1 219 ? -9.538 -4.899 7.743 1.00 42.98 ? 244 LYS A NZ 1 ATOM 1697 N N . VAL A 1 220 ? -15.572 -1.281 7.434 1.00 16.42 ? 245 VAL A N 1 ATOM 1698 C CA . VAL A 1 220 ? -17.021 -1.166 7.424 1.00 15.75 ? 245 VAL A CA 1 ATOM 1699 C C . VAL A 1 220 ? -17.620 -2.502 7.866 1.00 17.77 ? 245 VAL A C 1 ATOM 1700 O O . VAL A 1 220 ? -16.914 -3.510 7.959 1.00 18.14 ? 245 VAL A O 1 ATOM 1701 C CB . VAL A 1 220 ? -17.555 -0.789 6.029 1.00 16.47 ? 245 VAL A CB 1 ATOM 1702 C CG1 . VAL A 1 220 ? -17.051 0.588 5.632 1.00 17.73 ? 245 VAL A CG1 1 ATOM 1703 C CG2 . VAL A 1 220 ? -17.140 -1.828 4.994 1.00 17.62 ? 245 VAL A CG2 1 ATOM 1704 N N . THR A 1 221 ? -18.916 -2.508 8.151 1.00 18.03 ? 246 THR A N 1 ATOM 1705 C CA . THR A 1 221 ? -19.586 -3.731 8.576 1.00 17.59 ? 246 THR A CA 1 ATOM 1706 C C . THR A 1 221 ? -20.654 -4.101 7.573 1.00 18.98 ? 246 THR A C 1 ATOM 1707 O O . THR A 1 221 ? -21.446 -3.254 7.162 1.00 19.36 ? 246 THR A O 1 ATOM 1708 C CB . THR A 1 221 ? -20.230 -3.574 9.961 1.00 18.99 ? 246 THR A CB 1 ATOM 1709 O OG1 . THR A 1 221 ? -19.237 -3.143 10.896 1.00 20.85 ? 246 THR A OG1 1 ATOM 1710 C CG2 . THR A 1 221 ? -20.818 -4.905 10.424 1.00 23.14 ? 246 THR A CG2 1 ATOM 1711 N N . VAL A 1 222 ? -20.671 -5.364 7.171 1.00 16.89 ? 247 VAL A N 1 ATOM 1712 C CA . VAL A 1 222 ? -21.697 -5.855 6.269 1.00 16.41 ? 247 VAL A CA 1 ATOM 1713 C C . VAL A 1 222 ? -22.274 -7.165 6.780 1.00 19.81 ? 247 VAL A C 1 ATOM 1714 O O . VAL A 1 222 ? -21.665 -7.861 7.605 1.00 20.08 ? 247 VAL A O 1 ATOM 1715 C CB . VAL A 1 222 ? -21.164 -6.067 4.830 1.00 19.70 ? 247 VAL A CB 1 ATOM 1716 C CG1 . VAL A 1 222 ? -20.815 -4.733 4.177 1.00 21.46 ? 247 VAL A CG1 1 ATOM 1717 C CG2 . VAL A 1 222 ? -19.963 -7.002 4.830 1.00 24.77 ? 247 VAL A CG2 1 ATOM 1718 N N . PHE A 1 223 ? -23.477 -7.475 6.317 1.00 19.16 ? 248 PHE A N 1 ATOM 1719 C CA . PHE A 1 223 ? -23.998 -8.822 6.442 1.00 19.29 ? 248 PHE A CA 1 ATOM 1720 C C . PHE A 1 223 ? -24.704 -9.243 5.167 1.00 18.94 ? 248 PHE A C 1 ATOM 1721 O O . PHE A 1 223 ? -25.211 -8.408 4.409 1.00 18.37 ? 248 PHE A O 1 ATOM 1722 C CB . PHE A 1 223 ? -24.886 -9.011 7.684 1.00 19.26 ? 248 PHE A CB 1 ATOM 1723 C CG . PHE A 1 223 ? -26.029 -8.040 7.794 1.00 18.32 ? 248 PHE A CG 1 ATOM 1724 C CD1 . PHE A 1 223 ? -27.183 -8.210 7.042 1.00 19.48 ? 248 PHE A CD1 1 ATOM 1725 C CD2 . PHE A 1 223 ? -25.968 -6.983 8.694 1.00 20.39 ? 248 PHE A CD2 1 ATOM 1726 C CE1 . PHE A 1 223 ? -28.248 -7.323 7.162 1.00 18.88 ? 248 PHE A CE1 1 ATOM 1727 C CE2 . PHE A 1 223 ? -27.026 -6.095 8.821 1.00 20.30 ? 248 PHE A CE2 1 ATOM 1728 C CZ . PHE A 1 223 ? -28.167 -6.263 8.057 1.00 20.05 ? 248 PHE A CZ 1 ATOM 1729 N N A ARG A 1 224 ? -24.679 -10.542 4.897 0.43 19.28 ? 249 ARG A N 1 ATOM 1730 N N B ARG A 1 224 ? -24.736 -10.555 4.963 0.57 18.77 ? 249 ARG A N 1 ATOM 1731 C CA A ARG A 1 224 ? -25.411 -11.113 3.774 0.43 21.12 ? 249 ARG A CA 1 ATOM 1732 C CA B ARG A 1 224 ? -25.328 -11.172 3.790 0.57 22.25 ? 249 ARG A CA 1 ATOM 1733 C C A ARG A 1 224 ? -26.029 -12.411 4.262 0.43 21.69 ? 249 ARG A C 1 ATOM 1734 C C B ARG A 1 224 ? -26.010 -12.433 4.308 0.57 21.75 ? 249 ARG A C 1 ATOM 1735 O O A ARG A 1 224 ? -25.382 -13.458 4.283 0.43 23.56 ? 249 ARG A O 1 ATOM 1736 O O B ARG A 1 224 ? -25.381 -13.488 4.408 0.57 21.33 ? 249 ARG A O 1 ATOM 1737 C CB A ARG A 1 224 ? -24.493 -11.353 2.574 0.43 20.99 ? 249 ARG A CB 1 ATOM 1738 C CB B ARG A 1 224 ? -24.214 -11.525 2.801 0.57 23.38 ? 249 ARG A CB 1 ATOM 1739 C CG A ARG A 1 224 ? -25.157 -12.111 1.429 0.43 21.96 ? 249 ARG A CG 1 ATOM 1740 C CG B ARG A 1 224 ? -24.655 -11.836 1.381 0.57 23.90 ? 249 ARG A CG 1 ATOM 1741 C CD A ARG A 1 224 ? -24.211 -12.269 0.248 0.43 28.18 ? 249 ARG A CD 1 ATOM 1742 C CD B ARG A 1 224 ? -23.451 -12.237 0.531 0.57 21.09 ? 249 ARG A CD 1 ATOM 1743 N NE A ARG A 1 224 ? -24.756 -13.155 -0.778 0.43 37.45 ? 249 ARG A NE 1 ATOM 1744 N NE B ARG A 1 224 ? -22.880 -13.508 0.972 0.57 27.37 ? 249 ARG A NE 1 ATOM 1745 C CZ A ARG A 1 224 ? -25.250 -12.740 -1.940 0.43 42.02 ? 249 ARG A CZ 1 ATOM 1746 C CZ B ARG A 1 224 ? -21.680 -13.958 0.617 0.57 21.24 ? 249 ARG A CZ 1 ATOM 1747 N NH1 A ARG A 1 224 ? -25.265 -11.447 -2.232 0.43 44.95 ? 249 ARG A NH1 1 ATOM 1748 N NH1 B ARG A 1 224 ? -20.904 -13.241 -0.185 0.57 15.04 ? 249 ARG A NH1 1 ATOM 1749 N NH2 A ARG A 1 224 ? -25.725 -13.618 -2.813 0.43 36.35 ? 249 ARG A NH2 1 ATOM 1750 N NH2 B ARG A 1 224 ? -21.253 -15.132 1.069 0.57 23.88 ? 249 ARG A NH2 1 ATOM 1751 N N . VAL A 1 225 ? -27.287 -12.318 4.673 1.00 19.83 ? 250 VAL A N 1 ATOM 1752 C CA . VAL A 1 225 ? -27.963 -13.395 5.377 1.00 20.06 ? 250 VAL A CA 1 ATOM 1753 C C . VAL A 1 225 ? -29.265 -13.777 4.701 1.00 18.40 ? 250 VAL A C 1 ATOM 1754 O O . VAL A 1 225 ? -30.154 -12.940 4.532 1.00 21.06 ? 250 VAL A O 1 ATOM 1755 C CB . VAL A 1 225 ? -28.289 -12.975 6.823 1.00 25.08 ? 250 VAL A CB 1 ATOM 1756 C CG1 . VAL A 1 225 ? -29.095 -14.058 7.527 1.00 23.69 ? 250 VAL A CG1 1 ATOM 1757 C CG2 . VAL A 1 225 ? -27.011 -12.661 7.592 1.00 26.60 ? 250 VAL A CG2 1 ATOM 1758 N N . THR A 1 226 ? -29.380 -15.040 4.316 1.00 20.88 ? 251 THR A N 1 ATOM 1759 C CA . THR A 1 226 ? -30.595 -15.518 3.680 1.00 21.44 ? 251 THR A CA 1 ATOM 1760 C C . THR A 1 226 ? -31.513 -16.151 4.714 1.00 21.78 ? 251 THR A C 1 ATOM 1761 O O . THR A 1 226 ? -31.128 -17.099 5.413 1.00 26.81 ? 251 THR A O 1 ATOM 1762 C CB . THR A 1 226 ? -30.279 -16.522 2.571 1.00 21.53 ? 251 THR A CB 1 ATOM 1763 O OG1 . THR A 1 226 ? -29.443 -15.892 1.594 1.00 24.79 ? 251 THR A OG1 1 ATOM 1764 C CG2 . THR A 1 226 ? -31.566 -17.009 1.902 1.00 25.56 ? 251 THR A CG2 1 ATOM 1765 N N . LYS A 1 227 ? -32.715 -15.598 4.827 1.00 22.95 ? 252 LYS A N 1 ATOM 1766 C CA . LYS A 1 227 ? -33.752 -16.153 5.682 1.00 20.63 ? 252 LYS A CA 1 ATOM 1767 C C . LYS A 1 227 ? -34.594 -17.124 4.868 1.00 25.25 ? 252 LYS A C 1 ATOM 1768 O O . LYS A 1 227 ? -35.067 -16.788 3.780 1.00 24.59 ? 252 LYS A O 1 ATOM 1769 C CB . LYS A 1 227 ? -34.658 -15.049 6.227 1.00 26.96 ? 252 LYS A CB 1 ATOM 1770 C CG . LYS A 1 227 ? -33.930 -13.860 6.839 1.00 26.24 ? 252 LYS A CG 1 ATOM 1771 C CD . LYS A 1 227 ? -33.206 -14.243 8.115 1.00 31.81 ? 252 LYS A CD 1 ATOM 1772 C CE . LYS A 1 227 ? -34.180 -14.729 9.177 1.00 31.95 ? 252 LYS A CE 1 ATOM 1773 N NZ . LYS A 1 227 ? -33.470 -15.036 10.446 1.00 34.83 ? 252 LYS A NZ 1 ATOM 1774 N N . ASN A 1 228 ? -34.771 -18.328 5.395 1.00 24.58 ? 253 ASN A N 1 ATOM 1775 C CA . ASN A 1 228 ? -35.638 -19.315 4.777 1.00 25.25 ? 253 ASN A CA 1 ATOM 1776 C C . ASN A 1 228 ? -36.890 -19.443 5.620 1.00 22.99 ? 253 ASN A C 1 ATOM 1777 O O . ASN A 1 228 ? -36.867 -20.022 6.707 1.00 27.64 ? 253 ASN A O 1 ATOM 1778 C CB . ASN A 1 228 ? -34.912 -20.650 4.633 1.00 29.91 ? 253 ASN A CB 1 ATOM 1779 C CG . ASN A 1 228 ? -33.721 -20.554 3.705 1.00 39.31 ? 253 ASN A CG 1 ATOM 1780 O OD1 . ASN A 1 228 ? -33.870 -20.264 2.515 1.00 39.84 ? 253 ASN A OD1 1 ATOM 1781 N ND2 . ASN A 1 228 ? -32.527 -20.778 4.244 1.00 42.96 ? 253 ASN A ND2 1 ATOM 1782 N N . VAL A 1 229 ? -37.976 -18.866 5.119 1.00 23.19 ? 254 VAL A N 1 ATOM 1783 C CA . VAL A 1 229 ? -39.186 -18.694 5.905 1.00 24.11 ? 254 VAL A CA 1 ATOM 1784 C C . VAL A 1 229 ? -40.439 -19.009 5.100 1.00 24.13 ? 254 VAL A C 1 ATOM 1785 O O . VAL A 1 229 ? -40.369 -19.314 3.907 1.00 28.18 ? 254 VAL A O 1 ATOM 1786 C CB . VAL A 1 229 ? -39.290 -17.250 6.439 1.00 23.39 ? 254 VAL A CB 1 ATOM 1787 C CG1 . VAL A 1 229 ? -38.153 -16.960 7.413 1.00 25.71 ? 254 VAL A CG1 1 ATOM 1788 C CG2 . VAL A 1 229 ? -39.264 -16.251 5.287 1.00 27.13 ? 254 VAL A CG2 1 ATOM 1789 N N . ALA A 1 230 ? -41.584 -18.941 5.768 1.00 23.26 ? 255 ALA A N 1 ATOM 1790 C CA . ALA A 1 230 ? -42.875 -19.142 5.119 1.00 24.76 ? 255 ALA A CA 1 ATOM 1791 C C . ALA A 1 230 ? -43.486 -17.791 4.780 1.00 25.93 ? 255 ALA A C 1 ATOM 1792 O O . ALA A 1 230 ? -43.005 -16.758 5.239 1.00 23.11 ? 255 ALA A O 1 ATOM 1793 C CB . ALA A 1 230 ? -43.803 -19.934 6.018 1.00 29.47 ? 255 ALA A CB 1 ATOM 1794 N N . ILE A 1 231 ? -44.559 -17.795 3.996 1.00 23.15 ? 256 ILE A N 1 ATOM 1795 C CA . ILE A 1 231 ? -45.077 -16.546 3.446 1.00 22.38 ? 256 ILE A CA 1 ATOM 1796 C C . ILE A 1 231 ? -45.592 -15.549 4.498 1.00 25.54 ? 256 ILE A C 1 ATOM 1797 O O . ILE A 1 231 ? -45.461 -14.339 4.322 1.00 23.28 ? 256 ILE A O 1 ATOM 1798 C CB . ILE A 1 231 ? -46.134 -16.798 2.344 1.00 22.33 ? 256 ILE A CB 1 ATOM 1799 C CG1 . ILE A 1 231 ? -46.480 -15.499 1.622 1.00 22.05 ? 256 ILE A CG1 1 ATOM 1800 C CG2 . ILE A 1 231 ? -47.386 -17.440 2.922 1.00 23.80 ? 256 ILE A CG2 1 ATOM 1801 C CD1 . ILE A 1 231 ? -47.218 -15.715 0.310 1.00 22.37 ? 256 ILE A CD1 1 ATOM 1802 N N . ASP A 1 232 ? -46.161 -16.035 5.595 1.00 25.09 ? 257 ASP A N 1 ATOM 1803 C CA A ASP A 1 232 ? -46.651 -15.124 6.610 0.30 24.94 ? 257 ASP A CA 1 ATOM 1804 C CA B ASP A 1 232 ? -46.649 -15.142 6.653 0.70 25.05 ? 257 ASP A CA 1 ATOM 1805 C C . ASP A 1 232 ? -45.502 -14.312 7.205 1.00 22.84 ? 257 ASP A C 1 ATOM 1806 O O . ASP A 1 232 ? -45.590 -13.087 7.292 1.00 23.10 ? 257 ASP A O 1 ATOM 1807 C CB A ASP A 1 232 ? -47.445 -15.892 7.662 0.30 26.69 ? 257 ASP A CB 1 ATOM 1808 C CB B ASP A 1 232 ? -47.308 -15.918 7.803 0.70 25.41 ? 257 ASP A CB 1 ATOM 1809 C CG A ASP A 1 232 ? -48.585 -16.672 7.045 0.30 27.91 ? 257 ASP A CG 1 ATOM 1810 C CG B ASP A 1 232 ? -47.747 -15.003 8.957 0.70 30.43 ? 257 ASP A CG 1 ATOM 1811 O OD1 A ASP A 1 232 ? -48.840 -16.459 5.843 0.30 25.62 ? 257 ASP A OD1 1 ATOM 1812 O OD1 B ASP A 1 232 ? -48.783 -14.311 8.824 0.70 25.74 ? 257 ASP A OD1 1 ATOM 1813 O OD2 A ASP A 1 232 ? -49.217 -17.495 7.735 0.30 26.80 ? 257 ASP A OD2 1 ATOM 1814 O OD2 B ASP A 1 232 ? -47.063 -14.981 10.008 0.70 27.87 ? 257 ASP A OD2 1 ATOM 1815 N N . GLU A 1 233 ? -44.423 -14.991 7.586 1.00 23.43 ? 258 GLU A N 1 ATOM 1816 C CA . GLU A 1 233 ? -43.257 -14.310 8.137 1.00 22.19 ? 258 GLU A CA 1 ATOM 1817 C C . GLU A 1 233 ? -42.547 -13.463 7.084 1.00 19.91 ? 258 GLU A C 1 ATOM 1818 O O . GLU A 1 233 ? -42.132 -12.346 7.366 1.00 19.73 ? 258 GLU A O 1 ATOM 1819 C CB . GLU A 1 233 ? -42.270 -15.301 8.765 1.00 22.21 ? 258 GLU A CB 1 ATOM 1820 C CG . GLU A 1 233 ? -41.063 -14.612 9.379 1.00 22.92 ? 258 GLU A CG 1 ATOM 1821 C CD . GLU A 1 233 ? -40.188 -15.541 10.197 1.00 27.08 ? 258 GLU A CD 1 ATOM 1822 O OE1 . GLU A 1 233 ? -40.425 -16.765 10.175 1.00 28.54 ? 258 GLU A OE1 1 ATOM 1823 O OE2 . GLU A 1 233 ? -39.258 -15.039 10.863 1.00 28.33 ? 258 GLU A OE2 1 ATOM 1824 N N . ALA A 1 234 ? -42.407 -13.991 5.871 1.00 19.36 ? 259 ALA A N 1 ATOM 1825 C CA . ALA A 1 234 ? -41.773 -13.225 4.798 1.00 21.19 ? 259 ALA A CA 1 ATOM 1826 C C . ALA A 1 234 ? -42.530 -11.927 4.533 1.00 20.51 ? 259 ALA A C 1 ATOM 1827 O O . ALA A 1 234 ? -41.929 -10.880 4.302 1.00 18.41 ? 259 ALA A O 1 ATOM 1828 C CB . ALA A 1 234 ? -41.685 -14.050 3.527 1.00 20.98 ? 259 ALA A CB 1 ATOM 1829 N N . THR A 1 235 ? -43.857 -12.003 4.561 1.00 18.25 ? 260 THR A N 1 ATOM 1830 C CA . THR A 1 235 ? -44.685 -10.829 4.317 1.00 18.17 ? 260 THR A CA 1 ATOM 1831 C C . THR A 1 235 ? -44.484 -9.782 5.414 1.00 18.85 ? 260 THR A C 1 ATOM 1832 O O . THR A 1 235 ? -44.306 -8.595 5.127 1.00 19.52 ? 260 THR A O 1 ATOM 1833 C CB . THR A 1 235 ? -46.172 -11.217 4.183 1.00 19.32 ? 260 THR A CB 1 ATOM 1834 O OG1 . THR A 1 235 ? -46.336 -12.046 3.026 1.00 20.35 ? 260 THR A OG1 1 ATOM 1835 C CG2 . THR A 1 235 ? -47.042 -9.989 4.024 1.00 19.63 ? 260 THR A CG2 1 ATOM 1836 N N . SER A 1 236 ? -44.501 -10.213 6.672 1.00 17.51 ? 261 SER A N 1 ATOM 1837 C CA . SER A 1 236 ? -44.300 -9.262 7.764 1.00 19.85 ? 261 SER A CA 1 ATOM 1838 C C . SER A 1 236 ? -42.872 -8.694 7.791 1.00 18.03 ? 261 SER A C 1 ATOM 1839 O O . SER A 1 236 ? -42.650 -7.540 8.175 1.00 18.88 ? 261 SER A O 1 ATOM 1840 C CB . SER A 1 236 ? -44.684 -9.875 9.116 1.00 22.14 ? 261 SER A CB 1 ATOM 1841 O OG . SER A 1 236 ? -43.898 -11.010 9.407 1.00 26.59 ? 261 SER A OG 1 ATOM 1842 N N . LEU A 1 237 ? -41.902 -9.502 7.378 1.00 18.61 ? 262 LEU A N 1 ATOM 1843 C CA . LEU A 1 237 ? -40.528 -9.022 7.273 1.00 20.58 ? 262 LEU A CA 1 ATOM 1844 C C . LEU A 1 237 ? -40.418 -7.940 6.208 1.00 19.06 ? 262 LEU A C 1 ATOM 1845 O O . LEU A 1 237 ? -39.859 -6.876 6.457 1.00 18.81 ? 262 LEU A O 1 ATOM 1846 C CB . LEU A 1 237 ? -39.561 -10.162 6.963 1.00 20.05 ? 262 LEU A CB 1 ATOM 1847 C CG . LEU A 1 237 ? -39.190 -11.053 8.152 1.00 22.54 ? 262 LEU A CG 1 ATOM 1848 C CD1 . LEU A 1 237 ? -38.346 -12.233 7.691 1.00 23.53 ? 262 LEU A CD1 1 ATOM 1849 C CD2 . LEU A 1 237 ? -38.464 -10.259 9.238 1.00 22.35 ? 262 LEU A CD2 1 ATOM 1850 N N . LEU A 1 238 ? -40.945 -8.208 5.018 1.00 18.06 ? 263 LEU A N 1 ATOM 1851 C CA . LEU A 1 238 ? -40.857 -7.220 3.946 1.00 18.30 ? 263 LEU A CA 1 ATOM 1852 C C . LEU A 1 238 ? -41.659 -5.964 4.271 1.00 18.04 ? 263 LEU A C 1 ATOM 1853 O O . LEU A 1 238 ? -41.223 -4.851 3.983 1.00 18.00 ? 263 LEU A O 1 ATOM 1854 C CB . LEU A 1 238 ? -41.307 -7.809 2.605 1.00 17.93 ? 263 LEU A CB 1 ATOM 1855 C CG . LEU A 1 238 ? -40.407 -8.890 2.003 1.00 17.71 ? 263 LEU A CG 1 ATOM 1856 C CD1 . LEU A 1 238 ? -40.905 -9.286 0.630 1.00 21.68 ? 263 LEU A CD1 1 ATOM 1857 C CD2 . LEU A 1 238 ? -38.965 -8.430 1.925 1.00 21.01 ? 263 LEU A CD2 1 ATOM 1858 N N . HIS A 1 239 ? -42.831 -6.138 4.875 1.00 17.99 ? 264 HIS A N 1 ATOM 1859 C CA . HIS A 1 239 ? -43.669 -4.994 5.208 1.00 19.61 ? 264 HIS A CA 1 ATOM 1860 C C . HIS A 1 239 ? -42.990 -4.064 6.220 1.00 20.85 ? 264 HIS A C 1 ATOM 1861 O O . HIS A 1 239 ? -43.098 -2.840 6.113 1.00 20.47 ? 264 HIS A O 1 ATOM 1862 C CB . HIS A 1 239 ? -45.043 -5.433 5.719 1.00 19.30 ? 264 HIS A CB 1 ATOM 1863 C CG . HIS A 1 239 ? -45.955 -4.285 6.011 1.00 19.33 ? 264 HIS A CG 1 ATOM 1864 N ND1 . HIS A 1 239 ? -46.171 -3.812 7.288 1.00 24.33 ? 264 HIS A ND1 1 ATOM 1865 C CD2 . HIS A 1 239 ? -46.663 -3.479 5.185 1.00 20.17 ? 264 HIS A CD2 1 ATOM 1866 C CE1 . HIS A 1 239 ? -46.994 -2.780 7.236 1.00 26.56 ? 264 HIS A CE1 1 ATOM 1867 N NE2 . HIS A 1 239 ? -47.303 -2.554 5.972 1.00 26.02 ? 264 HIS A NE2 1 ATOM 1868 N N . LYS A 1 240 ? -42.289 -4.636 7.197 1.00 18.95 ? 265 LYS A N 1 ATOM 1869 C CA . LYS A 1 240 ? -41.541 -3.810 8.144 1.00 18.70 ? 265 LYS A CA 1 ATOM 1870 C C . LYS A 1 240 ? -40.251 -3.289 7.502 1.00 18.54 ? 265 LYS A C 1 ATOM 1871 O O . LYS A 1 240 ? -39.848 -2.141 7.732 1.00 18.52 ? 265 LYS A O 1 ATOM 1872 C CB . LYS A 1 240 ? -41.227 -4.570 9.439 1.00 20.40 ? 265 LYS A CB 1 ATOM 1873 C CG . LYS A 1 240 ? -40.338 -3.764 10.389 1.00 19.29 ? 265 LYS A CG 1 ATOM 1874 C CD . LYS A 1 240 ? -40.337 -4.319 11.810 1.00 23.77 ? 265 LYS A CD 1 ATOM 1875 C CE . LYS A 1 240 ? -39.430 -3.473 12.694 1.00 24.06 ? 265 LYS A CE 1 ATOM 1876 N NZ . LYS A 1 240 ? -39.440 -3.915 14.122 1.00 24.31 ? 265 LYS A NZ 1 ATOM 1877 N N . TRP A 1 241 ? -39.617 -4.128 6.684 1.00 17.71 ? 266 TRP A N 1 ATOM 1878 C CA . TRP A 1 241 ? -38.391 -3.728 5.996 1.00 19.26 ? 266 TRP A CA 1 ATOM 1879 C C . TRP A 1 241 ? -38.512 -2.360 5.323 1.00 18.69 ? 266 TRP A C 1 ATOM 1880 O O . TRP A 1 241 ? -37.591 -1.551 5.382 1.00 17.94 ? 266 TRP A O 1 ATOM 1881 C CB . TRP A 1 241 ? -37.937 -4.779 4.957 1.00 17.77 ? 266 TRP A CB 1 ATOM 1882 C CG . TRP A 1 241 ? -36.916 -4.183 4.035 1.00 18.18 ? 266 TRP A CG 1 ATOM 1883 C CD1 . TRP A 1 241 ? -35.576 -4.081 4.256 1.00 18.17 ? 266 TRP A CD1 1 ATOM 1884 C CD2 . TRP A 1 241 ? -37.171 -3.529 2.782 1.00 16.61 ? 266 TRP A CD2 1 ATOM 1885 N NE1 . TRP A 1 241 ? -34.970 -3.416 3.203 1.00 19.08 ? 266 TRP A NE1 1 ATOM 1886 C CE2 . TRP A 1 241 ? -35.931 -3.069 2.290 1.00 16.98 ? 266 TRP A CE2 1 ATOM 1887 C CE3 . TRP A 1 241 ? -38.328 -3.290 2.029 1.00 17.89 ? 266 TRP A CE3 1 ATOM 1888 C CZ2 . TRP A 1 241 ? -35.814 -2.385 1.079 1.00 17.60 ? 266 TRP A CZ2 1 ATOM 1889 C CZ3 . TRP A 1 241 ? -38.209 -2.610 0.823 1.00 19.36 ? 266 TRP A CZ3 1 ATOM 1890 C CH2 . TRP A 1 241 ? -36.959 -2.166 0.363 1.00 18.35 ? 266 TRP A CH2 1 ATOM 1891 N N . GLN A 1 242 ? -39.633 -2.103 4.659 1.00 17.65 ? 267 GLN A N 1 ATOM 1892 C CA . GLN A 1 242 ? -39.742 -0.862 3.894 1.00 20.39 ? 267 GLN A CA 1 ATOM 1893 C C . GLN A 1 242 ? -39.576 0.374 4.777 1.00 19.14 ? 267 GLN A C 1 ATOM 1894 O O . GLN A 1 242 ? -39.014 1.382 4.350 1.00 21.19 ? 267 GLN A O 1 ATOM 1895 C CB . GLN A 1 242 ? -41.066 -0.804 3.140 1.00 19.90 ? 267 GLN A CB 1 ATOM 1896 C CG . GLN A 1 242 ? -42.271 -0.588 4.037 1.00 19.39 ? 267 GLN A CG 1 ATOM 1897 C CD . GLN A 1 242 ? -43.557 -0.613 3.251 1.00 18.18 ? 267 GLN A CD 1 ATOM 1898 O OE1 . GLN A 1 242 ? -43.680 0.073 2.235 1.00 21.54 ? 267 GLN A OE1 1 ATOM 1899 N NE2 . GLN A 1 242 ? -44.529 -1.404 3.710 1.00 18.63 ? 267 GLN A NE2 1 ATOM 1900 N N . PHE A 1 243 ? -40.058 0.296 6.012 1.00 18.20 ? 268 PHE A N 1 ATOM 1901 C CA . PHE A 1 243 ? -39.963 1.439 6.911 1.00 20.63 ? 268 PHE A CA 1 ATOM 1902 C C . PHE A 1 243 ? -38.549 1.559 7.471 1.00 24.72 ? 268 PHE A C 1 ATOM 1903 O O . PHE A 1 243 ? -37.967 2.650 7.483 1.00 24.07 ? 268 PHE A O 1 ATOM 1904 C CB . PHE A 1 243 ? -41.018 1.348 8.021 1.00 20.54 ? 268 PHE A CB 1 ATOM 1905 C CG . PHE A 1 243 ? -42.430 1.295 7.501 1.00 21.37 ? 268 PHE A CG 1 ATOM 1906 C CD1 . PHE A 1 243 ? -43.025 2.423 6.958 1.00 24.07 ? 268 PHE A CD1 1 ATOM 1907 C CD2 . PHE A 1 243 ? -43.156 0.113 7.537 1.00 20.76 ? 268 PHE A CD2 1 ATOM 1908 C CE1 . PHE A 1 243 ? -44.327 2.375 6.470 1.00 25.29 ? 268 PHE A CE1 1 ATOM 1909 C CE2 . PHE A 1 243 ? -44.451 0.058 7.044 1.00 22.78 ? 268 PHE A CE2 1 ATOM 1910 C CZ . PHE A 1 243 ? -45.036 1.191 6.511 1.00 23.40 ? 268 PHE A CZ 1 ATOM 1911 N N . VAL A 1 244 ? -37.991 0.436 7.915 1.00 20.10 ? 269 VAL A N 1 ATOM 1912 C CA . VAL A 1 244 ? -36.614 0.421 8.407 1.00 19.53 ? 269 VAL A CA 1 ATOM 1913 C C . VAL A 1 244 ? -35.652 0.972 7.350 1.00 20.09 ? 269 VAL A C 1 ATOM 1914 O O . VAL A 1 244 ? -34.840 1.850 7.639 1.00 22.36 ? 269 VAL A O 1 ATOM 1915 C CB . VAL A 1 244 ? -36.183 -1.001 8.829 1.00 19.98 ? 269 VAL A CB 1 ATOM 1916 C CG1 . VAL A 1 244 ? -34.708 -1.019 9.230 1.00 21.36 ? 269 VAL A CG1 1 ATOM 1917 C CG2 . VAL A 1 244 ? -37.072 -1.514 9.963 1.00 24.06 ? 269 VAL A CG2 1 ATOM 1918 N N . ALA A 1 245 ? -35.770 0.476 6.121 1.00 18.68 ? 270 ALA A N 1 ATOM 1919 C CA . ALA A 1 245 ? -34.879 0.869 5.025 1.00 19.11 ? 270 ALA A CA 1 ATOM 1920 C C . ALA A 1 245 ? -34.866 2.361 4.693 1.00 23.77 ? 270 ALA A C 1 ATOM 1921 O O . ALA A 1 245 ? -33.800 2.961 4.560 1.00 25.61 ? 270 ALA A O 1 ATOM 1922 C CB . ALA A 1 245 ? -35.208 0.072 3.779 1.00 20.41 ? 270 ALA A CB 1 ATOM 1923 N N . GLU A 1 246 ? -36.043 2.953 4.527 1.00 21.19 ? 271 GLU A N 1 ATOM 1924 C CA A GLU A 1 246 ? -36.127 4.361 4.160 0.55 23.97 ? 271 GLU A CA 1 ATOM 1925 C CA B GLU A 1 246 ? -36.140 4.362 4.163 0.45 23.95 ? 271 GLU A CA 1 ATOM 1926 C C . GLU A 1 246 ? -35.741 5.260 5.328 1.00 22.33 ? 271 GLU A C 1 ATOM 1927 O O . GLU A 1 246 ? -35.198 6.349 5.130 1.00 24.48 ? 271 GLU A O 1 ATOM 1928 C CB A GLU A 1 246 ? -37.532 4.726 3.667 0.55 25.91 ? 271 GLU A CB 1 ATOM 1929 C CB B GLU A 1 246 ? -37.563 4.695 3.700 0.45 25.85 ? 271 GLU A CB 1 ATOM 1930 C CG A GLU A 1 246 ? -37.659 6.191 3.253 0.55 24.71 ? 271 GLU A CG 1 ATOM 1931 C CG B GLU A 1 246 ? -37.723 6.079 3.072 0.45 26.55 ? 271 GLU A CG 1 ATOM 1932 C CD A GLU A 1 246 ? -39.093 6.636 3.028 0.55 22.12 ? 271 GLU A CD 1 ATOM 1933 C CD B GLU A 1 246 ? -37.827 7.197 4.097 0.45 28.52 ? 271 GLU A CD 1 ATOM 1934 O OE1 A GLU A 1 246 ? -40.009 5.788 3.079 0.55 24.83 ? 271 GLU A OE1 1 ATOM 1935 O OE1 B GLU A 1 246 ? -38.170 6.914 5.265 0.45 28.04 ? 271 GLU A OE1 1 ATOM 1936 O OE2 A GLU A 1 246 ? -39.305 7.845 2.799 0.55 26.27 ? 271 GLU A OE2 1 ATOM 1937 O OE2 B GLU A 1 246 ? -37.567 8.363 3.732 0.45 39.49 ? 271 GLU A OE2 1 ATOM 1938 N N . GLU A 1 247 ? -36.017 4.798 6.543 1.00 20.49 ? 272 GLU A N 1 ATOM 1939 C CA . GLU A 1 247 ? -35.791 5.617 7.724 1.00 20.72 ? 272 GLU A CA 1 ATOM 1940 C C . GLU A 1 247 ? -34.399 5.526 8.359 1.00 22.72 ? 272 GLU A C 1 ATOM 1941 O O . GLU A 1 247 ? -34.035 6.390 9.156 1.00 27.80 ? 272 GLU A O 1 ATOM 1942 C CB . GLU A 1 247 ? -36.871 5.330 8.772 1.00 24.76 ? 272 GLU A CB 1 ATOM 1943 C CG . GLU A 1 247 ? -38.288 5.568 8.261 1.00 29.36 ? 272 GLU A CG 1 ATOM 1944 C CD . GLU A 1 247 ? -39.344 4.873 9.108 1.00 39.70 ? 272 GLU A CD 1 ATOM 1945 O OE1 . GLU A 1 247 ? -39.002 4.366 10.198 1.00 49.01 ? 272 GLU A OE1 1 ATOM 1946 O OE2 . GLU A 1 247 ? -40.517 4.832 8.682 1.00 44.86 ? 272 GLU A OE2 1 ATOM 1947 N N . LEU A 1 248 ? -33.632 4.490 8.023 1.00 23.77 ? 273 LEU A N 1 ATOM 1948 C CA . LEU A 1 248 ? -32.289 4.341 8.582 1.00 24.96 ? 273 LEU A CA 1 ATOM 1949 C C . LEU A 1 248 ? -31.480 5.612 8.372 1.00 21.77 ? 273 LEU A C 1 ATOM 1950 O O . LEU A 1 248 ? -31.624 6.286 7.350 1.00 24.29 ? 273 LEU A O 1 ATOM 1951 C CB . LEU A 1 248 ? -31.554 3.163 7.937 1.00 22.27 ? 273 LEU A CB 1 ATOM 1952 C CG . LEU A 1 248 ? -31.788 1.756 8.489 1.00 21.72 ? 273 LEU A CG 1 ATOM 1953 C CD1 . LEU A 1 248 ? -31.317 0.740 7.476 1.00 21.20 ? 273 LEU A CD1 1 ATOM 1954 C CD2 . LEU A 1 248 ? -31.059 1.559 9.807 1.00 21.46 ? 273 LEU A CD2 1 ATOM 1955 N N . GLU A 1 249 ? -30.622 5.944 9.332 1.00 21.14 ? 274 GLU A N 1 ATOM 1956 C CA . GLU A 1 249 ? -29.681 7.036 9.125 1.00 20.46 ? 274 GLU A CA 1 ATOM 1957 C C . GLU A 1 249 ? -28.797 6.740 7.918 1.00 19.67 ? 274 GLU A C 1 ATOM 1958 O O . GLU A 1 249 ? -28.642 5.582 7.514 1.00 20.39 ? 274 GLU A O 1 ATOM 1959 C CB . GLU A 1 249 ? -28.835 7.281 10.380 1.00 22.47 ? 274 GLU A CB 1 ATOM 1960 C CG . GLU A 1 249 ? -29.638 7.804 11.563 1.00 34.81 ? 274 GLU A CG 1 ATOM 1961 C CD . GLU A 1 249 ? -28.830 7.847 12.844 1.00 64.12 ? 274 GLU A CD 1 ATOM 1962 O OE1 . GLU A 1 249 ? -27.799 7.145 12.923 1.00 74.22 ? 274 GLU A OE1 1 ATOM 1963 O OE2 . GLU A 1 249 ? -29.230 8.580 13.775 1.00 72.45 ? 274 GLU A OE2 1 ATOM 1964 N N . GLU A 1 250 ? -28.210 7.786 7.344 1.00 19.97 ? 275 GLU A N 1 ATOM 1965 C CA . GLU A 1 250 ? -27.482 7.646 6.078 1.00 19.41 ? 275 GLU A CA 1 ATOM 1966 C C . GLU A 1 250 ? -26.269 6.710 6.132 1.00 19.89 ? 275 GLU A C 1 ATOM 1967 O O . GLU A 1 250 ? -25.797 6.252 5.090 1.00 21.14 ? 275 GLU A O 1 ATOM 1968 C CB . GLU A 1 250 ? -27.064 9.016 5.545 1.00 24.25 ? 275 GLU A CB 1 ATOM 1969 C CG . GLU A 1 250 ? -26.027 9.706 6.391 1.00 23.11 ? 275 GLU A CG 1 ATOM 1970 C CD . GLU A 1 250 ? -25.558 11.017 5.787 1.00 31.75 ? 275 GLU A CD 1 ATOM 1971 O OE1 . GLU A 1 250 ? -26.372 11.690 5.120 1.00 37.45 ? 275 GLU A OE1 1 ATOM 1972 O OE2 . GLU A 1 250 ? -24.379 11.367 5.991 1.00 33.76 ? 275 GLU A OE2 1 ATOM 1973 N N . ASP A 1 251 ? -25.762 6.433 7.332 1.00 18.16 ? 276 ASP A N 1 ATOM 1974 C CA . ASP A 1 251 ? -24.616 5.539 7.489 1.00 17.91 ? 276 ASP A CA 1 ATOM 1975 C C . ASP A 1 251 ? -24.995 4.058 7.425 1.00 19.59 ? 276 ASP A C 1 ATOM 1976 O O . ASP A 1 251 ? -24.148 3.194 7.662 1.00 19.26 ? 276 ASP A O 1 ATOM 1977 C CB . ASP A 1 251 ? -23.905 5.813 8.819 1.00 20.85 ? 276 ASP A CB 1 ATOM 1978 C CG . ASP A 1 251 ? -22.984 7.016 8.758 1.00 27.90 ? 276 ASP A CG 1 ATOM 1979 O OD1 . ASP A 1 251 ? -22.719 7.512 7.647 1.00 25.69 ? 276 ASP A OD1 1 ATOM 1980 O OD2 . ASP A 1 251 ? -22.509 7.459 9.827 1.00 30.41 ? 276 ASP A OD2 1 ATOM 1981 N N . PHE A 1 252 ? -26.257 3.765 7.112 1.00 19.07 ? 277 PHE A N 1 ATOM 1982 C CA . PHE A 1 252 ? -26.725 2.382 7.011 1.00 17.26 ? 277 PHE A CA 1 ATOM 1983 C C . PHE A 1 252 ? -27.502 2.161 5.727 1.00 18.26 ? 277 PHE A C 1 ATOM 1984 O O . PHE A 1 252 ? -28.219 3.051 5.267 1.00 19.79 ? 277 PHE A O 1 ATOM 1985 C CB . PHE A 1 252 ? -27.663 2.018 8.173 1.00 18.20 ? 277 PHE A CB 1 ATOM 1986 C CG . PHE A 1 252 ? -27.065 2.193 9.538 1.00 20.52 ? 277 PHE A CG 1 ATOM 1987 C CD1 . PHE A 1 252 ? -26.606 1.099 10.259 1.00 28.39 ? 277 PHE A CD1 1 ATOM 1988 C CD2 . PHE A 1 252 ? -26.994 3.445 10.117 1.00 23.76 ? 277 PHE A CD2 1 ATOM 1989 C CE1 . PHE A 1 252 ? -26.069 1.268 11.533 1.00 25.32 ? 277 PHE A CE1 1 ATOM 1990 C CE2 . PHE A 1 252 ? -26.455 3.618 11.385 1.00 28.84 ? 277 PHE A CE2 1 ATOM 1991 C CZ . PHE A 1 252 ? -25.993 2.525 12.087 1.00 30.04 ? 277 PHE A CZ 1 ATOM 1992 N N . THR A 1 253 ? -27.382 0.961 5.172 1.00 15.63 ? 278 THR A N 1 ATOM 1993 C CA . THR A 1 253 ? -28.247 0.525 4.081 1.00 17.75 ? 278 THR A CA 1 ATOM 1994 C C . THR A 1 253 ? -28.693 -0.905 4.355 1.00 18.30 ? 278 THR A C 1 ATOM 1995 O O . THR A 1 253 ? -27.878 -1.756 4.721 1.00 18.85 ? 278 THR A O 1 ATOM 1996 C CB . THR A 1 253 ? -27.531 0.582 2.721 1.00 17.01 ? 278 THR A CB 1 ATOM 1997 O OG1 . THR A 1 253 ? -27.216 1.944 2.404 1.00 22.81 ? 278 THR A OG1 1 ATOM 1998 C CG2 . THR A 1 253 ? -28.408 0.010 1.617 1.00 18.24 ? 278 THR A CG2 1 ATOM 1999 N N . LEU A 1 254 ? -29.987 -1.165 4.191 1.00 15.56 ? 279 LEU A N 1 ATOM 2000 C CA . LEU A 1 254 ? -30.510 -2.529 4.253 1.00 16.49 ? 279 LEU A CA 1 ATOM 2001 C C . LEU A 1 254 ? -31.335 -2.799 3.015 1.00 16.58 ? 279 LEU A C 1 ATOM 2002 O O . LEU A 1 254 ? -32.380 -2.182 2.810 1.00 16.34 ? 279 LEU A O 1 ATOM 2003 C CB . LEU A 1 254 ? -31.382 -2.731 5.496 1.00 17.09 ? 279 LEU A CB 1 ATOM 2004 C CG . LEU A 1 254 ? -31.975 -4.136 5.635 1.00 18.30 ? 279 LEU A CG 1 ATOM 2005 C CD1 . LEU A 1 254 ? -30.895 -5.218 5.703 1.00 19.16 ? 279 LEU A CD1 1 ATOM 2006 C CD2 . LEU A 1 254 ? -32.880 -4.210 6.872 1.00 20.60 ? 279 LEU A CD2 1 ATOM 2007 N N . SER A 1 255 ? -30.869 -3.733 2.194 1.00 14.19 ? 280 SER A N 1 ATOM 2008 C CA . SER A 1 255 ? -31.560 -4.086 0.956 1.00 16.90 ? 280 SER A CA 1 ATOM 2009 C C . SER A 1 255 ? -31.901 -5.567 0.927 1.00 16.49 ? 280 SER A C 1 ATOM 2010 O O . SER A 1 255 ? -31.406 -6.337 1.756 1.00 18.35 ? 280 SER A O 1 ATOM 2011 C CB . SER A 1 255 ? -30.695 -3.703 -0.238 1.00 19.59 ? 280 SER A CB 1 ATOM 2012 O OG . SER A 1 255 ? -30.534 -2.292 -0.267 1.00 20.96 ? 280 SER A OG 1 ATOM 2013 N N . VAL A 1 256 ? -32.755 -5.975 -0.010 1.00 16.49 ? 281 VAL A N 1 ATOM 2014 C CA . VAL A 1 256 ? -33.224 -7.360 -0.045 1.00 16.88 ? 281 VAL A CA 1 ATOM 2015 C C . VAL A 1 256 ? -33.242 -7.940 -1.455 1.00 21.27 ? 281 VAL A C 1 ATOM 2016 O O . VAL A 1 256 ? -33.638 -7.271 -2.414 1.00 21.21 ? 281 VAL A O 1 ATOM 2017 C CB . VAL A 1 256 ? -34.656 -7.490 0.523 1.00 19.24 ? 281 VAL A CB 1 ATOM 2018 C CG1 . VAL A 1 256 ? -35.029 -8.962 0.746 1.00 21.56 ? 281 VAL A CG1 1 ATOM 2019 C CG2 . VAL A 1 256 ? -34.797 -6.701 1.815 1.00 20.96 ? 281 VAL A CG2 1 ATOM 2020 N N . LEU A 1 257 ? -32.805 -9.187 -1.569 1.00 18.91 ? 282 LEU A N 1 ATOM 2021 C CA . LEU A 1 257 ? -33.085 -10.007 -2.744 1.00 21.74 ? 282 LEU A CA 1 ATOM 2022 C C . LEU A 1 257 ? -34.049 -11.098 -2.304 1.00 21.99 ? 282 LEU A C 1 ATOM 2023 O O . LEU A 1 257 ? -33.842 -11.726 -1.268 1.00 23.55 ? 282 LEU A O 1 ATOM 2024 C CB . LEU A 1 257 ? -31.802 -10.634 -3.283 1.00 23.34 ? 282 LEU A CB 1 ATOM 2025 C CG . LEU A 1 257 ? -30.802 -9.672 -3.920 1.00 26.82 ? 282 LEU A CG 1 ATOM 2026 C CD1 . LEU A 1 257 ? -29.464 -10.363 -4.140 1.00 32.71 ? 282 LEU A CD1 1 ATOM 2027 C CD2 . LEU A 1 257 ? -31.360 -9.159 -5.237 1.00 36.22 ? 282 LEU A CD2 1 ATOM 2028 N N . GLY A 1 258 ? -35.110 -11.329 -3.070 1.00 20.80 ? 283 GLY A N 1 ATOM 2029 C CA . GLY A 1 258 ? -36.115 -12.284 -2.640 1.00 20.61 ? 283 GLY A CA 1 ATOM 2030 C C . GLY A 1 258 ? -36.674 -13.171 -3.735 1.00 19.85 ? 283 GLY A C 1 ATOM 2031 O O . GLY A 1 258 ? -36.733 -12.777 -4.897 1.00 21.23 ? 283 GLY A O 1 ATOM 2032 N N . GLY A 1 259 ? -37.094 -14.371 -3.349 1.00 19.60 ? 284 GLY A N 1 ATOM 2033 C CA . GLY A 1 259 ? -37.691 -15.317 -4.272 1.00 19.08 ? 284 GLY A CA 1 ATOM 2034 C C . GLY A 1 259 ? -38.403 -16.408 -3.498 1.00 20.33 ? 284 GLY A C 1 ATOM 2035 O O . GLY A 1 259 ? -38.415 -16.403 -2.266 1.00 22.56 ? 284 GLY A O 1 ATOM 2036 N N . ALA A 1 260 ? -39.012 -17.351 -4.204 1.00 21.03 ? 285 ALA A N 1 ATOM 2037 C CA . ALA A 1 260 ? -39.721 -18.417 -3.520 1.00 21.31 ? 285 ALA A CA 1 ATOM 2038 C C . ALA A 1 260 ? -39.949 -19.623 -4.414 1.00 24.19 ? 285 ALA A C 1 ATOM 2039 O O . ALA A 1 260 ? -39.676 -19.589 -5.609 1.00 26.55 ? 285 ALA A O 1 ATOM 2040 C CB . ALA A 1 260 ? -41.055 -17.906 -2.974 1.00 23.29 ? 285 ALA A CB 1 ATOM 2041 N N . ASP A 1 261 ? -40.462 -20.685 -3.812 1.00 24.22 ? 286 ASP A N 1 ATOM 2042 C CA . ASP A 1 261 ? -40.808 -21.896 -4.541 1.00 28.25 ? 286 ASP A CA 1 ATOM 2043 C C . ASP A 1 261 ? -41.813 -22.644 -3.686 1.00 31.00 ? 286 ASP A C 1 ATOM 2044 O O . ASP A 1 261 ? -41.451 -23.235 -2.666 1.00 28.09 ? 286 ASP A O 1 ATOM 2045 C CB . ASP A 1 261 ? -39.565 -22.754 -4.783 1.00 30.11 ? 286 ASP A CB 1 ATOM 2046 C CG . ASP A 1 261 ? -39.843 -23.957 -5.675 1.00 33.27 ? 286 ASP A CG 1 ATOM 2047 O OD1 . ASP A 1 261 ? -41.025 -24.316 -5.865 1.00 35.87 ? 286 ASP A OD1 1 ATOM 2048 O OD2 . ASP A 1 261 ? -38.870 -24.548 -6.188 1.00 39.03 ? 286 ASP A OD2 1 ATOM 2049 N N . GLU A 1 262 ? -43.077 -22.592 -4.096 1.00 28.19 ? 287 GLU A N 1 ATOM 2050 C CA . GLU A 1 262 ? -44.174 -23.123 -3.293 1.00 26.02 ? 287 GLU A CA 1 ATOM 2051 C C . GLU A 1 262 ? -44.119 -22.573 -1.865 1.00 29.96 ? 287 GLU A C 1 ATOM 2052 O O . GLU A 1 262 ? -44.137 -21.358 -1.676 1.00 30.15 ? 287 GLU A O 1 ATOM 2053 C CB . GLU A 1 262 ? -44.198 -24.649 -3.341 1.00 31.76 ? 287 GLU A CB 1 ATOM 2054 C CG . GLU A 1 262 ? -44.368 -25.173 -4.759 1.00 33.92 ? 287 GLU A CG 1 ATOM 2055 C CD . GLU A 1 262 ? -44.560 -26.676 -4.819 1.00 52.16 ? 287 GLU A CD 1 ATOM 2056 O OE1 . GLU A 1 262 ? -45.014 -27.263 -3.814 1.00 56.91 ? 287 GLU A OE1 1 ATOM 2057 O OE2 . GLU A 1 262 ? -44.261 -27.268 -5.877 1.00 58.35 ? 287 GLU A OE2 1 ATOM 2058 N N . LYS A 1 263 ? -44.039 -23.440 -0.862 1.00 28.89 ? 288 LYS A N 1 ATOM 2059 C CA . LYS A 1 263 ? -44.087 -22.964 0.525 1.00 26.91 ? 288 LYS A CA 1 ATOM 2060 C C . LYS A 1 263 ? -42.795 -22.321 1.022 1.00 29.26 ? 288 LYS A C 1 ATOM 2061 O O . LYS A 1 263 ? -42.783 -21.670 2.068 1.00 28.70 ? 288 LYS A O 1 ATOM 2062 C CB . LYS A 1 263 ? -44.489 -24.088 1.479 1.00 29.19 ? 288 LYS A CB 1 ATOM 2063 C CG . LYS A 1 263 ? -45.984 -24.365 1.534 1.00 42.52 ? 288 LYS A CG 1 ATOM 2064 C CD . LYS A 1 263 ? -46.487 -25.008 0.256 1.00 59.94 ? 288 LYS A CD 1 ATOM 2065 C CE . LYS A 1 263 ? -47.788 -25.757 0.500 1.00 67.46 ? 288 LYS A CE 1 ATOM 2066 N NZ . LYS A 1 263 ? -47.612 -26.833 1.516 1.00 70.25 ? 288 LYS A NZ 1 ATOM 2067 N N . GLN A 1 264 ? -41.707 -22.505 0.287 1.00 27.26 ? 289 GLN A N 1 ATOM 2068 C CA . GLN A 1 264 ? -40.420 -21.991 0.733 1.00 29.39 ? 289 GLN A CA 1 ATOM 2069 C C . GLN A 1 264 ? -40.124 -20.610 0.165 1.00 26.21 ? 289 GLN A C 1 ATOM 2070 O O . GLN A 1 264 ? -40.046 -20.434 -1.050 1.00 27.13 ? 289 GLN A O 1 ATOM 2071 C CB . GLN A 1 264 ? -39.301 -22.963 0.362 1.00 32.06 ? 289 GLN A CB 1 ATOM 2072 C CG . GLN A 1 264 ? -39.426 -24.321 1.040 1.00 38.38 ? 289 GLN A CG 1 ATOM 2073 C CD . GLN A 1 264 ? -38.300 -25.267 0.672 1.00 59.59 ? 289 GLN A CD 1 ATOM 2074 O OE1 . GLN A 1 264 ? -38.006 -25.477 -0.506 1.00 65.09 ? 289 GLN A OE1 1 ATOM 2075 N NE2 . GLN A 1 264 ? -37.665 -25.851 1.683 1.00 67.19 ? 289 GLN A NE2 1 ATOM 2076 N N . VAL A 1 265 ? -39.958 -19.631 1.048 1.00 25.00 ? 290 VAL A N 1 ATOM 2077 C CA . VAL A 1 265 ? -39.554 -18.294 0.631 1.00 23.79 ? 290 VAL A CA 1 ATOM 2078 C C . VAL A 1 265 ? -38.130 -18.036 1.090 1.00 23.06 ? 290 VAL A C 1 ATOM 2079 O O . VAL A 1 265 ? -37.749 -18.410 2.199 1.00 25.81 ? 290 VAL A O 1 ATOM 2080 C CB . VAL A 1 265 ? -40.463 -17.211 1.232 1.00 23.35 ? 290 VAL A CB 1 ATOM 2081 C CG1 . VAL A 1 265 ? -39.998 -15.818 0.800 1.00 25.56 ? 290 VAL A CG1 1 ATOM 2082 C CG2 . VAL A 1 265 ? -41.914 -17.460 0.833 1.00 28.39 ? 290 VAL A CG2 1 ATOM 2083 N N . TRP A 1 266 ? -37.335 -17.405 0.235 1.00 23.49 ? 291 TRP A N 1 ATOM 2084 C CA . TRP A 1 266 ? -35.997 -16.986 0.626 1.00 22.45 ? 291 TRP A CA 1 ATOM 2085 C C . TRP A 1 266 ? -35.859 -15.473 0.502 1.00 21.85 ? 291 TRP A C 1 ATOM 2086 O O . TRP A 1 266 ? -36.234 -14.891 -0.514 1.00 22.76 ? 291 TRP A O 1 ATOM 2087 C CB . TRP A 1 266 ? -34.920 -17.713 -0.193 1.00 23.33 ? 291 TRP A CB 1 ATOM 2088 C CG . TRP A 1 266 ? -34.985 -17.481 -1.682 1.00 26.56 ? 291 TRP A CG 1 ATOM 2089 C CD1 . TRP A 1 266 ? -35.647 -18.243 -2.602 1.00 27.56 ? 291 TRP A CD1 1 ATOM 2090 C CD2 . TRP A 1 266 ? -34.341 -16.433 -2.419 1.00 23.94 ? 291 TRP A CD2 1 ATOM 2091 N NE1 . TRP A 1 266 ? -35.468 -17.725 -3.864 1.00 25.37 ? 291 TRP A NE1 1 ATOM 2092 C CE2 . TRP A 1 266 ? -34.672 -16.615 -3.779 1.00 23.47 ? 291 TRP A CE2 1 ATOM 2093 C CE3 . TRP A 1 266 ? -33.531 -15.347 -2.061 1.00 24.84 ? 291 TRP A CE3 1 ATOM 2094 C CZ2 . TRP A 1 266 ? -34.218 -15.757 -4.780 1.00 23.20 ? 291 TRP A CZ2 1 ATOM 2095 C CZ3 . TRP A 1 266 ? -33.077 -14.500 -3.059 1.00 26.78 ? 291 TRP A CZ3 1 ATOM 2096 C CH2 . TRP A 1 266 ? -33.421 -14.710 -4.401 1.00 25.27 ? 291 TRP A CH2 1 ATOM 2097 N N . LEU A 1 267 ? -35.335 -14.844 1.551 1.00 19.85 ? 292 LEU A N 1 ATOM 2098 C CA . LEU A 1 267 ? -35.034 -13.419 1.549 1.00 20.63 ? 292 LEU A CA 1 ATOM 2099 C C . LEU A 1 267 ? -33.580 -13.220 1.935 1.00 22.37 ? 292 LEU A C 1 ATOM 2100 O O . LEU A 1 267 ? -33.193 -13.491 3.071 1.00 22.17 ? 292 LEU A O 1 ATOM 2101 C CB . LEU A 1 267 ? -35.922 -12.672 2.548 1.00 18.88 ? 292 LEU A CB 1 ATOM 2102 C CG . LEU A 1 267 ? -37.434 -12.806 2.394 1.00 21.09 ? 292 LEU A CG 1 ATOM 2103 C CD1 . LEU A 1 267 ? -38.169 -12.097 3.531 1.00 23.50 ? 292 LEU A CD1 1 ATOM 2104 C CD2 . LEU A 1 267 ? -37.874 -12.258 1.043 1.00 21.86 ? 292 LEU A CD2 1 ATOM 2105 N N . THR A 1 268 ? -32.770 -12.762 0.990 1.00 18.32 ? 293 THR A N 1 ATOM 2106 C CA . THR A 1 268 ? -31.375 -12.451 1.279 1.00 18.65 ? 293 THR A CA 1 ATOM 2107 C C . THR A 1 268 ? -31.248 -10.994 1.705 1.00 20.23 ? 293 THR A C 1 ATOM 2108 O O . THR A 1 268 ? -31.490 -10.075 0.918 1.00 20.63 ? 293 THR A O 1 ATOM 2109 C CB . THR A 1 268 ? -30.470 -12.727 0.069 1.00 21.84 ? 293 THR A CB 1 ATOM 2110 O OG1 . THR A 1 268 ? -30.575 -14.107 -0.288 1.00 22.95 ? 293 THR A OG1 1 ATOM 2111 C CG2 . THR A 1 268 ? -29.015 -12.416 0.407 1.00 21.89 ? 293 THR A CG2 1 ATOM 2112 N N . MET A 1 269 ? -30.880 -10.794 2.965 1.00 18.20 ? 294 MET A N 1 ATOM 2113 C CA . MET A 1 269 ? -30.758 -9.461 3.528 1.00 16.30 ? 294 MET A CA 1 ATOM 2114 C C . MET A 1 269 ? -29.336 -8.979 3.343 1.00 17.82 ? 294 MET A C 1 ATOM 2115 O O . MET A 1 269 ? -28.391 -9.647 3.768 1.00 19.18 ? 294 MET A O 1 ATOM 2116 C CB . MET A 1 269 ? -31.073 -9.480 5.025 1.00 19.78 ? 294 MET A CB 1 ATOM 2117 C CG . MET A 1 269 ? -32.363 -10.176 5.398 1.00 23.94 ? 294 MET A CG 1 ATOM 2118 S SD . MET A 1 269 ? -33.797 -9.477 4.575 1.00 27.37 ? 294 MET A SD 1 ATOM 2119 C CE . MET A 1 269 ? -33.712 -7.785 5.093 1.00 20.05 ? 294 MET A CE 1 ATOM 2120 N N . LEU A 1 270 ? -29.196 -7.824 2.703 1.00 15.19 ? 295 LEU A N 1 ATOM 2121 C CA . LEU A 1 270 ? -27.898 -7.229 2.417 1.00 16.67 ? 295 LEU A CA 1 ATOM 2122 C C . LEU A 1 270 ? -27.737 -5.969 3.243 1.00 16.67 ? 295 LEU A C 1 ATOM 2123 O O . LEU A 1 270 ? -28.433 -4.975 3.021 1.00 17.80 ? 295 LEU A O 1 ATOM 2124 C CB . LEU A 1 270 ? -27.802 -6.873 0.935 1.00 18.16 ? 295 LEU A CB 1 ATOM 2125 C CG . LEU A 1 270 ? -28.004 -8.038 -0.033 1.00 20.13 ? 295 LEU A CG 1 ATOM 2126 C CD1 . LEU A 1 270 ? -28.184 -7.528 -1.460 1.00 25.16 ? 295 LEU A CD1 1 ATOM 2127 C CD2 . LEU A 1 270 ? -26.838 -8.998 0.052 1.00 21.92 ? 295 LEU A CD2 1 ATOM 2128 N N . GLY A 1 271 ? -26.818 -6.005 4.201 1.00 17.12 ? 296 GLY A N 1 ATOM 2129 C CA . GLY A 1 271 ? -26.626 -4.879 5.098 1.00 18.47 ? 296 GLY A CA 1 ATOM 2130 C C . GLY A 1 271 ? -25.254 -4.245 4.986 1.00 17.15 ? 296 GLY A C 1 ATOM 2131 O O . GLY A 1 271 ? -24.250 -4.935 4.788 1.00 19.06 ? 296 GLY A O 1 ATOM 2132 N N . PHE A 1 272 ? -25.215 -2.921 5.124 1.00 18.10 ? 297 PHE A N 1 ATOM 2133 C CA . PHE A 1 272 ? -23.971 -2.163 5.061 1.00 16.85 ? 297 PHE A CA 1 ATOM 2134 C C . PHE A 1 272 ? -24.015 -1.074 6.117 1.00 18.15 ? 297 PHE A C 1 ATOM 2135 O O . PHE A 1 272 ? -25.005 -0.343 6.224 1.00 20.58 ? 297 PHE A O 1 ATOM 2136 C CB . PHE A 1 272 ? -23.791 -1.537 3.667 1.00 18.65 ? 297 PHE A CB 1 ATOM 2137 C CG . PHE A 1 272 ? -22.516 -0.742 3.501 1.00 18.98 ? 297 PHE A CG 1 ATOM 2138 C CD1 . PHE A 1 272 ? -21.390 -1.332 2.941 1.00 19.56 ? 297 PHE A CD1 1 ATOM 2139 C CD2 . PHE A 1 272 ? -22.453 0.596 3.870 1.00 21.11 ? 297 PHE A CD2 1 ATOM 2140 C CE1 . PHE A 1 272 ? -20.217 -0.617 2.778 1.00 23.33 ? 297 PHE A CE1 1 ATOM 2141 C CE2 . PHE A 1 272 ? -21.280 1.320 3.706 1.00 21.99 ? 297 PHE A CE2 1 ATOM 2142 C CZ . PHE A 1 272 ? -20.163 0.709 3.158 1.00 20.64 ? 297 PHE A CZ 1 ATOM 2143 N N . HIS A 1 273 ? -22.950 -0.972 6.907 1.00 16.96 ? 298 HIS A N 1 ATOM 2144 C CA . HIS A 1 273 ? -22.788 0.144 7.823 1.00 19.21 ? 298 HIS A CA 1 ATOM 2145 C C . HIS A 1 273 ? -21.421 0.792 7.671 1.00 16.25 ? 298 HIS A C 1 ATOM 2146 O O . HIS A 1 273 ? -20.394 0.108 7.628 1.00 17.63 ? 298 HIS A O 1 ATOM 2147 C CB . HIS A 1 273 ? -23.006 -0.282 9.278 1.00 19.27 ? 298 HIS A CB 1 ATOM 2148 C CG . HIS A 1 273 ? -22.700 0.801 10.269 1.00 19.61 ? 298 HIS A CG 1 ATOM 2149 N ND1 . HIS A 1 273 ? -23.284 2.050 10.213 1.00 18.38 ? 298 HIS A ND1 1 ATOM 2150 C CD2 . HIS A 1 273 ? -21.858 0.829 11.330 1.00 19.19 ? 298 HIS A CD2 1 ATOM 2151 C CE1 . HIS A 1 273 ? -22.817 2.798 11.197 1.00 23.81 ? 298 HIS A CE1 1 ATOM 2152 N NE2 . HIS A 1 273 ? -21.953 2.080 11.891 1.00 24.96 ? 298 HIS A NE2 1 ATOM 2153 N N . PHE A 1 274 ? -21.446 2.121 7.579 1.00 17.79 ? 299 PHE A N 1 ATOM 2154 C CA A PHE A 1 274 ? -20.232 2.939 7.530 0.47 17.95 ? 299 PHE A CA 1 ATOM 2155 C CA B PHE A 1 274 ? -20.273 2.979 7.527 0.53 19.79 ? 299 PHE A CA 1 ATOM 2156 C C . PHE A 1 274 ? -19.616 3.049 8.913 1.00 20.20 ? 299 PHE A C 1 ATOM 2157 O O . PHE A 1 274 ? -19.558 4.128 9.508 1.00 22.83 ? 299 PHE A O 1 ATOM 2158 C CB A PHE A 1 274 ? -20.542 4.353 7.046 0.47 20.75 ? 299 PHE A CB 1 ATOM 2159 C CB B PHE A 1 274 ? -20.777 4.372 7.124 0.53 23.63 ? 299 PHE A CB 1 ATOM 2160 C CG A PHE A 1 274 ? -20.798 4.460 5.576 0.47 19.08 ? 299 PHE A CG 1 ATOM 2161 C CG B PHE A 1 274 ? -19.750 5.260 6.478 0.53 19.33 ? 299 PHE A CG 1 ATOM 2162 C CD1 A PHE A 1 274 ? -19.755 4.687 4.690 0.47 17.78 ? 299 PHE A CD1 1 ATOM 2163 C CD1 B PHE A 1 274 ? -19.483 5.170 5.120 0.53 20.48 ? 299 PHE A CD1 1 ATOM 2164 C CD2 A PHE A 1 274 ? -22.084 4.368 5.081 0.47 18.56 ? 299 PHE A CD2 1 ATOM 2165 C CD2 B PHE A 1 274 ? -19.105 6.238 7.217 0.53 18.34 ? 299 PHE A CD2 1 ATOM 2166 C CE1 A PHE A 1 274 ? -19.991 4.802 3.340 0.47 16.26 ? 299 PHE A CE1 1 ATOM 2167 C CE1 B PHE A 1 274 ? -18.556 6.010 4.524 0.53 22.18 ? 299 PHE A CE1 1 ATOM 2168 C CE2 A PHE A 1 274 ? -22.326 4.484 3.729 0.47 18.21 ? 299 PHE A CE2 1 ATOM 2169 C CE2 B PHE A 1 274 ? -18.177 7.079 6.627 0.53 24.41 ? 299 PHE A CE2 1 ATOM 2170 C CZ A PHE A 1 274 ? -21.279 4.700 2.858 0.47 17.07 ? 299 PHE A CZ 1 ATOM 2171 C CZ B PHE A 1 274 ? -17.905 6.965 5.279 0.53 26.91 ? 299 PHE A CZ 1 ATOM 2172 N N . GLY A 1 275 ? -19.151 1.921 9.433 1.00 18.94 ? 300 GLY A N 1 ATOM 2173 C CA . GLY A 1 275 ? -18.591 1.888 10.773 1.00 20.15 ? 300 GLY A CA 1 ATOM 2174 C C . GLY A 1 275 ? -18.454 0.471 11.292 1.00 21.72 ? 300 GLY A C 1 ATOM 2175 O O . GLY A 1 275 ? -18.540 -0.487 10.525 1.00 19.68 ? 300 GLY A O 1 ATOM 2176 N N . LEU A 1 276 ? -18.247 0.352 12.602 1.00 24.60 ? 301 LEU A N 1 ATOM 2177 C CA . LEU A 1 276 ? -17.942 -0.923 13.249 1.00 23.14 ? 301 LEU A CA 1 ATOM 2178 C C . LEU A 1 276 ? -19.175 -1.726 13.666 1.00 22.80 ? 301 LEU A C 1 ATOM 2179 O O . LEU A 1 276 ? -20.297 -1.213 13.681 1.00 22.66 ? 301 LEU A O 1 ATOM 2180 C CB . LEU A 1 276 ? -17.026 -0.691 14.454 1.00 21.62 ? 301 LEU A CB 1 ATOM 2181 C CG . LEU A 1 276 ? -15.685 -0.048 14.098 1.00 27.08 ? 301 LEU A CG 1 ATOM 2182 C CD1 . LEU A 1 276 ? -14.879 0.257 15.358 1.00 34.88 ? 301 LEU A CD1 1 ATOM 2183 C CD2 . LEU A 1 276 ? -14.894 -0.937 13.151 1.00 30.21 ? 301 LEU A CD2 1 ATOM 2184 N N . LYS A 1 277 ? -18.952 -2.988 14.023 1.00 20.76 ? 302 LYS A N 1 ATOM 2185 C CA . LYS A 1 277 ? -20.051 -3.943 14.144 1.00 23.12 ? 302 LYS A CA 1 ATOM 2186 C C . LYS A 1 277 ? -20.892 -3.762 15.405 1.00 22.60 ? 302 LYS A C 1 ATOM 2187 O O . LYS A 1 277 ? -22.068 -4.126 15.425 1.00 23.61 ? 302 LYS A O 1 ATOM 2188 C CB . LYS A 1 277 ? -19.537 -5.385 14.036 1.00 27.37 ? 302 LYS A CB 1 ATOM 2189 C CG . LYS A 1 277 ? -18.723 -5.858 15.229 1.00 34.24 ? 302 LYS A CG 1 ATOM 2190 C CD . LYS A 1 277 ? -18.001 -7.166 14.924 1.00 44.91 ? 302 LYS A CD 1 ATOM 2191 C CE . LYS A 1 277 ? -18.954 -8.238 14.417 1.00 47.82 ? 302 LYS A CE 1 ATOM 2192 N NZ . LYS A 1 277 ? -19.939 -8.663 15.450 1.00 55.21 ? 302 LYS A NZ 1 ATOM 2193 N N . THR A 1 278 ? -20.292 -3.205 16.453 1.00 24.52 ? 303 THR A N 1 ATOM 2194 C CA . THR A 1 278 ? -21.033 -2.923 17.675 1.00 24.45 ? 303 THR A CA 1 ATOM 2195 C C . THR A 1 278 ? -22.199 -1.975 17.401 1.00 24.25 ? 303 THR A C 1 ATOM 2196 O O . THR A 1 278 ? -23.334 -2.238 17.801 1.00 25.27 ? 303 THR A O 1 ATOM 2197 C CB . THR A 1 278 ? -20.116 -2.335 18.759 1.00 29.80 ? 303 THR A CB 1 ATOM 2198 O OG1 . THR A 1 278 ? -19.378 -1.235 18.214 1.00 46.60 ? 303 THR A OG1 1 ATOM 2199 C CG2 . THR A 1 278 ? -19.144 -3.391 19.241 1.00 32.01 ? 303 THR A CG2 1 ATOM 2200 N N . VAL A 1 279 ? -21.910 -0.878 16.707 1.00 25.24 ? 304 VAL A N 1 ATOM 2201 C CA . VAL A 1 279 ? -22.938 0.086 16.338 1.00 24.63 ? 304 VAL A CA 1 ATOM 2202 C C . VAL A 1 279 ? -23.910 -0.522 15.333 1.00 24.20 ? 304 VAL A C 1 ATOM 2203 O O . VAL A 1 279 ? -25.121 -0.331 15.429 1.00 24.44 ? 304 VAL A O 1 ATOM 2204 C CB . VAL A 1 279 ? -22.322 1.381 15.756 1.00 27.53 ? 304 VAL A CB 1 ATOM 2205 C CG1 . VAL A 1 279 ? -23.410 2.284 15.193 1.00 29.23 ? 304 VAL A CG1 1 ATOM 2206 C CG2 . VAL A 1 279 ? -21.517 2.114 16.825 1.00 30.80 ? 304 VAL A CG2 1 ATOM 2207 N N . ALA A 1 280 ? -23.379 -1.261 14.365 1.00 23.05 ? 305 ALA A N 1 ATOM 2208 C CA . ALA A 1 280 ? -24.225 -1.897 13.367 1.00 21.80 ? 305 ALA A CA 1 ATOM 2209 C C . ALA A 1 280 ? -25.280 -2.792 14.018 1.00 21.09 ? 305 ALA A C 1 ATOM 2210 O O . ALA A 1 280 ? -26.478 -2.683 13.727 1.00 21.21 ? 305 ALA A O 1 ATOM 2211 C CB . ALA A 1 280 ? -23.381 -2.697 12.386 1.00 21.64 ? 305 ALA A CB 1 ATOM 2212 N N . LYS A 1 281 ? -24.836 -3.669 14.913 1.00 21.15 ? 306 LYS A N 1 ATOM 2213 C CA . LYS A 1 281 ? -25.752 -4.619 15.532 1.00 22.96 ? 306 LYS A CA 1 ATOM 2214 C C . LYS A 1 281 ? -26.701 -3.943 16.522 1.00 24.03 ? 306 LYS A C 1 ATOM 2215 O O . LYS A 1 281 ? -27.865 -4.310 16.618 1.00 23.27 ? 306 LYS A O 1 ATOM 2216 C CB . LYS A 1 281 ? -24.996 -5.767 16.205 1.00 26.51 ? 306 LYS A CB 1 ATOM 2217 C CG . LYS A 1 281 ? -25.928 -6.825 16.774 1.00 30.66 ? 306 LYS A CG 1 ATOM 2218 C CD . LYS A 1 281 ? -25.185 -8.078 17.193 1.00 32.19 ? 306 LYS A CD 1 ATOM 2219 C CE . LYS A 1 281 ? -26.161 -9.162 17.629 1.00 36.09 ? 306 LYS A CE 1 ATOM 2220 N NZ . LYS A 1 281 ? -26.944 -8.755 18.834 1.00 36.08 ? 306 LYS A NZ 1 ATOM 2221 N N . SER A 1 282 ? -26.200 -2.953 17.253 1.00 24.83 ? 307 SER A N 1 ATOM 2222 C CA . SER A 1 282 ? -27.050 -2.198 18.162 1.00 24.94 ? 307 SER A CA 1 ATOM 2223 C C . SER A 1 282 ? -28.237 -1.589 17.411 1.00 22.04 ? 307 SER A C 1 ATOM 2224 O O . SER A 1 282 ? -29.379 -1.631 17.877 1.00 25.77 ? 307 SER A O 1 ATOM 2225 C CB . SER A 1 282 ? -26.236 -1.102 18.858 1.00 27.28 ? 307 SER A CB 1 ATOM 2226 O OG . SER A 1 282 ? -27.047 -0.370 19.760 1.00 43.70 ? 307 SER A OG 1 ATOM 2227 N N . THR A 1 283 ? -27.965 -1.060 16.223 1.00 23.88 ? 308 THR A N 1 ATOM 2228 C CA . THR A 1 283 ? -28.991 -0.407 15.417 1.00 22.95 ? 308 THR A CA 1 ATOM 2229 C C . THR A 1 283 ? -30.050 -1.379 14.893 1.00 23.07 ? 308 THR A C 1 ATOM 2230 O O . THR A 1 283 ? -31.250 -1.103 14.960 1.00 22.50 ? 308 THR A O 1 ATOM 2231 C CB . THR A 1 283 ? -28.359 0.362 14.237 1.00 22.83 ? 308 THR A CB 1 ATOM 2232 O OG1 . THR A 1 283 ? -27.613 1.477 14.745 1.00 28.43 ? 308 THR A OG1 1 ATOM 2233 C CG2 . THR A 1 283 ? -29.439 0.869 13.285 1.00 29.35 ? 308 THR A CG2 1 ATOM 2234 N N . PHE A 1 284 ? -29.614 -2.520 14.368 1.00 20.63 ? 309 PHE A N 1 ATOM 2235 C CA . PHE A 1 284 ? -30.576 -3.490 13.853 1.00 21.03 ? 309 PHE A CA 1 ATOM 2236 C C . PHE A 1 284 ? -31.291 -4.267 14.963 1.00 23.59 ? 309 PHE A C 1 ATOM 2237 O O . PHE A 1 284 ? -32.436 -4.688 14.792 1.00 24.25 ? 309 PHE A O 1 ATOM 2238 C CB . PHE A 1 284 ? -29.921 -4.403 12.814 1.00 22.07 ? 309 PHE A CB 1 ATOM 2239 C CG . PHE A 1 284 ? -29.624 -3.700 11.518 1.00 20.22 ? 309 PHE A CG 1 ATOM 2240 C CD1 . PHE A 1 284 ? -30.663 -3.325 10.681 1.00 21.50 ? 309 PHE A CD1 1 ATOM 2241 C CD2 . PHE A 1 284 ? -28.326 -3.378 11.157 1.00 19.33 ? 309 PHE A CD2 1 ATOM 2242 C CE1 . PHE A 1 284 ? -30.419 -2.663 9.498 1.00 21.53 ? 309 PHE A CE1 1 ATOM 2243 C CE2 . PHE A 1 284 ? -28.073 -2.715 9.960 1.00 23.14 ? 309 PHE A CE2 1 ATOM 2244 C CZ . PHE A 1 284 ? -29.126 -2.359 9.134 1.00 20.51 ? 309 PHE A CZ 1 ATOM 2245 N N . ASP A 1 285 ? -30.629 -4.423 16.109 1.00 24.16 ? 310 ASP A N 1 ATOM 2246 C CA . ASP A 1 285 ? -31.285 -5.008 17.278 1.00 23.71 ? 310 ASP A CA 1 ATOM 2247 C C . ASP A 1 285 ? -32.460 -4.126 17.699 1.00 27.58 ? 310 ASP A C 1 ATOM 2248 O O . ASP A 1 285 ? -33.531 -4.620 18.048 1.00 27.82 ? 310 ASP A O 1 ATOM 2249 C CB . ASP A 1 285 ? -30.307 -5.149 18.448 1.00 26.36 ? 310 ASP A CB 1 ATOM 2250 C CG . ASP A 1 285 ? -29.391 -6.366 18.326 1.00 28.28 ? 310 ASP A CG 1 ATOM 2251 O OD1 . ASP A 1 285 ? -29.568 -7.187 17.404 1.00 27.94 ? 310 ASP A OD1 1 ATOM 2252 O OD2 . ASP A 1 285 ? -28.487 -6.501 19.174 1.00 30.09 ? 310 ASP A OD2 1 ATOM 2253 N N . LEU A 1 286 ? -32.247 -2.814 17.663 1.00 23.59 ? 311 LEU A N 1 ATOM 2254 C CA . LEU A 1 286 ? -33.281 -1.848 18.020 1.00 24.32 ? 311 LEU A CA 1 ATOM 2255 C C . LEU A 1 286 ? -34.392 -1.774 16.973 1.00 25.22 ? 311 LEU A C 1 ATOM 2256 O O . LEU A 1 286 ? -35.576 -1.886 17.293 1.00 26.37 ? 311 LEU A O 1 ATOM 2257 C CB . LEU A 1 286 ? -32.668 -0.454 18.199 1.00 28.12 ? 311 LEU A CB 1 ATOM 2258 C CG . LEU A 1 286 ? -33.657 0.699 18.399 1.00 30.91 ? 311 LEU A CG 1 ATOM 2259 C CD1 . LEU A 1 286 ? -34.383 0.565 19.733 1.00 33.92 ? 311 LEU A CD1 1 ATOM 2260 C CD2 . LEU A 1 286 ? -32.966 2.051 18.306 1.00 35.94 ? 311 LEU A CD2 1 ATOM 2261 N N . LEU A 1 287 ? -34.000 -1.596 15.716 1.00 22.26 ? 312 LEU A N 1 ATOM 2262 C CA . LEU A 1 287 ? -34.955 -1.276 14.664 1.00 22.69 ? 312 LEU A CA 1 ATOM 2263 C C . LEU A 1 287 ? -35.589 -2.484 13.974 1.00 20.85 ? 312 LEU A C 1 ATOM 2264 O O . LEU A 1 287 ? -36.688 -2.378 13.437 1.00 24.50 ? 312 LEU A O 1 ATOM 2265 C CB . LEU A 1 287 ? -34.293 -0.382 13.612 1.00 21.14 ? 312 LEU A CB 1 ATOM 2266 C CG . LEU A 1 287 ? -33.752 0.957 14.109 1.00 27.46 ? 312 LEU A CG 1 ATOM 2267 C CD1 . LEU A 1 287 ? -33.104 1.726 12.965 1.00 27.73 ? 312 LEU A CD1 1 ATOM 2268 C CD2 . LEU A 1 287 ? -34.869 1.771 14.755 1.00 29.48 ? 312 LEU A CD2 1 ATOM 2269 N N . PHE A 1 288 ? -34.905 -3.623 13.981 1.00 22.69 ? 313 PHE A N 1 ATOM 2270 C CA . PHE A 1 288 ? -35.376 -4.773 13.210 1.00 22.71 ? 313 PHE A CA 1 ATOM 2271 C C . PHE A 1 288 ? -34.986 -6.092 13.869 1.00 23.44 ? 313 PHE A C 1 ATOM 2272 O O . PHE A 1 288 ? -34.326 -6.927 13.255 1.00 22.65 ? 313 PHE A O 1 ATOM 2273 C CB . PHE A 1 288 ? -34.796 -4.720 11.791 1.00 18.53 ? 313 PHE A CB 1 ATOM 2274 C CG . PHE A 1 288 ? -35.706 -5.276 10.724 1.00 20.18 ? 313 PHE A CG 1 ATOM 2275 C CD1 . PHE A 1 288 ? -35.402 -5.078 9.384 1.00 20.76 ? 313 PHE A CD1 1 ATOM 2276 C CD2 . PHE A 1 288 ? -36.863 -5.970 11.047 1.00 19.79 ? 313 PHE A CD2 1 ATOM 2277 C CE1 . PHE A 1 288 ? -36.215 -5.569 8.384 1.00 19.98 ? 313 PHE A CE1 1 ATOM 2278 C CE2 . PHE A 1 288 ? -37.698 -6.468 10.046 1.00 21.67 ? 313 PHE A CE2 1 ATOM 2279 C CZ . PHE A 1 288 ? -37.371 -6.265 8.711 1.00 18.72 ? 313 PHE A CZ 1 ATOM 2280 N N . PRO A 1 289 ? -35.387 -6.291 15.130 1.00 22.75 ? 314 PRO A N 1 ATOM 2281 C CA . PRO A 1 289 ? -34.997 -7.531 15.807 1.00 19.55 ? 314 PRO A CA 1 ATOM 2282 C C . PRO A 1 289 ? -35.623 -8.764 15.163 1.00 22.28 ? 314 PRO A C 1 ATOM 2283 O O . PRO A 1 289 ? -35.114 -9.870 15.357 1.00 24.15 ? 314 PRO A O 1 ATOM 2284 C CB . PRO A 1 289 ? -35.560 -7.337 17.222 1.00 22.66 ? 314 PRO A CB 1 ATOM 2285 C CG . PRO A 1 289 ? -36.671 -6.337 17.041 1.00 23.91 ? 314 PRO A CG 1 ATOM 2286 C CD . PRO A 1 289 ? -36.111 -5.384 16.034 1.00 24.06 ? 314 PRO A CD 1 ATOM 2287 N N . GLU A 1 290 ? -36.699 -8.562 14.405 1.00 21.90 ? 315 GLU A N 1 ATOM 2288 C CA . GLU A 1 290 ? -37.397 -9.645 13.721 1.00 23.94 ? 315 GLU A CA 1 ATOM 2289 C C . GLU A 1 290 ? -36.520 -10.363 12.698 1.00 24.74 ? 315 GLU A C 1 ATOM 2290 O O . GLU A 1 290 ? -36.806 -11.501 12.329 1.00 26.79 ? 315 GLU A O 1 ATOM 2291 C CB . GLU A 1 290 ? -38.664 -9.123 13.035 1.00 28.03 ? 315 GLU A CB 1 ATOM 2292 C CG . GLU A 1 290 ? -39.745 -8.631 13.989 1.00 26.79 ? 315 GLU A CG 1 ATOM 2293 C CD . GLU A 1 290 ? -39.556 -7.184 14.428 1.00 28.44 ? 315 GLU A CD 1 ATOM 2294 O OE1 . GLU A 1 290 ? -38.538 -6.558 14.066 1.00 24.73 ? 315 GLU A OE1 1 ATOM 2295 O OE2 . GLU A 1 290 ? -40.445 -6.669 15.140 1.00 31.53 ? 315 GLU A OE2 1 ATOM 2296 N N . LEU A 1 291 ? -35.469 -9.694 12.231 1.00 22.02 ? 316 LEU A N 1 ATOM 2297 C CA . LEU A 1 291 ? -34.530 -10.308 11.296 1.00 23.79 ? 316 LEU A CA 1 ATOM 2298 C C . LEU A 1 291 ? -33.788 -11.475 11.931 1.00 25.77 ? 316 LEU A C 1 ATOM 2299 O O . LEU A 1 291 ? -33.318 -12.376 11.235 1.00 29.57 ? 316 LEU A O 1 ATOM 2300 C CB . LEU A 1 291 ? -33.511 -9.283 10.796 1.00 27.75 ? 316 LEU A CB 1 ATOM 2301 C CG . LEU A 1 291 ? -33.957 -8.347 9.681 1.00 30.23 ? 316 LEU A CG 1 ATOM 2302 C CD1 . LEU A 1 291 ? -32.790 -7.473 9.252 1.00 31.49 ? 316 LEU A CD1 1 ATOM 2303 C CD2 . LEU A 1 291 ? -34.501 -9.155 8.505 1.00 28.51 ? 316 LEU A CD2 1 ATOM 2304 N N . GLY A 1 292 ? -33.668 -11.448 13.254 1.00 24.60 ? 317 GLY A N 1 ATOM 2305 C CA . GLY A 1 292 ? -32.986 -12.509 13.971 1.00 27.75 ? 317 GLY A CA 1 ATOM 2306 C C . GLY A 1 292 ? -31.517 -12.643 13.612 1.00 27.99 ? 317 GLY A C 1 ATOM 2307 O O . GLY A 1 292 ? -30.992 -13.753 13.531 1.00 31.76 ? 317 GLY A O 1 ATOM 2308 N N . LEU A 1 293 ? -30.849 -11.515 13.395 1.00 25.95 ? 318 LEU A N 1 ATOM 2309 C CA . LEU A 1 293 ? -29.417 -11.526 13.108 1.00 25.16 ? 318 LEU A CA 1 ATOM 2310 C C . LEU A 1 293 ? -28.630 -11.792 14.381 1.00 31.34 ? 318 LEU A C 1 ATOM 2311 O O . LEU A 1 293 ? -29.033 -11.372 15.467 1.00 33.71 ? 318 LEU A O 1 ATOM 2312 C CB . LEU A 1 293 ? -28.976 -10.201 12.488 1.00 24.11 ? 318 LEU A CB 1 ATOM 2313 C CG . LEU A 1 293 ? -29.712 -9.767 11.222 1.00 24.26 ? 318 LEU A CG 1 ATOM 2314 C CD1 . LEU A 1 293 ? -29.142 -8.464 10.676 1.00 24.64 ? 318 LEU A CD1 1 ATOM 2315 C CD2 . LEU A 1 293 ? -29.663 -10.867 10.167 1.00 32.28 ? 318 LEU A CD2 1 ATOM 2316 N N . VAL A 1 294 ? -27.514 -12.499 14.244 1.00 27.40 ? 319 VAL A N 1 ATOM 2317 C CA . VAL A 1 294 ? -26.654 -12.802 15.380 1.00 26.75 ? 319 VAL A CA 1 ATOM 2318 C C . VAL A 1 294 ? -25.271 -12.194 15.164 1.00 25.40 ? 319 VAL A C 1 ATOM 2319 O O . VAL A 1 294 ? -24.934 -11.773 14.055 1.00 24.38 ? 319 VAL A O 1 ATOM 2320 C CB . VAL A 1 294 ? -26.524 -14.323 15.605 1.00 32.28 ? 319 VAL A CB 1 ATOM 2321 C CG1 . VAL A 1 294 ? -27.891 -14.932 15.883 1.00 40.92 ? 319 VAL A CG1 1 ATOM 2322 C CG2 . VAL A 1 294 ? -25.877 -14.987 14.399 1.00 35.27 ? 319 VAL A CG2 1 ATOM 2323 N N . GLU A 1 295 ? -24.471 -12.142 16.225 1.00 27.01 ? 320 GLU A N 1 ATOM 2324 C CA . GLU A 1 295 ? -23.158 -11.517 16.152 1.00 30.59 ? 320 GLU A CA 1 ATOM 2325 C C . GLU A 1 295 ? -22.339 -12.036 14.974 1.00 27.52 ? 320 GLU A C 1 ATOM 2326 O O . GLU A 1 295 ? -21.688 -11.259 14.278 1.00 24.95 ? 320 GLU A O 1 ATOM 2327 C CB . GLU A 1 295 ? -22.393 -11.711 17.464 1.00 33.74 ? 320 GLU A CB 1 ATOM 2328 C CG . GLU A 1 295 ? -23.071 -11.066 18.660 1.00 43.56 ? 320 GLU A CG 1 ATOM 2329 C CD . GLU A 1 295 ? -22.192 -11.046 19.892 1.00 57.00 ? 320 GLU A CD 1 ATOM 2330 O OE1 . GLU A 1 295 ? -21.075 -11.606 19.840 1.00 60.11 ? 320 GLU A OE1 1 ATOM 2331 O OE2 . GLU A 1 295 ? -22.619 -10.467 20.912 1.00 61.35 ? 320 GLU A OE2 1 ATOM 2332 N N . GLU A 1 296 ? -22.390 -13.344 14.742 1.00 26.73 ? 321 GLU A N 1 ATOM 2333 C CA . GLU A 1 296 ? -21.583 -13.963 13.693 1.00 24.00 ? 321 GLU A CA 1 ATOM 2334 C C . GLU A 1 296 ? -22.020 -13.568 12.284 1.00 21.47 ? 321 GLU A C 1 ATOM 2335 O O . GLU A 1 296 ? -21.312 -13.835 11.313 1.00 26.50 ? 321 GLU A O 1 ATOM 2336 C CB . GLU A 1 296 ? -21.589 -15.490 13.834 1.00 32.11 ? 321 GLU A CB 1 ATOM 2337 C CG . GLU A 1 296 ? -20.859 -16.005 15.072 1.00 41.06 ? 321 GLU A CG 1 ATOM 2338 C CD . GLU A 1 296 ? -21.610 -15.723 16.363 1.00 51.69 ? 321 GLU A CD 1 ATOM 2339 O OE1 . GLU A 1 296 ? -20.949 -15.583 17.415 1.00 59.71 ? 321 GLU A OE1 1 ATOM 2340 O OE2 . GLU A 1 296 ? -22.857 -15.639 16.328 1.00 40.60 ? 321 GLU A OE2 1 ATOM 2341 N N . ASP A 1 297 ? -23.187 -12.939 12.170 1.00 23.18 ? 322 ASP A N 1 ATOM 2342 C CA . ASP A 1 297 ? -23.664 -12.464 10.871 1.00 23.81 ? 322 ASP A CA 1 ATOM 2343 C C . ASP A 1 297 ? -22.954 -11.185 10.433 1.00 23.43 ? 322 ASP A C 1 ATOM 2344 O O . ASP A 1 297 ? -22.830 -10.910 9.236 1.00 24.77 ? 322 ASP A O 1 ATOM 2345 C CB . ASP A 1 297 ? -25.171 -12.207 10.909 1.00 20.86 ? 322 ASP A CB 1 ATOM 2346 C CG . ASP A 1 297 ? -25.984 -13.484 10.976 1.00 26.12 ? 322 ASP A CG 1 ATOM 2347 O OD1 . ASP A 1 297 ? -25.534 -14.516 10.431 1.00 27.31 ? 322 ASP A OD1 1 ATOM 2348 O OD2 . ASP A 1 297 ? -27.081 -13.450 11.570 1.00 27.90 ? 322 ASP A OD2 1 ATOM 2349 N N . TYR A 1 298 ? -22.504 -10.399 11.406 1.00 22.24 ? 323 TYR A N 1 ATOM 2350 C CA . TYR A 1 298 ? -21.857 -9.118 11.134 1.00 20.45 ? 323 TYR A CA 1 ATOM 2351 C C . TYR A 1 298 ? -20.361 -9.281 10.892 1.00 20.67 ? 323 TYR A C 1 ATOM 2352 O O . TYR A 1 298 ? -19.624 -9.752 11.768 1.00 22.72 ? 323 TYR A O 1 ATOM 2353 C CB . TYR A 1 298 ? -22.078 -8.147 12.295 1.00 21.82 ? 323 TYR A CB 1 ATOM 2354 C CG . TYR A 1 298 ? -23.517 -7.739 12.511 1.00 22.58 ? 323 TYR A CG 1 ATOM 2355 C CD1 . TYR A 1 298 ? -24.002 -6.541 12.003 1.00 19.80 ? 323 TYR A CD1 1 ATOM 2356 C CD2 . TYR A 1 298 ? -24.386 -8.544 13.237 1.00 22.62 ? 323 TYR A CD2 1 ATOM 2357 C CE1 . TYR A 1 298 ? -25.312 -6.160 12.204 1.00 17.38 ? 323 TYR A CE1 1 ATOM 2358 C CE2 . TYR A 1 298 ? -25.699 -8.170 13.447 1.00 20.76 ? 323 TYR A CE2 1 ATOM 2359 C CZ . TYR A 1 298 ? -26.157 -6.977 12.927 1.00 19.35 ? 323 TYR A CZ 1 ATOM 2360 O OH . TYR A 1 298 ? -27.463 -6.597 13.130 1.00 25.95 ? 323 TYR A OH 1 ATOM 2361 N N . LEU A 1 299 ? -19.912 -8.878 9.708 1.00 19.46 ? 324 LEU A N 1 ATOM 2362 C CA . LEU A 1 299 ? -18.506 -8.999 9.351 1.00 22.63 ? 324 LEU A CA 1 ATOM 2363 C C . LEU A 1 299 ? -17.876 -7.633 9.112 1.00 19.29 ? 324 LEU A C 1 ATOM 2364 O O . LEU A 1 299 ? -18.396 -6.820 8.341 1.00 19.70 ? 324 LEU A O 1 ATOM 2365 C CB . LEU A 1 299 ? -18.343 -9.865 8.102 1.00 21.36 ? 324 LEU A CB 1 ATOM 2366 C CG . LEU A 1 299 ? -18.966 -11.262 8.177 1.00 27.76 ? 324 LEU A CG 1 ATOM 2367 C CD1 . LEU A 1 299 ? -18.735 -12.012 6.873 1.00 35.34 ? 324 LEU A CD1 1 ATOM 2368 C CD2 . LEU A 1 299 ? -18.407 -12.040 9.352 1.00 37.18 ? 324 LEU A CD2 1 ATOM 2369 N N . GLU A 1 300 ? -16.748 -7.392 9.773 1.00 19.15 ? 325 GLU A N 1 ATOM 2370 C CA . GLU A 1 300 ? -15.969 -6.176 9.565 1.00 18.50 ? 325 GLU A CA 1 ATOM 2371 C C . GLU A 1 300 ? -14.907 -6.432 8.511 1.00 17.04 ? 325 GLU A C 1 ATOM 2372 O O . GLU A 1 300 ? -14.173 -7.421 8.574 1.00 20.97 ? 325 GLU A O 1 ATOM 2373 C CB . GLU A 1 300 ? -15.308 -5.726 10.873 1.00 20.15 ? 325 GLU A CB 1 ATOM 2374 C CG . GLU A 1 300 ? -16.296 -5.187 11.893 1.00 26.49 ? 325 GLU A CG 1 ATOM 2375 C CD . GLU A 1 300 ? -15.624 -4.717 13.167 1.00 29.76 ? 325 GLU A CD 1 ATOM 2376 O OE1 . GLU A 1 300 ? -14.459 -5.098 13.408 1.00 31.17 ? 325 GLU A OE1 1 ATOM 2377 O OE2 . GLU A 1 300 ? -16.265 -3.963 13.929 1.00 25.38 ? 325 GLU A OE2 1 ATOM 2378 N N . MET A 1 301 ? -14.823 -5.534 7.538 1.00 19.26 ? 326 MET A N 1 ATOM 2379 C CA . MET A 1 301 ? -13.879 -5.696 6.442 1.00 19.40 ? 326 MET A CA 1 ATOM 2380 C C . MET A 1 301 ? -13.628 -4.348 5.771 1.00 17.40 ? 326 MET A C 1 ATOM 2381 O O . MET A 1 301 ? -14.277 -3.349 6.094 1.00 18.08 ? 326 MET A O 1 ATOM 2382 C CB . MET A 1 301 ? -14.400 -6.725 5.429 1.00 17.77 ? 326 MET A CB 1 ATOM 2383 C CG . MET A 1 301 ? -15.704 -6.339 4.736 1.00 17.49 ? 326 MET A CG 1 ATOM 2384 S SD . MET A 1 301 ? -16.411 -7.649 3.680 1.00 18.84 ? 326 MET A SD 1 ATOM 2385 C CE . MET A 1 301 ? -16.968 -8.796 4.945 1.00 18.20 ? 326 MET A CE 1 ATOM 2386 N N . SER A 1 302 ? -12.675 -4.302 4.847 1.00 17.25 ? 327 SER A N 1 ATOM 2387 C CA . SER A 1 302 ? -12.417 -3.057 4.129 1.00 17.51 ? 327 SER A CA 1 ATOM 2388 C C . SER A 1 302 ? -13.589 -2.720 3.205 1.00 16.14 ? 327 SER A C 1 ATOM 2389 O O . SER A 1 302 ? -14.410 -3.588 2.880 1.00 17.22 ? 327 SER A O 1 ATOM 2390 C CB . SER A 1 302 ? -11.132 -3.165 3.310 1.00 19.00 ? 327 SER A CB 1 ATOM 2391 O OG . SER A 1 302 ? -11.326 -3.998 2.172 1.00 18.40 ? 327 SER A OG 1 ATOM 2392 N N . TRP A 1 303 ? -13.673 -1.464 2.777 1.00 15.89 ? 328 TRP A N 1 ATOM 2393 C CA . TRP A 1 303 ? -14.708 -1.092 1.812 1.00 16.34 ? 328 TRP A CA 1 ATOM 2394 C C . TRP A 1 303 ? -14.642 -1.952 0.539 1.00 14.73 ? 328 TRP A C 1 ATOM 2395 O O . TRP A 1 303 ? -15.667 -2.439 0.047 1.00 15.20 ? 328 TRP A O 1 ATOM 2396 C CB . TRP A 1 303 ? -14.644 0.404 1.462 1.00 15.92 ? 328 TRP A CB 1 ATOM 2397 C CG . TRP A 1 303 ? -15.488 0.722 0.273 1.00 15.98 ? 328 TRP A CG 1 ATOM 2398 C CD1 . TRP A 1 303 ? -16.843 0.899 0.250 1.00 19.00 ? 328 TRP A CD1 1 ATOM 2399 C CD2 . TRP A 1 303 ? -15.041 0.855 -1.080 1.00 17.83 ? 328 TRP A CD2 1 ATOM 2400 N NE1 . TRP A 1 303 ? -17.266 1.137 -1.039 1.00 22.08 ? 328 TRP A NE1 1 ATOM 2401 C CE2 . TRP A 1 303 ? -16.178 1.117 -1.872 1.00 18.88 ? 328 TRP A CE2 1 ATOM 2402 C CE3 . TRP A 1 303 ? -13.789 0.779 -1.699 1.00 17.82 ? 328 TRP A CE3 1 ATOM 2403 C CZ2 . TRP A 1 303 ? -16.100 1.315 -3.250 1.00 17.88 ? 328 TRP A CZ2 1 ATOM 2404 C CZ3 . TRP A 1 303 ? -13.713 0.967 -3.071 1.00 20.11 ? 328 TRP A CZ3 1 ATOM 2405 C CH2 . TRP A 1 303 ? -14.863 1.230 -3.829 1.00 18.31 ? 328 TRP A CH2 1 ATOM 2406 N N . GLY A 1 304 ? -13.442 -2.148 0.003 1.00 17.04 ? 329 GLY A N 1 ATOM 2407 C CA . GLY A 1 304 ? -13.309 -2.943 -1.207 1.00 17.56 ? 329 GLY A CA 1 ATOM 2408 C C . GLY A 1 304 ? -13.778 -4.374 -1.003 1.00 16.29 ? 329 GLY A C 1 ATOM 2409 O O . GLY A 1 304 ? -14.490 -4.940 -1.838 1.00 17.43 ? 329 GLY A O 1 ATOM 2410 N N . GLU A 1 305 ? -13.377 -4.967 0.115 1.00 16.27 ? 330 GLU A N 1 ATOM 2411 C CA . GLU A 1 305 ? -13.845 -6.303 0.461 1.00 17.24 ? 330 GLU A CA 1 ATOM 2412 C C . GLU A 1 305 ? -15.364 -6.327 0.554 1.00 16.64 ? 330 GLU A C 1 ATOM 2413 O O . GLU A 1 305 ? -15.989 -7.284 0.107 1.00 16.95 ? 330 GLU A O 1 ATOM 2414 C CB . GLU A 1 305 ? -13.236 -6.776 1.785 1.00 17.04 ? 330 GLU A CB 1 ATOM 2415 C CG . GLU A 1 305 ? -11.763 -7.155 1.672 1.00 16.12 ? 330 GLU A CG 1 ATOM 2416 C CD . GLU A 1 305 ? -11.103 -7.415 3.017 1.00 21.02 ? 330 GLU A CD 1 ATOM 2417 O OE1 . GLU A 1 305 ? -11.489 -6.778 4.021 1.00 22.82 ? 330 GLU A OE1 1 ATOM 2418 O OE2 . GLU A 1 305 ? -10.180 -8.254 3.066 1.00 22.19 ? 330 GLU A OE2 1 ATOM 2419 N N . SER A 1 306 ? -15.951 -5.279 1.132 1.00 15.79 ? 331 SER A N 1 ATOM 2420 C CA . SER A 1 306 ? -17.389 -5.252 1.369 1.00 16.54 ? 331 SER A CA 1 ATOM 2421 C C . SER A 1 306 ? -18.180 -5.259 0.065 1.00 17.87 ? 331 SER A C 1 ATOM 2422 O O . SER A 1 306 ? -19.226 -5.895 -0.021 1.00 18.59 ? 331 SER A O 1 ATOM 2423 C CB . SER A 1 306 ? -17.788 -4.051 2.246 1.00 17.69 ? 331 SER A CB 1 ATOM 2424 O OG . SER A 1 306 ? -17.888 -2.846 1.493 1.00 17.58 ? 331 SER A OG 1 ATOM 2425 N N . PHE A 1 307 ? -17.686 -4.554 -0.948 1.00 17.79 ? 332 PHE A N 1 ATOM 2426 C CA . PHE A 1 307 ? -18.390 -4.510 -2.226 1.00 17.75 ? 332 PHE A CA 1 ATOM 2427 C C . PHE A 1 307 ? -18.268 -5.840 -2.967 1.00 21.15 ? 332 PHE A C 1 ATOM 2428 O O . PHE A 1 307 ? -19.217 -6.288 -3.620 1.00 22.51 ? 332 PHE A O 1 ATOM 2429 C CB . PHE A 1 307 ? -17.914 -3.322 -3.068 1.00 19.46 ? 332 PHE A CB 1 ATOM 2430 C CG . PHE A 1 307 ? -18.741 -2.076 -2.868 1.00 19.73 ? 332 PHE A CG 1 ATOM 2431 C CD1 . PHE A 1 307 ? -19.322 -1.804 -1.637 1.00 20.65 ? 332 PHE A CD1 1 ATOM 2432 C CD2 . PHE A 1 307 ? -18.945 -1.183 -3.908 1.00 19.87 ? 332 PHE A CD2 1 ATOM 2433 C CE1 . PHE A 1 307 ? -20.092 -0.665 -1.453 1.00 20.18 ? 332 PHE A CE1 1 ATOM 2434 C CE2 . PHE A 1 307 ? -19.714 -0.042 -3.732 1.00 21.34 ? 332 PHE A CE2 1 ATOM 2435 C CZ . PHE A 1 307 ? -20.291 0.216 -2.501 1.00 22.11 ? 332 PHE A CZ 1 ATOM 2436 N N . ALA A 1 308 ? -17.118 -6.494 -2.840 1.00 17.64 ? 333 ALA A N 1 ATOM 2437 C CA . ALA A 1 308 ? -16.971 -7.829 -3.415 1.00 18.29 ? 333 ALA A CA 1 ATOM 2438 C C . ALA A 1 308 ? -17.887 -8.816 -2.693 1.00 20.51 ? 333 ALA A C 1 ATOM 2439 O O . ALA A 1 308 ? -18.580 -9.615 -3.324 1.00 22.70 ? 333 ALA A O 1 ATOM 2440 C CB . ALA A 1 308 ? -15.518 -8.297 -3.348 1.00 20.24 ? 333 ALA A CB 1 ATOM 2441 N N . TYR A 1 309 ? -17.898 -8.747 -1.365 1.00 17.67 ? 334 TYR A N 1 ATOM 2442 C CA . TYR A 1 309 ? -18.689 -9.659 -0.546 1.00 19.75 ? 334 TYR A CA 1 ATOM 2443 C C . TYR A 1 309 ? -20.197 -9.512 -0.772 1.00 20.87 ? 334 TYR A C 1 ATOM 2444 O O . TYR A 1 309 ? -20.906 -10.507 -0.936 1.00 20.89 ? 334 TYR A O 1 ATOM 2445 C CB . TYR A 1 309 ? -18.350 -9.452 0.936 1.00 19.83 ? 334 TYR A CB 1 ATOM 2446 C CG . TYR A 1 309 ? -19.124 -10.325 1.908 1.00 22.17 ? 334 TYR A CG 1 ATOM 2447 C CD1 . TYR A 1 309 ? -18.759 -11.643 2.135 1.00 27.40 ? 334 TYR A CD1 1 ATOM 2448 C CD2 . TYR A 1 309 ? -20.203 -9.814 2.612 1.00 25.46 ? 334 TYR A CD2 1 ATOM 2449 C CE1 . TYR A 1 309 ? -19.462 -12.436 3.031 1.00 26.37 ? 334 TYR A CE1 1 ATOM 2450 C CE2 . TYR A 1 309 ? -20.912 -10.596 3.507 1.00 29.96 ? 334 TYR A CE2 1 ATOM 2451 C CZ . TYR A 1 309 ? -20.537 -11.902 3.715 1.00 31.03 ? 334 TYR A CZ 1 ATOM 2452 O OH . TYR A 1 309 ? -21.244 -12.679 4.614 1.00 36.06 ? 334 TYR A OH 1 ATOM 2453 N N . LEU A 1 310 ? -20.685 -8.277 -0.785 1.00 18.99 ? 335 LEU A N 1 ATOM 2454 C CA . LEU A 1 310 ? -22.121 -8.052 -0.964 1.00 19.19 ? 335 LEU A CA 1 ATOM 2455 C C . LEU A 1 310 ? -22.614 -8.556 -2.319 1.00 23.76 ? 335 LEU A C 1 ATOM 2456 O O . LEU A 1 310 ? -23.775 -8.948 -2.441 1.00 22.44 ? 335 LEU A O 1 ATOM 2457 C CB . LEU A 1 310 ? -22.478 -6.576 -0.787 1.00 19.81 ? 335 LEU A CB 1 ATOM 2458 C CG . LEU A 1 310 ? -22.423 -6.062 0.650 1.00 21.07 ? 335 LEU A CG 1 ATOM 2459 C CD1 . LEU A 1 310 ? -22.509 -4.547 0.652 1.00 26.27 ? 335 LEU A CD1 1 ATOM 2460 C CD2 . LEU A 1 310 ? -23.542 -6.679 1.482 1.00 26.14 ? 335 LEU A CD2 1 ATOM 2461 N N . ALA A 1 311 ? -21.739 -8.539 -3.326 1.00 21.02 ? 336 ALA A N 1 ATOM 2462 C CA . ALA A 1 311 ? -22.074 -9.044 -4.663 1.00 20.86 ? 336 ALA A CA 1 ATOM 2463 C C . ALA A 1 311 ? -21.843 -10.548 -4.824 1.00 23.14 ? 336 ALA A C 1 ATOM 2464 O O . ALA A 1 311 ? -22.072 -11.106 -5.900 1.00 24.19 ? 336 ALA A O 1 ATOM 2465 C CB . ALA A 1 311 ? -21.288 -8.296 -5.722 1.00 19.30 ? 336 ALA A CB 1 ATOM 2466 N N . GLY A 1 312 ? -21.374 -11.201 -3.766 1.00 21.87 ? 337 GLY A N 1 ATOM 2467 C CA . GLY A 1 312 ? -21.156 -12.636 -3.794 1.00 19.70 ? 337 GLY A CA 1 ATOM 2468 C C . GLY A 1 312 ? -19.886 -13.102 -4.488 1.00 22.13 ? 337 GLY A C 1 ATOM 2469 O O . GLY A 1 312 ? -19.755 -14.288 -4.800 1.00 25.45 ? 337 GLY A O 1 ATOM 2470 N N . LEU A 1 313 ? -18.945 -12.192 -4.728 1.00 22.28 ? 338 LEU A N 1 ATOM 2471 C CA . LEU A 1 313 ? -17.671 -12.574 -5.333 1.00 20.75 ? 338 LEU A CA 1 ATOM 2472 C C . LEU A 1 313 ? -16.822 -13.334 -4.324 1.00 23.80 ? 338 LEU A C 1 ATOM 2473 O O . LEU A 1 313 ? -17.040 -13.231 -3.113 1.00 26.57 ? 338 LEU A O 1 ATOM 2474 C CB . LEU A 1 313 ? -16.899 -11.352 -5.838 1.00 22.11 ? 338 LEU A CB 1 ATOM 2475 C CG . LEU A 1 313 ? -17.573 -10.485 -6.901 1.00 31.23 ? 338 LEU A CG 1 ATOM 2476 C CD1 . LEU A 1 313 ? -16.590 -9.463 -7.456 1.00 27.46 ? 338 LEU A CD1 1 ATOM 2477 C CD2 . LEU A 1 313 ? -18.144 -11.343 -8.017 1.00 33.35 ? 338 LEU A CD2 1 ATOM 2478 N N . GLU A 1 314 ? -15.853 -14.091 -4.820 1.00 23.14 ? 339 GLU A N 1 ATOM 2479 C CA . GLU A 1 314 ? -14.963 -14.850 -3.946 1.00 23.00 ? 339 GLU A CA 1 ATOM 2480 C C . GLU A 1 314 ? -13.909 -13.959 -3.279 1.00 28.70 ? 339 GLU A C 1 ATOM 2481 O O . GLU A 1 314 ? -13.578 -14.150 -2.108 1.00 32.21 ? 339 GLU A O 1 ATOM 2482 C CB . GLU A 1 314 ? -14.290 -15.985 -4.723 1.00 26.81 ? 339 GLU A CB 1 ATOM 2483 C CG . GLU A 1 314 ? -15.272 -16.980 -5.326 1.00 27.68 ? 339 GLU A CG 1 ATOM 2484 C CD . GLU A 1 314 ? -16.114 -17.678 -4.272 1.00 45.16 ? 339 GLU A CD 1 ATOM 2485 O OE1 . GLU A 1 314 ? -15.542 -18.130 -3.260 1.00 46.92 ? 339 GLU A OE1 1 ATOM 2486 O OE2 . GLU A 1 314 ? -17.348 -17.773 -4.456 1.00 44.61 ? 339 GLU A OE2 1 ATOM 2487 N N . THR A 1 315 ? -13.391 -12.986 -4.024 1.00 24.52 ? 340 THR A N 1 ATOM 2488 C CA . THR A 1 315 ? -12.300 -12.131 -3.554 1.00 22.90 ? 340 THR A CA 1 ATOM 2489 C C . THR A 1 315 ? -12.410 -10.737 -4.138 1.00 24.02 ? 340 THR A C 1 ATOM 2490 O O . THR A 1 315 ? -13.101 -10.530 -5.134 1.00 22.81 ? 340 THR A O 1 ATOM 2491 C CB . THR A 1 315 ? -10.938 -12.645 -4.060 1.00 26.04 ? 340 THR A CB 1 ATOM 2492 O OG1 . THR A 1 315 ? -10.917 -12.566 -5.495 1.00 25.23 ? 340 THR A OG1 1 ATOM 2493 C CG2 . THR A 1 315 ? -10.692 -14.073 -3.626 1.00 28.91 ? 340 THR A CG2 1 ATOM 2494 N N . VAL A 1 316 ? -11.703 -9.784 -3.534 1.00 21.22 ? 341 VAL A N 1 ATOM 2495 C CA . VAL A 1 316 ? -11.520 -8.466 -4.127 1.00 20.96 ? 341 VAL A CA 1 ATOM 2496 C C . VAL A 1 316 ? -10.878 -8.570 -5.505 1.00 20.76 ? 341 VAL A C 1 ATOM 2497 O O . VAL A 1 316 ? -11.233 -7.830 -6.420 1.00 21.55 ? 341 VAL A O 1 ATOM 2498 C CB . VAL A 1 316 ? -10.668 -7.547 -3.224 1.00 25.87 ? 341 VAL A CB 1 ATOM 2499 C CG1 . VAL A 1 316 ? -10.186 -6.320 -3.989 1.00 27.48 ? 341 VAL A CG1 1 ATOM 2500 C CG2 . VAL A 1 316 ? -11.473 -7.128 -2.006 1.00 26.38 ? 341 VAL A CG2 1 ATOM 2501 N N . SER A 1 317 ? -9.936 -9.494 -5.665 1.00 19.22 ? 342 SER A N 1 ATOM 2502 C CA . SER A 1 317 ? -9.293 -9.662 -6.958 1.00 18.54 ? 342 SER A CA 1 ATOM 2503 C C . SER A 1 317 ? -10.309 -9.875 -8.067 1.00 20.88 ? 342 SER A C 1 ATOM 2504 O O . SER A 1 317 ? -10.116 -9.399 -9.186 1.00 20.27 ? 342 SER A O 1 ATOM 2505 C CB . SER A 1 317 ? -8.307 -10.829 -6.924 1.00 19.29 ? 342 SER A CB 1 ATOM 2506 O OG . SER A 1 317 ? -7.083 -10.418 -6.342 1.00 23.69 ? 342 SER A OG 1 ATOM 2507 N N . GLN A 1 318 ? -11.385 -10.595 -7.768 1.00 19.86 ? 343 GLN A N 1 ATOM 2508 C CA . GLN A 1 318 ? -12.394 -10.876 -8.786 1.00 20.87 ? 343 GLN A CA 1 ATOM 2509 C C . GLN A 1 318 ? -13.054 -9.608 -9.324 1.00 19.50 ? 343 GLN A C 1 ATOM 2510 O O . GLN A 1 318 ? -13.563 -9.608 -10.447 1.00 19.94 ? 343 GLN A O 1 ATOM 2511 C CB . GLN A 1 318 ? -13.452 -11.854 -8.273 1.00 22.98 ? 343 GLN A CB 1 ATOM 2512 C CG . GLN A 1 318 ? -12.959 -13.284 -8.175 1.00 25.01 ? 343 GLN A CG 1 ATOM 2513 C CD . GLN A 1 318 ? -14.093 -14.289 -8.120 1.00 26.55 ? 343 GLN A CD 1 ATOM 2514 O OE1 . GLN A 1 318 ? -15.162 -14.013 -7.573 1.00 30.12 ? 343 GLN A OE1 1 ATOM 2515 N NE2 . GLN A 1 318 ? -13.865 -15.462 -8.698 1.00 28.36 ? 343 GLN A NE2 1 ATOM 2516 N N . LEU A 1 319 ? -13.048 -8.532 -8.540 1.00 18.85 ? 344 LEU A N 1 ATOM 2517 C CA . LEU A 1 319 ? -13.575 -7.256 -9.022 1.00 16.77 ? 344 LEU A CA 1 ATOM 2518 C C . LEU A 1 319 ? -12.868 -6.819 -10.299 1.00 19.26 ? 344 LEU A C 1 ATOM 2519 O O . LEU A 1 319 ? -13.470 -6.170 -11.152 1.00 19.30 ? 344 LEU A O 1 ATOM 2520 C CB . LEU A 1 319 ? -13.403 -6.164 -7.967 1.00 18.26 ? 344 LEU A CB 1 ATOM 2521 C CG . LEU A 1 319 ? -14.279 -6.276 -6.725 1.00 17.00 ? 344 LEU A CG 1 ATOM 2522 C CD1 . LEU A 1 319 ? -13.793 -5.295 -5.667 1.00 18.46 ? 344 LEU A CD1 1 ATOM 2523 C CD2 . LEU A 1 319 ? -15.742 -6.029 -7.061 1.00 20.61 ? 344 LEU A CD2 1 ATOM 2524 N N . ASN A 1 320 ? -11.592 -7.171 -10.425 1.00 18.14 ? 345 ASN A N 1 ATOM 2525 C CA . ASN A 1 320 ? -10.785 -6.692 -11.545 1.00 19.26 ? 345 ASN A CA 1 ATOM 2526 C C . ASN A 1 320 ? -10.899 -7.551 -12.798 1.00 18.57 ? 345 ASN A C 1 ATOM 2527 O O . ASN A 1 320 ? -10.154 -7.350 -13.756 1.00 24.00 ? 345 ASN A O 1 ATOM 2528 C CB . ASN A 1 320 ? -9.315 -6.553 -11.139 1.00 20.46 ? 345 ASN A CB 1 ATOM 2529 C CG . ASN A 1 320 ? -8.587 -5.491 -11.950 1.00 22.02 ? 345 ASN A CG 1 ATOM 2530 O OD1 . ASN A 1 320 ? -9.179 -4.480 -12.331 1.00 21.74 ? 345 ASN A OD1 1 ATOM 2531 N ND2 . ASN A 1 320 ? -7.303 -5.716 -12.217 1.00 28.40 ? 345 ASN A ND2 1 ATOM 2532 N N . ASN A 1 321 ? -11.823 -8.506 -12.794 1.00 21.09 ? 346 ASN A N 1 ATOM 2533 C CA . ASN A 1 321 ? -11.990 -9.401 -13.938 1.00 20.74 ? 346 ASN A CA 1 ATOM 2534 C C . ASN A 1 321 ? -13.280 -9.098 -14.693 1.00 22.94 ? 346 ASN A C 1 ATOM 2535 O O . ASN A 1 321 ? -14.340 -9.603 -14.335 1.00 22.53 ? 346 ASN A O 1 ATOM 2536 C CB . ASN A 1 321 ? -11.977 -10.859 -13.477 1.00 23.14 ? 346 ASN A CB 1 ATOM 2537 C CG . ASN A 1 321 ? -12.042 -11.838 -14.636 1.00 29.57 ? 346 ASN A CG 1 ATOM 2538 O OD1 . ASN A 1 321 ? -12.097 -11.438 -15.801 1.00 29.70 ? 346 ASN A OD1 1 ATOM 2539 N ND2 . ASN A 1 321 ? -12.034 -13.128 -14.321 1.00 37.32 ? 346 ASN A ND2 1 ATOM 2540 N N . ARG A 1 322 ? -13.183 -8.287 -15.745 1.00 23.68 ? 347 ARG A N 1 ATOM 2541 C CA . ARG A 1 322 ? -14.371 -7.809 -16.456 1.00 21.49 ? 347 ARG A CA 1 ATOM 2542 C C . ARG A 1 322 ? -15.105 -8.924 -17.189 1.00 21.35 ? 347 ARG A C 1 ATOM 2543 O O . ARG A 1 322 ? -16.275 -8.778 -17.536 1.00 26.60 ? 347 ARG A O 1 ATOM 2544 C CB . ARG A 1 322 ? -14.006 -6.693 -17.443 1.00 23.06 ? 347 ARG A CB 1 ATOM 2545 C CG . ARG A 1 322 ? -13.227 -7.172 -18.661 1.00 24.42 ? 347 ARG A CG 1 ATOM 2546 C CD . ARG A 1 322 ? -12.759 -6.005 -19.527 1.00 24.10 ? 347 ARG A CD 1 ATOM 2547 N NE . ARG A 1 322 ? -13.872 -5.281 -20.145 1.00 24.18 ? 347 ARG A NE 1 ATOM 2548 C CZ . ARG A 1 322 ? -14.131 -3.992 -19.948 1.00 24.77 ? 347 ARG A CZ 1 ATOM 2549 N NH1 . ARG A 1 322 ? -13.354 -3.271 -19.150 1.00 20.57 ? 347 ARG A NH1 1 ATOM 2550 N NH2 . ARG A 1 322 ? -15.162 -3.420 -20.561 1.00 21.80 ? 347 ARG A NH2 1 ATOM 2551 N N . PHE A 1 323 ? -14.418 -10.037 -17.414 1.00 23.98 ? 348 PHE A N 1 ATOM 2552 C CA . PHE A 1 323 ? -15.015 -11.146 -18.144 1.00 27.84 ? 348 PHE A CA 1 ATOM 2553 C C . PHE A 1 323 ? -15.434 -12.301 -17.237 1.00 27.65 ? 348 PHE A C 1 ATOM 2554 O O . PHE A 1 323 ? -15.773 -13.387 -17.714 1.00 31.69 ? 348 PHE A O 1 ATOM 2555 C CB . PHE A 1 323 ? -14.084 -11.611 -19.265 1.00 27.62 ? 348 PHE A CB 1 ATOM 2556 C CG . PHE A 1 323 ? -13.864 -10.568 -20.326 1.00 27.54 ? 348 PHE A CG 1 ATOM 2557 C CD1 . PHE A 1 323 ? -14.944 -9.968 -20.952 1.00 32.03 ? 348 PHE A CD1 1 ATOM 2558 C CD2 . PHE A 1 323 ? -12.586 -10.175 -20.684 1.00 36.11 ? 348 PHE A CD2 1 ATOM 2559 C CE1 . PHE A 1 323 ? -14.755 -9.000 -21.920 1.00 34.00 ? 348 PHE A CE1 1 ATOM 2560 C CE2 . PHE A 1 323 ? -12.390 -9.210 -21.655 1.00 32.30 ? 348 PHE A CE2 1 ATOM 2561 C CZ . PHE A 1 323 ? -13.478 -8.622 -22.273 1.00 32.04 ? 348 PHE A CZ 1 ATOM 2562 N N . LEU A 1 324 ? -15.433 -12.060 -15.930 1.00 28.41 ? 349 LEU A N 1 ATOM 2563 C CA . LEU A 1 324 ? -15.925 -13.055 -14.989 1.00 32.59 ? 349 LEU A CA 1 ATOM 2564 C C . LEU A 1 324 ? -17.437 -13.166 -15.133 1.00 27.25 ? 349 LEU A C 1 ATOM 2565 O O . LEU A 1 324 ? -18.155 -12.170 -15.019 1.00 35.70 ? 349 LEU A O 1 ATOM 2566 C CB . LEU A 1 324 ? -15.557 -12.678 -13.553 1.00 40.44 ? 349 LEU A CB 1 ATOM 2567 C CG . LEU A 1 324 ? -15.883 -13.725 -12.484 1.00 40.36 ? 349 LEU A CG 1 ATOM 2568 C CD1 . LEU A 1 324 ? -15.156 -15.030 -12.773 1.00 50.58 ? 349 LEU A CD1 1 ATOM 2569 C CD2 . LEU A 1 324 ? -15.531 -13.214 -11.099 1.00 36.63 ? 349 LEU A CD2 1 ATOM 2570 N N . LYS A 1 325 ? -17.919 -14.376 -15.393 1.00 30.82 ? 350 LYS A N 1 ATOM 2571 C CA . LYS A 1 325 ? -19.345 -14.595 -15.601 1.00 41.03 ? 350 LYS A CA 1 ATOM 2572 C C . LYS A 1 325 ? -20.113 -14.395 -14.302 1.00 37.35 ? 350 LYS A C 1 ATOM 2573 O O . LYS A 1 325 ? -20.083 -15.250 -13.418 1.00 53.94 ? 350 LYS A O 1 ATOM 2574 C CB . LYS A 1 325 ? -19.599 -16.007 -16.126 1.00 51.72 ? 350 LYS A CB 1 ATOM 2575 C CG . LYS A 1 325 ? -18.475 -16.583 -16.968 1.00 58.92 ? 350 LYS A CG 1 ATOM 2576 C CD . LYS A 1 325 ? -18.872 -17.950 -17.492 1.00 68.47 ? 350 LYS A CD 1 ATOM 2577 C CE . LYS A 1 325 ? -17.672 -18.837 -17.743 1.00 71.26 ? 350 LYS A CE 1 ATOM 2578 N NZ . LYS A 1 325 ? -18.106 -20.225 -18.073 1.00 76.19 ? 350 LYS A NZ 1 ATOM 2579 N N . PHE A 1 326 ? -20.805 -13.268 -14.192 1.00 35.18 ? 351 PHE A N 1 ATOM 2580 C CA . PHE A 1 326 ? -21.545 -12.955 -12.977 1.00 32.50 ? 351 PHE A CA 1 ATOM 2581 C C . PHE A 1 326 ? -22.859 -13.728 -12.928 1.00 36.78 ? 351 PHE A C 1 ATOM 2582 O O . PHE A 1 326 ? -23.195 -14.336 -11.913 1.00 34.56 ? 351 PHE A O 1 ATOM 2583 C CB . PHE A 1 326 ? -21.796 -11.447 -12.872 1.00 31.64 ? 351 PHE A CB 1 ATOM 2584 C CG . PHE A 1 326 ? -22.393 -11.020 -11.560 1.00 30.84 ? 351 PHE A CG 1 ATOM 2585 C CD1 . PHE A 1 326 ? -23.692 -10.541 -11.498 1.00 36.06 ? 351 PHE A CD1 1 ATOM 2586 C CD2 . PHE A 1 326 ? -21.656 -11.103 -10.385 1.00 26.80 ? 351 PHE A CD2 1 ATOM 2587 C CE1 . PHE A 1 326 ? -24.249 -10.145 -10.294 1.00 30.84 ? 351 PHE A CE1 1 ATOM 2588 C CE2 . PHE A 1 326 ? -22.205 -10.709 -9.175 1.00 25.23 ? 351 PHE A CE2 1 ATOM 2589 C CZ . PHE A 1 326 ? -23.503 -10.231 -9.128 1.00 26.45 ? 351 PHE A CZ 1 ATOM 2590 N N . ASP A 1 327 ? -23.590 -13.710 -14.038 1.00 37.74 ? 352 ASP A N 1 ATOM 2591 C CA . ASP A 1 327 ? -24.859 -14.426 -14.154 1.00 35.27 ? 352 ASP A CA 1 ATOM 2592 C C . ASP A 1 327 ? -25.137 -14.661 -15.635 1.00 38.36 ? 352 ASP A C 1 ATOM 2593 O O . ASP A 1 327 ? -25.479 -13.730 -16.361 1.00 50.02 ? 352 ASP A O 1 ATOM 2594 C CB . ASP A 1 327 ? -25.991 -13.615 -13.511 1.00 33.17 ? 352 ASP A CB 1 ATOM 2595 C CG . ASP A 1 327 ? -27.294 -14.395 -13.413 1.00 36.90 ? 352 ASP A CG 1 ATOM 2596 O OD1 . ASP A 1 327 ? -27.441 -15.403 -14.131 1.00 40.75 ? 352 ASP A OD1 1 ATOM 2597 O OD2 . ASP A 1 327 ? -28.175 -13.999 -12.621 1.00 36.60 ? 352 ASP A OD2 1 ATOM 2598 N N . GLU A 1 328 ? -24.990 -15.905 -16.083 1.00 33.21 ? 353 GLU A N 1 ATOM 2599 C CA . GLU A 1 328 ? -25.047 -16.209 -17.512 1.00 35.27 ? 353 GLU A CA 1 ATOM 2600 C C . GLU A 1 328 ? -26.448 -16.484 -18.055 1.00 29.83 ? 353 GLU A C 1 ATOM 2601 O O . GLU A 1 328 ? -26.597 -17.159 -19.069 1.00 36.58 ? 353 GLU A O 1 ATOM 2602 C CB . GLU A 1 328 ? -24.148 -17.401 -17.844 1.00 51.03 ? 353 GLU A CB 1 ATOM 2603 C CG . GLU A 1 328 ? -22.665 -17.120 -17.740 1.00 66.94 ? 353 GLU A CG 1 ATOM 2604 C CD . GLU A 1 328 ? -21.891 -17.714 -18.899 1.00 80.61 ? 353 GLU A CD 1 ATOM 2605 O OE1 . GLU A 1 328 ? -21.380 -18.845 -18.761 1.00 84.67 ? 353 GLU A OE1 1 ATOM 2606 O OE2 . GLU A 1 328 ? -21.809 -17.054 -19.957 1.00 83.45 ? 353 GLU A OE2 1 ATOM 2607 N N . ARG A 1 329 ? -27.471 -15.955 -17.396 1.00 25.68 ? 354 ARG A N 1 ATOM 2608 C CA . ARG A 1 329 ? -28.845 -16.233 -17.805 1.00 24.16 ? 354 ARG A CA 1 ATOM 2609 C C . ARG A 1 329 ? -29.454 -15.117 -18.646 1.00 22.06 ? 354 ARG A C 1 ATOM 2610 O O . ARG A 1 329 ? -29.200 -13.937 -18.414 1.00 24.79 ? 354 ARG A O 1 ATOM 2611 C CB . ARG A 1 329 ? -29.719 -16.476 -16.570 1.00 26.63 ? 354 ARG A CB 1 ATOM 2612 C CG . ARG A 1 329 ? -29.415 -17.784 -15.856 1.00 36.08 ? 354 ARG A CG 1 ATOM 2613 C CD . ARG A 1 329 ? -29.288 -17.572 -14.362 1.00 45.25 ? 354 ARG A CD 1 ATOM 2614 N NE . ARG A 1 329 ? -30.573 -17.414 -13.697 1.00 40.94 ? 354 ARG A NE 1 ATOM 2615 C CZ . ARG A 1 329 ? -30.756 -16.687 -12.599 1.00 49.33 ? 354 ARG A CZ 1 ATOM 2616 N NH1 . ARG A 1 329 ? -31.955 -16.603 -12.051 1.00 58.36 ? 354 ARG A NH1 1 ATOM 2617 N NH2 . ARG A 1 329 ? -29.743 -16.034 -12.053 1.00 56.74 ? 354 ARG A NH2 1 ATOM 2618 N N . ALA A 1 330 ? -30.263 -15.507 -19.627 1.00 22.97 ? 355 ALA A N 1 ATOM 2619 C CA . ALA A 1 330 ? -31.127 -14.558 -20.315 1.00 22.46 ? 355 ALA A CA 1 ATOM 2620 C C . ALA A 1 330 ? -32.107 -14.022 -19.287 1.00 22.48 ? 355 ALA A C 1 ATOM 2621 O O . ALA A 1 330 ? -32.535 -14.749 -18.392 1.00 23.77 ? 355 ALA A O 1 ATOM 2622 C CB . ALA A 1 330 ? -31.871 -15.242 -21.453 1.00 22.95 ? 355 ALA A CB 1 ATOM 2623 N N . PHE A 1 331 ? -32.478 -12.754 -19.408 1.00 19.23 ? 356 PHE A N 1 ATOM 2624 C CA . PHE A 1 331 ? -33.418 -12.193 -18.451 1.00 19.18 ? 356 PHE A CA 1 ATOM 2625 C C . PHE A 1 331 ? -34.233 -11.041 -19.010 1.00 24.74 ? 356 PHE A C 1 ATOM 2626 O O . PHE A 1 331 ? -33.856 -10.406 -19.998 1.00 22.91 ? 356 PHE A O 1 ATOM 2627 C CB . PHE A 1 331 ? -32.691 -11.739 -17.177 1.00 19.81 ? 356 PHE A CB 1 ATOM 2628 C CG . PHE A 1 331 ? -31.774 -10.565 -17.385 1.00 19.40 ? 356 PHE A CG 1 ATOM 2629 C CD1 . PHE A 1 331 ? -32.200 -9.270 -17.114 1.00 21.85 ? 356 PHE A CD1 1 ATOM 2630 C CD2 . PHE A 1 331 ? -30.479 -10.756 -17.848 1.00 22.37 ? 356 PHE A CD2 1 ATOM 2631 C CE1 . PHE A 1 331 ? -31.346 -8.188 -17.308 1.00 21.75 ? 356 PHE A CE1 1 ATOM 2632 C CE2 . PHE A 1 331 ? -29.623 -9.687 -18.043 1.00 23.13 ? 356 PHE A CE2 1 ATOM 2633 C CZ . PHE A 1 331 ? -30.054 -8.398 -17.773 1.00 23.10 ? 356 PHE A CZ 1 ATOM 2634 N N . LYS A 1 332 ? -35.362 -10.789 -18.360 1.00 21.17 ? 357 LYS A N 1 ATOM 2635 C CA . LYS A 1 332 ? -36.104 -9.559 -18.566 1.00 20.63 ? 357 LYS A CA 1 ATOM 2636 C C . LYS A 1 332 ? -36.403 -9.006 -17.191 1.00 19.25 ? 357 LYS A C 1 ATOM 2637 O O . LYS A 1 332 ? -36.584 -9.761 -16.231 1.00 20.26 ? 357 LYS A O 1 ATOM 2638 C CB . LYS A 1 332 ? -37.400 -9.805 -19.341 1.00 21.86 ? 357 LYS A CB 1 ATOM 2639 C CG . LYS A 1 332 ? -38.065 -8.526 -19.831 1.00 33.58 ? 357 LYS A CG 1 ATOM 2640 C CD . LYS A 1 332 ? -38.700 -8.721 -21.199 1.00 50.04 ? 357 LYS A CD 1 ATOM 2641 C CE . LYS A 1 332 ? -39.546 -7.523 -21.590 1.00 54.05 ? 357 LYS A CE 1 ATOM 2642 N NZ . LYS A 1 332 ? -40.718 -7.373 -20.684 1.00 52.23 ? 357 LYS A NZ 1 ATOM 2643 N N . THR A 1 333 ? -36.440 -7.685 -17.088 1.00 19.86 ? 358 THR A N 1 ATOM 2644 C CA . THR A 1 333 ? -36.652 -7.060 -15.802 1.00 19.41 ? 358 THR A CA 1 ATOM 2645 C C . THR A 1 333 ? -37.509 -5.816 -15.963 1.00 19.76 ? 358 THR A C 1 ATOM 2646 O O . THR A 1 333 ? -37.544 -5.208 -17.034 1.00 23.52 ? 358 THR A O 1 ATOM 2647 C CB . THR A 1 333 ? -35.302 -6.727 -15.127 1.00 21.53 ? 358 THR A CB 1 ATOM 2648 O OG1 . THR A 1 333 ? -35.532 -6.007 -13.914 1.00 20.84 ? 358 THR A OG1 1 ATOM 2649 C CG2 . THR A 1 333 ? -34.419 -5.898 -16.048 1.00 23.67 ? 358 THR A CG2 1 ATOM 2650 N N . LYS A 1 334 ? -38.224 -5.470 -14.900 1.00 18.45 ? 359 LYS A N 1 ATOM 2651 C CA . LYS A 1 334 ? -38.967 -4.224 -14.831 1.00 19.79 ? 359 LYS A CA 1 ATOM 2652 C C . LYS A 1 334 ? -38.717 -3.606 -13.468 1.00 18.78 ? 359 LYS A C 1 ATOM 2653 O O . LYS A 1 334 ? -38.275 -4.287 -12.548 1.00 20.63 ? 359 LYS A O 1 ATOM 2654 C CB . LYS A 1 334 ? -40.458 -4.469 -15.039 1.00 20.25 ? 359 LYS A CB 1 ATOM 2655 C CG . LYS A 1 334 ? -40.821 -4.817 -16.471 1.00 22.62 ? 359 LYS A CG 1 ATOM 2656 C CD . LYS A 1 334 ? -42.320 -4.745 -16.675 1.00 30.82 ? 359 LYS A CD 1 ATOM 2657 C CE . LYS A 1 334 ? -42.647 -4.107 -18.004 1.00 44.84 ? 359 LYS A CE 1 ATOM 2658 N NZ . LYS A 1 334 ? -41.742 -4.635 -19.048 1.00 39.29 ? 359 LYS A NZ 1 ATOM 2659 N N . VAL A 1 335 ? -38.986 -2.314 -13.341 1.00 17.46 ? 360 VAL A N 1 ATOM 2660 C CA . VAL A 1 335 ? -38.745 -1.631 -12.083 1.00 17.41 ? 360 VAL A CA 1 ATOM 2661 C C . VAL A 1 335 ? -39.891 -0.684 -11.742 1.00 16.95 ? 360 VAL A C 1 ATOM 2662 O O . VAL A 1 335 ? -40.586 -0.173 -12.630 1.00 19.26 ? 360 VAL A O 1 ATOM 2663 C CB . VAL A 1 335 ? -37.414 -0.850 -12.125 1.00 17.41 ? 360 VAL A CB 1 ATOM 2664 C CG1 . VAL A 1 335 ? -37.506 0.307 -13.112 1.00 19.52 ? 360 VAL A CG1 1 ATOM 2665 C CG2 . VAL A 1 335 ? -37.043 -0.343 -10.730 1.00 18.24 ? 360 VAL A CG2 1 ATOM 2666 N N . ASP A 1 336 ? -40.112 -0.493 -10.445 1.00 14.79 ? 361 ASP A N 1 ATOM 2667 C CA . ASP A 1 336 ? -41.024 0.535 -9.961 1.00 16.11 ? 361 ASP A CA 1 ATOM 2668 C C . ASP A 1 336 ? -40.328 1.413 -8.931 1.00 17.44 ? 361 ASP A C 1 ATOM 2669 O O . ASP A 1 336 ? -39.416 0.963 -8.229 1.00 17.10 ? 361 ASP A O 1 ATOM 2670 C CB . ASP A 1 336 ? -42.268 -0.082 -9.313 1.00 16.90 ? 361 ASP A CB 1 ATOM 2671 C CG . ASP A 1 336 ? -43.349 -0.404 -10.316 1.00 16.95 ? 361 ASP A CG 1 ATOM 2672 O OD1 . ASP A 1 336 ? -43.636 0.464 -11.173 1.00 18.59 ? 361 ASP A OD1 1 ATOM 2673 O OD2 . ASP A 1 336 ? -43.932 -1.513 -10.234 1.00 17.90 ? 361 ASP A OD2 1 ATOM 2674 N N . LEU A 1 337 ? -40.777 2.663 -8.855 1.00 16.45 ? 362 LEU A N 1 ATOM 2675 C CA . LEU A 1 337 ? -40.446 3.564 -7.757 1.00 17.33 ? 362 LEU A CA 1 ATOM 2676 C C . LEU A 1 337 ? -41.749 3.829 -7.014 1.00 20.58 ? 362 LEU A C 1 ATOM 2677 O O . LEU A 1 337 ? -42.824 3.868 -7.621 1.00 19.76 ? 362 LEU A O 1 ATOM 2678 C CB . LEU A 1 337 ? -39.880 4.889 -8.279 1.00 18.51 ? 362 LEU A CB 1 ATOM 2679 C CG . LEU A 1 337 ? -38.501 4.916 -8.949 1.00 27.01 ? 362 LEU A CG 1 ATOM 2680 C CD1 . LEU A 1 337 ? -37.461 4.237 -8.083 1.00 29.95 ? 362 LEU A CD1 1 ATOM 2681 C CD2 . LEU A 1 337 ? -38.529 4.307 -10.342 1.00 24.16 ? 362 LEU A CD2 1 ATOM 2682 N N . THR A 1 338 ? -41.666 4.007 -5.700 1.00 17.35 ? 363 THR A N 1 ATOM 2683 C CA . THR A 1 338 ? -42.867 4.209 -4.901 1.00 17.34 ? 363 THR A CA 1 ATOM 2684 C C . THR A 1 338 ? -42.857 5.544 -4.177 1.00 19.57 ? 363 THR A C 1 ATOM 2685 O O . THR A 1 338 ? -41.794 6.127 -3.926 1.00 18.54 ? 363 THR A O 1 ATOM 2686 C CB . THR A 1 338 ? -43.043 3.105 -3.851 1.00 17.98 ? 363 THR A CB 1 ATOM 2687 O OG1 . THR A 1 338 ? -41.999 3.207 -2.874 1.00 20.11 ? 363 THR A OG1 1 ATOM 2688 C CG2 . THR A 1 338 ? -43.008 1.721 -4.496 1.00 21.10 ? 363 THR A CG2 1 ATOM 2689 N N . LYS A 1 339 ? -44.049 6.017 -3.836 1.00 20.13 ? 364 LYS A N 1 ATOM 2690 C CA . LYS A 1 339 ? -44.212 7.272 -3.109 1.00 21.47 ? 364 LYS A CA 1 ATOM 2691 C C . LYS A 1 339 ? -45.006 7.064 -1.820 1.00 21.81 ? 364 LYS A C 1 ATOM 2692 O O . LYS A 1 339 ? -44.892 7.843 -0.880 1.00 24.98 ? 364 LYS A O 1 ATOM 2693 C CB . LYS A 1 339 ? -44.880 8.321 -4.004 1.00 27.27 ? 364 LYS A CB 1 ATOM 2694 C CG . LYS A 1 339 ? -44.084 8.597 -5.280 1.00 34.03 ? 364 LYS A CG 1 ATOM 2695 C CD . LYS A 1 339 ? -44.727 9.664 -6.154 1.00 48.80 ? 364 LYS A CD 1 ATOM 2696 C CE . LYS A 1 339 ? -44.375 11.062 -5.673 1.00 54.90 ? 364 LYS A CE 1 ATOM 2697 N NZ . LYS A 1 339 ? -44.825 12.104 -6.641 1.00 56.60 ? 364 LYS A NZ 1 ATOM 2698 N N . GLU A 1 340 ? -45.819 6.013 -1.795 1.00 19.80 ? 365 GLU A N 1 ATOM 2699 C CA A GLU A 1 340 ? -46.599 5.659 -0.615 0.55 22.55 ? 365 GLU A CA 1 ATOM 2700 C CA B GLU A 1 340 ? -46.602 5.658 -0.617 0.45 22.79 ? 365 GLU A CA 1 ATOM 2701 C C . GLU A 1 340 ? -46.161 4.287 -0.115 1.00 23.18 ? 365 GLU A C 1 ATOM 2702 O O . GLU A 1 340 ? -45.758 3.440 -0.903 1.00 21.49 ? 365 GLU A O 1 ATOM 2703 C CB A GLU A 1 340 ? -48.091 5.630 -0.955 0.55 26.19 ? 365 GLU A CB 1 ATOM 2704 C CB B GLU A 1 340 ? -48.095 5.626 -0.960 0.45 26.05 ? 365 GLU A CB 1 ATOM 2705 C CG A GLU A 1 340 ? -48.626 6.938 -1.518 0.55 30.33 ? 365 GLU A CG 1 ATOM 2706 C CG B GLU A 1 340 ? -48.679 6.978 -1.349 0.45 29.84 ? 365 GLU A CG 1 ATOM 2707 C CD A GLU A 1 340 ? -48.603 8.061 -0.501 0.55 38.50 ? 365 GLU A CD 1 ATOM 2708 C CD B GLU A 1 340 ? -50.089 6.871 -1.903 0.45 36.57 ? 365 GLU A CD 1 ATOM 2709 O OE1 A GLU A 1 340 ? -48.860 7.786 0.689 0.55 38.41 ? 365 GLU A OE1 1 ATOM 2710 O OE1 B GLU A 1 340 ? -50.404 5.850 -2.551 0.45 43.51 ? 365 GLU A OE1 1 ATOM 2711 O OE2 A GLU A 1 340 ? -48.334 9.217 -0.892 0.55 44.12 ? 365 GLU A OE2 1 ATOM 2712 O OE2 B GLU A 1 340 ? -50.884 7.813 -1.696 0.45 49.78 ? 365 GLU A OE2 1 ATOM 2713 N N . PRO A 1 341 ? -46.230 4.064 1.205 1.00 19.59 ? 366 PRO A N 1 ATOM 2714 C CA . PRO A 1 341 ? -45.875 2.738 1.720 1.00 18.22 ? 366 PRO A CA 1 ATOM 2715 C C . PRO A 1 341 ? -46.678 1.641 1.025 1.00 18.12 ? 366 PRO A C 1 ATOM 2716 O O . PRO A 1 341 ? -47.851 1.849 0.691 1.00 22.95 ? 366 PRO A O 1 ATOM 2717 C CB . PRO A 1 341 ? -46.270 2.823 3.198 1.00 23.05 ? 366 PRO A CB 1 ATOM 2718 C CG . PRO A 1 341 ? -46.151 4.274 3.522 1.00 24.56 ? 366 PRO A CG 1 ATOM 2719 C CD . PRO A 1 341 ? -46.605 4.994 2.283 1.00 25.78 ? 366 PRO A CD 1 ATOM 2720 N N . LEU A 1 342 ? -46.051 0.492 0.801 1.00 18.86 ? 367 LEU A N 1 ATOM 2721 C CA . LEU A 1 342 ? -46.753 -0.647 0.220 1.00 20.95 ? 367 LEU A CA 1 ATOM 2722 C C . LEU A 1 342 ? -47.572 -1.338 1.302 1.00 22.46 ? 367 LEU A C 1 ATOM 2723 O O . LEU A 1 342 ? -47.075 -1.581 2.404 1.00 20.52 ? 367 LEU A O 1 ATOM 2724 C CB . LEU A 1 342 ? -45.753 -1.629 -0.391 1.00 18.23 ? 367 LEU A CB 1 ATOM 2725 C CG . LEU A 1 342 ? -44.862 -1.071 -1.503 1.00 21.38 ? 367 LEU A CG 1 ATOM 2726 C CD1 . LEU A 1 342 ? -43.883 -2.132 -1.977 1.00 23.06 ? 367 LEU A CD1 1 ATOM 2727 C CD2 . LEU A 1 342 ? -45.718 -0.571 -2.659 1.00 29.81 ? 367 LEU A CD2 1 ATOM 2728 N N . PRO A 1 343 ? -48.838 -1.653 1.001 1.00 19.89 ? 368 PRO A N 1 ATOM 2729 C CA . PRO A 1 343 ? -49.613 -2.359 2.020 1.00 20.03 ? 368 PRO A CA 1 ATOM 2730 C C . PRO A 1 343 ? -49.121 -3.799 2.107 1.00 16.92 ? 368 PRO A C 1 ATOM 2731 O O . PRO A 1 343 ? -48.518 -4.310 1.163 1.00 18.86 ? 368 PRO A O 1 ATOM 2732 C CB . PRO A 1 343 ? -51.043 -2.293 1.468 1.00 19.78 ? 368 PRO A CB 1 ATOM 2733 C CG . PRO A 1 343 ? -50.846 -2.271 -0.014 1.00 18.79 ? 368 PRO A CG 1 ATOM 2734 C CD . PRO A 1 343 ? -49.649 -1.354 -0.194 1.00 22.66 ? 368 PRO A CD 1 ATOM 2735 N N . SER A 1 344 ? -49.365 -4.438 3.244 1.00 19.29 ? 369 SER A N 1 ATOM 2736 C CA . SER A 1 344 ? -48.936 -5.808 3.456 1.00 18.20 ? 369 SER A CA 1 ATOM 2737 C C . SER A 1 344 ? -49.386 -6.735 2.320 1.00 17.88 ? 369 SER A C 1 ATOM 2738 O O . SER A 1 344 ? -48.631 -7.604 1.879 1.00 20.48 ? 369 SER A O 1 ATOM 2739 C CB . SER A 1 344 ? -49.479 -6.298 4.803 1.00 25.10 ? 369 SER A CB 1 ATOM 2740 O OG . SER A 1 344 ? -49.192 -7.661 5.013 1.00 28.08 ? 369 SER A OG 1 ATOM 2741 N N . LYS A 1 345 ? -50.623 -6.550 1.857 1.00 18.81 ? 370 LYS A N 1 ATOM 2742 C CA . LYS A 1 345 ? -51.181 -7.415 0.825 1.00 18.08 ? 370 LYS A CA 1 ATOM 2743 C C . LYS A 1 345 ? -50.402 -7.322 -0.484 1.00 17.45 ? 370 LYS A C 1 ATOM 2744 O O . LYS A 1 345 ? -50.435 -8.250 -1.288 1.00 19.37 ? 370 LYS A O 1 ATOM 2745 C CB . LYS A 1 345 ? -52.655 -7.084 0.577 1.00 19.24 ? 370 LYS A CB 1 ATOM 2746 C CG . LYS A 1 345 ? -52.879 -5.739 -0.101 1.00 17.09 ? 370 LYS A CG 1 ATOM 2747 C CD . LYS A 1 345 ? -54.358 -5.424 -0.207 1.00 19.25 ? 370 LYS A CD 1 ATOM 2748 C CE . LYS A 1 345 ? -54.565 -4.052 -0.829 1.00 23.55 ? 370 LYS A CE 1 ATOM 2749 N NZ . LYS A 1 345 ? -56.019 -3.730 -0.939 1.00 28.80 ? 370 LYS A NZ 1 ATOM 2750 N N . ALA A 1 346 ? -49.716 -6.205 -0.708 1.00 18.91 ? 371 ALA A N 1 ATOM 2751 C CA . ALA A 1 346 ? -48.885 -6.081 -1.902 1.00 19.61 ? 371 ALA A CA 1 ATOM 2752 C C . ALA A 1 346 ? -47.697 -7.033 -1.832 1.00 19.41 ? 371 ALA A C 1 ATOM 2753 O O . ALA A 1 346 ? -47.392 -7.726 -2.801 1.00 19.54 ? 371 ALA A O 1 ATOM 2754 C CB . ALA A 1 346 ? -48.411 -4.641 -2.092 1.00 18.23 ? 371 ALA A CB 1 ATOM 2755 N N . PHE A 1 347 ? -47.024 -7.066 -0.684 1.00 17.95 ? 372 PHE A N 1 ATOM 2756 C CA . PHE A 1 347 ? -45.944 -8.024 -0.486 1.00 18.58 ? 372 PHE A CA 1 ATOM 2757 C C . PHE A 1 347 ? -46.454 -9.466 -0.483 1.00 17.89 ? 372 PHE A C 1 ATOM 2758 O O . PHE A 1 347 ? -45.795 -10.359 -1.017 1.00 18.79 ? 372 PHE A O 1 ATOM 2759 C CB . PHE A 1 347 ? -45.182 -7.726 0.806 1.00 18.26 ? 372 PHE A CB 1 ATOM 2760 C CG . PHE A 1 347 ? -44.269 -6.531 0.711 1.00 20.57 ? 372 PHE A CG 1 ATOM 2761 C CD1 . PHE A 1 347 ? -43.252 -6.489 -0.234 1.00 17.31 ? 372 PHE A CD1 1 ATOM 2762 C CD2 . PHE A 1 347 ? -44.422 -5.450 1.563 1.00 20.05 ? 372 PHE A CD2 1 ATOM 2763 C CE1 . PHE A 1 347 ? -42.406 -5.393 -0.321 1.00 19.12 ? 372 PHE A CE1 1 ATOM 2764 C CE2 . PHE A 1 347 ? -43.575 -4.347 1.476 1.00 21.38 ? 372 PHE A CE2 1 ATOM 2765 C CZ . PHE A 1 347 ? -42.566 -4.325 0.536 1.00 21.21 ? 372 PHE A CZ 1 ATOM 2766 N N . TYR A 1 348 ? -47.614 -9.702 0.127 1.00 19.33 ? 373 TYR A N 1 ATOM 2767 C CA . TYR A 1 348 ? -48.176 -11.050 0.142 1.00 19.02 ? 373 TYR A CA 1 ATOM 2768 C C . TYR A 1 348 ? -48.415 -11.558 -1.281 1.00 17.70 ? 373 TYR A C 1 ATOM 2769 O O . TYR A 1 348 ? -48.025 -12.675 -1.625 1.00 19.90 ? 373 TYR A O 1 ATOM 2770 C CB . TYR A 1 348 ? -49.477 -11.086 0.952 1.00 17.24 ? 373 TYR A CB 1 ATOM 2771 C CG . TYR A 1 348 ? -49.916 -12.478 1.365 1.00 19.83 ? 373 TYR A CG 1 ATOM 2772 C CD1 . TYR A 1 348 ? -49.511 -13.024 2.577 1.00 20.24 ? 373 TYR A CD1 1 ATOM 2773 C CD2 . TYR A 1 348 ? -50.741 -13.243 0.546 1.00 23.03 ? 373 TYR A CD2 1 ATOM 2774 C CE1 . TYR A 1 348 ? -49.914 -14.292 2.967 1.00 23.37 ? 373 TYR A CE1 1 ATOM 2775 C CE2 . TYR A 1 348 ? -51.149 -14.517 0.929 1.00 22.19 ? 373 TYR A CE2 1 ATOM 2776 C CZ . TYR A 1 348 ? -50.730 -15.032 2.141 1.00 22.67 ? 373 TYR A CZ 1 ATOM 2777 O OH . TYR A 1 348 ? -51.133 -16.297 2.518 1.00 26.02 ? 373 TYR A OH 1 ATOM 2778 N N . GLY A 1 349 ? -49.047 -10.732 -2.109 1.00 18.74 ? 374 GLY A N 1 ATOM 2779 C CA . GLY A 1 349 ? -49.339 -11.115 -3.481 1.00 18.40 ? 374 GLY A CA 1 ATOM 2780 C C . GLY A 1 349 ? -48.088 -11.249 -4.334 1.00 18.87 ? 374 GLY A C 1 ATOM 2781 O O . GLY A 1 349 ? -48.013 -12.102 -5.222 1.00 19.13 ? 374 GLY A O 1 ATOM 2782 N N . LEU A 1 350 ? -47.097 -10.406 -4.072 1.00 18.37 ? 375 LEU A N 1 ATOM 2783 C CA . LEU A 1 350 ? -45.829 -10.499 -4.784 1.00 17.69 ? 375 LEU A CA 1 ATOM 2784 C C . LEU A 1 350 ? -45.167 -11.832 -4.462 1.00 19.84 ? 375 LEU A C 1 ATOM 2785 O O . LEU A 1 350 ? -44.663 -12.524 -5.344 1.00 19.51 ? 375 LEU A O 1 ATOM 2786 C CB . LEU A 1 350 ? -44.914 -9.331 -4.397 1.00 19.52 ? 375 LEU A CB 1 ATOM 2787 C CG . LEU A 1 350 ? -43.631 -9.065 -5.183 1.00 24.11 ? 375 LEU A CG 1 ATOM 2788 C CD1 . LEU A 1 350 ? -43.890 -9.037 -6.686 1.00 22.43 ? 375 LEU A CD1 1 ATOM 2789 C CD2 . LEU A 1 350 ? -43.061 -7.740 -4.718 1.00 22.68 ? 375 LEU A CD2 1 ATOM 2790 N N . LEU A 1 351 ? -45.167 -12.186 -3.182 1.00 18.87 ? 376 LEU A N 1 ATOM 2791 C CA . LEU A 1 351 ? -44.585 -13.443 -2.742 1.00 20.38 ? 376 LEU A CA 1 ATOM 2792 C C . LEU A 1 351 ? -45.346 -14.663 -3.278 1.00 19.76 ? 376 LEU A C 1 ATOM 2793 O O . LEU A 1 351 ? -44.734 -15.678 -3.613 1.00 20.65 ? 376 LEU A O 1 ATOM 2794 C CB . LEU A 1 351 ? -44.479 -13.477 -1.213 1.00 18.88 ? 376 LEU A CB 1 ATOM 2795 C CG . LEU A 1 351 ? -43.461 -12.492 -0.627 1.00 19.53 ? 376 LEU A CG 1 ATOM 2796 C CD1 . LEU A 1 351 ? -43.593 -12.394 0.890 1.00 19.86 ? 376 LEU A CD1 1 ATOM 2797 C CD2 . LEU A 1 351 ? -42.033 -12.899 -1.008 1.00 22.75 ? 376 LEU A CD2 1 ATOM 2798 N N . GLU A 1 352 ? -46.671 -14.568 -3.368 1.00 19.32 ? 377 GLU A N 1 ATOM 2799 C CA . GLU A 1 352 ? -47.462 -15.660 -3.939 1.00 18.40 ? 377 GLU A CA 1 ATOM 2800 C C . GLU A 1 352 ? -47.048 -15.893 -5.389 1.00 21.99 ? 377 GLU A C 1 ATOM 2801 O O . GLU A 1 352 ? -46.871 -17.032 -5.826 1.00 22.58 ? 377 GLU A O 1 ATOM 2802 C CB . GLU A 1 352 ? -48.958 -15.351 -3.881 1.00 20.50 ? 377 GLU A CB 1 ATOM 2803 C CG . GLU A 1 352 ? -49.594 -15.481 -2.511 1.00 23.92 ? 377 GLU A CG 1 ATOM 2804 C CD . GLU A 1 352 ? -51.066 -15.109 -2.543 1.00 31.89 ? 377 GLU A CD 1 ATOM 2805 O OE1 . GLU A 1 352 ? -51.379 -13.961 -2.928 1.00 31.70 ? 377 GLU A OE1 1 ATOM 2806 O OE2 . GLU A 1 352 ? -51.908 -15.964 -2.192 1.00 31.63 ? 377 GLU A OE2 1 ATOM 2807 N N . ARG A 1 353 ? -46.873 -14.802 -6.125 1.00 20.47 ? 378 ARG A N 1 ATOM 2808 C CA . ARG A 1 353 ? -46.489 -14.896 -7.527 1.00 19.91 ? 378 ARG A CA 1 ATOM 2809 C C . ARG A 1 353 ? -45.065 -15.448 -7.688 1.00 22.21 ? 378 ARG A C 1 ATOM 2810 O O . ARG A 1 353 ? -44.800 -16.271 -8.572 1.00 20.60 ? 378 ARG A O 1 ATOM 2811 C CB . ARG A 1 353 ? -46.680 -13.534 -8.209 1.00 18.64 ? 378 ARG A CB 1 ATOM 2812 C CG . ARG A 1 353 ? -48.171 -13.193 -8.374 1.00 19.09 ? 378 ARG A CG 1 ATOM 2813 C CD . ARG A 1 353 ? -48.436 -11.722 -8.685 1.00 20.84 ? 378 ARG A CD 1 ATOM 2814 N NE . ARG A 1 353 ? -49.851 -11.503 -8.981 1.00 22.64 ? 378 ARG A NE 1 ATOM 2815 C CZ . ARG A 1 353 ? -50.828 -11.511 -8.075 1.00 34.09 ? 378 ARG A CZ 1 ATOM 2816 N NH1 . ARG A 1 353 ? -50.564 -11.727 -6.789 1.00 28.92 ? 378 ARG A NH1 1 ATOM 2817 N NH2 . ARG A 1 353 ? -52.081 -11.305 -8.459 1.00 34.22 ? 378 ARG A NH2 1 ATOM 2818 N N . LEU A 1 354 ? -44.156 -15.013 -6.822 1.00 20.15 ? 379 LEU A N 1 ATOM 2819 C CA . LEU A 1 354 ? -42.810 -15.579 -6.793 1.00 18.28 ? 379 LEU A CA 1 ATOM 2820 C C . LEU A 1 354 ? -42.838 -17.082 -6.498 1.00 22.58 ? 379 LEU A C 1 ATOM 2821 O O . LEU A 1 354 ? -42.070 -17.848 -7.075 1.00 21.05 ? 379 LEU A O 1 ATOM 2822 C CB . LEU A 1 354 ? -41.928 -14.840 -5.776 1.00 18.08 ? 379 LEU A CB 1 ATOM 2823 C CG . LEU A 1 354 ? -41.493 -13.434 -6.197 1.00 20.22 ? 379 LEU A CG 1 ATOM 2824 C CD1 . LEU A 1 354 ? -41.035 -12.623 -4.993 1.00 19.77 ? 379 LEU A CD1 1 ATOM 2825 C CD2 . LEU A 1 354 ? -40.404 -13.479 -7.270 1.00 20.55 ? 379 LEU A CD2 1 ATOM 2826 N N . SER A 1 355 ? -43.728 -17.505 -5.606 1.00 21.43 ? 380 SER A N 1 ATOM 2827 C CA . SER A 1 355 ? -43.790 -18.914 -5.225 1.00 21.69 ? 380 SER A CA 1 ATOM 2828 C C . SER A 1 355 ? -44.219 -19.801 -6.395 1.00 21.33 ? 380 SER A C 1 ATOM 2829 O O . SER A 1 355 ? -43.948 -21.004 -6.411 1.00 25.02 ? 380 SER A O 1 ATOM 2830 C CB . SER A 1 355 ? -44.729 -19.107 -4.033 1.00 24.31 ? 380 SER A CB 1 ATOM 2831 O OG . SER A 1 355 ? -46.086 -19.067 -4.436 1.00 26.98 ? 380 SER A OG 1 ATOM 2832 N N . LYS A 1 356 ? -44.872 -19.195 -7.378 1.00 20.93 ? 381 LYS A N 1 ATOM 2833 C CA . LYS A 1 356 ? -45.366 -19.929 -8.535 1.00 24.15 ? 381 LYS A CA 1 ATOM 2834 C C . LYS A 1 356 ? -44.365 -19.907 -9.679 1.00 23.68 ? 381 LYS A C 1 ATOM 2835 O O . LYS A 1 356 ? -44.535 -20.609 -10.674 1.00 25.98 ? 381 LYS A O 1 ATOM 2836 C CB . LYS A 1 356 ? -46.698 -19.340 -8.998 1.00 23.27 ? 381 LYS A CB 1 ATOM 2837 C CG . LYS A 1 356 ? -47.829 -19.576 -8.011 1.00 25.35 ? 381 LYS A CG 1 ATOM 2838 C CD . LYS A 1 356 ? -49.096 -18.849 -8.426 1.00 35.84 ? 381 LYS A CD 1 ATOM 2839 C CE . LYS A 1 356 ? -50.214 -19.091 -7.423 1.00 49.71 ? 381 LYS A CE 1 ATOM 2840 N NZ . LYS A 1 356 ? -51.469 -18.390 -7.808 1.00 59.19 ? 381 LYS A NZ 1 ATOM 2841 N N . GLU A 1 357 ? -43.322 -19.093 -9.535 1.00 23.00 ? 382 GLU A N 1 ATOM 2842 C CA . GLU A 1 357 ? -42.303 -18.971 -10.573 1.00 22.16 ? 382 GLU A CA 1 ATOM 2843 C C . GLU A 1 357 ? -40.905 -18.843 -9.968 1.00 21.73 ? 382 GLU A C 1 ATOM 2844 O O . GLU A 1 357 ? -40.403 -17.735 -9.779 1.00 22.31 ? 382 GLU A O 1 ATOM 2845 C CB . GLU A 1 357 ? -42.601 -17.773 -11.477 1.00 23.00 ? 382 GLU A CB 1 ATOM 2846 C CG . GLU A 1 357 ? -41.605 -17.624 -12.609 1.00 25.45 ? 382 GLU A CG 1 ATOM 2847 C CD . GLU A 1 357 ? -41.320 -18.952 -13.280 1.00 23.85 ? 382 GLU A CD 1 ATOM 2848 O OE1 . GLU A 1 357 ? -40.310 -19.600 -12.922 1.00 24.58 ? 382 GLU A OE1 1 ATOM 2849 O OE2 . GLU A 1 357 ? -42.121 -19.358 -14.148 1.00 28.01 ? 382 GLU A OE2 1 ATOM 2850 N N . PRO A 1 358 ? -40.272 -19.985 -9.666 1.00 23.15 ? 383 PRO A N 1 ATOM 2851 C CA . PRO A 1 358 ? -38.972 -19.983 -8.987 1.00 22.39 ? 383 PRO A CA 1 ATOM 2852 C C . PRO A 1 358 ? -37.868 -19.295 -9.789 1.00 24.77 ? 383 PRO A C 1 ATOM 2853 O O . PRO A 1 358 ? -36.819 -18.996 -9.218 1.00 23.47 ? 383 PRO A O 1 ATOM 2854 C CB . PRO A 1 358 ? -38.654 -21.475 -8.831 1.00 25.06 ? 383 PRO A CB 1 ATOM 2855 C CG . PRO A 1 358 ? -39.972 -22.155 -8.905 1.00 29.92 ? 383 PRO A CG 1 ATOM 2856 C CD . PRO A 1 358 ? -40.796 -21.350 -9.849 1.00 24.34 ? 383 PRO A CD 1 ATOM 2857 N N . ASN A 1 359 ? -38.089 -19.062 -11.081 1.00 21.73 ? 384 ASN A N 1 ATOM 2858 C CA . ASN A 1 359 ? -37.108 -18.344 -11.897 1.00 22.12 ? 384 ASN A CA 1 ATOM 2859 C C . ASN A 1 359 ? -37.212 -16.831 -11.741 1.00 22.04 ? 384 ASN A C 1 ATOM 2860 O O . ASN A 1 359 ? -36.392 -16.085 -12.275 1.00 21.10 ? 384 ASN A O 1 ATOM 2861 C CB . ASN A 1 359 ? -37.242 -18.718 -13.378 1.00 21.78 ? 384 ASN A CB 1 ATOM 2862 C CG . ASN A 1 359 ? -36.667 -20.087 -13.694 1.00 30.47 ? 384 ASN A CG 1 ATOM 2863 O OD1 . ASN A 1 359 ? -37.118 -21.103 -13.164 1.00 31.86 ? 384 ASN A OD1 1 ATOM 2864 N ND2 . ASN A 1 359 ? -35.677 -20.121 -14.579 1.00 31.77 ? 384 ASN A ND2 1 ATOM 2865 N N . GLY A 1 360 ? -38.225 -16.377 -11.014 1.00 22.24 ? 385 GLY A N 1 ATOM 2866 C CA . GLY A 1 360 ? -38.377 -14.956 -10.766 1.00 19.53 ? 385 GLY A CA 1 ATOM 2867 C C . GLY A 1 360 ? -37.711 -14.551 -9.465 1.00 20.65 ? 385 GLY A C 1 ATOM 2868 O O . GLY A 1 360 ? -37.581 -15.357 -8.543 1.00 22.23 ? 385 GLY A O 1 ATOM 2869 N N . PHE A 1 361 ? -37.273 -13.301 -9.389 1.00 20.39 ? 386 PHE A N 1 ATOM 2870 C CA . PHE A 1 361 ? -36.795 -12.762 -8.124 1.00 19.78 ? 386 PHE A CA 1 ATOM 2871 C C . PHE A 1 361 ? -37.026 -11.260 -8.051 1.00 19.54 ? 386 PHE A C 1 ATOM 2872 O O . PHE A 1 361 ? -37.332 -10.617 -9.061 1.00 20.37 ? 386 PHE A O 1 ATOM 2873 C CB . PHE A 1 361 ? -35.338 -13.168 -7.814 1.00 22.81 ? 386 PHE A CB 1 ATOM 2874 C CG . PHE A 1 361 ? -34.292 -12.572 -8.733 1.00 24.57 ? 386 PHE A CG 1 ATOM 2875 C CD1 . PHE A 1 361 ? -33.635 -11.395 -8.393 1.00 26.49 ? 386 PHE A CD1 1 ATOM 2876 C CD2 . PHE A 1 361 ? -33.923 -13.225 -9.902 1.00 28.63 ? 386 PHE A CD2 1 ATOM 2877 C CE1 . PHE A 1 361 ? -32.652 -10.858 -9.226 1.00 26.46 ? 386 PHE A CE1 1 ATOM 2878 C CE2 . PHE A 1 361 ? -32.942 -12.696 -10.737 1.00 27.53 ? 386 PHE A CE2 1 ATOM 2879 C CZ . PHE A 1 361 ? -32.307 -11.514 -10.396 1.00 28.74 ? 386 PHE A CZ 1 ATOM 2880 N N . ILE A 1 362 ? -36.928 -10.706 -6.849 1.00 18.51 ? 387 ILE A N 1 ATOM 2881 C CA . ILE A 1 362 ? -37.073 -9.270 -6.685 1.00 19.43 ? 387 ILE A CA 1 ATOM 2882 C C . ILE A 1 362 ? -35.853 -8.688 -5.992 1.00 17.68 ? 387 ILE A C 1 ATOM 2883 O O . ILE A 1 362 ? -35.155 -9.381 -5.250 1.00 19.27 ? 387 ILE A O 1 ATOM 2884 C CB . ILE A 1 362 ? -38.344 -8.895 -5.900 1.00 15.77 ? 387 ILE A CB 1 ATOM 2885 C CG1 . ILE A 1 362 ? -38.355 -9.583 -4.528 1.00 19.65 ? 387 ILE A CG1 1 ATOM 2886 C CG2 . ILE A 1 362 ? -39.589 -9.235 -6.710 1.00 18.48 ? 387 ILE A CG2 1 ATOM 2887 C CD1 . ILE A 1 362 ? -39.601 -9.281 -3.708 1.00 22.10 ? 387 ILE A CD1 1 ATOM 2888 N N . ALA A 1 363 ? -35.586 -7.416 -6.257 1.00 18.78 ? 388 ALA A N 1 ATOM 2889 C CA . ALA A 1 363 ? -34.545 -6.687 -5.550 1.00 18.05 ? 388 ALA A CA 1 ATOM 2890 C C . ALA A 1 363 ? -35.178 -5.431 -4.980 1.00 19.03 ? 388 ALA A C 1 ATOM 2891 O O . ALA A 1 363 ? -35.827 -4.676 -5.705 1.00 19.57 ? 388 ALA A O 1 ATOM 2892 C CB . ALA A 1 363 ? -33.388 -6.340 -6.483 1.00 18.44 ? 388 ALA A CB 1 ATOM 2893 N N . LEU A 1 364 ? -35.014 -5.225 -3.677 1.00 15.30 ? 389 LEU A N 1 ATOM 2894 C CA . LEU A 1 364 ? -35.661 -4.115 -2.981 1.00 16.64 ? 389 LEU A CA 1 ATOM 2895 C C . LEU A 1 364 ? -34.647 -3.157 -2.361 1.00 16.73 ? 389 LEU A C 1 ATOM 2896 O O . LEU A 1 364 ? -33.750 -3.576 -1.624 1.00 16.53 ? 389 LEU A O 1 ATOM 2897 C CB . LEU A 1 364 ? -36.579 -4.653 -1.877 1.00 15.86 ? 389 LEU A CB 1 ATOM 2898 C CG . LEU A 1 364 ? -37.641 -5.673 -2.298 1.00 18.59 ? 389 LEU A CG 1 ATOM 2899 C CD1 . LEU A 1 364 ? -38.322 -6.261 -1.060 1.00 19.97 ? 389 LEU A CD1 1 ATOM 2900 C CD2 . LEU A 1 364 ? -38.654 -5.044 -3.228 1.00 24.20 ? 389 LEU A CD2 1 ATOM 2901 N N . ASN A 1 365 ? -34.814 -1.865 -2.638 1.00 17.03 ? 390 ASN A N 1 ATOM 2902 C CA . ASN A 1 365 ? -33.934 -0.827 -2.102 1.00 15.66 ? 390 ASN A CA 1 ATOM 2903 C C . ASN A 1 365 ? -34.725 0.338 -1.570 1.00 17.60 ? 390 ASN A C 1 ATOM 2904 O O . ASN A 1 365 ? -35.708 0.761 -2.178 1.00 18.62 ? 390 ASN A O 1 ATOM 2905 C CB . ASN A 1 365 ? -33.014 -0.292 -3.200 1.00 16.31 ? 390 ASN A CB 1 ATOM 2906 C CG . ASN A 1 365 ? -31.789 -1.144 -3.394 1.00 23.79 ? 390 ASN A CG 1 ATOM 2907 O OD1 . ASN A 1 365 ? -30.864 -1.115 -2.580 1.00 23.01 ? 390 ASN A OD1 1 ATOM 2908 N ND2 . ASN A 1 365 ? -31.763 -1.896 -4.481 1.00 22.04 ? 390 ASN A ND2 1 ATOM 2909 N N . GLY A 1 366 ? -34.298 0.854 -0.427 1.00 17.29 ? 391 GLY A N 1 ATOM 2910 C CA . GLY A 1 366 ? -34.882 2.058 0.119 1.00 16.63 ? 391 GLY A CA 1 ATOM 2911 C C . GLY A 1 366 ? -34.112 3.275 -0.349 1.00 16.18 ? 391 GLY A C 1 ATOM 2912 O O . GLY A 1 366 ? -32.893 3.218 -0.545 1.00 18.85 ? 391 GLY A O 1 ATOM 2913 N N . PHE A 1 367 ? -34.827 4.374 -0.555 1.00 16.44 ? 392 PHE A N 1 ATOM 2914 C CA . PHE A 1 367 ? -34.173 5.653 -0.787 1.00 17.79 ? 392 PHE A CA 1 ATOM 2915 C C . PHE A 1 367 ? -34.085 6.370 0.562 1.00 18.99 ? 392 PHE A C 1 ATOM 2916 O O . PHE A 1 367 ? -33.763 5.738 1.573 1.00 18.17 ? 392 PHE A O 1 ATOM 2917 C CB . PHE A 1 367 ? -34.925 6.472 -1.846 1.00 17.64 ? 392 PHE A CB 1 ATOM 2918 C CG . PHE A 1 367 ? -34.634 6.055 -3.271 1.00 18.18 ? 392 PHE A CG 1 ATOM 2919 C CD1 . PHE A 1 367 ? -34.110 4.803 -3.562 1.00 20.52 ? 392 PHE A CD1 1 ATOM 2920 C CD2 . PHE A 1 367 ? -34.891 6.916 -4.319 1.00 20.00 ? 392 PHE A CD2 1 ATOM 2921 C CE1 . PHE A 1 367 ? -33.848 4.425 -4.880 1.00 19.97 ? 392 PHE A CE1 1 ATOM 2922 C CE2 . PHE A 1 367 ? -34.638 6.538 -5.636 1.00 19.03 ? 392 PHE A CE2 1 ATOM 2923 C CZ . PHE A 1 367 ? -34.121 5.296 -5.915 1.00 19.45 ? 392 PHE A CZ 1 ATOM 2924 N N . GLY A 1 368 ? -34.377 7.667 0.605 1.00 17.51 ? 393 GLY A N 1 ATOM 2925 C CA . GLY A 1 368 ? -34.176 8.418 1.833 1.00 18.29 ? 393 GLY A CA 1 ATOM 2926 C C . GLY A 1 368 ? -32.706 8.768 1.987 1.00 17.33 ? 393 GLY A C 1 ATOM 2927 O O . GLY A 1 368 ? -31.923 8.665 1.034 1.00 18.66 ? 393 GLY A O 1 ATOM 2928 N N . GLY A 1 369 ? -32.317 9.183 3.187 1.00 19.91 ? 394 GLY A N 1 ATOM 2929 C CA . GLY A 1 369 ? -30.945 9.598 3.404 1.00 18.41 ? 394 GLY A CA 1 ATOM 2930 C C . GLY A 1 369 ? -30.564 10.714 2.449 1.00 17.76 ? 394 GLY A C 1 ATOM 2931 O O . GLY A 1 369 ? -31.334 11.649 2.232 1.00 20.51 ? 394 GLY A O 1 ATOM 2932 N N . GLN A 1 370 ? -29.379 10.614 1.858 1.00 18.29 ? 395 GLN A N 1 ATOM 2933 C CA A GLN A 1 370 ? -28.866 11.627 0.941 0.50 19.09 ? 395 GLN A CA 1 ATOM 2934 C CA B GLN A 1 370 ? -28.917 11.678 0.976 0.50 19.33 ? 395 GLN A CA 1 ATOM 2935 C C . GLN A 1 370 ? -29.730 11.754 -0.314 1.00 19.37 ? 395 GLN A C 1 ATOM 2936 O O . GLN A 1 370 ? -29.755 12.801 -0.964 1.00 21.16 ? 395 GLN A O 1 ATOM 2937 C CB A GLN A 1 370 ? -27.425 11.285 0.551 0.50 18.17 ? 395 GLN A CB 1 ATOM 2938 C CB B GLN A 1 370 ? -27.420 11.556 0.686 0.50 21.71 ? 395 GLN A CB 1 ATOM 2939 C CG A GLN A 1 370 ? -26.800 12.219 -0.473 0.50 20.24 ? 395 GLN A CG 1 ATOM 2940 C CG B GLN A 1 370 ? -26.537 12.057 1.821 0.50 24.91 ? 395 GLN A CG 1 ATOM 2941 C CD A GLN A 1 370 ? -26.413 13.567 0.110 0.50 21.83 ? 395 GLN A CD 1 ATOM 2942 C CD B GLN A 1 370 ? -26.695 13.546 2.092 0.50 18.51 ? 395 GLN A CD 1 ATOM 2943 O OE1 A GLN A 1 370 ? -26.750 13.888 1.249 0.50 27.85 ? 395 GLN A OE1 1 ATOM 2944 O OE1 B GLN A 1 370 ? -26.932 14.338 1.178 0.50 24.62 ? 395 GLN A OE1 1 ATOM 2945 N NE2 A GLN A 1 370 ? -25.692 14.363 -0.676 0.50 21.58 ? 395 GLN A NE2 1 ATOM 2946 N NE2 B GLN A 1 370 ? -26.543 13.934 3.355 0.50 21.79 ? 395 GLN A NE2 1 ATOM 2947 N N . MET A 1 371 ? -30.423 10.677 -0.668 1.00 19.81 ? 396 MET A N 1 ATOM 2948 C CA . MET A 1 371 ? -31.269 10.728 -1.858 1.00 19.38 ? 396 MET A CA 1 ATOM 2949 C C . MET A 1 371 ? -32.412 11.733 -1.694 1.00 25.46 ? 396 MET A C 1 ATOM 2950 O O . MET A 1 371 ? -32.924 12.248 -2.684 1.00 27.94 ? 396 MET A O 1 ATOM 2951 C CB . MET A 1 371 ? -31.806 9.343 -2.238 1.00 19.02 ? 396 MET A CB 1 ATOM 2952 C CG . MET A 1 371 ? -30.732 8.389 -2.765 1.00 18.08 ? 396 MET A CG 1 ATOM 2953 S SD . MET A 1 371 ? -30.017 8.894 -4.346 1.00 18.29 ? 396 MET A SD 1 ATOM 2954 C CE . MET A 1 371 ? -31.366 8.547 -5.490 1.00 19.22 ? 396 MET A CE 1 ATOM 2955 N N . SER A 1 372 ? -32.798 12.021 -0.450 1.00 20.32 ? 397 SER A N 1 ATOM 2956 C CA . SER A 1 372 ? -33.840 13.014 -0.174 1.00 22.82 ? 397 SER A CA 1 ATOM 2957 C C . SER A 1 372 ? -33.299 14.435 -0.041 1.00 23.89 ? 397 SER A C 1 ATOM 2958 O O . SER A 1 372 ? -34.068 15.397 -0.003 1.00 27.47 ? 397 SER A O 1 ATOM 2959 C CB . SER A 1 372 ? -34.608 12.657 1.101 1.00 22.85 ? 397 SER A CB 1 ATOM 2960 O OG . SER A 1 372 ? -35.402 11.509 0.906 1.00 23.45 ? 397 SER A OG 1 ATOM 2961 N N . LYS A 1 373 ? -31.981 14.569 0.044 1.00 20.18 ? 398 LYS A N 1 ATOM 2962 C CA . LYS A 1 373 ? -31.370 15.876 0.251 1.00 22.15 ? 398 LYS A CA 1 ATOM 2963 C C . LYS A 1 373 ? -30.821 16.470 -1.040 1.00 21.48 ? 398 LYS A C 1 ATOM 2964 O O . LYS A 1 373 ? -30.503 17.655 -1.105 1.00 32.22 ? 398 LYS A O 1 ATOM 2965 C CB . LYS A 1 373 ? -30.280 15.789 1.319 1.00 27.24 ? 398 LYS A CB 1 ATOM 2966 C CG . LYS A 1 373 ? -30.828 15.402 2.684 1.00 29.22 ? 398 LYS A CG 1 ATOM 2967 C CD . LYS A 1 373 ? -29.740 15.302 3.737 1.00 32.69 ? 398 LYS A CD 1 ATOM 2968 C CE . LYS A 1 373 ? -30.349 15.027 5.108 1.00 39.97 ? 398 LYS A CE 1 ATOM 2969 N NZ . LYS A 1 373 ? -29.306 14.829 6.151 1.00 46.38 ? 398 LYS A NZ 1 ATOM 2970 N N . ILE A 1 374 ? -30.709 15.635 -2.066 1.00 19.86 ? 399 ILE A N 1 ATOM 2971 C CA . ILE A 1 374 ? -30.288 16.086 -3.380 1.00 22.47 ? 399 ILE A CA 1 ATOM 2972 C C . ILE A 1 374 ? -31.513 16.577 -4.148 1.00 20.64 ? 399 ILE A C 1 ATOM 2973 O O . ILE A 1 374 ? -32.551 15.910 -4.169 1.00 21.20 ? 399 ILE A O 1 ATOM 2974 C CB . ILE A 1 374 ? -29.580 14.947 -4.135 1.00 18.86 ? 399 ILE A CB 1 ATOM 2975 C CG1 . ILE A 1 374 ? -28.286 14.560 -3.404 1.00 19.82 ? 399 ILE A CG1 1 ATOM 2976 C CG2 . ILE A 1 374 ? -29.313 15.341 -5.573 1.00 20.02 ? 399 ILE A CG2 1 ATOM 2977 C CD1 . ILE A 1 374 ? -27.680 13.237 -3.861 1.00 21.83 ? 399 ILE A CD1 1 ATOM 2978 N N . SER A 1 375 ? -31.406 17.753 -4.759 1.00 20.89 ? 400 SER A N 1 ATOM 2979 C CA . SER A 1 375 ? -32.543 18.345 -5.450 1.00 19.15 ? 400 SER A CA 1 ATOM 2980 C C . SER A 1 375 ? -32.921 17.507 -6.668 1.00 22.44 ? 400 SER A C 1 ATOM 2981 O O . SER A 1 375 ? -32.058 16.868 -7.271 1.00 22.56 ? 400 SER A O 1 ATOM 2982 C CB . SER A 1 375 ? -32.218 19.779 -5.873 1.00 28.73 ? 400 SER A CB 1 ATOM 2983 O OG . SER A 1 375 ? -33.304 20.348 -6.579 1.00 41.46 ? 400 SER A OG 1 ATOM 2984 N N . SER A 1 376 ? -34.203 17.507 -7.022 1.00 21.67 ? 401 SER A N 1 ATOM 2985 C CA . SER A 1 376 ? -34.674 16.718 -8.159 1.00 18.96 ? 401 SER A CA 1 ATOM 2986 C C . SER A 1 376 ? -34.036 17.146 -9.473 1.00 20.44 ? 401 SER A C 1 ATOM 2987 O O . SER A 1 376 ? -33.984 16.361 -10.417 1.00 19.90 ? 401 SER A O 1 ATOM 2988 C CB . SER A 1 376 ? -36.201 16.771 -8.280 1.00 20.11 ? 401 SER A CB 1 ATOM 2989 O OG . SER A 1 376 ? -36.631 18.072 -8.659 1.00 26.73 ? 401 SER A OG 1 ATOM 2990 N N . ASP A 1 377 ? -33.549 18.381 -9.541 1.00 21.73 ? 402 ASP A N 1 ATOM 2991 C CA . ASP A 1 377 ? -32.907 18.836 -10.773 1.00 22.42 ? 402 ASP A CA 1 ATOM 2992 C C . ASP A 1 377 ? -31.389 19.026 -10.673 1.00 21.12 ? 402 ASP A C 1 ATOM 2993 O O . ASP A 1 377 ? -30.777 19.569 -11.592 1.00 22.35 ? 402 ASP A O 1 ATOM 2994 C CB . ASP A 1 377 ? -33.586 20.094 -11.324 1.00 28.42 ? 402 ASP A CB 1 ATOM 2995 C CG . ASP A 1 377 ? -33.250 21.331 -10.532 1.00 33.03 ? 402 ASP A CG 1 ATOM 2996 O OD1 . ASP A 1 377 ? -32.925 21.208 -9.336 1.00 30.46 ? 402 ASP A OD1 1 ATOM 2997 O OD2 . ASP A 1 377 ? -33.319 22.436 -11.110 1.00 48.91 ? 402 ASP A OD2 1 ATOM 2998 N N . PHE A 1 378 ? -30.781 18.568 -9.581 1.00 20.22 ? 403 PHE A N 1 ATOM 2999 C CA . PHE A 1 378 ? -29.323 18.631 -9.450 1.00 17.71 ? 403 PHE A CA 1 ATOM 3000 C C . PHE A 1 378 ? -28.655 17.922 -10.631 1.00 18.48 ? 403 PHE A C 1 ATOM 3001 O O . PHE A 1 378 ? -27.737 18.456 -11.267 1.00 19.82 ? 403 PHE A O 1 ATOM 3002 C CB . PHE A 1 378 ? -28.863 18.023 -8.120 1.00 21.19 ? 403 PHE A CB 1 ATOM 3003 C CG . PHE A 1 378 ? -27.371 17.921 -7.993 1.00 23.75 ? 403 PHE A CG 1 ATOM 3004 C CD1 . PHE A 1 378 ? -26.596 19.065 -7.881 1.00 22.95 ? 403 PHE A CD1 1 ATOM 3005 C CD2 . PHE A 1 378 ? -26.743 16.688 -8.003 1.00 22.33 ? 403 PHE A CD2 1 ATOM 3006 C CE1 . PHE A 1 378 ? -25.219 18.979 -7.781 1.00 25.66 ? 403 PHE A CE1 1 ATOM 3007 C CE2 . PHE A 1 378 ? -25.370 16.595 -7.898 1.00 22.79 ? 403 PHE A CE2 1 ATOM 3008 C CZ . PHE A 1 378 ? -24.606 17.740 -7.790 1.00 24.20 ? 403 PHE A CZ 1 ATOM 3009 N N . THR A 1 379 ? -29.121 16.711 -10.911 1.00 18.25 ? 404 THR A N 1 ATOM 3010 C CA . THR A 1 379 ? -28.753 15.991 -12.125 1.00 18.57 ? 404 THR A CA 1 ATOM 3011 C C . THR A 1 379 ? -30.055 15.450 -12.729 1.00 19.38 ? 404 THR A C 1 ATOM 3012 O O . THR A 1 379 ? -31.119 15.598 -12.136 1.00 18.81 ? 404 THR A O 1 ATOM 3013 C CB . THR A 1 379 ? -27.722 14.861 -11.852 1.00 17.12 ? 404 THR A CB 1 ATOM 3014 O OG1 . THR A 1 379 ? -28.213 13.992 -10.822 1.00 19.92 ? 404 THR A OG1 1 ATOM 3015 C CG2 . THR A 1 379 ? -26.385 15.452 -11.415 1.00 18.85 ? 404 THR A CG2 1 ATOM 3016 N N . PRO A 1 380 ? -29.988 14.844 -13.921 1.00 17.23 ? 405 PRO A N 1 ATOM 3017 C CA . PRO A 1 380 ? -31.245 14.434 -14.561 1.00 18.59 ? 405 PRO A CA 1 ATOM 3018 C C . PRO A 1 380 ? -32.124 13.428 -13.802 1.00 15.30 ? 405 PRO A C 1 ATOM 3019 O O . PRO A 1 380 ? -33.336 13.451 -13.996 1.00 17.75 ? 405 PRO A O 1 ATOM 3020 C CB . PRO A 1 380 ? -30.771 13.873 -15.905 1.00 19.38 ? 405 PRO A CB 1 ATOM 3021 C CG . PRO A 1 380 ? -29.582 14.731 -16.228 1.00 17.91 ? 405 PRO A CG 1 ATOM 3022 C CD . PRO A 1 380 ? -28.880 14.913 -14.894 1.00 16.42 ? 405 PRO A CD 1 ATOM 3023 N N . PHE A 1 381 ? -31.542 12.564 -12.975 1.00 16.47 ? 406 PHE A N 1 ATOM 3024 C CA . PHE A 1 381 ? -32.338 11.594 -12.218 1.00 16.16 ? 406 PHE A CA 1 ATOM 3025 C C . PHE A 1 381 ? -33.189 12.354 -11.206 1.00 16.74 ? 406 PHE A C 1 ATOM 3026 O O . PHE A 1 381 ? -32.644 12.997 -10.305 1.00 17.48 ? 406 PHE A O 1 ATOM 3027 C CB . PHE A 1 381 ? -31.426 10.597 -11.497 1.00 17.72 ? 406 PHE A CB 1 ATOM 3028 C CG . PHE A 1 381 ? -32.163 9.535 -10.726 1.00 17.88 ? 406 PHE A CG 1 ATOM 3029 C CD1 . PHE A 1 381 ? -32.488 8.322 -11.319 1.00 19.94 ? 406 PHE A CD1 1 ATOM 3030 C CD2 . PHE A 1 381 ? -32.510 9.735 -9.395 1.00 16.51 ? 406 PHE A CD2 1 ATOM 3031 C CE1 . PHE A 1 381 ? -33.151 7.334 -10.606 1.00 22.55 ? 406 PHE A CE1 1 ATOM 3032 C CE2 . PHE A 1 381 ? -33.173 8.758 -8.676 1.00 16.32 ? 406 PHE A CE2 1 ATOM 3033 C CZ . PHE A 1 381 ? -33.497 7.552 -9.276 1.00 20.70 ? 406 PHE A CZ 1 ATOM 3034 N N . PRO A 1 382 ? -34.527 12.301 -11.356 1.00 17.11 ? 407 PRO A N 1 ATOM 3035 C CA . PRO A 1 382 ? -35.386 13.215 -10.596 1.00 17.24 ? 407 PRO A CA 1 ATOM 3036 C C . PRO A 1 382 ? -35.988 12.639 -9.322 1.00 18.75 ? 407 PRO A C 1 ATOM 3037 O O . PRO A 1 382 ? -36.630 13.392 -8.577 1.00 19.29 ? 407 PRO A O 1 ATOM 3038 C CB . PRO A 1 382 ? -36.506 13.495 -11.591 1.00 20.86 ? 407 PRO A CB 1 ATOM 3039 C CG . PRO A 1 382 ? -36.722 12.149 -12.221 1.00 17.62 ? 407 PRO A CG 1 ATOM 3040 C CD . PRO A 1 382 ? -35.303 11.560 -12.371 1.00 16.95 ? 407 PRO A CD 1 ATOM 3041 N N . HIS A 1 383 ? -35.803 11.347 -9.072 1.00 18.08 ? 408 HIS A N 1 ATOM 3042 C CA . HIS A 1 383 ? -36.539 10.686 -7.993 1.00 18.59 ? 408 HIS A CA 1 ATOM 3043 C C . HIS A 1 383 ? -35.811 10.803 -6.661 1.00 17.38 ? 408 HIS A C 1 ATOM 3044 O O . HIS A 1 383 ? -35.055 9.909 -6.259 1.00 18.95 ? 408 HIS A O 1 ATOM 3045 C CB . HIS A 1 383 ? -36.841 9.236 -8.365 1.00 19.33 ? 408 HIS A CB 1 ATOM 3046 C CG . HIS A 1 383 ? -37.386 9.082 -9.753 1.00 16.63 ? 408 HIS A CG 1 ATOM 3047 N ND1 . HIS A 1 383 ? -38.544 9.704 -10.168 1.00 20.99 ? 408 HIS A ND1 1 ATOM 3048 C CD2 . HIS A 1 383 ? -36.924 8.390 -10.823 1.00 20.79 ? 408 HIS A CD2 1 ATOM 3049 C CE1 . HIS A 1 383 ? -38.775 9.398 -11.435 1.00 22.39 ? 408 HIS A CE1 1 ATOM 3050 N NE2 . HIS A 1 383 ? -37.806 8.605 -11.855 1.00 21.05 ? 408 HIS A NE2 1 ATOM 3051 N N . ARG A 1 384 ? -36.046 11.925 -5.985 1.00 18.19 ? 409 ARG A N 1 ATOM 3052 C CA . ARG A 1 384 ? -35.307 12.265 -4.776 1.00 17.26 ? 409 ARG A CA 1 ATOM 3053 C C . ARG A 1 384 ? -36.279 12.327 -3.598 1.00 17.19 ? 409 ARG A C 1 ATOM 3054 O O . ARG A 1 384 ? -36.942 11.329 -3.306 1.00 17.69 ? 409 ARG A O 1 ATOM 3055 C CB . ARG A 1 384 ? -34.517 13.563 -4.987 1.00 18.08 ? 409 ARG A CB 1 ATOM 3056 C CG . ARG A 1 384 ? -33.672 13.544 -6.273 1.00 16.92 ? 409 ARG A CG 1 ATOM 3057 C CD . ARG A 1 384 ? -32.546 12.496 -6.255 1.00 16.79 ? 409 ARG A CD 1 ATOM 3058 N NE . ARG A 1 384 ? -31.638 12.771 -7.372 1.00 17.31 ? 409 ARG A NE 1 ATOM 3059 C CZ . ARG A 1 384 ? -30.351 12.436 -7.449 1.00 16.29 ? 409 ARG A CZ 1 ATOM 3060 N NH1 . ARG A 1 384 ? -29.746 11.748 -6.482 1.00 16.77 ? 409 ARG A NH1 1 ATOM 3061 N NH2 . ARG A 1 384 ? -29.666 12.803 -8.523 1.00 15.77 ? 409 ARG A NH2 1 ATOM 3062 N N . SER A 1 385 ? -36.391 13.474 -2.930 1.00 17.41 ? 410 SER A N 1 ATOM 3063 C CA . SER A 1 385 ? -37.339 13.588 -1.825 1.00 19.69 ? 410 SER A CA 1 ATOM 3064 C C . SER A 1 385 ? -38.728 13.095 -2.234 1.00 20.86 ? 410 SER A C 1 ATOM 3065 O O . SER A 1 385 ? -39.207 13.399 -3.326 1.00 21.28 ? 410 SER A O 1 ATOM 3066 C CB . SER A 1 385 ? -37.416 15.027 -1.324 1.00 21.75 ? 410 SER A CB 1 ATOM 3067 O OG . SER A 1 385 ? -38.238 15.113 -0.171 1.00 27.60 ? 410 SER A OG 1 ATOM 3068 N N . GLY A 1 386 ? -39.363 12.325 -1.358 1.00 20.05 ? 411 GLY A N 1 ATOM 3069 C CA . GLY A 1 386 ? -40.684 11.783 -1.641 1.00 22.25 ? 411 GLY A CA 1 ATOM 3070 C C . GLY A 1 386 ? -40.656 10.368 -2.195 1.00 23.52 ? 411 GLY A C 1 ATOM 3071 O O . GLY A 1 386 ? -41.653 9.642 -2.136 1.00 25.54 ? 411 GLY A O 1 ATOM 3072 N N . THR A 1 387 ? -39.515 9.966 -2.741 1.00 20.47 ? 412 THR A N 1 ATOM 3073 C CA . THR A 1 387 ? -39.356 8.613 -3.257 1.00 19.25 ? 412 THR A CA 1 ATOM 3074 C C . THR A 1 387 ? -38.975 7.692 -2.116 1.00 19.68 ? 412 THR A C 1 ATOM 3075 O O . THR A 1 387 ? -37.991 7.937 -1.416 1.00 22.29 ? 412 THR A O 1 ATOM 3076 C CB . THR A 1 387 ? -38.258 8.553 -4.318 1.00 20.45 ? 412 THR A CB 1 ATOM 3077 O OG1 . THR A 1 387 ? -38.458 9.611 -5.260 1.00 23.82 ? 412 THR A OG1 1 ATOM 3078 C CG2 . THR A 1 387 ? -38.283 7.217 -5.046 1.00 20.15 ? 412 THR A CG2 1 ATOM 3079 N N . ARG A 1 388 ? -39.756 6.635 -1.922 1.00 17.82 ? 413 ARG A N 1 ATOM 3080 C CA . ARG A 1 388 ? -39.545 5.738 -0.794 1.00 16.43 ? 413 ARG A CA 1 ATOM 3081 C C . ARG A 1 388 ? -38.705 4.516 -1.166 1.00 18.03 ? 413 ARG A C 1 ATOM 3082 O O . ARG A 1 388 ? -37.685 4.252 -0.533 1.00 18.83 ? 413 ARG A O 1 ATOM 3083 C CB . ARG A 1 388 ? -40.890 5.274 -0.228 1.00 17.17 ? 413 ARG A CB 1 ATOM 3084 C CG . ARG A 1 388 ? -41.723 6.398 0.369 1.00 21.80 ? 413 ARG A CG 1 ATOM 3085 C CD . ARG A 1 388 ? -42.975 5.848 1.046 1.00 23.22 ? 413 ARG A CD 1 ATOM 3086 N NE . ARG A 1 388 ? -43.810 6.905 1.613 1.00 27.18 ? 413 ARG A NE 1 ATOM 3087 C CZ . ARG A 1 388 ? -43.692 7.375 2.851 1.00 35.16 ? 413 ARG A CZ 1 ATOM 3088 N NH1 . ARG A 1 388 ? -42.760 6.892 3.665 1.00 31.76 ? 413 ARG A NH1 1 ATOM 3089 N NH2 . ARG A 1 388 ? -44.505 8.334 3.274 1.00 33.42 ? 413 ARG A NH2 1 ATOM 3090 N N . LEU A 1 389 ? -39.148 3.762 -2.171 1.00 16.78 ? 414 LEU A N 1 ATOM 3091 C CA . LEU A 1 389 ? -38.474 2.530 -2.551 1.00 15.81 ? 414 LEU A CA 1 ATOM 3092 C C . LEU A 1 389 ? -38.236 2.422 -4.036 1.00 16.15 ? 414 LEU A C 1 ATOM 3093 O O . LEU A 1 389 ? -38.941 3.042 -4.841 1.00 18.87 ? 414 LEU A O 1 ATOM 3094 C CB . LEU A 1 389 ? -39.319 1.312 -2.165 1.00 16.05 ? 414 LEU A CB 1 ATOM 3095 C CG . LEU A 1 389 ? -39.946 1.261 -0.777 1.00 18.65 ? 414 LEU A CG 1 ATOM 3096 C CD1 . LEU A 1 389 ? -40.887 0.063 -0.677 1.00 21.33 ? 414 LEU A CD1 1 ATOM 3097 C CD2 . LEU A 1 389 ? -38.856 1.183 0.281 1.00 20.66 ? 414 LEU A CD2 1 ATOM 3098 N N . MET A 1 390 ? -37.243 1.607 -4.380 1.00 15.51 ? 415 MET A N 1 ATOM 3099 C CA . MET A 1 390 ? -37.089 1.088 -5.732 1.00 16.09 ? 415 MET A CA 1 ATOM 3100 C C . MET A 1 390 ? -37.301 -0.423 -5.668 1.00 18.80 ? 415 MET A C 1 ATOM 3101 O O . MET A 1 390 ? -36.705 -1.110 -4.834 1.00 19.61 ? 415 MET A O 1 ATOM 3102 C CB . MET A 1 390 ? -35.707 1.407 -6.297 1.00 18.25 ? 415 MET A CB 1 ATOM 3103 C CG . MET A 1 390 ? -35.527 0.941 -7.737 1.00 18.80 ? 415 MET A CG 1 ATOM 3104 S SD . MET A 1 390 ? -34.213 1.800 -8.633 1.00 28.14 ? 415 MET A SD 1 ATOM 3105 C CE . MET A 1 390 ? -32.786 1.238 -7.716 1.00 33.22 ? 415 MET A CE 1 ATOM 3106 N N . VAL A 1 391 ? -38.160 -0.932 -6.542 1.00 16.35 ? 416 VAL A N 1 ATOM 3107 C CA . VAL A 1 391 ? -38.559 -2.332 -6.530 1.00 18.78 ? 416 VAL A CA 1 ATOM 3108 C C . VAL A 1 391 ? -38.311 -2.912 -7.911 1.00 19.71 ? 416 VAL A C 1 ATOM 3109 O O . VAL A 1 391 ? -38.914 -2.468 -8.892 1.00 19.73 ? 416 VAL A O 1 ATOM 3110 C CB . VAL A 1 391 ? -40.060 -2.466 -6.191 1.00 20.10 ? 416 VAL A CB 1 ATOM 3111 C CG1 . VAL A 1 391 ? -40.500 -3.929 -6.211 1.00 22.52 ? 416 VAL A CG1 1 ATOM 3112 C CG2 . VAL A 1 391 ? -40.359 -1.816 -4.838 1.00 23.24 ? 416 VAL A CG2 1 ATOM 3113 N N . GLU A 1 392 ? -37.409 -3.885 -7.994 1.00 17.13 ? 417 GLU A N 1 ATOM 3114 C CA A GLU A 1 392 ? -37.068 -4.512 -9.269 0.61 16.52 ? 417 GLU A CA 1 ATOM 3115 C CA B GLU A 1 392 ? -37.090 -4.509 -9.273 0.39 16.53 ? 417 GLU A CA 1 ATOM 3116 C C . GLU A 1 392 ? -37.642 -5.926 -9.333 1.00 18.16 ? 417 GLU A C 1 ATOM 3117 O O . GLU A 1 392 ? -37.562 -6.675 -8.355 1.00 18.62 ? 417 GLU A O 1 ATOM 3118 C CB A GLU A 1 392 ? -35.545 -4.543 -9.457 0.61 19.23 ? 417 GLU A CB 1 ATOM 3119 C CB B GLU A 1 392 ? -35.579 -4.520 -9.522 0.39 19.73 ? 417 GLU A CB 1 ATOM 3120 C CG A GLU A 1 392 ? -34.874 -3.172 -9.405 0.61 18.35 ? 417 GLU A CG 1 ATOM 3121 C CG B GLU A 1 392 ? -35.210 -4.980 -10.922 0.39 24.13 ? 417 GLU A CG 1 ATOM 3122 C CD A GLU A 1 392 ? -33.359 -3.268 -9.381 0.61 28.72 ? 417 GLU A CD 1 ATOM 3123 C CD B GLU A 1 392 ? -33.716 -5.123 -11.125 0.39 29.45 ? 417 GLU A CD 1 ATOM 3124 O OE1 A GLU A 1 392 ? -32.771 -3.686 -10.401 0.61 28.36 ? 417 GLU A OE1 1 ATOM 3125 O OE1 B GLU A 1 392 ? -32.961 -4.953 -10.146 0.39 27.32 ? 417 GLU A OE1 1 ATOM 3126 O OE2 A GLU A 1 392 ? -32.755 -2.918 -8.344 0.61 21.36 ? 417 GLU A OE2 1 ATOM 3127 O OE2 B GLU A 1 392 ? -33.297 -5.409 -12.269 0.39 29.14 ? 417 GLU A OE2 1 ATOM 3128 N N . TYR A 1 393 ? -38.227 -6.278 -10.479 1.00 16.59 ? 418 TYR A N 1 ATOM 3129 C CA . TYR A 1 393 ? -38.777 -7.613 -10.717 1.00 16.35 ? 418 TYR A CA 1 ATOM 3130 C C . TYR A 1 393 ? -37.999 -8.212 -11.873 1.00 19.54 ? 418 TYR A C 1 ATOM 3131 O O . TYR A 1 393 ? -37.859 -7.584 -12.917 1.00 20.12 ? 418 TYR A O 1 ATOM 3132 C CB . TYR A 1 393 ? -40.264 -7.558 -11.097 1.00 19.95 ? 418 TYR A CB 1 ATOM 3133 C CG . TYR A 1 393 ? -41.066 -6.469 -10.420 1.00 16.60 ? 418 TYR A CG 1 ATOM 3134 C CD1 . TYR A 1 393 ? -41.611 -6.664 -9.163 1.00 18.75 ? 418 TYR A CD1 1 ATOM 3135 C CD2 . TYR A 1 393 ? -41.272 -5.241 -11.044 1.00 19.21 ? 418 TYR A CD2 1 ATOM 3136 C CE1 . TYR A 1 393 ? -42.347 -5.672 -8.541 1.00 17.98 ? 418 TYR A CE1 1 ATOM 3137 C CE2 . TYR A 1 393 ? -42.011 -4.233 -10.428 1.00 18.19 ? 418 TYR A CE2 1 ATOM 3138 C CZ . TYR A 1 393 ? -42.545 -4.458 -9.174 1.00 17.58 ? 418 TYR A CZ 1 ATOM 3139 O OH . TYR A 1 393 ? -43.277 -3.474 -8.550 1.00 17.32 ? 418 TYR A OH 1 ATOM 3140 N N . ILE A 1 394 ? -37.487 -9.422 -11.688 1.00 18.35 ? 419 ILE A N 1 ATOM 3141 C CA . ILE A 1 394 ? -36.623 -10.040 -12.685 1.00 17.84 ? 419 ILE A CA 1 ATOM 3142 C C . ILE A 1 394 ? -37.068 -11.468 -12.913 1.00 19.13 ? 419 ILE A C 1 ATOM 3143 O O . ILE A 1 394 ? -37.420 -12.172 -11.969 1.00 20.30 ? 419 ILE A O 1 ATOM 3144 C CB . ILE A 1 394 ? -35.150 -10.088 -12.218 1.00 19.07 ? 419 ILE A CB 1 ATOM 3145 C CG1 . ILE A 1 394 ? -34.632 -8.699 -11.835 1.00 23.56 ? 419 ILE A CG1 1 ATOM 3146 C CG2 . ILE A 1 394 ? -34.255 -10.685 -13.306 1.00 21.48 ? 419 ILE A CG2 1 ATOM 3147 C CD1 . ILE A 1 394 ? -34.918 -8.300 -10.396 1.00 28.60 ? 419 ILE A CD1 1 ATOM 3148 N N . VAL A 1 395 ? -37.069 -11.901 -14.168 1.00 18.41 ? 420 VAL A N 1 ATOM 3149 C CA . VAL A 1 395 ? -37.195 -13.321 -14.459 1.00 18.64 ? 420 VAL A CA 1 ATOM 3150 C C . VAL A 1 395 ? -36.014 -13.717 -15.345 1.00 20.62 ? 420 VAL A C 1 ATOM 3151 O O . VAL A 1 395 ? -35.663 -12.998 -16.277 1.00 20.27 ? 420 VAL A O 1 ATOM 3152 C CB . VAL A 1 395 ? -38.562 -13.671 -15.096 1.00 21.08 ? 420 VAL A CB 1 ATOM 3153 C CG1 . VAL A 1 395 ? -38.684 -13.079 -16.497 1.00 20.82 ? 420 VAL A CG1 1 ATOM 3154 C CG2 . VAL A 1 395 ? -38.774 -15.186 -15.112 1.00 22.41 ? 420 VAL A CG2 1 ATOM 3155 N N . ALA A 1 396 ? -35.380 -14.839 -15.026 1.00 20.15 ? 421 ALA A N 1 ATOM 3156 C CA . ALA A 1 396 ? -34.136 -15.227 -15.684 1.00 22.10 ? 421 ALA A CA 1 ATOM 3157 C C . ALA A 1 396 ? -34.112 -16.730 -15.902 1.00 21.71 ? 421 ALA A C 1 ATOM 3158 O O . ALA A 1 396 ? -34.702 -17.488 -15.128 1.00 25.50 ? 421 ALA A O 1 ATOM 3159 C CB . ALA A 1 396 ? -32.937 -14.797 -14.844 1.00 19.52 ? 421 ALA A CB 1 ATOM 3160 N N . TRP A 1 397 ? -33.437 -17.169 -16.960 1.00 21.72 ? 422 TRP A N 1 ATOM 3161 C CA . TRP A 1 397 ? -33.453 -18.587 -17.301 1.00 23.26 ? 422 TRP A CA 1 ATOM 3162 C C . TRP A 1 397 ? -32.208 -18.975 -18.083 1.00 26.29 ? 422 TRP A C 1 ATOM 3163 O O . TRP A 1 397 ? -31.596 -18.140 -18.744 1.00 25.10 ? 422 TRP A O 1 ATOM 3164 C CB . TRP A 1 397 ? -34.719 -18.932 -18.102 1.00 22.80 ? 422 TRP A CB 1 ATOM 3165 C CG . TRP A 1 397 ? -34.803 -18.255 -19.447 1.00 24.91 ? 422 TRP A CG 1 ATOM 3166 C CD1 . TRP A 1 397 ? -34.379 -18.759 -20.643 1.00 26.43 ? 422 TRP A CD1 1 ATOM 3167 C CD2 . TRP A 1 397 ? -35.345 -16.955 -19.730 1.00 24.21 ? 422 TRP A CD2 1 ATOM 3168 N NE1 . TRP A 1 397 ? -34.621 -17.855 -21.651 1.00 26.30 ? 422 TRP A NE1 1 ATOM 3169 C CE2 . TRP A 1 397 ? -35.214 -16.741 -21.119 1.00 24.38 ? 422 TRP A CE2 1 ATOM 3170 C CE3 . TRP A 1 397 ? -35.930 -15.955 -18.946 1.00 24.18 ? 422 TRP A CE3 1 ATOM 3171 C CZ2 . TRP A 1 397 ? -35.640 -15.568 -21.739 1.00 25.11 ? 422 TRP A CZ2 1 ATOM 3172 C CZ3 . TRP A 1 397 ? -36.348 -14.785 -19.563 1.00 24.04 ? 422 TRP A CZ3 1 ATOM 3173 C CH2 . TRP A 1 397 ? -36.203 -14.604 -20.947 1.00 24.80 ? 422 TRP A CH2 1 ATOM 3174 N N . ASN A 1 398 ? -31.827 -20.244 -17.997 1.00 26.94 ? 423 ASN A N 1 ATOM 3175 C CA . ASN A 1 398 ? -30.689 -20.726 -18.767 1.00 30.14 ? 423 ASN A CA 1 ATOM 3176 C C . ASN A 1 398 ? -31.132 -21.329 -20.093 1.00 29.14 ? 423 ASN A C 1 ATOM 3177 O O . ASN A 1 398 ? -32.329 -21.452 -20.366 1.00 28.40 ? 423 ASN A O 1 ATOM 3178 C CB . ASN A 1 398 ? -29.840 -21.712 -17.956 1.00 32.40 ? 423 ASN A CB 1 ATOM 3179 C CG . ASN A 1 398 ? -30.605 -22.954 -17.556 1.00 36.89 ? 423 ASN A CG 1 ATOM 3180 O OD1 . ASN A 1 398 ? -31.349 -23.524 -18.354 1.00 40.38 ? 423 ASN A OD1 1 ATOM 3181 N ND2 . ASN A 1 398 ? -30.418 -23.388 -16.313 1.00 39.49 ? 423 ASN A ND2 1 ATOM 3182 N N . GLN A 1 399 ? -30.162 -21.695 -20.922 1.00 31.61 ? 424 GLN A N 1 ATOM 3183 C CA . GLN A 1 399 ? -30.454 -22.154 -22.274 1.00 36.48 ? 424 GLN A CA 1 ATOM 3184 C C . GLN A 1 399 ? -31.360 -23.381 -22.291 1.00 33.97 ? 424 GLN A C 1 ATOM 3185 O O . GLN A 1 399 ? -32.157 -23.557 -23.212 1.00 34.68 ? 424 GLN A O 1 ATOM 3186 C CB . GLN A 1 399 ? -29.156 -22.433 -23.035 1.00 52.14 ? 424 GLN A CB 1 ATOM 3187 C CG . GLN A 1 399 ? -29.354 -22.704 -24.517 1.00 72.37 ? 424 GLN A CG 1 ATOM 3188 C CD . GLN A 1 399 ? -28.047 -22.718 -25.286 1.00 88.65 ? 424 GLN A CD 1 ATOM 3189 O OE1 . GLN A 1 399 ? -27.815 -23.592 -26.123 1.00 94.74 ? 424 GLN A OE1 1 ATOM 3190 N NE2 . GLN A 1 399 ? -27.182 -21.749 -25.003 1.00 90.63 ? 424 GLN A NE2 1 ATOM 3191 N N . SER A 1 400 ? -31.246 -24.226 -21.272 1.00 33.70 ? 425 SER A N 1 ATOM 3192 C CA . SER A 1 400 ? -32.036 -25.452 -21.226 1.00 32.58 ? 425 SER A CA 1 ATOM 3193 C C . SER A 1 400 ? -33.507 -25.170 -20.933 1.00 33.27 ? 425 SER A C 1 ATOM 3194 O O . SER A 1 400 ? -34.354 -26.054 -21.069 1.00 36.44 ? 425 SER A O 1 ATOM 3195 C CB . SER A 1 400 ? -31.468 -26.432 -20.194 1.00 36.51 ? 425 SER A CB 1 ATOM 3196 O OG . SER A 1 400 ? -31.678 -25.970 -18.870 1.00 37.21 ? 425 SER A OG 1 ATOM 3197 N N . GLU A 1 401 ? -33.805 -23.934 -20.541 1.00 30.81 ? 426 GLU A N 1 ATOM 3198 C CA . GLU A 1 401 ? -35.161 -23.546 -20.163 1.00 32.72 ? 426 GLU A CA 1 ATOM 3199 C C . GLU A 1 401 ? -35.824 -22.661 -21.217 1.00 33.43 ? 426 GLU A C 1 ATOM 3200 O O . GLU A 1 401 ? -36.900 -22.111 -20.983 1.00 30.41 ? 426 GLU A O 1 ATOM 3201 C CB . GLU A 1 401 ? -35.140 -22.806 -18.821 1.00 28.97 ? 426 GLU A CB 1 ATOM 3202 C CG . GLU A 1 401 ? -34.494 -23.589 -17.688 1.00 30.03 ? 426 GLU A CG 1 ATOM 3203 C CD . GLU A 1 401 ? -34.373 -22.776 -16.408 1.00 34.99 ? 426 GLU A CD 1 ATOM 3204 O OE1 . GLU A 1 401 ? -35.089 -23.093 -15.437 1.00 37.33 ? 426 GLU A OE1 1 ATOM 3205 O OE2 . GLU A 1 401 ? -33.567 -21.819 -16.373 1.00 31.06 ? 426 GLU A OE2 1 ATOM 3206 N N . GLN A 1 402 ? -35.179 -22.530 -22.374 1.00 33.44 ? 427 GLN A N 1 ATOM 3207 C CA . GLN A 1 402 ? -35.642 -21.629 -23.429 1.00 36.52 ? 427 GLN A CA 1 ATOM 3208 C C . GLN A 1 402 ? -37.095 -21.849 -23.853 1.00 34.68 ? 427 GLN A C 1 ATOM 3209 O O . GLN A 1 402 ? -37.780 -20.903 -24.241 1.00 33.49 ? 427 GLN A O 1 ATOM 3210 C CB . GLN A 1 402 ? -34.725 -21.719 -24.653 1.00 47.14 ? 427 GLN A CB 1 ATOM 3211 C CG . GLN A 1 402 ? -33.392 -21.010 -24.481 1.00 65.05 ? 427 GLN A CG 1 ATOM 3212 C CD . GLN A 1 402 ? -32.483 -21.177 -25.684 1.00 78.69 ? 427 GLN A CD 1 ATOM 3213 O OE1 . GLN A 1 402 ? -31.388 -20.616 -25.732 1.00 82.68 ? 427 GLN A OE1 1 ATOM 3214 N NE2 . GLN A 1 402 ? -32.935 -21.954 -26.663 1.00 80.67 ? 427 GLN A NE2 1 ATOM 3215 N N . LYS A 1 403 ? -37.558 -23.094 -23.784 1.00 34.05 ? 428 LYS A N 1 ATOM 3216 C CA . LYS A 1 403 ? -38.921 -23.427 -24.189 1.00 38.41 ? 428 LYS A CA 1 ATOM 3217 C C . LYS A 1 403 ? -39.950 -22.605 -23.421 1.00 35.69 ? 428 LYS A C 1 ATOM 3218 O O . LYS A 1 403 ? -41.042 -22.340 -23.921 1.00 32.58 ? 428 LYS A O 1 ATOM 3219 C CB . LYS A 1 403 ? -39.194 -24.924 -23.998 1.00 40.80 ? 428 LYS A CB 1 ATOM 3220 C CG . LYS A 1 403 ? -40.537 -25.390 -24.552 1.00 57.84 ? 428 LYS A CG 1 ATOM 3221 C CD . LYS A 1 403 ? -40.598 -26.906 -24.676 1.00 67.58 ? 428 LYS A CD 1 ATOM 3222 C CE . LYS A 1 403 ? -40.996 -27.571 -23.368 1.00 72.53 ? 428 LYS A CE 1 ATOM 3223 N NZ . LYS A 1 403 ? -42.465 -27.497 -23.127 1.00 72.03 ? 428 LYS A NZ 1 ATOM 3224 N N . LYS A 1 404 ? -39.588 -22.192 -22.210 1.00 31.08 ? 429 LYS A N 1 ATOM 3225 C CA . LYS A 1 404 ? -40.523 -21.506 -21.323 1.00 29.03 ? 429 LYS A CA 1 ATOM 3226 C C . LYS A 1 404 ? -40.463 -19.982 -21.414 1.00 26.82 ? 429 LYS A C 1 ATOM 3227 O O . LYS A 1 404 ? -41.102 -19.288 -20.624 1.00 24.59 ? 429 LYS A O 1 ATOM 3228 C CB . LYS A 1 404 ? -40.298 -21.945 -19.874 1.00 30.43 ? 429 LYS A CB 1 ATOM 3229 C CG . LYS A 1 404 ? -40.710 -23.381 -19.600 1.00 35.68 ? 429 LYS A CG 1 ATOM 3230 C CD . LYS A 1 404 ? -40.248 -23.844 -18.231 1.00 38.62 ? 429 LYS A CD 1 ATOM 3231 C CE . LYS A 1 404 ? -40.855 -23.006 -17.118 1.00 32.72 ? 429 LYS A CE 1 ATOM 3232 N NZ . LYS A 1 404 ? -40.481 -23.556 -15.784 1.00 31.79 ? 429 LYS A NZ 1 ATOM 3233 N N . LYS A 1 405 ? -39.706 -19.467 -22.378 1.00 25.52 ? 430 LYS A N 1 ATOM 3234 C CA . LYS A 1 405 ? -39.528 -18.026 -22.523 1.00 26.82 ? 430 LYS A CA 1 ATOM 3235 C C . LYS A 1 405 ? -40.839 -17.238 -22.480 1.00 24.15 ? 430 LYS A C 1 ATOM 3236 O O . LYS A 1 405 ? -40.986 -16.304 -21.695 1.00 24.22 ? 430 LYS A O 1 ATOM 3237 C CB . LYS A 1 405 ? -38.760 -17.712 -23.811 1.00 28.30 ? 430 LYS A CB 1 ATOM 3238 C CG . LYS A 1 405 ? -38.576 -16.230 -24.074 1.00 32.40 ? 430 LYS A CG 1 ATOM 3239 C CD . LYS A 1 405 ? -37.804 -16.003 -25.367 1.00 38.83 ? 430 LYS A CD 1 ATOM 3240 C CE . LYS A 1 405 ? -37.799 -14.539 -25.763 1.00 44.63 ? 430 LYS A CE 1 ATOM 3241 N NZ . LYS A 1 405 ? -37.107 -14.331 -27.068 1.00 51.71 ? 430 LYS A NZ 1 ATOM 3242 N N . THR A 1 406 ? -41.790 -17.603 -23.330 1.00 26.46 ? 431 THR A N 1 ATOM 3243 C CA . THR A 1 406 ? -43.050 -16.874 -23.390 1.00 22.87 ? 431 THR A CA 1 ATOM 3244 C C . THR A 1 406 ? -43.738 -16.876 -22.029 1.00 23.34 ? 431 THR A C 1 ATOM 3245 O O . THR A 1 406 ? -44.241 -15.846 -21.579 1.00 22.81 ? 431 THR A O 1 ATOM 3246 C CB . THR A 1 406 ? -43.983 -17.451 -24.462 1.00 26.07 ? 431 THR A CB 1 ATOM 3247 O OG1 . THR A 1 406 ? -43.340 -17.359 -25.740 1.00 32.29 ? 431 THR A OG1 1 ATOM 3248 C CG2 . THR A 1 406 ? -45.292 -16.678 -24.506 1.00 31.42 ? 431 THR A CG2 1 ATOM 3249 N N . GLU A 1 407 ? -43.742 -18.034 -21.375 1.00 22.25 ? 432 GLU A N 1 ATOM 3250 C CA . GLU A 1 407 ? -44.323 -18.172 -20.038 1.00 22.11 ? 432 GLU A CA 1 ATOM 3251 C C . GLU A 1 407 ? -43.629 -17.267 -19.019 1.00 22.14 ? 432 GLU A C 1 ATOM 3252 O O . GLU A 1 407 ? -44.288 -16.624 -18.194 1.00 22.50 ? 432 GLU A O 1 ATOM 3253 C CB . GLU A 1 407 ? -44.271 -19.635 -19.575 1.00 25.39 ? 432 GLU A CB 1 ATOM 3254 C CG . GLU A 1 407 ? -44.736 -19.848 -18.141 1.00 29.09 ? 432 GLU A CG 1 ATOM 3255 C CD . GLU A 1 407 ? -44.675 -21.307 -17.710 1.00 35.55 ? 432 GLU A CD 1 ATOM 3256 O OE1 . GLU A 1 407 ? -44.607 -22.191 -18.593 1.00 36.52 ? 432 GLU A OE1 1 ATOM 3257 O OE2 . GLU A 1 407 ? -44.698 -21.570 -16.486 1.00 30.86 ? 432 GLU A OE2 1 ATOM 3258 N N . PHE A 1 408 ? -42.301 -17.225 -19.069 1.00 21.64 ? 433 PHE A N 1 ATOM 3259 C CA . PHE A 1 408 ? -41.535 -16.383 -18.155 1.00 20.66 ? 433 PHE A CA 1 ATOM 3260 C C . PHE A 1 408 ? -41.905 -14.916 -18.332 1.00 19.07 ? 433 PHE A C 1 ATOM 3261 O O . PHE A 1 408 ? -42.130 -14.193 -17.354 1.00 20.12 ? 433 PHE A O 1 ATOM 3262 C CB . PHE A 1 408 ? -40.035 -16.555 -18.382 1.00 22.95 ? 433 PHE A CB 1 ATOM 3263 C CG . PHE A 1 408 ? -39.493 -17.875 -17.922 1.00 22.31 ? 433 PHE A CG 1 ATOM 3264 C CD1 . PHE A 1 408 ? -39.940 -18.456 -16.744 1.00 23.74 ? 433 PHE A CD1 1 ATOM 3265 C CD2 . PHE A 1 408 ? -38.507 -18.520 -18.651 1.00 23.97 ? 433 PHE A CD2 1 ATOM 3266 C CE1 . PHE A 1 408 ? -39.425 -19.669 -16.315 1.00 25.35 ? 433 PHE A CE1 1 ATOM 3267 C CE2 . PHE A 1 408 ? -37.987 -19.734 -18.231 1.00 24.94 ? 433 PHE A CE2 1 ATOM 3268 C CZ . PHE A 1 408 ? -38.450 -20.311 -17.060 1.00 29.81 ? 433 PHE A CZ 1 ATOM 3269 N N . LEU A 1 409 ? -41.959 -14.474 -19.584 1.00 21.53 ? 434 LEU A N 1 ATOM 3270 C CA . LEU A 1 409 ? -42.292 -13.084 -19.877 1.00 22.66 ? 434 LEU A CA 1 ATOM 3271 C C . LEU A 1 409 ? -43.728 -12.763 -19.474 1.00 22.08 ? 434 LEU A C 1 ATOM 3272 O O . LEU A 1 409 ? -44.012 -11.658 -19.003 1.00 24.01 ? 434 LEU A O 1 ATOM 3273 C CB . LEU A 1 409 ? -42.053 -12.764 -21.358 1.00 25.91 ? 434 LEU A CB 1 ATOM 3274 C CG . LEU A 1 409 ? -40.609 -12.941 -21.836 1.00 35.29 ? 434 LEU A CG 1 ATOM 3275 C CD1 . LEU A 1 409 ? -40.435 -12.328 -23.219 1.00 35.71 ? 434 LEU A CD1 1 ATOM 3276 C CD2 . LEU A 1 409 ? -39.618 -12.342 -20.851 1.00 34.99 ? 434 LEU A CD2 1 ATOM 3277 N N . ASP A 1 410 ? -44.632 -13.724 -19.655 1.00 22.66 ? 435 ASP A N 1 ATOM 3278 C CA . ASP A 1 410 ? -46.015 -13.536 -19.235 1.00 20.84 ? 435 ASP A CA 1 ATOM 3279 C C . ASP A 1 410 ? -46.085 -13.345 -17.718 1.00 22.11 ? 435 ASP A C 1 ATOM 3280 O O . ASP A 1 410 ? -46.821 -12.490 -17.225 1.00 21.55 ? 435 ASP A O 1 ATOM 3281 C CB . ASP A 1 410 ? -46.883 -14.720 -19.672 1.00 23.79 ? 435 ASP A CB 1 ATOM 3282 C CG . ASP A 1 410 ? -48.343 -14.553 -19.282 1.00 23.59 ? 435 ASP A CG 1 ATOM 3283 O OD1 . ASP A 1 410 ? -48.989 -13.587 -19.746 1.00 26.51 ? 435 ASP A OD1 1 ATOM 3284 O OD2 . ASP A 1 410 ? -48.849 -15.394 -18.514 1.00 30.56 ? 435 ASP A OD2 1 ATOM 3285 N N . TRP A 1 411 ? -45.308 -14.137 -16.986 1.00 20.23 ? 436 TRP A N 1 ATOM 3286 C CA . TRP A 1 411 ? -45.288 -14.036 -15.530 1.00 18.50 ? 436 TRP A CA 1 ATOM 3287 C C . TRP A 1 411 ? -44.873 -12.627 -15.112 1.00 21.97 ? 436 TRP A C 1 ATOM 3288 O O . TRP A 1 411 ? -45.508 -12.009 -14.255 1.00 20.26 ? 436 TRP A O 1 ATOM 3289 C CB . TRP A 1 411 ? -44.355 -15.084 -14.919 1.00 19.94 ? 436 TRP A CB 1 ATOM 3290 C CG . TRP A 1 411 ? -44.206 -14.947 -13.423 1.00 20.07 ? 436 TRP A CG 1 ATOM 3291 C CD1 . TRP A 1 411 ? -45.006 -15.504 -12.465 1.00 24.06 ? 436 TRP A CD1 1 ATOM 3292 C CD2 . TRP A 1 411 ? -43.213 -14.185 -12.724 1.00 20.37 ? 436 TRP A CD2 1 ATOM 3293 N NE1 . TRP A 1 411 ? -44.568 -15.138 -11.211 1.00 20.45 ? 436 TRP A NE1 1 ATOM 3294 C CE2 . TRP A 1 411 ? -43.467 -14.331 -11.344 1.00 20.95 ? 436 TRP A CE2 1 ATOM 3295 C CE3 . TRP A 1 411 ? -42.132 -13.394 -13.131 1.00 20.84 ? 436 TRP A CE3 1 ATOM 3296 C CZ2 . TRP A 1 411 ? -42.674 -13.726 -10.370 1.00 21.51 ? 436 TRP A CZ2 1 ATOM 3297 C CZ3 . TRP A 1 411 ? -41.348 -12.788 -12.162 1.00 20.21 ? 436 TRP A CZ3 1 ATOM 3298 C CH2 . TRP A 1 411 ? -41.625 -12.956 -10.797 1.00 20.43 ? 436 TRP A CH2 1 ATOM 3299 N N . LEU A 1 412 ? -43.815 -12.119 -15.733 1.00 19.93 ? 437 LEU A N 1 ATOM 3300 C CA . LEU A 1 412 ? -43.292 -10.799 -15.397 1.00 21.64 ? 437 LEU A CA 1 ATOM 3301 C C . LEU A 1 412 ? -44.313 -9.707 -15.710 1.00 21.20 ? 437 LEU A C 1 ATOM 3302 O O . LEU A 1 412 ? -44.521 -8.776 -14.925 1.00 18.43 ? 437 LEU A O 1 ATOM 3303 C CB . LEU A 1 412 ? -41.992 -10.539 -16.158 1.00 20.76 ? 437 LEU A CB 1 ATOM 3304 C CG . LEU A 1 412 ? -41.352 -9.175 -15.904 1.00 21.48 ? 437 LEU A CG 1 ATOM 3305 C CD1 . LEU A 1 412 ? -41.013 -9.036 -14.430 1.00 25.69 ? 437 LEU A CD1 1 ATOM 3306 C CD2 . LEU A 1 412 ? -40.105 -9.013 -16.757 1.00 22.88 ? 437 LEU A CD2 1 ATOM 3307 N N . GLU A 1 413 ? -44.956 -9.829 -16.865 1.00 20.44 ? 438 GLU A N 1 ATOM 3308 C CA . GLU A 1 413 ? -45.987 -8.885 -17.267 1.00 20.17 ? 438 GLU A CA 1 ATOM 3309 C C . GLU A 1 413 ? -47.092 -8.823 -16.217 1.00 20.02 ? 438 GLU A C 1 ATOM 3310 O O . GLU A 1 413 ? -47.572 -7.744 -15.858 1.00 19.31 ? 438 GLU A O 1 ATOM 3311 C CB . GLU A 1 413 ? -46.559 -9.291 -18.632 1.00 21.56 ? 438 GLU A CB 1 ATOM 3312 C CG . GLU A 1 413 ? -47.647 -8.368 -19.155 1.00 25.74 ? 438 GLU A CG 1 ATOM 3313 C CD . GLU A 1 413 ? -48.186 -8.804 -20.511 1.00 34.40 ? 438 GLU A CD 1 ATOM 3314 O OE1 . GLU A 1 413 ? -47.477 -9.540 -21.230 1.00 41.03 ? 438 GLU A OE1 1 ATOM 3315 O OE2 . GLU A 1 413 ? -49.317 -8.409 -20.855 1.00 46.39 ? 438 GLU A OE2 1 ATOM 3316 N N . LYS A 1 414 ? -47.490 -9.990 -15.721 1.00 19.70 ? 439 LYS A N 1 ATOM 3317 C CA . LYS A 1 414 ? -48.583 -10.068 -14.759 1.00 20.02 ? 439 LYS A CA 1 ATOM 3318 C C . LYS A 1 414 ? -48.186 -9.526 -13.385 1.00 18.34 ? 439 LYS A C 1 ATOM 3319 O O . LYS A 1 414 ? -49.008 -8.928 -12.694 1.00 21.18 ? 439 LYS A O 1 ATOM 3320 C CB . LYS A 1 414 ? -49.128 -11.498 -14.671 1.00 21.31 ? 439 LYS A CB 1 ATOM 3321 C CG . LYS A 1 414 ? -49.880 -11.928 -15.933 1.00 24.53 ? 439 LYS A CG 1 ATOM 3322 C CD . LYS A 1 414 ? -50.661 -13.211 -15.715 1.00 35.42 ? 439 LYS A CD 1 ATOM 3323 C CE . LYS A 1 414 ? -49.740 -14.390 -15.464 1.00 44.22 ? 439 LYS A CE 1 ATOM 3324 N NZ . LYS A 1 414 ? -50.510 -15.663 -15.294 1.00 40.37 ? 439 LYS A NZ 1 ATOM 3325 N N . VAL A 1 415 ? -46.930 -9.722 -12.992 1.00 18.64 ? 440 VAL A N 1 ATOM 3326 C CA . VAL A 1 415 ? -46.430 -9.118 -11.757 1.00 17.61 ? 440 VAL A CA 1 ATOM 3327 C C . VAL A 1 415 ? -46.494 -7.592 -11.826 1.00 19.75 ? 440 VAL A C 1 ATOM 3328 O O . VAL A 1 415 ? -46.940 -6.928 -10.886 1.00 18.70 ? 440 VAL A O 1 ATOM 3329 C CB . VAL A 1 415 ? -44.983 -9.549 -11.467 1.00 19.30 ? 440 VAL A CB 1 ATOM 3330 C CG1 . VAL A 1 415 ? -44.369 -8.669 -10.376 1.00 20.74 ? 440 VAL A CG1 1 ATOM 3331 C CG2 . VAL A 1 415 ? -44.939 -11.020 -11.077 1.00 22.96 ? 440 VAL A CG2 1 ATOM 3332 N N . TYR A 1 416 ? -46.036 -7.035 -12.941 1.00 19.05 ? 441 TYR A N 1 ATOM 3333 C CA . TYR A 1 416 ? -46.035 -5.589 -13.119 1.00 17.62 ? 441 TYR A CA 1 ATOM 3334 C C . TYR A 1 416 ? -47.472 -5.037 -13.091 1.00 18.10 ? 441 TYR A C 1 ATOM 3335 O O . TYR A 1 416 ? -47.736 -3.978 -12.505 1.00 19.02 ? 441 TYR A O 1 ATOM 3336 C CB . TYR A 1 416 ? -45.303 -5.234 -14.416 1.00 20.11 ? 441 TYR A CB 1 ATOM 3337 C CG . TYR A 1 416 ? -44.917 -3.780 -14.587 1.00 19.20 ? 441 TYR A CG 1 ATOM 3338 C CD1 . TYR A 1 416 ? -43.901 -3.202 -13.829 1.00 22.10 ? 441 TYR A CD1 1 ATOM 3339 C CD2 . TYR A 1 416 ? -45.556 -2.996 -15.538 1.00 22.03 ? 441 TYR A CD2 1 ATOM 3340 C CE1 . TYR A 1 416 ? -43.550 -1.859 -14.020 1.00 18.33 ? 441 TYR A CE1 1 ATOM 3341 C CE2 . TYR A 1 416 ? -45.222 -1.675 -15.728 1.00 23.82 ? 441 TYR A CE2 1 ATOM 3342 C CZ . TYR A 1 416 ? -44.229 -1.109 -14.972 1.00 20.26 ? 441 TYR A CZ 1 ATOM 3343 O OH . TYR A 1 416 ? -43.915 0.221 -15.188 1.00 27.47 ? 441 TYR A OH 1 ATOM 3344 N N . GLU A 1 417 ? -48.410 -5.764 -13.697 1.00 18.28 ? 442 GLU A N 1 ATOM 3345 C CA . GLU A 1 417 ? -49.806 -5.341 -13.659 1.00 20.38 ? 442 GLU A CA 1 ATOM 3346 C C . GLU A 1 417 ? -50.366 -5.429 -12.236 1.00 19.42 ? 442 GLU A C 1 ATOM 3347 O O . GLU A 1 417 ? -51.114 -4.552 -11.800 1.00 21.08 ? 442 GLU A O 1 ATOM 3348 C CB . GLU A 1 417 ? -50.653 -6.150 -14.649 1.00 21.77 ? 442 GLU A CB 1 ATOM 3349 C CG . GLU A 1 417 ? -52.154 -5.861 -14.590 1.00 23.15 ? 442 GLU A CG 1 ATOM 3350 C CD . GLU A 1 417 ? -52.522 -4.450 -15.025 1.00 35.53 ? 442 GLU A CD 1 ATOM 3351 O OE1 . GLU A 1 417 ? -51.738 -3.812 -15.761 1.00 34.78 ? 442 GLU A OE1 1 ATOM 3352 O OE2 . GLU A 1 417 ? -53.611 -3.981 -14.632 1.00 38.72 ? 442 GLU A OE2 1 ATOM 3353 N N . PHE A 1 418 ? -49.994 -6.476 -11.504 1.00 19.47 ? 443 PHE A N 1 ATOM 3354 C CA . PHE A 1 418 ? -50.455 -6.611 -10.125 1.00 19.97 ? 443 PHE A CA 1 ATOM 3355 C C . PHE A 1 418 ? -49.997 -5.442 -9.239 1.00 18.00 ? 443 PHE A C 1 ATOM 3356 O O . PHE A 1 418 ? -50.738 -4.974 -8.373 1.00 19.03 ? 443 PHE A O 1 ATOM 3357 C CB . PHE A 1 418 ? -49.987 -7.933 -9.514 1.00 19.13 ? 443 PHE A CB 1 ATOM 3358 C CG . PHE A 1 418 ? -50.153 -7.990 -8.021 1.00 16.79 ? 443 PHE A CG 1 ATOM 3359 C CD1 . PHE A 1 418 ? -51.406 -8.180 -7.462 1.00 21.43 ? 443 PHE A CD1 1 ATOM 3360 C CD2 . PHE A 1 418 ? -49.064 -7.820 -7.182 1.00 18.14 ? 443 PHE A CD2 1 ATOM 3361 C CE1 . PHE A 1 418 ? -51.573 -8.214 -6.087 1.00 22.06 ? 443 PHE A CE1 1 ATOM 3362 C CE2 . PHE A 1 418 ? -49.221 -7.859 -5.802 1.00 21.24 ? 443 PHE A CE2 1 ATOM 3363 C CZ . PHE A 1 418 ? -50.478 -8.056 -5.256 1.00 21.48 ? 443 PHE A CZ 1 ATOM 3364 N N . MET A 1 419 ? -48.771 -4.973 -9.446 1.00 16.74 ? 444 MET A N 1 ATOM 3365 C CA . MET A 1 419 ? -48.218 -3.931 -8.589 1.00 17.62 ? 444 MET A CA 1 ATOM 3366 C C . MET A 1 419 ? -48.732 -2.528 -8.911 1.00 18.38 ? 444 MET A C 1 ATOM 3367 O O . MET A 1 419 ? -48.554 -1.597 -8.122 1.00 17.41 ? 444 MET A O 1 ATOM 3368 C CB . MET A 1 419 ? -46.691 -3.959 -8.656 1.00 17.70 ? 444 MET A CB 1 ATOM 3369 C CG . MET A 1 419 ? -46.082 -5.202 -8.041 1.00 17.79 ? 444 MET A CG 1 ATOM 3370 S SD . MET A 1 419 ? -46.380 -5.315 -6.263 1.00 19.59 ? 444 MET A SD 1 ATOM 3371 C CE . MET A 1 419 ? -45.433 -3.921 -5.656 1.00 20.86 ? 444 MET A CE 1 ATOM 3372 N N . LYS A 1 420 ? -49.369 -2.380 -10.068 1.00 18.62 ? 445 LYS A N 1 ATOM 3373 C CA . LYS A 1 420 ? -49.799 -1.067 -10.556 1.00 19.09 ? 445 LYS A CA 1 ATOM 3374 C C . LYS A 1 420 ? -50.453 -0.135 -9.522 1.00 20.41 ? 445 LYS A C 1 ATOM 3375 O O . LYS A 1 420 ? -50.052 1.013 -9.405 1.00 21.98 ? 445 LYS A O 1 ATOM 3376 C CB . LYS A 1 420 ? -50.695 -1.213 -11.792 1.00 19.35 ? 445 LYS A CB 1 ATOM 3377 C CG . LYS A 1 420 ? -51.002 0.108 -12.485 1.00 24.40 ? 445 LYS A CG 1 ATOM 3378 C CD . LYS A 1 420 ? -51.722 -0.120 -13.809 1.00 31.39 ? 445 LYS A CD 1 ATOM 3379 C CE . LYS A 1 420 ? -53.011 -0.888 -13.600 1.00 39.74 ? 445 LYS A CE 1 ATOM 3380 N NZ . LYS A 1 420 ? -53.813 -0.966 -14.852 1.00 53.61 ? 445 LYS A NZ 1 ATOM 3381 N N . PRO A 1 421 ? -51.455 -0.619 -8.768 1.00 19.39 ? 446 PRO A N 1 ATOM 3382 C CA . PRO A 1 421 ? -52.156 0.285 -7.843 1.00 20.12 ? 446 PRO A CA 1 ATOM 3383 C C . PRO A 1 421 ? -51.314 0.737 -6.653 1.00 22.51 ? 446 PRO A C 1 ATOM 3384 O O . PRO A 1 421 ? -51.673 1.711 -5.986 1.00 21.75 ? 446 PRO A O 1 ATOM 3385 C CB . PRO A 1 421 ? -53.325 -0.569 -7.322 1.00 24.11 ? 446 PRO A CB 1 ATOM 3386 C CG . PRO A 1 421 ? -53.392 -1.765 -8.206 1.00 30.61 ? 446 PRO A CG 1 ATOM 3387 C CD . PRO A 1 421 ? -52.024 -1.977 -8.755 1.00 21.44 ? 446 PRO A CD 1 ATOM 3388 N N . PHE A 1 422 ? -50.218 0.040 -6.377 1.00 20.23 ? 447 PHE A N 1 ATOM 3389 C CA . PHE A 1 422 ? -49.460 0.307 -5.159 1.00 21.69 ? 447 PHE A CA 1 ATOM 3390 C C . PHE A 1 422 ? -48.268 1.220 -5.373 1.00 22.59 ? 447 PHE A C 1 ATOM 3391 O O . PHE A 1 422 ? -47.712 1.756 -4.418 1.00 22.51 ? 447 PHE A O 1 ATOM 3392 C CB . PHE A 1 422 ? -48.968 -1.000 -4.546 1.00 20.62 ? 447 PHE A CB 1 ATOM 3393 C CG . PHE A 1 422 ? -50.037 -2.033 -4.397 1.00 20.41 ? 447 PHE A CG 1 ATOM 3394 C CD1 . PHE A 1 422 ? -51.129 -1.800 -3.578 1.00 20.08 ? 447 PHE A CD1 1 ATOM 3395 C CD2 . PHE A 1 422 ? -49.951 -3.240 -5.070 1.00 20.61 ? 447 PHE A CD2 1 ATOM 3396 C CE1 . PHE A 1 422 ? -52.120 -2.753 -3.437 1.00 27.04 ? 447 PHE A CE1 1 ATOM 3397 C CE2 . PHE A 1 422 ? -50.936 -4.201 -4.925 1.00 22.43 ? 447 PHE A CE2 1 ATOM 3398 C CZ . PHE A 1 422 ? -52.025 -3.953 -4.109 1.00 23.75 ? 447 PHE A CZ 1 ATOM 3399 N N . VAL A 1 423 ? -47.865 1.394 -6.625 1.00 19.33 ? 448 VAL A N 1 ATOM 3400 C CA . VAL A 1 423 ? -46.625 2.102 -6.909 1.00 19.14 ? 448 VAL A CA 1 ATOM 3401 C C . VAL A 1 423 ? -46.923 3.479 -7.477 1.00 19.89 ? 448 VAL A C 1 ATOM 3402 O O . VAL A 1 423 ? -48.074 3.897 -7.509 1.00 22.46 ? 448 VAL A O 1 ATOM 3403 C CB . VAL A 1 423 ? -45.725 1.292 -7.860 1.00 18.51 ? 448 VAL A CB 1 ATOM 3404 C CG1 . VAL A 1 423 ? -45.411 -0.069 -7.248 1.00 18.03 ? 448 VAL A CG1 1 ATOM 3405 C CG2 . VAL A 1 423 ? -46.393 1.115 -9.217 1.00 21.14 ? 448 VAL A CG2 1 ATOM 3406 N N . SER A 1 424 ? -45.887 4.197 -7.900 1.00 20.63 ? 449 SER A N 1 ATOM 3407 C CA . SER A 1 424 ? -46.084 5.536 -8.437 1.00 18.68 ? 449 SER A CA 1 ATOM 3408 C C . SER A 1 424 ? -47.025 5.507 -9.629 1.00 20.79 ? 449 SER A C 1 ATOM 3409 O O . SER A 1 424 ? -47.047 4.545 -10.397 1.00 21.06 ? 449 SER A O 1 ATOM 3410 C CB . SER A 1 424 ? -44.752 6.167 -8.847 1.00 20.06 ? 449 SER A CB 1 ATOM 3411 O OG . SER A 1 424 ? -44.159 5.465 -9.927 1.00 20.09 ? 449 SER A OG 1 ATOM 3412 N N . LYS A 1 425 ? -47.806 6.568 -9.779 1.00 23.07 ? 450 LYS A N 1 ATOM 3413 C CA . LYS A 1 425 ? -48.747 6.652 -10.889 1.00 23.43 ? 450 LYS A CA 1 ATOM 3414 C C . LYS A 1 425 ? -48.870 8.091 -11.371 1.00 27.49 ? 450 LYS A C 1 ATOM 3415 O O . LYS A 1 425 ? -48.576 9.027 -10.629 1.00 27.19 ? 450 LYS A O 1 ATOM 3416 C CB . LYS A 1 425 ? -50.113 6.087 -10.481 1.00 37.01 ? 450 LYS A CB 1 ATOM 3417 C CG . LYS A 1 425 ? -50.590 6.525 -9.107 1.00 42.37 ? 450 LYS A CG 1 ATOM 3418 C CD . LYS A 1 425 ? -51.817 5.729 -8.656 1.00 36.97 ? 450 LYS A CD 1 ATOM 3419 C CE . LYS A 1 425 ? -51.436 4.365 -8.086 1.00 35.01 ? 450 LYS A CE 1 ATOM 3420 N NZ . LYS A 1 425 ? -50.798 4.457 -6.731 1.00 30.66 ? 450 LYS A NZ 1 ATOM 3421 N N . ASN A 1 426 ? -49.287 8.255 -12.623 1.00 27.27 ? 451 ASN A N 1 ATOM 3422 C CA . ASN A 1 426 ? -49.501 9.578 -13.206 1.00 28.81 ? 451 ASN A CA 1 ATOM 3423 C C . ASN A 1 426 ? -48.269 10.485 -13.177 1.00 32.07 ? 451 ASN A C 1 ATOM 3424 O O . ASN A 1 426 ? -48.313 11.576 -12.607 1.00 36.24 ? 451 ASN A O 1 ATOM 3425 C CB . ASN A 1 426 ? -50.680 10.270 -12.516 1.00 34.26 ? 451 ASN A CB 1 ATOM 3426 C CG . ASN A 1 426 ? -51.954 9.459 -12.601 1.00 41.60 ? 451 ASN A CG 1 ATOM 3427 O OD1 . ASN A 1 426 ? -52.432 9.148 -13.693 1.00 42.38 ? 451 ASN A OD1 1 ATOM 3428 N ND2 . ASN A 1 426 ? -52.512 9.106 -11.447 1.00 41.53 ? 451 ASN A ND2 1 ATOM 3429 N N . PRO A 1 427 ? -47.167 10.040 -13.800 1.00 26.19 ? 452 PRO A N 1 ATOM 3430 C CA . PRO A 1 427 ? -47.054 8.759 -14.504 1.00 23.95 ? 452 PRO A CA 1 ATOM 3431 C C . PRO A 1 427 ? -46.397 7.684 -13.643 1.00 23.78 ? 452 PRO A C 1 ATOM 3432 O O . PRO A 1 427 ? -45.846 7.980 -12.579 1.00 22.79 ? 452 PRO A O 1 ATOM 3433 C CB . PRO A 1 427 ? -46.113 9.097 -15.656 1.00 25.90 ? 452 PRO A CB 1 ATOM 3434 C CG . PRO A 1 427 ? -45.208 10.158 -15.084 1.00 27.85 ? 452 PRO A CG 1 ATOM 3435 C CD . PRO A 1 427 ? -45.956 10.863 -13.973 1.00 27.22 ? 452 PRO A CD 1 ATOM 3436 N N . ARG A 1 428 ? -46.445 6.444 -14.113 1.00 21.28 ? 453 ARG A N 1 ATOM 3437 C CA . ARG A 1 428 ? -45.709 5.369 -13.461 1.00 17.64 ? 453 ARG A CA 1 ATOM 3438 C C . ARG A 1 428 ? -44.223 5.582 -13.736 1.00 20.09 ? 453 ARG A C 1 ATOM 3439 O O . ARG A 1 428 ? -43.778 5.562 -14.888 1.00 20.68 ? 453 ARG A O 1 ATOM 3440 C CB . ARG A 1 428 ? -46.186 4.010 -13.971 1.00 20.40 ? 453 ARG A CB 1 ATOM 3441 C CG . ARG A 1 428 ? -45.644 2.822 -13.180 1.00 17.43 ? 453 ARG A CG 1 ATOM 3442 C CD . ARG A 1 428 ? -46.406 1.555 -13.536 1.00 18.64 ? 453 ARG A CD 1 ATOM 3443 N NE . ARG A 1 428 ? -46.013 0.420 -12.706 1.00 17.78 ? 453 ARG A NE 1 ATOM 3444 C CZ . ARG A 1 428 ? -46.625 -0.759 -12.724 1.00 19.85 ? 453 ARG A CZ 1 ATOM 3445 N NH1 . ARG A 1 428 ? -47.659 -0.960 -13.535 1.00 21.75 ? 453 ARG A NH1 1 ATOM 3446 N NH2 . ARG A 1 428 ? -46.208 -1.735 -11.926 1.00 17.03 ? 453 ARG A NH2 1 ATOM 3447 N N . LEU A 1 429 ? -43.464 5.804 -12.669 1.00 18.66 ? 454 LEU A N 1 ATOM 3448 C CA . LEU A 1 429 ? -42.077 6.243 -12.789 1.00 19.43 ? 454 LEU A CA 1 ATOM 3449 C C . LEU A 1 429 ? -41.137 5.113 -13.169 1.00 19.17 ? 454 LEU A C 1 ATOM 3450 O O . LEU A 1 429 ? -41.409 3.945 -12.907 1.00 19.54 ? 454 LEU A O 1 ATOM 3451 C CB . LEU A 1 429 ? -41.612 6.884 -11.479 1.00 17.87 ? 454 LEU A CB 1 ATOM 3452 C CG . LEU A 1 429 ? -42.507 8.027 -10.995 1.00 19.36 ? 454 LEU A CG 1 ATOM 3453 C CD1 . LEU A 1 429 ? -42.048 8.511 -9.626 1.00 24.50 ? 454 LEU A CD1 1 ATOM 3454 C CD2 . LEU A 1 429 ? -42.530 9.174 -11.999 1.00 24.26 ? 454 LEU A CD2 1 ATOM 3455 N N . GLY A 1 430 ? -40.027 5.480 -13.794 1.00 17.52 ? 455 GLY A N 1 ATOM 3456 C CA . GLY A 1 430 ? -38.998 4.525 -14.152 1.00 17.36 ? 455 GLY A CA 1 ATOM 3457 C C . GLY A 1 430 ? -37.607 5.108 -13.975 1.00 16.37 ? 455 GLY A C 1 ATOM 3458 O O . GLY A 1 430 ? -37.437 6.185 -13.405 1.00 16.85 ? 455 GLY A O 1 ATOM 3459 N N . TYR A 1 431 ? -36.616 4.397 -14.491 1.00 15.61 ? 456 TYR A N 1 ATOM 3460 C CA . TYR A 1 431 ? -35.211 4.726 -14.269 1.00 16.99 ? 456 TYR A CA 1 ATOM 3461 C C . TYR A 1 431 ? -34.480 4.402 -15.561 1.00 17.57 ? 456 TYR A C 1 ATOM 3462 O O . TYR A 1 431 ? -34.579 3.282 -16.056 1.00 16.94 ? 456 TYR A O 1 ATOM 3463 C CB . TYR A 1 431 ? -34.702 3.874 -13.097 1.00 17.08 ? 456 TYR A CB 1 ATOM 3464 C CG . TYR A 1 431 ? -33.215 3.906 -12.812 1.00 16.69 ? 456 TYR A CG 1 ATOM 3465 C CD1 . TYR A 1 431 ? -32.444 5.034 -13.084 1.00 16.50 ? 456 TYR A CD1 1 ATOM 3466 C CD2 . TYR A 1 431 ? -32.592 2.815 -12.223 1.00 19.14 ? 456 TYR A CD2 1 ATOM 3467 C CE1 . TYR A 1 431 ? -31.084 5.055 -12.805 1.00 18.82 ? 456 TYR A CE1 1 ATOM 3468 C CE2 . TYR A 1 431 ? -31.238 2.831 -11.935 1.00 20.87 ? 456 TYR A CE2 1 ATOM 3469 C CZ . TYR A 1 431 ? -30.488 3.952 -12.230 1.00 18.03 ? 456 TYR A CZ 1 ATOM 3470 O OH . TYR A 1 431 ? -29.139 3.941 -11.939 1.00 17.18 ? 456 TYR A OH 1 ATOM 3471 N N . VAL A 1 432 ? -33.769 5.376 -16.127 1.00 14.43 ? 457 VAL A N 1 ATOM 3472 C CA . VAL A 1 432 ? -33.217 5.175 -17.471 1.00 15.57 ? 457 VAL A CA 1 ATOM 3473 C C . VAL A 1 432 ? -32.185 4.040 -17.550 1.00 18.52 ? 457 VAL A C 1 ATOM 3474 O O . VAL A 1 432 ? -32.050 3.412 -18.591 1.00 19.71 ? 457 VAL A O 1 ATOM 3475 C CB . VAL A 1 432 ? -32.685 6.484 -18.093 1.00 14.51 ? 457 VAL A CB 1 ATOM 3476 C CG1 . VAL A 1 432 ? -31.337 6.862 -17.503 1.00 15.38 ? 457 VAL A CG1 1 ATOM 3477 C CG2 . VAL A 1 432 ? -32.587 6.352 -19.624 1.00 16.75 ? 457 VAL A CG2 1 ATOM 3478 N N . ASN A 1 433 ? -31.463 3.761 -16.467 1.00 16.21 ? 458 ASN A N 1 ATOM 3479 C CA . ASN A 1 433 ? -30.570 2.598 -16.472 1.00 17.93 ? 458 ASN A CA 1 ATOM 3480 C C . ASN A 1 433 ? -31.343 1.281 -16.500 1.00 18.42 ? 458 ASN A C 1 ATOM 3481 O O . ASN A 1 433 ? -30.770 0.223 -16.783 1.00 20.21 ? 458 ASN A O 1 ATOM 3482 C CB . ASN A 1 433 ? -29.594 2.617 -15.288 1.00 15.89 ? 458 ASN A CB 1 ATOM 3483 C CG . ASN A 1 433 ? -28.275 3.301 -15.627 1.00 16.90 ? 458 ASN A CG 1 ATOM 3484 O OD1 . ASN A 1 433 ? -27.845 3.311 -16.784 1.00 17.50 ? 458 ASN A OD1 1 ATOM 3485 N ND2 . ASN A 1 433 ? -27.621 3.866 -14.619 1.00 17.13 ? 458 ASN A ND2 1 ATOM 3486 N N . HIS A 1 434 ? -32.634 1.358 -16.184 1.00 18.16 ? 459 HIS A N 1 ATOM 3487 C CA A HIS A 1 434 ? -33.508 0.190 -16.261 0.44 19.01 ? 459 HIS A CA 1 ATOM 3488 C CA B HIS A 1 434 ? -33.540 0.219 -16.224 0.56 19.04 ? 459 HIS A CA 1 ATOM 3489 C C . HIS A 1 434 ? -34.422 0.370 -17.456 1.00 20.99 ? 459 HIS A C 1 ATOM 3490 O O . HIS A 1 434 ? -35.638 0.192 -17.376 1.00 22.26 ? 459 HIS A O 1 ATOM 3491 C CB A HIS A 1 434 ? -34.315 0.002 -14.976 0.44 21.58 ? 459 HIS A CB 1 ATOM 3492 C CB B HIS A 1 434 ? -34.413 0.215 -14.967 0.56 21.54 ? 459 HIS A CB 1 ATOM 3493 C CG A HIS A 1 434 ? -33.475 -0.297 -13.772 0.44 21.11 ? 459 HIS A CG 1 ATOM 3494 C CG B HIS A 1 434 ? -34.474 -1.109 -14.273 0.56 22.15 ? 459 HIS A CG 1 ATOM 3495 N ND1 A HIS A 1 434 ? -32.131 -0.590 -13.854 0.44 28.97 ? 459 HIS A ND1 1 ATOM 3496 N ND1 B HIS A 1 434 ? -35.236 -2.160 -14.738 0.56 29.74 ? 459 HIS A ND1 1 ATOM 3497 C CD2 A HIS A 1 434 ? -33.796 -0.372 -12.459 0.44 27.73 ? 459 HIS A CD2 1 ATOM 3498 C CD2 B HIS A 1 434 ? -33.872 -1.552 -13.143 0.56 15.80 ? 459 HIS A CD2 1 ATOM 3499 C CE1 A HIS A 1 434 ? -31.656 -0.816 -12.642 0.44 26.56 ? 459 HIS A CE1 1 ATOM 3500 C CE1 B HIS A 1 434 ? -35.096 -3.194 -13.929 0.56 27.42 ? 459 HIS A CE1 1 ATOM 3501 N NE2 A HIS A 1 434 ? -32.647 -0.693 -11.778 0.44 28.31 ? 459 HIS A NE2 1 ATOM 3502 N NE2 B HIS A 1 434 ? -34.270 -2.854 -12.957 0.56 23.44 ? 459 HIS A NE2 1 ATOM 3503 N N . ILE A 1 435 ? -33.802 0.718 -18.579 1.00 23.07 ? 460 ILE A N 1 ATOM 3504 C CA A ILE A 1 435 ? -34.514 1.007 -19.817 0.38 21.54 ? 460 ILE A CA 1 ATOM 3505 C CA B ILE A 1 435 ? -34.529 1.010 -19.805 0.62 19.99 ? 460 ILE A CA 1 ATOM 3506 C C . ILE A 1 435 ? -35.534 -0.084 -20.138 1.00 23.99 ? 460 ILE A C 1 ATOM 3507 O O . ILE A 1 435 ? -35.216 -1.274 -20.089 1.00 25.28 ? 460 ILE A O 1 ATOM 3508 C CB A ILE A 1 435 ? -33.519 1.190 -20.989 0.38 24.49 ? 460 ILE A CB 1 ATOM 3509 C CB B ILE A 1 435 ? -33.571 1.217 -20.988 0.62 23.73 ? 460 ILE A CB 1 ATOM 3510 C CG1 A ILE A 1 435 ? -34.203 1.837 -22.197 0.38 26.57 ? 460 ILE A CG1 1 ATOM 3511 C CG1 B ILE A 1 435 ? -34.362 1.575 -22.246 0.62 27.04 ? 460 ILE A CG1 1 ATOM 3512 C CG2 A ILE A 1 435 ? -32.854 -0.138 -21.353 0.38 27.75 ? 460 ILE A CG2 1 ATOM 3513 C CG2 B ILE A 1 435 ? -32.707 -0.026 -21.209 0.62 26.78 ? 460 ILE A CG2 1 ATOM 3514 C CD1 A ILE A 1 435 ? -34.976 0.870 -23.062 0.38 26.95 ? 460 ILE A CD1 1 ATOM 3515 C CD1 B ILE A 1 435 ? -33.549 2.287 -23.286 0.62 30.10 ? 460 ILE A CD1 1 ATOM 3516 N N . ASP A 1 436 ? -36.752 0.336 -20.471 1.00 20.65 ? 461 ASP A N 1 ATOM 3517 C CA . ASP A 1 436 ? -37.851 -0.586 -20.725 1.00 23.49 ? 461 ASP A CA 1 ATOM 3518 C C . ASP A 1 436 ? -38.574 -0.205 -22.008 1.00 20.48 ? 461 ASP A C 1 ATOM 3519 O O . ASP A 1 436 ? -39.271 0.810 -22.064 1.00 22.20 ? 461 ASP A O 1 ATOM 3520 C CB . ASP A 1 436 ? -38.821 -0.572 -19.540 1.00 28.58 ? 461 ASP A CB 1 ATOM 3521 C CG . ASP A 1 436 ? -39.858 -1.677 -19.616 1.00 39.57 ? 461 ASP A CG 1 ATOM 3522 O OD1 . ASP A 1 436 ? -40.106 -2.192 -20.725 1.00 29.44 ? 461 ASP A OD1 1 ATOM 3523 O OD2 . ASP A 1 436 ? -40.431 -2.028 -18.563 1.00 42.84 ? 461 ASP A OD2 1 ATOM 3524 N N . LEU A 1 437 ? -38.412 -1.028 -23.038 1.00 19.96 ? 462 LEU A N 1 ATOM 3525 C CA . LEU A 1 437 ? -38.989 -0.727 -24.343 1.00 21.94 ? 462 LEU A CA 1 ATOM 3526 C C . LEU A 1 437 ? -40.480 -1.014 -24.418 1.00 22.08 ? 462 LEU A C 1 ATOM 3527 O O . LEU A 1 437 ? -41.122 -0.704 -25.421 1.00 25.68 ? 462 LEU A O 1 ATOM 3528 C CB . LEU A 1 437 ? -38.260 -1.487 -25.449 1.00 21.38 ? 462 LEU A CB 1 ATOM 3529 C CG . LEU A 1 437 ? -36.838 -1.011 -25.737 1.00 26.36 ? 462 LEU A CG 1 ATOM 3530 C CD1 . LEU A 1 437 ? -36.257 -1.757 -26.933 1.00 30.03 ? 462 LEU A CD1 1 ATOM 3531 C CD2 . LEU A 1 437 ? -36.840 0.481 -25.980 1.00 25.81 ? 462 LEU A CD2 1 ATOM 3532 N N . ASP A 1 438 ? -41.038 -1.601 -23.365 1.00 23.77 ? 463 ASP A N 1 ATOM 3533 C CA . ASP A 1 438 ? -42.480 -1.813 -23.333 1.00 22.88 ? 463 ASP A CA 1 ATOM 3534 C C . ASP A 1 438 ? -43.187 -0.460 -23.310 1.00 33.97 ? 463 ASP A C 1 ATOM 3535 O O . ASP A 1 438 ? -44.353 -0.350 -23.683 1.00 41.43 ? 463 ASP A O 1 ATOM 3536 C CB . ASP A 1 438 ? -42.890 -2.646 -22.116 1.00 27.19 ? 463 ASP A CB 1 ATOM 3537 C CG . ASP A 1 438 ? -42.380 -4.074 -22.185 1.00 39.68 ? 463 ASP A CG 1 ATOM 3538 O OD1 . ASP A 1 438 ? -41.791 -4.458 -23.217 1.00 46.82 ? 463 ASP A OD1 1 ATOM 3539 O OD2 . ASP A 1 438 ? -42.572 -4.818 -21.203 1.00 39.32 ? 463 ASP A OD2 1 ATOM 3540 N N . LEU A 1 439 ? -42.469 0.567 -22.864 1.00 31.00 ? 464 LEU A N 1 ATOM 3541 C CA . LEU A 1 439 ? -43.000 1.928 -22.830 1.00 35.83 ? 464 LEU A CA 1 ATOM 3542 C C . LEU A 1 439 ? -43.184 2.498 -24.235 1.00 39.27 ? 464 LEU A C 1 ATOM 3543 O O . LEU A 1 439 ? -43.838 3.525 -24.412 1.00 48.65 ? 464 LEU A O 1 ATOM 3544 C CB . LEU A 1 439 ? -42.068 2.843 -22.030 1.00 36.82 ? 464 LEU A CB 1 ATOM 3545 C CG . LEU A 1 439 ? -41.941 2.590 -20.526 1.00 37.58 ? 464 LEU A CG 1 ATOM 3546 C CD1 . LEU A 1 439 ? -40.713 3.299 -19.961 1.00 31.36 ? 464 LEU A CD1 1 ATOM 3547 C CD2 . LEU A 1 439 ? -43.207 3.037 -19.811 1.00 44.72 ? 464 LEU A CD2 1 ATOM 3548 N N . GLY A 1 440 ? -42.599 1.831 -25.228 1.00 32.90 ? 465 GLY A N 1 ATOM 3549 C CA . GLY A 1 440 ? -42.658 2.284 -26.607 1.00 27.38 ? 465 GLY A CA 1 ATOM 3550 C C . GLY A 1 440 ? -41.276 2.633 -27.143 1.00 23.56 ? 465 GLY A C 1 ATOM 3551 O O . GLY A 1 440 ? -40.272 2.416 -26.466 1.00 25.70 ? 465 GLY A O 1 ATOM 3552 N N . GLY A 1 441 ? -41.221 3.170 -28.358 1.00 22.78 ? 466 GLY A N 1 ATOM 3553 C CA . GLY A 1 441 ? -39.958 3.549 -28.967 1.00 22.21 ? 466 GLY A CA 1 ATOM 3554 C C . GLY A 1 441 ? -40.136 4.311 -30.269 1.00 23.24 ? 466 GLY A C 1 ATOM 3555 O O . GLY A 1 441 ? -41.163 4.188 -30.940 1.00 28.33 ? 466 GLY A O 1 ATOM 3556 N N . ILE A 1 442 ? -39.130 5.101 -30.617 1.00 20.09 ? 467 ILE A N 1 ATOM 3557 C CA . ILE A 1 442 ? -39.124 5.880 -31.846 1.00 20.82 ? 467 ILE A CA 1 ATOM 3558 C C . ILE A 1 442 ? -38.373 5.168 -32.957 1.00 21.50 ? 467 ILE A C 1 ATOM 3559 O O . ILE A 1 442 ? -37.236 4.737 -32.767 1.00 23.53 ? 467 ILE A O 1 ATOM 3560 C CB . ILE A 1 442 ? -38.400 7.236 -31.633 1.00 24.82 ? 467 ILE A CB 1 ATOM 3561 C CG1 . ILE A 1 442 ? -39.141 8.097 -30.610 1.00 31.58 ? 467 ILE A CG1 1 ATOM 3562 C CG2 . ILE A 1 442 ? -38.215 7.971 -32.966 1.00 23.77 ? 467 ILE A CG2 1 ATOM 3563 C CD1 . ILE A 1 442 ? -40.493 8.554 -31.059 1.00 32.10 ? 467 ILE A CD1 1 ATOM 3564 N N . ASP A 1 443 ? -39.007 5.058 -34.122 1.00 24.16 ? 468 ASP A N 1 ATOM 3565 C CA . ASP A 1 443 ? -38.301 4.682 -35.341 1.00 25.30 ? 468 ASP A CA 1 ATOM 3566 C C . ASP A 1 443 ? -37.841 5.966 -36.023 1.00 24.16 ? 468 ASP A C 1 ATOM 3567 O O . ASP A 1 443 ? -38.645 6.691 -36.621 1.00 21.83 ? 468 ASP A O 1 ATOM 3568 C CB . ASP A 1 443 ? -39.212 3.887 -36.270 1.00 24.43 ? 468 ASP A CB 1 ATOM 3569 C CG . ASP A 1 443 ? -38.547 3.540 -37.597 1.00 23.15 ? 468 ASP A CG 1 ATOM 3570 O OD1 . ASP A 1 443 ? -37.388 3.937 -37.832 1.00 25.46 ? 468 ASP A OD1 1 ATOM 3571 O OD2 . ASP A 1 443 ? -39.198 2.861 -38.410 1.00 28.95 ? 468 ASP A OD2 1 ATOM 3572 N N . TRP A 1 444 ? -36.546 6.246 -35.920 1.00 23.33 ? 469 TRP A N 1 ATOM 3573 C CA . TRP A 1 444 ? -35.995 7.495 -36.428 1.00 18.92 ? 469 TRP A CA 1 ATOM 3574 C C . TRP A 1 444 ? -36.015 7.571 -37.952 1.00 20.67 ? 469 TRP A C 1 ATOM 3575 O O . TRP A 1 444 ? -35.727 8.614 -38.529 1.00 25.98 ? 469 TRP A O 1 ATOM 3576 C CB . TRP A 1 444 ? -34.586 7.735 -35.876 1.00 25.42 ? 469 TRP A CB 1 ATOM 3577 C CG . TRP A 1 444 ? -34.599 7.979 -34.395 1.00 19.42 ? 469 TRP A CG 1 ATOM 3578 C CD1 . TRP A 1 444 ? -34.210 7.112 -33.414 1.00 22.12 ? 469 TRP A CD1 1 ATOM 3579 C CD2 . TRP A 1 444 ? -35.054 9.161 -33.728 1.00 20.85 ? 469 TRP A CD2 1 ATOM 3580 N NE1 . TRP A 1 444 ? -34.380 7.692 -32.179 1.00 21.04 ? 469 TRP A NE1 1 ATOM 3581 C CE2 . TRP A 1 444 ? -34.901 8.948 -32.345 1.00 21.62 ? 469 TRP A CE2 1 ATOM 3582 C CE3 . TRP A 1 444 ? -35.574 10.381 -34.167 1.00 22.15 ? 469 TRP A CE3 1 ATOM 3583 C CZ2 . TRP A 1 444 ? -35.253 9.911 -31.399 1.00 20.65 ? 469 TRP A CZ2 1 ATOM 3584 C CZ3 . TRP A 1 444 ? -35.921 11.332 -33.229 1.00 23.26 ? 469 TRP A CZ3 1 ATOM 3585 C CH2 . TRP A 1 444 ? -35.754 11.095 -31.861 1.00 21.43 ? 469 TRP A CH2 1 ATOM 3586 N N . GLY A 1 445 ? -36.379 6.467 -38.596 1.00 24.07 ? 470 GLY A N 1 ATOM 3587 C CA . GLY A 1 445 ? -36.488 6.451 -40.045 1.00 26.96 ? 470 GLY A CA 1 ATOM 3588 C C . GLY A 1 445 ? -37.893 6.742 -40.534 1.00 26.52 ? 470 GLY A C 1 ATOM 3589 O O . GLY A 1 445 ? -38.148 6.772 -41.738 1.00 29.14 ? 470 GLY A O 1 ATOM 3590 N N . ASN A 1 446 ? -38.804 6.969 -39.594 1.00 24.98 ? 471 ASN A N 1 ATOM 3591 C CA . ASN A 1 446 ? -40.219 7.169 -39.889 1.00 23.34 ? 471 ASN A CA 1 ATOM 3592 C C . ASN A 1 446 ? -40.591 8.642 -39.744 1.00 25.33 ? 471 ASN A C 1 ATOM 3593 O O . ASN A 1 446 ? -40.655 9.167 -38.637 1.00 23.64 ? 471 ASN A O 1 ATOM 3594 C CB . ASN A 1 446 ? -41.054 6.290 -38.948 1.00 23.14 ? 471 ASN A CB 1 ATOM 3595 C CG . ASN A 1 446 ? -42.526 6.270 -39.303 1.00 26.03 ? 471 ASN A CG 1 ATOM 3596 O OD1 . ASN A 1 446 ? -43.128 7.310 -39.568 1.00 29.91 ? 471 ASN A OD1 1 ATOM 3597 N ND2 . ASN A 1 446 ? -43.118 5.073 -39.293 1.00 31.24 ? 471 ASN A ND2 1 ATOM 3598 N N . LYS A 1 447 ? -40.835 9.304 -40.870 1.00 25.53 ? 472 LYS A N 1 ATOM 3599 C CA . LYS A 1 447 ? -41.002 10.753 -40.891 1.00 28.00 ? 472 LYS A CA 1 ATOM 3600 C C . LYS A 1 447 ? -42.161 11.249 -40.025 1.00 24.90 ? 472 LYS A C 1 ATOM 3601 O O . LYS A 1 447 ? -42.023 12.249 -39.314 1.00 27.47 ? 472 LYS A O 1 ATOM 3602 C CB . LYS A 1 447 ? -41.189 11.237 -42.334 1.00 38.16 ? 472 LYS A CB 1 ATOM 3603 C CG . LYS A 1 447 ? -40.456 12.530 -42.666 1.00 57.12 ? 472 LYS A CG 1 ATOM 3604 C CD . LYS A 1 447 ? -41.040 13.727 -41.936 1.00 66.02 ? 472 LYS A CD 1 ATOM 3605 C CE . LYS A 1 447 ? -40.339 15.015 -42.349 1.00 71.17 ? 472 LYS A CE 1 ATOM 3606 N NZ . LYS A 1 447 ? -40.389 15.233 -43.823 1.00 73.44 ? 472 LYS A NZ 1 ATOM 3607 N N . THR A 1 448 ? -43.304 10.571 -40.093 1.00 24.57 ? 473 THR A N 1 ATOM 3608 C CA . THR A 1 448 ? -44.480 11.021 -39.349 1.00 21.51 ? 473 THR A CA 1 ATOM 3609 C C . THR A 1 448 ? -44.221 10.914 -37.847 1.00 22.64 ? 473 THR A C 1 ATOM 3610 O O . THR A 1 448 ? -44.630 11.778 -37.074 1.00 23.11 ? 473 THR A O 1 ATOM 3611 C CB . THR A 1 448 ? -45.777 10.272 -39.754 1.00 25.45 ? 473 THR A CB 1 ATOM 3612 O OG1 . THR A 1 448 ? -46.902 10.848 -39.081 1.00 27.88 ? 473 THR A OG1 1 ATOM 3613 C CG2 . THR A 1 448 ? -45.703 8.793 -39.405 1.00 30.66 ? 473 THR A CG2 1 ATOM 3614 N N . VAL A 1 449 ? -43.527 9.859 -37.440 1.00 22.60 ? 474 VAL A N 1 ATOM 3615 C CA . VAL A 1 449 ? -43.171 9.686 -36.037 1.00 22.25 ? 474 VAL A CA 1 ATOM 3616 C C . VAL A 1 449 ? -42.170 10.753 -35.602 1.00 21.02 ? 474 VAL A C 1 ATOM 3617 O O . VAL A 1 449 ? -42.357 11.416 -34.577 1.00 23.04 ? 474 VAL A O 1 ATOM 3618 C CB . VAL A 1 449 ? -42.608 8.271 -35.778 1.00 21.93 ? 474 VAL A CB 1 ATOM 3619 C CG1 . VAL A 1 449 ? -41.903 8.205 -34.432 1.00 23.56 ? 474 VAL A CG1 1 ATOM 3620 C CG2 . VAL A 1 449 ? -43.737 7.250 -35.848 1.00 25.86 ? 474 VAL A CG2 1 ATOM 3621 N N . VAL A 1 450 ? -41.123 10.945 -36.394 1.00 21.13 ? 475 VAL A N 1 ATOM 3622 C CA . VAL A 1 450 ? -40.111 11.940 -36.054 1.00 22.45 ? 475 VAL A CA 1 ATOM 3623 C C . VAL A 1 450 ? -40.686 13.358 -35.943 1.00 20.62 ? 475 VAL A C 1 ATOM 3624 O O . VAL A 1 450 ? -40.272 14.128 -35.079 1.00 24.13 ? 475 VAL A O 1 ATOM 3625 C CB . VAL A 1 450 ? -38.924 11.898 -37.038 1.00 25.84 ? 475 VAL A CB 1 ATOM 3626 C CG1 . VAL A 1 450 ? -37.940 13.015 -36.729 1.00 28.13 ? 475 VAL A CG1 1 ATOM 3627 C CG2 . VAL A 1 450 ? -38.233 10.541 -36.955 1.00 24.96 ? 475 VAL A CG2 1 ATOM 3628 N N . ASN A 1 451 ? -41.643 13.699 -36.803 1.00 21.07 ? 476 ASN A N 1 ATOM 3629 C CA . ASN A 1 451 ? -42.303 15.000 -36.719 1.00 23.69 ? 476 ASN A CA 1 ATOM 3630 C C . ASN A 1 451 ? -42.879 15.258 -35.329 1.00 21.74 ? 476 ASN A C 1 ATOM 3631 O O . ASN A 1 451 ? -42.889 16.394 -34.850 1.00 27.36 ? 476 ASN A O 1 ATOM 3632 C CB . ASN A 1 451 ? -43.417 15.111 -37.762 1.00 26.25 ? 476 ASN A CB 1 ATOM 3633 C CG . ASN A 1 451 ? -42.904 15.531 -39.120 1.00 35.85 ? 476 ASN A CG 1 ATOM 3634 O OD1 . ASN A 1 451 ? -41.819 16.097 -39.238 1.00 36.67 ? 476 ASN A OD1 1 ATOM 3635 N ND2 . ASN A 1 451 ? -43.687 15.261 -40.159 1.00 40.40 ? 476 ASN A ND2 1 ATOM 3636 N N . ASN A 1 452 ? -43.361 14.196 -34.689 1.00 21.98 ? 477 ASN A N 1 ATOM 3637 C CA . ASN A 1 452 ? -44.027 14.313 -33.402 1.00 23.74 ? 477 ASN A CA 1 ATOM 3638 C C . ASN A 1 452 ? -43.204 13.689 -32.287 1.00 24.28 ? 477 ASN A C 1 ATOM 3639 O O . ASN A 1 452 ? -43.756 13.223 -31.287 1.00 21.12 ? 477 ASN A O 1 ATOM 3640 C CB . ASN A 1 452 ? -45.399 13.640 -33.467 1.00 22.04 ? 477 ASN A CB 1 ATOM 3641 C CG . ASN A 1 452 ? -46.297 14.032 -32.316 1.00 24.08 ? 477 ASN A CG 1 ATOM 3642 O OD1 . ASN A 1 452 ? -46.199 15.140 -31.784 1.00 22.72 ? 477 ASN A OD1 1 ATOM 3643 N ND2 . ASN A 1 452 ? -47.192 13.127 -31.929 1.00 26.33 ? 477 ASN A ND2 1 ATOM 3644 N N . ALA A 1 453 ? -41.886 13.677 -32.468 1.00 21.27 ? 478 ALA A N 1 ATOM 3645 C CA . ALA A 1 453 ? -40.995 12.934 -31.586 1.00 18.38 ? 478 ALA A CA 1 ATOM 3646 C C . ALA A 1 453 ? -41.036 13.410 -30.144 1.00 20.18 ? 478 ALA A C 1 ATOM 3647 O O . ALA A 1 453 ? -40.940 12.606 -29.224 1.00 20.74 ? 478 ALA A O 1 ATOM 3648 C CB . ALA A 1 453 ? -39.564 12.964 -32.117 1.00 22.80 ? 478 ALA A CB 1 ATOM 3649 N N . ILE A 1 454 ? -41.165 14.714 -29.941 1.00 21.43 ? 479 ILE A N 1 ATOM 3650 C CA . ILE A 1 454 ? -41.165 15.231 -28.578 1.00 21.27 ? 479 ILE A CA 1 ATOM 3651 C C . ILE A 1 454 ? -42.368 14.723 -27.776 1.00 22.97 ? 479 ILE A C 1 ATOM 3652 O O . ILE A 1 454 ? -42.195 14.208 -26.671 1.00 23.18 ? 479 ILE A O 1 ATOM 3653 C CB . ILE A 1 454 ? -41.027 16.765 -28.538 1.00 24.83 ? 479 ILE A CB 1 ATOM 3654 C CG1 . ILE A 1 454 ? -39.636 17.164 -29.040 1.00 26.67 ? 479 ILE A CG1 1 ATOM 3655 C CG2 . ILE A 1 454 ? -41.262 17.292 -27.124 1.00 28.24 ? 479 ILE A CG2 1 ATOM 3656 C CD1 . ILE A 1 454 ? -39.341 18.643 -28.921 1.00 34.43 ? 479 ILE A CD1 1 ATOM 3657 N N . GLU A 1 455 ? -43.577 14.829 -28.325 1.00 21.07 ? 480 GLU A N 1 ATOM 3658 C CA A GLU A 1 455 ? -44.766 14.338 -27.637 0.57 22.73 ? 480 GLU A CA 1 ATOM 3659 C CA B GLU A 1 455 ? -44.766 14.334 -27.627 0.43 22.74 ? 480 GLU A CA 1 ATOM 3660 C C . GLU A 1 455 ? -44.715 12.824 -27.434 1.00 24.41 ? 480 GLU A C 1 ATOM 3661 O O . GLU A 1 455 ? -45.000 12.320 -26.347 1.00 24.18 ? 480 GLU A O 1 ATOM 3662 C CB A GLU A 1 455 ? -46.028 14.719 -28.413 0.57 22.76 ? 480 GLU A CB 1 ATOM 3663 C CB B GLU A 1 455 ? -46.064 14.705 -28.357 0.43 24.56 ? 480 GLU A CB 1 ATOM 3664 C CG A GLU A 1 455 ? -47.309 14.150 -27.826 0.57 26.96 ? 480 GLU A CG 1 ATOM 3665 C CG B GLU A 1 455 ? -47.312 14.410 -27.516 0.43 29.53 ? 480 GLU A CG 1 ATOM 3666 C CD A GLU A 1 455 ? -47.659 14.748 -26.474 0.57 33.20 ? 480 GLU A CD 1 ATOM 3667 C CD B GLU A 1 455 ? -48.588 14.250 -28.333 0.43 30.35 ? 480 GLU A CD 1 ATOM 3668 O OE1 A GLU A 1 455 ? -46.996 15.724 -26.053 0.57 26.30 ? 480 GLU A OE1 1 ATOM 3669 O OE1 B GLU A 1 455 ? -49.632 14.797 -27.915 0.43 32.58 ? 480 GLU A OE1 1 ATOM 3670 O OE2 A GLU A 1 455 ? -48.607 14.244 -25.834 0.57 37.80 ? 480 GLU A OE2 1 ATOM 3671 O OE2 B GLU A 1 455 ? -48.557 13.570 -29.379 0.43 36.83 ? 480 GLU A OE2 1 ATOM 3672 N N . ILE A 1 456 ? -44.359 12.105 -28.490 1.00 21.26 ? 481 ILE A N 1 ATOM 3673 C CA . ILE A 1 456 ? -44.302 10.652 -28.433 1.00 21.11 ? 481 ILE A CA 1 ATOM 3674 C C . ILE A 1 456 ? -43.333 10.184 -27.352 1.00 23.04 ? 481 ILE A C 1 ATOM 3675 O O . ILE A 1 456 ? -43.648 9.285 -26.571 1.00 24.12 ? 481 ILE A O 1 ATOM 3676 C CB . ILE A 1 456 ? -43.877 10.056 -29.789 1.00 20.40 ? 481 ILE A CB 1 ATOM 3677 C CG1 . ILE A 1 456 ? -44.966 10.283 -30.836 1.00 22.36 ? 481 ILE A CG1 1 ATOM 3678 C CG2 . ILE A 1 456 ? -43.591 8.571 -29.656 1.00 25.58 ? 481 ILE A CG2 1 ATOM 3679 C CD1 . ILE A 1 456 ? -44.536 9.884 -32.242 1.00 24.61 ? 481 ILE A CD1 1 ATOM 3680 N N . SER A 1 457 ? -42.170 10.824 -27.295 1.00 19.55 ? 482 SER A N 1 ATOM 3681 C CA A SER A 1 457 ? -41.115 10.411 -26.374 0.26 19.70 ? 482 SER A CA 1 ATOM 3682 C CA B SER A 1 457 ? -41.105 10.430 -26.373 0.74 18.68 ? 482 SER A CA 1 ATOM 3683 C C . SER A 1 457 ? -41.419 10.776 -24.921 1.00 22.96 ? 482 SER A C 1 ATOM 3684 O O . SER A 1 457 ? -40.735 10.308 -24.008 1.00 23.37 ? 482 SER A O 1 ATOM 3685 C CB A SER A 1 457 ? -39.770 11.005 -26.795 0.26 19.56 ? 482 SER A CB 1 ATOM 3686 C CB B SER A 1 457 ? -39.787 11.078 -26.785 0.74 18.89 ? 482 SER A CB 1 ATOM 3687 O OG A SER A 1 457 ? -39.752 12.409 -26.611 0.26 15.95 ? 482 SER A OG 1 ATOM 3688 O OG B SER A 1 457 ? -39.386 10.623 -28.063 0.74 21.24 ? 482 SER A OG 1 ATOM 3689 N N . ARG A 1 458 ? -42.434 11.611 -24.711 1.00 21.94 ? 483 ARG A N 1 ATOM 3690 C CA . ARG A 1 458 ? -42.826 11.995 -23.356 1.00 24.73 ? 483 ARG A CA 1 ATOM 3691 C C . ARG A 1 458 ? -43.270 10.784 -22.547 1.00 25.16 ? 483 ARG A C 1 ATOM 3692 O O . ARG A 1 458 ? -43.101 10.752 -21.327 1.00 24.36 ? 483 ARG A O 1 ATOM 3693 C CB . ARG A 1 458 ? -43.948 13.036 -23.379 1.00 24.85 ? 483 ARG A CB 1 ATOM 3694 C CG . ARG A 1 458 ? -43.469 14.454 -23.534 1.00 30.62 ? 483 ARG A CG 1 ATOM 3695 C CD . ARG A 1 458 ? -44.617 15.448 -23.369 1.00 37.15 ? 483 ARG A CD 1 ATOM 3696 N NE . ARG A 1 458 ? -44.245 16.749 -23.905 1.00 37.02 ? 483 ARG A NE 1 ATOM 3697 C CZ . ARG A 1 458 ? -43.482 17.625 -23.264 1.00 41.04 ? 483 ARG A CZ 1 ATOM 3698 N NH1 . ARG A 1 458 ? -43.022 17.337 -22.054 1.00 35.69 ? 483 ARG A NH1 1 ATOM 3699 N NH2 . ARG A 1 458 ? -43.182 18.787 -23.831 1.00 46.23 ? 483 ARG A NH2 1 ATOM 3700 N N . SER A 1 459 ? -43.831 9.786 -23.223 1.00 24.87 ? 484 SER A N 1 ATOM 3701 C CA . SER A 1 459 ? -44.290 8.572 -22.549 1.00 23.49 ? 484 SER A CA 1 ATOM 3702 C C . SER A 1 459 ? -43.220 8.023 -21.612 1.00 24.76 ? 484 SER A C 1 ATOM 3703 O O . SER A 1 459 ? -43.451 7.855 -20.412 1.00 35.31 ? 484 SER A O 1 ATOM 3704 C CB . SER A 1 459 ? -44.674 7.494 -23.565 1.00 26.63 ? 484 SER A CB 1 ATOM 3705 O OG . SER A 1 459 ? -45.859 7.856 -24.255 1.00 46.81 ? 484 SER A OG 1 ATOM 3706 N N . TRP A 1 460 ? -42.048 7.742 -22.160 1.00 20.28 ? 485 TRP A N 1 ATOM 3707 C CA . TRP A 1 460 ? -40.958 7.234 -21.337 1.00 20.24 ? 485 TRP A CA 1 ATOM 3708 C C . TRP A 1 460 ? -40.113 8.358 -20.741 1.00 21.18 ? 485 TRP A C 1 ATOM 3709 O O . TRP A 1 460 ? -39.612 8.234 -19.623 1.00 19.84 ? 485 TRP A O 1 ATOM 3710 C CB . TRP A 1 460 ? -40.088 6.255 -22.129 1.00 21.38 ? 485 TRP A CB 1 ATOM 3711 C CG . TRP A 1 460 ? -39.744 6.718 -23.516 1.00 21.51 ? 485 TRP A CG 1 ATOM 3712 C CD1 . TRP A 1 460 ? -38.648 7.431 -23.888 1.00 22.23 ? 485 TRP A CD1 1 ATOM 3713 C CD2 . TRP A 1 460 ? -40.497 6.479 -24.715 1.00 21.44 ? 485 TRP A CD2 1 ATOM 3714 N NE1 . TRP A 1 460 ? -38.671 7.661 -25.247 1.00 21.78 ? 485 TRP A NE1 1 ATOM 3715 C CE2 . TRP A 1 460 ? -39.793 7.084 -25.776 1.00 21.66 ? 485 TRP A CE2 1 ATOM 3716 C CE3 . TRP A 1 460 ? -41.697 5.816 -24.993 1.00 27.41 ? 485 TRP A CE3 1 ATOM 3717 C CZ2 . TRP A 1 460 ? -40.251 7.049 -27.099 1.00 21.10 ? 485 TRP A CZ2 1 ATOM 3718 C CZ3 . TRP A 1 460 ? -42.153 5.783 -26.306 1.00 28.32 ? 485 TRP A CZ3 1 ATOM 3719 C CH2 . TRP A 1 460 ? -41.426 6.396 -27.341 1.00 25.14 ? 485 TRP A CH2 1 ATOM 3720 N N . GLY A 1 461 ? -39.951 9.449 -21.482 1.00 19.81 ? 486 GLY A N 1 ATOM 3721 C CA . GLY A 1 461 ? -39.122 10.555 -21.036 1.00 19.16 ? 486 GLY A CA 1 ATOM 3722 C C . GLY A 1 461 ? -39.536 11.118 -19.691 1.00 19.98 ? 486 GLY A C 1 ATOM 3723 O O . GLY A 1 461 ? -38.696 11.365 -18.822 1.00 20.58 ? 486 GLY A O 1 ATOM 3724 N N . GLU A 1 462 ? -40.832 11.330 -19.510 1.00 18.84 ? 487 GLU A N 1 ATOM 3725 C CA . GLU A 1 462 ? -41.322 11.863 -18.248 1.00 21.51 ? 487 GLU A CA 1 ATOM 3726 C C . GLU A 1 462 ? -41.265 10.833 -17.124 1.00 20.87 ? 487 GLU A C 1 ATOM 3727 O O . GLU A 1 462 ? -41.110 11.194 -15.960 1.00 21.67 ? 487 GLU A O 1 ATOM 3728 C CB . GLU A 1 462 ? -42.716 12.469 -18.416 1.00 24.00 ? 487 GLU A CB 1 ATOM 3729 C CG . GLU A 1 462 ? -42.679 13.738 -19.266 1.00 31.12 ? 487 GLU A CG 1 ATOM 3730 C CD . GLU A 1 462 ? -44.011 14.458 -19.349 1.00 44.04 ? 487 GLU A CD 1 ATOM 3731 O OE1 . GLU A 1 462 ? -45.041 13.873 -18.951 1.00 41.38 ? 487 GLU A OE1 1 ATOM 3732 O OE2 . GLU A 1 462 ? -44.021 15.615 -19.823 1.00 39.29 ? 487 GLU A OE2 1 ATOM 3733 N N . SER A 1 463 ? -41.363 9.550 -17.465 1.00 19.41 ? 488 SER A N 1 ATOM 3734 C CA A SER A 1 463 ? -41.246 8.493 -16.461 0.60 19.77 ? 488 SER A CA 1 ATOM 3735 C CA B SER A 1 463 ? -41.252 8.500 -16.454 0.40 20.03 ? 488 SER A CA 1 ATOM 3736 C C . SER A 1 463 ? -39.825 8.406 -15.918 1.00 18.76 ? 488 SER A C 1 ATOM 3737 O O . SER A 1 463 ? -39.613 8.172 -14.727 1.00 18.06 ? 488 SER A O 1 ATOM 3738 C CB A SER A 1 463 ? -41.676 7.145 -17.038 0.60 21.66 ? 488 SER A CB 1 ATOM 3739 C CB B SER A 1 463 ? -41.705 7.147 -17.007 0.40 22.32 ? 488 SER A CB 1 ATOM 3740 O OG A SER A 1 463 ? -43.085 7.093 -17.186 0.60 25.07 ? 488 SER A OG 1 ATOM 3741 O OG B SER A 1 463 ? -40.714 6.567 -17.833 0.40 23.55 ? 488 SER A OG 1 ATOM 3742 N N . TYR A 1 464 ? -38.849 8.602 -16.797 1.00 17.45 ? 489 TYR A N 1 ATOM 3743 C CA . TYR A 1 464 ? -37.442 8.562 -16.406 1.00 15.31 ? 489 TYR A CA 1 ATOM 3744 C C . TYR A 1 464 ? -36.960 9.866 -15.759 1.00 15.42 ? 489 TYR A C 1 ATOM 3745 O O . TYR A 1 464 ? -36.096 9.839 -14.867 1.00 16.26 ? 489 TYR A O 1 ATOM 3746 C CB . TYR A 1 464 ? -36.552 8.305 -17.628 1.00 17.38 ? 489 TYR A CB 1 ATOM 3747 C CG . TYR A 1 464 ? -36.765 6.996 -18.362 1.00 16.19 ? 489 TYR A CG 1 ATOM 3748 C CD1 . TYR A 1 464 ? -37.106 5.824 -17.687 1.00 20.30 ? 489 TYR A CD1 1 ATOM 3749 C CD2 . TYR A 1 464 ? -36.577 6.925 -19.735 1.00 16.13 ? 489 TYR A CD2 1 ATOM 3750 C CE1 . TYR A 1 464 ? -37.279 4.626 -18.373 1.00 19.76 ? 489 TYR A CE1 1 ATOM 3751 C CE2 . TYR A 1 464 ? -36.746 5.736 -20.426 1.00 16.18 ? 489 TYR A CE2 1 ATOM 3752 C CZ . TYR A 1 464 ? -37.089 4.591 -19.746 1.00 17.08 ? 489 TYR A CZ 1 ATOM 3753 O OH . TYR A 1 464 ? -37.258 3.408 -20.440 1.00 21.71 ? 489 TYR A OH 1 ATOM 3754 N N . PHE A 1 465 ? -37.480 11.002 -16.234 1.00 16.94 ? 490 PHE A N 1 ATOM 3755 C CA . PHE A 1 465 ? -36.871 12.300 -15.940 1.00 17.74 ? 490 PHE A CA 1 ATOM 3756 C C . PHE A 1 465 ? -37.813 13.371 -15.407 1.00 18.69 ? 490 PHE A C 1 ATOM 3757 O O . PHE A 1 465 ? -37.359 14.451 -15.018 1.00 19.03 ? 490 PHE A O 1 ATOM 3758 C CB . PHE A 1 465 ? -36.181 12.846 -17.197 1.00 16.44 ? 490 PHE A CB 1 ATOM 3759 C CG . PHE A 1 465 ? -35.183 11.903 -17.793 1.00 17.17 ? 490 PHE A CG 1 ATOM 3760 C CD1 . PHE A 1 465 ? -34.050 11.540 -17.085 1.00 17.26 ? 490 PHE A CD1 1 ATOM 3761 C CD2 . PHE A 1 465 ? -35.368 11.384 -19.066 1.00 16.39 ? 490 PHE A CD2 1 ATOM 3762 C CE1 . PHE A 1 465 ? -33.120 10.675 -17.632 1.00 18.73 ? 490 PHE A CE1 1 ATOM 3763 C CE2 . PHE A 1 465 ? -34.435 10.508 -19.618 1.00 17.99 ? 490 PHE A CE2 1 ATOM 3764 C CZ . PHE A 1 465 ? -33.314 10.160 -18.899 1.00 19.63 ? 490 PHE A CZ 1 ATOM 3765 N N . LEU A 1 466 ? -39.113 13.084 -15.401 1.00 18.45 ? 491 LEU A N 1 ATOM 3766 C CA . LEU A 1 466 ? -40.111 14.057 -14.959 1.00 20.37 ? 491 LEU A CA 1 ATOM 3767 C C . LEU A 1 466 ? -39.845 15.445 -15.544 1.00 22.27 ? 491 LEU A C 1 ATOM 3768 O O . LEU A 1 466 ? -39.691 15.581 -16.759 1.00 22.01 ? 491 LEU A O 1 ATOM 3769 C CB . LEU A 1 466 ? -40.201 14.086 -13.431 1.00 22.63 ? 491 LEU A CB 1 ATOM 3770 C CG . LEU A 1 466 ? -40.857 12.819 -12.874 1.00 22.89 ? 491 LEU A CG 1 ATOM 3771 C CD1 . LEU A 1 466 ? -40.722 12.732 -11.356 1.00 23.37 ? 491 LEU A CD1 1 ATOM 3772 C CD2 . LEU A 1 466 ? -42.324 12.752 -13.288 1.00 22.79 ? 491 LEU A CD2 1 ATOM 3773 N N . SER A 1 467 ? -39.779 16.465 -14.692 1.00 21.08 ? 492 SER A N 1 ATOM 3774 C CA . SER A 1 467 ? -39.661 17.845 -15.167 1.00 24.94 ? 492 SER A CA 1 ATOM 3775 C C . SER A 1 467 ? -38.316 18.165 -15.807 1.00 21.66 ? 492 SER A C 1 ATOM 3776 O O . SER A 1 467 ? -38.160 19.221 -16.427 1.00 27.94 ? 492 SER A O 1 ATOM 3777 C CB . SER A 1 467 ? -39.933 18.845 -14.037 1.00 25.89 ? 492 SER A CB 1 ATOM 3778 O OG . SER A 1 467 ? -41.300 18.835 -13.663 1.00 41.23 ? 492 SER A OG 1 ATOM 3779 N N . ASN A 1 468 ? -37.351 17.266 -15.655 1.00 21.13 ? 493 ASN A N 1 ATOM 3780 C CA . ASN A 1 468 ? -36.030 17.465 -16.244 1.00 20.98 ? 493 ASN A CA 1 ATOM 3781 C C . ASN A 1 468 ? -36.007 17.205 -17.748 1.00 22.81 ? 493 ASN A C 1 ATOM 3782 O O . ASN A 1 468 ? -35.022 17.505 -18.428 1.00 22.06 ? 493 ASN A O 1 ATOM 3783 C CB . ASN A 1 468 ? -35.001 16.577 -15.549 1.00 18.75 ? 493 ASN A CB 1 ATOM 3784 C CG . ASN A 1 468 ? -34.784 16.963 -14.107 1.00 18.61 ? 493 ASN A CG 1 ATOM 3785 O OD1 . ASN A 1 468 ? -34.978 18.118 -13.723 1.00 22.95 ? 493 ASN A OD1 1 ATOM 3786 N ND2 . ASN A 1 468 ? -34.369 16.000 -13.298 1.00 19.08 ? 493 ASN A ND2 1 ATOM 3787 N N . TYR A 1 469 ? -37.101 16.657 -18.265 1.00 21.15 ? 494 TYR A N 1 ATOM 3788 C CA A TYR A 1 469 ? -37.170 16.303 -19.675 0.37 18.59 ? 494 TYR A CA 1 ATOM 3789 C CA B TYR A 1 469 ? -37.213 16.301 -19.685 0.63 18.07 ? 494 TYR A CA 1 ATOM 3790 C C . TYR A 1 469 ? -36.939 17.503 -20.591 1.00 22.31 ? 494 TYR A C 1 ATOM 3791 O O . TYR A 1 469 ? -36.217 17.395 -21.586 1.00 22.61 ? 494 TYR A O 1 ATOM 3792 C CB A TYR A 1 469 ? -38.498 15.622 -19.999 0.37 19.17 ? 494 TYR A CB 1 ATOM 3793 C CB B TYR A 1 469 ? -38.608 15.708 -19.955 0.63 20.72 ? 494 TYR A CB 1 ATOM 3794 C CG A TYR A 1 469 ? -38.427 14.806 -21.260 0.37 19.85 ? 494 TYR A CG 1 ATOM 3795 C CG B TYR A 1 469 ? -38.893 15.260 -21.381 0.63 19.02 ? 494 TYR A CG 1 ATOM 3796 C CD1 A TYR A 1 469 ? -37.467 13.818 -21.404 0.37 21.02 ? 494 TYR A CD1 1 ATOM 3797 C CD1 B TYR A 1 469 ? -39.997 15.753 -22.074 0.63 21.72 ? 494 TYR A CD1 1 ATOM 3798 C CD2 A TYR A 1 469 ? -39.306 15.026 -22.308 0.37 17.37 ? 494 TYR A CD2 1 ATOM 3799 C CD2 B TYR A 1 469 ? -38.082 14.328 -22.020 0.63 21.50 ? 494 TYR A CD2 1 ATOM 3800 C CE1 A TYR A 1 469 ? -37.387 13.069 -22.549 0.37 19.57 ? 494 TYR A CE1 1 ATOM 3801 C CE1 B TYR A 1 469 ? -40.277 15.342 -23.369 0.63 19.35 ? 494 TYR A CE1 1 ATOM 3802 C CE2 A TYR A 1 469 ? -39.233 14.277 -23.466 0.37 19.84 ? 494 TYR A CE2 1 ATOM 3803 C CE2 B TYR A 1 469 ? -38.351 13.911 -23.315 0.63 20.89 ? 494 TYR A CE2 1 ATOM 3804 C CZ A TYR A 1 469 ? -38.269 13.299 -23.578 0.37 15.90 ? 494 TYR A CZ 1 ATOM 3805 C CZ B TYR A 1 469 ? -39.448 14.422 -23.982 0.63 21.33 ? 494 TYR A CZ 1 ATOM 3806 O OH A TYR A 1 469 ? -38.172 12.540 -24.717 0.37 23.02 ? 494 TYR A OH 1 ATOM 3807 O OH B TYR A 1 469 ? -39.713 14.007 -25.266 0.63 20.83 ? 494 TYR A OH 1 ATOM 3808 N N . GLU A 1 470 ? -37.522 18.648 -20.245 1.00 22.99 ? 495 GLU A N 1 ATOM 3809 C CA . GLU A 1 470 ? -37.369 19.855 -21.056 1.00 23.26 ? 495 GLU A CA 1 ATOM 3810 C C . GLU A 1 470 ? -35.916 20.311 -21.213 1.00 23.67 ? 495 GLU A C 1 ATOM 3811 O O . GLU A 1 470 ? -35.471 20.603 -22.325 1.00 23.80 ? 495 GLU A O 1 ATOM 3812 C CB . GLU A 1 470 ? -38.227 20.990 -20.495 1.00 25.42 ? 495 GLU A CB 1 ATOM 3813 C CG . GLU A 1 470 ? -39.687 20.934 -20.925 1.00 33.28 ? 495 GLU A CG 1 ATOM 3814 C CD . GLU A 1 470 ? -40.450 19.777 -20.305 1.00 40.17 ? 495 GLU A CD 1 ATOM 3815 O OE1 . GLU A 1 470 ? -39.979 19.214 -19.290 1.00 34.37 ? 495 GLU A OE1 1 ATOM 3816 O OE2 . GLU A 1 470 ? -41.531 19.434 -20.832 1.00 37.89 ? 495 GLU A OE2 1 ATOM 3817 N N . ARG A 1 471 ? -35.178 20.378 -20.110 1.00 21.84 ? 496 ARG A N 1 ATOM 3818 C CA . ARG A 1 471 ? -33.770 20.769 -20.179 1.00 24.37 ? 496 ARG A CA 1 ATOM 3819 C C . ARG A 1 471 ? -32.943 19.739 -20.962 1.00 23.87 ? 496 ARG A C 1 ATOM 3820 O O . ARG A 1 471 ? -32.021 20.098 -21.694 1.00 23.05 ? 496 ARG A O 1 ATOM 3821 C CB . ARG A 1 471 ? -33.194 20.988 -18.776 1.00 24.51 ? 496 ARG A CB 1 ATOM 3822 C CG . ARG A 1 471 ? -31.796 21.592 -18.761 1.00 26.18 ? 496 ARG A CG 1 ATOM 3823 C CD . ARG A 1 471 ? -31.316 21.813 -17.333 1.00 23.90 ? 496 ARG A CD 1 ATOM 3824 N NE . ARG A 1 471 ? -29.971 22.379 -17.280 1.00 27.92 ? 496 ARG A NE 1 ATOM 3825 C CZ . ARG A 1 471 ? -29.243 22.457 -16.169 1.00 28.94 ? 496 ARG A CZ 1 ATOM 3826 N NH1 . ARG A 1 471 ? -29.733 22.005 -15.021 1.00 25.49 ? 496 ARG A NH1 1 ATOM 3827 N NH2 . ARG A 1 471 ? -28.027 22.987 -16.204 1.00 31.65 ? 496 ARG A NH2 1 ATOM 3828 N N . LEU A 1 472 ? -33.279 18.460 -20.821 1.00 20.03 ? 497 LEU A N 1 ATOM 3829 C CA . LEU A 1 472 ? -32.585 17.422 -21.569 1.00 18.27 ? 497 LEU A CA 1 ATOM 3830 C C . LEU A 1 472 ? -32.721 17.659 -23.075 1.00 21.13 ? 497 LEU A C 1 ATOM 3831 O O . LEU A 1 472 ? -31.749 17.529 -23.822 1.00 20.05 ? 497 LEU A O 1 ATOM 3832 C CB . LEU A 1 472 ? -33.116 16.040 -21.188 1.00 18.31 ? 497 LEU A CB 1 ATOM 3833 C CG . LEU A 1 472 ? -32.674 15.516 -19.814 1.00 18.97 ? 497 LEU A CG 1 ATOM 3834 C CD1 . LEU A 1 472 ? -33.473 14.271 -19.449 1.00 20.27 ? 497 LEU A CD1 1 ATOM 3835 C CD2 . LEU A 1 472 ? -31.172 15.226 -19.763 1.00 18.74 ? 497 LEU A CD2 1 ATOM 3836 N N . ILE A 1 473 ? -33.927 18.013 -23.511 1.00 20.16 ? 498 ILE A N 1 ATOM 3837 C CA . ILE A 1 473 ? -34.165 18.290 -24.923 1.00 20.56 ? 498 ILE A CA 1 ATOM 3838 C C . ILE A 1 473 ? -33.309 19.469 -25.397 1.00 22.01 ? 498 ILE A C 1 ATOM 3839 O O . ILE A 1 473 ? -32.708 19.418 -26.469 1.00 22.47 ? 498 ILE A O 1 ATOM 3840 C CB . ILE A 1 473 ? -35.658 18.568 -25.200 1.00 21.04 ? 498 ILE A CB 1 ATOM 3841 C CG1 . ILE A 1 473 ? -36.471 17.281 -25.076 1.00 22.13 ? 498 ILE A CG1 1 ATOM 3842 C CG2 . ILE A 1 473 ? -35.836 19.165 -26.592 1.00 22.98 ? 498 ILE A CG2 1 ATOM 3843 C CD1 . ILE A 1 473 ? -37.969 17.512 -25.060 1.00 27.41 ? 498 ILE A CD1 1 ATOM 3844 N N . ARG A 1 474 ? -33.241 20.526 -24.596 1.00 21.98 ? 499 ARG A N 1 ATOM 3845 C CA A ARG A 1 474 ? -32.419 21.681 -24.943 0.62 21.94 ? 499 ARG A CA 1 ATOM 3846 C CA B ARG A 1 474 ? -32.422 21.678 -24.950 0.38 23.10 ? 499 ARG A CA 1 ATOM 3847 C C . ARG A 1 474 ? -30.945 21.291 -25.038 1.00 22.54 ? 499 ARG A C 1 ATOM 3848 O O . ARG A 1 474 ? -30.229 21.723 -25.945 1.00 26.36 ? 499 ARG A O 1 ATOM 3849 C CB A ARG A 1 474 ? -32.612 22.810 -23.927 0.62 28.47 ? 499 ARG A CB 1 ATOM 3850 C CB B ARG A 1 474 ? -32.637 22.824 -23.957 0.38 29.05 ? 499 ARG A CB 1 ATOM 3851 C CG A ARG A 1 474 ? -34.036 23.353 -23.880 0.62 33.82 ? 499 ARG A CG 1 ATOM 3852 C CG B ARG A 1 474 ? -34.021 23.459 -24.060 0.38 33.26 ? 499 ARG A CG 1 ATOM 3853 C CD A ARG A 1 474 ? -34.098 24.737 -23.244 0.62 33.52 ? 499 ARG A CD 1 ATOM 3854 C CD B ARG A 1 474 ? -34.122 24.765 -23.281 0.38 33.53 ? 499 ARG A CD 1 ATOM 3855 N NE A ARG A 1 474 ? -33.501 24.762 -21.912 0.62 34.73 ? 499 ARG A NE 1 ATOM 3856 N NE B ARG A 1 474 ? -34.218 24.552 -21.839 0.38 32.94 ? 499 ARG A NE 1 ATOM 3857 C CZ A ARG A 1 474 ? -34.169 24.511 -20.791 0.62 35.38 ? 499 ARG A CZ 1 ATOM 3858 C CZ B ARG A 1 474 ? -33.184 24.594 -21.005 0.38 35.45 ? 499 ARG A CZ 1 ATOM 3859 N NH1 A ARG A 1 474 ? -35.458 24.214 -20.842 0.62 26.90 ? 499 ARG A NH1 1 ATOM 3860 N NH1 B ARG A 1 474 ? -33.367 24.388 -19.707 0.38 34.79 ? 499 ARG A NH1 1 ATOM 3861 N NH2 A ARG A 1 474 ? -33.547 24.555 -19.620 0.62 36.60 ? 499 ARG A NH2 1 ATOM 3862 N NH2 B ARG A 1 474 ? -31.965 24.841 -21.465 0.38 27.71 ? 499 ARG A NH2 1 ATOM 3863 N N . ALA A 1 475 ? -30.493 20.463 -24.105 1.00 22.80 ? 500 ALA A N 1 ATOM 3864 C CA . ALA A 1 475 ? -29.111 20.012 -24.114 1.00 20.43 ? 500 ALA A CA 1 ATOM 3865 C C . ALA A 1 475 ? -28.821 19.153 -25.346 1.00 23.82 ? 500 ALA A C 1 ATOM 3866 O O . ALA A 1 475 ? -27.757 19.264 -25.953 1.00 23.36 ? 500 ALA A O 1 ATOM 3867 C CB . ALA A 1 475 ? -28.800 19.233 -22.837 1.00 21.72 ? 500 ALA A CB 1 ATOM 3868 N N . LYS A 1 476 ? -29.772 18.298 -25.706 1.00 20.75 ? 501 LYS A N 1 ATOM 3869 C CA . LYS A 1 476 ? -29.636 17.432 -26.875 1.00 17.78 ? 501 LYS A CA 1 ATOM 3870 C C . LYS A 1 476 ? -29.479 18.264 -28.140 1.00 22.82 ? 501 LYS A C 1 ATOM 3871 O O . LYS A 1 476 ? -28.650 17.967 -29.001 1.00 23.41 ? 501 LYS A O 1 ATOM 3872 C CB . LYS A 1 476 ? -30.858 16.520 -26.998 1.00 21.46 ? 501 LYS A CB 1 ATOM 3873 C CG . LYS A 1 476 ? -30.947 15.739 -28.301 1.00 20.04 ? 501 LYS A CG 1 ATOM 3874 C CD . LYS A 1 476 ? -29.892 14.637 -28.385 1.00 19.91 ? 501 LYS A CD 1 ATOM 3875 C CE . LYS A 1 476 ? -30.029 13.877 -29.697 1.00 20.26 ? 501 LYS A CE 1 ATOM 3876 N NZ . LYS A 1 476 ? -29.143 12.677 -29.767 1.00 19.78 ? 501 LYS A NZ 1 ATOM 3877 N N . THR A 1 477 ? -30.282 19.311 -28.243 1.00 20.94 ? 502 THR A N 1 ATOM 3878 C CA . THR A 1 477 ? -30.252 20.168 -29.424 1.00 23.96 ? 502 THR A CA 1 ATOM 3879 C C . THR A 1 477 ? -28.909 20.890 -29.552 1.00 24.67 ? 502 THR A C 1 ATOM 3880 O O . THR A 1 477 ? -28.400 21.079 -30.659 1.00 29.46 ? 502 THR A O 1 ATOM 3881 C CB . THR A 1 477 ? -31.408 21.181 -29.413 1.00 23.94 ? 502 THR A CB 1 ATOM 3882 O OG1 . THR A 1 477 ? -32.649 20.490 -29.228 1.00 29.76 ? 502 THR A OG1 1 ATOM 3883 C CG2 . THR A 1 477 ? -31.453 21.941 -30.723 1.00 32.29 ? 502 THR A CG2 1 ATOM 3884 N N . LEU A 1 478 ? -28.333 21.279 -28.418 1.00 25.06 ? 503 LEU A N 1 ATOM 3885 C CA . LEU A 1 478 ? -27.029 21.935 -28.394 1.00 25.85 ? 503 LEU A CA 1 ATOM 3886 C C . LEU A 1 478 ? -25.884 21.020 -28.827 1.00 25.96 ? 503 LEU A C 1 ATOM 3887 O O . LEU A 1 478 ? -25.025 21.419 -29.615 1.00 32.52 ? 503 LEU A O 1 ATOM 3888 C CB . LEU A 1 478 ? -26.725 22.470 -26.993 1.00 33.61 ? 503 LEU A CB 1 ATOM 3889 C CG . LEU A 1 478 ? -27.486 23.700 -26.502 1.00 43.02 ? 503 LEU A CG 1 ATOM 3890 C CD1 . LEU A 1 478 ? -27.333 23.844 -24.995 1.00 46.62 ? 503 LEU A CD1 1 ATOM 3891 C CD2 . LEU A 1 478 ? -26.994 24.949 -27.219 1.00 45.73 ? 503 LEU A CD2 1 ATOM 3892 N N . ILE A 1 479 ? -25.860 19.801 -28.302 1.00 24.94 ? 504 ILE A N 1 ATOM 3893 C CA . ILE A 1 479 ? -24.701 18.933 -28.477 1.00 23.03 ? 504 ILE A CA 1 ATOM 3894 C C . ILE A 1 479 ? -24.816 17.955 -29.656 1.00 22.22 ? 504 ILE A C 1 ATOM 3895 O O . ILE A 1 479 ? -23.803 17.530 -30.213 1.00 24.49 ? 504 ILE A O 1 ATOM 3896 C CB . ILE A 1 479 ? -24.364 18.175 -27.159 1.00 21.47 ? 504 ILE A CB 1 ATOM 3897 C CG1 . ILE A 1 479 ? -22.921 17.668 -27.171 1.00 25.21 ? 504 ILE A CG1 1 ATOM 3898 C CG2 . ILE A 1 479 ? -25.330 17.017 -26.916 1.00 19.67 ? 504 ILE A CG2 1 ATOM 3899 C CD1 . ILE A 1 479 ? -21.886 18.772 -27.187 1.00 27.58 ? 504 ILE A CD1 1 ATOM 3900 N N . ASP A 1 480 ? -26.038 17.605 -30.045 1.00 23.75 ? 505 ASP A N 1 ATOM 3901 C CA . ASP A 1 480 ? -26.228 16.627 -31.122 1.00 22.83 ? 505 ASP A CA 1 ATOM 3902 C C . ASP A 1 480 ? -27.453 16.983 -31.967 1.00 22.48 ? 505 ASP A C 1 ATOM 3903 O O . ASP A 1 480 ? -28.387 16.190 -32.079 1.00 23.56 ? 505 ASP A O 1 ATOM 3904 C CB . ASP A 1 480 ? -26.340 15.204 -30.542 1.00 23.76 ? 505 ASP A CB 1 ATOM 3905 C CG . ASP A 1 480 ? -26.376 14.119 -31.621 1.00 20.31 ? 505 ASP A CG 1 ATOM 3906 O OD1 . ASP A 1 480 ? -25.909 14.374 -32.755 1.00 22.91 ? 505 ASP A OD1 1 ATOM 3907 O OD2 . ASP A 1 480 ? -26.875 13.005 -31.333 1.00 20.71 ? 505 ASP A OD2 1 ATOM 3908 N N . PRO A 1 481 ? -27.451 18.187 -32.568 1.00 25.39 ? 506 PRO A N 1 ATOM 3909 C CA . PRO A 1 481 ? -28.619 18.685 -33.303 1.00 26.62 ? 506 PRO A CA 1 ATOM 3910 C C . PRO A 1 481 ? -29.025 17.771 -34.457 1.00 26.03 ? 506 PRO A C 1 ATOM 3911 O O . PRO A 1 481 ? -30.202 17.724 -34.817 1.00 29.06 ? 506 PRO A O 1 ATOM 3912 C CB . PRO A 1 481 ? -28.138 20.044 -33.845 1.00 28.41 ? 506 PRO A CB 1 ATOM 3913 C CG . PRO A 1 481 ? -26.636 19.951 -33.812 1.00 25.94 ? 506 PRO A CG 1 ATOM 3914 C CD . PRO A 1 481 ? -26.367 19.180 -32.554 1.00 24.50 ? 506 PRO A CD 1 ATOM 3915 N N . ASN A 1 482 ? -28.064 17.050 -35.021 1.00 25.03 ? 507 ASN A N 1 ATOM 3916 C CA . ASN A 1 482 ? -28.337 16.191 -36.165 1.00 29.39 ? 507 ASN A CA 1 ATOM 3917 C C . ASN A 1 482 ? -28.665 14.757 -35.755 1.00 25.17 ? 507 ASN A C 1 ATOM 3918 O O . ASN A 1 482 ? -28.826 13.880 -36.602 1.00 26.72 ? 507 ASN A O 1 ATOM 3919 C CB . ASN A 1 482 ? -27.171 16.232 -37.154 1.00 27.94 ? 507 ASN A CB 1 ATOM 3920 C CG . ASN A 1 482 ? -26.948 17.622 -37.728 1.00 31.93 ? 507 ASN A CG 1 ATOM 3921 O OD1 . ASN A 1 482 ? -27.893 18.290 -38.143 1.00 36.48 ? 507 ASN A OD1 1 ATOM 3922 N ND2 . ASN A 1 482 ? -25.697 18.065 -37.745 1.00 34.65 ? 507 ASN A ND2 1 ATOM 3923 N N . ASN A 1 483 ? -28.764 14.530 -34.447 1.00 21.41 ? 508 ASN A N 1 ATOM 3924 C CA . ASN A 1 483 ? -29.209 13.242 -33.912 1.00 22.88 ? 508 ASN A CA 1 ATOM 3925 C C . ASN A 1 483 ? -28.345 12.066 -34.354 1.00 21.43 ? 508 ASN A C 1 ATOM 3926 O O . ASN A 1 483 ? -28.857 11.017 -34.744 1.00 22.51 ? 508 ASN A O 1 ATOM 3927 C CB . ASN A 1 483 ? -30.683 12.980 -34.258 1.00 25.22 ? 508 ASN A CB 1 ATOM 3928 C CG . ASN A 1 483 ? -31.383 12.122 -33.215 1.00 24.98 ? 508 ASN A CG 1 ATOM 3929 O OD1 . ASN A 1 483 ? -30.913 11.997 -32.085 1.00 22.81 ? 508 ASN A OD1 1 ATOM 3930 N ND2 . ASN A 1 483 ? -32.519 11.535 -33.588 1.00 26.21 ? 508 ASN A ND2 1 ATOM 3931 N N . VAL A 1 484 ? -27.031 12.248 -34.286 1.00 20.17 ? 509 VAL A N 1 ATOM 3932 C CA . VAL A 1 484 ? -26.090 11.189 -34.631 1.00 20.40 ? 509 VAL A CA 1 ATOM 3933 C C . VAL A 1 484 ? -26.126 10.057 -33.602 1.00 20.72 ? 509 VAL A C 1 ATOM 3934 O O . VAL A 1 484 ? -25.888 8.895 -33.924 1.00 21.30 ? 509 VAL A O 1 ATOM 3935 C CB . VAL A 1 484 ? -24.658 11.749 -34.757 1.00 23.78 ? 509 VAL A CB 1 ATOM 3936 C CG1 . VAL A 1 484 ? -23.653 10.628 -34.910 1.00 25.94 ? 509 VAL A CG1 1 ATOM 3937 C CG2 . VAL A 1 484 ? -24.578 12.716 -35.939 1.00 22.18 ? 509 VAL A CG2 1 ATOM 3938 N N . PHE A 1 485 ? -26.443 10.403 -32.360 1.00 19.08 ? 510 PHE A N 1 ATOM 3939 C CA . PHE A 1 485 ? -26.511 9.416 -31.296 1.00 19.56 ? 510 PHE A CA 1 ATOM 3940 C C . PHE A 1 485 ? -27.961 9.178 -30.919 1.00 19.69 ? 510 PHE A C 1 ATOM 3941 O O . PHE A 1 485 ? -28.581 9.988 -30.234 1.00 20.22 ? 510 PHE A O 1 ATOM 3942 C CB . PHE A 1 485 ? -25.673 9.873 -30.104 1.00 18.40 ? 510 PHE A CB 1 ATOM 3943 C CG . PHE A 1 485 ? -24.223 10.058 -30.450 1.00 19.48 ? 510 PHE A CG 1 ATOM 3944 C CD1 . PHE A 1 485 ? -23.349 8.991 -30.385 1.00 20.03 ? 510 PHE A CD1 1 ATOM 3945 C CD2 . PHE A 1 485 ? -23.749 11.283 -30.893 1.00 20.64 ? 510 PHE A CD2 1 ATOM 3946 C CE1 . PHE A 1 485 ? -22.013 9.146 -30.733 1.00 21.35 ? 510 PHE A CE1 1 ATOM 3947 C CE2 . PHE A 1 485 ? -22.410 11.448 -31.241 1.00 20.29 ? 510 PHE A CE2 1 ATOM 3948 C CZ . PHE A 1 485 ? -21.548 10.379 -31.160 1.00 21.07 ? 510 PHE A CZ 1 ATOM 3949 N N . ASN A 1 486 ? -28.500 8.060 -31.389 1.00 17.27 ? 511 ASN A N 1 ATOM 3950 C CA . ASN A 1 486 ? -29.928 7.798 -31.246 1.00 17.85 ? 511 ASN A CA 1 ATOM 3951 C C . ASN A 1 486 ? -30.222 6.328 -31.001 1.00 19.07 ? 511 ASN A C 1 ATOM 3952 O O . ASN A 1 486 ? -29.431 5.461 -31.354 1.00 20.61 ? 511 ASN A O 1 ATOM 3953 C CB . ASN A 1 486 ? -30.689 8.297 -32.485 1.00 20.35 ? 511 ASN A CB 1 ATOM 3954 C CG . ASN A 1 486 ? -30.287 7.563 -33.762 1.00 23.00 ? 511 ASN A CG 1 ATOM 3955 O OD1 . ASN A 1 486 ? -30.757 6.461 -34.029 1.00 24.01 ? 511 ASN A OD1 1 ATOM 3956 N ND2 . ASN A 1 486 ? -29.423 8.186 -34.561 1.00 24.11 ? 511 ASN A ND2 1 ATOM 3957 N N . HIS A 1 487 ? -31.359 6.064 -30.365 1.00 18.36 ? 512 HIS A N 1 ATOM 3958 C CA . HIS A 1 487 ? -31.848 4.707 -30.152 1.00 17.73 ? 512 HIS A CA 1 ATOM 3959 C C . HIS A 1 487 ? -33.357 4.837 -29.919 1.00 16.82 ? 512 HIS A C 1 ATOM 3960 O O . HIS A 1 487 ? -33.879 5.938 -29.973 1.00 17.54 ? 512 HIS A O 1 ATOM 3961 C CB . HIS A 1 487 ? -31.093 3.993 -29.014 1.00 17.16 ? 512 HIS A CB 1 ATOM 3962 C CG . HIS A 1 487 ? -31.253 4.620 -27.663 1.00 17.49 ? 512 HIS A CG 1 ATOM 3963 N ND1 . HIS A 1 487 ? -32.401 4.486 -26.912 1.00 17.93 ? 512 HIS A ND1 1 ATOM 3964 C CD2 . HIS A 1 487 ? -30.387 5.334 -26.904 1.00 20.45 ? 512 HIS A CD2 1 ATOM 3965 C CE1 . HIS A 1 487 ? -32.245 5.114 -25.759 1.00 20.80 ? 512 HIS A CE1 1 ATOM 3966 N NE2 . HIS A 1 487 ? -31.032 5.638 -25.729 1.00 20.25 ? 512 HIS A NE2 1 ATOM 3967 N N . PRO A 1 488 ? -34.068 3.725 -29.691 1.00 17.19 ? 513 PRO A N 1 ATOM 3968 C CA . PRO A 1 488 ? -35.531 3.852 -29.659 1.00 18.91 ? 513 PRO A CA 1 ATOM 3969 C C . PRO A 1 488 ? -36.065 4.803 -28.589 1.00 18.68 ? 513 PRO A C 1 ATOM 3970 O O . PRO A 1 488 ? -37.167 5.332 -28.754 1.00 20.34 ? 513 PRO A O 1 ATOM 3971 C CB . PRO A 1 488 ? -35.994 2.422 -29.377 1.00 21.97 ? 513 PRO A CB 1 ATOM 3972 C CG . PRO A 1 488 ? -34.916 1.574 -29.988 1.00 22.69 ? 513 PRO A CG 1 ATOM 3973 C CD . PRO A 1 488 ? -33.638 2.316 -29.686 1.00 19.08 ? 513 PRO A CD 1 ATOM 3974 N N . GLN A 1 489 ? -35.307 5.025 -27.519 1.00 19.55 ? 514 GLN A N 1 ATOM 3975 C CA . GLN A 1 489 ? -35.763 5.926 -26.460 1.00 17.80 ? 514 GLN A CA 1 ATOM 3976 C C . GLN A 1 489 ? -34.812 7.090 -26.184 1.00 20.21 ? 514 GLN A C 1 ATOM 3977 O O . GLN A 1 489 ? -34.800 7.645 -25.084 1.00 24.02 ? 514 GLN A O 1 ATOM 3978 C CB . GLN A 1 489 ? -36.054 5.145 -25.170 1.00 18.65 ? 514 GLN A CB 1 ATOM 3979 C CG . GLN A 1 489 ? -37.301 4.286 -25.283 1.00 17.00 ? 514 GLN A CG 1 ATOM 3980 C CD . GLN A 1 489 ? -37.697 3.654 -23.973 1.00 18.17 ? 514 GLN A CD 1 ATOM 3981 O OE1 . GLN A 1 489 ? -36.960 3.730 -22.988 1.00 20.35 ? 514 GLN A OE1 1 ATOM 3982 N NE2 . GLN A 1 489 ? -38.856 3.011 -23.954 1.00 20.16 ? 514 GLN A NE2 1 ATOM 3983 N N . SER A 1 490 ? -34.029 7.479 -27.183 1.00 16.76 ? 515 SER A N 1 ATOM 3984 C CA . SER A 1 490 ? -33.109 8.596 -27.010 1.00 19.09 ? 515 SER A CA 1 ATOM 3985 C C . SER A 1 490 ? -33.862 9.931 -27.000 1.00 19.58 ? 515 SER A C 1 ATOM 3986 O O . SER A 1 490 ? -34.902 10.069 -27.635 1.00 20.08 ? 515 SER A O 1 ATOM 3987 C CB . SER A 1 490 ? -32.029 8.586 -28.098 1.00 18.69 ? 515 SER A CB 1 ATOM 3988 O OG . SER A 1 490 ? -32.610 8.579 -29.398 1.00 17.63 ? 515 SER A OG 1 ATOM 3989 N N . ILE A 1 491 ? -33.339 10.896 -26.253 1.00 19.59 ? 516 ILE A N 1 ATOM 3990 C CA . ILE A 1 491 ? -33.932 12.229 -26.174 1.00 20.27 ? 516 ILE A CA 1 ATOM 3991 C C . ILE A 1 491 ? -33.948 12.900 -27.549 1.00 18.45 ? 516 ILE A C 1 ATOM 3992 O O . ILE A 1 491 ? -32.910 13.015 -28.203 1.00 21.10 ? 516 ILE A O 1 ATOM 3993 C CB . ILE A 1 491 ? -33.147 13.119 -25.196 1.00 20.93 ? 516 ILE A CB 1 ATOM 3994 C CG1 . ILE A 1 491 ? -33.097 12.486 -23.799 1.00 24.15 ? 516 ILE A CG1 1 ATOM 3995 C CG2 . ILE A 1 491 ? -33.729 14.530 -25.165 1.00 21.11 ? 516 ILE A CG2 1 ATOM 3996 C CD1 . ILE A 1 491 ? -34.412 12.514 -23.063 1.00 28.19 ? 516 ILE A CD1 1 ATOM 3997 N N . PRO A 1 492 ? -35.128 13.349 -28.007 1.00 20.26 ? 517 PRO A N 1 ATOM 3998 C CA . PRO A 1 492 ? -35.207 13.988 -29.329 1.00 21.20 ? 517 PRO A CA 1 ATOM 3999 C C . PRO A 1 492 ? -34.582 15.379 -29.333 1.00 24.73 ? 517 PRO A C 1 ATOM 4000 O O . PRO A 1 492 ? -34.702 16.104 -28.345 1.00 24.63 ? 517 PRO A O 1 ATOM 4001 C CB . PRO A 1 492 ? -36.722 14.115 -29.577 1.00 23.52 ? 517 PRO A CB 1 ATOM 4002 C CG . PRO A 1 492 ? -37.378 13.234 -28.549 1.00 28.07 ? 517 PRO A CG 1 ATOM 4003 C CD . PRO A 1 492 ? -36.450 13.219 -27.371 1.00 24.17 ? 517 PRO A CD 1 ATOM 4004 N N . PRO A 1 493 ? -33.916 15.747 -30.438 1.00 22.46 ? 518 PRO A N 1 ATOM 4005 C CA . PRO A 1 493 ? -33.484 17.126 -30.639 1.00 24.05 ? 518 PRO A CA 1 ATOM 4006 C C . PRO A 1 493 ? -34.682 17.883 -31.173 1.00 32.74 ? 518 PRO A C 1 ATOM 4007 O O . PRO A 1 493 ? -35.576 17.251 -31.737 1.00 31.22 ? 518 PRO A O 1 ATOM 4008 C CB . PRO A 1 493 ? -32.441 17.018 -31.762 1.00 27.23 ? 518 PRO A CB 1 ATOM 4009 C CG . PRO A 1 493 ? -32.426 15.588 -32.206 1.00 32.99 ? 518 PRO A CG 1 ATOM 4010 C CD . PRO A 1 493 ? -33.598 14.893 -31.591 1.00 24.11 ? 518 PRO A CD 1 ATOM 4011 N N . MET A 1 494 ? -34.710 19.200 -31.015 1.00 31.72 ? 519 MET A N 1 ATOM 4012 C CA . MET A 1 494 ? -35.745 19.982 -31.676 1.00 30.96 ? 519 MET A CA 1 ATOM 4013 C C . MET A 1 494 ? -35.394 20.163 -33.144 1.00 40.08 ? 519 MET A C 1 ATOM 4014 O O . MET A 1 494 ? -34.225 20.315 -33.493 1.00 42.63 ? 519 MET A O 1 ATOM 4015 C CB . MET A 1 494 ? -35.939 21.326 -30.987 1.00 38.44 ? 519 MET A CB 1 ATOM 4016 C CG . MET A 1 494 ? -36.909 21.253 -29.827 1.00 47.50 ? 519 MET A CG 1 ATOM 4017 S SD . MET A 1 494 ? -37.372 22.877 -29.215 1.00 70.59 ? 519 MET A SD 1 ATOM 4018 C CE . MET A 1 494 ? -38.843 22.463 -28.285 1.00 41.47 ? 519 MET A CE 1 ATOM 4019 N N . ALA A 1 495 ? -36.409 20.130 -34.002 1.00 43.19 ? 520 ALA A N 1 ATOM 4020 C CA . ALA A 1 495 ? -36.198 20.240 -35.441 1.00 58.79 ? 520 ALA A CA 1 ATOM 4021 C C . ALA A 1 495 ? -35.915 21.680 -35.853 1.00 69.83 ? 520 ALA A C 1 ATOM 4022 O O . ALA A 1 495 ? -36.711 22.301 -36.557 1.00 75.60 ? 520 ALA A O 1 ATOM 4023 C CB . ALA A 1 495 ? -37.402 19.698 -36.196 1.00 62.51 ? 520 ALA A CB 1 HETATM 4024 P PA . FAD B 2 . ? -23.918 -0.828 -22.303 1.00 15.59 ? 1 FAD A PA 1 HETATM 4025 O O1A . FAD B 2 . ? -24.944 -1.810 -22.825 1.00 16.76 ? 1 FAD A O1A 1 HETATM 4026 O O2A . FAD B 2 . ? -22.535 -0.978 -22.886 1.00 15.69 ? 1 FAD A O2A 1 HETATM 4027 O O5B . FAD B 2 . ? -24.408 0.686 -22.491 1.00 15.71 ? 1 FAD A O5B 1 HETATM 4028 C C5B . FAD B 2 . ? -25.686 1.108 -22.031 1.00 14.85 ? 1 FAD A C5B 1 HETATM 4029 C C4B . FAD B 2 . ? -26.115 2.314 -22.873 1.00 14.38 ? 1 FAD A C4B 1 HETATM 4030 O O4B . FAD B 2 . ? -25.154 3.352 -22.721 1.00 16.23 ? 1 FAD A O4B 1 HETATM 4031 C C3B . FAD B 2 . ? -26.193 2.031 -24.365 1.00 14.63 ? 1 FAD A C3B 1 HETATM 4032 O O3B . FAD B 2 . ? -27.136 2.923 -24.925 1.00 17.83 ? 1 FAD A O3B 1 HETATM 4033 C C2B . FAD B 2 . ? -24.812 2.421 -24.854 1.00 14.76 ? 1 FAD A C2B 1 HETATM 4034 O O2B . FAD B 2 . ? -24.752 2.759 -26.226 1.00 16.85 ? 1 FAD A O2B 1 HETATM 4035 C C1B . FAD B 2 . ? -24.512 3.607 -23.954 1.00 15.37 ? 1 FAD A C1B 1 HETATM 4036 N N9A . FAD B 2 . ? -23.069 3.790 -23.706 1.00 15.93 ? 1 FAD A N9A 1 HETATM 4037 C C8A . FAD B 2 . ? -22.159 2.843 -23.325 1.00 17.28 ? 1 FAD A C8A 1 HETATM 4038 N N7A . FAD B 2 . ? -20.953 3.443 -23.206 1.00 15.35 ? 1 FAD A N7A 1 HETATM 4039 C C5A . FAD B 2 . ? -21.082 4.754 -23.498 1.00 14.50 ? 1 FAD A C5A 1 HETATM 4040 C C6A . FAD B 2 . ? -20.188 5.813 -23.535 1.00 16.04 ? 1 FAD A C6A 1 HETATM 4041 N N6A . FAD B 2 . ? -18.900 5.639 -23.225 1.00 16.42 ? 1 FAD A N6A 1 HETATM 4042 N N1A . FAD B 2 . ? -20.652 7.062 -23.875 1.00 15.81 ? 1 FAD A N1A 1 HETATM 4043 C C2A . FAD B 2 . ? -21.981 7.262 -24.183 1.00 18.12 ? 1 FAD A C2A 1 HETATM 4044 N N3A . FAD B 2 . ? -22.860 6.203 -24.151 1.00 16.17 ? 1 FAD A N3A 1 HETATM 4045 C C4A . FAD B 2 . ? -22.413 4.980 -23.815 1.00 14.96 ? 1 FAD A C4A 1 HETATM 4046 N N1 . FAD B 2 . ? -27.871 -0.290 -12.387 1.00 20.90 ? 1 FAD A N1 1 HETATM 4047 C C2 . FAD B 2 . ? -27.809 0.434 -11.210 1.00 25.09 ? 1 FAD A C2 1 HETATM 4048 O O2 . FAD B 2 . ? -28.006 1.660 -11.215 1.00 20.52 ? 1 FAD A O2 1 HETATM 4049 N N3 . FAD B 2 . ? -27.418 -0.197 -10.049 1.00 22.53 ? 1 FAD A N3 1 HETATM 4050 C C4 . FAD B 2 . ? -27.073 -1.533 -10.054 1.00 19.52 ? 1 FAD A C4 1 HETATM 4051 O O4 . FAD B 2 . ? -26.762 -2.062 -8.973 1.00 21.83 ? 1 FAD A O4 1 HETATM 4052 C C4X . FAD B 2 . ? -27.244 -2.284 -11.216 1.00 19.81 ? 1 FAD A C4X 1 HETATM 4053 N N5 . FAD B 2 . ? -26.911 -3.627 -11.259 1.00 20.05 ? 1 FAD A N5 1 HETATM 4054 C C5X . FAD B 2 . ? -26.820 -4.290 -12.469 1.00 17.09 ? 1 FAD A C5X 1 HETATM 4055 C C6 . FAD B 2 . ? -26.361 -5.604 -12.518 1.00 18.73 ? 1 FAD A C6 1 HETATM 4056 C C7 . FAD B 2 . ? -26.255 -6.284 -13.723 1.00 19.50 ? 1 FAD A C7 1 HETATM 4057 C C7M . FAD B 2 . ? -25.818 -7.722 -13.728 1.00 26.56 ? 1 FAD A C7M 1 HETATM 4058 C C8 . FAD B 2 . ? -26.573 -5.631 -14.913 1.00 18.70 ? 1 FAD A C8 1 HETATM 4059 C C8M . FAD B 2 . ? -26.404 -6.315 -16.235 1.00 17.95 ? 1 FAD A C8M 1 HETATM 4060 C C9 . FAD B 2 . ? -27.026 -4.315 -14.867 1.00 18.18 ? 1 FAD A C9 1 HETATM 4061 C C9A . FAD B 2 . ? -27.164 -3.648 -13.652 1.00 16.83 ? 1 FAD A C9A 1 HETATM 4062 N N10 . FAD B 2 . ? -27.654 -2.353 -13.594 1.00 18.56 ? 1 FAD A N10 1 HETATM 4063 C C10 . FAD B 2 . ? -27.602 -1.647 -12.401 1.00 21.14 ? 1 FAD A C10 1 HETATM 4064 C "C1'" . FAD B 2 . ? -28.086 -1.645 -14.847 1.00 18.63 ? 1 FAD A "C1'" 1 HETATM 4065 C "C2'" . FAD B 2 . ? -26.951 -0.808 -15.441 1.00 18.25 ? 1 FAD A "C2'" 1 HETATM 4066 O "O2'" . FAD B 2 . ? -26.750 0.356 -14.657 1.00 18.23 ? 1 FAD A "O2'" 1 HETATM 4067 C "C3'" . FAD B 2 . ? -27.288 -0.393 -16.867 1.00 15.99 ? 1 FAD A "C3'" 1 HETATM 4068 O "O3'" . FAD B 2 . ? -27.549 -1.557 -17.638 1.00 17.69 ? 1 FAD A "O3'" 1 HETATM 4069 C "C4'" . FAD B 2 . ? -26.129 0.404 -17.457 1.00 16.50 ? 1 FAD A "C4'" 1 HETATM 4070 O "O4'" . FAD B 2 . ? -26.593 1.364 -18.385 1.00 16.54 ? 1 FAD A "O4'" 1 HETATM 4071 C "C5'" . FAD B 2 . ? -25.135 -0.536 -18.129 1.00 17.73 ? 1 FAD A "C5'" 1 HETATM 4072 O "O5'" . FAD B 2 . ? -23.979 0.163 -18.583 1.00 16.34 ? 1 FAD A "O5'" 1 HETATM 4073 P P . FAD B 2 . ? -22.953 -0.639 -19.512 1.00 16.02 ? 1 FAD A P 1 HETATM 4074 O O1P . FAD B 2 . ? -21.834 0.262 -19.956 1.00 15.01 ? 1 FAD A O1P 1 HETATM 4075 O O2P . FAD B 2 . ? -22.570 -1.924 -18.839 1.00 16.54 ? 1 FAD A O2P 1 HETATM 4076 O O3P . FAD B 2 . ? -23.939 -1.065 -20.723 1.00 14.70 ? 1 FAD A O3P 1 HETATM 4077 C C1 . SLX C 3 . ? -29.303 -8.317 -10.952 0.84 26.50 ? 2 SLX A C1 1 HETATM 4078 C C2 . SLX C 3 . ? -28.702 -9.516 -10.654 0.84 27.22 ? 2 SLX A C2 1 HETATM 4079 C C3 . SLX C 3 . ? -28.720 -10.567 -11.560 0.84 29.13 ? 2 SLX A C3 1 HETATM 4080 C C5 . SLX C 3 . ? -29.335 -10.434 -12.770 0.84 25.41 ? 2 SLX A C5 1 HETATM 4081 C C8 . SLX C 3 . ? -29.969 -9.218 -13.118 0.84 22.43 ? 2 SLX A C8 1 HETATM 4082 C C9 . SLX C 3 . ? -29.950 -8.142 -12.188 0.84 24.42 ? 2 SLX A C9 1 HETATM 4083 C C10 . SLX C 3 . ? -30.824 -6.908 -12.428 0.84 26.55 ? 2 SLX A C10 1 HETATM 4084 C C11 . SLX C 3 . ? -30.290 -5.747 -11.597 0.84 25.30 ? 2 SLX A C11 1 HETATM 4085 N N12 . SLX C 3 . ? -30.316 -6.233 -10.221 0.84 25.26 ? 2 SLX A N12 1 HETATM 4086 C C14 . SLX C 3 . ? -29.291 -7.233 -9.938 0.84 23.78 ? 2 SLX A C14 1 HETATM 4087 C C16 . SLX C 3 . ? -29.543 -7.883 -8.583 0.84 28.30 ? 2 SLX A C16 1 HETATM 4088 C C17 . SLX C 3 . ? -29.526 -6.778 -7.528 0.84 28.51 ? 2 SLX A C17 1 HETATM 4089 C C25 . SLX C 3 . ? -29.135 -7.066 -6.236 0.84 29.24 ? 2 SLX A C25 1 HETATM 4090 C C24 . SLX C 3 . ? -29.122 -6.071 -5.290 0.84 24.92 ? 2 SLX A C24 1 HETATM 4091 C C21 . SLX C 3 . ? -29.513 -4.746 -5.657 0.84 23.64 ? 2 SLX A C21 1 HETATM 4092 O O22 . SLX C 3 . ? -29.504 -3.778 -4.760 0.84 26.50 ? 2 SLX A O22 1 HETATM 4093 C C23 . SLX C 3 . ? -28.901 -4.006 -3.466 0.84 27.35 ? 2 SLX A C23 1 HETATM 4094 C C19 . SLX C 3 . ? -29.891 -4.477 -6.918 0.84 25.79 ? 2 SLX A C19 1 HETATM 4095 O O20 . SLX C 3 . ? -30.261 -3.204 -7.256 0.84 34.54 ? 2 SLX A O20 1 HETATM 4096 C C18 . SLX C 3 . ? -29.901 -5.464 -7.865 0.84 23.35 ? 2 SLX A C18 1 HETATM 4097 C C13 . SLX C 3 . ? -30.329 -5.117 -9.273 0.84 27.00 ? 2 SLX A C13 1 HETATM 4098 O O6 . SLX C 3 . ? -29.332 -11.490 -13.624 0.84 35.72 ? 2 SLX A O6 1 HETATM 4099 C C7 . SLX C 3 . ? -29.432 -11.288 -14.957 0.84 39.78 ? 2 SLX A C7 1 HETATM 4100 O O4 . SLX C 3 . ? -28.123 -11.738 -11.243 0.84 32.96 ? 2 SLX A O4 1 HETATM 4101 C C1 . MAN D 4 . ? -2.904 -11.617 -24.111 1.00 75.64 ? 3 MAN A C1 1 HETATM 4102 C C2 . MAN D 4 . ? -2.483 -11.693 -22.656 1.00 80.06 ? 3 MAN A C2 1 HETATM 4103 C C3 . MAN D 4 . ? -1.461 -12.809 -22.600 1.00 81.73 ? 3 MAN A C3 1 HETATM 4104 C C4 . MAN D 4 . ? -2.142 -14.100 -23.050 1.00 83.66 ? 3 MAN A C4 1 HETATM 4105 C C5 . MAN D 4 . ? -3.005 -13.946 -24.312 1.00 81.68 ? 3 MAN A C5 1 HETATM 4106 C C6 . MAN D 4 . ? -3.976 -15.120 -24.401 1.00 76.97 ? 3 MAN A C6 1 HETATM 4107 O O2 . MAN D 4 . ? -3.590 -11.996 -21.839 1.00 82.10 ? 3 MAN A O2 1 HETATM 4108 O O3 . MAN D 4 . ? -0.967 -12.945 -21.287 1.00 78.51 ? 3 MAN A O3 1 HETATM 4109 O O4 . MAN D 4 . ? -1.151 -15.075 -23.295 1.00 86.14 ? 3 MAN A O4 1 HETATM 4110 O O5 . MAN D 4 . ? -3.740 -12.731 -24.343 1.00 83.21 ? 3 MAN A O5 1 HETATM 4111 O O6 . MAN D 4 . ? -4.589 -15.155 -25.670 1.00 74.96 ? 3 MAN A O6 1 HETATM 4112 C C1 . NAG E 5 . ? -7.768 -5.195 -30.569 1.00 32.99 ? 521 NAG A C1 1 HETATM 4113 C C2 . NAG E 5 . ? -6.394 -5.829 -30.778 1.00 44.85 ? 521 NAG A C2 1 HETATM 4114 C C3 . NAG E 5 . ? -6.190 -7.151 -30.040 1.00 45.89 ? 521 NAG A C3 1 HETATM 4115 C C4 . NAG E 5 . ? -6.889 -7.213 -28.685 1.00 37.78 ? 521 NAG A C4 1 HETATM 4116 C C5 . NAG E 5 . ? -8.284 -6.611 -28.762 1.00 26.63 ? 521 NAG A C5 1 HETATM 4117 C C6 . NAG E 5 . ? -8.987 -6.645 -27.409 1.00 31.25 ? 521 NAG A C6 1 HETATM 4118 C C7 . NAG E 5 . ? -5.336 -5.307 -32.889 1.00 52.53 ? 521 NAG A C7 1 HETATM 4119 C C8 . NAG E 5 . ? -5.248 -5.577 -34.362 1.00 49.91 ? 521 NAG A C8 1 HETATM 4120 N N2 . NAG E 5 . ? -6.194 -6.049 -32.199 1.00 49.73 ? 521 NAG A N2 1 HETATM 4121 O O3 . NAG E 5 . ? -4.807 -7.366 -29.858 1.00 55.60 ? 521 NAG A O3 1 HETATM 4122 O O4 . NAG E 5 . ? -6.936 -8.566 -28.283 1.00 38.27 ? 521 NAG A O4 1 HETATM 4123 O O5 . NAG E 5 . ? -8.173 -5.278 -29.216 1.00 28.83 ? 521 NAG A O5 1 HETATM 4124 O O6 . NAG E 5 . ? -8.192 -6.009 -26.433 1.00 32.11 ? 521 NAG A O6 1 HETATM 4125 O O7 . NAG E 5 . ? -4.642 -4.437 -32.366 1.00 60.70 ? 521 NAG A O7 1 HETATM 4126 C C1 . NAG F 5 . ? -6.176 -8.730 -27.071 1.00 41.69 ? 522 NAG A C1 1 HETATM 4127 C C2 . NAG F 5 . ? -6.644 -9.996 -26.348 1.00 38.98 ? 522 NAG A C2 1 HETATM 4128 C C3 . NAG F 5 . ? -5.731 -10.439 -25.199 1.00 44.43 ? 522 NAG A C3 1 HETATM 4129 C C4 . NAG F 5 . ? -4.253 -10.246 -25.534 1.00 52.64 ? 522 NAG A C4 1 HETATM 4130 C C5 . NAG F 5 . ? -4.029 -8.871 -26.142 1.00 49.59 ? 522 NAG A C5 1 HETATM 4131 C C6 . NAG F 5 . ? -2.551 -8.619 -26.423 1.00 49.46 ? 522 NAG A C6 1 HETATM 4132 C C7 . NAG F 5 . ? -9.010 -10.411 -26.582 1.00 42.89 ? 522 NAG A C7 1 HETATM 4133 C C8 . NAG F 5 . ? -10.353 -10.425 -25.917 1.00 45.81 ? 522 NAG A C8 1 HETATM 4134 N N2 . NAG F 5 . ? -8.017 -9.840 -25.905 1.00 44.80 ? 522 NAG A N2 1 HETATM 4135 O O3 . NAG F 5 . ? -6.003 -11.790 -24.902 1.00 46.55 ? 522 NAG A O3 1 HETATM 4136 O O4 . NAG F 5 . ? -3.413 -10.298 -24.400 1.00 63.67 ? 522 NAG A O4 1 HETATM 4137 O O5 . NAG F 5 . ? -4.787 -8.742 -27.323 1.00 44.43 ? 522 NAG A O5 1 HETATM 4138 O O6 . NAG F 5 . ? -2.072 -9.568 -27.349 1.00 52.31 ? 522 NAG A O6 1 HETATM 4139 O O7 . NAG F 5 . ? -8.861 -10.907 -27.699 1.00 46.37 ? 522 NAG A O7 1 HETATM 4140 C C1 . NAG G 5 . ? -44.553 5.186 -39.237 1.00 26.72 ? 523 NAG A C1 1 HETATM 4141 C C2 . NAG G 5 . ? -45.049 4.159 -40.263 1.00 28.29 ? 523 NAG A C2 1 HETATM 4142 C C3 . NAG G 5 . ? -46.510 3.763 -40.068 1.00 38.51 ? 523 NAG A C3 1 HETATM 4143 C C4 . NAG G 5 . ? -46.838 3.536 -38.601 1.00 43.16 ? 523 NAG A C4 1 HETATM 4144 C C5 . NAG G 5 . ? -46.408 4.758 -37.806 1.00 40.09 ? 523 NAG A C5 1 HETATM 4145 C C6 . NAG G 5 . ? -46.774 4.633 -36.332 1.00 42.77 ? 523 NAG A C6 1 HETATM 4146 C C7 . NAG G 5 . ? -43.977 4.250 -42.445 1.00 40.42 ? 523 NAG A C7 1 HETATM 4147 C C8 . NAG G 5 . ? -44.048 4.774 -43.849 1.00 41.33 ? 523 NAG A C8 1 HETATM 4148 N N2 . NAG G 5 . ? -44.899 4.701 -41.598 1.00 33.47 ? 523 NAG A N2 1 HETATM 4149 O O3 . NAG G 5 . ? -46.786 2.593 -40.807 1.00 43.79 ? 523 NAG A O3 1 HETATM 4150 O O4 . NAG G 5 . ? -48.225 3.325 -38.443 1.00 49.39 ? 523 NAG A O4 1 HETATM 4151 O O5 . NAG G 5 . ? -45.015 4.921 -37.926 1.00 31.56 ? 523 NAG A O5 1 HETATM 4152 O O6 . NAG G 5 . ? -45.987 3.629 -35.735 1.00 44.35 ? 523 NAG A O6 1 HETATM 4153 O O7 . NAG G 5 . ? -43.099 3.449 -42.121 1.00 36.83 ? 523 NAG A O7 1 HETATM 4154 MG MG . MG H 6 . ? -14.841 -21.569 -38.126 1.00 46.92 ? 524 MG A MG 1 HETATM 4155 O O . HOH I 7 . ? -16.771 -22.644 -38.284 1.00 47.38 ? 4 HOH A O 1 HETATM 4156 O O . HOH I 7 . ? -14.204 -22.359 -39.887 1.00 34.33 ? 5 HOH A O 1 HETATM 4157 O O . HOH I 7 . ? -31.229 8.986 -14.626 1.00 16.80 ? 6 HOH A O 1 HETATM 4158 O O . HOH I 7 . ? -37.571 2.085 -15.991 1.00 19.52 ? 7 HOH A O 1 HETATM 4159 O O . HOH I 7 . ? -22.678 14.977 -29.969 1.00 22.00 ? 8 HOH A O 1 HETATM 4160 O O . HOH I 7 . ? -27.052 -6.736 -22.661 1.00 20.85 ? 9 HOH A O 1 HETATM 4161 O O . HOH I 7 . ? -28.718 0.967 -20.159 1.00 18.55 ? 10 HOH A O 1 HETATM 4162 O O . HOH I 7 . ? -24.272 9.634 -24.737 1.00 18.22 ? 11 HOH A O 1 HETATM 4163 O O . HOH I 7 . ? -8.616 -1.843 -12.224 1.00 21.62 ? 12 HOH A O 1 HETATM 4164 O O . HOH I 7 . ? -13.325 21.273 -17.486 1.00 23.92 ? 13 HOH A O 1 HETATM 4165 O O . HOH I 7 . ? -29.858 3.488 -20.166 1.00 18.93 ? 14 HOH A O 1 HETATM 4166 O O . HOH I 7 . ? -42.990 3.063 -10.759 1.00 17.76 ? 15 HOH A O 1 HETATM 4167 O O . HOH I 7 . ? -11.783 -0.185 -27.171 1.00 21.11 ? 16 HOH A O 1 HETATM 4168 O O . HOH I 7 . ? -24.992 3.824 -28.830 1.00 20.02 ? 17 HOH A O 1 HETATM 4169 O O . HOH I 7 . ? -39.262 -16.928 -7.054 1.00 21.25 ? 18 HOH A O 1 HETATM 4170 O O . HOH I 7 . ? -27.547 4.947 -19.553 1.00 19.35 ? 19 HOH A O 1 HETATM 4171 O O . HOH I 7 . ? -26.483 6.316 -32.729 1.00 23.02 ? 20 HOH A O 1 HETATM 4172 O O . HOH I 7 . ? -43.281 2.300 -0.760 1.00 21.64 ? 21 HOH A O 1 HETATM 4173 O O . HOH I 7 . ? -23.226 -12.248 6.865 1.00 21.46 ? 22 HOH A O 1 HETATM 4174 O O . HOH I 7 . ? -36.937 -19.032 -6.247 1.00 25.94 ? 23 HOH A O 1 HETATM 4175 O O . HOH I 7 . ? -14.995 -6.173 -13.482 1.00 23.25 ? 24 HOH A O 1 HETATM 4176 O O . HOH I 7 . ? -10.949 -0.766 0.678 1.00 21.40 ? 25 HOH A O 1 HETATM 4177 O O . HOH I 7 . ? -35.903 -14.489 11.957 1.00 55.64 ? 525 HOH A O 1 HETATM 4178 O O . HOH I 7 . ? -37.766 -20.432 9.411 1.00 48.16 ? 526 HOH A O 1 HETATM 4179 O O . HOH I 7 . ? -35.769 -17.546 10.551 1.00 55.45 ? 527 HOH A O 1 HETATM 4180 O O A HOH I 7 . ? -17.753 7.485 5.399 0.34 21.35 ? 528 HOH A O 1 HETATM 4181 O O . HOH I 7 . ? -9.783 -8.672 -37.473 1.00 47.19 ? 529 HOH A O 1 HETATM 4182 O O . HOH I 7 . ? -9.982 -5.221 -40.411 1.00 43.60 ? 530 HOH A O 1 HETATM 4183 O O . HOH I 7 . ? -21.814 3.640 -45.644 1.00 54.21 ? 531 HOH A O 1 HETATM 4184 O O . HOH I 7 . ? -21.156 -12.729 -19.171 1.00 50.09 ? 532 HOH A O 1 HETATM 4185 O O . HOH I 7 . ? -16.445 -13.683 -20.433 1.00 48.30 ? 533 HOH A O 1 HETATM 4186 O O . HOH I 7 . ? -37.851 -21.482 3.019 1.00 36.90 ? 534 HOH A O 1 HETATM 4187 O O . HOH I 7 . ? -41.960 -27.126 2.052 1.00 50.05 ? 535 HOH A O 1 HETATM 4188 O O . HOH I 7 . ? -47.296 -23.390 -2.523 1.00 51.46 ? 536 HOH A O 1 HETATM 4189 O O . HOH I 7 . ? -49.584 -23.535 1.770 1.00 52.05 ? 537 HOH A O 1 HETATM 4190 O O . HOH I 7 . ? -55.245 -1.823 -11.303 1.00 47.86 ? 538 HOH A O 1 HETATM 4191 O O . HOH I 7 . ? -38.986 -5.434 -19.495 1.00 38.90 ? 539 HOH A O 1 HETATM 4192 O O . HOH I 7 . ? -44.609 -6.938 -20.275 1.00 53.63 ? 540 HOH A O 1 HETATM 4193 O O . HOH I 7 . ? -50.747 -6.217 -18.480 1.00 47.90 ? 541 HOH A O 1 HETATM 4194 O O . HOH I 7 . ? -51.088 -10.392 -19.239 1.00 53.81 ? 542 HOH A O 1 HETATM 4195 O O . HOH I 7 . ? -42.697 -7.608 16.266 1.00 44.43 ? 543 HOH A O 1 HETATM 4196 O O . HOH I 7 . ? -31.312 -18.487 -23.714 1.00 44.23 ? 544 HOH A O 1 HETATM 4197 O O . HOH I 7 . ? -53.562 -14.760 -18.399 1.00 56.18 ? 545 HOH A O 1 HETATM 4198 O O . HOH I 7 . ? -21.865 -16.679 -37.719 1.00 52.44 ? 546 HOH A O 1 HETATM 4199 O O . HOH I 7 . ? -34.242 -12.014 -37.998 1.00 54.33 ? 547 HOH A O 1 HETATM 4200 O O . HOH I 7 . ? -32.677 -4.091 -33.236 1.00 42.85 ? 548 HOH A O 1 HETATM 4201 O O . HOH I 7 . ? -6.707 13.025 -34.924 1.00 47.23 ? 549 HOH A O 1 HETATM 4202 O O . HOH I 7 . ? -39.139 -4.730 -23.948 1.00 49.83 ? 550 HOH A O 1 HETATM 4203 O O . HOH I 7 . ? -2.520 6.342 -7.917 1.00 49.47 ? 551 HOH A O 1 HETATM 4204 O O . HOH I 7 . ? -0.995 9.679 -0.503 1.00 52.26 ? 552 HOH A O 1 HETATM 4205 O O . HOH I 7 . ? 0.442 6.014 -2.067 1.00 54.41 ? 553 HOH A O 1 HETATM 4206 O O . HOH I 7 . ? -3.066 -5.325 -9.373 1.00 44.71 ? 554 HOH A O 1 HETATM 4207 O O . HOH I 7 . ? -2.410 0.805 -0.638 1.00 60.16 ? 555 HOH A O 1 HETATM 4208 O O . HOH I 7 . ? -28.833 21.557 -6.299 1.00 46.98 ? 556 HOH A O 1 HETATM 4209 O O . HOH I 7 . ? -20.248 22.164 -33.252 1.00 55.39 ? 557 HOH A O 1 HETATM 4210 O O . HOH I 7 . ? -23.392 24.844 -12.915 1.00 54.49 ? 558 HOH A O 1 HETATM 4211 O O . HOH I 7 . ? -31.099 4.346 -22.465 1.00 39.07 ? 559 HOH A O 1 HETATM 4212 O O . HOH I 7 . ? -33.853 5.191 -22.692 1.00 34.03 ? 560 HOH A O 1 HETATM 4213 O O . HOH I 7 . ? -43.789 -17.678 13.369 1.00 56.84 ? 561 HOH A O 1 HETATM 4214 O O . HOH I 7 . ? -48.411 2.782 6.340 1.00 45.35 ? 562 HOH A O 1 HETATM 4215 O O . HOH I 7 . ? -35.223 8.861 9.306 1.00 46.25 ? 563 HOH A O 1 HETATM 4216 O O . HOH I 7 . ? -23.606 10.567 9.270 1.00 53.43 ? 564 HOH A O 1 HETATM 4217 O O . HOH I 7 . ? -25.151 7.157 12.112 1.00 49.86 ? 565 HOH A O 1 HETATM 4218 O O . HOH I 7 . ? -19.337 4.810 17.635 1.00 44.33 ? 566 HOH A O 1 HETATM 4219 O O . HOH I 7 . ? -46.952 -23.399 -7.005 1.00 53.24 ? 567 HOH A O 1 HETATM 4220 O O . HOH I 7 . ? -15.920 7.402 9.370 1.00 50.86 ? 568 HOH A O 1 HETATM 4221 O O . HOH I 7 . ? -22.541 -6.663 19.294 1.00 51.53 ? 569 HOH A O 1 HETATM 4222 O O . HOH I 7 . ? -16.098 -6.031 18.199 1.00 56.60 ? 570 HOH A O 1 HETATM 4223 O O . HOH I 7 . ? -12.898 -3.789 15.398 1.00 48.34 ? 571 HOH A O 1 HETATM 4224 O O . HOH I 7 . ? -12.992 -1.839 17.487 1.00 63.50 ? 572 HOH A O 1 HETATM 4225 O O . HOH I 7 . ? -26.116 -1.125 22.601 1.00 56.61 ? 573 HOH A O 1 HETATM 4226 O O . HOH I 7 . ? -32.720 -7.967 19.897 1.00 56.23 ? 574 HOH A O 1 HETATM 4227 O O . HOH I 7 . ? -31.835 -15.938 14.913 1.00 48.04 ? 575 HOH A O 1 HETATM 4228 O O . HOH I 7 . ? -13.137 -20.532 -37.947 1.00 39.50 ? 576 HOH A O 1 HETATM 4229 O O . HOH I 7 . ? -19.887 -14.599 -20.521 1.00 54.26 ? 577 HOH A O 1 HETATM 4230 O O . HOH I 7 . ? -13.889 -23.202 -37.063 1.00 44.86 ? 578 HOH A O 1 HETATM 4231 O O . HOH I 7 . ? -27.176 -12.302 -17.652 1.00 52.32 ? 579 HOH A O 1 HETATM 4232 O O . HOH I 7 . ? -50.552 -15.777 -7.161 1.00 49.90 ? 580 HOH A O 1 HETATM 4233 O O . HOH I 7 . ? -36.302 22.334 -13.530 1.00 50.29 ? 581 HOH A O 1 HETATM 4234 O O . HOH I 7 . ? -30.235 22.059 -8.524 1.00 51.45 ? 582 HOH A O 1 HETATM 4235 O O . HOH I 7 . ? -28.374 -24.825 -19.733 1.00 37.60 ? 583 HOH A O 1 HETATM 4236 O O . HOH I 7 . ? -43.690 -25.099 -18.110 1.00 48.29 ? 584 HOH A O 1 HETATM 4237 O O . HOH I 7 . ? -49.248 10.850 -16.252 1.00 54.44 ? 585 HOH A O 1 HETATM 4238 O O . HOH I 7 . ? -40.783 -3.386 -27.777 1.00 50.09 ? 586 HOH A O 1 HETATM 4239 O O . HOH I 7 . ? -38.574 -3.674 -29.605 1.00 62.85 ? 587 HOH A O 1 HETATM 4240 O O . HOH I 7 . ? -48.510 7.983 -36.930 1.00 56.27 ? 588 HOH A O 1 HETATM 4241 O O . HOH I 7 . ? -47.154 11.184 -22.306 1.00 55.13 ? 589 HOH A O 1 HETATM 4242 O O . HOH I 7 . ? -36.596 23.379 -18.245 1.00 46.82 ? 590 HOH A O 1 HETATM 4243 O O . HOH I 7 . ? -33.598 23.961 -28.023 1.00 50.71 ? 591 HOH A O 1 HETATM 4244 O O . HOH I 7 . ? -29.971 25.560 -29.173 1.00 51.11 ? 592 HOH A O 1 HETATM 4245 O O . HOH I 7 . ? -32.186 26.068 -30.896 1.00 57.67 ? 593 HOH A O 1 HETATM 4246 O O . HOH I 7 . ? -22.276 25.306 -25.886 1.00 57.19 ? 594 HOH A O 1 HETATM 4247 O O . HOH I 7 . ? -31.407 13.016 -38.050 1.00 50.81 ? 595 HOH A O 1 HETATM 4248 O O . HOH I 7 . ? -46.334 6.243 -32.395 1.00 48.88 ? 596 HOH A O 1 HETATM 4249 O O . HOH I 7 . ? -33.226 -6.838 -30.477 1.00 49.62 ? 597 HOH A O 1 HETATM 4250 O O . HOH I 7 . ? -35.477 -5.127 -31.582 1.00 55.23 ? 598 HOH A O 1 HETATM 4251 O O . HOH I 7 . ? -11.692 23.605 -14.510 1.00 51.78 ? 599 HOH A O 1 HETATM 4252 O O . HOH I 7 . ? -9.607 21.678 -16.316 1.00 56.06 ? 600 HOH A O 1 HETATM 4253 O O . HOH I 7 . ? -33.422 -4.583 -40.058 1.00 49.35 ? 601 HOH A O 1 HETATM 4254 O O . HOH I 7 . ? -20.955 5.759 11.253 1.00 46.08 ? 602 HOH A O 1 HETATM 4255 O O . HOH I 7 . ? -22.024 8.282 13.293 1.00 48.90 ? 603 HOH A O 1 HETATM 4256 O O . HOH I 7 . ? -37.544 -24.831 -10.558 1.00 53.53 ? 604 HOH A O 1 HETATM 4257 O O . HOH I 7 . ? -38.947 -26.039 -8.543 1.00 56.91 ? 605 HOH A O 1 HETATM 4258 O O . HOH I 7 . ? -39.699 -22.397 5.909 1.00 57.53 ? 606 HOH A O 1 HETATM 4259 O O . HOH I 7 . ? -47.799 -9.776 11.016 1.00 47.27 ? 607 HOH A O 1 HETATM 4260 O O . HOH I 7 . ? -49.767 -5.831 8.944 1.00 50.90 ? 608 HOH A O 1 HETATM 4261 O O . HOH I 7 . ? -33.086 -18.818 -13.036 1.00 46.58 ? 609 HOH A O 1 HETATM 4262 O O . HOH I 7 . ? -45.655 7.505 -26.868 1.00 35.69 ? 610 HOH A O 1 HETATM 4263 O O . HOH I 7 . ? -33.699 -16.689 -24.720 1.00 32.24 ? 611 HOH A O 1 HETATM 4264 O O . HOH I 7 . ? -46.790 6.719 -42.391 1.00 37.48 ? 612 HOH A O 1 HETATM 4265 O O . HOH I 7 . ? -51.178 -25.837 4.420 1.00 35.57 ? 613 HOH A O 1 HETATM 4266 O O . HOH I 7 . ? -23.546 0.762 19.957 1.00 35.42 ? 614 HOH A O 1 HETATM 4267 O O . HOH I 7 . ? -42.543 -24.432 -10.348 1.00 45.02 ? 615 HOH A O 1 HETATM 4268 O O . HOH I 7 . ? -31.116 15.290 -9.292 1.00 17.18 ? 616 HOH A O 1 HETATM 4269 O O . HOH I 7 . ? -33.859 7.963 -14.903 1.00 16.71 ? 617 HOH A O 1 HETATM 4270 O O . HOH I 7 . ? -23.337 2.986 -4.030 1.00 18.83 ? 618 HOH A O 1 HETATM 4271 O O . HOH I 7 . ? -29.993 -1.217 -18.914 1.00 18.72 ? 619 HOH A O 1 HETATM 4272 O O . HOH I 7 . ? -31.664 1.164 3.719 1.00 20.54 ? 620 HOH A O 1 HETATM 4273 O O . HOH I 7 . ? -35.315 9.717 -1.298 1.00 22.86 ? 621 HOH A O 1 HETATM 4274 O O . HOH I 7 . ? -32.166 0.075 1.153 1.00 20.31 ? 622 HOH A O 1 HETATM 4275 O O . HOH I 7 . ? -28.646 11.750 -12.386 1.00 19.95 ? 623 HOH A O 1 HETATM 4276 O O . HOH I 7 . ? -27.772 2.850 -27.618 1.00 19.36 ? 624 HOH A O 1 HETATM 4277 O O . HOH I 7 . ? -23.662 9.552 -22.069 1.00 23.52 ? 625 HOH A O 1 HETATM 4278 O O . HOH I 7 . ? -15.624 -10.723 10.261 1.00 21.92 ? 626 HOH A O 1 HETATM 4279 O O . HOH I 7 . ? -25.289 16.490 -34.420 1.00 24.18 ? 627 HOH A O 1 HETATM 4280 O O . HOH I 7 . ? -35.065 16.162 -3.149 1.00 23.47 ? 628 HOH A O 1 HETATM 4281 O O . HOH I 7 . ? -5.388 10.669 -0.418 1.00 24.91 ? 629 HOH A O 1 HETATM 4282 O O . HOH I 7 . ? -32.162 9.206 -22.720 1.00 21.39 ? 630 HOH A O 1 HETATM 4283 O O . HOH I 7 . ? -50.432 -3.070 5.461 1.00 25.85 ? 631 HOH A O 1 HETATM 4284 O O . HOH I 7 . ? -19.136 -6.286 -18.953 1.00 25.06 ? 632 HOH A O 1 HETATM 4285 O O . HOH I 7 . ? -46.503 13.962 -37.436 1.00 21.82 ? 633 HOH A O 1 HETATM 4286 O O . HOH I 7 . ? -46.546 4.400 -4.182 1.00 22.70 ? 634 HOH A O 1 HETATM 4287 O O . HOH I 7 . ? -22.117 -2.972 -3.341 1.00 22.57 ? 635 HOH A O 1 HETATM 4288 O O . HOH I 7 . ? -22.133 15.490 -10.262 1.00 21.66 ? 636 HOH A O 1 HETATM 4289 O O . HOH I 7 . ? -32.312 11.145 -29.980 1.00 22.37 ? 637 HOH A O 1 HETATM 4290 O O . HOH I 7 . ? -10.586 9.473 3.208 1.00 24.20 ? 638 HOH A O 1 HETATM 4291 O O . HOH I 7 . ? -41.924 4.656 -33.861 1.00 25.37 ? 639 HOH A O 1 HETATM 4292 O O . HOH I 7 . ? -48.837 2.595 -11.313 1.00 22.27 ? 640 HOH A O 1 HETATM 4293 O O . HOH I 7 . ? -49.012 1.635 -1.902 1.00 23.14 ? 641 HOH A O 1 HETATM 4294 O O . HOH I 7 . ? -23.960 23.190 -22.215 1.00 23.51 ? 642 HOH A O 1 HETATM 4295 O O . HOH I 7 . ? -23.438 -0.992 -4.657 1.00 19.61 ? 643 HOH A O 1 HETATM 4296 O O . HOH I 7 . ? -42.440 2.502 1.837 1.00 22.86 ? 644 HOH A O 1 HETATM 4297 O O . HOH I 7 . ? -44.082 16.559 -30.640 1.00 23.61 ? 645 HOH A O 1 HETATM 4298 O O . HOH I 7 . ? -29.783 2.859 -24.215 1.00 21.84 ? 646 HOH A O 1 HETATM 4299 O O . HOH I 7 . ? -12.021 0.642 3.683 1.00 21.50 ? 647 HOH A O 1 HETATM 4300 O O . HOH I 7 . ? -48.035 8.350 -7.050 1.00 27.84 ? 648 HOH A O 1 HETATM 4301 O O . HOH I 7 . ? -10.807 15.158 -0.590 1.00 24.99 ? 649 HOH A O 1 HETATM 4302 O O . HOH I 7 . ? -34.136 -2.098 -6.165 1.00 22.50 ? 650 HOH A O 1 HETATM 4303 O O . HOH I 7 . ? -36.717 18.294 -11.549 1.00 27.70 ? 651 HOH A O 1 HETATM 4304 O O . HOH I 7 . ? -10.635 1.878 0.520 1.00 24.98 ? 652 HOH A O 1 HETATM 4305 O O . HOH I 7 . ? -28.756 19.297 -4.597 1.00 24.91 ? 653 HOH A O 1 HETATM 4306 O O . HOH I 7 . ? -31.884 -8.572 13.835 1.00 27.63 ? 654 HOH A O 1 HETATM 4307 O O . HOH I 7 . ? -6.334 11.330 -12.160 1.00 24.82 ? 655 HOH A O 1 HETATM 4308 O O . HOH I 7 . ? -23.939 21.391 -15.046 1.00 24.20 ? 656 HOH A O 1 HETATM 4309 O O . HOH I 7 . ? -25.221 7.291 -36.011 1.00 23.47 ? 657 HOH A O 1 HETATM 4310 O O . HOH I 7 . ? -30.758 1.403 -0.760 1.00 19.64 ? 658 HOH A O 1 HETATM 4311 O O . HOH I 7 . ? -36.219 20.749 -17.393 1.00 26.81 ? 659 HOH A O 1 HETATM 4312 O O . HOH I 7 . ? -50.784 -9.545 4.137 1.00 25.05 ? 660 HOH A O 1 HETATM 4313 O O . HOH I 7 . ? -39.632 -1.160 -16.082 1.00 27.80 ? 661 HOH A O 1 HETATM 4314 O O . HOH I 7 . ? -29.206 0.610 -22.812 1.00 20.62 ? 662 HOH A O 1 HETATM 4315 O O . HOH I 7 . ? -10.826 -6.759 -16.328 1.00 26.98 ? 663 HOH A O 1 HETATM 4316 O O . HOH I 7 . ? -49.034 -3.034 -15.943 1.00 26.92 ? 664 HOH A O 1 HETATM 4317 O O . HOH I 7 . ? -4.766 -1.123 -9.136 1.00 27.75 ? 665 HOH A O 1 HETATM 4318 O O . HOH I 7 . ? -14.221 20.455 -12.662 1.00 28.36 ? 666 HOH A O 1 HETATM 4319 O O . HOH I 7 . ? -25.735 -8.050 -32.349 1.00 25.54 ? 667 HOH A O 1 HETATM 4320 O O . HOH I 7 . ? -4.807 1.538 -8.083 1.00 24.93 ? 668 HOH A O 1 HETATM 4321 O O . HOH I 7 . ? -40.168 11.302 -8.510 1.00 26.47 ? 669 HOH A O 1 HETATM 4322 O O . HOH I 7 . ? -28.114 2.758 -0.851 1.00 22.01 ? 670 HOH A O 1 HETATM 4323 O O . HOH I 7 . ? -8.509 17.408 -14.405 1.00 32.97 ? 671 HOH A O 1 HETATM 4324 O O . HOH I 7 . ? -34.693 20.571 -14.840 1.00 26.72 ? 672 HOH A O 1 HETATM 4325 O O . HOH I 7 . ? -32.184 -6.794 -33.081 1.00 29.89 ? 673 HOH A O 1 HETATM 4326 O O . HOH I 7 . ? -45.049 -20.225 2.480 1.00 29.85 ? 674 HOH A O 1 HETATM 4327 O O . HOH I 7 . ? -13.449 -12.052 -38.059 1.00 31.33 ? 675 HOH A O 1 HETATM 4328 O O . HOH I 7 . ? -8.003 13.263 -11.226 1.00 25.36 ? 676 HOH A O 1 HETATM 4329 O O . HOH I 7 . ? -6.162 1.104 -14.916 1.00 27.41 ? 677 HOH A O 1 HETATM 4330 O O . HOH I 7 . ? -41.750 -18.662 8.613 1.00 28.52 ? 678 HOH A O 1 HETATM 4331 O O . HOH I 7 . ? -45.682 9.702 -10.434 1.00 30.82 ? 679 HOH A O 1 HETATM 4332 O O . HOH I 7 . ? -38.051 14.358 -5.633 1.00 23.58 ? 680 HOH A O 1 HETATM 4333 O O . HOH I 7 . ? -35.555 -6.234 -19.461 1.00 28.39 ? 681 HOH A O 1 HETATM 4334 O O . HOH I 7 . ? -50.968 -16.798 5.283 1.00 27.47 ? 682 HOH A O 1 HETATM 4335 O O . HOH I 7 . ? -37.328 8.933 -27.391 1.00 27.72 ? 683 HOH A O 1 HETATM 4336 O O . HOH I 7 . ? -27.476 5.083 -29.245 1.00 25.46 ? 684 HOH A O 1 HETATM 4337 O O . HOH I 7 . ? -11.092 4.551 9.805 1.00 26.03 ? 685 HOH A O 1 HETATM 4338 O O . HOH I 7 . ? -53.503 -5.447 -8.039 1.00 26.00 ? 686 HOH A O 1 HETATM 4339 O O . HOH I 7 . ? -21.345 12.886 -2.090 1.00 27.86 ? 687 HOH A O 1 HETATM 4340 O O . HOH I 7 . ? -30.559 4.619 11.841 1.00 29.29 ? 688 HOH A O 1 HETATM 4341 O O . HOH I 7 . ? -39.362 13.965 -8.115 1.00 29.13 ? 689 HOH A O 1 HETATM 4342 O O . HOH I 7 . ? -24.234 -14.732 8.081 1.00 28.63 ? 690 HOH A O 1 HETATM 4343 O O . HOH I 7 . ? -14.400 -9.765 -0.171 1.00 24.23 ? 691 HOH A O 1 HETATM 4344 O O . HOH I 7 . ? -13.590 -10.235 -40.017 1.00 29.90 ? 692 HOH A O 1 HETATM 4345 O O . HOH I 7 . ? -30.251 -18.368 -21.209 1.00 34.01 ? 693 HOH A O 1 HETATM 4346 O O . HOH I 7 . ? -48.043 -16.019 -10.833 1.00 26.96 ? 694 HOH A O 1 HETATM 4347 O O . HOH I 7 . ? -39.586 -22.118 -13.368 1.00 31.26 ? 695 HOH A O 1 HETATM 4348 O O . HOH I 7 . ? -21.877 -8.005 -12.816 1.00 24.64 ? 696 HOH A O 1 HETATM 4349 O O . HOH I 7 . ? -41.814 1.485 -14.211 1.00 25.49 ? 697 HOH A O 1 HETATM 4350 O O . HOH I 7 . ? -11.354 11.806 1.918 1.00 33.15 ? 698 HOH A O 1 HETATM 4351 O O . HOH I 7 . ? -41.282 -7.865 10.782 1.00 26.38 ? 699 HOH A O 1 HETATM 4352 O O . HOH I 7 . ? -11.881 -14.315 -38.188 1.00 30.45 ? 700 HOH A O 1 HETATM 4353 O O . HOH I 7 . ? -11.091 9.791 5.787 1.00 30.72 ? 701 HOH A O 1 HETATM 4354 O O . HOH I 7 . ? -20.575 3.915 13.550 1.00 30.76 ? 702 HOH A O 1 HETATM 4355 O O . HOH I 7 . ? -7.244 -14.561 -36.417 1.00 29.71 ? 703 HOH A O 1 HETATM 4356 O O . HOH I 7 . ? -41.733 16.920 -32.111 1.00 27.13 ? 704 HOH A O 1 HETATM 4357 O O . HOH I 7 . ? -55.061 -4.340 -6.024 1.00 32.43 ? 705 HOH A O 1 HETATM 4358 O O . HOH I 7 . ? -25.379 -3.892 -39.341 1.00 27.03 ? 706 HOH A O 1 HETATM 4359 O O . HOH I 7 . ? -20.856 -4.650 -5.128 1.00 26.15 ? 707 HOH A O 1 HETATM 4360 O O . HOH I 7 . ? -25.319 10.528 -20.335 1.00 23.34 ? 708 HOH A O 1 HETATM 4361 O O . HOH I 7 . ? -41.855 2.721 -38.346 1.00 33.91 ? 709 HOH A O 1 HETATM 4362 O O . HOH I 7 . ? -3.775 5.270 -10.739 1.00 28.57 ? 710 HOH A O 1 HETATM 4363 O O . HOH I 7 . ? -29.970 -1.664 20.416 1.00 29.09 ? 711 HOH A O 1 HETATM 4364 O O . HOH I 7 . ? -42.721 -9.238 -19.781 1.00 34.68 ? 712 HOH A O 1 HETATM 4365 O O . HOH I 7 . ? -32.181 -20.864 -14.258 1.00 37.15 ? 713 HOH A O 1 HETATM 4366 O O . HOH I 7 . ? -40.755 4.714 -42.079 1.00 31.89 ? 714 HOH A O 1 HETATM 4367 O O . HOH I 7 . ? -39.081 16.709 -11.752 1.00 34.47 ? 715 HOH A O 1 HETATM 4368 O O . HOH I 7 . ? -53.696 -4.295 -10.748 1.00 36.68 ? 716 HOH A O 1 HETATM 4369 O O . HOH I 7 . ? -47.949 -5.337 -17.251 1.00 25.96 ? 717 HOH A O 1 HETATM 4370 O O . HOH I 7 . ? -21.939 18.789 -31.651 1.00 33.44 ? 718 HOH A O 1 HETATM 4371 O O . HOH I 7 . ? -30.408 6.716 -23.091 1.00 29.86 ? 719 HOH A O 1 HETATM 4372 O O . HOH I 7 . ? -39.597 -12.528 11.812 1.00 31.66 ? 720 HOH A O 1 HETATM 4373 O O . HOH I 7 . ? -18.193 11.130 4.779 1.00 32.65 ? 721 HOH A O 1 HETATM 4374 O O . HOH I 7 . ? -6.505 -0.615 0.637 1.00 30.55 ? 722 HOH A O 1 HETATM 4375 O O . HOH I 7 . ? -13.994 -14.514 -41.945 1.00 33.07 ? 723 HOH A O 1 HETATM 4376 O O . HOH I 7 . ? -50.378 3.521 -13.270 1.00 27.75 ? 724 HOH A O 1 HETATM 4377 O O . HOH I 7 . ? -18.629 -14.653 11.447 1.00 30.26 ? 725 HOH A O 1 HETATM 4378 O O . HOH I 7 . ? -25.748 8.495 9.733 1.00 34.09 ? 726 HOH A O 1 HETATM 4379 O O . HOH I 7 . ? -43.587 10.110 -0.357 1.00 36.30 ? 727 HOH A O 1 HETATM 4380 O O . HOH I 7 . ? -7.368 -0.650 -29.478 1.00 36.56 ? 728 HOH A O 1 HETATM 4381 O O . HOH I 7 . ? -16.726 -14.264 -27.108 1.00 29.27 ? 729 HOH A O 1 HETATM 4382 O O . HOH I 7 . ? -47.806 -8.368 7.334 1.00 32.46 ? 730 HOH A O 1 HETATM 4383 O O . HOH I 7 . ? -27.786 2.697 -41.114 1.00 36.41 ? 731 HOH A O 1 HETATM 4384 O O . HOH I 7 . ? -41.722 -10.628 11.068 1.00 25.88 ? 732 HOH A O 1 HETATM 4385 O O . HOH I 7 . ? -15.928 -8.970 -11.936 1.00 28.80 ? 733 HOH A O 1 HETATM 4386 O O . HOH I 7 . ? -25.844 -12.966 18.917 1.00 32.97 ? 734 HOH A O 1 HETATM 4387 O O . HOH I 7 . ? -31.683 4.052 -33.497 1.00 28.96 ? 735 HOH A O 1 HETATM 4388 O O . HOH I 7 . ? -6.072 -1.317 -11.522 1.00 28.30 ? 736 HOH A O 1 HETATM 4389 O O . HOH I 7 . ? -38.172 -2.571 16.343 1.00 28.06 ? 737 HOH A O 1 HETATM 4390 O O . HOH I 7 . ? -43.597 -20.688 -22.921 1.00 30.02 ? 738 HOH A O 1 HETATM 4391 O O . HOH I 7 . ? -40.856 3.536 3.713 1.00 30.93 ? 739 HOH A O 1 HETATM 4392 O O . HOH I 7 . ? -6.753 7.952 -34.477 1.00 34.37 ? 740 HOH A O 1 HETATM 4393 O O . HOH I 7 . ? -12.007 7.393 6.626 1.00 30.26 ? 741 HOH A O 1 HETATM 4394 O O . HOH I 7 . ? -44.450 -17.931 8.637 1.00 33.23 ? 742 HOH A O 1 HETATM 4395 O O . HOH I 7 . ? -19.218 14.076 -0.201 1.00 39.08 ? 743 HOH A O 1 HETATM 4396 O O . HOH I 7 . ? -29.238 10.593 8.110 1.00 34.68 ? 744 HOH A O 1 HETATM 4397 O O . HOH I 7 . ? -9.872 -14.491 -7.382 1.00 28.40 ? 745 HOH A O 1 HETATM 4398 O O . HOH I 7 . ? -24.113 -4.191 19.740 1.00 37.19 ? 746 HOH A O 1 HETATM 4399 O O . HOH I 7 . ? -40.836 5.386 6.266 1.00 34.68 ? 747 HOH A O 1 HETATM 4400 O O . HOH I 7 . ? -31.601 2.354 -35.720 1.00 30.40 ? 748 HOH A O 1 HETATM 4401 O O . HOH I 7 . ? -51.740 -9.445 -12.820 1.00 27.28 ? 749 HOH A O 1 HETATM 4402 O O . HOH I 7 . ? -18.362 15.818 -6.278 1.00 29.01 ? 750 HOH A O 1 HETATM 4403 O O . HOH I 7 . ? -36.903 -2.195 -16.797 1.00 30.84 ? 751 HOH A O 1 HETATM 4404 O O . HOH I 7 . ? -26.617 20.832 -11.018 1.00 31.29 ? 752 HOH A O 1 HETATM 4405 O O . HOH I 7 . ? -27.292 -16.874 5.028 1.00 35.88 ? 753 HOH A O 1 HETATM 4406 O O . HOH I 7 . ? -36.272 -3.671 -19.421 1.00 31.18 ? 754 HOH A O 1 HETATM 4407 O O . HOH I 7 . ? -38.503 11.543 1.223 1.00 30.91 ? 755 HOH A O 1 HETATM 4408 O O . HOH I 7 . ? -48.632 -18.869 9.554 1.00 32.16 ? 756 HOH A O 1 HETATM 4409 O O . HOH I 7 . ? -5.285 2.951 -10.586 1.00 35.75 ? 757 HOH A O 1 HETATM 4410 O O . HOH I 7 . ? -18.385 -10.556 -17.677 1.00 31.34 ? 758 HOH A O 1 HETATM 4411 O O . HOH I 7 . ? -21.327 -10.737 -16.109 1.00 33.60 ? 759 HOH A O 1 HETATM 4412 O O . HOH I 7 . ? -45.053 -13.562 -23.017 1.00 28.91 ? 760 HOH A O 1 HETATM 4413 O O . HOH I 7 . ? -16.100 -12.012 -0.707 1.00 32.98 ? 761 HOH A O 1 HETATM 4414 O O . HOH I 7 . ? -22.216 26.937 -19.425 1.00 31.40 ? 762 HOH A O 1 HETATM 4415 O O . HOH I 7 . ? -34.961 8.885 -22.703 1.00 31.37 ? 763 HOH A O 1 HETATM 4416 O O . HOH I 7 . ? -18.532 19.952 -33.026 1.00 33.27 ? 764 HOH A O 1 HETATM 4417 O O . HOH I 7 . ? -42.957 -26.239 -0.705 1.00 42.02 ? 765 HOH A O 1 HETATM 4418 O O . HOH I 7 . ? -50.146 -12.403 -11.397 1.00 33.38 ? 766 HOH A O 1 HETATM 4419 O O . HOH I 7 . ? -47.805 -11.250 7.525 1.00 29.46 ? 767 HOH A O 1 HETATM 4420 O O . HOH I 7 . ? -6.209 7.660 1.651 1.00 33.75 ? 768 HOH A O 1 HETATM 4421 O O . HOH I 7 . ? -42.604 -21.921 -14.602 1.00 33.05 ? 769 HOH A O 1 HETATM 4422 O O . HOH I 7 . ? -11.623 -7.468 -40.664 1.00 32.59 ? 770 HOH A O 1 HETATM 4423 O O . HOH I 7 . ? -29.268 -7.682 14.738 1.00 30.92 ? 771 HOH A O 1 HETATM 4424 O O . HOH I 7 . ? -46.428 -17.469 -16.503 1.00 39.22 ? 772 HOH A O 1 HETATM 4425 O O . HOH I 7 . ? -44.749 -6.033 9.465 1.00 33.41 ? 773 HOH A O 1 HETATM 4426 O O . HOH I 7 . ? -48.170 10.691 -33.556 1.00 31.99 ? 774 HOH A O 1 HETATM 4427 O O . HOH I 7 . ? -10.368 15.716 -32.573 1.00 31.94 ? 775 HOH A O 1 HETATM 4428 O O . HOH I 7 . ? -33.805 -18.575 8.293 1.00 32.97 ? 776 HOH A O 1 HETATM 4429 O O . HOH I 7 . ? -18.918 14.490 -4.043 1.00 29.77 ? 777 HOH A O 1 HETATM 4430 O O . HOH I 7 . ? -53.042 3.547 -12.288 1.00 36.02 ? 778 HOH A O 1 HETATM 4431 O O . HOH I 7 . ? -24.219 13.495 -3.027 1.00 32.49 ? 779 HOH A O 1 HETATM 4432 O O . HOH I 7 . ? -45.295 17.540 -26.365 1.00 36.56 ? 780 HOH A O 1 HETATM 4433 O O . HOH I 7 . ? -32.104 -2.380 -31.157 1.00 33.66 ? 781 HOH A O 1 HETATM 4434 O O . HOH I 7 . ? -52.602 -9.537 -2.531 1.00 27.84 ? 782 HOH A O 1 HETATM 4435 O O . HOH I 7 . ? -36.072 19.007 -5.368 1.00 38.10 ? 783 HOH A O 1 HETATM 4436 O O . HOH I 7 . ? -26.056 -9.842 -16.822 1.00 31.83 ? 784 HOH A O 1 HETATM 4437 O O . HOH I 7 . ? -7.989 9.716 2.457 1.00 28.69 ? 785 HOH A O 1 HETATM 4438 O O . HOH I 7 . ? -19.574 10.960 7.324 1.00 37.13 ? 786 HOH A O 1 HETATM 4439 O O . HOH I 7 . ? -1.716 9.988 -6.671 1.00 32.93 ? 787 HOH A O 1 HETATM 4440 O O . HOH I 7 . ? -46.859 8.882 1.749 1.00 42.64 ? 788 HOH A O 1 HETATM 4441 O O . HOH I 7 . ? -44.092 -22.787 -21.126 1.00 33.25 ? 789 HOH A O 1 HETATM 4442 O O . HOH I 7 . ? -4.439 4.303 2.511 1.00 38.80 ? 790 HOH A O 1 HETATM 4443 O O . HOH I 7 . ? -36.790 -1.701 -30.652 1.00 36.00 ? 791 HOH A O 1 HETATM 4444 O O . HOH I 7 . ? -29.055 -15.170 11.776 1.00 32.50 ? 792 HOH A O 1 HETATM 4445 O O . HOH I 7 . ? -15.013 8.105 6.894 1.00 37.59 ? 793 HOH A O 1 HETATM 4446 O O . HOH I 7 . ? -29.411 -21.374 -14.179 1.00 38.52 ? 794 HOH A O 1 HETATM 4447 O O . HOH I 7 . ? -46.955 -18.965 6.274 1.00 32.86 ? 795 HOH A O 1 HETATM 4448 O O . HOH I 7 . ? -23.343 17.004 -36.751 1.00 41.56 ? 796 HOH A O 1 HETATM 4449 O O . HOH I 7 . ? -26.167 -10.419 -31.016 1.00 28.73 ? 797 HOH A O 1 HETATM 4450 O O . HOH I 7 . ? -36.503 -25.531 -22.767 1.00 48.61 ? 798 HOH A O 1 HETATM 4451 O O . HOH I 7 . ? -50.163 6.082 -14.233 1.00 31.93 ? 799 HOH A O 1 HETATM 4452 O O . HOH I 7 . ? -47.502 -13.218 -12.039 1.00 29.09 ? 800 HOH A O 1 HETATM 4453 O O . HOH I 7 . ? -10.067 25.497 -19.167 1.00 39.70 ? 801 HOH A O 1 HETATM 4454 O O . HOH I 7 . ? -39.346 18.407 -7.970 1.00 42.68 ? 802 HOH A O 1 HETATM 4455 O O . HOH I 7 . ? -47.107 -7.342 9.544 1.00 39.44 ? 803 HOH A O 1 HETATM 4456 O O . HOH I 7 . ? -11.089 22.642 -18.548 1.00 28.75 ? 804 HOH A O 1 HETATM 4457 O O . HOH I 7 . ? -14.788 1.873 11.162 1.00 32.58 ? 805 HOH A O 1 HETATM 4458 O O . HOH I 7 . ? -5.115 1.203 -12.519 1.00 31.27 ? 806 HOH A O 1 HETATM 4459 O O . HOH I 7 . ? -11.350 19.055 -13.745 1.00 32.89 ? 807 HOH A O 1 HETATM 4460 O O . HOH I 7 . ? -23.598 8.581 -38.013 1.00 31.38 ? 808 HOH A O 1 HETATM 4461 O O . HOH I 7 . ? -12.872 -16.235 -39.845 1.00 30.60 ? 809 HOH A O 1 HETATM 4462 O O . HOH I 7 . ? -53.839 -17.138 1.859 1.00 27.94 ? 810 HOH A O 1 HETATM 4463 O O . HOH I 7 . ? -1.333 3.889 -2.922 1.00 33.85 ? 811 HOH A O 1 HETATM 4464 O O . HOH I 7 . ? -3.240 5.765 0.146 1.00 32.67 ? 812 HOH A O 1 HETATM 4465 O O . HOH I 7 . ? -40.768 10.709 -5.968 1.00 34.90 ? 813 HOH A O 1 HETATM 4466 O O . HOH I 7 . ? -43.159 -23.187 -7.909 1.00 33.84 ? 814 HOH A O 1 HETATM 4467 O O . HOH I 7 . ? -42.887 12.164 -8.593 1.00 34.59 ? 815 HOH A O 1 HETATM 4468 O O . HOH I 7 . ? -8.857 -4.711 1.319 1.00 30.32 ? 816 HOH A O 1 HETATM 4469 O O . HOH I 7 . ? -54.175 1.302 -10.543 1.00 37.93 ? 817 HOH A O 1 HETATM 4470 O O . HOH I 7 . ? -25.575 4.264 2.959 1.00 33.78 ? 818 HOH A O 1 HETATM 4471 O O . HOH I 7 . ? -15.811 -9.028 12.217 1.00 35.37 ? 819 HOH A O 1 HETATM 4472 O O . HOH I 7 . ? -34.608 -7.785 -21.443 1.00 30.05 ? 820 HOH A O 1 HETATM 4473 O O . HOH I 7 . ? -31.792 19.957 -34.445 1.00 39.35 ? 821 HOH A O 1 HETATM 4474 O O . HOH I 7 . ? -27.353 -21.257 -19.926 1.00 43.11 ? 822 HOH A O 1 HETATM 4475 O O . HOH I 7 . ? -37.249 16.893 -4.637 1.00 41.64 ? 823 HOH A O 1 HETATM 4476 O O . HOH I 7 . ? -36.440 5.529 -43.597 1.00 40.56 ? 824 HOH A O 1 HETATM 4477 O O . HOH I 7 . ? -37.352 21.742 -24.178 1.00 31.89 ? 825 HOH A O 1 HETATM 4478 O O . HOH I 7 . ? -41.091 9.931 2.157 1.00 39.90 ? 826 HOH A O 1 HETATM 4479 O O . HOH I 7 . ? -43.393 -22.717 -12.163 1.00 37.09 ? 827 HOH A O 1 HETATM 4480 O O . HOH I 7 . ? -43.511 -0.439 -19.154 1.00 41.57 ? 828 HOH A O 1 HETATM 4481 O O . HOH I 7 . ? -34.415 -5.382 20.422 1.00 36.47 ? 829 HOH A O 1 HETATM 4482 O O . HOH I 7 . ? -43.278 3.205 -35.851 1.00 40.44 ? 830 HOH A O 1 HETATM 4483 O O . HOH I 7 . ? -28.668 -1.191 -6.771 1.00 37.21 ? 831 HOH A O 1 HETATM 4484 O O . HOH I 7 . ? -26.666 -4.920 20.368 1.00 36.50 ? 832 HOH A O 1 HETATM 4485 O O . HOH I 7 . ? -45.699 -12.479 10.953 1.00 31.42 ? 833 HOH A O 1 HETATM 4486 O O . HOH I 7 . ? -26.967 23.375 -31.672 1.00 41.70 ? 834 HOH A O 1 HETATM 4487 O O . HOH I 7 . ? -44.716 9.276 -18.721 1.00 43.73 ? 835 HOH A O 1 HETATM 4488 O O . HOH I 7 . ? -18.495 -14.487 -1.187 1.00 33.81 ? 836 HOH A O 1 HETATM 4489 O O . HOH I 7 . ? -18.346 2.851 14.364 1.00 31.43 ? 837 HOH A O 1 HETATM 4490 O O . HOH I 7 . ? -26.386 22.294 -13.744 1.00 38.47 ? 838 HOH A O 1 HETATM 4491 O O . HOH I 7 . ? -19.240 24.239 -18.193 1.00 28.83 ? 839 HOH A O 1 HETATM 4492 O O . HOH I 7 . ? -29.048 4.094 13.982 1.00 44.67 ? 840 HOH A O 1 HETATM 4493 O O . HOH I 7 . ? -55.714 -5.781 -3.725 1.00 34.68 ? 841 HOH A O 1 HETATM 4494 O O . HOH I 7 . ? -15.598 -3.547 16.505 1.00 36.46 ? 842 HOH A O 1 HETATM 4495 O O . HOH I 7 . ? -27.850 7.429 -37.106 1.00 32.39 ? 843 HOH A O 1 HETATM 4496 O O . HOH I 7 . ? -43.921 4.517 -29.385 1.00 38.30 ? 844 HOH A O 1 HETATM 4497 O O . HOH I 7 . ? -36.242 15.132 -33.608 1.00 35.07 ? 845 HOH A O 1 HETATM 4498 O O . HOH I 7 . ? -8.028 -6.520 3.811 1.00 32.29 ? 846 HOH A O 1 HETATM 4499 O O . HOH I 7 . ? -40.720 -0.615 -28.177 1.00 34.30 ? 847 HOH A O 1 HETATM 4500 O O . HOH I 7 . ? -29.147 12.063 5.492 1.00 35.42 ? 848 HOH A O 1 HETATM 4501 O O . HOH I 7 . ? -0.328 14.711 0.423 1.00 47.43 ? 849 HOH A O 1 HETATM 4502 O O . HOH I 7 . ? -23.306 12.274 3.181 1.00 36.78 ? 850 HOH A O 1 HETATM 4503 O O . HOH I 7 . ? -31.873 0.183 -31.812 1.00 33.54 ? 851 HOH A O 1 HETATM 4504 O O . HOH I 7 . ? -32.279 21.707 -13.997 1.00 37.19 ? 852 HOH A O 1 HETATM 4505 O O . HOH I 7 . ? -16.718 23.833 -27.530 1.00 47.25 ? 853 HOH A O 1 HETATM 4506 O O . HOH I 7 . ? -5.662 -7.945 -11.285 1.00 37.32 ? 854 HOH A O 1 HETATM 4507 O O . HOH I 7 . ? -2.838 -2.827 -8.136 1.00 40.40 ? 855 HOH A O 1 HETATM 4508 O O . HOH I 7 . ? -44.773 -19.201 -14.791 1.00 32.88 ? 856 HOH A O 1 HETATM 4509 O O . HOH I 7 . ? -7.563 7.328 -17.101 1.00 31.42 ? 857 HOH A O 1 HETATM 4510 O O . HOH I 7 . ? -50.374 -14.120 6.577 1.00 29.04 ? 858 HOH A O 1 HETATM 4511 O O . HOH I 7 . ? -17.714 -3.900 -24.714 1.00 35.70 ? 859 HOH A O 1 HETATM 4512 O O . HOH I 7 . ? -52.891 -9.357 -15.332 1.00 38.37 ? 860 HOH A O 1 HETATM 4513 O O . HOH I 7 . ? -15.745 10.807 6.623 1.00 33.25 ? 861 HOH A O 1 HETATM 4514 O O . HOH I 7 . ? -48.359 -0.141 4.909 1.00 38.54 ? 862 HOH A O 1 HETATM 4515 O O . HOH I 7 . ? -14.745 13.583 -1.091 1.00 30.57 ? 863 HOH A O 1 HETATM 4516 O O . HOH I 7 . ? -21.937 22.552 -26.063 1.00 39.73 ? 864 HOH A O 1 HETATM 4517 O O . HOH I 7 . ? -21.044 16.236 -3.549 1.00 40.08 ? 865 HOH A O 1 HETATM 4518 O O . HOH I 7 . ? -6.077 5.470 -23.893 1.00 42.39 ? 866 HOH A O 1 HETATM 4519 O O . HOH I 7 . ? -23.566 15.316 -4.923 1.00 33.99 ? 867 HOH A O 1 HETATM 4520 O O . HOH I 7 . ? -37.453 9.096 1.202 1.00 31.41 ? 868 HOH A O 1 HETATM 4521 O O . HOH I 7 . ? -37.621 -24.162 -15.686 1.00 41.59 ? 869 HOH A O 1 HETATM 4522 O O . HOH I 7 . ? -8.117 -1.070 -14.940 1.00 32.26 ? 870 HOH A O 1 HETATM 4523 O O . HOH I 7 . ? -38.998 2.957 -41.008 1.00 38.40 ? 871 HOH A O 1 HETATM 4524 O O . HOH I 7 . ? -36.934 -2.373 19.527 1.00 48.26 ? 872 HOH A O 1 HETATM 4525 O O . HOH I 7 . ? -37.308 2.363 11.573 1.00 40.78 ? 873 HOH A O 1 HETATM 4526 O O . HOH I 7 . ? -5.166 -3.585 -13.072 1.00 37.13 ? 874 HOH A O 1 HETATM 4527 O O . HOH I 7 . ? -30.983 -15.949 10.032 1.00 44.23 ? 875 HOH A O 1 HETATM 4528 O O . HOH I 7 . ? -6.368 8.603 -24.662 1.00 31.61 ? 876 HOH A O 1 HETATM 4529 O O . HOH I 7 . ? -35.059 -16.857 -8.424 1.00 30.19 ? 877 HOH A O 1 HETATM 4530 O O . HOH I 7 . ? -51.371 -16.397 -17.927 1.00 44.03 ? 878 HOH A O 1 HETATM 4531 O O . HOH I 7 . ? -33.347 12.408 -36.313 1.00 31.92 ? 879 HOH A O 1 HETATM 4532 O O . HOH I 7 . ? -47.891 5.997 -16.607 1.00 36.49 ? 880 HOH A O 1 HETATM 4533 O O . HOH I 7 . ? -2.490 2.418 -7.052 1.00 44.49 ? 881 HOH A O 1 HETATM 4534 O O . HOH I 7 . ? -8.642 10.449 6.867 1.00 47.21 ? 882 HOH A O 1 HETATM 4535 O O . HOH I 7 . ? -51.158 -8.606 -17.200 1.00 37.41 ? 883 HOH A O 1 HETATM 4536 O O . HOH I 7 . ? -15.792 3.887 12.465 1.00 38.44 ? 884 HOH A O 1 HETATM 4537 O O . HOH I 7 . ? -30.286 26.191 -25.053 1.00 44.64 ? 885 HOH A O 1 HETATM 4538 O O . HOH I 7 . ? -30.724 24.135 -27.043 1.00 33.78 ? 886 HOH A O 1 HETATM 4539 O O . HOH I 7 . ? -36.701 -7.267 -23.235 1.00 37.06 ? 887 HOH A O 1 HETATM 4540 O O . HOH I 7 . ? -34.411 8.874 5.482 1.00 33.32 ? 888 HOH A O 1 HETATM 4541 O O . HOH I 7 . ? -45.425 -19.554 -0.170 1.00 34.19 ? 889 HOH A O 1 HETATM 4542 O O . HOH I 7 . ? -43.575 5.884 -32.035 1.00 38.05 ? 890 HOH A O 1 HETATM 4543 O O . HOH I 7 . ? -30.636 25.587 -18.581 1.00 40.10 ? 891 HOH A O 1 HETATM 4544 O O . HOH I 7 . ? -34.129 -4.654 -27.935 1.00 36.88 ? 892 HOH A O 1 HETATM 4545 O O . HOH I 7 . ? -36.146 -21.351 -5.058 1.00 46.32 ? 893 HOH A O 1 HETATM 4546 O O . HOH I 7 . ? -14.773 -16.365 -0.791 1.00 38.75 ? 894 HOH A O 1 HETATM 4547 O O . HOH I 7 . ? -20.688 16.640 -7.560 1.00 32.77 ? 895 HOH A O 1 HETATM 4548 O O . HOH I 7 . ? -25.547 -18.042 -14.130 1.00 39.95 ? 896 HOH A O 1 HETATM 4549 O O . HOH I 7 . ? -40.375 -24.475 -12.049 1.00 42.22 ? 897 HOH A O 1 HETATM 4550 O O . HOH I 7 . ? -50.080 2.955 1.731 1.00 36.36 ? 898 HOH A O 1 HETATM 4551 O O . HOH I 7 . ? -12.183 -10.652 -0.413 1.00 35.77 ? 899 HOH A O 1 HETATM 4552 O O . HOH I 7 . ? -21.484 5.936 15.413 1.00 43.31 ? 900 HOH A O 1 HETATM 4553 O O . HOH I 7 . ? -9.959 -9.942 1.239 1.00 30.50 ? 901 HOH A O 1 HETATM 4554 O O . HOH I 7 . ? -23.608 20.599 -10.991 1.00 33.13 ? 902 HOH A O 1 HETATM 4555 O O . HOH I 7 . ? -34.460 -11.515 -28.272 1.00 44.12 ? 903 HOH A O 1 HETATM 4556 O O . HOH I 7 . ? -33.130 5.620 -40.262 1.00 42.98 ? 904 HOH A O 1 HETATM 4557 O O . HOH I 7 . ? -9.113 -10.759 -11.408 1.00 46.77 ? 905 HOH A O 1 HETATM 4558 O O . HOH I 7 . ? -46.070 -19.940 -12.682 1.00 41.30 ? 906 HOH A O 1 HETATM 4559 O O . HOH I 7 . ? -41.637 17.314 -18.288 1.00 36.20 ? 907 HOH A O 1 HETATM 4560 O O . HOH I 7 . ? -14.034 22.196 -14.960 1.00 32.11 ? 908 HOH A O 1 HETATM 4561 O O . HOH I 7 . ? -34.494 10.900 -38.130 1.00 37.59 ? 909 HOH A O 1 HETATM 4562 O O . HOH I 7 . ? -31.914 8.958 6.785 1.00 35.19 ? 910 HOH A O 1 HETATM 4563 O O . HOH I 7 . ? -38.787 0.967 15.835 1.00 47.06 ? 911 HOH A O 1 HETATM 4564 O O . HOH I 7 . ? -19.710 -5.783 -43.319 1.00 40.64 ? 912 HOH A O 1 HETATM 4565 O O . HOH I 7 . ? -18.122 -11.095 -12.091 1.00 32.61 ? 913 HOH A O 1 HETATM 4566 O O . HOH I 7 . ? -43.254 -10.241 13.354 1.00 45.13 ? 914 HOH A O 1 HETATM 4567 O O . HOH I 7 . ? -29.293 21.891 -12.127 1.00 37.13 ? 915 HOH A O 1 HETATM 4568 O O . HOH I 7 . ? -37.286 -21.272 -1.978 1.00 39.54 ? 916 HOH A O 1 HETATM 4569 O O . HOH I 7 . ? -18.852 -16.233 -6.382 1.00 36.33 ? 917 HOH A O 1 HETATM 4570 O O . HOH I 7 . ? -6.279 10.367 4.499 1.00 35.54 ? 918 HOH A O 1 HETATM 4571 O O . HOH I 7 . ? -38.118 -0.073 13.500 1.00 41.48 ? 919 HOH A O 1 HETATM 4572 O O . HOH I 7 . ? -38.231 -18.317 11.056 1.00 45.40 ? 920 HOH A O 1 HETATM 4573 O O . HOH I 7 . ? -47.945 -16.495 -14.514 1.00 40.83 ? 921 HOH A O 1 HETATM 4574 O O . HOH I 7 . ? -7.853 9.299 -19.230 1.00 43.84 ? 922 HOH A O 1 HETATM 4575 O O . HOH I 7 . ? -29.717 -4.141 -38.587 1.00 43.30 ? 923 HOH A O 1 HETATM 4576 O O . HOH I 7 . ? -50.656 -15.752 -9.965 1.00 38.16 ? 924 HOH A O 1 HETATM 4577 O O . HOH I 7 . ? -16.825 -18.542 -1.057 1.00 38.24 ? 925 HOH A O 1 HETATM 4578 O O . HOH I 7 . ? -4.027 17.212 -7.752 1.00 38.06 ? 926 HOH A O 1 HETATM 4579 O O . HOH I 7 . ? -18.637 -21.234 -39.796 1.00 47.31 ? 927 HOH A O 1 HETATM 4580 O O . HOH I 7 . ? -17.004 22.406 -30.444 1.00 43.41 ? 928 HOH A O 1 HETATM 4581 O O . HOH I 7 . ? -21.658 -15.425 9.081 1.00 38.73 ? 929 HOH A O 1 HETATM 4582 O O . HOH I 7 . ? -38.713 0.204 -29.948 1.00 35.27 ? 930 HOH A O 1 HETATM 4583 O O . HOH I 7 . ? -12.076 -16.557 -33.350 1.00 44.61 ? 931 HOH A O 1 HETATM 4584 O O . HOH I 7 . ? -40.212 -5.084 17.320 1.00 35.67 ? 932 HOH A O 1 HETATM 4585 O O . HOH I 7 . ? -26.699 -15.661 1.780 1.00 46.23 ? 933 HOH A O 1 HETATM 4586 O O . HOH I 7 . ? -45.056 -16.315 11.057 1.00 36.43 ? 934 HOH A O 1 HETATM 4587 O O . HOH I 7 . ? -4.159 0.306 1.494 1.00 43.96 ? 935 HOH A O 1 HETATM 4588 O O . HOH I 7 . ? -15.564 -17.759 -9.050 1.00 35.18 ? 936 HOH A O 1 HETATM 4589 O O . HOH I 7 . ? -8.587 -1.563 2.145 1.00 36.13 ? 937 HOH A O 1 HETATM 4590 O O . HOH I 7 . ? -40.389 -25.719 -2.419 1.00 39.22 ? 938 HOH A O 1 HETATM 4591 O O . HOH I 7 . ? -15.780 6.419 -43.756 1.00 40.15 ? 939 HOH A O 1 HETATM 4592 O O . HOH I 7 . ? -39.939 8.602 -43.525 1.00 43.86 ? 940 HOH A O 1 HETATM 4593 O O . HOH I 7 . ? -25.595 10.405 -38.951 1.00 42.36 ? 941 HOH A O 1 HETATM 4594 O O . HOH I 7 . ? -34.103 -16.592 -10.989 1.00 40.19 ? 942 HOH A O 1 HETATM 4595 O O . HOH I 7 . ? -48.620 5.996 -5.065 1.00 37.68 ? 943 HOH A O 1 HETATM 4596 O O . HOH I 7 . ? -10.356 18.800 -17.355 1.00 41.57 ? 944 HOH A O 1 HETATM 4597 O O . HOH I 7 . ? -45.813 -4.851 -18.939 1.00 32.92 ? 945 HOH A O 1 HETATM 4598 O O . HOH I 7 . ? -20.369 18.095 -9.873 1.00 37.58 ? 946 HOH A O 1 HETATM 4599 O O . HOH I 7 . ? -15.954 -6.604 -25.514 1.00 41.05 ? 947 HOH A O 1 HETATM 4600 O O . HOH I 7 . ? -32.001 15.848 -36.148 1.00 38.33 ? 948 HOH A O 1 HETATM 4601 O O . HOH I 7 . ? -46.736 10.672 -25.048 1.00 41.56 ? 949 HOH A O 1 HETATM 4602 O O . HOH I 7 . ? -16.386 -5.631 -21.619 1.00 41.81 ? 950 HOH A O 1 HETATM 4603 O O . HOH I 7 . ? -46.957 10.078 -35.963 1.00 38.27 ? 951 HOH A O 1 HETATM 4604 O O . HOH I 7 . ? -37.011 9.970 -40.563 1.00 41.73 ? 952 HOH A O 1 HETATM 4605 O O . HOH I 7 . ? -4.216 8.352 -30.513 1.00 43.97 ? 953 HOH A O 1 HETATM 4606 O O . HOH I 7 . ? -50.302 -18.410 0.916 1.00 41.48 ? 954 HOH A O 1 HETATM 4607 O O . HOH I 7 . ? -42.080 -3.164 14.944 1.00 39.86 ? 955 HOH A O 1 HETATM 4608 O O . HOH I 7 . ? -52.829 -11.248 -4.928 1.00 34.94 ? 956 HOH A O 1 HETATM 4609 O O . HOH I 7 . ? -41.062 15.216 -0.566 1.00 47.67 ? 957 HOH A O 1 HETATM 4610 O O . HOH I 7 . ? -5.873 15.191 -29.582 1.00 50.29 ? 958 HOH A O 1 HETATM 4611 O O . HOH I 7 . ? -37.588 12.668 -40.591 1.00 46.83 ? 959 HOH A O 1 HETATM 4612 O O . HOH I 7 . ? -48.272 10.015 -3.948 1.00 49.95 ? 960 HOH A O 1 HETATM 4613 O O . HOH I 7 . ? -54.514 -15.157 -1.570 1.00 51.15 ? 961 HOH A O 1 HETATM 4614 O O . HOH I 7 . ? -9.331 -0.608 4.908 1.00 38.78 ? 962 HOH A O 1 HETATM 4615 O O . HOH I 7 . ? -43.005 -6.792 12.606 1.00 40.29 ? 963 HOH A O 1 HETATM 4616 O O . HOH I 7 . ? -52.888 -12.066 -1.824 1.00 35.00 ? 964 HOH A O 1 HETATM 4617 O O . HOH I 7 . ? -29.012 -14.528 -2.409 1.00 40.56 ? 965 HOH A O 1 HETATM 4618 O O . HOH I 7 . ? -17.483 5.374 10.880 1.00 47.58 ? 966 HOH A O 1 HETATM 4619 O O . HOH I 7 . ? -51.642 1.755 -1.939 1.00 39.62 ? 967 HOH A O 1 HETATM 4620 O O . HOH I 7 . ? -33.242 0.304 -33.902 1.00 38.91 ? 968 HOH A O 1 HETATM 4621 O O . HOH I 7 . ? -48.224 8.372 -32.175 1.00 47.28 ? 969 HOH A O 1 HETATM 4622 O O . HOH I 7 . ? -20.674 -12.118 -21.855 1.00 52.51 ? 970 HOH A O 1 HETATM 4623 O O . HOH I 7 . ? -8.573 0.103 11.085 1.00 48.30 ? 971 HOH A O 1 HETATM 4624 O O . HOH I 7 . ? -42.123 -25.850 -15.752 1.00 46.46 ? 972 HOH A O 1 HETATM 4625 O O . HOH I 7 . ? -41.669 12.875 -4.784 1.00 39.87 ? 973 HOH A O 1 HETATM 4626 O O . HOH I 7 . ? -30.491 -17.472 8.040 1.00 42.74 ? 974 HOH A O 1 HETATM 4627 O O . HOH I 7 . ? -27.723 -18.615 -20.902 1.00 41.03 ? 975 HOH A O 1 HETATM 4628 O O . HOH I 7 . ? -25.640 6.401 -29.961 1.00 35.48 ? 976 HOH A O 1 HETATM 4629 O O . HOH I 7 . ? -37.176 9.582 -43.217 1.00 54.40 ? 977 HOH A O 1 HETATM 4630 O O . HOH I 7 . ? -8.083 -6.048 -0.758 1.00 37.10 ? 978 HOH A O 1 HETATM 4631 O O . HOH I 7 . ? -44.934 12.297 -10.515 1.00 36.22 ? 979 HOH A O 1 HETATM 4632 O O . HOH I 7 . ? -18.871 -13.664 -10.667 1.00 39.61 ? 980 HOH A O 1 HETATM 4633 O O . HOH I 7 . ? -17.658 -16.502 -28.248 1.00 49.52 ? 981 HOH A O 1 HETATM 4634 O O . HOH I 7 . ? -33.745 5.217 11.497 1.00 39.50 ? 982 HOH A O 1 HETATM 4635 O O . HOH I 7 . ? -34.315 3.511 -33.165 1.00 36.14 ? 983 HOH A O 1 HETATM 4636 O O . HOH I 7 . ? -30.997 6.201 -36.765 1.00 41.88 ? 984 HOH A O 1 HETATM 4637 O O . HOH I 7 . ? -45.561 1.758 -17.334 1.00 39.38 ? 985 HOH A O 1 HETATM 4638 O O . HOH I 7 . ? -34.490 14.851 -35.557 1.00 44.17 ? 986 HOH A O 1 HETATM 4639 O O . HOH I 7 . ? -13.078 11.902 6.041 1.00 38.92 ? 987 HOH A O 1 HETATM 4640 O O . HOH I 7 . ? -34.844 -9.105 -29.863 1.00 41.66 ? 988 HOH A O 1 HETATM 4641 O O . HOH I 7 . ? -34.470 3.970 -41.972 1.00 44.54 ? 989 HOH A O 1 HETATM 4642 O O . HOH I 7 . ? -37.844 20.980 -11.696 1.00 42.21 ? 990 HOH A O 1 HETATM 4643 O O . HOH I 7 . ? -31.675 8.702 -38.134 1.00 42.09 ? 991 HOH A O 1 HETATM 4644 O O . HOH I 7 . ? -12.619 13.510 3.667 1.00 41.58 ? 992 HOH A O 1 HETATM 4645 O O . HOH I 7 . ? -5.754 -3.540 -38.965 1.00 39.74 ? 993 HOH A O 1 HETATM 4646 O O . HOH I 7 . ? -32.837 12.430 4.424 1.00 33.44 ? 994 HOH A O 1 HETATM 4647 O O . HOH I 7 . ? -35.832 2.424 -39.678 1.00 44.73 ? 995 HOH A O 1 HETATM 4648 O O . HOH I 7 . ? -13.537 6.150 10.640 1.00 48.82 ? 996 HOH A O 1 HETATM 4649 O O . HOH I 7 . ? -19.414 20.806 -29.770 1.00 37.16 ? 997 HOH A O 1 HETATM 4650 O O . HOH I 7 . ? -41.889 -22.989 4.372 1.00 47.71 ? 998 HOH A O 1 HETATM 4651 O O . HOH I 7 . ? -14.424 -15.366 -25.970 1.00 42.08 ? 999 HOH A O 1 HETATM 4652 O O . HOH I 7 . ? -7.313 -9.398 -9.986 1.00 39.47 ? 1000 HOH A O 1 HETATM 4653 O O . HOH I 7 . ? -28.116 -1.063 -4.051 1.00 48.96 ? 1001 HOH A O 1 HETATM 4654 O O . HOH I 7 . ? -13.817 -7.833 13.663 1.00 45.01 ? 1002 HOH A O 1 HETATM 4655 O O . HOH I 7 . ? -47.041 -21.041 4.135 1.00 46.08 ? 1003 HOH A O 1 HETATM 4656 O O . HOH I 7 . ? -34.814 2.698 10.544 1.00 40.63 ? 1004 HOH A O 1 HETATM 4657 O O . HOH I 7 . ? -45.550 -2.150 -19.270 1.00 42.12 ? 1005 HOH A O 1 HETATM 4658 O O . HOH I 7 . ? -25.132 -16.568 6.387 1.00 39.97 ? 1006 HOH A O 1 HETATM 4659 O O . HOH I 7 . ? 0.206 10.545 -4.501 1.00 40.71 ? 1007 HOH A O 1 HETATM 4660 O O . HOH I 7 . ? -24.047 -10.616 -15.426 1.00 38.07 ? 1008 HOH A O 1 HETATM 4661 O O . HOH I 7 . ? -53.719 -8.006 -11.444 1.00 40.88 ? 1009 HOH A O 1 HETATM 4662 O O . HOH I 7 . ? -12.065 -5.184 12.310 1.00 39.71 ? 1010 HOH A O 1 HETATM 4663 O O . HOH I 7 . ? -15.836 -11.442 -43.649 1.00 51.99 ? 1011 HOH A O 1 HETATM 4664 O O . HOH I 7 . ? -23.749 -14.101 -33.713 1.00 46.98 ? 1012 HOH A O 1 HETATM 4665 O O . HOH I 7 . ? -33.254 19.832 -2.240 1.00 42.76 ? 1013 HOH A O 1 HETATM 4666 O O . HOH I 7 . ? -54.891 -8.197 -2.859 1.00 31.07 ? 1014 HOH A O 1 HETATM 4667 O O . HOH I 7 . ? -48.358 0.489 -16.173 1.00 31.21 ? 1015 HOH A O 1 HETATM 4668 O O . HOH I 7 . ? -13.418 -11.834 -42.266 1.00 38.56 ? 1016 HOH A O 1 HETATM 4669 O O . HOH I 7 . ? -8.393 -8.393 0.000 0.50 40.21 ? 1017 HOH A O 1 HETATM 4670 O O . HOH I 7 . ? -40.221 1.462 -16.209 1.00 39.58 ? 1018 HOH A O 1 HETATM 4671 O O . HOH I 7 . ? -3.766 8.583 0.494 1.00 35.99 ? 1019 HOH A O 1 HETATM 4672 O O . HOH I 7 . ? -46.153 -20.232 9.197 1.00 34.41 ? 1020 HOH A O 1 HETATM 4673 O O . HOH I 7 . ? -55.424 -17.693 -1.954 1.00 36.77 ? 1021 HOH A O 1 HETATM 4674 O O . HOH I 7 . ? -30.425 -1.338 -10.108 1.00 46.71 ? 1022 HOH A O 1 HETATM 4675 O O . HOH I 7 . ? -50.267 -11.519 6.046 1.00 34.09 ? 1023 HOH A O 1 HETATM 4676 O O . HOH I 7 . ? -48.108 -18.174 -12.435 1.00 41.03 ? 1024 HOH A O 1 HETATM 4677 O O . HOH I 7 . ? -4.282 8.085 -33.275 1.00 41.68 ? 1025 HOH A O 1 HETATM 4678 O O . HOH I 7 . ? -5.329 -6.814 3.070 1.00 39.38 ? 1026 HOH A O 1 HETATM 4679 O O . HOH I 7 . ? -43.479 -13.232 -25.233 1.00 41.17 ? 1027 HOH A O 1 HETATM 4680 O O . HOH I 7 . ? -23.168 18.339 -34.290 1.00 40.69 ? 1028 HOH A O 1 HETATM 4681 O O . HOH I 7 . ? -19.433 22.288 -27.369 1.00 47.57 ? 1029 HOH A O 1 HETATM 4682 O O . HOH I 7 . ? -7.899 -4.548 5.602 1.00 40.66 ? 1030 HOH A O 1 HETATM 4683 O O . HOH I 7 . ? -38.355 1.718 -32.201 1.00 44.20 ? 1031 HOH A O 1 HETATM 4684 O O . HOH I 7 . ? -34.529 14.798 4.400 1.00 46.07 ? 1032 HOH A O 1 HETATM 4685 O O . HOH I 7 . ? -40.184 16.261 -9.401 1.00 38.41 ? 1033 HOH A O 1 HETATM 4686 O O . HOH I 7 . ? -16.953 -7.600 -19.980 1.00 41.27 ? 1034 HOH A O 1 HETATM 4687 O O . HOH I 7 . ? -18.925 -11.401 -20.032 1.00 51.15 ? 1035 HOH A O 1 HETATM 4688 O O . HOH I 7 . ? -8.427 17.403 -9.340 1.00 44.28 ? 1036 HOH A O 1 HETATM 4689 O O . HOH I 7 . ? -49.442 -12.051 10.105 1.00 43.01 ? 1037 HOH A O 1 HETATM 4690 O O . HOH I 7 . ? -17.442 -15.178 -8.671 1.00 42.87 ? 1038 HOH A O 1 HETATM 4691 O O . HOH I 7 . ? -14.392 -12.175 11.553 1.00 42.95 ? 1039 HOH A O 1 HETATM 4692 O O . HOH I 7 . ? -34.481 -2.684 -29.956 1.00 40.82 ? 1040 HOH A O 1 HETATM 4693 O O . HOH I 7 . ? -29.833 10.603 -37.400 1.00 42.18 ? 1041 HOH A O 1 HETATM 4694 O O . HOH I 7 . ? -6.847 -11.897 -10.281 1.00 37.17 ? 1042 HOH A O 1 HETATM 4695 O O . HOH I 7 . ? -6.241 15.745 -10.437 1.00 47.87 ? 1043 HOH A O 1 HETATM 4696 O O . HOH I 7 . ? -33.100 4.958 -37.694 1.00 50.72 ? 1044 HOH A O 1 HETATM 4697 O O . HOH I 7 . ? -7.744 -1.527 9.120 1.00 39.32 ? 1045 HOH A O 1 HETATM 4698 O O . HOH I 7 . ? -34.982 18.132 -1.037 1.00 42.04 ? 1046 HOH A O 1 HETATM 4699 O O . HOH I 7 . ? -35.420 20.826 -3.644 1.00 45.30 ? 1047 HOH A O 1 HETATM 4700 O O . HOH I 7 . ? -51.603 -18.322 -1.183 1.00 48.92 ? 1048 HOH A O 1 HETATM 4701 O O . HOH I 7 . ? -26.244 -9.361 -39.830 1.00 46.19 ? 1049 HOH A O 1 HETATM 4702 O O . HOH I 7 . ? -45.344 -10.801 -22.206 1.00 40.47 ? 1050 HOH A O 1 HETATM 4703 O O . HOH I 7 . ? -36.334 -23.617 -6.501 1.00 47.54 ? 1051 HOH A O 1 HETATM 4704 O O . HOH I 7 . ? -48.837 12.159 -10.015 1.00 48.02 ? 1052 HOH A O 1 HETATM 4705 O O . HOH I 7 . ? -42.399 1.312 -40.912 1.00 43.40 ? 1053 HOH A O 1 HETATM 4706 O O . HOH I 7 . ? -24.238 -7.507 -40.553 1.00 46.87 ? 1054 HOH A O 1 HETATM 4707 O O . HOH I 7 . ? -18.146 -16.927 12.849 1.00 40.30 ? 1055 HOH A O 1 HETATM 4708 O O . HOH I 7 . ? -6.004 -1.075 -23.235 1.00 40.98 ? 1056 HOH A O 1 HETATM 4709 O O . HOH I 7 . ? -27.103 2.116 -43.781 1.00 42.97 ? 1057 HOH A O 1 HETATM 4710 O O . HOH I 7 . ? -49.955 2.485 -15.676 1.00 44.00 ? 1058 HOH A O 1 HETATM 4711 O O . HOH I 7 . ? -36.396 -5.666 -26.829 1.00 46.73 ? 1059 HOH A O 1 HETATM 4712 O O . HOH I 7 . ? -19.774 -15.935 7.395 1.00 44.19 ? 1060 HOH A O 1 HETATM 4713 O O . HOH I 7 . ? -27.983 -2.854 21.856 1.00 46.15 ? 1061 HOH A O 1 HETATM 4714 O O . HOH I 7 . ? -35.325 13.544 -39.391 1.00 50.28 ? 1062 HOH A O 1 HETATM 4715 O O . HOH I 7 . ? -47.262 -21.587 -4.657 1.00 45.43 ? 1063 HOH A O 1 HETATM 4716 O O . HOH I 7 . ? -9.414 -7.824 -18.314 1.00 50.31 ? 1064 HOH A O 1 HETATM 4717 O O . HOH I 7 . ? -17.573 -12.083 12.456 1.00 41.72 ? 1065 HOH A O 1 HETATM 4718 O O . HOH I 7 . ? -48.161 -19.356 -0.717 1.00 43.53 ? 1066 HOH A O 1 HETATM 4719 O O . HOH I 7 . ? -3.911 17.163 -29.506 1.00 48.93 ? 1067 HOH A O 1 HETATM 4720 O O . HOH I 7 . ? -8.447 -8.782 -23.161 1.00 43.84 ? 1068 HOH A O 1 HETATM 4721 O O . HOH I 7 . ? -50.583 -27.252 1.388 1.00 50.54 ? 1069 HOH A O 1 HETATM 4722 O O . HOH I 7 . ? -45.941 4.584 -25.580 1.00 50.43 ? 1070 HOH A O 1 HETATM 4723 O O . HOH I 7 . ? -8.730 -10.789 -36.204 1.00 39.51 ? 1071 HOH A O 1 HETATM 4724 O O . HOH I 7 . ? -21.010 12.727 4.561 1.00 46.42 ? 1072 HOH A O 1 HETATM 4725 O O . HOH I 7 . ? -19.483 25.989 -23.753 1.00 56.49 ? 1073 HOH A O 1 HETATM 4726 O O . HOH I 7 . ? -42.080 13.597 1.370 1.00 52.34 ? 1074 HOH A O 1 HETATM 4727 O O . HOH I 7 . ? -55.656 -9.208 -5.282 1.00 44.56 ? 1075 HOH A O 1 HETATM 4728 O O . HOH I 7 . ? -11.254 0.287 12.113 1.00 42.59 ? 1076 HOH A O 1 HETATM 4729 O O . HOH I 7 . ? -46.505 -22.603 -10.549 1.00 45.10 ? 1077 HOH A O 1 HETATM 4730 O O . HOH I 7 . ? -40.606 -21.260 8.786 1.00 49.38 ? 1078 HOH A O 1 HETATM 4731 O O . HOH I 7 . ? -22.713 -6.930 -42.859 1.00 52.03 ? 1079 HOH A O 1 HETATM 4732 O O . HOH I 7 . ? -37.012 10.317 -24.454 1.00 34.97 ? 1080 HOH A O 1 HETATM 4733 O O . HOH I 7 . ? -24.248 -12.664 -18.864 1.00 43.73 ? 1081 HOH A O 1 HETATM 4734 O O . HOH I 7 . ? -10.055 -4.824 -21.843 1.00 46.94 ? 1082 HOH A O 1 HETATM 4735 O O . HOH I 7 . ? -24.215 -2.133 -11.259 1.00 36.78 ? 1083 HOH A O 1 HETATM 4736 O O . HOH I 7 . ? -24.813 -14.157 -9.124 1.00 53.95 ? 1084 HOH A O 1 HETATM 4737 O O . HOH I 7 . ? -25.789 -12.533 -5.454 1.00 60.15 ? 1085 HOH A O 1 HETATM 4738 O O . HOH I 7 . ? -5.394 -2.599 -30.287 1.00 47.63 ? 1086 HOH A O 1 HETATM 4739 O O . HOH I 7 . ? -4.323 -0.622 -32.504 1.00 44.49 ? 1087 HOH A O 1 HETATM 4740 O O . HOH I 7 . ? -5.017 1.271 -30.311 1.00 49.40 ? 1088 HOH A O 1 HETATM 4741 O O . HOH I 7 . ? -5.517 -0.643 -27.050 1.00 55.21 ? 1089 HOH A O 1 HETATM 4742 O O . HOH I 7 . ? -4.742 1.770 -33.733 1.00 49.24 ? 1090 HOH A O 1 HETATM 4743 O O . HOH I 7 . ? -30.219 -3.311 -41.141 1.00 48.19 ? 1091 HOH A O 1 HETATM 4744 O O . HOH I 7 . ? -23.150 7.634 -40.538 1.00 47.88 ? 1092 HOH A O 1 HETATM 4745 O O . HOH I 7 . ? -18.526 3.916 -44.951 1.00 62.21 ? 1093 HOH A O 1 HETATM 4746 O O . HOH I 7 . ? -18.052 -16.799 -30.802 1.00 61.34 ? 1094 HOH A O 1 HETATM 4747 O O . HOH I 7 . ? -28.216 -18.599 -32.209 1.00 57.97 ? 1095 HOH A O 1 HETATM 4748 O O A HOH I 7 . ? -35.715 -3.229 -14.127 0.44 24.17 ? 1096 HOH A O 1 HETATM 4749 O O B HOH I 7 . ? -30.995 -1.457 -12.827 0.38 22.87 ? 1097 HOH A O 1 HETATM 4750 O O . HOH I 7 . ? -28.837 -12.017 -37.814 1.00 53.01 ? 1098 HOH A O 1 HETATM 4751 O O . HOH I 7 . ? -4.208 6.475 -45.744 1.00 49.21 ? 1099 HOH A O 1 HETATM 4752 O O . HOH I 7 . ? -1.899 7.236 -42.922 1.00 55.83 ? 1100 HOH A O 1 HETATM 4753 O O . HOH I 7 . ? -40.289 0.373 11.797 1.00 49.10 ? 1101 HOH A O 1 HETATM 4754 O O A HOH I 7 . ? -49.260 12.694 -29.777 0.77 28.43 ? 1102 HOH A O 1 HETATM 4755 O O B HOH I 7 . ? -25.092 -11.735 -2.933 0.60 33.72 ? 1103 HOH A O 1 HETATM 4756 O O . HOH I 7 . ? -43.136 -13.957 12.181 1.00 44.93 ? 1104 HOH A O 1 HETATM 4757 O O . HOH I 7 . ? -41.136 -17.629 12.818 1.00 52.65 ? 1105 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . ASP A 1 ? 0.8626 1.0661 0.7835 0.0364 0.0837 -0.0345 26 ASP A N 2 C CA . ASP A 1 ? 0.7629 0.9656 0.7036 0.0402 0.0753 -0.0408 26 ASP A CA 3 C C . ASP A 1 ? 0.6894 0.8936 0.6496 0.0325 0.0737 -0.0342 26 ASP A C 4 O O . ASP A 1 ? 0.5660 0.7787 0.5304 0.0254 0.0813 -0.0273 26 ASP A O 5 C CB . ASP A 1 ? 0.8547 1.0707 0.8046 0.0481 0.0792 -0.0506 26 ASP A CB 6 C CG . ASP A 1 ? 0.9962 1.2073 0.9612 0.0536 0.0693 -0.0582 26 ASP A CG 7 O OD1 . ASP A 1 ? 1.0318 1.2280 0.9931 0.0541 0.0593 -0.0588 26 ASP A OD1 8 O OD2 . ASP A 1 ? 1.0432 1.2654 1.0238 0.0575 0.0714 -0.0637 26 ASP A OD2 9 N N . LEU A 2 ? 0.5853 0.7807 0.5568 0.0337 0.0638 -0.0364 27 LEU A N 10 C CA . LEU A 2 ? 0.4874 0.6829 0.4766 0.0274 0.0614 -0.0310 27 LEU A CA 11 C C . LEU A 2 ? 0.5127 0.7252 0.5195 0.0270 0.0679 -0.0325 27 LEU A C 12 O O . LEU A 2 ? 0.4221 0.6405 0.4381 0.0197 0.0716 -0.0258 27 LEU A O 13 C CB . LEU A 2 ? 0.4452 0.6290 0.4429 0.0299 0.0503 -0.0344 27 LEU A CB 14 C CG . LEU A 2 ? 0.3889 0.5717 0.4046 0.0249 0.0470 -0.0302 27 LEU A CG 15 C CD1 . LEU A 2 ? 0.3890 0.5685 0.4011 0.0159 0.0492 -0.0199 27 LEU A CD1 16 C CD2 . LEU A 2 ? 0.5026 0.6732 0.5241 0.0277 0.0369 -0.0339 27 LEU A CD2 17 N N . LEU A 3 ? 0.6360 0.8565 0.6477 0.0351 0.0689 -0.0417 28 LEU A N 18 C CA . LEU A 3 ? 0.6915 0.9289 0.7209 0.0366 0.0742 -0.0447 28 LEU A CA 19 C C . LEU A 3 ? 0.6732 0.9258 0.7015 0.0310 0.0861 -0.0395 28 LEU A C 20 O O . LEU A 3 ? 0.6104 0.8746 0.6553 0.0265 0.0894 -0.0365 28 LEU A O 21 C CB . LEU A 3 ? 0.7627 1.0047 0.7940 0.0475 0.0734 -0.0561 28 LEU A CB 22 C CG . LEU A 3 ? 0.8579 1.0850 0.8905 0.0532 0.0620 -0.0622 28 LEU A CG 23 C CD1 . LEU A 3 ? 0.9087 1.1401 0.9418 0.0639 0.0617 -0.0736 28 LEU A CD1 24 C CD2 . LEU A 3 ? 0.8549 1.0772 0.9050 0.0496 0.0553 -0.0592 28 LEU A CD2 25 N N . SER A 4 ? 0.6793 0.9317 0.6879 0.0311 0.0923 -0.0383 29 SER A N 26 C CA . SER A 4 ? 0.7109 0.9770 0.7164 0.0253 0.1045 -0.0330 29 SER A CA 27 C C . SER A 4 ? 0.6007 0.8636 0.6101 0.0136 0.1051 -0.0219 29 SER A C 28 O O . SER A 4 ? 0.5175 0.7947 0.5370 0.0073 0.1132 -0.0178 29 SER A O 29 C CB . SER A 4 ? 0.8221 1.0854 0.8022 0.0277 0.1105 -0.0334 29 SER A CB 30 O OG . SER A 4 ? 0.9107 1.1554 0.8724 0.0238 0.1054 -0.0271 29 SER A OG 31 N N . CYS A 5 ? 0.4313 0.6758 0.4333 0.0106 0.0964 -0.0173 30 CYS A N 32 C CA . CYS A 5 ? 0.4050 0.6442 0.4104 0.0003 0.0956 -0.0074 30 CYS A CA 33 C C . CYS A 5 ? 0.4089 0.6563 0.4394 -0.0018 0.0929 -0.0079 30 CYS A C 34 O O . CYS A 5 ? 0.3614 0.6174 0.4015 -0.0096 0.0977 -0.0023 30 CYS A O 35 C CB . CYS A 5 ? 0.3780 0.5957 0.3702 -0.0009 0.0865 -0.0035 30 CYS A CB 36 S SG . CYS A 5 ? 0.4605 0.6693 0.4535 -0.0129 0.0853 0.0085 30 CYS A SG 37 N N . LEU A 6 ? 0.3748 0.6189 0.4155 0.0052 0.0849 -0.0148 31 LEU A N 38 C CA . LEU A 6 ? 0.3312 0.5808 0.3940 0.0045 0.0810 -0.0158 31 LEU A CA 39 C C . LEU A 6 ? 0.3710 0.6428 0.4490 0.0039 0.0894 -0.0177 31 LEU A C 40 O O . LEU A 6 ? 0.3605 0.6392 0.4538 -0.0017 0.0895 -0.0141 31 LEU A O 41 C CB . LEU A 6 ? 0.3353 0.5773 0.4040 0.0130 0.0719 -0.0235 31 LEU A CB 42 C CG . LEU A 6 ? 0.3137 0.5353 0.3739 0.0125 0.0627 -0.0214 31 LEU A CG 43 C CD1 . LEU A 6 ? 0.3472 0.5621 0.4117 0.0208 0.0550 -0.0296 31 LEU A CD1 44 C CD2 . LEU A 6 ? 0.2524 0.4679 0.3201 0.0046 0.0591 -0.0138 31 LEU A CD2 45 N N . THR A 7 ? 0.4623 0.7455 0.5359 0.0098 0.0963 -0.0237 32 THR A N 46 C CA . THR A 7 ? 0.4583 0.7646 0.5468 0.0104 0.1051 -0.0266 32 THR A CA 47 C C . THR A 7 ? 0.4038 0.7198 0.4916 -0.0005 0.1147 -0.0181 32 THR A C 48 O O . THR A 7 ? 0.5347 0.8661 0.6414 -0.0049 0.1181 -0.0167 32 THR A O 49 C CB . THR A 7 ? 0.5850 0.9005 0.6678 0.0205 0.1103 -0.0358 32 THR A CB 50 O OG1 . THR A 7 ? 0.5273 0.8359 0.6155 0.0303 0.1011 -0.0443 32 THR A OG1 51 C CG2 . THR A 7 ? 0.6343 0.9754 0.7315 0.0205 0.1211 -0.0383 32 THR A CG2 52 N N . PHE A 8 ? 0.4286 0.7351 0.4948 -0.0050 0.1187 -0.0123 33 PHE A N 53 C CA . PHE A 8 ? 0.5641 0.8761 0.6267 -0.0162 0.1275 -0.0032 33 PHE A CA 54 C C . PHE A 8 ? 0.5150 0.8231 0.5909 -0.0254 0.1224 0.0037 33 PHE A C 55 O O . PHE A 8 ? 0.4911 0.8091 0.5739 -0.0348 0.1291 0.0096 33 PHE A O 56 C CB . PHE A 8 ? 0.6867 0.9835 0.7210 -0.0187 0.1299 0.0022 33 PHE A CB 57 C CG . PHE A 8 ? 0.8043 1.1026 0.8320 -0.0309 0.1382 0.0125 33 PHE A CG 58 C CD1 . PHE A 8 ? 0.8256 1.1408 0.8515 -0.0339 0.1517 0.0134 33 PHE A CD1 59 C CD2 . PHE A 8 ? 0.8626 1.1447 0.8854 -0.0393 0.1326 0.0212 33 PHE A CD2 60 C CE1 . PHE A 8 ? 0.8874 1.2030 0.9070 -0.0459 0.1595 0.0233 33 PHE A CE1 61 C CE2 . PHE A 8 ? 0.8999 1.1815 0.9160 -0.0506 0.1397 0.0307 33 PHE A CE2 62 C CZ . PHE A 8 ? 0.9023 1.2004 0.9168 -0.0544 0.1532 0.0320 33 PHE A CZ 63 N N . ASN A 9 ? 0.3505 0.6439 0.4297 -0.0228 0.1106 0.0028 34 ASN A N 64 C CA . ASN A 9 ? 0.4198 0.7069 0.5092 -0.0306 0.1048 0.0090 34 ASN A CA 65 C C . ASN A 9 ? 0.4149 0.7109 0.5283 -0.0275 0.0993 0.0042 34 ASN A C 66 O O . ASN A 9 ? 0.4645 0.7534 0.5857 -0.0323 0.0928 0.0081 34 ASN A O 67 C CB . ASN A 9 ? 0.4635 0.7261 0.5377 -0.0318 0.0961 0.0134 34 ASN A CB 68 C CG . ASN A 9 ? 0.6088 0.8612 0.6606 -0.0375 0.1007 0.0206 34 ASN A CG 69 O OD1 . ASN A 9 ? 0.5836 0.8361 0.6201 -0.0334 0.1053 0.0184 34 ASN A OD1 70 N ND2 . ASN A 9 ? 0.6264 0.8689 0.6752 -0.0467 0.0989 0.0291 34 ASN A ND2 71 N N . GLY A 10 ? 0.3681 0.6787 0.4920 -0.0190 0.1014 -0.0044 35 GLY A N 72 C CA . GLY A 10 ? 0.3659 0.6871 0.5129 -0.0156 0.0970 -0.0092 35 GLY A CA 73 C C . GLY A 10 ? 0.4031 0.7091 0.5526 -0.0092 0.0850 -0.0127 35 GLY A C 74 O O . GLY A 10 ? 0.3878 0.6959 0.5531 -0.0092 0.0792 -0.0134 35 GLY A O 75 N N . VAL A 11 ? 0.2790 0.5694 0.4125 -0.0039 0.0812 -0.0149 36 VAL A N 76 C CA . VAL A 11 ? 0.2859 0.5623 0.4212 0.0024 0.0708 -0.0189 36 VAL A CA 77 C C . VAL A 11 ? 0.3258 0.6075 0.4623 0.0137 0.0709 -0.0289 36 VAL A C 78 O O . VAL A 11 ? 0.3805 0.6583 0.5021 0.0175 0.0734 -0.0317 36 VAL A O 79 C CB . VAL A 11 ? 0.2736 0.5281 0.3919 0.0002 0.0653 -0.0146 36 VAL A CB 80 C CG1 . VAL A 11 ? 0.3212 0.5621 0.4431 0.0054 0.0553 -0.0181 36 VAL A CG1 81 C CG2 . VAL A 11 ? 0.2847 0.5335 0.3994 -0.0105 0.0660 -0.0049 36 VAL A CG2 82 N N . ARG A 12 ? 0.2957 0.5855 0.4491 0.0193 0.0677 -0.0345 37 ARG A N 83 C CA . ARG A 12 ? 0.3035 0.6008 0.4599 0.0302 0.0686 -0.0444 37 ARG A CA 84 C C . ARG A 12 ? 0.2806 0.5622 0.4369 0.0377 0.0585 -0.0497 37 ARG A C 85 O O . ARG A 12 ? 0.2865 0.5678 0.4396 0.0467 0.0579 -0.0577 37 ARG A O 86 C CB . ARG A 12 ? 0.4508 0.7710 0.6268 0.0327 0.0733 -0.0482 37 ARG A CB 87 C CG . ARG A 12 ? 0.6088 0.9458 0.7885 0.0238 0.0833 -0.0425 37 ARG A CG 88 C CD . ARG A 12 ? 0.7653 1.1264 0.9674 0.0264 0.0872 -0.0468 37 ARG A CD 89 N NE . ARG A 12 ? 0.8984 1.2737 1.1082 0.0156 0.0944 -0.0400 37 ARG A NE 90 C CZ . ARG A 12 ? 0.9442 1.3182 1.1649 0.0080 0.0897 -0.0343 37 ARG A CZ 91 N NH1 . ARG A 12 ? 0.9773 1.3643 1.2050 -0.0022 0.0965 -0.0285 37 ARG A NH1 92 N NH2 . ARG A 12 ? 0.8995 1.2589 1.1237 0.0103 0.0783 -0.0344 37 ARG A NH2 93 N N . ASN A 13 ? 0.2248 0.4928 0.3842 0.0341 0.0506 -0.0453 38 ASN A N 94 C CA . ASN A 13 ? 0.2195 0.4724 0.3795 0.0402 0.0414 -0.0495 38 ASN A CA 95 C C . ASN A 13 ? 0.2096 0.4446 0.3529 0.0399 0.0382 -0.0490 38 ASN A C 96 O O . ASN A 13 ? 0.2074 0.4289 0.3458 0.0341 0.0340 -0.0430 38 ASN A O 97 C CB . ASN A 13 ? 0.2387 0.4851 0.4095 0.0372 0.0344 -0.0457 38 ASN A CB 98 C CG . ASN A 13 ? 0.3025 0.5391 0.4785 0.0453 0.0264 -0.0516 38 ASN A CG 99 O OD1 . ASN A 13 ? 0.3421 0.5684 0.5100 0.0505 0.0237 -0.0564 38 ASN A OD1 100 N ND2 . ASN A 13 ? 0.2658 0.5050 0.4550 0.0463 0.0220 -0.0513 38 ASN A ND2 101 N N . HIS A 14 ? 0.2426 0.4784 0.3776 0.0464 0.0401 -0.0556 39 HIS A N 102 C CA . HIS A 14 ? 0.2965 0.5167 0.4166 0.0470 0.0365 -0.0564 39 HIS A CA 103 C C . HIS A 14 ? 0.3496 0.5671 0.4669 0.0570 0.0339 -0.0665 39 HIS A C 104 O O . HIS A 14 ? 0.3402 0.5705 0.4627 0.0634 0.0379 -0.0727 39 HIS A O 105 C CB . HIS A 14 ? 0.3068 0.5289 0.4125 0.0418 0.0425 -0.0516 39 HIS A CB 106 C CG . HIS A 14 ? 0.2901 0.5303 0.3947 0.0430 0.0523 -0.0533 39 HIS A CG 107 N ND1 . HIS A 14 ? 0.3515 0.5976 0.4507 0.0513 0.0553 -0.0616 39 HIS A ND1 108 C CD2 . HIS A 14 ? 0.4333 0.6870 0.5414 0.0369 0.0601 -0.0478 39 HIS A CD2 109 C CE1 . HIS A 14 ? 0.4066 0.6698 0.5060 0.0504 0.0652 -0.0611 39 HIS A CE1 110 N NE2 . HIS A 14 ? 0.4012 0.6695 0.5064 0.0413 0.0683 -0.0526 39 HIS A NE2 111 N N . THR A 15 ? 0.2879 0.4886 0.3975 0.0581 0.0272 -0.0683 40 THR A N 112 C CA A THR A 15 ? 0.2597 0.4545 0.3658 0.0668 0.0234 -0.0778 40 THR A CA 113 C CA B THR A 15 ? 0.2483 0.4431 0.3545 0.0668 0.0233 -0.0777 40 THR A CA 114 C C . THR A 15 ? 0.2527 0.4350 0.3441 0.0658 0.0201 -0.0784 40 THR A C 115 O O . THR A 15 ? 0.2507 0.4210 0.3404 0.0603 0.0154 -0.0735 40 THR A O 116 C CB A THR A 15 ? 0.2717 0.4567 0.3887 0.0705 0.0156 -0.0810 40 THR A CB 117 C CB B THR A 15 ? 0.2629 0.4477 0.3800 0.0702 0.0155 -0.0807 40 THR A CB 118 O OG1 A THR A 15 ? 0.2353 0.4044 0.3510 0.0646 0.0095 -0.0758 40 THR A OG1 119 O OG1 B THR A 15 ? 0.3406 0.5372 0.4716 0.0718 0.0176 -0.0804 40 THR A OG1 120 C CG2 A THR A 15 ? 0.3029 0.4992 0.4349 0.0712 0.0173 -0.0797 40 THR A CG2 121 C CG2 B THR A 15 ? 0.2641 0.4414 0.3775 0.0789 0.0111 -0.0907 40 THR A CG2 122 N N . VAL A 16 ? 0.2634 0.4486 0.3441 0.0715 0.0224 -0.0849 41 VAL A N 123 C CA . VAL A 16 ? 0.2729 0.4466 0.3394 0.0714 0.0186 -0.0864 41 VAL A CA 124 C C . VAL A 16 ? 0.2649 0.4242 0.3338 0.0756 0.0093 -0.0931 41 VAL A C 125 O O . VAL A 16 ? 0.2833 0.4422 0.3613 0.0810 0.0070 -0.0986 41 VAL A O 126 C CB . VAL A 16 ? 0.3492 0.5301 0.4006 0.0758 0.0242 -0.0908 41 VAL A CB 127 C CG1 . VAL A 16 ? 0.4221 0.6164 0.4700 0.0706 0.0339 -0.0835 41 VAL A CG1 128 C CG2 . VAL A 16 ? 0.3470 0.5332 0.4006 0.0859 0.0249 -0.1013 41 VAL A CG2 129 N N . PHE A 17 ? 0.2802 0.4275 0.3412 0.0731 0.0039 -0.0927 42 PHE A N 130 C CA . PHE A 17 ? 0.3090 0.4421 0.3716 0.0759 -0.0048 -0.0989 42 PHE A CA 131 C C . PHE A 17 ? 0.3445 0.4785 0.4055 0.0855 -0.0059 -0.1097 42 PHE A C 132 O O . PHE A 17 ? 0.3627 0.5056 0.4142 0.0904 -0.0009 -0.1138 42 PHE A O 133 C CB . PHE A 17 ? 0.3345 0.4584 0.3869 0.0730 -0.0095 -0.0985 42 PHE A CB 134 C CG . PHE A 17 ? 0.3781 0.4888 0.4317 0.0759 -0.0183 -0.1060 42 PHE A CG 135 C CD1 . PHE A 17 ? 0.3925 0.4922 0.4556 0.0709 -0.0242 -0.1033 42 PHE A CD1 136 C CD2 . PHE A 17 ? 0.4723 0.5812 0.5172 0.0834 -0.0206 -0.1158 42 PHE A CD2 137 C CE1 . PHE A 17 ? 0.4606 0.5481 0.5256 0.0726 -0.0320 -0.1100 42 PHE A CE1 138 C CE2 . PHE A 17 ? 0.5049 0.6010 0.5513 0.0855 -0.0292 -0.1229 42 PHE A CE2 139 C CZ . PHE A 17 ? 0.4817 0.5672 0.5386 0.0798 -0.0349 -0.1198 42 PHE A CZ 140 N N . SER A 18 ? 0.3383 0.4622 0.4078 0.0882 -0.0122 -0.1142 43 SER A N 141 C CA . SER A 18 ? 0.3322 0.4534 0.4001 0.0976 -0.0150 -0.1250 43 SER A CA 142 C C . SER A 18 ? 0.4297 0.5327 0.4994 0.0977 -0.0248 -0.1296 43 SER A C 143 O O . SER A 18 ? 0.4030 0.4970 0.4813 0.0918 -0.0287 -0.1246 43 SER A O 144 C CB . SER A 18 ? 0.3471 0.4765 0.4257 0.1028 -0.0118 -0.1268 43 SER A CB 145 O OG . SER A 18 ? 0.3877 0.5124 0.4652 0.1123 -0.0155 -0.1376 43 SER A OG 146 N N . ALA A 19 ? 0.5289 0.6261 0.5899 0.1040 -0.0288 -0.1392 44 ALA A N 147 C CA . ALA A 19 ? 0.7199 0.7996 0.7826 0.1041 -0.0384 -0.1447 44 ALA A CA 148 C C . ALA A 19 ? 0.7063 0.7785 0.7785 0.1089 -0.0418 -0.1489 44 ALA A C 149 O O . ALA A 19 ? 0.7033 0.7597 0.7800 0.1070 -0.0493 -0.1509 44 ALA A O 150 C CB . ALA A 19 ? 0.7624 0.8379 0.8119 0.1093 -0.0422 -0.1538 44 ALA A CB 151 N N . ASP A 20 ? 0.6070 0.6905 0.6824 0.1150 -0.0364 -0.1502 45 ASP A N 152 C CA . ASP A 20 ? 0.5175 0.5950 0.6020 0.1203 -0.0394 -0.1538 45 ASP A CA 153 C C . ASP A 20 ? 0.6227 0.6892 0.7173 0.1125 -0.0433 -0.1459 45 ASP A C 154 O O . ASP A 20 ? 0.4900 0.5642 0.5899 0.1062 -0.0389 -0.1366 45 ASP A O 155 C CB . ASP A 20 ? 0.4170 0.5122 0.5057 0.1267 -0.0319 -0.1544 45 ASP A CB 156 C CG . ASP A 20 ? 0.3653 0.4552 0.4633 0.1336 -0.0356 -0.1587 45 ASP A CG 157 O OD1 . ASP A 20 ? 0.4884 0.5596 0.5868 0.1350 -0.0439 -0.1628 45 ASP A OD1 158 O OD2 . ASP A 20 ? 0.3332 0.4375 0.4382 0.1377 -0.0303 -0.1580 45 ASP A OD2 159 N N . SER A 21 ? 0.7171 0.7651 0.8139 0.1128 -0.0514 -0.1496 46 SER A N 160 C CA . SER A 21 ? 0.8122 0.8474 0.9167 0.1050 -0.0552 -0.1425 46 SER A CA 161 C C . SER A 21 ? 0.7000 0.7408 0.8131 0.1042 -0.0518 -0.1354 46 SER A C 162 O O . SER A 21 ? 0.6624 0.7016 0.7797 0.0960 -0.0508 -0.1263 46 SER A O 163 C CB . SER A 21 ? 0.9767 0.9907 1.0818 0.1066 -0.0639 -0.1485 46 SER A CB 164 O OG . SER A 21 ? 1.0869 1.0976 1.1935 0.1164 -0.0660 -0.1550 46 SER A OG 165 N N . ASP A 22 ? 0.5278 0.5754 0.6436 0.1132 -0.0504 -0.1401 47 ASP A N 166 C CA . ASP A 22 ? 0.5690 0.6234 0.6937 0.1134 -0.0480 -0.1343 47 ASP A CA 167 C C . ASP A 22 ? 0.4443 0.5224 0.5706 0.1162 -0.0395 -0.1334 47 ASP A C 168 O O . ASP A 22 ? 0.3897 0.4769 0.5236 0.1213 -0.0378 -0.1338 47 ASP A O 169 C CB . ASP A 22 ? 0.6621 0.7045 0.7913 0.1210 -0.0540 -0.1391 47 ASP A CB 170 C CG . ASP A 22 ? 0.7602 0.8033 0.8856 0.1325 -0.0556 -0.1510 47 ASP A CG 171 O OD1 . ASP A 22 ? 0.6973 0.7500 0.8159 0.1344 -0.0520 -0.1556 47 ASP A OD1 172 O OD2 . ASP A 22 ? 0.8657 0.8992 0.9941 0.1400 -0.0607 -0.1559 47 ASP A OD2 173 N N . SER A 23 ? 0.3811 0.4692 0.5005 0.1125 -0.0345 -0.1320 48 SER A N 174 C CA . SER A 23 ? 0.3465 0.4563 0.4665 0.1125 -0.0256 -0.1293 48 SER A CA 175 C C . SER A 23 ? 0.3775 0.4929 0.5062 0.1057 -0.0231 -0.1192 48 SER A C 176 O O . SER A 23 ? 0.3184 0.4210 0.4497 0.0995 -0.0275 -0.1134 48 SER A O 177 C CB . SER A 23 ? 0.3051 0.4200 0.4139 0.1085 -0.0217 -0.1283 48 SER A CB 178 O OG . SER A 23 ? 0.3216 0.4274 0.4290 0.0986 -0.0240 -0.1206 48 SER A OG 179 N N . ASP A 24 ? 0.2946 0.4295 0.4278 0.1066 -0.0160 -0.1173 49 ASP A N 180 C CA . ASP A 24 ? 0.2525 0.3943 0.3931 0.0995 -0.0133 -0.1078 49 ASP A CA 181 C C . ASP A 24 ? 0.2641 0.4000 0.3985 0.0889 -0.0126 -0.0995 49 ASP A C 182 O O . ASP A 24 ? 0.2856 0.4155 0.4241 0.0826 -0.0146 -0.0921 49 ASP A O 183 C CB . ASP A 24 ? 0.2828 0.4478 0.4287 0.1014 -0.0051 -0.1077 49 ASP A CB 184 C CG . ASP A 24 ? 0.4486 0.6218 0.6029 0.1123 -0.0055 -0.1159 49 ASP A CG 185 O OD1 . ASP A 24 ? 0.4662 0.6272 0.6255 0.1168 -0.0128 -0.1186 49 ASP A OD1 186 O OD2 . ASP A 24 ? 0.3785 0.5703 0.5342 0.1165 0.0016 -0.1197 49 ASP A OD2 187 N N . PHE A 25 ? 0.2453 0.3828 0.3692 0.0877 -0.0101 -0.1009 50 PHE A N 188 C CA . PHE A 25 ? 0.2573 0.3889 0.3746 0.0789 -0.0101 -0.0941 50 PHE A CA 189 C C . PHE A 25 ? 0.2591 0.3723 0.3789 0.0749 -0.0173 -0.0916 50 PHE A C 190 O O . PHE A 25 ? 0.2237 0.3335 0.3456 0.0674 -0.0173 -0.0835 50 PHE A O 191 C CB . PHE A 25 ? 0.2322 0.3647 0.3369 0.0803 -0.0087 -0.0983 50 PHE A CB 192 C CG . PHE A 25 ? 0.2486 0.3726 0.3468 0.0729 -0.0108 -0.0931 50 PHE A CG 193 C CD1 . PHE A 25 ? 0.2508 0.3819 0.3454 0.0664 -0.0059 -0.0851 50 PHE A CD1 194 C CD2 . PHE A 25 ? 0.3141 0.4231 0.4102 0.0725 -0.0179 -0.0963 50 PHE A CD2 195 C CE1 . PHE A 25 ? 0.2406 0.3640 0.3294 0.0604 -0.0082 -0.0807 50 PHE A CE1 196 C CE2 . PHE A 25 ? 0.3236 0.4262 0.4151 0.0661 -0.0199 -0.0920 50 PHE A CE2 197 C CZ . PHE A 25 ? 0.2705 0.3805 0.3583 0.0604 -0.0152 -0.0843 50 PHE A CZ 198 N N . ASN A 26 ? 0.2719 0.3729 0.3912 0.0797 -0.0232 -0.0985 51 ASN A N 199 C CA A ASN A 26 ? 0.3045 0.3874 0.4261 0.0757 -0.0297 -0.0967 51 ASN A CA 200 C CA B ASN A 26 ? 0.2922 0.3753 0.4137 0.0755 -0.0296 -0.0964 51 ASN A CA 201 C C . ASN A 26 ? 0.2931 0.3722 0.4232 0.0737 -0.0309 -0.0909 51 ASN A C 202 O O . ASN A 26 ? 0.2952 0.3641 0.4265 0.0670 -0.0329 -0.0847 51 ASN A O 203 C CB A ASN A 26 ? 0.3328 0.4034 0.4524 0.0817 -0.0358 -0.1058 51 ASN A CB 204 C CB B ASN A 26 ? 0.3416 0.4119 0.4606 0.0806 -0.0357 -0.1053 51 ASN A CB 205 C CG A ASN A 26 ? 0.3766 0.4290 0.4970 0.0761 -0.0418 -0.1041 51 ASN A CG 206 C CG B ASN A 26 ? 0.3164 0.3843 0.4269 0.0789 -0.0370 -0.1085 51 ASN A CG 207 O OD1 A ASN A 26 ? 0.5129 0.5636 0.6306 0.0694 -0.0416 -0.1004 51 ASN A OD1 208 O OD1 B ASN A 26 ? 0.3216 0.3895 0.4300 0.0717 -0.0361 -0.1027 51 ASN A OD1 209 N ND2 A ASN A 26 ? 0.4442 0.4828 0.5683 0.0788 -0.0470 -0.1069 51 ASN A ND2 210 N ND2 B ASN A 26 ? 0.4075 0.4731 0.5128 0.0859 -0.0396 -0.1181 51 ASN A ND2 211 N N . ARG A 27 ? 0.2508 0.3381 0.3864 0.0798 -0.0297 -0.0933 52 ARG A N 212 C CA . ARG A 27 ? 0.2413 0.3255 0.3845 0.0791 -0.0315 -0.0886 52 ARG A CA 213 C C . ARG A 27 ? 0.2781 0.3679 0.4223 0.0705 -0.0278 -0.0788 52 ARG A C 214 O O . ARG A 27 ? 0.2588 0.3375 0.4043 0.0656 -0.0306 -0.0729 52 ARG A O 215 C CB . ARG A 27 ? 0.2861 0.3816 0.4360 0.0878 -0.0307 -0.0935 52 ARG A CB 216 C CG . ARG A 27 ? 0.3219 0.4131 0.4794 0.0885 -0.0341 -0.0898 52 ARG A CG 217 C CD . ARG A 27 ? 0.4371 0.5364 0.6018 0.0990 -0.0354 -0.0968 52 ARG A CD 218 N NE . ARG A 27 ? 0.5128 0.6356 0.6811 0.1017 -0.0282 -0.0993 52 ARG A NE 219 C CZ . ARG A 27 ? 0.5422 0.6809 0.7178 0.0987 -0.0240 -0.0945 52 ARG A CZ 220 N NH1 . ARG A 27 ? 0.4605 0.5937 0.6399 0.0936 -0.0268 -0.0872 52 ARG A NH1 221 N NH2 . ARG A 27 ? 0.5177 0.6775 0.6966 0.1007 -0.0168 -0.0970 52 ARG A NH2 222 N N . PHE A 28 ? 0.2245 0.3304 0.3672 0.0686 -0.0215 -0.0771 53 PHE A N 223 C CA . PHE A 28 ? 0.2602 0.3710 0.4030 0.0605 -0.0181 -0.0681 53 PHE A CA 224 C C . PHE A 28 ? 0.2025 0.3010 0.3392 0.0534 -0.0198 -0.0634 53 PHE A C 225 O O . PHE A 28 ? 0.2119 0.3052 0.3497 0.0475 -0.0203 -0.0563 53 PHE A O 226 C CB . PHE A 28 ? 0.2513 0.3805 0.3924 0.0596 -0.0109 -0.0672 53 PHE A CB 227 C CG . PHE A 28 ? 0.3055 0.4501 0.4550 0.0650 -0.0080 -0.0702 53 PHE A CG 228 C CD1 . PHE A 28 ? 0.3882 0.5331 0.5472 0.0658 -0.0107 -0.0681 53 PHE A CD1 229 C CD2 . PHE A 28 ? 0.3171 0.4763 0.4647 0.0693 -0.0025 -0.0752 53 PHE A CD2 230 C CE1 . PHE A 28 ? 0.3159 0.4765 0.4844 0.0709 -0.0083 -0.0714 53 PHE A CE1 231 C CE2 . PHE A 28 ? 0.3296 0.5048 0.4863 0.0742 0.0009 -0.0783 53 PHE A CE2 232 C CZ . PHE A 28 ? 0.3139 0.4904 0.4820 0.0750 -0.0022 -0.0765 53 PHE A CZ 233 N N . LEU A 29 ? 0.2049 0.2992 0.3353 0.0543 -0.0208 -0.0678 54 LEU A N 234 C CA . LEU A 29 ? 0.2222 0.3063 0.3484 0.0481 -0.0227 -0.0643 54 LEU A CA 235 C C . LEU A 29 ? 0.2280 0.2969 0.3583 0.0451 -0.0271 -0.0612 54 LEU A C 236 O O . LEU A 29 ? 0.2257 0.2905 0.3558 0.0387 -0.0265 -0.0544 54 LEU A O 237 C CB . LEU A 29 ? 0.2158 0.2967 0.3360 0.0505 -0.0247 -0.0709 54 LEU A CB 238 C CG . LEU A 29 ? 0.2390 0.3102 0.3567 0.0447 -0.0275 -0.0687 54 LEU A CG 239 C CD1 . LEU A 29 ? 0.2467 0.3236 0.3614 0.0386 -0.0237 -0.0609 54 LEU A CD1 240 C CD2 . LEU A 29 ? 0.2470 0.3158 0.3594 0.0478 -0.0305 -0.0762 54 LEU A CD2 241 N N . HIS A 30 ? 0.2472 0.3073 0.3804 0.0500 -0.0313 -0.0662 55 HIS A N 242 C CA . HIS A 30 ? 0.2396 0.2829 0.3749 0.0471 -0.0356 -0.0638 55 HIS A CA 243 C C . HIS A 30 ? 0.2666 0.3076 0.4054 0.0459 -0.0356 -0.0577 55 HIS A C 244 O O . HIS A 30 ? 0.2824 0.3101 0.4211 0.0419 -0.0378 -0.0534 55 HIS A O 245 C CB . HIS A 30 ? 0.3045 0.3365 0.4401 0.0524 -0.0407 -0.0714 55 HIS A CB 246 C CG . HIS A 30 ? 0.3701 0.4001 0.5020 0.0521 -0.0421 -0.0769 55 HIS A CG 247 N ND1 . HIS A 30 ? 0.4424 0.4614 0.5742 0.0461 -0.0445 -0.0755 55 HIS A ND1 248 C CD2 . HIS A 30 ? 0.4565 0.4947 0.5848 0.0570 -0.0416 -0.0839 55 HIS A CD2 249 C CE1 . HIS A 30 ? 0.4872 0.5075 0.6160 0.0474 -0.0462 -0.0816 55 HIS A CE1 250 N NE2 . HIS A 30 ? 0.3906 0.4219 0.5162 0.0541 -0.0445 -0.0867 55 HIS A NE2 251 N N . LEU A 31 ? 0.2347 0.2889 0.3764 0.0492 -0.0332 -0.0575 56 LEU A N 252 C CA . LEU A 31 ? 0.2447 0.2982 0.3903 0.0492 -0.0341 -0.0529 56 LEU A CA 253 C C . LEU A 31 ? 0.2622 0.3084 0.4054 0.0412 -0.0334 -0.0443 56 LEU A C 254 O O . LEU A 31 ? 0.2866 0.3220 0.4301 0.0405 -0.0364 -0.0408 56 LEU A O 255 C CB . LEU A 31 ? 0.3664 0.4390 0.5166 0.0522 -0.0305 -0.0536 56 LEU A CB 256 C CG . LEU A 31 ? 0.4181 0.4932 0.5746 0.0550 -0.0326 -0.0518 56 LEU A CG 257 C CD1 . LEU A 31 ? 0.3459 0.4093 0.5043 0.0621 -0.0386 -0.0567 56 LEU A CD1 258 C CD2 . LEU A 31 ? 0.3856 0.4821 0.5482 0.0574 -0.0283 -0.0535 56 LEU A CD2 259 N N . SER A 32 ? 0.2194 0.2708 0.3592 0.0357 -0.0297 -0.0411 57 SER A N 260 C CA . SER A 32 ? 0.2499 0.2958 0.3873 0.0287 -0.0286 -0.0334 57 SER A CA 261 C C . SER A 32 ? 0.2459 0.2838 0.3797 0.0240 -0.0283 -0.0325 57 SER A C 262 O O . SER A 32 ? 0.2632 0.3019 0.3945 0.0187 -0.0259 -0.0273 57 SER A O 263 C CB . SER A 32 ? 0.2452 0.3041 0.3823 0.0258 -0.0246 -0.0289 57 SER A CB 264 O OG . SER A 32 ? 0.3648 0.4302 0.5068 0.0289 -0.0253 -0.0287 57 SER A OG 265 N N . ILE A 33 ? 0.2012 0.2318 0.3354 0.0261 -0.0310 -0.0378 58 ILE A N 266 C CA . ILE A 33 ? 0.2180 0.2400 0.3510 0.0212 -0.0315 -0.0371 58 ILE A CA 267 C C . ILE A 33 ? 0.2804 0.2870 0.4138 0.0183 -0.0333 -0.0331 58 ILE A C 268 O O . ILE A 33 ? 0.3147 0.3114 0.4490 0.0214 -0.0367 -0.0360 58 ILE A O 269 C CB . ILE A 33 ? 0.2386 0.2593 0.3721 0.0239 -0.0340 -0.0447 58 ILE A CB 270 C CG1 . ILE A 33 ? 0.2020 0.2370 0.3327 0.0260 -0.0317 -0.0478 58 ILE A CG1 271 C CG2 . ILE A 33 ? 0.2286 0.2393 0.3632 0.0185 -0.0353 -0.0441 58 ILE A CG2 272 C CD1 . ILE A 33 ? 0.2346 0.2687 0.3642 0.0293 -0.0346 -0.0558 58 ILE A CD1 273 N N . GLN A 34 ? 0.2162 0.2200 0.3479 0.0126 -0.0309 -0.0265 59 GLN A N 274 C CA . GLN A 34 ? 0.2073 0.1967 0.3375 0.0097 -0.0316 -0.0218 59 GLN A CA 275 C C . GLN A 34 ? 0.3043 0.2837 0.4355 0.0046 -0.0312 -0.0213 59 GLN A C 276 O O . GLN A 34 ? 0.3654 0.3323 0.4948 0.0014 -0.0310 -0.0172 59 GLN A O 277 C CB . GLN A 34 ? 0.1993 0.1905 0.3263 0.0073 -0.0293 -0.0148 59 GLN A CB 278 C CG . GLN A 34 ? 0.2503 0.2507 0.3778 0.0117 -0.0300 -0.0150 59 GLN A CG 279 C CD . GLN A 34 ? 0.3288 0.3209 0.4568 0.0163 -0.0341 -0.0164 59 GLN A CD 280 O OE1 . GLN A 34 ? 0.3840 0.3635 0.5115 0.0173 -0.0366 -0.0184 59 GLN A OE1 281 N NE2 . GLN A 34 ? 0.4330 0.4317 0.5621 0.0193 -0.0351 -0.0152 59 GLN A NE2 282 N N . ASN A 35 ? 0.2554 0.2407 0.3895 0.0037 -0.0312 -0.0255 60 ASN A N 283 C CA . ASN A 35 ? 0.2119 0.1892 0.3494 -0.0009 -0.0316 -0.0266 60 ASN A CA 284 C C . ASN A 35 ? 0.2405 0.2181 0.3811 0.0020 -0.0354 -0.0348 60 ASN A C 285 O O . ASN A 35 ? 0.2957 0.2840 0.4370 0.0034 -0.0357 -0.0386 60 ASN A O 286 C CB . ASN A 35 ? 0.2384 0.2219 0.3774 -0.0059 -0.0283 -0.0235 60 ASN A CB 287 C CG . ASN A 35 ? 0.2058 0.1817 0.3500 -0.0114 -0.0281 -0.0239 60 ASN A CG 288 O OD1 . ASN A 35 ? 0.2418 0.2078 0.3883 -0.0118 -0.0308 -0.0270 60 ASN A OD1 289 N ND2 . ASN A 35 ? 0.2444 0.2250 0.3909 -0.0157 -0.0250 -0.0210 60 ASN A ND2 290 N N . PRO A 36 ? 0.2707 0.2356 0.4119 0.0033 -0.0387 -0.0375 61 PRO A N 291 C CA . PRO A 36 ? 0.2750 0.2374 0.4185 0.0064 -0.0431 -0.0458 61 PRO A CA 292 C C . PRO A 36 ? 0.2784 0.2447 0.4264 0.0025 -0.0438 -0.0493 61 PRO A C 293 O O . PRO A 36 ? 0.3080 0.2757 0.4568 0.0058 -0.0476 -0.0567 61 PRO A O 294 C CB . PRO A 36 ? 0.3030 0.2469 0.4461 0.0057 -0.0459 -0.0455 61 PRO A CB 295 C CG . PRO A 36 ? 0.3385 0.2785 0.4773 0.0064 -0.0439 -0.0387 61 PRO A CG 296 C CD . PRO A 36 ? 0.2824 0.2332 0.4208 0.0024 -0.0389 -0.0329 61 PRO A CD 297 N N . LEU A 37 ? 0.2817 0.2499 0.4327 -0.0039 -0.0406 -0.0445 62 LEU A N 298 C CA . LEU A 37 ? 0.2587 0.2324 0.4152 -0.0074 -0.0415 -0.0477 62 LEU A CA 299 C C . LEU A 37 ? 0.2690 0.2560 0.4229 -0.0023 -0.0432 -0.0528 62 LEU A C 300 O O . LEU A 37 ? 0.3153 0.3055 0.4725 -0.0027 -0.0464 -0.0584 62 LEU A O 301 C CB . LEU A 37 ? 0.2642 0.2410 0.4239 -0.0137 -0.0370 -0.0413 62 LEU A CB 302 C CG . LEU A 37 ? 0.2743 0.2579 0.4416 -0.0175 -0.0379 -0.0443 62 LEU A CG 303 C CD1 . LEU A 37 ? 0.3419 0.3168 0.5162 -0.0205 -0.0420 -0.0497 62 LEU A CD1 304 C CD2 . LEU A 37 ? 0.2707 0.2575 0.4411 -0.0228 -0.0329 -0.0378 62 LEU A CD2 305 N N . PHE A 38 ? 0.2742 0.2690 0.4220 0.0022 -0.0411 -0.0508 63 PHE A N 306 C CA . PHE A 38 ? 0.2932 0.3006 0.4368 0.0066 -0.0415 -0.0544 63 PHE A CA 307 C C . PHE A 38 ? 0.2986 0.3076 0.4377 0.0139 -0.0430 -0.0595 63 PHE A C 308 O O . PHE A 38 ? 0.3267 0.3465 0.4607 0.0177 -0.0411 -0.0599 63 PHE A O 309 C CB . PHE A 38 ? 0.2585 0.2754 0.3986 0.0054 -0.0370 -0.0479 63 PHE A CB 310 C CG . PHE A 38 ? 0.2687 0.2847 0.4128 -0.0007 -0.0353 -0.0434 63 PHE A CG 311 C CD1 . PHE A 38 ? 0.2497 0.2705 0.3965 -0.0022 -0.0372 -0.0463 63 PHE A CD1 312 C CD2 . PHE A 38 ? 0.2764 0.2867 0.4214 -0.0045 -0.0320 -0.0365 63 PHE A CD2 313 C CE1 . PHE A 38 ? 0.3543 0.3757 0.5062 -0.0072 -0.0355 -0.0425 63 PHE A CE1 314 C CE2 . PHE A 38 ? 0.2800 0.2901 0.4287 -0.0097 -0.0298 -0.0327 63 PHE A CE2 315 C CZ . PHE A 38 ? 0.2908 0.3069 0.4436 -0.0110 -0.0314 -0.0358 63 PHE A CZ 316 N N . GLN A 39 ? 0.3449 0.3432 0.4860 0.0157 -0.0463 -0.0634 64 GLN A N 317 C CA . GLN A 39 ? 0.3999 0.3992 0.5375 0.0233 -0.0478 -0.0685 64 GLN A CA 318 C C . GLN A 39 ? 0.5924 0.5902 0.7288 0.0274 -0.0525 -0.0781 64 GLN A C 319 O O . GLN A 39 ? 0.6451 0.6474 0.7775 0.0346 -0.0530 -0.0833 64 GLN A O 320 C CB . GLN A 39 ? 0.4377 0.4253 0.5767 0.0242 -0.0486 -0.0663 64 GLN A CB 321 C CG . GLN A 39 ? 0.6664 0.6591 0.8028 0.0318 -0.0482 -0.0683 64 GLN A CG 322 C CD . GLN A 39 ? 0.7164 0.7034 0.8536 0.0314 -0.0472 -0.0621 64 GLN A CD 323 O OE1 . GLN A 39 ? 0.8145 0.7898 0.9527 0.0261 -0.0475 -0.0573 64 GLN A OE1 324 N NE2 . GLN A 39 ? 0.5550 0.5506 0.6916 0.0370 -0.0460 -0.0623 64 GLN A NE2 325 N N . ASN A 40 ? 0.5494 0.5413 0.6894 0.0231 -0.0558 -0.0807 65 ASN A N 326 C CA . ASN A 40 ? 0.6231 0.6105 0.7625 0.0263 -0.0615 -0.0902 65 ASN A CA 327 C C . ASN A 40 ? 0.5939 0.5929 0.7265 0.0318 -0.0621 -0.0958 65 ASN A C 328 O O . ASN A 40 ? 0.5459 0.5570 0.6748 0.0318 -0.0581 -0.0919 65 ASN A O 329 C CB . ASN A 40 ? 0.6094 0.5878 0.7561 0.0192 -0.0652 -0.0913 65 ASN A CB 330 C CG . ASN A 40 ? 0.5757 0.5639 0.7247 0.0149 -0.0644 -0.0896 65 ASN A CG 331 O OD1 . ASN A 40 ? 0.5201 0.5157 0.6652 0.0182 -0.0669 -0.0949 65 ASN A OD1 332 N ND2 . ASN A 40 ? 0.6264 0.6144 0.7812 0.0079 -0.0610 -0.0823 65 ASN A ND2 333 N N . SER A 41 ? 0.6659 0.6602 0.7961 0.0363 -0.0673 -0.1050 66 SER A N 334 C CA . SER A 41 ? 0.6879 0.6913 0.8095 0.0428 -0.0681 -0.1114 66 SER A CA 335 C C . SER A 41 ? 0.6383 0.6492 0.7578 0.0400 -0.0692 -0.1115 66 SER A C 336 O O . SER A 41 ? 0.7572 0.7767 0.8675 0.0449 -0.0686 -0.1147 66 SER A O 337 C CB . SER A 41 ? 0.7452 0.7395 0.8640 0.0487 -0.0741 -0.1219 66 SER A CB 338 O OG . SER A 41 ? 0.7501 0.7328 0.8751 0.0437 -0.0804 -0.1253 66 SER A OG 339 N N . LEU A 42 ? 0.5346 0.5421 0.6621 0.0324 -0.0708 -0.1081 67 LEU A N 340 C CA . LEU A 42 ? 0.5993 0.6138 0.7263 0.0299 -0.0726 -0.1083 67 LEU A CA 341 C C . LEU A 42 ? 0.5900 0.6150 0.7145 0.0279 -0.0666 -0.0996 67 LEU A C 342 O O . LEU A 42 ? 0.7265 0.7578 0.8491 0.0267 -0.0678 -0.0991 67 LEU A O 343 C CB . LEU A 42 ? 0.7429 0.7503 0.8811 0.0230 -0.0775 -0.1098 67 LEU A CB 344 C CG . LEU A 42 ? 0.8378 0.8351 0.9780 0.0244 -0.0852 -0.1196 67 LEU A CG 345 C CD1 . LEU A 42 ? 0.8821 0.8727 1.0358 0.0159 -0.0888 -0.1196 67 LEU A CD1 346 C CD2 . LEU A 42 ? 0.8507 0.8531 0.9814 0.0306 -0.0900 -0.1277 67 LEU A CD2 347 N N . ILE A 43 ? 0.4218 0.4482 0.5463 0.0276 -0.0607 -0.0930 68 ILE A N 348 C CA . ILE A 43 ? 0.3473 0.3821 0.4694 0.0253 -0.0551 -0.0846 68 ILE A CA 349 C C . ILE A 43 ? 0.3999 0.4447 0.5104 0.0308 -0.0522 -0.0851 68 ILE A C 350 O O . ILE A 43 ? 0.4086 0.4544 0.5140 0.0366 -0.0521 -0.0902 68 ILE A O 351 C CB . ILE A 43 ? 0.4215 0.4531 0.5479 0.0226 -0.0504 -0.0774 68 ILE A CB 352 C CG1 . ILE A 43 ? 0.4755 0.4960 0.6118 0.0170 -0.0524 -0.0763 68 ILE A CG1 353 C CG2 . ILE A 43 ? 0.4179 0.4573 0.5417 0.0201 -0.0451 -0.0691 68 ILE A CG2 354 C CD1 . ILE A 43 ? 0.4924 0.5143 0.6345 0.0106 -0.0522 -0.0724 68 ILE A CD1 355 N N . SER A 44 ? 0.4106 0.4625 0.5168 0.0289 -0.0495 -0.0798 69 SER A N 356 C CA . SER A 44 ? 0.4706 0.5314 0.5653 0.0327 -0.0457 -0.0786 69 SER A CA 357 C C . SER A 44 ? 0.3083 0.3725 0.4024 0.0350 -0.0403 -0.0763 69 SER A C 358 O O . SER A 44 ? 0.3235 0.3846 0.4252 0.0320 -0.0385 -0.0719 69 SER A O 359 C CB . SER A 44 ? 0.3513 0.4167 0.4427 0.0291 -0.0434 -0.0714 69 SER A CB 360 O OG . SER A 44 ? 0.2747 0.3389 0.3729 0.0242 -0.0398 -0.0637 69 SER A OG 361 N N . LYS A 45 ? 0.3160 0.3871 0.4012 0.0404 -0.0379 -0.0796 70 LYS A N 362 C CA . LYS A 45 ? 0.2806 0.3576 0.3662 0.0430 -0.0325 -0.0780 70 LYS A CA 363 C C . LYS A 45 ? 0.2769 0.3649 0.3533 0.0434 -0.0264 -0.0739 70 LYS A C 364 O O . LYS A 45 ? 0.2899 0.3804 0.3559 0.0450 -0.0267 -0.0756 70 LYS A O 365 C CB . LYS A 45 ? 0.3707 0.4460 0.4564 0.0497 -0.0344 -0.0867 70 LYS A CB 366 C CG . LYS A 45 ? 0.4695 0.5323 0.5621 0.0496 -0.0412 -0.0919 70 LYS A CG 367 C CD . LYS A 45 ? 0.4416 0.4977 0.5447 0.0458 -0.0411 -0.0872 70 LYS A CD 368 C CE . LYS A 45 ? 0.4684 0.5109 0.5776 0.0450 -0.0475 -0.0920 70 LYS A CE 369 N NZ . LYS A 45 ? 0.5102 0.5443 0.6278 0.0408 -0.0473 -0.0868 70 LYS A NZ 370 N N . PRO A 46 ? 0.2352 0.3292 0.3151 0.0419 -0.0210 -0.0684 71 PRO A N 371 C CA . PRO A 46 ? 0.2416 0.3459 0.3137 0.0412 -0.0147 -0.0639 71 PRO A CA 372 C C . PRO A 46 ? 0.2732 0.3848 0.3363 0.0474 -0.0120 -0.0700 71 PRO A C 373 O O . PRO A 46 ? 0.2822 0.3934 0.3482 0.0530 -0.0136 -0.0773 71 PRO A O 374 C CB . PRO A 46 ? 0.2308 0.3399 0.3114 0.0388 -0.0106 -0.0585 71 PRO A CB 375 C CG . PRO A 46 ? 0.2827 0.3831 0.3740 0.0385 -0.0148 -0.0597 71 PRO A CG 376 C CD . PRO A 46 ? 0.2383 0.3294 0.3291 0.0408 -0.0209 -0.0664 71 PRO A CD 377 N N . SER A 47 ? 0.2433 0.3611 0.2951 0.0467 -0.0077 -0.0671 72 SER A N 378 C CA . SER A 47 ? 0.2600 0.3857 0.3018 0.0523 -0.0036 -0.0720 72 SER A CA 379 C C . SER A 47 ? 0.2497 0.3873 0.2976 0.0534 0.0036 -0.0710 72 SER A C 380 O O . SER A 47 ? 0.2756 0.4204 0.3200 0.0594 0.0069 -0.0769 72 SER A O 381 C CB . SER A 47 ? 0.3280 0.4551 0.3540 0.0508 -0.0013 -0.0686 72 SER A CB 382 O OG . SER A 47 ? 0.3639 0.4810 0.3853 0.0505 -0.0086 -0.0703 72 SER A OG 383 N N . ALA A 48 ? 0.2384 0.3783 0.2958 0.0479 0.0057 -0.0638 73 ALA A N 384 C CA . ALA A 48 ? 0.2174 0.3686 0.2838 0.0485 0.0112 -0.0627 73 ALA A CA 385 C C . ALA A 48 ? 0.1931 0.3409 0.2710 0.0429 0.0095 -0.0562 73 ALA A C 386 O O . ALA A 48 ? 0.2036 0.3429 0.2800 0.0377 0.0065 -0.0510 73 ALA A O 387 C CB . ALA A 48 ? 0.2654 0.4290 0.3240 0.0470 0.0198 -0.0594 73 ALA A CB 388 N N . ILE A 49 ? 0.1871 0.3420 0.2764 0.0445 0.0113 -0.0569 74 ILE A N 389 C CA . ILE A 49 ? 0.2088 0.3612 0.3084 0.0398 0.0097 -0.0511 74 ILE A CA 390 C C . ILE A 49 ? 0.2096 0.3768 0.3145 0.0376 0.0163 -0.0475 74 ILE A C 391 O O . ILE A 49 ? 0.2078 0.3868 0.3166 0.0425 0.0200 -0.0523 74 ILE A O 392 C CB . ILE A 49 ? 0.1980 0.3432 0.3075 0.0439 0.0040 -0.0555 74 ILE A CB 393 C CG1 . ILE A 49 ? 0.2496 0.3804 0.3546 0.0453 -0.0021 -0.0592 74 ILE A CG1 394 C CG2 . ILE A 49 ? 0.2040 0.3462 0.3226 0.0395 0.0024 -0.0493 74 ILE A CG2 395 C CD1 . ILE A 49 ? 0.2556 0.3769 0.3684 0.0490 -0.0078 -0.0636 74 ILE A CD1 396 N N . ILE A 50 ? 0.2018 0.3686 0.3070 0.0302 0.0177 -0.0392 75 ILE A N 397 C CA . ILE A 50 ? 0.2097 0.3898 0.3204 0.0264 0.0234 -0.0350 75 ILE A CA 398 C C . ILE A 50 ? 0.1652 0.3424 0.2874 0.0234 0.0198 -0.0312 75 ILE A C 399 O O . ILE A 50 ? 0.1750 0.3391 0.2953 0.0201 0.0152 -0.0273 75 ILE A O 400 C CB . ILE A 50 ? 0.2231 0.4042 0.3234 0.0195 0.0280 -0.0279 75 ILE A CB 401 C CG1 . ILE A 50 ? 0.2909 0.4682 0.3760 0.0219 0.0290 -0.0304 75 ILE A CG1 402 C CG2 . ILE A 50 ? 0.2463 0.4430 0.3517 0.0159 0.0352 -0.0248 75 ILE A CG2 403 C CD1 . ILE A 50 ? 0.3262 0.5129 0.4094 0.0291 0.0325 -0.0383 75 ILE A CD1 404 N N . LEU A 51 ? 0.1755 0.3650 0.3092 0.0250 0.0219 -0.0326 76 LEU A N 405 C CA . LEU A 51 ? 0.1880 0.3760 0.3326 0.0226 0.0181 -0.0294 76 LEU A CA 406 C C . LEU A 51 ? 0.1921 0.3931 0.3425 0.0166 0.0230 -0.0243 76 LEU A C 407 O O . LEU A 51 ? 0.2320 0.4479 0.3937 0.0191 0.0254 -0.0273 76 LEU A O 408 C CB . LEU A 51 ? 0.2411 0.4311 0.3963 0.0304 0.0143 -0.0360 76 LEU A CB 409 C CG . LEU A 51 ? 0.3592 0.5324 0.5124 0.0347 0.0072 -0.0393 76 LEU A CG 410 C CD1 . LEU A 51 ? 0.3538 0.5202 0.4962 0.0371 0.0074 -0.0429 76 LEU A CD1 411 C CD2 . LEU A 51 ? 0.4416 0.6181 0.6053 0.0424 0.0039 -0.0454 76 LEU A CD2 412 N N . PRO A 52 ? 0.1790 0.3747 0.3222 0.0087 0.0242 -0.0170 77 PRO A N 413 C CA . PRO A 52 ? 0.1707 0.3772 0.3188 0.0018 0.0285 -0.0117 77 PRO A CA 414 C C . PRO A 52 ? 0.2219 0.4318 0.3842 0.0012 0.0244 -0.0111 77 PRO A C 415 O O . PRO A 52 ? 0.2035 0.4007 0.3666 0.0025 0.0177 -0.0107 77 PRO A O 416 C CB . PRO A 52 ? 0.2026 0.3971 0.3385 -0.0055 0.0284 -0.0043 77 PRO A CB 417 C CG . PRO A 52 ? 0.2324 0.4098 0.3612 -0.0025 0.0224 -0.0054 77 PRO A CG 418 C CD . PRO A 52 ? 0.2204 0.3997 0.3514 0.0060 0.0213 -0.0134 77 PRO A CD 419 N N . GLY A 53 ? 0.2200 0.4472 0.3934 -0.0009 0.0285 -0.0111 78 GLY A N 420 C CA . GLY A 53 ? 0.2568 0.4894 0.4449 -0.0009 0.0242 -0.0113 78 GLY A CA 421 C C . GLY A 53 ? 0.2322 0.4653 0.4229 -0.0104 0.0241 -0.0042 78 GLY A C 422 O O . GLY A 53 ? 0.2592 0.4973 0.4620 -0.0112 0.0201 -0.0041 78 GLY A O 423 N N . SER A 54 ? 0.1920 0.4195 0.3708 -0.0174 0.0278 0.0016 79 SER A N 424 C CA . SER A 54 ? 0.2153 0.4412 0.3947 -0.0268 0.0276 0.0085 79 SER A CA 425 C C . SER A 54 ? 0.2413 0.4524 0.4034 -0.0320 0.0289 0.0144 79 SER A C 426 O O . SER A 54 ? 0.2392 0.4449 0.3900 -0.0287 0.0309 0.0130 79 SER A O 427 C CB . SER A 54 ? 0.2663 0.5131 0.4568 -0.0316 0.0344 0.0089 79 SER A CB 428 O OG . SER A 54 ? 0.2570 0.5093 0.4382 -0.0334 0.0429 0.0099 79 SER A OG 429 N N . LYS A 55 ? 0.2557 0.4598 0.4155 -0.0397 0.0270 0.0206 80 LYS A N 430 C CA . LYS A 55 ? 0.2984 0.4878 0.4418 -0.0444 0.0276 0.0263 80 LYS A CA 431 C C . LYS A 55 ? 0.2582 0.4548 0.3937 -0.0473 0.0358 0.0280 80 LYS A C 432 O O . LYS A 55 ? 0.2695 0.4554 0.3899 -0.0470 0.0368 0.0299 80 LYS A O 433 C CB . LYS A 55 ? 0.3432 0.5236 0.4858 -0.0519 0.0238 0.0323 80 LYS A CB 434 C CG . LYS A 55 ? 0.3828 0.5762 0.5347 -0.0598 0.0274 0.0352 80 LYS A CG 435 C CD . LYS A 55 ? 0.4573 0.6393 0.6073 -0.0668 0.0224 0.0406 80 LYS A CD 436 C CE . LYS A 55 ? 0.5038 0.6988 0.6645 -0.0755 0.0254 0.0433 80 LYS A CE 437 N NZ . LYS A 55 ? 0.6182 0.8005 0.7759 -0.0825 0.0200 0.0483 80 LYS A NZ 438 N N . GLU A 56 ? 0.2723 0.4872 0.4179 -0.0500 0.0418 0.0271 81 GLU A N 439 C CA . GLU A 56 ? 0.2814 0.5044 0.4194 -0.0526 0.0507 0.0286 81 GLU A CA 440 C C . GLU A 56 ? 0.2335 0.4574 0.3641 -0.0439 0.0528 0.0229 81 GLU A C 441 O O . GLU A 56 ? 0.2343 0.4524 0.3493 -0.0443 0.0565 0.0249 81 GLU A O 442 C CB . GLU A 56 ? 0.2946 0.5392 0.4474 -0.0572 0.0573 0.0283 81 GLU A CB 443 C CG . GLU A 56 ? 0.3424 0.5863 0.4997 -0.0680 0.0568 0.0349 81 GLU A CG 444 C CD . GLU A 56 ? 0.4338 0.6747 0.6037 -0.0679 0.0480 0.0340 81 GLU A CD 445 O OE1 . GLU A 56 ? 0.3535 0.5978 0.5323 -0.0596 0.0436 0.0279 81 GLU A OE1 446 O OE2 . GLU A 56 ? 0.5452 0.7792 0.7151 -0.0759 0.0451 0.0394 81 GLU A OE2 447 N N . GLU A 57 ? 0.2285 0.4584 0.3694 -0.0357 0.0500 0.0158 82 GLU A N 448 C CA . GLU A 57 ? 0.2395 0.4687 0.3738 -0.0271 0.0508 0.0097 82 GLU A CA 449 C C . GLU A 57 ? 0.1986 0.4077 0.3182 -0.0251 0.0454 0.0109 82 GLU A C 450 O O . GLU A 57 ? 0.2091 0.4146 0.3168 -0.0214 0.0472 0.0088 82 GLU A O 451 C CB . GLU A 57 ? 0.2108 0.4489 0.3594 -0.0187 0.0480 0.0018 82 GLU A CB 452 C CG . GLU A 57 ? 0.2055 0.4665 0.3680 -0.0181 0.0546 -0.0016 82 GLU A CG 453 C CD . GLU A 57 ? 0.2947 0.5636 0.4696 -0.0083 0.0517 -0.0101 82 GLU A CD 454 O OE1 . GLU A 57 ? 0.2419 0.4986 0.4113 -0.0015 0.0462 -0.0140 82 GLU A OE1 455 O OE2 . GLU A 57 ? 0.3359 0.6232 0.5265 -0.0072 0.0547 -0.0131 82 GLU A OE2 456 N N . LEU A 58 ? 0.1914 0.3876 0.3120 -0.0273 0.0386 0.0140 83 LEU A N 457 C CA . LEU A 58 ? 0.2019 0.3802 0.3103 -0.0259 0.0338 0.0153 83 LEU A CA 458 C C . LEU A 58 ? 0.2345 0.4065 0.3271 -0.0306 0.0372 0.0207 83 LEU A C 459 O O . LEU A 58 ? 0.2286 0.3930 0.3095 -0.0272 0.0364 0.0193 83 LEU A O 460 C CB . LEU A 58 ? 0.1665 0.3332 0.2790 -0.0277 0.0269 0.0179 83 LEU A CB 461 C CG . LEU A 58 ? 0.1775 0.3265 0.2800 -0.0265 0.0219 0.0193 83 LEU A CG 462 C CD1 . LEU A 58 ? 0.2050 0.3515 0.3037 -0.0193 0.0208 0.0134 83 LEU A CD1 463 C CD2 . LEU A 58 ? 0.1771 0.3167 0.2851 -0.0273 0.0159 0.0209 83 LEU A CD2 464 N N . SER A 59 ? 0.2547 0.4296 0.3471 -0.0385 0.0405 0.0267 84 SER A N 465 C CA . SER A 59 ? 0.2777 0.4459 0.3545 -0.0435 0.0438 0.0325 84 SER A CA 466 C C . SER A 59 ? 0.2783 0.4531 0.3454 -0.0404 0.0499 0.0301 84 SER A C 467 O O . SER A 59 ? 0.2754 0.4400 0.3268 -0.0390 0.0493 0.0314 84 SER A O 468 C CB . SER A 59 ? 0.2846 0.4565 0.3648 -0.0530 0.0469 0.0389 84 SER A CB 469 O OG . SER A 59 ? 0.3330 0.5003 0.3981 -0.0580 0.0516 0.0444 84 SER A OG 470 N N . ASN A 60 ? 0.2671 0.4592 0.3434 -0.0389 0.0557 0.0263 85 ASN A N 471 C CA . ASN A 60 ? 0.2569 0.4565 0.3239 -0.0357 0.0624 0.0236 85 ASN A CA 472 C C . ASN A 60 ? 0.2730 0.4673 0.3341 -0.0262 0.0585 0.0166 85 ASN A C 473 O O . ASN A 60 ? 0.3027 0.4947 0.3492 -0.0235 0.0612 0.0156 85 ASN A O 474 C CB . ASN A 60 ? 0.3198 0.5407 0.3995 -0.0366 0.0702 0.0211 85 ASN A CB 475 C CG . ASN A 60 ? 0.3685 0.5953 0.4511 -0.0472 0.0757 0.0284 85 ASN A CG 476 O OD1 . ASN A 60 ? 0.4862 0.7025 0.5542 -0.0533 0.0773 0.0353 85 ASN A OD1 477 N ND2 . ASN A 60 ? 0.3239 0.5671 0.4255 -0.0494 0.0782 0.0269 85 ASN A ND2 478 N N . THR A 61 ? 0.2810 0.4726 0.3529 -0.0214 0.0520 0.0120 86 THR A N 479 C CA . THR A 61 ? 0.2506 0.4358 0.3181 -0.0132 0.0475 0.0055 86 THR A CA 480 C C . THR A 61 ? 0.2798 0.4489 0.3314 -0.0138 0.0436 0.0086 86 THR A C 481 O O . THR A 61 ? 0.2650 0.4312 0.3052 -0.0093 0.0435 0.0052 86 THR A O 482 C CB . THR A 61 ? 0.2171 0.3999 0.2985 -0.0090 0.0409 0.0010 86 THR A CB 483 O OG1 . THR A 61 ? 0.2337 0.4318 0.3289 -0.0062 0.0440 -0.0034 86 THR A OG1 484 C CG2 . THR A 61 ? 0.2410 0.4144 0.3171 -0.0021 0.0357 -0.0047 86 THR A CG2 485 N N . ILE A 62 ? 0.2554 0.4143 0.3063 -0.0191 0.0400 0.0147 87 ILE A N 486 C CA . ILE A 62 ? 0.2848 0.4290 0.3218 -0.0198 0.0361 0.0179 87 ILE A CA 487 C C . ILE A 62 ? 0.3280 0.4718 0.3481 -0.0217 0.0411 0.0213 87 ILE A C 488 O O . ILE A 62 ? 0.3188 0.4557 0.3263 -0.0178 0.0389 0.0195 87 ILE A O 489 C CB . ILE A 62 ? 0.2813 0.4154 0.3210 -0.0250 0.0320 0.0238 87 ILE A CB 490 C CG1 . ILE A 62 ? 0.2890 0.4209 0.3420 -0.0221 0.0267 0.0202 87 ILE A CG1 491 C CG2 . ILE A 62 ? 0.2935 0.4133 0.3184 -0.0258 0.0287 0.0276 87 ILE A CG2 492 C CD1 . ILE A 62 ? 0.2633 0.3881 0.3212 -0.0271 0.0236 0.0252 87 ILE A CD1 493 N N . ARG A 63 ? 0.3124 0.4637 0.3325 -0.0278 0.0478 0.0261 88 ARG A N 494 C CA . ARG A 63 ? 0.3600 0.5105 0.3631 -0.0305 0.0535 0.0302 88 ARG A CA 495 C C . ARG A 63 ? 0.4231 0.5789 0.4174 -0.0236 0.0563 0.0240 88 ARG A C 496 O O . ARG A 63 ? 0.3962 0.5439 0.3722 -0.0221 0.0562 0.0255 88 ARG A O 497 C CB . ARG A 63 ? 0.2920 0.4522 0.2994 -0.0388 0.0612 0.0357 88 ARG A CB 498 C CG . ARG A 63 ? 0.3585 0.5105 0.3699 -0.0465 0.0583 0.0426 88 ARG A CG 499 C CD . ARG A 63 ? 0.3183 0.4807 0.3358 -0.0553 0.0655 0.0476 88 ARG A CD 500 N NE . ARG A 63 ? 0.3676 0.5301 0.3690 -0.0590 0.0730 0.0521 88 ARG A NE 501 C CZ . ARG A 63 ? 0.4821 0.6602 0.4847 -0.0592 0.0820 0.0502 88 ARG A CZ 502 N NH1 . ARG A 63 ? 0.4845 0.6797 0.5047 -0.0554 0.0841 0.0436 88 ARG A NH1 503 N NH2 . ARG A 63 ? 0.4890 0.6652 0.4747 -0.0630 0.0889 0.0550 88 ARG A NH2 504 N N . CYS A 64 ? 0.3470 0.5155 0.3535 -0.0187 0.0581 0.0169 89 CYS A N 505 C CA . CYS A 64 ? 0.3388 0.5125 0.3375 -0.0114 0.0605 0.0101 89 CYS A CA 506 C C . CYS A 64 ? 0.3851 0.5467 0.3760 -0.0047 0.0523 0.0053 89 CYS A C 507 O O . CYS A 64 ? 0.3501 0.5076 0.3246 -0.0010 0.0526 0.0035 89 CYS A O 508 C CB . CYS A 64 ? 0.3556 0.5456 0.3703 -0.0074 0.0641 0.0033 89 CYS A CB 509 S SG . CYS A 64 ? 0.3608 0.5698 0.3817 -0.0134 0.0762 0.0067 89 CYS A SG 510 N N . ILE A 65 ? 0.3040 0.4599 0.3067 -0.0032 0.0449 0.0031 90 ILE A N 511 C CA . ILE A 65 ? 0.3284 0.4738 0.3269 0.0024 0.0369 -0.0016 90 ILE A CA 512 C C . ILE A 65 ? 0.4084 0.5418 0.3891 0.0012 0.0342 0.0028 90 ILE A C 513 O O . ILE A 65 ? 0.4193 0.5471 0.3900 0.0065 0.0301 -0.0015 90 ILE A O 514 C CB . ILE A 65 ? 0.2768 0.4172 0.2905 0.0024 0.0303 -0.0028 90 ILE A CB 515 C CG1 . ILE A 65 ? 0.2777 0.4282 0.3072 0.0056 0.0314 -0.0085 90 ILE A CG1 516 C CG2 . ILE A 65 ? 0.3190 0.4482 0.3285 0.0064 0.0224 -0.0063 90 ILE A CG2 517 C CD1 . ILE A 65 ? 0.2390 0.3848 0.2830 0.0045 0.0262 -0.0084 90 ILE A CD1 518 N N . ARG A 66 ? 0.3804 0.5094 0.3567 -0.0056 0.0362 0.0112 91 ARG A N 519 C CA . ARG A 66 ? 0.4808 0.5971 0.4401 -0.0067 0.0331 0.0160 91 ARG A CA 520 C C . ARG A 66 ? 0.4940 0.6102 0.4333 -0.0046 0.0372 0.0161 91 ARG A C 521 O O . ARG A 66 ? 0.5460 0.6514 0.4701 -0.0020 0.0326 0.0167 91 ARG A O 522 C CB . ARG A 66 ? 0.5664 0.6766 0.5257 -0.0144 0.0339 0.0249 91 ARG A CB 523 C CG . ARG A 66 ? 0.5409 0.6475 0.5156 -0.0157 0.0286 0.0250 91 ARG A CG 524 C CD . ARG A 66 ? 0.6178 0.7122 0.5861 -0.0205 0.0259 0.0325 91 ARG A CD 525 N NE . ARG A 66 ? 0.4822 0.5655 0.4337 -0.0175 0.0218 0.0335 91 ARG A NE 526 C CZ . ARG A 66 ? 0.4481 0.5194 0.3892 -0.0205 0.0195 0.0399 91 ARG A CZ 527 N NH1 . ARG A 66 ? 0.4499 0.5113 0.3759 -0.0168 0.0150 0.0402 91 ARG A NH1 528 N NH2 . ARG A 66 ? 0.4695 0.5383 0.4153 -0.0271 0.0213 0.0458 91 ARG A NH2 529 N N . LYS A 67 ? 0.4226 0.5509 0.3618 -0.0055 0.0458 0.0153 92 LYS A N 530 C CA . LYS A 67 ? 0.4678 0.5969 0.3874 -0.0032 0.0508 0.0150 92 LYS A CA 531 C C . LYS A 67 ? 0.5186 0.6453 0.4318 0.0060 0.0454 0.0061 92 LYS A C 532 O O . LYS A 67 ? 0.5269 0.6508 0.4210 0.0094 0.0470 0.0050 92 LYS A O 533 C CB . LYS A 67 ? 0.5039 0.6487 0.4274 -0.0060 0.0620 0.0154 92 LYS A CB 534 C CG . LYS A 67 ? 0.5688 0.7154 0.4942 -0.0159 0.0683 0.0248 92 LYS A CG 535 C CD . LYS A 67 ? 0.7089 0.8739 0.6424 -0.0186 0.0793 0.0242 92 LYS A CD 536 C CE . LYS A 67 ? 0.8189 0.9853 0.7524 -0.0294 0.0858 0.0339 92 LYS A CE 537 N NZ . LYS A 67 ? 0.8543 1.0143 0.8011 -0.0346 0.0797 0.0380 92 LYS A NZ 538 N N . GLY A 68 ? 0.5001 0.6272 0.4288 0.0099 0.0387 -0.0001 93 GLY A N 539 C CA . GLY A 68 ? 0.4129 0.5368 0.3380 0.0179 0.0322 -0.0089 93 GLY A CA 540 C C . GLY A 68 ? 0.4507 0.5623 0.3769 0.0191 0.0218 -0.0092 93 GLY A C 541 O O . GLY A 68 ? 0.5838 0.6881 0.5091 0.0145 0.0198 -0.0023 93 GLY A O 542 N N . SER A 69 ? 0.4427 0.5524 0.3712 0.0255 0.0151 -0.0176 94 SER A N 543 C CA . SER A 69 ? 0.5682 0.6686 0.5013 0.0267 0.0054 -0.0191 94 SER A CA 544 C C . SER A 69 ? 0.6211 0.7249 0.5750 0.0278 0.0022 -0.0248 94 SER A C 545 O O . SER A 69 ? 0.6768 0.7806 0.6331 0.0330 -0.0023 -0.0330 94 SER A O 546 C CB . SER A 69 ? 0.6833 0.7768 0.6007 0.0326 -0.0011 -0.0238 94 SER A CB 547 O OG . SER A 69 ? 0.8535 0.9516 0.7705 0.0386 -0.0017 -0.0330 94 SER A OG 548 N N . TRP A 70 ? 0.4435 0.5493 0.4115 0.0227 0.0044 -0.0202 95 TRP A N 549 C CA . TRP A 70 ? 0.3826 0.4905 0.3694 0.0230 0.0019 -0.0242 95 TRP A CA 550 C C . TRP A 70 ? 0.3232 0.4248 0.3193 0.0186 -0.0016 -0.0193 95 TRP A C 551 O O . TRP A 70 ? 0.4352 0.5337 0.4262 0.0143 0.0002 -0.0119 95 TRP A O 552 C CB . TRP A 70 ? 0.3805 0.4985 0.3763 0.0217 0.0089 -0.0240 95 TRP A CB 553 C CG . TRP A 70 ? 0.4109 0.5369 0.3994 0.0261 0.0137 -0.0289 95 TRP A CG 554 C CD1 . TRP A 70 ? 0.3863 0.5196 0.3658 0.0245 0.0218 -0.0254 95 TRP A CD1 555 C CD2 . TRP A 70 ? 0.3755 0.5031 0.3652 0.0329 0.0111 -0.0384 95 TRP A CD2 556 N NE1 . TRP A 70 ? 0.4697 0.6098 0.4444 0.0303 0.0249 -0.0324 95 TRP A NE1 557 C CE2 . TRP A 70 ? 0.4066 0.5428 0.3870 0.0358 0.0180 -0.0406 95 TRP A CE2 558 C CE3 . TRP A 70 ? 0.3802 0.5023 0.3775 0.0366 0.0037 -0.0454 95 TRP A CE3 559 C CZ2 . TRP A 70 ? 0.3756 0.5149 0.3538 0.0430 0.0175 -0.0498 95 TRP A CZ2 560 C CZ3 . TRP A 70 ? 0.4469 0.5713 0.4422 0.0432 0.0026 -0.0543 95 TRP A CZ3 561 C CH2 . TRP A 70 ? 0.4896 0.6223 0.4751 0.0467 0.0093 -0.0567 95 TRP A CH2 562 N N . THR A 71 ? 0.2776 0.3769 0.2870 0.0196 -0.0063 -0.0234 96 THR A N 563 C CA . THR A 71 ? 0.2466 0.3414 0.2667 0.0154 -0.0081 -0.0190 96 THR A CA 564 C C . THR A 71 ? 0.2539 0.3537 0.2854 0.0129 -0.0039 -0.0174 96 THR A C 565 O O . THR A 71 ? 0.2721 0.3764 0.3099 0.0158 -0.0031 -0.0227 96 THR A O 566 C CB . THR A 71 ? 0.2272 0.3167 0.2557 0.0171 -0.0150 -0.0237 96 THR A CB 567 O OG1 . THR A 71 ? 0.3286 0.4142 0.3472 0.0196 -0.0198 -0.0254 96 THR A OG1 568 C CG2 . THR A 71 ? 0.2491 0.3343 0.2880 0.0128 -0.0158 -0.0192 96 THR A CG2 569 N N . ILE A 72 ? 0.2152 0.3138 0.2489 0.0079 -0.0014 -0.0103 97 ILE A N 570 C CA . ILE A 72 ? 0.2072 0.3101 0.2518 0.0054 0.0017 -0.0086 97 ILE A CA 571 C C . ILE A 72 ? 0.1940 0.2915 0.2508 0.0052 -0.0023 -0.0100 97 ILE A C 572 O O . ILE A 72 ? 0.2101 0.3002 0.2672 0.0037 -0.0057 -0.0081 97 ILE A O 573 C CB . ILE A 72 ? 0.1897 0.2931 0.2313 -0.0002 0.0055 -0.0005 97 ILE A CB 574 C CG1 . ILE A 72 ? 0.2589 0.3694 0.2904 -0.0008 0.0111 0.0010 97 ILE A CG1 575 C CG2 . ILE A 72 ? 0.2236 0.3295 0.2776 -0.0029 0.0068 0.0013 97 ILE A CG2 576 C CD1 . ILE A 72 ? 0.2749 0.3848 0.3019 -0.0070 0.0148 0.0091 97 ILE A CD1 577 N N . ARG A 73 ? 0.1746 0.2754 0.2408 0.0070 -0.0019 -0.0135 98 ARG A N 578 C CA . ARG A 73 ? 0.1810 0.2759 0.2578 0.0061 -0.0048 -0.0138 98 ARG A CA 579 C C . ARG A 73 ? 0.1931 0.2917 0.2771 0.0045 -0.0023 -0.0113 98 ARG A C 580 O O . ARG A 73 ? 0.2394 0.3459 0.3261 0.0072 -0.0001 -0.0144 98 ARG A O 581 C CB . ARG A 73 ? 0.1902 0.2824 0.2716 0.0103 -0.0086 -0.0212 98 ARG A CB 582 C CG . ARG A 73 ? 0.1678 0.2546 0.2456 0.0111 -0.0127 -0.0237 98 ARG A CG 583 C CD . ARG A 73 ? 0.1766 0.2561 0.2593 0.0072 -0.0146 -0.0196 98 ARG A CD 584 N NE . ARG A 73 ? 0.1876 0.2634 0.2688 0.0076 -0.0184 -0.0215 98 ARG A NE 585 C CZ . ARG A 73 ? 0.1866 0.2619 0.2605 0.0066 -0.0188 -0.0182 98 ARG A CZ 586 N NH1 . ARG A 73 ? 0.2136 0.2909 0.2800 0.0049 -0.0154 -0.0126 98 ARG A NH1 587 N NH2 . ARG A 73 ? 0.2151 0.2878 0.2895 0.0075 -0.0230 -0.0207 98 ARG A NH2 588 N N . LEU A 74 ? 0.1534 0.2465 0.2402 0.0005 -0.0030 -0.0060 99 LEU A N 589 C CA . LEU A 74 ? 0.1594 0.2546 0.2528 -0.0012 -0.0018 -0.0033 99 LEU A CA 590 C C . LEU A 74 ? 0.1518 0.2402 0.2529 0.0004 -0.0052 -0.0055 99 LEU A C 591 O O . LEU A 74 ? 0.1734 0.2527 0.2744 -0.0006 -0.0076 -0.0050 99 LEU A O 592 C CB . LEU A 74 ? 0.1591 0.2510 0.2493 -0.0065 -0.0009 0.0040 99 LEU A CB 593 C CG . LEU A 74 ? 0.1933 0.2888 0.2742 -0.0091 0.0021 0.0074 99 LEU A CG 594 C CD1 . LEU A 74 ? 0.1985 0.2874 0.2758 -0.0141 0.0018 0.0142 99 LEU A CD1 595 C CD2 . LEU A 74 ? 0.2402 0.3478 0.3225 -0.0090 0.0064 0.0066 99 LEU A CD2 596 N N . ARG A 75 ? 0.1554 0.2479 0.2632 0.0028 -0.0052 -0.0078 100 ARG A N 597 C CA . ARG A 75 ? 0.1334 0.2178 0.2472 0.0042 -0.0085 -0.0090 100 ARG A CA 598 C C . ARG A 75 ? 0.1289 0.2154 0.2478 0.0035 -0.0087 -0.0064 100 ARG A C 599 O O . ARG A 75 ? 0.1472 0.2445 0.2697 0.0051 -0.0069 -0.0077 100 ARG A O 600 C CB . ARG A 75 ? 0.1527 0.2366 0.2696 0.0096 -0.0105 -0.0163 100 ARG A CB 601 C CG . ARG A 75 ? 0.1579 0.2307 0.2794 0.0107 -0.0143 -0.0174 100 ARG A CG 602 C CD . ARG A 75 ? 0.1452 0.2154 0.2687 0.0155 -0.0167 -0.0246 100 ARG A CD 603 N NE . ARG A 75 ? 0.1725 0.2517 0.2990 0.0210 -0.0162 -0.0295 100 ARG A NE 604 C CZ . ARG A 75 ? 0.2036 0.2814 0.3312 0.0262 -0.0183 -0.0366 100 ARG A CZ 605 N NH1 . ARG A 75 ? 0.2079 0.2947 0.3384 0.0317 -0.0174 -0.0411 100 ARG A NH1 606 N NH2 . ARG A 75 ? 0.1881 0.2559 0.3146 0.0259 -0.0213 -0.0393 100 ARG A NH2 607 N N . SER A 76 ? 0.1268 0.2030 0.2460 0.0012 -0.0110 -0.0027 101 SER A N 608 C CA A SER A 76 ? 0.1505 0.2262 0.2737 0.0009 -0.0126 -0.0003 101 SER A CA 609 C CA B SER A 76 ? 0.1471 0.2230 0.2704 0.0010 -0.0126 -0.0004 101 SER A CA 610 C C . SER A 76 ? 0.1362 0.2035 0.2631 0.0048 -0.0163 -0.0033 101 SER A C 611 O O . SER A 76 ? 0.1852 0.2576 0.3173 0.0095 -0.0174 -0.0078 101 SER A O 612 C CB A SER A 76 ? 0.1183 0.1869 0.2370 -0.0042 -0.0127 0.0063 101 SER A CB 613 C CB B SER A 76 ? 0.1392 0.2088 0.2582 -0.0041 -0.0126 0.0062 101 SER A CB 614 O OG A SER A 76 ? 0.1353 0.2005 0.2567 -0.0043 -0.0154 0.0084 101 SER A OG 615 O OG B SER A 76 ? 0.1292 0.2070 0.2457 -0.0075 -0.0097 0.0090 101 SER A OG 616 N N . GLY A 77 ? 0.1284 0.1822 0.2520 0.0029 -0.0179 -0.0008 102 GLY A N 617 C CA . GLY A 77 ? 0.1425 0.1858 0.2678 0.0058 -0.0213 -0.0029 102 GLY A CA 618 C C . GLY A 77 ? 0.1557 0.1938 0.2812 0.0073 -0.0217 -0.0073 102 GLY A C 619 O O . GLY A 77 ? 0.1718 0.2016 0.2990 0.0101 -0.0246 -0.0098 102 GLY A O 620 N N . GLY A 78 ? 0.1420 0.1841 0.2655 0.0054 -0.0195 -0.0081 103 GLY A N 621 C CA . GLY A 78 ? 0.1368 0.1752 0.2612 0.0066 -0.0205 -0.0128 103 GLY A CA 622 C C . GLY A 78 ? 0.1652 0.1904 0.2892 0.0035 -0.0215 -0.0110 103 GLY A C 623 O O . GLY A 78 ? 0.1845 0.2046 0.3107 0.0043 -0.0232 -0.0151 103 GLY A O 624 N N . HIS A 79 ? 0.1565 0.1761 0.2776 -0.0003 -0.0202 -0.0050 104 HIS A N 625 C CA . HIS A 79 ? 0.1592 0.1666 0.2797 -0.0035 -0.0201 -0.0028 104 HIS A CA 626 C C . HIS A 79 ? 0.1703 0.1788 0.2913 -0.0070 -0.0180 -0.0025 104 HIS A C 627 O O . HIS A 79 ? 0.1764 0.1764 0.2982 -0.0101 -0.0172 -0.0009 104 HIS A O 628 C CB . HIS A 79 ? 0.1563 0.1555 0.2726 -0.0053 -0.0197 0.0031 104 HIS A CB 629 C CG . HIS A 79 ? 0.1822 0.1721 0.2982 -0.0026 -0.0227 0.0027 104 HIS A CG 630 N ND1 . HIS A 79 ? 0.2119 0.1879 0.3266 -0.0041 -0.0233 0.0036 104 HIS A ND1 631 C CD2 . HIS A 79 ? 0.1986 0.1912 0.3157 0.0016 -0.0256 0.0013 104 HIS A CD2 632 C CE1 . HIS A 79 ? 0.2184 0.1873 0.3320 -0.0006 -0.0267 0.0030 104 HIS A CE1 633 N NE2 . HIS A 79 ? 0.2174 0.1968 0.3330 0.0033 -0.0284 0.0013 104 HIS A NE2 634 N N . SER A 80 ? 0.1494 0.1683 0.2700 -0.0065 -0.0173 -0.0040 105 SER A N 635 C CA . SER A 80 ? 0.1499 0.1705 0.2713 -0.0090 -0.0163 -0.0042 105 SER A CA 636 C C . SER A 80 ? 0.1729 0.1867 0.2997 -0.0105 -0.0173 -0.0072 105 SER A C 637 O O . SER A 80 ? 0.1692 0.1820 0.2991 -0.0084 -0.0198 -0.0123 105 SER A O 638 C CB . SER A 80 ? 0.1457 0.1768 0.2659 -0.0068 -0.0169 -0.0077 105 SER A CB 639 O OG . SER A 80 ? 0.1749 0.2072 0.2966 -0.0084 -0.0170 -0.0086 105 SER A OG 640 N N . TYR A 81 ? 0.1558 0.1651 0.2840 -0.0144 -0.0153 -0.0042 106 TYR A N 641 C CA . TYR A 81 ? 0.1691 0.1724 0.3036 -0.0170 -0.0155 -0.0064 106 TYR A CA 642 C C . TYR A 81 ? 0.1805 0.1902 0.3203 -0.0160 -0.0183 -0.0128 106 TYR A C 643 O O . TYR A 81 ? 0.2534 0.2585 0.3990 -0.0175 -0.0200 -0.0164 106 TYR A O 644 C CB . TYR A 81 ? 0.2239 0.2235 0.3593 -0.0213 -0.0119 -0.0021 106 TYR A CB 645 C CG . TYR A 81 ? 0.2290 0.2192 0.3585 -0.0227 -0.0093 0.0038 106 TYR A CG 646 C CD1 . TYR A 81 ? 0.2158 0.1990 0.3414 -0.0207 -0.0111 0.0046 106 TYR A CD1 647 C CD2 . TYR A 81 ? 0.2537 0.2416 0.3813 -0.0256 -0.0054 0.0083 106 TYR A CD2 648 C CE1 . TYR A 81 ? 0.2368 0.2106 0.3560 -0.0217 -0.0095 0.0098 106 TYR A CE1 649 C CE2 . TYR A 81 ? 0.2426 0.2209 0.3633 -0.0266 -0.0032 0.0135 106 TYR A CE2 650 C CZ . TYR A 81 ? 0.2772 0.2482 0.3933 -0.0247 -0.0056 0.0143 106 TYR A CZ 651 O OH . TYR A 81 ? 0.3286 0.2893 0.4368 -0.0254 -0.0042 0.0194 106 TYR A OH 652 N N . GLU A 82 ? 0.1638 0.1832 0.3009 -0.0137 -0.0191 -0.0141 107 GLU A N 653 C CA . GLU A 82 ? 0.1709 0.1967 0.3113 -0.0122 -0.0222 -0.0200 107 GLU A CA 654 C C . GLU A 82 ? 0.1903 0.2213 0.3258 -0.0074 -0.0244 -0.0239 107 GLU A C 655 O O . GLU A 82 ? 0.1954 0.2323 0.3302 -0.0052 -0.0270 -0.0284 107 GLU A O 656 C CB . GLU A 82 ? 0.2024 0.2345 0.3428 -0.0131 -0.0216 -0.0185 107 GLU A CB 657 C CG . GLU A 82 ? 0.2259 0.2550 0.3725 -0.0175 -0.0190 -0.0156 107 GLU A CG 658 C CD . GLU A 82 ? 0.2608 0.2896 0.4179 -0.0199 -0.0211 -0.0205 107 GLU A CD 659 O OE1 . GLU A 82 ? 0.2607 0.2881 0.4201 -0.0188 -0.0246 -0.0258 107 GLU A OE1 660 O OE2 . GLU A 82 ? 0.2601 0.2902 0.4237 -0.0231 -0.0192 -0.0193 107 GLU A OE2 661 N N . GLY A 83 ? 0.1812 0.2104 0.3133 -0.0054 -0.0235 -0.0225 108 GLY A N 662 C CA . GLY A 83 ? 0.2139 0.2487 0.3424 -0.0006 -0.0248 -0.0264 108 GLY A CA 663 C C . GLY A 83 ? 0.1702 0.2148 0.2923 0.0010 -0.0236 -0.0256 108 GLY A C 664 O O . GLY A 83 ? 0.1914 0.2415 0.3102 0.0048 -0.0246 -0.0300 108 GLY A O 665 N N . LEU A 84 ? 0.1696 0.2154 0.2890 -0.0017 -0.0213 -0.0199 109 LEU A N 666 C CA . LEU A 84 ? 0.1944 0.2474 0.3069 -0.0007 -0.0205 -0.0186 109 LEU A CA 667 C C . LEU A 84 ? 0.1859 0.2447 0.2928 0.0010 -0.0181 -0.0169 109 LEU A C 668 O O . LEU A 84 ? 0.1901 0.2544 0.2902 0.0017 -0.0170 -0.0158 109 LEU A O 669 C CB . LEU A 84 ? 0.1733 0.2248 0.2845 -0.0038 -0.0194 -0.0135 109 LEU A CB 670 C CG . LEU A 84 ? 0.2440 0.2930 0.3615 -0.0053 -0.0214 -0.0157 109 LEU A CG 671 C CD1 . LEU A 84 ? 0.2769 0.3256 0.3927 -0.0073 -0.0201 -0.0111 109 LEU A CD1 672 C CD2 . LEU A 84 ? 0.2919 0.3450 0.4097 -0.0025 -0.0253 -0.0223 109 LEU A CD2 673 N N . SER A 85 ? 0.1507 0.2083 0.2605 0.0017 -0.0172 -0.0166 110 SER A N 674 C CA . SER A 85 ? 0.1516 0.2165 0.2586 0.0033 -0.0149 -0.0157 110 SER A CA 675 C C . SER A 85 ? 0.1564 0.2271 0.2629 0.0082 -0.0155 -0.0223 110 SER A C 676 O O . SER A 85 ? 0.1939 0.2727 0.2982 0.0098 -0.0129 -0.0223 110 SER A O 677 C CB . SER A 85 ? 0.1570 0.2190 0.2678 0.0023 -0.0142 -0.0123 110 SER A CB 678 O OG . SER A 85 ? 0.1645 0.2187 0.2805 0.0035 -0.0166 -0.0151 110 SER A OG 679 N N . TYR A 86 ? 0.1509 0.2179 0.2598 0.0103 -0.0187 -0.0282 111 TYR A N 680 C CA . TYR A 86 ? 0.1744 0.2455 0.2823 0.0156 -0.0196 -0.0352 111 TYR A CA 681 C C . TYR A 86 ? 0.2135 0.2823 0.3198 0.0173 -0.0233 -0.0412 111 TYR A C 682 O O . TYR A 86 ? 0.2055 0.2742 0.3119 0.0217 -0.0254 -0.0480 111 TYR A O 683 C CB . TYR A 86 ? 0.2083 0.2759 0.3224 0.0182 -0.0207 -0.0377 111 TYR A CB 684 C CG . TYR A 86 ? 0.1939 0.2495 0.3136 0.0157 -0.0236 -0.0369 111 TYR A CG 685 C CD1 . TYR A 86 ? 0.2146 0.2633 0.3368 0.0167 -0.0275 -0.0425 111 TYR A CD1 686 C CD2 . TYR A 86 ? 0.1631 0.2137 0.2849 0.0119 -0.0225 -0.0305 111 TYR A CD2 687 C CE1 . TYR A 86 ? 0.1921 0.2295 0.3194 0.0135 -0.0295 -0.0413 111 TYR A CE1 688 C CE2 . TYR A 86 ? 0.2063 0.2454 0.3319 0.0093 -0.0243 -0.0293 111 TYR A CE2 689 C CZ . TYR A 86 ? 0.2052 0.2380 0.3338 0.0098 -0.0275 -0.0346 111 TYR A CZ 690 O OH . TYR A 86 ? 0.2110 0.2321 0.3434 0.0064 -0.0287 -0.0330 111 TYR A OH 691 N N . THR A 87 ? 0.1817 0.2485 0.2866 0.0143 -0.0246 -0.0391 112 THR A N 692 C CA . THR A 87 ? 0.1804 0.2462 0.2836 0.0158 -0.0287 -0.0446 112 THR A CA 693 C C . THR A 87 ? 0.1829 0.2528 0.2787 0.0149 -0.0283 -0.0416 112 THR A C 694 O O . THR A 87 ? 0.2215 0.2921 0.3156 0.0118 -0.0254 -0.0349 112 THR A O 695 C CB . THR A 87 ? 0.1921 0.2499 0.3045 0.0130 -0.0324 -0.0465 112 THR A CB 696 O OG1 . THR A 87 ? 0.2328 0.2884 0.3484 0.0081 -0.0307 -0.0401 112 THR A OG1 697 C CG2 . THR A 87 ? 0.2176 0.2689 0.3361 0.0138 -0.0333 -0.0491 112 THR A CG2 698 N N . SER A 88 ? 0.2273 0.2988 0.3178 0.0179 -0.0317 -0.0469 113 SER A N 699 C CA . SER A 88 ? 0.2444 0.3185 0.3264 0.0180 -0.0325 -0.0449 113 SER A CA 700 C C . SER A 88 ? 0.2803 0.3541 0.3587 0.0217 -0.0382 -0.0525 113 SER A C 701 O O . SER A 88 ? 0.3044 0.3784 0.3814 0.0254 -0.0396 -0.0588 113 SER A O 702 C CB . SER A 88 ? 0.2776 0.3571 0.3486 0.0189 -0.0275 -0.0407 113 SER A CB 703 O OG . SER A 88 ? 0.2723 0.3527 0.3326 0.0198 -0.0288 -0.0392 113 SER A OG 704 N N . ASP A 89 ? 0.3172 0.3905 0.3941 0.0211 -0.0419 -0.0521 114 ASP A N 705 C CA . ASP A 89 ? 0.4051 0.4781 0.4783 0.0247 -0.0483 -0.0593 114 ASP A CA 706 C C . ASP A 89 ? 0.4573 0.5333 0.5136 0.0293 -0.0476 -0.0603 114 ASP A C 707 O O . ASP A 89 ? 0.5666 0.6422 0.6168 0.0334 -0.0524 -0.0670 114 ASP A O 708 C CB . ASP A 89 ? 0.4879 0.5601 0.5670 0.0229 -0.0532 -0.0590 114 ASP A CB 709 C CG . ASP A 89 ? 0.7234 0.7929 0.8194 0.0191 -0.0553 -0.0613 114 ASP A CG 710 O OD1 . ASP A 89 ? 0.6079 0.6745 0.7093 0.0186 -0.0545 -0.0643 114 ASP A OD1 711 O OD2 . ASP A 89 ? 0.8843 0.9543 0.9880 0.0167 -0.0576 -0.0602 114 ASP A OD2 712 N N . THR A 90 ? 0.2827 0.3308 0.3295 0.0283 -0.0452 -0.0249 115 THR A N 713 C CA . THR A 90 ? 0.3005 0.3566 0.3369 0.0286 -0.0430 -0.0250 115 THR A CA 714 C C . THR A 90 ? 0.3033 0.3655 0.3386 0.0295 -0.0398 -0.0302 115 THR A C 715 O O . THR A 90 ? 0.3064 0.3654 0.3480 0.0289 -0.0379 -0.0307 115 THR A O 716 C CB . THR A 90 ? 0.3061 0.3613 0.3376 0.0256 -0.0393 -0.0164 115 THR A CB 717 O OG1 . THR A 90 ? 0.3330 0.3844 0.3690 0.0233 -0.0348 -0.0132 115 THR A OG1 718 C CG2 . THR A 90 ? 0.3549 0.4047 0.3880 0.0256 -0.0430 -0.0119 115 THR A CG2 719 N N . PRO A 91 ? 0.2694 0.3411 0.2967 0.0310 -0.0392 -0.0343 116 PRO A N 720 C CA . PRO A 91 ? 0.3209 0.4007 0.3475 0.0321 -0.0360 -0.0400 116 PRO A CA 721 C C . PRO A 91 ? 0.2923 0.3711 0.3211 0.0288 -0.0302 -0.0350 116 PRO A C 722 O O . PRO A 91 ? 0.2883 0.3655 0.3130 0.0252 -0.0270 -0.0272 116 PRO A O 723 C CB . PRO A 91 ? 0.3720 0.4631 0.3873 0.0324 -0.0345 -0.0417 116 PRO A CB 724 C CG . PRO A 91 ? 0.3267 0.4148 0.3390 0.0338 -0.0401 -0.0414 116 PRO A CG 725 C CD . PRO A 91 ? 0.3210 0.3974 0.3396 0.0319 -0.0418 -0.0344 116 PRO A CD 726 N N . PHE A 92 ? 0.2511 0.3302 0.2864 0.0301 -0.0294 -0.0396 117 PHE A N 727 C CA . PHE A 92 ? 0.2490 0.3259 0.2875 0.0270 -0.0247 -0.0351 117 PHE A CA 728 C C . PHE A 92 ? 0.2555 0.3407 0.2962 0.0284 -0.0220 -0.0410 117 PHE A C 729 O O . PHE A 92 ? 0.2595 0.3497 0.3016 0.0326 -0.0247 -0.0496 117 PHE A O 730 C CB . PHE A 92 ? 0.2517 0.3165 0.2984 0.0261 -0.0267 -0.0315 117 PHE A CB 731 C CG . PHE A 92 ? 0.2114 0.2715 0.2654 0.0293 -0.0314 -0.0377 117 PHE A CG 732 C CD1 . PHE A 92 ? 0.2265 0.2837 0.2866 0.0293 -0.0306 -0.0389 117 PHE A CD1 733 C CD2 . PHE A 92 ? 0.2573 0.3152 0.3123 0.0320 -0.0372 -0.0419 117 PHE A CD2 734 C CE1 . PHE A 92 ? 0.2326 0.2840 0.2989 0.0319 -0.0357 -0.0438 117 PHE A CE1 735 C CE2 . PHE A 92 ? 0.2732 0.3253 0.3349 0.0343 -0.0421 -0.0471 117 PHE A CE2 736 C CZ . PHE A 92 ? 0.2609 0.3095 0.3281 0.0342 -0.0414 -0.0477 117 PHE A CZ 737 N N . ILE A 93 ? 0.2534 0.3403 0.2945 0.0249 -0.0168 -0.0368 118 ILE A N 738 C CA . ILE A 93 ? 0.2117 0.3063 0.2561 0.0257 -0.0140 -0.0417 118 ILE A CA 739 C C . ILE A 93 ? 0.2027 0.2880 0.2551 0.0250 -0.0144 -0.0395 118 ILE A C 740 O O . ILE A 93 ? 0.2298 0.3077 0.2824 0.0213 -0.0126 -0.0320 118 ILE A O 741 C CB . ILE A 93 ? 0.2241 0.3296 0.2624 0.0216 -0.0075 -0.0385 118 ILE A CB 742 C CG1 . ILE A 93 ? 0.2538 0.3690 0.2825 0.0216 -0.0068 -0.0398 118 ILE A CG1 743 C CG2 . ILE A 93 ? 0.2622 0.3770 0.3053 0.0223 -0.0046 -0.0440 118 ILE A CG2 744 C CD1 . ILE A 93 ? 0.3102 0.4350 0.3393 0.0271 -0.0094 -0.0508 118 ILE A CD1 745 N N . LEU A 94 ? 0.2029 0.2882 0.2618 0.0287 -0.0172 -0.0463 119 LEU A N 746 C CA . LEU A 94 ? 0.1933 0.2701 0.2590 0.0281 -0.0181 -0.0446 119 LEU A CA 747 C C . LEU A 94 ? 0.1932 0.2777 0.2607 0.0266 -0.0134 -0.0451 119 LEU A C 748 O O . LEU A 94 ? 0.2119 0.3070 0.2807 0.0294 -0.0130 -0.0522 119 LEU A O 749 C CB . LEU A 94 ? 0.1868 0.2576 0.2583 0.0327 -0.0246 -0.0508 119 LEU A CB 750 C CG . LEU A 94 ? 0.2327 0.2959 0.3108 0.0326 -0.0261 -0.0500 119 LEU A CG 751 C CD1 . LEU A 94 ? 0.2743 0.3277 0.3524 0.0280 -0.0246 -0.0412 119 LEU A CD1 752 C CD2 . LEU A 94 ? 0.2439 0.3007 0.3269 0.0370 -0.0334 -0.0561 119 LEU A CD2 753 N N . ILE A 95 ? 0.1986 0.2785 0.2663 0.0221 -0.0101 -0.0380 120 ILE A N 754 C CA . ILE A 95 ? 0.1808 0.2663 0.2511 0.0201 -0.0062 -0.0381 120 ILE A CA 755 C C . ILE A 95 ? 0.1895 0.2663 0.2666 0.0215 -0.0092 -0.0387 120 ILE A C 756 O O . ILE A 95 ? 0.1939 0.2605 0.2717 0.0190 -0.0094 -0.0330 120 ILE A O 757 C CB . ILE A 95 ? 0.1887 0.2741 0.2549 0.0142 -0.0009 -0.0301 120 ILE A CB 758 C CG1 . ILE A 95 ? 0.2303 0.3223 0.2885 0.0124 0.0014 -0.0280 120 ILE A CG1 759 C CG2 . ILE A 95 ? 0.2083 0.3008 0.2778 0.0118 0.0030 -0.0308 120 ILE A CG2 760 C CD1 . ILE A 95 ? 0.2324 0.3223 0.2860 0.0064 0.0055 -0.0195 120 ILE A CD1 761 N N . ASP A 96 ? 0.1914 0.2726 0.2733 0.0256 -0.0119 -0.0461 121 ASP A N 762 C CA . ASP A 96 ? 0.1946 0.2679 0.2824 0.0273 -0.0157 -0.0472 121 ASP A CA 763 C C . ASP A 96 ? 0.1965 0.2749 0.2871 0.0251 -0.0121 -0.0466 121 ASP A C 764 O O . ASP A 96 ? 0.2114 0.3026 0.3032 0.0259 -0.0094 -0.0511 121 ASP A O 765 C CB . ASP A 96 ? 0.2421 0.3160 0.3338 0.0335 -0.0217 -0.0557 121 ASP A CB 766 C CG . ASP A 96 ? 0.4046 0.4671 0.5012 0.0351 -0.0271 -0.0557 121 ASP A CG 767 O OD1 . ASP A 96 ? 0.2633 0.3252 0.3623 0.0335 -0.0257 -0.0539 121 ASP A OD1 768 O OD2 . ASP A 96 ? 0.5199 0.5738 0.6175 0.0376 -0.0330 -0.0575 121 ASP A OD2 769 N N . LEU A 97 ? 0.1724 0.2416 0.2644 0.0224 -0.0121 -0.0413 122 LEU A N 770 C CA . LEU A 97 ? 0.1670 0.2397 0.2611 0.0194 -0.0086 -0.0396 122 LEU A CA 771 C C . LEU A 97 ? 0.1811 0.2530 0.2812 0.0226 -0.0125 -0.0441 122 LEU A C 772 O O . LEU A 97 ? 0.1904 0.2631 0.2926 0.0202 -0.0107 -0.0424 122 LEU A O 773 C CB . LEU A 97 ? 0.1659 0.2296 0.2574 0.0145 -0.0061 -0.0315 122 LEU A CB 774 C CG . LEU A 97 ? 0.1944 0.2576 0.2803 0.0116 -0.0031 -0.0266 122 LEU A CG 775 C CD1 . LEU A 97 ? 0.2433 0.2963 0.3279 0.0081 -0.0020 -0.0196 122 LEU A CD1 776 C CD2 . LEU A 97 ? 0.2753 0.3504 0.3587 0.0090 0.0019 -0.0268 122 LEU A CD2 777 N N . MET A 98 ? 0.1964 0.2664 0.2991 0.0279 -0.0182 -0.0498 123 MET A N 778 C CA . MET A 98 ? 0.2100 0.2769 0.3181 0.0313 -0.0233 -0.0536 123 MET A CA 779 C C . MET A 98 ? 0.2427 0.3215 0.3553 0.0320 -0.0212 -0.0579 123 MET A C 780 O O . MET A 98 ? 0.2475 0.3229 0.3638 0.0330 -0.0242 -0.0585 123 MET A O 781 C CB . MET A 98 ? 0.2267 0.2897 0.3372 0.0373 -0.0305 -0.0596 123 MET A CB 782 C CG . MET A 98 ? 0.2519 0.3275 0.3635 0.0415 -0.0301 -0.0677 123 MET A CG 783 S SD . MET A 98 ? 0.3247 0.3951 0.4409 0.0495 -0.0399 -0.0764 123 MET A SD 784 C CE . MET A 98 ? 0.7605 0.8375 0.8727 0.0513 -0.0387 -0.0805 123 MET A CE 785 N N . ASN A 99 ? 0.1818 0.2751 0.2943 0.0312 -0.0162 -0.0608 124 ASN A N 786 C CA . ASN A 99 ? 0.2100 0.3166 0.3275 0.0311 -0.0136 -0.0649 124 ASN A CA 787 C C . ASN A 99 ? 0.2186 0.3247 0.3351 0.0246 -0.0087 -0.0584 124 ASN A C 788 O O . ASN A 99 ? 0.2651 0.3802 0.3863 0.0238 -0.0071 -0.0610 124 ASN A O 789 C CB . ASN A 99 ? 0.2329 0.3567 0.3507 0.0323 -0.0099 -0.0708 124 ASN A CB 790 C CG . ASN A 99 ? 0.2826 0.4096 0.4036 0.0400 -0.0153 -0.0800 124 ASN A CG 791 O OD1 . ASN A 99 ? 0.3213 0.4389 0.4460 0.0447 -0.0223 -0.0827 124 ASN A OD1 792 N ND2 . ASN A 99 ? 0.2941 0.4343 0.4135 0.0413 -0.0124 -0.0849 124 ASN A ND2 793 N N . LEU A 100 ? 0.1794 0.2752 0.2902 0.0201 -0.0066 -0.0504 125 LEU A N 794 C CA . LEU A 100 ? 0.1994 0.2923 0.3091 0.0143 -0.0028 -0.0443 125 LEU A CA 795 C C . LEU A 100 ? 0.1928 0.2726 0.3033 0.0147 -0.0069 -0.0416 125 LEU A C 796 O O . LEU A 100 ? 0.1851 0.2541 0.2916 0.0121 -0.0064 -0.0355 125 LEU A O 797 C CB . LEU A 100 ? 0.2152 0.3048 0.3184 0.0095 0.0016 -0.0375 125 LEU A CB 798 C CG . LEU A 100 ? 0.2291 0.3310 0.3297 0.0083 0.0057 -0.0390 125 LEU A CG 799 C CD1 . LEU A 100 ? 0.2759 0.3725 0.3697 0.0037 0.0090 -0.0317 125 LEU A CD1 800 C CD2 . LEU A 100 ? 0.2441 0.3605 0.3487 0.0060 0.0094 -0.0422 125 LEU A CD2 801 N N . ASN A 101 ? 0.1995 0.2808 0.3151 0.0183 -0.0110 -0.0463 126 ASN A N 802 C CA . ASN A 101 ? 0.2453 0.3144 0.3609 0.0188 -0.0156 -0.0439 126 ASN A CA 803 C C . ASN A 101 ? 0.2439 0.3160 0.3630 0.0175 -0.0156 -0.0446 126 ASN A C 804 O O . ASN A 101 ? 0.2418 0.3073 0.3622 0.0196 -0.0208 -0.0451 126 ASN A O 805 C CB . ASN A 101 ? 0.2978 0.3605 0.4147 0.0245 -0.0228 -0.0474 126 ASN A CB 806 C CG . ASN A 101 ? 0.3205 0.3922 0.4439 0.0300 -0.0266 -0.0557 126 ASN A CG 807 O OD1 . ASN A 101 ? 0.2813 0.3671 0.4083 0.0299 -0.0230 -0.0598 126 ASN A OD1 808 N ND2 . ASN A 101 ? 0.3413 0.4050 0.4665 0.0348 -0.0342 -0.0583 126 ASN A ND2 809 N N . ARG A 102 ? 0.2041 0.2860 0.3246 0.0136 -0.0102 -0.0443 127 ARG A N 810 C CA . ARG A 102 ? 0.2187 0.3045 0.3429 0.0116 -0.0098 -0.0451 127 ARG A CA 811 C C . ARG A 102 ? 0.1966 0.2714 0.3168 0.0072 -0.0088 -0.0387 127 ARG A C 812 O O . ARG A 102 ? 0.2160 0.2862 0.3317 0.0033 -0.0048 -0.0336 127 ARG A O 813 C CB . ARG A 102 ? 0.2605 0.3614 0.3881 0.0083 -0.0043 -0.0472 127 ARG A CB 814 C CG . ARG A 102 ? 0.5159 0.6311 0.6488 0.0127 -0.0050 -0.0550 127 ARG A CG 815 C CD . ARG A 102 ? 0.5869 0.7173 0.7213 0.0081 0.0017 -0.0557 127 ARG A CD 816 N NE . ARG A 102 ? 0.5983 0.7427 0.7358 0.0120 0.0022 -0.0626 127 ARG A NE 817 C CZ . ARG A 102 ? 0.5923 0.7355 0.7254 0.0142 0.0024 -0.0629 127 ARG A CZ 818 N NH1 . ARG A 102 ? 0.4085 0.5373 0.5345 0.0128 0.0020 -0.0564 127 ARG A NH1 819 N NH2 . ARG A 102 ? 0.5745 0.7317 0.7105 0.0179 0.0029 -0.0700 127 ARG A NH2 820 N N . VAL A 103 ? 0.1818 0.2527 0.3036 0.0081 -0.0126 -0.0394 128 VAL A N 821 C CA . VAL A 103 ? 0.1808 0.2430 0.2990 0.0043 -0.0118 -0.0347 128 VAL A CA 822 C C . VAL A 103 ? 0.1933 0.2634 0.3161 0.0020 -0.0108 -0.0370 128 VAL A C 823 O O . VAL A 103 ? 0.2388 0.3153 0.3668 0.0053 -0.0145 -0.0420 128 VAL A O 824 C CB . VAL A 103 ? 0.1924 0.2431 0.3075 0.0066 -0.0174 -0.0330 128 VAL A CB 825 C CG1 . VAL A 103 ? 0.2057 0.2495 0.3171 0.0027 -0.0163 -0.0290 128 VAL A CG1 826 C CG2 . VAL A 103 ? 0.2182 0.2612 0.3295 0.0083 -0.0187 -0.0307 128 VAL A CG2 827 N N . SER A 104 ? 0.1826 0.2524 0.3039 -0.0034 -0.0062 -0.0337 129 SER A N 828 C CA A SER A 104 ? 0.1823 0.2589 0.3079 -0.0065 -0.0052 -0.0356 129 SER A CA 829 C CA B SER A 104 ? 0.1794 0.2561 0.3051 -0.0065 -0.0051 -0.0356 129 SER A CA 830 C C . SER A 104 ? 0.1914 0.2585 0.3135 -0.0093 -0.0057 -0.0324 129 SER A C 831 O O . SER A 104 ? 0.2042 0.2651 0.3224 -0.0130 -0.0023 -0.0282 129 SER A O 832 C CB A SER A 104 ? 0.1872 0.2734 0.3151 -0.0112 0.0006 -0.0352 129 SER A CB 833 C CB B SER A 104 ? 0.1822 0.2682 0.3099 -0.0112 0.0007 -0.0351 129 SER A CB 834 O OG A SER A 104 ? 0.2221 0.3141 0.3543 -0.0150 0.0016 -0.0367 129 SER A OG 835 O OG B SER A 104 ? 0.2412 0.3365 0.3710 -0.0088 0.0017 -0.0380 129 SER A OG 836 N N . ILE A 105 ? 0.1644 0.2302 0.2877 -0.0072 -0.0104 -0.0347 130 ILE A N 837 C CA . ILE A 105 ? 0.1826 0.2401 0.3019 -0.0094 -0.0114 -0.0323 130 ILE A CA 838 C C . ILE A 105 ? 0.1809 0.2442 0.3041 -0.0134 -0.0099 -0.0341 130 ILE A C 839 O O . ILE A 105 ? 0.1941 0.2676 0.3239 -0.0126 -0.0114 -0.0385 130 ILE A O 840 C CB . ILE A 105 ? 0.2106 0.2627 0.3277 -0.0054 -0.0178 -0.0332 130 ILE A CB 841 C CG1 . ILE A 105 ? 0.3137 0.3578 0.4261 -0.0026 -0.0194 -0.0305 130 ILE A CG1 842 C CG2 . ILE A 105 ? 0.2114 0.2570 0.3242 -0.0078 -0.0189 -0.0315 130 ILE A CG2 843 C CD1 . ILE A 105 ? 0.3104 0.3498 0.4214 0.0015 -0.0263 -0.0312 130 ILE A CD1 844 N N . ASP A 106 ? 0.1837 0.2409 0.3036 -0.0176 -0.0070 -0.0311 131 ASP A N 845 C CA . ASP A 106 ? 0.1986 0.2594 0.3218 -0.0219 -0.0060 -0.0327 131 ASP A CA 846 C C . ASP A 106 ? 0.1918 0.2450 0.3108 -0.0216 -0.0092 -0.0327 131 ASP A C 847 O O . ASP A 106 ? 0.1911 0.2352 0.3045 -0.0230 -0.0077 -0.0298 131 ASP A O 848 C CB . ASP A 106 ? 0.2070 0.2662 0.3299 -0.0272 -0.0008 -0.0297 131 ASP A CB 849 C CG . ASP A 106 ? 0.2780 0.3404 0.4048 -0.0322 0.0000 -0.0313 131 ASP A CG 850 O OD1 . ASP A 106 ? 0.2622 0.3257 0.3905 -0.0317 -0.0035 -0.0343 131 ASP A OD1 851 O OD2 . ASP A 106 ? 0.3521 0.4155 0.4803 -0.0371 0.0037 -0.0292 131 ASP A OD2 852 N N . LEU A 107 ? 0.1875 0.2449 0.3090 -0.0197 -0.0138 -0.0363 132 LEU A N 853 C CA . LEU A 107 ? 0.1617 0.2127 0.2784 -0.0193 -0.0174 -0.0364 132 LEU A CA 854 C C . LEU A 107 ? 0.2038 0.2534 0.3206 -0.0241 -0.0155 -0.0371 132 LEU A C 855 O O . LEU A 107 ? 0.2396 0.2826 0.3508 -0.0244 -0.0170 -0.0367 132 LEU A O 856 C CB . LEU A 107 ? 0.1811 0.2366 0.3003 -0.0156 -0.0237 -0.0399 132 LEU A CB 857 C CG . LEU A 107 ? 0.1759 0.2293 0.2935 -0.0103 -0.0273 -0.0392 132 LEU A CG 858 C CD1 . LEU A 107 ? 0.2466 0.3053 0.3682 -0.0064 -0.0341 -0.0432 132 LEU A CD1 859 C CD2 . LEU A 107 ? 0.2109 0.2523 0.3188 -0.0098 -0.0279 -0.0345 132 LEU A CD2 860 N N . GLU A 108 ? 0.1808 0.2367 0.3038 -0.0280 -0.0122 -0.0381 133 GLU A N 861 C CA . GLU A 108 ? 0.1995 0.2531 0.3231 -0.0329 -0.0109 -0.0388 133 GLU A CA 862 C C . GLU A 108 ? 0.1942 0.2372 0.3122 -0.0347 -0.0075 -0.0352 133 GLU A C 863 O O . GLU A 108 ? 0.2183 0.2557 0.3338 -0.0367 -0.0078 -0.0361 133 GLU A O 864 C CB . GLU A 108 ? 0.2040 0.2676 0.3362 -0.0373 -0.0089 -0.0407 133 GLU A CB 865 C CG . GLU A 108 ? 0.2666 0.3423 0.4058 -0.0355 -0.0123 -0.0453 133 GLU A CG 866 C CD . GLU A 108 ? 0.6234 0.6967 0.7600 -0.0323 -0.0182 -0.0480 133 GLU A CD 867 O OE1 . GLU A 108 ? 0.7149 0.7880 0.8493 -0.0270 -0.0218 -0.0483 133 GLU A OE1 868 O OE2 . GLU A 108 ? 0.7567 0.8276 0.8928 -0.0353 -0.0194 -0.0496 133 GLU A OE2 869 N N . SER A 109 ? 0.1643 0.2049 0.2805 -0.0336 -0.0045 -0.0317 134 SER A N 870 C CA . SER A 109 ? 0.1809 0.2119 0.2922 -0.0344 -0.0018 -0.0285 134 SER A CA 871 C C . SER A 109 ? 0.1811 0.2063 0.2859 -0.0302 -0.0028 -0.0267 134 SER A C 872 O O . SER A 109 ? 0.2057 0.2235 0.3064 -0.0302 -0.0011 -0.0249 134 SER A O 873 C CB . SER A 109 ? 0.2180 0.2495 0.3312 -0.0367 0.0020 -0.0254 134 SER A CB 874 O OG . SER A 109 ? 0.2477 0.2849 0.3618 -0.0339 0.0023 -0.0246 134 SER A OG 875 N N . GLU A 110 ? 0.1820 0.2106 0.2863 -0.0268 -0.0058 -0.0274 135 GLU A N 876 C CA . GLU A 110 ? 0.1865 0.2099 0.2849 -0.0234 -0.0069 -0.0251 135 GLU A CA 877 C C . GLU A 110 ? 0.1753 0.1954 0.2726 -0.0231 -0.0034 -0.0217 135 GLU A C 878 O O . GLU A 110 ? 0.1944 0.2083 0.2873 -0.0227 -0.0021 -0.0196 135 GLU A O 879 C CB . GLU A 110 ? 0.2166 0.2347 0.3090 -0.0234 -0.0086 -0.0255 135 GLU A CB 880 C CG . GLU A 110 ? 0.2070 0.2287 0.2997 -0.0229 -0.0132 -0.0285 135 GLU A CG 881 C CD . GLU A 110 ? 0.1974 0.2147 0.2831 -0.0230 -0.0152 -0.0290 135 GLU A CD 882 O OE1 . GLU A 110 ? 0.2520 0.2645 0.3334 -0.0240 -0.0124 -0.0280 135 GLU A OE1 883 O OE2 . GLU A 110 ? 0.2680 0.2874 0.3525 -0.0219 -0.0199 -0.0307 135 GLU A OE2 884 N N . THR A 111 ? 0.1780 0.2034 0.2798 -0.0233 -0.0019 -0.0214 136 THR A N 885 C CA . THR A 111 ? 0.1964 0.2201 0.2973 -0.0226 0.0007 -0.0184 136 THR A CA 886 C C . THR A 111 ? 0.2176 0.2482 0.3215 -0.0200 -0.0007 -0.0196 136 THR A C 887 O O . THR A 111 ? 0.1964 0.2333 0.3039 -0.0191 -0.0032 -0.0228 136 THR A O 888 C CB . THR A 111 ? 0.1621 0.1856 0.2651 -0.0264 0.0044 -0.0169 136 THR A CB 889 O OG1 . THR A 111 ? 0.1944 0.2260 0.3025 -0.0290 0.0048 -0.0190 136 THR A OG1 890 C CG2 . THR A 111 ? 0.1993 0.2152 0.2999 -0.0284 0.0053 -0.0164 136 THR A CG2 891 N N . ALA A 112 ? 0.1794 0.2091 0.2822 -0.0186 0.0007 -0.0174 137 ALA A N 892 C CA . ALA A 112 ? 0.1722 0.2087 0.2779 -0.0160 -0.0003 -0.0191 137 ALA A CA 893 C C . ALA A 112 ? 0.1734 0.2110 0.2786 -0.0168 0.0031 -0.0168 137 ALA A C 894 O O . ALA A 112 ? 0.1968 0.2275 0.2984 -0.0175 0.0047 -0.0135 137 ALA A O 895 C CB . ALA A 112 ? 0.2127 0.2459 0.3164 -0.0117 -0.0046 -0.0196 137 ALA A CB 896 N N . TRP A 113 ? 0.1664 0.2133 0.2752 -0.0167 0.0041 -0.0189 138 TRP A N 897 C CA . TRP A 113 ? 0.1653 0.2145 0.2728 -0.0167 0.0066 -0.0172 138 TRP A CA 898 C C . TRP A 113 ? 0.1740 0.2247 0.2816 -0.0116 0.0036 -0.0194 138 TRP A C 899 O O . TRP A 113 ? 0.2107 0.2675 0.3220 -0.0088 0.0008 -0.0238 138 TRP A O 900 C CB . TRP A 113 ? 0.1810 0.2404 0.2916 -0.0201 0.0099 -0.0180 138 TRP A CB 901 C CG . TRP A 113 ? 0.1591 0.2150 0.2682 -0.0257 0.0132 -0.0141 138 TRP A CG 902 C CD1 . TRP A 113 ? 0.1858 0.2431 0.2977 -0.0300 0.0140 -0.0145 138 TRP A CD1 903 C CD2 . TRP A 113 ? 0.1723 0.2221 0.2771 -0.0277 0.0154 -0.0093 138 TRP A CD2 904 N NE1 . TRP A 113 ? 0.2050 0.2566 0.3144 -0.0345 0.0165 -0.0102 138 TRP A NE1 905 C CE2 . TRP A 113 ? 0.1883 0.2352 0.2933 -0.0330 0.0173 -0.0068 138 TRP A CE2 906 C CE3 . TRP A 113 ? 0.2055 0.2516 0.3063 -0.0253 0.0155 -0.0070 138 TRP A CE3 907 C CZ2 . TRP A 113 ? 0.2264 0.2662 0.3277 -0.0358 0.0190 -0.0019 138 TRP A CZ2 908 C CZ3 . TRP A 113 ? 0.2093 0.2494 0.3065 -0.0280 0.0174 -0.0022 138 TRP A CZ3 909 C CH2 . TRP A 113 ? 0.2286 0.2653 0.3260 -0.0331 0.0189 0.0004 138 TRP A CH2 910 N N . VAL A 114 ? 0.1591 0.2040 0.2629 -0.0102 0.0036 -0.0168 139 VAL A N 911 C CA . VAL A 114 ? 0.1779 0.2217 0.2814 -0.0057 0.0002 -0.0185 139 VAL A CA 912 C C . VAL A 114 ? 0.1716 0.2188 0.2737 -0.0050 0.0020 -0.0181 139 VAL A C 913 O O . VAL A 114 ? 0.1686 0.2107 0.2673 -0.0065 0.0039 -0.0141 139 VAL A O 914 C CB . VAL A 114 ? 0.1958 0.2287 0.2958 -0.0049 -0.0021 -0.0156 139 VAL A CB 915 C CG1 . VAL A 114 ? 0.1994 0.2300 0.2991 -0.0008 -0.0064 -0.0172 139 VAL A CG1 916 C CG2 . VAL A 114 ? 0.2057 0.2350 0.3054 -0.0061 -0.0035 -0.0156 139 VAL A CG2 917 N N . GLU A 115 ? 0.1793 0.2359 0.2842 -0.0026 0.0014 -0.0224 140 GLU A N 918 C CA . GLU A 115 ? 0.1736 0.2340 0.2766 -0.0015 0.0028 -0.0226 140 GLU A CA 919 C C . GLU A 115 ? 0.1787 0.2298 0.2788 0.0011 -0.0003 -0.0210 140 GLU A C 920 O O . GLU A 115 ? 0.1717 0.2168 0.2726 0.0036 -0.0044 -0.0219 140 GLU A O 921 C CB . GLU A 115 ? 0.1712 0.2441 0.2781 0.0014 0.0022 -0.0288 140 GLU A CB 922 C CG . GLU A 115 ? 0.1846 0.2693 0.2942 -0.0023 0.0064 -0.0301 140 GLU A CG 923 C CD . GLU A 115 ? 0.1856 0.2849 0.2995 0.0007 0.0064 -0.0369 140 GLU A CD 924 O OE1 . GLU A 115 ? 0.2122 0.3117 0.3287 0.0065 0.0018 -0.0419 140 GLU A OE1 925 O OE2 . GLU A 115 ? 0.2665 0.3772 0.3811 -0.0029 0.0109 -0.0373 140 GLU A OE2 926 N N . SER A 116 ? 0.1633 0.2135 0.2599 0.0004 0.0016 -0.0184 141 SER A N 927 C CA . SER A 116 ? 0.1888 0.2301 0.2828 0.0017 -0.0006 -0.0159 141 SER A CA 928 C C . SER A 116 ? 0.1893 0.2299 0.2844 0.0063 -0.0052 -0.0196 141 SER A C 929 O O . SER A 116 ? 0.1948 0.2277 0.2885 0.0070 -0.0076 -0.0177 141 SER A O 930 C CB . SER A 116 ? 0.2046 0.2453 0.2948 -0.0003 0.0023 -0.0121 141 SER A CB 931 O OG . SER A 116 ? 0.1835 0.2331 0.2727 0.0007 0.0034 -0.0146 141 SER A OG 932 N N . GLY A 117 ? 0.1678 0.2164 0.2659 0.0092 -0.0067 -0.0252 142 GLY A N 933 C CA . GLY A 117 ? 0.1618 0.2085 0.2617 0.0140 -0.0122 -0.0296 142 GLY A CA 934 C C . GLY A 117 ? 0.1724 0.2124 0.2746 0.0155 -0.0168 -0.0303 142 GLY A C 935 O O . GLY A 117 ? 0.2055 0.2407 0.3089 0.0189 -0.0223 -0.0327 142 GLY A O 936 N N . SER A 118 ? 0.1862 0.2255 0.2889 0.0128 -0.0151 -0.0281 143 SER A N 937 C CA . SER A 118 ? 0.1760 0.2088 0.2798 0.0137 -0.0196 -0.0281 143 SER A CA 938 C C . SER A 118 ? 0.1810 0.2022 0.2816 0.0127 -0.0222 -0.0238 143 SER A C 939 O O . SER A 118 ? 0.2050 0.2230 0.3026 0.0096 -0.0189 -0.0194 143 SER A O 940 C CB . SER A 118 ? 0.1877 0.2221 0.2919 0.0104 -0.0168 -0.0263 143 SER A CB 941 O OG . SER A 118 ? 0.2057 0.2515 0.3132 0.0100 -0.0137 -0.0296 143 SER A OG 942 N N . THR A 119 ? 0.1775 0.1924 0.2788 0.0152 -0.0284 -0.0250 144 THR A N 943 C CA . THR A 119 ? 0.1699 0.1739 0.2679 0.0132 -0.0309 -0.0203 144 THR A CA 944 C C . THR A 119 ? 0.1806 0.1807 0.2761 0.0098 -0.0300 -0.0165 144 THR A C 945 O O . THR A 119 ? 0.1833 0.1877 0.2800 0.0099 -0.0290 -0.0181 144 THR A O 946 C CB . THR A 119 ? 0.1777 0.1750 0.2767 0.0165 -0.0386 -0.0223 144 THR A CB 947 O OG1 . THR A 119 ? 0.1929 0.1900 0.2938 0.0189 -0.0428 -0.0250 144 THR A OG1 948 C CG2 . THR A 119 ? 0.1921 0.1932 0.2937 0.0204 -0.0402 -0.0272 144 THR A CG2 949 N N . LEU A 120 ? 0.1691 0.1617 0.2611 0.0068 -0.0302 -0.0117 145 LEU A N 950 C CA . LEU A 120 ? 0.1739 0.1628 0.2626 0.0036 -0.0297 -0.0082 145 LEU A CA 951 C C . LEU A 120 ? 0.1685 0.1547 0.2574 0.0056 -0.0355 -0.0098 145 LEU A C 952 O O . LEU A 120 ? 0.1804 0.1684 0.2683 0.0045 -0.0346 -0.0098 145 LEU A O 953 C CB . LEU A 120 ? 0.1851 0.1674 0.2703 0.0001 -0.0296 -0.0033 145 LEU A CB 954 C CG . LEU A 120 ? 0.1970 0.1817 0.2825 -0.0016 -0.0246 -0.0016 145 LEU A CG 955 C CD1 . LEU A 120 ? 0.1937 0.1739 0.2764 -0.0054 -0.0241 0.0029 145 LEU A CD1 956 C CD2 . LEU A 120 ? 0.2109 0.2017 0.2970 -0.0023 -0.0188 -0.0023 145 LEU A CD2 957 N N . GLY A 121 ? 0.1749 0.1564 0.2649 0.0086 -0.0419 -0.0115 146 GLY A N 958 C CA . GLY A 121 ? 0.1786 0.1565 0.2691 0.0111 -0.0486 -0.0131 146 GLY A CA 959 C C . GLY A 121 ? 0.1886 0.1756 0.2835 0.0142 -0.0478 -0.0184 146 GLY A C 960 O O . GLY A 121 ? 0.1880 0.1747 0.2822 0.0143 -0.0500 -0.0185 146 GLY A O 961 N N . GLU A 122 ? 0.1863 0.1821 0.2856 0.0166 -0.0448 -0.0228 147 GLU A N 962 C CA . GLU A 122 ? 0.1864 0.1929 0.2906 0.0189 -0.0433 -0.0280 147 GLU A CA 963 C C . GLU A 122 ? 0.1853 0.1953 0.2879 0.0148 -0.0382 -0.0256 147 GLU A C 964 O O . GLU A 122 ? 0.1936 0.2079 0.2987 0.0156 -0.0395 -0.0281 147 GLU A O 965 C CB . GLU A 122 ? 0.1715 0.1877 0.2795 0.0210 -0.0397 -0.0323 147 GLU A CB 966 C CG . GLU A 122 ? 0.1757 0.1913 0.2869 0.0265 -0.0454 -0.0374 147 GLU A CG 967 C CD . GLU A 122 ? 0.2022 0.2268 0.3154 0.0278 -0.0414 -0.0409 147 GLU A CD 968 O OE1 . GLU A 122 ? 0.2236 0.2515 0.3342 0.0239 -0.0349 -0.0377 147 GLU A OE1 969 O OE2 . GLU A 122 ? 0.2383 0.2666 0.3553 0.0330 -0.0453 -0.0471 147 GLU A OE2 970 N N . LEU A 123 ? 0.1879 0.1959 0.2868 0.0105 -0.0327 -0.0212 148 LEU A N 971 C CA . LEU A 123 ? 0.1688 0.1786 0.2659 0.0066 -0.0282 -0.0190 148 LEU A CA 972 C C . LEU A 123 ? 0.1746 0.1785 0.2682 0.0055 -0.0318 -0.0170 148 LEU A C 973 O O . LEU A 123 ? 0.1853 0.1930 0.2800 0.0049 -0.0316 -0.0186 148 LEU A O 974 C CB . LEU A 123 ? 0.1883 0.1960 0.2823 0.0030 -0.0227 -0.0149 148 LEU A CB 975 C CG . LEU A 123 ? 0.1722 0.1800 0.2640 -0.0008 -0.0184 -0.0128 148 LEU A CG 976 C CD1 . LEU A 123 ? 0.2228 0.2387 0.3185 -0.0013 -0.0161 -0.0159 148 LEU A CD1 977 C CD2 . LEU A 123 ? 0.2226 0.2282 0.3122 -0.0033 -0.0138 -0.0094 148 LEU A CD2 978 N N . TYR A 124 ? 0.1684 0.1634 0.2576 0.0048 -0.0353 -0.0134 149 TYR A N 979 C CA . TYR A 124 ? 0.1821 0.1711 0.2665 0.0033 -0.0389 -0.0107 149 TYR A CA 980 C C . TYR A 124 ? 0.2044 0.1947 0.2917 0.0070 -0.0452 -0.0144 149 TYR A C 981 O O . TYR A 124 ? 0.2077 0.1984 0.2930 0.0060 -0.0464 -0.0143 149 TYR A O 982 C CB . TYR A 124 ? 0.1919 0.1712 0.2713 0.0017 -0.0421 -0.0060 149 TYR A CB 983 C CG . TYR A 124 ? 0.1961 0.1743 0.2729 -0.0021 -0.0367 -0.0023 149 TYR A CG 984 C CD1 . TYR A 124 ? 0.2018 0.1850 0.2784 -0.0045 -0.0299 -0.0021 149 TYR A CD1 985 C CD2 . TYR A 124 ? 0.1998 0.1718 0.2748 -0.0032 -0.0388 0.0009 149 TYR A CD2 986 C CE1 . TYR A 124 ? 0.2028 0.1853 0.2777 -0.0073 -0.0254 0.0008 149 TYR A CE1 987 C CE2 . TYR A 124 ? 0.1901 0.1623 0.2636 -0.0065 -0.0340 0.0039 149 TYR A CE2 988 C CZ . TYR A 124 ? 0.2041 0.1818 0.2777 -0.0082 -0.0274 0.0037 149 TYR A CZ 989 O OH . TYR A 124 ? 0.2344 0.2126 0.3073 -0.0108 -0.0232 0.0061 149 TYR A OH 990 N N . TYR A 125 ? 0.1913 0.1827 0.2833 0.0116 -0.0494 -0.0182 150 TYR A N 991 C CA . TYR A 125 ? 0.1926 0.1859 0.2886 0.0161 -0.0558 -0.0226 150 TYR A CA 992 C C . TYR A 125 ? 0.1861 0.1907 0.2868 0.0161 -0.0523 -0.0266 150 TYR A C 993 O O . TYR A 125 ? 0.1895 0.1948 0.2904 0.0168 -0.0559 -0.0278 150 TYR A O 994 C CB . TYR A 125 ? 0.1881 0.1821 0.2894 0.0215 -0.0602 -0.0271 150 TYR A CB 995 C CG . TYR A 125 ? 0.1912 0.1879 0.2978 0.0271 -0.0674 -0.0327 150 TYR A CG 996 C CD1 . TYR A 125 ? 0.2263 0.2124 0.3302 0.0292 -0.0764 -0.0311 150 TYR A CD1 997 C CD2 . TYR A 125 ? 0.2211 0.2313 0.3357 0.0302 -0.0653 -0.0396 150 TYR A CD2 998 C CE1 . TYR A 125 ? 0.2498 0.2381 0.3592 0.0350 -0.0838 -0.0366 150 TYR A CE1 999 C CE2 . TYR A 125 ? 0.2409 0.2550 0.3615 0.0359 -0.0720 -0.0455 150 TYR A CE2 1000 C CZ . TYR A 125 ? 0.2468 0.2497 0.3650 0.0386 -0.0814 -0.0441 150 TYR A CZ 1001 O OH . TYR A 125 ? 0.2780 0.2843 0.4026 0.0448 -0.0888 -0.0502 150 TYR A OH 1002 N N . ALA A 126 ? 0.1892 0.2025 0.2933 0.0149 -0.0454 -0.0285 151 ALA A N 1003 C CA . ALA A 126 ? 0.1760 0.2003 0.2848 0.0139 -0.0416 -0.0319 151 ALA A CA 1004 C C . ALA A 126 ? 0.1560 0.1779 0.2607 0.0097 -0.0400 -0.0290 151 ALA A C 1005 O O . ALA A 126 ? 0.1836 0.2110 0.2915 0.0100 -0.0414 -0.0319 151 ALA A O 1006 C CB . ALA A 126 ? 0.1862 0.2183 0.2977 0.0122 -0.0345 -0.0329 151 ALA A CB 1007 N N . ILE A 127 ? 0.1635 0.1780 0.2616 0.0060 -0.0371 -0.0237 152 ILE A N 1008 C CA . ILE A 127 ? 0.1738 0.1861 0.2674 0.0022 -0.0354 -0.0214 152 ILE A CA 1009 C C . ILE A 127 ? 0.2087 0.2168 0.2993 0.0036 -0.0423 -0.0213 152 ILE A C 1010 O O . ILE A 127 ? 0.1988 0.2105 0.2902 0.0029 -0.0431 -0.0232 152 ILE A O 1011 C CB . ILE A 127 ? 0.1586 0.1645 0.2460 -0.0014 -0.0312 -0.0164 152 ILE A CB 1012 C CG1 . ILE A 127 ? 0.1760 0.1859 0.2661 -0.0029 -0.0246 -0.0164 152 ILE A CG1 1013 C CG2 . ILE A 127 ? 0.1935 0.1971 0.2757 -0.0046 -0.0303 -0.0148 152 ILE A CG2 1014 C CD1 . ILE A 127 ? 0.1862 0.1905 0.2717 -0.0052 -0.0213 -0.0122 152 ILE A CD1 1015 N N . THR A 128 ? 0.2103 0.2103 0.2973 0.0054 -0.0477 -0.0189 153 THR A N 1016 C CA A THR A 128 ? 0.2274 0.2216 0.3105 0.0067 -0.0553 -0.0178 153 THR A CA 1017 C CA B THR A 128 ? 0.2136 0.2081 0.2966 0.0064 -0.0549 -0.0177 153 THR A CA 1018 C C . THR A 128 ? 0.2439 0.2446 0.3336 0.0108 -0.0601 -0.0234 153 THR A C 1019 O O . THR A 128 ? 0.2534 0.2532 0.3408 0.0109 -0.0645 -0.0236 153 THR A O 1020 C CB A THR A 128 ? 0.1919 0.1761 0.2717 0.0083 -0.0611 -0.0146 153 THR A CB 1021 C CB B THR A 128 ? 0.2305 0.2138 0.3078 0.0067 -0.0601 -0.0132 153 THR A CB 1022 O OG1 A THR A 128 ? 0.2328 0.2115 0.3065 0.0040 -0.0568 -0.0092 153 THR A OG1 1023 O OG1 B THR A 128 ? 0.2664 0.2433 0.3373 0.0061 -0.0664 -0.0105 153 THR A OG1 1024 C CG2 A THR A 128 ? 0.2398 0.2168 0.3151 0.0097 -0.0699 -0.0129 153 THR A CG2 1025 C CG2 B THR A 128 ? 0.2163 0.1989 0.2995 0.0118 -0.0647 -0.0163 153 THR A CG2 1026 N N . GLU A 129 ? 0.2110 0.2192 0.3092 0.0145 -0.0597 -0.0284 154 GLU A N 1027 C CA . GLU A 129 ? 0.2298 0.2467 0.3361 0.0187 -0.0637 -0.0347 154 GLU A CA 1028 C C . GLU A 129 ? 0.2513 0.2773 0.3603 0.0157 -0.0596 -0.0369 154 GLU A C 1029 O O . GLU A 129 ? 0.2880 0.3187 0.4007 0.0178 -0.0641 -0.0405 154 GLU A O 1030 C CB . GLU A 129 ? 0.2496 0.2744 0.3643 0.0229 -0.0631 -0.0400 154 GLU A CB 1031 C CG . GLU A 129 ? 0.3476 0.3643 0.4621 0.0278 -0.0702 -0.0403 154 GLU A CG 1032 C CD . GLU A 129 ? 0.5122 0.5266 0.6291 0.0329 -0.0802 -0.0433 154 GLU A CD 1033 O OE1 . GLU A 129 ? 0.5538 0.5795 0.6795 0.0367 -0.0817 -0.0501 154 GLU A OE1 1034 O OE2 . GLU A 129 ? 0.4958 0.4973 0.6058 0.0329 -0.0866 -0.0386 154 GLU A OE2 1035 N N . SER A 130 ? 0.1831 0.2112 0.2904 0.0108 -0.0515 -0.0348 155 SER A N 1036 C CA . SER A 130 ? 0.1726 0.2086 0.2829 0.0074 -0.0473 -0.0369 155 SER A CA 1037 C C . SER A 130 ? 0.2296 0.2603 0.3332 0.0045 -0.0487 -0.0344 155 SER A C 1038 O O . SER A 130 ? 0.2241 0.2608 0.3307 0.0031 -0.0487 -0.0373 155 SER A O 1039 C CB . SER A 130 ? 0.2139 0.2534 0.3252 0.0035 -0.0387 -0.0357 155 SER A CB 1040 O OG . SER A 130 ? 0.2750 0.3055 0.3783 0.0001 -0.0355 -0.0304 155 SER A OG 1041 N N . SER A 131 ? 0.2292 0.2492 0.3236 0.0032 -0.0497 -0.0292 156 SER A N 1042 C CA . SER A 131 ? 0.1946 0.2103 0.2814 -0.0002 -0.0497 -0.0268 156 SER A CA 1043 C C . SER A 131 ? 0.2106 0.2156 0.2876 -0.0007 -0.0530 -0.0214 156 SER A C 1044 O O . SER A 131 ? 0.2745 0.2746 0.3497 -0.0004 -0.0521 -0.0184 156 SER A O 1045 C CB . SER A 131 ? 0.2523 0.2699 0.3385 -0.0047 -0.0417 -0.0262 156 SER A CB 1046 O OG . SER A 131 ? 0.2620 0.2751 0.3403 -0.0076 -0.0415 -0.0243 156 SER A OG 1047 N N . SER A 132 ? 0.2402 0.2420 0.3104 -0.0020 -0.0566 -0.0201 157 SER A N 1048 C CA . SER A 132 ? 0.2836 0.2759 0.3431 -0.0037 -0.0595 -0.0144 157 SER A CA 1049 C C . SER A 132 ? 0.2258 0.2168 0.2783 -0.0086 -0.0529 -0.0117 157 SER A C 1050 O O . SER A 132 ? 0.2648 0.2497 0.3083 -0.0109 -0.0537 -0.0069 157 SER A O 1051 C CB . SER A 132 ? 0.3133 0.3026 0.3680 -0.0023 -0.0678 -0.0141 157 SER A CB 1052 O OG . SER A 132 ? 0.3532 0.3483 0.4080 -0.0038 -0.0668 -0.0174 157 SER A OG 1053 N N . LYS A 133 ? 0.1996 0.1967 0.2567 -0.0101 -0.0465 -0.0149 158 LYS A N 1054 C CA . LYS A 133 ? 0.2343 0.2308 0.2858 -0.0140 -0.0406 -0.0137 158 LYS A CA 1055 C C . LYS A 133 ? 0.2004 0.1985 0.2565 -0.0150 -0.0334 -0.0137 158 LYS A C 1056 O O . LYS A 133 ? 0.2192 0.2179 0.2731 -0.0174 -0.0284 -0.0142 158 LYS A O 1057 C CB . LYS A 133 ? 0.2596 0.2602 0.3107 -0.0153 -0.0404 -0.0176 158 LYS A CB 1058 C CG . LYS A 133 ? 0.3430 0.3418 0.3875 -0.0150 -0.0472 -0.0172 158 LYS A CG 1059 C CD . LYS A 133 ? 0.4178 0.4211 0.4621 -0.0165 -0.0467 -0.0216 158 LYS A CD 1060 C CE . LYS A 133 ? 0.5911 0.5928 0.6281 -0.0161 -0.0538 -0.0213 158 LYS A CE 1061 N NZ . LYS A 133 ? 0.6790 0.6850 0.7154 -0.0177 -0.0535 -0.0259 158 LYS A NZ 1062 N N . LEU A 134 ? 0.1890 0.1876 0.2510 -0.0128 -0.0333 -0.0135 159 LEU A N 1063 C CA . LEU A 134 ? 0.1824 0.1822 0.2482 -0.0135 -0.0273 -0.0132 159 LEU A CA 1064 C C . LEU A 134 ? 0.1883 0.1841 0.2533 -0.0124 -0.0280 -0.0098 159 LEU A C 1065 O O . LEU A 134 ? 0.1997 0.1931 0.2650 -0.0100 -0.0334 -0.0091 159 LEU A O 1066 C CB . LEU A 134 ? 0.1767 0.1829 0.2515 -0.0124 -0.0254 -0.0170 159 LEU A CB 1067 C CG . LEU A 134 ? 0.1918 0.2023 0.2689 -0.0143 -0.0240 -0.0205 159 LEU A CG 1068 C CD1 . LEU A 134 ? 0.2238 0.2415 0.3099 -0.0136 -0.0232 -0.0238 159 LEU A CD1 1069 C CD2 . LEU A 134 ? 0.2146 0.2230 0.2890 -0.0172 -0.0187 -0.0199 159 LEU A CD2 1070 N N . GLY A 135 ? 0.1722 0.1669 0.2366 -0.0139 -0.0229 -0.0079 160 GLY A N 1071 C CA . GLY A 135 ? 0.1898 0.1813 0.2542 -0.0132 -0.0231 -0.0049 160 GLY A CA 1072 C C . GLY A 135 ? 0.1709 0.1646 0.2390 -0.0137 -0.0173 -0.0051 160 GLY A C 1073 O O . GLY A 135 ? 0.1731 0.1702 0.2443 -0.0143 -0.0138 -0.0074 160 GLY A O 1074 N N . PHE A 136 ? 0.1969 0.1881 0.2648 -0.0136 -0.0167 -0.0025 161 PHE A N 1075 C CA . PHE A 136 ? 0.1898 0.1824 0.2605 -0.0139 -0.0119 -0.0023 161 PHE A CA 1076 C C . PHE A 136 ? 0.1836 0.1732 0.2519 -0.0151 -0.0113 0.0012 161 PHE A C 1077 O O . PHE A 136 ? 0.2318 0.2178 0.2978 -0.0150 -0.0153 0.0033 161 PHE A O 1078 C CB . PHE A 136 ? 0.1993 0.1951 0.2759 -0.0115 -0.0117 -0.0042 161 PHE A CB 1079 C CG . PHE A 136 ? 0.1779 0.1753 0.2570 -0.0121 -0.0069 -0.0039 161 PHE A CG 1080 C CD1 . PHE A 136 ? 0.1749 0.1735 0.2546 -0.0136 -0.0033 -0.0049 161 PHE A CD1 1081 C CD2 . PHE A 136 ? 0.1874 0.1842 0.2679 -0.0109 -0.0066 -0.0026 161 PHE A CD2 1082 C CE1 . PHE A 136 ? 0.1851 0.1840 0.2668 -0.0140 0.0002 -0.0043 161 PHE A CE1 1083 C CE2 . PHE A 136 ? 0.1846 0.1825 0.2669 -0.0112 -0.0028 -0.0021 161 PHE A CE2 1084 C CZ . PHE A 136 ? 0.1888 0.1873 0.2716 -0.0127 0.0005 -0.0027 161 PHE A CZ 1085 N N . THR A 137 ? 0.1835 0.1744 0.2526 -0.0161 -0.0067 0.0016 162 THR A N 1086 C CA . THR A 137 ? 0.2159 0.2056 0.2836 -0.0175 -0.0056 0.0044 162 THR A CA 1087 C C . THR A 137 ? 0.1805 0.1702 0.2525 -0.0157 -0.0056 0.0047 162 THR A C 1088 O O . THR A 137 ? 0.1845 0.1763 0.2599 -0.0146 -0.0027 0.0034 162 THR A O 1089 C CB . THR A 137 ? 0.1849 0.1770 0.2513 -0.0193 -0.0009 0.0041 162 THR A CB 1090 O OG1 . THR A 137 ? 0.1998 0.1921 0.2658 -0.0207 0.0001 0.0066 162 THR A OG1 1091 C CG2 . THR A 137 ? 0.1908 0.1847 0.2615 -0.0178 0.0025 0.0015 162 THR A CG2 1092 N N . ALA A 138 ? 0.1745 0.1613 0.2459 -0.0155 -0.0092 0.0066 163 ALA A N 1093 C CA . ALA A 138 ? 0.1798 0.1664 0.2546 -0.0141 -0.0096 0.0069 163 ALA A CA 1094 C C . ALA A 138 ? 0.2070 0.1895 0.2800 -0.0157 -0.0133 0.0098 163 ALA A C 1095 O O . ALA A 138 ? 0.2000 0.1802 0.2687 -0.0185 -0.0144 0.0122 163 ALA A O 1096 C CB . ALA A 138 ? 0.1907 0.1787 0.2690 -0.0108 -0.0113 0.0041 163 ALA A CB 1097 N N . GLY A 139 ? 0.1724 0.1537 0.2483 -0.0141 -0.0153 0.0097 164 GLY A N 1098 C CA . GLY A 139 ? 0.1890 0.1660 0.2640 -0.0160 -0.0187 0.0124 164 GLY A CA 1099 C C . GLY A 139 ? 0.1912 0.1619 0.2632 -0.0164 -0.0249 0.0137 164 GLY A C 1100 O O . GLY A 139 ? 0.2289 0.1987 0.3001 -0.0143 -0.0272 0.0119 164 GLY A O 1101 N N . TRP A 140 ? 0.2169 0.1830 0.2877 -0.0191 -0.0279 0.0170 165 TRP A N 1102 C CA . TRP A 140 ? 0.2568 0.2150 0.3238 -0.0208 -0.0342 0.0197 165 TRP A CA 1103 C C . TRP A 140 ? 0.2834 0.2364 0.3536 -0.0167 -0.0408 0.0172 165 TRP A C 1104 O O . TRP A 140 ? 0.2899 0.2370 0.3582 -0.0152 -0.0467 0.0171 165 TRP A O 1105 C CB . TRP A 140 ? 0.2714 0.2278 0.3356 -0.0267 -0.0337 0.0249 165 TRP A CB 1106 C CG . TRP A 140 ? 0.2995 0.2470 0.3591 -0.0303 -0.0401 0.0294 165 TRP A CG 1107 C CD1 . TRP A 140 ? 0.3111 0.2558 0.3637 -0.0338 -0.0414 0.0332 165 TRP A CD1 1108 C CD2 . TRP A 140 ? 0.2864 0.2261 0.3474 -0.0311 -0.0462 0.0311 165 TRP A CD2 1109 N NE1 . TRP A 140 ? 0.2921 0.2272 0.3414 -0.0370 -0.0482 0.0377 165 TRP A NE1 1110 C CE2 . TRP A 140 ? 0.3416 0.2732 0.3964 -0.0354 -0.0514 0.0364 165 TRP A CE2 1111 C CE3 . TRP A 140 ? 0.3157 0.2542 0.3824 -0.0287 -0.0482 0.0286 165 TRP A CE3 1112 C CZ2 . TRP A 140 ? 0.3534 0.2748 0.4079 -0.0375 -0.0587 0.0394 165 TRP A CZ2 1113 C CZ3 . TRP A 140 ? 0.3274 0.2564 0.3941 -0.0305 -0.0553 0.0309 165 TRP A CZ3 1114 C CH2 . TRP A 140 ? 0.3504 0.2705 0.4113 -0.0349 -0.0606 0.0364 165 TRP A CH2 1115 N N . CYS A 141 ? 0.2395 0.1946 0.3144 -0.0144 -0.0402 0.0146 166 CYS A N 1116 C CA . CYS A 141 ? 0.2487 0.1998 0.3269 -0.0101 -0.0462 0.0112 166 CYS A CA 1117 C C . CYS A 141 ? 0.2095 0.1653 0.2902 -0.0046 -0.0462 0.0057 166 CYS A C 1118 O O . CYS A 141 ? 0.2385 0.2021 0.3213 -0.0032 -0.0407 0.0033 166 CYS A O 1119 C CB . CYS A 141 ? 0.2472 0.1997 0.3290 -0.0098 -0.0455 0.0102 166 CYS A CB 1120 S SG . CYS A 141 ? 0.2629 0.2120 0.3439 -0.0163 -0.0454 0.0158 166 CYS A SG 1121 N N . PRO A 142 ? 0.2308 0.1820 0.3117 -0.0015 -0.0526 0.0037 167 PRO A N 1122 C CA . PRO A 142 ? 0.2322 0.1894 0.3159 0.0033 -0.0523 -0.0016 167 PRO A CA 1123 C C . PRO A 142 ? 0.2354 0.1991 0.3242 0.0079 -0.0513 -0.0074 167 PRO A C 1124 O O . PRO A 142 ? 0.2473 0.2189 0.3384 0.0105 -0.0486 -0.0113 167 PRO A O 1125 C CB . PRO A 142 ? 0.2867 0.2366 0.3696 0.0055 -0.0605 -0.0022 167 PRO A CB 1126 C CG . PRO A 142 ? 0.3883 0.3276 0.4695 0.0033 -0.0662 0.0013 167 PRO A CG 1127 C CD . PRO A 142 ? 0.2989 0.2393 0.3769 -0.0029 -0.0602 0.0068 167 PRO A CD 1128 N N . THR A 143 ? 0.2325 0.1934 0.3228 0.0086 -0.0535 -0.0082 168 THR A N 1129 C CA . THR A 143 ? 0.2146 0.1820 0.3089 0.0131 -0.0529 -0.0140 168 THR A CA 1130 C C . THR A 143 ? 0.1891 0.1638 0.2833 0.0114 -0.0456 -0.0132 168 THR A C 1131 O O . THR A 143 ? 0.2113 0.1922 0.3076 0.0144 -0.0444 -0.0174 168 THR A O 1132 C CB . THR A 143 ? 0.2063 0.1673 0.3027 0.0162 -0.0602 -0.0170 168 THR A CB 1133 O OG1 . THR A 143 ? 0.2470 0.2014 0.3417 0.0120 -0.0610 -0.0124 168 THR A OG1 1134 C CG2 . THR A 143 ? 0.2247 0.1783 0.3218 0.0190 -0.0683 -0.0186 168 THR A CG2 1135 N N . VAL A 144 ? 0.1887 0.1630 0.2802 0.0067 -0.0410 -0.0081 169 VAL A N 1136 C CA . VAL A 144 ? 0.1822 0.1627 0.2738 0.0053 -0.0346 -0.0070 169 VAL A CA 1137 C C . VAL A 144 ? 0.1899 0.1789 0.2824 0.0071 -0.0303 -0.0099 169 VAL A C 1138 O O . VAL A 144 ? 0.1792 0.1694 0.2716 0.0073 -0.0303 -0.0107 169 VAL A O 1139 C CB . VAL A 144 ? 0.1749 0.1534 0.2640 0.0004 -0.0310 -0.0017 169 VAL A CB 1140 C CG1 . VAL A 144 ? 0.1958 0.1806 0.2851 -0.0005 -0.0244 -0.0010 169 VAL A CG1 1141 C CG2 . VAL A 144 ? 0.1773 0.1500 0.2663 -0.0021 -0.0339 0.0012 169 VAL A CG2 1142 N N . GLY A 145 ? 0.1806 0.1753 0.2736 0.0080 -0.0270 -0.0113 170 GLY A N 1143 C CA . GLY A 145 ? 0.1797 0.1826 0.2733 0.0087 -0.0228 -0.0134 170 GLY A CA 1144 C C . GLY A 145 ? 0.1617 0.1655 0.2536 0.0052 -0.0174 -0.0096 170 GLY A C 1145 O O . GLY A 145 ? 0.1733 0.1741 0.2640 0.0030 -0.0157 -0.0061 170 GLY A O 1146 N N . THR A 146 ? 0.1464 0.1548 0.2389 0.0047 -0.0148 -0.0106 171 THR A N 1147 C CA . THR A 146 ? 0.1584 0.1672 0.2496 0.0015 -0.0101 -0.0076 171 THR A CA 1148 C C . THR A 146 ? 0.1883 0.1994 0.2785 0.0008 -0.0067 -0.0060 171 THR A C 1149 O O . THR A 146 ? 0.1882 0.1971 0.2773 -0.0014 -0.0039 -0.0029 171 THR A O 1150 C CB . THR A 146 ? 0.1849 0.1980 0.2772 0.0007 -0.0084 -0.0092 171 THR A CB 1151 O OG1 . THR A 146 ? 0.1867 0.2076 0.2809 0.0025 -0.0080 -0.0128 171 THR A OG1 1152 C CG2 . THR A 146 ? 0.1939 0.2039 0.2864 0.0011 -0.0118 -0.0101 171 THR A CG2 1153 N N . GLY A 147 ? 0.1979 0.2136 0.2883 0.0028 -0.0073 -0.0083 172 GLY A N 1154 C CA . GLY A 147 ? 0.1981 0.2162 0.2867 0.0021 -0.0046 -0.0066 172 GLY A CA 1155 C C . GLY A 147 ? 0.1849 0.1975 0.2726 0.0015 -0.0049 -0.0033 172 GLY A C 1156 O O . GLY A 147 ? 0.2216 0.2327 0.3082 -0.0004 -0.0022 -0.0002 172 GLY A O 1157 N N . GLY A 148 ? 0.1660 0.1755 0.2545 0.0029 -0.0084 -0.0040 173 GLY A N 1158 C CA . GLY A 148 ? 0.1477 0.1532 0.2363 0.0020 -0.0088 -0.0013 173 GLY A CA 1159 C C . GLY A 148 ? 0.1625 0.1641 0.2518 -0.0003 -0.0076 0.0013 173 GLY A C 1160 O O . GLY A 148 ? 0.1760 0.1765 0.2655 -0.0015 -0.0056 0.0036 173 GLY A O 1161 N N . HIS A 149 ? 0.1571 0.1569 0.2465 -0.0009 -0.0089 0.0005 174 HIS A N 1162 C CA . HIS A 149 ? 0.1652 0.1617 0.2544 -0.0033 -0.0083 0.0026 174 HIS A CA 1163 C C . HIS A 149 ? 0.1628 0.1601 0.2514 -0.0048 -0.0041 0.0039 174 HIS A C 1164 O O . HIS A 149 ? 0.1650 0.1613 0.2540 -0.0061 -0.0024 0.0056 174 HIS A O 1165 C CB . HIS A 149 ? 0.1816 0.1758 0.2700 -0.0033 -0.0113 0.0015 174 HIS A CB 1166 C CG . HIS A 149 ? 0.1804 0.1714 0.2672 -0.0060 -0.0111 0.0039 174 HIS A CG 1167 N ND1 . HIS A 149 ? 0.1743 0.1622 0.2608 -0.0079 -0.0127 0.0061 174 HIS A ND1 1168 C CD2 . HIS A 149 ? 0.1908 0.1815 0.2759 -0.0074 -0.0098 0.0041 174 HIS A CD2 1169 C CE1 . HIS A 149 ? 0.1814 0.1679 0.2657 -0.0106 -0.0120 0.0079 174 HIS A CE1 1170 N NE2 . HIS A 149 ? 0.1808 0.1688 0.2640 -0.0100 -0.0104 0.0066 174 HIS A NE2 1171 N N . ILE A 150 ? 0.1573 0.1569 0.2455 -0.0046 -0.0026 0.0026 175 ILE A N 1172 C CA . ILE A 150 ? 0.1508 0.1503 0.2388 -0.0061 0.0008 0.0035 175 ILE A CA 1173 C C . ILE A 150 ? 0.1612 0.1606 0.2495 -0.0059 0.0026 0.0052 175 ILE A C 1174 O O . ILE A 150 ? 0.1721 0.1696 0.2608 -0.0067 0.0045 0.0062 175 ILE A O 1175 C CB . ILE A 150 ? 0.1534 0.1552 0.2412 -0.0067 0.0017 0.0019 175 ILE A CB 1176 C CG1 . ILE A 150 ? 0.1654 0.1669 0.2531 -0.0065 -0.0009 0.0002 175 ILE A CG1 1177 C CG2 . ILE A 150 ? 0.1784 0.1790 0.2661 -0.0086 0.0047 0.0027 175 ILE A CG2 1178 C CD1 . ILE A 150 ? 0.2030 0.2074 0.2913 -0.0071 -0.0004 -0.0017 175 ILE A CD1 1179 N N . SER A 151 ? 0.1526 0.1538 0.2406 -0.0045 0.0017 0.0052 176 SER A N 1180 C CA . SER A 151 ? 0.1750 0.1758 0.2628 -0.0040 0.0025 0.0071 176 SER A CA 1181 C C . SER A 151 ? 0.1550 0.1537 0.2447 -0.0037 0.0022 0.0082 176 SER A C 1182 O O . SER A 151 ? 0.1636 0.1611 0.2540 -0.0034 0.0031 0.0096 176 SER A O 1183 C CB . SER A 151 ? 0.1791 0.1828 0.2655 -0.0025 0.0010 0.0066 176 SER A CB 1184 O OG . SER A 151 ? 0.1766 0.1840 0.2615 -0.0031 0.0022 0.0057 176 SER A OG 1185 N N . GLY A 152 ? 0.1501 0.1485 0.2408 -0.0040 0.0006 0.0075 177 GLY A N 1186 C CA . GLY A 152 ? 0.1586 0.1568 0.2517 -0.0043 0.0005 0.0084 177 GLY A CA 1187 C C . GLY A 152 ? 0.1553 0.1531 0.2489 -0.0061 0.0023 0.0084 177 GLY A C 1188 O O . GLY A 152 ? 0.1821 0.1813 0.2779 -0.0068 0.0026 0.0088 177 GLY A O 1189 N N . GLY A 153 ? 0.1642 0.1611 0.2559 -0.0070 0.0035 0.0076 178 GLY A N 1190 C CA . GLY A 153 ? 0.1697 0.1666 0.2610 -0.0086 0.0052 0.0073 178 GLY A CA 1191 C C . GLY A 153 ? 0.1523 0.1483 0.2410 -0.0101 0.0037 0.0070 178 GLY A C 1192 O O . GLY A 153 ? 0.1656 0.1610 0.2528 -0.0101 0.0040 0.0059 178 GLY A O 1193 N N . GLY A 154 ? 0.1532 0.1488 0.2413 -0.0114 0.0017 0.0081 179 GLY A N 1194 C CA . GLY A 154 ? 0.1666 0.1600 0.2521 -0.0124 -0.0010 0.0083 179 GLY A CA 1195 C C . GLY A 154 ? 0.1675 0.1608 0.2502 -0.0152 -0.0002 0.0093 179 GLY A C 1196 O O . GLY A 154 ? 0.1777 0.1715 0.2585 -0.0156 0.0015 0.0082 179 GLY A O 1197 N N . PHE A 155 ? 0.1663 0.1592 0.2484 -0.0175 -0.0014 0.0114 180 PHE A N 1198 C CA . PHE A 155 ? 0.1802 0.1741 0.2590 -0.0210 -0.0002 0.0130 180 PHE A CA 1199 C C . PHE A 155 ? 0.2090 0.1983 0.2837 -0.0230 -0.0046 0.0151 180 PHE A C 1200 O O . PHE A 155 ? 0.2262 0.2117 0.3017 -0.0225 -0.0086 0.0161 180 PHE A O 1201 C CB . PHE A 155 ? 0.2049 0.2028 0.2862 -0.0232 0.0018 0.0142 180 PHE A CB 1202 C CG . PHE A 155 ? 0.1960 0.1971 0.2739 -0.0272 0.0039 0.0157 180 PHE A CG 1203 C CD1 . PHE A 155 ? 0.2062 0.2128 0.2846 -0.0271 0.0085 0.0134 180 PHE A CD1 1204 C CD2 . PHE A 155 ? 0.2397 0.2382 0.3137 -0.0313 0.0012 0.0192 180 PHE A CD2 1205 C CE1 . PHE A 155 ? 0.2634 0.2745 0.3383 -0.0308 0.0109 0.0142 180 PHE A CE1 1206 C CE2 . PHE A 155 ? 0.2439 0.2461 0.3137 -0.0357 0.0034 0.0210 180 PHE A CE2 1207 C CZ . PHE A 155 ? 0.2599 0.2691 0.3301 -0.0354 0.0086 0.0182 180 PHE A CZ 1208 N N . GLY A 156 ? 0.1840 0.1731 0.2539 -0.0250 -0.0042 0.0158 181 GLY A N 1209 C CA . GLY A 156 ? 0.2152 0.1990 0.2804 -0.0269 -0.0089 0.0183 181 GLY A CA 1210 C C . GLY A 156 ? 0.2003 0.1853 0.2592 -0.0306 -0.0078 0.0202 181 GLY A C 1211 O O . GLY A 156 ? 0.2197 0.2105 0.2783 -0.0322 -0.0029 0.0194 181 GLY A O 1212 N N . MET A 157 ? 0.2197 0.1993 0.2737 -0.0318 -0.0125 0.0223 182 MET A N 1213 C CA . MET A 157 ? 0.2222 0.2018 0.2686 -0.0361 -0.0126 0.0253 182 MET A CA 1214 C C . MET A 157 ? 0.2386 0.2231 0.2823 -0.0355 -0.0089 0.0223 182 MET A C 1215 O O . MET A 157 ? 0.2654 0.2520 0.3027 -0.0392 -0.0076 0.0240 182 MET A O 1216 C CB . MET A 157 ? 0.2656 0.2369 0.3071 -0.0370 -0.0198 0.0285 182 MET A CB 1217 C CG . MET A 157 ? 0.3272 0.2926 0.3694 -0.0393 -0.0241 0.0325 182 MET A CG 1218 S SD . MET A 157 ? 0.3300 0.2985 0.3681 -0.0472 -0.0211 0.0380 182 MET A SD 1219 C CE . MET A 157 ? 0.2868 0.2529 0.3133 -0.0517 -0.0232 0.0421 182 MET A CE 1220 N N . MET A 158 ? 0.2128 0.1990 0.2612 -0.0313 -0.0073 0.0178 183 MET A N 1221 C CA . MET A 158 ? 0.2030 0.1932 0.2497 -0.0307 -0.0040 0.0145 183 MET A CA 1222 C C . MET A 158 ? 0.1822 0.1778 0.2340 -0.0293 0.0017 0.0113 183 MET A C 1223 O O . MET A 158 ? 0.1978 0.1959 0.2499 -0.0281 0.0041 0.0077 183 MET A O 1224 C CB . MET A 158 ? 0.2532 0.2409 0.3005 -0.0278 -0.0071 0.0119 183 MET A CB 1225 C CG . MET A 158 ? 0.2574 0.2404 0.2988 -0.0288 -0.0129 0.0144 183 MET A CG 1226 S SD . MET A 158 ? 0.3026 0.2854 0.3450 -0.0256 -0.0159 0.0104 183 MET A SD 1227 C CE . MET A 158 ? 0.3102 0.2945 0.3624 -0.0215 -0.0145 0.0071 183 MET A CE 1228 N N . SER A 159 ? 0.1897 0.1868 0.2458 -0.0294 0.0032 0.0123 184 SER A N 1229 C CA . SER A 159 ? 0.1944 0.1959 0.2558 -0.0275 0.0077 0.0093 184 SER A CA 1230 C C . SER A 159 ? 0.1811 0.1888 0.2405 -0.0291 0.0121 0.0073 184 SER A C 1231 O O . SER A 159 ? 0.2011 0.2115 0.2641 -0.0267 0.0151 0.0035 184 SER A O 1232 C CB . SER A 159 ? 0.1946 0.1965 0.2614 -0.0268 0.0077 0.0106 184 SER A CB 1233 O OG . SER A 159 ? 0.1907 0.1882 0.2603 -0.0240 0.0047 0.0105 184 SER A OG 1234 N N . ARG A 160 ? 0.1906 0.2007 0.2441 -0.0332 0.0123 0.0097 185 ARG A N 1235 C CA A ARG A 160 ? 0.1985 0.2160 0.2496 -0.0347 0.0167 0.0072 185 ARG A CA 1236 C CA B ARG A 160 ? 0.1957 0.2132 0.2466 -0.0349 0.0166 0.0073 185 ARG A CA 1237 C C . ARG A 160 ? 0.2002 0.2172 0.2479 -0.0332 0.0169 0.0034 185 ARG A C 1238 O O . ARG A 160 ? 0.2162 0.2388 0.2634 -0.0328 0.0206 -0.0006 185 ARG A O 1239 C CB A ARG A 160 ? 0.2085 0.2296 0.2534 -0.0403 0.0172 0.0112 185 ARG A CB 1240 C CB B ARG A 160 ? 0.1898 0.2104 0.2341 -0.0405 0.0168 0.0115 185 ARG A CB 1241 C CG A ARG A 160 ? 0.1857 0.2074 0.2344 -0.0425 0.0167 0.0150 185 ARG A CG 1242 C CG B ARG A 160 ? 0.2366 0.2575 0.2843 -0.0429 0.0162 0.0155 185 ARG A CG 1243 C CD A ARG A 160 ? 0.2885 0.3164 0.3325 -0.0488 0.0187 0.0184 185 ARG A CD 1244 C CD B ARG A 160 ? 0.1670 0.1922 0.2085 -0.0495 0.0171 0.0198 185 ARG A CD 1245 N NE A ARG A 160 ? 0.2709 0.3004 0.3054 -0.0519 0.0191 0.0192 185 ARG A NE 1246 N NE B ARG A 160 ? 0.1717 0.2087 0.2138 -0.0509 0.0232 0.0166 185 ARG A NE 1247 C CZ A ARG A 160 ? 0.2205 0.2596 0.2523 -0.0532 0.0241 0.0159 185 ARG A CZ 1248 C CZ B ARG A 160 ? 0.2265 0.2686 0.2621 -0.0523 0.0258 0.0144 185 ARG A CZ 1249 N NH1 A ARG A 160 ? 0.1894 0.2297 0.2115 -0.0561 0.0239 0.0168 185 ARG A NH1 1250 N NH1 B ARG A 160 ? 0.1802 0.2341 0.2173 -0.0529 0.0315 0.0105 185 ARG A NH1 1251 N NH2 A ARG A 160 ? 0.2315 0.2796 0.2704 -0.0512 0.0290 0.0113 185 ARG A NH2 1252 N NH2 B ARG A 160 ? 0.2011 0.2371 0.2289 -0.0527 0.0225 0.0157 185 ARG A NH2 1253 N N . LYS A 161 ? 0.1880 0.1985 0.2340 -0.0321 0.0128 0.0041 186 LYS A N 1254 C CA . LYS A 161 ? 0.2296 0.2393 0.2734 -0.0307 0.0123 0.0005 186 LYS A CA 1255 C C . LYS A 161 ? 0.2102 0.2176 0.2610 -0.0268 0.0127 -0.0031 186 LYS A C 1256 O O . LYS A 161 ? 0.2404 0.2490 0.2919 -0.0255 0.0144 -0.0075 186 LYS A O 1257 C CB . LYS A 161 ? 0.2302 0.2351 0.2683 -0.0319 0.0072 0.0031 186 LYS A CB 1258 C CG . LYS A 161 ? 0.3111 0.3150 0.3475 -0.0305 0.0059 -0.0006 186 LYS A CG 1259 C CD . LYS A 161 ? 0.3171 0.3257 0.3467 -0.0325 0.0080 -0.0028 186 LYS A CD 1260 C CE . LYS A 161 ? 0.3255 0.3327 0.3527 -0.0315 0.0056 -0.0062 186 LYS A CE 1261 N NZ . LYS A 161 ? 0.3257 0.3379 0.3459 -0.0333 0.0078 -0.0091 186 LYS A NZ 1262 N N . TYR A 162 ? 0.1902 0.1942 0.2459 -0.0252 0.0111 -0.0012 187 TYR A N 1263 C CA . TYR A 162 ? 0.1942 0.1956 0.2553 -0.0224 0.0109 -0.0035 187 TYR A CA 1264 C C . TYR A 162 ? 0.1851 0.1862 0.2524 -0.0204 0.0123 -0.0029 187 TYR A C 1265 O O . TYR A 162 ? 0.2041 0.2030 0.2753 -0.0186 0.0121 -0.0040 187 TYR A O 1266 C CB . TYR A 162 ? 0.1945 0.1925 0.2552 -0.0219 0.0068 -0.0024 187 TYR A CB 1267 C CG . TYR A 162 ? 0.1852 0.1830 0.2411 -0.0230 0.0047 -0.0039 187 TYR A CG 1268 C CD1 . TYR A 162 ? 0.1950 0.1940 0.2505 -0.0229 0.0064 -0.0078 187 TYR A CD1 1269 C CD2 . TYR A 162 ? 0.1934 0.1892 0.2452 -0.0238 0.0005 -0.0014 187 TYR A CD2 1270 C CE1 . TYR A 162 ? 0.2084 0.2076 0.2595 -0.0238 0.0042 -0.0094 187 TYR A CE1 1271 C CE2 . TYR A 162 ? 0.2017 0.1974 0.2491 -0.0246 -0.0020 -0.0027 187 TYR A CE2 1272 C CZ . TYR A 162 ? 0.2185 0.2163 0.2655 -0.0246 0.0000 -0.0067 187 TYR A CZ 1273 O OH . TYR A 162 ? 0.2438 0.2417 0.2863 -0.0253 -0.0028 -0.0083 187 TYR A OH 1274 N N . GLY A 163 ? 0.1837 0.1872 0.2517 -0.0212 0.0134 -0.0010 188 GLY A N 1275 C CA . GLY A 163 ? 0.2004 0.2039 0.2741 -0.0193 0.0143 -0.0005 188 GLY A CA 1276 C C . GLY A 163 ? 0.1630 0.1633 0.2381 -0.0186 0.0112 0.0022 188 GLY A C 1277 O O . GLY A 163 ? 0.1887 0.1871 0.2607 -0.0199 0.0083 0.0041 188 GLY A O 1278 N N . LEU A 164 ? 0.1710 0.1705 0.2505 -0.0165 0.0115 0.0022 189 LEU A N 1279 C CA . LEU A 164 ? 0.1689 0.1664 0.2499 -0.0155 0.0089 0.0040 189 LEU A CA 1280 C C . LEU A 164 ? 0.1696 0.1651 0.2504 -0.0146 0.0074 0.0031 189 LEU A C 1281 O O . LEU A 164 ? 0.1872 0.1824 0.2679 -0.0146 0.0087 0.0012 189 LEU A O 1282 C CB . LEU A 164 ? 0.1632 0.1614 0.2484 -0.0137 0.0097 0.0044 189 LEU A CB 1283 C CG . LEU A 164 ? 0.1881 0.1897 0.2753 -0.0143 0.0114 0.0047 189 LEU A CG 1284 C CD1 . LEU A 164 ? 0.1819 0.1839 0.2735 -0.0119 0.0115 0.0047 189 LEU A CD1 1285 C CD2 . LEU A 164 ? 0.1997 0.2021 0.2850 -0.0169 0.0097 0.0071 189 LEU A CD2 1286 N N . ALA A 165 ? 0.1588 0.1533 0.2399 -0.0138 0.0047 0.0040 190 ALA A N 1287 C CA . ALA A 165 ? 0.1632 0.1579 0.2453 -0.0127 0.0037 0.0027 190 ALA A CA 1288 C C . ALA A 165 ? 0.1891 0.1841 0.2734 -0.0122 0.0063 0.0020 190 ALA A C 1289 O O . ALA A 165 ? 0.1840 0.1792 0.2685 -0.0128 0.0070 0.0007 190 ALA A O 1290 C CB . ALA A 165 ? 0.1735 0.1683 0.2566 -0.0112 0.0008 0.0031 190 ALA A CB 1291 N N . ALA A 166 ? 0.1712 0.1660 0.2571 -0.0113 0.0074 0.0032 191 ALA A N 1292 C CA . ALA A 166 ? 0.1733 0.1671 0.2608 -0.0108 0.0090 0.0033 191 ALA A CA 1293 C C . ALA A 166 ? 0.1688 0.1608 0.2566 -0.0116 0.0108 0.0018 191 ALA A C 1294 O O . ALA A 166 ? 0.1931 0.1831 0.2818 -0.0118 0.0115 0.0018 191 ALA A O 1295 C CB . ALA A 166 ? 0.1997 0.1934 0.2889 -0.0093 0.0090 0.0048 191 ALA A CB 1296 N N . ASP A 167 ? 0.1698 0.1625 0.2565 -0.0121 0.0115 0.0006 192 ASP A N 1297 C CA . ASP A 167 ? 0.1807 0.1722 0.2674 -0.0124 0.0130 -0.0018 192 ASP A CA 1298 C C . ASP A 167 ? 0.1988 0.1895 0.2842 -0.0139 0.0125 -0.0033 192 ASP A C 1299 O O . ASP A 167 ? 0.2474 0.2364 0.3329 -0.0144 0.0132 -0.0056 192 ASP A O 1300 C CB . ASP A 167 ? 0.1873 0.1814 0.2725 -0.0128 0.0140 -0.0030 192 ASP A CB 1301 C CG . ASP A 167 ? 0.1943 0.1905 0.2820 -0.0115 0.0150 -0.0023 192 ASP A CG 1302 O OD1 . ASP A 167 ? 0.2223 0.2168 0.3131 -0.0097 0.0149 -0.0018 192 ASP A OD1 1303 O OD2 . ASP A 167 ? 0.1944 0.1942 0.2809 -0.0126 0.0156 -0.0020 192 ASP A OD2 1304 N N . ASN A 168 ? 0.1712 0.1634 0.2559 -0.0145 0.0108 -0.0024 193 ASN A N 1305 C CA . ASN A 168 ? 0.1778 0.1705 0.2619 -0.0159 0.0100 -0.0041 193 ASN A CA 1306 C C . ASN A 168 ? 0.1771 0.1712 0.2634 -0.0164 0.0096 -0.0035 193 ASN A C 1307 O O . ASN A 168 ? 0.2061 0.2027 0.2928 -0.0173 0.0085 -0.0048 193 ASN A O 1308 C CB . ASN A 168 ? 0.1758 0.1702 0.2570 -0.0162 0.0079 -0.0045 193 ASN A CB 1309 C CG . ASN A 168 ? 0.1994 0.1937 0.2775 -0.0167 0.0087 -0.0052 193 ASN A CG 1310 O OD1 . ASN A 168 ? 0.2104 0.2045 0.2871 -0.0176 0.0092 -0.0075 193 ASN A OD1 1311 N ND2 . ASN A 168 ? 0.1878 0.1825 0.2649 -0.0164 0.0090 -0.0033 193 ASN A ND2 1312 N N . VAL A 169 ? 0.1759 0.1689 0.2635 -0.0159 0.0106 -0.0016 194 VAL A N 1313 C CA . VAL A 169 ? 0.1728 0.1677 0.2618 -0.0169 0.0108 -0.0005 194 VAL A CA 1314 C C . VAL A 169 ? 0.1767 0.1682 0.2667 -0.0191 0.0120 -0.0004 194 VAL A C 1315 O O . VAL A 169 ? 0.2073 0.1939 0.2974 -0.0186 0.0125 0.0002 194 VAL A O 1316 C CB . VAL A 169 ? 0.1919 0.1872 0.2806 -0.0154 0.0109 0.0018 194 VAL A CB 1317 C CG1 . VAL A 169 ? 0.2014 0.1983 0.2906 -0.0170 0.0117 0.0034 194 VAL A CG1 1318 C CG2 . VAL A 169 ? 0.2015 0.1998 0.2898 -0.0135 0.0091 0.0014 194 VAL A CG2 1319 N N . VAL A 170 ? 0.1782 0.1722 0.2694 -0.0217 0.0122 -0.0010 195 VAL A N 1320 C CA . VAL A 170 ? 0.1909 0.1811 0.2833 -0.0247 0.0129 -0.0008 195 VAL A CA 1321 C C . VAL A 170 ? 0.2241 0.2155 0.3169 -0.0274 0.0138 0.0021 195 VAL A C 1322 O O . VAL A 170 ? 0.2185 0.2051 0.3117 -0.0302 0.0140 0.0036 195 VAL A O 1323 C CB . VAL A 170 ? 0.2058 0.1973 0.2994 -0.0265 0.0122 -0.0041 195 VAL A CB 1324 C CG1 . VAL A 170 ? 0.2291 0.2185 0.3210 -0.0243 0.0114 -0.0066 195 VAL A CG1 1325 C CG2 . VAL A 170 ? 0.2399 0.2394 0.3350 -0.0274 0.0117 -0.0053 195 VAL A CG2 1326 N N . ASP A 171 ? 0.2024 0.2002 0.2948 -0.0268 0.0142 0.0029 196 ASP A N 1327 C CA . ASP A 171 ? 0.1917 0.1923 0.2835 -0.0293 0.0154 0.0058 196 ASP A CA 1328 C C . ASP A 171 ? 0.1827 0.1891 0.2734 -0.0265 0.0153 0.0058 196 ASP A C 1329 O O . ASP A 171 ? 0.1869 0.1946 0.2778 -0.0231 0.0140 0.0035 196 ASP A O 1330 C CB . ASP A 171 ? 0.2074 0.2135 0.3016 -0.0338 0.0165 0.0049 196 ASP A CB 1331 C CG . ASP A 171 ? 0.2636 0.2698 0.3566 -0.0384 0.0180 0.0089 196 ASP A CG 1332 O OD1 . ASP A 171 ? 0.2132 0.2177 0.3030 -0.0377 0.0183 0.0123 196 ASP A OD1 1333 O OD2 . ASP A 171 ? 0.2720 0.2799 0.3671 -0.0432 0.0188 0.0089 196 ASP A OD2 1334 N N . ALA A 172 ? 0.1989 0.2085 0.2878 -0.0280 0.0165 0.0084 197 ALA A N 1335 C CA . ALA A 172 ? 0.1756 0.1913 0.2633 -0.0254 0.0163 0.0078 197 ALA A CA 1336 C C . ALA A 172 ? 0.1825 0.2036 0.2681 -0.0287 0.0183 0.0102 197 ALA A C 1337 O O . ALA A 172 ? 0.2157 0.2329 0.3000 -0.0328 0.0193 0.0137 197 ALA A O 1338 C CB . ALA A 172 ? 0.2099 0.2201 0.2956 -0.0217 0.0148 0.0091 197 ALA A CB 1339 N N . ILE A 173 ? 0.1985 0.2287 0.2838 -0.0271 0.0187 0.0081 198 ILE A N 1340 C CA . ILE A 173 ? 0.1895 0.2259 0.2717 -0.0299 0.0207 0.0104 198 ILE A CA 1341 C C . ILE A 173 ? 0.1982 0.2335 0.2766 -0.0263 0.0194 0.0114 198 ILE A C 1342 O O . ILE A 173 ? 0.1980 0.2365 0.2777 -0.0220 0.0179 0.0077 198 ILE A O 1343 C CB . ILE A 173 ? 0.1994 0.2496 0.2843 -0.0310 0.0225 0.0065 198 ILE A CB 1344 C CG1 . ILE A 173 ? 0.2702 0.3225 0.3595 -0.0348 0.0236 0.0053 198 ILE A CG1 1345 C CG2 . ILE A 173 ? 0.1908 0.2489 0.2716 -0.0340 0.0250 0.0087 198 ILE A CG2 1346 C CD1 . ILE A 173 ? 0.3418 0.3902 0.4291 -0.0415 0.0255 0.0104 198 ILE A CD1 1347 N N . LEU A 174 ? 0.2059 0.2359 0.2798 -0.0283 0.0196 0.0165 199 LEU A N 1348 C CA . LEU A 174 ? 0.1875 0.2160 0.2576 -0.0252 0.0180 0.0179 199 LEU A CA 1349 C C . LEU A 174 ? 0.2292 0.2652 0.2940 -0.0281 0.0199 0.0202 199 LEU A C 1350 O O . LEU A 174 ? 0.2615 0.2966 0.3237 -0.0334 0.0215 0.0245 199 LEU A O 1351 C CB . LEU A 174 ? 0.2169 0.2334 0.2857 -0.0244 0.0160 0.0219 199 LEU A CB 1352 C CG . LEU A 174 ? 0.2509 0.2651 0.3159 -0.0215 0.0139 0.0239 199 LEU A CG 1353 C CD1 . LEU A 174 ? 0.2367 0.2533 0.3042 -0.0165 0.0121 0.0195 199 LEU A CD1 1354 C CD2 . LEU A 174 ? 0.2880 0.2910 0.3524 -0.0213 0.0120 0.0279 199 LEU A CD2 1355 N N . ILE A 175 ? 0.1982 0.2416 0.2614 -0.0249 0.0194 0.0172 200 ILE A N 1356 C CA . ILE A 175 ? 0.1921 0.2433 0.2492 -0.0272 0.0211 0.0190 200 ILE A CA 1357 C C . ILE A 175 ? 0.2301 0.2742 0.2820 -0.0255 0.0186 0.0230 200 ILE A C 1358 O O . ILE A 175 ? 0.2185 0.2602 0.2716 -0.0204 0.0158 0.0204 200 ILE A O 1359 C CB . ILE A 175 ? 0.2138 0.2785 0.2721 -0.0244 0.0219 0.0125 200 ILE A CB 1360 C CG1 . ILE A 175 ? 0.2493 0.3205 0.3146 -0.0243 0.0232 0.0073 200 ILE A CG1 1361 C CG2 . ILE A 175 ? 0.2132 0.2881 0.2648 -0.0275 0.0245 0.0141 200 ILE A CG2 1362 C CD1 . ILE A 175 ? 0.2948 0.3695 0.3609 -0.0307 0.0266 0.0099 200 ILE A CD1 1363 N N . ASP A 176 ? 0.2258 0.2659 0.2718 -0.0298 0.0190 0.0295 201 ASP A N 1364 C CA . ASP A 176 ? 0.2086 0.2403 0.2499 -0.0280 0.0159 0.0338 201 ASP A CA 1365 C C . ASP A 176 ? 0.2641 0.3034 0.2985 -0.0272 0.0156 0.0339 201 ASP A C 1366 O O . ASP A 176 ? 0.2447 0.2963 0.2782 -0.0275 0.0180 0.0299 201 ASP A O 1367 C CB . ASP A 176 ? 0.2412 0.2615 0.2800 -0.0320 0.0149 0.0409 201 ASP A CB 1368 C CG . ASP A 176 ? 0.3008 0.3242 0.3318 -0.0384 0.0167 0.0467 201 ASP A CG 1369 O OD1 . ASP A 176 ? 0.2770 0.3131 0.3046 -0.0402 0.0195 0.0450 201 ASP A OD1 1370 O OD2 . ASP A 176 ? 0.3275 0.3403 0.3556 -0.0417 0.0150 0.0531 201 ASP A OD2 1371 N N . ALA A 177 ? 0.2835 0.3157 0.3134 -0.0257 0.0123 0.0378 202 ALA A N 1372 C CA . ALA A 177 ? 0.2732 0.3115 0.2961 -0.0242 0.0112 0.0378 202 ALA A CA 1373 C C . ALA A 177 ? 0.3002 0.3487 0.3152 -0.0296 0.0147 0.0402 202 ALA A C 1374 O O . ALA A 177 ? 0.3121 0.3702 0.3222 -0.0284 0.0150 0.0376 202 ALA A O 1375 C CB . ALA A 177 ? 0.2925 0.3206 0.3117 -0.0223 0.0067 0.0425 202 ALA A CB 1376 N N . ASN A 178 ? 0.3144 0.3612 0.3284 -0.0359 0.0172 0.0449 203 ASN A N 1377 C CA . ASN A 178 ? 0.3454 0.4027 0.3521 -0.0423 0.0211 0.0477 203 ASN A CA 1378 C C . ASN A 178 ? 0.3307 0.4012 0.3430 -0.0444 0.0259 0.0422 203 ASN A C 1379 O O . ASN A 178 ? 0.3504 0.4314 0.3582 -0.0503 0.0299 0.0439 203 ASN A O 1380 C CB . ASN A 178 ? 0.3670 0.4145 0.3679 -0.0491 0.0206 0.0575 203 ASN A CB 1381 C CG . ASN A 178 ? 0.4940 0.5292 0.4888 -0.0469 0.0153 0.0632 203 ASN A CG 1382 O OD1 . ASN A 178 ? 0.5399 0.5793 0.5292 -0.0438 0.0136 0.0623 203 ASN A OD1 1383 N ND2 . ASN A 178 ? 0.4555 0.4756 0.4517 -0.0482 0.0123 0.0687 203 ASN A ND2 1384 N N . GLY A 179 ? 0.2722 0.3426 0.2941 -0.0398 0.0255 0.0356 204 GLY A N 1385 C CA . GLY A 179 ? 0.2412 0.3232 0.2693 -0.0409 0.0291 0.0298 204 GLY A CA 1386 C C . GLY A 179 ? 0.2255 0.3034 0.2579 -0.0463 0.0309 0.0328 204 GLY A C 1387 O O . GLY A 179 ? 0.2840 0.3723 0.3214 -0.0484 0.0341 0.0288 204 GLY A O 1388 N N . ALA A 180 ? 0.2694 0.3322 0.3002 -0.0485 0.0286 0.0394 205 ALA A N 1389 C CA . ALA A 180 ? 0.2855 0.3426 0.3206 -0.0535 0.0297 0.0420 205 ALA A CA 1390 C C . ALA A 180 ? 0.3034 0.3608 0.3483 -0.0493 0.0293 0.0352 205 ALA A C 1391 O O . ALA A 180 ? 0.3113 0.3652 0.3591 -0.0426 0.0267 0.0311 205 ALA A O 1392 C CB . ALA A 180 ? 0.2923 0.3321 0.3243 -0.0552 0.0263 0.0494 205 ALA A CB 1393 N N . ILE A 181 ? 0.2447 0.3062 0.2944 -0.0535 0.0317 0.0341 206 ILE A N 1394 C CA . ILE A 181 ? 0.2402 0.3020 0.2986 -0.0501 0.0311 0.0280 206 ILE A CA 1395 C C . ILE A 181 ? 0.2377 0.2853 0.2986 -0.0521 0.0293 0.0312 206 ILE A C 1396 O O . ILE A 181 ? 0.2232 0.2701 0.2846 -0.0586 0.0308 0.0343 206 ILE A O 1397 C CB . ILE A 181 ? 0.2419 0.3196 0.3049 -0.0526 0.0346 0.0231 206 ILE A CB 1398 C CG1 . ILE A 181 ? 0.2330 0.3256 0.2935 -0.0504 0.0364 0.0192 206 ILE A CG1 1399 C CG2 . ILE A 181 ? 0.2352 0.3127 0.3069 -0.0489 0.0333 0.0170 206 ILE A CG2 1400 C CD1 . ILE A 181 ? 0.3024 0.4128 0.3677 -0.0526 0.0401 0.0139 206 ILE A CD1 1401 N N . LEU A 182 ? 0.2176 0.2544 0.2802 -0.0467 0.0261 0.0302 207 LEU A N 1402 C CA . LEU A 182 ? 0.2519 0.2746 0.3159 -0.0477 0.0239 0.0332 207 LEU A CA 1403 C C . LEU A 182 ? 0.2238 0.2439 0.2945 -0.0444 0.0229 0.0281 207 LEU A C 1404 O O . LEU A 182 ? 0.2046 0.2253 0.2772 -0.0386 0.0216 0.0242 207 LEU A O 1405 C CB . LEU A 182 ? 0.2605 0.2723 0.3204 -0.0443 0.0208 0.0368 207 LEU A CB 1406 C CG . LEU A 182 ? 0.2425 0.2558 0.2947 -0.0463 0.0208 0.0420 207 LEU A CG 1407 C CD1 . LEU A 182 ? 0.3004 0.3046 0.3502 -0.0412 0.0171 0.0437 207 LEU A CD1 1408 C CD2 . LEU A 182 ? 0.2667 0.2766 0.3148 -0.0541 0.0217 0.0485 207 LEU A CD2 1409 N N . ASP A 183 ? 0.2144 0.2312 0.2883 -0.0483 0.0233 0.0282 208 ASP A N 1410 C CA . ASP A 183 ? 0.2010 0.2134 0.2801 -0.0454 0.0219 0.0240 208 ASP A CA 1411 C C . ASP A 183 ? 0.2181 0.2163 0.2964 -0.0434 0.0192 0.0262 208 ASP A C 1412 O O . ASP A 183 ? 0.2263 0.2181 0.3006 -0.0435 0.0180 0.0307 208 ASP A O 1413 C CB . ASP A 183 ? 0.2040 0.2210 0.2876 -0.0498 0.0233 0.0218 208 ASP A CB 1414 C CG . ASP A 183 ? 0.2296 0.2406 0.3120 -0.0568 0.0236 0.0267 208 ASP A CG 1415 O OD1 . ASP A 183 ? 0.2467 0.2468 0.3253 -0.0575 0.0219 0.0315 208 ASP A OD1 1416 O OD2 . ASP A 183 ? 0.3113 0.3285 0.3971 -0.0618 0.0251 0.0255 208 ASP A OD2 1417 N N . ARG A 184 ? 0.2179 0.2117 0.3000 -0.0413 0.0181 0.0227 209 ARG A N 1418 C CA . ARG A 184 ? 0.2327 0.2149 0.3150 -0.0386 0.0157 0.0233 209 ARG A CA 1419 C C . ARG A 184 ? 0.2719 0.2443 0.3522 -0.0426 0.0145 0.0282 209 ARG A C 1420 O O . ARG A 184 ? 0.2494 0.2136 0.3277 -0.0403 0.0123 0.0309 209 ARG A O 1421 C CB . ARG A 184 ? 0.2291 0.2097 0.3154 -0.0368 0.0152 0.0185 209 ARG A CB 1422 C CG . ARG A 184 ? 0.2619 0.2315 0.3490 -0.0345 0.0131 0.0181 209 ARG A CG 1423 C CD . ARG A 184 ? 0.2464 0.2163 0.3365 -0.0326 0.0129 0.0129 209 ARG A CD 1424 N NE . ARG A 184 ? 0.2698 0.2312 0.3608 -0.0296 0.0113 0.0115 209 ARG A NE 1425 C CZ . ARG A 184 ? 0.2466 0.2078 0.3393 -0.0273 0.0111 0.0070 209 ARG A CZ 1426 N NH1 . ARG A 184 ? 0.2724 0.2403 0.3656 -0.0277 0.0121 0.0040 209 ARG A NH1 1427 N NH2 . ARG A 184 ? 0.2992 0.2539 0.3930 -0.0243 0.0098 0.0053 209 ARG A NH2 1428 N N . GLN A 185 ? 0.2424 0.2156 0.3235 -0.0487 0.0154 0.0295 210 GLN A N 1429 C CA . GLN A 185 ? 0.2762 0.2390 0.3553 -0.0533 0.0137 0.0346 210 GLN A CA 1430 C C . GLN A 185 ? 0.3270 0.2885 0.4001 -0.0549 0.0133 0.0410 210 GLN A C 1431 O O . GLN A 185 ? 0.3830 0.3326 0.4535 -0.0553 0.0103 0.0453 210 GLN A O 1432 C CB . GLN A 185 ? 0.2720 0.2371 0.3534 -0.0605 0.0149 0.0349 210 GLN A CB 1433 C CG . GLN A 185 ? 0.3268 0.2917 0.4137 -0.0592 0.0145 0.0288 210 GLN A CG 1434 C CD . GLN A 185 ? 0.5607 0.5134 0.6487 -0.0545 0.0114 0.0266 210 GLN A CD 1435 O OE1 . GLN A 185 ? 0.6018 0.5426 0.6884 -0.0554 0.0086 0.0300 210 GLN A OE1 1436 N NE2 . GLN A 185 ? 0.5543 0.5101 0.6449 -0.0494 0.0115 0.0209 210 GLN A NE2 1437 N N . ALA A 186 ? 0.2575 0.2311 0.3282 -0.0555 0.0161 0.0413 211 ALA A N 1438 C CA . ALA A 186 ? 0.2632 0.2374 0.3272 -0.0573 0.0160 0.0471 211 ALA A CA 1439 C C . ALA A 186 ? 0.2950 0.2637 0.3566 -0.0507 0.0133 0.0476 211 ALA A C 1440 O O . ALA A 186 ? 0.3215 0.2826 0.3782 -0.0516 0.0108 0.0532 211 ALA A O 1441 C CB . ALA A 186 ? 0.2730 0.2632 0.3352 -0.0596 0.0199 0.0461 211 ALA A CB 1442 N N . MET A 187 ? 0.2426 0.2152 0.3078 -0.0445 0.0134 0.0421 212 MET A N 1443 C CA . MET A 187 ? 0.2681 0.2375 0.3320 -0.0386 0.0110 0.0422 212 MET A CA 1444 C C . MET A 187 ? 0.2694 0.2256 0.3354 -0.0357 0.0074 0.0428 212 MET A C 1445 O O . MET A 187 ? 0.2944 0.2459 0.3587 -0.0321 0.0047 0.0447 212 MET A O 1446 C CB . MET A 187 ? 0.2671 0.2452 0.3339 -0.0335 0.0122 0.0365 212 MET A CB 1447 C CG . MET A 187 ? 0.2364 0.2129 0.3091 -0.0309 0.0122 0.0313 212 MET A CG 1448 S SD . MET A 187 ? 0.2357 0.2214 0.3110 -0.0260 0.0130 0.0257 212 MET A SD 1449 C CE . MET A 187 ? 0.2292 0.2262 0.3052 -0.0295 0.0158 0.0234 212 MET A CE 1450 N N . GLY A 188 ? 0.2601 0.2110 0.3301 -0.0370 0.0072 0.0407 213 GLY A N 1451 C CA . GLY A 188 ? 0.2735 0.2124 0.3461 -0.0341 0.0038 0.0402 213 GLY A CA 1452 C C . GLY A 188 ? 0.2845 0.2256 0.3620 -0.0280 0.0039 0.0341 213 GLY A C 1453 O O . GLY A 188 ? 0.2538 0.2041 0.3318 -0.0256 0.0058 0.0314 213 GLY A O 1454 N N . GLU A 189 ? 0.2830 0.2157 0.3641 -0.0255 0.0017 0.0317 214 GLU A N 1455 C CA . GLU A 189 ? 0.2795 0.2154 0.3651 -0.0207 0.0024 0.0256 214 GLU A CA 1456 C C . GLU A 189 ? 0.2820 0.2215 0.3682 -0.0154 0.0018 0.0248 214 GLU A C 1457 O O . GLU A 189 ? 0.2885 0.2350 0.3770 -0.0130 0.0036 0.0208 214 GLU A O 1458 C CB . GLU A 189 ? 0.3271 0.2545 0.4164 -0.0194 0.0005 0.0223 214 GLU A CB 1459 C CG . GLU A 189 ? 0.3352 0.2619 0.4252 -0.0241 0.0017 0.0207 214 GLU A CG 1460 C CD . GLU A 189 ? 0.3945 0.3322 0.4851 -0.0247 0.0052 0.0170 214 GLU A CD 1461 O OE1 . GLU A 189 ? 0.3514 0.2925 0.4442 -0.0209 0.0059 0.0124 214 GLU A OE1 1462 O OE2 . GLU A 189 ? 0.3997 0.3429 0.4886 -0.0289 0.0070 0.0188 214 GLU A OE2 1463 N N . ASP A 190 ? 0.2384 0.1735 0.3227 -0.0140 -0.0010 0.0287 215 ASP A N 1464 C CA . ASP A 190 ? 0.2693 0.2084 0.3546 -0.0093 -0.0019 0.0280 215 ASP A CA 1465 C C . ASP A 190 ? 0.2496 0.1992 0.3327 -0.0101 0.0007 0.0280 215 ASP A C 1466 O O . ASP A 190 ? 0.2491 0.2046 0.3347 -0.0071 0.0015 0.0248 215 ASP A O 1467 C CB . ASP A 190 ? 0.3214 0.2533 0.4047 -0.0076 -0.0060 0.0324 215 ASP A CB 1468 C CG . ASP A 190 ? 0.4321 0.3551 0.5199 -0.0036 -0.0095 0.0304 215 ASP A CG 1469 O OD1 . ASP A 190 ? 0.3454 0.2705 0.4386 -0.0010 -0.0083 0.0247 215 ASP A OD1 1470 O OD2 . ASP A 190 ? 0.4826 0.3966 0.5687 -0.0030 -0.0138 0.0344 215 ASP A OD2 1471 N N . VAL A 191 ? 0.2447 0.1967 0.3230 -0.0143 0.0018 0.0314 216 VAL A N 1472 C CA . VAL A 191 ? 0.2410 0.2028 0.3173 -0.0147 0.0039 0.0306 216 VAL A CA 1473 C C . VAL A 191 ? 0.2250 0.1930 0.3044 -0.0150 0.0066 0.0260 216 VAL A C 1474 O O . VAL A 191 ? 0.2178 0.1920 0.2981 -0.0129 0.0072 0.0235 216 VAL A O 1475 C CB . VAL A 191 ? 0.2235 0.1879 0.2940 -0.0189 0.0046 0.0350 216 VAL A CB 1476 C CG1 . VAL A 191 ? 0.2301 0.2052 0.2992 -0.0184 0.0065 0.0329 216 VAL A CG1 1477 C CG2 . VAL A 191 ? 0.2572 0.2152 0.3237 -0.0185 0.0014 0.0401 216 VAL A CG2 1478 N N . PHE A 192 ? 0.2277 0.1932 0.3085 -0.0176 0.0076 0.0249 217 PHE A N 1479 C CA . PHE A 192 ? 0.2031 0.1738 0.2864 -0.0179 0.0096 0.0206 217 PHE A CA 1480 C C . PHE A 192 ? 0.2250 0.1959 0.3115 -0.0140 0.0092 0.0171 217 PHE A C 1481 O O . PHE A 192 ? 0.1944 0.1708 0.2817 -0.0133 0.0102 0.0144 217 PHE A O 1482 C CB . PHE A 192 ? 0.2132 0.1811 0.2974 -0.0217 0.0104 0.0199 217 PHE A CB 1483 C CG . PHE A 192 ? 0.2027 0.1759 0.2891 -0.0218 0.0118 0.0156 217 PHE A CG 1484 C CD1 . PHE A 192 ? 0.2106 0.1922 0.2965 -0.0228 0.0130 0.0146 217 PHE A CD1 1485 C CD2 . PHE A 192 ? 0.1994 0.1693 0.2882 -0.0206 0.0115 0.0123 217 PHE A CD2 1486 C CE1 . PHE A 192 ? 0.2056 0.1913 0.2933 -0.0225 0.0135 0.0109 217 PHE A CE1 1487 C CE2 . PHE A 192 ? 0.2289 0.2033 0.3187 -0.0208 0.0124 0.0088 217 PHE A CE2 1488 C CZ . PHE A 192 ? 0.2117 0.1936 0.3010 -0.0217 0.0132 0.0083 217 PHE A CZ 1489 N N . TRP A 193 ? 0.2225 0.1877 0.3107 -0.0115 0.0076 0.0171 218 TRP A N 1490 C CA . TRP A 193 ? 0.2192 0.1862 0.3107 -0.0078 0.0075 0.0140 218 TRP A CA 1491 C C . TRP A 193 ? 0.2105 0.1829 0.3016 -0.0060 0.0071 0.0147 218 TRP A C 1492 O O . TRP A 193 ? 0.2045 0.1819 0.2968 -0.0053 0.0080 0.0124 218 TRP A O 1493 C CB . TRP A 193 ? 0.2302 0.1905 0.3244 -0.0052 0.0056 0.0135 218 TRP A CB 1494 C CG . TRP A 193 ? 0.2112 0.1748 0.3095 -0.0014 0.0056 0.0101 218 TRP A CG 1495 C CD1 . TRP A 193 ? 0.2449 0.2109 0.3457 -0.0005 0.0072 0.0057 218 TRP A CD1 1496 C CD2 . TRP A 193 ? 0.2130 0.1785 0.3133 0.0018 0.0040 0.0108 218 TRP A CD2 1497 N NE1 . TRP A 193 ? 0.2121 0.1822 0.3165 0.0027 0.0071 0.0037 218 TRP A NE1 1498 C CE2 . TRP A 193 ? 0.2194 0.1893 0.3240 0.0042 0.0051 0.0066 218 TRP A CE2 1499 C CE3 . TRP A 193 ? 0.2282 0.1928 0.3269 0.0027 0.0018 0.0143 218 TRP A CE3 1500 C CZ2 . TRP A 193 ? 0.2165 0.1902 0.3248 0.0073 0.0040 0.0058 218 TRP A CZ2 1501 C CZ3 . TRP A 193 ? 0.2436 0.2114 0.3457 0.0062 0.0003 0.0135 218 TRP A CZ3 1502 C CH2 . TRP A 193 ? 0.2020 0.1745 0.3094 0.0084 0.0015 0.0092 218 TRP A CH2 1503 N N . ALA A 194 ? 0.1999 0.1711 0.2889 -0.0055 0.0054 0.0180 219 ALA A N 1504 C CA . ALA A 194 ? 0.2080 0.1838 0.2967 -0.0036 0.0045 0.0184 219 ALA A CA 1505 C C . ALA A 194 ? 0.1829 0.1652 0.2704 -0.0047 0.0057 0.0170 219 ALA A C 1506 O O . ALA A 194 ? 0.1847 0.1705 0.2737 -0.0031 0.0051 0.0155 219 ALA A O 1507 C CB . ALA A 194 ? 0.2260 0.1993 0.3114 -0.0033 0.0023 0.0223 219 ALA A CB 1508 N N . ILE A 195 ? 0.2009 0.1846 0.2859 -0.0075 0.0070 0.0173 220 ILE A N 1509 C CA . ILE A 195 ? 0.1751 0.1649 0.2593 -0.0078 0.0075 0.0155 220 ILE A CA 1510 C C . ILE A 195 ? 0.1755 0.1667 0.2622 -0.0075 0.0080 0.0125 220 ILE A C 1511 O O . ILE A 195 ? 0.1930 0.1879 0.2797 -0.0070 0.0073 0.0109 220 ILE A O 1512 C CB . ILE A 195 ? 0.1756 0.1687 0.2572 -0.0106 0.0088 0.0161 220 ILE A CB 1513 C CG1 . ILE A 195 ? 0.1893 0.1802 0.2720 -0.0133 0.0104 0.0155 220 ILE A CG1 1514 C CG2 . ILE A 195 ? 0.2100 0.2027 0.2879 -0.0115 0.0085 0.0196 220 ILE A CG2 1515 C CD1 . ILE A 195 ? 0.2091 0.2052 0.2906 -0.0163 0.0119 0.0154 220 ILE A CD1 1516 N N . ARG A 196 ? 0.1779 0.1659 0.2664 -0.0077 0.0088 0.0116 221 ARG A N 1517 C CA . ARG A 196 ? 0.1901 0.1795 0.2799 -0.0079 0.0093 0.0091 221 ARG A CA 1518 C C . ARG A 196 ? 0.1748 0.1652 0.2665 -0.0062 0.0088 0.0085 221 ARG A C 1519 O O . ARG A 196 ? 0.1745 0.1646 0.2677 -0.0061 0.0097 0.0070 221 ARG A O 1520 C CB . ARG A 196 ? 0.1869 0.1733 0.2773 -0.0092 0.0106 0.0077 221 ARG A CB 1521 C CG . ARG A 196 ? 0.2177 0.2043 0.3069 -0.0118 0.0112 0.0077 221 ARG A CG 1522 C CD . ARG A 196 ? 0.1811 0.1642 0.2712 -0.0130 0.0119 0.0060 221 ARG A CD 1523 N NE . ARG A 196 ? 0.2281 0.2053 0.3190 -0.0126 0.0116 0.0072 221 ARG A NE 1524 C CZ . ARG A 196 ? 0.2696 0.2427 0.3620 -0.0122 0.0116 0.0051 221 ARG A CZ 1525 N NH1 . ARG A 196 ? 0.2660 0.2410 0.3587 -0.0124 0.0124 0.0018 221 ARG A NH1 1526 N NH2 . ARG A 196 ? 0.2699 0.2368 0.3633 -0.0115 0.0105 0.0062 221 ARG A NH2 1527 N N . GLY A 197 ? 0.1843 0.1767 0.2761 -0.0051 0.0072 0.0094 222 GLY A N 1528 C CA . GLY A 197 ? 0.1923 0.1864 0.2864 -0.0041 0.0066 0.0090 222 GLY A CA 1529 C C . GLY A 197 ? 0.1637 0.1583 0.2594 -0.0022 0.0050 0.0102 222 GLY A C 1530 O O . GLY A 197 ? 0.1656 0.1625 0.2638 -0.0017 0.0042 0.0099 222 GLY A O 1531 N N . GLY A 198 ? 0.1610 0.1535 0.2549 -0.0015 0.0045 0.0118 223 GLY A N 1532 C CA . GLY A 198 ? 0.1719 0.1644 0.2666 0.0005 0.0025 0.0133 223 GLY A CA 1533 C C . GLY A 198 ? 0.1836 0.1791 0.2770 0.0010 0.0005 0.0133 223 GLY A C 1534 O O . GLY A 198 ? 0.1879 0.1838 0.2817 0.0026 -0.0015 0.0143 223 GLY A O 1535 N N . GLY A 199 ? 0.1696 0.1670 0.2618 -0.0002 0.0006 0.0120 224 GLY A N 1536 C CA . GLY A 199 ? 0.1644 0.1642 0.2558 0.0005 -0.0018 0.0112 224 GLY A CA 1537 C C . GLY A 199 ? 0.1597 0.1611 0.2471 0.0006 -0.0019 0.0109 224 GLY A C 1538 O O . GLY A 199 ? 0.1811 0.1821 0.2658 0.0003 -0.0008 0.0126 224 GLY A O 1539 N N . GLY A 200 ? 0.1711 0.1747 0.2582 0.0010 -0.0034 0.0086 225 GLY A N 1540 C CA . GLY A 200 ? 0.1598 0.1669 0.2437 0.0016 -0.0036 0.0072 225 GLY A CA 1541 C C . GLY A 200 ? 0.1758 0.1850 0.2573 0.0031 -0.0053 0.0076 225 GLY A C 1542 O O . GLY A 200 ? 0.1904 0.1982 0.2733 0.0041 -0.0073 0.0082 225 GLY A O 1543 N N . GLY A 201 ? 0.1628 0.1760 0.2403 0.0030 -0.0043 0.0071 226 GLY A N 1544 C CA . GLY A 201 ? 0.1663 0.1825 0.2401 0.0043 -0.0059 0.0071 226 GLY A CA 1545 C C . GLY A 201 ? 0.1843 0.1979 0.2556 0.0038 -0.0058 0.0115 226 GLY A C 1546 O O . GLY A 201 ? 0.1896 0.2045 0.2584 0.0052 -0.0081 0.0119 226 GLY A O 1547 N N . VAL A 202 ? 0.1859 0.1956 0.2577 0.0019 -0.0037 0.0146 227 VAL A N 1548 C CA . VAL A 202 ? 0.1900 0.1953 0.2606 0.0019 -0.0045 0.0186 227 VAL A CA 1549 C C . VAL A 202 ? 0.1987 0.2019 0.2651 -0.0008 -0.0024 0.0223 227 VAL A C 1550 O O . VAL A 202 ? 0.2110 0.2115 0.2737 -0.0010 -0.0038 0.0261 227 VAL A O 1551 C CB . VAL A 202 ? 0.2030 0.2038 0.2794 0.0029 -0.0050 0.0186 227 VAL A CB 1552 C CG1 . VAL A 202 ? 0.2188 0.2149 0.2949 0.0036 -0.0064 0.0221 227 VAL A CG1 1553 C CG2 . VAL A 202 ? 0.2047 0.2075 0.2852 0.0047 -0.0072 0.0158 227 VAL A CG2 1554 N N . TRP A 203 ? 0.1933 0.1974 0.2604 -0.0032 0.0005 0.0216 228 TRP A N 1555 C CA . TRP A 203 ? 0.1937 0.1946 0.2583 -0.0065 0.0023 0.0252 228 TRP A CA 1556 C C . TRP A 203 ? 0.2106 0.2178 0.2704 -0.0096 0.0046 0.0258 228 TRP A C 1557 O O . TRP A 203 ? 0.2350 0.2400 0.2913 -0.0131 0.0058 0.0298 228 TRP A O 1558 C CB . TRP A 203 ? 0.2571 0.2543 0.3265 -0.0075 0.0039 0.0240 228 TRP A CB 1559 C CG . TRP A 203 ? 0.2331 0.2272 0.3074 -0.0046 0.0024 0.0222 228 TRP A CG 1560 C CD1 . TRP A 203 ? 0.2004 0.1971 0.2784 -0.0032 0.0024 0.0186 228 TRP A CD1 1561 C CD2 . TRP A 203 ? 0.2097 0.1983 0.2859 -0.0028 0.0005 0.0239 228 TRP A CD2 1562 N NE1 . TRP A 203 ? 0.1951 0.1889 0.2769 -0.0013 0.0012 0.0182 228 TRP A NE1 1563 C CE2 . TRP A 203 ? 0.1999 0.1894 0.2813 -0.0007 0.0001 0.0210 228 TRP A CE2 1564 C CE3 . TRP A 203 ? 0.2196 0.2025 0.2938 -0.0027 -0.0011 0.0277 228 TRP A CE3 1565 C CZ2 . TRP A 203 ? 0.2049 0.1914 0.2901 0.0016 -0.0015 0.0210 228 TRP A CZ2 1566 C CZ3 . TRP A 203 ? 0.2342 0.2129 0.3123 0.0002 -0.0033 0.0276 228 TRP A CZ3 1567 C CH2 . TRP A 203 ? 0.2079 0.1893 0.2918 0.0024 -0.0032 0.0240 228 TRP A CH2 1568 N N . GLY A 204 ? 0.2160 0.2311 0.2758 -0.0084 0.0050 0.0217 229 GLY A N 1569 C CA . GLY A 204 ? 0.1992 0.2227 0.2564 -0.0109 0.0077 0.0204 229 GLY A CA 1570 C C . GLY A 204 ? 0.1977 0.2262 0.2597 -0.0088 0.0079 0.0144 229 GLY A C 1571 O O . GLY A 204 ? 0.2038 0.2287 0.2699 -0.0059 0.0058 0.0122 229 GLY A O 1572 N N . ALA A 205 ? 0.1764 0.2133 0.2383 -0.0104 0.0103 0.0119 230 ALA A N 1573 C CA . ALA A 205 ? 0.1712 0.2128 0.2379 -0.0081 0.0099 0.0061 230 ALA A CA 1574 C C . ALA A 205 ? 0.1916 0.2318 0.2621 -0.0105 0.0117 0.0061 230 ALA A C 1575 O O . ALA A 205 ? 0.1952 0.2397 0.2648 -0.0144 0.0146 0.0075 230 ALA A O 1576 C CB . ALA A 205 ? 0.1953 0.2486 0.2603 -0.0071 0.0108 0.0018 230 ALA A CB 1577 N N . ILE A 206 ? 0.1511 0.1857 0.2258 -0.0087 0.0099 0.0046 231 ILE A N 1578 C CA . ILE A 206 ? 0.1737 0.2078 0.2519 -0.0106 0.0112 0.0038 231 ILE A CA 1579 C C . ILE A 206 ? 0.1745 0.2187 0.2551 -0.0098 0.0117 -0.0011 231 ILE A C 1580 O O . ILE A 206 ? 0.1842 0.2312 0.2663 -0.0060 0.0092 -0.0053 231 ILE A O 1581 C CB . ILE A 206 ? 0.1622 0.1890 0.2434 -0.0087 0.0091 0.0031 231 ILE A CB 1582 C CG1 . ILE A 206 ? 0.1893 0.2077 0.2693 -0.0090 0.0087 0.0071 231 ILE A CG1 1583 C CG2 . ILE A 206 ? 0.1725 0.1998 0.2568 -0.0104 0.0100 0.0016 231 ILE A CG2 1584 C CD1 . ILE A 206 ? 0.2124 0.2267 0.2919 -0.0124 0.0107 0.0103 231 ILE A CD1 1585 N N . TYR A 207 ? 0.1596 0.2093 0.2409 -0.0135 0.0145 -0.0009 232 TYR A N 1586 C CA . TYR A 207 ? 0.1466 0.2070 0.2316 -0.0128 0.0151 -0.0061 232 TYR A CA 1587 C C . TYR A 207 ? 0.1636 0.2210 0.2535 -0.0115 0.0131 -0.0087 232 TYR A C 1588 O O . TYR A 207 ? 0.1849 0.2461 0.2779 -0.0077 0.0106 -0.0137 232 TYR A O 1589 C CB . TYR A 207 ? 0.1954 0.2651 0.2797 -0.0178 0.0191 -0.0050 232 TYR A CB 1590 C CG . TYR A 207 ? 0.2047 0.2845 0.2946 -0.0177 0.0197 -0.0104 232 TYR A CG 1591 C CD1 . TYR A 207 ? 0.2321 0.3209 0.3250 -0.0130 0.0181 -0.0169 232 TYR A CD1 1592 C CD2 . TYR A 207 ? 0.2187 0.2987 0.3118 -0.0217 0.0212 -0.0094 232 TYR A CD2 1593 C CE1 . TYR A 207 ? 0.2711 0.3694 0.3701 -0.0122 0.0180 -0.0223 232 TYR A CE1 1594 C CE2 . TYR A 207 ? 0.2260 0.3158 0.3250 -0.0214 0.0213 -0.0146 232 TYR A CE2 1595 C CZ . TYR A 207 ? 0.2635 0.3626 0.3656 -0.0164 0.0197 -0.0210 232 TYR A CZ 1596 O OH . TYR A 207 ? 0.3038 0.4130 0.4125 -0.0155 0.0193 -0.0266 232 TYR A OH 1597 N N . ALA A 208 ? 0.1780 0.2282 0.2681 -0.0143 0.0138 -0.0055 233 ALA A N 1598 C CA . ALA A 208 ? 0.1706 0.2180 0.2642 -0.0136 0.0121 -0.0076 233 ALA A CA 1599 C C . ALA A 208 ? 0.1901 0.2270 0.2824 -0.0154 0.0121 -0.0040 233 ALA A C 1600 O O . ALA A 208 ? 0.1920 0.2249 0.2819 -0.0181 0.0140 -0.0001 233 ALA A O 1601 C CB . ALA A 208 ? 0.2003 0.2570 0.2979 -0.0159 0.0136 -0.0105 233 ALA A CB 1602 N N . TRP A 209 ? 0.1682 0.2006 0.2619 -0.0136 0.0098 -0.0054 234 TRP A N 1603 C CA . TRP A 209 ? 0.1737 0.1978 0.2664 -0.0149 0.0099 -0.0032 234 TRP A CA 1604 C C . TRP A 209 ? 0.1814 0.2071 0.2766 -0.0170 0.0099 -0.0051 234 TRP A C 1605 O O . TRP A 209 ? 0.1902 0.2210 0.2878 -0.0155 0.0082 -0.0085 234 TRP A O 1606 C CB . TRP A 209 ? 0.1566 0.1753 0.2484 -0.0120 0.0072 -0.0034 234 TRP A CB 1607 C CG . TRP A 209 ? 0.1602 0.1768 0.2503 -0.0099 0.0064 -0.0019 234 TRP A CG 1608 C CD1 . TRP A 209 ? 0.2201 0.2386 0.3105 -0.0069 0.0038 -0.0037 234 TRP A CD1 1609 C CD2 . TRP A 209 ? 0.1646 0.1766 0.2529 -0.0104 0.0076 0.0013 234 TRP A CD2 1610 N NE1 . TRP A 209 ? 0.1898 0.2054 0.2785 -0.0060 0.0036 -0.0017 234 TRP A NE1 1611 C CE2 . TRP A 209 ? 0.1697 0.1816 0.2572 -0.0079 0.0059 0.0014 234 TRP A CE2 1612 C CE3 . TRP A 209 ? 0.1854 0.1930 0.2731 -0.0124 0.0095 0.0038 234 TRP A CE3 1613 C CZ2 . TRP A 209 ? 0.1994 0.2079 0.2857 -0.0075 0.0061 0.0040 234 TRP A CZ2 1614 C CZ3 . TRP A 209 ? 0.2224 0.2261 0.3088 -0.0116 0.0095 0.0063 234 TRP A CZ3 1615 C CH2 . TRP A 209 ? 0.1848 0.1895 0.2706 -0.0092 0.0079 0.0064 234 TRP A CH2 1616 N N . LYS A 210 ? 0.1731 0.1940 0.2678 -0.0200 0.0114 -0.0033 235 LYS A N 1617 C CA . LYS A 210 ? 0.1653 0.1863 0.2620 -0.0216 0.0108 -0.0054 235 LYS A CA 1618 C C . LYS A 210 ? 0.1536 0.1672 0.2483 -0.0203 0.0096 -0.0053 235 LYS A C 1619 O O . LYS A 210 ? 0.1837 0.1912 0.2767 -0.0207 0.0106 -0.0032 235 LYS A O 1620 C CB . LYS A 210 ? 0.1762 0.1978 0.2743 -0.0262 0.0130 -0.0044 235 LYS A CB 1621 C CG . LYS A 210 ? 0.1799 0.2027 0.2806 -0.0280 0.0121 -0.0073 235 LYS A CG 1622 C CD . LYS A 210 ? 0.1751 0.1972 0.2774 -0.0332 0.0139 -0.0061 235 LYS A CD 1623 C CE . LYS A 210 ? 0.2262 0.2498 0.3314 -0.0349 0.0125 -0.0094 235 LYS A CE 1624 N NZ . LYS A 210 ? 0.2865 0.3086 0.3936 -0.0404 0.0139 -0.0083 235 LYS A NZ 1625 N N . ILE A 211 ? 0.1666 0.1811 0.2613 -0.0186 0.0071 -0.0075 236 ILE A N 1626 C CA . ILE A 211 ? 0.2004 0.2093 0.2924 -0.0176 0.0060 -0.0073 236 ILE A CA 1627 C C . ILE A 211 ? 0.1750 0.1836 0.2670 -0.0191 0.0051 -0.0095 236 ILE A C 1628 O O . ILE A 211 ? 0.1830 0.1966 0.2777 -0.0198 0.0040 -0.0117 236 ILE A O 1629 C CB . ILE A 211 ? 0.1781 0.1867 0.2685 -0.0147 0.0032 -0.0072 236 ILE A CB 1630 C CG1 . ILE A 211 ? 0.1745 0.1879 0.2669 -0.0133 0.0001 -0.0099 236 ILE A CG1 1631 C CG2 . ILE A 211 ? 0.2133 0.2215 0.3035 -0.0132 0.0038 -0.0053 236 ILE A CG2 1632 C CD1 . ILE A 211 ? 0.2000 0.2113 0.2907 -0.0105 -0.0036 -0.0097 236 ILE A CD1 1633 N N . LYS A 212 ? 0.1848 0.1886 0.2741 -0.0194 0.0055 -0.0093 237 LYS A N 1634 C CA . LYS A 212 ? 0.1899 0.1933 0.2781 -0.0204 0.0042 -0.0116 237 LYS A CA 1635 C C . LYS A 212 ? 0.1919 0.1955 0.2769 -0.0187 0.0012 -0.0117 237 LYS A C 1636 O O . LYS A 212 ? 0.2131 0.2141 0.2952 -0.0176 0.0012 -0.0097 237 LYS A O 1637 C CB . LYS A 212 ? 0.2173 0.2159 0.3036 -0.0214 0.0060 -0.0120 237 LYS A CB 1638 C CG . LYS A 212 ? 0.2304 0.2289 0.3153 -0.0226 0.0048 -0.0150 237 LYS A CG 1639 C CD . LYS A 212 ? 0.2381 0.2389 0.3267 -0.0249 0.0043 -0.0171 237 LYS A CD 1640 C CE . LYS A 212 ? 0.3125 0.3141 0.3995 -0.0257 0.0021 -0.0204 237 LYS A CE 1641 N NZ . LYS A 212 ? 0.4654 0.4698 0.5570 -0.0284 0.0015 -0.0226 237 LYS A NZ 1642 N N . LEU A 213 ? 0.1688 0.1755 0.2545 -0.0186 -0.0016 -0.0138 238 LEU A N 1643 C CA . LEU A 213 ? 0.1937 0.1996 0.2760 -0.0171 -0.0054 -0.0137 238 LEU A CA 1644 C C . LEU A 213 ? 0.2044 0.2072 0.2814 -0.0185 -0.0053 -0.0138 238 LEU A C 1645 O O . LEU A 213 ? 0.2123 0.2150 0.2896 -0.0202 -0.0036 -0.0159 238 LEU A O 1646 C CB . LEU A 213 ? 0.1839 0.1943 0.2693 -0.0160 -0.0091 -0.0162 238 LEU A CB 1647 C CG . LEU A 213 ? 0.1887 0.2039 0.2793 -0.0143 -0.0092 -0.0169 238 LEU A CG 1648 C CD1 . LEU A 213 ? 0.2285 0.2497 0.3232 -0.0127 -0.0130 -0.0204 238 LEU A CD1 1649 C CD2 . LEU A 213 ? 0.2133 0.2255 0.3022 -0.0120 -0.0101 -0.0145 238 LEU A CD2 1650 N N . LEU A 214 ? 0.2026 0.2028 0.2744 -0.0180 -0.0072 -0.0118 239 LEU A N 1651 C CA . LEU A 214 ? 0.2042 0.2025 0.2702 -0.0195 -0.0062 -0.0115 239 LEU A CA 1652 C C . LEU A 214 ? 0.1931 0.1909 0.2537 -0.0199 -0.0105 -0.0114 239 LEU A C 1653 O O . LEU A 214 ? 0.2160 0.2129 0.2762 -0.0186 -0.0147 -0.0099 239 LEU A O 1654 C CB . LEU A 214 ? 0.2061 0.2025 0.2700 -0.0197 -0.0038 -0.0085 239 LEU A CB 1655 C CG . LEU A 214 ? 0.2232 0.2196 0.2920 -0.0190 -0.0003 -0.0082 239 LEU A CG 1656 C CD1 . LEU A 214 ? 0.2340 0.2293 0.3018 -0.0188 0.0008 -0.0051 239 LEU A CD1 1657 C CD2 . LEU A 214 ? 0.2925 0.2889 0.3626 -0.0198 0.0030 -0.0108 239 LEU A CD2 1658 N N . PRO A 215 ? 0.1942 0.1923 0.2502 -0.0214 -0.0098 -0.0130 240 PRO A N 1659 C CA . PRO A 215 ? 0.2035 0.2011 0.2534 -0.0219 -0.0143 -0.0128 240 PRO A CA 1660 C C . PRO A 215 ? 0.2328 0.2275 0.2763 -0.0226 -0.0164 -0.0081 240 PRO A C 1661 O O . PRO A 215 ? 0.2260 0.2200 0.2673 -0.0238 -0.0130 -0.0059 240 PRO A O 1662 C CB . PRO A 215 ? 0.2497 0.2487 0.2957 -0.0236 -0.0123 -0.0159 240 PRO A CB 1663 C CG . PRO A 215 ? 0.2774 0.2771 0.3291 -0.0236 -0.0076 -0.0184 240 PRO A CG 1664 C CD . PRO A 215 ? 0.2649 0.2636 0.3209 -0.0226 -0.0055 -0.0155 240 PRO A CD 1665 N N . VAL A 216 ? 0.2120 0.2046 0.2526 -0.0218 -0.0223 -0.0067 241 VAL A N 1666 C CA . VAL A 216 ? 0.2163 0.2049 0.2493 -0.0233 -0.0254 -0.0018 241 VAL A CA 1667 C C . VAL A 216 ? 0.2271 0.2146 0.2540 -0.0235 -0.0311 -0.0019 241 VAL A C 1668 O O . VAL A 216 ? 0.2211 0.2105 0.2521 -0.0214 -0.0340 -0.0055 241 VAL A O 1669 C CB . VAL A 216 ? 0.2220 0.2067 0.2584 -0.0215 -0.0287 0.0011 241 VAL A CB 1670 C CG1 . VAL A 216 ? 0.2380 0.2236 0.2792 -0.0215 -0.0235 0.0016 241 VAL A CG1 1671 C CG2 . VAL A 216 ? 0.2046 0.1899 0.2473 -0.0178 -0.0334 -0.0018 241 VAL A CG2 1672 N N . PRO A 217 ? 0.2210 0.2060 0.2378 -0.0264 -0.0326 0.0020 242 PRO A N 1673 C CA . PRO A 217 ? 0.2605 0.2436 0.2702 -0.0267 -0.0389 0.0027 242 PRO A CA 1674 C C . PRO A 217 ? 0.2041 0.1822 0.2167 -0.0236 -0.0467 0.0044 242 PRO A C 1675 O O . PRO A 217 ? 0.2317 0.2068 0.2488 -0.0223 -0.0470 0.0063 242 PRO A O 1676 C CB . PRO A 217 ? 0.3025 0.2837 0.3003 -0.0311 -0.0383 0.0079 242 PRO A CB 1677 C CG . PRO A 217 ? 0.3104 0.2945 0.3103 -0.0330 -0.0307 0.0084 242 PRO A CG 1678 C CD . PRO A 217 ? 0.2415 0.2256 0.2530 -0.0297 -0.0290 0.0062 242 PRO A CD 1679 N N . GLU A 218 ? 0.2632 0.2404 0.2733 -0.0221 -0.0531 0.0032 243 GLU A N 1680 C CA . GLU A 218 ? 0.2519 0.2246 0.2654 -0.0184 -0.0612 0.0041 243 GLU A CA 1681 C C . GLU A 218 ? 0.2634 0.2272 0.2699 -0.0200 -0.0657 0.0111 243 GLU A C 1682 O O . GLU A 218 ? 0.3013 0.2602 0.3124 -0.0169 -0.0709 0.0119 243 GLU A O 1683 C CB . GLU A 218 ? 0.3203 0.2946 0.3332 -0.0163 -0.0676 0.0010 243 GLU A CB 1684 C CG . GLU A 218 ? 0.3539 0.3368 0.3768 -0.0143 -0.0643 -0.0062 243 GLU A CG 1685 C CD . GLU A 218 ? 0.6026 0.5881 0.6275 -0.0117 -0.0712 -0.0098 243 GLU A CD 1686 O OE1 . GLU A 218 ? 0.6234 0.6064 0.6387 -0.0131 -0.0755 -0.0080 243 GLU A OE1 1687 O OE2 . GLU A 218 ? 0.6314 0.6220 0.6674 -0.0082 -0.0723 -0.0146 243 GLU A OE2 1688 N N . LYS A 219 ? 0.2638 0.2256 0.2594 -0.0251 -0.0636 0.0159 244 LYS A N 1689 C CA . LYS A 219 ? 0.2775 0.2313 0.2663 -0.0281 -0.0665 0.0232 244 LYS A CA 1690 C C . LYS A 219 ? 0.2775 0.2345 0.2634 -0.0329 -0.0580 0.0256 244 LYS A C 1691 O O . LYS A 219 ? 0.2962 0.2591 0.2767 -0.0359 -0.0527 0.0245 244 LYS A O 1692 C CB . LYS A 219 ? 0.3256 0.2731 0.3020 -0.0304 -0.0741 0.0283 244 LYS A CB 1693 C CG . LYS A 219 ? 0.3912 0.3347 0.3702 -0.0253 -0.0838 0.0263 244 LYS A CG 1694 C CD . LYS A 219 ? 0.5005 0.4383 0.4889 -0.0207 -0.0890 0.0258 244 LYS A CD 1695 C CE . LYS A 219 ? 0.5742 0.5098 0.5666 -0.0148 -0.0986 0.0226 244 LYS A CE 1696 N NZ . LYS A 219 ? 0.5680 0.4970 0.5681 -0.0101 -0.1050 0.0222 244 LYS A NZ 1697 N N . VAL A 220 ? 0.1686 0.2134 0.2418 -0.0187 -0.0154 -0.0042 245 VAL A N 1698 C CA . VAL A 220 ? 0.1621 0.2004 0.2361 -0.0191 -0.0137 -0.0080 245 VAL A CA 1699 C C . VAL A 220 ? 0.1872 0.2265 0.2616 -0.0179 -0.0145 -0.0016 245 VAL A C 1700 O O . VAL A 220 ? 0.1906 0.2328 0.2660 -0.0159 -0.0165 0.0058 245 VAL A O 1701 C CB . VAL A 220 ? 0.1745 0.1994 0.2520 -0.0155 -0.0132 -0.0113 245 VAL A CB 1702 C CG1 . VAL A 220 ? 0.1904 0.2144 0.2687 -0.0171 -0.0125 -0.0168 245 VAL A CG1 1703 C CG2 . VAL A 220 ? 0.1905 0.2090 0.2698 -0.0105 -0.0150 -0.0061 245 VAL A CG2 1704 N N . THR A 221 ? 0.1912 0.2283 0.2657 -0.0193 -0.0131 -0.0040 246 THR A N 1705 C CA . THR A 221 ? 0.1851 0.2230 0.2602 -0.0190 -0.0139 0.0022 246 THR A CA 1706 C C . THR A 221 ? 0.2061 0.2309 0.2841 -0.0157 -0.0136 0.0011 246 THR A C 1707 O O . THR A 221 ? 0.2124 0.2323 0.2910 -0.0161 -0.0118 -0.0051 246 THR A O 1708 C CB . THR A 221 ? 0.1998 0.2500 0.2719 -0.0244 -0.0127 0.0014 246 THR A CB 1709 O OG1 . THR A 221 ? 0.2197 0.2839 0.2885 -0.0285 -0.0129 0.0015 246 THR A OG1 1710 C CG2 . THR A 221 ? 0.2512 0.3034 0.3244 -0.0245 -0.0141 0.0095 246 THR A CG2 1711 N N . VAL A 222 ? 0.1807 0.1999 0.2611 -0.0128 -0.0152 0.0073 247 VAL A N 1712 C CA . VAL A 222 ? 0.1776 0.1855 0.2604 -0.0106 -0.0150 0.0065 247 VAL A CA 1713 C C . VAL A 222 ? 0.2201 0.2280 0.3046 -0.0111 -0.0160 0.0132 247 VAL A C 1714 O O . VAL A 222 ? 0.2209 0.2359 0.3061 -0.0118 -0.0174 0.0200 247 VAL A O 1715 C CB . VAL A 222 ? 0.2218 0.2196 0.3070 -0.0062 -0.0156 0.0055 247 VAL A CB 1716 C CG1 . VAL A 222 ? 0.2447 0.2417 0.3289 -0.0061 -0.0147 -0.0005 247 VAL A CG1 1717 C CG2 . VAL A 222 ? 0.2850 0.2838 0.3724 -0.0034 -0.0172 0.0113 247 VAL A CG2 1718 N N . PHE A 223 ? 0.2138 0.2146 0.2995 -0.0111 -0.0155 0.0119 248 PHE A N 1719 C CA . PHE A 223 ? 0.2158 0.2129 0.3043 -0.0111 -0.0167 0.0181 248 PHE A CA 1720 C C . PHE A 223 ? 0.2148 0.1993 0.3055 -0.0090 -0.0165 0.0154 248 PHE A C 1721 O O . PHE A 223 ? 0.2091 0.1903 0.2987 -0.0088 -0.0154 0.0094 248 PHE A O 1722 C CB . PHE A 223 ? 0.2128 0.2192 0.2999 -0.0156 -0.0166 0.0213 248 PHE A CB 1723 C CG . PHE A 223 ? 0.2008 0.2097 0.2855 -0.0180 -0.0144 0.0148 248 PHE A CG 1724 C CD1 . PHE A 223 ? 0.2177 0.2185 0.3039 -0.0176 -0.0139 0.0127 248 PHE A CD1 1725 C CD2 . PHE A 223 ? 0.2244 0.2446 0.3059 -0.0210 -0.0127 0.0107 248 PHE A CD2 1726 C CE1 . PHE A 223 ? 0.2093 0.2133 0.2948 -0.0194 -0.0118 0.0074 248 PHE A CE1 1727 C CE2 . PHE A 223 ? 0.2225 0.2450 0.3036 -0.0228 -0.0102 0.0043 248 PHE A CE2 1728 C CZ . PHE A 223 ? 0.2213 0.2358 0.3047 -0.0217 -0.0098 0.0031 248 PHE A CZ 1729 N N A ARG A 224 ? 0.2201 0.1978 0.3147 -0.0076 -0.0177 0.0200 249 ARG A N 1730 N N B ARG A 224 ? 0.2135 0.1915 0.3081 -0.0078 -0.0177 0.0203 249 ARG A N 1731 C CA A ARG A 224 ? 0.2463 0.2130 0.3431 -0.0067 -0.0175 0.0175 249 ARG A CA 1732 C CA B ARG A 224 ? 0.2606 0.2271 0.3576 -0.0065 -0.0176 0.0178 249 ARG A CA 1733 C C A ARG A 224 ? 0.2533 0.2170 0.3537 -0.0084 -0.0185 0.0237 249 ARG A C 1734 C C B ARG A 224 ? 0.2540 0.2179 0.3545 -0.0084 -0.0186 0.0240 249 ARG A C 1735 O O A ARG A 224 ? 0.2768 0.2360 0.3822 -0.0064 -0.0195 0.0284 249 ARG A O 1736 O O B ARG A 224 ? 0.2483 0.2083 0.3539 -0.0066 -0.0196 0.0292 249 ARG A O 1737 C CB A ARG A 224 ? 0.2465 0.2056 0.3454 -0.0028 -0.0174 0.0145 249 ARG A CB 1738 C CB B ARG A 224 ? 0.2762 0.2362 0.3759 -0.0023 -0.0177 0.0162 249 ARG A CB 1739 C CG A ARG A 224 ? 0.2615 0.2102 0.3628 -0.0025 -0.0171 0.0115 249 ARG A CG 1740 C CG B ARG A 224 ? 0.2857 0.2359 0.3865 -0.0014 -0.0170 0.0109 249 ARG A CG 1741 C CD A ARG A 224 ? 0.3414 0.2849 0.4444 0.0010 -0.0165 0.0074 249 ARG A CD 1742 C CD B ARG A 224 ? 0.2505 0.1964 0.3543 0.0027 -0.0167 0.0091 249 ARG A CD 1743 N NE A ARG A 224 ? 0.4610 0.3954 0.5666 0.0007 -0.0159 0.0041 249 ARG A NE 1744 N NE B ARG A 224 ? 0.3292 0.2714 0.4395 0.0048 -0.0172 0.0146 249 ARG A NE 1745 C CZ A ARG A 224 ? 0.5203 0.4531 0.6234 -0.0005 -0.0153 -0.0020 249 ARG A CZ 1746 C CZ B ARG A 224 ? 0.2506 0.1909 0.3654 0.0089 -0.0169 0.0149 249 ARG A CZ 1747 N NH1 A ARG A 224 ? 0.5566 0.4955 0.6556 -0.0010 -0.0152 -0.0045 249 ARG A NH1 1748 N NH1 B ARG A 224 ? 0.1722 0.1147 0.2846 0.0109 -0.0161 0.0098 249 ARG A NH1 1749 N NH2 A ARG A 224 ? 0.4501 0.3757 0.5553 -0.0016 -0.0147 -0.0053 249 ARG A NH2 1750 N NH2 B ARG A 224 ? 0.2828 0.2194 0.4052 0.0110 -0.0173 0.0208 249 ARG A NH2 1751 N N . VAL A 225 ? 0.2294 0.1959 0.3281 -0.0120 -0.0183 0.0239 250 VAL A N 1752 C CA . VAL A 225 ? 0.2313 0.1979 0.3329 -0.0148 -0.0194 0.0308 250 VAL A CA 1753 C C . VAL A 225 ? 0.2124 0.1721 0.3146 -0.0169 -0.0192 0.0284 250 VAL A C 1754 O O . VAL A 225 ? 0.2461 0.2093 0.3448 -0.0186 -0.0180 0.0239 250 VAL A O 1755 C CB . VAL A 225 ? 0.2911 0.2721 0.3898 -0.0186 -0.0195 0.0347 250 VAL A CB 1756 C CG1 . VAL A 225 ? 0.2719 0.2544 0.3736 -0.0222 -0.0209 0.0425 250 VAL A CG1 1757 C CG2 . VAL A 225 ? 0.3076 0.2976 0.4055 -0.0176 -0.0201 0.0378 250 VAL A CG2 1758 N N . THR A 226 ? 0.2453 0.1954 0.3525 -0.0170 -0.0201 0.0314 251 THR A N 1759 C CA . THR A 226 ? 0.2543 0.1981 0.3622 -0.0198 -0.0200 0.0293 251 THR A CA 1760 C C . THR A 226 ? 0.2566 0.2051 0.3659 -0.0242 -0.0211 0.0366 251 THR A C 1761 O O . THR A 226 ? 0.3188 0.2667 0.4330 -0.0247 -0.0226 0.0444 251 THR A O 1762 C CB . THR A 226 ? 0.2584 0.1885 0.3711 -0.0181 -0.0200 0.0268 251 THR A CB 1763 O OG1 . THR A 226 ? 0.3010 0.2289 0.4119 -0.0144 -0.0188 0.0200 251 THR A OG1 1764 C CG2 . THR A 226 ? 0.3113 0.2358 0.4242 -0.0220 -0.0199 0.0242 251 THR A CG2 1765 N N . LYS A 227 ? 0.2706 0.2250 0.3763 -0.0275 -0.0205 0.0345 252 LYS A N 1766 C CA . LYS A 227 ? 0.2391 0.1989 0.3457 -0.0323 -0.0214 0.0406 252 LYS A CA 1767 C C . LYS A 227 ? 0.3002 0.2494 0.4100 -0.0348 -0.0221 0.0403 252 LYS A C 1768 O O . LYS A 227 ? 0.2939 0.2385 0.4020 -0.0347 -0.0211 0.0335 252 LYS A O 1769 C CB . LYS A 227 ? 0.3166 0.2893 0.4184 -0.0346 -0.0200 0.0380 252 LYS A CB 1770 C CG . LYS A 227 ? 0.3054 0.2880 0.4037 -0.0325 -0.0186 0.0351 252 LYS A CG 1771 C CD . LYS A 227 ? 0.3728 0.3642 0.4715 -0.0337 -0.0197 0.0425 252 LYS A CD 1772 C CE . LYS A 227 ? 0.3711 0.3729 0.4700 -0.0391 -0.0204 0.0491 252 LYS A CE 1773 N NZ . LYS A 227 ? 0.4037 0.4170 0.5028 -0.0410 -0.0217 0.0570 252 LYS A NZ 1774 N N . ASN A 228 ? 0.2909 0.2370 0.4059 -0.0375 -0.0238 0.0480 253 ASN A N 1775 C CA . ASN A 228 ? 0.3014 0.2379 0.4199 -0.0410 -0.0245 0.0482 253 ASN A CA 1776 C C . ASN A 228 ? 0.2700 0.2162 0.3875 -0.0467 -0.0253 0.0537 253 ASN A C 1777 O O . ASN A 228 ? 0.3261 0.2777 0.4465 -0.0491 -0.0268 0.0629 253 ASN A O 1778 C CB . ASN A 228 ? 0.3620 0.2856 0.4890 -0.0399 -0.0256 0.0524 253 ASN A CB 1779 C CG . ASN A 228 ? 0.4836 0.3980 0.6121 -0.0343 -0.0243 0.0459 253 ASN A CG 1780 O OD1 . ASN A 228 ? 0.4930 0.4020 0.6189 -0.0336 -0.0230 0.0369 253 ASN A OD1 1781 N ND2 . ASN A 228 ? 0.5283 0.4429 0.6610 -0.0304 -0.0249 0.0508 253 ASN A ND2 1782 N N . VAL A 229 ? 0.2727 0.2224 0.3861 -0.0489 -0.0243 0.0485 254 VAL A N 1783 C CA . VAL A 229 ? 0.2809 0.2429 0.3925 -0.0537 -0.0244 0.0523 254 VAL A CA 1784 C C . VAL A 229 ? 0.2822 0.2407 0.3939 -0.0578 -0.0246 0.0497 254 VAL A C 1785 O O . VAL A 229 ? 0.3370 0.2842 0.4497 -0.0572 -0.0245 0.0444 254 VAL A O 1786 C CB . VAL A 229 ? 0.2687 0.2451 0.3750 -0.0518 -0.0224 0.0487 254 VAL A CB 1787 C CG1 . VAL A 229 ? 0.2961 0.2789 0.4018 -0.0494 -0.0224 0.0518 254 VAL A CG1 1788 C CG2 . VAL A 229 ? 0.3181 0.2909 0.4219 -0.0483 -0.0207 0.0393 254 VAL A CG2 1789 N N . ALA A 230 ? 0.2677 0.2375 0.3784 -0.0623 -0.0247 0.0535 255 ALA A N 1790 C CA . ALA A 230 ? 0.2868 0.2566 0.3974 -0.0666 -0.0249 0.0518 255 ALA A CA 1791 C C . ALA A 230 ? 0.2996 0.2793 0.4065 -0.0647 -0.0227 0.0456 255 ALA A C 1792 O O . ALA A 230 ? 0.2621 0.2492 0.3669 -0.0607 -0.0211 0.0432 255 ALA A O 1793 C CB . ALA A 230 ? 0.3435 0.3201 0.4563 -0.0730 -0.0265 0.0603 255 ALA A CB 1794 N N . ILE A 231 ? 0.2640 0.2445 0.3709 -0.0678 -0.0228 0.0433 256 ILE A N 1795 C CA . ILE A 231 ? 0.2522 0.2405 0.3575 -0.0655 -0.0209 0.0378 256 ILE A CA 1796 C C . ILE A 231 ? 0.2870 0.2913 0.3919 -0.0643 -0.0189 0.0387 256 ILE A C 1797 O O . ILE A 231 ? 0.2569 0.2660 0.3617 -0.0600 -0.0168 0.0338 256 ILE A O 1798 C CB . ILE A 231 ? 0.2517 0.2390 0.3577 -0.0695 -0.0217 0.0360 256 ILE A CB 1799 C CG1 . ILE A 231 ? 0.2459 0.2402 0.3517 -0.0663 -0.0201 0.0311 256 ILE A CG1 1800 C CG2 . ILE A 231 ? 0.2674 0.2623 0.3746 -0.0758 -0.0226 0.0416 256 ILE A CG2 1801 C CD1 . ILE A 231 ? 0.2503 0.2432 0.3563 -0.0698 -0.0211 0.0290 256 ILE A CD1 1802 N N . ASP A 232 ? 0.2783 0.2913 0.3836 -0.0684 -0.0193 0.0446 257 ASP A N 1803 C CA A ASP A 232 ? 0.2711 0.3006 0.3761 -0.0677 -0.0169 0.0443 257 ASP A CA 1804 C CA B ASP A 232 ? 0.2724 0.3021 0.3774 -0.0678 -0.0169 0.0445 257 ASP A CA 1805 C C . ASP A 232 ? 0.2444 0.2757 0.3477 -0.0628 -0.0151 0.0411 257 ASP A C 1806 O O . ASP A 232 ? 0.2451 0.2837 0.3488 -0.0593 -0.0123 0.0356 257 ASP A O 1807 C CB A ASP A 232 ? 0.2896 0.3295 0.3950 -0.0738 -0.0178 0.0517 257 ASP A CB 1808 C CB B ASP A 232 ? 0.2734 0.3135 0.3786 -0.0737 -0.0178 0.0521 257 ASP A CB 1809 C CG A ASP A 232 ? 0.3050 0.3431 0.4122 -0.0791 -0.0196 0.0547 257 ASP A CG 1810 C CG B ASP A 232 ? 0.3309 0.3900 0.4355 -0.0734 -0.0148 0.0510 257 ASP A CG 1811 O OD1 A ASP A 232 ? 0.2781 0.3094 0.3859 -0.0780 -0.0196 0.0503 257 ASP A OD1 1812 O OD1 B ASP A 232 ? 0.2677 0.3363 0.3740 -0.0733 -0.0127 0.0479 257 ASP A OD1 1813 O OD2 A ASP A 232 ? 0.2888 0.3328 0.3968 -0.0849 -0.0210 0.0616 257 ASP A OD2 1814 O OD2 B ASP A 232 ? 0.2969 0.3624 0.3996 -0.0735 -0.0145 0.0531 257 ASP A OD2 1815 N N . GLU A 233 ? 0.2544 0.2792 0.3567 -0.0626 -0.0168 0.0446 258 GLU A N 1816 C CA . GLU A 233 ? 0.2386 0.2655 0.3390 -0.0586 -0.0156 0.0421 258 GLU A CA 1817 C C . GLU A 233 ? 0.2129 0.2305 0.3131 -0.0530 -0.0145 0.0347 258 GLU A C 1818 O O . GLU A 233 ? 0.2091 0.2321 0.3084 -0.0497 -0.0122 0.0298 258 GLU A O 1819 C CB . GLU A 233 ? 0.2402 0.2631 0.3406 -0.0598 -0.0179 0.0490 258 GLU A CB 1820 C CG . GLU A 233 ? 0.2485 0.2756 0.3467 -0.0564 -0.0168 0.0469 258 GLU A CG 1821 C CD . GLU A 233 ? 0.3007 0.3283 0.3997 -0.0580 -0.0192 0.0554 258 GLU A CD 1822 O OE1 . GLU A 233 ? 0.3200 0.3418 0.4224 -0.0612 -0.0218 0.0629 258 GLU A OE1 1823 O OE2 . GLU A 233 ? 0.3150 0.3492 0.4120 -0.0564 -0.0186 0.0550 258 GLU A OE2 1824 N N . ALA A 234 ? 0.2101 0.2144 0.3112 -0.0524 -0.0161 0.0337 259 ALA A N 1825 C CA . ALA A 234 ? 0.2357 0.2328 0.3366 -0.0477 -0.0154 0.0274 259 ALA A CA 1826 C C . ALA A 234 ? 0.2239 0.2292 0.3262 -0.0459 -0.0131 0.0227 259 ALA A C 1827 O O . ALA A 234 ? 0.1972 0.2024 0.2998 -0.0417 -0.0116 0.0181 259 ALA A O 1828 C CB . ALA A 234 ? 0.2372 0.2214 0.3387 -0.0486 -0.0172 0.0267 259 ALA A CB 1829 N N . THR A 235 ? 0.1923 0.2048 0.2964 -0.0492 -0.0128 0.0244 260 THR A N 1830 C CA . THR A 235 ? 0.1874 0.2082 0.2949 -0.0473 -0.0105 0.0209 260 THR A CA 1831 C C . THR A 235 ? 0.1924 0.2232 0.3007 -0.0447 -0.0073 0.0177 260 THR A C 1832 O O . THR A 235 ? 0.1995 0.2313 0.3109 -0.0406 -0.0052 0.0128 260 THR A O 1833 C CB . THR A 235 ? 0.1988 0.2267 0.3085 -0.0515 -0.0108 0.0240 260 THR A CB 1834 O OG1 . THR A 235 ? 0.2151 0.2339 0.3241 -0.0542 -0.0135 0.0253 260 THR A OG1 1835 C CG2 . THR A 235 ? 0.1977 0.2355 0.3126 -0.0490 -0.0082 0.0211 260 THR A CG2 1836 N N . SER A 236 ? 0.1735 0.2121 0.2797 -0.0475 -0.0069 0.0204 261 SER A N 1837 C CA . SER A 236 ? 0.1994 0.2491 0.3058 -0.0460 -0.0036 0.0164 261 SER A CA 1838 C C . SER A 236 ? 0.1790 0.2227 0.2834 -0.0424 -0.0032 0.0126 261 SER A C 1839 O O . SER A 236 ? 0.1874 0.2365 0.2936 -0.0398 -0.0001 0.0066 261 SER A O 1840 C CB . SER A 236 ? 0.2249 0.2873 0.3290 -0.0509 -0.0034 0.0207 261 SER A CB 1841 O OG . SER A 236 ? 0.2844 0.3413 0.3847 -0.0534 -0.0066 0.0270 261 SER A OG 1842 N N . LEU A 237 ? 0.1910 0.2238 0.2924 -0.0422 -0.0062 0.0158 262 LEU A N 1843 C CA . LEU A 237 ? 0.2184 0.2454 0.3181 -0.0387 -0.0061 0.0128 262 LEU A CA 1844 C C . LEU A 237 ? 0.2000 0.2213 0.3030 -0.0344 -0.0049 0.0071 262 LEU A C 1845 O O . LEU A 237 ? 0.1958 0.2193 0.2997 -0.0318 -0.0028 0.0021 262 LEU A O 1846 C CB . LEU A 237 ? 0.2160 0.2325 0.3134 -0.0390 -0.0094 0.0175 262 LEU A CB 1847 C CG . LEU A 237 ? 0.2463 0.2686 0.3415 -0.0423 -0.0107 0.0239 262 LEU A CG 1848 C CD1 . LEU A 237 ? 0.2628 0.2729 0.3582 -0.0419 -0.0137 0.0290 262 LEU A CD1 1849 C CD2 . LEU A 237 ? 0.2411 0.2741 0.3339 -0.0419 -0.0088 0.0214 262 LEU A CD2 1850 N N . LEU A 238 ? 0.1889 0.2035 0.2938 -0.0342 -0.0064 0.0081 263 LEU A N 1851 C CA . LEU A 238 ? 0.1922 0.2027 0.3006 -0.0306 -0.0058 0.0043 263 LEU A CA 1852 C C . LEU A 238 ? 0.1839 0.2034 0.2983 -0.0289 -0.0025 0.0007 263 LEU A C 1853 O O . LEU A 238 ? 0.1825 0.2007 0.3005 -0.0255 -0.0010 -0.0033 263 LEU A O 1854 C CB . LEU A 238 ? 0.1893 0.1934 0.2984 -0.0318 -0.0081 0.0065 263 LEU A CB 1855 C CG . LEU A 238 ? 0.1915 0.1849 0.2965 -0.0325 -0.0108 0.0081 263 LEU A CG 1856 C CD1 . LEU A 238 ? 0.2430 0.2319 0.3487 -0.0341 -0.0125 0.0084 263 LEU A CD1 1857 C CD2 . LEU A 238 ? 0.2355 0.2239 0.3388 -0.0289 -0.0107 0.0054 263 LEU A CD2 1858 N N . HIS A 239 ? 0.1796 0.2083 0.2958 -0.0314 -0.0012 0.0021 264 HIS A N 1859 C CA . HIS A 239 ? 0.1947 0.2325 0.3180 -0.0295 0.0024 -0.0017 264 HIS A CA 1860 C C . HIS A 239 ? 0.2087 0.2509 0.3326 -0.0277 0.0057 -0.0079 264 HIS A C 1861 O O . HIS A 239 ? 0.2011 0.2446 0.3320 -0.0243 0.0086 -0.0128 264 HIS A O 1862 C CB . HIS A 239 ? 0.1867 0.2350 0.3117 -0.0327 0.0033 0.0009 264 HIS A CB 1863 C CG . HIS A 239 ? 0.1809 0.2389 0.3147 -0.0302 0.0074 -0.0032 264 HIS A CG 1864 N ND1 . HIS A 239 ? 0.2401 0.3092 0.3752 -0.0306 0.0113 -0.0078 264 HIS A ND1 1865 C CD2 . HIS A 239 ? 0.1884 0.2470 0.3312 -0.0271 0.0083 -0.0035 264 HIS A CD2 1866 C CE1 . HIS A 239 ? 0.2630 0.3382 0.4079 -0.0275 0.0148 -0.0115 264 HIS A CE1 1867 N NE2 . HIS A 239 ? 0.2565 0.3254 0.4068 -0.0252 0.0130 -0.0084 264 HIS A NE2 1868 N N . LYS A 240 ? 0.1860 0.2308 0.3031 -0.0302 0.0053 -0.0074 265 LYS A N 1869 C CA . LYS A 240 ? 0.1814 0.2313 0.2979 -0.0295 0.0082 -0.0135 265 LYS A CA 1870 C C . LYS A 240 ? 0.1831 0.2225 0.2990 -0.0263 0.0072 -0.0157 265 LYS A C 1871 O O . LYS A 240 ? 0.1812 0.2216 0.3007 -0.0242 0.0100 -0.0221 265 LYS A O 1872 C CB . LYS A 240 ? 0.2021 0.2613 0.3117 -0.0340 0.0080 -0.0113 265 LYS A CB 1873 C CG . LYS A 240 ? 0.1866 0.2521 0.2944 -0.0342 0.0107 -0.0177 265 LYS A CG 1874 C CD . LYS A 240 ? 0.2402 0.3205 0.3425 -0.0394 0.0113 -0.0161 265 LYS A CD 1875 C CE . LYS A 240 ? 0.2421 0.3297 0.3424 -0.0403 0.0140 -0.0232 265 LYS A CE 1876 N NZ . LYS A 240 ? 0.2411 0.3465 0.3360 -0.0462 0.0149 -0.0219 265 LYS A NZ 1877 N N . TRP A 241 ? 0.1772 0.2066 0.2891 -0.0262 0.0033 -0.0107 266 TRP A N 1878 C CA . TRP A 241 ? 0.2002 0.2205 0.3113 -0.0234 0.0021 -0.0122 266 TRP A CA 1879 C C . TRP A 241 ? 0.1912 0.2090 0.3098 -0.0198 0.0041 -0.0167 266 TRP A C 1880 O O . TRP A 241 ? 0.1823 0.1977 0.3017 -0.0181 0.0050 -0.0206 266 TRP A O 1881 C CB . TRP A 241 ? 0.1858 0.1959 0.2935 -0.0234 -0.0018 -0.0070 266 TRP A CB 1882 C CG . TRP A 241 ? 0.1933 0.1956 0.3018 -0.0202 -0.0027 -0.0089 266 TRP A CG 1883 C CD1 . TRP A 241 ? 0.1952 0.1948 0.3003 -0.0192 -0.0032 -0.0101 266 TRP A CD1 1884 C CD2 . TRP A 241 ? 0.1733 0.1712 0.2866 -0.0180 -0.0031 -0.0095 266 TRP A CD2 1885 N NE1 . TRP A 241 ? 0.2080 0.2015 0.3154 -0.0166 -0.0039 -0.0116 266 TRP A NE1 1886 C CE2 . TRP A 241 ? 0.1800 0.1726 0.2925 -0.0159 -0.0039 -0.0111 266 TRP A CE2 1887 C CE3 . TRP A 241 ? 0.1872 0.1865 0.3059 -0.0179 -0.0030 -0.0081 266 TRP A CE3 1888 C CZ2 . TRP A 241 ? 0.1878 0.1766 0.3044 -0.0139 -0.0047 -0.0111 266 TRP A CZ2 1889 C CZ3 . TRP A 241 ? 0.2054 0.2014 0.3286 -0.0159 -0.0039 -0.0078 266 TRP A CZ3 1890 C CH2 . TRP A 241 ? 0.1948 0.1856 0.3168 -0.0140 -0.0047 -0.0092 266 TRP A CH2 1891 N N . GLN A 242 ? 0.1757 0.1943 0.3007 -0.0189 0.0045 -0.0156 267 GLN A N 1892 C CA . GLN A 242 ? 0.2084 0.2242 0.3421 -0.0154 0.0057 -0.0179 267 GLN A CA 1893 C C . GLN A 242 ? 0.1893 0.2093 0.3286 -0.0138 0.0100 -0.0252 267 GLN A C 1894 O O . GLN A 242 ? 0.2151 0.2304 0.3598 -0.0112 0.0107 -0.0279 267 GLN A O 1895 C CB . GLN A 242 ? 0.1990 0.2174 0.3397 -0.0149 0.0055 -0.0145 267 GLN A CB 1896 C CG . GLN A 242 ? 0.1875 0.2161 0.3330 -0.0154 0.0089 -0.0165 267 GLN A CG 1897 C CD . GLN A 242 ? 0.1688 0.2009 0.3212 -0.0151 0.0083 -0.0121 267 GLN A CD 1898 O OE1 . GLN A 242 ? 0.2098 0.2390 0.3696 -0.0125 0.0076 -0.0102 267 GLN A OE1 1899 N NE2 . GLN A 242 ? 0.1728 0.2122 0.3230 -0.0181 0.0084 -0.0098 267 GLN A NE2 1900 N N . PHE A 243 ? 0.1747 0.2041 0.3128 -0.0159 0.0129 -0.0286 268 PHE A N 1901 C CA . PHE A 243 ? 0.2020 0.2365 0.3453 -0.0151 0.0176 -0.0371 268 PHE A CA 1902 C C . PHE A 243 ? 0.2566 0.2895 0.3932 -0.0165 0.0174 -0.0405 268 PHE A C 1903 O O . PHE A 243 ? 0.2478 0.2776 0.3893 -0.0149 0.0195 -0.0462 268 PHE A O 1904 C CB . PHE A 243 ? 0.1962 0.2436 0.3409 -0.0172 0.0212 -0.0403 268 PHE A CB 1905 C CG . PHE A 243 ? 0.2032 0.2535 0.3554 -0.0157 0.0217 -0.0369 268 PHE A CG 1906 C CD1 . PHE A 243 ? 0.2334 0.2821 0.3989 -0.0115 0.0242 -0.0394 268 PHE A CD1 1907 C CD2 . PHE A 243 ? 0.1956 0.2505 0.3425 -0.0187 0.0194 -0.0306 268 PHE A CD2 1908 C CE1 . PHE A 243 ? 0.2449 0.2977 0.4181 -0.0102 0.0245 -0.0354 268 PHE A CE1 1909 C CE2 . PHE A 243 ? 0.2177 0.2764 0.3714 -0.0178 0.0196 -0.0272 268 PHE A CE2 1910 C CZ . PHE A 243 ? 0.2214 0.2796 0.3882 -0.0135 0.0221 -0.0295 268 PHE A CZ 1911 N N . VAL A 244 ? 0.2009 0.2358 0.3270 -0.0197 0.0147 -0.0365 269 VAL A N 1912 C CA . VAL A 244 ? 0.1960 0.2306 0.3155 -0.0212 0.0139 -0.0381 269 VAL A CA 1913 C C . VAL A 244 ? 0.2062 0.2293 0.3277 -0.0181 0.0120 -0.0378 269 VAL A C 1914 O O . VAL A 244 ? 0.2347 0.2575 0.3574 -0.0180 0.0137 -0.0433 269 VAL A O 1915 C CB . VAL A 244 ? 0.2041 0.2414 0.3138 -0.0243 0.0105 -0.0313 269 VAL A CB 1916 C CG1 . VAL A 244 ? 0.2235 0.2608 0.3274 -0.0255 0.0093 -0.0317 269 VAL A CG1 1917 C CG2 . VAL A 244 ? 0.2521 0.3025 0.3597 -0.0282 0.0122 -0.0308 269 VAL A CG2 1918 N N . ALA A 245 ? 0.1909 0.2059 0.3130 -0.0162 0.0088 -0.0318 270 ALA A N 1919 C CA . ALA A 245 ? 0.1990 0.2047 0.3224 -0.0137 0.0066 -0.0305 270 ALA A CA 1920 C C . ALA A 245 ? 0.2557 0.2588 0.3888 -0.0113 0.0090 -0.0353 270 ALA A C 1921 O O . ALA A 245 ? 0.2803 0.2797 0.4133 -0.0109 0.0087 -0.0374 270 ALA A O 1922 C CB . ALA A 245 ? 0.2176 0.2175 0.3403 -0.0128 0.0032 -0.0240 270 ALA A CB 1923 N N . GLU A 246 ? 0.2193 0.2242 0.3618 -0.0098 0.0112 -0.0364 271 GLU A N 1924 C CA A GLU A 246 ? 0.2517 0.2533 0.4059 -0.0071 0.0135 -0.0398 271 GLU A CA 1925 C CA B GLU A 246 ? 0.2513 0.2530 0.4057 -0.0071 0.0135 -0.0398 271 GLU A CA 1926 C C . GLU A 246 ? 0.2289 0.2339 0.3855 -0.0081 0.0178 -0.0491 271 GLU A C 1927 O O . GLU A 246 ? 0.2554 0.2556 0.4190 -0.0068 0.0191 -0.0528 271 GLU A O 1928 C CB A GLU A 246 ? 0.2719 0.2754 0.4372 -0.0048 0.0148 -0.0377 271 GLU A CB 1929 C CB B GLU A 246 ? 0.2711 0.2749 0.4363 -0.0048 0.0148 -0.0377 271 GLU A CB 1930 C CG A GLU A 246 ? 0.2531 0.2527 0.4332 -0.0015 0.0171 -0.0400 271 GLU A CG 1931 C CG B GLU A 246 ? 0.2765 0.2760 0.4564 -0.0015 0.0164 -0.0386 271 GLU A CG 1932 C CD A GLU A 246 ? 0.2146 0.2181 0.4076 0.0010 0.0192 -0.0385 271 GLU A CD 1933 C CD B GLU A 246 ? 0.2979 0.2993 0.4864 -0.0007 0.0219 -0.0482 271 GLU A CD 1934 O OE1 A GLU A 246 ? 0.2482 0.2575 0.4379 0.0001 0.0186 -0.0352 271 GLU A OE1 1935 O OE1 B GLU A 246 ? 0.2908 0.2996 0.4752 -0.0027 0.0250 -0.0540 271 GLU A OE1 1936 O OE2 A GLU A 246 ? 0.2633 0.2641 0.4707 0.0040 0.0216 -0.0403 271 GLU A OE2 1937 O OE2 B GLU A 246 ? 0.4348 0.4308 0.6348 0.0016 0.0232 -0.0501 271 GLU A OE2 1938 N N . GLU A 247 ? 0.2046 0.2185 0.3556 -0.0109 0.0200 -0.0530 272 GLU A N 1939 C CA . GLU A 247 ? 0.2049 0.2246 0.3578 -0.0128 0.0247 -0.0630 272 GLU A CA 1940 C C . GLU A 247 ? 0.2328 0.2542 0.3762 -0.0161 0.0239 -0.0658 272 GLU A C 1941 O O . GLU A 247 ? 0.2952 0.3202 0.4410 -0.0180 0.0276 -0.0748 272 GLU A O 1942 C CB . GLU A 247 ? 0.2521 0.2836 0.4049 -0.0146 0.0282 -0.0668 272 GLU A CB 1943 C CG . GLU A 247 ? 0.3067 0.3384 0.4705 -0.0113 0.0298 -0.0650 272 GLU A CG 1944 C CD . GLU A 247 ? 0.4346 0.4784 0.5954 -0.0136 0.0317 -0.0653 272 GLU A CD 1945 O OE1 . GLU A 247 ? 0.5525 0.6057 0.7039 -0.0179 0.0324 -0.0681 272 GLU A OE1 1946 O OE2 . GLU A 247 ? 0.4971 0.5424 0.6651 -0.0113 0.0323 -0.0623 272 GLU A OE2 1947 N N . LEU A 248 ? 0.2500 0.2695 0.3835 -0.0171 0.0193 -0.0585 273 LEU A N 1948 C CA . LEU A 248 ? 0.2671 0.2892 0.3921 -0.0200 0.0181 -0.0598 273 LEU A CA 1949 C C . LEU A 248 ? 0.2267 0.2433 0.3572 -0.0195 0.0196 -0.0656 273 LEU A C 1950 O O . LEU A 248 ? 0.2588 0.2662 0.3980 -0.0161 0.0191 -0.0644 273 LEU A O 1951 C CB . LEU A 248 ? 0.2372 0.2551 0.3540 -0.0196 0.0129 -0.0505 273 LEU A CB 1952 C CG . LEU A 248 ? 0.2307 0.2551 0.3394 -0.0218 0.0109 -0.0447 273 LEU A CG 1953 C CD1 . LEU A 248 ? 0.2280 0.2443 0.3331 -0.0198 0.0064 -0.0363 273 LEU A CD1 1954 C CD2 . LEU A 248 ? 0.2260 0.2618 0.3276 -0.0262 0.0117 -0.0468 273 LEU A CD2 1955 N N . GLU A 249 ? 0.2180 0.2411 0.3440 -0.0234 0.0211 -0.0716 274 GLU A N 1956 C CA . GLU A 249 ? 0.2099 0.2277 0.3399 -0.0237 0.0219 -0.0765 274 GLU A CA 1957 C C . GLU A 249 ? 0.2035 0.2122 0.3315 -0.0213 0.0170 -0.0683 274 GLU A C 1958 O O . GLU A 249 ? 0.2151 0.2236 0.3362 -0.0203 0.0133 -0.0602 274 GLU A O 1959 C CB . GLU A 249 ? 0.2341 0.2622 0.3576 -0.0293 0.0239 -0.0837 274 GLU A CB 1960 C CG . GLU A 249 ? 0.3860 0.4242 0.5125 -0.0323 0.0296 -0.0942 274 GLU A CG 1961 C CD . GLU A 249 ? 0.7555 0.8073 0.8735 -0.0390 0.0311 -0.1004 274 GLU A CD 1962 O OE1 . GLU A 249 ? 0.8854 0.9409 0.9939 -0.0411 0.0272 -0.0941 274 GLU A OE1 1963 O OE2 . GLU A 249 ? 0.8573 0.9170 0.9786 -0.0424 0.0365 -0.1118 274 GLU A OE2 1964 N N . GLU A 250 ? 0.2075 0.2089 0.3422 -0.0204 0.0172 -0.0706 275 GLU A N 1965 C CA . GLU A 250 ? 0.2032 0.1967 0.3375 -0.0180 0.0129 -0.0631 275 GLU A CA 1966 C C . GLU A 250 ? 0.2120 0.2090 0.3348 -0.0196 0.0094 -0.0582 275 GLU A C 1967 O O . GLU A 250 ? 0.2300 0.2221 0.3510 -0.0173 0.0058 -0.0514 275 GLU A O 1968 C CB . GLU A 250 ? 0.2635 0.2498 0.4080 -0.0176 0.0139 -0.0662 275 GLU A CB 1969 C CG . GLU A 250 ? 0.2488 0.2384 0.3911 -0.0218 0.0156 -0.0736 275 GLU A CG 1970 C CD . GLU A 250 ? 0.3574 0.3388 0.5102 -0.0216 0.0161 -0.0758 275 GLU A CD 1971 O OE1 . GLU A 250 ? 0.4277 0.4021 0.5930 -0.0185 0.0172 -0.0748 275 GLU A OE1 1972 O OE2 . GLU A 250 ? 0.3836 0.3661 0.5328 -0.0248 0.0153 -0.0778 275 GLU A OE2 1973 N N . ASP A 251 ? 0.1894 0.1958 0.3048 -0.0234 0.0104 -0.0617 276 ASP A N 1974 C CA . ASP A 251 ? 0.1879 0.1990 0.2937 -0.0248 0.0071 -0.0564 276 ASP A CA 1975 C C . ASP A 251 ? 0.2104 0.2234 0.3105 -0.0232 0.0047 -0.0487 276 ASP A C 1976 O O . ASP A 251 ? 0.2071 0.2244 0.3003 -0.0240 0.0022 -0.0438 276 ASP A O 1977 C CB . ASP A 251 ? 0.2231 0.2455 0.3236 -0.0301 0.0089 -0.0621 276 ASP A CB 1978 C CG . ASP A 251 ? 0.3120 0.3323 0.4157 -0.0323 0.0098 -0.0677 276 ASP A CG 1979 O OD1 . ASP A 251 ? 0.2854 0.2959 0.3946 -0.0294 0.0083 -0.0655 276 ASP A OD1 1980 O OD2 . ASP A 251 ? 0.3417 0.3712 0.4424 -0.0374 0.0119 -0.0743 276 ASP A OD2 1981 N N . PHE A 252 ? 0.2037 0.2135 0.3073 -0.0211 0.0054 -0.0475 277 PHE A N 1982 C CA . PHE A 252 ? 0.1820 0.1924 0.2812 -0.0201 0.0032 -0.0406 277 PHE A CA 1983 C C . PHE A 252 ? 0.1963 0.1975 0.3001 -0.0164 0.0019 -0.0368 277 PHE A C 1984 O O . PHE A 252 ? 0.2144 0.2118 0.3257 -0.0151 0.0036 -0.0397 277 PHE A O 1985 C CB . PHE A 252 ? 0.1915 0.2112 0.2890 -0.0228 0.0054 -0.0424 277 PHE A CB 1986 C CG . PHE A 252 ? 0.2184 0.2504 0.3109 -0.0276 0.0070 -0.0462 277 PHE A CG 1987 C CD1 . PHE A 252 ? 0.3175 0.3581 0.4030 -0.0299 0.0049 -0.0403 277 PHE A CD1 1988 C CD2 . PHE A 252 ? 0.2571 0.2928 0.3528 -0.0300 0.0106 -0.0557 277 PHE A CD2 1989 C CE1 . PHE A 252 ? 0.2756 0.3301 0.3564 -0.0351 0.0061 -0.0432 277 PHE A CE1 1990 C CE2 . PHE A 252 ? 0.3188 0.3676 0.4094 -0.0353 0.0122 -0.0600 277 PHE A CE2 1991 C CZ . PHE A 252 ? 0.3332 0.3923 0.4159 -0.0380 0.0098 -0.0534 277 PHE A CZ 1992 N N . THR A 253 ? 0.1651 0.1635 0.2651 -0.0150 -0.0011 -0.0302 278 THR A N 1993 C CA . THR A 253 ? 0.1932 0.1852 0.2961 -0.0127 -0.0023 -0.0268 278 THR A CA 1994 C C . THR A 253 ? 0.2012 0.1944 0.2997 -0.0134 -0.0037 -0.0220 278 THR A C 1995 O O . THR A 253 ? 0.2092 0.2041 0.3029 -0.0139 -0.0053 -0.0187 278 THR A O 1996 C CB . THR A 253 ? 0.1857 0.1710 0.2895 -0.0104 -0.0047 -0.0242 278 THR A CB 1997 O OG1 . THR A 253 ? 0.2578 0.2417 0.3670 -0.0100 -0.0037 -0.0276 278 THR A OG1 1998 C CG2 . THR A 253 ? 0.2022 0.1830 0.3079 -0.0090 -0.0061 -0.0207 278 THR A CG2 1999 N N . LEU A 254 ? 0.1658 0.1586 0.2668 -0.0135 -0.0031 -0.0211 279 LEU A N 2000 C CA . LEU A 254 ? 0.1787 0.1711 0.2767 -0.0144 -0.0047 -0.0162 279 LEU A CA 2001 C C . LEU A 254 ? 0.1808 0.1672 0.2818 -0.0132 -0.0058 -0.0143 279 LEU A C 2002 O O . LEU A 254 ? 0.1757 0.1635 0.2815 -0.0131 -0.0044 -0.0159 279 LEU A O 2003 C CB . LEU A 254 ? 0.1837 0.1847 0.2809 -0.0172 -0.0029 -0.0167 279 LEU A CB 2004 C CG . LEU A 254 ? 0.1999 0.2008 0.2948 -0.0187 -0.0046 -0.0108 279 LEU A CG 2005 C CD1 . LEU A 254 ? 0.2128 0.2111 0.3039 -0.0186 -0.0072 -0.0058 279 LEU A CD1 2006 C CD2 . LEU A 254 ? 0.2257 0.2370 0.3200 -0.0220 -0.0027 -0.0112 279 LEU A CD2 2007 N N . SER A 255 ? 0.1533 0.1339 0.2519 -0.0124 -0.0081 -0.0111 280 SER A N 2008 C CA . SER A 255 ? 0.1885 0.1646 0.2890 -0.0121 -0.0093 -0.0097 280 SER A CA 2009 C C . SER A 255 ? 0.1852 0.1583 0.2831 -0.0136 -0.0107 -0.0063 280 SER A C 2010 O O . SER A 255 ? 0.2094 0.1830 0.3046 -0.0141 -0.0112 -0.0041 280 SER A O 2011 C CB . SER A 255 ? 0.2237 0.1959 0.3247 -0.0102 -0.0105 -0.0104 280 SER A CB 2012 O OG . SER A 255 ? 0.2390 0.2135 0.3440 -0.0093 -0.0093 -0.0129 280 SER A OG 2013 N N . VAL A 256 ? 0.1856 0.1561 0.2847 -0.0146 -0.0115 -0.0055 281 VAL A N 2014 C CA . VAL A 256 ? 0.1923 0.1594 0.2898 -0.0167 -0.0127 -0.0029 281 VAL A CA 2015 C C . VAL A 256 ? 0.2497 0.2114 0.3471 -0.0172 -0.0140 -0.0036 281 VAL A C 2016 O O . VAL A 256 ? 0.2477 0.2114 0.3469 -0.0173 -0.0141 -0.0049 281 VAL A O 2017 C CB . VAL A 256 ? 0.2200 0.1919 0.3190 -0.0194 -0.0120 -0.0012 281 VAL A CB 2018 C CG1 . VAL A 256 ? 0.2510 0.2194 0.3486 -0.0221 -0.0133 0.0022 281 VAL A CG1 2019 C CG2 . VAL A 256 ? 0.2391 0.2186 0.3387 -0.0193 -0.0101 -0.0020 281 VAL A CG2 2020 N N . LEU A 257 ? 0.2223 0.1780 0.3183 -0.0176 -0.0148 -0.0028 282 LEU A N 2021 C CA . LEU A 257 ? 0.2597 0.2106 0.3557 -0.0194 -0.0156 -0.0043 282 LEU A CA 2022 C C . LEU A 257 ? 0.2636 0.2120 0.3601 -0.0228 -0.0161 -0.0018 282 LEU A C 2023 O O . LEU A 257 ? 0.2836 0.2306 0.3806 -0.0228 -0.0162 0.0015 282 LEU A O 2024 C CB . LEU A 257 ? 0.2822 0.2270 0.3776 -0.0173 -0.0158 -0.0064 282 LEU A CB 2025 C CG . LEU A 257 ? 0.3256 0.2730 0.4203 -0.0145 -0.0156 -0.0089 282 LEU A CG 2026 C CD1 . LEU A 257 ? 0.4018 0.3444 0.4966 -0.0119 -0.0154 -0.0104 282 LEU A CD1 2027 C CD2 . LEU A 257 ? 0.4435 0.3944 0.5382 -0.0165 -0.0159 -0.0112 282 LEU A CD2 2028 N N . GLY A 258 ? 0.2480 0.1973 0.3449 -0.0262 -0.0165 -0.0026 283 GLY A N 2029 C CA . GLY A 258 ? 0.2459 0.1937 0.3434 -0.0301 -0.0170 0.0001 283 GLY A CA 2030 C C . GLY A 258 ? 0.2376 0.1813 0.3352 -0.0340 -0.0176 -0.0024 283 GLY A C 2031 O O . GLY A 258 ? 0.2547 0.2007 0.3513 -0.0348 -0.0177 -0.0057 283 GLY A O 2032 N N . GLY A 259 ? 0.2359 0.1741 0.3346 -0.0371 -0.0181 -0.0004 284 GLY A N 2033 C CA . GLY A 259 ? 0.2307 0.1644 0.3298 -0.0418 -0.0186 -0.0032 284 GLY A CA 2034 C C . GLY A 259 ? 0.2471 0.1768 0.3484 -0.0456 -0.0193 0.0009 284 GLY A C 2035 O O . GLY A 259 ? 0.2744 0.2060 0.3767 -0.0445 -0.0196 0.0064 284 GLY A O 2036 N N . ALA A 260 ? 0.2574 0.1823 0.3595 -0.0507 -0.0197 -0.0015 285 ALA A N 2037 C CA . ALA A 260 ? 0.2614 0.1820 0.3663 -0.0549 -0.0206 0.0028 285 ALA A CA 2038 C C . ALA A 260 ? 0.3004 0.2116 0.4073 -0.0598 -0.0206 -0.0019 285 ALA A C 2039 O O . ALA A 260 ? 0.3312 0.2411 0.4364 -0.0606 -0.0198 -0.0091 285 ALA A O 2040 C CB . ALA A 260 ? 0.2832 0.2149 0.3868 -0.0581 -0.0213 0.0075 285 ALA A CB 2041 N N . ASP A 261 ? 0.3015 0.2067 0.4121 -0.0637 -0.0215 0.0021 286 ASP A N 2042 C CA . ASP A 261 ? 0.3548 0.2503 0.4684 -0.0694 -0.0214 -0.0023 286 ASP A CA 2043 C C . ASP A 261 ? 0.3888 0.2836 0.5054 -0.0746 -0.0230 0.0049 286 ASP A C 2044 O O . ASP A 261 ? 0.3522 0.2414 0.4738 -0.0731 -0.0236 0.0115 286 ASP A O 2045 C CB . ASP A 261 ? 0.3812 0.2625 0.5003 -0.0661 -0.0200 -0.0064 286 ASP A CB 2046 C CG . ASP A 261 ? 0.4237 0.2941 0.5464 -0.0719 -0.0192 -0.0134 286 ASP A CG 2047 O OD1 . ASP A 261 ? 0.4561 0.3288 0.5778 -0.0791 -0.0202 -0.0132 286 ASP A OD1 2048 O OD2 . ASP A 261 ? 0.4986 0.3585 0.6257 -0.0693 -0.0173 -0.0197 286 ASP A OD2 2049 N N . GLU A 262 ? 0.3518 0.2537 0.4656 -0.0810 -0.0237 0.0044 287 GLU A N 2050 C CA . GLU A 262 ? 0.3228 0.2274 0.4386 -0.0865 -0.0254 0.0117 287 GLU A CA 2051 C C . GLU A 262 ? 0.3699 0.2826 0.4860 -0.0826 -0.0260 0.0208 287 GLU A C 2052 O O . GLU A 262 ? 0.3698 0.2938 0.4818 -0.0788 -0.0254 0.0211 287 GLU A O 2053 C CB . GLU A 262 ? 0.3981 0.2880 0.5205 -0.0915 -0.0258 0.0113 287 GLU A CB 2054 C CG . GLU A 262 ? 0.4278 0.3115 0.5495 -0.0965 -0.0248 0.0009 287 GLU A CG 2055 C CD . GLU A 262 ? 0.6613 0.5302 0.7903 -0.1025 -0.0250 -0.0002 287 GLU A CD 2056 O OE1 . GLU A 262 ? 0.7206 0.5874 0.8542 -0.1049 -0.0266 0.0088 287 GLU A OE1 2057 O OE2 . GLU A 262 ? 0.7422 0.6022 0.8728 -0.1050 -0.0233 -0.0103 287 GLU A OE2 2058 N N . LYS A 263 ? 0.3564 0.2637 0.4775 -0.0839 -0.0271 0.0281 288 LYS A N 2059 C CA . LYS A 263 ? 0.3280 0.2456 0.4487 -0.0817 -0.0278 0.0368 288 LYS A CA 2060 C C . LYS A 263 ? 0.3578 0.2760 0.4780 -0.0739 -0.0268 0.0372 288 LYS A C 2061 O O . LYS A 263 ? 0.3476 0.2769 0.4660 -0.0719 -0.0269 0.0424 288 LYS A O 2062 C CB . LYS A 263 ? 0.3560 0.2707 0.4825 -0.0865 -0.0297 0.0460 288 LYS A CB 2063 C CG . LYS A 263 ? 0.5226 0.4446 0.6482 -0.0944 -0.0308 0.0490 288 LYS A CG 2064 C CD . LYS A 263 ? 0.7461 0.6590 0.8723 -0.0997 -0.0308 0.0419 288 LYS A CD 2065 C CE . LYS A 263 ? 0.8397 0.7556 0.9679 -0.1086 -0.0326 0.0470 288 LYS A CE 2066 N NZ . LYS A 263 ? 0.8749 0.7839 1.0105 -0.1109 -0.0344 0.0565 288 LYS A NZ 2067 N N . GLN A 264 ? 0.3356 0.2429 0.4574 -0.0700 -0.0259 0.0315 289 GLN A N 2068 C CA . GLN A 264 ? 0.3625 0.2700 0.4843 -0.0629 -0.0252 0.0322 289 GLN A CA 2069 C C . GLN A 264 ? 0.3218 0.2369 0.4374 -0.0587 -0.0237 0.0258 289 GLN A C 2070 O O . GLN A 264 ? 0.3351 0.2467 0.4489 -0.0585 -0.0228 0.0181 289 GLN A O 2071 C CB . GLN A 264 ? 0.3992 0.2914 0.5276 -0.0603 -0.0248 0.0304 289 GLN A CB 2072 C CG . GLN A 264 ? 0.4791 0.3628 0.6161 -0.0637 -0.0264 0.0382 289 GLN A CG 2073 C CD . GLN A 264 ? 0.7502 0.6182 0.8958 -0.0603 -0.0256 0.0364 289 GLN A CD 2074 O OE1 . GLN A 264 ? 0.8226 0.6817 0.9688 -0.0597 -0.0239 0.0265 289 GLN A OE1 2075 N NE2 . GLN A 264 ? 0.8446 0.7103 0.9978 -0.0582 -0.0269 0.0460 289 GLN A NE2 2076 N N . VAL A 265 ? 0.3037 0.2298 0.4165 -0.0556 -0.0234 0.0290 290 VAL A N 2077 C CA . VAL A 265 ? 0.2877 0.2201 0.3961 -0.0512 -0.0220 0.0238 290 VAL A CA 2078 C C . VAL A 265 ? 0.2789 0.2093 0.3879 -0.0455 -0.0215 0.0244 290 VAL A C 2079 O O . VAL A 265 ? 0.3124 0.2446 0.4236 -0.0451 -0.0223 0.0309 290 VAL A O 2080 C CB . VAL A 265 ? 0.2783 0.2251 0.3838 -0.0519 -0.0214 0.0253 290 VAL A CB 2081 C CG1 . VAL A 265 ? 0.3056 0.2574 0.4083 -0.0471 -0.0199 0.0202 290 VAL A CG1 2082 C CG2 . VAL A 265 ? 0.3409 0.2914 0.4464 -0.0575 -0.0219 0.0257 290 VAL A CG2 2083 N N . TRP A 266 ? 0.2857 0.2138 0.3928 -0.0416 -0.0205 0.0182 291 TRP A N 2084 C CA . TRP A 266 ? 0.2725 0.2008 0.3797 -0.0363 -0.0200 0.0185 291 TRP A CA 2085 C C . TRP A 266 ? 0.2634 0.2005 0.3663 -0.0335 -0.0189 0.0149 291 TRP A C 2086 O O . TRP A 266 ? 0.2751 0.2132 0.3763 -0.0338 -0.0184 0.0100 291 TRP A O 2087 C CB . TRP A 266 ? 0.2865 0.2031 0.3968 -0.0336 -0.0197 0.0149 291 TRP A CB 2088 C CG . TRP A 266 ? 0.3291 0.2427 0.4375 -0.0339 -0.0188 0.0067 291 TRP A CG 2089 C CD1 . TRP A 266 ? 0.3434 0.2510 0.4527 -0.0380 -0.0187 0.0027 291 TRP A CD1 2090 C CD2 . TRP A 266 ? 0.2958 0.2132 0.4008 -0.0306 -0.0179 0.0015 291 TRP A CD2 2091 N NE1 . TRP A 266 ? 0.3162 0.2252 0.4226 -0.0377 -0.0178 -0.0045 291 TRP A NE1 2092 C CE2 . TRP A 266 ? 0.2910 0.2059 0.3950 -0.0330 -0.0174 -0.0049 291 TRP A CE2 2093 C CE3 . TRP A 266 ? 0.3058 0.2293 0.4087 -0.0264 -0.0175 0.0019 291 TRP A CE3 2094 C CZ2 . TRP A 266 ? 0.2871 0.2062 0.3881 -0.0313 -0.0168 -0.0100 291 TRP A CZ2 2095 C CZ3 . TRP A 266 ? 0.3303 0.2563 0.4307 -0.0245 -0.0168 -0.0034 291 TRP A CZ3 2096 C CH2 . TRP A 266 ? 0.3121 0.2363 0.4117 -0.0269 -0.0166 -0.0088 291 TRP A CH2 2097 N N . LEU A 267 ? 0.2361 0.1802 0.3380 -0.0313 -0.0186 0.0177 292 LEU A N 2098 C CA . LEU A 267 ? 0.2444 0.1957 0.3436 -0.0285 -0.0173 0.0141 292 LEU A CA 2099 C C . LEU A 267 ? 0.2667 0.2175 0.3657 -0.0246 -0.0172 0.0145 292 LEU A C 2100 O O . LEU A 267 ? 0.2627 0.2175 0.3621 -0.0248 -0.0177 0.0195 292 LEU A O 2101 C CB . LEU A 267 ? 0.2189 0.1816 0.3169 -0.0303 -0.0164 0.0158 292 LEU A CB 2102 C CG . LEU A 267 ? 0.2455 0.2117 0.3443 -0.0342 -0.0164 0.0165 292 LEU A CG 2103 C CD1 . LEU A 267 ? 0.2720 0.2506 0.3703 -0.0355 -0.0151 0.0179 292 LEU A CD1 2104 C CD2 . LEU A 267 ? 0.2559 0.2201 0.3548 -0.0338 -0.0161 0.0118 292 LEU A CD2 2105 N N . THR A 268 ? 0.2169 0.1640 0.3153 -0.0215 -0.0168 0.0099 293 THR A N 2106 C CA . THR A 268 ? 0.2209 0.1686 0.3190 -0.0179 -0.0167 0.0100 293 THR A CA 2107 C C . THR A 268 ? 0.2390 0.1953 0.3344 -0.0169 -0.0156 0.0077 293 THR A C 2108 O O . THR A 268 ? 0.2439 0.2011 0.3388 -0.0163 -0.0149 0.0035 293 THR A O 2109 C CB . THR A 268 ? 0.2635 0.2036 0.3626 -0.0151 -0.0166 0.0060 293 THR A CB 2110 O OG1 . THR A 268 ? 0.2794 0.2106 0.3819 -0.0160 -0.0171 0.0070 293 THR A OG1 2111 C CG2 . THR A 268 ? 0.2636 0.2054 0.3627 -0.0113 -0.0166 0.0067 293 THR A CG2 2112 N N . MET A 269 ? 0.2112 0.1746 0.3058 -0.0172 -0.0155 0.0108 294 MET A N 2113 C CA . MET A 269 ? 0.1849 0.1568 0.2775 -0.0169 -0.0141 0.0079 294 MET A CA 2114 C C . MET A 269 ? 0.2046 0.1760 0.2965 -0.0139 -0.0141 0.0063 294 MET A C 2115 O O . MET A 269 ? 0.2218 0.1931 0.3140 -0.0129 -0.0152 0.0100 294 MET A O 2116 C CB . MET A 269 ? 0.2260 0.2080 0.3175 -0.0198 -0.0136 0.0113 294 MET A CB 2117 C CG . MET A 269 ? 0.2778 0.2617 0.3702 -0.0232 -0.0139 0.0146 294 MET A CG 2118 S SD . MET A 269 ? 0.3210 0.3042 0.4146 -0.0239 -0.0125 0.0098 294 MET A SD 2119 C CE . MET A 269 ? 0.2255 0.2175 0.3188 -0.0228 -0.0098 0.0039 294 MET A CE 2120 N N . LEU A 270 ? 0.1713 0.1429 0.2629 -0.0126 -0.0132 0.0014 295 LEU A N 2121 C CA . LEU A 270 ? 0.1902 0.1619 0.2811 -0.0101 -0.0133 -0.0005 295 LEU A CA 2122 C C . LEU A 270 ? 0.1880 0.1675 0.2780 -0.0110 -0.0118 -0.0033 295 LEU A C 2123 O O . LEU A 270 ? 0.2013 0.1819 0.2930 -0.0115 -0.0104 -0.0070 295 LEU A O 2124 C CB . LEU A 270 ? 0.2106 0.1768 0.3027 -0.0084 -0.0135 -0.0038 295 LEU A CB 2125 C CG . LEU A 270 ? 0.2377 0.1965 0.3305 -0.0081 -0.0144 -0.0030 295 LEU A CG 2126 C CD1 . LEU A 270 ? 0.3019 0.2588 0.3953 -0.0078 -0.0145 -0.0065 295 LEU A CD1 2127 C CD2 . LEU A 270 ? 0.2613 0.2169 0.3547 -0.0059 -0.0152 -0.0009 295 LEU A CD2 2128 N N . GLY A 271 ? 0.1923 0.1777 0.2804 -0.0115 -0.0120 -0.0016 296 GLY A N 2129 C CA . GLY A 271 ? 0.2071 0.2008 0.2939 -0.0134 -0.0104 -0.0051 296 GLY A CA 2130 C C . GLY A 271 ? 0.1902 0.1853 0.2760 -0.0122 -0.0107 -0.0066 296 GLY A C 2131 O O . GLY A 271 ? 0.2151 0.2089 0.3003 -0.0105 -0.0123 -0.0030 296 GLY A O 2132 N N . PHE A 272 ? 0.2010 0.1990 0.2875 -0.0132 -0.0089 -0.0121 297 PHE A N 2133 C CA . PHE A 272 ? 0.1849 0.1847 0.2706 -0.0129 -0.0091 -0.0142 297 PHE A CA 2134 C C . PHE A 272 ? 0.1989 0.2067 0.2841 -0.0163 -0.0068 -0.0195 297 PHE A C 2135 O O . PHE A 272 ? 0.2287 0.2362 0.3169 -0.0172 -0.0045 -0.0241 297 PHE A O 2136 C CB . PHE A 272 ? 0.2092 0.2013 0.2980 -0.0103 -0.0095 -0.0161 297 PHE A CB 2137 C CG . PHE A 272 ? 0.2130 0.2069 0.3013 -0.0103 -0.0099 -0.0177 297 PHE A CG 2138 C CD1 . PHE A 272 ? 0.2211 0.2142 0.3080 -0.0082 -0.0118 -0.0144 297 PHE A CD1 2139 C CD2 . PHE A 272 ? 0.2384 0.2348 0.3287 -0.0124 -0.0082 -0.0229 297 PHE A CD2 2140 C CE1 . PHE A 272 ? 0.2680 0.2637 0.3546 -0.0084 -0.0123 -0.0155 297 PHE A CE1 2141 C CE2 . PHE A 272 ? 0.2491 0.2471 0.3392 -0.0129 -0.0087 -0.0242 297 PHE A CE2 2142 C CZ . PHE A 272 ? 0.2327 0.2309 0.3206 -0.0110 -0.0109 -0.0201 297 PHE A CZ 2143 N N . HIS A 273 ? 0.1822 0.1980 0.2641 -0.0184 -0.0071 -0.0192 298 HIS A N 2144 C CA . HIS A 273 ? 0.2083 0.2320 0.2895 -0.0223 -0.0048 -0.0256 298 HIS A CA 2145 C C . HIS A 273 ? 0.1705 0.1959 0.2508 -0.0228 -0.0055 -0.0269 298 HIS A C 2146 O O . HIS A 273 ? 0.1880 0.2161 0.2657 -0.0219 -0.0079 -0.0215 298 HIS A O 2147 C CB . HIS A 273 ? 0.2060 0.2428 0.2833 -0.0266 -0.0039 -0.0248 298 HIS A CB 2148 C CG . HIS A 273 ? 0.2074 0.2543 0.2833 -0.0314 -0.0014 -0.0323 298 HIS A CG 2149 N ND1 . HIS A 273 ? 0.1915 0.2352 0.2715 -0.0322 0.0020 -0.0415 298 HIS A ND1 2150 C CD2 . HIS A 273 ? 0.1992 0.2596 0.2704 -0.0360 -0.0015 -0.0323 298 HIS A CD2 2151 C CE1 . HIS A 273 ? 0.2576 0.3116 0.3355 -0.0372 0.0041 -0.0478 298 HIS A CE1 2152 N NE2 . HIS A 273 ? 0.2705 0.3355 0.3423 -0.0399 0.0019 -0.0424 298 HIS A NE2 2153 N N . PHE A 274 ? 0.1896 0.2131 0.2730 -0.0242 -0.0034 -0.0341 299 PHE A N 2154 C CA A PHE A 274 ? 0.1912 0.2167 0.2742 -0.0259 -0.0038 -0.0366 299 PHE A CA 2155 C CA B PHE A 274 ? 0.2144 0.2398 0.2976 -0.0259 -0.0037 -0.0368 299 PHE A CA 2156 C C . PHE A 274 ? 0.2166 0.2561 0.2947 -0.0313 -0.0030 -0.0388 299 PHE A C 2157 O O . PHE A 274 ? 0.2484 0.2918 0.3273 -0.0353 -0.0004 -0.0467 299 PHE A O 2158 C CB A PHE A 274 ? 0.2268 0.2455 0.3163 -0.0262 -0.0016 -0.0435 299 PHE A CB 2159 C CB B PHE A 274 ? 0.2631 0.2817 0.3531 -0.0262 -0.0012 -0.0441 299 PHE A CB 2160 C CG A PHE A 274 ? 0.2076 0.2150 0.3022 -0.0218 -0.0031 -0.0404 299 PHE A CG 2161 C CG B PHE A 274 ? 0.2090 0.2242 0.3013 -0.0265 -0.0021 -0.0453 299 PHE A CG 2162 C CD1 A PHE A 274 ? 0.1920 0.1965 0.2869 -0.0206 -0.0053 -0.0377 299 PHE A CD1 2163 C CD1 B PHE A 274 ? 0.2253 0.2325 0.3203 -0.0227 -0.0044 -0.0406 299 PHE A CD1 2164 C CD2 A PHE A 274 ? 0.2016 0.2029 0.3006 -0.0193 -0.0022 -0.0402 299 PHE A CD2 2165 C CD2 B PHE A 274 ? 0.1947 0.2152 0.2869 -0.0312 -0.0004 -0.0517 299 PHE A CD2 2166 C CE1 A PHE A 274 ? 0.1739 0.1705 0.2732 -0.0173 -0.0066 -0.0347 299 PHE A CE1 2167 C CE1 B PHE A 274 ? 0.2468 0.2518 0.3442 -0.0234 -0.0053 -0.0411 299 PHE A CE1 2168 C CE2 A PHE A 274 ? 0.1984 0.1915 0.3019 -0.0161 -0.0037 -0.0370 299 PHE A CE2 2169 C CE2 B PHE A 274 ? 0.2717 0.2890 0.3666 -0.0319 -0.0013 -0.0525 299 PHE A CE2 2170 C CZ A PHE A 274 ? 0.1847 0.1758 0.2882 -0.0152 -0.0059 -0.0343 299 PHE A CZ 2171 C CZ B PHE A 274 ? 0.3051 0.3147 0.4026 -0.0279 -0.0039 -0.0468 299 PHE A CZ 2172 N N . GLY A 275 ? 0.1997 0.2471 0.2731 -0.0316 -0.0051 -0.0317 300 GLY A N 2173 C CA . GLY A 275 ? 0.2113 0.2746 0.2797 -0.0372 -0.0048 -0.0321 300 GLY A CA 2174 C C . GLY A 275 ? 0.2296 0.3008 0.2951 -0.0368 -0.0073 -0.0222 300 GLY A C 2175 O O . GLY A 275 ? 0.2058 0.2686 0.2734 -0.0318 -0.0094 -0.0154 300 GLY A O 2176 N N . LEU A 276 ? 0.2619 0.3496 0.3231 -0.0425 -0.0070 -0.0215 301 LEU A N 2177 C CA . LEU A 276 ? 0.2406 0.3387 0.2998 -0.0431 -0.0097 -0.0108 301 LEU A CA 2178 C C . LEU A 276 ? 0.2359 0.3351 0.2955 -0.0433 -0.0094 -0.0074 301 LEU A C 2179 O O . LEU A 276 ? 0.2350 0.3304 0.2955 -0.0440 -0.0065 -0.0146 301 LEU A O 2180 C CB . LEU A 276 ? 0.2162 0.3346 0.2707 -0.0499 -0.0102 -0.0100 301 LEU A CB 2181 C CG . LEU A 276 ? 0.2853 0.4044 0.3392 -0.0501 -0.0111 -0.0114 301 LEU A CG 2182 C CD1 . LEU A 276 ? 0.3785 0.5194 0.4272 -0.0581 -0.0113 -0.0116 301 LEU A CD1 2183 C CD2 . LEU A 276 ? 0.3264 0.4375 0.3839 -0.0434 -0.0144 -0.0018 301 LEU A CD2 2184 N N . LYS A 277 ? 0.2079 0.3129 0.2679 -0.0427 -0.0123 0.0039 302 LYS A N 2185 C CA . LYS A 277 ? 0.2381 0.3406 0.2999 -0.0417 -0.0127 0.0091 302 LYS A CA 2186 C C . LYS A 277 ? 0.2275 0.3457 0.2857 -0.0484 -0.0107 0.0066 302 LYS A C 2187 O O . LYS A 277 ? 0.2409 0.3558 0.3003 -0.0482 -0.0098 0.0067 302 LYS A O 2188 C CB . LYS A 277 ? 0.2909 0.3926 0.3563 -0.0385 -0.0164 0.0224 302 LYS A CB 2189 C CG . LYS A 277 ? 0.3718 0.4936 0.4355 -0.0431 -0.0186 0.0313 302 LYS A CG 2190 C CD . LYS A 277 ? 0.5061 0.6244 0.5759 -0.0385 -0.0222 0.0444 302 LYS A CD 2191 C CE . LYS A 277 ? 0.5456 0.6506 0.6206 -0.0347 -0.0229 0.0493 302 LYS A CE 2192 N NZ . LYS A 277 ? 0.6360 0.7523 0.7095 -0.0400 -0.0230 0.0536 302 LYS A NZ 2193 N N . THR A 278 ? 0.2473 0.3836 0.3009 -0.0548 -0.0100 0.0040 303 THR A N 2194 C CA . THR A 278 ? 0.2420 0.3955 0.2916 -0.0620 -0.0076 -0.0001 303 THR A CA 2195 C C . THR A 278 ? 0.2419 0.3870 0.2926 -0.0616 -0.0031 -0.0130 303 THR A C 2196 O O . THR A 278 ? 0.2534 0.4024 0.3043 -0.0632 -0.0016 -0.0135 303 THR A O 2197 C CB . THR A 278 ? 0.3044 0.4792 0.3486 -0.0696 -0.0072 -0.0027 303 THR A CB 2198 O OG1 . THR A 278 ? 0.5197 0.6869 0.5638 -0.0687 -0.0057 -0.0119 303 THR A OG1 2199 C CG2 . THR A 278 ? 0.3284 0.5158 0.3723 -0.0708 -0.0118 0.0122 303 THR A CG2 2200 N N . VAL A 279 ? 0.2574 0.3915 0.3099 -0.0594 -0.0011 -0.0227 304 VAL A N 2201 C CA . VAL A 279 ? 0.2517 0.3764 0.3075 -0.0581 0.0031 -0.0342 304 VAL A CA 2202 C C . VAL A 279 ? 0.2502 0.3585 0.3108 -0.0517 0.0022 -0.0301 304 VAL A C 2203 O O . VAL A 279 ? 0.2529 0.3602 0.3157 -0.0518 0.0049 -0.0346 304 VAL A O 2204 C CB . VAL A 279 ? 0.2907 0.4063 0.3488 -0.0571 0.0050 -0.0439 304 VAL A CB 2205 C CG1 . VAL A 279 ? 0.3144 0.4177 0.3787 -0.0544 0.0088 -0.0536 304 VAL A CG1 2206 C CG2 . VAL A 279 ? 0.3281 0.4607 0.3816 -0.0647 0.0067 -0.0504 304 VAL A CG2 2207 N N . ALA A 280 ? 0.2390 0.3353 0.3014 -0.0464 -0.0014 -0.0218 305 ALA A N 2208 C CA . ALA A 280 ? 0.2268 0.3082 0.2933 -0.0411 -0.0024 -0.0180 305 ALA A CA 2209 C C . ALA A 280 ? 0.2157 0.3042 0.2816 -0.0432 -0.0025 -0.0130 305 ALA A C 2210 O O . ALA A 280 ? 0.2181 0.3012 0.2866 -0.0420 -0.0007 -0.0162 305 ALA A O 2211 C CB . ALA A 280 ? 0.2279 0.2985 0.2959 -0.0360 -0.0060 -0.0100 305 ALA A CB 2212 N N . LYS A 281 ? 0.2131 0.3146 0.2759 -0.0467 -0.0048 -0.0045 306 LYS A N 2213 C CA . LYS A 281 ? 0.2337 0.3425 0.2963 -0.0491 -0.0056 0.0022 306 LYS A CA 2214 C C . LYS A 281 ? 0.2433 0.3663 0.3035 -0.0546 -0.0017 -0.0056 306 LYS A C 2215 O O . LYS A 281 ? 0.2331 0.3565 0.2947 -0.0551 -0.0009 -0.0047 306 LYS A O 2216 C CB . LYS A 281 ? 0.2754 0.3948 0.3370 -0.0513 -0.0094 0.0151 306 LYS A CB 2217 C CG . LYS A 281 ? 0.3255 0.4514 0.3881 -0.0539 -0.0107 0.0237 306 LYS A CG 2218 C CD . LYS A 281 ? 0.3422 0.4743 0.4068 -0.0546 -0.0151 0.0384 306 LYS A CD 2219 C CE . LYS A 281 ? 0.3895 0.5255 0.4564 -0.0569 -0.0166 0.0476 306 LYS A CE 2220 N NZ . LYS A 281 ? 0.3840 0.5408 0.4461 -0.0644 -0.0144 0.0446 306 LYS A NZ 2221 N N . SER A 282 ? 0.2505 0.3856 0.3074 -0.0590 0.0008 -0.0138 307 SER A N 2222 C CA . SER A 282 ? 0.2479 0.3966 0.3032 -0.0642 0.0053 -0.0235 307 SER A CA 2223 C C . SER A 282 ? 0.2139 0.3490 0.2746 -0.0599 0.0086 -0.0317 307 SER A C 2224 O O . SER A 282 ? 0.2584 0.4007 0.3200 -0.0620 0.0110 -0.0341 307 SER A O 2225 C CB . SER A 282 ? 0.2748 0.4352 0.3266 -0.0691 0.0080 -0.0333 307 SER A CB 2226 O OG . SER A 282 ? 0.4785 0.6526 0.5292 -0.0743 0.0130 -0.0442 307 SER A OG 2227 N N . THR A 283 ? 0.2419 0.3584 0.3069 -0.0541 0.0085 -0.0349 308 THR A N 2228 C CA . THR A 283 ? 0.2323 0.3361 0.3037 -0.0498 0.0113 -0.0416 308 THR A CA 2229 C C . THR A 283 ? 0.2352 0.3324 0.3089 -0.0470 0.0095 -0.0342 308 THR A C 2230 O O . THR A 283 ? 0.2265 0.3250 0.3036 -0.0469 0.0124 -0.0384 308 THR A O 2231 C CB . THR A 283 ? 0.2350 0.3219 0.3106 -0.0448 0.0109 -0.0450 308 THR A CB 2232 O OG1 . THR A 283 ? 0.3041 0.3968 0.3791 -0.0479 0.0135 -0.0542 308 THR A OG1 2233 C CG2 . THR A 283 ? 0.3193 0.3933 0.4025 -0.0401 0.0128 -0.0488 308 THR A CG2 2234 N N . PHE A 284 ? 0.2070 0.2973 0.2795 -0.0449 0.0050 -0.0233 309 PHE A N 2235 C CA . PHE A 284 ? 0.2136 0.2971 0.2883 -0.0429 0.0032 -0.0165 309 PHE A CA 2236 C C . PHE A 284 ? 0.2419 0.3407 0.3139 -0.0480 0.0031 -0.0115 309 PHE A C 2237 O O . PHE A 284 ? 0.2499 0.3471 0.3242 -0.0478 0.0034 -0.0095 309 PHE A O 2238 C CB . PHE A 284 ? 0.2312 0.3005 0.3067 -0.0387 -0.0010 -0.0083 309 PHE A CB 2239 C CG . PHE A 284 ? 0.2118 0.2658 0.2907 -0.0336 -0.0007 -0.0130 309 PHE A CG 2240 C CD1 . PHE A 284 ? 0.2293 0.2747 0.3128 -0.0309 0.0006 -0.0164 309 PHE A CD1 2241 C CD2 . PHE A 284 ? 0.2021 0.2522 0.2801 -0.0319 -0.0019 -0.0135 309 PHE A CD2 2242 C CE1 . PHE A 284 ? 0.2326 0.2660 0.3196 -0.0269 0.0006 -0.0197 309 PHE A CE1 2243 C CE2 . PHE A 284 ? 0.2535 0.2910 0.3347 -0.0277 -0.0018 -0.0172 309 PHE A CE2 2244 C CZ . PHE A 284 ? 0.2214 0.2508 0.3071 -0.0254 -0.0006 -0.0201 309 PHE A CZ 2245 N N . ASP A 285 ? 0.2451 0.3603 0.3125 -0.0531 0.0027 -0.0091 310 ASP A N 2246 C CA . ASP A 285 ? 0.2342 0.3677 0.2989 -0.0591 0.0029 -0.0047 310 ASP A CA 2247 C C . ASP A 285 ? 0.2801 0.4216 0.3460 -0.0611 0.0080 -0.0154 310 ASP A C 2248 O O . ASP A 285 ? 0.2808 0.4291 0.3473 -0.0632 0.0084 -0.0124 310 ASP A O 2249 C CB . ASP A 285 ? 0.2632 0.4156 0.3226 -0.0649 0.0017 -0.0010 310 ASP A CB 2250 C CG . ASP A 285 ? 0.2885 0.4380 0.3481 -0.0640 -0.0036 0.0132 310 ASP A CG 2251 O OD1 . ASP A 285 ? 0.2883 0.4214 0.3520 -0.0592 -0.0063 0.0198 310 ASP A OD1 2252 O OD2 . ASP A 285 ? 0.3075 0.4720 0.3638 -0.0682 -0.0051 0.0177 310 ASP A OD2 2253 N N . LEU A 286 ? 0.2296 0.3701 0.2967 -0.0603 0.0119 -0.0278 311 LEU A N 2254 C CA . LEU A 286 ? 0.2357 0.3826 0.3060 -0.0613 0.0175 -0.0394 311 LEU A CA 2255 C C . LEU A 286 ? 0.2496 0.3817 0.3269 -0.0556 0.0183 -0.0401 311 LEU A C 2256 O O . LEU A 286 ? 0.2611 0.4005 0.3405 -0.0569 0.0204 -0.0412 311 LEU A O 2257 C CB . LEU A 286 ? 0.2831 0.4308 0.3546 -0.0617 0.0215 -0.0525 311 LEU A CB 2258 C CG . LEU A 286 ? 0.3154 0.4658 0.3930 -0.0613 0.0279 -0.0662 311 LEU A CG 2259 C CD1 . LEU A 286 ? 0.3468 0.5208 0.4211 -0.0680 0.0312 -0.0696 311 LEU A CD1 2260 C CD2 . LEU A 286 ? 0.3798 0.5252 0.4607 -0.0607 0.0314 -0.0784 311 LEU A CD2 2261 N N . LEU A 287 ? 0.2174 0.3300 0.2983 -0.0498 0.0164 -0.0391 312 LEU A N 2262 C CA . LEU A 287 ? 0.2247 0.3243 0.3130 -0.0446 0.0174 -0.0410 312 LEU A CA 2263 C C . LEU A 287 ? 0.2038 0.2960 0.2922 -0.0430 0.0136 -0.0305 312 LEU A C 2264 O O . LEU A 287 ? 0.2497 0.3378 0.3433 -0.0408 0.0147 -0.0314 312 LEU A O 2265 C CB . LEU A 287 ? 0.2088 0.2929 0.3016 -0.0397 0.0174 -0.0454 312 LEU A CB 2266 C CG . LEU A 287 ? 0.2869 0.3749 0.3816 -0.0408 0.0215 -0.0568 312 LEU A CG 2267 C CD1 . LEU A 287 ? 0.2940 0.3658 0.3937 -0.0361 0.0208 -0.0589 312 LEU A CD1 2268 C CD2 . LEU A 287 ? 0.3074 0.4047 0.4078 -0.0420 0.0273 -0.0666 312 LEU A CD2 2269 N N . PHE A 288 ? 0.2293 0.3199 0.3129 -0.0443 0.0091 -0.0208 313 PHE A N 2270 C CA . PHE A 288 ? 0.2324 0.3133 0.3170 -0.0427 0.0055 -0.0117 313 PHE A CA 2271 C C . PHE A 288 ? 0.2411 0.3283 0.3213 -0.0464 0.0019 -0.0011 313 PHE A C 2272 O O . PHE A 288 ? 0.2346 0.3112 0.3148 -0.0444 -0.0017 0.0059 313 PHE A O 2273 C CB . PHE A 288 ? 0.1849 0.2473 0.2718 -0.0373 0.0034 -0.0110 313 PHE A CB 2274 C CG . PHE A 288 ? 0.2082 0.2600 0.2985 -0.0351 0.0018 -0.0074 313 PHE A CG 2275 C CD1 . PHE A 288 ? 0.2195 0.2570 0.3124 -0.0308 0.0005 -0.0082 313 PHE A CD1 2276 C CD2 . PHE A 288 ? 0.2012 0.2587 0.2920 -0.0379 0.0017 -0.0035 313 PHE A CD2 2277 C CE1 . PHE A 288 ? 0.2114 0.2408 0.3070 -0.0296 -0.0009 -0.0053 313 PHE A CE1 2278 C CE2 . PHE A 288 ? 0.2270 0.2755 0.3208 -0.0365 0.0002 -0.0005 313 PHE A CE2 2279 C CZ . PHE A 288 ? 0.1936 0.2282 0.2896 -0.0325 -0.0010 -0.0016 313 PHE A CZ 2280 N N . PRO A 289 ? 0.2272 0.3326 0.3048 -0.0519 0.0030 0.0004 314 PRO A N 2281 C CA . PRO A 289 ? 0.1851 0.2978 0.2598 -0.0558 -0.0007 0.0120 314 PRO A CA 2282 C C . PRO A 289 ? 0.2223 0.3245 0.2998 -0.0550 -0.0040 0.0213 314 PRO A C 2283 O O . PRO A 289 ? 0.2462 0.3476 0.3237 -0.0564 -0.0077 0.0317 314 PRO A O 2284 C CB . PRO A 289 ? 0.2177 0.3539 0.2894 -0.0624 0.0018 0.0105 314 PRO A CB 2285 C CG . PRO A 289 ? 0.2323 0.3694 0.3069 -0.0611 0.0065 -0.0004 314 PRO A CG 2286 C CD . PRO A 289 ? 0.2386 0.3597 0.3160 -0.0551 0.0078 -0.0084 314 PRO A CD 2287 N N . GLU A 290 ? 0.2190 0.3135 0.2997 -0.0529 -0.0026 0.0175 315 GLU A N 2288 C CA . GLU A 290 ? 0.2472 0.3316 0.3306 -0.0527 -0.0054 0.0247 315 GLU A CA 2289 C C . GLU A 290 ? 0.2629 0.3293 0.3479 -0.0489 -0.0088 0.0291 315 GLU A C 2290 O O . GLU A 290 ? 0.2906 0.3495 0.3778 -0.0497 -0.0116 0.0364 315 GLU A O 2291 C CB . GLU A 290 ? 0.2993 0.3800 0.3859 -0.0511 -0.0031 0.0189 315 GLU A CB 2292 C CG . GLU A 290 ? 0.2776 0.3760 0.3642 -0.0547 0.0003 0.0154 315 GLU A CG 2293 C CD . GLU A 290 ? 0.2958 0.4023 0.3826 -0.0534 0.0050 0.0041 315 GLU A CD 2294 O OE1 . GLU A 290 ? 0.2515 0.3504 0.3379 -0.0502 0.0053 -0.0003 315 GLU A OE1 2295 O OE2 . GLU A 290 ? 0.3298 0.4504 0.4176 -0.0558 0.0086 -0.0007 315 GLU A OE2 2296 N N . LEU A 291 ? 0.2309 0.2906 0.3152 -0.0450 -0.0083 0.0242 316 LEU A N 2297 C CA . LEU A 291 ? 0.2578 0.3023 0.3437 -0.0413 -0.0110 0.0275 316 LEU A CA 2298 C C . LEU A 291 ? 0.2819 0.3289 0.3682 -0.0432 -0.0142 0.0379 316 LEU A C 2299 O O . LEU A 291 ? 0.3332 0.3675 0.4227 -0.0408 -0.0166 0.0425 316 LEU A O 2300 C CB . LEU A 291 ? 0.3100 0.3497 0.3949 -0.0373 -0.0098 0.0204 316 LEU A CB 2301 C CG . LEU A 291 ? 0.3436 0.3745 0.4305 -0.0338 -0.0079 0.0124 316 LEU A CG 2302 C CD1 . LEU A 291 ? 0.3612 0.3878 0.4475 -0.0304 -0.0073 0.0074 316 LEU A CD1 2303 C CD2 . LEU A 291 ? 0.3253 0.3432 0.4148 -0.0323 -0.0098 0.0150 316 LEU A CD2 2304 N N . GLY A 292 ? 0.2623 0.3264 0.3461 -0.0476 -0.0140 0.0415 317 GLY A N 2305 C CA . GLY A 292 ? 0.2998 0.3693 0.3852 -0.0499 -0.0172 0.0529 317 GLY A CA 2306 C C . GLY A 292 ? 0.3048 0.3671 0.3916 -0.0459 -0.0188 0.0549 317 GLY A C 2307 O O . GLY A 292 ? 0.3530 0.4094 0.4444 -0.0449 -0.0218 0.0642 317 GLY A O 2308 N N . LEU A 293 ? 0.2799 0.3426 0.3635 -0.0435 -0.0168 0.0463 318 LEU A N 2309 C CA . LEU A 293 ? 0.2711 0.3293 0.3556 -0.0400 -0.0182 0.0477 318 LEU A CA 2310 C C . LEU A 293 ? 0.3440 0.4195 0.4273 -0.0438 -0.0198 0.0557 318 LEU A C 2311 O O . LEU A 293 ? 0.3695 0.4626 0.4488 -0.0492 -0.0186 0.0551 318 LEU A O 2312 C CB . LEU A 293 ? 0.2601 0.3143 0.3418 -0.0369 -0.0156 0.0364 318 LEU A CB 2313 C CG . LEU A 293 ? 0.2664 0.3060 0.3494 -0.0334 -0.0141 0.0288 318 LEU A CG 2314 C CD1 . LEU A 293 ? 0.2727 0.3093 0.3541 -0.0307 -0.0121 0.0195 318 LEU A CD1 2315 C CD2 . LEU A 293 ? 0.3718 0.3956 0.4591 -0.0301 -0.0163 0.0333 318 LEU A CD2 2316 N N . VAL A 294 ? 0.2940 0.3656 0.3814 -0.0411 -0.0224 0.0633 319 VAL A N 2317 C CA . VAL A 294 ? 0.2802 0.3687 0.3676 -0.0444 -0.0244 0.0726 319 VAL A CA 2318 C C . VAL A 294 ? 0.2633 0.3523 0.3495 -0.0414 -0.0243 0.0696 319 VAL A C 2319 O O . VAL A 294 ? 0.2552 0.3294 0.3418 -0.0362 -0.0232 0.0622 319 VAL A O 2320 C CB . VAL A 294 ? 0.3482 0.4346 0.4437 -0.0444 -0.0281 0.0874 319 VAL A CB 2321 C CG1 . VAL A 294 ? 0.4570 0.5441 0.5536 -0.0483 -0.0284 0.0911 319 VAL A CG1 2322 C CG2 . VAL A 294 ? 0.3907 0.4562 0.4934 -0.0373 -0.0291 0.0885 319 VAL A CG2 2323 N N . GLU A 295 ? 0.2781 0.3856 0.3627 -0.0452 -0.0257 0.0756 320 GLU A N 2324 C CA . GLU A 295 ? 0.3228 0.4337 0.4057 -0.0435 -0.0257 0.0731 320 GLU A CA 2325 C C . GLU A 295 ? 0.2879 0.3804 0.3772 -0.0358 -0.0269 0.0749 320 GLU A C 2326 O O . GLU A 295 ? 0.2582 0.3444 0.3455 -0.0326 -0.0255 0.0669 320 GLU A O 2327 C CB . GLU A 295 ? 0.3552 0.4896 0.4371 -0.0489 -0.0278 0.0828 320 GLU A CB 2328 C CG . GLU A 295 ? 0.4750 0.6306 0.5494 -0.0573 -0.0261 0.0791 320 GLU A CG 2329 C CD . GLU A 295 ? 0.6375 0.8186 0.7095 -0.0634 -0.0279 0.0868 320 GLU A CD 2330 O OE1 . GLU A 295 ? 0.6749 0.8570 0.7519 -0.0608 -0.0309 0.0965 320 GLU A OE1 2331 O OE2 . GLU A 295 ? 0.6882 0.8893 0.7535 -0.0710 -0.0262 0.0828 320 GLU A OE2 2332 N N . GLU A 296 ? 0.2780 0.3621 0.3756 -0.0331 -0.0292 0.0850 321 GLU A N 2333 C CA . GLU A 296 ? 0.2463 0.3142 0.3513 -0.0260 -0.0300 0.0869 321 GLU A CA 2334 C C . GLU A 296 ? 0.2211 0.2696 0.3249 -0.0215 -0.0277 0.0750 321 GLU A C 2335 O O . GLU A 296 ? 0.2874 0.3237 0.3957 -0.0158 -0.0276 0.0735 321 GLU A O 2336 C CB . GLU A 296 ? 0.3469 0.4102 0.4628 -0.0245 -0.0327 0.1002 321 GLU A CB 2337 C CG . GLU A 296 ? 0.4527 0.5350 0.5726 -0.0276 -0.0357 0.1146 321 GLU A CG 2338 C CD . GLU A 296 ? 0.5826 0.6852 0.6961 -0.0361 -0.0362 0.1180 321 GLU A CD 2339 O OE1 . GLU A 296 ? 0.6777 0.8014 0.7897 -0.0403 -0.0379 0.1254 321 GLU A OE1 2340 O OE2 . GLU A 296 ? 0.4445 0.5436 0.5544 -0.0389 -0.0349 0.1133 321 GLU A OE2 2341 N N . ASP A 297 ? 0.2453 0.2920 0.3436 -0.0242 -0.0257 0.0670 322 ASP A N 2342 C CA . ASP A 297 ? 0.2590 0.2899 0.3559 -0.0207 -0.0237 0.0564 322 ASP A CA 2343 C C . ASP A 297 ? 0.2554 0.2872 0.3476 -0.0191 -0.0220 0.0473 322 ASP A C 2344 O O . ASP A 297 ? 0.2763 0.2957 0.3691 -0.0152 -0.0210 0.0410 322 ASP A O 2345 C CB . ASP A 297 ? 0.2229 0.2529 0.3167 -0.0240 -0.0222 0.0519 322 ASP A CB 2346 C CG . ASP A 297 ? 0.2896 0.3142 0.3886 -0.0251 -0.0237 0.0595 322 ASP A CG 2347 O OD1 . ASP A 297 ? 0.3060 0.3198 0.4119 -0.0217 -0.0252 0.0645 322 ASP A OD1 2348 O OD2 . ASP A 297 ? 0.3107 0.3420 0.4073 -0.0296 -0.0233 0.0600 322 ASP A OD2 2349 N N . TYR A 298 ? 0.2367 0.2841 0.3242 -0.0228 -0.0216 0.0467 323 TYR A N 2350 C CA . TYR A 298 ? 0.2148 0.2641 0.2981 -0.0224 -0.0200 0.0380 323 TYR A CA 2351 C C . TYR A 298 ? 0.2166 0.2667 0.3022 -0.0192 -0.0215 0.0418 323 TYR A C 2352 O O . TYR A 298 ? 0.2380 0.3003 0.3251 -0.0209 -0.0234 0.0502 323 TYR A O 2353 C CB . TYR A 298 ? 0.2286 0.2944 0.3060 -0.0286 -0.0185 0.0340 323 TYR A CB 2354 C CG . TYR A 298 ? 0.2388 0.3050 0.3140 -0.0315 -0.0162 0.0282 323 TYR A CG 2355 C CD1 . TYR A 298 ? 0.2059 0.2669 0.2794 -0.0310 -0.0133 0.0171 323 TYR A CD1 2356 C CD2 . TYR A 298 ? 0.2370 0.3096 0.3129 -0.0347 -0.0169 0.0344 323 TYR A CD2 2357 C CE1 . TYR A 298 ? 0.1751 0.2372 0.2480 -0.0331 -0.0110 0.0121 323 TYR A CE1 2358 C CE2 . TYR A 298 ? 0.2135 0.2877 0.2877 -0.0373 -0.0147 0.0292 323 TYR A CE2 2359 C CZ . TYR A 298 ? 0.1978 0.2668 0.2707 -0.0362 -0.0116 0.0178 323 TYR A CZ 2360 O OH . TYR A 298 ? 0.2807 0.3519 0.3533 -0.0383 -0.0092 0.0128 323 TYR A OH 2361 N N . LEU A 299 ? 0.2046 0.2435 0.2911 -0.0148 -0.0208 0.0360 324 LEU A N 2362 C CA . LEU A 299 ? 0.2437 0.2832 0.3328 -0.0114 -0.0219 0.0387 324 LEU A CA 2363 C C . LEU A 299 ? 0.2020 0.2448 0.2863 -0.0123 -0.0207 0.0308 324 LEU A C 2364 O O . LEU A 299 ? 0.2104 0.2451 0.2929 -0.0118 -0.0190 0.0225 324 LEU A O 2365 C CB . LEU A 299 ? 0.2308 0.2549 0.3259 -0.0053 -0.0222 0.0395 324 LEU A CB 2366 C CG . LEU A 299 ? 0.3119 0.3296 0.4131 -0.0041 -0.0232 0.0465 324 LEU A CG 2367 C CD1 . LEU A 299 ? 0.4110 0.4135 0.5181 0.0015 -0.0228 0.0448 324 LEU A CD1 2368 C CD2 . LEU A 299 ? 0.4260 0.4554 0.5312 -0.0056 -0.0254 0.0582 324 LEU A CD2 2369 N N . GLU A 300 ? 0.1963 0.2517 0.2796 -0.0139 -0.0217 0.0341 325 GLU A N 2370 C CA . GLU A 300 ? 0.1881 0.2470 0.2677 -0.0151 -0.0209 0.0276 325 GLU A CA 2371 C C . GLU A 300 ? 0.1705 0.2229 0.2539 -0.0096 -0.0217 0.0290 325 GLU A C 2372 O O . GLU A 300 ? 0.2180 0.2726 0.3064 -0.0065 -0.0234 0.0371 325 GLU A O 2373 C CB . GLU A 300 ? 0.2040 0.2819 0.2798 -0.0209 -0.0215 0.0298 325 GLU A CB 2374 C CG . GLU A 300 ? 0.2830 0.3695 0.3540 -0.0272 -0.0199 0.0256 325 GLU A CG 2375 C CD . GLU A 300 ? 0.3192 0.4260 0.3857 -0.0339 -0.0202 0.0266 325 GLU A CD 2376 O OE1 . GLU A 300 ? 0.3335 0.4494 0.4014 -0.0336 -0.0224 0.0340 325 GLU A OE1 2377 O OE2 . GLU A 300 ? 0.2625 0.3774 0.3245 -0.0397 -0.0181 0.0199 325 GLU A OE2 2378 N N . MET A 301 ? 0.2016 0.2466 0.2836 -0.0083 -0.0205 0.0213 326 MET A N 2379 C CA . MET A 301 ? 0.2041 0.2437 0.2893 -0.0035 -0.0210 0.0215 326 MET A CA 2380 C C . MET A 301 ? 0.1804 0.2181 0.2625 -0.0048 -0.0200 0.0138 326 MET A C 2381 O O . MET A 301 ? 0.1898 0.2282 0.2687 -0.0088 -0.0188 0.0080 326 MET A O 2382 C CB . MET A 301 ? 0.1863 0.2125 0.2762 0.0016 -0.0208 0.0223 326 MET A CB 2383 C CG . MET A 301 ? 0.1869 0.2026 0.2751 0.0009 -0.0194 0.0158 326 MET A CG 2384 S SD . MET A 301 ? 0.2069 0.2086 0.3002 0.0054 -0.0191 0.0165 326 MET A SD 2385 C CE . MET A 301 ? 0.1969 0.2018 0.2928 0.0039 -0.0201 0.0246 326 MET A CE 2386 N N . SER A 302 ? 0.1784 0.2144 0.2625 -0.0014 -0.0205 0.0137 327 SER A N 2387 C CA . SER A 302 ? 0.1830 0.2173 0.2652 -0.0028 -0.0199 0.0075 327 SER A CA 2388 C C . SER A 302 ? 0.1693 0.1919 0.2519 -0.0021 -0.0187 0.0023 327 SER A C 2389 O O . SER A 302 ? 0.1848 0.2002 0.2692 0.0002 -0.0184 0.0033 327 SER A O 2390 C CB . SER A 302 ? 0.2004 0.2369 0.2847 0.0005 -0.0207 0.0093 327 SER A CB 2391 O OG . SER A 302 ? 0.1946 0.2221 0.2825 0.0056 -0.0203 0.0093 327 SER A OG 2392 N N . TRP A 303 ? 0.1670 0.1881 0.2486 -0.0044 -0.0181 -0.0029 328 TRP A N 2393 C CA . TRP A 303 ? 0.1753 0.1869 0.2585 -0.0037 -0.0173 -0.0066 328 TRP A CA 2394 C C . TRP A 303 ? 0.1561 0.1619 0.2415 0.0006 -0.0178 -0.0051 328 TRP A C 2395 O O . TRP A 303 ? 0.1642 0.1629 0.2506 0.0018 -0.0173 -0.0059 328 TRP A O 2396 C CB . TRP A 303 ? 0.1699 0.1811 0.2537 -0.0066 -0.0169 -0.0109 328 TRP A CB 2397 C CG . TRP A 303 ? 0.1725 0.1757 0.2592 -0.0054 -0.0167 -0.0127 328 TRP A CG 2398 C CD1 . TRP A 303 ? 0.2120 0.2096 0.3005 -0.0059 -0.0156 -0.0147 328 TRP A CD1 2399 C CD2 . TRP A 303 ? 0.1958 0.1976 0.2841 -0.0036 -0.0176 -0.0119 328 TRP A CD2 2400 N NE1 . TRP A 303 ? 0.2517 0.2445 0.3429 -0.0047 -0.0161 -0.0147 328 TRP A NE1 2401 C CE2 . TRP A 303 ? 0.2103 0.2059 0.3011 -0.0036 -0.0173 -0.0131 328 TRP A CE2 2402 C CE3 . TRP A 303 ? 0.1942 0.2006 0.2821 -0.0024 -0.0187 -0.0102 328 TRP A CE3 2403 C CZ2 . TRP A 303 ? 0.1972 0.1921 0.2899 -0.0028 -0.0182 -0.0124 328 TRP A CZ2 2404 C CZ3 . TRP A 303 ? 0.2231 0.2284 0.3126 -0.0015 -0.0193 -0.0101 328 TRP A CZ3 2405 C CH2 . TRP A 303 ? 0.2013 0.2013 0.2931 -0.0019 -0.0191 -0.0110 328 TRP A CH2 2406 N N . GLY A 304 ? 0.1839 0.1934 0.2700 0.0028 -0.0185 -0.0034 329 GLY A N 2407 C CA . GLY A 304 ? 0.1912 0.1966 0.2794 0.0066 -0.0184 -0.0034 329 GLY A CA 2408 C C . GLY A 304 ? 0.1760 0.1766 0.2663 0.0095 -0.0180 -0.0012 329 GLY A C 2409 O O . GLY A 304 ? 0.1924 0.1861 0.2839 0.0109 -0.0174 -0.0032 329 GLY A O 2410 N N . GLU A 305 ? 0.1742 0.1790 0.2652 0.0099 -0.0184 0.0032 330 GLU A N 2411 C CA . GLU A 305 ? 0.1868 0.1871 0.2810 0.0121 -0.0183 0.0065 330 GLU A CA 2412 C C . GLU A 305 ? 0.1820 0.1754 0.2748 0.0099 -0.0178 0.0044 330 GLU A C 2413 O O . GLU A 305 ? 0.1876 0.1735 0.2829 0.0116 -0.0173 0.0044 330 GLU A O 2414 C CB . GLU A 305 ? 0.1812 0.1894 0.2767 0.0119 -0.0193 0.0131 330 GLU A CB 2415 C CG . GLU A 305 ? 0.1662 0.1808 0.2655 0.0154 -0.0198 0.0168 330 GLU A CG 2416 C CD . GLU A 305 ? 0.2243 0.2498 0.3246 0.0143 -0.0212 0.0242 330 GLU A CD 2417 O OE1 . GLU A 305 ? 0.2466 0.2782 0.3423 0.0093 -0.0217 0.0246 330 GLU A OE1 2418 O OE2 . GLU A 305 ? 0.2359 0.2649 0.3423 0.0182 -0.0216 0.0297 330 GLU A OE2 2419 N N . SER A 306 ? 0.1716 0.1676 0.2608 0.0059 -0.0177 0.0024 331 SER A N 2420 C CA . SER A 306 ? 0.1829 0.1744 0.2713 0.0037 -0.0170 0.0008 331 SER A CA 2421 C C . SER A 306 ? 0.2021 0.1855 0.2914 0.0046 -0.0165 -0.0028 331 SER A C 2422 O O . SER A 306 ? 0.2127 0.1907 0.3028 0.0044 -0.0162 -0.0028 331 SER A O 2423 C CB . SER A 306 ? 0.1966 0.1933 0.2821 -0.0004 -0.0164 -0.0017 331 SER A CB 2424 O OG . SER A 306 ? 0.1959 0.1907 0.2814 -0.0014 -0.0159 -0.0063 331 SER A OG 2425 N N . PHE A 307 ? 0.2010 0.1848 0.2903 0.0052 -0.0166 -0.0056 332 PHE A N 2426 C CA . PHE A 307 ? 0.2019 0.1807 0.2919 0.0053 -0.0163 -0.0084 332 PHE A CA 2427 C C . PHE A 307 ? 0.2459 0.2202 0.3376 0.0080 -0.0160 -0.0085 332 PHE A C 2428 O O . PHE A 307 ? 0.2646 0.2339 0.3568 0.0073 -0.0157 -0.0104 332 PHE A O 2429 C CB . PHE A 307 ? 0.2225 0.2046 0.3124 0.0044 -0.0167 -0.0103 332 PHE A CB 2430 C CG . PHE A 307 ? 0.2258 0.2078 0.3162 0.0015 -0.0165 -0.0116 332 PHE A CG 2431 C CD1 . PHE A 307 ? 0.2374 0.2197 0.3275 -0.0002 -0.0158 -0.0118 332 PHE A CD1 2432 C CD2 . PHE A 307 ? 0.2267 0.2091 0.3190 0.0004 -0.0170 -0.0125 332 PHE A CD2 2433 C CE1 . PHE A 307 ? 0.2309 0.2128 0.3231 -0.0024 -0.0151 -0.0138 332 PHE A CE1 2434 C CE2 . PHE A 307 ? 0.2447 0.2264 0.3398 -0.0018 -0.0167 -0.0132 332 PHE A CE2 2435 C CZ . PHE A 307 ? 0.2546 0.2356 0.3499 -0.0029 -0.0155 -0.0144 332 PHE A CZ 2436 N N . ALA A 308 ? 0.2002 0.1765 0.2937 0.0109 -0.0160 -0.0068 333 ALA A N 2437 C CA . ALA A 308 ? 0.2089 0.1802 0.3058 0.0138 -0.0152 -0.0075 333 ALA A CA 2438 C C . ALA A 308 ? 0.2385 0.2037 0.3373 0.0135 -0.0152 -0.0050 333 ALA A C 2439 O O . ALA A 308 ? 0.2678 0.2263 0.3683 0.0135 -0.0144 -0.0073 333 ALA A O 2440 C CB . ALA A 308 ? 0.2312 0.2065 0.3313 0.0176 -0.0150 -0.0056 333 ALA A CB 2441 N N . TYR A 309 ? 0.2015 0.1699 0.2999 0.0125 -0.0159 -0.0002 334 TYR A N 2442 C CA . TYR A 309 ? 0.2284 0.1931 0.3289 0.0117 -0.0162 0.0036 334 TYR A CA 2443 C C . TYR A 309 ? 0.2448 0.2050 0.3431 0.0085 -0.0159 0.0010 334 TYR A C 2444 O O . TYR A 309 ? 0.2464 0.2000 0.3472 0.0083 -0.0157 0.0014 334 TYR A O 2445 C CB . TYR A 309 ? 0.2270 0.1997 0.3266 0.0103 -0.0172 0.0093 334 TYR A CB 2446 C CG . TYR A 309 ? 0.2565 0.2279 0.3581 0.0087 -0.0178 0.0146 334 TYR A CG 2447 C CD1 . TYR A 309 ? 0.3216 0.2897 0.4298 0.0113 -0.0183 0.0200 334 TYR A CD1 2448 C CD2 . TYR A 309 ? 0.2984 0.2727 0.3963 0.0047 -0.0178 0.0144 334 TYR A CD2 2449 C CE1 . TYR A 309 ? 0.3079 0.2755 0.4186 0.0094 -0.0192 0.0260 334 TYR A CE1 2450 C CE2 . TYR A 309 ? 0.3547 0.3296 0.4542 0.0027 -0.0185 0.0196 334 TYR A CE2 2451 C CZ . TYR A 309 ? 0.3673 0.3389 0.4730 0.0048 -0.0193 0.0259 334 TYR A CZ 2452 O OH . TYR A 309 ? 0.4298 0.4025 0.5377 0.0024 -0.0203 0.0322 334 TYR A OH 2453 N N . LEU A 310 ? 0.2211 0.1849 0.3155 0.0060 -0.0159 -0.0016 335 LEU A N 2454 C CA . LEU A 310 ? 0.2249 0.1859 0.3182 0.0032 -0.0156 -0.0034 335 LEU A CA 2455 C C . LEU A 310 ? 0.2845 0.2395 0.3787 0.0033 -0.0153 -0.0068 335 LEU A C 2456 O O . LEU A 310 ? 0.2688 0.2204 0.3633 0.0013 -0.0152 -0.0072 335 LEU A O 2457 C CB . LEU A 310 ? 0.2319 0.1978 0.3230 0.0011 -0.0153 -0.0056 335 LEU A CB 2458 C CG . LEU A 310 ? 0.2463 0.2185 0.3359 -0.0007 -0.0151 -0.0038 335 LEU A CG 2459 C CD1 . LEU A 310 ? 0.3111 0.2870 0.4001 -0.0022 -0.0144 -0.0073 335 LEU A CD1 2460 C CD2 . LEU A 310 ? 0.3105 0.2825 0.4003 -0.0027 -0.0149 -0.0015 335 LEU A CD2 2461 N N . ALA A 311 ? 0.2495 0.2047 0.3442 0.0053 -0.0150 -0.0096 336 ALA A N 2462 C CA . ALA A 311 ? 0.2486 0.2003 0.3439 0.0049 -0.0144 -0.0137 336 ALA A CA 2463 C C . ALA A 311 ? 0.2785 0.2234 0.3775 0.0067 -0.0136 -0.0144 336 ALA A C 2464 O O . ALA A 311 ? 0.2925 0.2344 0.3922 0.0060 -0.0127 -0.0190 336 ALA A O 2465 C CB . ALA A 311 ? 0.2274 0.1842 0.3215 0.0055 -0.0144 -0.0167 336 ALA A CB 2466 N N . GLY A 312 ? 0.2619 0.2051 0.3640 0.0088 -0.0138 -0.0099 337 GLY A N 2467 C CA . GLY A 312 ? 0.2349 0.1707 0.3428 0.0109 -0.0130 -0.0095 337 GLY A CA 2468 C C . GLY A 312 ? 0.2645 0.1999 0.3764 0.0150 -0.0117 -0.0124 337 GLY A C 2469 O O . GLY A 312 ? 0.3070 0.2352 0.4249 0.0168 -0.0104 -0.0141 337 GLY A O 2470 N N . LEU A 313 ? 0.2647 0.2077 0.3741 0.0164 -0.0118 -0.0131 338 LEU A N 2471 C CA . LEU A 313 ? 0.2434 0.1880 0.3568 0.0205 -0.0104 -0.0156 338 LEU A CA 2472 C C . LEU A 313 ? 0.2802 0.2239 0.4003 0.0245 -0.0106 -0.0094 338 LEU A C 2473 O O . LEU A 313 ? 0.3148 0.2601 0.4345 0.0235 -0.0122 -0.0026 338 LEU A O 2474 C CB . LEU A 313 ? 0.2590 0.2131 0.3678 0.0204 -0.0108 -0.0172 338 LEU A CB 2475 C CG . LEU A 313 ? 0.3754 0.3327 0.4787 0.0165 -0.0109 -0.0219 338 LEU A CG 2476 C CD1 . LEU A 313 ? 0.3253 0.2920 0.4262 0.0169 -0.0112 -0.0228 338 LEU A CD1 2477 C CD2 . LEU A 313 ? 0.4033 0.3560 0.5080 0.0154 -0.0092 -0.0283 338 LEU A CD2 2478 N N . GLU A 314 ? 0.2700 0.2123 0.3968 0.0289 -0.0088 -0.0114 339 GLU A N 2479 C CA . GLU A 314 ? 0.2655 0.2078 0.4008 0.0333 -0.0089 -0.0047 339 GLU A CA 2480 C C . GLU A 314 ? 0.3346 0.2886 0.4675 0.0344 -0.0104 0.0006 339 GLU A C 2481 O O . GLU A 314 ? 0.3768 0.3342 0.5127 0.0352 -0.0120 0.0089 339 GLU A O 2482 C CB . GLU A 314 ? 0.3123 0.2488 0.4574 0.0382 -0.0060 -0.0091 339 GLU A CB 2483 C CG . GLU A 314 ? 0.3262 0.2506 0.4749 0.0367 -0.0043 -0.0148 339 GLU A CG 2484 C CD . GLU A 314 ? 0.5487 0.4658 0.7013 0.0352 -0.0059 -0.0075 339 GLU A CD 2485 O OE1 . GLU A 314 ? 0.5684 0.4864 0.7281 0.0382 -0.0070 0.0015 339 GLU A OE1 2486 O OE2 . GLU A 314 ? 0.5450 0.4564 0.6935 0.0306 -0.0062 -0.0101 339 GLU A OE2 2487 N N . THR A 315 ? 0.2810 0.2420 0.4084 0.0338 -0.0101 -0.0040 340 THR A N 2488 C CA . THR A 315 ? 0.2576 0.2297 0.3829 0.0345 -0.0113 -0.0001 340 THR A CA 2489 C C . THR A 315 ? 0.2727 0.2507 0.3893 0.0308 -0.0120 -0.0042 340 THR A C 2490 O O . THR A 315 ? 0.2595 0.2343 0.3729 0.0287 -0.0112 -0.0102 340 THR A O 2491 C CB . THR A 315 ? 0.2937 0.2697 0.4261 0.0400 -0.0097 -0.0009 340 THR A CB 2492 O OG1 . THR A 315 ? 0.2841 0.2595 0.4151 0.0401 -0.0075 -0.0098 340 THR A OG1 2493 C CG2 . THR A 315 ? 0.3282 0.2980 0.4722 0.0447 -0.0086 0.0032 340 THR A CG2 2494 N N . VAL A 316 ? 0.2352 0.2224 0.3485 0.0296 -0.0135 -0.0007 341 VAL A N 2495 C CA . VAL A 316 ? 0.2320 0.2253 0.3392 0.0266 -0.0140 -0.0038 341 VAL A CA 2496 C C . VAL A 316 ? 0.2280 0.2240 0.3367 0.0287 -0.0125 -0.0090 341 VAL A C 2497 O O . VAL A 316 ? 0.2389 0.2365 0.3435 0.0258 -0.0125 -0.0130 341 VAL A O 2498 C CB . VAL A 316 ? 0.2917 0.2947 0.3966 0.0251 -0.0157 0.0006 341 VAL A CB 2499 C CG1 . VAL A 316 ? 0.3112 0.3207 0.4122 0.0228 -0.0161 -0.0023 341 VAL A CG1 2500 C CG2 . VAL A 316 ? 0.2995 0.3018 0.4011 0.0213 -0.0170 0.0036 341 VAL A CG2 2501 N N . SER A 317 ? 0.2059 0.2032 0.3211 0.0336 -0.0110 -0.0087 342 SER A N 2502 C CA . SER A 317 ? 0.1954 0.1966 0.3124 0.0356 -0.0090 -0.0145 342 SER A CA 2503 C C . SER A 317 ? 0.2276 0.2232 0.3424 0.0333 -0.0076 -0.0216 342 SER A C 2504 O O . SER A 317 ? 0.2188 0.2206 0.3307 0.0316 -0.0070 -0.0263 342 SER A O 2505 C CB . SER A 317 ? 0.2016 0.2032 0.3281 0.0419 -0.0069 -0.0140 342 SER A CB 2506 O OG . SER A 317 ? 0.2534 0.2653 0.3815 0.0438 -0.0079 -0.0084 342 SER A OG 2507 N N . GLN A 318 ? 0.2178 0.2029 0.3338 0.0327 -0.0074 -0.0221 343 GLN A N 2508 C CA . GLN A 318 ? 0.2329 0.2132 0.3469 0.0299 -0.0061 -0.0288 343 GLN A CA 2509 C C . GLN A 318 ? 0.2165 0.2018 0.3227 0.0245 -0.0079 -0.0295 343 GLN A C 2510 O O . GLN A 318 ? 0.2223 0.2091 0.3263 0.0218 -0.0070 -0.0349 343 GLN A O 2511 C CB . GLN A 318 ? 0.2627 0.2310 0.3796 0.0297 -0.0058 -0.0283 343 GLN A CB 2512 C CG . GLN A 318 ? 0.2873 0.2490 0.4139 0.0347 -0.0034 -0.0295 343 GLN A CG 2513 C CD . GLN A 318 ? 0.3098 0.2595 0.4394 0.0334 -0.0026 -0.0315 343 GLN A CD 2514 O OE1 . GLN A 318 ? 0.3576 0.3038 0.4830 0.0297 -0.0046 -0.0283 343 GLN A OE1 2515 N NE2 . GLN A 318 ? 0.3322 0.2757 0.4697 0.0363 0.0004 -0.0372 343 GLN A NE2 2516 N N . LEU A 319 ? 0.2084 0.1969 0.3111 0.0226 -0.0102 -0.0241 344 LEU A N 2517 C CA . LEU A 319 ? 0.1821 0.1752 0.2797 0.0180 -0.0118 -0.0240 344 LEU A CA 2518 C C . LEU A 319 ? 0.2109 0.2137 0.3073 0.0171 -0.0114 -0.0272 344 LEU A C 2519 O O . LEU A 319 ? 0.2111 0.2177 0.3047 0.0132 -0.0122 -0.0284 344 LEU A O 2520 C CB . LEU A 319 ? 0.2009 0.1963 0.2965 0.0166 -0.0139 -0.0187 344 LEU A CB 2521 C CG . LEU A 319 ? 0.1874 0.1760 0.2827 0.0158 -0.0145 -0.0157 344 LEU A CG 2522 C CD1 . LEU A 319 ? 0.2048 0.1979 0.2986 0.0145 -0.0159 -0.0118 344 LEU A CD1 2523 C CD2 . LEU A 319 ? 0.2352 0.2191 0.3287 0.0124 -0.0148 -0.0172 344 LEU A CD2 2524 N N . ASN A 320 ? 0.1939 0.2023 0.2931 0.0206 -0.0102 -0.0279 345 ASN A N 2525 C CA . ASN A 320 ? 0.2047 0.2245 0.3027 0.0197 -0.0098 -0.0304 345 ASN A CA 2526 C C . ASN A 320 ? 0.1949 0.2168 0.2939 0.0198 -0.0071 -0.0379 345 ASN A C 2527 O O . ASN A 320 ? 0.2601 0.2931 0.3587 0.0192 -0.0062 -0.0408 345 ASN A O 2528 C CB . ASN A 320 ? 0.2167 0.2438 0.3171 0.0230 -0.0097 -0.0277 345 ASN A CB 2529 C CG . ASN A 320 ? 0.2330 0.2729 0.3307 0.0201 -0.0108 -0.0270 345 ASN A CG 2530 O OD1 . ASN A 320 ? 0.2299 0.2722 0.3241 0.0153 -0.0127 -0.0253 345 ASN A OD1 2531 N ND2 . ASN A 320 ? 0.3099 0.3588 0.4103 0.0231 -0.0095 -0.0278 345 ASN A ND2 2532 N N . ASN A 321 ? 0.2295 0.2418 0.3300 0.0200 -0.0057 -0.0415 346 ASN A N 2533 C CA . ASN A 321 ? 0.2243 0.2379 0.3260 0.0195 -0.0028 -0.0501 346 ASN A CA 2534 C C . ASN A 321 ? 0.2535 0.2678 0.3503 0.0134 -0.0038 -0.0521 346 ASN A C 2535 O O . ASN A 321 ? 0.2515 0.2559 0.3486 0.0124 -0.0039 -0.0525 346 ASN A O 2536 C CB . ASN A 321 ? 0.2561 0.2583 0.3647 0.0242 -0.0001 -0.0535 346 ASN A CB 2537 C CG . ASN A 321 ? 0.3365 0.3395 0.4474 0.0238 0.0037 -0.0640 346 ASN A CG 2538 O OD1 . ASN A 321 ? 0.3360 0.3499 0.4426 0.0197 0.0042 -0.0687 346 ASN A OD1 2539 N ND2 . ASN A 321 ? 0.4358 0.4280 0.5542 0.0278 0.0064 -0.0676 346 ASN A ND2 2540 N N . ARG A 322 ? 0.2599 0.2872 0.3528 0.0092 -0.0046 -0.0528 347 ARG A N 2541 C CA . ARG A 322 ? 0.2323 0.2632 0.3212 0.0030 -0.0062 -0.0526 347 ARG A CA 2542 C C . ARG A 322 ? 0.2313 0.2597 0.3201 0.0009 -0.0037 -0.0610 347 ARG A C 2543 O O . ARG A 322 ? 0.2987 0.3271 0.3848 -0.0039 -0.0049 -0.0606 347 ARG A O 2544 C CB . ARG A 322 ? 0.2478 0.2949 0.3335 -0.0013 -0.0079 -0.0501 347 ARG A CB 2545 C CG . ARG A 322 ? 0.2608 0.3210 0.3460 -0.0022 -0.0052 -0.0576 347 ARG A CG 2546 C CD . ARG A 322 ? 0.2518 0.3295 0.3343 -0.0066 -0.0074 -0.0534 347 ARG A CD 2547 N NE . ARG A 322 ? 0.2519 0.3355 0.3315 -0.0131 -0.0102 -0.0492 347 ARG A NE 2548 C CZ . ARG A 322 ? 0.2583 0.3445 0.3382 -0.0156 -0.0139 -0.0396 347 ARG A CZ 2549 N NH1 . ARG A 322 ? 0.2055 0.2887 0.2874 -0.0126 -0.0153 -0.0341 347 ARG A NH1 2550 N NH2 . ARG A 322 ? 0.2190 0.3112 0.2980 -0.0212 -0.0163 -0.0355 347 ARG A NH2 2551 N N . PHE A 323 ? 0.2641 0.2904 0.3566 0.0044 0.0000 -0.0687 348 PHE A N 2552 C CA . PHE A 323 ? 0.3136 0.3373 0.4068 0.0021 0.0030 -0.0783 348 PHE A CA 2553 C C . PHE A 323 ? 0.3153 0.3211 0.4140 0.0058 0.0046 -0.0799 348 PHE A C 2554 O O . PHE A 323 ? 0.3673 0.3683 0.4685 0.0049 0.0076 -0.0886 348 PHE A O 2555 C CB . PHE A 323 ? 0.3067 0.3420 0.4009 0.0022 0.0068 -0.0878 348 PHE A CB 2556 C CG . PHE A 323 ? 0.3010 0.3561 0.3895 -0.0032 0.0052 -0.0865 348 PHE A CG 2557 C CD1 . PHE A 323 ? 0.3572 0.4195 0.4402 -0.0105 0.0026 -0.0841 348 PHE A CD1 2558 C CD2 . PHE A 323 ? 0.4052 0.4725 0.4943 -0.0012 0.0060 -0.0867 348 PHE A CD2 2559 C CE1 . PHE A 323 ? 0.3773 0.4586 0.4560 -0.0158 0.0008 -0.0813 348 PHE A CE1 2560 C CE2 . PHE A 323 ? 0.3523 0.4384 0.4364 -0.0066 0.0042 -0.0844 348 PHE A CE2 2561 C CZ . PHE A 323 ? 0.3483 0.4414 0.4275 -0.0140 0.0015 -0.0814 348 PHE A CZ 2562 N N . LEU A 324 ? 0.3274 0.3239 0.4280 0.0094 0.0024 -0.0714 349 LEU A N 2563 C CA . LEU A 324 ? 0.3839 0.3647 0.4896 0.0122 0.0031 -0.0707 349 LEU A CA 2564 C C . LEU A 324 ? 0.3190 0.2951 0.4212 0.0066 0.0019 -0.0713 349 LEU A C 2565 O O . LEU A 324 ? 0.4264 0.4066 0.5234 0.0030 -0.0012 -0.0655 349 LEU A O 2566 C CB . LEU A 324 ? 0.4845 0.4598 0.5923 0.0164 0.0008 -0.0609 349 LEU A CB 2567 C CG . LEU A 324 ? 0.4862 0.4471 0.6003 0.0196 0.0013 -0.0584 349 LEU A CG 2568 C CD1 . LEU A 324 ? 0.6144 0.5699 0.7374 0.0241 0.0051 -0.0650 349 LEU A CD1 2569 C CD2 . LEU A 324 ? 0.4392 0.3986 0.5540 0.0225 -0.0013 -0.0485 349 LEU A CD2 2570 N N . LYS A 325 ? 0.2890 0.3274 0.5545 0.0149 0.0008 -0.0939 350 LYS A N 2571 C CA . LYS A 325 ? 0.4241 0.4578 0.6771 0.0123 0.0009 -0.0934 350 LYS A CA 2572 C C . LYS A 325 ? 0.3827 0.4088 0.6275 0.0122 -0.0057 -0.0825 350 LYS A C 2573 O O . LYS A 325 ? 0.5921 0.6111 0.8463 0.0143 -0.0105 -0.0785 350 LYS A O 2574 C CB . LYS A 325 ? 0.5571 0.5868 0.8214 0.0131 0.0029 -0.1012 350 LYS A CB 2575 C CG . LYS A 325 ? 0.6409 0.6759 0.9219 0.0150 0.0082 -0.1117 350 LYS A CG 2576 C CD . LYS A 325 ? 0.7602 0.7902 1.0512 0.0153 0.0105 -0.1199 350 LYS A CD 2577 C CE . LYS A 325 ? 0.7874 0.8183 1.1019 0.0193 0.0133 -0.1277 350 LYS A CE 2578 N NZ . LYS A 325 ? 0.8486 0.8722 1.1741 0.0199 0.0148 -0.1349 350 LYS A NZ 2579 N N . PHE A 326 ? 0.3604 0.3882 0.5881 0.0094 -0.0058 -0.0776 351 PHE A N 2580 C CA . PHE A 326 ? 0.3315 0.3530 0.5503 0.0088 -0.0110 -0.0680 351 PHE A CA 2581 C C . PHE A 326 ? 0.3891 0.4046 0.6038 0.0075 -0.0120 -0.0674 351 PHE A C 2582 O O . PHE A 326 ? 0.3625 0.3708 0.5799 0.0082 -0.0168 -0.0617 351 PHE A O 2583 C CB . PHE A 326 ? 0.3245 0.3497 0.5281 0.0066 -0.0102 -0.0637 351 PHE A CB 2584 C CG . PHE A 326 ? 0.3190 0.3384 0.5142 0.0059 -0.0148 -0.0546 351 PHE A CG 2585 C CD1 . PHE A 326 ? 0.3903 0.4079 0.5721 0.0036 -0.0142 -0.0516 351 PHE A CD1 2586 C CD2 . PHE A 326 ? 0.2670 0.2835 0.4678 0.0071 -0.0198 -0.0492 351 PHE A CD2 2587 C CE1 . PHE A 326 ? 0.3283 0.3411 0.5025 0.0027 -0.0176 -0.0442 351 PHE A CE1 2588 C CE2 . PHE A 326 ? 0.2517 0.2634 0.4436 0.0056 -0.0236 -0.0415 351 PHE A CE2 2589 C CZ . PHE A 326 ? 0.2722 0.2820 0.4507 0.0034 -0.0222 -0.0393 351 PHE A CZ 2590 N N . ASP A 327 ? 0.4022 0.4211 0.6104 0.0052 -0.0076 -0.0730 352 ASP A N 2591 C CA . ASP A 327 ? 0.3738 0.3882 0.5781 0.0034 -0.0081 -0.0732 352 ASP A CA 2592 C C . ASP A 327 ? 0.4116 0.4317 0.6143 0.0010 -0.0027 -0.0825 352 ASP A C 2593 O O . ASP A 327 ? 0.5608 0.5875 0.7522 -0.0015 0.0001 -0.0832 352 ASP A O 2594 C CB . ASP A 327 ? 0.3525 0.3654 0.5422 0.0014 -0.0102 -0.0653 352 ASP A CB 2595 C CG . ASP A 327 ? 0.4023 0.4104 0.5893 -0.0004 -0.0114 -0.0643 352 ASP A CG 2596 O OD1 . ASP A 327 ? 0.4492 0.4564 0.6428 -0.0010 -0.0098 -0.0709 352 ASP A OD1 2597 O OD2 . ASP A 327 ? 0.4023 0.4075 0.5807 -0.0016 -0.0137 -0.0574 352 ASP A OD2 2598 N N . GLU A 328 ? 0.3434 0.3609 0.5575 0.0016 -0.0014 -0.0896 353 GLU A N 2599 C CA . GLU A 328 ? 0.3677 0.3910 0.5814 -0.0011 0.0042 -0.1001 353 GLU A CA 2600 C C . GLU A 328 ? 0.3021 0.3253 0.5061 -0.0052 0.0048 -0.1014 353 GLU A C 2601 O O . GLU A 328 ? 0.3861 0.4116 0.5922 -0.0077 0.0085 -0.1105 353 GLU A O 2602 C CB . GLU A 328 ? 0.5620 0.5831 0.7937 0.0012 0.0065 -0.1089 353 GLU A CB 2603 C CG . GLU A 328 ? 0.7587 0.7835 1.0014 0.0047 0.0077 -0.1105 353 GLU A CG 2604 C CD . GLU A 328 ? 0.9264 0.9565 1.1798 0.0045 0.0142 -0.1233 353 GLU A CD 2605 O OE1 . GLU A 328 ? 0.9737 0.9986 1.2447 0.0075 0.0143 -0.1280 353 GLU A OE1 2606 O OE2 . GLU A 328 ? 0.9623 1.0016 1.2066 0.0010 0.0194 -0.1286 353 GLU A OE2 2607 N N . ARG A 329 ? 0.2539 0.2748 0.4472 -0.0063 0.0013 -0.0927 354 ARG A N 2608 C CA . ARG A 329 ? 0.2373 0.2582 0.4226 -0.0101 0.0012 -0.0929 354 ARG A CA 2609 C C . ARG A 329 ? 0.2123 0.2424 0.3833 -0.0136 0.0033 -0.0919 354 ARG A C 2610 O O . ARG A 329 ? 0.2480 0.2815 0.4126 -0.0127 0.0031 -0.0865 354 ARG A O 2611 C CB . ARG A 329 ? 0.2716 0.2846 0.4556 -0.0093 -0.0037 -0.0841 354 ARG A CB 2612 C CG . ARG A 329 ? 0.3899 0.3934 0.5875 -0.0071 -0.0064 -0.0846 354 ARG A CG 2613 C CD . ARG A 329 ? 0.5077 0.5052 0.7062 -0.0046 -0.0113 -0.0745 354 ARG A CD 2614 N NE . ARG A 329 ? 0.4570 0.4520 0.6464 -0.0068 -0.0139 -0.0674 354 ARG A NE 2615 C CZ . ARG A 329 ? 0.5660 0.5594 0.7490 -0.0061 -0.0166 -0.0586 354 ARG A CZ 2616 N NH1 . ARG A 329 ? 0.6834 0.6750 0.8589 -0.0083 -0.0181 -0.0531 354 ARG A NH1 2617 N NH2 . ARG A 329 ? 0.6592 0.6533 0.8433 -0.0037 -0.0176 -0.0557 354 ARG A NH2 2618 N N . ALA A 330 ? 0.2242 0.2581 0.3905 -0.0179 0.0051 -0.0969 355 ALA A N 2619 C CA . ALA A 330 ? 0.2195 0.2615 0.3725 -0.0217 0.0057 -0.0940 355 ALA A CA 2620 C C . ALA A 330 ? 0.2227 0.2610 0.3705 -0.0206 0.0017 -0.0835 355 ALA A C 2621 O O . ALA A 330 ? 0.2400 0.2705 0.3925 -0.0192 -0.0011 -0.0808 355 ALA A O 2622 C CB . ALA A 330 ? 0.2253 0.2717 0.3750 -0.0271 0.0075 -0.1010 355 ALA A CB 2623 N N . PHE A 331 ? 0.1828 0.2267 0.3213 -0.0213 0.0015 -0.0775 356 PHE A N 2624 C CA . PHE A 331 ? 0.1846 0.2254 0.3189 -0.0202 -0.0014 -0.0683 356 PHE A CA 2625 C C . PHE A 331 ? 0.2557 0.3041 0.3804 -0.0224 -0.0013 -0.0635 356 PHE A C 2626 O O . PHE A 331 ? 0.2313 0.2872 0.3517 -0.0243 0.0008 -0.0654 356 PHE A O 2627 C CB . PHE A 331 ? 0.1936 0.2282 0.3308 -0.0159 -0.0029 -0.0632 356 PHE A CB 2628 C CG . PHE A 331 ? 0.1879 0.2268 0.3223 -0.0147 -0.0012 -0.0621 356 PHE A CG 2629 C CD1 . PHE A 331 ? 0.2207 0.2617 0.3479 -0.0145 -0.0014 -0.0553 356 PHE A CD1 2630 C CD2 . PHE A 331 ? 0.2232 0.2639 0.3629 -0.0139 0.0010 -0.0680 356 PHE A CD2 2631 C CE1 . PHE A 331 ? 0.2191 0.2634 0.3439 -0.0137 0.0001 -0.0542 356 PHE A CE1 2632 C CE2 . PHE A 331 ? 0.2323 0.2772 0.3695 -0.0132 0.0026 -0.0669 356 PHE A CE2 2633 C CZ . PHE A 331 ? 0.2339 0.2803 0.3634 -0.0133 0.0020 -0.0599 356 PHE A CZ 2634 N N . LYS A 332 ? 0.2119 0.2585 0.3341 -0.0222 -0.0034 -0.0568 357 LYS A N 2635 C CA . LYS A 332 ? 0.2053 0.2576 0.3209 -0.0229 -0.0037 -0.0504 357 LYS A CA 2636 C C . LYS A 332 ? 0.1897 0.2359 0.3058 -0.0196 -0.0048 -0.0434 357 LYS A C 2637 O O . LYS A 332 ? 0.2035 0.2429 0.3233 -0.0185 -0.0062 -0.0429 357 LYS A O 2638 C CB . LYS A 332 ? 0.2199 0.2784 0.3324 -0.0270 -0.0047 -0.0498 357 LYS A CB 2639 C CG . LYS A 332 ? 0.3676 0.4337 0.4747 -0.0280 -0.0051 -0.0434 357 LYS A CG 2640 C CD . LYS A 332 ? 0.5742 0.6500 0.6772 -0.0333 -0.0057 -0.0454 357 LYS A CD 2641 C CE . LYS A 332 ? 0.6237 0.7069 0.7230 -0.0342 -0.0071 -0.0373 357 LYS A CE 2642 N NZ . LYS A 332 ? 0.6005 0.6811 0.7031 -0.0321 -0.0088 -0.0310 357 LYS A NZ 2643 N N . THR A 333 ? 0.1978 0.2464 0.3102 -0.0184 -0.0042 -0.0382 358 THR A N 2644 C CA . THR A 333 ? 0.1940 0.2371 0.3064 -0.0156 -0.0045 -0.0327 358 THR A CA 2645 C C . THR A 333 ? 0.1980 0.2455 0.3073 -0.0155 -0.0040 -0.0267 358 THR A C 2646 O O . THR A 333 ? 0.2442 0.2986 0.3510 -0.0170 -0.0036 -0.0261 358 THR A O 2647 C CB . THR A 333 ? 0.2221 0.2602 0.3357 -0.0130 -0.0039 -0.0335 358 THR A CB 2648 O OG1 . THR A 333 ? 0.2154 0.2488 0.3275 -0.0111 -0.0040 -0.0284 358 THR A OG1 2649 C CG2 . THR A 333 ? 0.2482 0.2916 0.3598 -0.0134 -0.0022 -0.0350 358 THR A CG2 2650 N N . LYS A 334 ? 0.1826 0.2262 0.2923 -0.0139 -0.0040 -0.0222 359 LYS A N 2651 C CA . LYS A 334 ? 0.1989 0.2453 0.3078 -0.0129 -0.0030 -0.0166 359 LYS A CA 2652 C C . LYS A 334 ? 0.1885 0.2279 0.2972 -0.0104 -0.0016 -0.0143 359 LYS A C 2653 O O . LYS A 334 ? 0.2139 0.2472 0.3227 -0.0100 -0.0021 -0.0162 359 LYS A O 2654 C CB . LYS A 334 ? 0.2027 0.2535 0.3134 -0.0143 -0.0038 -0.0137 359 LYS A CB 2655 C CG . LYS A 334 ? 0.2301 0.2895 0.3401 -0.0175 -0.0054 -0.0149 359 LYS A CG 2656 C CD . LYS A 334 ? 0.3312 0.3963 0.4436 -0.0188 -0.0065 -0.0106 359 LYS A CD 2657 C CE . LYS A 334 ? 0.5059 0.5806 0.6170 -0.0210 -0.0079 -0.0078 359 LYS A CE 2658 N NZ . LYS A 334 ? 0.4361 0.5137 0.5429 -0.0240 -0.0083 -0.0133 359 LYS A NZ 2659 N N . VAL A 335 ? 0.1717 0.2118 0.2801 -0.0089 0.0001 -0.0104 360 VAL A N 2660 C CA . VAL A 335 ? 0.1733 0.2070 0.2810 -0.0071 0.0020 -0.0091 360 VAL A CA 2661 C C . VAL A 335 ? 0.1665 0.2012 0.2765 -0.0058 0.0041 -0.0048 360 VAL A C 2662 O O . VAL A 335 ? 0.1928 0.2335 0.3055 -0.0057 0.0039 -0.0018 360 VAL A O 2663 C CB . VAL A 335 ? 0.1749 0.2062 0.2805 -0.0063 0.0027 -0.0103 360 VAL A CB 2664 C CG1 . VAL A 335 ? 0.1998 0.2359 0.3060 -0.0060 0.0036 -0.0073 360 VAL A CG1 2665 C CG2 . VAL A 335 ? 0.1883 0.2125 0.2922 -0.0053 0.0043 -0.0100 360 VAL A CG2 2666 N N . ASP A 336 ? 0.1411 0.1704 0.2505 -0.0051 0.0061 -0.0045 361 ASP A N 2667 C CA . ASP A 336 ? 0.1569 0.1860 0.2692 -0.0035 0.0093 -0.0015 361 ASP A CA 2668 C C . ASP A 336 ? 0.1769 0.1993 0.2865 -0.0027 0.0120 -0.0027 361 ASP A C 2669 O O . ASP A 336 ? 0.1757 0.1933 0.2807 -0.0038 0.0112 -0.0053 361 ASP A O 2670 C CB . ASP A 336 ? 0.1657 0.1959 0.2803 -0.0042 0.0102 -0.0006 361 ASP A CB 2671 C CG . ASP A 336 ? 0.1622 0.2003 0.2817 -0.0046 0.0086 0.0019 361 ASP A CG 2672 O OD1 . ASP A 336 ? 0.1800 0.2228 0.3034 -0.0034 0.0085 0.0049 361 ASP A OD1 2673 O OD2 . ASP A 336 ? 0.1734 0.2132 0.2933 -0.0065 0.0071 0.0013 361 ASP A OD2 2674 N N . LEU A 337 ? 0.1633 0.1854 0.2764 -0.0009 0.0151 -0.0006 362 LEU A N 2675 C CA . LEU A 337 ? 0.1772 0.1928 0.2885 -0.0005 0.0187 -0.0021 362 LEU A CA 2676 C C . LEU A 337 ? 0.2169 0.2328 0.3322 0.0003 0.0226 -0.0013 362 LEU A C 2677 O O . LEU A 337 ? 0.2025 0.2239 0.3246 0.0016 0.0226 0.0017 362 LEU A O 2678 C CB . LEU A 337 ? 0.1919 0.2062 0.3053 0.0010 0.0199 -0.0009 362 LEU A CB 2679 C CG . LEU A 337 ? 0.3008 0.3149 0.4105 0.0001 0.0172 -0.0018 362 LEU A CG 2680 C CD1 . LEU A 337 ? 0.3417 0.3513 0.4450 -0.0018 0.0160 -0.0057 362 LEU A CD1 2681 C CD2 . LEU A 337 ? 0.2619 0.2831 0.3729 -0.0003 0.0137 -0.0001 362 LEU A CD2 2682 N N . THR A 338 ? 0.1791 0.1896 0.2906 -0.0009 0.0258 -0.0041 363 THR A N 2683 C CA . THR A 338 ? 0.1776 0.1886 0.2925 -0.0007 0.0303 -0.0043 363 THR A CA 2684 C C . THR A 338 ? 0.2070 0.2131 0.3235 0.0002 0.0358 -0.0065 363 THR A C 2685 O O . THR A 338 ? 0.1972 0.1981 0.3090 -0.0004 0.0360 -0.0086 363 THR A O 2686 C CB . THR A 338 ? 0.1882 0.1980 0.2969 -0.0040 0.0301 -0.0061 363 THR A CB 2687 O OG1 . THR A 338 ? 0.2201 0.2237 0.3202 -0.0064 0.0304 -0.0091 363 THR A OG1 2688 C CG2 . THR A 338 ? 0.2268 0.2402 0.3346 -0.0051 0.0248 -0.0045 363 THR A CG2 2689 N N . LYS A 339 ? 0.2112 0.2191 0.3347 0.0017 0.0405 -0.0063 364 LYS A N 2690 C CA . LYS A 339 ? 0.2287 0.2318 0.3554 0.0027 0.0468 -0.0092 364 LYS A CA 2691 C C . LYS A 339 ? 0.2337 0.2364 0.3587 0.0006 0.0523 -0.0127 364 LYS A C 2692 O O . LYS A 339 ? 0.2762 0.2738 0.3991 -0.0005 0.0577 -0.0172 364 LYS A O 2693 C CB . LYS A 339 ? 0.2968 0.3025 0.4368 0.0071 0.0484 -0.0056 364 LYS A CB 2694 C CG . LYS A 339 ? 0.3819 0.3884 0.5227 0.0085 0.0432 -0.0018 364 LYS A CG 2695 C CD . LYS A 339 ? 0.5638 0.5727 0.7177 0.0124 0.0441 0.0029 364 LYS A CD 2696 C CE . LYS A 339 ? 0.6424 0.6436 0.8000 0.0138 0.0490 0.0005 364 LYS A CE 2697 N NZ . LYS A 339 ? 0.6590 0.6618 0.8297 0.0176 0.0487 0.0063 364 LYS A NZ 2698 N N . GLU A 340 ? 0.2061 0.2144 0.3317 -0.0005 0.0510 -0.0110 365 GLU A N 2699 C CA A GLU A 340 ? 0.2416 0.2506 0.3648 -0.0033 0.0558 -0.0138 365 GLU A CA 2700 C CA B GLU A 340 ? 0.2446 0.2536 0.3679 -0.0033 0.0558 -0.0138 365 GLU A CA 2701 C C . GLU A 340 ? 0.2533 0.2621 0.3652 -0.0079 0.0516 -0.0136 365 GLU A C 2702 O O . GLU A 340 ? 0.2318 0.2424 0.3424 -0.0077 0.0452 -0.0106 365 GLU A O 2703 C CB A GLU A 340 ? 0.2811 0.2974 0.4167 -0.0008 0.0584 -0.0114 365 GLU A CB 2704 C CB B GLU A 340 ? 0.2793 0.2957 0.4150 -0.0008 0.0584 -0.0114 365 GLU A CB 2705 C CG A GLU A 340 ? 0.3286 0.3459 0.4781 0.0042 0.0620 -0.0104 365 GLU A CG 2706 C CG B GLU A 340 ? 0.3225 0.3395 0.4718 0.0039 0.0629 -0.0111 365 GLU A CG 2707 C CD A GLU A 340 ? 0.4337 0.4451 0.5841 0.0042 0.0700 -0.0161 365 GLU A CD 2708 C CD B GLU A 340 ? 0.4001 0.4258 0.5635 0.0067 0.0638 -0.0073 365 GLU A CD 2709 O OE1 A GLU A 340 ? 0.4350 0.4454 0.5791 0.0005 0.0747 -0.0207 365 GLU A OE1 2710 O OE1 B GLU A 340 ? 0.4861 0.5177 0.6493 0.0058 0.0585 -0.0034 365 GLU A OE1 2711 O OE2 A GLU A 340 ? 0.5037 0.5115 0.6610 0.0075 0.0716 -0.0162 365 GLU A OE2 2712 O OE2 B GLU A 340 ? 0.5631 0.5898 0.7384 0.0097 0.0698 -0.0083 365 GLU A OE2 2713 N N . PRO A 341 ? 0.2113 0.2178 0.3152 -0.0122 0.0551 -0.0169 366 PRO A N 2714 C CA . PRO A 341 ? 0.1973 0.2036 0.2914 -0.0167 0.0507 -0.0156 366 PRO A CA 2715 C C . PRO A 341 ? 0.1922 0.2045 0.2918 -0.0162 0.0472 -0.0115 366 PRO A C 2716 O O . PRO A 341 ? 0.2483 0.2660 0.3575 -0.0140 0.0503 -0.0105 366 PRO A O 2717 C CB . PRO A 341 ? 0.2612 0.2664 0.3483 -0.0215 0.0567 -0.0191 366 PRO A CB 2718 C CG . PRO A 341 ? 0.2808 0.2824 0.3699 -0.0200 0.0630 -0.0239 366 PRO A CG 2719 C CD . PRO A 341 ? 0.2907 0.2948 0.3940 -0.0136 0.0633 -0.0219 366 PRO A CD 2720 N N . LEU A 342 ? 0.2036 0.2150 0.2979 -0.0181 0.0407 -0.0092 367 LEU A N 2721 C CA . LEU A 342 ? 0.2271 0.2433 0.3256 -0.0184 0.0372 -0.0059 367 LEU A CA 2722 C C . LEU A 342 ? 0.2469 0.2646 0.3419 -0.0230 0.0399 -0.0057 367 LEU A C 2723 O O . LEU A 342 ? 0.2269 0.2407 0.3122 -0.0272 0.0403 -0.0066 367 LEU A O 2724 C CB . LEU A 342 ? 0.1945 0.2084 0.2897 -0.0189 0.0298 -0.0043 367 LEU A CB 2725 C CG . LEU A 342 ? 0.2339 0.2469 0.3316 -0.0151 0.0269 -0.0046 367 LEU A CG 2726 C CD1 . LEU A 342 ? 0.2568 0.2677 0.3516 -0.0160 0.0205 -0.0038 367 LEU A CD1 2727 C CD2 . LEU A 342 ? 0.3353 0.3544 0.4431 -0.0115 0.0278 -0.0030 367 LEU A CD2 2728 N N . PRO A 343 ? 0.2095 0.2337 0.3125 -0.0226 0.0417 -0.0040 368 PRO A N 2729 C CA . PRO A 343 ? 0.2118 0.2379 0.3113 -0.0274 0.0443 -0.0036 368 PRO A CA 2730 C C . PRO A 343 ? 0.1754 0.1988 0.2687 -0.0311 0.0377 -0.0006 368 PRO A C 2731 O O . PRO A 343 ? 0.1999 0.2219 0.2950 -0.0292 0.0317 0.0008 368 PRO A O 2732 C CB . PRO A 343 ? 0.2019 0.2362 0.3136 -0.0254 0.0472 -0.0023 368 PRO A CB 2733 C CG . PRO A 343 ? 0.1863 0.2226 0.3051 -0.0210 0.0420 -0.0003 368 PRO A CG 2734 C CD . PRO A 343 ? 0.2385 0.2690 0.3536 -0.0183 0.0414 -0.0023 368 PRO A CD 2735 N N . SER A 344 ? 0.2080 0.2306 0.2943 -0.0367 0.0389 0.0003 369 SER A N 2736 C CA . SER A 344 ? 0.1970 0.2164 0.2780 -0.0406 0.0328 0.0037 369 SER A CA 2737 C C . SER A 344 ? 0.1892 0.2114 0.2786 -0.0390 0.0282 0.0061 369 SER A C 2738 O O . SER A 344 ? 0.2238 0.2421 0.3123 -0.0391 0.0219 0.0077 369 SER A O 2739 C CB . SER A 344 ? 0.2866 0.3067 0.3604 -0.0472 0.0357 0.0051 369 SER A CB 2740 O OG . SER A 344 ? 0.3265 0.3436 0.3967 -0.0512 0.0296 0.0094 369 SER A OG 2741 N N . LYS A 345 ? 0.1958 0.2251 0.2939 -0.0376 0.0315 0.0061 370 LYS A N 2742 C CA . LYS A 345 ? 0.1828 0.2158 0.2885 -0.0371 0.0275 0.0081 370 LYS A CA 2743 C C . LYS A 345 ? 0.1741 0.2057 0.2831 -0.0328 0.0227 0.0073 370 LYS A C 2744 O O . LYS A 345 ? 0.1972 0.2294 0.3094 -0.0333 0.0180 0.0083 370 LYS A O 2745 C CB . LYS A 345 ? 0.1912 0.2333 0.3064 -0.0364 0.0321 0.0085 370 LYS A CB 2746 C CG . LYS A 345 ? 0.1602 0.2064 0.2830 -0.0309 0.0353 0.0068 370 LYS A CG 2747 C CD . LYS A 345 ? 0.1807 0.2363 0.3143 -0.0303 0.0399 0.0076 370 LYS A CD 2748 C CE . LYS A 345 ? 0.2310 0.2902 0.3734 -0.0245 0.0428 0.0066 370 LYS A CE 2749 N NZ . LYS A 345 ? 0.2900 0.3591 0.4452 -0.0235 0.0471 0.0079 370 LYS A NZ 2750 N N . ALA A 346 ? 0.1934 0.2234 0.3016 -0.0290 0.0241 0.0052 371 ALA A N 2751 C CA . ALA A 346 ? 0.2020 0.2309 0.3122 -0.0255 0.0199 0.0044 371 ALA A CA 2752 C C . ALA A 346 ? 0.2036 0.2258 0.3081 -0.0271 0.0145 0.0043 371 ALA A C 2753 O O . ALA A 346 ? 0.2042 0.2265 0.3116 -0.0264 0.0101 0.0041 371 ALA A O 2754 C CB . ALA A 346 ? 0.1845 0.2130 0.2952 -0.0215 0.0228 0.0026 371 ALA A CB 2755 N N . PHE A 347 ? 0.1896 0.2062 0.2863 -0.0294 0.0148 0.0045 372 PHE A N 2756 C CA . PHE A 347 ? 0.2010 0.2114 0.2937 -0.0311 0.0094 0.0053 372 PHE A CA 2757 C C . PHE A 347 ? 0.1916 0.2015 0.2867 -0.0344 0.0061 0.0077 372 PHE A C 2758 O O . PHE A 347 ? 0.2034 0.2099 0.3006 -0.0342 0.0011 0.0077 372 PHE A O 2759 C CB . PHE A 347 ? 0.2014 0.2070 0.2854 -0.0336 0.0100 0.0058 372 PHE A CB 2760 C CG . PHE A 347 ? 0.2321 0.2361 0.3136 -0.0306 0.0114 0.0032 372 PHE A CG 2761 C CD1 . PHE A 347 ? 0.1903 0.1928 0.2746 -0.0273 0.0078 0.0018 372 PHE A CD1 2762 C CD2 . PHE A 347 ? 0.2270 0.2311 0.3037 -0.0314 0.0166 0.0016 372 PHE A CD2 2763 C CE1 . PHE A 347 ? 0.2143 0.2155 0.2966 -0.0249 0.0090 -0.0004 372 PHE A CE1 2764 C CE2 . PHE A 347 ? 0.2452 0.2473 0.3200 -0.0291 0.0179 -0.0009 372 PHE A CE2 2765 C CZ . PHE A 347 ? 0.2425 0.2432 0.3201 -0.0258 0.0139 -0.0016 372 PHE A CZ 2766 N N . TYR A 348 ? 0.2086 0.2218 0.3038 -0.0377 0.0090 0.0096 373 TYR A N 2767 C CA . TYR A 348 ? 0.2041 0.2168 0.3018 -0.0413 0.0061 0.0121 373 TYR A CA 2768 C C . TYR A 348 ? 0.1838 0.1991 0.2895 -0.0392 0.0032 0.0106 373 TYR A C 2769 O O . TYR A 348 ? 0.2124 0.2237 0.3202 -0.0405 -0.0014 0.0108 373 TYR A O 2770 C CB . TYR A 348 ? 0.1802 0.1975 0.2774 -0.0452 0.0105 0.0142 373 TYR A CB 2771 C CG . TYR A 348 ? 0.2136 0.2289 0.3110 -0.0505 0.0076 0.0177 373 TYR A CG 2772 C CD1 . TYR A 348 ? 0.2231 0.2332 0.3130 -0.0551 0.0061 0.0212 373 TYR A CD1 2773 C CD2 . TYR A 348 ? 0.2505 0.2691 0.3554 -0.0512 0.0060 0.0180 373 TYR A CD2 2774 C CE1 . TYR A 348 ? 0.2632 0.2711 0.3537 -0.0602 0.0032 0.0253 373 TYR A CE1 2775 C CE2 . TYR A 348 ? 0.2405 0.2567 0.3461 -0.0563 0.0034 0.0214 373 TYR A CE2 2776 C CZ . TYR A 348 ? 0.2507 0.2612 0.3493 -0.0606 0.0020 0.0252 373 TYR A CZ 2777 O OH . TYR A 348 ? 0.2938 0.3014 0.3934 -0.0659 -0.0009 0.0292 373 TYR A OH 2778 N N . GLY A 349 ? 0.1932 0.2153 0.3036 -0.0363 0.0059 0.0089 374 GLY A N 2779 C CA . GLY A 349 ? 0.1853 0.2115 0.3023 -0.0351 0.0033 0.0074 374 GLY A CA 2780 C C . GLY A 349 ? 0.1927 0.2149 0.3093 -0.0325 -0.0004 0.0046 374 GLY A C 2781 O O . GLY A 349 ? 0.1950 0.2171 0.3150 -0.0332 -0.0037 0.0029 374 GLY A O 2782 N N . LEU A 350 ? 0.1888 0.2079 0.3012 -0.0298 0.0004 0.0037 375 LEU A N 2783 C CA . LEU A 350 ? 0.1813 0.1971 0.2936 -0.0275 -0.0027 0.0010 375 LEU A CA 2784 C C . LEU A 350 ? 0.2109 0.2197 0.3232 -0.0297 -0.0068 0.0011 375 LEU A C 2785 O O . LEU A 350 ? 0.2059 0.2134 0.3219 -0.0291 -0.0097 -0.0016 375 LEU A O 2786 C CB . LEU A 350 ? 0.2067 0.2204 0.3146 -0.0248 -0.0008 0.0003 375 LEU A CB 2787 C CG . LEU A 350 ? 0.2653 0.2774 0.3733 -0.0220 -0.0029 -0.0025 375 LEU A CG 2788 C CD1 . LEU A 350 ? 0.2407 0.2584 0.3531 -0.0207 -0.0035 -0.0047 375 LEU A CD1 2789 C CD2 . LEU A 350 ? 0.2489 0.2600 0.3528 -0.0199 -0.0001 -0.0025 375 LEU A CD2 2790 N N . LEU A 351 ? 0.2013 0.2057 0.3099 -0.0324 -0.0070 0.0043 376 LEU A N 2791 C CA . LEU A 351 ? 0.2224 0.2200 0.3320 -0.0346 -0.0114 0.0059 376 LEU A CA 2792 C C . LEU A 351 ? 0.2125 0.2101 0.3280 -0.0371 -0.0133 0.0058 376 LEU A C 2793 O O . LEU A 351 ? 0.2241 0.2166 0.3439 -0.0373 -0.0171 0.0046 376 LEU A O 2794 C CB . LEU A 351 ? 0.2068 0.2006 0.3101 -0.0377 -0.0114 0.0104 376 LEU A CB 2795 C CG . LEU A 351 ? 0.2175 0.2096 0.3149 -0.0360 -0.0106 0.0102 376 LEU A CG 2796 C CD1 . LEU A 351 ? 0.2250 0.2152 0.3145 -0.0403 -0.0097 0.0143 376 LEU A CD1 2797 C CD2 . LEU A 351 ? 0.2588 0.2462 0.3593 -0.0337 -0.0152 0.0089 376 LEU A CD2 2798 N N . GLU A 352 ? 0.2047 0.2081 0.3211 -0.0391 -0.0107 0.0067 377 GLU A N 2799 C CA . GLU A 352 ? 0.1909 0.1953 0.3129 -0.0420 -0.0125 0.0062 377 GLU A CA 2800 C C . GLU A 352 ? 0.2344 0.2399 0.3610 -0.0398 -0.0143 0.0010 377 GLU A C 2801 O O . GLU A 352 ? 0.2418 0.2433 0.3730 -0.0415 -0.0173 -0.0009 377 GLU A O 2802 C CB . GLU A 352 ? 0.2146 0.2267 0.3376 -0.0441 -0.0092 0.0080 377 GLU A CB 2803 C CG . GLU A 352 ? 0.2594 0.2708 0.3788 -0.0479 -0.0072 0.0126 377 GLU A CG 2804 C CD . GLU A 352 ? 0.3563 0.3768 0.4785 -0.0496 -0.0033 0.0137 377 GLU A CD 2805 O OE1 . GLU A 352 ? 0.3515 0.3785 0.4746 -0.0463 0.0000 0.0123 377 GLU A OE1 2806 O OE2 . GLU A 352 ? 0.3522 0.3733 0.4764 -0.0541 -0.0036 0.0161 377 GLU A OE2 2807 N N . ARG A 353 ? 0.2137 0.2248 0.3392 -0.0365 -0.0124 -0.0014 378 ARG A N 2808 C CA . ARG A 353 ? 0.2047 0.2185 0.3333 -0.0350 -0.0136 -0.0063 378 ARG A CA 2809 C C . ARG A 353 ? 0.2359 0.2424 0.3657 -0.0334 -0.0161 -0.0095 378 ARG A C 2810 O O . ARG A 353 ? 0.2145 0.2198 0.3485 -0.0342 -0.0178 -0.0139 378 ARG A O 2811 C CB . ARG A 353 ? 0.1866 0.2083 0.3134 -0.0323 -0.0111 -0.0068 378 ARG A CB 2812 C CG . ARG A 353 ? 0.1887 0.2188 0.3177 -0.0339 -0.0093 -0.0043 378 ARG A CG 2813 C CD . ARG A 353 ? 0.2089 0.2458 0.3373 -0.0308 -0.0065 -0.0029 378 ARG A CD 2814 N NE . ARG A 353 ? 0.2273 0.2730 0.3600 -0.0323 -0.0055 -0.0004 378 ARG A NE 2815 C CZ . ARG A 353 ? 0.3712 0.4185 0.5057 -0.0338 -0.0032 0.0028 378 ARG A CZ 2816 N NH1 . ARG A 353 ? 0.3091 0.3498 0.4400 -0.0345 -0.0017 0.0041 378 ARG A NH1 2817 N NH2 . ARG A 353 ? 0.3680 0.4243 0.5080 -0.0349 -0.0024 0.0049 378 ARG A NH2 2818 N N . LEU A 354 ? 0.2123 0.2143 0.3390 -0.0314 -0.0161 -0.0075 379 LEU A N 2819 C CA . LEU A 354 ? 0.1900 0.1852 0.3193 -0.0298 -0.0188 -0.0095 379 LEU A CA 2820 C C . LEU A 354 ? 0.2449 0.2332 0.3798 -0.0324 -0.0220 -0.0089 379 LEU A C 2821 O O . LEU A 354 ? 0.2248 0.2092 0.3657 -0.0315 -0.0240 -0.0129 379 LEU A O 2822 C CB . LEU A 354 ? 0.1900 0.1822 0.3148 -0.0279 -0.0187 -0.0065 379 LEU A CB 2823 C CG . LEU A 354 ? 0.2168 0.2138 0.3378 -0.0248 -0.0160 -0.0083 379 LEU A CG 2824 C CD1 . LEU A 354 ? 0.2137 0.2085 0.3289 -0.0243 -0.0153 -0.0047 379 LEU A CD1 2825 C CD2 . LEU A 354 ? 0.2196 0.2170 0.3443 -0.0222 -0.0168 -0.0134 379 LEU A CD2 2826 N N . SER A 355 ? 0.2313 0.2182 0.3649 -0.0359 -0.0224 -0.0041 380 SER A N 2827 C CA . SER A 355 ? 0.2352 0.2148 0.3742 -0.0388 -0.0257 -0.0023 380 SER A CA 2828 C C . SER A 355 ? 0.2282 0.2083 0.3738 -0.0403 -0.0262 -0.0077 380 SER A C 2829 O O . SER A 355 ? 0.2752 0.2481 0.4275 -0.0417 -0.0290 -0.0086 380 SER A O 2830 C CB . SER A 355 ? 0.2698 0.2487 0.4050 -0.0429 -0.0256 0.0043 380 SER A CB 2831 O OG . SER A 355 ? 0.3015 0.2868 0.4366 -0.0455 -0.0232 0.0039 380 SER A OG 2832 N N . LYS A 356 ? 0.2210 0.2095 0.3648 -0.0402 -0.0237 -0.0112 381 LYS A N 2833 C CA . LYS A 356 ? 0.2595 0.2500 0.4079 -0.0424 -0.0240 -0.0166 381 LYS A CA 2834 C C . LYS A 356 ? 0.2527 0.2436 0.4036 -0.0399 -0.0238 -0.0240 381 LYS A C 2835 O O . LYS A 356 ? 0.2802 0.2718 0.4350 -0.0420 -0.0240 -0.0298 381 LYS A O 2836 C CB . LYS A 356 ? 0.2461 0.2466 0.3915 -0.0446 -0.0220 -0.0158 381 LYS A CB 2837 C CG . LYS A 356 ? 0.2725 0.2734 0.4172 -0.0480 -0.0217 -0.0098 381 LYS A CG 2838 C CD . LYS A 356 ? 0.4023 0.4142 0.5455 -0.0493 -0.0195 -0.0086 381 LYS A CD 2839 C CE . LYS A 356 ? 0.5775 0.5905 0.7208 -0.0529 -0.0186 -0.0030 381 LYS A CE 2840 N NZ . LYS A 356 ? 0.6936 0.7179 0.8375 -0.0538 -0.0164 -0.0017 381 LYS A NZ 2841 N N . GLU A 357 ? 0.2448 0.2357 0.3933 -0.0358 -0.0231 -0.0240 382 GLU A N 2842 C CA . GLU A 357 ? 0.2331 0.2252 0.3837 -0.0334 -0.0223 -0.0308 382 GLU A CA 2843 C C . GLU A 357 ? 0.2289 0.2153 0.3816 -0.0296 -0.0233 -0.0300 382 GLU A C 2844 O O . GLU A 357 ? 0.2368 0.2263 0.3846 -0.0269 -0.0221 -0.0283 382 GLU A O 2845 C CB . GLU A 357 ? 0.2423 0.2446 0.3869 -0.0327 -0.0198 -0.0324 382 GLU A CB 2846 C CG . GLU A 357 ? 0.2722 0.2770 0.4179 -0.0311 -0.0186 -0.0394 382 GLU A CG 2847 C CD . GLU A 357 ? 0.2510 0.2516 0.4038 -0.0331 -0.0192 -0.0465 382 GLU A CD 2848 O OE1 . GLU A 357 ? 0.2606 0.2536 0.4199 -0.0310 -0.0202 -0.0484 382 GLU A OE1 2849 O OE2 . GLU A 357 ? 0.3023 0.3072 0.4547 -0.0369 -0.0189 -0.0502 382 GLU A OE2 2850 N N . PRO A 358 ? 0.2470 0.2249 0.4079 -0.0295 -0.0258 -0.0310 383 PRO A N 2851 C CA . PRO A 358 ? 0.2378 0.2103 0.4025 -0.0261 -0.0276 -0.0292 383 PRO A CA 2852 C C . PRO A 358 ? 0.2664 0.2430 0.4316 -0.0226 -0.0256 -0.0347 383 PRO A C 2853 O O . PRO A 358 ? 0.2502 0.2244 0.4171 -0.0198 -0.0268 -0.0326 383 PRO A O 2854 C CB . PRO A 358 ? 0.2710 0.2343 0.4469 -0.0268 -0.0305 -0.0304 383 PRO A CB 2855 C CG . PRO A 358 ? 0.3329 0.2956 0.5083 -0.0313 -0.0307 -0.0296 383 PRO A CG 2856 C CD . PRO A 358 ? 0.2614 0.2340 0.4293 -0.0327 -0.0273 -0.0331 383 PRO A CD 2857 N N . ASN A 359 ? 0.2263 0.2094 0.3900 -0.0233 -0.0227 -0.0413 384 ASN A N 2858 C CA . ASN A 359 ? 0.2298 0.2178 0.3928 -0.0208 -0.0203 -0.0464 384 ASN A CA 2859 C C . ASN A 359 ? 0.2299 0.2244 0.3833 -0.0197 -0.0188 -0.0423 384 ASN A C 2860 O O . ASN A 359 ? 0.2171 0.2157 0.3691 -0.0177 -0.0170 -0.0450 384 ASN A O 2861 C CB . ASN A 359 ? 0.2233 0.2161 0.3879 -0.0228 -0.0178 -0.0553 384 ASN A CB 2862 C CG . ASN A 359 ? 0.3318 0.3181 0.5079 -0.0229 -0.0182 -0.0618 384 ASN A CG 2863 O OD1 . ASN A 359 ? 0.3499 0.3290 0.5315 -0.0243 -0.0205 -0.0601 384 ASN A OD1 2864 N ND2 . ASN A 359 ? 0.3460 0.3346 0.5263 -0.0215 -0.0156 -0.0696 384 ASN A ND2 2865 N N . GLY A 360 ? 0.2341 0.2295 0.3815 -0.0210 -0.0192 -0.0360 385 GLY A N 2866 C CA . GLY A 360 ? 0.2007 0.2011 0.3403 -0.0198 -0.0175 -0.0321 385 GLY A CA 2867 C C . GLY A 360 ? 0.2169 0.2125 0.3550 -0.0179 -0.0188 -0.0270 385 GLY A C 2868 O O . GLY A 360 ? 0.2381 0.2272 0.3795 -0.0186 -0.0215 -0.0240 385 GLY A O 2869 N N . PHE A 361 ? 0.2142 0.2131 0.3473 -0.0161 -0.0172 -0.0258 386 PHE A N 2870 C CA . PHE A 361 ? 0.2088 0.2042 0.3387 -0.0152 -0.0181 -0.0210 386 PHE A CA 2871 C C . PHE A 361 ? 0.2066 0.2064 0.3293 -0.0144 -0.0152 -0.0192 386 PHE A C 2872 O O . PHE A 361 ? 0.2156 0.2213 0.3370 -0.0140 -0.0130 -0.0214 386 PHE A O 2873 C CB . PHE A 361 ? 0.2467 0.2378 0.3821 -0.0133 -0.0206 -0.0220 386 PHE A CB 2874 C CG . PHE A 361 ? 0.2671 0.2622 0.4043 -0.0110 -0.0190 -0.0267 386 PHE A CG 2875 C CD1 . PHE A 361 ? 0.2923 0.2891 0.4250 -0.0097 -0.0180 -0.0251 386 PHE A CD1 2876 C CD2 . PHE A 361 ? 0.3158 0.3128 0.4593 -0.0105 -0.0182 -0.0331 386 PHE A CD2 2877 C CE1 . PHE A 361 ? 0.2900 0.2908 0.4246 -0.0080 -0.0165 -0.0291 386 PHE A CE1 2878 C CE2 . PHE A 361 ? 0.2998 0.3012 0.4449 -0.0088 -0.0162 -0.0375 386 PHE A CE2 2879 C CZ . PHE A 361 ? 0.3160 0.3193 0.4567 -0.0076 -0.0155 -0.0352 386 PHE A CZ 2880 N N . ILE A 362 ? 0.1960 0.1931 0.3142 -0.0147 -0.0154 -0.0150 387 ILE A N 2881 C CA . ILE A 362 ? 0.2086 0.2087 0.3210 -0.0139 -0.0124 -0.0137 387 ILE A CA 2882 C C . ILE A 362 ? 0.1881 0.1854 0.2983 -0.0129 -0.0132 -0.0130 387 ILE A C 2883 O O . ILE A 362 ? 0.2091 0.2021 0.3211 -0.0135 -0.0164 -0.0116 387 ILE A O 2884 C CB . ILE A 362 ? 0.1636 0.1642 0.2714 -0.0156 -0.0103 -0.0101 387 ILE A CB 2885 C CG1 . ILE A 362 ? 0.2152 0.2104 0.3210 -0.0181 -0.0124 -0.0065 387 ILE A CG1 2886 C CG2 . ILE A 362 ? 0.1955 0.2006 0.3058 -0.0164 -0.0092 -0.0106 387 ILE A CG2 2887 C CD1 . ILE A 362 ? 0.2474 0.2436 0.3487 -0.0204 -0.0097 -0.0035 387 ILE A CD1 2888 N N . ALA A 363 ? 0.2021 0.2023 0.3092 -0.0116 -0.0106 -0.0137 388 ALA A N 2889 C CA . ALA A 363 ? 0.1945 0.1925 0.2988 -0.0113 -0.0110 -0.0130 388 ALA A CA 2890 C C . ALA A 363 ? 0.2089 0.2073 0.3069 -0.0119 -0.0074 -0.0113 388 ALA A C 2891 O O . ALA A 363 ? 0.2146 0.2166 0.3126 -0.0108 -0.0044 -0.0119 388 ALA A O 2892 C CB . ALA A 363 ? 0.1975 0.1980 0.3052 -0.0093 -0.0110 -0.0163 388 ALA A CB 2893 N N . LEU A 364 ? 0.1645 0.1592 0.2575 -0.0139 -0.0078 -0.0092 389 LEU A N 2894 C CA . LEU A 364 ? 0.1836 0.1780 0.2707 -0.0149 -0.0038 -0.0084 389 LEU A CA 2895 C C . LEU A 364 ? 0.1869 0.1792 0.2698 -0.0156 -0.0034 -0.0090 389 LEU A C 2896 O O . LEU A 364 ? 0.1857 0.1755 0.2669 -0.0173 -0.0069 -0.0080 389 LEU A O 2897 C CB . LEU A 364 ? 0.1756 0.1681 0.2589 -0.0180 -0.0035 -0.0058 389 LEU A CB 2898 C CG . LEU A 364 ? 0.2083 0.2026 0.2956 -0.0182 -0.0040 -0.0048 389 LEU A CG 2899 C CD1 . LEU A 364 ? 0.2279 0.2200 0.3108 -0.0220 -0.0041 -0.0018 389 LEU A CD1 2900 C CD2 . LEU A 364 ? 0.2767 0.2757 0.3670 -0.0162 -0.0003 -0.0059 389 LEU A CD2 2901 N N . ASN A 365 ? 0.1907 0.1839 0.2724 -0.0144 0.0005 -0.0104 390 ASN A N 2902 C CA . ASN A 365 ? 0.1754 0.1664 0.2531 -0.0153 0.0015 -0.0115 390 ASN A CA 2903 C C . ASN A 365 ? 0.2016 0.1913 0.2757 -0.0160 0.0068 -0.0123 390 ASN A C 2904 O O . ASN A 365 ? 0.2128 0.2046 0.2903 -0.0139 0.0101 -0.0123 390 ASN A O 2905 C CB . ASN A 365 ? 0.1815 0.1747 0.2634 -0.0129 0.0011 -0.0131 390 ASN A CB 2906 C CG . ASN A 365 ? 0.2751 0.2687 0.3601 -0.0128 -0.0036 -0.0134 390 ASN A CG 2907 O OD1 . ASN A 365 ? 0.2667 0.2583 0.3493 -0.0147 -0.0060 -0.0130 390 ASN A OD1 2908 N ND2 . ASN A 365 ? 0.2499 0.2467 0.3409 -0.0108 -0.0050 -0.0142 390 ASN A ND2 2909 N N . GLY A 366 ? 0.2010 0.1874 0.2686 -0.0190 0.0077 -0.0131 391 GLY A N 2910 C CA . GLY A 366 ? 0.1942 0.1787 0.2587 -0.0199 0.0133 -0.0151 391 GLY A CA 2911 C C . GLY A 366 ? 0.1886 0.1718 0.2545 -0.0185 0.0149 -0.0171 391 GLY A C 2912 O O . GLY A 366 ? 0.2224 0.2055 0.2882 -0.0189 0.0113 -0.0172 391 GLY A O 2913 N N . PHE A 367 ? 0.1913 0.1736 0.2596 -0.0169 0.0201 -0.0184 392 PHE A N 2914 C CA . PHE A 367 ? 0.2090 0.1887 0.2782 -0.0164 0.0222 -0.0202 392 PHE A CA 2915 C C . PHE A 367 ? 0.2281 0.2032 0.2902 -0.0204 0.0257 -0.0236 392 PHE A C 2916 O O . PHE A 367 ? 0.2204 0.1948 0.2753 -0.0243 0.0236 -0.0239 392 PHE A O 2917 C CB . PHE A 367 ? 0.2040 0.1851 0.2811 -0.0124 0.0255 -0.0192 392 PHE A CB 2918 C CG . PHE A 367 ? 0.2075 0.1933 0.2900 -0.0097 0.0219 -0.0165 392 PHE A CG 2919 C CD1 . PHE A 367 ? 0.2365 0.2253 0.3181 -0.0101 0.0171 -0.0156 392 PHE A CD1 2920 C CD2 . PHE A 367 ? 0.2280 0.2153 0.3166 -0.0070 0.0236 -0.0148 392 PHE A CD2 2921 C CE1 . PHE A 367 ? 0.2264 0.2198 0.3126 -0.0081 0.0145 -0.0142 392 PHE A CE1 2922 C CE2 . PHE A 367 ? 0.2128 0.2052 0.3051 -0.0054 0.0205 -0.0125 392 PHE A CE2 2923 C CZ . PHE A 367 ? 0.2176 0.2132 0.3084 -0.0061 0.0163 -0.0127 392 PHE A CZ 2924 N N . GLY A 368 ? 0.2097 0.1815 0.2739 -0.0197 0.0310 -0.0261 393 GLY A N 2925 C CA . GLY A 368 ? 0.2236 0.1906 0.2808 -0.0239 0.0347 -0.0304 393 GLY A CA 2926 C C . GLY A 368 ? 0.2134 0.1785 0.2665 -0.0267 0.0314 -0.0315 393 GLY A C 2927 O O . GLY A 368 ? 0.2282 0.1953 0.2855 -0.0245 0.0275 -0.0292 393 GLY A O 2928 N N . GLY A 369 ? 0.2501 0.2117 0.2947 -0.0319 0.0330 -0.0353 394 GLY A N 2929 C CA . GLY A 369 ? 0.2330 0.1930 0.2738 -0.0351 0.0299 -0.0365 394 GLY A CA 2930 C C . GLY A 369 ? 0.2231 0.1808 0.2711 -0.0322 0.0319 -0.0371 394 GLY A C 2931 O O . GLY A 369 ? 0.2574 0.2117 0.3102 -0.0300 0.0376 -0.0389 394 GLY A O 2932 N N . GLN A 370 ? 0.2284 0.1882 0.2782 -0.0321 0.0270 -0.0352 395 GLN A N 2933 C CA A GLN A 370 ? 0.2371 0.1952 0.2931 -0.0301 0.0282 -0.0351 395 GLN A CA 2934 C CA B GLN A 370 ? 0.2403 0.1981 0.2962 -0.0301 0.0286 -0.0353 395 GLN A CA 2935 C C . GLN A 370 ? 0.2370 0.1968 0.3021 -0.0244 0.0301 -0.0319 395 GLN A C 2936 O O . GLN A 370 ? 0.2586 0.2159 0.3294 -0.0226 0.0329 -0.0317 395 GLN A O 2937 C CB A GLN A 370 ? 0.2242 0.1859 0.2804 -0.0314 0.0224 -0.0334 395 GLN A CB 2938 C CB B GLN A 370 ? 0.2697 0.2300 0.3253 -0.0320 0.0234 -0.0343 395 GLN A CB 2939 C CG A GLN A 370 ? 0.2484 0.2096 0.3108 -0.0299 0.0232 -0.0327 395 GLN A CG 2940 C CG B GLN A 370 ? 0.3137 0.2710 0.3617 -0.0381 0.0228 -0.0379 395 GLN A CG 2941 C CD A GLN A 370 ? 0.2716 0.2263 0.3316 -0.0335 0.0268 -0.0366 395 GLN A CD 2942 C CD B GLN A 370 ? 0.2351 0.1853 0.2829 -0.0399 0.0288 -0.0422 395 GLN A CD 2943 O OE1 A GLN A 370 ? 0.3514 0.3017 0.4053 -0.0369 0.0296 -0.0405 395 GLN A OE1 2944 O OE1 B GLN A 370 ? 0.3107 0.2588 0.3660 -0.0365 0.0317 -0.0413 395 GLN A OE1 2945 N NE2 A GLN A 370 ? 0.2670 0.2212 0.3318 -0.0332 0.0268 -0.0357 395 GLN A NE2 2946 N NE2 B GLN A 370 ? 0.2806 0.2272 0.3199 -0.0456 0.0305 -0.0468 395 GLN A NE2 2947 N N . MET A 371 ? 0.2405 0.2049 0.3074 -0.0218 0.0282 -0.0291 396 MET A N 2948 C CA . MET A 371 ? 0.2314 0.1985 0.3064 -0.0170 0.0294 -0.0258 396 MET A CA 2949 C C . MET A 371 ? 0.3083 0.2713 0.3877 -0.0152 0.0356 -0.0270 396 MET A C 2950 O O . MET A 371 ? 0.3368 0.3008 0.4240 -0.0117 0.0368 -0.0240 396 MET A O 2951 C CB . MET A 371 ? 0.2247 0.1975 0.3006 -0.0151 0.0261 -0.0231 396 MET A CB 2952 C CG . MET A 371 ? 0.2114 0.1886 0.2868 -0.0154 0.0203 -0.0217 396 MET A CG 2953 S SD . MET A 371 ? 0.2108 0.1916 0.2925 -0.0132 0.0191 -0.0195 396 MET A SD 2954 C CE . MET A 371 ? 0.2191 0.2044 0.3068 -0.0093 0.0199 -0.0161 396 MET A CE 2955 N N . SER A 372 ? 0.2463 0.2050 0.3209 -0.0180 0.0395 -0.0312 397 SER A N 2956 C CA . SER A 372 ? 0.2776 0.2321 0.3573 -0.0164 0.0463 -0.0335 397 SER A CA 2957 C C . SER A 372 ? 0.2928 0.2404 0.3744 -0.0177 0.0498 -0.0365 397 SER A C 2958 O O . SER A 372 ? 0.3373 0.2806 0.4258 -0.0157 0.0555 -0.0381 397 SER A O 2959 C CB . SER A 372 ? 0.2803 0.2338 0.3542 -0.0191 0.0500 -0.0374 397 SER A CB 2960 O OG . SER A 372 ? 0.2856 0.2449 0.3604 -0.0173 0.0480 -0.0342 397 SER A OG 2961 N N . LYS A 373 ? 0.2480 0.1944 0.3244 -0.0210 0.0465 -0.0375 398 LYS A N 2962 C CA . LYS A 373 ? 0.2750 0.2146 0.3522 -0.0232 0.0496 -0.0408 398 LYS A CA 2963 C C . LYS A 373 ? 0.2638 0.2038 0.3485 -0.0206 0.0475 -0.0363 398 LYS A C 2964 O O . LYS A 373 ? 0.4007 0.3346 0.4890 -0.0215 0.0503 -0.0378 398 LYS A O 2965 C CB . LYS A 373 ? 0.3436 0.2815 0.4099 -0.0296 0.0478 -0.0452 398 LYS A CB 2966 C CG . LYS A 373 ? 0.3719 0.3088 0.4296 -0.0333 0.0506 -0.0498 398 LYS A CG 2967 C CD . LYS A 373 ? 0.4200 0.3560 0.4662 -0.0403 0.0480 -0.0534 398 LYS A CD 2968 C CE . LYS A 373 ? 0.5156 0.4507 0.5524 -0.0449 0.0513 -0.0581 398 LYS A CE 2969 N NZ . LYS A 373 ? 0.6007 0.5363 0.6255 -0.0525 0.0478 -0.0606 398 LYS A NZ 2970 N N . ILE A 374 ? 0.2402 0.1873 0.3271 -0.0180 0.0427 -0.0309 399 ILE A N 2971 C CA . ILE A 374 ? 0.2704 0.2195 0.3637 -0.0160 0.0407 -0.0262 399 ILE A CA 2972 C C . ILE A 374 ? 0.2440 0.1929 0.3472 -0.0113 0.0434 -0.0222 399 ILE A C 2973 O O . ILE A 374 ? 0.2493 0.2018 0.3544 -0.0088 0.0437 -0.0209 399 ILE A O 2974 C CB . ILE A 374 ? 0.2227 0.1800 0.3137 -0.0158 0.0347 -0.0230 399 ILE A CB 2975 C CG1 . ILE A 374 ? 0.2374 0.1950 0.3208 -0.0202 0.0317 -0.0263 399 ILE A CG1 2976 C CG2 . ILE A 374 ? 0.2343 0.1950 0.3314 -0.0140 0.0332 -0.0180 399 ILE A CG2 2977 C CD1 . ILE A 374 ? 0.2608 0.2263 0.3425 -0.0199 0.0262 -0.0244 399 ILE A CD1 2978 N N . SER A 375 ? 0.2462 0.1912 0.3564 -0.0105 0.0451 -0.0198 400 SER A N 2979 C CA . SER A 375 ? 0.2206 0.1651 0.3417 -0.0062 0.0474 -0.0152 400 SER A CA 2980 C C . SER A 375 ? 0.2585 0.2124 0.3818 -0.0036 0.0429 -0.0087 400 SER A C 2981 O O . SER A 375 ? 0.2598 0.2193 0.3782 -0.0053 0.0385 -0.0072 400 SER A O 2982 C CB . SER A 375 ? 0.3418 0.2796 0.4702 -0.0063 0.0494 -0.0133 400 SER A CB 2983 O OG . SER A 375 ? 0.4991 0.4369 0.6394 -0.0019 0.0509 -0.0077 400 SER A OG 2984 N N . SER A 376 ? 0.2454 0.2016 0.3766 0.0002 0.0440 -0.0052 401 SER A N 2985 C CA . SER A 376 ? 0.2072 0.1727 0.3403 0.0020 0.0398 0.0008 401 SER A CA 2986 C C . SER A 376 ? 0.2243 0.1931 0.3594 0.0013 0.0364 0.0068 401 SER A C 2987 O O . SER A 376 ? 0.2153 0.1925 0.3482 0.0011 0.0324 0.0103 401 SER A O 2988 C CB . SER A 376 ? 0.2180 0.1855 0.3604 0.0060 0.0416 0.0039 401 SER A CB 2989 O OG . SER A 376 ? 0.2995 0.2627 0.4533 0.0082 0.0440 0.0079 401 SER A OG 2990 N N . ASP A 377 ? 0.2414 0.2037 0.3805 0.0005 0.0383 0.0079 402 ASP A N 2991 C CA . ASP A 377 ? 0.2485 0.2141 0.3891 -0.0009 0.0352 0.0140 402 ASP A CA 2992 C C . ASP A 377 ? 0.2351 0.1987 0.3688 -0.0050 0.0345 0.0110 402 ASP A C 2993 O O . ASP A 377 ? 0.2497 0.2149 0.3847 -0.0068 0.0328 0.0156 402 ASP A O 2994 C CB . ASP A 377 ? 0.3218 0.2836 0.4744 0.0014 0.0366 0.0206 402 ASP A CB 2995 C CG . ASP A 377 ? 0.3827 0.3327 0.5394 0.0008 0.0411 0.0173 402 ASP A CG 2996 O OD1 . ASP A 377 ? 0.3538 0.2985 0.5052 -0.0005 0.0441 0.0091 402 ASP A OD1 2997 O OD2 . ASP A 377 ? 0.5823 0.5284 0.7478 0.0014 0.0414 0.0229 402 ASP A OD2 2998 N N . PHE A 378 ? 0.2270 0.1878 0.3535 -0.0069 0.0354 0.0036 403 PHE A N 2999 C CA . PHE A 378 ? 0.1973 0.1576 0.3178 -0.0109 0.0342 0.0007 403 PHE A CA 3000 C C . PHE A 378 ? 0.2048 0.1749 0.3224 -0.0122 0.0300 0.0042 403 PHE A C 3001 O O . PHE A 378 ? 0.2214 0.1926 0.3391 -0.0148 0.0292 0.0063 403 PHE A O 3002 C CB . PHE A 378 ? 0.2448 0.2026 0.3578 -0.0129 0.0348 -0.0068 403 PHE A CB 3003 C CG . PHE A 378 ? 0.2786 0.2377 0.3861 -0.0169 0.0326 -0.0094 403 PHE A CG 3004 C CD1 . PHE A 378 ? 0.2699 0.2232 0.3788 -0.0198 0.0342 -0.0101 403 PHE A CD1 3005 C CD2 . PHE A 378 ? 0.2600 0.2261 0.3622 -0.0178 0.0290 -0.0111 403 PHE A CD2 3006 C CE1 . PHE A 378 ? 0.3050 0.2603 0.4097 -0.0237 0.0321 -0.0123 403 PHE A CE1 3007 C CE2 . PHE A 378 ? 0.2663 0.2344 0.3653 -0.0213 0.0270 -0.0132 403 PHE A CE2 3008 C CZ . PHE A 378 ? 0.2854 0.2486 0.3855 -0.0243 0.0285 -0.0137 403 PHE A CZ 3009 N N . THR A 379 ? 0.2003 0.1776 0.3155 -0.0106 0.0278 0.0043 404 THR A N 3010 C CA . THR A 379 ? 0.2017 0.1889 0.3151 -0.0115 0.0245 0.0072 404 THR A CA 3011 C C . THR A 379 ? 0.2093 0.2015 0.3254 -0.0087 0.0234 0.0110 404 THR A C 3012 O O . THR A 379 ? 0.2022 0.1905 0.3219 -0.0060 0.0252 0.0111 404 THR A O 3013 C CB . THR A 379 ? 0.1839 0.1755 0.2912 -0.0133 0.0224 0.0020 404 THR A CB 3014 O OG1 . THR A 379 ? 0.2208 0.2105 0.3255 -0.0118 0.0224 -0.0021 404 THR A OG1 3015 C CG2 . THR A 379 ? 0.2075 0.1957 0.3130 -0.0165 0.0229 -0.0008 404 THR A CG2 3016 N N . PRO A 380 ? 0.1796 0.1809 0.2942 -0.0096 0.0207 0.0140 405 PRO A N 3017 C CA . PRO A 380 ? 0.1941 0.2008 0.3116 -0.0076 0.0193 0.0182 405 PRO A CA 3018 C C . PRO A 380 ? 0.1527 0.1592 0.2694 -0.0052 0.0194 0.0147 405 PRO A C 3019 O O . PRO A 380 ? 0.1816 0.1898 0.3030 -0.0030 0.0193 0.0182 405 PRO A O 3020 C CB . PRO A 380 ? 0.2019 0.2187 0.3157 -0.0104 0.0165 0.0203 405 PRO A CB 3021 C CG . PRO A 380 ? 0.1841 0.1995 0.2970 -0.0133 0.0172 0.0212 405 PRO A CG 3022 C CD . PRO A 380 ? 0.1682 0.1753 0.2802 -0.0130 0.0193 0.0152 405 PRO A CD 3023 N N . PHE A 381 ? 0.1696 0.1748 0.2814 -0.0058 0.0193 0.0084 406 PHE A N 3024 C CA . PHE A 381 ? 0.1661 0.1710 0.2769 -0.0040 0.0193 0.0055 406 PHE A CA 3025 C C . PHE A 381 ? 0.1746 0.1721 0.2893 -0.0020 0.0227 0.0054 406 PHE A C 3026 O O . PHE A 381 ? 0.1867 0.1772 0.3001 -0.0028 0.0250 0.0023 406 PHE A O 3027 C CB . PHE A 381 ? 0.1878 0.1922 0.2931 -0.0054 0.0182 -0.0003 406 PHE A CB 3028 C CG . PHE A 381 ? 0.1905 0.1945 0.2943 -0.0043 0.0178 -0.0027 406 PHE A CG 3029 C CD1 . PHE A 381 ? 0.2148 0.2251 0.3180 -0.0041 0.0153 -0.0029 406 PHE A CD1 3030 C CD2 . PHE A 381 ? 0.1756 0.1731 0.2784 -0.0039 0.0201 -0.0051 406 PHE A CD2 3031 C CE1 . PHE A 381 ? 0.2483 0.2580 0.3505 -0.0035 0.0148 -0.0047 406 PHE A CE1 3032 C CE2 . PHE A 381 ? 0.1738 0.1713 0.2748 -0.0035 0.0197 -0.0069 406 PHE A CE2 3033 C CZ . PHE A 381 ? 0.2274 0.2308 0.3283 -0.0032 0.0170 -0.0064 406 PHE A CZ 3034 N N . PRO A 382 ? 0.1769 0.1764 0.2967 0.0004 0.0232 0.0084 407 PRO A N 3035 C CA . PRO A 382 ? 0.1786 0.1718 0.3045 0.0026 0.0272 0.0087 407 PRO A CA 3036 C C . PRO A 382 ? 0.1994 0.1896 0.3234 0.0032 0.0296 0.0040 407 PRO A C 3037 O O . PRO A 382 ? 0.2065 0.1912 0.3351 0.0047 0.0338 0.0028 407 PRO A O 3038 C CB . PRO A 382 ? 0.2199 0.2185 0.3540 0.0048 0.0261 0.0156 407 PRO A CB 3039 C CG . PRO A 382 ? 0.1774 0.1846 0.3074 0.0039 0.0223 0.0159 407 PRO A CG 3040 C CD . PRO A 382 ? 0.1715 0.1796 0.2929 0.0009 0.0204 0.0122 407 PRO A CD 3041 N N . HIS A 383 ? 0.1919 0.1854 0.3096 0.0020 0.0273 0.0012 408 HIS A N 3042 C CA . HIS A 383 ? 0.1994 0.1915 0.3153 0.0022 0.0291 -0.0020 408 HIS A CA 3043 C C . HIS A 383 ? 0.1885 0.1738 0.2979 -0.0002 0.0312 -0.0075 408 HIS A C 3044 O O . HIS A 383 ? 0.2105 0.1964 0.3131 -0.0024 0.0285 -0.0100 408 HIS A O 3045 C CB . HIS A 383 ? 0.2075 0.2062 0.3209 0.0018 0.0255 -0.0016 408 HIS A CB 3046 C CG . HIS A 383 ? 0.1692 0.1753 0.2873 0.0029 0.0229 0.0033 408 HIS A CG 3047 N ND1 . HIS A 383 ? 0.2209 0.2293 0.3473 0.0052 0.0242 0.0077 408 HIS A ND1 3048 C CD2 . HIS A 383 ? 0.2206 0.2328 0.3364 0.0017 0.0191 0.0045 408 HIS A CD2 3049 C CE1 . HIS A 383 ? 0.2356 0.2515 0.3637 0.0050 0.0207 0.0119 408 HIS A CE1 3050 N NE2 . HIS A 383 ? 0.2201 0.2383 0.3414 0.0027 0.0179 0.0097 408 HIS A NE2 3051 N N . ARG A 384 ? 0.2000 0.1790 0.3122 0.0001 0.0358 -0.0093 409 ARG A N 3052 C CA . ARG A 384 ? 0.1925 0.1650 0.2982 -0.0029 0.0380 -0.0146 409 ARG A CA 3053 C C . ARG A 384 ? 0.1928 0.1622 0.2982 -0.0031 0.0429 -0.0182 409 ARG A C 3054 O O . ARG A 384 ? 0.1985 0.1716 0.3019 -0.0031 0.0421 -0.0181 409 ARG A O 3055 C CB . ARG A 384 ? 0.2040 0.1712 0.3118 -0.0035 0.0395 -0.0148 409 ARG A CB 3056 C CG . ARG A 384 ? 0.1876 0.1590 0.2964 -0.0034 0.0352 -0.0107 409 ARG A CG 3057 C CD . ARG A 384 ? 0.1873 0.1623 0.2885 -0.0059 0.0307 -0.0124 409 ARG A CD 3058 N NE . ARG A 384 ? 0.1923 0.1705 0.2949 -0.0064 0.0282 -0.0096 409 ARG A NE 3059 C CZ . ARG A 384 ? 0.1802 0.1601 0.2787 -0.0088 0.0255 -0.0112 409 ARG A CZ 3060 N NH1 . ARG A 384 ? 0.1885 0.1674 0.2813 -0.0109 0.0240 -0.0150 409 ARG A NH1 3061 N NH2 . ARG A 384 ? 0.1718 0.1550 0.2724 -0.0093 0.0241 -0.0086 409 ARG A NH2 3062 N N . SER A 385 ? 0.1971 0.1598 0.3046 -0.0035 0.0482 -0.0216 410 SER A N 3063 C CA . SER A 385 ? 0.2267 0.1869 0.3344 -0.0040 0.0538 -0.0258 410 SER A CA 3064 C C . SER A 385 ? 0.2371 0.2031 0.3525 -0.0005 0.0546 -0.0224 410 SER A C 3065 O O . SER A 385 ? 0.2381 0.2072 0.3632 0.0032 0.0534 -0.0173 410 SER A O 3066 C CB . SER A 385 ? 0.2539 0.2063 0.3663 -0.0040 0.0602 -0.0298 410 SER A CB 3067 O OG . SER A 385 ? 0.3290 0.2792 0.4404 -0.0053 0.0663 -0.0352 410 SER A OG 3068 N N . GLY A 386 ? 0.2276 0.1955 0.3386 -0.0022 0.0564 -0.0250 411 GLY A N 3069 C CA . GLY A 386 ? 0.2511 0.2249 0.3692 0.0005 0.0572 -0.0222 411 GLY A CA 3070 C C . GLY A 386 ? 0.2663 0.2468 0.3804 0.0000 0.0509 -0.0184 411 GLY A C 3071 O O . GLY A 386 ? 0.2894 0.2748 0.4061 0.0006 0.0512 -0.0171 411 GLY A O 3072 N N . THR A 387 ? 0.2295 0.2103 0.3381 -0.0011 0.0454 -0.0169 412 THR A N 3073 C CA . THR A 387 ? 0.2134 0.1997 0.3185 -0.0017 0.0397 -0.0143 412 THR A CA 3074 C C . THR A 387 ? 0.2226 0.2073 0.3178 -0.0057 0.0387 -0.0173 412 THR A C 3075 O O . THR A 387 ? 0.2595 0.2398 0.3477 -0.0086 0.0385 -0.0202 412 THR A O 3076 C CB . THR A 387 ? 0.2283 0.2160 0.3327 -0.0014 0.0347 -0.0121 412 THR A CB 3077 O OG1 . THR A 387 ? 0.2682 0.2564 0.3806 0.0014 0.0358 -0.0091 412 THR A OG1 3078 C CG2 . THR A 387 ? 0.2229 0.2167 0.3262 -0.0014 0.0296 -0.0097 412 THR A CG2 3079 N N . ARG A 388 ? 0.1979 0.1865 0.2926 -0.0063 0.0377 -0.0162 413 ARG A N 3080 C CA . ARG A 388 ? 0.1838 0.1710 0.2695 -0.0104 0.0367 -0.0179 413 ARG A CA 3081 C C . ARG A 388 ? 0.2047 0.1936 0.2866 -0.0116 0.0299 -0.0160 413 ARG A C 3082 O O . ARG A 388 ? 0.2181 0.2042 0.2931 -0.0145 0.0274 -0.0172 413 ARG A O 3083 C CB . ARG A 388 ? 0.1917 0.1817 0.2789 -0.0111 0.0401 -0.0179 413 ARG A CB 3084 C CG . ARG A 388 ? 0.2496 0.2378 0.3407 -0.0105 0.0477 -0.0209 413 ARG A CG 3085 C CD . ARG A 388 ? 0.2661 0.2579 0.3582 -0.0119 0.0513 -0.0213 413 ARG A CD 3086 N NE . ARG A 388 ? 0.3149 0.3056 0.4123 -0.0110 0.0594 -0.0249 413 ARG A NE 3087 C CZ . ARG A 388 ? 0.4196 0.4062 0.5099 -0.0148 0.0646 -0.0302 413 ARG A CZ 3088 N NH1 . ARG A 388 ? 0.3819 0.3656 0.4592 -0.0200 0.0619 -0.0317 413 ARG A NH1 3089 N NH2 . ARG A 388 ? 0.3956 0.3815 0.4926 -0.0137 0.0726 -0.0341 413 ARG A NH2 3090 N N . LEU A 389 ? 0.1856 0.1793 0.2727 -0.0095 0.0270 -0.0131 414 LEU A N 3091 C CA . LEU A 389 ? 0.1735 0.1687 0.2586 -0.0103 0.0212 -0.0119 414 LEU A CA 3092 C C . LEU A 389 ? 0.1747 0.1738 0.2652 -0.0076 0.0184 -0.0104 414 LEU A C 3093 O O . LEU A 389 ? 0.2061 0.2085 0.3025 -0.0052 0.0202 -0.0088 414 LEU A O 3094 C CB . LEU A 389 ? 0.1760 0.1732 0.2605 -0.0119 0.0200 -0.0105 414 LEU A CB 3095 C CG . LEU A 389 ? 0.2113 0.2066 0.2908 -0.0151 0.0234 -0.0114 414 LEU A CG 3096 C CD1 . LEU A 389 ? 0.2438 0.2421 0.3245 -0.0164 0.0221 -0.0093 414 LEU A CD1 3097 C CD2 . LEU A 389 ? 0.2411 0.2318 0.3119 -0.0188 0.0217 -0.0126 414 LEU A CD2 3098 N N . MET A 390 ? 0.1670 0.1664 0.2560 -0.0083 0.0139 -0.0107 415 MET A N 3099 C CA . MET A 390 ? 0.1713 0.1753 0.2646 -0.0067 0.0111 -0.0100 415 MET A CA 3100 C C . MET A 390 ? 0.2053 0.2103 0.2988 -0.0080 0.0079 -0.0099 415 MET A C 3101 O O . MET A 390 ? 0.2178 0.2193 0.3081 -0.0097 0.0057 -0.0104 415 MET A O 3102 C CB . MET A 390 ? 0.1989 0.2027 0.2918 -0.0064 0.0093 -0.0113 415 MET A CB 3103 C CG . MET A 390 ? 0.2029 0.2121 0.2995 -0.0054 0.0072 -0.0113 415 MET A CG 3104 S SD . MET A 390 ? 0.3205 0.3311 0.4176 -0.0050 0.0070 -0.0123 415 MET A SD 3105 C CE . MET A 390 ? 0.3869 0.3936 0.4817 -0.0063 0.0045 -0.0148 415 MET A CE 3106 N N . VAL A 391 ? 0.1714 0.1810 0.2688 -0.0073 0.0073 -0.0090 416 VAL A N 3107 C CA . VAL A 391 ? 0.2016 0.2119 0.3000 -0.0087 0.0047 -0.0090 416 VAL A CA 3108 C C . VAL A 391 ? 0.2109 0.2255 0.3127 -0.0081 0.0023 -0.0103 416 VAL A C 3109 O O . VAL A 391 ? 0.2085 0.2283 0.3128 -0.0074 0.0031 -0.0094 416 VAL A O 3110 C CB . VAL A 391 ? 0.2172 0.2295 0.3171 -0.0093 0.0067 -0.0070 416 VAL A CB 3111 C CG1 . VAL A 391 ? 0.2472 0.2601 0.3484 -0.0112 0.0040 -0.0069 416 VAL A CG1 3112 C CG2 . VAL A 391 ? 0.2593 0.2681 0.3556 -0.0103 0.0102 -0.0065 416 VAL A CG2 3113 N N . GLU A 392 ? 0.1786 0.1913 0.2810 -0.0087 -0.0007 -0.0125 417 GLU A N 3114 C CA A GLU A 392 ? 0.1685 0.1852 0.2741 -0.0086 -0.0023 -0.0151 417 GLU A CA 3115 C CA B GLU A 392 ? 0.1686 0.1853 0.2742 -0.0086 -0.0023 -0.0150 417 GLU A CA 3116 C C . GLU A 392 ? 0.1885 0.2048 0.2967 -0.0101 -0.0044 -0.0160 417 GLU A C 3117 O O . GLU A 392 ? 0.1960 0.2074 0.3042 -0.0110 -0.0060 -0.0152 417 GLU A O 3118 C CB A GLU A 392 ? 0.2031 0.2182 0.3093 -0.0079 -0.0036 -0.0178 417 GLU A CB 3119 C CB B GLU A 392 ? 0.2093 0.2248 0.3156 -0.0079 -0.0035 -0.0178 417 GLU A CB 3120 C CG A GLU A 392 ? 0.1927 0.2079 0.2965 -0.0069 -0.0017 -0.0171 417 GLU A CG 3121 C CG B GLU A 392 ? 0.2624 0.2829 0.3716 -0.0081 -0.0040 -0.0213 417 GLU A CG 3122 C CD A GLU A 392 ? 0.3241 0.3380 0.4291 -0.0066 -0.0030 -0.0195 417 GLU A CD 3123 C CD B GLU A 392 ? 0.3293 0.3491 0.4407 -0.0074 -0.0047 -0.0246 417 GLU A CD 3124 O OE1 A GLU A 392 ? 0.3173 0.3347 0.4254 -0.0064 -0.0035 -0.0226 417 GLU A OE1 3125 O OE1 B GLU A 392 ? 0.3039 0.3193 0.4149 -0.0068 -0.0056 -0.0237 417 GLU A OE1 3126 O OE2 A GLU A 392 ? 0.2330 0.2427 0.3360 -0.0067 -0.0035 -0.0185 417 GLU A OE2 3127 O OE2 B GLU A 392 ? 0.3232 0.3474 0.4367 -0.0078 -0.0044 -0.0283 417 GLU A OE2 3128 N N . TYR A 393 ? 0.1661 0.1877 0.2764 -0.0109 -0.0046 -0.0173 418 TYR A N 3129 C CA . TYR A 393 ? 0.1621 0.1837 0.2754 -0.0128 -0.0065 -0.0189 418 TYR A CA 3130 C C . TYR A 393 ? 0.2009 0.2248 0.3166 -0.0132 -0.0074 -0.0240 418 TYR A C 3131 O O . TYR A 393 ? 0.2067 0.2364 0.3212 -0.0133 -0.0063 -0.0252 418 TYR A O 3132 C CB . TYR A 393 ? 0.2059 0.2327 0.3196 -0.0142 -0.0058 -0.0167 418 TYR A CB 3133 C CG . TYR A 393 ? 0.1635 0.1913 0.2758 -0.0132 -0.0035 -0.0123 418 TYR A CG 3134 C CD1 . TYR A 393 ? 0.1924 0.2162 0.3039 -0.0138 -0.0027 -0.0099 418 TYR A CD1 3135 C CD2 . TYR A 393 ? 0.1950 0.2277 0.3071 -0.0118 -0.0018 -0.0104 418 TYR A CD2 3136 C CE1 . TYR A 393 ? 0.1825 0.2074 0.2933 -0.0129 0.0003 -0.0069 418 TYR A CE1 3137 C CE2 . TYR A 393 ? 0.1818 0.2150 0.2944 -0.0105 0.0008 -0.0069 418 TYR A CE2 3138 C CZ . TYR A 393 ? 0.1755 0.2048 0.2875 -0.0110 0.0022 -0.0056 418 TYR A CZ 3139 O OH . TYR A 393 ? 0.1717 0.2016 0.2848 -0.0098 0.0056 -0.0031 418 TYR A OH 3140 N N . ILE A 394 ? 0.1860 0.2056 0.3056 -0.0136 -0.0092 -0.0269 419 ILE A N 3141 C CA . ILE A 394 ? 0.1779 0.1989 0.3009 -0.0138 -0.0094 -0.0329 419 ILE A CA 3142 C C . ILE A 394 ? 0.1934 0.2124 0.3211 -0.0158 -0.0109 -0.0360 419 ILE A C 3143 O O . ILE A 394 ? 0.2094 0.2226 0.3392 -0.0162 -0.0126 -0.0335 419 ILE A O 3144 C CB . ILE A 394 ? 0.1939 0.2107 0.3200 -0.0116 -0.0100 -0.0344 419 ILE A CB 3145 C CG1 . ILE A 394 ? 0.2519 0.2697 0.3737 -0.0100 -0.0088 -0.0314 419 ILE A CG1 3146 C CG2 . ILE A 394 ? 0.2220 0.2413 0.3530 -0.0117 -0.0093 -0.0413 419 ILE A CG2 3147 C CD1 . ILE A 394 ? 0.3183 0.3311 0.4370 -0.0096 -0.0095 -0.0261 419 ILE A CD1 3148 N N . VAL A 395 ? 0.1824 0.2059 0.3113 -0.0176 -0.0101 -0.0415 420 VAL A N 3149 C CA . VAL A 395 ? 0.1845 0.2050 0.3190 -0.0194 -0.0111 -0.0462 420 VAL A CA 3150 C C . VAL A 395 ? 0.2077 0.2293 0.3465 -0.0190 -0.0096 -0.0539 420 VAL A C 3151 O O . VAL A 395 ? 0.2022 0.2307 0.3373 -0.0196 -0.0075 -0.0563 420 VAL A O 3152 C CB . VAL A 395 ? 0.2144 0.2395 0.3469 -0.0232 -0.0113 -0.0465 420 VAL A CB 3153 C CG1 . VAL A 395 ? 0.2095 0.2442 0.3374 -0.0253 -0.0096 -0.0496 420 VAL A CG1 3154 C CG2 . VAL A 395 ? 0.2310 0.2508 0.3696 -0.0252 -0.0126 -0.0507 420 VAL A CG2 3155 N N . ALA A 396 ? 0.2012 0.2161 0.3483 -0.0180 -0.0106 -0.0573 421 ALA A N 3156 C CA . ALA A 396 ? 0.2236 0.2389 0.3770 -0.0169 -0.0088 -0.0647 421 ALA A CA 3157 C C . ALA A 396 ? 0.2174 0.2273 0.3800 -0.0179 -0.0092 -0.0707 421 ALA A C 3158 O O . ALA A 396 ? 0.2666 0.2699 0.4326 -0.0183 -0.0119 -0.0674 421 ALA A O 3159 C CB . ALA A 396 ? 0.1909 0.2029 0.3480 -0.0130 -0.0097 -0.0618 421 ALA A CB 3160 N N . TRP A 397 ? 0.2151 0.2279 0.3822 -0.0186 -0.0063 -0.0798 422 TRP A N 3161 C CA . TRP A 397 ? 0.2332 0.2409 0.4096 -0.0200 -0.0059 -0.0870 422 TRP A CA 3162 C C . TRP A 397 ? 0.2683 0.2776 0.4532 -0.0187 -0.0023 -0.0967 422 TRP A C 3163 O O . TRP A 397 ? 0.2521 0.2690 0.4325 -0.0187 0.0006 -0.0992 422 TRP A O 3164 C CB . TRP A 397 ? 0.2282 0.2397 0.3986 -0.0253 -0.0053 -0.0899 422 TRP A CB 3165 C CG . TRP A 397 ? 0.2540 0.2767 0.4157 -0.0287 -0.0020 -0.0949 422 TRP A CG 3166 C CD1 . TRP A 397 ? 0.2713 0.2979 0.4348 -0.0316 0.0017 -0.1057 422 TRP A CD1 3167 C CD2 . TRP A 397 ? 0.2462 0.2774 0.3962 -0.0300 -0.0021 -0.0892 422 TRP A CD2 3168 N NE1 . TRP A 397 ? 0.2696 0.3074 0.4221 -0.0351 0.0036 -0.1065 422 TRP A NE1 3169 C CE2 . TRP A 397 ? 0.2470 0.2875 0.3917 -0.0340 0.0010 -0.0961 422 TRP A CE2 3170 C CE3 . TRP A 397 ? 0.2475 0.2795 0.3915 -0.0284 -0.0044 -0.0790 422 TRP A CE3 3171 C CZ2 . TRP A 397 ? 0.2566 0.3069 0.3906 -0.0363 0.0012 -0.0920 422 TRP A CZ2 3172 C CZ3 . TRP A 397 ? 0.2459 0.2871 0.3805 -0.0302 -0.0038 -0.0757 422 TRP A CZ3 3173 C CH2 . TRP A 397 ? 0.2542 0.3043 0.3839 -0.0340 -0.0014 -0.0816 422 TRP A CH2 3174 N N . ASN A 398 ? 0.2747 0.2765 0.4724 -0.0178 -0.0023 -0.1020 423 ASN A N 3175 C CA . ASN A 398 ? 0.3115 0.3146 0.5192 -0.0166 0.0018 -0.1124 423 ASN A CA 3176 C C . ASN A 398 ? 0.2980 0.3052 0.5039 -0.0217 0.0059 -0.1235 423 ASN A C 3177 O O . ASN A 398 ? 0.2910 0.2994 0.4887 -0.0261 0.0049 -0.1226 423 ASN A O 3178 C CB . ASN A 398 ? 0.3376 0.3307 0.5629 -0.0120 -0.0002 -0.1125 423 ASN A CB 3179 C CG . ASN A 398 ? 0.3954 0.3788 0.6276 -0.0133 -0.0029 -0.1121 423 ASN A CG 3180 O OD1 . ASN A 398 ? 0.4401 0.4242 0.6700 -0.0177 -0.0007 -0.1189 423 ASN A OD1 3181 N ND2 . ASN A 398 ? 0.4285 0.4030 0.6691 -0.0101 -0.0077 -0.1041 423 ASN A ND2 3182 N N . GLN A 399 ? 0.3259 0.3356 0.5395 -0.0214 0.0108 -0.1343 424 GLN A N 3183 C CA . GLN A 399 ? 0.3868 0.4020 0.5971 -0.0270 0.0157 -0.1461 424 GLN A CA 3184 C C . GLN A 399 ? 0.3562 0.3638 0.5709 -0.0300 0.0145 -0.1498 424 GLN A C 3185 O O . GLN A 399 ? 0.3662 0.3788 0.5725 -0.0362 0.0163 -0.1555 424 GLN A O 3186 C CB . GLN A 399 ? 0.5809 0.5993 0.8010 -0.0258 0.0217 -0.1577 424 GLN A CB 3187 C CG . GLN A 399 ? 0.8365 0.8628 1.0504 -0.0325 0.0276 -0.1706 424 GLN A CG 3188 C CD . GLN A 399 ? 1.0383 1.0703 1.2595 -0.0317 0.0344 -0.1815 424 GLN A CD 3189 O OE1 . GLN A 399 ? 1.1133 1.1454 1.3409 -0.0346 0.0398 -0.1948 424 GLN A OE1 3190 N NE2 . GLN A 399 ? 1.0620 1.0988 1.2827 -0.0281 0.0345 -0.1763 424 GLN A NE2 3191 N N . SER A 400 ? 0.3523 0.3481 0.5802 -0.0261 0.0111 -0.1461 425 SER A N 3192 C CA . SER A 400 ? 0.3388 0.3261 0.5728 -0.0289 0.0099 -0.1494 425 SER A CA 3193 C C . SER A 400 ? 0.3516 0.3401 0.5725 -0.0330 0.0058 -0.1411 425 SER A C 3194 O O . SER A 400 ? 0.3927 0.3766 0.6154 -0.0369 0.0050 -0.1439 425 SER A O 3195 C CB . SER A 400 ? 0.3868 0.3610 0.6394 -0.0236 0.0070 -0.1466 425 SER A CB 3196 O OG . SER A 400 ? 0.3977 0.3680 0.6480 -0.0204 0.0009 -0.1323 425 SER A OG 3197 N N . GLU A 401 ? 0.3224 0.3173 0.5312 -0.0321 0.0035 -0.1311 426 GLU A N 3198 C CA . GLU A 401 ? 0.3496 0.3463 0.5474 -0.0352 -0.0002 -0.1224 426 GLU A CA 3199 C C . GLU A 401 ? 0.3593 0.3689 0.5421 -0.0402 0.0016 -0.1238 426 GLU A C 3200 O O . GLU A 401 ? 0.3229 0.3362 0.4964 -0.0422 -0.0012 -0.1161 426 GLU A O 3201 C CB . GLU A 401 ? 0.3036 0.2975 0.4996 -0.0306 -0.0043 -0.1093 426 GLU A CB 3202 C CG . GLU A 401 ? 0.3164 0.2985 0.5260 -0.0261 -0.0071 -0.1057 426 GLU A CG 3203 C CD . GLU A 401 ? 0.3809 0.3615 0.5871 -0.0225 -0.0109 -0.0935 426 GLU A CD 3204 O OE1 . GLU A 401 ? 0.4125 0.3872 0.6186 -0.0230 -0.0147 -0.0857 426 GLU A OE1 3205 O OE2 . GLU A 401 ? 0.3304 0.3159 0.5336 -0.0196 -0.0099 -0.0919 426 GLU A OE2 3206 N N . GLN A 402 ? 0.3577 0.3743 0.5385 -0.0422 0.0062 -0.1335 427 GLN A N 3207 C CA . GLN A 402 ? 0.3971 0.4268 0.5636 -0.0472 0.0077 -0.1344 427 GLN A CA 3208 C C . GLN A 402 ? 0.3752 0.4088 0.5336 -0.0536 0.0055 -0.1333 427 GLN A C 3209 O O . GLN A 402 ? 0.3609 0.4041 0.5076 -0.0564 0.0041 -0.1278 427 GLN A O 3210 C CB . GLN A 402 ? 0.5295 0.5656 0.6959 -0.0497 0.0135 -0.1467 427 GLN A CB 3211 C CG . GLN A 402 ? 0.7547 0.7926 0.9245 -0.0446 0.0158 -0.1461 427 GLN A CG 3212 C CD . GLN A 402 ? 0.9249 0.9694 1.0955 -0.0474 0.0222 -0.1589 427 GLN A CD 3213 O OE1 . GLN A 402 ? 0.9736 1.0213 1.1467 -0.0442 0.0249 -0.1598 427 GLN A OE1 3214 N NE2 . GLN A 402 ? 0.9499 0.9970 1.1183 -0.0538 0.0250 -0.1693 427 GLN A NE2 3215 N N . LYS A 403 ? 0.3674 0.3935 0.5329 -0.0560 0.0050 -0.1384 428 LYS A N 3216 C CA . LYS A 403 ? 0.4235 0.4532 0.5828 -0.0626 0.0029 -0.1381 428 LYS A CA 3217 C C . LYS A 403 ? 0.3903 0.4228 0.5431 -0.0616 -0.0018 -0.1245 428 LYS A C 3218 O O . LYS A 403 ? 0.3510 0.3915 0.4955 -0.0668 -0.0036 -0.1221 428 LYS A O 3219 C CB . LYS A 403 ? 0.4538 0.4727 0.6238 -0.0645 0.0028 -0.1445 428 LYS A CB 3220 C CG . LYS A 403 ? 0.6702 0.6930 0.8344 -0.0723 0.0010 -0.1463 428 LYS A CG 3221 C CD . LYS A 403 ? 0.7934 0.8061 0.9682 -0.0753 0.0024 -0.1562 428 LYS A CD 3222 C CE . LYS A 403 ? 0.8570 0.8572 1.0418 -0.0720 -0.0015 -0.1483 428 LYS A CE 3223 N NZ . LYS A 403 ? 0.8516 0.8553 1.0298 -0.0765 -0.0056 -0.1407 428 LYS A NZ 3224 N N . LYS A 404 ? 0.3326 0.3588 0.4895 -0.0550 -0.0037 -0.1157 429 LYS A N 3225 C CA . LYS A 404 ? 0.3077 0.3350 0.4602 -0.0537 -0.0074 -0.1034 429 LYS A CA 3226 C C . LYS A 404 ? 0.2797 0.3162 0.4230 -0.0517 -0.0075 -0.0965 429 LYS A C 3227 O O . LYS A 404 ? 0.2522 0.2894 0.3928 -0.0498 -0.0098 -0.0867 429 LYS A O 3228 C CB . LYS A 404 ? 0.3265 0.3418 0.4877 -0.0488 -0.0096 -0.0973 429 LYS A CB 3229 C CG . LYS A 404 ? 0.3933 0.3992 0.5632 -0.0512 -0.0108 -0.1008 429 LYS A CG 3230 C CD . LYS A 404 ? 0.4314 0.4254 0.6105 -0.0463 -0.0130 -0.0949 429 LYS A CD 3231 C CE . LYS A 404 ? 0.3582 0.3533 0.5317 -0.0443 -0.0158 -0.0825 429 LYS A CE 3232 N NZ . LYS A 404 ? 0.3476 0.3314 0.5289 -0.0410 -0.0183 -0.0766 429 LYS A NZ 3233 N N . LYS A 405 ? 0.2623 0.3058 0.4013 -0.0526 -0.0046 -0.1018 430 LYS A N 3234 C CA . LYS A 405 ? 0.2788 0.3303 0.4099 -0.0508 -0.0045 -0.0955 430 LYS A CA 3235 C C . LYS A 405 ? 0.2449 0.3036 0.3691 -0.0528 -0.0075 -0.0864 430 LYS A C 3236 O O . LYS A 405 ? 0.2463 0.3047 0.3692 -0.0489 -0.0088 -0.0774 430 LYS A O 3237 C CB . LYS A 405 ? 0.2964 0.3563 0.4225 -0.0537 -0.0010 -0.1031 430 LYS A CB 3238 C CG . LYS A 405 ? 0.3482 0.4167 0.4662 -0.0527 -0.0010 -0.0965 430 LYS A CG 3239 C CD . LYS A 405 ? 0.4286 0.5056 0.5413 -0.0565 0.0026 -0.1042 430 LYS A CD 3240 C CE . LYS A 405 ? 0.5019 0.5882 0.6056 -0.0568 0.0021 -0.0968 430 LYS A CE 3241 N NZ . LYS A 405 ? 0.5905 0.6862 0.6879 -0.0616 0.0055 -0.1038 430 LYS A NZ 3242 N N . THR A 406 ? 0.2732 0.3386 0.3934 -0.0591 -0.0086 -0.0889 431 THR A N 3243 C CA . THR A 406 ? 0.2267 0.3003 0.3418 -0.0612 -0.0116 -0.0803 431 THR A CA 3244 C C . THR A 406 ? 0.2332 0.3002 0.3534 -0.0574 -0.0138 -0.0721 431 THR A C 3245 O O . THR A 406 ? 0.2260 0.2966 0.3441 -0.0550 -0.0150 -0.0631 431 THR A O 3246 C CB . THR A 406 ? 0.2659 0.3476 0.3771 -0.0692 -0.0130 -0.0846 431 THR A CB 3247 O OG1 . THR A 406 ? 0.3442 0.4333 0.4492 -0.0735 -0.0107 -0.0922 431 THR A OG1 3248 C CG2 . THR A 406 ? 0.3317 0.4227 0.4394 -0.0711 -0.0166 -0.0749 431 THR A CG2 3249 N N . GLU A 407 ? 0.2205 0.2775 0.3475 -0.0572 -0.0139 -0.0752 432 GLU A N 3250 C CA . GLU A 407 ? 0.2194 0.2696 0.3509 -0.0543 -0.0157 -0.0679 432 GLU A CA 3251 C C . GLU A 407 ? 0.2212 0.2672 0.3530 -0.0478 -0.0150 -0.0616 432 GLU A C 3252 O O . GLU A 407 ? 0.2258 0.2723 0.3567 -0.0458 -0.0160 -0.0535 432 GLU A O 3253 C CB . GLU A 407 ? 0.2621 0.3017 0.4012 -0.0555 -0.0161 -0.0725 432 GLU A CB 3254 C CG . GLU A 407 ? 0.3100 0.3420 0.4534 -0.0530 -0.0178 -0.0649 432 GLU A CG 3255 C CD . GLU A 407 ? 0.3927 0.4138 0.5441 -0.0545 -0.0186 -0.0687 432 GLU A CD 3256 O OE1 . GLU A 407 ? 0.4044 0.4250 0.5582 -0.0584 -0.0179 -0.0773 432 GLU A OE1 3257 O OE2 . GLU A 407 ? 0.3347 0.3479 0.4899 -0.0521 -0.0199 -0.0629 432 GLU A OE2 3258 N N . PHE A 408 ? 0.2157 0.2576 0.3489 -0.0447 -0.0132 -0.0658 433 PHE A N 3259 C CA . PHE A 408 ? 0.2045 0.2426 0.3377 -0.0391 -0.0127 -0.0606 433 PHE A CA 3260 C C . PHE A 408 ? 0.1838 0.2303 0.3104 -0.0382 -0.0125 -0.0543 433 PHE A C 3261 O O . PHE A 408 ? 0.1979 0.2424 0.3240 -0.0350 -0.0128 -0.0472 433 PHE A O 3262 C CB . PHE A 408 ? 0.2337 0.2681 0.3700 -0.0366 -0.0107 -0.0668 433 PHE A CB 3263 C CG . PHE A 408 ? 0.2260 0.2503 0.3713 -0.0358 -0.0110 -0.0714 433 PHE A CG 3264 C CD1 . PHE A 408 ? 0.2454 0.2616 0.3951 -0.0349 -0.0134 -0.0663 433 PHE A CD1 3265 C CD2 . PHE A 408 ? 0.2459 0.2688 0.3962 -0.0360 -0.0088 -0.0807 433 PHE A CD2 3266 C CE1 . PHE A 408 ? 0.2659 0.2724 0.4249 -0.0341 -0.0143 -0.0696 433 PHE A CE1 3267 C CE2 . PHE A 408 ? 0.2580 0.2711 0.4186 -0.0348 -0.0092 -0.0848 433 PHE A CE2 3268 C CZ . PHE A 408 ? 0.3209 0.3256 0.4861 -0.0338 -0.0123 -0.0788 433 PHE A CZ 3269 N N . LEU A 409 ? 0.2135 0.2694 0.3352 -0.0411 -0.0118 -0.0569 434 LEU A N 3270 C CA . LEU A 409 ? 0.2268 0.2908 0.3433 -0.0405 -0.0119 -0.0506 434 LEU A CA 3271 C C . LEU A 409 ? 0.2182 0.2858 0.3350 -0.0412 -0.0139 -0.0432 434 LEU A C 3272 O O . LEU A 409 ? 0.2423 0.3117 0.3583 -0.0383 -0.0138 -0.0362 434 LEU A O 3273 C CB . LEU A 409 ? 0.2666 0.3405 0.3775 -0.0444 -0.0113 -0.0545 434 LEU A CB 3274 C CG . LEU A 409 ? 0.3860 0.4580 0.4966 -0.0438 -0.0085 -0.0620 434 LEU A CG 3275 C CD1 . LEU A 409 ? 0.3901 0.4731 0.4935 -0.0480 -0.0077 -0.0639 434 LEU A CD1 3276 C CD2 . LEU A 409 ? 0.3837 0.4488 0.4970 -0.0378 -0.0073 -0.0591 434 LEU A CD2 3277 N N . ASP A 410 ? 0.2246 0.2932 0.3434 -0.0452 -0.0155 -0.0450 435 ASP A N 3278 C CA . ASP A 410 ? 0.1996 0.2719 0.3202 -0.0462 -0.0172 -0.0384 435 ASP A CA 3279 C C . ASP A 410 ? 0.2173 0.2817 0.3412 -0.0417 -0.0164 -0.0332 435 ASP A C 3280 O O . ASP A 410 ? 0.2089 0.2766 0.3334 -0.0399 -0.0163 -0.0265 435 ASP A O 3281 C CB . ASP A 410 ? 0.2358 0.3100 0.3582 -0.0518 -0.0190 -0.0421 435 ASP A CB 3282 C CG . ASP A 410 ? 0.2306 0.3099 0.3558 -0.0531 -0.0207 -0.0352 435 ASP A CG 3283 O OD1 . ASP A 410 ? 0.2647 0.3539 0.3886 -0.0534 -0.0218 -0.0298 435 ASP A OD1 3284 O OD2 . ASP A 410 ? 0.3193 0.3931 0.4486 -0.0540 -0.0211 -0.0350 435 ASP A OD2 3285 N N . TRP A 411 ? 0.1961 0.2502 0.3224 -0.0401 -0.0158 -0.0365 436 TRP A N 3286 C CA . TRP A 411 ? 0.1760 0.2225 0.3043 -0.0368 -0.0153 -0.0318 436 TRP A CA 3287 C C . TRP A 411 ? 0.2205 0.2682 0.3460 -0.0326 -0.0137 -0.0273 436 TRP A C 3288 O O . TRP A 411 ? 0.1987 0.2465 0.3244 -0.0310 -0.0129 -0.0216 436 TRP A O 3289 C CB . TRP A 411 ? 0.1967 0.2325 0.3283 -0.0359 -0.0156 -0.0356 436 TRP A CB 3290 C CG . TRP A 411 ? 0.2006 0.2291 0.3329 -0.0332 -0.0155 -0.0303 436 TRP A CG 3291 C CD1 . TRP A 411 ? 0.2517 0.2766 0.3859 -0.0347 -0.0163 -0.0265 436 TRP A CD1 3292 C CD2 . TRP A 411 ? 0.2064 0.2310 0.3367 -0.0292 -0.0146 -0.0284 436 TRP A CD2 3293 N NE1 . TRP A 411 ? 0.2083 0.2275 0.3411 -0.0322 -0.0159 -0.0223 436 TRP A NE1 3294 C CE2 . TRP A 411 ? 0.2155 0.2344 0.3460 -0.0288 -0.0149 -0.0235 436 TRP A CE2 3295 C CE3 . TRP A 411 ? 0.2125 0.2384 0.3408 -0.0264 -0.0134 -0.0303 436 TRP A CE3 3296 C CZ2 . TRP A 411 ? 0.2249 0.2393 0.3532 -0.0259 -0.0144 -0.0207 436 TRP A CZ2 3297 C CZ3 . TRP A 411 ? 0.2067 0.2278 0.3335 -0.0233 -0.0129 -0.0275 436 TRP A CZ3 3298 C CH2 . TRP A 411 ? 0.2114 0.2270 0.3381 -0.0231 -0.0135 -0.0228 436 TRP A CH2 3299 N N . LEU A 412 ? 0.1951 0.2438 0.3181 -0.0310 -0.0128 -0.0301 437 LEU A N 3300 C CA . LEU A 412 ? 0.2176 0.2666 0.3381 -0.0273 -0.0113 -0.0265 437 LEU A CA 3301 C C . LEU A 412 ? 0.2095 0.2668 0.3292 -0.0273 -0.0111 -0.0208 437 LEU A C 3302 O O . LEU A 412 ? 0.1748 0.2309 0.2947 -0.0244 -0.0096 -0.0160 437 LEU A O 3303 C CB . LEU A 412 ? 0.2070 0.2566 0.3254 -0.0265 -0.0105 -0.0309 437 LEU A CB 3304 C CG . LEU A 412 ? 0.2168 0.2666 0.3327 -0.0231 -0.0089 -0.0275 437 LEU A CG 3305 C CD1 . LEU A 412 ? 0.2726 0.3141 0.3895 -0.0201 -0.0084 -0.0249 437 LEU A CD1 3306 C CD2 . LEU A 412 ? 0.2346 0.2861 0.3487 -0.0231 -0.0080 -0.0322 437 LEU A CD2 3307 N N . GLU A 413 ? 0.1972 0.2630 0.3164 -0.0307 -0.0125 -0.0214 438 GLU A N 3308 C CA . GLU A 413 ? 0.1905 0.2652 0.3106 -0.0310 -0.0131 -0.0155 438 GLU A CA 3309 C C . GLU A 413 ? 0.1875 0.2611 0.3120 -0.0298 -0.0126 -0.0106 438 GLU A C 3310 O O . GLU A 413 ? 0.1770 0.2531 0.3038 -0.0272 -0.0113 -0.0052 438 GLU A O 3311 C CB . GLU A 413 ? 0.2054 0.2897 0.3242 -0.0361 -0.0156 -0.0171 438 GLU A CB 3312 C CG . GLU A 413 ? 0.2542 0.3488 0.3749 -0.0368 -0.0172 -0.0101 438 GLU A CG 3313 C CD . GLU A 413 ? 0.3612 0.4661 0.4797 -0.0428 -0.0203 -0.0115 438 GLU A CD 3314 O OE1 . GLU A 413 ? 0.4469 0.5513 0.5607 -0.0461 -0.0204 -0.0185 438 GLU A OE1 3315 O OE2 . GLU A 413 ? 0.5090 0.6228 0.6307 -0.0443 -0.0226 -0.0057 438 GLU A OE2 3316 N N . LYS A 414 ? 0.1841 0.2539 0.3105 -0.0320 -0.0132 -0.0128 439 LYS A N 3317 C CA . LYS A 414 ? 0.1869 0.2566 0.3174 -0.0319 -0.0124 -0.0086 439 LYS A CA 3318 C C . LYS A 414 ? 0.1683 0.2304 0.2983 -0.0280 -0.0096 -0.0065 439 LYS A C 3319 O O . LYS A 414 ? 0.2025 0.2666 0.3354 -0.0267 -0.0077 -0.0022 439 LYS A O 3320 C CB . LYS A 414 ? 0.2032 0.2711 0.3356 -0.0360 -0.0141 -0.0113 439 LYS A CB 3321 C CG . LYS A 414 ? 0.2405 0.3176 0.3739 -0.0406 -0.0168 -0.0126 439 LYS A CG 3322 C CD . LYS A 414 ? 0.3778 0.4537 0.5142 -0.0449 -0.0181 -0.0143 439 LYS A CD 3323 C CE . LYS A 414 ? 0.4931 0.5584 0.6284 -0.0459 -0.0183 -0.0203 439 LYS A CE 3324 N NZ . LYS A 414 ? 0.4439 0.5073 0.5826 -0.0505 -0.0198 -0.0217 439 LYS A NZ 3325 N N . VAL A 415 ? 0.1759 0.2298 0.3025 -0.0265 -0.0092 -0.0096 440 VAL A N 3326 C CA . VAL A 415 ? 0.1656 0.2130 0.2905 -0.0234 -0.0069 -0.0077 440 VAL A CA 3327 C C . VAL A 415 ? 0.1914 0.2426 0.3163 -0.0203 -0.0046 -0.0045 440 VAL A C 3328 O O . VAL A 415 ? 0.1782 0.2281 0.3041 -0.0187 -0.0019 -0.0015 440 VAL A O 3329 C CB . VAL A 415 ? 0.1907 0.2300 0.3127 -0.0224 -0.0076 -0.0113 440 VAL A CB 3330 C CG1 . VAL A 415 ? 0.2116 0.2458 0.3308 -0.0196 -0.0054 -0.0093 440 VAL A CG1 3331 C CG2 . VAL A 415 ? 0.2384 0.2721 0.3619 -0.0250 -0.0095 -0.0135 440 VAL A CG2 3332 N N . TYR A 416 ? 0.1814 0.2369 0.3054 -0.0198 -0.0055 -0.0052 441 TYR A N 3333 C CA . TYR A 416 ? 0.1621 0.2207 0.2868 -0.0170 -0.0038 -0.0017 441 TYR A CA 3334 C C . TYR A 416 ? 0.1640 0.2293 0.2946 -0.0166 -0.0030 0.0033 441 TYR A C 3335 O O . TYR A 416 ? 0.1749 0.2396 0.3082 -0.0137 -0.0002 0.0063 441 TYR A O 3336 C CB . TYR A 416 ? 0.1931 0.2558 0.3153 -0.0174 -0.0054 -0.0030 441 TYR A CB 3337 C CG . TYR A 416 ? 0.1812 0.2448 0.3034 -0.0146 -0.0039 0.0002 441 TYR A CG 3338 C CD1 . TYR A 416 ? 0.2212 0.2776 0.3409 -0.0121 -0.0018 -0.0009 441 TYR A CD1 3339 C CD2 . TYR A 416 ? 0.2133 0.2853 0.3383 -0.0149 -0.0050 0.0047 441 TYR A CD2 3340 C CE1 . TYR A 416 ? 0.1732 0.2299 0.2932 -0.0099 -0.0004 0.0019 441 TYR A CE1 3341 C CE2 . TYR A 416 ? 0.2356 0.3080 0.3614 -0.0125 -0.0039 0.0082 441 TYR A CE2 3342 C CZ . TYR A 416 ? 0.1939 0.2585 0.3174 -0.0100 -0.0014 0.0066 441 TYR A CZ 3343 O OH . TYR A 416 ? 0.2848 0.3494 0.4096 -0.0080 -0.0002 0.0100 441 TYR A OH 3344 N N . GLU A 417 ? 0.1630 0.2349 0.2965 -0.0197 -0.0053 0.0039 442 GLU A N 3345 C CA . GLU A 417 ? 0.1848 0.2640 0.3254 -0.0195 -0.0048 0.0087 442 GLU A CA 3346 C C . GLU A 417 ? 0.1732 0.2482 0.3163 -0.0185 -0.0013 0.0094 442 GLU A C 3347 O O . GLU A 417 ? 0.1914 0.2693 0.3404 -0.0161 0.0014 0.0129 442 GLU A O 3348 C CB . GLU A 417 ? 0.1989 0.2867 0.3417 -0.0237 -0.0085 0.0090 442 GLU A CB 3349 C CG . GLU A 417 ? 0.2106 0.3070 0.3621 -0.0239 -0.0084 0.0142 442 GLU A CG 3350 C CD . GLU A 417 ? 0.3632 0.4660 0.5207 -0.0207 -0.0081 0.0199 442 GLU A CD 3351 O OE1 . GLU A 417 ? 0.3548 0.4578 0.5088 -0.0198 -0.0093 0.0204 442 GLU A OE1 3352 O OE2 . GLU A 417 ? 0.3990 0.5068 0.5655 -0.0192 -0.0066 0.0242 442 GLU A OE2 3353 N N . PHE A 418 ? 0.1775 0.2456 0.3166 -0.0204 -0.0013 0.0061 443 PHE A N 3354 C CA . PHE A 418 ? 0.1850 0.2491 0.3248 -0.0204 0.0019 0.0068 443 PHE A CA 3355 C C . PHE A 418 ? 0.1621 0.2216 0.3004 -0.0168 0.0061 0.0074 443 PHE A C 3356 O O . PHE A 418 ? 0.1737 0.2340 0.3153 -0.0161 0.0099 0.0090 443 PHE A O 3357 C CB . PHE A 418 ? 0.1783 0.2351 0.3134 -0.0233 0.0005 0.0040 443 PHE A CB 3358 C CG . PHE A 418 ? 0.1510 0.2027 0.2844 -0.0237 0.0037 0.0049 443 PHE A CG 3359 C CD1 . PHE A 418 ? 0.2069 0.2628 0.3445 -0.0256 0.0059 0.0072 443 PHE A CD1 3360 C CD2 . PHE A 418 ? 0.1729 0.2162 0.3001 -0.0227 0.0047 0.0035 443 PHE A CD2 3361 C CE1 . PHE A 418 ? 0.2170 0.2690 0.3521 -0.0267 0.0093 0.0079 443 PHE A CE1 3362 C CE2 . PHE A 418 ? 0.2145 0.2538 0.3388 -0.0240 0.0075 0.0045 443 PHE A CE2 3363 C CZ . PHE A 418 ? 0.2150 0.2585 0.3427 -0.0261 0.0100 0.0065 443 PHE A CZ 3364 N N . MET A 419 ? 0.1493 0.2040 0.2829 -0.0150 0.0056 0.0056 444 MET A N 3365 C CA . MET A 419 ? 0.1629 0.2124 0.2943 -0.0123 0.0092 0.0054 444 MET A CA 3366 C C . MET A 419 ? 0.1689 0.2228 0.3065 -0.0091 0.0118 0.0083 444 MET A C 3367 O O . MET A 419 ? 0.1579 0.2080 0.2955 -0.0070 0.0158 0.0080 444 MET A O 3368 C CB . MET A 419 ? 0.1684 0.2112 0.2931 -0.0118 0.0076 0.0025 444 MET A CB 3369 C CG . MET A 419 ? 0.1730 0.2098 0.2929 -0.0143 0.0056 0.0001 444 MET A CG 3370 S SD . MET A 419 ? 0.1987 0.2302 0.3153 -0.0159 0.0088 0.0008 444 MET A SD 3371 C CE . MET A 419 ? 0.2177 0.2445 0.3303 -0.0133 0.0119 -0.0002 444 MET A CE 3372 N N . LYS A 420 ? 0.1673 0.2294 0.3106 -0.0089 0.0094 0.0111 445 LYS A N 3373 C CA . LYS A 420 ? 0.1693 0.2360 0.3198 -0.0058 0.0107 0.0149 445 LYS A CA 3374 C C . LYS A 420 ? 0.1845 0.2498 0.3411 -0.0030 0.0164 0.0159 445 LYS A C 3375 O O . LYS A 420 ? 0.2049 0.2671 0.3632 -0.0001 0.0188 0.0163 445 LYS A O 3376 C CB . LYS A 420 ? 0.1671 0.2444 0.3239 -0.0069 0.0070 0.0189 445 LYS A CB 3377 C CG . LYS A 420 ? 0.2268 0.3092 0.3913 -0.0039 0.0069 0.0240 445 LYS A CG 3378 C CD . LYS A 420 ? 0.3101 0.4035 0.4790 -0.0060 0.0019 0.0284 445 LYS A CD 3379 C CE . LYS A 420 ? 0.4116 0.5116 0.5866 -0.0079 0.0015 0.0294 445 LYS A CE 3380 N NZ . LYS A 420 ? 0.5815 0.6933 0.7620 -0.0101 -0.0035 0.0344 445 LYS A NZ 3381 N N . PRO A 421 ? 0.1696 0.2372 0.3299 -0.0042 0.0188 0.0158 446 PRO A N 3382 C CA . PRO A 421 ? 0.1766 0.2440 0.3438 -0.0018 0.0249 0.0160 446 PRO A CA 3383 C C . PRO A 421 ? 0.2126 0.2703 0.3725 -0.0014 0.0294 0.0118 446 PRO A C 3384 O O . PRO A 421 ? 0.2017 0.2581 0.3667 0.0008 0.0349 0.0111 446 PRO A O 3385 C CB . PRO A 421 ? 0.2242 0.2967 0.3953 -0.0043 0.0263 0.0163 446 PRO A CB 3386 C CG . PRO A 421 ? 0.3059 0.3825 0.4744 -0.0076 0.0202 0.0173 446 PRO A CG 3387 C CD . PRO A 421 ? 0.1949 0.2657 0.3539 -0.0081 0.0164 0.0153 446 PRO A CD 3388 N N . PHE A 422 ? 0.1896 0.2409 0.3382 -0.0038 0.0270 0.0090 447 PHE A N 3389 C CA . PHE A 422 ? 0.2135 0.2564 0.3543 -0.0046 0.0306 0.0053 447 PHE A CA 3390 C C . PHE A 422 ? 0.2279 0.2653 0.3651 -0.0026 0.0303 0.0041 447 PHE A C 3391 O O . PHE A 422 ? 0.2306 0.2617 0.3629 -0.0029 0.0338 0.0012 447 PHE A O 3392 C CB . PHE A 422 ? 0.2044 0.2434 0.3358 -0.0087 0.0280 0.0036 447 PHE A CB 3393 C CG . PHE A 422 ? 0.1991 0.2430 0.3333 -0.0114 0.0275 0.0050 447 PHE A CG 3394 C CD1 . PHE A 422 ? 0.1924 0.2395 0.3311 -0.0121 0.0328 0.0051 447 PHE A CD1 3395 C CD2 . PHE A 422 ? 0.2016 0.2470 0.3344 -0.0136 0.0222 0.0059 447 PHE A CD2 3396 C CE1 . PHE A 422 ? 0.2780 0.3300 0.4194 -0.0150 0.0325 0.0066 447 PHE A CE1 3397 C CE2 . PHE A 422 ? 0.2223 0.2719 0.3579 -0.0166 0.0216 0.0072 447 PHE A CE2 3398 C CZ . PHE A 422 ? 0.2365 0.2896 0.3763 -0.0173 0.0267 0.0078 447 PHE A CZ 3399 N N . VAL A 423 ? 0.1852 0.2251 0.3244 -0.0011 0.0263 0.0062 448 VAL A N 3400 C CA . VAL A 423 ? 0.1858 0.2206 0.3207 0.0001 0.0254 0.0052 448 VAL A CA 3401 C C . VAL A 423 ? 0.1919 0.2286 0.3353 0.0036 0.0274 0.0080 448 VAL A C 3402 O O . VAL A 423 ? 0.2196 0.2610 0.3726 0.0054 0.0297 0.0104 448 VAL A O 3403 C CB . VAL A 423 ? 0.1793 0.2149 0.3091 -0.0013 0.0197 0.0050 448 VAL A CB 3404 C CG1 . VAL A 423 ? 0.1764 0.2091 0.2996 -0.0044 0.0178 0.0025 448 VAL A CG1 3405 C CG2 . VAL A 423 ? 0.2079 0.2520 0.3435 -0.0010 0.0164 0.0086 448 VAL A CG2 3406 N N . SER A 424 ? 0.2033 0.2364 0.3442 0.0046 0.0264 0.0078 449 SER A N 3407 C CA . SER A 424 ? 0.1756 0.2095 0.3246 0.0077 0.0279 0.0111 449 SER A CA 3408 C C . SER A 424 ? 0.1963 0.2395 0.3540 0.0088 0.0248 0.0168 449 SER A C 3409 O O . SER A 424 ? 0.1990 0.2475 0.3536 0.0066 0.0202 0.0178 449 SER A O 3410 C CB . SER A 424 ? 0.1963 0.2255 0.3404 0.0078 0.0266 0.0105 449 SER A CB 3411 O OG . SER A 424 ? 0.1968 0.2301 0.3364 0.0060 0.0213 0.0118 449 SER A OG 3412 N N . LYS A 425 ? 0.2208 0.2660 0.3899 0.0119 0.0271 0.0205 450 LYS A N 3413 C CA . LYS A 425 ? 0.2188 0.2737 0.3976 0.0128 0.0236 0.0270 450 LYS A CA 3414 C C . LYS A 425 ? 0.2670 0.3215 0.4560 0.0163 0.0245 0.0321 450 LYS A C 3415 O O . LYS A 425 ? 0.2649 0.3118 0.4565 0.0185 0.0293 0.0297 450 LYS A O 3416 C CB . LYS A 425 ? 0.3864 0.4473 0.5725 0.0130 0.0251 0.0276 450 LYS A CB 3417 C CG . LYS A 425 ? 0.4544 0.5105 0.6449 0.0148 0.0324 0.0237 450 LYS A CG 3418 C CD . LYS A 425 ? 0.3822 0.4446 0.5777 0.0138 0.0339 0.0235 450 LYS A CD 3419 C CE . LYS A 425 ? 0.3625 0.4227 0.5452 0.0094 0.0327 0.0191 450 LYS A CE 3420 N NZ . LYS A 425 ? 0.3132 0.3641 0.4875 0.0084 0.0378 0.0131 450 LYS A NZ 3421 N N . ASN A 426 ? 0.2595 0.3223 0.4544 0.0163 0.0196 0.0391 451 ASN A N 3422 C CA . ASN A 426 ? 0.2749 0.3385 0.4811 0.0194 0.0193 0.0457 451 ASN A CA 3423 C C . ASN A 426 ? 0.3208 0.3754 0.5222 0.0198 0.0206 0.0445 451 ASN A C 3424 O O . ASN A 426 ? 0.3731 0.4212 0.5825 0.0230 0.0251 0.0443 451 ASN A O 3425 C CB . ASN A 426 ? 0.3386 0.4024 0.5607 0.0236 0.0241 0.0470 451 ASN A CB 3426 C CG . ASN A 426 ? 0.4260 0.4999 0.6547 0.0231 0.0227 0.0490 451 ASN A CG 3427 O OD1 . ASN A 426 ? 0.4317 0.5153 0.6634 0.0217 0.0167 0.0553 451 ASN A OD1 3428 N ND2 . ASN A 426 ? 0.4252 0.4971 0.6557 0.0238 0.0282 0.0436 451 ASN A ND2 3429 N N . PRO A 427 ? 0.2505 0.3049 0.4395 0.0164 0.0169 0.0434 452 PRO A N 3430 C CA . PRO A 427 ? 0.2229 0.2843 0.4029 0.0125 0.0121 0.0427 452 PRO A CA 3431 C C . PRO A 427 ? 0.2262 0.2825 0.3947 0.0104 0.0139 0.0343 452 PRO A C 3432 O O . PRO A 427 ? 0.2176 0.2651 0.3832 0.0115 0.0181 0.0294 452 PRO A O 3433 C CB . PRO A 427 ? 0.2488 0.3121 0.4231 0.0102 0.0082 0.0460 452 PRO A CB 3434 C CG . PRO A 427 ? 0.2770 0.3302 0.4510 0.0120 0.0119 0.0442 452 PRO A CG 3435 C CD . PRO A 427 ? 0.2675 0.3151 0.4519 0.0161 0.0173 0.0431 452 PRO A CD 3436 N N . ARG A 428 ? 0.1948 0.2566 0.3571 0.0073 0.0103 0.0328 453 ARG A N 3437 C CA . ARG A 428 ? 0.1536 0.2107 0.3057 0.0051 0.0109 0.0258 453 ARG A CA 3438 C C . ARG A 428 ? 0.1890 0.2414 0.3329 0.0040 0.0102 0.0233 453 ARG A C 3439 O O . ARG A 428 ? 0.1958 0.2531 0.3368 0.0020 0.0069 0.0254 453 ARG A O 3440 C CB . ARG A 428 ? 0.1874 0.2512 0.3366 0.0021 0.0074 0.0249 453 ARG A CB 3441 C CG . ARG A 428 ? 0.1541 0.2128 0.2954 0.0002 0.0080 0.0184 453 ARG A CG 3442 C CD . ARG A 428 ? 0.1674 0.2322 0.3086 -0.0025 0.0052 0.0178 453 ARG A CD 3443 N NE . ARG A 428 ? 0.1603 0.2197 0.2957 -0.0041 0.0057 0.0125 453 ARG A NE 3444 C CZ . ARG A 428 ? 0.1856 0.2478 0.3209 -0.0065 0.0040 0.0113 453 ARG A CZ 3445 N NH1 . ARG A 428 ? 0.2050 0.2760 0.3452 -0.0079 0.0017 0.0145 453 ARG A NH1 3446 N NH2 . ARG A 428 ? 0.1533 0.2097 0.2839 -0.0079 0.0043 0.0072 453 ARG A NH2 3447 N N . LEU A 429 ? 0.1751 0.2187 0.3151 0.0048 0.0135 0.0188 454 LEU A N 3448 C CA . LEU A 429 ? 0.1885 0.2274 0.3226 0.0041 0.0135 0.0169 454 LEU A CA 3449 C C . LEU A 429 ? 0.1874 0.2276 0.3132 0.0012 0.0107 0.0129 454 LEU A C 3450 O O . LEU A 429 ? 0.1925 0.2338 0.3161 0.0000 0.0096 0.0101 454 LEU A O 3451 C CB . LEU A 429 ? 0.1722 0.2017 0.3052 0.0054 0.0178 0.0134 454 LEU A CB 3452 C CG . LEU A 429 ? 0.1887 0.2160 0.3309 0.0084 0.0218 0.0159 454 LEU A CG 3453 C CD1 . LEU A 429 ? 0.2578 0.2759 0.3972 0.0087 0.0264 0.0109 454 LEU A CD1 3454 C CD2 . LEU A 429 ? 0.2478 0.2772 0.3966 0.0097 0.0207 0.0218 454 LEU A CD2 3455 N N . GLY A 430 ? 0.1679 0.2078 0.2901 0.0002 0.0097 0.0126 455 GLY A N 3456 C CA . GLY A 430 ? 0.1676 0.2086 0.2833 -0.0022 0.0077 0.0082 455 GLY A CA 3457 C C . GLY A 430 ? 0.1578 0.1941 0.2701 -0.0024 0.0088 0.0060 455 GLY A C 3458 O O . GLY A 430 ? 0.1650 0.1960 0.2791 -0.0010 0.0111 0.0073 455 GLY A O 3459 N N . TYR A 431 ? 0.1488 0.1872 0.2570 -0.0044 0.0072 0.0025 456 TYR A N 3460 C CA . TYR A 431 ? 0.1684 0.2032 0.2738 -0.0049 0.0080 -0.0002 456 TYR A CA 3461 C C . TYR A 431 ? 0.1743 0.2159 0.2775 -0.0074 0.0065 -0.0014 456 TYR A C 3462 O O . TYR A 431 ? 0.1652 0.2110 0.2673 -0.0087 0.0051 -0.0043 456 TYR A O 3463 C CB . TYR A 431 ? 0.1720 0.2013 0.2755 -0.0045 0.0080 -0.0050 456 TYR A CB 3464 C CG . TYR A 431 ? 0.1687 0.1952 0.2701 -0.0053 0.0079 -0.0083 456 TYR A CG 3465 C CD1 . TYR A 431 ? 0.1666 0.1925 0.2677 -0.0057 0.0091 -0.0070 456 TYR A CD1 3466 C CD2 . TYR A 431 ? 0.2007 0.2253 0.3013 -0.0055 0.0064 -0.0123 456 TYR A CD2 3467 C CE1 . TYR A 431 ? 0.1970 0.2212 0.2969 -0.0066 0.0089 -0.0101 456 TYR A CE1 3468 C CE2 . TYR A 431 ? 0.2234 0.2462 0.3235 -0.0061 0.0060 -0.0149 456 TYR A CE2 3469 C CZ . TYR A 431 ? 0.1875 0.2105 0.2872 -0.0067 0.0073 -0.0140 456 TYR A CZ 3470 O OH . TYR A 431 ? 0.1770 0.1990 0.2768 -0.0075 0.0068 -0.0166 456 TYR A OH 3471 N N . VAL A 432 ? 0.1343 0.1771 0.2369 -0.0084 0.0072 0.0007 457 VAL A N 3472 C CA . VAL A 432 ? 0.1469 0.1976 0.2470 -0.0114 0.0063 0.0002 457 VAL A CA 3473 C C . VAL A 432 ? 0.1844 0.2365 0.2826 -0.0126 0.0062 -0.0068 457 VAL A C 3474 O O . VAL A 432 ? 0.1978 0.2570 0.2942 -0.0151 0.0057 -0.0091 457 VAL A O 3475 C CB . VAL A 432 ? 0.1331 0.1852 0.2329 -0.0128 0.0071 0.0045 457 VAL A CB 3476 C CG1 . VAL A 432 ? 0.1460 0.1932 0.2452 -0.0127 0.0087 0.0014 457 VAL A CG1 3477 C CG2 . VAL A 432 ? 0.1592 0.2213 0.2557 -0.0167 0.0059 0.0060 457 VAL A CG2 3478 N N . ASN A 433 ? 0.1570 0.2027 0.2561 -0.0109 0.0067 -0.0104 458 ASN A N 3479 C CA . ASN A 433 ? 0.1782 0.2250 0.2779 -0.0114 0.0063 -0.0166 458 ASN A CA 3480 C C . ASN A 433 ? 0.1838 0.2317 0.2844 -0.0113 0.0049 -0.0192 458 ASN A C 3481 O O . ASN A 433 ? 0.2054 0.2552 0.3075 -0.0119 0.0046 -0.0244 458 ASN A O 3482 C CB . ASN A 433 ? 0.1541 0.1944 0.2553 -0.0100 0.0064 -0.0188 458 ASN A CB 3483 C CG . ASN A 433 ? 0.1662 0.2084 0.2676 -0.0112 0.0076 -0.0198 458 ASN A CG 3484 O OD1 . ASN A 433 ? 0.1717 0.2208 0.2725 -0.0134 0.0084 -0.0210 458 ASN A OD1 3485 N ND2 . ASN A 433 ? 0.1707 0.2074 0.2727 -0.0105 0.0077 -0.0195 458 ASN A ND2 3486 N N . HIS A 434 ? 0.1810 0.2275 0.2816 -0.0104 0.0043 -0.0156 459 HIS A N 3487 C CA A HIS A 434 ? 0.1910 0.2389 0.2924 -0.0108 0.0029 -0.0173 459 HIS A CA 3488 C CA B HIS A 434 ? 0.1915 0.2392 0.2929 -0.0107 0.0029 -0.0171 459 HIS A CA 3489 C C . HIS A 434 ? 0.2139 0.2695 0.3140 -0.0130 0.0023 -0.0145 459 HIS A C 3490 O O . HIS A 434 ? 0.2293 0.2860 0.3304 -0.0128 0.0013 -0.0117 459 HIS A O 3491 C CB A HIS A 434 ? 0.2253 0.2668 0.3280 -0.0087 0.0026 -0.0155 459 HIS A CB 3492 C CB B HIS A 434 ? 0.2248 0.2663 0.3275 -0.0086 0.0028 -0.0146 459 HIS A CB 3493 C CG A HIS A 434 ? 0.2214 0.2559 0.3246 -0.0074 0.0025 -0.0178 459 HIS A CG 3494 C CG B HIS A 434 ? 0.2332 0.2712 0.3372 -0.0084 0.0015 -0.0180 459 HIS A CG 3495 N ND1 A HIS A 434 ? 0.3207 0.3550 0.4249 -0.0076 0.0022 -0.0215 459 HIS A ND1 3496 N ND1 B HIS A 434 ? 0.3279 0.3689 0.4330 -0.0096 0.0002 -0.0195 459 HIS A ND1 3497 C CD2 A HIS A 434 ? 0.3075 0.3358 0.4106 -0.0063 0.0024 -0.0167 459 HIS A CD2 3498 C CD2 B HIS A 434 ? 0.1547 0.1863 0.2594 -0.0073 0.0009 -0.0197 459 HIS A CD2 3499 C CE1 A HIS A 434 ? 0.2921 0.3202 0.3969 -0.0066 0.0014 -0.0221 459 HIS A CE1 3500 C CE1 B HIS A 434 ? 0.2997 0.3357 0.4065 -0.0092 -0.0009 -0.0219 459 HIS A CE1 3501 N NE2 A HIS A 434 ? 0.3159 0.3403 0.4193 -0.0061 0.0015 -0.0192 459 HIS A NE2 3502 N NE2 B HIS A 434 ? 0.2512 0.2817 0.3578 -0.0078 -0.0007 -0.0217 459 HIS A NE2 3503 N N . ILE A 435 ? 0.2391 0.3009 0.3367 -0.0154 0.0028 -0.0150 460 ILE A N 3504 C CA A ILE A 435 ? 0.2176 0.2880 0.3129 -0.0185 0.0018 -0.0116 460 ILE A CA 3505 C CA B ILE A 435 ? 0.1979 0.2682 0.2933 -0.0185 0.0018 -0.0116 460 ILE A CA 3506 C C . ILE A 435 ? 0.2475 0.3213 0.3428 -0.0200 0.0001 -0.0133 460 ILE A C 3507 O O . ILE A 435 ? 0.2640 0.3368 0.3598 -0.0207 0.0002 -0.0198 460 ILE A O 3508 C CB A ILE A 435 ? 0.2540 0.3311 0.3456 -0.0221 0.0028 -0.0139 460 ILE A CB 3509 C CB B ILE A 435 ? 0.2443 0.3215 0.3359 -0.0220 0.0027 -0.0136 460 ILE A CB 3510 C CG1 A ILE A 435 ? 0.2784 0.3644 0.3666 -0.0257 0.0014 -0.0082 460 ILE A CG1 3511 C CG1 B ILE A 435 ? 0.2842 0.3707 0.3723 -0.0260 0.0011 -0.0090 460 ILE A CG1 3512 C CG2 A ILE A 435 ? 0.2946 0.3738 0.3859 -0.0238 0.0037 -0.0227 460 ILE A CG2 3513 C CG2 B ILE A 435 ? 0.2826 0.3607 0.3742 -0.0232 0.0039 -0.0225 460 ILE A CG2 3514 C CD1 A ILE A 435 ? 0.2817 0.3750 0.3673 -0.0293 -0.0002 -0.0104 460 ILE A CD1 3515 C CD1 B ILE A 435 ? 0.3223 0.4153 0.4062 -0.0296 0.0021 -0.0077 460 ILE A CD1 3516 N N . ASP A 436 ? 0.2125 0.2454 0.3268 -0.0169 -0.0143 0.0273 461 ASP A N 3517 C CA . ASP A 436 ? 0.2434 0.2850 0.3639 -0.0217 -0.0198 0.0298 461 ASP A CA 3518 C C . ASP A 436 ? 0.2030 0.2504 0.3249 -0.0187 -0.0228 0.0306 461 ASP A C 3519 O O . ASP A 436 ? 0.2208 0.2767 0.3461 -0.0138 -0.0197 0.0327 461 ASP A O 3520 C CB . ASP A 436 ? 0.3009 0.3552 0.4297 -0.0238 -0.0172 0.0338 461 ASP A CB 3521 C CG . ASP A 436 ? 0.4347 0.4982 0.5705 -0.0309 -0.0230 0.0372 461 ASP A CG 3522 O OD1 . ASP A 436 ? 0.3073 0.3692 0.4423 -0.0330 -0.0290 0.0363 461 ASP A OD1 3523 O OD2 . ASP A 436 ? 0.4710 0.5437 0.6129 -0.0347 -0.0217 0.0410 461 ASP A OD2 3524 N N . LEU A 437 ? 0.1988 0.2418 0.3176 -0.0210 -0.0292 0.0285 462 LEU A N 3525 C CA . LEU A 437 ? 0.2220 0.2705 0.3412 -0.0178 -0.0326 0.0287 462 LEU A CA 3526 C C . LEU A 437 ? 0.2157 0.2793 0.3439 -0.0210 -0.0359 0.0322 462 LEU A C 3527 O O . LEU A 437 ? 0.2583 0.3295 0.3880 -0.0181 -0.0383 0.0329 462 LEU A O 3528 C CB . LEU A 437 ? 0.2204 0.2596 0.3322 -0.0183 -0.0385 0.0247 462 LEU A CB 3529 C CG . LEU A 437 ? 0.2902 0.3184 0.3929 -0.0135 -0.0354 0.0218 462 LEU A CG 3530 C CD1 . LEU A 437 ? 0.3411 0.3634 0.4366 -0.0125 -0.0417 0.0180 462 LEU A CD1 3531 C CD2 . LEU A 437 ? 0.2821 0.3138 0.3850 -0.0067 -0.0296 0.0240 462 LEU A CD2 3532 N N . ASP A 438 ? 0.2331 0.3025 0.3676 -0.0270 -0.0359 0.0350 463 ASP A N 3533 C CA . ASP A 438 ? 0.2129 0.2995 0.3568 -0.0305 -0.0386 0.0393 463 ASP A CA 3534 C C . ASP A 438 ? 0.3481 0.4473 0.4954 -0.0225 -0.0331 0.0421 463 ASP A C 3535 O O . ASP A 438 ? 0.4351 0.5501 0.5888 -0.0224 -0.0351 0.0452 463 ASP A O 3536 C CB . ASP A 438 ? 0.2638 0.3555 0.4140 -0.0384 -0.0390 0.0428 463 ASP A CB 3537 C CG . ASP A 438 ? 0.4272 0.5063 0.5744 -0.0467 -0.0456 0.0407 463 ASP A CG 3538 O OD1 . ASP A 438 ? 0.5237 0.5913 0.6640 -0.0459 -0.0503 0.0362 463 ASP A OD1 3539 O OD2 . ASP A 438 ? 0.4206 0.5014 0.5721 -0.0534 -0.0461 0.0439 463 ASP A OD2 3540 N N . LEU A 439 ? 0.3143 0.4065 0.4571 -0.0158 -0.0264 0.0408 464 LEU A N 3541 C CA . LEU A 439 ? 0.3724 0.4725 0.5166 -0.0072 -0.0211 0.0428 464 LEU A CA 3542 C C . LEU A 439 ? 0.4165 0.5175 0.5580 -0.0016 -0.0230 0.0425 464 LEU A C 3543 O O . LEU A 439 ? 0.5320 0.6413 0.6751 0.0056 -0.0199 0.0448 464 LEU A O 3544 C CB . LEU A 439 ? 0.3904 0.4794 0.5293 -0.0022 -0.0144 0.0409 464 LEU A CB 3545 C CG . LEU A 439 ? 0.3988 0.4892 0.5400 -0.0051 -0.0110 0.0414 464 LEU A CG 3546 C CD1 . LEU A 439 ? 0.3272 0.4029 0.4614 -0.0016 -0.0059 0.0379 464 LEU A CD1 3547 C CD2 . LEU A 439 ? 0.4806 0.5894 0.6292 -0.0020 -0.0085 0.0455 464 LEU A CD2 3548 N N . GLY A 440 ? 0.3401 0.4329 0.4771 -0.0044 -0.0281 0.0396 465 GLY A N 3549 C CA . GLY A 440 ? 0.2708 0.3647 0.4048 0.0009 -0.0301 0.0391 465 GLY A CA 3550 C C . GLY A 440 ? 0.2308 0.3088 0.3556 0.0042 -0.0286 0.0360 465 GLY A C 3551 O O . GLY A 440 ? 0.2631 0.3294 0.3839 0.0018 -0.0266 0.0338 465 GLY A O 3552 N N . GLY A 441 ? 0.2218 0.3008 0.3432 0.0098 -0.0296 0.0363 466 GLY A N 3553 C CA . GLY A 441 ? 0.2213 0.2881 0.3344 0.0131 -0.0283 0.0344 466 GLY A CA 3554 C C . GLY A 441 ? 0.2335 0.3050 0.3444 0.0202 -0.0287 0.0364 466 GLY A C 3555 O O . GLY A 441 ? 0.2925 0.3766 0.4074 0.0217 -0.0320 0.0378 466 GLY A O 3556 N N . ILE A 442 ? 0.1988 0.2611 0.3036 0.0245 -0.0252 0.0369 467 ILE A N 3557 C CA . ILE A 442 ? 0.2079 0.2734 0.3098 0.0314 -0.0251 0.0397 467 ILE A CA 3558 C C . ILE A 442 ? 0.2186 0.2834 0.3148 0.0312 -0.0299 0.0371 467 ILE A C 3559 O O . ILE A 442 ? 0.2492 0.3046 0.3402 0.0285 -0.0301 0.0344 467 ILE A O 3560 C CB . ILE A 442 ? 0.2631 0.3187 0.3613 0.0359 -0.0186 0.0427 467 ILE A CB 3561 C CG1 . ILE A 442 ? 0.3473 0.4029 0.4498 0.0381 -0.0138 0.0449 467 ILE A CG1 3562 C CG2 . ILE A 442 ? 0.2502 0.3083 0.3448 0.0424 -0.0186 0.0463 467 ILE A CG2 3563 C CD1 . ILE A 442 ? 0.3480 0.4166 0.4551 0.0438 -0.0142 0.0482 467 ILE A CD1 3564 N N . ASP A 443 ? 0.2485 0.3241 0.3453 0.0348 -0.0340 0.0379 468 ASP A N 3565 C CA . ASP A 443 ? 0.2647 0.3413 0.3552 0.0374 -0.0379 0.0362 468 ASP A CA 3566 C C . ASP A 443 ? 0.2516 0.3278 0.3387 0.0446 -0.0333 0.0414 468 ASP A C 3567 O O . ASP A 443 ? 0.2182 0.3033 0.3079 0.0501 -0.0324 0.0454 468 ASP A O 3568 C CB . ASP A 443 ? 0.2489 0.3379 0.3414 0.0377 -0.0450 0.0340 468 ASP A CB 3569 C CG . ASP A 443 ? 0.2341 0.3258 0.3196 0.0419 -0.0494 0.0319 468 ASP A CG 3570 O OD1 . ASP A 443 ? 0.2676 0.3529 0.3468 0.0447 -0.0465 0.0330 468 ASP A OD1 3571 O OD2 . ASP A 443 ? 0.3042 0.4055 0.3903 0.0424 -0.0558 0.0292 468 ASP A OD2 3572 N N . TRP A 444 ? 0.2462 0.3126 0.3277 0.0443 -0.0304 0.0418 469 TRP A N 3573 C CA . TRP A 444 ? 0.1921 0.2563 0.2706 0.0496 -0.0258 0.0476 469 TRP A CA 3574 C C . TRP A 444 ? 0.2116 0.2868 0.2871 0.0558 -0.0288 0.0499 469 TRP A C 3575 O O . TRP A 444 ? 0.2793 0.3548 0.3529 0.0607 -0.0254 0.0559 469 TRP A O 3576 C CB . TRP A 444 ? 0.2799 0.3322 0.3537 0.0465 -0.0223 0.0476 469 TRP A CB 3577 C CG . TRP A 444 ? 0.2064 0.2484 0.2831 0.0418 -0.0183 0.0464 469 TRP A CG 3578 C CD1 . TRP A 444 ? 0.2425 0.2789 0.3191 0.0357 -0.0191 0.0415 469 TRP A CD1 3579 C CD2 . TRP A 444 ? 0.2253 0.2618 0.3051 0.0435 -0.0132 0.0500 469 TRP A CD2 3580 N NE1 . TRP A 444 ? 0.2302 0.2594 0.3100 0.0335 -0.0145 0.0419 469 TRP A NE1 3581 C CE2 . TRP A 444 ? 0.2371 0.2658 0.3186 0.0384 -0.0110 0.0467 469 TRP A CE2 3582 C CE3 . TRP A 444 ? 0.2412 0.2783 0.3220 0.0495 -0.0103 0.0557 469 TRP A CE3 3583 C CZ2 . TRP A 444 ? 0.2262 0.2482 0.3102 0.0393 -0.0064 0.0482 469 TRP A CZ2 3584 C CZ3 . TRP A 444 ? 0.2574 0.2862 0.3402 0.0505 -0.0058 0.0572 469 TRP A CZ3 3585 C CH2 . TRP A 444 ? 0.2361 0.2577 0.3204 0.0455 -0.0040 0.0532 469 TRP A CH2 3586 N N . GLY A 445 ? 0.2520 0.3359 0.3269 0.0557 -0.0353 0.0453 470 GLY A N 3587 C CA . GLY A 445 ? 0.2854 0.3815 0.3574 0.0621 -0.0388 0.0466 470 GLY A CA 3588 C C . GLY A 445 ? 0.2739 0.3823 0.3513 0.0660 -0.0402 0.0488 470 GLY A C 3589 O O . GLY A 445 ? 0.3037 0.4242 0.3794 0.0718 -0.0431 0.0500 470 GLY A O 3590 N N . ASN A 446 ? 0.2527 0.3596 0.3366 0.0632 -0.0381 0.0493 471 ASN A N 3591 C CA . ASN A 446 ? 0.2257 0.3458 0.3154 0.0662 -0.0394 0.0511 471 ASN A CA 3592 C C . ASN A 446 ? 0.2507 0.3697 0.3422 0.0723 -0.0328 0.0585 471 ASN A C 3593 O O . ASN A 446 ? 0.2316 0.3414 0.3254 0.0703 -0.0282 0.0597 471 ASN A O 3594 C CB . ASN A 446 ? 0.2206 0.3421 0.3164 0.0590 -0.0424 0.0468 471 ASN A CB 3595 C CG . ASN A 446 ? 0.2496 0.3878 0.3517 0.0610 -0.0450 0.0480 471 ASN A CG 3596 O OD1 . ASN A 446 ? 0.2959 0.4409 0.3998 0.0679 -0.0413 0.0535 471 ASN A OD1 3597 N ND2 . ASN A 446 ? 0.3122 0.4571 0.4176 0.0549 -0.0518 0.0431 471 ASN A ND2 3598 N N . LYS A 447 ? 0.2506 0.3790 0.3406 0.0802 -0.0324 0.0633 472 LYS A N 3599 C CA . LYS A 447 ? 0.2830 0.4080 0.3728 0.0869 -0.0263 0.0709 472 LYS A CA 3600 C C . LYS A 447 ? 0.2414 0.3679 0.3369 0.0882 -0.0236 0.0722 472 LYS A C 3601 O O . LYS A 447 ? 0.2780 0.3927 0.3729 0.0902 -0.0181 0.0757 472 LYS A O 3602 C CB . LYS A 447 ? 0.4083 0.5458 0.4959 0.0954 -0.0272 0.0760 472 LYS A CB 3603 C CG . LYS A 447 ? 0.6528 0.7813 0.7361 0.1006 -0.0217 0.0840 472 LYS A CG 3604 C CD . LYS A 447 ? 0.7678 0.8876 0.8532 0.1042 -0.0162 0.0889 472 LYS A CD 3605 C CE . LYS A 447 ? 0.8379 0.9473 0.9188 0.1089 -0.0115 0.0974 472 LYS A CE 3606 N NZ . LYS A 447 ? 0.8627 0.9861 0.9414 0.1162 -0.0130 0.1029 472 LYS A NZ 3607 N N . THR A 448 ? 0.2305 0.3721 0.3312 0.0875 -0.0276 0.0696 473 THR A N 3608 C CA . THR A 448 ? 0.1880 0.3352 0.2943 0.0897 -0.0252 0.0714 473 THR A CA 3609 C C . THR A 448 ? 0.2060 0.3403 0.3140 0.0834 -0.0224 0.0686 473 THR A C 3610 O O . THR A 448 ? 0.2130 0.3429 0.3221 0.0871 -0.0177 0.0713 473 THR A O 3611 C CB . THR A 448 ? 0.2286 0.3974 0.3408 0.0893 -0.0306 0.0696 473 THR A CB 3612 O OG1 . THR A 448 ? 0.2552 0.4316 0.3723 0.0930 -0.0276 0.0725 473 THR A OG1 3613 C CG2 . THR A 448 ? 0.2933 0.4636 0.4081 0.0787 -0.0366 0.0626 473 THR A CG2 3614 N N . VAL A 449 ? 0.2077 0.3357 0.3151 0.0745 -0.0254 0.0632 474 VAL A N 3615 C CA . VAL A 449 ? 0.2069 0.3231 0.3155 0.0684 -0.0228 0.0605 474 VAL A CA 3616 C C . VAL A 449 ? 0.1989 0.2972 0.3024 0.0707 -0.0168 0.0630 474 VAL A C 3617 O O . VAL A 449 ? 0.2265 0.3178 0.3312 0.0718 -0.0125 0.0638 474 VAL A O 3618 C CB . VAL A 449 ? 0.2037 0.3171 0.3123 0.0589 -0.0276 0.0544 474 VAL A CB 3619 C CG1 . VAL A 449 ? 0.2294 0.3283 0.3374 0.0533 -0.0242 0.0522 474 VAL A CG1 3620 C CG2 . VAL A 449 ? 0.2462 0.3752 0.3611 0.0547 -0.0334 0.0521 474 VAL A CG2 3621 N N . VAL A 450 ? 0.2044 0.2961 0.3023 0.0717 -0.0169 0.0643 475 VAL A N 3622 C CA . VAL A 450 ? 0.2282 0.3032 0.3214 0.0726 -0.0118 0.0671 475 VAL A CA 3623 C C . VAL A 450 ? 0.2065 0.2775 0.2996 0.0805 -0.0072 0.0727 475 VAL A C 3624 O O . VAL A 450 ? 0.2564 0.3126 0.3477 0.0803 -0.0030 0.0733 475 VAL A O 3625 C CB . VAL A 450 ? 0.2741 0.3461 0.3616 0.0724 -0.0129 0.0686 475 VAL A CB 3626 C CG1 . VAL A 450 ? 0.3098 0.3657 0.3933 0.0728 -0.0078 0.0727 475 VAL A CG1 3627 C CG2 . VAL A 450 ? 0.2631 0.3358 0.3493 0.0653 -0.0171 0.0624 475 VAL A CG2 3628 N N . ASN A 451 ? 0.2074 0.2912 0.3021 0.0879 -0.0081 0.0765 476 ASN A N 3629 C CA . ASN A 451 ? 0.2418 0.3223 0.3359 0.0967 -0.0040 0.0817 476 ASN A CA 3630 C C . ASN A 451 ? 0.2178 0.2935 0.3146 0.0966 -0.0013 0.0793 476 ASN A C 3631 O O . ASN A 451 ? 0.2941 0.3573 0.3880 0.1018 0.0027 0.0819 476 ASN A O 3632 C CB . ASN A 451 ? 0.2673 0.3663 0.3636 0.1045 -0.0060 0.0854 476 ASN A CB 3633 C CG . ASN A 451 ? 0.3898 0.4904 0.4819 0.1090 -0.0064 0.0907 476 ASN A CG 3634 O OD1 . ASN A 451 ? 0.4066 0.4927 0.4941 0.1079 -0.0041 0.0935 476 ASN A OD1 3635 N ND2 . ASN A 451 ? 0.4406 0.5600 0.5345 0.1140 -0.0094 0.0923 476 ASN A ND2 3636 N N . ASN A 452 ? 0.2160 0.3015 0.3178 0.0909 -0.0039 0.0743 477 ASN A N 3637 C CA . ASN A 452 ? 0.2370 0.3228 0.3421 0.0911 -0.0017 0.0723 477 ASN A CA 3638 C C . ASN A 452 ? 0.2474 0.3227 0.3526 0.0820 -0.0012 0.0672 477 ASN A C 3639 O O . ASN A 452 ? 0.2040 0.2851 0.3135 0.0792 -0.0012 0.0645 477 ASN A O 3640 C CB . ASN A 452 ? 0.2056 0.3142 0.3175 0.0920 -0.0046 0.0720 477 ASN A CB 3641 C CG . ASN A 452 ? 0.2289 0.3419 0.3440 0.0957 -0.0018 0.0719 477 ASN A CG 3642 O OD1 . ASN A 452 ? 0.2172 0.3179 0.3283 0.1023 0.0026 0.0733 477 ASN A OD1 3643 N ND2 . ASN A 452 ? 0.2492 0.3802 0.3711 0.0917 -0.0045 0.0704 477 ASN A ND2 3644 N N . ALA A 453 ? 0.2155 0.2767 0.3160 0.0775 -0.0009 0.0663 478 ALA A N 3645 C CA . ALA A 453 ? 0.1818 0.2347 0.2819 0.0686 -0.0012 0.0614 478 ALA A CA 3646 C C . ALA A 453 ? 0.2074 0.2515 0.3079 0.0685 0.0027 0.0593 478 ALA A C 3647 O O . ALA A 453 ? 0.2132 0.2587 0.3163 0.0623 0.0021 0.0554 478 ALA A O 3648 C CB . ALA A 453 ? 0.2435 0.2848 0.3381 0.0651 -0.0012 0.0616 478 ALA A CB 3649 N N . ILE A 454 ? 0.2274 0.2619 0.3249 0.0756 0.0064 0.0620 479 ILE A N 3650 C CA . ILE A 454 ? 0.2287 0.2539 0.3256 0.0765 0.0098 0.0593 479 ILE A CA 3651 C C . ILE A 454 ? 0.2430 0.2841 0.3458 0.0779 0.0095 0.0576 479 ILE A C 3652 O O . ILE A 454 ? 0.2451 0.2859 0.3498 0.0729 0.0101 0.0539 479 ILE A O 3653 C CB . ILE A 454 ? 0.2810 0.2901 0.3723 0.0841 0.0132 0.0620 479 ILE A CB 3654 C CG1 . ILE A 454 ? 0.3116 0.3041 0.3976 0.0798 0.0135 0.0635 479 ILE A CG1 3655 C CG2 . ILE A 454 ? 0.3268 0.3287 0.4173 0.0869 0.0160 0.0585 479 ILE A CG2 3656 C CD1 . ILE A 454 ? 0.4182 0.3914 0.4985 0.0852 0.0164 0.0661 479 ILE A CD1 3657 N N . GLU A 455 ? 0.2126 0.2692 0.3186 0.0843 0.0084 0.0608 480 GLU A N 3658 C CA A GLU A 455 ? 0.2254 0.3004 0.3377 0.0854 0.0080 0.0602 480 GLU A CA 3659 C CA B GLU A 455 ? 0.2256 0.3006 0.3380 0.0854 0.0080 0.0602 480 GLU A CA 3660 C C . GLU A 455 ? 0.2413 0.3269 0.3591 0.0746 0.0043 0.0577 480 GLU A C 3661 O O . GLU A 455 ? 0.2351 0.3267 0.3568 0.0711 0.0048 0.0557 480 GLU A O 3662 C CB A GLU A 455 ? 0.2196 0.3109 0.3342 0.0942 0.0072 0.0646 480 GLU A CB 3663 C CB B GLU A 455 ? 0.2422 0.3340 0.3570 0.0942 0.0073 0.0645 480 GLU A CB 3664 C CG A GLU A 455 ? 0.2627 0.3769 0.3846 0.0947 0.0063 0.0650 480 GLU A CG 3665 C CG B GLU A 455 ? 0.2964 0.4080 0.4174 0.0965 0.0075 0.0647 480 GLU A CG 3666 C CD A GLU A 455 ? 0.3424 0.4552 0.4638 0.1000 0.0102 0.0636 480 GLU A CD 3667 C CD B GLU A 455 ? 0.2975 0.4323 0.4233 0.1011 0.0052 0.0686 480 GLU A CD 3668 O OE1 A GLU A 455 ? 0.2639 0.3567 0.3786 0.1046 0.0135 0.0621 480 GLU A OE1 3669 O OE1 B GLU A 455 ? 0.3211 0.4683 0.4484 0.1098 0.0072 0.0707 480 GLU A OE1 3670 O OE2 A GLU A 455 ? 0.3922 0.5244 0.5197 0.0997 0.0098 0.0641 480 GLU A OE2 3671 O OE2 B GLU A 455 ? 0.3766 0.5183 0.5044 0.0965 0.0012 0.0695 480 GLU A OE2 3672 N N . ILE A 456 ? 0.2006 0.2885 0.3186 0.0697 0.0003 0.0579 481 ILE A N 3673 C CA . ILE A 456 ? 0.1947 0.2905 0.3170 0.0598 -0.0041 0.0553 481 ILE A CA 3674 C C . ILE A 456 ? 0.2236 0.3074 0.3445 0.0526 -0.0028 0.0514 481 ILE A C 3675 O O . ILE A 456 ? 0.2333 0.3245 0.3589 0.0466 -0.0042 0.0500 481 ILE A O 3676 C CB . ILE A 456 ? 0.1859 0.2826 0.3064 0.0570 -0.0086 0.0552 481 ILE A CB 3677 C CG1 . ILE A 456 ? 0.2046 0.3174 0.3277 0.0631 -0.0108 0.0587 481 ILE A CG1 3678 C CG2 . ILE A 456 ? 0.2500 0.3492 0.3729 0.0467 -0.0135 0.0516 481 ILE A CG2 3679 C CD1 . ILE A 456 ? 0.2336 0.3475 0.3539 0.0623 -0.0150 0.0586 481 ILE A CD1 3680 N N . SER A 457 ? 0.1875 0.2532 0.3020 0.0533 0.0000 0.0503 482 SER A N 3681 C CA A SER A 457 ? 0.1940 0.2482 0.3063 0.0467 0.0012 0.0465 482 SER A CA 3682 C CA B SER A 457 ? 0.1812 0.2351 0.2934 0.0467 0.0012 0.0465 482 SER A CA 3683 C C . SER A 457 ? 0.2349 0.2886 0.3489 0.0481 0.0049 0.0451 482 SER A C 3684 O O . SER A 457 ? 0.2421 0.2900 0.3556 0.0426 0.0058 0.0420 482 SER A O 3685 C CB A SER A 457 ? 0.2003 0.2374 0.3055 0.0465 0.0027 0.0461 482 SER A CB 3686 C CB B SER A 457 ? 0.1920 0.2287 0.2971 0.0469 0.0029 0.0462 482 SER A CB 3687 O OG A SER A 457 ? 0.1590 0.1862 0.2608 0.0534 0.0068 0.0478 482 SER A OG 3688 O OG B SER A 457 ? 0.2218 0.2603 0.3250 0.0454 -0.0006 0.0472 482 SER A OG 3689 N N . ARG A 458 ? 0.2192 0.2797 0.3348 0.0562 0.0071 0.0474 483 ARG A N 3690 C CA . ARG A 458 ? 0.2534 0.3157 0.3703 0.0593 0.0105 0.0459 483 ARG A CA 3691 C C . ARG A 458 ? 0.2519 0.3285 0.3754 0.0524 0.0089 0.0452 483 ARG A C 3692 O O . ARG A 458 ? 0.2421 0.3176 0.3660 0.0514 0.0113 0.0431 483 ARG A O 3693 C CB . ARG A 458 ? 0.2525 0.3221 0.3697 0.0705 0.0126 0.0487 483 ARG A CB 3694 C CG . ARG A 458 ? 0.3342 0.3853 0.4438 0.0783 0.0155 0.0486 483 ARG A CG 3695 C CD . ARG A 458 ? 0.4149 0.4727 0.5240 0.0905 0.0176 0.0507 483 ARG A CD 3696 N NE . ARG A 458 ? 0.4218 0.4614 0.5236 0.0979 0.0193 0.0519 483 ARG A NE 3697 C CZ . ARG A 458 ? 0.4816 0.5007 0.5771 0.0998 0.0216 0.0490 483 ARG A CZ 3698 N NH1 . ARG A 458 ? 0.4150 0.4306 0.5106 0.0955 0.0229 0.0443 483 ARG A NH1 3699 N NH2 . ARG A 458 ? 0.5551 0.5571 0.6442 0.1057 0.0226 0.0509 483 ARG A NH2 3700 N N . SER A 459 ? 0.2421 0.3320 0.3707 0.0475 0.0045 0.0472 484 SER A N 3701 C CA . SER A 459 ? 0.2180 0.3211 0.3534 0.0399 0.0022 0.0475 484 SER A CA 3702 C C . SER A 459 ? 0.2387 0.3304 0.3718 0.0332 0.0033 0.0440 484 SER A C 3703 O O . SER A 459 ? 0.3693 0.4669 0.5054 0.0322 0.0054 0.0438 484 SER A O 3704 C CB . SER A 459 ? 0.2535 0.3658 0.3927 0.0336 -0.0038 0.0489 484 SER A CB 3705 O OG . SER A 459 ? 0.5025 0.6305 0.6454 0.0391 -0.0050 0.0524 484 SER A OG 3706 N N . TRP A 460 ? 0.1886 0.2654 0.3165 0.0291 0.0019 0.0415 485 TRP A N 3707 C CA . TRP A 460 ? 0.1925 0.2588 0.3177 0.0233 0.0029 0.0382 485 TRP A CA 3708 C C . TRP A 460 ? 0.2111 0.2632 0.3303 0.0278 0.0078 0.0357 485 TRP A C 3709 O O . TRP A 460 ? 0.1955 0.2441 0.3140 0.0255 0.0102 0.0334 485 TRP A O 3710 C CB . TRP A 460 ? 0.2104 0.2692 0.3327 0.0166 -0.0013 0.0366 485 TRP A CB 3711 C CG . TRP A 460 ? 0.2154 0.2685 0.3333 0.0199 -0.0029 0.0369 485 TRP A CG 3712 C CD1 . TRP A 460 ? 0.2314 0.2707 0.3425 0.0221 -0.0008 0.0357 485 TRP A CD1 3713 C CD2 . TRP A 460 ? 0.2107 0.2730 0.3308 0.0212 -0.0070 0.0391 485 TRP A CD2 3714 N NE1 . TRP A 460 ? 0.2262 0.2660 0.3352 0.0250 -0.0032 0.0374 485 TRP A NE1 3715 C CE2 . TRP A 460 ? 0.2183 0.2721 0.3326 0.0248 -0.0070 0.0391 485 TRP A CE2 3716 C CE3 . TRP A 460 ? 0.2789 0.3569 0.4056 0.0193 -0.0109 0.0411 485 TRP A CE3 3717 C CZ2 . TRP A 460 ? 0.2089 0.2694 0.3233 0.0275 -0.0105 0.0409 485 TRP A CZ2 3718 C CZ3 . TRP A 460 ? 0.2883 0.3726 0.4151 0.0216 -0.0147 0.0424 485 TRP A CZ3 3719 C CH2 . TRP A 460 ? 0.2531 0.3287 0.3737 0.0260 -0.0143 0.0422 485 TRP A CH2 3720 N N . GLY A 461 ? 0.1979 0.2419 0.3129 0.0339 0.0091 0.0364 486 GLY A N 3721 C CA . GLY A 461 ? 0.1968 0.2253 0.3058 0.0373 0.0130 0.0342 486 GLY A CA 3722 C C . GLY A 461 ? 0.2063 0.2368 0.3162 0.0416 0.0166 0.0324 486 GLY A C 3723 O O . GLY A 461 ? 0.2183 0.2389 0.3247 0.0401 0.0189 0.0289 486 GLY A O 3724 N N . GLU A 462 ? 0.1857 0.2302 0.2998 0.0474 0.0170 0.0348 487 GLU A N 3725 C CA . GLU A 462 ? 0.2179 0.2668 0.3326 0.0530 0.0202 0.0332 487 GLU A CA 3726 C C . GLU A 462 ? 0.2052 0.2636 0.3240 0.0468 0.0205 0.0320 487 GLU A C 3727 O O . GLU A 462 ? 0.2162 0.2735 0.3336 0.0494 0.0234 0.0292 487 GLU A O 3728 C CB . GLU A 462 ? 0.2441 0.3064 0.3614 0.0625 0.0208 0.0363 487 GLU A CB 3729 C CG . GLU A 462 ? 0.3405 0.3899 0.4519 0.0706 0.0215 0.0370 487 GLU A CG 3730 C CD . GLU A 462 ? 0.4997 0.5611 0.6123 0.0817 0.0225 0.0398 487 GLU A CD 3731 O OE1 . GLU A 462 ? 0.4567 0.5398 0.5758 0.0824 0.0221 0.0419 487 GLU A OE1 3732 O OE2 . GLU A 462 ? 0.4455 0.4950 0.5525 0.0899 0.0236 0.0402 487 GLU A OE2 3733 N N . SER A 463 ? 0.1822 0.2495 0.3060 0.0386 0.0171 0.0341 488 SER A N 3734 C CA A SER A 463 ? 0.1829 0.2578 0.3105 0.0319 0.0170 0.0339 488 SER A CA 3735 C CA B SER A 463 ? 0.1861 0.2611 0.3138 0.0320 0.0170 0.0339 488 SER A CA 3736 C C . SER A 463 ? 0.1772 0.2365 0.2993 0.0278 0.0185 0.0295 488 SER A C 3737 O O . SER A 463 ? 0.1670 0.2294 0.2898 0.0266 0.0207 0.0279 488 SER A O 3738 C CB A SER A 463 ? 0.2015 0.2868 0.3349 0.0238 0.0123 0.0372 488 SER A CB 3739 C CB B SER A 463 ? 0.2095 0.2953 0.3431 0.0239 0.0123 0.0373 488 SER A CB 3740 O OG A SER A 463 ? 0.2361 0.3405 0.3762 0.0265 0.0111 0.0416 488 SER A OG 3741 O OG B SER A 463 ? 0.2307 0.3035 0.3604 0.0179 0.0094 0.0356 488 SER A OG 3742 N N . TYR A 464 ? 0.1674 0.2116 0.2841 0.0258 0.0174 0.0279 489 TYR A N 3743 C CA . TYR A 464 ? 0.1467 0.1770 0.2579 0.0219 0.0187 0.0240 489 TYR A CA 3744 C C . TYR A 464 ? 0.1535 0.1729 0.2596 0.0273 0.0225 0.0205 489 TYR A C 3745 O O . TYR A 464 ? 0.1670 0.1807 0.2703 0.0249 0.0244 0.0170 489 TYR A O 3746 C CB . TYR A 464 ? 0.1778 0.1978 0.2849 0.0180 0.0160 0.0240 489 TYR A CB 3747 C CG . TYR A 464 ? 0.1595 0.1862 0.2696 0.0124 0.0114 0.0261 489 TYR A CG 3748 C CD1 . TYR A 464 ? 0.2069 0.2427 0.3215 0.0073 0.0098 0.0268 489 TYR A CD1 3749 C CD2 . TYR A 464 ? 0.1606 0.1837 0.2685 0.0123 0.0083 0.0272 489 TYR A CD2 3750 C CE1 . TYR A 464 ? 0.1983 0.2376 0.3149 0.0019 0.0049 0.0283 489 TYR A CE1 3751 C CE2 . TYR A 464 ? 0.1591 0.1870 0.2688 0.0076 0.0034 0.0281 489 TYR A CE2 3752 C CZ . TYR A 464 ? 0.1668 0.2017 0.2806 0.0022 0.0015 0.0284 489 TYR A CZ 3753 O OH . TYR A 464 ? 0.2241 0.2616 0.3391 -0.0027 -0.0040 0.0289 489 TYR A OH 3754 N N . PHE A 465 ? 0.1746 0.1900 0.2789 0.0347 0.0233 0.0214 490 PHE A N 3755 C CA . PHE A 465 ? 0.1920 0.1919 0.2900 0.0390 0.0258 0.0181 490 PHE A CA 3756 C C . PHE A 465 ? 0.2038 0.2053 0.3011 0.0491 0.0279 0.0174 490 PHE A C 3757 O O . PHE A 465 ? 0.2146 0.2020 0.3063 0.0531 0.0295 0.0139 490 PHE A O 3758 C CB . PHE A 465 ? 0.1816 0.1678 0.2753 0.0380 0.0245 0.0196 490 PHE A CB 3759 C CG . PHE A 465 ? 0.1918 0.1760 0.2847 0.0296 0.0224 0.0200 490 PHE A CG 3760 C CD1 . PHE A 465 ? 0.1956 0.1745 0.2859 0.0239 0.0233 0.0166 490 PHE A CD1 3761 C CD2 . PHE A 465 ? 0.1801 0.1685 0.2744 0.0281 0.0194 0.0236 490 PHE A CD2 3762 C CE1 . PHE A 465 ? 0.2150 0.1928 0.3039 0.0173 0.0214 0.0169 490 PHE A CE1 3763 C CE2 . PHE A 465 ? 0.2014 0.1882 0.2941 0.0215 0.0172 0.0234 490 PHE A CE2 3764 C CZ . PHE A 465 ? 0.2249 0.2062 0.3147 0.0164 0.0183 0.0202 490 PHE A CZ 3765 N N . LEU A 466 ? 0.1931 0.2119 0.2959 0.0534 0.0275 0.0205 491 LEU A N 3766 C CA . LEU A 466 ? 0.2163 0.2394 0.3183 0.0645 0.0293 0.0202 491 LEU A CA 3767 C C . LEU A 466 ? 0.2491 0.2530 0.3440 0.0709 0.0298 0.0192 491 LEU A C 3768 O O . LEU A 466 ? 0.2482 0.2459 0.3421 0.0696 0.0281 0.0224 491 LEU A O 3769 C CB . LEU A 466 ? 0.2429 0.2721 0.3448 0.0672 0.0318 0.0164 491 LEU A CB 3770 C CG . LEU A 466 ? 0.2358 0.2880 0.3459 0.0629 0.0315 0.0194 491 LEU A CG 3771 C CD1 . LEU A 466 ? 0.2398 0.2982 0.3498 0.0644 0.0340 0.0159 491 LEU A CD1 3772 C CD2 . LEU A 466 ? 0.2263 0.2977 0.3419 0.0684 0.0306 0.0246 491 LEU A CD2 3773 N N . SER A 467 ? 0.2391 0.2332 0.3287 0.0780 0.0318 0.0148 492 SER A N 3774 C CA . SER A 467 ? 0.2968 0.2715 0.3792 0.0850 0.0319 0.0141 492 SER A CA 3775 C C . SER A 467 ? 0.2637 0.2175 0.3417 0.0775 0.0309 0.0136 492 SER A C 3776 O O . SER A 467 ? 0.3505 0.2878 0.4233 0.0814 0.0305 0.0147 492 SER A O 3777 C CB . SER A 467 ? 0.3129 0.2811 0.3899 0.0948 0.0336 0.0087 492 SER A CB 3778 O OG . SER A 467 ? 0.4997 0.4871 0.5797 0.1046 0.0345 0.0101 492 SER A OG 3779 N N . ASN A 468 ? 0.2560 0.2109 0.3358 0.0669 0.0305 0.0125 493 ASN A N 3780 C CA . ASN A 468 ? 0.2609 0.1994 0.3369 0.0593 0.0296 0.0126 493 ASN A CA 3781 C C . ASN A 468 ? 0.2831 0.2229 0.3606 0.0567 0.0277 0.0186 493 ASN A C 3782 O O . ASN A 468 ? 0.2789 0.2064 0.3531 0.0517 0.0270 0.0200 493 ASN A O 3783 C CB . ASN A 468 ? 0.2316 0.1725 0.3085 0.0499 0.0299 0.0093 493 ASN A CB 3784 C CG . ASN A 468 ? 0.2318 0.1692 0.3061 0.0520 0.0317 0.0030 493 ASN A CG 3785 O OD1 . ASN A 468 ? 0.2923 0.2179 0.3619 0.0589 0.0323 0.0000 493 ASN A OD1 3786 N ND2 . ASN A 468 ? 0.2337 0.1808 0.3106 0.0465 0.0324 0.0006 493 ASN A ND2 3787 N N . TYR A 469 ? 0.2550 0.2109 0.3375 0.0600 0.0268 0.0222 494 TYR A N 3788 C CA A TYR A 469 ? 0.2208 0.1807 0.3050 0.0580 0.0247 0.0274 494 TYR A CA 3789 C CA B TYR A 469 ? 0.2140 0.1743 0.2983 0.0583 0.0247 0.0275 494 TYR A CA 3790 C C . TYR A 469 ? 0.2747 0.2191 0.3538 0.0621 0.0247 0.0306 494 TYR A C 3791 O O . TYR A 469 ? 0.2803 0.2204 0.3583 0.0574 0.0233 0.0337 494 TYR A O 3792 C CB A TYR A 469 ? 0.2192 0.1994 0.3097 0.0615 0.0235 0.0305 494 TYR A CB 3793 C CB B TYR A 469 ? 0.2387 0.2192 0.3292 0.0626 0.0237 0.0305 494 TYR A CB 3794 C CG A TYR A 469 ? 0.2246 0.2121 0.3177 0.0568 0.0206 0.0342 494 TYR A CG 3795 C CG B TYR A 469 ? 0.2140 0.2019 0.3068 0.0614 0.0210 0.0353 494 TYR A CG 3796 C CD1 A TYR A 469 ? 0.2394 0.2265 0.3328 0.0476 0.0190 0.0330 494 TYR A CD1 3797 C CD1 B TYR A 469 ? 0.2454 0.2406 0.3393 0.0696 0.0206 0.0392 494 TYR A CD1 3798 C CD2 A TYR A 469 ? 0.1902 0.1851 0.2848 0.0623 0.0192 0.0387 494 TYR A CD2 3799 C CD2 B TYR A 469 ? 0.2449 0.2336 0.3383 0.0530 0.0187 0.0358 494 TYR A CD2 3800 C CE1 A TYR A 469 ? 0.2185 0.2117 0.3133 0.0442 0.0159 0.0356 494 TYR A CE1 3801 C CE1 B TYR A 469 ? 0.2120 0.2153 0.3081 0.0689 0.0180 0.0433 494 TYR A CE1 3802 C CE2 A TYR A 469 ? 0.2184 0.2204 0.3150 0.0584 0.0162 0.0414 494 TYR A CE2 3803 C CE2 B TYR A 469 ? 0.2342 0.2303 0.3292 0.0526 0.0160 0.0396 494 TYR A CE2 3804 C CZ A TYR A 469 ? 0.1690 0.1697 0.2655 0.0494 0.0144 0.0397 494 TYR A CZ 3805 C CZ B TYR A 469 ? 0.2368 0.2404 0.3334 0.0603 0.0156 0.0433 494 TYR A CZ 3806 O OH A TYR A 469 ? 0.2566 0.2638 0.3541 0.0463 0.0110 0.0416 494 TYR A OH 3807 O OH B TYR A 469 ? 0.2272 0.2391 0.3253 0.0602 0.0127 0.0467 494 TYR A OH 3808 N N . GLU A 470 ? 0.2872 0.2233 0.3630 0.0711 0.0260 0.0300 495 GLU A N 3809 C CA . GLU A 470 ? 0.2979 0.2175 0.3684 0.0756 0.0259 0.0334 495 GLU A CA 3810 C C . GLU A 470 ? 0.3109 0.2117 0.3769 0.0679 0.0256 0.0332 495 GLU A C 3811 O O . GLU A 470 ? 0.3149 0.2099 0.3794 0.0659 0.0247 0.0384 495 GLU A O 3812 C CB . GLU A 470 ? 0.3291 0.2412 0.3957 0.0873 0.0271 0.0318 495 GLU A CB 3813 C CG . GLU A 470 ? 0.4221 0.3508 0.4918 0.0970 0.0271 0.0353 495 GLU A CG 3814 C CD . GLU A 470 ? 0.4988 0.4519 0.5756 0.0960 0.0272 0.0337 495 GLU A CD 3815 O OE1 . GLU A 470 ? 0.4242 0.3793 0.5024 0.0904 0.0279 0.0291 495 GLU A OE1 3816 O OE2 . GLU A 470 ? 0.4626 0.4334 0.5437 0.1007 0.0266 0.0374 495 GLU A OE2 3817 N N . ARG A 471 ? 0.2911 0.1837 0.3550 0.0635 0.0264 0.0275 496 ARG A N 3818 C CA . ARG A 471 ? 0.3297 0.2064 0.3897 0.0552 0.0260 0.0271 496 ARG A CA 3819 C C . ARG A 471 ? 0.3192 0.2057 0.3821 0.0460 0.0250 0.0302 496 ARG A C 3820 O O . ARG A 471 ? 0.3125 0.1902 0.3730 0.0409 0.0243 0.0338 496 ARG A O 3821 C CB . ARG A 471 ? 0.3352 0.2035 0.3925 0.0525 0.0269 0.0198 496 ARG A CB 3822 C CG . ARG A 471 ? 0.3636 0.2144 0.4166 0.0443 0.0262 0.0192 496 ARG A CG 3823 C CD . ARG A 471 ? 0.3379 0.1817 0.3883 0.0423 0.0268 0.0112 496 ARG A CD 3824 N NE . ARG A 471 ? 0.3953 0.2235 0.4419 0.0335 0.0259 0.0105 496 ARG A NE 3825 C CZ . ARG A 471 ? 0.4107 0.2338 0.4552 0.0290 0.0260 0.0039 496 ARG A CZ 3826 N NH1 . ARG A 471 ? 0.3634 0.1959 0.4090 0.0331 0.0272 -0.0025 496 ARG A NH1 3827 N NH2 . ARG A 471 ? 0.4504 0.2604 0.4919 0.0203 0.0248 0.0039 496 ARG A NH2 3828 N N . LEU A 472 ? 0.2628 0.1674 0.3307 0.0441 0.0247 0.0290 497 LEU A N 3829 C CA . LEU A 472 ? 0.2370 0.1506 0.3067 0.0369 0.0232 0.0312 497 LEU A CA 3830 C C . LEU A 472 ? 0.2729 0.1877 0.3423 0.0389 0.0218 0.0379 497 LEU A C 3831 O O . LEU A 472 ? 0.2603 0.1734 0.3281 0.0336 0.0210 0.0408 497 LEU A O 3832 C CB . LEU A 472 ? 0.2299 0.1613 0.3047 0.0355 0.0226 0.0289 497 LEU A CB 3833 C CG . LEU A 472 ? 0.2376 0.1704 0.3128 0.0313 0.0238 0.0232 497 LEU A CG 3834 C CD1 . LEU A 472 ? 0.2464 0.1964 0.3272 0.0312 0.0231 0.0223 497 LEU A CD1 3835 C CD2 . LEU A 472 ? 0.2376 0.1648 0.3098 0.0229 0.0237 0.0218 497 LEU A CD2 3836 N N . ILE A 473 ? 0.2586 0.1777 0.3295 0.0471 0.0217 0.0406 498 ILE A N 3837 C CA . ILE A 473 ? 0.2631 0.1844 0.3337 0.0503 0.0205 0.0471 498 ILE A CA 3838 C C . ILE A 473 ? 0.2890 0.1927 0.3546 0.0491 0.0210 0.0511 498 ILE A C 3839 O O . ILE A 473 ? 0.2946 0.1998 0.3594 0.0462 0.0200 0.0562 498 ILE A O 3840 C CB . ILE A 473 ? 0.2657 0.1951 0.3386 0.0602 0.0205 0.0492 498 ILE A CB 3841 C CG1 . ILE A 473 ? 0.2707 0.2206 0.3495 0.0597 0.0191 0.0472 498 ILE A CG1 3842 C CG2 . ILE A 473 ? 0.2911 0.2194 0.3625 0.0645 0.0197 0.0563 498 ILE A CG2 3843 C CD1 . ILE A 473 ? 0.3331 0.2934 0.4148 0.0688 0.0193 0.0485 498 ILE A CD1 3844 N N . ARG A 474 ? 0.2954 0.1823 0.3574 0.0512 0.0224 0.0490 499 ARG A N 3845 C CA A ARG A 474 ? 0.3029 0.1707 0.3601 0.0489 0.0225 0.0528 499 ARG A CA 3846 C CA B ARG A 474 ? 0.3176 0.1855 0.3748 0.0489 0.0225 0.0528 499 ARG A CA 3847 C C . ARG A 474 ? 0.3111 0.1779 0.3676 0.0378 0.0220 0.0531 499 ARG A C 3848 O O . ARG A 474 ? 0.3616 0.2237 0.4164 0.0344 0.0214 0.0594 499 ARG A O 3849 C CB A ARG A 474 ? 0.3934 0.2421 0.4463 0.0529 0.0233 0.0489 499 ARG A CB 3850 C CB B ARG A 474 ? 0.4007 0.2494 0.4537 0.0531 0.0233 0.0490 499 ARG A CB 3851 C CG A ARG A 474 ? 0.4613 0.3101 0.5136 0.0654 0.0238 0.0491 499 ARG A CG 3852 C CG B ARG A 474 ? 0.4547 0.3023 0.5067 0.0656 0.0237 0.0502 499 ARG A CG 3853 C CD A ARG A 474 ? 0.4675 0.2926 0.5135 0.0704 0.0239 0.0470 499 ARG A CD 3854 C CD B ARG A 474 ? 0.4678 0.2926 0.5137 0.0707 0.0239 0.0472 499 ARG A CD 3855 N NE A ARG A 474 ? 0.4862 0.3031 0.5303 0.0658 0.0242 0.0390 499 ARG A NE 3856 N NE B ARG A 474 ? 0.4604 0.2854 0.5059 0.0711 0.0246 0.0384 499 ARG A NE 3857 C CZ A ARG A 474 ? 0.4922 0.3152 0.5369 0.0711 0.0250 0.0321 499 ARG A CZ 3858 C CZ B ARG A 474 ? 0.4959 0.3114 0.5396 0.0630 0.0244 0.0334 499 ARG A CZ 3859 N NH1 A ARG A 474 ? 0.3789 0.2168 0.4263 0.0806 0.0258 0.0325 499 ARG A NH1 3860 N NH1 B ARG A 474 ? 0.4869 0.3046 0.5304 0.0647 0.0251 0.0254 499 ARG A NH1 3861 N NH2 A ARG A 474 ? 0.5106 0.3266 0.5533 0.0669 0.0252 0.0250 499 ARG A NH2 3862 N NH2 B ARG A 474 ? 0.4018 0.2070 0.4440 0.0533 0.0235 0.0366 499 ARG A NH2 3863 N N . ALA A 475 ? 0.3119 0.1845 0.3698 0.0325 0.0223 0.0469 500 ALA A N 3864 C CA . ALA A 475 ? 0.2817 0.1557 0.3389 0.0227 0.0220 0.0467 500 ALA A CA 3865 C C . ALA A 475 ? 0.3191 0.2081 0.3779 0.0208 0.0207 0.0516 500 ALA A C 3866 O O . ALA A 475 ? 0.3141 0.2023 0.3711 0.0152 0.0202 0.0556 500 ALA A O 3867 C CB . ALA A 475 ? 0.2962 0.1748 0.3544 0.0187 0.0227 0.0389 500 ALA A CB 3868 N N . LYS A 476 ? 0.2743 0.1775 0.3364 0.0257 0.0198 0.0511 501 LYS A N 3869 C CA . LYS A 476 ? 0.2315 0.1492 0.2948 0.0252 0.0179 0.0546 501 LYS A CA 3870 C C . LYS A 476 ? 0.2970 0.2115 0.3584 0.0275 0.0176 0.0628 501 LYS A C 3871 O O . LYS A 476 ? 0.3028 0.2237 0.3629 0.0241 0.0166 0.0666 501 LYS A O 3872 C CB . LYS A 476 ? 0.2722 0.2038 0.3395 0.0303 0.0166 0.0525 501 LYS A CB 3873 C CG . LYS A 476 ? 0.2493 0.1948 0.3174 0.0315 0.0140 0.0558 501 LYS A CG 3874 C CD . LYS A 476 ? 0.2458 0.1982 0.3125 0.0253 0.0124 0.0534 501 LYS A CD 3875 C CE . LYS A 476 ? 0.2458 0.2116 0.3124 0.0276 0.0093 0.0559 501 LYS A CE 3876 N NZ . LYS A 476 ? 0.2380 0.2109 0.3026 0.0232 0.0072 0.0527 501 LYS A NZ 3877 N N . THR A 477 ? 0.2765 0.1816 0.3374 0.0337 0.0184 0.0656 502 THR A N 3878 C CA . THR A 477 ? 0.3166 0.2181 0.3757 0.0367 0.0183 0.0742 502 THR A CA 3879 C C . THR A 477 ? 0.3304 0.2205 0.3863 0.0292 0.0187 0.0784 502 THR A C 3880 O O . THR A 477 ? 0.3899 0.2843 0.4450 0.0282 0.0182 0.0859 502 THR A O 3881 C CB . THR A 477 ? 0.3196 0.2118 0.3781 0.0457 0.0191 0.0762 502 THR A CB 3882 O OG1 . THR A 477 ? 0.3879 0.2930 0.4498 0.0520 0.0187 0.0724 502 THR A OG1 3883 C CG2 . THR A 477 ? 0.4265 0.3171 0.4833 0.0495 0.0189 0.0857 502 THR A CG2 3884 N N . LEU A 478 ? 0.3403 0.2171 0.3946 0.0239 0.0196 0.0739 503 LEU A N 3885 C CA . LEU A 478 ? 0.3546 0.2210 0.4064 0.0154 0.0197 0.0773 503 LEU A CA 3886 C C . LEU A 478 ? 0.3510 0.2324 0.4032 0.0083 0.0191 0.0785 503 LEU A C 3887 O O . LEU A 478 ? 0.4342 0.3163 0.4851 0.0040 0.0188 0.0859 503 LEU A O 3888 C CB . LEU A 478 ? 0.4589 0.3090 0.5089 0.0114 0.0203 0.0707 503 LEU A CB 3889 C CG . LEU A 478 ? 0.5858 0.4155 0.6333 0.0171 0.0206 0.0699 503 LEU A CG 3890 C CD1 . LEU A 478 ? 0.6354 0.4547 0.6815 0.0147 0.0209 0.0607 503 LEU A CD1 3891 C CD2 . LEU A 478 ? 0.6264 0.4401 0.6709 0.0146 0.0199 0.0786 503 LEU A CD2 3892 N N . ILE A 479 ? 0.3335 0.2269 0.3872 0.0074 0.0188 0.0717 504 ILE A N 3893 C CA . ILE A 479 ? 0.3055 0.2112 0.3585 0.0011 0.0182 0.0714 504 ILE A CA 3894 C C . ILE A 479 ? 0.2888 0.2132 0.3422 0.0048 0.0166 0.0741 504 ILE A C 3895 O O . ILE A 479 ? 0.3148 0.2492 0.3665 0.0012 0.0159 0.0769 504 ILE A O 3896 C CB . ILE A 479 ? 0.2853 0.1920 0.3385 -0.0029 0.0188 0.0624 504 ILE A CB 3897 C CG1 . ILE A 479 ? 0.3306 0.2454 0.3819 -0.0104 0.0186 0.0628 504 ILE A CG1 3898 C CG2 . ILE A 479 ? 0.2582 0.1753 0.3139 0.0023 0.0180 0.0568 504 ILE A CG2 3899 C CD1 . ILE A 479 ? 0.3645 0.2697 0.4139 -0.0176 0.0192 0.0678 504 ILE A CD1 3900 N N . ASP A 480 ? 0.3057 0.2355 0.3612 0.0124 0.0157 0.0732 505 ASP A N 3901 C CA . ASP A 480 ? 0.2882 0.2352 0.3439 0.0162 0.0135 0.0745 505 ASP A CA 3902 C C . ASP A 480 ? 0.2824 0.2319 0.3399 0.0243 0.0128 0.0784 505 ASP A C 3903 O O . ASP A 480 ? 0.2923 0.2508 0.3520 0.0288 0.0112 0.0747 505 ASP A O 3904 C CB . ASP A 480 ? 0.2968 0.2526 0.3533 0.0154 0.0120 0.0664 505 ASP A CB 3905 C CG . ASP A 480 ? 0.2480 0.2201 0.3036 0.0187 0.0089 0.0667 505 ASP A CG 3906 O OD1 . ASP A 480 ? 0.2794 0.2581 0.3329 0.0203 0.0082 0.0729 505 ASP A OD1 3907 O OD2 . ASP A 480 ? 0.2507 0.2288 0.3075 0.0198 0.0068 0.0607 505 ASP A OD2 3908 N N . PRO A 481 ? 0.3221 0.2640 0.3786 0.0261 0.0140 0.0861 506 PRO A N 3909 C CA . PRO A 481 ? 0.3368 0.2799 0.3946 0.0344 0.0138 0.0903 506 PRO A CA 3910 C C . PRO A 481 ? 0.3226 0.2851 0.3812 0.0394 0.0113 0.0914 506 PRO A C 3911 O O . PRO A 481 ? 0.3587 0.3263 0.4193 0.0463 0.0105 0.0913 506 PRO A O 3912 C CB . PRO A 481 ? 0.3639 0.2958 0.4195 0.0337 0.0152 0.0997 506 PRO A CB 3913 C CG . PRO A 481 ? 0.3331 0.2658 0.3868 0.0248 0.0153 0.1015 506 PRO A CG 3914 C CD . PRO A 481 ? 0.3152 0.2464 0.3694 0.0200 0.0154 0.0918 506 PRO A CD 3915 N N . ASN A 482 ? 0.3069 0.2806 0.3636 0.0362 0.0098 0.0920 507 ASN A N 3916 C CA . ASN A 482 ? 0.3562 0.3479 0.4125 0.0412 0.0068 0.0925 507 ASN A CA 3917 C C . ASN A 482 ? 0.2998 0.2996 0.3570 0.0408 0.0040 0.0833 507 ASN A C 3918 O O . ASN A 482 ? 0.3150 0.3287 0.3713 0.0442 0.0007 0.0820 507 ASN A O 3919 C CB . ASN A 482 ? 0.3359 0.3369 0.3888 0.0398 0.0064 0.0989 507 ASN A CB 3920 C CG . ASN A 482 ? 0.3888 0.3832 0.4413 0.0403 0.0088 0.1096 507 ASN A CG 3921 O OD1 . ASN A 482 ? 0.4469 0.4385 0.5008 0.0462 0.0093 0.1135 507 ASN A OD1 3922 N ND2 . ASN A 482 ? 0.4247 0.4168 0.4752 0.0340 0.0100 0.1146 507 ASN A ND2 3923 N N . ASN A 483 ? 0.2547 0.2454 0.3135 0.0366 0.0051 0.0770 508 ASN A N 3924 C CA . ASN A 483 ? 0.2710 0.2672 0.3313 0.0358 0.0026 0.0689 508 ASN A CA 3925 C C . ASN A 483 ? 0.2504 0.2566 0.3071 0.0340 -0.0005 0.0659 508 ASN A C 3926 O O . ASN A 483 ? 0.2610 0.2763 0.3180 0.0364 -0.0043 0.0619 508 ASN A O 3927 C CB . ASN A 483 ? 0.2970 0.3002 0.3611 0.0416 0.0006 0.0678 508 ASN A CB 3928 C CG . ASN A 483 ? 0.2928 0.2959 0.3603 0.0393 -0.0006 0.0606 508 ASN A CG 3929 O OD1 . ASN A 483 ? 0.2681 0.2633 0.3355 0.0344 0.0012 0.0569 508 ASN A OD1 3930 N ND2 . ASN A 483 ? 0.3041 0.3169 0.3748 0.0428 -0.0035 0.0590 508 ASN A ND2 3931 N N . VAL A 484 ? 0.2363 0.2408 0.2895 0.0299 0.0010 0.0678 509 VAL A N 3932 C CA . VAL A 484 ? 0.2375 0.2514 0.2863 0.0290 -0.0016 0.0651 509 VAL A CA 3933 C C . VAL A 484 ? 0.2424 0.2536 0.2913 0.0258 -0.0030 0.0566 509 VAL A C 3934 O O . VAL A 484 ? 0.2483 0.2668 0.2940 0.0272 -0.0066 0.0524 509 VAL A O 3935 C CB . VAL A 484 ? 0.2813 0.2956 0.3266 0.0252 0.0007 0.0700 509 VAL A CB 3936 C CG1 . VAL A 484 ? 0.3072 0.3311 0.3474 0.0247 -0.0016 0.0664 509 VAL A CG1 3937 C CG2 . VAL A 484 ? 0.2595 0.2789 0.3045 0.0284 0.0015 0.0794 509 VAL A CG2 3938 N N . PHE A 485 ? 0.2241 0.2245 0.2763 0.0221 -0.0004 0.0541 510 PHE A N 3939 C CA . PHE A 485 ? 0.2309 0.2287 0.2836 0.0189 -0.0012 0.0470 510 PHE A CA 3940 C C . PHE A 485 ? 0.2311 0.2281 0.2891 0.0207 -0.0023 0.0444 510 PHE A C 3941 O O . PHE A 485 ? 0.2388 0.2291 0.3006 0.0206 0.0006 0.0453 510 PHE A O 3942 C CB . PHE A 485 ? 0.2194 0.2083 0.2716 0.0132 0.0025 0.0459 510 PHE A CB 3943 C CG . PHE A 485 ? 0.2336 0.2256 0.2810 0.0107 0.0033 0.0487 510 PHE A CG 3944 C CD1 . PHE A 485 ? 0.2399 0.2381 0.2829 0.0097 0.0016 0.0452 510 PHE A CD1 3945 C CD2 . PHE A 485 ? 0.2493 0.2387 0.2964 0.0096 0.0057 0.0555 510 PHE A CD2 3946 C CE1 . PHE A 485 ? 0.2563 0.2601 0.2948 0.0079 0.0024 0.0482 510 PHE A CE1 3947 C CE2 . PHE A 485 ? 0.2444 0.2390 0.2876 0.0067 0.0063 0.0590 510 PHE A CE2 3948 C CZ . PHE A 485 ? 0.2529 0.2558 0.2919 0.0060 0.0048 0.0553 510 PHE A CZ 3949 N N . ASN A 486 ? 0.1979 0.2023 0.2560 0.0227 -0.0068 0.0412 511 ASN A N 3950 C CA . ASN A 486 ? 0.2026 0.2095 0.2661 0.0242 -0.0085 0.0398 511 ASN A CA 3951 C C . ASN A 486 ? 0.2169 0.2270 0.2807 0.0221 -0.0130 0.0341 511 ASN A C 3952 O O . ASN A 486 ? 0.2376 0.2493 0.2962 0.0216 -0.0159 0.0315 511 ASN A O 3953 C CB . ASN A 486 ? 0.2313 0.2456 0.2961 0.0300 -0.0099 0.0440 511 ASN A CB 3954 C CG . ASN A 486 ? 0.2634 0.2869 0.3237 0.0330 -0.0145 0.0436 511 ASN A CG 3955 O OD1 . ASN A 486 ? 0.2744 0.3031 0.3347 0.0332 -0.0194 0.0393 511 ASN A OD1 3956 N ND2 . ASN A 486 ? 0.2780 0.3038 0.3342 0.0353 -0.0131 0.0482 511 ASN A ND2 3957 N N . HIS A 487 ? 0.2057 0.2166 0.2752 0.0208 -0.0136 0.0326 512 HIS A N 3958 C CA . HIS A 487 ? 0.1964 0.2101 0.2673 0.0180 -0.0183 0.0283 512 HIS A CA 3959 C C . HIS A 487 ? 0.1805 0.1997 0.2589 0.0184 -0.0188 0.0295 512 HIS A C 3960 O O . HIS A 487 ? 0.1882 0.2088 0.2694 0.0218 -0.0155 0.0332 512 HIS A O 3961 C CB . HIS A 487 ? 0.1921 0.1990 0.2610 0.0130 -0.0175 0.0247 512 HIS A CB 3962 C CG . HIS A 487 ? 0.1964 0.1987 0.2693 0.0105 -0.0123 0.0252 512 HIS A CG 3963 N ND1 . HIS A 487 ? 0.1988 0.2041 0.2784 0.0090 -0.0121 0.0252 512 HIS A ND1 3964 C CD2 . HIS A 487 ? 0.2367 0.2325 0.3077 0.0092 -0.0075 0.0255 512 HIS A CD2 3965 C CE1 . HIS A 487 ? 0.2361 0.2369 0.3172 0.0078 -0.0073 0.0253 512 HIS A CE1 3966 N NE2 . HIS A 487 ? 0.2330 0.2274 0.3090 0.0077 -0.0046 0.0251 512 HIS A NE2 3967 N N . PRO A 488 ? 0.1830 0.2059 0.2645 0.0150 -0.0232 0.0268 513 PRO A N 3968 C CA . PRO A 488 ? 0.1993 0.2310 0.2882 0.0155 -0.0242 0.0287 513 PRO A CA 3969 C C . PRO A 488 ? 0.1948 0.2262 0.2886 0.0162 -0.0185 0.0312 513 PRO A C 3970 O O . PRO A 488 ? 0.2116 0.2511 0.3103 0.0194 -0.0179 0.0339 513 PRO A O 3971 C CB . PRO A 488 ? 0.2366 0.2704 0.3278 0.0098 -0.0298 0.0254 513 PRO A CB 3972 C CG . PRO A 488 ? 0.2504 0.2781 0.3338 0.0094 -0.0338 0.0217 513 PRO A CG 3973 C CD . PRO A 488 ? 0.2089 0.2291 0.2870 0.0112 -0.0284 0.0223 513 PRO A CD 3974 N N . GLN A 489 ? 0.2092 0.2322 0.3014 0.0139 -0.0144 0.0301 514 GLN A N 3975 C CA . GLN A 489 ? 0.1861 0.2083 0.2820 0.0153 -0.0092 0.0316 514 GLN A CA 3976 C C . GLN A 489 ? 0.2216 0.2333 0.3131 0.0176 -0.0042 0.0322 514 GLN A C 3977 O O . GLN A 489 ? 0.2708 0.2783 0.3634 0.0175 -0.0002 0.0316 514 GLN A O 3978 C CB . GLN A 489 ? 0.1950 0.2189 0.2948 0.0102 -0.0091 0.0297 514 GLN A CB 3979 C CG . GLN A 489 ? 0.1680 0.2037 0.2743 0.0079 -0.0134 0.0306 514 GLN A CG 3980 C CD . GLN A 489 ? 0.1800 0.2192 0.2910 0.0031 -0.0127 0.0304 514 GLN A CD 3981 O OE1 . GLN A 489 ? 0.2106 0.2430 0.3195 0.0016 -0.0092 0.0288 514 GLN A OE1 3982 N NE2 . GLN A 489 ? 0.1992 0.2500 0.3169 0.0004 -0.0160 0.0322 514 GLN A NE2 3983 N N . SER A 490 ? 0.1808 0.1888 0.2673 0.0195 -0.0045 0.0336 515 SER A N 3984 C CA . SER A 490 ? 0.2149 0.2130 0.2975 0.0206 -0.0003 0.0350 515 SER A CA 3985 C C . SER A 490 ? 0.2211 0.2171 0.3056 0.0260 0.0028 0.0384 515 SER A C 3986 O O . SER A 490 ? 0.2239 0.2276 0.3114 0.0304 0.0013 0.0408 515 SER A O 3987 C CB . SER A 490 ? 0.2123 0.2089 0.2892 0.0207 -0.0017 0.0364 515 SER A CB 3988 O OG . SER A 490 ? 0.1961 0.2005 0.2733 0.0250 -0.0047 0.0392 515 SER A OG 3989 N N . ILE A 491 ? 0.2255 0.2109 0.3080 0.0260 0.0067 0.0383 516 ILE A N 3990 C CA . ILE A 491 ? 0.2357 0.2157 0.3186 0.0317 0.0095 0.0410 516 ILE A CA 3991 C C . ILE A 491 ? 0.2135 0.1933 0.2943 0.0360 0.0088 0.0463 516 ILE A C 3992 O O . ILE A 491 ? 0.2496 0.2256 0.3265 0.0337 0.0084 0.0482 516 ILE A O 3993 C CB . ILE A 491 ? 0.2498 0.2158 0.3295 0.0300 0.0131 0.0394 516 ILE A CB 3994 C CG1 . ILE A 491 ? 0.2895 0.2568 0.3712 0.0264 0.0141 0.0342 516 ILE A CG1 3995 C CG2 . ILE A 491 ? 0.2552 0.2129 0.3341 0.0365 0.0154 0.0419 516 ILE A CG2 3996 C CD1 . ILE A 491 ? 0.3370 0.3111 0.4232 0.0307 0.0149 0.0332 516 ILE A CD1 3997 N N . PRO A 492 ? 0.2336 0.2192 0.3170 0.0425 0.0085 0.0492 517 PRO A N 3998 C CA . PRO A 492 ? 0.2458 0.2323 0.3272 0.0473 0.0079 0.0548 517 PRO A CA 3999 C C . PRO A 492 ? 0.2972 0.2682 0.3744 0.0490 0.0110 0.0584 517 PRO A C 4000 O O . PRO A 492 ? 0.2996 0.2602 0.3762 0.0501 0.0136 0.0567 517 PRO A O 4001 C CB . PRO A 492 ? 0.2703 0.2675 0.3558 0.0542 0.0072 0.0564 517 PRO A CB 4002 C CG . PRO A 492 ? 0.3237 0.3288 0.4140 0.0514 0.0065 0.0518 517 PRO A CG 4003 C CD . PRO A 492 ? 0.2788 0.2725 0.3670 0.0460 0.0087 0.0479 517 PRO A CD 4004 N N . PRO A 493 ? 0.2699 0.2395 0.3440 0.0492 0.0105 0.0634 518 PRO A N 4005 C CA . PRO A 493 ? 0.2960 0.2513 0.3666 0.0512 0.0129 0.0685 518 PRO A CA 4006 C C . PRO A 493 ? 0.4051 0.3622 0.4766 0.0604 0.0133 0.0727 518 PRO A C 4007 O O . PRO A 493 ? 0.3797 0.3521 0.4543 0.0642 0.0113 0.0728 518 PRO A O 4008 C CB . PRO A 493 ? 0.3360 0.2946 0.4039 0.0482 0.0117 0.0732 518 PRO A CB 4009 C CG . PRO A 493 ? 0.4032 0.3778 0.4725 0.0463 0.0085 0.0699 518 PRO A CG 4010 C CD . PRO A 493 ? 0.2868 0.2687 0.3606 0.0483 0.0073 0.0648 518 PRO A CD 4011 N N . MET A 494 ? 0.3983 0.3402 0.4668 0.0641 0.0155 0.0762 519 MET A N 4012 C CA . MET A 494 ? 0.3883 0.3314 0.4566 0.0737 0.0160 0.0813 519 MET A CA 4013 C C . MET A 494 ? 0.5024 0.4509 0.5694 0.0751 0.0150 0.0889 519 MET A C 4014 O O . MET A 494 ? 0.5376 0.4803 0.6020 0.0693 0.0150 0.0919 519 MET A O 4015 C CB . MET A 494 ? 0.4908 0.4141 0.5555 0.0782 0.0183 0.0821 519 MET A CB 4016 C CG . MET A 494 ? 0.6046 0.5292 0.6710 0.0826 0.0192 0.0759 519 MET A CG 4017 S SD . MET A 494 ? 0.9061 0.8089 0.9671 0.0915 0.0213 0.0768 519 MET A SD 4018 C CE . MET A 494 ? 0.5314 0.4484 0.5958 0.0994 0.0218 0.0712 519 MET A CE 4019 N N . ALA A 495 ? 0.5370 0.4983 0.6056 0.0829 0.0140 0.0922 520 ALA A N 4020 C CA . ALA A 495 ? 0.7323 0.7019 0.7997 0.0854 0.0129 0.0994 520 ALA A CA 4021 C C . ALA A 495 ? 0.8787 0.8324 0.9420 0.0891 0.0151 0.1077 520 ALA A C 4022 O O . ALA A 495 ? 0.9510 0.9076 1.0136 0.0979 0.0155 0.1133 520 ALA A O 4023 C CB . ALA A 495 ? 0.7716 0.7614 0.8423 0.0925 0.0109 0.0998 520 ALA A CB # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ASP 1 26 26 ASP ASP A . n A 1 2 LEU 2 27 27 LEU LEU A . n A 1 3 LEU 3 28 28 LEU LEU A . n A 1 4 SER 4 29 29 SER SER A . n A 1 5 CYS 5 30 30 CYS CYS A . n A 1 6 LEU 6 31 31 LEU LEU A . n A 1 7 THR 7 32 32 THR THR A . n A 1 8 PHE 8 33 33 PHE PHE A . n A 1 9 ASN 9 34 34 ASN ASN A . n A 1 10 GLY 10 35 35 GLY GLY A . n A 1 11 VAL 11 36 36 VAL VAL A . n A 1 12 ARG 12 37 37 ARG ARG A . n A 1 13 ASN 13 38 38 ASN ASN A . n A 1 14 HIS 14 39 39 HIS HIS A . n A 1 15 THR 15 40 40 THR THR A . n A 1 16 VAL 16 41 41 VAL VAL A . n A 1 17 PHE 17 42 42 PHE PHE A . n A 1 18 SER 18 43 43 SER SER A . n A 1 19 ALA 19 44 44 ALA ALA A . n A 1 20 ASP 20 45 45 ASP ASP A . n A 1 21 SER 21 46 46 SER SER A . n A 1 22 ASP 22 47 47 ASP ASP A . n A 1 23 SER 23 48 48 SER SER A . n A 1 24 ASP 24 49 49 ASP ASP A . n A 1 25 PHE 25 50 50 PHE PHE A . n A 1 26 ASN 26 51 51 ASN ASN A . n A 1 27 ARG 27 52 52 ARG ARG A . n A 1 28 PHE 28 53 53 PHE PHE A . n A 1 29 LEU 29 54 54 LEU LEU A . n A 1 30 HIS 30 55 55 HIS HIS A . n A 1 31 LEU 31 56 56 LEU LEU A . n A 1 32 SER 32 57 57 SER SER A . n A 1 33 ILE 33 58 58 ILE ILE A . n A 1 34 GLN 34 59 59 GLN GLN A . n A 1 35 ASN 35 60 60 ASN ASN A . n A 1 36 PRO 36 61 61 PRO PRO A . n A 1 37 LEU 37 62 62 LEU LEU A . n A 1 38 PHE 38 63 63 PHE PHE A . n A 1 39 GLN 39 64 64 GLN GLN A . n A 1 40 ASN 40 65 65 ASN ASN A . n A 1 41 SER 41 66 66 SER SER A . n A 1 42 LEU 42 67 67 LEU LEU A . n A 1 43 ILE 43 68 68 ILE ILE A . n A 1 44 SER 44 69 69 SER SER A . n A 1 45 LYS 45 70 70 LYS LYS A . n A 1 46 PRO 46 71 71 PRO PRO A . n A 1 47 SER 47 72 72 SER SER A . n A 1 48 ALA 48 73 73 ALA ALA A . n A 1 49 ILE 49 74 74 ILE ILE A . n A 1 50 ILE 50 75 75 ILE ILE A . n A 1 51 LEU 51 76 76 LEU LEU A . n A 1 52 PRO 52 77 77 PRO PRO A . n A 1 53 GLY 53 78 78 GLY GLY A . n A 1 54 SER 54 79 79 SER SER A . n A 1 55 LYS 55 80 80 LYS LYS A . n A 1 56 GLU 56 81 81 GLU GLU A . n A 1 57 GLU 57 82 82 GLU GLU A . n A 1 58 LEU 58 83 83 LEU LEU A . n A 1 59 SER 59 84 84 SER SER A . n A 1 60 ASN 60 85 85 ASN ASN A . n A 1 61 THR 61 86 86 THR THR A . n A 1 62 ILE 62 87 87 ILE ILE A . n A 1 63 ARG 63 88 88 ARG ARG A . n A 1 64 CYS 64 89 89 CYS CYS A . n A 1 65 ILE 65 90 90 ILE ILE A . n A 1 66 ARG 66 91 91 ARG ARG A . n A 1 67 LYS 67 92 92 LYS LYS A . n A 1 68 GLY 68 93 93 GLY GLY A . n A 1 69 SER 69 94 94 SER SER A . n A 1 70 TRP 70 95 95 TRP TRP A . n A 1 71 THR 71 96 96 THR THR A . n A 1 72 ILE 72 97 97 ILE ILE A . n A 1 73 ARG 73 98 98 ARG ARG A . n A 1 74 LEU 74 99 99 LEU LEU A . n A 1 75 ARG 75 100 100 ARG ARG A . n A 1 76 SER 76 101 101 SER SER A . n A 1 77 GLY 77 102 102 GLY GLY A . n A 1 78 GLY 78 103 103 GLY GLY A . n A 1 79 HIS 79 104 104 HIS HIS A . n A 1 80 SER 80 105 105 SER SER A . n A 1 81 TYR 81 106 106 TYR TYR A . n A 1 82 GLU 82 107 107 GLU GLU A . n A 1 83 GLY 83 108 108 GLY GLY A . n A 1 84 LEU 84 109 109 LEU LEU A . n A 1 85 SER 85 110 110 SER SER A . n A 1 86 TYR 86 111 111 TYR TYR A . n A 1 87 THR 87 112 112 THR THR A . n A 1 88 SER 88 113 113 SER SER A . n A 1 89 ASP 89 114 114 ASP ASP A . n A 1 90 THR 90 115 115 THR THR A . n A 1 91 PRO 91 116 116 PRO PRO A . n A 1 92 PHE 92 117 117 PHE PHE A . n A 1 93 ILE 93 118 118 ILE ILE A . n A 1 94 LEU 94 119 119 LEU LEU A . n A 1 95 ILE 95 120 120 ILE ILE A . n A 1 96 ASP 96 121 121 ASP ASP A . n A 1 97 LEU 97 122 122 LEU LEU A . n A 1 98 MET 98 123 123 MET MET A . n A 1 99 ASN 99 124 124 ASN ASN A . n A 1 100 LEU 100 125 125 LEU LEU A . n A 1 101 ASN 101 126 126 ASN ASN A . n A 1 102 ARG 102 127 127 ARG ARG A . n A 1 103 VAL 103 128 128 VAL VAL A . n A 1 104 SER 104 129 129 SER SER A . n A 1 105 ILE 105 130 130 ILE ILE A . n A 1 106 ASP 106 131 131 ASP ASP A . n A 1 107 LEU 107 132 132 LEU LEU A . n A 1 108 GLU 108 133 133 GLU GLU A . n A 1 109 SER 109 134 134 SER SER A . n A 1 110 GLU 110 135 135 GLU GLU A . n A 1 111 THR 111 136 136 THR THR A . n A 1 112 ALA 112 137 137 ALA ALA A . n A 1 113 TRP 113 138 138 TRP TRP A . n A 1 114 VAL 114 139 139 VAL VAL A . n A 1 115 GLU 115 140 140 GLU GLU A . n A 1 116 SER 116 141 141 SER SER A . n A 1 117 GLY 117 142 142 GLY GLY A . n A 1 118 SER 118 143 143 SER SER A . n A 1 119 THR 119 144 144 THR THR A . n A 1 120 LEU 120 145 145 LEU LEU A . n A 1 121 GLY 121 146 146 GLY GLY A . n A 1 122 GLU 122 147 147 GLU GLU A . n A 1 123 LEU 123 148 148 LEU LEU A . n A 1 124 TYR 124 149 149 TYR TYR A . n A 1 125 TYR 125 150 150 TYR TYR A . n A 1 126 ALA 126 151 151 ALA ALA A . n A 1 127 ILE 127 152 152 ILE ILE A . n A 1 128 THR 128 153 153 THR THR A . n A 1 129 GLU 129 154 154 GLU GLU A . n A 1 130 SER 130 155 155 SER SER A . n A 1 131 SER 131 156 156 SER SER A . n A 1 132 SER 132 157 157 SER SER A . n A 1 133 LYS 133 158 158 LYS LYS A . n A 1 134 LEU 134 159 159 LEU LEU A . n A 1 135 GLY 135 160 160 GLY GLY A . n A 1 136 PHE 136 161 161 PHE PHE A . n A 1 137 THR 137 162 162 THR THR A . n A 1 138 ALA 138 163 163 ALA ALA A . n A 1 139 GLY 139 164 164 GLY GLY A . n A 1 140 TRP 140 165 165 TRP TRP A . n A 1 141 CYS 141 166 166 CYS CYS A . n A 1 142 PRO 142 167 167 PRO PRO A . n A 1 143 THR 143 168 168 THR THR A . n A 1 144 VAL 144 169 169 VAL VAL A . n A 1 145 GLY 145 170 170 GLY GLY A . n A 1 146 THR 146 171 171 THR THR A . n A 1 147 GLY 147 172 172 GLY GLY A . n A 1 148 GLY 148 173 173 GLY GLY A . n A 1 149 HIS 149 174 174 HIS HIS A . n A 1 150 ILE 150 175 175 ILE ILE A . n A 1 151 SER 151 176 176 SER SER A . n A 1 152 GLY 152 177 177 GLY GLY A . n A 1 153 GLY 153 178 178 GLY GLY A . n A 1 154 GLY 154 179 179 GLY GLY A . n A 1 155 PHE 155 180 180 PHE PHE A . n A 1 156 GLY 156 181 181 GLY GLY A . n A 1 157 MET 157 182 182 MET MET A . n A 1 158 MET 158 183 183 MET MET A . n A 1 159 SER 159 184 184 SER SER A . n A 1 160 ARG 160 185 185 ARG ARG A . n A 1 161 LYS 161 186 186 LYS LYS A . n A 1 162 TYR 162 187 187 TYR TYR A . n A 1 163 GLY 163 188 188 GLY GLY A . n A 1 164 LEU 164 189 189 LEU LEU A . n A 1 165 ALA 165 190 190 ALA ALA A . n A 1 166 ALA 166 191 191 ALA ALA A . n A 1 167 ASP 167 192 192 ASP ASP A . n A 1 168 ASN 168 193 193 ASN ASN A . n A 1 169 VAL 169 194 194 VAL VAL A . n A 1 170 VAL 170 195 195 VAL VAL A . n A 1 171 ASP 171 196 196 ASP ASP A . n A 1 172 ALA 172 197 197 ALA ALA A . n A 1 173 ILE 173 198 198 ILE ILE A . n A 1 174 LEU 174 199 199 LEU LEU A . n A 1 175 ILE 175 200 200 ILE ILE A . n A 1 176 ASP 176 201 201 ASP ASP A . n A 1 177 ALA 177 202 202 ALA ALA A . n A 1 178 ASN 178 203 203 ASN ASN A . n A 1 179 GLY 179 204 204 GLY GLY A . n A 1 180 ALA 180 205 205 ALA ALA A . n A 1 181 ILE 181 206 206 ILE ILE A . n A 1 182 LEU 182 207 207 LEU LEU A . n A 1 183 ASP 183 208 208 ASP ASP A . n A 1 184 ARG 184 209 209 ARG ARG A . n A 1 185 GLN 185 210 210 GLN GLN A . n A 1 186 ALA 186 211 211 ALA ALA A . n A 1 187 MET 187 212 212 MET MET A . n A 1 188 GLY 188 213 213 GLY GLY A . n A 1 189 GLU 189 214 214 GLU GLU A . n A 1 190 ASP 190 215 215 ASP ASP A . n A 1 191 VAL 191 216 216 VAL VAL A . n A 1 192 PHE 192 217 217 PHE PHE A . n A 1 193 TRP 193 218 218 TRP TRP A . n A 1 194 ALA 194 219 219 ALA ALA A . n A 1 195 ILE 195 220 220 ILE ILE A . n A 1 196 ARG 196 221 221 ARG ARG A . n A 1 197 GLY 197 222 222 GLY GLY A . n A 1 198 GLY 198 223 223 GLY GLY A . n A 1 199 GLY 199 224 224 GLY GLY A . n A 1 200 GLY 200 225 225 GLY GLY A . n A 1 201 GLY 201 226 226 GLY GLY A . n A 1 202 VAL 202 227 227 VAL VAL A . n A 1 203 TRP 203 228 228 TRP TRP A . n A 1 204 GLY 204 229 229 GLY GLY A . n A 1 205 ALA 205 230 230 ALA ALA A . n A 1 206 ILE 206 231 231 ILE ILE A . n A 1 207 TYR 207 232 232 TYR TYR A . n A 1 208 ALA 208 233 233 ALA ALA A . n A 1 209 TRP 209 234 234 TRP TRP A . n A 1 210 LYS 210 235 235 LYS LYS A . n A 1 211 ILE 211 236 236 ILE ILE A . n A 1 212 LYS 212 237 237 LYS LYS A . n A 1 213 LEU 213 238 238 LEU LEU A . n A 1 214 LEU 214 239 239 LEU LEU A . n A 1 215 PRO 215 240 240 PRO PRO A . n A 1 216 VAL 216 241 241 VAL VAL A . n A 1 217 PRO 217 242 242 PRO PRO A . n A 1 218 GLU 218 243 243 GLU GLU A . n A 1 219 LYS 219 244 244 LYS LYS A . n A 1 220 VAL 220 245 245 VAL VAL A . n A 1 221 THR 221 246 246 THR THR A . n A 1 222 VAL 222 247 247 VAL VAL A . n A 1 223 PHE 223 248 248 PHE PHE A . n A 1 224 ARG 224 249 249 ARG ARG A . n A 1 225 VAL 225 250 250 VAL VAL A . n A 1 226 THR 226 251 251 THR THR A . n A 1 227 LYS 227 252 252 LYS LYS A . n A 1 228 ASN 228 253 253 ASN ASN A . n A 1 229 VAL 229 254 254 VAL VAL A . n A 1 230 ALA 230 255 255 ALA ALA A . n A 1 231 ILE 231 256 256 ILE ILE A . n A 1 232 ASP 232 257 257 ASP ASP A . n A 1 233 GLU 233 258 258 GLU GLU A . n A 1 234 ALA 234 259 259 ALA ALA A . n A 1 235 THR 235 260 260 THR THR A . n A 1 236 SER 236 261 261 SER SER A . n A 1 237 LEU 237 262 262 LEU LEU A . n A 1 238 LEU 238 263 263 LEU LEU A . n A 1 239 HIS 239 264 264 HIS HIS A . n A 1 240 LYS 240 265 265 LYS LYS A . n A 1 241 TRP 241 266 266 TRP TRP A . n A 1 242 GLN 242 267 267 GLN GLN A . n A 1 243 PHE 243 268 268 PHE PHE A . n A 1 244 VAL 244 269 269 VAL VAL A . n A 1 245 ALA 245 270 270 ALA ALA A . n A 1 246 GLU 246 271 271 GLU GLU A . n A 1 247 GLU 247 272 272 GLU GLU A . n A 1 248 LEU 248 273 273 LEU LEU A . n A 1 249 GLU 249 274 274 GLU GLU A . n A 1 250 GLU 250 275 275 GLU GLU A . n A 1 251 ASP 251 276 276 ASP ASP A . n A 1 252 PHE 252 277 277 PHE PHE A . n A 1 253 THR 253 278 278 THR THR A . n A 1 254 LEU 254 279 279 LEU LEU A . n A 1 255 SER 255 280 280 SER SER A . n A 1 256 VAL 256 281 281 VAL VAL A . n A 1 257 LEU 257 282 282 LEU LEU A . n A 1 258 GLY 258 283 283 GLY GLY A . n A 1 259 GLY 259 284 284 GLY GLY A . n A 1 260 ALA 260 285 285 ALA ALA A . n A 1 261 ASP 261 286 286 ASP ASP A . n A 1 262 GLU 262 287 287 GLU GLU A . n A 1 263 LYS 263 288 288 LYS LYS A . n A 1 264 GLN 264 289 289 GLN GLN A . n A 1 265 VAL 265 290 290 VAL VAL A . n A 1 266 TRP 266 291 291 TRP TRP A . n A 1 267 LEU 267 292 292 LEU LEU A . n A 1 268 THR 268 293 293 THR THR A . n A 1 269 MET 269 294 294 MET MET A . n A 1 270 LEU 270 295 295 LEU LEU A . n A 1 271 GLY 271 296 296 GLY GLY A . n A 1 272 PHE 272 297 297 PHE PHE A . n A 1 273 HIS 273 298 298 HIS HIS A . n A 1 274 PHE 274 299 299 PHE PHE A . n A 1 275 GLY 275 300 300 GLY GLY A . n A 1 276 LEU 276 301 301 LEU LEU A . n A 1 277 LYS 277 302 302 LYS LYS A . n A 1 278 THR 278 303 303 THR THR A . n A 1 279 VAL 279 304 304 VAL VAL A . n A 1 280 ALA 280 305 305 ALA ALA A . n A 1 281 LYS 281 306 306 LYS LYS A . n A 1 282 SER 282 307 307 SER SER A . n A 1 283 THR 283 308 308 THR THR A . n A 1 284 PHE 284 309 309 PHE PHE A . n A 1 285 ASP 285 310 310 ASP ASP A . n A 1 286 LEU 286 311 311 LEU LEU A . n A 1 287 LEU 287 312 312 LEU LEU A . n A 1 288 PHE 288 313 313 PHE PHE A . n A 1 289 PRO 289 314 314 PRO PRO A . n A 1 290 GLU 290 315 315 GLU GLU A . n A 1 291 LEU 291 316 316 LEU LEU A . n A 1 292 GLY 292 317 317 GLY GLY A . n A 1 293 LEU 293 318 318 LEU LEU A . n A 1 294 VAL 294 319 319 VAL VAL A . n A 1 295 GLU 295 320 320 GLU GLU A . n A 1 296 GLU 296 321 321 GLU GLU A . n A 1 297 ASP 297 322 322 ASP ASP A . n A 1 298 TYR 298 323 323 TYR TYR A . n A 1 299 LEU 299 324 324 LEU LEU A . n A 1 300 GLU 300 325 325 GLU GLU A . n A 1 301 MET 301 326 326 MET MET A . n A 1 302 SER 302 327 327 SER SER A . n A 1 303 TRP 303 328 328 TRP TRP A . n A 1 304 GLY 304 329 329 GLY GLY A . n A 1 305 GLU 305 330 330 GLU GLU A . n A 1 306 SER 306 331 331 SER SER A . n A 1 307 PHE 307 332 332 PHE PHE A . n A 1 308 ALA 308 333 333 ALA ALA A . n A 1 309 TYR 309 334 334 TYR TYR A . n A 1 310 LEU 310 335 335 LEU LEU A . n A 1 311 ALA 311 336 336 ALA ALA A . n A 1 312 GLY 312 337 337 GLY GLY A . n A 1 313 LEU 313 338 338 LEU LEU A . n A 1 314 GLU 314 339 339 GLU GLU A . n A 1 315 THR 315 340 340 THR THR A . n A 1 316 VAL 316 341 341 VAL VAL A . n A 1 317 SER 317 342 342 SER SER A . n A 1 318 GLN 318 343 343 GLN GLN A . n A 1 319 LEU 319 344 344 LEU LEU A . n A 1 320 ASN 320 345 345 ASN ASN A . n A 1 321 ASN 321 346 346 ASN ASN A . n A 1 322 ARG 322 347 347 ARG ARG A . n A 1 323 PHE 323 348 348 PHE PHE A . n A 1 324 LEU 324 349 349 LEU LEU A . n A 1 325 LYS 325 350 350 LYS LYS A . n A 1 326 PHE 326 351 351 PHE PHE A . n A 1 327 ASP 327 352 352 ASP ASP A . n A 1 328 GLU 328 353 353 GLU GLU A . n A 1 329 ARG 329 354 354 ARG ARG A . n A 1 330 ALA 330 355 355 ALA ALA A . n A 1 331 PHE 331 356 356 PHE PHE A . n A 1 332 LYS 332 357 357 LYS LYS A . n A 1 333 THR 333 358 358 THR THR A . n A 1 334 LYS 334 359 359 LYS LYS A . n A 1 335 VAL 335 360 360 VAL VAL A . n A 1 336 ASP 336 361 361 ASP ASP A . n A 1 337 LEU 337 362 362 LEU LEU A . n A 1 338 THR 338 363 363 THR THR A . n A 1 339 LYS 339 364 364 LYS LYS A . n A 1 340 GLU 340 365 365 GLU GLU A . n A 1 341 PRO 341 366 366 PRO PRO A . n A 1 342 LEU 342 367 367 LEU LEU A . n A 1 343 PRO 343 368 368 PRO PRO A . n A 1 344 SER 344 369 369 SER SER A . n A 1 345 LYS 345 370 370 LYS LYS A . n A 1 346 ALA 346 371 371 ALA ALA A . n A 1 347 PHE 347 372 372 PHE PHE A . n A 1 348 TYR 348 373 373 TYR TYR A . n A 1 349 GLY 349 374 374 GLY GLY A . n A 1 350 LEU 350 375 375 LEU LEU A . n A 1 351 LEU 351 376 376 LEU LEU A . n A 1 352 GLU 352 377 377 GLU GLU A . n A 1 353 ARG 353 378 378 ARG ARG A . n A 1 354 LEU 354 379 379 LEU LEU A . n A 1 355 SER 355 380 380 SER SER A . n A 1 356 LYS 356 381 381 LYS LYS A . n A 1 357 GLU 357 382 382 GLU GLU A . n A 1 358 PRO 358 383 383 PRO PRO A . n A 1 359 ASN 359 384 384 ASN ASN A . n A 1 360 GLY 360 385 385 GLY GLY A . n A 1 361 PHE 361 386 386 PHE PHE A . n A 1 362 ILE 362 387 387 ILE ILE A . n A 1 363 ALA 363 388 388 ALA ALA A . n A 1 364 LEU 364 389 389 LEU LEU A . n A 1 365 ASN 365 390 390 ASN ASN A . n A 1 366 GLY 366 391 391 GLY GLY A . n A 1 367 PHE 367 392 392 PHE PHE A . n A 1 368 GLY 368 393 393 GLY GLY A . n A 1 369 GLY 369 394 394 GLY GLY A . n A 1 370 GLN 370 395 395 GLN GLN A . n A 1 371 MET 371 396 396 MET MET A . n A 1 372 SER 372 397 397 SER SER A . n A 1 373 LYS 373 398 398 LYS LYS A . n A 1 374 ILE 374 399 399 ILE ILE A . n A 1 375 SER 375 400 400 SER SER A . n A 1 376 SER 376 401 401 SER SER A . n A 1 377 ASP 377 402 402 ASP ASP A . n A 1 378 PHE 378 403 403 PHE PHE A . n A 1 379 THR 379 404 404 THR THR A . n A 1 380 PRO 380 405 405 PRO PRO A . n A 1 381 PHE 381 406 406 PHE PHE A . n A 1 382 PRO 382 407 407 PRO PRO A . n A 1 383 HIS 383 408 408 HIS HIS A . n A 1 384 ARG 384 409 409 ARG ARG A . n A 1 385 SER 385 410 410 SER SER A . n A 1 386 GLY 386 411 411 GLY GLY A . n A 1 387 THR 387 412 412 THR THR A . n A 1 388 ARG 388 413 413 ARG ARG A . n A 1 389 LEU 389 414 414 LEU LEU A . n A 1 390 MET 390 415 415 MET MET A . n A 1 391 VAL 391 416 416 VAL VAL A . n A 1 392 GLU 392 417 417 GLU GLU A . n A 1 393 TYR 393 418 418 TYR TYR A . n A 1 394 ILE 394 419 419 ILE ILE A . n A 1 395 VAL 395 420 420 VAL VAL A . n A 1 396 ALA 396 421 421 ALA ALA A . n A 1 397 TRP 397 422 422 TRP TRP A . n A 1 398 ASN 398 423 423 ASN ASN A . n A 1 399 GLN 399 424 424 GLN GLN A . n A 1 400 SER 400 425 425 SER SER A . n A 1 401 GLU 401 426 426 GLU GLU A . n A 1 402 GLN 402 427 427 GLN GLN A . n A 1 403 LYS 403 428 428 LYS LYS A . n A 1 404 LYS 404 429 429 LYS LYS A . n A 1 405 LYS 405 430 430 LYS LYS A . n A 1 406 THR 406 431 431 THR THR A . n A 1 407 GLU 407 432 432 GLU GLU A . n A 1 408 PHE 408 433 433 PHE PHE A . n A 1 409 LEU 409 434 434 LEU LEU A . n A 1 410 ASP 410 435 435 ASP ASP A . n A 1 411 TRP 411 436 436 TRP TRP A . n A 1 412 LEU 412 437 437 LEU LEU A . n A 1 413 GLU 413 438 438 GLU GLU A . n A 1 414 LYS 414 439 439 LYS LYS A . n A 1 415 VAL 415 440 440 VAL VAL A . n A 1 416 TYR 416 441 441 TYR TYR A . n A 1 417 GLU 417 442 442 GLU GLU A . n A 1 418 PHE 418 443 443 PHE PHE A . n A 1 419 MET 419 444 444 MET MET A . n A 1 420 LYS 420 445 445 LYS LYS A . n A 1 421 PRO 421 446 446 PRO PRO A . n A 1 422 PHE 422 447 447 PHE PHE A . n A 1 423 VAL 423 448 448 VAL VAL A . n A 1 424 SER 424 449 449 SER SER A . n A 1 425 LYS 425 450 450 LYS LYS A . n A 1 426 ASN 426 451 451 ASN ASN A . n A 1 427 PRO 427 452 452 PRO PRO A . n A 1 428 ARG 428 453 453 ARG ARG A . n A 1 429 LEU 429 454 454 LEU LEU A . n A 1 430 GLY 430 455 455 GLY GLY A . n A 1 431 TYR 431 456 456 TYR TYR A . n A 1 432 VAL 432 457 457 VAL VAL A . n A 1 433 ASN 433 458 458 ASN ASN A . n A 1 434 HIS 434 459 459 HIS HIS A . n A 1 435 ILE 435 460 460 ILE ILE A . n A 1 436 ASP 436 461 461 ASP ASP A . n A 1 437 LEU 437 462 462 LEU LEU A . n A 1 438 ASP 438 463 463 ASP ASP A . n A 1 439 LEU 439 464 464 LEU LEU A . n A 1 440 GLY 440 465 465 GLY GLY A . n A 1 441 GLY 441 466 466 GLY GLY A . n A 1 442 ILE 442 467 467 ILE ILE A . n A 1 443 ASP 443 468 468 ASP ASP A . n A 1 444 TRP 444 469 469 TRP TRP A . n A 1 445 GLY 445 470 470 GLY GLY A . n A 1 446 ASN 446 471 471 ASN ASN A . n A 1 447 LYS 447 472 472 LYS LYS A . n A 1 448 THR 448 473 473 THR THR A . n A 1 449 VAL 449 474 474 VAL VAL A . n A 1 450 VAL 450 475 475 VAL VAL A . n A 1 451 ASN 451 476 476 ASN ASN A . n A 1 452 ASN 452 477 477 ASN ASN A . n A 1 453 ALA 453 478 478 ALA ALA A . n A 1 454 ILE 454 479 479 ILE ILE A . n A 1 455 GLU 455 480 480 GLU GLU A . n A 1 456 ILE 456 481 481 ILE ILE A . n A 1 457 SER 457 482 482 SER SER A . n A 1 458 ARG 458 483 483 ARG ARG A . n A 1 459 SER 459 484 484 SER SER A . n A 1 460 TRP 460 485 485 TRP TRP A . n A 1 461 GLY 461 486 486 GLY GLY A . n A 1 462 GLU 462 487 487 GLU GLU A . n A 1 463 SER 463 488 488 SER SER A . n A 1 464 TYR 464 489 489 TYR TYR A . n A 1 465 PHE 465 490 490 PHE PHE A . n A 1 466 LEU 466 491 491 LEU LEU A . n A 1 467 SER 467 492 492 SER SER A . n A 1 468 ASN 468 493 493 ASN ASN A . n A 1 469 TYR 469 494 494 TYR TYR A . n A 1 470 GLU 470 495 495 GLU GLU A . n A 1 471 ARG 471 496 496 ARG ARG A . n A 1 472 LEU 472 497 497 LEU LEU A . n A 1 473 ILE 473 498 498 ILE ILE A . n A 1 474 ARG 474 499 499 ARG ARG A . n A 1 475 ALA 475 500 500 ALA ALA A . n A 1 476 LYS 476 501 501 LYS LYS A . n A 1 477 THR 477 502 502 THR THR A . n A 1 478 LEU 478 503 503 LEU LEU A . n A 1 479 ILE 479 504 504 ILE ILE A . n A 1 480 ASP 480 505 505 ASP ASP A . n A 1 481 PRO 481 506 506 PRO PRO A . n A 1 482 ASN 482 507 507 ASN ASN A . n A 1 483 ASN 483 508 508 ASN ASN A . n A 1 484 VAL 484 509 509 VAL VAL A . n A 1 485 PHE 485 510 510 PHE PHE A . n A 1 486 ASN 486 511 511 ASN ASN A . n A 1 487 HIS 487 512 512 HIS HIS A . n A 1 488 PRO 488 513 513 PRO PRO A . n A 1 489 GLN 489 514 514 GLN GLN A . n A 1 490 SER 490 515 515 SER SER A . n A 1 491 ILE 491 516 516 ILE ILE A . n A 1 492 PRO 492 517 517 PRO PRO A . n A 1 493 PRO 493 518 518 PRO PRO A . n A 1 494 MET 494 519 519 MET MET A . n A 1 495 ALA 495 520 520 ALA ALA 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 FAD 1 1 1 FAD FAD A . C 3 SLX 1 2 2 SLX SLX A . D 4 MAN 1 3 3 MAN MAN A . E 5 NAG 2 521 1 NAG NAG A . F 5 NAG 3 522 2 NAG NAG A . G 5 NAG 1 523 1 NAG NAG A . H 6 MG 1 524 1 MG MG A . I 7 HOH 1 4 4 HOH HOH A . I 7 HOH 2 5 5 HOH HOH A . I 7 HOH 3 6 6 HOH HOH A . I 7 HOH 4 7 7 HOH HOH A . I 7 HOH 5 8 8 HOH HOH A . I 7 HOH 6 9 9 HOH HOH A . I 7 HOH 7 10 10 HOH HOH A . I 7 HOH 8 11 11 HOH HOH A . I 7 HOH 9 12 12 HOH HOH A . I 7 HOH 10 13 13 HOH HOH A . I 7 HOH 11 14 14 HOH HOH A . I 7 HOH 12 15 15 HOH HOH A . I 7 HOH 13 16 16 HOH HOH A . I 7 HOH 14 17 17 HOH HOH A . I 7 HOH 15 18 18 HOH HOH A . I 7 HOH 16 19 19 HOH HOH A . I 7 HOH 17 20 20 HOH HOH A . I 7 HOH 18 21 21 HOH HOH A . I 7 HOH 19 22 22 HOH HOH A . I 7 HOH 20 23 23 HOH HOH A . I 7 HOH 21 24 24 HOH HOH A . I 7 HOH 22 25 25 HOH HOH A . I 7 HOH 23 525 525 HOH HOH A . I 7 HOH 24 526 526 HOH HOH A . I 7 HOH 25 527 527 HOH HOH A . I 7 HOH 26 528 528 HOH HOH A . I 7 HOH 27 529 529 HOH HOH A . I 7 HOH 28 530 530 HOH HOH A . I 7 HOH 29 531 531 HOH HOH A . I 7 HOH 30 532 532 HOH HOH A . I 7 HOH 31 533 533 HOH HOH A . I 7 HOH 32 534 534 HOH HOH A . I 7 HOH 33 535 535 HOH HOH A . I 7 HOH 34 536 536 HOH HOH A . I 7 HOH 35 537 537 HOH HOH A . I 7 HOH 36 538 538 HOH HOH A . I 7 HOH 37 539 539 HOH HOH A . I 7 HOH 38 540 540 HOH HOH A . I 7 HOH 39 541 541 HOH HOH A . I 7 HOH 40 542 542 HOH HOH A . I 7 HOH 41 543 543 HOH HOH A . I 7 HOH 42 544 544 HOH HOH A . I 7 HOH 43 545 545 HOH HOH A . I 7 HOH 44 546 546 HOH HOH A . I 7 HOH 45 547 547 HOH HOH A . I 7 HOH 46 548 548 HOH HOH A . I 7 HOH 47 549 549 HOH HOH A . I 7 HOH 48 550 550 HOH HOH A . I 7 HOH 49 551 551 HOH HOH A . I 7 HOH 50 552 552 HOH HOH A . I 7 HOH 51 553 553 HOH HOH A . I 7 HOH 52 554 554 HOH HOH A . I 7 HOH 53 555 555 HOH HOH A . I 7 HOH 54 556 556 HOH HOH A . I 7 HOH 55 557 557 HOH HOH A . I 7 HOH 56 558 558 HOH HOH A . I 7 HOH 57 559 559 HOH HOH A . I 7 HOH 58 560 560 HOH HOH A . I 7 HOH 59 561 561 HOH HOH A . I 7 HOH 60 562 562 HOH HOH A . I 7 HOH 61 563 563 HOH HOH A . I 7 HOH 62 564 564 HOH HOH A . I 7 HOH 63 565 565 HOH HOH A . I 7 HOH 64 566 566 HOH HOH A . I 7 HOH 65 567 567 HOH HOH A . I 7 HOH 66 568 568 HOH HOH A . I 7 HOH 67 569 569 HOH HOH A . I 7 HOH 68 570 570 HOH HOH A . I 7 HOH 69 571 571 HOH HOH A . I 7 HOH 70 572 572 HOH HOH A . I 7 HOH 71 573 573 HOH HOH A . I 7 HOH 72 574 574 HOH HOH A . I 7 HOH 73 575 575 HOH HOH A . I 7 HOH 74 576 2 HOH HOH A . I 7 HOH 75 577 577 HOH HOH A . I 7 HOH 76 578 3 HOH HOH A . I 7 HOH 77 579 579 HOH HOH A . I 7 HOH 78 580 580 HOH HOH A . I 7 HOH 79 581 581 HOH HOH A . I 7 HOH 80 582 582 HOH HOH A . I 7 HOH 81 583 583 HOH HOH A . I 7 HOH 82 584 584 HOH HOH A . I 7 HOH 83 585 585 HOH HOH A . I 7 HOH 84 586 586 HOH HOH A . I 7 HOH 85 587 587 HOH HOH A . I 7 HOH 86 588 588 HOH HOH A . I 7 HOH 87 589 589 HOH HOH A . I 7 HOH 88 590 590 HOH HOH A . I 7 HOH 89 591 591 HOH HOH A . I 7 HOH 90 592 592 HOH HOH A . I 7 HOH 91 593 593 HOH HOH A . I 7 HOH 92 594 594 HOH HOH A . I 7 HOH 93 595 595 HOH HOH A . I 7 HOH 94 596 596 HOH HOH A . I 7 HOH 95 597 597 HOH HOH A . I 7 HOH 96 598 598 HOH HOH A . I 7 HOH 97 599 599 HOH HOH A . I 7 HOH 98 600 600 HOH HOH A . I 7 HOH 99 601 601 HOH HOH A . I 7 HOH 100 602 602 HOH HOH A . I 7 HOH 101 603 603 HOH HOH A . I 7 HOH 102 604 604 HOH HOH A . I 7 HOH 103 605 605 HOH HOH A . I 7 HOH 104 606 606 HOH HOH A . I 7 HOH 105 607 607 HOH HOH A . I 7 HOH 106 608 608 HOH HOH A . I 7 HOH 107 609 609 HOH HOH A . I 7 HOH 108 610 610 HOH HOH A . I 7 HOH 109 611 611 HOH HOH A . I 7 HOH 110 612 612 HOH HOH A . I 7 HOH 111 613 613 HOH HOH A . I 7 HOH 112 614 614 HOH HOH A . I 7 HOH 113 615 615 HOH HOH A . I 7 HOH 114 616 1 HOH HOH A . I 7 HOH 115 617 2 HOH HOH A . I 7 HOH 116 618 3 HOH HOH A . I 7 HOH 117 619 4 HOH HOH A . I 7 HOH 118 620 5 HOH HOH A . I 7 HOH 119 621 26 HOH HOH A . I 7 HOH 120 622 27 HOH HOH A . I 7 HOH 121 623 28 HOH HOH A . I 7 HOH 122 624 29 HOH HOH A . I 7 HOH 123 625 30 HOH HOH A . I 7 HOH 124 626 31 HOH HOH A . I 7 HOH 125 627 32 HOH HOH A . I 7 HOH 126 628 33 HOH HOH A . I 7 HOH 127 629 34 HOH HOH A . I 7 HOH 128 630 35 HOH HOH A . I 7 HOH 129 631 36 HOH HOH A . I 7 HOH 130 632 37 HOH HOH A . I 7 HOH 131 633 38 HOH HOH A . I 7 HOH 132 634 39 HOH HOH A . I 7 HOH 133 635 40 HOH HOH A . I 7 HOH 134 636 41 HOH HOH A . I 7 HOH 135 637 42 HOH HOH A . I 7 HOH 136 638 43 HOH HOH A . I 7 HOH 137 639 44 HOH HOH A . I 7 HOH 138 640 45 HOH HOH A . I 7 HOH 139 641 46 HOH HOH A . I 7 HOH 140 642 47 HOH HOH A . I 7 HOH 141 643 48 HOH HOH A . I 7 HOH 142 644 49 HOH HOH A . I 7 HOH 143 645 50 HOH HOH A . I 7 HOH 144 646 51 HOH HOH A . I 7 HOH 145 647 52 HOH HOH A . I 7 HOH 146 648 53 HOH HOH A . I 7 HOH 147 649 54 HOH HOH A . I 7 HOH 148 650 55 HOH HOH A . I 7 HOH 149 651 56 HOH HOH A . I 7 HOH 150 652 57 HOH HOH A . I 7 HOH 151 653 58 HOH HOH A . I 7 HOH 152 654 59 HOH HOH A . I 7 HOH 153 655 60 HOH HOH A . I 7 HOH 154 656 61 HOH HOH A . I 7 HOH 155 657 62 HOH HOH A . I 7 HOH 156 658 63 HOH HOH A . I 7 HOH 157 659 64 HOH HOH A . I 7 HOH 158 660 65 HOH HOH A . I 7 HOH 159 661 66 HOH HOH A . I 7 HOH 160 662 68 HOH HOH A . I 7 HOH 161 663 69 HOH HOH A . I 7 HOH 162 664 70 HOH HOH A . I 7 HOH 163 665 71 HOH HOH A . I 7 HOH 164 666 72 HOH HOH A . I 7 HOH 165 667 73 HOH HOH A . I 7 HOH 166 668 74 HOH HOH A . I 7 HOH 167 669 75 HOH HOH A . I 7 HOH 168 670 76 HOH HOH A . I 7 HOH 169 671 77 HOH HOH A . I 7 HOH 170 672 79 HOH HOH A . I 7 HOH 171 673 80 HOH HOH A . I 7 HOH 172 674 81 HOH HOH A . I 7 HOH 173 675 82 HOH HOH A . I 7 HOH 174 676 83 HOH HOH A . I 7 HOH 175 677 84 HOH HOH A . I 7 HOH 176 678 85 HOH HOH A . I 7 HOH 177 679 86 HOH HOH A . I 7 HOH 178 680 87 HOH HOH A . I 7 HOH 179 681 88 HOH HOH A . I 7 HOH 180 682 89 HOH HOH A . I 7 HOH 181 683 90 HOH HOH A . I 7 HOH 182 684 91 HOH HOH A . I 7 HOH 183 685 92 HOH HOH A . I 7 HOH 184 686 93 HOH HOH A . I 7 HOH 185 687 94 HOH HOH A . I 7 HOH 186 688 95 HOH HOH A . I 7 HOH 187 689 96 HOH HOH A . I 7 HOH 188 690 97 HOH HOH A . I 7 HOH 189 691 99 HOH HOH A . I 7 HOH 190 692 100 HOH HOH A . I 7 HOH 191 693 101 HOH HOH A . I 7 HOH 192 694 102 HOH HOH A . I 7 HOH 193 695 103 HOH HOH A . I 7 HOH 194 696 104 HOH HOH A . I 7 HOH 195 697 105 HOH HOH A . I 7 HOH 196 698 106 HOH HOH A . I 7 HOH 197 699 107 HOH HOH A . I 7 HOH 198 700 108 HOH HOH A . I 7 HOH 199 701 109 HOH HOH A . I 7 HOH 200 702 110 HOH HOH A . I 7 HOH 201 703 111 HOH HOH A . I 7 HOH 202 704 112 HOH HOH A . I 7 HOH 203 705 113 HOH HOH A . I 7 HOH 204 706 114 HOH HOH A . I 7 HOH 205 707 115 HOH HOH A . I 7 HOH 206 708 116 HOH HOH A . I 7 HOH 207 709 117 HOH HOH A . I 7 HOH 208 710 119 HOH HOH A . I 7 HOH 209 711 120 HOH HOH A . I 7 HOH 210 712 121 HOH HOH A . I 7 HOH 211 713 122 HOH HOH A . I 7 HOH 212 714 123 HOH HOH A . I 7 HOH 213 715 124 HOH HOH A . I 7 HOH 214 716 125 HOH HOH A . I 7 HOH 215 717 126 HOH HOH A . I 7 HOH 216 718 127 HOH HOH A . I 7 HOH 217 719 128 HOH HOH A . I 7 HOH 218 720 129 HOH HOH A . I 7 HOH 219 721 130 HOH HOH A . I 7 HOH 220 722 131 HOH HOH A . I 7 HOH 221 723 132 HOH HOH A . I 7 HOH 222 724 133 HOH HOH A . I 7 HOH 223 725 134 HOH HOH A . I 7 HOH 224 726 135 HOH HOH A . I 7 HOH 225 727 136 HOH HOH A . I 7 HOH 226 728 137 HOH HOH A . I 7 HOH 227 729 138 HOH HOH A . I 7 HOH 228 730 139 HOH HOH A . I 7 HOH 229 731 140 HOH HOH A . I 7 HOH 230 732 141 HOH HOH A . I 7 HOH 231 733 142 HOH HOH A . I 7 HOH 232 734 143 HOH HOH A . I 7 HOH 233 735 144 HOH HOH A . I 7 HOH 234 736 145 HOH HOH A . I 7 HOH 235 737 146 HOH HOH A . I 7 HOH 236 738 147 HOH HOH A . I 7 HOH 237 739 148 HOH HOH A . I 7 HOH 238 740 149 HOH HOH A . I 7 HOH 239 741 150 HOH HOH A . I 7 HOH 240 742 151 HOH HOH A . I 7 HOH 241 743 152 HOH HOH A . I 7 HOH 242 744 153 HOH HOH A . I 7 HOH 243 745 154 HOH HOH A . I 7 HOH 244 746 155 HOH HOH A . I 7 HOH 245 747 156 HOH HOH A . I 7 HOH 246 748 157 HOH HOH A . I 7 HOH 247 749 158 HOH HOH A . I 7 HOH 248 750 159 HOH HOH A . I 7 HOH 249 751 160 HOH HOH A . I 7 HOH 250 752 161 HOH HOH A . I 7 HOH 251 753 162 HOH HOH A . I 7 HOH 252 754 163 HOH HOH A . I 7 HOH 253 755 164 HOH HOH A . I 7 HOH 254 756 165 HOH HOH A . I 7 HOH 255 757 166 HOH HOH A . I 7 HOH 256 758 167 HOH HOH A . I 7 HOH 257 759 168 HOH HOH A . I 7 HOH 258 760 169 HOH HOH A . I 7 HOH 259 761 170 HOH HOH A . I 7 HOH 260 762 171 HOH HOH A . I 7 HOH 261 763 172 HOH HOH A . I 7 HOH 262 764 174 HOH HOH A . I 7 HOH 263 765 175 HOH HOH A . I 7 HOH 264 766 176 HOH HOH A . I 7 HOH 265 767 177 HOH HOH A . I 7 HOH 266 768 178 HOH HOH A . I 7 HOH 267 769 179 HOH HOH A . I 7 HOH 268 770 180 HOH HOH A . I 7 HOH 269 771 182 HOH HOH A . I 7 HOH 270 772 183 HOH HOH A . I 7 HOH 271 773 184 HOH HOH A . I 7 HOH 272 774 185 HOH HOH A . I 7 HOH 273 775 186 HOH HOH A . I 7 HOH 274 776 187 HOH HOH A . I 7 HOH 275 777 188 HOH HOH A . I 7 HOH 276 778 189 HOH HOH A . I 7 HOH 277 779 190 HOH HOH A . I 7 HOH 278 780 191 HOH HOH A . I 7 HOH 279 781 192 HOH HOH A . I 7 HOH 280 782 194 HOH HOH A . I 7 HOH 281 783 195 HOH HOH A . I 7 HOH 282 784 196 HOH HOH A . I 7 HOH 283 785 197 HOH HOH A . I 7 HOH 284 786 198 HOH HOH A . I 7 HOH 285 787 199 HOH HOH A . I 7 HOH 286 788 200 HOH HOH A . I 7 HOH 287 789 202 HOH HOH A . I 7 HOH 288 790 203 HOH HOH A . I 7 HOH 289 791 204 HOH HOH A . I 7 HOH 290 792 205 HOH HOH A . I 7 HOH 291 793 206 HOH HOH A . I 7 HOH 292 794 207 HOH HOH A . I 7 HOH 293 795 208 HOH HOH A . I 7 HOH 294 796 209 HOH HOH A . I 7 HOH 295 797 210 HOH HOH A . I 7 HOH 296 798 211 HOH HOH A . I 7 HOH 297 799 212 HOH HOH A . I 7 HOH 298 800 213 HOH HOH A . I 7 HOH 299 801 214 HOH HOH A . I 7 HOH 300 802 215 HOH HOH A . I 7 HOH 301 803 216 HOH HOH A . I 7 HOH 302 804 217 HOH HOH A . I 7 HOH 303 805 218 HOH HOH A . I 7 HOH 304 806 219 HOH HOH A . I 7 HOH 305 807 220 HOH HOH A . I 7 HOH 306 808 221 HOH HOH A . I 7 HOH 307 809 222 HOH HOH A . I 7 HOH 308 810 223 HOH HOH A . I 7 HOH 309 811 224 HOH HOH A . I 7 HOH 310 812 225 HOH HOH A . I 7 HOH 311 813 226 HOH HOH A . I 7 HOH 312 814 227 HOH HOH A . I 7 HOH 313 815 228 HOH HOH A . I 7 HOH 314 816 229 HOH HOH A . I 7 HOH 315 817 230 HOH HOH A . I 7 HOH 316 818 231 HOH HOH A . I 7 HOH 317 819 232 HOH HOH A . I 7 HOH 318 820 233 HOH HOH A . I 7 HOH 319 821 234 HOH HOH A . I 7 HOH 320 822 235 HOH HOH A . I 7 HOH 321 823 236 HOH HOH A . I 7 HOH 322 824 237 HOH HOH A . I 7 HOH 323 825 238 HOH HOH A . I 7 HOH 324 826 239 HOH HOH A . I 7 HOH 325 827 240 HOH HOH A . I 7 HOH 326 828 241 HOH HOH A . I 7 HOH 327 829 242 HOH HOH A . I 7 HOH 328 830 243 HOH HOH A . I 7 HOH 329 831 244 HOH HOH A . I 7 HOH 330 832 245 HOH HOH A . I 7 HOH 331 833 246 HOH HOH A . I 7 HOH 332 834 247 HOH HOH A . I 7 HOH 333 835 248 HOH HOH A . I 7 HOH 334 836 249 HOH HOH A . I 7 HOH 335 837 250 HOH HOH A . I 7 HOH 336 838 251 HOH HOH A . I 7 HOH 337 839 252 HOH HOH A . I 7 HOH 338 840 253 HOH HOH A . I 7 HOH 339 841 254 HOH HOH A . I 7 HOH 340 842 255 HOH HOH A . I 7 HOH 341 843 256 HOH HOH A . I 7 HOH 342 844 257 HOH HOH A . I 7 HOH 343 845 258 HOH HOH A . I 7 HOH 344 846 260 HOH HOH A . I 7 HOH 345 847 261 HOH HOH A . I 7 HOH 346 848 262 HOH HOH A . I 7 HOH 347 849 263 HOH HOH A . I 7 HOH 348 850 264 HOH HOH A . I 7 HOH 349 851 265 HOH HOH A . I 7 HOH 350 852 266 HOH HOH A . I 7 HOH 351 853 267 HOH HOH A . I 7 HOH 352 854 268 HOH HOH A . I 7 HOH 353 855 269 HOH HOH A . I 7 HOH 354 856 270 HOH HOH A . I 7 HOH 355 857 271 HOH HOH A . I 7 HOH 356 858 272 HOH HOH A . I 7 HOH 357 859 273 HOH HOH A . I 7 HOH 358 860 274 HOH HOH A . I 7 HOH 359 861 275 HOH HOH A . I 7 HOH 360 862 276 HOH HOH A . I 7 HOH 361 863 277 HOH HOH A . I 7 HOH 362 864 278 HOH HOH A . I 7 HOH 363 865 279 HOH HOH A . I 7 HOH 364 866 280 HOH HOH A . I 7 HOH 365 867 281 HOH HOH A . I 7 HOH 366 868 282 HOH HOH A . I 7 HOH 367 869 283 HOH HOH A . I 7 HOH 368 870 284 HOH HOH A . I 7 HOH 369 871 285 HOH HOH A . I 7 HOH 370 872 286 HOH HOH A . I 7 HOH 371 873 287 HOH HOH A . I 7 HOH 372 874 288 HOH HOH A . I 7 HOH 373 875 289 HOH HOH A . I 7 HOH 374 876 290 HOH HOH A . I 7 HOH 375 877 291 HOH HOH A . I 7 HOH 376 878 292 HOH HOH A . I 7 HOH 377 879 293 HOH HOH A . I 7 HOH 378 880 294 HOH HOH A . I 7 HOH 379 881 295 HOH HOH A . I 7 HOH 380 882 296 HOH HOH A . I 7 HOH 381 883 297 HOH HOH A . I 7 HOH 382 884 298 HOH HOH A . I 7 HOH 383 885 299 HOH HOH A . I 7 HOH 384 886 300 HOH HOH A . I 7 HOH 385 887 301 HOH HOH A . I 7 HOH 386 888 302 HOH HOH A . I 7 HOH 387 889 303 HOH HOH A . I 7 HOH 388 890 304 HOH HOH A . I 7 HOH 389 891 305 HOH HOH A . I 7 HOH 390 892 306 HOH HOH A . I 7 HOH 391 893 307 HOH HOH A . I 7 HOH 392 894 308 HOH HOH A . I 7 HOH 393 895 309 HOH HOH A . I 7 HOH 394 896 310 HOH HOH A . I 7 HOH 395 897 311 HOH HOH A . I 7 HOH 396 898 312 HOH HOH A . I 7 HOH 397 899 313 HOH HOH A . I 7 HOH 398 900 314 HOH HOH A . I 7 HOH 399 901 315 HOH HOH A . I 7 HOH 400 902 316 HOH HOH A . I 7 HOH 401 903 317 HOH HOH A . I 7 HOH 402 904 318 HOH HOH A . I 7 HOH 403 905 319 HOH HOH A . I 7 HOH 404 906 320 HOH HOH A . I 7 HOH 405 907 321 HOH HOH A . I 7 HOH 406 908 322 HOH HOH A . I 7 HOH 407 909 323 HOH HOH A . I 7 HOH 408 910 324 HOH HOH A . I 7 HOH 409 911 325 HOH HOH A . I 7 HOH 410 912 326 HOH HOH A . I 7 HOH 411 913 327 HOH HOH A . I 7 HOH 412 914 328 HOH HOH A . I 7 HOH 413 915 329 HOH HOH A . I 7 HOH 414 916 330 HOH HOH A . I 7 HOH 415 917 331 HOH HOH A . I 7 HOH 416 918 332 HOH HOH A . I 7 HOH 417 919 333 HOH HOH A . I 7 HOH 418 920 334 HOH HOH A . I 7 HOH 419 921 335 HOH HOH A . I 7 HOH 420 922 336 HOH HOH A . I 7 HOH 421 923 337 HOH HOH A . I 7 HOH 422 924 338 HOH HOH A . I 7 HOH 423 925 339 HOH HOH A . I 7 HOH 424 926 340 HOH HOH A . I 7 HOH 425 927 341 HOH HOH A . I 7 HOH 426 928 342 HOH HOH A . I 7 HOH 427 929 343 HOH HOH A . I 7 HOH 428 930 344 HOH HOH A . I 7 HOH 429 931 345 HOH HOH A . I 7 HOH 430 932 346 HOH HOH A . I 7 HOH 431 933 347 HOH HOH A . I 7 HOH 432 934 348 HOH HOH A . I 7 HOH 433 935 350 HOH HOH A . I 7 HOH 434 936 351 HOH HOH A . I 7 HOH 435 937 352 HOH HOH A . I 7 HOH 436 938 353 HOH HOH A . I 7 HOH 437 939 354 HOH HOH A . I 7 HOH 438 940 355 HOH HOH A . I 7 HOH 439 941 356 HOH HOH A . I 7 HOH 440 942 357 HOH HOH A . I 7 HOH 441 943 358 HOH HOH A . I 7 HOH 442 944 359 HOH HOH A . I 7 HOH 443 945 360 HOH HOH A . I 7 HOH 444 946 361 HOH HOH A . I 7 HOH 445 947 362 HOH HOH A . I 7 HOH 446 948 363 HOH HOH A . I 7 HOH 447 949 364 HOH HOH A . I 7 HOH 448 950 365 HOH HOH A . I 7 HOH 449 951 366 HOH HOH A . I 7 HOH 450 952 367 HOH HOH A . I 7 HOH 451 953 368 HOH HOH A . I 7 HOH 452 954 369 HOH HOH A . I 7 HOH 453 955 370 HOH HOH A . I 7 HOH 454 956 371 HOH HOH A . I 7 HOH 455 957 372 HOH HOH A . I 7 HOH 456 958 373 HOH HOH A . I 7 HOH 457 959 374 HOH HOH A . I 7 HOH 458 960 375 HOH HOH A . I 7 HOH 459 961 376 HOH HOH A . I 7 HOH 460 962 377 HOH HOH A . I 7 HOH 461 963 378 HOH HOH A . I 7 HOH 462 964 379 HOH HOH A . I 7 HOH 463 965 380 HOH HOH A . I 7 HOH 464 966 381 HOH HOH A . I 7 HOH 465 967 382 HOH HOH A . I 7 HOH 466 968 383 HOH HOH A . I 7 HOH 467 969 384 HOH HOH A . I 7 HOH 468 970 385 HOH HOH A . I 7 HOH 469 971 386 HOH HOH A . I 7 HOH 470 972 387 HOH HOH A . I 7 HOH 471 973 388 HOH HOH A . I 7 HOH 472 974 389 HOH HOH A . I 7 HOH 473 975 390 HOH HOH A . I 7 HOH 474 976 391 HOH HOH A . I 7 HOH 475 977 392 HOH HOH A . I 7 HOH 476 978 393 HOH HOH A . I 7 HOH 477 979 394 HOH HOH A . I 7 HOH 478 980 395 HOH HOH A . I 7 HOH 479 981 396 HOH HOH A . I 7 HOH 480 982 397 HOH HOH A . I 7 HOH 481 983 398 HOH HOH A . I 7 HOH 482 984 399 HOH HOH A . I 7 HOH 483 985 400 HOH HOH A . I 7 HOH 484 986 401 HOH HOH A . I 7 HOH 485 987 402 HOH HOH A . I 7 HOH 486 988 403 HOH HOH A . I 7 HOH 487 989 404 HOH HOH A . I 7 HOH 488 990 405 HOH HOH A . I 7 HOH 489 991 406 HOH HOH A . I 7 HOH 490 992 407 HOH HOH A . I 7 HOH 491 993 408 HOH HOH A . I 7 HOH 492 994 409 HOH HOH A . I 7 HOH 493 995 410 HOH HOH A . I 7 HOH 494 996 411 HOH HOH A . I 7 HOH 495 997 412 HOH HOH A . I 7 HOH 496 998 413 HOH HOH A . I 7 HOH 497 999 414 HOH HOH A . I 7 HOH 498 1000 415 HOH HOH A . I 7 HOH 499 1001 416 HOH HOH A . I 7 HOH 500 1002 417 HOH HOH A . I 7 HOH 501 1003 418 HOH HOH A . I 7 HOH 502 1004 419 HOH HOH A . I 7 HOH 503 1005 420 HOH HOH A . I 7 HOH 504 1006 421 HOH HOH A . I 7 HOH 505 1007 422 HOH HOH A . I 7 HOH 506 1008 423 HOH HOH A . I 7 HOH 507 1009 424 HOH HOH A . I 7 HOH 508 1010 425 HOH HOH A . I 7 HOH 509 1011 426 HOH HOH A . I 7 HOH 510 1012 427 HOH HOH A . I 7 HOH 511 1013 429 HOH HOH A . I 7 HOH 512 1014 431 HOH HOH A . I 7 HOH 513 1015 432 HOH HOH A . I 7 HOH 514 1016 433 HOH HOH A . I 7 HOH 515 1017 434 HOH HOH A . I 7 HOH 516 1018 435 HOH HOH A . I 7 HOH 517 1019 436 HOH HOH A . I 7 HOH 518 1020 437 HOH HOH A . I 7 HOH 519 1021 438 HOH HOH A . I 7 HOH 520 1022 439 HOH HOH A . I 7 HOH 521 1023 440 HOH HOH A . I 7 HOH 522 1024 441 HOH HOH A . I 7 HOH 523 1025 442 HOH HOH A . I 7 HOH 524 1026 443 HOH HOH A . I 7 HOH 525 1027 444 HOH HOH A . I 7 HOH 526 1028 445 HOH HOH A . I 7 HOH 527 1029 446 HOH HOH A . I 7 HOH 528 1030 447 HOH HOH A . I 7 HOH 529 1031 448 HOH HOH A . I 7 HOH 530 1032 449 HOH HOH A . I 7 HOH 531 1033 450 HOH HOH A . I 7 HOH 532 1034 451 HOH HOH A . I 7 HOH 533 1035 452 HOH HOH A . I 7 HOH 534 1036 453 HOH HOH A . I 7 HOH 535 1037 454 HOH HOH A . I 7 HOH 536 1038 455 HOH HOH A . I 7 HOH 537 1039 456 HOH HOH A . I 7 HOH 538 1040 457 HOH HOH A . I 7 HOH 539 1041 458 HOH HOH A . I 7 HOH 540 1042 459 HOH HOH A . I 7 HOH 541 1043 460 HOH HOH A . I 7 HOH 542 1044 461 HOH HOH A . I 7 HOH 543 1045 462 HOH HOH A . I 7 HOH 544 1046 463 HOH HOH A . I 7 HOH 545 1047 464 HOH HOH A . I 7 HOH 546 1048 465 HOH HOH A . I 7 HOH 547 1049 466 HOH HOH A . I 7 HOH 548 1050 467 HOH HOH A . I 7 HOH 549 1051 468 HOH HOH A . I 7 HOH 550 1052 469 HOH HOH A . I 7 HOH 551 1053 470 HOH HOH A . I 7 HOH 552 1054 471 HOH HOH A . I 7 HOH 553 1055 472 HOH HOH A . I 7 HOH 554 1056 473 HOH HOH A . I 7 HOH 555 1057 474 HOH HOH A . I 7 HOH 556 1058 475 HOH HOH A . I 7 HOH 557 1059 476 HOH HOH A . I 7 HOH 558 1060 477 HOH HOH A . I 7 HOH 559 1061 478 HOH HOH A . I 7 HOH 560 1062 479 HOH HOH A . I 7 HOH 561 1063 480 HOH HOH A . I 7 HOH 562 1064 481 HOH HOH A . I 7 HOH 563 1065 482 HOH HOH A . I 7 HOH 564 1066 483 HOH HOH A . I 7 HOH 565 1067 484 HOH HOH A . I 7 HOH 566 1068 485 HOH HOH A . I 7 HOH 567 1069 486 HOH HOH A . I 7 HOH 568 1070 487 HOH HOH A . I 7 HOH 569 1071 488 HOH HOH A . I 7 HOH 570 1072 489 HOH HOH A . I 7 HOH 571 1073 490 HOH HOH A . I 7 HOH 572 1074 491 HOH HOH A . I 7 HOH 573 1075 492 HOH HOH A . I 7 HOH 574 1076 493 HOH HOH A . I 7 HOH 575 1077 494 HOH HOH A . I 7 HOH 576 1078 495 HOH HOH A . I 7 HOH 577 1079 496 HOH HOH A . I 7 HOH 578 1080 497 HOH HOH A . I 7 HOH 579 1081 498 HOH HOH A . I 7 HOH 580 1082 499 HOH HOH A . I 7 HOH 581 1083 501 HOH HOH A . I 7 HOH 582 1084 502 HOH HOH A . I 7 HOH 583 1085 503 HOH HOH A . I 7 HOH 584 1086 504 HOH HOH A . I 7 HOH 585 1087 505 HOH HOH A . I 7 HOH 586 1088 506 HOH HOH A . I 7 HOH 587 1089 507 HOH HOH A . I 7 HOH 588 1090 508 HOH HOH A . I 7 HOH 589 1091 509 HOH HOH A . I 7 HOH 590 1092 510 HOH HOH A . I 7 HOH 591 1093 511 HOH HOH A . I 7 HOH 592 1094 512 HOH HOH A . I 7 HOH 593 1095 513 HOH HOH A . I 7 HOH 594 1096 514 HOH HOH A . I 7 HOH 595 1097 515 HOH HOH A . I 7 HOH 596 1098 517 HOH HOH A . I 7 HOH 597 1099 518 HOH HOH A . I 7 HOH 598 1100 519 HOH HOH A . I 7 HOH 599 1101 520 HOH HOH A . I 7 HOH 600 1102 521 HOH HOH A . I 7 HOH 601 1103 522 HOH HOH A . I 7 HOH 602 1104 523 HOH HOH A . I 7 HOH 603 1105 524 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 13 A ASN 38 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 446 A ASN 471 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # _pdbx_struct_special_symmetry.id 1 _pdbx_struct_special_symmetry.PDB_model_num 1 _pdbx_struct_special_symmetry.auth_asym_id A _pdbx_struct_special_symmetry.auth_comp_id HOH _pdbx_struct_special_symmetry.auth_seq_id 1017 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id I _pdbx_struct_special_symmetry.label_comp_id HOH _pdbx_struct_special_symmetry.label_seq_id . # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 OD1 ? A ASP 20 ? A ASP 45 ? 1_555 MG ? H MG . ? A MG 524 ? 1_555 OD1 ? A ASP 22 ? A ASP 47 ? 1_555 81.3 ? 2 OD1 ? A ASP 20 ? A ASP 45 ? 1_555 MG ? H MG . ? A MG 524 ? 1_555 O ? I HOH . ? A HOH 4 ? 1_555 85.4 ? 3 OD1 ? A ASP 22 ? A ASP 47 ? 1_555 MG ? H MG . ? A MG 524 ? 1_555 O ? I HOH . ? A HOH 4 ? 1_555 93.0 ? 4 OD1 ? A ASP 20 ? A ASP 45 ? 1_555 MG ? H MG . ? A MG 524 ? 1_555 O ? I HOH . ? A HOH 5 ? 1_555 100.1 ? 5 OD1 ? A ASP 22 ? A ASP 47 ? 1_555 MG ? H MG . ? A MG 524 ? 1_555 O ? I HOH . ? A HOH 5 ? 1_555 175.6 ? 6 O ? I HOH . ? A HOH 4 ? 1_555 MG ? H MG . ? A MG 524 ? 1_555 O ? I HOH . ? A HOH 5 ? 1_555 91.3 ? 7 OD1 ? A ASP 20 ? A ASP 45 ? 1_555 MG ? H MG . ? A MG 524 ? 1_555 O ? I HOH . ? A HOH 578 ? 1_555 170.2 ? 8 OD1 ? A ASP 22 ? A ASP 47 ? 1_555 MG ? H MG . ? A MG 524 ? 1_555 O ? I HOH . ? A HOH 578 ? 1_555 89.1 ? 9 O ? I HOH . ? A HOH 4 ? 1_555 MG ? H MG . ? A MG 524 ? 1_555 O ? I HOH . ? A HOH 578 ? 1_555 93.0 ? 10 O ? I HOH . ? A HOH 5 ? 1_555 MG ? H MG . ? A MG 524 ? 1_555 O ? I HOH . ? A HOH 578 ? 1_555 89.7 ? 11 OD1 ? A ASP 20 ? A ASP 45 ? 1_555 MG ? H MG . ? A MG 524 ? 1_555 O ? I HOH . ? A HOH 576 ? 1_555 92.9 ? 12 OD1 ? A ASP 22 ? A ASP 47 ? 1_555 MG ? H MG . ? A MG 524 ? 1_555 O ? I HOH . ? A HOH 576 ? 1_555 85.0 ? 13 O ? I HOH . ? A HOH 4 ? 1_555 MG ? H MG . ? A MG 524 ? 1_555 O ? I HOH . ? A HOH 576 ? 1_555 177.6 ? 14 O ? I HOH . ? A HOH 5 ? 1_555 MG ? H MG . ? A MG 524 ? 1_555 O ? I HOH . ? A HOH 576 ? 1_555 90.7 ? 15 O ? I HOH . ? A HOH 578 ? 1_555 MG ? H MG . ? A MG 524 ? 1_555 O ? I HOH . ? A HOH 576 ? 1_555 88.4 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2009-05-19 2 'Structure model' 1 1 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Non-polymer description' 2 2 'Structure model' 'Version format compliance' # loop_ _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[3][3] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.pdbx_refine_id 1 ? refined -18.8983 -2.7810 -33.2379 0.1592 0.2875 0.2561 0.0291 0.0017 -0.0407 0.4936 0.9610 0.8735 -0.1582 0.2163 0.1966 0.0933 -0.0407 -0.0521 0.2964 -0.1685 -0.1025 -0.1776 0.0670 0.2360 'X-RAY DIFFRACTION' 2 ? refined -17.3638 7.5324 -13.9017 0.1087 0.1199 0.1992 -0.0081 0.0015 -0.0043 0.7983 0.5054 0.7349 0.0874 0.4015 0.2297 0.0582 0.0253 -0.0719 0.0576 -0.0002 -0.0395 0.0142 -0.0037 0.1047 'X-RAY DIFFRACTION' 3 ? refined -28.0751 -7.3168 4.4395 0.1499 0.1331 0.2389 -0.0134 -0.0127 0.0030 1.4822 0.2218 0.5986 0.4276 -0.0772 -0.1857 0.0562 -0.0451 -0.0118 -0.2220 -0.0945 0.0170 0.0327 0.0803 -0.0003 'X-RAY DIFFRACTION' 4 ? refined -39.1067 -4.0280 -10.2457 0.1263 0.1512 0.2338 -0.0090 -0.0004 -0.0119 1.0264 0.6537 0.4510 0.4837 -0.0278 -0.0559 0.0297 0.0376 -0.0600 0.0876 -0.0464 0.0304 0.0345 0.0228 -0.0630 'X-RAY DIFFRACTION' 5 ? refined -36.7031 12.2810 -27.1826 0.1586 0.1605 0.2496 0.0430 0.0068 0.0458 0.8689 0.0938 1.2074 -0.3237 0.2756 -0.2079 0.0746 -0.0132 -0.0772 0.1107 0.1425 0.0969 -0.0256 -0.1972 -0.2270 'X-RAY DIFFRACTION' # loop_ _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 _pdbx_refine_tls_group.pdbx_refine_id 1 1 ? ? ? ? ? ? ? ? ? '(chain A and resid 26:114)' 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '(chain A and resid 115:244)' 'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? '(chain A and resid 245:349)' 'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? '(chain A and resid 350:460)' 'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? '(chain A and resid 461:520)' 'X-RAY DIFFRACTION' # loop_ _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id _software.pdbx_ordinal PHENIX ? ? package 'Paul D. Adams' PDAdams@lbl.gov refinement http://www.phenix-online.org/ C++ ? 1 PDB_EXTRACT 3.006 'June 11, 2008' package PDB help@deposit.rcsb.org 'data extraction' http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++ ? 2 MAR345dtb . ? ? ? ? 'data collection' ? ? ? 3 XDS . ? ? ? ? 'data reduction' ? ? ? 4 XSCALE . ? ? ? ? 'data scaling' ? ? ? 5 PHASER . ? ? ? ? phasing ? ? ? 6 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 SER A 101 ? ? -105.77 -82.21 2 1 SER A 101 ? ? -106.80 -80.58 3 1 TYR A 111 ? ? -146.71 18.93 4 1 GLU A 287 ? ? 51.23 -122.27 5 1 PHE A 313 ? ? -149.17 56.69 6 1 PHE A 392 ? ? -94.79 -136.74 7 1 ARG A 409 ? ? -117.09 -120.27 8 1 HIS A 459 ? ? -107.51 48.63 9 1 HIS A 459 ? ? -105.11 44.90 10 1 LEU A 491 ? ? 44.85 -127.29 11 1 ASP A 505 ? ? -144.59 59.00 # _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 MAN _pdbx_validate_chiral.auth_seq_id 3 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details 'WRONG HAND' _pdbx_validate_chiral.omega . # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 3 '(13aS)-3,10-dimethoxy-5,8,13,13a-tetrahydro-6H-isoquino[3,2-a]isoquinoline-2,9-diol' SLX 4 ALPHA-D-MANNOSE MAN 5 N-ACETYL-D-GLUCOSAMINE NAG 6 'MAGNESIUM ION' MG 7 water HOH #