data_3MK2 # _entry.id 3MK2 # _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 3MK2 RCSB RCSB058642 WWPDB D_1000058642 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1zef ;structure of alkaline phosphatase from human placenta in complex with its uncompetitive inhibitor L-Phe. THIS ENTRY 3MK2 REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA R1ZEFSF. ; re-refinement PDB 3MK0 . unspecified PDB 3MK1 . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3MK2 _pdbx_database_status.recvd_initial_deposition_date 2010-04-13 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Stec, B.' 1 'Cheltsov, A.' 2 'Millan, J.L.' 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 'Refined structures of placental alkaline phosphatase show a consistent pattern of interactions at the peripheral site.' 'Acta Crystallogr.,Sect.F' 66 866 870 2010 ? DK 1744-3091 ? ? 20693656 10.1107/S1744309110019767 original_data_1 'Structural studies of human placental alkaline phosphatase in complex with functional ligands.' J.Mol.Biol. 350 441 451 2005 JMOBAK UK 0022-2836 0070 ? 15946677 10.1016/j.jmb.2005.04.068 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Stec, B.' 1 primary 'Cheltsov, A.' 2 primary 'Millan, J.L.' 3 original_data_1 'Llinas, P.' 4 original_data_1 'Stura, E.A.' 5 original_data_1 'Menez, A.' 6 original_data_1 'Kiss, Z.' 7 original_data_1 'Stigbrand, T.' 8 original_data_1 'Millan, J.L.' 9 original_data_1 'Le Du, M.H.' 10 # _cell.entry_id 3MK2 _cell.length_a 87.791 _cell.length_b 114.944 _cell.length_c 106.341 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 3MK2 _symmetry.space_group_name_H-M 'C 2 2 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 20 # 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 nat 'Alkaline phosphatase, placental type' 52888.105 1 3.1.3.1 ? ? ? 2 non-polymer syn PHENYLALANINE 165.189 2 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 4 non-polymer syn 'ZINC ION' 65.409 2 ? ? ? ? 5 non-polymer syn 'MAGNESIUM ION' 24.305 1 ? ? ? ? 6 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 7 non-polymer syn 'ACETATE ION' 59.044 3 ? ? ? ? 8 non-polymer syn GLYCEROL 92.094 2 ? ? ? ? 9 water nat water 18.015 559 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'Placental alkaline phosphatase 1, PLAP-1, Alkaline phosphatase Regan isozyme' # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer yes _entity_poly.pdbx_seq_one_letter_code ;IIPVEEENPDFWNREAAEALGAAKKLQPAQTAAKNLIIFLGDGMGVSTVTAARILKGQKKDKLGPEIPLAMDRFPYVALS KTYNVDKHVPD(SEP)GATATAYLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASP AGTYAHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFRMGTPDPEYPDDYSQGGTRLDGKNLVQE WLAKRQGARYVWNRTELMQASLDPSVTHLMGLFEPGDMKYEIHRDSTLDPSLMEMTEAALRLLSRNPRGFFLFVEGGRID HGHHESRAYRALTETIMFDDAIERAGQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNG PGYVLKDGARPDVTESESGSPEYRQQSAVPLDEETHAGEDVAVFARGPQAHLVHGVQEQTFIAHVMAFAACLEPYTACDL APPAGTTD ; _entity_poly.pdbx_seq_one_letter_code_can ;IIPVEEENPDFWNREAAEALGAAKKLQPAQTAAKNLIIFLGDGMGVSTVTAARILKGQKKDKLGPEIPLAMDRFPYVALS KTYNVDKHVPDSGATATAYLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGTY AHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFRMGTPDPEYPDDYSQGGTRLDGKNLVQEWLAK RQGARYVWNRTELMQASLDPSVTHLMGLFEPGDMKYEIHRDSTLDPSLMEMTEAALRLLSRNPRGFFLFVEGGRIDHGHH ESRAYRALTETIMFDDAIERAGQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYV LKDGARPDVTESESGSPEYRQQSAVPLDEETHAGEDVAVFARGPQAHLVHGVQEQTFIAHVMAFAACLEPYTACDLAPPA GTTD ; _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 ILE n 1 2 ILE n 1 3 PRO n 1 4 VAL n 1 5 GLU n 1 6 GLU n 1 7 GLU n 1 8 ASN n 1 9 PRO n 1 10 ASP n 1 11 PHE n 1 12 TRP n 1 13 ASN n 1 14 ARG n 1 15 GLU n 1 16 ALA n 1 17 ALA n 1 18 GLU n 1 19 ALA n 1 20 LEU n 1 21 GLY n 1 22 ALA n 1 23 ALA n 1 24 LYS n 1 25 LYS n 1 26 LEU n 1 27 GLN n 1 28 PRO n 1 29 ALA n 1 30 GLN n 1 31 THR n 1 32 ALA n 1 33 ALA n 1 34 LYS n 1 35 ASN n 1 36 LEU n 1 37 ILE n 1 38 ILE n 1 39 PHE n 1 40 LEU n 1 41 GLY n 1 42 ASP n 1 43 GLY n 1 44 MET n 1 45 GLY n 1 46 VAL n 1 47 SER n 1 48 THR n 1 49 VAL n 1 50 THR n 1 51 ALA n 1 52 ALA n 1 53 ARG n 1 54 ILE n 1 55 LEU n 1 56 LYS n 1 57 GLY n 1 58 GLN n 1 59 LYS n 1 60 LYS n 1 61 ASP n 1 62 LYS n 1 63 LEU n 1 64 GLY n 1 65 PRO n 1 66 GLU n 1 67 ILE n 1 68 PRO n 1 69 LEU n 1 70 ALA n 1 71 MET n 1 72 ASP n 1 73 ARG n 1 74 PHE n 1 75 PRO n 1 76 TYR n 1 77 VAL n 1 78 ALA n 1 79 LEU n 1 80 SER n 1 81 LYS n 1 82 THR n 1 83 TYR n 1 84 ASN n 1 85 VAL n 1 86 ASP n 1 87 LYS n 1 88 HIS n 1 89 VAL n 1 90 PRO n 1 91 ASP n 1 92 SEP n 1 93 GLY n 1 94 ALA n 1 95 THR n 1 96 ALA n 1 97 THR n 1 98 ALA n 1 99 TYR n 1 100 LEU n 1 101 CYS n 1 102 GLY n 1 103 VAL n 1 104 LYS n 1 105 GLY n 1 106 ASN n 1 107 PHE n 1 108 GLN n 1 109 THR n 1 110 ILE n 1 111 GLY n 1 112 LEU n 1 113 SER n 1 114 ALA n 1 115 ALA n 1 116 ALA n 1 117 ARG n 1 118 PHE n 1 119 ASN n 1 120 GLN n 1 121 CYS n 1 122 ASN n 1 123 THR n 1 124 THR n 1 125 ARG n 1 126 GLY n 1 127 ASN n 1 128 GLU n 1 129 VAL n 1 130 ILE n 1 131 SER n 1 132 VAL n 1 133 MET n 1 134 ASN n 1 135 ARG n 1 136 ALA n 1 137 LYS n 1 138 LYS n 1 139 ALA n 1 140 GLY n 1 141 LYS n 1 142 SER n 1 143 VAL n 1 144 GLY n 1 145 VAL n 1 146 VAL n 1 147 THR n 1 148 THR n 1 149 THR n 1 150 ARG n 1 151 VAL n 1 152 GLN n 1 153 HIS n 1 154 ALA n 1 155 SER n 1 156 PRO n 1 157 ALA n 1 158 GLY n 1 159 THR n 1 160 TYR n 1 161 ALA n 1 162 HIS n 1 163 THR n 1 164 VAL n 1 165 ASN n 1 166 ARG n 1 167 ASN n 1 168 TRP n 1 169 TYR n 1 170 SER n 1 171 ASP n 1 172 ALA n 1 173 ASP n 1 174 VAL n 1 175 PRO n 1 176 ALA n 1 177 SER n 1 178 ALA n 1 179 ARG n 1 180 GLN n 1 181 GLU n 1 182 GLY n 1 183 CYS n 1 184 GLN n 1 185 ASP n 1 186 ILE n 1 187 ALA n 1 188 THR n 1 189 GLN n 1 190 LEU n 1 191 ILE n 1 192 SER n 1 193 ASN n 1 194 MET n 1 195 ASP n 1 196 ILE n 1 197 ASP n 1 198 VAL n 1 199 ILE n 1 200 LEU n 1 201 GLY n 1 202 GLY n 1 203 GLY n 1 204 ARG n 1 205 LYS n 1 206 TYR n 1 207 MET n 1 208 PHE n 1 209 ARG n 1 210 MET n 1 211 GLY n 1 212 THR n 1 213 PRO n 1 214 ASP n 1 215 PRO n 1 216 GLU n 1 217 TYR n 1 218 PRO n 1 219 ASP n 1 220 ASP n 1 221 TYR n 1 222 SER n 1 223 GLN n 1 224 GLY n 1 225 GLY n 1 226 THR n 1 227 ARG n 1 228 LEU n 1 229 ASP n 1 230 GLY n 1 231 LYS n 1 232 ASN n 1 233 LEU n 1 234 VAL n 1 235 GLN n 1 236 GLU n 1 237 TRP n 1 238 LEU n 1 239 ALA n 1 240 LYS n 1 241 ARG n 1 242 GLN n 1 243 GLY n 1 244 ALA n 1 245 ARG n 1 246 TYR n 1 247 VAL n 1 248 TRP n 1 249 ASN n 1 250 ARG n 1 251 THR n 1 252 GLU n 1 253 LEU n 1 254 MET n 1 255 GLN n 1 256 ALA n 1 257 SER n 1 258 LEU n 1 259 ASP n 1 260 PRO n 1 261 SER n 1 262 VAL n 1 263 THR n 1 264 HIS n 1 265 LEU n 1 266 MET n 1 267 GLY n 1 268 LEU n 1 269 PHE n 1 270 GLU n 1 271 PRO n 1 272 GLY n 1 273 ASP n 1 274 MET n 1 275 LYS n 1 276 TYR n 1 277 GLU n 1 278 ILE n 1 279 HIS n 1 280 ARG n 1 281 ASP n 1 282 SER n 1 283 THR n 1 284 LEU n 1 285 ASP n 1 286 PRO n 1 287 SER n 1 288 LEU n 1 289 MET n 1 290 GLU n 1 291 MET n 1 292 THR n 1 293 GLU n 1 294 ALA n 1 295 ALA n 1 296 LEU n 1 297 ARG n 1 298 LEU n 1 299 LEU n 1 300 SER n 1 301 ARG n 1 302 ASN n 1 303 PRO n 1 304 ARG n 1 305 GLY n 1 306 PHE n 1 307 PHE n 1 308 LEU n 1 309 PHE n 1 310 VAL n 1 311 GLU n 1 312 GLY n 1 313 GLY n 1 314 ARG n 1 315 ILE n 1 316 ASP n 1 317 HIS n 1 318 GLY n 1 319 HIS n 1 320 HIS n 1 321 GLU n 1 322 SER n 1 323 ARG n 1 324 ALA n 1 325 TYR n 1 326 ARG n 1 327 ALA n 1 328 LEU n 1 329 THR n 1 330 GLU n 1 331 THR n 1 332 ILE n 1 333 MET n 1 334 PHE n 1 335 ASP n 1 336 ASP n 1 337 ALA n 1 338 ILE n 1 339 GLU n 1 340 ARG n 1 341 ALA n 1 342 GLY n 1 343 GLN n 1 344 LEU n 1 345 THR n 1 346 SER n 1 347 GLU n 1 348 GLU n 1 349 ASP n 1 350 THR n 1 351 LEU n 1 352 SER n 1 353 LEU n 1 354 VAL n 1 355 THR n 1 356 ALA n 1 357 ASP n 1 358 HIS n 1 359 SER n 1 360 HIS n 1 361 VAL n 1 362 PHE n 1 363 SER n 1 364 PHE n 1 365 GLY n 1 366 GLY n 1 367 TYR n 1 368 PRO n 1 369 LEU n 1 370 ARG n 1 371 GLY n 1 372 SER n 1 373 SER n 1 374 ILE n 1 375 PHE n 1 376 GLY n 1 377 LEU n 1 378 ALA n 1 379 PRO n 1 380 GLY n 1 381 LYS n 1 382 ALA n 1 383 ARG n 1 384 ASP n 1 385 ARG n 1 386 LYS n 1 387 ALA n 1 388 TYR n 1 389 THR n 1 390 VAL n 1 391 LEU n 1 392 LEU n 1 393 TYR n 1 394 GLY n 1 395 ASN n 1 396 GLY n 1 397 PRO n 1 398 GLY n 1 399 TYR n 1 400 VAL n 1 401 LEU n 1 402 LYS n 1 403 ASP n 1 404 GLY n 1 405 ALA n 1 406 ARG n 1 407 PRO n 1 408 ASP n 1 409 VAL n 1 410 THR n 1 411 GLU n 1 412 SER n 1 413 GLU n 1 414 SER n 1 415 GLY n 1 416 SER n 1 417 PRO n 1 418 GLU n 1 419 TYR n 1 420 ARG n 1 421 GLN n 1 422 GLN n 1 423 SER n 1 424 ALA n 1 425 VAL n 1 426 PRO n 1 427 LEU n 1 428 ASP n 1 429 GLU n 1 430 GLU n 1 431 THR n 1 432 HIS n 1 433 ALA n 1 434 GLY n 1 435 GLU n 1 436 ASP n 1 437 VAL n 1 438 ALA n 1 439 VAL n 1 440 PHE n 1 441 ALA n 1 442 ARG n 1 443 GLY n 1 444 PRO n 1 445 GLN n 1 446 ALA n 1 447 HIS n 1 448 LEU n 1 449 VAL n 1 450 HIS n 1 451 GLY n 1 452 VAL n 1 453 GLN n 1 454 GLU n 1 455 GLN n 1 456 THR n 1 457 PHE n 1 458 ILE n 1 459 ALA n 1 460 HIS n 1 461 VAL n 1 462 MET n 1 463 ALA n 1 464 PHE n 1 465 ALA n 1 466 ALA n 1 467 CYS n 1 468 LEU n 1 469 GLU n 1 470 PRO n 1 471 TYR n 1 472 THR n 1 473 ALA n 1 474 CYS n 1 475 ASP n 1 476 LEU n 1 477 ALA n 1 478 PRO n 1 479 PRO n 1 480 ALA n 1 481 GLY n 1 482 THR n 1 483 THR n 1 484 ASP n # _entity_src_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name human _entity_src_nat.pdbx_organism_scientific 'Homo sapiens' _entity_src_nat.pdbx_ncbi_taxonomy_id 9606 _entity_src_nat.genus ? _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code PPB1_HUMAN _struct_ref.pdbx_db_accession P05187 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;IIPVEEENPDFWNREAAEALGAAKKLQPAQTAAKNLIIFLGDGMGVSTVTAARILKGQKKDKLGPEIPLAMDRFPYVALS KTYNVDKHVPDSGATATAYLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGTY AHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFRMGTPDPEYPDDYSQGGTRLDGKNLVQEWLAK RQGARYVWNRTELMQASLDPSVTHLMGLFEPGDMKYEIHRDSTLDPSLMEMTEAALRLLSRNPRGFFLFVEGGRIDHGHH ESRAYRALTETIMFDDAIERAGQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYV LKDGARPDVTESESGSPEYRQQSAVPLDEETHAGEDVAVFARGPQAHLVHGVQEQTFIAHVMAFAACLEPYTACDLAPPA G ; _struct_ref.pdbx_align_begin 23 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 3MK2 _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 481 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P05187 _struct_ref_seq.db_align_beg 23 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 503 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 481 # 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 ACT non-polymer . 'ACETATE ION' ? 'C2 H3 O2 -1' 59.044 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 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 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 SEP 'L-peptide linking' n PHOSPHOSERINE PHOSPHONOSERINE 'C3 H8 N O6 P' 185.072 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 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 ZN non-polymer . 'ZINC ION' ? 'Zn 2' 65.409 # _exptl.entry_id 3MK2 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number ? # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.54 _exptl_crystal.density_percent_sol 51.49 _exptl_crystal.description 'AUTHOR USED THE SF DATA FROM ENTRY 1ZEF' # _diffrn.id 1 _diffrn.crystal_id 1 _diffrn.ambient_temp ? _diffrn.ambient_temp_details ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 3MK2 _refine.ls_number_reflns_obs 40824 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 69.84 _refine.ls_d_res_high 1.89 _refine.ls_percent_reflns_obs 98.6 _refine.ls_R_factor_obs 0.125 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.123 _refine.ls_R_factor_R_free 0.163 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.100 _refine.ls_number_reflns_R_free 2174 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.974 _refine.correlation_coeff_Fo_to_Fc_free 0.956 _refine.B_iso_mean 22.07 _refine.aniso_B[1][1] -0.32000 _refine.aniso_B[2][2] 0.82000 _refine.aniso_B[3][3] -0.50000 _refine.aniso_B[1][2] 0.00000 _refine.aniso_B[1][3] 0.00000 _refine.aniso_B[2][3] 0.00000 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct ? _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.391 _refine.pdbx_overall_ESU_R_Free 0.103 _refine.overall_SU_ML 0.063 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 4.563 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3691 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 108 _refine_hist.number_atoms_solvent 559 _refine_hist.number_atoms_total 4358 _refine_hist.d_res_high 1.89 _refine_hist.d_res_low 69.84 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.010 0.021 ? 3877 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.272 1.977 ? 5254 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.974 5.000 ? 480 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 33.901 23.672 ? 177 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 12.526 15.000 ? 608 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 15.967 15.000 ? 29 'X-RAY DIFFRACTION' ? r_chiral_restr 0.081 0.200 ? 575 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.005 0.020 ? 2978 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined 0.216 0.200 ? 2408 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined 0.312 0.200 ? 2712 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.146 0.200 ? 614 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined 0.131 0.200 ? 10 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.189 0.200 ? 151 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.165 0.200 ? 58 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 0.996 1.500 ? 2443 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 1.553 2.000 ? 3840 'X-RAY DIFFRACTION' ? r_scbond_it 2.659 3.000 ? 1573 'X-RAY DIFFRACTION' ? r_scangle_it 4.087 4.500 ? 1414 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.89 _refine_ls_shell.d_res_low 1.94 _refine_ls_shell.number_reflns_R_work 2964 _refine_ls_shell.R_factor_R_work 0.1330 _refine_ls_shell.percent_reflns_obs 98.58 _refine_ls_shell.R_factor_R_free 0.2110 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 160 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 3MK2 _struct.title 'Placental alkaline phosphatase complexed with Phe' _struct.pdbx_descriptor 'Alkaline phosphatase, placental type (E.C.3.1.3.1)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3MK2 _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'Phe binding, HYDROLASE' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 3 ? E N N 3 ? F N N 3 ? G N N 3 ? H N N 4 ? I N N 4 ? J N N 5 ? K N N 6 ? L N N 7 ? M N N 7 ? N N N 7 ? O N N 8 ? P N N 8 ? Q N N 9 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 PRO A 3 ? GLU A 7 ? PRO A 3 GLU A 7 5 ? 5 HELX_P HELX_P2 2 ASN A 8 ? LEU A 26 ? ASN A 8 LEU A 26 1 ? 19 HELX_P HELX_P3 3 GLY A 45 ? LYS A 60 ? GLY A 45 LYS A 60 1 ? 16 HELX_P HELX_P4 4 ALA A 70 ? PHE A 74 ? ALA A 70 PHE A 74 5 ? 5 HELX_P HELX_P5 5 ASP A 91 ? GLY A 102 ? ASP A 91 GLY A 102 1 ? 12 HELX_P HELX_P6 6 GLN A 120 ? THR A 124 ? GLN A 120 THR A 124 5 ? 5 HELX_P HELX_P7 7 SER A 131 ? ALA A 139 ? SER A 131 ALA A 139 1 ? 9 HELX_P HELX_P8 8 HIS A 153 ? GLY A 158 ? HIS A 153 GLY A 158 1 ? 6 HELX_P HELX_P9 9 SER A 170 ? VAL A 174 ? SER A 170 VAL A 174 5 ? 5 HELX_P HELX_P10 10 PRO A 175 ? GLU A 181 ? PRO A 175 GLU A 181 1 ? 7 HELX_P HELX_P11 11 ASP A 185 ? ASN A 193 ? ASP A 185 ASN A 193 1 ? 9 HELX_P HELX_P12 12 ARG A 204 ? PHE A 208 ? ARG A 204 PHE A 208 5 ? 5 HELX_P HELX_P13 13 ASP A 220 ? GLY A 224 ? ASP A 220 GLY A 224 5 ? 5 HELX_P HELX_P14 14 ASN A 232 ? LYS A 240 ? ASN A 232 LYS A 240 1 ? 9 HELX_P HELX_P15 15 ASN A 249 ? LEU A 258 ? ASN A 249 LEU A 258 1 ? 10 HELX_P HELX_P16 16 TYR A 276 ? ARG A 280 ? TYR A 276 ARG A 280 5 ? 5 HELX_P HELX_P17 17 SER A 287 ? SER A 300 ? SER A 287 SER A 300 1 ? 14 HELX_P HELX_P18 18 ARG A 314 ? GLU A 321 ? ARG A 314 GLU A 321 1 ? 8 HELX_P HELX_P19 19 ARG A 323 ? THR A 345 ? ARG A 323 THR A 345 1 ? 23 HELX_P HELX_P20 20 THR A 410 ? GLY A 415 ? THR A 410 GLY A 415 1 ? 6 HELX_P HELX_P21 21 GLN A 445 ? VAL A 449 ? GLN A 445 VAL A 449 5 ? 5 HELX_P HELX_P22 22 THR A 456 ? ALA A 466 ? THR A 456 ALA A 466 1 ? 11 # _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 121 SG ? ? ? 1_555 A CYS 183 SG ? ? A CYS 121 A CYS 183 1_555 ? ? ? ? ? ? ? 2.047 ? disulf2 disulf ? ? A CYS 467 SG ? ? ? 1_555 A CYS 474 SG ? ? A CYS 467 A CYS 474 1_555 ? ? ? ? ? ? ? 2.055 ? covale1 covale ? ? A ASP 91 C ? ? ? 1_555 A SEP 92 N ? ? A ASP 91 A SEP 92 1_555 ? ? ? ? ? ? ? 1.324 ? covale2 covale ? ? A SEP 92 C ? ? ? 1_555 A GLY 93 N ? ? A SEP 92 A GLY 93 1_555 ? ? ? ? ? ? ? 1.330 ? covale3 covale ? ? A ASN 122 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 122 A NAG 801 1_555 ? ? ? ? ? ? ? 1.432 ? covale4 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 801 A NAG 802 1_555 ? ? ? ? ? ? ? 1.440 ? covale5 covale ? ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 803 A NAG 804 1_555 ? ? ? ? ? ? ? 1.440 ? covale6 covale ? ? A ASN 249 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 249 A NAG 803 1_555 ? ? ? ? ? ? ? 1.447 ? metalc1 metalc ? ? A ASP 42 OD1 ? ? ? 1_555 I ZN . ZN ? ? A ASP 42 A ZN 902 1_555 ? ? ? ? ? ? ? 1.827 ? metalc2 metalc ? ? A ASP 42 OD2 ? ? ? 1_555 J MG . MG ? ? A ASP 42 A MG 903 1_555 ? ? ? ? ? ? ? 1.905 ? metalc3 metalc ? ? A GLU 311 OE2 ? ? ? 1_555 J MG . MG ? ? A GLU 311 A MG 903 1_555 ? ? ? ? ? ? ? 1.959 ? metalc4 metalc ? ? A HIS 432 NE2 ? ? ? 1_555 H ZN . ZN ? ? A HIS 432 A ZN 901 1_555 ? ? ? ? ? ? ? 2.017 ? metalc5 metalc ? ? A ASP 316 OD1 ? ? ? 1_555 H ZN . ZN ? ? A ASP 316 A ZN 901 1_555 ? ? ? ? ? ? ? 2.044 ? metalc6 metalc ? ? J MG . MG ? ? ? 1_555 Q HOH . O ? ? A MG 903 A HOH 1034 1_555 ? ? ? ? ? ? ? 2.066 ? metalc7 metalc ? ? A HIS 320 NE2 ? ? ? 1_555 H ZN . ZN ? ? A HIS 320 A ZN 901 1_555 ? ? ? ? ? ? ? 2.073 ? metalc8 metalc ? ? A SEP 92 OG ? ? ? 1_555 I ZN . ZN ? ? A SEP 92 A ZN 902 1_555 ? ? ? ? ? ? ? 2.095 ? metalc9 metalc ? ? J MG . MG ? ? ? 1_555 Q HOH . O ? ? A MG 903 A HOH 1053 1_555 ? ? ? ? ? ? ? 2.101 ? metalc10 metalc ? ? A HIS 358 NE2 ? ? ? 1_555 I ZN . ZN ? ? A HIS 358 A ZN 902 1_555 ? ? ? ? ? ? ? 2.112 ? metalc11 metalc ? ? A ASP 357 OD2 ? ? ? 1_555 I ZN . ZN ? ? A ASP 357 A ZN 902 1_555 ? ? ? ? ? ? ? 2.112 ? metalc12 metalc ? ? J MG . MG ? ? ? 1_555 Q HOH . O ? ? A MG 903 A HOH 1003 1_555 ? ? ? ? ? ? ? 2.130 ? metalc13 metalc ? ? A SEP 92 O3P ? ? ? 1_555 H ZN . ZN ? ? A SEP 92 A ZN 901 1_555 ? ? ? ? ? ? ? 2.146 ? metalc14 metalc ? ? B PHE . N A ? ? 1_555 H ZN . ZN ? ? A PHE 912 A ZN 901 1_555 ? ? ? ? ? ? ? 2.160 ? metalc15 metalc ? ? A SER 155 OG ? ? ? 1_555 J MG . MG ? ? A SER 155 A MG 903 1_555 ? ? ? ? ? ? ? 2.185 ? metalc16 metalc ? ? A GLU 270 OE2 ? ? ? 1_555 K CA . CA ? ? A GLU 270 A CA 904 1_555 ? ? ? ? ? ? ? 2.201 ? metalc17 metalc ? ? A SEP 92 O3P ? ? ? 1_555 I ZN . ZN ? ? A SEP 92 A ZN 902 1_555 ? ? ? ? ? ? ? 2.227 ? metalc18 metalc ? ? A PHE 269 O ? ? ? 1_555 K CA . CA ? ? A PHE 269 A CA 904 1_555 ? ? ? ? ? ? ? 2.234 ? metalc19 metalc ? ? A ASP 285 OD2 ? ? ? 1_555 K CA . CA ? ? A ASP 285 A CA 904 1_555 ? ? ? ? ? ? ? 2.284 ? metalc20 metalc ? ? A GLU 216 OE1 ? ? ? 1_555 K CA . CA ? ? A GLU 216 A CA 904 1_555 ? ? ? ? ? ? ? 2.293 ? metalc21 metalc ? ? K CA . CA ? ? ? 1_555 Q HOH . O ? ? A CA 904 A HOH 1246 1_555 ? ? ? ? ? ? ? 2.339 ? metalc22 metalc ? ? A GLU 216 OE2 ? ? ? 1_555 K CA . CA ? ? A GLU 216 A CA 904 1_555 ? ? ? ? ? ? ? 2.419 ? metalc23 metalc ? ? A ASP 316 OD2 ? ? ? 1_555 H ZN . ZN ? ? A ASP 316 A ZN 901 1_555 ? ? ? ? ? ? ? 2.425 ? metalc24 metalc ? ? A ASP 285 OD1 ? ? ? 1_555 K CA . CA ? ? A ASP 285 A CA 904 1_555 ? ? ? ? ? ? ? 2.600 ? # 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 GLU _struct_mon_prot_cis.label_seq_id 469 _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 GLU _struct_mon_prot_cis.auth_seq_id 469 _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_2 470 _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_2 470 _struct_mon_prot_cis.pdbx_auth_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle -2.39 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 10 ? B ? 2 ? C ? 3 ? # 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 ? parallel A 2 3 ? parallel A 3 4 ? parallel A 4 5 ? parallel A 5 6 ? parallel A 6 7 ? parallel A 7 8 ? anti-parallel A 8 9 ? anti-parallel A 9 10 ? parallel B 1 2 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? 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 ALA A 244 ? VAL A 247 ? ALA A 244 VAL A 247 A 2 HIS A 264 ? LEU A 268 ? HIS A 264 LEU A 268 A 3 VAL A 198 ? GLY A 202 ? VAL A 198 GLY A 202 A 4 SER A 142 ? ARG A 150 ? SER A 142 ARG A 150 A 5 PHE A 306 ? GLY A 312 ? PHE A 306 GLY A 312 A 6 ASN A 35 ? GLY A 41 ? ASN A 35 GLY A 41 A 7 THR A 350 ? ALA A 356 ? THR A 350 ALA A 356 A 8 VAL A 437 ? ARG A 442 ? VAL A 437 ARG A 442 A 9 TYR A 76 ? LYS A 81 ? TYR A 76 LYS A 81 A 10 VAL A 452 ? GLU A 454 ? VAL A 452 GLU A 454 B 1 SER A 359 ? HIS A 360 ? SER A 359 HIS A 360 B 2 HIS A 432 ? ALA A 433 ? HIS A 432 ALA A 433 C 1 PHE A 362 ? PHE A 364 ? PHE A 362 PHE A 364 C 2 LEU A 391 ? ASN A 395 ? LEU A 391 ASN A 395 C 3 SER A 423 ? VAL A 425 ? SER A 423 VAL A 425 # 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 ARG A 245 ? N ARG A 245 O MET A 266 ? O MET A 266 A 2 3 O GLY A 267 ? O GLY A 267 N ILE A 199 ? N ILE A 199 A 3 4 O LEU A 200 ? O LEU A 200 N VAL A 145 ? N VAL A 145 A 4 5 N GLY A 144 ? N GLY A 144 O PHE A 309 ? O PHE A 309 A 5 6 O VAL A 310 ? O VAL A 310 N LEU A 40 ? N LEU A 40 A 6 7 N PHE A 39 ? N PHE A 39 O LEU A 353 ? O LEU A 353 A 7 8 N SER A 352 ? N SER A 352 O ARG A 442 ? O ARG A 442 A 8 9 O VAL A 437 ? O VAL A 437 N SER A 80 ? N SER A 80 A 9 10 N LEU A 79 ? N LEU A 79 O GLN A 453 ? O GLN A 453 B 1 2 N SER A 359 ? N SER A 359 O ALA A 433 ? O ALA A 433 C 1 2 N SER A 363 ? N SER A 363 O LEU A 392 ? O LEU A 392 C 2 3 N GLY A 394 ? N GLY A 394 O ALA A 424 ? O ALA A 424 # 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 ? ? ? ? 14 'BINDING SITE FOR RESIDUE PHE A 912' AC2 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE PHE A 923' AC3 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 801' AC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 802' AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 803' AC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 804' AC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN A 901' AC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN A 902' AC9 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MG A 903' BC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 904' BC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ACT A 933' BC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE ACT A 934' BC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ACT A 935' BC5 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GOL A 936' BC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL A 937' # 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 14 ASP A 91 ? ASP A 91 . ? 1_555 ? 2 AC1 14 SEP A 92 ? SEP A 92 . ? 1_555 ? 3 AC1 14 PHE A 107 ? PHE A 107 . ? 1_555 ? 4 AC1 14 ARG A 166 ? ARG A 166 . ? 1_555 ? 5 AC1 14 ASP A 316 ? ASP A 316 . ? 1_555 ? 6 AC1 14 HIS A 317 ? HIS A 317 . ? 1_555 ? 7 AC1 14 HIS A 320 ? HIS A 320 . ? 1_555 ? 8 AC1 14 GLU A 429 ? GLU A 429 . ? 1_555 ? 9 AC1 14 HIS A 432 ? HIS A 432 . ? 1_555 ? 10 AC1 14 ZN H . ? ZN A 901 . ? 1_555 ? 11 AC1 14 HOH Q . ? HOH A 1182 . ? 1_555 ? 12 AC1 14 HOH Q . ? HOH A 1283 . ? 1_555 ? 13 AC1 14 HOH Q . ? HOH A 1547 . ? 1_555 ? 14 AC1 14 HOH Q . ? HOH A 1561 . ? 1_555 ? 15 AC2 11 ARG A 125 ? ARG A 125 . ? 8_555 ? 16 AC2 11 GLY A 126 ? GLY A 126 . ? 8_555 ? 17 AC2 11 ARG A 250 ? ARG A 250 . ? 1_555 ? 18 AC2 11 MET A 254 ? MET A 254 . ? 1_555 ? 19 AC2 11 GLU A 290 ? GLU A 290 . ? 1_555 ? 20 AC2 11 GLU A 293 ? GLU A 293 . ? 1_555 ? 21 AC2 11 ALA A 294 ? ALA A 294 . ? 1_555 ? 22 AC2 11 ARG A 297 ? ARG A 297 . ? 1_555 ? 23 AC2 11 HOH Q . ? HOH A 1173 . ? 1_555 ? 24 AC2 11 HOH Q . ? HOH A 1548 . ? 1_555 ? 25 AC2 11 HOH Q . ? HOH A 1550 . ? 1_555 ? 26 AC3 7 ASN A 122 ? ASN A 122 . ? 1_555 ? 27 AC3 7 LEU A 258 ? LEU A 258 . ? 8_455 ? 28 AC3 7 ARG A 297 ? ARG A 297 . ? 8_455 ? 29 AC3 7 NAG E . ? NAG A 802 . ? 1_555 ? 30 AC3 7 HOH Q . ? HOH A 1396 . ? 1_555 ? 31 AC3 7 HOH Q . ? HOH A 1441 . ? 8_455 ? 32 AC3 7 HOH Q . ? HOH A 1485 . ? 1_555 ? 33 AC4 3 ARG A 301 ? ARG A 301 . ? 8_455 ? 34 AC4 3 NAG D . ? NAG A 801 . ? 1_555 ? 35 AC4 3 HOH Q . ? HOH A 1485 . ? 1_555 ? 36 AC5 6 TRP A 248 ? TRP A 248 . ? 1_555 ? 37 AC5 6 ASN A 249 ? ASN A 249 . ? 1_555 ? 38 AC5 6 GLU A 252 ? GLU A 252 . ? 1_555 ? 39 AC5 6 NAG G . ? NAG A 804 . ? 1_555 ? 40 AC5 6 HOH Q . ? HOH A 1076 . ? 1_555 ? 41 AC5 6 HOH Q . ? HOH A 1104 . ? 1_555 ? 42 AC6 2 ASP A 403 ? ASP A 403 . ? 4_555 ? 43 AC6 2 NAG F . ? NAG A 803 . ? 1_555 ? 44 AC7 5 SEP A 92 ? SEP A 92 . ? 1_555 ? 45 AC7 5 ASP A 316 ? ASP A 316 . ? 1_555 ? 46 AC7 5 HIS A 320 ? HIS A 320 . ? 1_555 ? 47 AC7 5 HIS A 432 ? HIS A 432 . ? 1_555 ? 48 AC7 5 PHE B . ? PHE A 912 . ? 1_555 ? 49 AC8 5 ASP A 42 ? ASP A 42 . ? 1_555 ? 50 AC8 5 SEP A 92 ? SEP A 92 . ? 1_555 ? 51 AC8 5 ASP A 316 ? ASP A 316 . ? 1_555 ? 52 AC8 5 ASP A 357 ? ASP A 357 . ? 1_555 ? 53 AC8 5 HIS A 358 ? HIS A 358 . ? 1_555 ? 54 AC9 6 ASP A 42 ? ASP A 42 . ? 1_555 ? 55 AC9 6 SER A 155 ? SER A 155 . ? 1_555 ? 56 AC9 6 GLU A 311 ? GLU A 311 . ? 1_555 ? 57 AC9 6 HOH Q . ? HOH A 1003 . ? 1_555 ? 58 AC9 6 HOH Q . ? HOH A 1034 . ? 1_555 ? 59 AC9 6 HOH Q . ? HOH A 1053 . ? 1_555 ? 60 BC1 5 GLU A 216 ? GLU A 216 . ? 1_555 ? 61 BC1 5 PHE A 269 ? PHE A 269 . ? 1_555 ? 62 BC1 5 GLU A 270 ? GLU A 270 . ? 1_555 ? 63 BC1 5 ASP A 285 ? ASP A 285 . ? 1_555 ? 64 BC1 5 HOH Q . ? HOH A 1246 . ? 1_555 ? 65 BC2 6 ALA A 378 ? ALA A 378 . ? 1_555 ? 66 BC2 6 GLY A 380 ? GLY A 380 . ? 1_555 ? 67 BC2 6 LYS A 381 ? LYS A 381 . ? 1_555 ? 68 BC2 6 ALA A 387 ? ALA A 387 . ? 1_555 ? 69 BC2 6 HOH Q . ? HOH A 1105 . ? 1_555 ? 70 BC2 6 HOH Q . ? HOH A 1347 . ? 1_555 ? 71 BC3 3 GLU A 277 ? GLU A 277 . ? 1_555 ? 72 BC3 3 ARG A 280 ? ARG A 280 . ? 1_555 ? 73 BC3 3 HOH Q . ? HOH A 1382 . ? 1_555 ? 74 BC4 4 PHE A 208 ? PHE A 208 . ? 1_555 ? 75 BC4 4 ASN A 232 ? ASN A 232 . ? 1_555 ? 76 BC4 4 VAL A 234 ? VAL A 234 . ? 1_555 ? 77 BC4 4 TYR A 246 ? TYR A 246 . ? 1_555 ? 78 BC5 8 TYR A 217 ? TYR A 217 . ? 1_555 ? 79 BC5 8 GLN A 223 ? GLN A 223 . ? 1_555 ? 80 BC5 8 GLU A 270 ? GLU A 270 . ? 1_555 ? 81 BC5 8 PRO A 271 ? PRO A 271 . ? 1_555 ? 82 BC5 8 HOH Q . ? HOH A 1172 . ? 1_555 ? 83 BC5 8 HOH Q . ? HOH A 1406 . ? 1_555 ? 84 BC5 8 HOH Q . ? HOH A 1448 . ? 1_555 ? 85 BC5 8 HOH Q . ? HOH A 1477 . ? 1_555 ? 86 BC6 5 GLY A 211 ? GLY A 211 . ? 1_555 ? 87 BC6 5 TYR A 221 ? TYR A 221 . ? 1_555 ? 88 BC6 5 HOH Q . ? HOH A 1077 . ? 4_555 ? 89 BC6 5 HOH Q . ? HOH A 1137 . ? 2_654 ? 90 BC6 5 HOH Q . ? HOH A 1539 . ? 1_555 ? # _database_PDB_matrix.entry_id 3MK2 _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 3MK2 _atom_sites.fract_transf_matrix[1][1] 0.011391 _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] 0.008700 _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] 0.009404 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CA MG N O P S ZN # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ILE A 1 1 ? 67.483 15.745 30.574 1.00 26.31 ? 1 ILE A N 1 ATOM 2 C CA . ILE A 1 1 ? 68.658 16.599 30.955 1.00 27.08 ? 1 ILE A CA 1 ATOM 3 C C . ILE A 1 1 ? 68.261 17.987 31.504 1.00 26.33 ? 1 ILE A C 1 ATOM 4 O O . ILE A 1 1 ? 67.272 18.586 31.067 1.00 26.17 ? 1 ILE A O 1 ATOM 5 C CB . ILE A 1 1 ? 69.678 16.758 29.786 1.00 27.95 ? 1 ILE A CB 1 ATOM 6 C CG1 . ILE A 1 1 ? 69.195 17.768 28.752 1.00 29.11 ? 1 ILE A CG1 1 ATOM 7 C CG2 . ILE A 1 1 ? 69.995 15.417 29.105 1.00 29.74 ? 1 ILE A CG2 1 ATOM 8 C CD1 . ILE A 1 1 ? 69.827 19.146 28.933 1.00 32.21 ? 1 ILE A CD1 1 ATOM 9 N N . ILE A 1 2 ? 69.051 18.493 32.449 1.00 25.07 ? 2 ILE A N 1 ATOM 10 C CA . ILE A 1 2 ? 68.816 19.803 33.053 1.00 24.17 ? 2 ILE A CA 1 ATOM 11 C C . ILE A 1 2 ? 69.708 20.860 32.395 1.00 23.91 ? 2 ILE A C 1 ATOM 12 O O . ILE A 1 2 ? 70.938 20.830 32.567 1.00 23.84 ? 2 ILE A O 1 ATOM 13 C CB . ILE A 1 2 ? 69.088 19.771 34.575 1.00 24.28 ? 2 ILE A CB 1 ATOM 14 C CG1 . ILE A 1 2 ? 68.084 18.841 35.269 1.00 23.48 ? 2 ILE A CG1 1 ATOM 15 C CG2 . ILE A 1 2 ? 69.084 21.208 35.174 1.00 23.96 ? 2 ILE A CG2 1 ATOM 16 C CD1 . ILE A 1 2 ? 68.499 18.429 36.671 1.00 23.53 ? 2 ILE A CD1 1 ATOM 17 N N . PRO A 1 3 ? 69.107 21.794 31.632 1.00 23.41 ? 3 PRO A N 1 ATOM 18 C CA . PRO A 1 3 ? 69.911 22.870 31.040 1.00 23.08 ? 3 PRO A CA 1 ATOM 19 C C . PRO A 1 3 ? 70.489 23.793 32.123 1.00 22.86 ? 3 PRO A C 1 ATOM 20 O O . PRO A 1 3 ? 69.750 24.309 32.970 1.00 22.30 ? 3 PRO A O 1 ATOM 21 C CB . PRO A 1 3 ? 68.911 23.604 30.137 1.00 23.16 ? 3 PRO A CB 1 ATOM 22 C CG . PRO A 1 3 ? 67.599 23.272 30.684 1.00 23.34 ? 3 PRO A CG 1 ATOM 23 C CD . PRO A 1 3 ? 67.689 21.901 31.250 1.00 23.59 ? 3 PRO A CD 1 ATOM 24 N N . VAL A 1 4 ? 71.809 23.971 32.108 1.00 23.08 ? 4 VAL A N 1 ATOM 25 C CA . VAL A 1 4 ? 72.487 24.682 33.191 1.00 23.07 ? 4 VAL A CA 1 ATOM 26 C C . VAL A 1 4 ? 71.945 26.098 33.413 1.00 22.35 ? 4 VAL A C 1 ATOM 27 O O . VAL A 1 4 ? 71.731 26.516 34.561 1.00 21.27 ? 4 VAL A O 1 ATOM 28 C CB . VAL A 1 4 ? 74.038 24.659 33.032 1.00 23.42 ? 4 VAL A CB 1 ATOM 29 C CG1 . VAL A 1 4 ? 74.511 25.551 31.894 1.00 24.87 ? 4 VAL A CG1 1 ATOM 30 C CG2 . VAL A 1 4 ? 74.716 25.062 34.329 1.00 24.84 ? 4 VAL A CG2 1 ATOM 31 N N . GLU A 1 5 ? 71.706 26.822 32.322 1.00 21.84 ? 5 GLU A N 1 ATOM 32 C CA . GLU A 1 5 ? 71.233 28.205 32.413 1.00 22.86 ? 5 GLU A CA 1 ATOM 33 C C . GLU A 1 5 ? 69.929 28.320 33.231 1.00 21.16 ? 5 GLU A C 1 ATOM 34 O O . GLU A 1 5 ? 69.702 29.323 33.926 1.00 20.55 ? 5 GLU A O 1 ATOM 35 C CB . GLU A 1 5 ? 71.055 28.799 31.013 1.00 22.70 ? 5 GLU A CB 1 ATOM 36 C CG . GLU A 1 5 ? 69.886 28.216 30.242 1.00 26.23 ? 5 GLU A CG 1 ATOM 37 C CD . GLU A 1 5 ? 69.791 28.721 28.820 1.00 28.10 ? 5 GLU A CD 1 ATOM 38 O OE1 . GLU A 1 5 ? 70.313 29.832 28.522 1.00 35.04 ? 5 GLU A OE1 1 ATOM 39 O OE2 . GLU A 1 5 ? 69.189 27.998 27.999 1.00 33.55 ? 5 GLU A OE2 1 ATOM 40 N N . GLU A 1 6 ? 69.101 27.277 33.160 1.00 19.37 ? 6 GLU A N 1 ATOM 41 C CA . GLU A 1 6 ? 67.807 27.245 33.872 1.00 18.62 ? 6 GLU A CA 1 ATOM 42 C C . GLU A 1 6 ? 67.899 26.956 35.383 1.00 18.24 ? 6 GLU A C 1 ATOM 43 O O . GLU A 1 6 ? 66.909 27.098 36.129 1.00 17.89 ? 6 GLU A O 1 ATOM 44 C CB . GLU A 1 6 ? 66.861 26.260 33.193 1.00 18.16 ? 6 GLU A CB 1 ATOM 45 C CG . GLU A 1 6 ? 66.473 26.696 31.787 1.00 18.64 ? 6 GLU A CG 1 ATOM 46 C CD . GLU A 1 6 ? 65.476 25.759 31.132 1.00 19.09 ? 6 GLU A CD 1 ATOM 47 O OE1 . GLU A 1 6 ? 65.241 25.923 29.916 1.00 20.53 ? 6 GLU A OE1 1 ATOM 48 O OE2 . GLU A 1 6 ? 64.931 24.857 31.819 1.00 18.24 ? 6 GLU A OE2 1 ATOM 49 N N . GLU A 1 7 ? 69.083 26.562 35.838 1.00 18.09 ? 7 GLU A N 1 ATOM 50 C CA . GLU A 1 7 ? 69.309 26.309 37.263 1.00 18.42 ? 7 GLU A CA 1 ATOM 51 C C . GLU A 1 7 ? 69.425 27.593 38.064 1.00 18.14 ? 7 GLU A C 1 ATOM 52 O O . GLU A 1 7 ? 69.297 27.577 39.276 1.00 18.31 ? 7 GLU A O 1 ATOM 53 C CB . GLU A 1 7 ? 70.557 25.465 37.466 1.00 17.55 ? 7 GLU A CB 1 ATOM 54 C CG . GLU A 1 7 ? 70.432 24.119 36.816 1.00 21.06 ? 7 GLU A CG 1 ATOM 55 C CD . GLU A 1 7 ? 71.673 23.286 36.965 1.00 24.87 ? 7 GLU A CD 1 ATOM 56 O OE1 . GLU A 1 7 ? 71.661 22.360 37.764 1.00 27.32 ? 7 GLU A OE1 1 ATOM 57 O OE2 . GLU A 1 7 ? 72.668 23.552 36.280 1.00 31.37 ? 7 GLU A OE2 1 ATOM 58 N N . ASN A 1 8 ? 69.635 28.703 37.371 1.00 18.35 ? 8 ASN A N 1 ATOM 59 C CA . ASN A 1 8 ? 69.781 30.002 38.004 1.00 18.57 ? 8 ASN A CA 1 ATOM 60 C C . ASN A 1 8 ? 68.423 30.716 38.027 1.00 18.55 ? 8 ASN A C 1 ATOM 61 O O . ASN A 1 8 ? 67.839 30.934 36.975 1.00 18.68 ? 8 ASN A O 1 ATOM 62 C CB . ASN A 1 8 ? 70.814 30.806 37.197 1.00 19.09 ? 8 ASN A CB 1 ATOM 63 C CG . ASN A 1 8 ? 71.130 32.153 37.809 1.00 20.40 ? 8 ASN A CG 1 ATOM 64 O OD1 . ASN A 1 8 ? 70.384 32.673 38.637 1.00 21.16 ? 8 ASN A OD1 1 ATOM 65 N ND2 . ASN A 1 8 ? 72.259 32.731 37.401 1.00 21.11 ? 8 ASN A ND2 1 ATOM 66 N N . PRO A 1 9 ? 67.926 31.109 39.216 1.00 18.74 ? 9 PRO A N 1 ATOM 67 C CA . PRO A 1 9 ? 66.643 31.836 39.268 1.00 19.26 ? 9 PRO A CA 1 ATOM 68 C C . PRO A 1 9 ? 66.601 33.070 38.363 1.00 19.32 ? 9 PRO A C 1 ATOM 69 O O . PRO A 1 9 ? 65.543 33.380 37.817 1.00 19.18 ? 9 PRO A O 1 ATOM 70 C CB . PRO A 1 9 ? 66.521 32.273 40.733 1.00 19.52 ? 9 PRO A CB 1 ATOM 71 C CG . PRO A 1 9 ? 67.430 31.379 41.487 1.00 20.22 ? 9 PRO A CG 1 ATOM 72 C CD . PRO A 1 9 ? 68.519 30.922 40.549 1.00 18.92 ? 9 PRO A CD 1 ATOM 73 N N . ASP A 1 10 ? 67.739 33.752 38.198 1.00 19.71 ? 10 ASP A N 1 ATOM 74 C CA . ASP A 1 10 ? 67.827 34.940 37.334 1.00 20.15 ? 10 ASP A CA 1 ATOM 75 C C . ASP A 1 10 ? 67.336 34.653 35.922 1.00 19.14 ? 10 ASP A C 1 ATOM 76 O O . ASP A 1 10 ? 66.819 35.553 35.254 1.00 19.13 ? 10 ASP A O 1 ATOM 77 C CB . ASP A 1 10 ? 69.271 35.424 37.171 1.00 20.99 ? 10 ASP A CB 1 ATOM 78 C CG . ASP A 1 10 ? 69.941 35.811 38.470 1.00 25.48 ? 10 ASP A CG 1 ATOM 79 O OD1 . ASP A 1 10 ? 71.195 35.968 38.436 1.00 31.51 ? 10 ASP A OD1 1 ATOM 80 O OD2 . ASP A 1 10 ? 69.258 35.981 39.496 1.00 28.83 ? 10 ASP A OD2 1 ATOM 81 N N . PHE A 1 11 ? 67.565 33.429 35.438 1.00 17.36 ? 11 PHE A N 1 ATOM 82 C CA . PHE A 1 11 ? 67.114 33.059 34.088 1.00 16.86 ? 11 PHE A CA 1 ATOM 83 C C . PHE A 1 11 ? 65.594 33.237 34.012 1.00 15.54 ? 11 PHE A C 1 ATOM 84 O O . PHE A 1 11 ? 65.063 33.867 33.087 1.00 14.71 ? 11 PHE A O 1 ATOM 85 C CB . PHE A 1 11 ? 67.496 31.608 33.767 1.00 16.60 ? 11 PHE A CB 1 ATOM 86 C CG . PHE A 1 11 ? 66.940 31.103 32.456 1.00 17.71 ? 11 PHE A CG 1 ATOM 87 C CD1 . PHE A 1 11 ? 67.698 31.194 31.281 1.00 19.39 ? 11 PHE A CD1 1 ATOM 88 C CD2 . PHE A 1 11 ? 65.663 30.545 32.390 1.00 17.60 ? 11 PHE A CD2 1 ATOM 89 C CE1 . PHE A 1 11 ? 67.182 30.726 30.056 1.00 20.77 ? 11 PHE A CE1 1 ATOM 90 C CE2 . PHE A 1 11 ? 65.132 30.071 31.171 1.00 17.78 ? 11 PHE A CE2 1 ATOM 91 C CZ . PHE A 1 11 ? 65.898 30.155 30.007 1.00 19.15 ? 11 PHE A CZ 1 ATOM 92 N N . TRP A 1 12 ? 64.912 32.665 34.997 1.00 15.05 ? 12 TRP A N 1 ATOM 93 C CA . TRP A 1 12 ? 63.460 32.719 35.079 1.00 14.85 ? 12 TRP A CA 1 ATOM 94 C C . TRP A 1 12 ? 62.965 34.131 35.396 1.00 15.40 ? 12 TRP A C 1 ATOM 95 O O . TRP A 1 12 ? 61.975 34.598 34.820 1.00 15.46 ? 12 TRP A O 1 ATOM 96 C CB . TRP A 1 12 ? 62.962 31.669 36.082 1.00 14.34 ? 12 TRP A CB 1 ATOM 97 C CG . TRP A 1 12 ? 63.389 30.320 35.612 1.00 14.29 ? 12 TRP A CG 1 ATOM 98 C CD1 . TRP A 1 12 ? 64.426 29.558 36.099 1.00 14.70 ? 12 TRP A CD1 1 ATOM 99 C CD2 . TRP A 1 12 ? 62.862 29.609 34.485 1.00 14.35 ? 12 TRP A CD2 1 ATOM 100 N NE1 . TRP A 1 12 ? 64.547 28.400 35.352 1.00 14.59 ? 12 TRP A NE1 1 ATOM 101 C CE2 . TRP A 1 12 ? 63.597 28.408 34.363 1.00 14.69 ? 12 TRP A CE2 1 ATOM 102 C CE3 . TRP A 1 12 ? 61.828 29.867 33.572 1.00 13.95 ? 12 TRP A CE3 1 ATOM 103 C CZ2 . TRP A 1 12 ? 63.332 27.469 33.358 1.00 14.93 ? 12 TRP A CZ2 1 ATOM 104 C CZ3 . TRP A 1 12 ? 61.561 28.930 32.574 1.00 14.25 ? 12 TRP A CZ3 1 ATOM 105 C CH2 . TRP A 1 12 ? 62.313 27.744 32.478 1.00 14.50 ? 12 TRP A CH2 1 ATOM 106 N N . ASN A 1 13 ? 63.672 34.825 36.280 1.00 15.67 ? 13 ASN A N 1 ATOM 107 C CA . ASN A 1 13 ? 63.279 36.184 36.637 1.00 16.58 ? 13 ASN A CA 1 ATOM 108 C C . ASN A 1 13 ? 63.422 37.162 35.486 1.00 16.92 ? 13 ASN A C 1 ATOM 109 O O . ASN A 1 13 ? 62.541 37.980 35.256 1.00 17.40 ? 13 ASN A O 1 ATOM 110 C CB . ASN A 1 13 ? 64.030 36.636 37.893 1.00 16.92 ? 13 ASN A CB 1 ATOM 111 C CG . ASN A 1 13 ? 63.583 35.863 39.127 1.00 17.63 ? 13 ASN A CG 1 ATOM 112 O OD1 . ASN A 1 13 ? 62.426 35.457 39.225 1.00 18.11 ? 13 ASN A OD1 1 ATOM 113 N ND2 . ASN A 1 13 ? 64.505 35.625 40.051 1.00 19.04 ? 13 ASN A ND2 1 ATOM 114 N N . ARG A 1 14 ? 64.507 37.037 34.733 1.00 17.77 ? 14 ARG A N 1 ATOM 115 C CA . ARG A 1 14 ? 64.715 37.854 33.538 1.00 18.88 ? 14 ARG A CA 1 ATOM 116 C C . ARG A 1 14 ? 63.629 37.582 32.483 1.00 18.22 ? 14 ARG A C 1 ATOM 117 O O . ARG A 1 14 ? 63.050 38.517 31.922 1.00 17.39 ? 14 ARG A O 1 ATOM 118 C CB . ARG A 1 14 ? 66.097 37.570 32.961 1.00 19.54 ? 14 ARG A CB 1 ATOM 119 C CG . ARG A 1 14 ? 66.499 38.441 31.797 1.00 24.55 ? 14 ARG A CG 1 ATOM 120 C CD . ARG A 1 14 ? 67.916 38.098 31.345 1.00 31.67 ? 14 ARG A CD 1 ATOM 121 N NE . ARG A 1 14 ? 68.742 37.606 32.452 1.00 36.78 ? 14 ARG A NE 1 ATOM 122 C CZ . ARG A 1 14 ? 69.214 36.363 32.554 1.00 38.57 ? 14 ARG A CZ 1 ATOM 123 N NH1 . ARG A 1 14 ? 69.948 36.039 33.604 1.00 40.38 ? 14 ARG A NH1 1 ATOM 124 N NH2 . ARG A 1 14 ? 68.963 35.447 31.615 1.00 39.96 ? 14 ARG A NH2 1 ATOM 125 N N . GLU A 1 15 ? 63.364 36.306 32.218 1.00 17.89 ? 15 GLU A N 1 ATOM 126 C CA . GLU A 1 15 ? 62.361 35.913 31.236 1.00 18.06 ? 15 GLU A CA 1 ATOM 127 C C . GLU A 1 15 ? 61.002 36.495 31.614 1.00 17.90 ? 15 GLU A C 1 ATOM 128 O O . GLU A 1 15 ? 60.292 37.054 30.767 1.00 18.20 ? 15 GLU A O 1 ATOM 129 C CB . GLU A 1 15 ? 62.279 34.378 31.141 1.00 17.95 ? 15 GLU A CB 1 ATOM 130 C CG . GLU A 1 15 ? 61.371 33.839 30.005 1.00 20.77 ? 15 GLU A CG 1 ATOM 131 C CD . GLU A 1 15 ? 59.868 33.932 30.290 1.00 22.53 ? 15 GLU A CD 1 ATOM 132 O OE1 . GLU A 1 15 ? 59.459 33.777 31.464 1.00 23.28 ? 15 GLU A OE1 1 ATOM 133 O OE2 . GLU A 1 15 ? 59.087 34.150 29.322 1.00 24.53 ? 15 GLU A OE2 1 ATOM 134 N N . ALA A 1 16 ? 60.653 36.386 32.892 1.00 17.35 ? 16 ALA A N 1 ATOM 135 C CA . ALA A 1 16 ? 59.362 36.880 33.383 1.00 17.12 ? 16 ALA A CA 1 ATOM 136 C C . ALA A 1 16 ? 59.295 38.401 33.347 1.00 17.14 ? 16 ALA A C 1 ATOM 137 O O . ALA A 1 16 ? 58.279 38.971 32.953 1.00 16.63 ? 16 ALA A O 1 ATOM 138 C CB . ALA A 1 16 ? 59.103 36.369 34.775 1.00 17.12 ? 16 ALA A CB 1 ATOM 139 N N . ALA A 1 17 ? 60.392 39.056 33.727 1.00 17.41 ? 17 ALA A N 1 ATOM 140 C CA . ALA A 1 17 ? 60.483 40.505 33.622 1.00 17.64 ? 17 ALA A CA 1 ATOM 141 C C . ALA A 1 17 ? 60.255 40.953 32.179 1.00 18.23 ? 17 ALA A C 1 ATOM 142 O O . ALA A 1 17 ? 59.493 41.910 31.927 1.00 18.27 ? 17 ALA A O 1 ATOM 143 C CB . ALA A 1 17 ? 61.822 40.993 34.143 1.00 17.78 ? 17 ALA A CB 1 ATOM 144 N N . GLU A 1 18 ? 60.877 40.253 31.230 1.00 18.07 ? 18 GLU A N 1 ATOM 145 C CA . GLU A 1 18 ? 60.676 40.553 29.808 1.00 18.97 ? 18 GLU A CA 1 ATOM 146 C C . GLU A 1 18 ? 59.236 40.316 29.358 1.00 17.95 ? 18 GLU A C 1 ATOM 147 O O . GLU A 1 18 ? 58.651 41.142 28.642 1.00 17.32 ? 18 GLU A O 1 ATOM 148 C CB . GLU A 1 18 ? 61.653 39.764 28.943 1.00 19.77 ? 18 GLU A CB 1 ATOM 149 C CG . GLU A 1 18 ? 63.067 40.277 29.082 1.00 25.13 ? 18 GLU A CG 1 ATOM 150 C CD . GLU A 1 18 ? 64.129 39.233 28.744 1.00 32.33 ? 18 GLU A CD 1 ATOM 151 O OE1 . GLU A 1 18 ? 65.347 39.519 28.940 1.00 36.73 ? 18 GLU A OE1 1 ATOM 152 O OE2 . GLU A 1 18 ? 63.754 38.131 28.288 1.00 35.04 ? 18 GLU A OE2 1 ATOM 153 N N . ALA A 1 19 ? 58.662 39.197 29.797 1.00 17.13 ? 19 ALA A N 1 ATOM 154 C CA . ALA A 1 19 ? 57.256 38.896 29.538 1.00 16.93 ? 19 ALA A CA 1 ATOM 155 C C . ALA A 1 19 ? 56.343 39.981 30.103 1.00 17.15 ? 19 ALA A C 1 ATOM 156 O O . ALA A 1 19 ? 55.409 40.408 29.424 1.00 17.58 ? 19 ALA A O 1 ATOM 157 C CB . ALA A 1 19 ? 56.881 37.522 30.092 1.00 16.54 ? 19 ALA A CB 1 ATOM 158 N N . LEU A 1 20 ? 56.618 40.448 31.325 1.00 16.59 ? 20 LEU A N 1 ATOM 159 C CA . LEU A 1 20 ? 55.816 41.548 31.885 1.00 17.58 ? 20 LEU A CA 1 ATOM 160 C C . LEU A 1 20 ? 55.935 42.814 31.046 1.00 17.59 ? 20 LEU A C 1 ATOM 161 O O . LEU A 1 20 ? 54.926 43.474 30.758 1.00 17.29 ? 20 LEU A O 1 ATOM 162 C CB . LEU A 1 20 ? 56.178 41.841 33.347 1.00 17.71 ? 20 LEU A CB 1 ATOM 163 C CG . LEU A 1 20 ? 55.613 40.867 34.381 1.00 18.43 ? 20 LEU A CG 1 ATOM 164 C CD1 . LEU A 1 20 ? 56.319 41.128 35.711 1.00 17.62 ? 20 LEU A CD1 1 ATOM 165 C CD2 . LEU A 1 20 ? 54.089 41.009 34.513 1.00 19.61 ? 20 LEU A CD2 1 ATOM 166 N N . GLY A 1 21 ? 57.163 43.124 30.633 1.00 17.64 ? 21 GLY A N 1 ATOM 167 C CA . GLY A 1 21 ? 57.428 44.302 29.793 1.00 17.89 ? 21 GLY A CA 1 ATOM 168 C C . GLY A 1 21 ? 56.629 44.216 28.510 1.00 18.22 ? 21 GLY A C 1 ATOM 169 O O . GLY A 1 21 ? 55.972 45.190 28.109 1.00 18.89 ? 21 GLY A O 1 ATOM 170 N N . ALA A 1 22 ? 56.669 43.050 27.864 1.00 17.79 ? 22 ALA A N 1 ATOM 171 C CA . ALA A 1 22 ? 55.928 42.843 26.618 1.00 18.05 ? 22 ALA A CA 1 ATOM 172 C C . ALA A 1 22 ? 54.415 42.959 26.853 1.00 18.51 ? 22 ALA A C 1 ATOM 173 O O . ALA A 1 22 ? 53.702 43.595 26.072 1.00 19.32 ? 22 ALA A O 1 ATOM 174 C CB . ALA A 1 22 ? 56.284 41.482 26.008 1.00 18.04 ? 22 ALA A CB 1 ATOM 175 N N . ALA A 1 23 ? 53.933 42.353 27.935 1.00 18.35 ? 23 ALA A N 1 ATOM 176 C CA . ALA A 1 23 ? 52.512 42.397 28.280 1.00 18.62 ? 23 ALA A CA 1 ATOM 177 C C . ALA A 1 23 ? 52.036 43.839 28.447 1.00 18.99 ? 23 ALA A C 1 ATOM 178 O O . ALA A 1 23 ? 50.954 44.207 27.994 1.00 18.98 ? 23 ALA A O 1 ATOM 179 C CB . ALA A 1 23 ? 52.268 41.613 29.555 1.00 17.58 ? 23 ALA A CB 1 ATOM 180 N N . LYS A 1 24 ? 52.859 44.646 29.108 1.00 19.73 ? 24 LYS A N 1 ATOM 181 C CA . LYS A 1 24 ? 52.523 46.041 29.399 1.00 21.50 ? 24 LYS A CA 1 ATOM 182 C C . LYS A 1 24 ? 52.485 46.891 28.134 1.00 22.55 ? 24 LYS A C 1 ATOM 183 O O . LYS A 1 24 ? 51.764 47.884 28.076 1.00 23.34 ? 24 LYS A O 1 ATOM 184 C CB . LYS A 1 24 ? 53.529 46.623 30.394 1.00 21.24 ? 24 LYS A CB 1 ATOM 185 C CG . LYS A 1 24 ? 53.325 46.128 31.818 1.00 23.34 ? 24 LYS A CG 1 ATOM 186 C CD . LYS A 1 24 ? 54.540 46.434 32.687 1.00 27.76 ? 24 LYS A CD 1 ATOM 187 C CE . LYS A 1 24 ? 54.726 47.929 32.831 1.00 31.31 ? 24 LYS A CE 1 ATOM 188 N NZ . LYS A 1 24 ? 56.048 48.271 33.463 1.00 36.05 ? 24 LYS A NZ 1 ATOM 189 N N . LYS A 1 25 ? 53.251 46.492 27.123 1.00 23.36 ? 25 LYS A N 1 ATOM 190 C CA . LYS A 1 25 ? 53.347 47.255 25.866 1.00 24.71 ? 25 LYS A CA 1 ATOM 191 C C . LYS A 1 25 ? 52.169 47.019 24.933 1.00 24.64 ? 25 LYS A C 1 ATOM 192 O O . LYS A 1 25 ? 51.936 47.815 24.021 1.00 25.14 ? 25 LYS A O 1 ATOM 193 C CB . LYS A 1 25 ? 54.637 46.918 25.122 1.00 25.47 ? 25 LYS A CB 1 ATOM 194 C CG . LYS A 1 25 ? 55.881 47.482 25.763 1.00 29.11 ? 25 LYS A CG 1 ATOM 195 C CD . LYS A 1 25 ? 57.107 47.165 24.919 1.00 36.01 ? 25 LYS A CD 1 ATOM 196 C CE . LYS A 1 25 ? 58.291 48.059 25.298 1.00 39.33 ? 25 LYS A CE 1 ATOM 197 N NZ . LYS A 1 25 ? 58.909 47.689 26.612 1.00 43.44 ? 25 LYS A NZ 1 ATOM 198 N N . LEU A 1 26 ? 51.428 45.933 25.154 1.00 23.70 ? 26 LEU A N 1 ATOM 199 C CA . LEU A 1 26 ? 50.254 45.646 24.337 1.00 24.04 ? 26 LEU A CA 1 ATOM 200 C C . LEU A 1 26 ? 49.217 46.760 24.429 1.00 24.90 ? 26 LEU A C 1 ATOM 201 O O . LEU A 1 26 ? 48.816 47.174 25.525 1.00 24.50 ? 26 LEU A O 1 ATOM 202 C CB . LEU A 1 26 ? 49.611 44.317 24.734 1.00 23.12 ? 26 LEU A CB 1 ATOM 203 C CG . LEU A 1 26 ? 50.404 43.057 24.424 1.00 21.74 ? 26 LEU A CG 1 ATOM 204 C CD1 . LEU A 1 26 ? 49.672 41.831 24.971 1.00 19.83 ? 26 LEU A CD1 1 ATOM 205 C CD2 . LEU A 1 26 ? 50.649 42.916 22.908 1.00 20.79 ? 26 LEU A CD2 1 ATOM 206 N N . GLN A 1 27 ? 48.785 47.222 23.263 1.00 26.13 ? 27 GLN A N 1 ATOM 207 C CA . GLN A 1 27 ? 47.790 48.276 23.160 1.00 27.99 ? 27 GLN A CA 1 ATOM 208 C C . GLN A 1 27 ? 46.784 47.883 22.093 1.00 27.79 ? 27 GLN A C 1 ATOM 209 O O . GLN A 1 27 ? 47.177 47.446 21.016 1.00 28.29 ? 27 GLN A O 1 ATOM 210 C CB . GLN A 1 27 ? 48.456 49.577 22.732 1.00 28.65 ? 27 GLN A CB 1 ATOM 211 C CG . GLN A 1 27 ? 49.314 50.227 23.800 1.00 32.87 ? 27 GLN A CG 1 ATOM 212 C CD . GLN A 1 27 ? 49.679 51.649 23.444 1.00 38.46 ? 27 GLN A CD 1 ATOM 213 O OE1 . GLN A 1 27 ? 49.894 51.982 22.268 1.00 40.86 ? 27 GLN A OE1 1 ATOM 214 N NE2 . GLN A 1 27 ? 49.748 52.507 24.458 1.00 41.09 ? 27 GLN A NE2 1 ATOM 215 N N . PRO A 1 28 ? 45.487 48.060 22.371 1.00 28.28 ? 28 PRO A N 1 ATOM 216 C CA . PRO A 1 28 ? 44.459 47.793 21.363 1.00 28.00 ? 28 PRO A CA 1 ATOM 217 C C . PRO A 1 28 ? 44.522 48.788 20.196 1.00 27.84 ? 28 PRO A C 1 ATOM 218 O O . PRO A 1 28 ? 44.822 49.965 20.407 1.00 28.14 ? 28 PRO A O 1 ATOM 219 C CB . PRO A 1 28 ? 43.158 47.993 22.142 1.00 28.27 ? 28 PRO A CB 1 ATOM 220 C CG . PRO A 1 28 ? 43.520 48.946 23.232 1.00 29.02 ? 28 PRO A CG 1 ATOM 221 C CD . PRO A 1 28 ? 44.899 48.530 23.642 1.00 28.47 ? 28 PRO A CD 1 ATOM 222 N N . ALA A 1 29 ? 44.257 48.308 18.981 1.00 27.23 ? 29 ALA A N 1 ATOM 223 C CA . ALA A 1 29 ? 44.150 49.177 17.807 1.00 26.36 ? 29 ALA A CA 1 ATOM 224 C C . ALA A 1 29 ? 42.814 49.908 17.816 1.00 26.14 ? 29 ALA A C 1 ATOM 225 O O . ALA A 1 29 ? 41.817 49.384 18.291 1.00 24.61 ? 29 ALA A O 1 ATOM 226 C CB . ALA A 1 29 ? 44.296 48.368 16.511 1.00 26.12 ? 29 ALA A CB 1 ATOM 227 N N . GLN A 1 30 ? 42.806 51.126 17.282 1.00 26.35 ? 30 GLN A N 1 ATOM 228 C CA . GLN A 1 30 ? 41.571 51.873 17.088 1.00 26.89 ? 30 GLN A CA 1 ATOM 229 C C . GLN A 1 30 ? 41.125 51.731 15.625 1.00 25.88 ? 30 GLN A C 1 ATOM 230 O O . GLN A 1 30 ? 40.098 52.269 15.210 1.00 26.96 ? 30 GLN A O 1 ATOM 231 C CB . GLN A 1 30 ? 41.785 53.341 17.505 1.00 28.12 ? 30 GLN A CB 1 ATOM 232 C CG . GLN A 1 30 ? 42.473 53.441 18.882 1.00 31.62 ? 30 GLN A CG 1 ATOM 233 C CD . GLN A 1 30 ? 42.330 54.789 19.560 1.00 37.52 ? 30 GLN A CD 1 ATOM 234 O OE1 . GLN A 1 30 ? 41.850 55.759 18.967 1.00 40.89 ? 30 GLN A OE1 1 ATOM 235 N NE2 . GLN A 1 30 ? 42.758 54.858 20.822 1.00 40.13 ? 30 GLN A NE2 1 ATOM 236 N N . THR A 1 31 ? 41.888 50.949 14.862 1.00 24.39 ? 31 THR A N 1 ATOM 237 C CA . THR A 1 31 ? 41.713 50.823 13.424 1.00 22.18 ? 31 THR A CA 1 ATOM 238 C C . THR A 1 31 ? 41.232 49.426 13.030 1.00 20.75 ? 31 THR A C 1 ATOM 239 O O . THR A 1 31 ? 41.463 48.444 13.739 1.00 19.70 ? 31 THR A O 1 ATOM 240 C CB . THR A 1 31 ? 43.042 51.085 12.706 1.00 22.27 ? 31 THR A CB 1 ATOM 241 O OG1 . THR A 1 31 ? 44.046 50.223 13.266 1.00 23.32 ? 31 THR A OG1 1 ATOM 242 C CG2 . THR A 1 31 ? 43.472 52.565 12.863 1.00 22.82 ? 31 THR A CG2 1 ATOM 243 N N . ALA A 1 32 ? 40.575 49.368 11.878 1.00 19.13 ? 32 ALA A N 1 ATOM 244 C CA . ALA A 1 32 ? 40.031 48.151 11.306 1.00 18.07 ? 32 ALA A CA 1 ATOM 245 C C . ALA A 1 32 ? 41.125 47.256 10.729 1.00 17.59 ? 32 ALA A C 1 ATOM 246 O O . ALA A 1 32 ? 42.258 47.698 10.485 1.00 17.61 ? 32 ALA A O 1 ATOM 247 C CB . ALA A 1 32 ? 39.013 48.509 10.219 1.00 17.90 ? 32 ALA A CB 1 ATOM 248 N N . ALA A 1 33 ? 40.772 45.997 10.502 1.00 16.51 ? 33 ALA A N 1 ATOM 249 C CA . ALA A 1 33 ? 41.616 45.084 9.747 1.00 16.28 ? 33 ALA A CA 1 ATOM 250 C C . ALA A 1 33 ? 41.322 45.226 8.245 1.00 16.47 ? 33 ALA A C 1 ATOM 251 O O . ALA A 1 33 ? 40.167 45.172 7.821 1.00 16.62 ? 33 ALA A O 1 ATOM 252 C CB . ALA A 1 33 ? 41.375 43.648 10.203 1.00 15.88 ? 33 ALA A CB 1 ATOM 253 N N . LYS A 1 34 ? 42.371 45.438 7.458 1.00 15.96 ? 34 LYS A N 1 ATOM 254 C CA . LYS A 1 34 ? 42.269 45.395 6.001 1.00 15.87 ? 34 LYS A CA 1 ATOM 255 C C . LYS A 1 34 ? 42.154 43.938 5.548 1.00 15.05 ? 34 LYS A C 1 ATOM 256 O O . LYS A 1 34 ? 41.393 43.616 4.636 1.00 15.06 ? 34 LYS A O 1 ATOM 257 C CB . LYS A 1 34 ? 43.510 46.020 5.378 1.00 15.80 ? 34 LYS A CB 1 ATOM 258 C CG . LYS A 1 34 ? 43.551 45.979 3.852 1.00 16.87 ? 34 LYS A CG 1 ATOM 259 C CD . LYS A 1 34 ? 44.946 46.320 3.378 1.00 18.07 ? 34 LYS A CD 1 ATOM 260 C CE . LYS A 1 34 ? 45.075 46.152 1.883 1.00 19.01 ? 34 LYS A CE 1 ATOM 261 N NZ . LYS A 1 34 ? 46.461 46.466 1.429 1.00 19.35 ? 34 LYS A NZ 1 ATOM 262 N N . ASN A 1 35 ? 42.937 43.076 6.187 1.00 14.52 ? 35 ASN A N 1 ATOM 263 C CA . ASN A 1 35 ? 43.009 41.674 5.806 1.00 13.96 ? 35 ASN A CA 1 ATOM 264 C C . ASN A 1 35 ? 42.615 40.799 6.969 1.00 13.40 ? 35 ASN A C 1 ATOM 265 O O . ASN A 1 35 ? 42.849 41.153 8.126 1.00 14.23 ? 35 ASN A O 1 ATOM 266 C CB . ASN A 1 35 ? 44.441 41.292 5.408 1.00 13.72 ? 35 ASN A CB 1 ATOM 267 C CG . ASN A 1 35 ? 45.029 42.215 4.389 1.00 13.72 ? 35 ASN A CG 1 ATOM 268 O OD1 . ASN A 1 35 ? 44.422 42.497 3.351 1.00 13.12 ? 35 ASN A OD1 1 ATOM 269 N ND2 . ASN A 1 35 ? 46.234 42.690 4.663 1.00 15.36 ? 35 ASN A ND2 1 ATOM 270 N N . LEU A 1 36 ? 42.071 39.634 6.654 1.00 12.79 ? 36 LEU A N 1 ATOM 271 C CA . LEU A 1 36 ? 41.670 38.653 7.656 1.00 12.72 ? 36 LEU A CA 1 ATOM 272 C C . LEU A 1 36 ? 42.268 37.331 7.275 1.00 13.03 ? 36 LEU A C 1 ATOM 273 O O . LEU A 1 36 ? 42.155 36.916 6.123 1.00 13.31 ? 36 LEU A O 1 ATOM 274 C CB . LEU A 1 36 ? 40.148 38.510 7.666 1.00 12.03 ? 36 LEU A CB 1 ATOM 275 C CG . LEU A 1 36 ? 39.329 39.737 8.050 1.00 12.18 ? 36 LEU A CG 1 ATOM 276 C CD1 . LEU A 1 36 ? 37.865 39.429 7.769 1.00 12.26 ? 36 LEU A CD1 1 ATOM 277 C CD2 . LEU A 1 36 ? 39.561 40.074 9.529 1.00 12.89 ? 36 LEU A CD2 1 ATOM 278 N N . ILE A 1 37 ? 42.920 36.675 8.229 1.00 13.38 ? 37 ILE A N 1 ATOM 279 C CA . ILE A 1 37 ? 43.392 35.326 8.001 1.00 12.83 ? 37 ILE A CA 1 ATOM 280 C C . ILE A 1 37 ? 42.960 34.447 9.149 1.00 13.03 ? 37 ILE A C 1 ATOM 281 O O . ILE A 1 37 ? 43.170 34.780 10.322 1.00 13.46 ? 37 ILE A O 1 ATOM 282 C CB . ILE A 1 37 ? 44.925 35.223 7.887 1.00 12.81 ? 37 ILE A CB 1 ATOM 283 C CG1 . ILE A 1 37 ? 45.458 36.233 6.858 1.00 12.15 ? 37 ILE A CG1 1 ATOM 284 C CG2 . ILE A 1 37 ? 45.292 33.785 7.518 1.00 12.56 ? 37 ILE A CG2 1 ATOM 285 C CD1 . ILE A 1 37 ? 46.991 36.255 6.726 1.00 12.72 ? 37 ILE A CD1 1 ATOM 286 N N . ILE A 1 38 ? 42.358 33.322 8.806 1.00 12.80 ? 38 ILE A N 1 ATOM 287 C CA . ILE A 1 38 ? 42.124 32.305 9.801 1.00 13.09 ? 38 ILE A CA 1 ATOM 288 C C . ILE A 1 38 ? 42.952 31.059 9.464 1.00 13.01 ? 38 ILE A C 1 ATOM 289 O O . ILE A 1 38 ? 42.855 30.512 8.360 1.00 12.93 ? 38 ILE A O 1 ATOM 290 C CB . ILE A 1 38 ? 40.643 31.970 9.964 1.00 13.54 ? 38 ILE A CB 1 ATOM 291 C CG1 . ILE A 1 38 ? 40.511 30.835 11.007 1.00 13.74 ? 38 ILE A CG1 1 ATOM 292 C CG2 . ILE A 1 38 ? 39.994 31.673 8.574 1.00 13.67 ? 38 ILE A CG2 1 ATOM 293 C CD1 . ILE A 1 38 ? 39.105 30.546 11.441 1.00 18.01 ? 38 ILE A CD1 1 ATOM 294 N N . PHE A 1 39 ? 43.799 30.665 10.411 1.00 12.33 ? 39 PHE A N 1 ATOM 295 C CA . PHE A 1 39 ? 44.595 29.458 10.290 1.00 12.24 ? 39 PHE A CA 1 ATOM 296 C C . PHE A 1 39 ? 43.896 28.421 11.147 1.00 12.16 ? 39 PHE A C 1 ATOM 297 O O . PHE A 1 39 ? 43.775 28.584 12.358 1.00 12.49 ? 39 PHE A O 1 ATOM 298 C CB . PHE A 1 39 ? 46.018 29.658 10.824 1.00 12.61 ? 39 PHE A CB 1 ATOM 299 C CG . PHE A 1 39 ? 46.788 30.755 10.147 1.00 12.68 ? 39 PHE A CG 1 ATOM 300 C CD1 . PHE A 1 39 ? 46.812 32.043 10.690 1.00 12.94 ? 39 PHE A CD1 1 ATOM 301 C CD2 . PHE A 1 39 ? 47.489 30.506 8.981 1.00 12.80 ? 39 PHE A CD2 1 ATOM 302 C CE1 . PHE A 1 39 ? 47.543 33.055 10.083 1.00 13.79 ? 39 PHE A CE1 1 ATOM 303 C CE2 . PHE A 1 39 ? 48.224 31.506 8.362 1.00 11.93 ? 39 PHE A CE2 1 ATOM 304 C CZ . PHE A 1 39 ? 48.248 32.786 8.906 1.00 13.24 ? 39 PHE A CZ 1 ATOM 305 N N . LEU A 1 40 ? 43.430 27.367 10.507 1.00 11.37 ? 40 LEU A N 1 ATOM 306 C CA . LEU A 1 40 ? 42.660 26.331 11.176 1.00 11.47 ? 40 LEU A CA 1 ATOM 307 C C . LEU A 1 40 ? 43.484 25.052 11.215 1.00 11.26 ? 40 LEU A C 1 ATOM 308 O O . LEU A 1 40 ? 43.778 24.465 10.169 1.00 10.85 ? 40 LEU A O 1 ATOM 309 C CB . LEU A 1 40 ? 41.340 26.088 10.421 1.00 11.52 ? 40 LEU A CB 1 ATOM 310 C CG . LEU A 1 40 ? 40.240 25.301 11.132 1.00 12.45 ? 40 LEU A CG 1 ATOM 311 C CD1 . LEU A 1 40 ? 40.578 23.815 11.270 1.00 12.07 ? 40 LEU A CD1 1 ATOM 312 C CD2 . LEU A 1 40 ? 39.922 25.917 12.512 1.00 13.36 ? 40 LEU A CD2 1 ATOM 313 N N . GLY A 1 41 ? 43.868 24.639 12.421 1.00 11.16 ? 41 GLY A N 1 ATOM 314 C CA . GLY A 1 41 ? 44.575 23.373 12.627 1.00 11.06 ? 41 GLY A CA 1 ATOM 315 C C . GLY A 1 41 ? 43.506 22.350 12.935 1.00 11.15 ? 41 GLY A C 1 ATOM 316 O O . GLY A 1 41 ? 42.908 22.356 14.022 1.00 11.77 ? 41 GLY A O 1 ATOM 317 N N . ASP A 1 42 ? 43.207 21.494 11.969 1.00 11.09 ? 42 ASP A N 1 ATOM 318 C CA . ASP A 1 42 ? 42.090 20.594 12.166 1.00 10.77 ? 42 ASP A CA 1 ATOM 319 C C . ASP A 1 42 ? 42.495 19.545 13.185 1.00 10.33 ? 42 ASP A C 1 ATOM 320 O O . ASP A 1 42 ? 43.431 18.809 12.969 1.00 10.19 ? 42 ASP A O 1 ATOM 321 C CB . ASP A 1 42 ? 41.655 19.939 10.852 1.00 11.30 ? 42 ASP A CB 1 ATOM 322 C CG . ASP A 1 42 ? 40.253 19.371 10.939 1.00 10.60 ? 42 ASP A CG 1 ATOM 323 O OD1 . ASP A 1 42 ? 39.944 18.660 11.924 1.00 11.33 ? 42 ASP A OD1 1 ATOM 324 O OD2 . ASP A 1 42 ? 39.436 19.655 10.035 1.00 11.86 ? 42 ASP A OD2 1 ATOM 325 N N . GLY A 1 43 ? 41.803 19.512 14.320 1.00 10.70 ? 43 GLY A N 1 ATOM 326 C CA . GLY A 1 43 ? 42.111 18.544 15.361 1.00 10.61 ? 43 GLY A CA 1 ATOM 327 C C . GLY A 1 43 ? 43.216 18.998 16.308 1.00 10.64 ? 43 GLY A C 1 ATOM 328 O O . GLY A 1 43 ? 43.610 18.251 17.212 1.00 11.32 ? 43 GLY A O 1 ATOM 329 N N . MET A 1 44 ? 43.681 20.231 16.127 1.00 10.24 ? 44 MET A N 1 ATOM 330 C CA . MET A 1 44 ? 44.844 20.745 16.857 1.00 11.17 ? 44 MET A CA 1 ATOM 331 C C . MET A 1 44 ? 44.476 21.299 18.248 1.00 11.17 ? 44 MET A C 1 ATOM 332 O O . MET A 1 44 ? 44.516 22.516 18.496 1.00 11.57 ? 44 MET A O 1 ATOM 333 C CB . MET A 1 44 ? 45.575 21.794 15.998 1.00 10.76 ? 44 MET A CB 1 ATOM 334 C CG . MET A 1 44 ? 46.991 22.107 16.485 1.00 11.57 ? 44 MET A CG 1 ATOM 335 S SD . MET A 1 44 ? 47.593 23.669 15.812 1.00 12.24 ? 44 MET A SD 1 ATOM 336 C CE . MET A 1 44 ? 46.553 24.909 16.610 1.00 11.17 ? 44 MET A CE 1 ATOM 337 N N . GLY A 1 45 ? 44.134 20.386 19.157 1.00 10.99 ? 45 GLY A N 1 ATOM 338 C CA . GLY A 1 45 ? 43.860 20.755 20.538 1.00 10.85 ? 45 GLY A CA 1 ATOM 339 C C . GLY A 1 45 ? 45.111 21.121 21.308 1.00 10.90 ? 45 GLY A C 1 ATOM 340 O O . GLY A 1 45 ? 46.236 21.058 20.785 1.00 10.08 ? 45 GLY A O 1 ATOM 341 N N . VAL A 1 46 ? 44.906 21.476 22.573 1.00 10.75 ? 46 VAL A N 1 ATOM 342 C CA . VAL A 1 46 ? 45.965 21.996 23.410 1.00 11.28 ? 46 VAL A CA 1 ATOM 343 C C . VAL A 1 46 ? 47.096 20.968 23.545 1.00 11.14 ? 46 VAL A C 1 ATOM 344 O O . VAL A 1 46 ? 48.271 21.340 23.441 1.00 10.35 ? 46 VAL A O 1 ATOM 345 C CB . VAL A 1 46 ? 45.407 22.459 24.783 1.00 11.69 ? 46 VAL A CB 1 ATOM 346 C CG1 . VAL A 1 46 ? 46.547 22.800 25.741 1.00 12.74 ? 46 VAL A CG1 1 ATOM 347 C CG2 . VAL A 1 46 ? 44.479 23.692 24.580 1.00 11.14 ? 46 VAL A CG2 1 ATOM 348 N N . SER A 1 47 ? 46.748 19.682 23.719 1.00 10.77 ? 47 SER A N 1 ATOM 349 C CA . SER A 1 47 ? 47.782 18.633 23.843 1.00 11.30 ? 47 SER A CA 1 ATOM 350 C C . SER A 1 47 ? 48.562 18.484 22.535 1.00 11.17 ? 47 SER A C 1 ATOM 351 O O . SER A 1 47 ? 49.751 18.200 22.566 1.00 11.43 ? 47 SER A O 1 ATOM 352 C CB . SER A 1 47 ? 47.196 17.288 24.305 1.00 10.88 ? 47 SER A CB 1 ATOM 353 O OG . SER A 1 47 ? 46.261 16.802 23.343 1.00 13.71 ? 47 SER A OG 1 ATOM 354 N N . THR A 1 48 ? 47.893 18.700 21.398 1.00 10.38 ? 48 THR A N 1 ATOM 355 C CA . THR A 1 48 ? 48.575 18.697 20.094 1.00 10.86 ? 48 THR A CA 1 ATOM 356 C C . THR A 1 48 ? 49.561 19.852 19.982 1.00 10.81 ? 48 THR A C 1 ATOM 357 O O . THR A 1 48 ? 50.710 19.656 19.575 1.00 11.33 ? 48 THR A O 1 ATOM 358 C CB . THR A 1 48 ? 47.582 18.721 18.919 1.00 10.44 ? 48 THR A CB 1 ATOM 359 O OG1 . THR A 1 48 ? 46.697 17.604 19.054 1.00 10.32 ? 48 THR A OG1 1 ATOM 360 C CG2 . THR A 1 48 ? 48.332 18.614 17.573 1.00 10.06 ? 48 THR A CG2 1 ATOM 361 N N . VAL A 1 49 ? 49.121 21.043 20.369 1.00 10.21 ? 49 VAL A N 1 ATOM 362 C CA . VAL A 1 49 ? 49.995 22.216 20.349 1.00 10.54 ? 49 VAL A CA 1 ATOM 363 C C . VAL A 1 49 ? 51.263 21.972 21.172 1.00 10.51 ? 49 VAL A C 1 ATOM 364 O O . VAL A 1 49 ? 52.372 22.173 20.672 1.00 9.91 ? 49 VAL A O 1 ATOM 365 C CB . VAL A 1 49 ? 49.245 23.478 20.776 1.00 10.30 ? 49 VAL A CB 1 ATOM 366 C CG1 . VAL A 1 49 ? 50.216 24.669 20.943 1.00 11.43 ? 49 VAL A CG1 1 ATOM 367 C CG2 . VAL A 1 49 ? 48.184 23.799 19.721 1.00 10.70 ? 49 VAL A CG2 1 ATOM 368 N N . THR A 1 50 ? 51.105 21.507 22.410 1.00 10.61 ? 50 THR A N 1 ATOM 369 C CA . THR A 1 50 ? 52.276 21.327 23.280 1.00 11.19 ? 50 THR A CA 1 ATOM 370 C C . THR A 1 50 ? 53.202 20.259 22.735 1.00 11.32 ? 50 THR A C 1 ATOM 371 O O . THR A 1 50 ? 54.421 20.452 22.694 1.00 11.31 ? 50 THR A O 1 ATOM 372 C CB . THR A 1 50 ? 51.897 20.969 24.708 1.00 11.06 ? 50 THR A CB 1 ATOM 373 O OG1 . THR A 1 50 ? 51.059 21.998 25.226 1.00 12.15 ? 50 THR A OG1 1 ATOM 374 C CG2 . THR A 1 50 ? 53.163 20.871 25.604 1.00 11.48 ? 50 THR A CG2 1 ATOM 375 N N . ALA A 1 51 ? 52.634 19.129 22.324 1.00 11.26 ? 51 ALA A N 1 ATOM 376 C CA . ALA A 1 51 ? 53.465 18.046 21.798 1.00 11.58 ? 51 ALA A CA 1 ATOM 377 C C . ALA A 1 51 ? 54.191 18.492 20.523 1.00 11.88 ? 51 ALA A C 1 ATOM 378 O O . ALA A 1 51 ? 55.363 18.178 20.338 1.00 11.87 ? 51 ALA A O 1 ATOM 379 C CB . ALA A 1 51 ? 52.628 16.787 21.547 1.00 10.82 ? 51 ALA A CB 1 ATOM 380 N N . ALA A 1 52 ? 53.499 19.229 19.658 1.00 11.98 ? 52 ALA A N 1 ATOM 381 C CA . ALA A 1 52 ? 54.131 19.785 18.449 1.00 12.99 ? 52 ALA A CA 1 ATOM 382 C C . ALA A 1 52 ? 55.230 20.788 18.771 1.00 13.38 ? 52 ALA A C 1 ATOM 383 O O . ALA A 1 52 ? 56.284 20.786 18.118 1.00 14.29 ? 52 ALA A O 1 ATOM 384 C CB . ALA A 1 52 ? 53.090 20.431 17.539 1.00 12.79 ? 52 ALA A CB 1 ATOM 385 N N . ARG A 1 53 ? 54.980 21.650 19.759 1.00 13.17 ? 53 ARG A N 1 ATOM 386 C CA . ARG A 1 53 ? 56.002 22.593 20.226 1.00 13.22 ? 53 ARG A CA 1 ATOM 387 C C . ARG A 1 53 ? 57.288 21.860 20.614 1.00 13.20 ? 53 ARG A C 1 ATOM 388 O O . ARG A 1 53 ? 58.392 22.269 20.210 1.00 13.34 ? 53 ARG A O 1 ATOM 389 C CB . ARG A 1 53 ? 55.479 23.415 21.408 1.00 12.31 ? 53 ARG A CB 1 ATOM 390 C CG . ARG A 1 53 ? 56.473 24.453 21.929 1.00 12.73 ? 53 ARG A CG 1 ATOM 391 C CD . ARG A 1 53 ? 56.012 25.052 23.248 1.00 13.22 ? 53 ARG A CD 1 ATOM 392 N NE . ARG A 1 53 ? 54.707 25.677 23.095 1.00 12.56 ? 53 ARG A NE 1 ATOM 393 C CZ . ARG A 1 53 ? 53.653 25.436 23.876 1.00 14.32 ? 53 ARG A CZ 1 ATOM 394 N NH1 . ARG A 1 53 ? 52.506 26.061 23.633 1.00 13.31 ? 53 ARG A NH1 1 ATOM 395 N NH2 . ARG A 1 53 ? 53.734 24.565 24.887 1.00 14.57 ? 53 ARG A NH2 1 ATOM 396 N N . ILE A 1 54 ? 57.139 20.793 21.395 1.00 13.28 ? 54 ILE A N 1 ATOM 397 C CA . ILE A 1 54 ? 58.277 20.012 21.865 1.00 13.40 ? 54 ILE A CA 1 ATOM 398 C C . ILE A 1 54 ? 58.981 19.393 20.684 1.00 13.72 ? 54 ILE A C 1 ATOM 399 O O . ILE A 1 54 ? 60.192 19.499 20.569 1.00 13.62 ? 54 ILE A O 1 ATOM 400 C CB . ILE A 1 54 ? 57.857 18.920 22.896 1.00 13.42 ? 54 ILE A CB 1 ATOM 401 C CG1 . ILE A 1 54 ? 57.372 19.596 24.175 1.00 13.87 ? 54 ILE A CG1 1 ATOM 402 C CG2 . ILE A 1 54 ? 59.027 17.958 23.222 1.00 13.95 ? 54 ILE A CG2 1 ATOM 403 C CD1 . ILE A 1 54 ? 56.690 18.651 25.164 1.00 13.51 ? 54 ILE A CD1 1 ATOM 404 N N . LEU A 1 55 ? 58.221 18.770 19.791 1.00 13.76 ? 55 LEU A N 1 ATOM 405 C CA . LEU A 1 55 ? 58.810 18.161 18.599 1.00 14.85 ? 55 LEU A CA 1 ATOM 406 C C . LEU A 1 55 ? 59.541 19.200 17.752 1.00 15.66 ? 55 LEU A C 1 ATOM 407 O O . LEU A 1 55 ? 60.693 18.980 17.364 1.00 16.13 ? 55 LEU A O 1 ATOM 408 C CB . LEU A 1 55 ? 57.747 17.446 17.761 1.00 14.48 ? 55 LEU A CB 1 ATOM 409 C CG . LEU A 1 55 ? 58.235 16.805 16.456 1.00 14.59 ? 55 LEU A CG 1 ATOM 410 C CD1 . LEU A 1 55 ? 59.336 15.769 16.718 1.00 14.26 ? 55 LEU A CD1 1 ATOM 411 C CD2 . LEU A 1 55 ? 57.047 16.205 15.687 1.00 14.94 ? 55 LEU A CD2 1 ATOM 412 N N . LYS A 1 56 ? 58.900 20.339 17.503 1.00 17.34 ? 56 LYS A N 1 ATOM 413 C CA . LYS A 1 56 ? 59.502 21.402 16.681 1.00 19.39 ? 56 LYS A CA 1 ATOM 414 C C . LYS A 1 56 ? 60.790 21.916 17.321 1.00 20.81 ? 56 LYS A C 1 ATOM 415 O O . LYS A 1 56 ? 61.785 22.149 16.628 1.00 20.85 ? 56 LYS A O 1 ATOM 416 C CB . LYS A 1 56 ? 58.530 22.553 16.446 1.00 19.19 ? 56 LYS A CB 1 ATOM 417 C CG . LYS A 1 56 ? 59.073 23.652 15.483 1.00 20.37 ? 56 LYS A CG 1 ATOM 418 C CD . LYS A 1 56 ? 57.929 24.514 14.938 1.00 20.91 ? 56 LYS A CD 1 ATOM 419 C CE . LYS A 1 56 ? 58.414 25.544 13.895 1.00 22.72 ? 56 LYS A CE 1 ATOM 420 N NZ . LYS A 1 56 ? 57.220 26.170 13.259 1.00 23.37 ? 56 LYS A NZ 1 ATOM 421 N N . GLY A 1 57 ? 60.754 22.083 18.642 1.00 22.75 ? 57 GLY A N 1 ATOM 422 C CA . GLY A 1 57 ? 61.890 22.584 19.406 1.00 25.08 ? 57 GLY A CA 1 ATOM 423 C C . GLY A 1 57 ? 63.072 21.669 19.213 1.00 26.89 ? 57 GLY A C 1 ATOM 424 O O . GLY A 1 57 ? 64.190 22.128 18.958 1.00 27.94 ? 57 GLY A O 1 ATOM 425 N N . GLN A 1 58 ? 62.808 20.372 19.294 1.00 28.18 ? 58 GLN A N 1 ATOM 426 C CA . GLN A 1 58 ? 63.840 19.359 19.168 1.00 29.88 ? 58 GLN A CA 1 ATOM 427 C C . GLN A 1 58 ? 64.359 19.187 17.753 1.00 31.42 ? 58 GLN A C 1 ATOM 428 O O . GLN A 1 58 ? 65.537 18.894 17.573 1.00 31.76 ? 58 GLN A O 1 ATOM 429 C CB . GLN A 1 58 ? 63.354 18.032 19.728 1.00 29.45 ? 58 GLN A CB 1 ATOM 430 C CG . GLN A 1 58 ? 63.142 18.123 21.221 1.00 29.03 ? 58 GLN A CG 1 ATOM 431 C CD . GLN A 1 58 ? 62.598 16.859 21.810 1.00 27.59 ? 58 GLN A CD 1 ATOM 432 O OE1 . GLN A 1 58 ? 62.375 15.885 21.098 1.00 27.90 ? 58 GLN A OE1 1 ATOM 433 N NE2 . GLN A 1 58 ? 62.378 16.861 23.123 1.00 24.95 ? 58 GLN A NE2 1 ATOM 434 N N . LYS A 1 59 ? 63.487 19.376 16.761 1.00 33.17 ? 59 LYS A N 1 ATOM 435 C CA . LYS A 1 59 ? 63.903 19.376 15.349 1.00 34.83 ? 59 LYS A CA 1 ATOM 436 C C . LYS A 1 59 ? 64.886 20.508 15.092 1.00 35.43 ? 59 LYS A C 1 ATOM 437 O O . LYS A 1 59 ? 65.741 20.410 14.215 1.00 35.85 ? 59 LYS A O 1 ATOM 438 C CB . LYS A 1 59 ? 62.692 19.460 14.398 1.00 34.77 ? 59 LYS A CB 1 ATOM 439 C CG . LYS A 1 59 ? 61.863 18.177 14.362 1.00 36.65 ? 59 LYS A CG 1 ATOM 440 C CD . LYS A 1 59 ? 61.043 18.043 13.085 1.00 39.79 ? 59 LYS A CD 1 ATOM 441 C CE . LYS A 1 59 ? 60.444 16.634 12.969 1.00 41.43 ? 59 LYS A CE 1 ATOM 442 N NZ . LYS A 1 59 ? 59.915 16.312 11.607 1.00 42.43 ? 59 LYS A NZ 1 ATOM 443 N N . LYS A 1 60 ? 64.773 21.572 15.882 1.00 36.34 ? 60 LYS A N 1 ATOM 444 C CA . LYS A 1 60 ? 65.694 22.708 15.814 1.00 37.22 ? 60 LYS A CA 1 ATOM 445 C C . LYS A 1 60 ? 66.868 22.539 16.769 1.00 37.32 ? 60 LYS A C 1 ATOM 446 O O . LYS A 1 60 ? 67.560 23.512 17.069 1.00 38.03 ? 60 LYS A O 1 ATOM 447 C CB . LYS A 1 60 ? 64.973 24.010 16.170 1.00 37.49 ? 60 LYS A CB 1 ATOM 448 C CG . LYS A 1 60 ? 63.878 24.458 15.211 1.00 39.26 ? 60 LYS A CG 1 ATOM 449 C CD . LYS A 1 60 ? 62.956 25.432 15.936 1.00 42.53 ? 60 LYS A CD 1 ATOM 450 C CE . LYS A 1 60 ? 62.193 26.308 14.966 1.00 44.39 ? 60 LYS A CE 1 ATOM 451 N NZ . LYS A 1 60 ? 61.393 27.325 15.707 1.00 43.97 ? 60 LYS A NZ 1 ATOM 452 N N . ASP A 1 61 ? 67.072 21.312 17.249 1.00 37.56 ? 61 ASP A N 1 ATOM 453 C CA . ASP A 1 61 ? 68.150 20.956 18.195 1.00 37.73 ? 61 ASP A CA 1 ATOM 454 C C . ASP A 1 61 ? 68.083 21.690 19.551 1.00 36.82 ? 61 ASP A C 1 ATOM 455 O O . ASP A 1 61 ? 69.109 22.066 20.134 1.00 37.00 ? 61 ASP A O 1 ATOM 456 C CB . ASP A 1 61 ? 69.532 21.104 17.532 1.00 38.88 ? 61 ASP A CB 1 ATOM 457 C CG . ASP A 1 61 ? 69.587 20.451 16.155 1.00 41.73 ? 61 ASP A CG 1 ATOM 458 O OD1 . ASP A 1 61 ? 69.340 19.221 16.067 1.00 44.56 ? 61 ASP A OD1 1 ATOM 459 O OD2 . ASP A 1 61 ? 69.868 21.171 15.162 1.00 45.88 ? 61 ASP A OD2 1 ATOM 460 N N . LYS A 1 62 ? 66.865 21.891 20.043 1.00 34.78 ? 62 LYS A N 1 ATOM 461 C CA . LYS A 1 62 ? 66.656 22.450 21.372 1.00 33.23 ? 62 LYS A CA 1 ATOM 462 C C . LYS A 1 62 ? 65.994 21.357 22.204 1.00 31.64 ? 62 LYS A C 1 ATOM 463 O O . LYS A 1 62 ? 65.679 20.294 21.672 1.00 31.70 ? 62 LYS A O 1 ATOM 464 C CB . LYS A 1 62 ? 65.796 23.713 21.292 1.00 33.20 ? 62 LYS A CB 1 ATOM 465 C CG . LYS A 1 62 ? 66.343 24.776 20.332 1.00 35.48 ? 62 LYS A CG 1 ATOM 466 C CD . LYS A 1 62 ? 67.534 25.514 20.934 1.00 38.76 ? 62 LYS A CD 1 ATOM 467 C CE . LYS A 1 62 ? 68.189 26.465 19.933 1.00 42.19 ? 62 LYS A CE 1 ATOM 468 N NZ . LYS A 1 62 ? 69.129 25.759 19.007 1.00 44.94 ? 62 LYS A NZ 1 ATOM 469 N N . LEU A 1 63 ? 65.786 21.605 23.496 1.00 29.30 ? 63 LEU A N 1 ATOM 470 C CA . LEU A 1 63 ? 65.201 20.591 24.364 1.00 27.44 ? 63 LEU A CA 1 ATOM 471 C C . LEU A 1 63 ? 63.721 20.361 24.050 1.00 26.08 ? 63 LEU A C 1 ATOM 472 O O . LEU A 1 63 ? 63.197 19.256 24.254 1.00 25.50 ? 63 LEU A O 1 ATOM 473 C CB . LEU A 1 63 ? 65.411 20.948 25.832 1.00 27.42 ? 63 LEU A CB 1 ATOM 474 C CG . LEU A 1 63 ? 66.899 20.923 26.197 1.00 27.62 ? 63 LEU A CG 1 ATOM 475 C CD1 . LEU A 1 63 ? 67.119 21.486 27.577 1.00 27.48 ? 63 LEU A CD1 1 ATOM 476 C CD2 . LEU A 1 63 ? 67.473 19.502 26.070 1.00 28.45 ? 63 LEU A CD2 1 ATOM 477 N N . GLY A 1 64 ? 63.062 21.416 23.565 1.00 24.61 ? 64 GLY A N 1 ATOM 478 C CA . GLY A 1 64 ? 61.688 21.326 23.072 1.00 23.77 ? 64 GLY A CA 1 ATOM 479 C C . GLY A 1 64 ? 60.723 22.344 23.677 1.00 22.78 ? 64 GLY A C 1 ATOM 480 O O . GLY A 1 64 ? 60.383 23.344 23.030 1.00 23.13 ? 64 GLY A O 1 ATOM 481 N N . PRO A 1 65 ? 60.265 22.096 24.917 1.00 22.05 ? 65 PRO A N 1 ATOM 482 C CA . PRO A 1 65 ? 59.106 22.831 25.474 1.00 21.65 ? 65 PRO A CA 1 ATOM 483 C C . PRO A 1 65 ? 59.313 24.347 25.690 1.00 21.50 ? 65 PRO A C 1 ATOM 484 O O . PRO A 1 65 ? 58.343 25.104 25.779 1.00 20.49 ? 65 PRO A O 1 ATOM 485 C CB . PRO A 1 65 ? 58.848 22.107 26.801 1.00 21.94 ? 65 PRO A CB 1 ATOM 486 C CG . PRO A 1 65 ? 60.173 21.532 27.182 1.00 22.08 ? 65 PRO A CG 1 ATOM 487 C CD . PRO A 1 65 ? 60.784 21.096 25.873 1.00 22.17 ? 65 PRO A CD 1 ATOM 488 N N . GLU A 1 66 ? 60.567 24.779 25.752 1.00 21.74 ? 66 GLU A N 1 ATOM 489 C CA . GLU A 1 66 ? 60.899 26.195 25.955 1.00 22.24 ? 66 GLU A CA 1 ATOM 490 C C . GLU A 1 66 ? 60.876 27.003 24.652 1.00 22.54 ? 66 GLU A C 1 ATOM 491 O O . GLU A 1 66 ? 60.941 28.231 24.688 1.00 22.77 ? 66 GLU A O 1 ATOM 492 C CB . GLU A 1 66 ? 62.287 26.323 26.611 1.00 21.88 ? 66 GLU A CB 1 ATOM 493 C CG . GLU A 1 66 ? 63.472 25.943 25.706 1.00 22.45 ? 66 GLU A CG 1 ATOM 494 C CD . GLU A 1 66 ? 63.575 24.442 25.389 1.00 24.18 ? 66 GLU A CD 1 ATOM 495 O OE1 . GLU A 1 66 ? 62.963 23.608 26.098 1.00 20.96 ? 66 GLU A OE1 1 ATOM 496 O OE2 . GLU A 1 66 ? 64.284 24.098 24.414 1.00 25.00 ? 66 GLU A OE2 1 ATOM 497 N N . ILE A 1 67 ? 60.803 26.322 23.506 1.00 22.40 ? 67 ILE A N 1 ATOM 498 C CA . ILE A 1 67 ? 60.874 27.014 22.201 1.00 22.32 ? 67 ILE A CA 1 ATOM 499 C C . ILE A 1 67 ? 59.472 27.342 21.688 1.00 21.96 ? 67 ILE A C 1 ATOM 500 O O . ILE A 1 67 ? 58.671 26.429 21.472 1.00 22.04 ? 67 ILE A O 1 ATOM 501 C CB . ILE A 1 67 ? 61.628 26.154 21.140 1.00 22.58 ? 67 ILE A CB 1 ATOM 502 C CG1 . ILE A 1 67 ? 63.046 25.799 21.639 1.00 24.61 ? 67 ILE A CG1 1 ATOM 503 C CG2 . ILE A 1 67 ? 61.634 26.835 19.755 1.00 22.68 ? 67 ILE A CG2 1 ATOM 504 C CD1 . ILE A 1 67 ? 63.920 27.003 22.033 1.00 24.84 ? 67 ILE A CD1 1 ATOM 505 N N . PRO A 1 68 ? 59.159 28.647 21.512 1.00 21.05 ? 68 PRO A N 1 ATOM 506 C CA . PRO A 1 68 ? 57.826 28.982 21.011 1.00 20.01 ? 68 PRO A CA 1 ATOM 507 C C . PRO A 1 68 ? 57.552 28.523 19.569 1.00 18.95 ? 68 PRO A C 1 ATOM 508 O O . PRO A 1 68 ? 58.404 28.647 18.674 1.00 18.65 ? 68 PRO A O 1 ATOM 509 C CB . PRO A 1 68 ? 57.778 30.515 21.106 1.00 19.96 ? 68 PRO A CB 1 ATOM 510 C CG . PRO A 1 68 ? 58.865 30.872 22.122 1.00 21.36 ? 68 PRO A CG 1 ATOM 511 C CD . PRO A 1 68 ? 59.946 29.860 21.815 1.00 21.28 ? 68 PRO A CD 1 ATOM 512 N N . LEU A 1 69 ? 56.364 27.979 19.362 1.00 16.81 ? 69 LEU A N 1 ATOM 513 C CA . LEU A 1 69 ? 55.809 27.849 18.022 1.00 15.43 ? 69 LEU A CA 1 ATOM 514 C C . LEU A 1 69 ? 55.532 29.262 17.521 1.00 14.63 ? 69 LEU A C 1 ATOM 515 O O . LEU A 1 69 ? 55.419 30.203 18.321 1.00 14.03 ? 69 LEU A O 1 ATOM 516 C CB . LEU A 1 69 ? 54.486 27.086 18.099 1.00 15.01 ? 69 LEU A CB 1 ATOM 517 C CG . LEU A 1 69 ? 54.608 25.615 18.481 1.00 14.79 ? 69 LEU A CG 1 ATOM 518 C CD1 . LEU A 1 69 ? 53.236 25.063 18.886 1.00 15.20 ? 69 LEU A CD1 1 ATOM 519 C CD2 . LEU A 1 69 ? 55.236 24.810 17.347 1.00 14.69 ? 69 LEU A CD2 1 ATOM 520 N N . ALA A 1 70 ? 55.417 29.434 16.207 1.00 14.28 ? 70 ALA A N 1 ATOM 521 C CA . ALA A 1 70 ? 54.980 30.728 15.679 1.00 13.48 ? 70 ALA A CA 1 ATOM 522 C C . ALA A 1 70 ? 53.642 31.135 16.302 1.00 13.64 ? 70 ALA A C 1 ATOM 523 O O . ALA A 1 70 ? 53.448 32.303 16.659 1.00 12.61 ? 70 ALA A O 1 ATOM 524 C CB . ALA A 1 70 ? 54.875 30.692 14.161 1.00 14.20 ? 70 ALA A CB 1 ATOM 525 N N . MET A 1 71 ? 52.725 30.181 16.457 1.00 13.09 ? 71 MET A N 1 ATOM 526 C CA . MET A 1 71 ? 51.427 30.520 17.067 1.00 13.42 ? 71 MET A CA 1 ATOM 527 C C . MET A 1 71 ? 51.564 30.983 18.522 1.00 13.85 ? 71 MET A C 1 ATOM 528 O O . MET A 1 71 ? 50.766 31.802 18.982 1.00 13.66 ? 71 MET A O 1 ATOM 529 C CB . MET A 1 71 ? 50.419 29.374 16.947 1.00 13.44 ? 71 MET A CB 1 ATOM 530 C CG . MET A 1 71 ? 50.820 28.103 17.686 1.00 13.29 ? 71 MET A CG 1 ATOM 531 S SD . MET A 1 71 ? 49.664 26.775 17.382 1.00 15.56 ? 71 MET A SD 1 ATOM 532 C CE . MET A 1 71 ? 50.249 26.164 15.797 1.00 13.73 ? 71 MET A CE 1 ATOM 533 N N . ASP A 1 72 ? 52.586 30.484 19.230 1.00 13.60 ? 72 ASP A N 1 ATOM 534 C CA . ASP A 1 72 ? 52.808 30.833 20.634 1.00 14.45 ? 72 ASP A CA 1 ATOM 535 C C . ASP A 1 72 ? 53.147 32.311 20.816 1.00 15.04 ? 72 ASP A C 1 ATOM 536 O O . ASP A 1 72 ? 53.004 32.857 21.909 1.00 15.78 ? 72 ASP A O 1 ATOM 537 C CB . ASP A 1 72 ? 53.981 30.048 21.205 1.00 14.40 ? 72 ASP A CB 1 ATOM 538 C CG . ASP A 1 72 ? 53.680 28.583 21.423 1.00 15.01 ? 72 ASP A CG 1 ATOM 539 O OD1 . ASP A 1 72 ? 52.506 28.165 21.427 1.00 15.45 ? 72 ASP A OD1 1 ATOM 540 O OD2 . ASP A 1 72 ? 54.664 27.846 21.611 1.00 15.53 ? 72 ASP A OD2 1 ATOM 541 N N . ARG A 1 73 ? 53.595 32.950 19.744 1.00 14.87 ? 73 ARG A N 1 ATOM 542 C CA . ARG A 1 73 ? 54.010 34.347 19.785 1.00 15.05 ? 73 ARG A CA 1 ATOM 543 C C . ARG A 1 73 ? 52.839 35.306 19.641 1.00 15.07 ? 73 ARG A C 1 ATOM 544 O O . ARG A 1 73 ? 52.991 36.506 19.851 1.00 15.08 ? 73 ARG A O 1 ATOM 545 C CB . ARG A 1 73 ? 55.039 34.609 18.684 1.00 15.40 ? 73 ARG A CB 1 ATOM 546 C CG . ARG A 1 73 ? 56.249 33.726 18.845 1.00 17.87 ? 73 ARG A CG 1 ATOM 547 C CD . ARG A 1 73 ? 57.399 34.241 18.029 1.00 21.31 ? 73 ARG A CD 1 ATOM 548 N NE . ARG A 1 73 ? 58.576 33.395 18.220 1.00 27.33 ? 73 ARG A NE 1 ATOM 549 C CZ . ARG A 1 73 ? 59.478 33.568 19.181 1.00 28.70 ? 73 ARG A CZ 1 ATOM 550 N NH1 . ARG A 1 73 ? 59.348 34.560 20.054 1.00 30.45 ? 73 ARG A NH1 1 ATOM 551 N NH2 . ARG A 1 73 ? 60.515 32.744 19.269 1.00 31.26 ? 73 ARG A NH2 1 ATOM 552 N N . PHE A 1 74 ? 51.671 34.780 19.289 1.00 14.27 ? 74 PHE A N 1 ATOM 553 C CA . PHE A 1 74 ? 50.486 35.617 19.146 1.00 14.11 ? 74 PHE A CA 1 ATOM 554 C C . PHE A 1 74 ? 50.123 36.164 20.523 1.00 14.11 ? 74 PHE A C 1 ATOM 555 O O . PHE A 1 74 ? 50.120 35.416 21.512 1.00 14.34 ? 74 PHE A O 1 ATOM 556 C CB . PHE A 1 74 ? 49.322 34.805 18.594 1.00 12.97 ? 74 PHE A CB 1 ATOM 557 C CG . PHE A 1 74 ? 49.342 34.623 17.103 1.00 13.63 ? 74 PHE A CG 1 ATOM 558 C CD1 . PHE A 1 74 ? 50.482 34.167 16.436 1.00 14.05 ? 74 PHE A CD1 1 ATOM 559 C CD2 . PHE A 1 74 ? 48.184 34.859 16.363 1.00 11.96 ? 74 PHE A CD2 1 ATOM 560 C CE1 . PHE A 1 74 ? 50.481 33.988 15.053 1.00 13.63 ? 74 PHE A CE1 1 ATOM 561 C CE2 . PHE A 1 74 ? 48.164 34.679 14.969 1.00 13.89 ? 74 PHE A CE2 1 ATOM 562 C CZ . PHE A 1 74 ? 49.316 34.234 14.316 1.00 13.61 ? 74 PHE A CZ 1 ATOM 563 N N . PRO A 1 75 ? 49.848 37.469 20.606 1.00 14.34 ? 75 PRO A N 1 ATOM 564 C CA . PRO A 1 75 ? 49.663 38.081 21.926 1.00 14.47 ? 75 PRO A CA 1 ATOM 565 C C . PRO A 1 75 ? 48.360 37.700 22.612 1.00 14.63 ? 75 PRO A C 1 ATOM 566 O O . PRO A 1 75 ? 48.294 37.690 23.844 1.00 14.64 ? 75 PRO A O 1 ATOM 567 C CB . PRO A 1 75 ? 49.676 39.581 21.616 1.00 14.25 ? 75 PRO A CB 1 ATOM 568 C CG . PRO A 1 75 ? 49.236 39.674 20.172 1.00 14.80 ? 75 PRO A CG 1 ATOM 569 C CD . PRO A 1 75 ? 49.783 38.461 19.512 1.00 14.04 ? 75 PRO A CD 1 ATOM 570 N N . TYR A 1 76 ? 47.323 37.402 21.841 1.00 14.16 ? 76 TYR A N 1 ATOM 571 C CA . TYR A 1 76 ? 46.034 37.177 22.472 1.00 14.34 ? 76 TYR A CA 1 ATOM 572 C C . TYR A 1 76 ? 45.581 35.751 22.338 1.00 14.26 ? 76 TYR A C 1 ATOM 573 O O . TYR A 1 76 ? 45.574 35.192 21.242 1.00 13.93 ? 76 TYR A O 1 ATOM 574 C CB . TYR A 1 76 ? 44.996 38.151 21.926 1.00 14.77 ? 76 TYR A CB 1 ATOM 575 C CG . TYR A 1 76 ? 45.427 39.577 22.133 1.00 15.65 ? 76 TYR A CG 1 ATOM 576 C CD1 . TYR A 1 76 ? 45.452 40.133 23.411 1.00 14.65 ? 76 TYR A CD1 1 ATOM 577 C CD2 . TYR A 1 76 ? 45.861 40.352 21.058 1.00 14.53 ? 76 TYR A CD2 1 ATOM 578 C CE1 . TYR A 1 76 ? 45.859 41.443 23.603 1.00 17.45 ? 76 TYR A CE1 1 ATOM 579 C CE2 . TYR A 1 76 ? 46.264 41.661 21.240 1.00 17.13 ? 76 TYR A CE2 1 ATOM 580 C CZ . TYR A 1 76 ? 46.258 42.198 22.512 1.00 16.35 ? 76 TYR A CZ 1 ATOM 581 O OH . TYR A 1 76 ? 46.670 43.492 22.691 1.00 18.55 ? 76 TYR A OH 1 ATOM 582 N N . VAL A 1 77 ? 45.220 35.176 23.479 1.00 14.10 ? 77 VAL A N 1 ATOM 583 C CA . VAL A 1 77 ? 44.731 33.817 23.557 1.00 14.10 ? 77 VAL A CA 1 ATOM 584 C C . VAL A 1 77 ? 43.357 33.775 24.227 1.00 13.73 ? 77 VAL A C 1 ATOM 585 O O . VAL A 1 77 ? 43.074 34.526 25.163 1.00 14.11 ? 77 VAL A O 1 ATOM 586 C CB . VAL A 1 77 ? 45.761 32.895 24.269 1.00 14.24 ? 77 VAL A CB 1 ATOM 587 C CG1 . VAL A 1 77 ? 45.090 31.580 24.763 1.00 15.21 ? 77 VAL A CG1 1 ATOM 588 C CG2 . VAL A 1 77 ? 46.932 32.592 23.320 1.00 14.50 ? 77 VAL A CG2 1 ATOM 589 N N . ALA A 1 78 ? 42.484 32.931 23.696 1.00 12.94 ? 78 ALA A N 1 ATOM 590 C CA . ALA A 1 78 ? 41.232 32.610 24.346 1.00 12.57 ? 78 ALA A CA 1 ATOM 591 C C . ALA A 1 78 ? 41.019 31.106 24.258 1.00 12.52 ? 78 ALA A C 1 ATOM 592 O O . ALA A 1 78 ? 41.667 30.404 23.449 1.00 12.74 ? 78 ALA A O 1 ATOM 593 C CB . ALA A 1 78 ? 40.078 33.341 23.671 1.00 11.90 ? 78 ALA A CB 1 ATOM 594 N N . LEU A 1 79 ? 40.131 30.605 25.108 1.00 11.72 ? 79 LEU A N 1 ATOM 595 C CA . LEU A 1 79 ? 39.639 29.236 24.970 1.00 12.01 ? 79 LEU A CA 1 ATOM 596 C C . LEU A 1 79 ? 38.344 29.288 24.198 1.00 12.30 ? 79 LEU A C 1 ATOM 597 O O . LEU A 1 79 ? 37.538 30.208 24.373 1.00 13.45 ? 79 LEU A O 1 ATOM 598 C CB . LEU A 1 79 ? 39.436 28.572 26.334 1.00 11.76 ? 79 LEU A CB 1 ATOM 599 C CG . LEU A 1 79 ? 40.759 28.246 27.032 1.00 12.51 ? 79 LEU A CG 1 ATOM 600 C CD1 . LEU A 1 79 ? 40.500 27.823 28.449 1.00 14.10 ? 79 LEU A CD1 1 ATOM 601 C CD2 . LEU A 1 79 ? 41.493 27.148 26.257 1.00 14.02 ? 79 LEU A CD2 1 ATOM 602 N N . SER A 1 80 ? 38.173 28.312 23.315 1.00 12.17 ? 80 SER A N 1 ATOM 603 C CA . SER A 1 80 ? 37.033 28.251 22.428 1.00 12.29 ? 80 SER A CA 1 ATOM 604 C C . SER A 1 80 ? 36.234 26.990 22.703 1.00 11.98 ? 80 SER A C 1 ATOM 605 O O . SER A 1 80 ? 36.784 25.888 22.688 1.00 12.09 ? 80 SER A O 1 ATOM 606 C CB . SER A 1 80 ? 37.532 28.237 20.976 1.00 11.75 ? 80 SER A CB 1 ATOM 607 O OG . SER A 1 80 ? 36.456 28.027 20.092 1.00 14.98 ? 80 SER A OG 1 ATOM 608 N N . LYS A 1 81 ? 34.940 27.150 22.948 1.00 11.72 ? 81 LYS A N 1 ATOM 609 C CA . LYS A 1 81 ? 34.079 26.002 23.247 1.00 11.46 ? 81 LYS A CA 1 ATOM 610 C C . LYS A 1 81 ? 33.521 25.430 21.949 1.00 11.25 ? 81 LYS A C 1 ATOM 611 O O . LYS A 1 81 ? 32.827 26.128 21.205 1.00 11.45 ? 81 LYS A O 1 ATOM 612 C CB . LYS A 1 81 ? 32.971 26.408 24.207 1.00 11.09 ? 81 LYS A CB 1 ATOM 613 C CG . LYS A 1 81 ? 33.532 27.011 25.521 1.00 11.63 ? 81 LYS A CG 1 ATOM 614 C CD . LYS A 1 81 ? 32.425 27.146 26.565 1.00 13.63 ? 81 LYS A CD 1 ATOM 615 C CE . LYS A 1 81 ? 31.355 28.141 26.159 1.00 15.27 ? 81 LYS A CE 1 ATOM 616 N NZ . LYS A 1 81 ? 30.297 28.066 27.213 1.00 17.07 ? 81 LYS A NZ 1 ATOM 617 N N . THR A 1 82 ? 33.831 24.167 21.679 1.00 10.60 ? 82 THR A N 1 ATOM 618 C CA . THR A 1 82 ? 33.672 23.592 20.322 1.00 11.03 ? 82 THR A CA 1 ATOM 619 C C . THR A 1 82 ? 32.414 22.742 20.117 1.00 11.73 ? 82 THR A C 1 ATOM 620 O O . THR A 1 82 ? 32.159 22.262 18.988 1.00 12.31 ? 82 THR A O 1 ATOM 621 C CB . THR A 1 82 ? 34.858 22.686 19.983 1.00 10.56 ? 82 THR A CB 1 ATOM 622 O OG1 . THR A 1 82 ? 34.862 21.597 20.916 1.00 9.97 ? 82 THR A OG1 1 ATOM 623 C CG2 . THR A 1 82 ? 36.199 23.467 20.082 1.00 9.77 ? 82 THR A CG2 1 ATOM 624 N N . TYR A 1 83 ? 31.656 22.516 21.185 1.00 11.51 ? 83 TYR A N 1 ATOM 625 C CA . TYR A 1 83 ? 30.467 21.662 21.093 1.00 12.35 ? 83 TYR A CA 1 ATOM 626 C C . TYR A 1 83 ? 29.598 22.066 19.907 1.00 12.36 ? 83 TYR A C 1 ATOM 627 O O . TYR A 1 83 ? 29.427 23.261 19.606 1.00 12.92 ? 83 TYR A O 1 ATOM 628 C CB . TYR A 1 83 ? 29.638 21.666 22.392 1.00 12.62 ? 83 TYR A CB 1 ATOM 629 C CG . TYR A 1 83 ? 28.939 22.975 22.724 1.00 13.66 ? 83 TYR A CG 1 ATOM 630 C CD1 . TYR A 1 83 ? 29.588 23.958 23.473 1.00 12.02 ? 83 TYR A CD1 1 ATOM 631 C CD2 . TYR A 1 83 ? 27.629 23.231 22.290 1.00 12.87 ? 83 TYR A CD2 1 ATOM 632 C CE1 . TYR A 1 83 ? 28.959 25.157 23.794 1.00 13.08 ? 83 TYR A CE1 1 ATOM 633 C CE2 . TYR A 1 83 ? 26.998 24.433 22.596 1.00 13.93 ? 83 TYR A CE2 1 ATOM 634 C CZ . TYR A 1 83 ? 27.669 25.386 23.355 1.00 13.27 ? 83 TYR A CZ 1 ATOM 635 O OH . TYR A 1 83 ? 27.054 26.572 23.663 1.00 13.44 ? 83 TYR A OH 1 ATOM 636 N N . ASN A 1 84 ? 29.073 21.070 19.210 1.00 12.25 ? 84 ASN A N 1 ATOM 637 C CA . ASN A 1 84 ? 28.062 21.339 18.206 1.00 12.72 ? 84 ASN A CA 1 ATOM 638 C C . ASN A 1 84 ? 26.735 21.419 18.922 1.00 13.14 ? 84 ASN A C 1 ATOM 639 O O . ASN A 1 84 ? 26.622 21.016 20.080 1.00 13.43 ? 84 ASN A O 1 ATOM 640 C CB . ASN A 1 84 ? 28.019 20.226 17.152 1.00 11.91 ? 84 ASN A CB 1 ATOM 641 C CG . ASN A 1 84 ? 29.248 20.200 16.266 1.00 13.07 ? 84 ASN A CG 1 ATOM 642 O OD1 . ASN A 1 84 ? 29.654 19.127 15.833 1.00 13.84 ? 84 ASN A OD1 1 ATOM 643 N ND2 . ASN A 1 84 ? 29.835 21.369 15.969 1.00 12.22 ? 84 ASN A ND2 1 ATOM 644 N N . VAL A 1 85 ? 25.712 21.925 18.239 1.00 13.13 ? 85 VAL A N 1 ATOM 645 C CA . VAL A 1 85 ? 24.412 22.059 18.884 1.00 13.13 ? 85 VAL A CA 1 ATOM 646 C C . VAL A 1 85 ? 23.920 20.676 19.373 1.00 13.63 ? 85 VAL A C 1 ATOM 647 O O . VAL A 1 85 ? 23.417 20.553 20.483 1.00 13.97 ? 85 VAL A O 1 ATOM 648 C CB . VAL A 1 85 ? 23.392 22.772 17.956 1.00 13.23 ? 85 VAL A CB 1 ATOM 649 C CG1 . VAL A 1 85 ? 21.983 22.780 18.579 1.00 12.58 ? 85 VAL A CG1 1 ATOM 650 C CG2 . VAL A 1 85 ? 23.854 24.212 17.662 1.00 12.57 ? 85 VAL A CG2 1 ATOM 651 N N . ASP A 1 86 ? 24.117 19.642 18.553 1.00 13.26 ? 86 ASP A N 1 ATOM 652 C CA . ASP A 1 86 ? 23.594 18.303 18.839 1.00 14.09 ? 86 ASP A CA 1 ATOM 653 C C . ASP A 1 86 ? 24.578 17.303 19.481 1.00 14.50 ? 86 ASP A C 1 ATOM 654 O O . ASP A 1 86 ? 24.149 16.248 19.963 1.00 14.22 ? 86 ASP A O 1 ATOM 655 C CB . ASP A 1 86 ? 22.975 17.696 17.562 1.00 13.43 ? 86 ASP A CB 1 ATOM 656 C CG . ASP A 1 86 ? 24.004 17.456 16.467 1.00 14.65 ? 86 ASP A CG 1 ATOM 657 O OD1 . ASP A 1 86 ? 25.037 18.174 16.432 1.00 14.71 ? 86 ASP A OD1 1 ATOM 658 O OD2 . ASP A 1 86 ? 23.770 16.548 15.636 1.00 15.87 ? 86 ASP A OD2 1 ATOM 659 N N . LYS A 1 87 ? 25.876 17.623 19.492 1.00 14.26 ? 87 LYS A N 1 ATOM 660 C CA . LYS A 1 87 ? 26.905 16.701 20.003 1.00 15.06 ? 87 LYS A CA 1 ATOM 661 C C . LYS A 1 87 ? 27.961 17.475 20.783 1.00 14.33 ? 87 LYS A C 1 ATOM 662 O O . LYS A 1 87 ? 28.402 18.528 20.329 1.00 14.28 ? 87 LYS A O 1 ATOM 663 C CB . LYS A 1 87 ? 27.542 15.856 18.863 1.00 14.81 ? 87 LYS A CB 1 ATOM 664 C CG . LYS A 1 87 ? 26.525 14.890 18.195 1.00 17.11 ? 87 LYS A CG 1 ATOM 665 C CD . LYS A 1 87 ? 27.108 13.691 17.500 1.00 16.73 ? 87 LYS A CD 1 ATOM 666 C CE . LYS A 1 87 ? 26.018 12.947 16.720 1.00 17.34 ? 87 LYS A CE 1 ATOM 667 N NZ . LYS A 1 87 ? 26.596 11.772 15.972 1.00 21.58 ? 87 LYS A NZ 1 ATOM 668 N N . HIS A 1 88 ? 28.352 16.956 21.954 1.00 14.57 ? 88 HIS A N 1 ATOM 669 C CA . HIS A 1 88 ? 29.355 17.596 22.810 1.00 15.12 ? 88 HIS A CA 1 ATOM 670 C C . HIS A 1 88 ? 30.721 17.511 22.159 1.00 14.67 ? 88 HIS A C 1 ATOM 671 O O . HIS A 1 88 ? 31.532 18.430 22.307 1.00 14.61 ? 88 HIS A O 1 ATOM 672 C CB . HIS A 1 88 ? 29.469 16.891 24.168 1.00 15.63 ? 88 HIS A CB 1 ATOM 673 C CG . HIS A 1 88 ? 28.319 17.119 25.088 1.00 17.84 ? 88 HIS A CG 1 ATOM 674 N ND1 . HIS A 1 88 ? 27.988 16.230 26.086 1.00 20.94 ? 88 HIS A ND1 1 ATOM 675 C CD2 . HIS A 1 88 ? 27.438 18.142 25.185 1.00 20.49 ? 88 HIS A CD2 1 ATOM 676 C CE1 . HIS A 1 88 ? 26.944 16.690 26.751 1.00 21.48 ? 88 HIS A CE1 1 ATOM 677 N NE2 . HIS A 1 88 ? 26.594 17.852 26.227 1.00 21.44 ? 88 HIS A NE2 1 ATOM 678 N N . VAL A 1 89 ? 30.984 16.380 21.487 1.00 13.57 ? 89 VAL A N 1 ATOM 679 C CA . VAL A 1 89 ? 32.226 16.206 20.754 1.00 13.10 ? 89 VAL A CA 1 ATOM 680 C C . VAL A 1 89 ? 31.904 16.383 19.270 1.00 13.12 ? 89 VAL A C 1 ATOM 681 O O . VAL A 1 89 ? 31.157 15.588 18.692 1.00 13.33 ? 89 VAL A O 1 ATOM 682 C CB . VAL A 1 89 ? 32.875 14.847 21.020 1.00 12.98 ? 89 VAL A CB 1 ATOM 683 C CG1 . VAL A 1 89 ? 34.161 14.738 20.221 1.00 12.23 ? 89 VAL A CG1 1 ATOM 684 C CG2 . VAL A 1 89 ? 33.150 14.678 22.538 1.00 12.93 ? 89 VAL A CG2 1 ATOM 685 N N . PRO A 1 90 ? 32.431 17.456 18.665 1.00 12.50 ? 90 PRO A N 1 ATOM 686 C CA . PRO A 1 90 ? 31.937 17.920 17.369 1.00 12.42 ? 90 PRO A CA 1 ATOM 687 C C . PRO A 1 90 ? 32.641 17.290 16.181 1.00 12.40 ? 90 PRO A C 1 ATOM 688 O O . PRO A 1 90 ? 33.611 16.551 16.352 1.00 12.49 ? 90 PRO A O 1 ATOM 689 C CB . PRO A 1 90 ? 32.272 19.418 17.419 1.00 11.88 ? 90 PRO A CB 1 ATOM 690 C CG . PRO A 1 90 ? 33.597 19.433 18.158 1.00 12.57 ? 90 PRO A CG 1 ATOM 691 C CD . PRO A 1 90 ? 33.485 18.350 19.208 1.00 12.84 ? 90 PRO A CD 1 ATOM 692 N N . ASP A 1 91 ? 32.153 17.593 14.980 1.00 12.75 ? 91 ASP A N 1 ATOM 693 C CA . ASP A 1 91 ? 32.877 17.257 13.759 1.00 12.74 ? 91 ASP A CA 1 ATOM 694 C C . ASP A 1 91 ? 33.376 18.534 13.112 1.00 12.82 ? 91 ASP A C 1 ATOM 695 O O . ASP A 1 91 ? 33.139 19.639 13.606 1.00 13.08 ? 91 ASP A O 1 ATOM 696 C CB . ASP A 1 91 ? 31.996 16.477 12.775 1.00 13.01 ? 91 ASP A CB 1 ATOM 697 C CG . ASP A 1 91 ? 31.191 17.385 11.859 1.00 14.60 ? 91 ASP A CG 1 ATOM 698 O OD1 . ASP A 1 91 ? 31.260 17.158 10.633 1.00 14.28 ? 91 ASP A OD1 1 ATOM 699 O OD2 . ASP A 1 91 ? 30.519 18.336 12.340 1.00 15.87 ? 91 ASP A OD2 1 HETATM 700 N N . SEP A 1 92 ? 34.060 18.376 11.990 1.00 13.04 ? 92 SEP A N 1 HETATM 701 C CA . SEP A 1 92 ? 34.663 19.509 11.307 1.00 12.56 ? 92 SEP A CA 1 HETATM 702 C CB . SEP A 1 92 ? 35.655 19.008 10.277 1.00 11.75 ? 92 SEP A CB 1 HETATM 703 O OG . SEP A 1 92 ? 36.716 18.390 10.948 1.00 13.62 ? 92 SEP A OG 1 HETATM 704 C C . SEP A 1 92 ? 33.662 20.374 10.585 1.00 12.10 ? 92 SEP A C 1 HETATM 705 O O . SEP A 1 92 ? 33.911 21.559 10.394 1.00 12.51 ? 92 SEP A O 1 HETATM 706 P P . SEP A 1 92 ? 36.730 16.599 10.733 1.00 13.42 ? 92 SEP A P 1 HETATM 707 O O1P . SEP A 1 92 ? 35.446 16.010 11.243 1.00 14.04 ? 92 SEP A O1P 1 HETATM 708 O O2P . SEP A 1 92 ? 37.007 16.321 9.282 1.00 13.64 ? 92 SEP A O2P 1 HETATM 709 O O3P . SEP A 1 92 ? 37.910 16.380 11.663 1.00 12.16 ? 92 SEP A O3P 1 ATOM 710 N N . GLY A 1 93 ? 32.559 19.780 10.138 1.00 12.20 ? 93 GLY A N 1 ATOM 711 C CA . GLY A 1 93 ? 31.589 20.533 9.337 1.00 12.09 ? 93 GLY A CA 1 ATOM 712 C C . GLY A 1 93 ? 30.893 21.565 10.206 1.00 12.39 ? 93 GLY A C 1 ATOM 713 O O . GLY A 1 93 ? 30.869 22.748 9.877 1.00 11.49 ? 93 GLY A O 1 ATOM 714 N N . ALA A 1 94 ? 30.328 21.110 11.321 1.00 12.03 ? 94 ALA A N 1 ATOM 715 C CA . ALA A 1 94 ? 29.512 21.988 12.161 1.00 12.50 ? 94 ALA A CA 1 ATOM 716 C C . ALA A 1 94 ? 30.379 22.983 12.950 1.00 11.81 ? 94 ALA A C 1 ATOM 717 O O . ALA A 1 94 ? 29.950 24.101 13.247 1.00 12.10 ? 94 ALA A O 1 ATOM 718 C CB . ALA A 1 94 ? 28.613 21.157 13.074 1.00 13.05 ? 94 ALA A CB 1 ATOM 719 N N . THR A 1 95 ? 31.609 22.596 13.277 1.00 11.68 ? 95 THR A N 1 ATOM 720 C CA . THR A 1 95 ? 32.534 23.572 13.851 1.00 11.06 ? 95 THR A CA 1 ATOM 721 C C . THR A 1 95 ? 32.879 24.627 12.796 1.00 11.15 ? 95 THR A C 1 ATOM 722 O O . THR A 1 95 ? 32.921 25.800 13.115 1.00 11.90 ? 95 THR A O 1 ATOM 723 C CB . THR A 1 95 ? 33.786 22.946 14.441 1.00 11.16 ? 95 THR A CB 1 ATOM 724 O OG1 . THR A 1 95 ? 34.423 22.114 13.456 1.00 11.70 ? 95 THR A OG1 1 ATOM 725 C CG2 . THR A 1 95 ? 33.415 22.099 15.684 1.00 9.83 ? 95 THR A CG2 1 ATOM 726 N N . ALA A 1 96 ? 33.082 24.226 11.543 1.00 11.45 ? 96 ALA A N 1 ATOM 727 C CA . ALA A 1 96 ? 33.373 25.216 10.478 1.00 11.61 ? 96 ALA A CA 1 ATOM 728 C C . ALA A 1 96 ? 32.248 26.241 10.410 1.00 11.92 ? 96 ALA A C 1 ATOM 729 O O . ALA A 1 96 ? 32.483 27.440 10.285 1.00 11.79 ? 96 ALA A O 1 ATOM 730 C CB . ALA A 1 96 ? 33.585 24.541 9.137 1.00 11.73 ? 96 ALA A CB 1 ATOM 731 N N . THR A 1 97 ? 31.011 25.783 10.543 1.00 12.09 ? 97 THR A N 1 ATOM 732 C CA . THR A 1 97 ? 29.901 26.726 10.556 1.00 12.47 ? 97 THR A CA 1 ATOM 733 C C . THR A 1 97 ? 30.125 27.759 11.668 1.00 12.45 ? 97 THR A C 1 ATOM 734 O O . THR A 1 97 ? 29.904 28.954 11.460 1.00 12.04 ? 97 THR A O 1 ATOM 735 C CB . THR A 1 97 ? 28.576 26.004 10.744 1.00 12.41 ? 97 THR A CB 1 ATOM 736 O OG1 . THR A 1 97 ? 28.511 24.955 9.780 1.00 13.32 ? 97 THR A OG1 1 ATOM 737 C CG2 . THR A 1 97 ? 27.388 26.951 10.551 1.00 12.40 ? 97 THR A CG2 1 ATOM 738 N N . ALA A 1 98 ? 30.587 27.291 12.829 1.00 12.21 ? 98 ALA A N 1 ATOM 739 C CA . ALA A 1 98 ? 30.783 28.161 13.974 1.00 12.17 ? 98 ALA A CA 1 ATOM 740 C C . ALA A 1 98 ? 31.899 29.173 13.691 1.00 12.53 ? 98 ALA A C 1 ATOM 741 O O . ALA A 1 98 ? 31.681 30.387 13.750 1.00 12.81 ? 98 ALA A O 1 ATOM 742 C CB . ALA A 1 98 ? 31.072 27.328 15.246 1.00 11.39 ? 98 ALA A CB 1 ATOM 743 N N . TYR A 1 99 ? 33.089 28.693 13.365 1.00 12.46 ? 99 TYR A N 1 ATOM 744 C CA . TYR A 1 99 ? 34.230 29.619 13.277 1.00 12.63 ? 99 TYR A CA 1 ATOM 745 C C . TYR A 1 99 ? 34.316 30.357 11.940 1.00 13.16 ? 99 TYR A C 1 ATOM 746 O O . TYR A 1 99 ? 35.068 31.325 11.829 1.00 13.70 ? 99 TYR A O 1 ATOM 747 C CB . TYR A 1 99 ? 35.568 28.943 13.655 1.00 12.13 ? 99 TYR A CB 1 ATOM 748 C CG . TYR A 1 99 ? 35.978 27.791 12.766 1.00 12.79 ? 99 TYR A CG 1 ATOM 749 C CD1 . TYR A 1 99 ? 36.614 28.027 11.541 1.00 12.95 ? 99 TYR A CD1 1 ATOM 750 C CD2 . TYR A 1 99 ? 35.774 26.475 13.158 1.00 11.18 ? 99 TYR A CD2 1 ATOM 751 C CE1 . TYR A 1 99 ? 37.007 26.995 10.718 1.00 12.56 ? 99 TYR A CE1 1 ATOM 752 C CE2 . TYR A 1 99 ? 36.167 25.412 12.323 1.00 12.55 ? 99 TYR A CE2 1 ATOM 753 C CZ . TYR A 1 99 ? 36.778 25.688 11.103 1.00 12.52 ? 99 TYR A CZ 1 ATOM 754 O OH . TYR A 1 99 ? 37.170 24.663 10.257 1.00 13.88 ? 99 TYR A OH 1 ATOM 755 N N . LEU A 1 100 ? 33.550 29.910 10.938 1.00 12.75 ? 100 LEU A N 1 ATOM 756 C CA . LEU A 1 100 ? 33.535 30.582 9.626 1.00 12.79 ? 100 LEU A CA 1 ATOM 757 C C . LEU A 1 100 ? 32.274 31.387 9.358 1.00 13.10 ? 100 LEU A C 1 ATOM 758 O O . LEU A 1 100 ? 32.332 32.382 8.636 1.00 14.01 ? 100 LEU A O 1 ATOM 759 C CB . LEU A 1 100 ? 33.762 29.584 8.477 1.00 12.73 ? 100 LEU A CB 1 ATOM 760 C CG . LEU A 1 100 ? 35.118 28.880 8.547 1.00 12.05 ? 100 LEU A CG 1 ATOM 761 C CD1 . LEU A 1 100 ? 35.228 27.750 7.511 1.00 12.08 ? 100 LEU A CD1 1 ATOM 762 C CD2 . LEU A 1 100 ? 36.285 29.880 8.414 1.00 13.72 ? 100 LEU A CD2 1 ATOM 763 N N . CYS A 1 101 ? 31.147 30.964 9.932 1.00 12.43 ? 101 CYS A N 1 ATOM 764 C CA . CYS A 1 101 ? 29.873 31.630 9.690 1.00 12.75 ? 101 CYS A CA 1 ATOM 765 C C . CYS A 1 101 ? 29.301 32.265 10.944 1.00 12.84 ? 101 CYS A C 1 ATOM 766 O O . CYS A 1 101 ? 28.382 33.066 10.846 1.00 13.94 ? 101 CYS A O 1 ATOM 767 C CB . CYS A 1 101 ? 28.841 30.656 9.085 1.00 12.02 ? 101 CYS A CB 1 ATOM 768 S SG . CYS A 1 101 ? 29.423 29.765 7.638 1.00 14.22 ? 101 CYS A SG 1 ATOM 769 N N . GLY A 1 102 ? 29.831 31.902 12.112 1.00 12.63 ? 102 GLY A N 1 ATOM 770 C CA . GLY A 1 102 ? 29.484 32.565 13.384 1.00 12.61 ? 102 GLY A CA 1 ATOM 771 C C . GLY A 1 102 ? 28.205 32.050 14.002 1.00 12.35 ? 102 GLY A C 1 ATOM 772 O O . GLY A 1 102 ? 27.577 32.718 14.842 1.00 13.28 ? 102 GLY A O 1 ATOM 773 N N . VAL A 1 103 ? 27.827 30.848 13.591 1.00 12.25 ? 103 VAL A N 1 ATOM 774 C CA . VAL A 1 103 ? 26.600 30.207 14.045 1.00 12.74 ? 103 VAL A CA 1 ATOM 775 C C . VAL A 1 103 ? 26.929 28.744 14.300 1.00 12.69 ? 103 VAL A C 1 ATOM 776 O O . VAL A 1 103 ? 27.595 28.125 13.485 1.00 11.98 ? 103 VAL A O 1 ATOM 777 C CB . VAL A 1 103 ? 25.517 30.300 12.956 1.00 12.94 ? 103 VAL A CB 1 ATOM 778 C CG1 . VAL A 1 103 ? 24.304 29.470 13.335 1.00 13.42 ? 103 VAL A CG1 1 ATOM 779 C CG2 . VAL A 1 103 ? 25.121 31.768 12.706 1.00 13.68 ? 103 VAL A CG2 1 ATOM 780 N N . LYS A 1 104 ? 26.474 28.187 15.419 1.00 12.50 ? 104 LYS A N 1 ATOM 781 C CA . LYS A 1 104 ? 26.699 26.751 15.656 1.00 13.01 ? 104 LYS A CA 1 ATOM 782 C C . LYS A 1 104 ? 25.719 25.899 14.866 1.00 13.43 ? 104 LYS A C 1 ATOM 783 O O . LYS A 1 104 ? 24.603 26.322 14.594 1.00 13.59 ? 104 LYS A O 1 ATOM 784 C CB . LYS A 1 104 ? 26.666 26.384 17.142 1.00 12.65 ? 104 LYS A CB 1 ATOM 785 C CG . LYS A 1 104 ? 27.827 27.027 17.913 1.00 12.73 ? 104 LYS A CG 1 ATOM 786 C CD . LYS A 1 104 ? 28.280 26.142 19.068 1.00 12.26 ? 104 LYS A CD 1 ATOM 787 C CE . LYS A 1 104 ? 29.651 26.599 19.575 1.00 11.62 ? 104 LYS A CE 1 ATOM 788 N NZ . LYS A 1 104 ? 30.117 25.730 20.697 1.00 12.34 ? 104 LYS A NZ 1 ATOM 789 N N . GLY A 1 105 ? 26.153 24.702 14.485 1.00 13.50 ? 105 GLY A N 1 ATOM 790 C CA . GLY A 1 105 ? 25.305 23.832 13.689 1.00 13.54 ? 105 GLY A CA 1 ATOM 791 C C . GLY A 1 105 ? 25.311 22.421 14.220 1.00 13.88 ? 105 GLY A C 1 ATOM 792 O O . GLY A 1 105 ? 25.933 22.114 15.255 1.00 12.98 ? 105 GLY A O 1 ATOM 793 N N . ASN A 1 106 ? 24.620 21.557 13.489 1.00 13.74 ? 106 ASN A N 1 ATOM 794 C CA . ASN A 1 106 ? 24.569 20.143 13.811 1.00 13.69 ? 106 ASN A CA 1 ATOM 795 C C . ASN A 1 106 ? 25.657 19.360 13.115 1.00 13.72 ? 106 ASN A C 1 ATOM 796 O O . ASN A 1 106 ? 25.959 19.604 11.940 1.00 13.33 ? 106 ASN A O 1 ATOM 797 C CB . ASN A 1 106 ? 23.199 19.569 13.476 1.00 13.81 ? 106 ASN A CB 1 ATOM 798 C CG . ASN A 1 106 ? 22.095 20.174 14.332 1.00 14.20 ? 106 ASN A CG 1 ATOM 799 O OD1 . ASN A 1 106 ? 22.281 20.407 15.521 1.00 13.74 ? 106 ASN A OD1 1 ATOM 800 N ND2 . ASN A 1 106 ? 20.941 20.435 13.722 1.00 12.56 ? 106 ASN A ND2 1 ATOM 801 N N . PHE A 1 107 ? 26.246 18.444 13.886 1.00 13.32 ? 107 PHE A N 1 ATOM 802 C CA . PHE A 1 107 ? 27.249 17.470 13.476 1.00 13.77 ? 107 PHE A CA 1 ATOM 803 C C . PHE A 1 107 ? 27.065 17.049 12.011 1.00 14.31 ? 107 PHE A C 1 ATOM 804 O O . PHE A 1 107 ? 25.973 16.647 11.601 1.00 14.46 ? 107 PHE A O 1 ATOM 805 C CB . PHE A 1 107 ? 27.069 16.278 14.410 1.00 13.47 ? 107 PHE A CB 1 ATOM 806 C CG . PHE A 1 107 ? 28.229 15.344 14.494 1.00 14.56 ? 107 PHE A CG 1 ATOM 807 C CD1 . PHE A 1 107 ? 28.204 14.129 13.805 1.00 13.95 ? 107 PHE A CD1 1 ATOM 808 C CD2 . PHE A 1 107 ? 29.294 15.612 15.358 1.00 13.88 ? 107 PHE A CD2 1 ATOM 809 C CE1 . PHE A 1 107 ? 29.267 13.218 13.935 1.00 14.50 ? 107 PHE A CE1 1 ATOM 810 C CE2 . PHE A 1 107 ? 30.348 14.711 15.499 1.00 13.61 ? 107 PHE A CE2 1 ATOM 811 C CZ . PHE A 1 107 ? 30.332 13.519 14.798 1.00 14.57 ? 107 PHE A CZ 1 ATOM 812 N N . GLN A 1 108 ? 28.129 17.235 11.229 1.00 14.76 ? 108 GLN A N 1 ATOM 813 C CA . GLN A 1 108 ? 28.256 16.748 9.855 1.00 14.72 ? 108 GLN A CA 1 ATOM 814 C C . GLN A 1 108 ? 27.517 17.562 8.811 1.00 14.90 ? 108 GLN A C 1 ATOM 815 O O . GLN A 1 108 ? 27.505 17.179 7.650 1.00 14.16 ? 108 GLN A O 1 ATOM 816 C CB . GLN A 1 108 ? 27.905 15.269 9.731 1.00 15.58 ? 108 GLN A CB 1 ATOM 817 C CG . GLN A 1 108 ? 28.943 14.343 10.303 1.00 19.26 ? 108 GLN A CG 1 ATOM 818 C CD . GLN A 1 108 ? 28.589 12.901 10.039 1.00 24.96 ? 108 GLN A CD 1 ATOM 819 O OE1 . GLN A 1 108 ? 27.549 12.412 10.477 1.00 27.18 ? 108 GLN A OE1 1 ATOM 820 N NE2 . GLN A 1 108 ? 29.434 12.224 9.297 1.00 29.06 ? 108 GLN A NE2 1 ATOM 821 N N . THR A 1 109 ? 26.907 18.671 9.229 1.00 13.87 ? 109 THR A N 1 ATOM 822 C CA . THR A 1 109 ? 26.417 19.672 8.291 1.00 14.02 ? 109 THR A CA 1 ATOM 823 C C . THR A 1 109 ? 27.421 20.820 8.185 1.00 13.86 ? 109 THR A C 1 ATOM 824 O O . THR A 1 109 ? 28.290 20.980 9.051 1.00 14.02 ? 109 THR A O 1 ATOM 825 C CB . THR A 1 109 ? 25.062 20.238 8.738 1.00 13.97 ? 109 THR A CB 1 ATOM 826 O OG1 . THR A 1 109 ? 25.235 21.035 9.918 1.00 13.00 ? 109 THR A OG1 1 ATOM 827 C CG2 . THR A 1 109 ? 24.079 19.091 9.011 1.00 12.91 ? 109 THR A CG2 1 ATOM 828 N N . ILE A 1 110 ? 27.286 21.628 7.133 1.00 13.67 ? 110 ILE A N 1 ATOM 829 C CA . ILE A 1 110 ? 28.222 22.712 6.870 1.00 13.07 ? 110 ILE A CA 1 ATOM 830 C C . ILE A 1 110 ? 27.466 23.938 6.415 1.00 13.01 ? 110 ILE A C 1 ATOM 831 O O . ILE A 1 110 ? 26.662 23.854 5.494 1.00 12.86 ? 110 ILE A O 1 ATOM 832 C CB . ILE A 1 110 ? 29.207 22.357 5.727 1.00 12.71 ? 110 ILE A CB 1 ATOM 833 C CG1 . ILE A 1 110 ? 29.920 21.012 5.990 1.00 13.09 ? 110 ILE A CG1 1 ATOM 834 C CG2 . ILE A 1 110 ? 30.212 23.489 5.538 1.00 13.40 ? 110 ILE A CG2 1 ATOM 835 C CD1 . ILE A 1 110 ? 30.768 20.560 4.782 1.00 12.44 ? 110 ILE A CD1 1 ATOM 836 N N . GLY A 1 111 ? 27.730 25.074 7.050 1.00 13.18 ? 111 GLY A N 1 ATOM 837 C CA . GLY A 1 111 ? 27.202 26.348 6.587 1.00 13.26 ? 111 GLY A CA 1 ATOM 838 C C . GLY A 1 111 ? 25.706 26.449 6.780 1.00 14.14 ? 111 GLY A C 1 ATOM 839 O O . GLY A 1 111 ? 25.045 27.204 6.065 1.00 14.79 ? 111 GLY A O 1 ATOM 840 N N . LEU A 1 112 ? 25.182 25.684 7.746 1.00 14.19 ? 112 LEU A N 1 ATOM 841 C CA . LEU A 1 112 ? 23.752 25.656 8.038 1.00 13.91 ? 112 LEU A CA 1 ATOM 842 C C . LEU A 1 112 ? 23.520 25.852 9.529 1.00 14.39 ? 112 LEU A C 1 ATOM 843 O O . LEU A 1 112 ? 24.275 25.339 10.362 1.00 14.42 ? 112 LEU A O 1 ATOM 844 C CB . LEU A 1 112 ? 23.101 24.331 7.596 1.00 14.18 ? 112 LEU A CB 1 ATOM 845 C CG . LEU A 1 112 ? 23.119 24.002 6.101 1.00 13.39 ? 112 LEU A CG 1 ATOM 846 C CD1 . LEU A 1 112 ? 22.546 22.622 5.921 1.00 13.94 ? 112 LEU A CD1 1 ATOM 847 C CD2 . LEU A 1 112 ? 22.332 25.036 5.283 1.00 13.39 ? 112 LEU A CD2 1 ATOM 848 N N . SER A 1 113 ? 22.479 26.596 9.869 1.00 14.28 ? 113 SER A N 1 ATOM 849 C CA . SER A 1 113 ? 22.054 26.676 11.256 1.00 14.55 ? 113 SER A CA 1 ATOM 850 C C . SER A 1 113 ? 21.615 25.278 11.715 1.00 14.45 ? 113 SER A C 1 ATOM 851 O O . SER A 1 113 ? 21.414 24.349 10.895 1.00 14.20 ? 113 SER A O 1 ATOM 852 C CB . SER A 1 113 ? 20.886 27.651 11.412 1.00 14.27 ? 113 SER A CB 1 ATOM 853 O OG . SER A 1 113 ? 19.717 27.072 10.859 1.00 15.86 ? 113 SER A OG 1 ATOM 854 N N . ALA A 1 114 ? 21.430 25.147 13.020 1.00 14.30 ? 114 ALA A N 1 ATOM 855 C CA . ALA A 1 114 ? 21.031 23.876 13.602 1.00 14.61 ? 114 ALA A CA 1 ATOM 856 C C . ALA A 1 114 ? 19.544 23.562 13.420 1.00 14.79 ? 114 ALA A C 1 ATOM 857 O O . ALA A 1 114 ? 19.049 22.560 13.946 1.00 15.52 ? 114 ALA A O 1 ATOM 858 C CB . ALA A 1 114 ? 21.457 23.815 15.070 1.00 14.26 ? 114 ALA A CB 1 ATOM 859 N N . ALA A 1 115 ? 18.837 24.402 12.658 1.00 14.79 ? 115 ALA A N 1 ATOM 860 C CA . ALA A 1 115 ? 17.477 24.063 12.211 1.00 14.64 ? 115 ALA A CA 1 ATOM 861 C C . ALA A 1 115 ? 17.519 23.000 11.116 1.00 14.74 ? 115 ALA A C 1 ATOM 862 O O . ALA A 1 115 ? 16.569 22.237 10.945 1.00 13.81 ? 115 ALA A O 1 ATOM 863 C CB . ALA A 1 115 ? 16.726 25.289 11.740 1.00 15.03 ? 115 ALA A CB 1 ATOM 864 N N . ALA A 1 116 ? 18.640 22.932 10.402 1.00 14.49 ? 116 ALA A N 1 ATOM 865 C CA . ALA A 1 116 ? 18.842 21.895 9.402 1.00 14.59 ? 116 ALA A CA 1 ATOM 866 C C . ALA A 1 116 ? 19.121 20.563 10.077 1.00 14.68 ? 116 ALA A C 1 ATOM 867 O O . ALA A 1 116 ? 19.443 20.508 11.268 1.00 14.91 ? 116 ALA A O 1 ATOM 868 C CB . ALA A 1 116 ? 19.990 22.264 8.441 1.00 13.67 ? 116 ALA A CB 1 ATOM 869 N N . ARG A 1 117 ? 19.007 19.487 9.308 1.00 14.82 ? 117 ARG A N 1 ATOM 870 C CA . ARG A 1 117 ? 19.238 18.152 9.847 1.00 15.01 ? 117 ARG A CA 1 ATOM 871 C C . ARG A 1 117 ? 20.166 17.398 8.921 1.00 15.35 ? 117 ARG A C 1 ATOM 872 O O . ARG A 1 117 ? 19.983 17.421 7.700 1.00 15.88 ? 117 ARG A O 1 ATOM 873 C CB . ARG A 1 117 ? 17.902 17.390 9.975 1.00 15.55 ? 117 ARG A CB 1 ATOM 874 C CG . ARG A 1 117 ? 16.968 17.896 11.081 1.00 16.65 ? 117 ARG A CG 1 ATOM 875 C CD . ARG A 1 117 ? 17.559 17.685 12.466 1.00 18.84 ? 117 ARG A CD 1 ATOM 876 N NE . ARG A 1 117 ? 16.676 18.167 13.539 1.00 19.31 ? 117 ARG A NE 1 ATOM 877 C CZ . ARG A 1 117 ? 16.689 19.406 14.029 1.00 19.45 ? 117 ARG A CZ 1 ATOM 878 N NH1 . ARG A 1 117 ? 17.530 20.310 13.548 1.00 17.73 ? 117 ARG A NH1 1 ATOM 879 N NH2 . ARG A 1 117 ? 15.859 19.739 15.011 1.00 18.93 ? 117 ARG A NH2 1 ATOM 880 N N . PHE A 1 118 ? 21.156 16.734 9.508 1.00 15.33 ? 118 PHE A N 1 ATOM 881 C CA . PHE A 1 118 ? 22.099 15.923 8.759 1.00 15.73 ? 118 PHE A CA 1 ATOM 882 C C . PHE A 1 118 ? 21.406 14.996 7.764 1.00 15.96 ? 118 PHE A C 1 ATOM 883 O O . PHE A 1 118 ? 20.460 14.277 8.110 1.00 16.01 ? 118 PHE A O 1 ATOM 884 C CB . PHE A 1 118 ? 22.988 15.102 9.707 1.00 15.32 ? 118 PHE A CB 1 ATOM 885 C CG . PHE A 1 118 ? 23.854 14.111 8.991 1.00 15.77 ? 118 PHE A CG 1 ATOM 886 C CD1 . PHE A 1 118 ? 24.890 14.545 8.166 1.00 14.45 ? 118 PHE A CD1 1 ATOM 887 C CD2 . PHE A 1 118 ? 23.590 12.750 9.085 1.00 15.29 ? 118 PHE A CD2 1 ATOM 888 C CE1 . PHE A 1 118 ? 25.691 13.634 7.497 1.00 15.84 ? 118 PHE A CE1 1 ATOM 889 C CE2 . PHE A 1 118 ? 24.382 11.823 8.406 1.00 16.09 ? 118 PHE A CE2 1 ATOM 890 C CZ . PHE A 1 118 ? 25.425 12.264 7.610 1.00 15.80 ? 118 PHE A CZ 1 ATOM 891 N N . ASN A 1 119 ? 21.889 15.034 6.527 1.00 15.96 ? 119 ASN A N 1 ATOM 892 C CA . ASN A 1 119 ? 21.469 14.120 5.474 1.00 15.73 ? 119 ASN A CA 1 ATOM 893 C C . ASN A 1 119 ? 19.988 14.263 5.119 1.00 16.11 ? 119 ASN A C 1 ATOM 894 O O . ASN A 1 119 ? 19.397 13.342 4.570 1.00 16.24 ? 119 ASN A O 1 ATOM 895 C CB . ASN A 1 119 ? 21.806 12.658 5.858 1.00 15.82 ? 119 ASN A CB 1 ATOM 896 C CG . ASN A 1 119 ? 21.806 11.715 4.659 1.00 16.55 ? 119 ASN A CG 1 ATOM 897 O OD1 . ASN A 1 119 ? 22.193 12.096 3.561 1.00 17.49 ? 119 ASN A OD1 1 ATOM 898 N ND2 . ASN A 1 119 ? 21.392 10.460 4.881 1.00 18.01 ? 119 ASN A ND2 1 ATOM 899 N N . GLN A 1 120 ? 19.381 15.399 5.454 1.00 16.32 ? 120 GLN A N 1 ATOM 900 C CA . GLN A 1 120 ? 18.002 15.653 5.052 1.00 17.84 ? 120 GLN A CA 1 ATOM 901 C C . GLN A 1 120 ? 18.011 16.901 4.184 1.00 17.40 ? 120 GLN A C 1 ATOM 902 O O . GLN A 1 120 ? 17.899 18.024 4.685 1.00 16.83 ? 120 GLN A O 1 ATOM 903 C CB . GLN A 1 120 ? 17.087 15.832 6.270 1.00 17.16 ? 120 GLN A CB 1 ATOM 904 C CG . GLN A 1 120 ? 16.945 14.582 7.161 1.00 19.64 ? 120 GLN A CG 1 ATOM 905 C CD . GLN A 1 120 ? 15.937 14.809 8.274 1.00 21.27 ? 120 GLN A CD 1 ATOM 906 O OE1 . GLN A 1 120 ? 14.938 15.507 8.080 1.00 29.25 ? 120 GLN A OE1 1 ATOM 907 N NE2 . GLN A 1 120 ? 16.187 14.233 9.441 1.00 27.65 ? 120 GLN A NE2 1 ATOM 908 N N . CYS A 1 121 ? 18.162 16.692 2.881 1.00 18.00 ? 121 CYS A N 1 ATOM 909 C CA . CYS A 1 121 ? 18.257 17.798 1.925 1.00 17.98 ? 121 CYS A CA 1 ATOM 910 C C . CYS A 1 121 ? 17.112 18.806 2.067 1.00 17.91 ? 121 CYS A C 1 ATOM 911 O O . CYS A 1 121 ? 17.307 20.021 1.930 1.00 17.64 ? 121 CYS A O 1 ATOM 912 C CB . CYS A 1 121 ? 18.323 17.251 0.497 1.00 18.55 ? 121 CYS A CB 1 ATOM 913 S SG . CYS A 1 121 ? 18.258 18.515 -0.770 1.00 20.90 ? 121 CYS A SG 1 ATOM 914 N N . ASN A 1 122 ? 15.923 18.301 2.374 1.00 17.45 ? 122 ASN A N 1 ATOM 915 C CA . ASN A 1 122 ? 14.746 19.153 2.455 1.00 18.17 ? 122 ASN A CA 1 ATOM 916 C C . ASN A 1 122 ? 14.679 20.046 3.696 1.00 17.46 ? 122 ASN A C 1 ATOM 917 O O . ASN A 1 122 ? 13.699 20.763 3.886 1.00 17.88 ? 122 ASN A O 1 ATOM 918 C CB . ASN A 1 122 ? 13.471 18.314 2.327 1.00 18.69 ? 122 ASN A CB 1 ATOM 919 C CG . ASN A 1 122 ? 13.345 17.262 3.407 1.00 21.69 ? 122 ASN A CG 1 ATOM 920 O OD1 . ASN A 1 122 ? 14.199 17.124 4.293 1.00 22.00 ? 122 ASN A OD1 1 ATOM 921 N ND2 . ASN A 1 122 ? 12.258 16.512 3.334 1.00 25.49 ? 122 ASN A ND2 1 ATOM 922 N N . THR A 1 123 ? 15.719 20.014 4.530 1.00 16.73 ? 123 THR A N 1 ATOM 923 C CA . THR A 1 123 ? 15.807 20.914 5.681 1.00 16.13 ? 123 THR A CA 1 ATOM 924 C C . THR A 1 123 ? 16.844 22.017 5.442 1.00 16.09 ? 123 THR A C 1 ATOM 925 O O . THR A 1 123 ? 17.209 22.757 6.364 1.00 16.01 ? 123 THR A O 1 ATOM 926 C CB . THR A 1 123 ? 16.168 20.155 6.999 1.00 15.86 ? 123 THR A CB 1 ATOM 927 O OG1 . THR A 1 123 ? 17.508 19.681 6.926 1.00 14.89 ? 123 THR A OG1 1 ATOM 928 C CG2 . THR A 1 123 ? 15.229 18.979 7.253 1.00 16.16 ? 123 THR A CG2 1 ATOM 929 N N . THR A 1 124 ? 17.321 22.124 4.205 1.00 15.76 ? 124 THR A N 1 ATOM 930 C CA . THR A 1 124 ? 18.422 23.033 3.885 1.00 15.79 ? 124 THR A CA 1 ATOM 931 C C . THR A 1 124 ? 17.984 24.487 3.789 1.00 16.02 ? 124 THR A C 1 ATOM 932 O O . THR A 1 124 ? 18.539 25.358 4.445 1.00 15.81 ? 124 THR A O 1 ATOM 933 C CB . THR A 1 124 ? 19.081 22.653 2.562 1.00 15.54 ? 124 THR A CB 1 ATOM 934 O OG1 . THR A 1 124 ? 19.542 21.299 2.636 1.00 15.91 ? 124 THR A OG1 1 ATOM 935 C CG2 . THR A 1 124 ? 20.271 23.566 2.272 1.00 16.37 ? 124 THR A CG2 1 ATOM 936 N N . ARG A 1 125 ? 16.996 24.748 2.943 1.00 15.81 ? 125 ARG A N 1 ATOM 937 C CA . ARG A 1 125 ? 16.718 26.111 2.537 1.00 15.93 ? 125 ARG A CA 1 ATOM 938 C C . ARG A 1 125 ? 16.109 26.966 3.645 1.00 16.18 ? 125 ARG A C 1 ATOM 939 O O . ARG A 1 125 ? 15.225 26.519 4.378 1.00 16.09 ? 125 ARG A O 1 ATOM 940 C CB . ARG A 1 125 ? 15.865 26.107 1.282 1.00 15.78 ? 125 ARG A CB 1 ATOM 941 C CG . ARG A 1 125 ? 16.596 25.446 0.131 1.00 18.14 ? 125 ARG A CG 1 ATOM 942 C CD . ARG A 1 125 ? 16.531 26.306 -1.092 1.00 23.03 ? 125 ARG A CD 1 ATOM 943 N NE . ARG A 1 125 ? 16.992 25.614 -2.293 1.00 24.13 ? 125 ARG A NE 1 ATOM 944 C CZ . ARG A 1 125 ? 16.646 25.978 -3.523 1.00 25.64 ? 125 ARG A CZ 1 ATOM 945 N NH1 . ARG A 1 125 ? 17.097 25.309 -4.569 1.00 28.69 ? 125 ARG A NH1 1 ATOM 946 N NH2 . ARG A 1 125 ? 15.831 27.011 -3.706 1.00 27.06 ? 125 ARG A NH2 1 ATOM 947 N N . GLY A 1 126 ? 16.609 28.197 3.758 1.00 15.46 ? 126 GLY A N 1 ATOM 948 C CA . GLY A 1 126 ? 16.268 29.066 4.883 1.00 15.85 ? 126 GLY A CA 1 ATOM 949 C C . GLY A 1 126 ? 17.277 28.959 6.013 1.00 15.41 ? 126 GLY A C 1 ATOM 950 O O . GLY A 1 126 ? 17.329 29.823 6.872 1.00 16.30 ? 126 GLY A O 1 ATOM 951 N N . ASN A 1 127 ? 18.077 27.893 6.017 1.00 15.28 ? 127 ASN A N 1 ATOM 952 C CA . ASN A 1 127 ? 19.044 27.650 7.093 1.00 15.11 ? 127 ASN A CA 1 ATOM 953 C C . ASN A 1 127 ? 20.491 27.936 6.736 1.00 15.51 ? 127 ASN A C 1 ATOM 954 O O . ASN A 1 127 ? 21.382 27.717 7.548 1.00 15.56 ? 127 ASN A O 1 ATOM 955 C CB . ASN A 1 127 ? 18.893 26.223 7.615 1.00 15.34 ? 127 ASN A CB 1 ATOM 956 C CG . ASN A 1 127 ? 17.528 25.993 8.179 1.00 16.11 ? 127 ASN A CG 1 ATOM 957 O OD1 . ASN A 1 127 ? 17.013 26.861 8.878 1.00 18.96 ? 127 ASN A OD1 1 ATOM 958 N ND2 . ASN A 1 127 ? 16.898 24.869 7.836 1.00 16.41 ? 127 ASN A ND2 1 ATOM 959 N N . GLU A 1 128 ? 20.711 28.449 5.531 1.00 15.53 ? 128 GLU A N 1 ATOM 960 C CA . GLU A 1 128 ? 22.038 28.819 5.087 1.00 15.85 ? 128 GLU A CA 1 ATOM 961 C C . GLU A 1 128 ? 22.531 29.988 5.930 1.00 16.51 ? 128 GLU A C 1 ATOM 962 O O . GLU A 1 128 ? 21.804 30.963 6.155 1.00 16.29 ? 128 GLU A O 1 ATOM 963 C CB . GLU A 1 128 ? 22.046 29.180 3.595 1.00 16.48 ? 128 GLU A CB 1 ATOM 964 C CG . GLU A 1 128 ? 21.559 28.040 2.676 1.00 16.03 ? 128 GLU A CG 1 ATOM 965 C CD . GLU A 1 128 ? 20.061 28.109 2.364 1.00 18.60 ? 128 GLU A CD 1 ATOM 966 O OE1 . GLU A 1 128 ? 19.303 28.799 3.102 1.00 17.36 ? 128 GLU A OE1 1 ATOM 967 O OE2 . GLU A 1 128 ? 19.638 27.463 1.367 1.00 18.41 ? 128 GLU A OE2 1 ATOM 968 N N . VAL A 1 129 ? 23.749 29.858 6.441 1.00 15.74 ? 129 VAL A N 1 ATOM 969 C CA . VAL A 1 129 ? 24.370 30.956 7.165 1.00 16.27 ? 129 VAL A CA 1 ATOM 970 C C . VAL A 1 129 ? 25.627 31.315 6.391 1.00 16.25 ? 129 VAL A C 1 ATOM 971 O O . VAL A 1 129 ? 26.408 30.446 5.998 1.00 17.17 ? 129 VAL A O 1 ATOM 972 C CB . VAL A 1 129 ? 24.650 30.608 8.633 1.00 16.18 ? 129 VAL A CB 1 ATOM 973 C CG1 . VAL A 1 129 ? 23.335 30.462 9.411 1.00 17.05 ? 129 VAL A CG1 1 ATOM 974 C CG2 . VAL A 1 129 ? 25.473 29.327 8.732 1.00 16.88 ? 129 VAL A CG2 1 ATOM 975 N N . ILE A 1 130 ? 25.785 32.605 6.144 1.00 15.98 ? 130 ILE A N 1 ATOM 976 C CA . ILE A 1 130 ? 26.795 33.108 5.238 1.00 16.31 ? 130 ILE A CA 1 ATOM 977 C C . ILE A 1 130 ? 28.129 33.289 5.959 1.00 15.64 ? 130 ILE A C 1 ATOM 978 O O . ILE A 1 130 ? 28.182 33.862 7.043 1.00 15.46 ? 130 ILE A O 1 ATOM 979 C CB . ILE A 1 130 ? 26.320 34.443 4.598 1.00 16.87 ? 130 ILE A CB 1 ATOM 980 C CG1 . ILE A 1 130 ? 24.961 34.246 3.915 1.00 18.65 ? 130 ILE A CG1 1 ATOM 981 C CG2 . ILE A 1 130 ? 27.306 34.923 3.586 1.00 17.12 ? 130 ILE A CG2 1 ATOM 982 C CD1 . ILE A 1 130 ? 24.892 33.056 2.968 1.00 20.70 ? 130 ILE A CD1 1 ATOM 983 N N . SER A 1 131 ? 29.200 32.801 5.342 1.00 14.97 ? 131 SER A N 1 ATOM 984 C CA . SER A 1 131 ? 30.525 32.854 5.950 1.00 14.49 ? 131 SER A CA 1 ATOM 985 C C . SER A 1 131 ? 31.066 34.273 5.951 1.00 14.11 ? 131 SER A C 1 ATOM 986 O O . SER A 1 131 ? 30.644 35.120 5.162 1.00 13.60 ? 131 SER A O 1 ATOM 987 C CB . SER A 1 131 ? 31.504 31.928 5.229 1.00 13.80 ? 131 SER A CB 1 ATOM 988 O OG . SER A 1 131 ? 31.869 32.471 3.961 1.00 15.47 ? 131 SER A OG 1 ATOM 989 N N . VAL A 1 132 ? 32.016 34.514 6.836 1.00 13.72 ? 132 VAL A N 1 ATOM 990 C CA . VAL A 1 132 ? 32.741 35.778 6.850 1.00 14.28 ? 132 VAL A CA 1 ATOM 991 C C . VAL A 1 132 ? 33.474 35.956 5.535 1.00 13.98 ? 132 VAL A C 1 ATOM 992 O O . VAL A 1 132 ? 33.548 37.064 5.017 1.00 13.98 ? 132 VAL A O 1 ATOM 993 C CB . VAL A 1 132 ? 33.726 35.845 8.025 1.00 14.07 ? 132 VAL A CB 1 ATOM 994 C CG1 . VAL A 1 132 ? 34.508 37.194 8.019 1.00 15.07 ? 132 VAL A CG1 1 ATOM 995 C CG2 . VAL A 1 132 ? 32.956 35.704 9.340 1.00 14.69 ? 132 VAL A CG2 1 ATOM 996 N N . MET A 1 133 ? 34.000 34.861 4.985 1.00 13.88 ? 133 MET A N 1 ATOM 997 C CA . MET A 1 133 ? 34.692 34.931 3.706 1.00 14.11 ? 133 MET A CA 1 ATOM 998 C C . MET A 1 133 ? 33.759 35.434 2.604 1.00 14.28 ? 133 MET A C 1 ATOM 999 O O . MET A 1 133 ? 34.135 36.281 1.789 1.00 13.88 ? 133 MET A O 1 ATOM 1000 C CB . MET A 1 133 ? 35.272 33.575 3.309 1.00 13.55 ? 133 MET A CB 1 ATOM 1001 C CG . MET A 1 133 ? 36.157 33.691 2.066 1.00 13.52 ? 133 MET A CG 1 ATOM 1002 S SD . MET A 1 133 ? 36.935 32.162 1.556 1.00 14.84 ? 133 MET A SD 1 ATOM 1003 C CE . MET A 1 133 ? 35.651 31.524 0.474 1.00 11.95 ? 133 MET A CE 1 ATOM 1004 N N . ASN A 1 134 ? 32.537 34.919 2.587 1.00 14.56 ? 134 ASN A N 1 ATOM 1005 C CA . ASN A 1 134 ? 31.551 35.374 1.626 1.00 14.87 ? 134 ASN A CA 1 ATOM 1006 C C . ASN A 1 134 ? 31.291 36.876 1.804 1.00 14.82 ? 134 ASN A C 1 ATOM 1007 O O . ASN A 1 134 ? 31.254 37.635 0.819 1.00 14.62 ? 134 ASN A O 1 ATOM 1008 C CB . ASN A 1 134 ? 30.270 34.551 1.758 1.00 15.31 ? 134 ASN A CB 1 ATOM 1009 C CG . ASN A 1 134 ? 29.220 34.957 0.768 1.00 17.51 ? 134 ASN A CG 1 ATOM 1010 O OD1 . ASN A 1 134 ? 28.672 36.058 0.838 1.00 19.21 ? 134 ASN A OD1 1 ATOM 1011 N ND2 . ASN A 1 134 ? 28.900 34.059 -0.139 1.00 17.94 ? 134 ASN A ND2 1 ATOM 1012 N N . ARG A 1 135 ? 31.133 37.294 3.054 1.00 14.50 ? 135 ARG A N 1 ATOM 1013 C CA . ARG A 1 135 ? 30.929 38.702 3.385 1.00 15.61 ? 135 ARG A CA 1 ATOM 1014 C C . ARG A 1 135 ? 32.131 39.572 3.003 1.00 15.57 ? 135 ARG A C 1 ATOM 1015 O O . ARG A 1 135 ? 31.963 40.701 2.529 1.00 16.06 ? 135 ARG A O 1 ATOM 1016 C CB . ARG A 1 135 ? 30.540 38.851 4.859 1.00 15.04 ? 135 ARG A CB 1 ATOM 1017 C CG . ARG A 1 135 ? 29.104 38.371 5.115 1.00 16.43 ? 135 ARG A CG 1 ATOM 1018 C CD . ARG A 1 135 ? 28.796 38.288 6.597 1.00 17.50 ? 135 ARG A CD 1 ATOM 1019 N NE . ARG A 1 135 ? 29.031 36.955 7.158 1.00 19.60 ? 135 ARG A NE 1 ATOM 1020 C CZ . ARG A 1 135 ? 29.264 36.707 8.452 1.00 19.69 ? 135 ARG A CZ 1 ATOM 1021 N NH1 . ARG A 1 135 ? 29.446 35.460 8.852 1.00 17.16 ? 135 ARG A NH1 1 ATOM 1022 N NH2 . ARG A 1 135 ? 29.335 37.701 9.348 1.00 20.44 ? 135 ARG A NH2 1 ATOM 1023 N N . ALA A 1 136 ? 33.334 39.038 3.170 1.00 15.19 ? 136 ALA A N 1 ATOM 1024 C CA . ALA A 1 136 ? 34.540 39.727 2.730 1.00 15.42 ? 136 ALA A CA 1 ATOM 1025 C C . ALA A 1 136 ? 34.528 39.951 1.209 1.00 15.84 ? 136 ALA A C 1 ATOM 1026 O O . ALA A 1 136 ? 34.857 41.042 0.725 1.00 15.53 ? 136 ALA A O 1 ATOM 1027 C CB . ALA A 1 136 ? 35.781 38.943 3.164 1.00 14.72 ? 136 ALA A CB 1 ATOM 1028 N N . LYS A 1 137 ? 34.144 38.919 0.460 1.00 16.31 ? 137 LYS A N 1 ATOM 1029 C CA . LYS A 1 137 ? 34.030 39.020 -0.996 1.00 17.49 ? 137 LYS A CA 1 ATOM 1030 C C . LYS A 1 137 ? 32.997 40.072 -1.417 1.00 18.20 ? 137 LYS A C 1 ATOM 1031 O O . LYS A 1 137 ? 33.263 40.889 -2.309 1.00 17.90 ? 137 LYS A O 1 ATOM 1032 C CB . LYS A 1 137 ? 33.690 37.640 -1.594 1.00 17.09 ? 137 LYS A CB 1 ATOM 1033 C CG . LYS A 1 137 ? 33.349 37.604 -3.104 1.00 18.11 ? 137 LYS A CG 1 ATOM 1034 C CD . LYS A 1 137 ? 34.388 38.275 -4.017 1.00 19.03 ? 137 LYS A CD 1 ATOM 1035 C CE . LYS A 1 137 ? 35.726 37.556 -4.026 1.00 20.40 ? 137 LYS A CE 1 ATOM 1036 N NZ . LYS A 1 137 ? 36.498 37.943 -5.241 1.00 19.75 ? 137 LYS A NZ 1 ATOM 1037 N N . LYS A 1 138 ? 31.821 40.048 -0.793 1.00 19.12 ? 138 LYS A N 1 ATOM 1038 C CA . LYS A 1 138 ? 30.800 41.075 -1.068 1.00 20.84 ? 138 LYS A CA 1 ATOM 1039 C C . LYS A 1 138 ? 31.326 42.490 -0.846 1.00 20.81 ? 138 LYS A C 1 ATOM 1040 O O . LYS A 1 138 ? 30.931 43.409 -1.553 1.00 20.43 ? 138 LYS A O 1 ATOM 1041 C CB . LYS A 1 138 ? 29.498 40.858 -0.263 1.00 21.94 ? 138 LYS A CB 1 ATOM 1042 C CG . LYS A 1 138 ? 29.598 40.914 1.271 1.00 25.50 ? 138 LYS A CG 1 ATOM 1043 C CD . LYS A 1 138 ? 29.629 42.330 1.968 1.00 27.38 ? 138 LYS A CD 1 ATOM 1044 C CE . LYS A 1 138 ? 29.946 42.204 3.492 1.00 25.27 ? 138 LYS A CE 1 ATOM 1045 N NZ . LYS A 1 138 ? 30.017 43.490 4.313 1.00 29.36 ? 138 LYS A NZ 1 ATOM 1046 N N . ALA A 1 139 ? 32.219 42.645 0.127 1.00 20.73 ? 139 ALA A N 1 ATOM 1047 C CA . ALA A 1 139 ? 32.783 43.944 0.481 1.00 20.98 ? 139 ALA A CA 1 ATOM 1048 C C . ALA A 1 139 ? 33.948 44.285 -0.429 1.00 20.80 ? 139 ALA A C 1 ATOM 1049 O O . ALA A 1 139 ? 34.621 45.285 -0.227 1.00 22.35 ? 139 ALA A O 1 ATOM 1050 C CB . ALA A 1 139 ? 33.223 43.950 1.935 1.00 20.71 ? 139 ALA A CB 1 ATOM 1051 N N . GLY A 1 140 ? 34.187 43.445 -1.427 1.00 20.26 ? 140 GLY A N 1 ATOM 1052 C CA . GLY A 1 140 ? 35.189 43.745 -2.439 1.00 19.41 ? 140 GLY A CA 1 ATOM 1053 C C . GLY A 1 140 ? 36.573 43.186 -2.186 1.00 18.89 ? 140 GLY A C 1 ATOM 1054 O O . GLY A 1 140 ? 37.473 43.409 -2.995 1.00 19.27 ? 140 GLY A O 1 ATOM 1055 N N . LYS A 1 141 ? 36.747 42.446 -1.084 1.00 17.95 ? 141 LYS A N 1 ATOM 1056 C CA . LYS A 1 141 ? 38.023 41.798 -0.792 1.00 17.01 ? 141 LYS A CA 1 ATOM 1057 C C . LYS A 1 141 ? 38.243 40.575 -1.674 1.00 16.52 ? 141 LYS A C 1 ATOM 1058 O O . LYS A 1 141 ? 37.288 39.945 -2.138 1.00 16.58 ? 141 LYS A O 1 ATOM 1059 C CB . LYS A 1 141 ? 38.125 41.374 0.688 1.00 16.55 ? 141 LYS A CB 1 ATOM 1060 C CG . LYS A 1 141 ? 37.974 42.530 1.688 1.00 17.26 ? 141 LYS A CG 1 ATOM 1061 C CD . LYS A 1 141 ? 38.473 42.159 3.089 1.00 16.60 ? 141 LYS A CD 1 ATOM 1062 C CE . LYS A 1 141 ? 38.128 43.275 4.092 1.00 16.64 ? 141 LYS A CE 1 ATOM 1063 N NZ . LYS A 1 141 ? 38.810 44.558 3.733 1.00 16.86 ? 141 LYS A NZ 1 ATOM 1064 N N . SER A 1 142 ? 39.504 40.241 -1.907 1.00 15.54 ? 142 SER A N 1 ATOM 1065 C CA . SER A 1 142 ? 39.821 38.977 -2.563 1.00 15.36 ? 142 SER A CA 1 ATOM 1066 C C . SER A 1 142 ? 39.780 37.918 -1.478 1.00 14.81 ? 142 SER A C 1 ATOM 1067 O O . SER A 1 142 ? 40.013 38.214 -0.308 1.00 15.19 ? 142 SER A O 1 ATOM 1068 C CB . SER A 1 142 ? 41.194 39.002 -3.197 1.00 15.13 ? 142 SER A CB 1 ATOM 1069 O OG . SER A 1 142 ? 41.238 40.024 -4.172 1.00 17.54 ? 142 SER A OG 1 ATOM 1070 N N . VAL A 1 143 ? 39.472 36.690 -1.857 1.00 14.10 ? 143 VAL A N 1 ATOM 1071 C CA . VAL A 1 143 ? 39.333 35.632 -0.858 1.00 13.76 ? 143 VAL A CA 1 ATOM 1072 C C . VAL A 1 143 ? 40.030 34.353 -1.316 1.00 14.00 ? 143 VAL A C 1 ATOM 1073 O O . VAL A 1 143 ? 40.060 34.031 -2.513 1.00 13.99 ? 143 VAL A O 1 ATOM 1074 C CB . VAL A 1 143 ? 37.849 35.363 -0.450 1.00 13.50 ? 143 VAL A CB 1 ATOM 1075 C CG1 . VAL A 1 143 ? 37.161 36.651 0.107 1.00 13.69 ? 143 VAL A CG1 1 ATOM 1076 C CG2 . VAL A 1 143 ? 37.042 34.731 -1.603 1.00 14.22 ? 143 VAL A CG2 1 ATOM 1077 N N . GLY A 1 144 ? 40.565 33.620 -0.349 1.00 13.41 ? 144 GLY A N 1 ATOM 1078 C CA . GLY A 1 144 ? 41.374 32.443 -0.633 1.00 13.51 ? 144 GLY A CA 1 ATOM 1079 C C . GLY A 1 144 ? 41.074 31.332 0.353 1.00 13.72 ? 144 GLY A C 1 ATOM 1080 O O . GLY A 1 144 ? 40.798 31.573 1.542 1.00 13.31 ? 144 GLY A O 1 ATOM 1081 N N . VAL A 1 145 ? 41.128 30.111 -0.168 1.00 13.57 ? 145 VAL A N 1 ATOM 1082 C CA . VAL A 1 145 ? 40.922 28.902 0.598 1.00 13.92 ? 145 VAL A CA 1 ATOM 1083 C C . VAL A 1 145 ? 42.121 28.034 0.295 1.00 14.03 ? 145 VAL A C 1 ATOM 1084 O O . VAL A 1 145 ? 42.386 27.710 -0.865 1.00 14.13 ? 145 VAL A O 1 ATOM 1085 C CB . VAL A 1 145 ? 39.635 28.192 0.151 1.00 14.83 ? 145 VAL A CB 1 ATOM 1086 C CG1 . VAL A 1 145 ? 39.495 26.809 0.803 1.00 15.76 ? 145 VAL A CG1 1 ATOM 1087 C CG2 . VAL A 1 145 ? 38.410 29.074 0.442 1.00 13.54 ? 145 VAL A CG2 1 ATOM 1088 N N . VAL A 1 146 ? 42.857 27.677 1.343 1.00 13.33 ? 146 VAL A N 1 ATOM 1089 C CA . VAL A 1 146 ? 44.067 26.883 1.206 1.00 13.39 ? 146 VAL A CA 1 ATOM 1090 C C . VAL A 1 146 ? 43.990 25.767 2.230 1.00 12.93 ? 146 VAL A C 1 ATOM 1091 O O . VAL A 1 146 ? 43.761 26.036 3.412 1.00 12.38 ? 146 VAL A O 1 ATOM 1092 C CB . VAL A 1 146 ? 45.312 27.741 1.501 1.00 13.21 ? 146 VAL A CB 1 ATOM 1093 C CG1 . VAL A 1 146 ? 46.560 26.882 1.523 1.00 14.18 ? 146 VAL A CG1 1 ATOM 1094 C CG2 . VAL A 1 146 ? 45.452 28.874 0.507 1.00 14.40 ? 146 VAL A CG2 1 ATOM 1095 N N . THR A 1 147 ? 44.178 24.523 1.788 1.00 12.08 ? 147 THR A N 1 ATOM 1096 C CA . THR A 1 147 ? 44.150 23.395 2.719 1.00 12.55 ? 147 THR A CA 1 ATOM 1097 C C . THR A 1 147 ? 44.915 22.198 2.191 1.00 12.38 ? 147 THR A C 1 ATOM 1098 O O . THR A 1 147 ? 45.085 22.051 0.985 1.00 12.76 ? 147 THR A O 1 ATOM 1099 C CB . THR A 1 147 ? 42.702 22.974 3.061 1.00 11.98 ? 147 THR A CB 1 ATOM 1100 O OG1 . THR A 1 147 ? 42.730 21.818 3.903 1.00 13.20 ? 147 THR A OG1 1 ATOM 1101 C CG2 . THR A 1 147 ? 41.888 22.690 1.786 1.00 12.99 ? 147 THR A CG2 1 ATOM 1102 N N . THR A 1 148 ? 45.383 21.351 3.096 1.00 12.40 ? 148 THR A N 1 ATOM 1103 C CA . THR A 1 148 ? 46.018 20.086 2.705 1.00 13.08 ? 148 THR A CA 1 ATOM 1104 C C . THR A 1 148 ? 44.994 18.979 2.493 1.00 13.33 ? 148 THR A C 1 ATOM 1105 O O . THR A 1 148 ? 45.349 17.865 2.069 1.00 14.22 ? 148 THR A O 1 ATOM 1106 C CB . THR A 1 148 ? 46.989 19.619 3.799 1.00 12.81 ? 148 THR A CB 1 ATOM 1107 O OG1 . THR A 1 148 ? 46.322 19.706 5.068 1.00 12.52 ? 148 THR A OG1 1 ATOM 1108 C CG2 . THR A 1 148 ? 48.222 20.503 3.821 1.00 12.45 ? 148 THR A CG2 1 ATOM 1109 N N . THR A 1 149 ? 43.728 19.240 2.814 1.00 13.30 ? 149 THR A N 1 ATOM 1110 C CA . THR A 1 149 ? 42.687 18.272 2.457 1.00 12.89 ? 149 THR A CA 1 ATOM 1111 C C . THR A 1 149 ? 42.090 18.606 1.093 1.00 12.97 ? 149 THR A C 1 ATOM 1112 O O . THR A 1 149 ? 42.431 19.618 0.474 1.00 13.09 ? 149 THR A O 1 ATOM 1113 C CB . THR A 1 149 ? 41.537 18.185 3.496 1.00 12.96 ? 149 THR A CB 1 ATOM 1114 O OG1 . THR A 1 149 ? 40.808 19.423 3.521 1.00 12.42 ? 149 THR A OG1 1 ATOM 1115 C CG2 . THR A 1 149 ? 42.081 17.861 4.890 1.00 12.79 ? 149 THR A CG2 1 ATOM 1116 N N . ARG A 1 150 ? 41.193 17.743 0.631 1.00 13.51 ? 150 ARG A N 1 ATOM 1117 C CA . ARG A 1 150 ? 40.249 18.122 -0.411 1.00 13.29 ? 150 ARG A CA 1 ATOM 1118 C C . ARG A 1 150 ? 39.721 19.530 -0.131 1.00 13.63 ? 150 ARG A C 1 ATOM 1119 O O . ARG A 1 150 ? 39.359 19.857 1.008 1.00 12.76 ? 150 ARG A O 1 ATOM 1120 C CB . ARG A 1 150 ? 39.093 17.127 -0.415 1.00 13.58 ? 150 ARG A CB 1 ATOM 1121 C CG . ARG A 1 150 ? 39.485 15.777 -0.978 1.00 12.93 ? 150 ARG A CG 1 ATOM 1122 C CD . ARG A 1 150 ? 38.538 14.703 -0.481 1.00 13.56 ? 150 ARG A CD 1 ATOM 1123 N NE . ARG A 1 150 ? 38.917 14.213 0.841 1.00 15.00 ? 150 ARG A NE 1 ATOM 1124 C CZ . ARG A 1 150 ? 38.337 13.183 1.448 1.00 16.54 ? 150 ARG A CZ 1 ATOM 1125 N NH1 . ARG A 1 150 ? 38.760 12.786 2.649 1.00 16.81 ? 150 ARG A NH1 1 ATOM 1126 N NH2 . ARG A 1 150 ? 37.340 12.539 0.851 1.00 15.40 ? 150 ARG A NH2 1 ATOM 1127 N N . VAL A 1 151 ? 39.694 20.382 -1.150 1.00 13.83 ? 151 VAL A N 1 ATOM 1128 C CA . VAL A 1 151 ? 39.102 21.724 -0.977 1.00 13.59 ? 151 VAL A CA 1 ATOM 1129 C C . VAL A 1 151 ? 37.588 21.644 -0.722 1.00 13.21 ? 151 VAL A C 1 ATOM 1130 O O . VAL A 1 151 ? 36.971 22.627 -0.329 1.00 13.38 ? 151 VAL A O 1 ATOM 1131 C CB . VAL A 1 151 ? 39.402 22.671 -2.165 1.00 13.02 ? 151 VAL A CB 1 ATOM 1132 C CG1 . VAL A 1 151 ? 40.906 22.885 -2.295 1.00 12.42 ? 151 VAL A CG1 1 ATOM 1133 C CG2 . VAL A 1 151 ? 38.806 22.119 -3.472 1.00 14.24 ? 151 VAL A CG2 1 ATOM 1134 N N . GLN A 1 152 ? 37.021 20.462 -0.958 1.00 13.32 ? 152 GLN A N 1 ATOM 1135 C CA . GLN A 1 152 ? 35.608 20.162 -0.696 1.00 12.96 ? 152 GLN A CA 1 ATOM 1136 C C . GLN A 1 152 ? 35.419 19.495 0.660 1.00 13.03 ? 152 GLN A C 1 ATOM 1137 O O . GLN A 1 152 ? 34.303 19.112 1.011 1.00 13.20 ? 152 GLN A O 1 ATOM 1138 C CB . GLN A 1 152 ? 35.028 19.233 -1.794 1.00 12.53 ? 152 GLN A CB 1 ATOM 1139 C CG . GLN A 1 152 ? 35.266 19.690 -3.242 1.00 13.66 ? 152 GLN A CG 1 ATOM 1140 C CD . GLN A 1 152 ? 36.586 19.177 -3.811 1.00 14.89 ? 152 GLN A CD 1 ATOM 1141 O OE1 . GLN A 1 152 ? 37.413 18.607 -3.080 1.00 15.99 ? 152 GLN A OE1 1 ATOM 1142 N NE2 . GLN A 1 152 ? 36.784 19.359 -5.121 1.00 12.38 ? 152 GLN A NE2 1 ATOM 1143 N N . HIS A 1 153 ? 36.508 19.317 1.408 1.00 12.62 ? 153 HIS A N 1 ATOM 1144 C CA . HIS A 1 153 ? 36.412 18.740 2.747 1.00 12.19 ? 153 HIS A CA 1 ATOM 1145 C C . HIS A 1 153 ? 35.696 19.700 3.694 1.00 11.73 ? 153 HIS A C 1 ATOM 1146 O O . HIS A 1 153 ? 35.490 20.854 3.349 1.00 11.57 ? 153 HIS A O 1 ATOM 1147 C CB . HIS A 1 153 ? 37.787 18.428 3.305 1.00 12.10 ? 153 HIS A CB 1 ATOM 1148 C CG . HIS A 1 153 ? 37.804 17.213 4.166 1.00 13.15 ? 153 HIS A CG 1 ATOM 1149 N ND1 . HIS A 1 153 ? 37.871 17.261 5.542 1.00 15.35 ? 153 HIS A ND1 1 ATOM 1150 C CD2 . HIS A 1 153 ? 37.755 15.901 3.836 1.00 14.97 ? 153 HIS A CD2 1 ATOM 1151 C CE1 . HIS A 1 153 ? 37.871 16.030 6.022 1.00 15.15 ? 153 HIS A CE1 1 ATOM 1152 N NE2 . HIS A 1 153 ? 37.793 15.187 5.009 1.00 15.50 ? 153 HIS A NE2 1 ATOM 1153 N N . ALA A 1 154 ? 35.310 19.217 4.873 1.00 11.29 ? 154 ALA A N 1 ATOM 1154 C CA . ALA A 1 154 ? 34.352 19.945 5.708 1.00 11.40 ? 154 ALA A CA 1 ATOM 1155 C C . ALA A 1 154 ? 34.835 21.358 6.066 1.00 12.06 ? 154 ALA A C 1 ATOM 1156 O O . ALA A 1 154 ? 34.070 22.331 5.987 1.00 12.04 ? 154 ALA A O 1 ATOM 1157 C CB . ALA A 1 154 ? 34.040 19.153 6.960 1.00 11.58 ? 154 ALA A CB 1 ATOM 1158 N N . SER A 1 155 ? 36.095 21.468 6.476 1.00 11.76 ? 155 SER A N 1 ATOM 1159 C CA . SER A 1 155 ? 36.616 22.772 6.921 1.00 11.80 ? 155 SER A CA 1 ATOM 1160 C C . SER A 1 155 ? 36.628 23.859 5.833 1.00 11.64 ? 155 SER A C 1 ATOM 1161 O O . SER A 1 155 ? 36.006 24.933 6.019 1.00 11.64 ? 155 SER A O 1 ATOM 1162 C CB . SER A 1 155 ? 37.992 22.613 7.554 1.00 10.96 ? 155 SER A CB 1 ATOM 1163 O OG . SER A 1 155 ? 37.974 21.509 8.456 1.00 11.66 ? 155 SER A OG 1 ATOM 1164 N N . PRO A 1 156 ? 37.330 23.615 4.705 1.00 11.82 ? 156 PRO A N 1 ATOM 1165 C CA . PRO A 1 156 ? 37.285 24.644 3.660 1.00 11.76 ? 156 PRO A CA 1 ATOM 1166 C C . PRO A 1 156 ? 35.859 24.873 3.139 1.00 12.74 ? 156 PRO A C 1 ATOM 1167 O O . PRO A 1 156 ? 35.506 26.002 2.778 1.00 13.20 ? 156 PRO A O 1 ATOM 1168 C CB . PRO A 1 156 ? 38.153 24.050 2.537 1.00 11.76 ? 156 PRO A CB 1 ATOM 1169 C CG . PRO A 1 156 ? 38.198 22.557 2.792 1.00 10.86 ? 156 PRO A CG 1 ATOM 1170 C CD . PRO A 1 156 ? 38.149 22.449 4.297 1.00 11.76 ? 156 PRO A CD 1 ATOM 1171 N N . ALA A 1 157 ? 35.048 23.814 3.108 1.00 12.59 ? 157 ALA A N 1 ATOM 1172 C CA . ALA A 1 157 ? 33.671 23.924 2.611 1.00 12.94 ? 157 ALA A CA 1 ATOM 1173 C C . ALA A 1 157 ? 32.871 24.910 3.466 1.00 12.97 ? 157 ALA A C 1 ATOM 1174 O O . ALA A 1 157 ? 31.941 25.536 2.988 1.00 13.12 ? 157 ALA A O 1 ATOM 1175 C CB . ALA A 1 157 ? 33.005 22.559 2.583 1.00 12.00 ? 157 ALA A CB 1 ATOM 1176 N N . GLY A 1 158 ? 33.250 25.050 4.731 1.00 13.04 ? 158 GLY A N 1 ATOM 1177 C CA . GLY A 1 158 ? 32.613 26.025 5.621 1.00 12.99 ? 158 GLY A CA 1 ATOM 1178 C C . GLY A 1 158 ? 32.694 27.451 5.113 1.00 12.97 ? 158 GLY A C 1 ATOM 1179 O O . GLY A 1 158 ? 31.840 28.277 5.443 1.00 13.03 ? 158 GLY A O 1 ATOM 1180 N N . THR A 1 159 ? 33.712 27.755 4.310 1.00 13.31 ? 159 THR A N 1 ATOM 1181 C CA . THR A 1 159 ? 33.879 29.125 3.823 1.00 13.71 ? 159 THR A CA 1 ATOM 1182 C C . THR A 1 159 ? 32.929 29.467 2.698 1.00 13.53 ? 159 THR A C 1 ATOM 1183 O O . THR A 1 159 ? 32.705 30.650 2.437 1.00 14.42 ? 159 THR A O 1 ATOM 1184 C CB . THR A 1 159 ? 35.290 29.433 3.292 1.00 13.12 ? 159 THR A CB 1 ATOM 1185 O OG1 . THR A 1 159 ? 35.555 28.621 2.141 1.00 14.42 ? 159 THR A OG1 1 ATOM 1186 C CG2 . THR A 1 159 ? 36.368 29.223 4.362 1.00 13.57 ? 159 THR A CG2 1 ATOM 1187 N N . TYR A 1 160 ? 32.419 28.458 1.991 1.00 13.51 ? 160 TYR A N 1 ATOM 1188 C CA . TYR A 1 160 ? 31.611 28.734 0.792 1.00 13.62 ? 160 TYR A CA 1 ATOM 1189 C C . TYR A 1 160 ? 30.323 27.946 0.662 1.00 13.46 ? 160 TYR A C 1 ATOM 1190 O O . TYR A 1 160 ? 29.413 28.384 -0.036 1.00 14.63 ? 160 TYR A O 1 ATOM 1191 C CB . TYR A 1 160 ? 32.451 28.547 -0.495 1.00 14.10 ? 160 TYR A CB 1 ATOM 1192 C CG . TYR A 1 160 ? 33.015 27.142 -0.676 1.00 13.49 ? 160 TYR A CG 1 ATOM 1193 C CD1 . TYR A 1 160 ? 34.327 26.843 -0.294 1.00 12.74 ? 160 TYR A CD1 1 ATOM 1194 C CD2 . TYR A 1 160 ? 32.230 26.108 -1.228 1.00 14.13 ? 160 TYR A CD2 1 ATOM 1195 C CE1 . TYR A 1 160 ? 34.852 25.558 -0.454 1.00 13.71 ? 160 TYR A CE1 1 ATOM 1196 C CE2 . TYR A 1 160 ? 32.749 24.816 -1.396 1.00 13.84 ? 160 TYR A CE2 1 ATOM 1197 C CZ . TYR A 1 160 ? 34.063 24.551 -0.994 1.00 14.90 ? 160 TYR A CZ 1 ATOM 1198 O OH . TYR A 1 160 ? 34.593 23.290 -1.153 1.00 13.93 ? 160 TYR A OH 1 ATOM 1199 N N . ALA A 1 161 ? 30.243 26.791 1.322 1.00 12.46 ? 161 ALA A N 1 ATOM 1200 C CA . ALA A 1 161 ? 29.172 25.822 1.072 1.00 12.97 ? 161 ALA A CA 1 ATOM 1201 C C . ALA A 1 161 ? 28.091 25.826 2.132 1.00 12.74 ? 161 ALA A C 1 ATOM 1202 O O . ALA A 1 161 ? 28.302 26.297 3.243 1.00 11.69 ? 161 ALA A O 1 ATOM 1203 C CB . ALA A 1 161 ? 29.747 24.419 0.943 1.00 12.27 ? 161 ALA A CB 1 ATOM 1204 N N . HIS A 1 162 ? 26.936 25.272 1.766 1.00 13.00 ? 162 HIS A N 1 ATOM 1205 C CA . HIS A 1 162 ? 25.849 25.040 2.699 1.00 13.23 ? 162 HIS A CA 1 ATOM 1206 C C . HIS A 1 162 ? 25.320 23.670 2.349 1.00 13.32 ? 162 HIS A C 1 ATOM 1207 O O . HIS A 1 162 ? 24.805 23.457 1.248 1.00 13.38 ? 162 HIS A O 1 ATOM 1208 C CB . HIS A 1 162 ? 24.753 26.095 2.526 1.00 12.63 ? 162 HIS A CB 1 ATOM 1209 C CG . HIS A 1 162 ? 25.282 27.492 2.455 1.00 13.32 ? 162 HIS A CG 1 ATOM 1210 N ND1 . HIS A 1 162 ? 25.675 28.194 3.574 1.00 14.07 ? 162 HIS A ND1 1 ATOM 1211 C CD2 . HIS A 1 162 ? 25.546 28.292 1.395 1.00 13.77 ? 162 HIS A CD2 1 ATOM 1212 C CE1 . HIS A 1 162 ? 26.122 29.382 3.207 1.00 15.00 ? 162 HIS A CE1 1 ATOM 1213 N NE2 . HIS A 1 162 ? 26.072 29.458 1.890 1.00 14.17 ? 162 HIS A NE2 1 ATOM 1214 N N . THR A 1 163 ? 25.479 22.723 3.253 1.00 13.44 ? 163 THR A N 1 ATOM 1215 C CA . THR A 1 163 ? 25.031 21.361 2.952 1.00 13.74 ? 163 THR A CA 1 ATOM 1216 C C . THR A 1 163 ? 24.682 20.608 4.218 1.00 13.80 ? 163 THR A C 1 ATOM 1217 O O . THR A 1 163 ? 25.354 20.754 5.246 1.00 13.86 ? 163 THR A O 1 ATOM 1218 C CB . THR A 1 163 ? 26.062 20.544 2.126 1.00 13.65 ? 163 THR A CB 1 ATOM 1219 O OG1 . THR A 1 163 ? 25.501 19.261 1.829 1.00 13.75 ? 163 THR A OG1 1 ATOM 1220 C CG2 . THR A 1 163 ? 27.406 20.352 2.889 1.00 13.81 ? 163 THR A CG2 1 ATOM 1221 N N . VAL A 1 164 ? 23.634 19.794 4.127 1.00 13.84 ? 164 VAL A N 1 ATOM 1222 C CA . VAL A 1 164 ? 23.252 18.924 5.227 1.00 13.43 ? 164 VAL A CA 1 ATOM 1223 C C . VAL A 1 164 ? 24.123 17.687 5.297 1.00 13.87 ? 164 VAL A C 1 ATOM 1224 O O . VAL A 1 164 ? 23.942 16.862 6.175 1.00 13.58 ? 164 VAL A O 1 ATOM 1225 C CB . VAL A 1 164 ? 21.776 18.482 5.120 1.00 14.12 ? 164 VAL A CB 1 ATOM 1226 C CG1 . VAL A 1 164 ? 20.843 19.694 5.305 1.00 12.99 ? 164 VAL A CG1 1 ATOM 1227 C CG2 . VAL A 1 164 ? 21.528 17.742 3.789 1.00 12.51 ? 164 VAL A CG2 1 ATOM 1228 N N . ASN A 1 165 ? 25.058 17.527 4.371 1.00 13.50 ? 165 ASN A N 1 ATOM 1229 C CA . ASN A 1 165 ? 25.877 16.319 4.405 1.00 13.88 ? 165 ASN A CA 1 ATOM 1230 C C . ASN A 1 165 ? 27.262 16.587 3.860 1.00 13.72 ? 165 ASN A C 1 ATOM 1231 O O . ASN A 1 165 ? 27.466 16.629 2.647 1.00 12.67 ? 165 ASN A O 1 ATOM 1232 C CB . ASN A 1 165 ? 25.201 15.145 3.661 1.00 14.42 ? 165 ASN A CB 1 ATOM 1233 C CG . ASN A 1 165 ? 25.817 13.796 4.005 1.00 14.83 ? 165 ASN A CG 1 ATOM 1234 O OD1 . ASN A 1 165 ? 26.988 13.712 4.355 1.00 14.75 ? 165 ASN A OD1 1 ATOM 1235 N ND2 . ASN A 1 165 ? 25.019 12.730 3.906 1.00 15.14 ? 165 ASN A ND2 1 ATOM 1236 N N . ARG A 1 166 ? 28.204 16.735 4.785 1.00 13.32 ? 166 ARG A N 1 ATOM 1237 C CA . ARG A 1 166 ? 29.607 16.958 4.452 1.00 13.82 ? 166 ARG A CA 1 ATOM 1238 C C . ARG A 1 166 ? 30.195 15.885 3.520 1.00 14.14 ? 166 ARG A C 1 ATOM 1239 O O . ARG A 1 166 ? 31.196 16.131 2.876 1.00 14.45 ? 166 ARG A O 1 ATOM 1240 C CB . ARG A 1 166 ? 30.433 16.993 5.734 1.00 13.59 ? 166 ARG A CB 1 ATOM 1241 C CG . ARG A 1 166 ? 30.348 15.674 6.495 1.00 13.84 ? 166 ARG A CG 1 ATOM 1242 C CD . ARG A 1 166 ? 31.297 15.697 7.666 1.00 14.10 ? 166 ARG A CD 1 ATOM 1243 N NE . ARG A 1 166 ? 32.692 15.709 7.232 1.00 14.65 ? 166 ARG A NE 1 ATOM 1244 C CZ . ARG A 1 166 ? 33.719 15.814 8.069 1.00 14.03 ? 166 ARG A CZ 1 ATOM 1245 N NH1 . ARG A 1 166 ? 33.493 15.953 9.379 1.00 13.48 ? 166 ARG A NH1 1 ATOM 1246 N NH2 . ARG A 1 166 ? 34.963 15.808 7.601 1.00 13.95 ? 166 ARG A NH2 1 ATOM 1247 N N . ASN A 1 167 ? 29.578 14.703 3.460 1.00 14.74 ? 167 ASN A N 1 ATOM 1248 C CA . ASN A 1 167 ? 30.075 13.618 2.612 1.00 15.19 ? 167 ASN A CA 1 ATOM 1249 C C . ASN A 1 167 ? 29.739 13.789 1.140 1.00 15.12 ? 167 ASN A C 1 ATOM 1250 O O . ASN A 1 167 ? 30.205 13.019 0.297 1.00 15.33 ? 167 ASN A O 1 ATOM 1251 C CB . ASN A 1 167 ? 29.529 12.273 3.115 1.00 15.57 ? 167 ASN A CB 1 ATOM 1252 C CG . ASN A 1 167 ? 29.951 11.988 4.537 1.00 17.82 ? 167 ASN A CG 1 ATOM 1253 O OD1 . ASN A 1 167 ? 31.130 11.998 4.847 1.00 19.26 ? 167 ASN A OD1 1 ATOM 1254 N ND2 . ASN A 1 167 ? 28.986 11.751 5.407 1.00 20.01 ? 167 ASN A ND2 1 ATOM 1255 N N . TRP A 1 168 ? 28.941 14.805 0.825 1.00 15.02 ? 168 TRP A N 1 ATOM 1256 C CA . TRP A 1 168 ? 28.514 15.037 -0.559 1.00 14.79 ? 168 TRP A CA 1 ATOM 1257 C C . TRP A 1 168 ? 29.542 15.798 -1.386 1.00 14.92 ? 168 TRP A C 1 ATOM 1258 O O . TRP A 1 168 ? 29.283 16.907 -1.856 1.00 14.98 ? 168 TRP A O 1 ATOM 1259 C CB . TRP A 1 168 ? 27.172 15.749 -0.589 1.00 14.15 ? 168 TRP A CB 1 ATOM 1260 C CG . TRP A 1 168 ? 26.052 14.895 -0.077 1.00 15.42 ? 168 TRP A CG 1 ATOM 1261 C CD1 . TRP A 1 168 ? 26.082 13.542 0.185 1.00 14.10 ? 168 TRP A CD1 1 ATOM 1262 C CD2 . TRP A 1 168 ? 24.719 15.325 0.185 1.00 14.62 ? 168 TRP A CD2 1 ATOM 1263 N NE1 . TRP A 1 168 ? 24.845 13.117 0.609 1.00 15.10 ? 168 TRP A NE1 1 ATOM 1264 C CE2 . TRP A 1 168 ? 23.990 14.192 0.618 1.00 14.99 ? 168 TRP A CE2 1 ATOM 1265 C CE3 . TRP A 1 168 ? 24.072 16.566 0.120 1.00 13.82 ? 168 TRP A CE3 1 ATOM 1266 C CZ2 . TRP A 1 168 ? 22.655 14.270 1.003 1.00 15.78 ? 168 TRP A CZ2 1 ATOM 1267 C CZ3 . TRP A 1 168 ? 22.737 16.639 0.485 1.00 13.55 ? 168 TRP A CZ3 1 ATOM 1268 C CH2 . TRP A 1 168 ? 22.043 15.497 0.923 1.00 15.17 ? 168 TRP A CH2 1 ATOM 1269 N N . TYR A 1 169 ? 30.697 15.175 -1.599 1.00 15.34 ? 169 TYR A N 1 ATOM 1270 C CA . TYR A 1 169 ? 31.801 15.822 -2.294 1.00 15.30 ? 169 TYR A CA 1 ATOM 1271 C C . TYR A 1 169 ? 31.463 16.099 -3.754 1.00 15.52 ? 169 TYR A C 1 ATOM 1272 O O . TYR A 1 169 ? 31.699 17.193 -4.248 1.00 15.65 ? 169 TYR A O 1 ATOM 1273 C CB . TYR A 1 169 ? 33.059 14.961 -2.213 1.00 14.93 ? 169 TYR A CB 1 ATOM 1274 C CG . TYR A 1 169 ? 33.543 14.721 -0.808 1.00 14.73 ? 169 TYR A CG 1 ATOM 1275 C CD1 . TYR A 1 169 ? 34.061 15.769 -0.046 1.00 14.70 ? 169 TYR A CD1 1 ATOM 1276 C CD2 . TYR A 1 169 ? 33.477 13.455 -0.241 1.00 14.97 ? 169 TYR A CD2 1 ATOM 1277 C CE1 . TYR A 1 169 ? 34.507 15.568 1.251 1.00 15.08 ? 169 TYR A CE1 1 ATOM 1278 C CE2 . TYR A 1 169 ? 33.926 13.228 1.067 1.00 14.40 ? 169 TYR A CE2 1 ATOM 1279 C CZ . TYR A 1 169 ? 34.435 14.297 1.801 1.00 15.37 ? 169 TYR A CZ 1 ATOM 1280 O OH . TYR A 1 169 ? 34.882 14.102 3.068 1.00 16.42 ? 169 TYR A OH 1 ATOM 1281 N N . SER A 1 170 ? 30.921 15.095 -4.436 1.00 15.84 ? 170 SER A N 1 ATOM 1282 C CA . SER A 1 170 ? 30.536 15.247 -5.826 1.00 16.11 ? 170 SER A CA 1 ATOM 1283 C C . SER A 1 170 ? 29.132 14.692 -5.979 1.00 16.22 ? 170 SER A C 1 ATOM 1284 O O . SER A 1 170 ? 28.554 14.130 -5.032 1.00 15.94 ? 170 SER A O 1 ATOM 1285 C CB . SER A 1 170 ? 31.508 14.516 -6.764 1.00 16.71 ? 170 SER A CB 1 ATOM 1286 O OG . SER A 1 170 ? 31.153 13.145 -6.927 1.00 16.86 ? 170 SER A OG 1 ATOM 1287 N N . ASP A 1 171 ? 28.569 14.874 -7.163 1.00 16.52 ? 171 ASP A N 1 ATOM 1288 C CA . ASP A 1 171 ? 27.212 14.422 -7.409 1.00 17.39 ? 171 ASP A CA 1 ATOM 1289 C C . ASP A 1 171 ? 27.078 12.905 -7.223 1.00 17.10 ? 171 ASP A C 1 ATOM 1290 O O . ASP A 1 171 ? 25.996 12.424 -6.882 1.00 17.03 ? 171 ASP A O 1 ATOM 1291 C CB . ASP A 1 171 ? 26.734 14.875 -8.789 1.00 17.46 ? 171 ASP A CB 1 ATOM 1292 C CG . ASP A 1 171 ? 27.607 14.375 -9.903 1.00 19.73 ? 171 ASP A CG 1 ATOM 1293 O OD1 . ASP A 1 171 ? 28.837 14.307 -9.732 1.00 20.99 ? 171 ASP A OD1 1 ATOM 1294 O OD2 . ASP A 1 171 ? 27.056 14.063 -10.970 1.00 24.66 ? 171 ASP A OD2 1 ATOM 1295 N N . ALA A 1 172 ? 28.183 12.173 -7.405 1.00 17.08 ? 172 ALA A N 1 ATOM 1296 C CA . ALA A 1 172 ? 28.205 10.712 -7.198 1.00 17.56 ? 172 ALA A CA 1 ATOM 1297 C C . ALA A 1 172 ? 27.816 10.315 -5.775 1.00 17.53 ? 172 ALA A C 1 ATOM 1298 O O . ALA A 1 172 ? 27.347 9.192 -5.545 1.00 18.62 ? 172 ALA A O 1 ATOM 1299 C CB . ALA A 1 172 ? 29.564 10.141 -7.544 1.00 16.64 ? 172 ALA A CB 1 ATOM 1300 N N . ASP A 1 173 ? 28.021 11.236 -4.833 1.00 17.17 ? 173 ASP A N 1 ATOM 1301 C CA . ASP A 1 173 ? 27.755 11.005 -3.407 1.00 17.01 ? 173 ASP A CA 1 ATOM 1302 C C . ASP A 1 173 ? 26.345 11.391 -2.981 1.00 17.22 ? 173 ASP A C 1 ATOM 1303 O O . ASP A 1 173 ? 25.881 10.999 -1.895 1.00 17.00 ? 173 ASP A O 1 ATOM 1304 C CB . ASP A 1 173 ? 28.740 11.819 -2.576 1.00 16.81 ? 173 ASP A CB 1 ATOM 1305 C CG . ASP A 1 173 ? 30.156 11.449 -2.862 1.00 17.31 ? 173 ASP A CG 1 ATOM 1306 O OD1 . ASP A 1 173 ? 30.966 12.358 -3.106 1.00 18.17 ? 173 ASP A OD1 1 ATOM 1307 O OD2 . ASP A 1 173 ? 30.450 10.233 -2.864 1.00 18.45 ? 173 ASP A OD2 1 ATOM 1308 N N . VAL A 1 174 ? 25.696 12.203 -3.813 1.00 17.15 ? 174 VAL A N 1 ATOM 1309 C CA . VAL A 1 174 ? 24.387 12.759 -3.486 1.00 17.64 ? 174 VAL A CA 1 ATOM 1310 C C . VAL A 1 174 ? 23.286 11.792 -3.930 1.00 18.18 ? 174 VAL A C 1 ATOM 1311 O O . VAL A 1 174 ? 23.195 11.453 -5.113 1.00 18.28 ? 174 VAL A O 1 ATOM 1312 C CB . VAL A 1 174 ? 24.178 14.160 -4.137 1.00 17.43 ? 174 VAL A CB 1 ATOM 1313 C CG1 . VAL A 1 174 ? 22.835 14.757 -3.714 1.00 17.40 ? 174 VAL A CG1 1 ATOM 1314 C CG2 . VAL A 1 174 ? 25.313 15.123 -3.737 1.00 16.89 ? 174 VAL A CG2 1 ATOM 1315 N N . PRO A 1 175 ? 22.434 11.357 -2.987 1.00 18.92 ? 175 PRO A N 1 ATOM 1316 C CA . PRO A 1 175 ? 21.327 10.468 -3.336 1.00 19.43 ? 175 PRO A CA 1 ATOM 1317 C C . PRO A 1 175 ? 20.447 11.136 -4.385 1.00 20.21 ? 175 PRO A C 1 ATOM 1318 O O . PRO A 1 175 ? 20.325 12.365 -4.398 1.00 19.63 ? 175 PRO A O 1 ATOM 1319 C CB . PRO A 1 175 ? 20.554 10.341 -2.023 1.00 19.59 ? 175 PRO A CB 1 ATOM 1320 C CG . PRO A 1 175 ? 21.547 10.672 -0.963 1.00 19.49 ? 175 PRO A CG 1 ATOM 1321 C CD . PRO A 1 175 ? 22.447 11.692 -1.553 1.00 18.60 ? 175 PRO A CD 1 ATOM 1322 N N . ALA A 1 176 ? 19.843 10.333 -5.257 1.00 20.48 ? 176 ALA A N 1 ATOM 1323 C CA . ALA A 1 176 ? 18.992 10.869 -6.322 1.00 21.12 ? 176 ALA A CA 1 ATOM 1324 C C . ALA A 1 176 ? 17.942 11.856 -5.787 1.00 21.48 ? 176 ALA A C 1 ATOM 1325 O O . ALA A 1 176 ? 17.732 12.910 -6.379 1.00 21.42 ? 176 ALA A O 1 ATOM 1326 C CB . ALA A 1 176 ? 18.328 9.729 -7.109 1.00 21.74 ? 176 ALA A CB 1 ATOM 1327 N N . SER A 1 177 ? 17.322 11.546 -4.650 1.00 21.80 ? 177 SER A N 1 ATOM 1328 C CA . SER A 1 177 ? 16.272 12.420 -4.121 1.00 22.07 ? 177 SER A CA 1 ATOM 1329 C C . SER A 1 177 ? 16.812 13.817 -3.772 1.00 21.31 ? 177 SER A C 1 ATOM 1330 O O . SER A 1 177 ? 16.147 14.826 -4.032 1.00 21.28 ? 177 SER A O 1 ATOM 1331 C CB . SER A 1 177 ? 15.531 11.775 -2.939 1.00 22.32 ? 177 SER A CB 1 ATOM 1332 O OG . SER A 1 177 ? 16.429 11.471 -1.884 1.00 25.62 ? 177 SER A OG 1 ATOM 1333 N N . ALA A 1 178 ? 18.024 13.864 -3.216 1.00 20.11 ? 178 ALA A N 1 ATOM 1334 C CA . ALA A 1 178 ? 18.675 15.119 -2.847 1.00 19.38 ? 178 ALA A CA 1 ATOM 1335 C C . ALA A 1 178 ? 19.098 15.878 -4.100 1.00 19.43 ? 178 ALA A C 1 ATOM 1336 O O . ALA A 1 178 ? 18.991 17.100 -4.150 1.00 18.80 ? 178 ALA A O 1 ATOM 1337 C CB . ALA A 1 178 ? 19.865 14.851 -1.950 1.00 18.98 ? 178 ALA A CB 1 ATOM 1338 N N . ARG A 1 179 ? 19.549 15.155 -5.124 1.00 19.66 ? 179 ARG A N 1 ATOM 1339 C CA . ARG A 1 179 ? 19.918 15.794 -6.386 1.00 20.79 ? 179 ARG A CA 1 ATOM 1340 C C . ARG A 1 179 ? 18.679 16.456 -6.996 1.00 21.22 ? 179 ARG A C 1 ATOM 1341 O O . ARG A 1 179 ? 18.729 17.634 -7.401 1.00 20.15 ? 179 ARG A O 1 ATOM 1342 C CB . ARG A 1 179 ? 20.532 14.785 -7.367 1.00 20.93 ? 179 ARG A CB 1 ATOM 1343 C CG . ARG A 1 179 ? 21.916 14.287 -6.931 1.00 24.12 ? 179 ARG A CG 1 ATOM 1344 C CD . ARG A 1 179 ? 22.741 13.769 -8.098 1.00 28.86 ? 179 ARG A CD 1 ATOM 1345 N NE . ARG A 1 179 ? 21.998 12.788 -8.874 1.00 32.43 ? 179 ARG A NE 1 ATOM 1346 C CZ . ARG A 1 179 ? 22.004 11.483 -8.629 1.00 35.33 ? 179 ARG A CZ 1 ATOM 1347 N NH1 . ARG A 1 179 ? 22.719 10.999 -7.627 1.00 35.86 ? 179 ARG A NH1 1 ATOM 1348 N NH2 . ARG A 1 179 ? 21.297 10.661 -9.392 1.00 36.00 ? 179 ARG A NH2 1 ATOM 1349 N N . GLN A 1 180 ? 17.564 15.719 -7.016 1.00 22.03 ? 180 GLN A N 1 ATOM 1350 C CA . GLN A 1 180 ? 16.315 16.289 -7.553 1.00 24.18 ? 180 GLN A CA 1 ATOM 1351 C C . GLN A 1 180 ? 15.848 17.494 -6.736 1.00 23.27 ? 180 GLN A C 1 ATOM 1352 O O . GLN A 1 180 ? 15.379 18.480 -7.310 1.00 22.57 ? 180 GLN A O 1 ATOM 1353 C CB . GLN A 1 180 ? 15.197 15.255 -7.776 1.00 24.36 ? 180 GLN A CB 1 ATOM 1354 C CG . GLN A 1 180 ? 15.056 14.152 -6.760 1.00 28.48 ? 180 GLN A CG 1 ATOM 1355 C CD . GLN A 1 180 ? 14.400 12.854 -7.306 1.00 28.76 ? 180 GLN A CD 1 ATOM 1356 O OE1 . GLN A 1 180 ? 14.703 12.387 -8.419 1.00 35.32 ? 180 GLN A OE1 1 ATOM 1357 N NE2 . GLN A 1 180 ? 13.518 12.260 -6.498 1.00 33.96 ? 180 GLN A NE2 1 ATOM 1358 N N . GLU A 1 181 ? 16.041 17.439 -5.418 1.00 22.75 ? 181 GLU A N 1 ATOM 1359 C CA . GLU A 1 181 ? 15.695 18.564 -4.538 1.00 22.82 ? 181 GLU A CA 1 ATOM 1360 C C . GLU A 1 181 ? 16.685 19.732 -4.597 1.00 22.31 ? 181 GLU A C 1 ATOM 1361 O O . GLU A 1 181 ? 16.509 20.744 -3.911 1.00 22.81 ? 181 GLU A O 1 ATOM 1362 C CB . GLU A 1 181 ? 15.524 18.093 -3.104 1.00 23.09 ? 181 GLU A CB 1 ATOM 1363 C CG . GLU A 1 181 ? 14.340 17.172 -2.890 1.00 25.16 ? 181 GLU A CG 1 ATOM 1364 C CD . GLU A 1 181 ? 14.398 16.496 -1.545 1.00 29.33 ? 181 GLU A CD 1 ATOM 1365 O OE1 . GLU A 1 181 ? 13.393 15.886 -1.146 1.00 32.30 ? 181 GLU A OE1 1 ATOM 1366 O OE2 . GLU A 1 181 ? 15.454 16.569 -0.883 1.00 31.29 ? 181 GLU A OE2 1 ATOM 1367 N N . GLY A 1 182 ? 17.705 19.605 -5.433 1.00 21.93 ? 182 GLY A N 1 ATOM 1368 C CA . GLY A 1 182 ? 18.620 20.707 -5.689 1.00 21.19 ? 182 GLY A CA 1 ATOM 1369 C C . GLY A 1 182 ? 19.703 20.914 -4.651 1.00 21.37 ? 182 GLY A C 1 ATOM 1370 O O . GLY A 1 182 ? 20.295 21.996 -4.581 1.00 21.50 ? 182 GLY A O 1 ATOM 1371 N N . CYS A 1 183 ? 19.992 19.896 -3.839 1.00 20.68 ? 183 CYS A N 1 ATOM 1372 C CA . CYS A 1 183 ? 21.156 19.981 -2.954 1.00 20.44 ? 183 CYS A CA 1 ATOM 1373 C C . CYS A 1 183 ? 22.410 19.691 -3.749 1.00 20.30 ? 183 CYS A C 1 ATOM 1374 O O . CYS A 1 183 ? 22.684 18.535 -4.110 1.00 20.76 ? 183 CYS A O 1 ATOM 1375 C CB . CYS A 1 183 ? 21.068 19.023 -1.763 1.00 20.52 ? 183 CYS A CB 1 ATOM 1376 S SG . CYS A 1 183 ? 19.976 19.584 -0.457 1.00 22.61 ? 183 CYS A SG 1 ATOM 1377 N N . GLN A 1 184 ? 23.177 20.744 -4.006 1.00 19.05 ? 184 GLN A N 1 ATOM 1378 C CA . GLN A 1 184 ? 24.346 20.634 -4.843 1.00 18.51 ? 184 GLN A CA 1 ATOM 1379 C C . GLN A 1 184 ? 25.492 19.991 -4.082 1.00 17.18 ? 184 GLN A C 1 ATOM 1380 O O . GLN A 1 184 ? 25.716 20.275 -2.900 1.00 16.36 ? 184 GLN A O 1 ATOM 1381 C CB . GLN A 1 184 ? 24.761 22.008 -5.350 1.00 19.09 ? 184 GLN A CB 1 ATOM 1382 C CG . GLN A 1 184 ? 23.767 22.617 -6.346 1.00 21.90 ? 184 GLN A CG 1 ATOM 1383 C CD . GLN A 1 184 ? 24.207 23.971 -6.852 1.00 27.09 ? 184 GLN A CD 1 ATOM 1384 O OE1 . GLN A 1 184 ? 24.130 24.251 -8.057 1.00 30.76 ? 184 GLN A OE1 1 ATOM 1385 N NE2 . GLN A 1 184 ? 24.666 24.828 -5.945 1.00 28.35 ? 184 GLN A NE2 1 ATOM 1386 N N . ASP A 1 185 ? 26.224 19.127 -4.771 1.00 16.31 ? 185 ASP A N 1 ATOM 1387 C CA . ASP A 1 185 ? 27.422 18.569 -4.187 1.00 15.11 ? 185 ASP A CA 1 ATOM 1388 C C . ASP A 1 185 ? 28.397 19.710 -3.909 1.00 14.68 ? 185 ASP A C 1 ATOM 1389 O O . ASP A 1 185 ? 28.310 20.794 -4.509 1.00 13.66 ? 185 ASP A O 1 ATOM 1390 C CB . ASP A 1 185 ? 28.045 17.557 -5.131 1.00 15.71 ? 185 ASP A CB 1 ATOM 1391 C CG . ASP A 1 185 ? 28.419 18.169 -6.463 1.00 16.00 ? 185 ASP A CG 1 ATOM 1392 O OD1 . ASP A 1 185 ? 29.577 18.578 -6.625 1.00 16.75 ? 185 ASP A OD1 1 ATOM 1393 O OD2 . ASP A 1 185 ? 27.541 18.273 -7.338 1.00 17.14 ? 185 ASP A OD2 1 ATOM 1394 N N . ILE A 1 186 ? 29.317 19.461 -2.988 1.00 13.92 ? 186 ILE A N 1 ATOM 1395 C CA . ILE A 1 186 ? 30.239 20.496 -2.529 1.00 13.80 ? 186 ILE A CA 1 ATOM 1396 C C . ILE A 1 186 ? 31.157 21.013 -3.650 1.00 14.13 ? 186 ILE A C 1 ATOM 1397 O O . ILE A 1 186 ? 31.425 22.221 -3.730 1.00 13.40 ? 186 ILE A O 1 ATOM 1398 C CB . ILE A 1 186 ? 31.024 20.008 -1.298 1.00 13.56 ? 186 ILE A CB 1 ATOM 1399 C CG1 . ILE A 1 186 ? 30.022 19.685 -0.168 1.00 12.91 ? 186 ILE A CG1 1 ATOM 1400 C CG2 . ILE A 1 186 ? 31.998 21.086 -0.835 1.00 12.70 ? 186 ILE A CG2 1 ATOM 1401 C CD1 . ILE A 1 186 ? 30.595 18.802 0.957 1.00 14.38 ? 186 ILE A CD1 1 ATOM 1402 N N . ALA A 1 187 ? 31.624 20.113 -4.525 1.00 14.16 ? 187 ALA A N 1 ATOM 1403 C CA . ALA A 1 187 ? 32.458 20.540 -5.642 1.00 14.85 ? 187 ALA A CA 1 ATOM 1404 C C . ALA A 1 187 ? 31.725 21.561 -6.517 1.00 14.91 ? 187 ALA A C 1 ATOM 1405 O O . ALA A 1 187 ? 32.304 22.557 -6.936 1.00 15.12 ? 187 ALA A O 1 ATOM 1406 C CB . ALA A 1 187 ? 32.931 19.333 -6.473 1.00 14.98 ? 187 ALA A CB 1 ATOM 1407 N N . THR A 1 188 ? 30.442 21.317 -6.777 1.00 15.52 ? 188 THR A N 1 ATOM 1408 C CA . THR A 1 188 ? 29.629 22.278 -7.515 1.00 15.61 ? 188 THR A CA 1 ATOM 1409 C C . THR A 1 188 ? 29.547 23.606 -6.756 1.00 15.42 ? 188 THR A C 1 ATOM 1410 O O . THR A 1 188 ? 29.756 24.673 -7.344 1.00 15.49 ? 188 THR A O 1 ATOM 1411 C CB . THR A 1 188 ? 28.217 21.731 -7.797 1.00 15.37 ? 188 THR A CB 1 ATOM 1412 O OG1 . THR A 1 188 ? 28.331 20.568 -8.636 1.00 16.62 ? 188 THR A OG1 1 ATOM 1413 C CG2 . THR A 1 188 ? 27.372 22.778 -8.504 1.00 16.02 ? 188 THR A CG2 1 ATOM 1414 N N . GLN A 1 189 ? 29.249 23.532 -5.457 1.00 14.69 ? 189 GLN A N 1 ATOM 1415 C CA . GLN A 1 189 ? 29.122 24.736 -4.623 1.00 14.82 ? 189 GLN A CA 1 ATOM 1416 C C . GLN A 1 189 ? 30.408 25.541 -4.604 1.00 14.37 ? 189 GLN A C 1 ATOM 1417 O O . GLN A 1 189 ? 30.373 26.766 -4.592 1.00 14.78 ? 189 GLN A O 1 ATOM 1418 C CB . GLN A 1 189 ? 28.719 24.378 -3.201 1.00 14.22 ? 189 GLN A CB 1 ATOM 1419 C CG . GLN A 1 189 ? 27.366 23.671 -3.140 1.00 13.31 ? 189 GLN A CG 1 ATOM 1420 C CD . GLN A 1 189 ? 26.783 23.684 -1.768 1.00 13.88 ? 189 GLN A CD 1 ATOM 1421 O OE1 . GLN A 1 189 ? 26.931 24.668 -1.034 1.00 15.67 ? 189 GLN A OE1 1 ATOM 1422 N NE2 . GLN A 1 189 ? 26.099 22.603 -1.399 1.00 13.90 ? 189 GLN A NE2 1 ATOM 1423 N N . LEU A 1 190 ? 31.538 24.844 -4.627 1.00 15.01 ? 190 LEU A N 1 ATOM 1424 C CA . LEU A 1 190 ? 32.852 25.481 -4.704 1.00 14.84 ? 190 LEU A CA 1 ATOM 1425 C C . LEU A 1 190 ? 32.974 26.462 -5.868 1.00 15.13 ? 190 LEU A C 1 ATOM 1426 O O . LEU A 1 190 ? 33.522 27.558 -5.719 1.00 15.10 ? 190 LEU A O 1 ATOM 1427 C CB . LEU A 1 190 ? 33.938 24.420 -4.832 1.00 14.50 ? 190 LEU A CB 1 ATOM 1428 C CG . LEU A 1 190 ? 35.352 24.925 -5.122 1.00 14.92 ? 190 LEU A CG 1 ATOM 1429 C CD1 . LEU A 1 190 ? 35.893 25.618 -3.873 1.00 14.56 ? 190 LEU A CD1 1 ATOM 1430 C CD2 . LEU A 1 190 ? 36.244 23.735 -5.540 1.00 14.30 ? 190 LEU A CD2 1 ATOM 1431 N N . ILE A 1 191 ? 32.476 26.064 -7.029 1.00 15.85 ? 191 ILE A N 1 ATOM 1432 C CA . ILE A 1 191 ? 32.583 26.935 -8.211 1.00 16.37 ? 191 ILE A CA 1 ATOM 1433 C C . ILE A 1 191 ? 31.380 27.851 -8.392 1.00 17.14 ? 191 ILE A C 1 ATOM 1434 O O . ILE A 1 191 ? 31.466 28.842 -9.121 1.00 17.82 ? 191 ILE A O 1 ATOM 1435 C CB . ILE A 1 191 ? 32.867 26.135 -9.521 1.00 16.40 ? 191 ILE A CB 1 ATOM 1436 C CG1 . ILE A 1 191 ? 31.632 25.352 -9.983 1.00 15.75 ? 191 ILE A CG1 1 ATOM 1437 C CG2 . ILE A 1 191 ? 34.062 25.198 -9.324 1.00 16.51 ? 191 ILE A CG2 1 ATOM 1438 C CD1 . ILE A 1 191 ? 31.601 25.125 -11.501 1.00 17.67 ? 191 ILE A CD1 1 ATOM 1439 N N . SER A 1 192 ? 30.271 27.546 -7.723 1.00 17.69 ? 192 SER A N 1 ATOM 1440 C CA . SER A 1 192 ? 29.014 28.249 -8.008 1.00 19.05 ? 192 SER A CA 1 ATOM 1441 C C . SER A 1 192 ? 28.538 29.232 -6.958 1.00 18.51 ? 192 SER A C 1 ATOM 1442 O O . SER A 1 192 ? 27.939 30.237 -7.320 1.00 17.90 ? 192 SER A O 1 ATOM 1443 C CB . SER A 1 192 ? 27.871 27.269 -8.303 1.00 19.53 ? 192 SER A CB 1 ATOM 1444 O OG . SER A 1 192 ? 28.298 26.339 -9.264 1.00 24.44 ? 192 SER A OG 1 ATOM 1445 N N . ASN A 1 193 ? 28.759 28.934 -5.674 1.00 17.56 ? 193 ASN A N 1 ATOM 1446 C CA . ASN A 1 193 ? 28.138 29.739 -4.607 1.00 17.48 ? 193 ASN A CA 1 ATOM 1447 C C . ASN A 1 193 ? 28.670 31.158 -4.598 1.00 17.46 ? 193 ASN A C 1 ATOM 1448 O O . ASN A 1 193 ? 27.923 32.122 -4.431 1.00 17.14 ? 193 ASN A O 1 ATOM 1449 C CB . ASN A 1 193 ? 28.379 29.128 -3.227 1.00 16.99 ? 193 ASN A CB 1 ATOM 1450 C CG . ASN A 1 193 ? 27.509 27.929 -2.957 1.00 17.60 ? 193 ASN A CG 1 ATOM 1451 O OD1 . ASN A 1 193 ? 26.825 27.424 -3.856 1.00 18.90 ? 193 ASN A OD1 1 ATOM 1452 N ND2 . ASN A 1 193 ? 27.512 27.464 -1.709 1.00 15.23 ? 193 ASN A ND2 1 ATOM 1453 N N . MET A 1 194 ? 29.980 31.277 -4.748 1.00 16.79 ? 194 MET A N 1 ATOM 1454 C CA . MET A 1 194 ? 30.612 32.573 -4.676 1.00 17.59 ? 194 MET A CA 1 ATOM 1455 C C . MET A 1 194 ? 31.889 32.574 -5.477 1.00 17.37 ? 194 MET A C 1 ATOM 1456 O O . MET A 1 194 ? 32.431 31.511 -5.840 1.00 17.60 ? 194 MET A O 1 ATOM 1457 C CB . MET A 1 194 ? 30.907 32.959 -3.216 1.00 16.76 ? 194 MET A CB 1 ATOM 1458 C CG . MET A 1 194 ? 31.828 31.973 -2.485 1.00 17.44 ? 194 MET A CG 1 ATOM 1459 S SD . MET A 1 194 ? 32.302 32.526 -0.844 1.00 17.75 ? 194 MET A SD 1 ATOM 1460 C CE . MET A 1 194 ? 33.326 33.952 -1.211 1.00 15.91 ? 194 MET A CE 1 ATOM 1461 N N . ASP A 1 195 ? 32.362 33.783 -5.744 1.00 17.68 ? 195 ASP A N 1 ATOM 1462 C CA . ASP A 1 195 ? 33.632 33.962 -6.373 1.00 18.24 ? 195 ASP A CA 1 ATOM 1463 C C . ASP A 1 195 ? 34.718 33.774 -5.334 1.00 17.75 ? 195 ASP A C 1 ATOM 1464 O O . ASP A 1 195 ? 34.696 34.413 -4.283 1.00 18.78 ? 195 ASP A O 1 ATOM 1465 C CB . ASP A 1 195 ? 33.726 35.349 -6.999 1.00 18.92 ? 195 ASP A CB 1 ATOM 1466 C CG . ASP A 1 195 ? 35.053 35.575 -7.678 1.00 21.47 ? 195 ASP A CG 1 ATOM 1467 O OD1 . ASP A 1 195 ? 35.530 34.639 -8.362 1.00 21.73 ? 195 ASP A OD1 1 ATOM 1468 O OD2 . ASP A 1 195 ? 35.614 36.687 -7.519 1.00 27.02 ? 195 ASP A OD2 1 ATOM 1469 N N . ILE A 1 196 ? 35.644 32.869 -5.613 1.00 17.00 ? 196 ILE A N 1 ATOM 1470 C CA . ILE A 1 196 ? 36.778 32.623 -4.724 1.00 16.15 ? 196 ILE A CA 1 ATOM 1471 C C . ILE A 1 196 ? 38.006 32.854 -5.584 1.00 16.55 ? 196 ILE A C 1 ATOM 1472 O O . ILE A 1 196 ? 38.146 32.235 -6.643 1.00 17.14 ? 196 ILE A O 1 ATOM 1473 C CB . ILE A 1 196 ? 36.782 31.177 -4.152 1.00 15.79 ? 196 ILE A CB 1 ATOM 1474 C CG1 . ILE A 1 196 ? 35.475 30.888 -3.404 1.00 15.59 ? 196 ILE A CG1 1 ATOM 1475 C CG2 . ILE A 1 196 ? 37.978 30.981 -3.215 1.00 15.65 ? 196 ILE A CG2 1 ATOM 1476 C CD1 . ILE A 1 196 ? 35.275 29.405 -2.996 1.00 14.80 ? 196 ILE A CD1 1 ATOM 1477 N N . ASP A 1 197 ? 38.882 33.750 -5.150 1.00 15.52 ? 197 ASP A N 1 ATOM 1478 C CA . ASP A 1 197 ? 40.025 34.142 -5.974 1.00 15.58 ? 197 ASP A CA 1 ATOM 1479 C C . ASP A 1 197 ? 41.114 33.087 -6.008 1.00 15.14 ? 197 ASP A C 1 ATOM 1480 O O . ASP A 1 197 ? 41.762 32.888 -7.032 1.00 15.20 ? 197 ASP A O 1 ATOM 1481 C CB . ASP A 1 197 ? 40.589 35.463 -5.469 1.00 15.40 ? 197 ASP A CB 1 ATOM 1482 C CG . ASP A 1 197 ? 39.551 36.548 -5.478 1.00 17.82 ? 197 ASP A CG 1 ATOM 1483 O OD1 . ASP A 1 197 ? 39.458 37.251 -6.505 1.00 21.43 ? 197 ASP A OD1 1 ATOM 1484 O OD2 . ASP A 1 197 ? 38.803 36.669 -4.482 1.00 17.58 ? 197 ASP A OD2 1 ATOM 1485 N N . VAL A 1 198 ? 41.304 32.408 -4.882 1.00 14.24 ? 198 VAL A N 1 ATOM 1486 C CA . VAL A 1 198 ? 42.351 31.415 -4.766 1.00 14.48 ? 198 VAL A CA 1 ATOM 1487 C C . VAL A 1 198 ? 41.769 30.188 -4.086 1.00 14.26 ? 198 VAL A C 1 ATOM 1488 O O . VAL A 1 198 ? 41.218 30.284 -2.980 1.00 14.32 ? 198 VAL A O 1 ATOM 1489 C CB . VAL A 1 198 ? 43.546 31.931 -3.928 1.00 14.47 ? 198 VAL A CB 1 ATOM 1490 C CG1 . VAL A 1 198 ? 44.550 30.787 -3.674 1.00 15.35 ? 198 VAL A CG1 1 ATOM 1491 C CG2 . VAL A 1 198 ? 44.237 33.162 -4.606 1.00 14.90 ? 198 VAL A CG2 1 ATOM 1492 N N . ILE A 1 199 ? 41.901 29.038 -4.746 1.00 13.78 ? 199 ILE A N 1 ATOM 1493 C CA . ILE A 1 199 ? 41.455 27.771 -4.203 1.00 13.58 ? 199 ILE A CA 1 ATOM 1494 C C . ILE A 1 199 ? 42.606 26.788 -4.346 1.00 13.47 ? 199 ILE A C 1 ATOM 1495 O O . ILE A 1 199 ? 42.981 26.439 -5.470 1.00 13.07 ? 199 ILE A O 1 ATOM 1496 C CB . ILE A 1 199 ? 40.265 27.198 -5.000 1.00 13.65 ? 199 ILE A CB 1 ATOM 1497 C CG1 . ILE A 1 199 ? 39.042 28.123 -4.907 1.00 13.71 ? 199 ILE A CG1 1 ATOM 1498 C CG2 . ILE A 1 199 ? 39.927 25.789 -4.502 1.00 14.36 ? 199 ILE A CG2 1 ATOM 1499 C CD1 . ILE A 1 199 ? 38.060 27.928 -6.062 1.00 16.05 ? 199 ILE A CD1 1 ATOM 1500 N N . LEU A 1 200 ? 43.159 26.342 -3.222 1.00 12.51 ? 200 LEU A N 1 ATOM 1501 C CA . LEU A 1 200 ? 44.341 25.493 -3.248 1.00 12.53 ? 200 LEU A CA 1 ATOM 1502 C C . LEU A 1 200 ? 44.201 24.352 -2.259 1.00 12.42 ? 200 LEU A C 1 ATOM 1503 O O . LEU A 1 200 ? 43.925 24.578 -1.081 1.00 12.12 ? 200 LEU A O 1 ATOM 1504 C CB . LEU A 1 200 ? 45.611 26.294 -2.917 1.00 11.84 ? 200 LEU A CB 1 ATOM 1505 C CG . LEU A 1 200 ? 45.987 27.479 -3.815 1.00 11.03 ? 200 LEU A CG 1 ATOM 1506 C CD1 . LEU A 1 200 ? 47.182 28.234 -3.210 1.00 11.81 ? 200 LEU A CD1 1 ATOM 1507 C CD2 . LEU A 1 200 ? 46.280 27.017 -5.245 1.00 10.98 ? 200 LEU A CD2 1 ATOM 1508 N N . GLY A 1 201 ? 44.407 23.134 -2.751 1.00 12.50 ? 201 GLY A N 1 ATOM 1509 C CA . GLY A 1 201 ? 44.369 21.938 -1.903 1.00 12.11 ? 201 GLY A CA 1 ATOM 1510 C C . GLY A 1 201 ? 44.155 20.695 -2.730 1.00 12.67 ? 201 GLY A C 1 ATOM 1511 O O . GLY A 1 201 ? 44.558 20.647 -3.901 1.00 13.56 ? 201 GLY A O 1 ATOM 1512 N N . GLY A 1 202 ? 43.508 19.691 -2.149 1.00 12.87 ? 202 GLY A N 1 ATOM 1513 C CA . GLY A 1 202 ? 43.275 18.444 -2.880 1.00 13.33 ? 202 GLY A CA 1 ATOM 1514 C C . GLY A 1 202 ? 41.887 18.465 -3.481 1.00 13.88 ? 202 GLY A C 1 ATOM 1515 O O . GLY A 1 202 ? 41.214 19.507 -3.460 1.00 14.20 ? 202 GLY A O 1 ATOM 1516 N N . GLY A 1 203 ? 41.445 17.314 -3.986 1.00 14.06 ? 203 GLY A N 1 ATOM 1517 C CA . GLY A 1 203 ? 40.066 17.162 -4.450 1.00 14.62 ? 203 GLY A CA 1 ATOM 1518 C C . GLY A 1 203 ? 39.866 17.299 -5.950 1.00 15.75 ? 203 GLY A C 1 ATOM 1519 O O . GLY A 1 203 ? 38.801 17.722 -6.406 1.00 16.33 ? 203 GLY A O 1 ATOM 1520 N N . ARG A 1 204 ? 40.878 16.948 -6.734 1.00 16.10 ? 204 ARG A N 1 ATOM 1521 C CA . ARG A 1 204 ? 40.728 16.954 -8.183 1.00 16.87 ? 204 ARG A CA 1 ATOM 1522 C C . ARG A 1 204 ? 39.551 16.097 -8.655 1.00 17.06 ? 204 ARG A C 1 ATOM 1523 O O . ARG A 1 204 ? 38.814 16.495 -9.557 1.00 17.09 ? 204 ARG A O 1 ATOM 1524 C CB . ARG A 1 204 ? 41.983 16.415 -8.856 1.00 17.03 ? 204 ARG A CB 1 ATOM 1525 C CG . ARG A 1 204 ? 43.022 17.455 -9.121 1.00 17.51 ? 204 ARG A CG 1 ATOM 1526 C CD . ARG A 1 204 ? 44.006 17.011 -10.176 1.00 15.92 ? 204 ARG A CD 1 ATOM 1527 N NE . ARG A 1 204 ? 44.716 15.799 -9.778 1.00 17.28 ? 204 ARG A NE 1 ATOM 1528 C CZ . ARG A 1 204 ? 45.929 15.781 -9.239 1.00 17.43 ? 204 ARG A CZ 1 ATOM 1529 N NH1 . ARG A 1 204 ? 46.504 14.614 -8.942 1.00 16.57 ? 204 ARG A NH1 1 ATOM 1530 N NH2 . ARG A 1 204 ? 46.575 16.923 -9.018 1.00 16.73 ? 204 ARG A NH2 1 ATOM 1531 N N . LYS A 1 205 ? 39.393 14.925 -8.047 1.00 16.74 ? 205 LYS A N 1 ATOM 1532 C CA . LYS A 1 205 ? 38.557 13.880 -8.630 1.00 17.34 ? 205 LYS A CA 1 ATOM 1533 C C . LYS A 1 205 ? 37.090 14.283 -8.736 1.00 17.47 ? 205 LYS A C 1 ATOM 1534 O O . LYS A 1 205 ? 36.397 13.887 -9.672 1.00 17.55 ? 205 LYS A O 1 ATOM 1535 C CB . LYS A 1 205 ? 38.742 12.549 -7.892 1.00 17.42 ? 205 LYS A CB 1 ATOM 1536 C CG . LYS A 1 205 ? 38.201 12.451 -6.483 1.00 17.84 ? 205 LYS A CG 1 ATOM 1537 C CD . LYS A 1 205 ? 38.750 11.162 -5.878 1.00 19.21 ? 205 LYS A CD 1 ATOM 1538 C CE . LYS A 1 205 ? 38.117 10.832 -4.560 1.00 22.15 ? 205 LYS A CE 1 ATOM 1539 N NZ . LYS A 1 205 ? 38.633 9.513 -4.081 1.00 24.61 ? 205 LYS A NZ 1 ATOM 1540 N N . TYR A 1 206 ? 36.644 15.113 -7.789 1.00 17.13 ? 206 TYR A N 1 ATOM 1541 C CA . TYR A 1 206 ? 35.249 15.542 -7.715 1.00 17.08 ? 206 TYR A CA 1 ATOM 1542 C C . TYR A 1 206 ? 34.873 16.560 -8.788 1.00 16.94 ? 206 TYR A C 1 ATOM 1543 O O . TYR A 1 206 ? 33.710 16.913 -8.923 1.00 17.63 ? 206 TYR A O 1 ATOM 1544 C CB . TYR A 1 206 ? 34.963 16.121 -6.336 1.00 16.53 ? 206 TYR A CB 1 ATOM 1545 C CG . TYR A 1 206 ? 35.394 15.209 -5.209 1.00 16.28 ? 206 TYR A CG 1 ATOM 1546 C CD1 . TYR A 1 206 ? 36.335 15.629 -4.268 1.00 15.97 ? 206 TYR A CD1 1 ATOM 1547 C CD2 . TYR A 1 206 ? 34.858 13.924 -5.087 1.00 15.71 ? 206 TYR A CD2 1 ATOM 1548 C CE1 . TYR A 1 206 ? 36.738 14.780 -3.225 1.00 16.41 ? 206 TYR A CE1 1 ATOM 1549 C CE2 . TYR A 1 206 ? 35.244 13.071 -4.048 1.00 14.95 ? 206 TYR A CE2 1 ATOM 1550 C CZ . TYR A 1 206 ? 36.192 13.508 -3.124 1.00 15.24 ? 206 TYR A CZ 1 ATOM 1551 O OH . TYR A 1 206 ? 36.559 12.672 -2.092 1.00 15.91 ? 206 TYR A OH 1 ATOM 1552 N N . MET A 1 207 ? 35.860 17.038 -9.534 1.00 16.85 ? 207 MET A N 1 ATOM 1553 C CA . MET A 1 207 ? 35.650 18.114 -10.488 1.00 17.19 ? 207 MET A CA 1 ATOM 1554 C C . MET A 1 207 ? 35.414 17.597 -11.901 1.00 18.36 ? 207 MET A C 1 ATOM 1555 O O . MET A 1 207 ? 35.003 18.357 -12.782 1.00 19.04 ? 207 MET A O 1 ATOM 1556 C CB . MET A 1 207 ? 36.858 19.048 -10.495 1.00 17.04 ? 207 MET A CB 1 ATOM 1557 C CG . MET A 1 207 ? 37.243 19.566 -9.114 1.00 16.20 ? 207 MET A CG 1 ATOM 1558 S SD . MET A 1 207 ? 35.936 20.558 -8.350 1.00 17.25 ? 207 MET A SD 1 ATOM 1559 C CE . MET A 1 207 ? 36.203 22.120 -9.183 1.00 17.54 ? 207 MET A CE 1 ATOM 1560 N N . PHE A 1 208 ? 35.683 16.313 -12.116 1.00 18.85 ? 208 PHE A N 1 ATOM 1561 C CA . PHE A 1 208 ? 35.702 15.747 -13.463 1.00 19.38 ? 208 PHE A CA 1 ATOM 1562 C C . PHE A 1 208 ? 34.792 14.553 -13.616 1.00 20.57 ? 208 PHE A C 1 ATOM 1563 O O . PHE A 1 208 ? 34.559 13.803 -12.683 1.00 19.36 ? 208 PHE A O 1 ATOM 1564 C CB . PHE A 1 208 ? 37.125 15.354 -13.870 1.00 19.77 ? 208 PHE A CB 1 ATOM 1565 C CG . PHE A 1 208 ? 38.086 16.482 -13.805 1.00 19.52 ? 208 PHE A CG 1 ATOM 1566 C CD1 . PHE A 1 208 ? 38.170 17.399 -14.854 1.00 20.83 ? 208 PHE A CD1 1 ATOM 1567 C CD2 . PHE A 1 208 ? 38.882 16.662 -12.689 1.00 20.11 ? 208 PHE A CD2 1 ATOM 1568 C CE1 . PHE A 1 208 ? 39.039 18.464 -14.793 1.00 20.34 ? 208 PHE A CE1 1 ATOM 1569 C CE2 . PHE A 1 208 ? 39.772 17.743 -12.617 1.00 20.06 ? 208 PHE A CE2 1 ATOM 1570 C CZ . PHE A 1 208 ? 39.846 18.634 -13.675 1.00 19.98 ? 208 PHE A CZ 1 ATOM 1571 N N . ARG A 1 209 ? 34.310 14.361 -14.835 1.00 22.02 ? 209 ARG A N 1 ATOM 1572 C CA . ARG A 1 209 ? 33.345 13.320 -15.078 1.00 24.68 ? 209 ARG A CA 1 ATOM 1573 C C . ARG A 1 209 ? 34.010 11.969 -14.887 1.00 24.47 ? 209 ARG A C 1 ATOM 1574 O O . ARG A 1 209 ? 35.212 11.827 -15.102 1.00 23.26 ? 209 ARG A O 1 ATOM 1575 C CB . ARG A 1 209 ? 32.711 13.485 -16.461 1.00 24.32 ? 209 ARG A CB 1 ATOM 1576 C CG . ARG A 1 209 ? 33.629 13.339 -17.643 1.00 27.79 ? 209 ARG A CG 1 ATOM 1577 C CD . ARG A 1 209 ? 32.790 13.367 -18.941 1.00 28.75 ? 209 ARG A CD 1 ATOM 1578 N NE . ARG A 1 209 ? 33.559 12.959 -20.122 1.00 38.67 ? 209 ARG A NE 1 ATOM 1579 C CZ . ARG A 1 209 ? 34.242 13.798 -20.902 1.00 42.05 ? 209 ARG A CZ 1 ATOM 1580 N NH1 . ARG A 1 209 ? 34.264 15.103 -20.626 1.00 44.97 ? 209 ARG A NH1 1 ATOM 1581 N NH2 . ARG A 1 209 ? 34.909 13.335 -21.956 1.00 44.48 ? 209 ARG A NH2 1 ATOM 1582 N N . MET A 1 210 ? 33.224 11.015 -14.403 1.00 25.53 ? 210 MET A N 1 ATOM 1583 C CA . MET A 1 210 ? 33.647 9.636 -14.253 1.00 27.92 ? 210 MET A CA 1 ATOM 1584 C C . MET A 1 210 ? 34.329 9.180 -15.538 1.00 27.38 ? 210 MET A C 1 ATOM 1585 O O . MET A 1 210 ? 33.863 9.473 -16.646 1.00 27.27 ? 210 MET A O 1 ATOM 1586 C CB . MET A 1 210 ? 32.429 8.775 -13.936 1.00 27.99 ? 210 MET A CB 1 ATOM 1587 C CG . MET A 1 210 ? 32.725 7.355 -13.507 1.00 30.59 ? 210 MET A CG 1 ATOM 1588 S SD . MET A 1 210 ? 31.215 6.530 -12.977 1.00 32.88 ? 210 MET A SD 1 ATOM 1589 C CE . MET A 1 210 ? 30.142 6.813 -14.366 1.00 34.18 ? 210 MET A CE 1 ATOM 1590 N N . GLY A 1 211 ? 35.459 8.504 -15.388 1.00 27.39 ? 211 GLY A N 1 ATOM 1591 C CA . GLY A 1 211 ? 36.261 8.127 -16.545 1.00 27.06 ? 211 GLY A CA 1 ATOM 1592 C C . GLY A 1 211 ? 37.357 9.102 -16.944 1.00 26.40 ? 211 GLY A C 1 ATOM 1593 O O . GLY A 1 211 ? 38.181 8.778 -17.790 1.00 27.15 ? 211 GLY A O 1 ATOM 1594 N N . THR A 1 212 ? 37.391 10.294 -16.350 1.00 25.48 ? 212 THR A N 1 ATOM 1595 C CA . THR A 1 212 ? 38.484 11.228 -16.623 1.00 24.47 ? 212 THR A CA 1 ATOM 1596 C C . THR A 1 212 ? 39.720 10.798 -15.842 1.00 24.04 ? 212 THR A C 1 ATOM 1597 O O . THR A 1 212 ? 39.691 10.774 -14.610 1.00 24.00 ? 212 THR A O 1 ATOM 1598 C CB . THR A 1 212 ? 38.122 12.689 -16.228 1.00 23.96 ? 212 THR A CB 1 ATOM 1599 O OG1 . THR A 1 212 ? 36.881 13.060 -16.838 1.00 24.13 ? 212 THR A OG1 1 ATOM 1600 C CG2 . THR A 1 212 ? 39.226 13.673 -16.645 1.00 23.46 ? 212 THR A CG2 1 ATOM 1601 N N . PRO A 1 213 ? 40.811 10.458 -16.554 1.00 24.17 ? 213 PRO A N 1 ATOM 1602 C CA . PRO A 1 213 ? 42.033 10.076 -15.855 1.00 23.80 ? 213 PRO A CA 1 ATOM 1603 C C . PRO A 1 213 ? 42.536 11.240 -15.023 1.00 23.62 ? 213 PRO A C 1 ATOM 1604 O O . PRO A 1 213 ? 42.480 12.398 -15.463 1.00 23.90 ? 213 PRO A O 1 ATOM 1605 C CB . PRO A 1 213 ? 43.039 9.804 -16.985 1.00 24.29 ? 213 PRO A CB 1 ATOM 1606 C CG . PRO A 1 213 ? 42.239 9.668 -18.229 1.00 24.51 ? 213 PRO A CG 1 ATOM 1607 C CD . PRO A 1 213 ? 40.960 10.438 -18.022 1.00 24.09 ? 213 PRO A CD 1 ATOM 1608 N N . ASP A 1 214 ? 43.011 10.946 -13.821 1.00 23.22 ? 214 ASP A N 1 ATOM 1609 C CA . ASP A 1 214 ? 43.721 11.951 -13.046 1.00 23.01 ? 214 ASP A CA 1 ATOM 1610 C C . ASP A 1 214 ? 45.045 12.299 -13.779 1.00 23.05 ? 214 ASP A C 1 ATOM 1611 O O . ASP A 1 214 ? 45.711 11.391 -14.273 1.00 22.55 ? 214 ASP A O 1 ATOM 1612 C CB . ASP A 1 214 ? 43.991 11.426 -11.640 1.00 22.39 ? 214 ASP A CB 1 ATOM 1613 C CG . ASP A 1 214 ? 44.606 12.475 -10.757 1.00 22.02 ? 214 ASP A CG 1 ATOM 1614 O OD1 . ASP A 1 214 ? 45.850 12.500 -10.657 1.00 19.08 ? 214 ASP A OD1 1 ATOM 1615 O OD2 . ASP A 1 214 ? 43.837 13.300 -10.206 1.00 22.27 ? 214 ASP A OD2 1 ATOM 1616 N N . PRO A 1 215 ? 45.424 13.601 -13.864 1.00 23.32 ? 215 PRO A N 1 ATOM 1617 C CA . PRO A 1 215 ? 46.665 13.948 -14.593 1.00 23.38 ? 215 PRO A CA 1 ATOM 1618 C C . PRO A 1 215 ? 47.929 13.378 -13.955 1.00 23.42 ? 215 PRO A C 1 ATOM 1619 O O . PRO A 1 215 ? 48.945 13.198 -14.629 1.00 23.63 ? 215 PRO A O 1 ATOM 1620 C CB . PRO A 1 215 ? 46.705 15.486 -14.525 1.00 23.56 ? 215 PRO A CB 1 ATOM 1621 C CG . PRO A 1 215 ? 45.866 15.840 -13.352 1.00 23.03 ? 215 PRO A CG 1 ATOM 1622 C CD . PRO A 1 215 ? 44.763 14.808 -13.323 1.00 22.98 ? 215 PRO A CD 1 ATOM 1623 N N . GLU A 1 216 ? 47.864 13.087 -12.664 1.00 23.02 ? 216 GLU A N 1 ATOM 1624 C CA . GLU A 1 216 ? 49.042 12.675 -11.932 1.00 23.31 ? 216 GLU A CA 1 ATOM 1625 C C . GLU A 1 216 ? 49.091 11.162 -11.786 1.00 23.28 ? 216 GLU A C 1 ATOM 1626 O O . GLU A 1 216 ? 50.170 10.587 -11.669 1.00 24.33 ? 216 GLU A O 1 ATOM 1627 C CB . GLU A 1 216 ? 49.041 13.349 -10.569 1.00 22.79 ? 216 GLU A CB 1 ATOM 1628 C CG . GLU A 1 216 ? 50.339 13.298 -9.826 1.00 23.05 ? 216 GLU A CG 1 ATOM 1629 C CD . GLU A 1 216 ? 50.332 14.237 -8.634 1.00 22.08 ? 216 GLU A CD 1 ATOM 1630 O OE1 . GLU A 1 216 ? 49.303 14.902 -8.376 1.00 21.29 ? 216 GLU A OE1 1 ATOM 1631 O OE2 . GLU A 1 216 ? 51.352 14.320 -7.937 1.00 21.07 ? 216 GLU A OE2 1 ATOM 1632 N N . TYR A 1 217 ? 47.929 10.520 -11.804 1.00 23.41 ? 217 TYR A N 1 ATOM 1633 C CA . TYR A 1 217 ? 47.844 9.068 -11.661 1.00 24.14 ? 217 TYR A CA 1 ATOM 1634 C C . TYR A 1 217 ? 46.980 8.441 -12.764 1.00 25.30 ? 217 TYR A C 1 ATOM 1635 O O . TYR A 1 217 ? 46.008 7.745 -12.460 1.00 24.41 ? 217 TYR A O 1 ATOM 1636 C CB . TYR A 1 217 ? 47.269 8.699 -10.291 1.00 23.59 ? 217 TYR A CB 1 ATOM 1637 C CG . TYR A 1 217 ? 47.945 9.386 -9.140 1.00 23.46 ? 217 TYR A CG 1 ATOM 1638 C CD1 . TYR A 1 217 ? 49.125 8.870 -8.599 1.00 25.35 ? 217 TYR A CD1 1 ATOM 1639 C CD2 . TYR A 1 217 ? 47.412 10.551 -8.582 1.00 21.78 ? 217 TYR A CD2 1 ATOM 1640 C CE1 . TYR A 1 217 ? 49.765 9.495 -7.530 1.00 24.24 ? 217 TYR A CE1 1 ATOM 1641 C CE2 . TYR A 1 217 ? 48.052 11.197 -7.517 1.00 22.05 ? 217 TYR A CE2 1 ATOM 1642 C CZ . TYR A 1 217 ? 49.219 10.654 -6.990 1.00 24.06 ? 217 TYR A CZ 1 ATOM 1643 O OH . TYR A 1 217 ? 49.854 11.256 -5.938 1.00 22.92 ? 217 TYR A OH 1 ATOM 1644 N N . PRO A 1 218 ? 47.352 8.657 -14.048 1.00 26.77 ? 218 PRO A N 1 ATOM 1645 C CA . PRO A 1 218 ? 46.479 8.241 -15.171 1.00 27.79 ? 218 PRO A CA 1 ATOM 1646 C C . PRO A 1 218 ? 46.287 6.728 -15.265 1.00 28.53 ? 218 PRO A C 1 ATOM 1647 O O . PRO A 1 218 ? 45.345 6.255 -15.928 1.00 29.10 ? 218 PRO A O 1 ATOM 1648 C CB . PRO A 1 218 ? 47.233 8.746 -16.404 1.00 27.92 ? 218 PRO A CB 1 ATOM 1649 C CG . PRO A 1 218 ? 48.671 8.800 -15.972 1.00 27.46 ? 218 PRO A CG 1 ATOM 1650 C CD . PRO A 1 218 ? 48.604 9.271 -14.536 1.00 27.06 ? 218 PRO A CD 1 ATOM 1651 N N . ASP A 1 219 ? 47.171 5.995 -14.595 1.00 28.68 ? 219 ASP A N 1 ATOM 1652 C CA . ASP A 1 219 ? 47.155 4.541 -14.568 1.00 29.25 ? 219 ASP A CA 1 ATOM 1653 C C . ASP A 1 219 ? 46.505 3.975 -13.309 1.00 28.51 ? 219 ASP A C 1 ATOM 1654 O O . ASP A 1 219 ? 46.533 2.765 -13.085 1.00 29.43 ? 219 ASP A O 1 ATOM 1655 C CB . ASP A 1 219 ? 48.591 4.019 -14.687 1.00 30.26 ? 219 ASP A CB 1 ATOM 1656 C CG . ASP A 1 219 ? 49.498 4.546 -13.585 1.00 33.61 ? 219 ASP A CG 1 ATOM 1657 O OD1 . ASP A 1 219 ? 50.504 3.865 -13.287 1.00 39.02 ? 219 ASP A OD1 1 ATOM 1658 O OD2 . ASP A 1 219 ? 49.212 5.628 -13.013 1.00 36.45 ? 219 ASP A OD2 1 ATOM 1659 N N . ASP A 1 220 ? 45.946 4.841 -12.465 1.00 26.82 ? 220 ASP A N 1 ATOM 1660 C CA . ASP A 1 220 ? 45.167 4.366 -11.336 1.00 25.58 ? 220 ASP A CA 1 ATOM 1661 C C . ASP A 1 220 ? 43.736 4.853 -11.494 1.00 24.01 ? 220 ASP A C 1 ATOM 1662 O O . ASP A 1 220 ? 43.426 6.010 -11.195 1.00 23.26 ? 220 ASP A O 1 ATOM 1663 C CB . ASP A 1 220 ? 45.759 4.851 -10.011 1.00 25.89 ? 220 ASP A CB 1 ATOM 1664 C CG . ASP A 1 220 ? 45.021 4.307 -8.798 1.00 27.23 ? 220 ASP A CG 1 ATOM 1665 O OD1 . ASP A 1 220 ? 45.477 4.602 -7.670 1.00 28.41 ? 220 ASP A OD1 1 ATOM 1666 O OD2 . ASP A 1 220 ? 43.987 3.606 -8.950 1.00 28.23 ? 220 ASP A OD2 1 ATOM 1667 N N . TYR A 1 221 ? 42.868 3.965 -11.973 1.00 22.14 ? 221 TYR A N 1 ATOM 1668 C CA . TYR A 1 221 ? 41.495 4.342 -12.302 1.00 20.97 ? 221 TYR A CA 1 ATOM 1669 C C . TYR A 1 221 ? 40.733 4.870 -11.083 1.00 21.21 ? 221 TYR A C 1 ATOM 1670 O O . TYR A 1 221 ? 39.864 5.736 -11.220 1.00 20.88 ? 221 TYR A O 1 ATOM 1671 C CB . TYR A 1 221 ? 40.739 3.162 -12.925 1.00 19.97 ? 221 TYR A CB 1 ATOM 1672 C CG . TYR A 1 221 ? 41.322 2.641 -14.226 1.00 17.93 ? 221 TYR A CG 1 ATOM 1673 C CD1 . TYR A 1 221 ? 42.362 3.316 -14.892 1.00 16.59 ? 221 TYR A CD1 1 ATOM 1674 C CD2 . TYR A 1 221 ? 40.790 1.507 -14.828 1.00 16.31 ? 221 TYR A CD2 1 ATOM 1675 C CE1 . TYR A 1 221 ? 42.882 2.833 -16.096 1.00 16.94 ? 221 TYR A CE1 1 ATOM 1676 C CE2 . TYR A 1 221 ? 41.283 1.037 -16.029 1.00 16.50 ? 221 TYR A CE2 1 ATOM 1677 C CZ . TYR A 1 221 ? 42.321 1.702 -16.659 1.00 17.17 ? 221 TYR A CZ 1 ATOM 1678 O OH . TYR A 1 221 ? 42.808 1.211 -17.842 1.00 16.99 ? 221 TYR A OH 1 ATOM 1679 N N . SER A 1 222 ? 41.079 4.355 -9.899 1.00 21.23 ? 222 SER A N 1 ATOM 1680 C CA . SER A 1 222 ? 40.421 4.764 -8.650 1.00 21.94 ? 222 SER A CA 1 ATOM 1681 C C . SER A 1 222 ? 40.613 6.256 -8.341 1.00 21.55 ? 222 SER A C 1 ATOM 1682 O O . SER A 1 222 ? 39.840 6.833 -7.574 1.00 21.98 ? 222 SER A O 1 ATOM 1683 C CB . SER A 1 222 ? 40.881 3.904 -7.471 1.00 21.75 ? 222 SER A CB 1 ATOM 1684 O OG . SER A 1 222 ? 42.202 4.239 -7.088 1.00 23.89 ? 222 SER A OG 1 ATOM 1685 N N . GLN A 1 223 ? 41.628 6.864 -8.959 1.00 21.09 ? 223 GLN A N 1 ATOM 1686 C CA . GLN A 1 223 ? 41.947 8.276 -8.766 1.00 21.10 ? 223 GLN A CA 1 ATOM 1687 C C . GLN A 1 223 ? 41.239 9.190 -9.754 1.00 20.71 ? 223 GLN A C 1 ATOM 1688 O O . GLN A 1 223 ? 41.373 10.417 -9.665 1.00 20.63 ? 223 GLN A O 1 ATOM 1689 C CB . GLN A 1 223 ? 43.459 8.508 -8.873 1.00 21.27 ? 223 GLN A CB 1 ATOM 1690 C CG . GLN A 1 223 ? 44.278 7.668 -7.915 1.00 23.10 ? 223 GLN A CG 1 ATOM 1691 C CD . GLN A 1 223 ? 43.755 7.726 -6.486 1.00 25.70 ? 223 GLN A CD 1 ATOM 1692 O OE1 . GLN A 1 223 ? 43.390 8.787 -5.980 1.00 26.79 ? 223 GLN A OE1 1 ATOM 1693 N NE2 . GLN A 1 223 ? 43.714 6.579 -5.834 1.00 26.67 ? 223 GLN A NE2 1 ATOM 1694 N N . GLY A 1 224 ? 40.503 8.596 -10.699 1.00 20.19 ? 224 GLY A N 1 ATOM 1695 C CA . GLY A 1 224 ? 39.852 9.367 -11.764 1.00 19.74 ? 224 GLY A CA 1 ATOM 1696 C C . GLY A 1 224 ? 38.654 10.187 -11.318 1.00 19.82 ? 224 GLY A C 1 ATOM 1697 O O . GLY A 1 224 ? 38.243 10.141 -10.144 1.00 19.34 ? 224 GLY A O 1 ATOM 1698 N N . GLY A 1 225 ? 38.095 10.940 -12.269 1.00 19.68 ? 225 GLY A N 1 ATOM 1699 C CA . GLY A 1 225 ? 36.869 11.695 -12.062 1.00 19.64 ? 225 GLY A CA 1 ATOM 1700 C C . GLY A 1 225 ? 35.757 10.850 -11.462 1.00 20.11 ? 225 GLY A C 1 ATOM 1701 O O . GLY A 1 225 ? 35.641 9.640 -11.737 1.00 20.31 ? 225 GLY A O 1 ATOM 1702 N N . THR A 1 226 ? 34.928 11.502 -10.649 1.00 19.75 ? 226 THR A N 1 ATOM 1703 C CA . THR A 1 226 ? 33.842 10.830 -9.962 1.00 19.51 ? 226 THR A CA 1 ATOM 1704 C C . THR A 1 226 ? 32.489 11.237 -10.506 1.00 19.25 ? 226 THR A C 1 ATOM 1705 O O . THR A 1 226 ? 31.506 10.601 -10.190 1.00 18.95 ? 226 THR A O 1 ATOM 1706 C CB . THR A 1 226 ? 33.818 11.189 -8.464 1.00 19.21 ? 226 THR A CB 1 ATOM 1707 O OG1 . THR A 1 226 ? 33.512 12.583 -8.334 1.00 19.55 ? 226 THR A OG1 1 ATOM 1708 C CG2 . THR A 1 226 ? 35.153 10.863 -7.784 1.00 20.56 ? 226 THR A CG2 1 ATOM 1709 N N . ARG A 1 227 ? 32.431 12.309 -11.296 1.00 19.62 ? 227 ARG A N 1 ATOM 1710 C CA . ARG A 1 227 ? 31.149 12.967 -11.551 1.00 20.43 ? 227 ARG A CA 1 ATOM 1711 C C . ARG A 1 227 ? 30.250 12.170 -12.457 1.00 21.21 ? 227 ARG A C 1 ATOM 1712 O O . ARG A 1 227 ? 30.706 11.538 -13.409 1.00 21.81 ? 227 ARG A O 1 ATOM 1713 C CB . ARG A 1 227 ? 31.328 14.376 -12.109 1.00 19.96 ? 227 ARG A CB 1 ATOM 1714 C CG . ARG A 1 227 ? 32.041 15.299 -11.154 1.00 19.49 ? 227 ARG A CG 1 ATOM 1715 C CD . ARG A 1 227 ? 31.804 16.753 -11.495 1.00 18.42 ? 227 ARG A CD 1 ATOM 1716 N NE . ARG A 1 227 ? 30.421 17.129 -11.216 1.00 17.77 ? 227 ARG A NE 1 ATOM 1717 C CZ . ARG A 1 227 ? 29.929 17.406 -10.009 1.00 16.86 ? 227 ARG A CZ 1 ATOM 1718 N NH1 . ARG A 1 227 ? 30.707 17.356 -8.926 1.00 14.03 ? 227 ARG A NH1 1 ATOM 1719 N NH2 . ARG A 1 227 ? 28.645 17.741 -9.891 1.00 15.83 ? 227 ARG A NH2 1 ATOM 1720 N N . LEU A 1 228 ? 28.965 12.196 -12.141 1.00 22.15 ? 228 LEU A N 1 ATOM 1721 C CA . LEU A 1 228 ? 27.989 11.451 -12.913 1.00 23.46 ? 228 LEU A CA 1 ATOM 1722 C C . LEU A 1 228 ? 27.255 12.372 -13.891 1.00 23.39 ? 228 LEU A C 1 ATOM 1723 O O . LEU A 1 228 ? 26.589 11.900 -14.811 1.00 23.36 ? 228 LEU A O 1 ATOM 1724 C CB . LEU A 1 228 ? 27.021 10.719 -11.972 1.00 24.12 ? 228 LEU A CB 1 ATOM 1725 C CG . LEU A 1 228 ? 27.633 9.740 -10.956 1.00 25.62 ? 228 LEU A CG 1 ATOM 1726 C CD1 . LEU A 1 228 ? 26.539 8.981 -10.206 1.00 30.14 ? 228 LEU A CD1 1 ATOM 1727 C CD2 . LEU A 1 228 ? 28.568 8.758 -11.620 1.00 28.09 ? 228 LEU A CD2 1 ATOM 1728 N N . ASP A 1 229 ? 27.393 13.682 -13.698 1.00 23.17 ? 229 ASP A N 1 ATOM 1729 C CA . ASP A 1 229 ? 26.647 14.656 -14.518 1.00 23.53 ? 229 ASP A CA 1 ATOM 1730 C C . ASP A 1 229 ? 27.393 15.100 -15.776 1.00 23.65 ? 229 ASP A C 1 ATOM 1731 O O . ASP A 1 229 ? 26.935 15.994 -16.486 1.00 24.05 ? 229 ASP A O 1 ATOM 1732 C CB . ASP A 1 229 ? 26.202 15.870 -13.687 1.00 23.06 ? 229 ASP A CB 1 ATOM 1733 C CG . ASP A 1 229 ? 27.369 16.594 -13.012 1.00 22.80 ? 229 ASP A CG 1 ATOM 1734 O OD1 . ASP A 1 229 ? 28.539 16.251 -13.268 1.00 21.77 ? 229 ASP A OD1 1 ATOM 1735 O OD2 . ASP A 1 229 ? 27.107 17.509 -12.211 1.00 23.73 ? 229 ASP A OD2 1 ATOM 1736 N N . GLY A 1 230 ? 28.539 14.484 -16.049 1.00 23.28 ? 230 GLY A N 1 ATOM 1737 C CA . GLY A 1 230 ? 29.312 14.822 -17.239 1.00 23.46 ? 230 GLY A CA 1 ATOM 1738 C C . GLY A 1 230 ? 29.985 16.185 -17.226 1.00 23.41 ? 230 GLY A C 1 ATOM 1739 O O . GLY A 1 230 ? 30.582 16.578 -18.224 1.00 23.49 ? 230 GLY A O 1 ATOM 1740 N N . LYS A 1 231 ? 29.895 16.912 -16.108 1.00 23.01 ? 231 LYS A N 1 ATOM 1741 C CA . LYS A 1 231 ? 30.477 18.257 -16.028 1.00 22.88 ? 231 LYS A CA 1 ATOM 1742 C C . LYS A 1 231 ? 31.958 18.243 -15.715 1.00 22.30 ? 231 LYS A C 1 ATOM 1743 O O . LYS A 1 231 ? 32.448 17.406 -14.954 1.00 22.50 ? 231 LYS A O 1 ATOM 1744 C CB . LYS A 1 231 ? 29.781 19.100 -14.962 1.00 22.98 ? 231 LYS A CB 1 ATOM 1745 C CG . LYS A 1 231 ? 28.317 19.328 -15.235 1.00 25.61 ? 231 LYS A CG 1 ATOM 1746 C CD . LYS A 1 231 ? 27.746 20.211 -14.172 1.00 29.15 ? 231 LYS A CD 1 ATOM 1747 C CE . LYS A 1 231 ? 26.261 20.407 -14.386 1.00 32.78 ? 231 LYS A CE 1 ATOM 1748 N NZ . LYS A 1 231 ? 25.667 21.169 -13.246 1.00 36.22 ? 231 LYS A NZ 1 ATOM 1749 N N . ASN A 1 232 ? 32.659 19.191 -16.316 1.00 21.41 ? 232 ASN A N 1 ATOM 1750 C CA . ASN A 1 232 ? 34.014 19.486 -15.957 1.00 20.53 ? 232 ASN A CA 1 ATOM 1751 C C . ASN A 1 232 ? 33.924 20.792 -15.185 1.00 19.78 ? 232 ASN A C 1 ATOM 1752 O O . ASN A 1 232 ? 33.806 21.867 -15.776 1.00 19.47 ? 232 ASN A O 1 ATOM 1753 C CB . ASN A 1 232 ? 34.872 19.642 -17.219 1.00 20.45 ? 232 ASN A CB 1 ATOM 1754 C CG . ASN A 1 232 ? 36.327 19.903 -16.905 1.00 21.05 ? 232 ASN A CG 1 ATOM 1755 O OD1 . ASN A 1 232 ? 36.660 20.527 -15.891 1.00 22.17 ? 232 ASN A OD1 1 ATOM 1756 N ND2 . ASN A 1 232 ? 37.210 19.417 -17.764 1.00 22.45 ? 232 ASN A ND2 1 ATOM 1757 N N . LEU A 1 233 ? 33.955 20.695 -13.859 1.00 19.06 ? 233 LEU A N 1 ATOM 1758 C CA . LEU A 1 233 ? 33.765 21.876 -13.021 1.00 18.82 ? 233 LEU A CA 1 ATOM 1759 C C . LEU A 1 233 ? 34.953 22.828 -13.081 1.00 18.83 ? 233 LEU A C 1 ATOM 1760 O O . LEU A 1 233 ? 34.805 24.039 -12.859 1.00 18.51 ? 233 LEU A O 1 ATOM 1761 C CB . LEU A 1 233 ? 33.486 21.474 -11.579 1.00 18.63 ? 233 LEU A CB 1 ATOM 1762 C CG . LEU A 1 233 ? 32.211 20.662 -11.304 1.00 18.64 ? 233 LEU A CG 1 ATOM 1763 C CD1 . LEU A 1 233 ? 32.074 20.460 -9.823 1.00 17.25 ? 233 LEU A CD1 1 ATOM 1764 C CD2 . LEU A 1 233 ? 30.941 21.334 -11.879 1.00 18.98 ? 233 LEU A CD2 1 ATOM 1765 N N . VAL A 1 234 ? 36.132 22.286 -13.367 1.00 18.87 ? 234 VAL A N 1 ATOM 1766 C CA . VAL A 1 234 ? 37.313 23.135 -13.557 1.00 19.99 ? 234 VAL A CA 1 ATOM 1767 C C . VAL A 1 234 ? 37.126 24.020 -14.800 1.00 21.07 ? 234 VAL A C 1 ATOM 1768 O O . VAL A 1 234 ? 37.293 25.238 -14.747 1.00 21.03 ? 234 VAL A O 1 ATOM 1769 C CB . VAL A 1 234 ? 38.620 22.323 -13.633 1.00 19.81 ? 234 VAL A CB 1 ATOM 1770 C CG1 . VAL A 1 234 ? 39.768 23.223 -14.021 1.00 20.41 ? 234 VAL A CG1 1 ATOM 1771 C CG2 . VAL A 1 234 ? 38.929 21.660 -12.287 1.00 19.05 ? 234 VAL A CG2 1 ATOM 1772 N N . GLN A 1 235 ? 36.734 23.397 -15.903 1.00 22.41 ? 235 GLN A N 1 ATOM 1773 C CA . GLN A 1 235 ? 36.472 24.115 -17.136 1.00 24.92 ? 235 GLN A CA 1 ATOM 1774 C C . GLN A 1 235 ? 35.379 25.176 -16.928 1.00 23.97 ? 235 GLN A C 1 ATOM 1775 O O . GLN A 1 235 ? 35.519 26.330 -17.365 1.00 24.22 ? 235 GLN A O 1 ATOM 1776 C CB . GLN A 1 235 ? 36.089 23.113 -18.214 1.00 24.92 ? 235 GLN A CB 1 ATOM 1777 C CG . GLN A 1 235 ? 35.776 23.709 -19.567 1.00 28.39 ? 235 GLN A CG 1 ATOM 1778 C CD . GLN A 1 235 ? 35.567 22.636 -20.631 1.00 29.21 ? 235 GLN A CD 1 ATOM 1779 O OE1 . GLN A 1 235 ? 35.904 22.841 -21.809 1.00 37.35 ? 235 GLN A OE1 1 ATOM 1780 N NE2 . GLN A 1 235 ? 35.029 21.480 -20.226 1.00 33.84 ? 235 GLN A NE2 1 ATOM 1781 N N . GLU A 1 236 ? 34.313 24.799 -16.237 1.00 23.37 ? 236 GLU A N 1 ATOM 1782 C CA . GLU A 1 236 ? 33.229 25.734 -15.945 1.00 23.56 ? 236 GLU A CA 1 ATOM 1783 C C . GLU A 1 236 ? 33.709 26.940 -15.134 1.00 22.92 ? 236 GLU A C 1 ATOM 1784 O O . GLU A 1 236 ? 33.399 28.074 -15.459 1.00 22.51 ? 236 GLU A O 1 ATOM 1785 C CB . GLU A 1 236 ? 32.076 25.021 -15.239 1.00 23.67 ? 236 GLU A CB 1 ATOM 1786 C CG . GLU A 1 236 ? 31.387 23.963 -16.109 1.00 24.57 ? 236 GLU A CG 1 ATOM 1787 C CD . GLU A 1 236 ? 30.086 23.467 -15.497 1.00 26.01 ? 236 GLU A CD 1 ATOM 1788 O OE1 . GLU A 1 236 ? 29.539 24.169 -14.617 1.00 28.98 ? 236 GLU A OE1 1 ATOM 1789 O OE2 . GLU A 1 236 ? 29.610 22.380 -15.891 1.00 29.49 ? 236 GLU A OE2 1 ATOM 1790 N N . TRP A 1 237 ? 34.505 26.683 -14.108 1.00 22.47 ? 237 TRP A N 1 ATOM 1791 C CA . TRP A 1 237 ? 35.075 27.737 -13.275 1.00 22.39 ? 237 TRP A CA 1 ATOM 1792 C C . TRP A 1 237 ? 35.983 28.673 -14.081 1.00 22.84 ? 237 TRP A C 1 ATOM 1793 O O . TRP A 1 237 ? 35.889 29.890 -13.979 1.00 22.30 ? 237 TRP A O 1 ATOM 1794 C CB . TRP A 1 237 ? 35.856 27.098 -12.131 1.00 21.80 ? 237 TRP A CB 1 ATOM 1795 C CG . TRP A 1 237 ? 36.318 28.069 -11.084 1.00 22.44 ? 237 TRP A CG 1 ATOM 1796 C CD1 . TRP A 1 237 ? 35.570 28.587 -10.058 1.00 22.80 ? 237 TRP A CD1 1 ATOM 1797 C CD2 . TRP A 1 237 ? 37.628 28.623 -10.946 1.00 22.34 ? 237 TRP A CD2 1 ATOM 1798 N NE1 . TRP A 1 237 ? 36.347 29.427 -9.285 1.00 22.87 ? 237 TRP A NE1 1 ATOM 1799 C CE2 . TRP A 1 237 ? 37.611 29.464 -9.809 1.00 21.90 ? 237 TRP A CE2 1 ATOM 1800 C CE3 . TRP A 1 237 ? 38.825 28.481 -11.666 1.00 23.15 ? 237 TRP A CE3 1 ATOM 1801 C CZ2 . TRP A 1 237 ? 38.742 30.165 -9.378 1.00 22.32 ? 237 TRP A CZ2 1 ATOM 1802 C CZ3 . TRP A 1 237 ? 39.951 29.188 -11.236 1.00 21.51 ? 237 TRP A CZ3 1 ATOM 1803 C CH2 . TRP A 1 237 ? 39.899 30.011 -10.102 1.00 21.80 ? 237 TRP A CH2 1 ATOM 1804 N N . LEU A 1 238 ? 36.859 28.092 -14.886 1.00 23.55 ? 238 LEU A N 1 ATOM 1805 C CA . LEU A 1 238 ? 37.744 28.869 -15.744 1.00 24.77 ? 238 LEU A CA 1 ATOM 1806 C C . LEU A 1 238 ? 36.984 29.737 -16.734 1.00 25.98 ? 238 LEU A C 1 ATOM 1807 O O . LEU A 1 238 ? 37.351 30.882 -16.972 1.00 25.52 ? 238 LEU A O 1 ATOM 1808 C CB . LEU A 1 238 ? 38.658 27.942 -16.526 1.00 24.57 ? 238 LEU A CB 1 ATOM 1809 C CG . LEU A 1 238 ? 39.707 27.173 -15.728 1.00 24.54 ? 238 LEU A CG 1 ATOM 1810 C CD1 . LEU A 1 238 ? 40.340 26.139 -16.643 1.00 24.69 ? 238 LEU A CD1 1 ATOM 1811 C CD2 . LEU A 1 238 ? 40.753 28.090 -15.092 1.00 25.50 ? 238 LEU A CD2 1 ATOM 1812 N N . ALA A 1 239 ? 35.924 29.177 -17.303 1.00 27.51 ? 239 ALA A N 1 ATOM 1813 C CA . ALA A 1 239 ? 35.167 29.857 -18.348 1.00 29.77 ? 239 ALA A CA 1 ATOM 1814 C C . ALA A 1 239 ? 34.471 31.107 -17.810 1.00 31.28 ? 239 ALA A C 1 ATOM 1815 O O . ALA A 1 239 ? 34.233 32.053 -18.556 1.00 32.35 ? 239 ALA A O 1 ATOM 1816 C CB . ALA A 1 239 ? 34.168 28.905 -18.984 1.00 29.17 ? 239 ALA A CB 1 ATOM 1817 N N . LYS A 1 240 ? 34.161 31.107 -16.517 1.00 33.19 ? 240 LYS A N 1 ATOM 1818 C CA . LYS A 1 240 ? 33.478 32.226 -15.874 1.00 35.40 ? 240 LYS A CA 1 ATOM 1819 C C . LYS A 1 240 ? 34.364 33.452 -15.593 1.00 36.12 ? 240 LYS A C 1 ATOM 1820 O O . LYS A 1 240 ? 33.846 34.517 -15.263 1.00 36.85 ? 240 LYS A O 1 ATOM 1821 C CB . LYS A 1 240 ? 32.834 31.762 -14.568 1.00 35.58 ? 240 LYS A CB 1 ATOM 1822 C CG . LYS A 1 240 ? 31.325 31.653 -14.606 1.00 38.60 ? 240 LYS A CG 1 ATOM 1823 C CD . LYS A 1 240 ? 30.787 31.213 -13.247 1.00 42.07 ? 240 LYS A CD 1 ATOM 1824 C CE . LYS A 1 240 ? 29.260 31.298 -13.144 1.00 44.21 ? 240 LYS A CE 1 ATOM 1825 N NZ . LYS A 1 240 ? 28.783 30.795 -11.812 1.00 44.39 ? 240 LYS A NZ 1 ATOM 1826 N N . ARG A 1 241 ? 35.686 33.316 -15.721 1.00 36.77 ? 241 ARG A N 1 ATOM 1827 C CA . ARG A 1 241 ? 36.608 34.329 -15.190 1.00 36.82 ? 241 ARG A CA 1 ATOM 1828 C C . ARG A 1 241 ? 37.795 34.549 -16.104 1.00 36.93 ? 241 ARG A C 1 ATOM 1829 O O . ARG A 1 241 ? 38.535 33.614 -16.402 1.00 37.44 ? 241 ARG A O 1 ATOM 1830 C CB . ARG A 1 241 ? 37.113 33.898 -13.809 1.00 36.95 ? 241 ARG A CB 1 ATOM 1831 C CG . ARG A 1 241 ? 36.445 32.660 -13.298 1.00 36.81 ? 241 ARG A CG 1 ATOM 1832 C CD . ARG A 1 241 ? 36.871 32.258 -11.904 1.00 36.24 ? 241 ARG A CD 1 ATOM 1833 N NE . ARG A 1 241 ? 35.843 32.572 -10.916 1.00 36.11 ? 241 ARG A NE 1 ATOM 1834 C CZ . ARG A 1 241 ? 34.639 32.004 -10.871 1.00 36.22 ? 241 ARG A CZ 1 ATOM 1835 N NH1 . ARG A 1 241 ? 33.782 32.361 -9.926 1.00 35.32 ? 241 ARG A NH1 1 ATOM 1836 N NH2 . ARG A 1 241 ? 34.284 31.086 -11.772 1.00 34.58 ? 241 ARG A NH2 1 ATOM 1837 N N . GLN A 1 242 ? 37.992 35.782 -16.553 1.00 36.70 ? 242 GLN A N 1 ATOM 1838 C CA . GLN A 1 242 ? 39.187 36.085 -17.335 1.00 36.50 ? 242 GLN A CA 1 ATOM 1839 C C . GLN A 1 242 ? 40.384 36.200 -16.382 1.00 34.68 ? 242 GLN A C 1 ATOM 1840 O O . GLN A 1 242 ? 40.281 36.814 -15.326 1.00 35.15 ? 242 GLN A O 1 ATOM 1841 C CB . GLN A 1 242 ? 39.010 37.378 -18.134 1.00 37.31 ? 242 GLN A CB 1 ATOM 1842 C CG . GLN A 1 242 ? 40.172 37.677 -19.081 1.00 41.00 ? 242 GLN A CG 1 ATOM 1843 C CD . GLN A 1 242 ? 40.497 39.161 -19.159 1.00 45.53 ? 242 GLN A CD 1 ATOM 1844 O OE1 . GLN A 1 242 ? 40.222 39.923 -18.226 1.00 48.17 ? 242 GLN A OE1 1 ATOM 1845 N NE2 . GLN A 1 242 ? 41.101 39.577 -20.273 1.00 47.54 ? 242 GLN A NE2 1 ATOM 1846 N N . GLY A 1 243 ? 41.510 35.610 -16.763 1.00 32.82 ? 243 GLY A N 1 ATOM 1847 C CA . GLY A 1 243 ? 42.696 35.617 -15.919 1.00 30.51 ? 243 GLY A CA 1 ATOM 1848 C C . GLY A 1 243 ? 42.668 34.470 -14.928 1.00 28.56 ? 243 GLY A C 1 ATOM 1849 O O . GLY A 1 243 ? 43.459 34.436 -13.985 1.00 28.84 ? 243 GLY A O 1 ATOM 1850 N N . ALA A 1 244 ? 41.741 33.541 -15.131 1.00 26.35 ? 244 ALA A N 1 ATOM 1851 C CA . ALA A 1 244 ? 41.649 32.352 -14.291 1.00 24.37 ? 244 ALA A CA 1 ATOM 1852 C C . ALA A 1 244 ? 42.634 31.302 -14.781 1.00 23.82 ? 244 ALA A C 1 ATOM 1853 O O . ALA A 1 244 ? 42.837 31.146 -15.993 1.00 22.77 ? 244 ALA A O 1 ATOM 1854 C CB . ALA A 1 244 ? 40.246 31.799 -14.306 1.00 24.31 ? 244 ALA A CB 1 ATOM 1855 N N . ARG A 1 245 ? 43.234 30.585 -13.830 1.00 21.84 ? 245 ARG A N 1 ATOM 1856 C CA . ARG A 1 245 ? 44.215 29.555 -14.125 1.00 21.50 ? 245 ARG A CA 1 ATOM 1857 C C . ARG A 1 245 ? 43.933 28.344 -13.236 1.00 19.98 ? 245 ARG A C 1 ATOM 1858 O O . ARG A 1 245 ? 43.603 28.488 -12.059 1.00 18.96 ? 245 ARG A O 1 ATOM 1859 C CB . ARG A 1 245 ? 45.633 30.106 -13.874 1.00 21.98 ? 245 ARG A CB 1 ATOM 1860 C CG . ARG A 1 245 ? 46.781 29.085 -13.973 1.00 25.83 ? 245 ARG A CG 1 ATOM 1861 C CD . ARG A 1 245 ? 47.416 29.016 -15.364 1.00 31.07 ? 245 ARG A CD 1 ATOM 1862 N NE . ARG A 1 245 ? 47.756 30.333 -15.904 1.00 34.60 ? 245 ARG A NE 1 ATOM 1863 C CZ . ARG A 1 245 ? 48.956 30.915 -15.825 1.00 35.96 ? 245 ARG A CZ 1 ATOM 1864 N NH1 . ARG A 1 245 ? 49.968 30.313 -15.214 1.00 35.96 ? 245 ARG A NH1 1 ATOM 1865 N NH2 . ARG A 1 245 ? 49.145 32.116 -16.362 1.00 36.08 ? 245 ARG A NH2 1 ATOM 1866 N N . TYR A 1 246 ? 44.037 27.162 -13.821 1.00 18.87 ? 246 TYR A N 1 ATOM 1867 C CA . TYR A 1 246 ? 43.973 25.922 -13.084 1.00 18.52 ? 246 TYR A CA 1 ATOM 1868 C C . TYR A 1 246 ? 45.333 25.255 -13.135 1.00 18.64 ? 246 TYR A C 1 ATOM 1869 O O . TYR A 1 246 ? 45.947 25.170 -14.200 1.00 18.91 ? 246 TYR A O 1 ATOM 1870 C CB . TYR A 1 246 ? 42.937 25.004 -13.714 1.00 18.67 ? 246 TYR A CB 1 ATOM 1871 C CG . TYR A 1 246 ? 42.961 23.582 -13.190 1.00 18.97 ? 246 TYR A CG 1 ATOM 1872 C CD1 . TYR A 1 246 ? 42.538 23.286 -11.893 1.00 18.60 ? 246 TYR A CD1 1 ATOM 1873 C CD2 . TYR A 1 246 ? 43.387 22.533 -13.999 1.00 19.51 ? 246 TYR A CD2 1 ATOM 1874 C CE1 . TYR A 1 246 ? 42.531 21.967 -11.419 1.00 19.12 ? 246 TYR A CE1 1 ATOM 1875 C CE2 . TYR A 1 246 ? 43.387 21.212 -13.529 1.00 18.80 ? 246 TYR A CE2 1 ATOM 1876 C CZ . TYR A 1 246 ? 42.959 20.945 -12.244 1.00 19.02 ? 246 TYR A CZ 1 ATOM 1877 O OH . TYR A 1 246 ? 42.953 19.647 -11.788 1.00 18.33 ? 246 TYR A OH 1 ATOM 1878 N N . VAL A 1 247 ? 45.790 24.771 -11.986 1.00 18.19 ? 247 VAL A N 1 ATOM 1879 C CA . VAL A 1 247 ? 47.067 24.069 -11.887 1.00 17.72 ? 247 VAL A CA 1 ATOM 1880 C C . VAL A 1 247 ? 46.852 22.808 -11.057 1.00 17.92 ? 247 VAL A C 1 ATOM 1881 O O . VAL A 1 247 ? 45.995 22.790 -10.170 1.00 17.31 ? 247 VAL A O 1 ATOM 1882 C CB . VAL A 1 247 ? 48.182 24.964 -11.260 1.00 17.59 ? 247 VAL A CB 1 ATOM 1883 C CG1 . VAL A 1 247 ? 48.323 26.277 -12.030 1.00 17.74 ? 247 VAL A CG1 1 ATOM 1884 C CG2 . VAL A 1 247 ? 47.945 25.223 -9.738 1.00 15.06 ? 247 VAL A CG2 1 ATOM 1885 N N . TRP A 1 248 ? 47.611 21.759 -11.355 1.00 17.88 ? 248 TRP A N 1 ATOM 1886 C CA . TRP A 1 248 ? 47.529 20.524 -10.582 1.00 18.60 ? 248 TRP A CA 1 ATOM 1887 C C . TRP A 1 248 ? 48.872 20.118 -9.995 1.00 17.95 ? 248 TRP A C 1 ATOM 1888 O O . TRP A 1 248 ? 48.972 19.101 -9.301 1.00 18.12 ? 248 TRP A O 1 ATOM 1889 C CB . TRP A 1 248 ? 46.913 19.375 -11.397 1.00 19.35 ? 248 TRP A CB 1 ATOM 1890 C CG . TRP A 1 248 ? 47.667 19.082 -12.652 1.00 21.55 ? 248 TRP A CG 1 ATOM 1891 C CD1 . TRP A 1 248 ? 47.465 19.653 -13.867 1.00 23.45 ? 248 TRP A CD1 1 ATOM 1892 C CD2 . TRP A 1 248 ? 48.757 18.165 -12.809 1.00 22.47 ? 248 TRP A CD2 1 ATOM 1893 N NE1 . TRP A 1 248 ? 48.357 19.142 -14.787 1.00 24.63 ? 248 TRP A NE1 1 ATOM 1894 C CE2 . TRP A 1 248 ? 49.162 18.225 -14.161 1.00 24.00 ? 248 TRP A CE2 1 ATOM 1895 C CE3 . TRP A 1 248 ? 49.425 17.288 -11.943 1.00 22.63 ? 248 TRP A CE3 1 ATOM 1896 C CZ2 . TRP A 1 248 ? 50.216 17.448 -14.670 1.00 22.79 ? 248 TRP A CZ2 1 ATOM 1897 C CZ3 . TRP A 1 248 ? 50.481 16.509 -12.460 1.00 23.59 ? 248 TRP A CZ3 1 ATOM 1898 C CH2 . TRP A 1 248 ? 50.855 16.599 -13.807 1.00 22.64 ? 248 TRP A CH2 1 ATOM 1899 N N . ASN A 1 249 ? 49.900 20.913 -10.261 1.00 17.54 ? 249 ASN A N 1 ATOM 1900 C CA . ASN A 1 249 ? 51.193 20.645 -9.665 1.00 17.58 ? 249 ASN A CA 1 ATOM 1901 C C . ASN A 1 249 ? 51.906 21.895 -9.175 1.00 17.82 ? 249 ASN A C 1 ATOM 1902 O O . ASN A 1 249 ? 51.503 23.036 -9.484 1.00 17.60 ? 249 ASN A O 1 ATOM 1903 C CB . ASN A 1 249 ? 52.079 19.788 -10.582 1.00 17.26 ? 249 ASN A CB 1 ATOM 1904 C CG . ASN A 1 249 ? 52.389 20.465 -11.905 1.00 19.74 ? 249 ASN A CG 1 ATOM 1905 O OD1 . ASN A 1 249 ? 52.726 21.644 -11.938 1.00 18.73 ? 249 ASN A OD1 1 ATOM 1906 N ND2 . ASN A 1 249 ? 52.302 19.696 -13.006 1.00 23.35 ? 249 ASN A ND2 1 ATOM 1907 N N . ARG A 1 250 ? 52.954 21.656 -8.397 1.00 18.03 ? 250 ARG A N 1 ATOM 1908 C CA . ARG A 1 250 ? 53.676 22.697 -7.695 1.00 18.91 ? 250 ARG A CA 1 ATOM 1909 C C . ARG A 1 250 ? 54.310 23.699 -8.642 1.00 19.82 ? 250 ARG A C 1 ATOM 1910 O O . ARG A 1 250 ? 54.201 24.890 -8.424 1.00 20.03 ? 250 ARG A O 1 ATOM 1911 C CB . ARG A 1 250 ? 54.759 22.072 -6.821 1.00 18.73 ? 250 ARG A CB 1 ATOM 1912 C CG . ARG A 1 250 ? 55.534 23.070 -6.011 1.00 18.04 ? 250 ARG A CG 1 ATOM 1913 C CD . ARG A 1 250 ? 56.536 22.337 -5.180 1.00 20.32 ? 250 ARG A CD 1 ATOM 1914 N NE . ARG A 1 250 ? 57.349 23.269 -4.425 1.00 19.64 ? 250 ARG A NE 1 ATOM 1915 C CZ . ARG A 1 250 ? 58.535 23.709 -4.812 1.00 23.07 ? 250 ARG A CZ 1 ATOM 1916 N NH1 . ARG A 1 250 ? 59.062 23.292 -5.967 1.00 23.09 ? 250 ARG A NH1 1 ATOM 1917 N NH2 . ARG A 1 250 ? 59.199 24.555 -4.029 1.00 21.90 ? 250 ARG A NH2 1 ATOM 1918 N N . THR A 1 251 ? 54.993 23.224 -9.675 1.00 20.91 ? 251 THR A N 1 ATOM 1919 C CA . THR A 1 251 ? 55.717 24.162 -10.533 1.00 22.39 ? 251 THR A CA 1 ATOM 1920 C C . THR A 1 251 ? 54.756 25.125 -11.243 1.00 22.14 ? 251 THR A C 1 ATOM 1921 O O . THR A 1 251 ? 55.031 26.315 -11.358 1.00 22.21 ? 251 THR A O 1 ATOM 1922 C CB . THR A 1 251 ? 56.631 23.450 -11.532 1.00 22.89 ? 251 THR A CB 1 ATOM 1923 O OG1 . THR A 1 251 ? 55.878 22.454 -12.229 1.00 28.00 ? 251 THR A OG1 1 ATOM 1924 C CG2 . THR A 1 251 ? 57.780 22.780 -10.815 1.00 23.37 ? 251 THR A CG2 1 ATOM 1925 N N . GLU A 1 252 ? 53.617 24.622 -11.693 1.00 21.86 ? 252 GLU A N 1 ATOM 1926 C CA . GLU A 1 252 ? 52.626 25.507 -12.301 1.00 22.48 ? 252 GLU A CA 1 ATOM 1927 C C . GLU A 1 252 ? 52.019 26.478 -11.296 1.00 21.41 ? 252 GLU A C 1 ATOM 1928 O O . GLU A 1 252 ? 51.771 27.640 -11.628 1.00 20.33 ? 252 GLU A O 1 ATOM 1929 C CB . GLU A 1 252 ? 51.540 24.711 -12.998 1.00 23.31 ? 252 GLU A CB 1 ATOM 1930 C CG . GLU A 1 252 ? 52.080 23.875 -14.145 1.00 28.46 ? 252 GLU A CG 1 ATOM 1931 C CD . GLU A 1 252 ? 52.668 24.709 -15.261 1.00 35.45 ? 252 GLU A CD 1 ATOM 1932 O OE1 . GLU A 1 252 ? 51.886 25.423 -15.925 1.00 40.36 ? 252 GLU A OE1 1 ATOM 1933 O OE2 . GLU A 1 252 ? 53.909 24.651 -15.475 1.00 38.38 ? 252 GLU A OE2 1 ATOM 1934 N N . LEU A 1 253 ? 51.800 26.007 -10.070 1.00 20.74 ? 253 LEU A N 1 ATOM 1935 C CA . LEU A 1 253 ? 51.355 26.882 -8.993 1.00 20.67 ? 253 LEU A CA 1 ATOM 1936 C C . LEU A 1 253 ? 52.323 28.054 -8.801 1.00 22.02 ? 253 LEU A C 1 ATOM 1937 O O . LEU A 1 253 ? 51.897 29.219 -8.748 1.00 21.19 ? 253 LEU A O 1 ATOM 1938 C CB . LEU A 1 253 ? 51.226 26.106 -7.673 1.00 19.94 ? 253 LEU A CB 1 ATOM 1939 C CG . LEU A 1 253 ? 50.966 27.015 -6.461 1.00 19.38 ? 253 LEU A CG 1 ATOM 1940 C CD1 . LEU A 1 253 ? 49.632 27.711 -6.617 1.00 16.69 ? 253 LEU A CD1 1 ATOM 1941 C CD2 . LEU A 1 253 ? 51.014 26.255 -5.143 1.00 19.84 ? 253 LEU A CD2 1 ATOM 1942 N N . MET A 1 254 ? 53.614 27.735 -8.660 1.00 23.63 ? 254 MET A N 1 ATOM 1943 C CA . MET A 1 254 ? 54.650 28.766 -8.512 1.00 26.61 ? 254 MET A CA 1 ATOM 1944 C C . MET A 1 254 ? 54.507 29.779 -9.626 1.00 25.42 ? 254 MET A C 1 ATOM 1945 O O . MET A 1 254 ? 54.438 30.979 -9.375 1.00 25.58 ? 254 MET A O 1 ATOM 1946 C CB . MET A 1 254 ? 56.065 28.188 -8.648 1.00 26.65 ? 254 MET A CB 1 ATOM 1947 C CG . MET A 1 254 ? 56.462 26.978 -7.815 1.00 30.15 ? 254 MET A CG 1 ATOM 1948 S SD . MET A 1 254 ? 58.250 26.656 -8.016 1.00 33.86 ? 254 MET A SD 1 ATOM 1949 C CE . MET A 1 254 ? 58.446 26.753 -9.795 1.00 35.04 ? 254 MET A CE 1 ATOM 1950 N N . GLN A 1 255 ? 54.483 29.269 -10.856 1.00 25.41 ? 255 GLN A N 1 ATOM 1951 C CA . GLN A 1 255 ? 54.405 30.087 -12.066 1.00 25.92 ? 255 GLN A CA 1 ATOM 1952 C C . GLN A 1 255 ? 53.176 30.994 -12.054 1.00 24.46 ? 255 GLN A C 1 ATOM 1953 O O . GLN A 1 255 ? 53.293 32.196 -12.243 1.00 24.38 ? 255 GLN A O 1 ATOM 1954 C CB . GLN A 1 255 ? 54.456 29.213 -13.331 1.00 25.66 ? 255 GLN A CB 1 ATOM 1955 C CG . GLN A 1 255 ? 55.842 28.624 -13.601 1.00 27.97 ? 255 GLN A CG 1 ATOM 1956 C CD . GLN A 1 255 ? 55.883 27.493 -14.645 1.00 28.36 ? 255 GLN A CD 1 ATOM 1957 O OE1 . GLN A 1 255 ? 56.948 26.911 -14.890 1.00 32.50 ? 255 GLN A OE1 1 ATOM 1958 N NE2 . GLN A 1 255 ? 54.737 27.165 -15.237 1.00 32.70 ? 255 GLN A NE2 1 ATOM 1959 N N . ALA A 1 256 ? 52.010 30.415 -11.781 1.00 23.87 ? 256 ALA A N 1 ATOM 1960 C CA . ALA A 1 256 ? 50.767 31.172 -11.706 1.00 22.68 ? 256 ALA A CA 1 ATOM 1961 C C . ALA A 1 256 ? 50.809 32.261 -10.631 1.00 22.02 ? 256 ALA A C 1 ATOM 1962 O O . ALA A 1 256 ? 50.344 33.378 -10.861 1.00 21.38 ? 256 ALA A O 1 ATOM 1963 C CB . ALA A 1 256 ? 49.596 30.227 -11.462 1.00 23.43 ? 256 ALA A CB 1 ATOM 1964 N N . SER A 1 257 ? 51.373 31.944 -9.462 1.00 21.54 ? 257 SER A N 1 ATOM 1965 C CA . SER A 1 257 ? 51.368 32.889 -8.337 1.00 21.20 ? 257 SER A CA 1 ATOM 1966 C C . SER A 1 257 ? 52.202 34.149 -8.631 1.00 21.89 ? 257 SER A C 1 ATOM 1967 O O . SER A 1 257 ? 51.987 35.186 -8.023 1.00 20.83 ? 257 SER A O 1 ATOM 1968 C CB . SER A 1 257 ? 51.848 32.227 -7.042 1.00 20.61 ? 257 SER A CB 1 ATOM 1969 O OG . SER A 1 257 ? 53.237 31.967 -7.097 1.00 19.45 ? 257 SER A OG 1 ATOM 1970 N N . LEU A 1 258 ? 53.153 34.039 -9.557 1.00 22.42 ? 258 LEU A N 1 ATOM 1971 C CA . LEU A 1 258 ? 54.005 35.171 -9.913 1.00 24.26 ? 258 LEU A CA 1 ATOM 1972 C C . LEU A 1 258 ? 53.501 35.908 -11.152 1.00 25.12 ? 258 LEU A C 1 ATOM 1973 O O . LEU A 1 258 ? 54.091 36.904 -11.568 1.00 26.33 ? 258 LEU A O 1 ATOM 1974 C CB . LEU A 1 258 ? 55.442 34.697 -10.150 1.00 23.31 ? 258 LEU A CB 1 ATOM 1975 C CG . LEU A 1 258 ? 56.207 34.169 -8.937 1.00 24.58 ? 258 LEU A CG 1 ATOM 1976 C CD1 . LEU A 1 258 ? 57.565 33.653 -9.362 1.00 23.19 ? 258 LEU A CD1 1 ATOM 1977 C CD2 . LEU A 1 258 ? 56.369 35.227 -7.860 1.00 23.35 ? 258 LEU A CD2 1 ATOM 1978 N N . ASP A 1 259 ? 52.417 35.413 -11.738 1.00 26.10 ? 259 ASP A N 1 ATOM 1979 C CA . ASP A 1 259 ? 51.926 35.921 -13.009 1.00 27.14 ? 259 ASP A CA 1 ATOM 1980 C C . ASP A 1 259 ? 50.888 37.018 -12.763 1.00 27.97 ? 259 ASP A C 1 ATOM 1981 O O . ASP A 1 259 ? 49.811 36.762 -12.225 1.00 27.22 ? 259 ASP A O 1 ATOM 1982 C CB . ASP A 1 259 ? 51.346 34.764 -13.820 1.00 27.36 ? 259 ASP A CB 1 ATOM 1983 C CG . ASP A 1 259 ? 51.003 35.145 -15.243 1.00 28.88 ? 259 ASP A CG 1 ATOM 1984 O OD1 . ASP A 1 259 ? 50.909 34.219 -16.074 1.00 30.07 ? 259 ASP A OD1 1 ATOM 1985 O OD2 . ASP A 1 259 ? 50.813 36.345 -15.534 1.00 28.93 ? 259 ASP A OD2 1 ATOM 1986 N N . PRO A 1 260 ? 51.211 38.256 -13.180 1.00 29.19 ? 260 PRO A N 1 ATOM 1987 C CA . PRO A 1 260 ? 50.352 39.406 -12.937 1.00 29.45 ? 260 PRO A CA 1 ATOM 1988 C C . PRO A 1 260 ? 48.969 39.235 -13.577 1.00 29.03 ? 260 PRO A C 1 ATOM 1989 O O . PRO A 1 260 ? 47.988 39.746 -13.058 1.00 29.60 ? 260 PRO A O 1 ATOM 1990 C CB . PRO A 1 260 ? 51.113 40.557 -13.611 1.00 29.56 ? 260 PRO A CB 1 ATOM 1991 C CG . PRO A 1 260 ? 52.025 39.898 -14.603 1.00 30.48 ? 260 PRO A CG 1 ATOM 1992 C CD . PRO A 1 260 ? 52.423 38.624 -13.936 1.00 29.36 ? 260 PRO A CD 1 ATOM 1993 N N . SER A 1 261 ? 48.897 38.498 -14.681 1.00 28.74 ? 261 SER A N 1 ATOM 1994 C CA . SER A 1 261 ? 47.638 38.319 -15.408 1.00 27.91 ? 261 SER A CA 1 ATOM 1995 C C . SER A 1 261 ? 46.721 37.279 -14.751 1.00 27.26 ? 261 SER A C 1 ATOM 1996 O O . SER A 1 261 ? 45.559 37.122 -15.144 1.00 27.24 ? 261 SER A O 1 ATOM 1997 C CB . SER A 1 261 ? 47.917 37.945 -16.866 1.00 28.45 ? 261 SER A CB 1 ATOM 1998 O OG . SER A 1 261 ? 48.430 36.626 -16.980 1.00 29.29 ? 261 SER A OG 1 ATOM 1999 N N . VAL A 1 262 ? 47.246 36.553 -13.769 1.00 25.90 ? 262 VAL A N 1 ATOM 2000 C CA . VAL A 1 262 ? 46.444 35.558 -13.076 1.00 25.08 ? 262 VAL A CA 1 ATOM 2001 C C . VAL A 1 262 ? 45.685 36.236 -11.945 1.00 25.38 ? 262 VAL A C 1 ATOM 2002 O O . VAL A 1 262 ? 46.270 36.668 -10.940 1.00 25.84 ? 262 VAL A O 1 ATOM 2003 C CB . VAL A 1 262 ? 47.291 34.381 -12.550 1.00 24.83 ? 262 VAL A CB 1 ATOM 2004 C CG1 . VAL A 1 262 ? 46.433 33.417 -11.705 1.00 24.39 ? 262 VAL A CG1 1 ATOM 2005 C CG2 . VAL A 1 262 ? 47.921 33.637 -13.720 1.00 23.98 ? 262 VAL A CG2 1 ATOM 2006 N N . THR A 1 263 ? 44.374 36.309 -12.102 1.00 24.81 ? 263 THR A N 1 ATOM 2007 C CA . THR A 1 263 ? 43.544 36.947 -11.091 1.00 25.14 ? 263 THR A CA 1 ATOM 2008 C C . THR A 1 263 ? 42.789 35.925 -10.256 1.00 23.88 ? 263 THR A C 1 ATOM 2009 O O . THR A 1 263 ? 42.358 36.236 -9.141 1.00 24.90 ? 263 THR A O 1 ATOM 2010 C CB . THR A 1 263 ? 42.548 37.892 -11.740 1.00 25.40 ? 263 THR A CB 1 ATOM 2011 O OG1 . THR A 1 263 ? 41.683 37.125 -12.580 1.00 27.60 ? 263 THR A OG1 1 ATOM 2012 C CG2 . THR A 1 263 ? 43.282 38.919 -12.589 1.00 27.44 ? 263 THR A CG2 1 ATOM 2013 N N . HIS A 1 264 ? 42.610 34.723 -10.809 1.00 21.92 ? 264 HIS A N 1 ATOM 2014 C CA . HIS A 1 264 ? 41.924 33.645 -10.126 1.00 20.81 ? 264 HIS A CA 1 ATOM 2015 C C . HIS A 1 264 ? 42.735 32.385 -10.297 1.00 19.46 ? 264 HIS A C 1 ATOM 2016 O O . HIS A 1 264 ? 43.164 32.071 -11.394 1.00 18.99 ? 264 HIS A O 1 ATOM 2017 C CB . HIS A 1 264 ? 40.530 33.432 -10.703 1.00 21.28 ? 264 HIS A CB 1 ATOM 2018 C CG . HIS A 1 264 ? 39.552 34.481 -10.295 1.00 22.73 ? 264 HIS A CG 1 ATOM 2019 N ND1 . HIS A 1 264 ? 39.594 35.760 -10.802 1.00 24.89 ? 264 HIS A ND1 1 ATOM 2020 C CD2 . HIS A 1 264 ? 38.528 34.455 -9.411 1.00 23.32 ? 264 HIS A CD2 1 ATOM 2021 C CE1 . HIS A 1 264 ? 38.631 36.478 -10.251 1.00 26.06 ? 264 HIS A CE1 1 ATOM 2022 N NE2 . HIS A 1 264 ? 37.970 35.709 -9.402 1.00 25.76 ? 264 HIS A NE2 1 ATOM 2023 N N . LEU A 1 265 ? 42.963 31.667 -9.212 1.00 18.12 ? 265 LEU A N 1 ATOM 2024 C CA . LEU A 1 265 ? 43.813 30.502 -9.280 1.00 17.52 ? 265 LEU A CA 1 ATOM 2025 C C . LEU A 1 265 ? 43.162 29.339 -8.577 1.00 17.64 ? 265 LEU A C 1 ATOM 2026 O O . LEU A 1 265 ? 42.813 29.444 -7.408 1.00 18.23 ? 265 LEU A O 1 ATOM 2027 C CB . LEU A 1 265 ? 45.164 30.807 -8.636 1.00 17.82 ? 265 LEU A CB 1 ATOM 2028 C CG . LEU A 1 265 ? 46.180 29.674 -8.528 1.00 18.33 ? 265 LEU A CG 1 ATOM 2029 C CD1 . LEU A 1 265 ? 46.519 29.095 -9.910 1.00 18.50 ? 265 LEU A CD1 1 ATOM 2030 C CD2 . LEU A 1 265 ? 47.416 30.211 -7.832 1.00 20.31 ? 265 LEU A CD2 1 ATOM 2031 N N . MET A 1 266 ? 42.990 28.241 -9.294 1.00 16.57 ? 266 MET A N 1 ATOM 2032 C CA . MET A 1 266 ? 42.548 27.018 -8.674 1.00 17.07 ? 266 MET A CA 1 ATOM 2033 C C . MET A 1 266 ? 43.651 25.982 -8.808 1.00 16.50 ? 266 MET A C 1 ATOM 2034 O O . MET A 1 266 ? 44.057 25.633 -9.919 1.00 17.06 ? 266 MET A O 1 ATOM 2035 C CB . MET A 1 266 ? 41.259 26.515 -9.305 1.00 16.42 ? 266 MET A CB 1 ATOM 2036 C CG . MET A 1 266 ? 40.818 25.155 -8.730 1.00 17.08 ? 266 MET A CG 1 ATOM 2037 S SD . MET A 1 266 ? 39.403 24.477 -9.607 1.00 19.41 ? 266 MET A SD 1 ATOM 2038 C CE . MET A 1 266 ? 38.096 25.562 -9.053 1.00 18.65 ? 266 MET A CE 1 ATOM 2039 N N . GLY A 1 267 ? 44.143 25.502 -7.675 1.00 15.73 ? 267 GLY A N 1 ATOM 2040 C CA . GLY A 1 267 ? 45.239 24.531 -7.665 1.00 14.88 ? 267 GLY A CA 1 ATOM 2041 C C . GLY A 1 267 ? 44.752 23.324 -6.912 1.00 14.84 ? 267 GLY A C 1 ATOM 2042 O O . GLY A 1 267 ? 44.483 23.427 -5.719 1.00 14.38 ? 267 GLY A O 1 ATOM 2043 N N . LEU A 1 268 ? 44.602 22.199 -7.617 1.00 14.53 ? 268 LEU A N 1 ATOM 2044 C CA . LEU A 1 268 ? 44.135 20.952 -7.004 1.00 14.15 ? 268 LEU A CA 1 ATOM 2045 C C . LEU A 1 268 ? 45.192 19.885 -7.202 1.00 14.46 ? 268 LEU A C 1 ATOM 2046 O O . LEU A 1 268 ? 45.436 19.437 -8.321 1.00 14.39 ? 268 LEU A O 1 ATOM 2047 C CB . LEU A 1 268 ? 42.781 20.524 -7.570 1.00 14.26 ? 268 LEU A CB 1 ATOM 2048 C CG . LEU A 1 268 ? 41.646 21.552 -7.481 1.00 13.91 ? 268 LEU A CG 1 ATOM 2049 C CD1 . LEU A 1 268 ? 40.388 20.981 -8.139 1.00 13.38 ? 268 LEU A CD1 1 ATOM 2050 C CD2 . LEU A 1 268 ? 41.365 21.991 -6.039 1.00 13.58 ? 268 LEU A CD2 1 ATOM 2051 N N . PHE A 1 269 ? 45.818 19.485 -6.096 1.00 14.00 ? 269 PHE A N 1 ATOM 2052 C CA . PHE A 1 269 ? 47.131 18.851 -6.146 1.00 14.79 ? 269 PHE A CA 1 ATOM 2053 C C . PHE A 1 269 ? 47.117 17.351 -5.968 1.00 14.53 ? 269 PHE A C 1 ATOM 2054 O O . PHE A 1 269 ? 48.111 16.679 -6.240 1.00 15.55 ? 269 PHE A O 1 ATOM 2055 C CB . PHE A 1 269 ? 48.075 19.557 -5.160 1.00 14.20 ? 269 PHE A CB 1 ATOM 2056 C CG . PHE A 1 269 ? 48.253 21.000 -5.486 1.00 14.99 ? 269 PHE A CG 1 ATOM 2057 C CD1 . PHE A 1 269 ? 47.678 21.993 -4.683 1.00 14.77 ? 269 PHE A CD1 1 ATOM 2058 C CD2 . PHE A 1 269 ? 48.930 21.372 -6.662 1.00 14.73 ? 269 PHE A CD2 1 ATOM 2059 C CE1 . PHE A 1 269 ? 47.806 23.345 -5.027 1.00 13.34 ? 269 PHE A CE1 1 ATOM 2060 C CE2 . PHE A 1 269 ? 49.075 22.717 -7.016 1.00 15.96 ? 269 PHE A CE2 1 ATOM 2061 C CZ . PHE A 1 269 ? 48.508 23.708 -6.212 1.00 14.60 ? 269 PHE A CZ 1 ATOM 2062 N N . GLU A 1 270 ? 45.987 16.819 -5.532 1.00 14.64 ? 270 GLU A N 1 ATOM 2063 C CA . GLU A 1 270 ? 45.800 15.374 -5.461 1.00 15.10 ? 270 GLU A CA 1 ATOM 2064 C C . GLU A 1 270 ? 44.362 15.077 -5.827 1.00 15.29 ? 270 GLU A C 1 ATOM 2065 O O . GLU A 1 270 ? 43.526 15.983 -5.788 1.00 15.49 ? 270 GLU A O 1 ATOM 2066 C CB . GLU A 1 270 ? 46.106 14.839 -4.054 1.00 14.96 ? 270 GLU A CB 1 ATOM 2067 C CG . GLU A 1 270 ? 47.595 14.815 -3.690 1.00 15.41 ? 270 GLU A CG 1 ATOM 2068 C CD . GLU A 1 270 ? 48.405 13.842 -4.538 1.00 18.72 ? 270 GLU A CD 1 ATOM 2069 O OE1 . GLU A 1 270 ? 48.036 12.664 -4.664 1.00 18.87 ? 270 GLU A OE1 1 ATOM 2070 O OE2 . GLU A 1 270 ? 49.443 14.258 -5.079 1.00 20.90 ? 270 GLU A OE2 1 ATOM 2071 N N . PRO A 1 271 ? 44.063 13.812 -6.169 1.00 15.48 ? 271 PRO A N 1 ATOM 2072 C CA . PRO A 1 271 ? 42.675 13.444 -6.457 1.00 15.49 ? 271 PRO A CA 1 ATOM 2073 C C . PRO A 1 271 ? 41.793 13.648 -5.224 1.00 15.25 ? 271 PRO A C 1 ATOM 2074 O O . PRO A 1 271 ? 40.715 14.199 -5.349 1.00 15.27 ? 271 PRO A O 1 ATOM 2075 C CB . PRO A 1 271 ? 42.765 11.955 -6.841 1.00 15.24 ? 271 PRO A CB 1 ATOM 2076 C CG . PRO A 1 271 ? 44.211 11.744 -7.229 1.00 15.83 ? 271 PRO A CG 1 ATOM 2077 C CD . PRO A 1 271 ? 44.987 12.669 -6.338 1.00 15.63 ? 271 PRO A CD 1 ATOM 2078 N N . GLY A 1 272 ? 42.278 13.215 -4.055 1.00 15.03 ? 272 GLY A N 1 ATOM 2079 C CA . GLY A 1 272 ? 41.589 13.417 -2.785 1.00 14.80 ? 272 GLY A CA 1 ATOM 2080 C C . GLY A 1 272 ? 42.440 14.326 -1.922 1.00 14.90 ? 272 GLY A C 1 ATOM 2081 O O . GLY A 1 272 ? 42.932 15.352 -2.387 1.00 14.73 ? 272 GLY A O 1 ATOM 2082 N N . ASP A 1 273 ? 42.653 13.935 -0.671 1.00 14.93 ? 273 ASP A N 1 ATOM 2083 C CA . ASP A 1 273 ? 43.458 14.750 0.233 1.00 14.76 ? 273 ASP A CA 1 ATOM 2084 C C . ASP A 1 273 ? 44.898 14.773 -0.228 1.00 14.90 ? 273 ASP A C 1 ATOM 2085 O O . ASP A 1 273 ? 45.363 13.849 -0.896 1.00 14.89 ? 273 ASP A O 1 ATOM 2086 C CB . ASP A 1 273 ? 43.375 14.210 1.656 1.00 14.79 ? 273 ASP A CB 1 ATOM 2087 C CG . ASP A 1 273 ? 41.977 14.284 2.216 1.00 14.80 ? 273 ASP A CG 1 ATOM 2088 O OD1 . ASP A 1 273 ? 41.253 15.256 1.900 1.00 15.07 ? 273 ASP A OD1 1 ATOM 2089 O OD2 . ASP A 1 273 ? 41.595 13.365 2.956 1.00 14.18 ? 273 ASP A OD2 1 ATOM 2090 N N . MET A 1 274 ? 45.618 15.823 0.139 1.00 14.50 ? 274 MET A N 1 ATOM 2091 C CA . MET A 1 274 ? 47.027 15.865 -0.179 1.00 15.39 ? 274 MET A CA 1 ATOM 2092 C C . MET A 1 274 ? 47.778 14.878 0.705 1.00 14.71 ? 274 MET A C 1 ATOM 2093 O O . MET A 1 274 ? 47.275 14.445 1.752 1.00 14.42 ? 274 MET A O 1 ATOM 2094 C CB . MET A 1 274 ? 47.571 17.291 -0.080 1.00 15.09 ? 274 MET A CB 1 ATOM 2095 C CG . MET A 1 274 ? 46.952 18.171 -1.193 1.00 16.27 ? 274 MET A CG 1 ATOM 2096 S SD . MET A 1 274 ? 47.540 19.834 -1.161 1.00 19.64 ? 274 MET A SD 1 ATOM 2097 C CE . MET A 1 274 ? 49.254 19.573 -1.673 1.00 18.17 ? 274 MET A CE 1 ATOM 2098 N N . LYS A 1 275 ? 48.964 14.488 0.261 1.00 13.91 ? 275 LYS A N 1 ATOM 2099 C CA . LYS A 1 275 ? 49.781 13.602 1.051 1.00 13.90 ? 275 LYS A CA 1 ATOM 2100 C C . LYS A 1 275 ? 50.197 14.276 2.342 1.00 13.99 ? 275 LYS A C 1 ATOM 2101 O O . LYS A 1 275 ? 50.357 15.500 2.393 1.00 13.44 ? 275 LYS A O 1 ATOM 2102 C CB . LYS A 1 275 ? 50.997 13.154 0.235 1.00 14.22 ? 275 LYS A CB 1 ATOM 2103 C CG . LYS A 1 275 ? 50.560 12.238 -0.907 1.00 16.19 ? 275 LYS A CG 1 ATOM 2104 C CD . LYS A 1 275 ? 51.684 11.673 -1.696 1.00 21.22 ? 275 LYS A CD 1 ATOM 2105 C CE . LYS A 1 275 ? 51.117 10.664 -2.678 1.00 23.97 ? 275 LYS A CE 1 ATOM 2106 N NZ . LYS A 1 275 ? 52.194 10.103 -3.531 1.00 28.15 ? 275 LYS A NZ 1 ATOM 2107 N N . TYR A 1 276 ? 50.372 13.478 3.393 1.00 14.53 ? 276 TYR A N 1 ATOM 2108 C CA . TYR A 1 276 ? 51.065 13.958 4.574 1.00 15.04 ? 276 TYR A CA 1 ATOM 2109 C C . TYR A 1 276 ? 52.373 14.588 4.129 1.00 15.89 ? 276 TYR A C 1 ATOM 2110 O O . TYR A 1 276 ? 52.992 14.134 3.156 1.00 16.04 ? 276 TYR A O 1 ATOM 2111 C CB . TYR A 1 276 ? 51.358 12.806 5.533 1.00 14.68 ? 276 TYR A CB 1 ATOM 2112 C CG . TYR A 1 276 ? 50.133 12.305 6.252 1.00 15.09 ? 276 TYR A CG 1 ATOM 2113 C CD1 . TYR A 1 276 ? 49.653 11.017 6.028 1.00 14.23 ? 276 TYR A CD1 1 ATOM 2114 C CD2 . TYR A 1 276 ? 49.462 13.116 7.173 1.00 15.42 ? 276 TYR A CD2 1 ATOM 2115 C CE1 . TYR A 1 276 ? 48.528 10.539 6.710 1.00 13.49 ? 276 TYR A CE1 1 ATOM 2116 C CE2 . TYR A 1 276 ? 48.336 12.648 7.861 1.00 15.12 ? 276 TYR A CE2 1 ATOM 2117 C CZ . TYR A 1 276 ? 47.886 11.365 7.629 1.00 13.90 ? 276 TYR A CZ 1 ATOM 2118 O OH . TYR A 1 276 ? 46.792 10.915 8.308 1.00 13.93 ? 276 TYR A OH 1 ATOM 2119 N N . GLU A 1 277 ? 52.771 15.655 4.807 1.00 16.57 ? 277 GLU A N 1 ATOM 2120 C CA . GLU A 1 277 ? 54.039 16.297 4.509 1.00 17.90 ? 277 GLU A CA 1 ATOM 2121 C C . GLU A 1 277 ? 55.182 15.280 4.414 1.00 18.31 ? 277 GLU A C 1 ATOM 2122 O O . GLU A 1 277 ? 56.037 15.397 3.539 1.00 17.72 ? 277 GLU A O 1 ATOM 2123 C CB . GLU A 1 277 ? 54.354 17.375 5.557 1.00 18.09 ? 277 GLU A CB 1 ATOM 2124 C CG . GLU A 1 277 ? 55.738 18.002 5.400 1.00 18.09 ? 277 GLU A CG 1 ATOM 2125 C CD . GLU A 1 277 ? 55.884 18.777 4.105 1.00 19.57 ? 277 GLU A CD 1 ATOM 2126 O OE1 . GLU A 1 277 ? 54.863 19.101 3.467 1.00 20.45 ? 277 GLU A OE1 1 ATOM 2127 O OE2 . GLU A 1 277 ? 57.023 19.068 3.717 1.00 18.56 ? 277 GLU A OE2 1 ATOM 2128 N N . ILE A 1 278 ? 55.184 14.279 5.294 1.00 19.11 ? 278 ILE A N 1 ATOM 2129 C CA . ILE A 1 278 ? 56.267 13.280 5.303 1.00 20.48 ? 278 ILE A CA 1 ATOM 2130 C C . ILE A 1 278 ? 56.277 12.407 4.046 1.00 20.45 ? 278 ILE A C 1 ATOM 2131 O O . ILE A 1 278 ? 57.287 11.786 3.721 1.00 20.97 ? 278 ILE A O 1 ATOM 2132 C CB . ILE A 1 278 ? 56.267 12.406 6.583 1.00 20.30 ? 278 ILE A CB 1 ATOM 2133 C CG1 . ILE A 1 278 ? 54.952 11.612 6.707 1.00 21.62 ? 278 ILE A CG1 1 ATOM 2134 C CG2 . ILE A 1 278 ? 56.567 13.293 7.795 1.00 21.23 ? 278 ILE A CG2 1 ATOM 2135 C CD1 . ILE A 1 278 ? 54.945 10.547 7.805 1.00 21.81 ? 278 ILE A CD1 1 ATOM 2136 N N . HIS A 1 279 ? 55.150 12.388 3.340 1.00 20.44 ? 279 HIS A N 1 ATOM 2137 C CA . HIS A 1 279 ? 55.026 11.649 2.095 1.00 20.33 ? 279 HIS A CA 1 ATOM 2138 C C . HIS A 1 279 ? 54.972 12.529 0.861 1.00 19.96 ? 279 HIS A C 1 ATOM 2139 O O . HIS A 1 279 ? 54.893 12.011 -0.258 1.00 19.88 ? 279 HIS A O 1 ATOM 2140 C CB . HIS A 1 279 ? 53.792 10.763 2.133 1.00 20.39 ? 279 HIS A CB 1 ATOM 2141 C CG . HIS A 1 279 ? 53.781 9.816 3.288 1.00 22.42 ? 279 HIS A CG 1 ATOM 2142 N ND1 . HIS A 1 279 ? 52.623 9.438 3.929 1.00 24.90 ? 279 HIS A ND1 1 ATOM 2143 C CD2 . HIS A 1 279 ? 54.793 9.179 3.927 1.00 24.36 ? 279 HIS A CD2 1 ATOM 2144 C CE1 . HIS A 1 279 ? 52.921 8.604 4.913 1.00 26.92 ? 279 HIS A CE1 1 ATOM 2145 N NE2 . HIS A 1 279 ? 54.232 8.428 4.930 1.00 25.61 ? 279 HIS A NE2 1 ATOM 2146 N N . ARG A 1 280 ? 55.013 13.843 1.053 1.00 19.25 ? 280 ARG A N 1 ATOM 2147 C CA . ARG A 1 280 ? 54.855 14.772 -0.064 1.00 19.20 ? 280 ARG A CA 1 ATOM 2148 C C . ARG A 1 280 ? 55.980 14.611 -1.089 1.00 19.51 ? 280 ARG A C 1 ATOM 2149 O O . ARG A 1 280 ? 57.139 14.466 -0.729 1.00 19.02 ? 280 ARG A O 1 ATOM 2150 C CB . ARG A 1 280 ? 54.778 16.218 0.436 1.00 18.89 ? 280 ARG A CB 1 ATOM 2151 C CG . ARG A 1 280 ? 54.542 17.251 -0.674 1.00 17.82 ? 280 ARG A CG 1 ATOM 2152 C CD . ARG A 1 280 ? 54.270 18.630 -0.105 1.00 18.34 ? 280 ARG A CD 1 ATOM 2153 N NE . ARG A 1 280 ? 55.385 19.095 0.722 1.00 17.56 ? 280 ARG A NE 1 ATOM 2154 C CZ . ARG A 1 280 ? 56.459 19.737 0.265 1.00 17.47 ? 280 ARG A CZ 1 ATOM 2155 N NH1 . ARG A 1 280 ? 57.418 20.102 1.113 1.00 18.99 ? 280 ARG A NH1 1 ATOM 2156 N NH2 . ARG A 1 280 ? 56.584 20.030 -1.026 1.00 18.17 ? 280 ARG A NH2 1 ATOM 2157 N N . ASP A 1 281 ? 55.608 14.607 -2.362 1.00 19.93 ? 281 ASP A N 1 ATOM 2158 C CA . ASP A 1 281 ? 56.562 14.674 -3.446 1.00 21.36 ? 281 ASP A CA 1 ATOM 2159 C C . ASP A 1 281 ? 56.802 16.155 -3.713 1.00 21.52 ? 281 ASP A C 1 ATOM 2160 O O . ASP A 1 281 ? 55.938 16.840 -4.263 1.00 21.31 ? 281 ASP A O 1 ATOM 2161 C CB . ASP A 1 281 ? 55.972 13.996 -4.679 1.00 21.79 ? 281 ASP A CB 1 ATOM 2162 C CG . ASP A 1 281 ? 56.888 14.054 -5.884 1.00 23.87 ? 281 ASP A CG 1 ATOM 2163 O OD1 . ASP A 1 281 ? 57.687 15.012 -6.034 1.00 26.05 ? 281 ASP A OD1 1 ATOM 2164 O OD2 . ASP A 1 281 ? 56.792 13.119 -6.700 1.00 26.90 ? 281 ASP A OD2 1 ATOM 2165 N N . SER A 1 282 ? 57.969 16.646 -3.315 1.00 21.81 ? 282 SER A N 1 ATOM 2166 C CA . SER A 1 282 ? 58.252 18.078 -3.364 1.00 23.28 ? 282 SER A CA 1 ATOM 2167 C C . SER A 1 282 ? 58.494 18.605 -4.773 1.00 23.29 ? 282 SER A C 1 ATOM 2168 O O . SER A 1 282 ? 58.606 19.818 -4.973 1.00 24.02 ? 282 SER A O 1 ATOM 2169 C CB . SER A 1 282 ? 59.436 18.419 -2.453 1.00 23.31 ? 282 SER A CB 1 ATOM 2170 O OG . SER A 1 282 ? 60.545 17.591 -2.778 1.00 26.27 ? 282 SER A OG 1 ATOM 2171 N N . THR A 1 283 ? 58.583 17.703 -5.746 1.00 23.50 ? 283 THR A N 1 ATOM 2172 C CA . THR A 1 283 ? 58.641 18.127 -7.143 1.00 23.93 ? 283 THR A CA 1 ATOM 2173 C C . THR A 1 283 ? 57.242 18.371 -7.700 1.00 23.24 ? 283 THR A C 1 ATOM 2174 O O . THR A 1 283 ? 57.050 19.285 -8.501 1.00 23.60 ? 283 THR A O 1 ATOM 2175 C CB . THR A 1 283 ? 59.448 17.173 -8.047 1.00 23.83 ? 283 THR A CB 1 ATOM 2176 O OG1 . THR A 1 283 ? 58.756 15.921 -8.195 1.00 27.80 ? 283 THR A OG1 1 ATOM 2177 C CG2 . THR A 1 283 ? 60.802 16.934 -7.450 1.00 24.29 ? 283 THR A CG2 1 ATOM 2178 N N . LEU A 1 284 ? 56.268 17.582 -7.244 1.00 21.46 ? 284 LEU A N 1 ATOM 2179 C CA . LEU A 1 284 ? 54.911 17.669 -7.768 1.00 20.83 ? 284 LEU A CA 1 ATOM 2180 C C . LEU A 1 284 ? 53.952 18.462 -6.895 1.00 19.65 ? 284 LEU A C 1 ATOM 2181 O O . LEU A 1 284 ? 52.969 19.005 -7.398 1.00 18.63 ? 284 LEU A O 1 ATOM 2182 C CB . LEU A 1 284 ? 54.337 16.269 -7.991 1.00 21.41 ? 284 LEU A CB 1 ATOM 2183 C CG . LEU A 1 284 ? 54.687 15.590 -9.317 1.00 23.79 ? 284 LEU A CG 1 ATOM 2184 C CD1 . LEU A 1 284 ? 54.534 14.094 -9.123 1.00 27.88 ? 284 LEU A CD1 1 ATOM 2185 C CD2 . LEU A 1 284 ? 53.777 16.085 -10.430 1.00 26.77 ? 284 LEU A CD2 1 ATOM 2186 N N . ASP A 1 285 ? 54.226 18.508 -5.595 1.00 18.59 ? 285 ASP A N 1 ATOM 2187 C CA . ASP A 1 285 ? 53.250 19.031 -4.645 1.00 17.99 ? 285 ASP A CA 1 ATOM 2188 C C . ASP A 1 285 ? 53.792 20.122 -3.753 1.00 17.11 ? 285 ASP A C 1 ATOM 2189 O O . ASP A 1 285 ? 54.867 19.984 -3.166 1.00 15.84 ? 285 ASP A O 1 ATOM 2190 C CB . ASP A 1 285 ? 52.653 17.923 -3.775 1.00 18.93 ? 285 ASP A CB 1 ATOM 2191 C CG . ASP A 1 285 ? 51.646 17.093 -4.520 1.00 21.07 ? 285 ASP A CG 1 ATOM 2192 O OD1 . ASP A 1 285 ? 50.416 17.277 -4.321 1.00 22.94 ? 285 ASP A OD1 1 ATOM 2193 O OD2 . ASP A 1 285 ? 52.094 16.258 -5.323 1.00 22.17 ? 285 ASP A OD2 1 ATOM 2194 N N . PRO A 1 286 ? 53.016 21.204 -3.624 1.00 16.38 ? 286 PRO A N 1 ATOM 2195 C CA . PRO A 1 286 ? 53.427 22.267 -2.751 1.00 16.21 ? 286 PRO A CA 1 ATOM 2196 C C . PRO A 1 286 ? 53.118 21.908 -1.295 1.00 16.20 ? 286 PRO A C 1 ATOM 2197 O O . PRO A 1 286 ? 52.115 21.229 -1.012 1.00 15.64 ? 286 PRO A O 1 ATOM 2198 C CB . PRO A 1 286 ? 52.576 23.447 -3.209 1.00 16.26 ? 286 PRO A CB 1 ATOM 2199 C CG . PRO A 1 286 ? 51.297 22.799 -3.722 1.00 16.11 ? 286 PRO A CG 1 ATOM 2200 C CD . PRO A 1 286 ? 51.702 21.449 -4.255 1.00 16.46 ? 286 PRO A CD 1 ATOM 2201 N N . SER A 1 287 ? 53.983 22.347 -0.384 1.00 15.87 ? 287 SER A N 1 ATOM 2202 C CA . SER A 1 287 ? 53.688 22.239 1.042 1.00 15.93 ? 287 SER A CA 1 ATOM 2203 C C . SER A 1 287 ? 52.585 23.246 1.375 1.00 15.33 ? 287 SER A C 1 ATOM 2204 O O . SER A 1 287 ? 52.232 24.094 0.550 1.00 15.52 ? 287 SER A O 1 ATOM 2205 C CB . SER A 1 287 ? 54.924 22.589 1.870 1.00 15.97 ? 287 SER A CB 1 ATOM 2206 O OG . SER A 1 287 ? 55.217 23.960 1.709 1.00 16.28 ? 287 SER A OG 1 ATOM 2207 N N . LEU A 1 288 ? 52.045 23.144 2.580 1.00 14.92 ? 288 LEU A N 1 ATOM 2208 C CA . LEU A 1 288 ? 51.023 24.071 3.029 1.00 14.69 ? 288 LEU A CA 1 ATOM 2209 C C . LEU A 1 288 ? 51.582 25.499 3.050 1.00 14.72 ? 288 LEU A C 1 ATOM 2210 O O . LEU A 1 288 ? 50.902 26.456 2.665 1.00 13.32 ? 288 LEU A O 1 ATOM 2211 C CB . LEU A 1 288 ? 50.491 23.664 4.408 1.00 14.27 ? 288 LEU A CB 1 ATOM 2212 C CG . LEU A 1 288 ? 49.415 24.570 5.027 1.00 13.61 ? 288 LEU A CG 1 ATOM 2213 C CD1 . LEU A 1 288 ? 48.224 24.755 4.086 1.00 12.27 ? 288 LEU A CD1 1 ATOM 2214 C CD2 . LEU A 1 288 ? 48.986 24.047 6.391 1.00 14.55 ? 288 LEU A CD2 1 ATOM 2215 N N . MET A 1 289 ? 52.826 25.633 3.489 1.00 14.74 ? 289 MET A N 1 ATOM 2216 C CA . MET A 1 289 ? 53.468 26.935 3.527 1.00 17.22 ? 289 MET A CA 1 ATOM 2217 C C . MET A 1 289 ? 53.548 27.563 2.123 1.00 15.40 ? 289 MET A C 1 ATOM 2218 O O . MET A 1 289 ? 53.295 28.753 1.940 1.00 15.35 ? 289 MET A O 1 ATOM 2219 C CB . MET A 1 289 ? 54.852 26.781 4.123 1.00 16.56 ? 289 MET A CB 1 ATOM 2220 C CG . MET A 1 289 ? 55.595 28.069 4.268 1.00 21.19 ? 289 MET A CG 1 ATOM 2221 S SD . MET A 1 289 ? 57.209 27.774 5.004 1.00 23.64 ? 289 MET A SD 1 ATOM 2222 C CE . MET A 1 289 ? 57.915 26.516 3.952 1.00 27.25 ? 289 MET A CE 1 ATOM 2223 N N . GLU A 1 290 ? 53.915 26.747 1.140 1.00 15.17 ? 290 GLU A N 1 ATOM 2224 C CA . GLU A 1 290 ? 54.032 27.191 -0.237 1.00 14.53 ? 290 GLU A CA 1 ATOM 2225 C C . GLU A 1 290 ? 52.677 27.602 -0.805 1.00 13.90 ? 290 GLU A C 1 ATOM 2226 O O . GLU A 1 290 ? 52.553 28.633 -1.466 1.00 13.61 ? 290 GLU A O 1 ATOM 2227 C CB . GLU A 1 290 ? 54.650 26.080 -1.085 1.00 14.68 ? 290 GLU A CB 1 ATOM 2228 C CG . GLU A 1 290 ? 56.115 25.887 -0.746 1.00 17.32 ? 290 GLU A CG 1 ATOM 2229 C CD . GLU A 1 290 ? 56.759 24.677 -1.388 1.00 19.76 ? 290 GLU A CD 1 ATOM 2230 O OE1 . GLU A 1 290 ? 56.049 23.765 -1.864 1.00 19.94 ? 290 GLU A OE1 1 ATOM 2231 O OE2 . GLU A 1 290 ? 58.001 24.638 -1.390 1.00 22.37 ? 290 GLU A OE2 1 ATOM 2232 N N . MET A 1 291 ? 51.660 26.792 -0.545 1.00 14.17 ? 291 MET A N 1 ATOM 2233 C CA . MET A 1 291 ? 50.299 27.130 -0.968 1.00 14.09 ? 291 MET A CA 1 ATOM 2234 C C . MET A 1 291 ? 49.864 28.437 -0.320 1.00 14.94 ? 291 MET A C 1 ATOM 2235 O O . MET A 1 291 ? 49.255 29.297 -0.990 1.00 13.67 ? 291 MET A O 1 ATOM 2236 C CB . MET A 1 291 ? 49.328 26.004 -0.628 1.00 13.66 ? 291 MET A CB 1 ATOM 2237 C CG . MET A 1 291 ? 49.555 24.778 -1.448 1.00 13.70 ? 291 MET A CG 1 ATOM 2238 S SD . MET A 1 291 ? 48.218 23.580 -1.323 1.00 15.60 ? 291 MET A SD 1 ATOM 2239 C CE . MET A 1 291 ? 48.390 23.025 0.376 1.00 16.37 ? 291 MET A CE 1 ATOM 2240 N N . THR A 1 292 ? 50.212 28.597 0.973 1.00 13.58 ? 292 THR A N 1 ATOM 2241 C CA . THR A 1 292 ? 49.914 29.843 1.702 1.00 13.64 ? 292 THR A CA 1 ATOM 2242 C C . THR A 1 292 ? 50.556 31.071 1.036 1.00 13.72 ? 292 THR A C 1 ATOM 2243 O O . THR A 1 292 ? 49.899 32.091 0.816 1.00 12.89 ? 292 THR A O 1 ATOM 2244 C CB . THR A 1 292 ? 50.321 29.715 3.187 1.00 12.97 ? 292 THR A CB 1 ATOM 2245 O OG1 . THR A 1 292 ? 49.578 28.631 3.769 1.00 13.13 ? 292 THR A OG1 1 ATOM 2246 C CG2 . THR A 1 292 ? 50.049 31.007 3.961 1.00 13.24 ? 292 THR A CG2 1 ATOM 2247 N N . GLU A 1 293 ? 51.832 30.954 0.694 1.00 14.22 ? 293 GLU A N 1 ATOM 2248 C CA . GLU A 1 293 ? 52.523 32.022 0.017 1.00 14.63 ? 293 GLU A CA 1 ATOM 2249 C C . GLU A 1 293 ? 51.950 32.327 -1.362 1.00 14.65 ? 293 GLU A C 1 ATOM 2250 O O . GLU A 1 293 ? 51.757 33.507 -1.698 1.00 14.63 ? 293 GLU A O 1 ATOM 2251 C CB . GLU A 1 293 ? 54.007 31.719 -0.079 1.00 15.38 ? 293 GLU A CB 1 ATOM 2252 C CG . GLU A 1 293 ? 54.762 32.805 -0.810 1.00 15.48 ? 293 GLU A CG 1 ATOM 2253 C CD . GLU A 1 293 ? 56.186 32.907 -0.345 1.00 15.38 ? 293 GLU A CD 1 ATOM 2254 O OE1 . GLU A 1 293 ? 56.858 33.870 -0.754 1.00 17.63 ? 293 GLU A OE1 1 ATOM 2255 O OE2 . GLU A 1 293 ? 56.625 32.024 0.424 1.00 14.68 ? 293 GLU A OE2 1 ATOM 2256 N N . ALA A 1 294 ? 51.698 31.277 -2.154 1.00 14.50 ? 294 ALA A N 1 ATOM 2257 C CA . ALA A 1 294 ? 51.074 31.417 -3.470 1.00 14.52 ? 294 ALA A CA 1 ATOM 2258 C C . ALA A 1 294 ? 49.778 32.219 -3.361 1.00 14.37 ? 294 ALA A C 1 ATOM 2259 O O . ALA A 1 294 ? 49.553 33.181 -4.115 1.00 14.27 ? 294 ALA A O 1 ATOM 2260 C CB . ALA A 1 294 ? 50.795 30.044 -4.070 1.00 15.01 ? 294 ALA A CB 1 ATOM 2261 N N . ALA A 1 295 ? 48.945 31.834 -2.397 1.00 14.14 ? 295 ALA A N 1 ATOM 2262 C CA . ALA A 1 295 ? 47.671 32.489 -2.150 1.00 13.67 ? 295 ALA A CA 1 ATOM 2263 C C . ALA A 1 295 ? 47.897 33.946 -1.815 1.00 13.68 ? 295 ALA A C 1 ATOM 2264 O O . ALA A 1 295 ? 47.229 34.811 -2.383 1.00 14.07 ? 295 ALA A O 1 ATOM 2265 C CB . ALA A 1 295 ? 46.921 31.790 -1.026 1.00 13.38 ? 295 ALA A CB 1 ATOM 2266 N N . LEU A 1 296 ? 48.840 34.224 -0.917 1.00 13.52 ? 296 LEU A N 1 ATOM 2267 C CA . LEU A 1 296 ? 49.105 35.609 -0.490 1.00 14.20 ? 296 LEU A CA 1 ATOM 2268 C C . LEU A 1 296 ? 49.633 36.496 -1.625 1.00 14.65 ? 296 LEU A C 1 ATOM 2269 O O . LEU A 1 296 ? 49.267 37.680 -1.726 1.00 14.58 ? 296 LEU A O 1 ATOM 2270 C CB . LEU A 1 296 ? 50.057 35.657 0.711 1.00 13.99 ? 296 LEU A CB 1 ATOM 2271 C CG . LEU A 1 296 ? 49.438 35.228 2.047 1.00 12.53 ? 296 LEU A CG 1 ATOM 2272 C CD1 . LEU A 1 296 ? 50.522 34.982 3.092 1.00 14.04 ? 296 LEU A CD1 1 ATOM 2273 C CD2 . LEU A 1 296 ? 48.408 36.222 2.572 1.00 12.86 ? 296 LEU A CD2 1 ATOM 2274 N N . ARG A 1 297 ? 50.474 35.929 -2.485 1.00 15.22 ? 297 ARG A N 1 ATOM 2275 C CA . ARG A 1 297 ? 50.923 36.653 -3.685 1.00 15.73 ? 297 ARG A CA 1 ATOM 2276 C C . ARG A 1 297 ? 49.769 37.228 -4.486 1.00 16.60 ? 297 ARG A C 1 ATOM 2277 O O . ARG A 1 297 ? 49.804 38.399 -4.872 1.00 16.66 ? 297 ARG A O 1 ATOM 2278 C CB . ARG A 1 297 ? 51.780 35.763 -4.577 1.00 15.96 ? 297 ARG A CB 1 ATOM 2279 C CG . ARG A 1 297 ? 53.145 35.522 -3.981 1.00 15.26 ? 297 ARG A CG 1 ATOM 2280 C CD . ARG A 1 297 ? 53.858 34.417 -4.707 1.00 16.86 ? 297 ARG A CD 1 ATOM 2281 N NE . ARG A 1 297 ? 55.225 34.318 -4.231 1.00 16.22 ? 297 ARG A NE 1 ATOM 2282 C CZ . ARG A 1 297 ? 56.115 33.455 -4.692 1.00 16.03 ? 297 ARG A CZ 1 ATOM 2283 N NH1 . ARG A 1 297 ? 57.351 33.460 -4.199 1.00 16.43 ? 297 ARG A NH1 1 ATOM 2284 N NH2 . ARG A 1 297 ? 55.764 32.579 -5.626 1.00 17.08 ? 297 ARG A NH2 1 ATOM 2285 N N . LEU A 1 298 ? 48.750 36.405 -4.734 1.00 16.80 ? 298 LEU A N 1 ATOM 2286 C CA . LEU A 1 298 ? 47.604 36.849 -5.516 1.00 17.84 ? 298 LEU A CA 1 ATOM 2287 C C . LEU A 1 298 ? 46.668 37.718 -4.679 1.00 17.28 ? 298 LEU A C 1 ATOM 2288 O O . LEU A 1 298 ? 46.273 38.805 -5.106 1.00 17.32 ? 298 LEU A O 1 ATOM 2289 C CB . LEU A 1 298 ? 46.819 35.657 -6.072 1.00 18.30 ? 298 LEU A CB 1 ATOM 2290 C CG . LEU A 1 298 ? 47.353 34.766 -7.202 1.00 23.36 ? 298 LEU A CG 1 ATOM 2291 C CD1 . LEU A 1 298 ? 46.125 34.105 -7.878 1.00 24.23 ? 298 LEU A CD1 1 ATOM 2292 C CD2 . LEU A 1 298 ? 48.259 35.472 -8.264 1.00 25.11 ? 298 LEU A CD2 1 ATOM 2293 N N . LEU A 1 299 ? 46.308 37.236 -3.491 1.00 16.11 ? 299 LEU A N 1 ATOM 2294 C CA . LEU A 1 299 ? 45.321 37.933 -2.658 1.00 16.39 ? 299 LEU A CA 1 ATOM 2295 C C . LEU A 1 299 ? 45.750 39.346 -2.267 1.00 16.57 ? 299 LEU A C 1 ATOM 2296 O O . LEU A 1 299 ? 44.917 40.262 -2.191 1.00 16.57 ? 299 LEU A O 1 ATOM 2297 C CB . LEU A 1 299 ? 45.019 37.121 -1.404 1.00 15.29 ? 299 LEU A CB 1 ATOM 2298 C CG . LEU A 1 299 ? 44.316 35.778 -1.623 1.00 15.52 ? 299 LEU A CG 1 ATOM 2299 C CD1 . LEU A 1 299 ? 44.204 35.025 -0.281 1.00 14.95 ? 299 LEU A CD1 1 ATOM 2300 C CD2 . LEU A 1 299 ? 42.926 35.956 -2.262 1.00 16.10 ? 299 LEU A CD2 1 ATOM 2301 N N . SER A 1 300 ? 47.049 39.518 -2.027 1.00 17.14 ? 300 SER A N 1 ATOM 2302 C CA . SER A 1 300 ? 47.579 40.791 -1.553 1.00 18.35 ? 300 SER A CA 1 ATOM 2303 C C . SER A 1 300 ? 47.504 41.906 -2.596 1.00 18.35 ? 300 SER A C 1 ATOM 2304 O O . SER A 1 300 ? 47.730 43.060 -2.266 1.00 18.10 ? 300 SER A O 1 ATOM 2305 C CB . SER A 1 300 ? 49.028 40.622 -1.134 1.00 18.55 ? 300 SER A CB 1 ATOM 2306 O OG . SER A 1 300 ? 49.799 40.329 -2.281 1.00 21.40 ? 300 SER A OG 1 ATOM 2307 N N . ARG A 1 301 ? 47.192 41.574 -3.846 1.00 18.46 ? 301 ARG A N 1 ATOM 2308 C CA . ARG A 1 301 ? 47.156 42.603 -4.899 1.00 19.17 ? 301 ARG A CA 1 ATOM 2309 C C . ARG A 1 301 ? 45.970 43.552 -4.762 1.00 19.76 ? 301 ARG A C 1 ATOM 2310 O O . ARG A 1 301 ? 46.022 44.709 -5.199 1.00 19.95 ? 301 ARG A O 1 ATOM 2311 C CB . ARG A 1 301 ? 47.123 41.956 -6.264 1.00 19.82 ? 301 ARG A CB 1 ATOM 2312 C CG . ARG A 1 301 ? 48.385 41.184 -6.596 1.00 21.33 ? 301 ARG A CG 1 ATOM 2313 C CD . ARG A 1 301 ? 48.181 40.576 -7.940 1.00 25.64 ? 301 ARG A CD 1 ATOM 2314 N NE . ARG A 1 301 ? 49.182 39.591 -8.331 1.00 29.19 ? 301 ARG A NE 1 ATOM 2315 C CZ . ARG A 1 301 ? 48.968 38.713 -9.308 1.00 32.77 ? 301 ARG A CZ 1 ATOM 2316 N NH1 . ARG A 1 301 ? 47.800 38.718 -9.962 1.00 33.05 ? 301 ARG A NH1 1 ATOM 2317 N NH2 . ARG A 1 301 ? 49.902 37.842 -9.645 1.00 34.19 ? 301 ARG A NH2 1 ATOM 2318 N N . ASN A 1 302 ? 44.908 43.067 -4.135 1.00 19.34 ? 302 ASN A N 1 ATOM 2319 C CA . ASN A 1 302 ? 43.671 43.810 -4.037 1.00 19.47 ? 302 ASN A CA 1 ATOM 2320 C C . ASN A 1 302 ? 43.800 44.926 -3.007 1.00 19.91 ? 302 ASN A C 1 ATOM 2321 O O . ASN A 1 302 ? 44.064 44.651 -1.837 1.00 19.83 ? 302 ASN A O 1 ATOM 2322 C CB . ASN A 1 302 ? 42.554 42.851 -3.646 1.00 19.16 ? 302 ASN A CB 1 ATOM 2323 C CG . ASN A 1 302 ? 41.193 43.496 -3.647 1.00 19.59 ? 302 ASN A CG 1 ATOM 2324 O OD1 . ASN A 1 302 ? 41.054 44.729 -3.590 1.00 20.14 ? 302 ASN A OD1 1 ATOM 2325 N ND2 . ASN A 1 302 ? 40.167 42.661 -3.704 1.00 18.54 ? 302 ASN A ND2 1 ATOM 2326 N N . PRO A 1 303 ? 43.619 46.192 -3.433 1.00 20.39 ? 303 PRO A N 1 ATOM 2327 C CA . PRO A 1 303 ? 43.795 47.295 -2.484 1.00 20.37 ? 303 PRO A CA 1 ATOM 2328 C C . PRO A 1 303 ? 42.796 47.281 -1.326 1.00 20.13 ? 303 PRO A C 1 ATOM 2329 O O . PRO A 1 303 ? 43.048 47.917 -0.299 1.00 20.00 ? 303 PRO A O 1 ATOM 2330 C CB . PRO A 1 303 ? 43.584 48.540 -3.348 1.00 20.77 ? 303 PRO A CB 1 ATOM 2331 C CG . PRO A 1 303 ? 42.785 48.063 -4.512 1.00 21.45 ? 303 PRO A CG 1 ATOM 2332 C CD . PRO A 1 303 ? 43.274 46.679 -4.779 1.00 20.67 ? 303 PRO A CD 1 ATOM 2333 N N . ARG A 1 304 ? 41.681 46.565 -1.493 1.00 20.00 ? 304 ARG A N 1 ATOM 2334 C CA . ARG A 1 304 ? 40.631 46.485 -0.463 1.00 20.19 ? 304 ARG A CA 1 ATOM 2335 C C . ARG A 1 304 ? 40.938 45.432 0.596 1.00 19.48 ? 304 ARG A C 1 ATOM 2336 O O . ARG A 1 304 ? 40.257 45.348 1.620 1.00 20.04 ? 304 ARG A O 1 ATOM 2337 C CB . ARG A 1 304 ? 39.278 46.180 -1.097 1.00 20.67 ? 304 ARG A CB 1 ATOM 2338 C CG . ARG A 1 304 ? 38.793 47.243 -2.066 1.00 24.34 ? 304 ARG A CG 1 ATOM 2339 C CD . ARG A 1 304 ? 37.310 47.042 -2.353 1.00 29.89 ? 304 ARG A CD 1 ATOM 2340 N NE . ARG A 1 304 ? 36.817 48.043 -3.299 1.00 37.30 ? 304 ARG A NE 1 ATOM 2341 C CZ . ARG A 1 304 ? 36.454 49.285 -2.971 1.00 40.67 ? 304 ARG A CZ 1 ATOM 2342 N NH1 . ARG A 1 304 ? 36.513 49.697 -1.705 1.00 42.96 ? 304 ARG A NH1 1 ATOM 2343 N NH2 . ARG A 1 304 ? 36.030 50.123 -3.912 1.00 42.02 ? 304 ARG A NH2 1 ATOM 2344 N N . GLY A 1 305 ? 41.954 44.622 0.340 1.00 18.05 ? 305 GLY A N 1 ATOM 2345 C CA . GLY A 1 305 ? 42.353 43.587 1.287 1.00 16.95 ? 305 GLY A CA 1 ATOM 2346 C C . GLY A 1 305 ? 41.857 42.211 0.880 1.00 16.72 ? 305 GLY A C 1 ATOM 2347 O O . GLY A 1 305 ? 41.291 42.025 -0.212 1.00 16.06 ? 305 GLY A O 1 ATOM 2348 N N . PHE A 1 306 ? 42.064 41.247 1.773 1.00 15.98 ? 306 PHE A N 1 ATOM 2349 C CA . PHE A 1 306 ? 41.696 39.869 1.507 1.00 15.53 ? 306 PHE A CA 1 ATOM 2350 C C . PHE A 1 306 ? 41.240 39.154 2.769 1.00 15.12 ? 306 PHE A C 1 ATOM 2351 O O . PHE A 1 306 ? 41.527 39.580 3.894 1.00 14.72 ? 306 PHE A O 1 ATOM 2352 C CB . PHE A 1 306 ? 42.856 39.091 0.852 1.00 15.69 ? 306 PHE A CB 1 ATOM 2353 C CG . PHE A 1 306 ? 44.080 38.970 1.721 1.00 15.56 ? 306 PHE A CG 1 ATOM 2354 C CD1 . PHE A 1 306 ? 44.182 37.955 2.678 1.00 15.61 ? 306 PHE A CD1 1 ATOM 2355 C CD2 . PHE A 1 306 ? 45.127 39.882 1.588 1.00 16.30 ? 306 PHE A CD2 1 ATOM 2356 C CE1 . PHE A 1 306 ? 45.321 37.848 3.488 1.00 15.13 ? 306 PHE A CE1 1 ATOM 2357 C CE2 . PHE A 1 306 ? 46.266 39.792 2.391 1.00 15.62 ? 306 PHE A CE2 1 ATOM 2358 C CZ . PHE A 1 306 ? 46.356 38.781 3.350 1.00 16.53 ? 306 PHE A CZ 1 ATOM 2359 N N . PHE A 1 307 ? 40.512 38.065 2.546 1.00 14.05 ? 307 PHE A N 1 ATOM 2360 C CA . PHE A 1 307 ? 40.216 37.090 3.562 1.00 14.26 ? 307 PHE A CA 1 ATOM 2361 C C . PHE A 1 307 ? 40.916 35.819 3.108 1.00 13.95 ? 307 PHE A C 1 ATOM 2362 O O . PHE A 1 307 ? 40.756 35.391 1.961 1.00 13.29 ? 307 PHE A O 1 ATOM 2363 C CB . PHE A 1 307 ? 38.710 36.807 3.646 1.00 13.55 ? 307 PHE A CB 1 ATOM 2364 C CG . PHE A 1 307 ? 38.353 35.751 4.677 1.00 15.17 ? 307 PHE A CG 1 ATOM 2365 C CD1 . PHE A 1 307 ? 38.560 34.398 4.416 1.00 14.16 ? 307 PHE A CD1 1 ATOM 2366 C CD2 . PHE A 1 307 ? 37.844 36.116 5.913 1.00 14.17 ? 307 PHE A CD2 1 ATOM 2367 C CE1 . PHE A 1 307 ? 38.262 33.422 5.385 1.00 15.70 ? 307 PHE A CE1 1 ATOM 2368 C CE2 . PHE A 1 307 ? 37.526 35.145 6.876 1.00 15.89 ? 307 PHE A CE2 1 ATOM 2369 C CZ . PHE A 1 307 ? 37.739 33.808 6.612 1.00 15.20 ? 307 PHE A CZ 1 ATOM 2370 N N . LEU A 1 308 ? 41.668 35.204 4.006 1.00 14.02 ? 308 LEU A N 1 ATOM 2371 C CA . LEU A 1 308 ? 42.326 33.943 3.672 1.00 13.35 ? 308 LEU A CA 1 ATOM 2372 C C . LEU A 1 308 ? 42.059 32.877 4.733 1.00 13.05 ? 308 LEU A C 1 ATOM 2373 O O . LEU A 1 308 ? 42.237 33.128 5.924 1.00 12.92 ? 308 LEU A O 1 ATOM 2374 C CB . LEU A 1 308 ? 43.829 34.172 3.537 1.00 13.50 ? 308 LEU A CB 1 ATOM 2375 C CG . LEU A 1 308 ? 44.687 32.921 3.286 1.00 13.67 ? 308 LEU A CG 1 ATOM 2376 C CD1 . LEU A 1 308 ? 44.329 32.186 1.959 1.00 13.14 ? 308 LEU A CD1 1 ATOM 2377 C CD2 . LEU A 1 308 ? 46.154 33.322 3.316 1.00 13.39 ? 308 LEU A CD2 1 ATOM 2378 N N . PHE A 1 309 ? 41.649 31.693 4.277 1.00 12.55 ? 309 PHE A N 1 ATOM 2379 C CA . PHE A 1 309 ? 41.506 30.508 5.133 1.00 12.97 ? 309 PHE A CA 1 ATOM 2380 C C . PHE A 1 309 ? 42.682 29.584 4.821 1.00 12.86 ? 309 PHE A C 1 ATOM 2381 O O . PHE A 1 309 ? 42.897 29.219 3.660 1.00 12.02 ? 309 PHE A O 1 ATOM 2382 C CB . PHE A 1 309 ? 40.171 29.827 4.823 1.00 13.26 ? 309 PHE A CB 1 ATOM 2383 C CG . PHE A 1 309 ? 40.012 28.425 5.402 1.00 13.30 ? 309 PHE A CG 1 ATOM 2384 C CD1 . PHE A 1 309 ? 40.447 27.302 4.690 1.00 13.03 ? 309 PHE A CD1 1 ATOM 2385 C CD2 . PHE A 1 309 ? 39.363 28.228 6.614 1.00 14.85 ? 309 PHE A CD2 1 ATOM 2386 C CE1 . PHE A 1 309 ? 40.267 26.013 5.187 1.00 12.09 ? 309 PHE A CE1 1 ATOM 2387 C CE2 . PHE A 1 309 ? 39.184 26.927 7.135 1.00 13.79 ? 309 PHE A CE2 1 ATOM 2388 C CZ . PHE A 1 309 ? 39.640 25.818 6.417 1.00 13.61 ? 309 PHE A CZ 1 ATOM 2389 N N . VAL A 1 310 ? 43.439 29.216 5.853 1.00 12.18 ? 310 VAL A N 1 ATOM 2390 C CA . VAL A 1 310 ? 44.574 28.295 5.696 1.00 12.17 ? 310 VAL A CA 1 ATOM 2391 C C . VAL A 1 310 ? 44.374 27.142 6.668 1.00 12.06 ? 310 VAL A C 1 ATOM 2392 O O . VAL A 1 310 ? 44.309 27.355 7.875 1.00 11.94 ? 310 VAL A O 1 ATOM 2393 C CB . VAL A 1 310 ? 45.948 28.988 5.974 1.00 11.35 ? 310 VAL A CB 1 ATOM 2394 C CG1 . VAL A 1 310 ? 47.112 27.966 5.997 1.00 11.39 ? 310 VAL A CG1 1 ATOM 2395 C CG2 . VAL A 1 310 ? 46.222 30.085 4.964 1.00 11.27 ? 310 VAL A CG2 1 ATOM 2396 N N . GLU A 1 311 ? 44.279 25.920 6.153 1.00 11.74 ? 311 GLU A N 1 ATOM 2397 C CA . GLU A 1 311 ? 44.040 24.793 7.045 1.00 11.98 ? 311 GLU A CA 1 ATOM 2398 C C . GLU A 1 311 ? 45.169 23.783 7.084 1.00 12.48 ? 311 GLU A C 1 ATOM 2399 O O . GLU A 1 311 ? 45.577 23.243 6.035 1.00 12.54 ? 311 GLU A O 1 ATOM 2400 C CB . GLU A 1 311 ? 42.748 24.067 6.681 1.00 11.78 ? 311 GLU A CB 1 ATOM 2401 C CG . GLU A 1 311 ? 42.418 22.949 7.673 1.00 11.70 ? 311 GLU A CG 1 ATOM 2402 C CD . GLU A 1 311 ? 41.357 21.988 7.176 1.00 11.87 ? 311 GLU A CD 1 ATOM 2403 O OE1 . GLU A 1 311 ? 41.074 21.937 5.955 1.00 11.81 ? 311 GLU A OE1 1 ATOM 2404 O OE2 . GLU A 1 311 ? 40.808 21.263 8.029 1.00 10.34 ? 311 GLU A OE2 1 ATOM 2405 N N . GLY A 1 312 ? 45.632 23.503 8.303 1.00 12.52 ? 312 GLY A N 1 ATOM 2406 C CA . GLY A 1 312 ? 46.473 22.328 8.571 1.00 12.18 ? 312 GLY A CA 1 ATOM 2407 C C . GLY A 1 312 ? 45.502 21.179 8.674 1.00 12.50 ? 312 GLY A C 1 ATOM 2408 O O . GLY A 1 312 ? 45.098 20.780 9.773 1.00 12.80 ? 312 GLY A O 1 ATOM 2409 N N . GLY A 1 313 ? 45.084 20.660 7.522 1.00 12.09 ? 313 GLY A N 1 ATOM 2410 C CA . GLY A 1 313 ? 43.924 19.791 7.508 1.00 11.74 ? 313 GLY A CA 1 ATOM 2411 C C . GLY A 1 313 ? 44.153 18.361 7.897 1.00 11.48 ? 313 GLY A C 1 ATOM 2412 O O . GLY A 1 313 ? 43.203 17.664 8.245 1.00 12.11 ? 313 GLY A O 1 ATOM 2413 N N . ARG A 1 314 ? 45.404 17.914 7.840 1.00 10.81 ? 314 ARG A N 1 ATOM 2414 C CA . ARG A 1 314 ? 45.691 16.500 8.078 1.00 10.38 ? 314 ARG A CA 1 ATOM 2415 C C . ARG A 1 314 ? 46.324 16.225 9.432 1.00 10.37 ? 314 ARG A C 1 ATOM 2416 O O . ARG A 1 314 ? 46.629 15.079 9.733 1.00 10.99 ? 314 ARG A O 1 ATOM 2417 C CB . ARG A 1 314 ? 46.504 15.904 6.915 1.00 10.51 ? 314 ARG A CB 1 ATOM 2418 C CG . ARG A 1 314 ? 45.789 16.114 5.564 1.00 11.31 ? 314 ARG A CG 1 ATOM 2419 C CD . ARG A 1 314 ? 46.143 15.022 4.539 1.00 11.76 ? 314 ARG A CD 1 ATOM 2420 N NE . ARG A 1 314 ? 45.567 13.733 4.925 1.00 12.54 ? 314 ARG A NE 1 ATOM 2421 C CZ . ARG A 1 314 ? 46.058 12.552 4.576 1.00 13.32 ? 314 ARG A CZ 1 ATOM 2422 N NH1 . ARG A 1 314 ? 47.139 12.478 3.811 1.00 13.50 ? 314 ARG A NH1 1 ATOM 2423 N NH2 . ARG A 1 314 ? 45.475 11.437 5.006 1.00 14.06 ? 314 ARG A NH2 1 ATOM 2424 N N . ILE A 1 315 ? 46.470 17.266 10.259 1.00 9.66 ? 315 ILE A N 1 ATOM 2425 C CA . ILE A 1 315 ? 46.731 17.092 11.702 1.00 10.14 ? 315 ILE A CA 1 ATOM 2426 C C . ILE A 1 315 ? 45.704 16.079 12.226 1.00 10.67 ? 315 ILE A C 1 ATOM 2427 O O . ILE A 1 315 ? 46.039 15.055 12.848 1.00 11.01 ? 315 ILE A O 1 ATOM 2428 C CB . ILE A 1 315 ? 46.575 18.441 12.467 1.00 9.27 ? 315 ILE A CB 1 ATOM 2429 C CG1 . ILE A 1 315 ? 47.594 19.464 11.948 1.00 9.98 ? 315 ILE A CG1 1 ATOM 2430 C CG2 . ILE A 1 315 ? 46.695 18.235 13.996 1.00 9.68 ? 315 ILE A CG2 1 ATOM 2431 C CD1 . ILE A 1 315 ? 47.389 20.907 12.473 1.00 10.16 ? 315 ILE A CD1 1 ATOM 2432 N N . ASP A 1 316 ? 44.451 16.396 11.932 1.00 10.93 ? 316 ASP A N 1 ATOM 2433 C CA . ASP A 1 316 ? 43.294 15.609 12.308 1.00 11.04 ? 316 ASP A CA 1 ATOM 2434 C C . ASP A 1 316 ? 43.446 14.157 11.862 1.00 10.78 ? 316 ASP A C 1 ATOM 2435 O O . ASP A 1 316 ? 43.209 13.236 12.633 1.00 10.91 ? 316 ASP A O 1 ATOM 2436 C CB . ASP A 1 316 ? 42.051 16.228 11.656 1.00 10.91 ? 316 ASP A CB 1 ATOM 2437 C CG . ASP A 1 316 ? 40.775 15.529 12.058 1.00 12.32 ? 316 ASP A CG 1 ATOM 2438 O OD1 . ASP A 1 316 ? 40.132 14.896 11.182 1.00 12.33 ? 316 ASP A OD1 1 ATOM 2439 O OD2 . ASP A 1 316 ? 40.399 15.618 13.250 1.00 11.39 ? 316 ASP A OD2 1 ATOM 2440 N N . HIS A 1 317 ? 43.863 13.971 10.616 1.00 10.85 ? 317 HIS A N 1 ATOM 2441 C CA . HIS A 1 317 ? 43.992 12.646 10.028 1.00 11.33 ? 317 HIS A CA 1 ATOM 2442 C C . HIS A 1 317 ? 45.036 11.795 10.725 1.00 11.88 ? 317 HIS A C 1 ATOM 2443 O O . HIS A 1 317 ? 44.807 10.596 10.960 1.00 12.69 ? 317 HIS A O 1 ATOM 2444 C CB . HIS A 1 317 ? 44.250 12.768 8.527 1.00 11.82 ? 317 HIS A CB 1 ATOM 2445 C CG . HIS A 1 317 ? 43.103 13.391 7.792 1.00 13.72 ? 317 HIS A CG 1 ATOM 2446 N ND1 . HIS A 1 317 ? 43.122 13.646 6.438 1.00 15.78 ? 317 HIS A ND1 1 ATOM 2447 C CD2 . HIS A 1 317 ? 41.907 13.841 8.241 1.00 15.54 ? 317 HIS A CD2 1 ATOM 2448 C CE1 . HIS A 1 317 ? 41.975 14.198 6.078 1.00 16.08 ? 317 HIS A CE1 1 ATOM 2449 N NE2 . HIS A 1 317 ? 41.219 14.327 7.154 1.00 15.92 ? 317 HIS A NE2 1 ATOM 2450 N N . GLY A 1 318 ? 46.156 12.412 11.091 1.00 11.34 ? 318 GLY A N 1 ATOM 2451 C CA . GLY A 1 318 ? 47.202 11.711 11.835 1.00 11.78 ? 318 GLY A CA 1 ATOM 2452 C C . GLY A 1 318 ? 46.653 11.192 13.150 1.00 11.88 ? 318 GLY A C 1 ATOM 2453 O O . GLY A 1 318 ? 46.884 10.031 13.517 1.00 12.37 ? 318 GLY A O 1 ATOM 2454 N N . HIS A 1 319 ? 45.929 12.048 13.877 1.00 11.41 ? 319 HIS A N 1 ATOM 2455 C CA . HIS A 1 319 ? 45.347 11.603 15.141 1.00 11.61 ? 319 HIS A CA 1 ATOM 2456 C C . HIS A 1 319 ? 44.342 10.487 14.933 1.00 11.53 ? 319 HIS A C 1 ATOM 2457 O O . HIS A 1 319 ? 44.305 9.544 15.723 1.00 12.21 ? 319 HIS A O 1 ATOM 2458 C CB . HIS A 1 319 ? 44.689 12.745 15.910 1.00 11.20 ? 319 HIS A CB 1 ATOM 2459 C CG . HIS A 1 319 ? 45.654 13.637 16.626 1.00 11.48 ? 319 HIS A CG 1 ATOM 2460 N ND1 . HIS A 1 319 ? 46.770 13.158 17.280 1.00 11.15 ? 319 HIS A ND1 1 ATOM 2461 C CD2 . HIS A 1 319 ? 45.634 14.973 16.839 1.00 10.56 ? 319 HIS A CD2 1 ATOM 2462 C CE1 . HIS A 1 319 ? 47.405 14.164 17.855 1.00 11.27 ? 319 HIS A CE1 1 ATOM 2463 N NE2 . HIS A 1 319 ? 46.743 15.278 17.594 1.00 12.07 ? 319 HIS A NE2 1 ATOM 2464 N N . HIS A 1 320 ? 43.504 10.592 13.903 1.00 10.93 ? 320 HIS A N 1 ATOM 2465 C CA . HIS A 1 320 ? 42.524 9.507 13.642 1.00 11.84 ? 320 HIS A CA 1 ATOM 2466 C C . HIS A 1 320 ? 43.176 8.148 13.428 1.00 11.68 ? 320 HIS A C 1 ATOM 2467 O O . HIS A 1 320 ? 42.618 7.111 13.813 1.00 11.72 ? 320 HIS A O 1 ATOM 2468 C CB . HIS A 1 320 ? 41.671 9.821 12.420 1.00 11.36 ? 320 HIS A CB 1 ATOM 2469 C CG . HIS A 1 320 ? 40.617 10.827 12.695 1.00 11.97 ? 320 HIS A CG 1 ATOM 2470 N ND1 . HIS A 1 320 ? 39.688 10.663 13.701 1.00 12.71 ? 320 HIS A ND1 1 ATOM 2471 C CD2 . HIS A 1 320 ? 40.367 12.032 12.134 1.00 12.13 ? 320 HIS A CD2 1 ATOM 2472 C CE1 . HIS A 1 320 ? 38.884 11.712 13.721 1.00 13.24 ? 320 HIS A CE1 1 ATOM 2473 N NE2 . HIS A 1 320 ? 39.288 12.566 12.795 1.00 12.72 ? 320 HIS A NE2 1 ATOM 2474 N N . GLU A 1 321 ? 44.338 8.160 12.787 1.00 11.88 ? 321 GLU A N 1 ATOM 2475 C CA . GLU A 1 321 ? 45.116 6.933 12.587 1.00 12.33 ? 321 GLU A CA 1 ATOM 2476 C C . GLU A 1 321 ? 45.837 6.532 13.872 1.00 12.29 ? 321 GLU A C 1 ATOM 2477 O O . GLU A 1 321 ? 46.494 5.498 13.907 1.00 13.31 ? 321 GLU A O 1 ATOM 2478 C CB . GLU A 1 321 ? 46.146 7.134 11.475 1.00 11.76 ? 321 GLU A CB 1 ATOM 2479 C CG . GLU A 1 321 ? 45.524 7.436 10.129 1.00 13.99 ? 321 GLU A CG 1 ATOM 2480 C CD . GLU A 1 321 ? 46.552 7.801 9.069 1.00 13.93 ? 321 GLU A CD 1 ATOM 2481 O OE1 . GLU A 1 321 ? 47.744 7.525 9.273 1.00 14.49 ? 321 GLU A OE1 1 ATOM 2482 O OE2 . GLU A 1 321 ? 46.163 8.354 8.023 1.00 15.70 ? 321 GLU A OE2 1 ATOM 2483 N N . SER A 1 322 ? 45.717 7.363 14.909 1.00 12.69 ? 322 SER A N 1 ATOM 2484 C CA . SER A 1 322 ? 46.523 7.256 16.122 1.00 13.36 ? 322 SER A CA 1 ATOM 2485 C C . SER A 1 322 ? 47.998 7.181 15.783 1.00 13.11 ? 322 SER A C 1 ATOM 2486 O O . SER A 1 322 ? 48.755 6.442 16.420 1.00 13.74 ? 322 SER A O 1 ATOM 2487 C CB . SER A 1 322 ? 46.110 6.064 16.995 1.00 13.60 ? 322 SER A CB 1 ATOM 2488 O OG . SER A 1 322 ? 44.937 6.402 17.720 1.00 15.82 ? 322 SER A OG 1 ATOM 2489 N N . ARG A 1 323 ? 48.394 7.951 14.774 1.00 12.44 ? 323 ARG A N 1 ATOM 2490 C CA . ARG A 1 323 ? 49.808 8.094 14.416 1.00 12.30 ? 323 ARG A CA 1 ATOM 2491 C C . ARG A 1 323 ? 50.242 9.493 14.771 1.00 12.28 ? 323 ARG A C 1 ATOM 2492 O O . ARG A 1 323 ? 50.155 10.420 13.943 1.00 11.73 ? 323 ARG A O 1 ATOM 2493 C CB . ARG A 1 323 ? 50.029 7.762 12.932 1.00 12.33 ? 323 ARG A CB 1 ATOM 2494 C CG . ARG A 1 323 ? 49.698 6.282 12.609 1.00 12.50 ? 323 ARG A CG 1 ATOM 2495 C CD . ARG A 1 323 ? 50.130 5.968 11.188 1.00 14.50 ? 323 ARG A CD 1 ATOM 2496 N NE . ARG A 1 323 ? 50.161 4.528 10.903 1.00 15.49 ? 323 ARG A NE 1 ATOM 2497 C CZ . ARG A 1 323 ? 49.350 3.897 10.061 1.00 18.42 ? 323 ARG A CZ 1 ATOM 2498 N NH1 . ARG A 1 323 ? 48.405 4.560 9.405 1.00 19.12 ? 323 ARG A NH1 1 ATOM 2499 N NH2 . ARG A 1 323 ? 49.489 2.585 9.870 1.00 18.10 ? 323 ARG A NH2 1 ATOM 2500 N N . ALA A 1 324 ? 50.690 9.661 16.019 1.00 12.12 ? 324 ALA A N 1 ATOM 2501 C CA . ALA A 1 324 ? 51.023 11.000 16.504 1.00 12.43 ? 324 ALA A CA 1 ATOM 2502 C C . ALA A 1 324 ? 52.131 11.611 15.669 1.00 12.09 ? 324 ALA A C 1 ATOM 2503 O O . ALA A 1 324 ? 52.187 12.830 15.508 1.00 11.64 ? 324 ALA A O 1 ATOM 2504 C CB . ALA A 1 324 ? 51.417 10.977 17.960 1.00 11.38 ? 324 ALA A CB 1 ATOM 2505 N N . TYR A 1 325 ? 53.003 10.769 15.123 1.00 12.64 ? 325 TYR A N 1 ATOM 2506 C CA . TYR A 1 325 ? 54.070 11.267 14.265 1.00 13.44 ? 325 TYR A CA 1 ATOM 2507 C C . TYR A 1 325 ? 53.490 12.094 13.118 1.00 13.12 ? 325 TYR A C 1 ATOM 2508 O O . TYR A 1 325 ? 53.983 13.177 12.787 1.00 13.74 ? 325 TYR A O 1 ATOM 2509 C CB . TYR A 1 325 ? 54.895 10.117 13.713 1.00 15.22 ? 325 TYR A CB 1 ATOM 2510 C CG . TYR A 1 325 ? 56.178 10.571 13.079 1.00 17.53 ? 325 TYR A CG 1 ATOM 2511 C CD1 . TYR A 1 325 ? 56.208 11.016 11.764 1.00 18.19 ? 325 TYR A CD1 1 ATOM 2512 C CD2 . TYR A 1 325 ? 57.370 10.536 13.796 1.00 19.55 ? 325 TYR A CD2 1 ATOM 2513 C CE1 . TYR A 1 325 ? 57.387 11.430 11.183 1.00 19.33 ? 325 TYR A CE1 1 ATOM 2514 C CE2 . TYR A 1 325 ? 58.553 10.945 13.225 1.00 20.93 ? 325 TYR A CE2 1 ATOM 2515 C CZ . TYR A 1 325 ? 58.551 11.394 11.922 1.00 20.70 ? 325 TYR A CZ 1 ATOM 2516 O OH . TYR A 1 325 ? 59.735 11.800 11.358 1.00 22.76 ? 325 TYR A OH 1 ATOM 2517 N N . ARG A 1 326 ? 52.429 11.585 12.521 1.00 13.16 ? 326 ARG A N 1 ATOM 2518 C CA . ARG A 1 326 ? 51.771 12.290 11.421 1.00 12.70 ? 326 ARG A CA 1 ATOM 2519 C C . ARG A 1 326 ? 51.015 13.509 11.909 1.00 12.41 ? 326 ARG A C 1 ATOM 2520 O O . ARG A 1 326 ? 51.130 14.574 11.309 1.00 13.29 ? 326 ARG A O 1 ATOM 2521 C CB . ARG A 1 326 ? 50.883 11.340 10.639 1.00 11.93 ? 326 ARG A CB 1 ATOM 2522 C CG . ARG A 1 326 ? 51.705 10.221 9.989 1.00 14.45 ? 326 ARG A CG 1 ATOM 2523 C CD . ARG A 1 326 ? 50.822 9.163 9.378 1.00 15.11 ? 326 ARG A CD 1 ATOM 2524 N NE . ARG A 1 326 ? 51.637 8.103 8.793 1.00 17.14 ? 326 ARG A NE 1 ATOM 2525 C CZ . ARG A 1 326 ? 51.207 7.205 7.914 1.00 17.46 ? 326 ARG A CZ 1 ATOM 2526 N NH1 . ARG A 1 326 ? 52.061 6.293 7.448 1.00 18.22 ? 326 ARG A NH1 1 ATOM 2527 N NH2 . ARG A 1 326 ? 49.941 7.202 7.509 1.00 17.19 ? 326 ARG A NH2 1 ATOM 2528 N N . ALA A 1 327 ? 50.292 13.379 13.021 1.00 11.90 ? 327 ALA A N 1 ATOM 2529 C CA . ALA A 1 327 ? 49.551 14.520 13.569 1.00 11.81 ? 327 ALA A CA 1 ATOM 2530 C C . ALA A 1 327 ? 50.503 15.667 13.864 1.00 11.43 ? 327 ALA A C 1 ATOM 2531 O O . ALA A 1 327 ? 50.230 16.820 13.520 1.00 11.70 ? 327 ALA A O 1 ATOM 2532 C CB . ALA A 1 327 ? 48.797 14.127 14.829 1.00 11.46 ? 327 ALA A CB 1 ATOM 2533 N N . LEU A 1 328 ? 51.641 15.345 14.469 1.00 11.12 ? 328 LEU A N 1 ATOM 2534 C CA . LEU A 1 328 ? 52.527 16.394 14.964 1.00 11.59 ? 328 LEU A CA 1 ATOM 2535 C C . LEU A 1 328 ? 53.351 17.015 13.841 1.00 11.87 ? 328 LEU A C 1 ATOM 2536 O O . LEU A 1 328 ? 53.591 18.222 13.840 1.00 12.04 ? 328 LEU A O 1 ATOM 2537 C CB . LEU A 1 328 ? 53.401 15.895 16.121 1.00 11.40 ? 328 LEU A CB 1 ATOM 2538 C CG . LEU A 1 328 ? 52.638 15.438 17.382 1.00 12.18 ? 328 LEU A CG 1 ATOM 2539 C CD1 . LEU A 1 328 ? 53.624 15.027 18.462 1.00 12.86 ? 328 LEU A CD1 1 ATOM 2540 C CD2 . LEU A 1 328 ? 51.652 16.513 17.908 1.00 12.06 ? 328 LEU A CD2 1 ATOM 2541 N N . THR A 1 329 ? 53.781 16.203 12.880 1.00 11.71 ? 329 THR A N 1 ATOM 2542 C CA . THR A 1 329 ? 54.505 16.766 11.739 1.00 12.19 ? 329 THR A CA 1 ATOM 2543 C C . THR A 1 329 ? 53.594 17.652 10.901 1.00 11.72 ? 329 THR A C 1 ATOM 2544 O O . THR A 1 329 ? 54.017 18.700 10.440 1.00 11.83 ? 329 THR A O 1 ATOM 2545 C CB . THR A 1 329 ? 55.202 15.706 10.864 1.00 12.04 ? 329 THR A CB 1 ATOM 2546 O OG1 . THR A 1 329 ? 54.248 14.719 10.477 1.00 12.43 ? 329 THR A OG1 1 ATOM 2547 C CG2 . THR A 1 329 ? 56.364 15.037 11.644 1.00 14.14 ? 329 THR A CG2 1 ATOM 2548 N N . GLU A 1 330 ? 52.341 17.253 10.715 1.00 11.72 ? 330 GLU A N 1 ATOM 2549 C CA . GLU A 1 330 ? 51.365 18.163 10.095 1.00 11.60 ? 330 GLU A CA 1 ATOM 2550 C C . GLU A 1 330 ? 51.196 19.470 10.899 1.00 11.40 ? 330 GLU A C 1 ATOM 2551 O O . GLU A 1 330 ? 51.028 20.553 10.323 1.00 11.08 ? 330 GLU A O 1 ATOM 2552 C CB . GLU A 1 330 ? 50.010 17.473 9.915 1.00 11.87 ? 330 GLU A CB 1 ATOM 2553 C CG . GLU A 1 330 ? 50.019 16.293 8.922 1.00 12.86 ? 330 GLU A CG 1 ATOM 2554 C CD . GLU A 1 330 ? 50.454 16.700 7.530 1.00 15.45 ? 330 GLU A CD 1 ATOM 2555 O OE1 . GLU A 1 330 ? 51.536 16.235 7.114 1.00 16.91 ? 330 GLU A OE1 1 ATOM 2556 O OE2 . GLU A 1 330 ? 49.718 17.467 6.852 1.00 15.32 ? 330 GLU A OE2 1 ATOM 2557 N N . THR A 1 331 ? 51.245 19.370 12.222 1.00 11.08 ? 331 THR A N 1 ATOM 2558 C CA . THR A 1 331 ? 51.058 20.551 13.064 1.00 11.80 ? 331 THR A CA 1 ATOM 2559 C C . THR A 1 331 ? 52.227 21.506 12.858 1.00 12.13 ? 331 THR A C 1 ATOM 2560 O O . THR A 1 331 ? 52.033 22.733 12.731 1.00 12.77 ? 331 THR A O 1 ATOM 2561 C CB . THR A 1 331 ? 50.887 20.189 14.557 1.00 12.02 ? 331 THR A CB 1 ATOM 2562 O OG1 . THR A 1 331 ? 49.767 19.318 14.697 1.00 11.29 ? 331 THR A OG1 1 ATOM 2563 C CG2 . THR A 1 331 ? 50.623 21.460 15.399 1.00 11.91 ? 331 THR A CG2 1 ATOM 2564 N N . ILE A 1 332 ? 53.438 20.953 12.825 1.00 12.27 ? 332 ILE A N 1 ATOM 2565 C CA . ILE A 1 332 ? 54.615 21.786 12.581 1.00 13.33 ? 332 ILE A CA 1 ATOM 2566 C C . ILE A 1 332 ? 54.527 22.507 11.236 1.00 12.92 ? 332 ILE A C 1 ATOM 2567 O O . ILE A 1 332 ? 54.821 23.715 11.151 1.00 12.92 ? 332 ILE A O 1 ATOM 2568 C CB . ILE A 1 332 ? 55.921 20.992 12.714 1.00 13.41 ? 332 ILE A CB 1 ATOM 2569 C CG1 . ILE A 1 332 ? 56.091 20.570 14.184 1.00 14.09 ? 332 ILE A CG1 1 ATOM 2570 C CG2 . ILE A 1 332 ? 57.106 21.834 12.238 1.00 14.31 ? 332 ILE A CG2 1 ATOM 2571 C CD1 . ILE A 1 332 ? 57.195 19.559 14.391 1.00 16.50 ? 332 ILE A CD1 1 ATOM 2572 N N . MET A 1 333 ? 54.131 21.781 10.187 1.00 12.67 ? 333 MET A N 1 ATOM 2573 C CA . MET A 1 333 ? 53.989 22.419 8.864 1.00 13.15 ? 333 MET A CA 1 ATOM 2574 C C . MET A 1 333 ? 52.933 23.518 8.900 1.00 12.74 ? 333 MET A C 1 ATOM 2575 O O . MET A 1 333 ? 53.086 24.569 8.263 1.00 12.50 ? 333 MET A O 1 ATOM 2576 C CB . MET A 1 333 ? 53.650 21.404 7.773 1.00 13.91 ? 333 MET A CB 1 ATOM 2577 C CG . MET A 1 333 ? 53.338 22.059 6.383 1.00 17.08 ? 333 MET A CG 1 ATOM 2578 S SD . MET A 1 333 ? 54.528 23.275 5.726 1.00 24.64 ? 333 MET A SD 1 ATOM 2579 C CE . MET A 1 333 ? 55.915 22.190 5.371 1.00 24.31 ? 333 MET A CE 1 ATOM 2580 N N . PHE A 1 334 ? 51.861 23.262 9.639 1.00 12.00 ? 334 PHE A N 1 ATOM 2581 C CA . PHE A 1 334 ? 50.814 24.240 9.811 1.00 12.28 ? 334 PHE A CA 1 ATOM 2582 C C . PHE A 1 334 ? 51.395 25.487 10.500 1.00 12.09 ? 334 PHE A C 1 ATOM 2583 O O . PHE A 1 334 ? 51.147 26.624 10.088 1.00 12.22 ? 334 PHE A O 1 ATOM 2584 C CB . PHE A 1 334 ? 49.661 23.614 10.614 1.00 11.22 ? 334 PHE A CB 1 ATOM 2585 C CG . PHE A 1 334 ? 48.592 24.589 11.037 1.00 11.94 ? 334 PHE A CG 1 ATOM 2586 C CD1 . PHE A 1 334 ? 47.814 25.278 10.095 1.00 11.34 ? 334 PHE A CD1 1 ATOM 2587 C CD2 . PHE A 1 334 ? 48.333 24.787 12.397 1.00 11.02 ? 334 PHE A CD2 1 ATOM 2588 C CE1 . PHE A 1 334 ? 46.800 26.152 10.521 1.00 10.95 ? 334 PHE A CE1 1 ATOM 2589 C CE2 . PHE A 1 334 ? 47.352 25.665 12.823 1.00 9.94 ? 334 PHE A CE2 1 ATOM 2590 C CZ . PHE A 1 334 ? 46.574 26.343 11.878 1.00 9.89 ? 334 PHE A CZ 1 ATOM 2591 N N . ASP A 1 335 ? 52.161 25.274 11.557 1.00 12.19 ? 335 ASP A N 1 ATOM 2592 C CA . ASP A 1 335 ? 52.784 26.390 12.259 1.00 12.29 ? 335 ASP A CA 1 ATOM 2593 C C . ASP A 1 335 ? 53.775 27.138 11.357 1.00 12.66 ? 335 ASP A C 1 ATOM 2594 O O . ASP A 1 335 ? 53.887 28.360 11.423 1.00 13.12 ? 335 ASP A O 1 ATOM 2595 C CB . ASP A 1 335 ? 53.476 25.899 13.526 1.00 12.41 ? 335 ASP A CB 1 ATOM 2596 C CG . ASP A 1 335 ? 53.930 27.049 14.403 1.00 14.43 ? 335 ASP A CG 1 ATOM 2597 O OD1 . ASP A 1 335 ? 53.060 27.800 14.883 1.00 14.13 ? 335 ASP A OD1 1 ATOM 2598 O OD2 . ASP A 1 335 ? 55.147 27.211 14.588 1.00 15.67 ? 335 ASP A OD2 1 ATOM 2599 N N . ASP A 1 336 ? 54.487 26.403 10.510 1.00 12.61 ? 336 ASP A N 1 ATOM 2600 C CA . ASP A 1 336 ? 55.386 27.009 9.519 1.00 13.13 ? 336 ASP A CA 1 ATOM 2601 C C . ASP A 1 336 ? 54.626 27.918 8.539 1.00 12.75 ? 336 ASP A C 1 ATOM 2602 O O . ASP A 1 336 ? 55.142 28.972 8.141 1.00 12.17 ? 336 ASP A O 1 ATOM 2603 C CB . ASP A 1 336 ? 56.124 25.928 8.731 1.00 13.65 ? 336 ASP A CB 1 ATOM 2604 C CG . ASP A 1 336 ? 57.198 25.232 9.545 1.00 16.20 ? 336 ASP A CG 1 ATOM 2605 O OD1 . ASP A 1 336 ? 57.594 25.742 10.612 1.00 17.35 ? 336 ASP A OD1 1 ATOM 2606 O OD2 . ASP A 1 336 ? 57.650 24.160 9.096 1.00 19.23 ? 336 ASP A OD2 1 ATOM 2607 N N . ALA A 1 337 ? 53.416 27.505 8.151 1.00 12.21 ? 337 ALA A N 1 ATOM 2608 C CA . ALA A 1 337 ? 52.581 28.323 7.275 1.00 12.41 ? 337 ALA A CA 1 ATOM 2609 C C . ALA A 1 337 ? 52.126 29.600 7.975 1.00 12.57 ? 337 ALA A C 1 ATOM 2610 O O . ALA A 1 337 ? 52.058 30.667 7.346 1.00 13.09 ? 337 ALA A O 1 ATOM 2611 C CB . ALA A 1 337 ? 51.364 27.517 6.742 1.00 12.17 ? 337 ALA A CB 1 ATOM 2612 N N . ILE A 1 338 ? 51.783 29.487 9.257 1.00 12.66 ? 338 ILE A N 1 ATOM 2613 C CA . ILE A 1 338 ? 51.434 30.647 10.099 1.00 12.71 ? 338 ILE A CA 1 ATOM 2614 C C . ILE A 1 338 ? 52.622 31.610 10.135 1.00 13.34 ? 338 ILE A C 1 ATOM 2615 O O . ILE A 1 338 ? 52.493 32.809 9.897 1.00 13.93 ? 338 ILE A O 1 ATOM 2616 C CB . ILE A 1 338 ? 51.085 30.198 11.550 1.00 12.29 ? 338 ILE A CB 1 ATOM 2617 C CG1 . ILE A 1 338 ? 49.783 29.382 11.551 1.00 12.03 ? 338 ILE A CG1 1 ATOM 2618 C CG2 . ILE A 1 338 ? 50.977 31.415 12.522 1.00 12.90 ? 338 ILE A CG2 1 ATOM 2619 C CD1 . ILE A 1 338 ? 49.567 28.555 12.799 1.00 9.82 ? 338 ILE A CD1 1 ATOM 2620 N N . GLU A 1 339 ? 53.791 31.066 10.421 1.00 13.63 ? 339 GLU A N 1 ATOM 2621 C CA . GLU A 1 339 ? 54.995 31.870 10.447 1.00 14.74 ? 339 GLU A CA 1 ATOM 2622 C C . GLU A 1 339 ? 55.210 32.564 9.107 1.00 14.44 ? 339 GLU A C 1 ATOM 2623 O O . GLU A 1 339 ? 55.508 33.760 9.069 1.00 14.78 ? 339 GLU A O 1 ATOM 2624 C CB . GLU A 1 339 ? 56.179 30.992 10.785 1.00 15.25 ? 339 GLU A CB 1 ATOM 2625 C CG . GLU A 1 339 ? 57.490 31.725 10.834 1.00 19.89 ? 339 GLU A CG 1 ATOM 2626 C CD . GLU A 1 339 ? 58.590 30.813 11.281 1.00 26.19 ? 339 GLU A CD 1 ATOM 2627 O OE1 . GLU A 1 339 ? 59.148 31.076 12.356 1.00 31.11 ? 339 GLU A OE1 1 ATOM 2628 O OE2 . GLU A 1 339 ? 58.868 29.822 10.579 1.00 27.93 ? 339 GLU A OE2 1 ATOM 2629 N N . ARG A 1 340 ? 55.062 31.816 8.015 1.00 14.05 ? 340 ARG A N 1 ATOM 2630 C CA . ARG A 1 340 ? 55.284 32.375 6.676 1.00 14.26 ? 340 ARG A CA 1 ATOM 2631 C C . ARG A 1 340 ? 54.282 33.501 6.377 1.00 14.01 ? 340 ARG A C 1 ATOM 2632 O O . ARG A 1 340 ? 54.661 34.567 5.858 1.00 14.07 ? 340 ARG A O 1 ATOM 2633 C CB . ARG A 1 340 ? 55.238 31.279 5.597 1.00 14.31 ? 340 ARG A CB 1 ATOM 2634 C CG . ARG A 1 340 ? 55.635 31.777 4.185 1.00 14.97 ? 340 ARG A CG 1 ATOM 2635 C CD . ARG A 1 340 ? 56.978 32.484 4.223 1.00 14.96 ? 340 ARG A CD 1 ATOM 2636 N NE . ARG A 1 340 ? 57.311 33.107 2.942 1.00 15.99 ? 340 ARG A NE 1 ATOM 2637 C CZ . ARG A 1 340 ? 58.170 34.110 2.810 1.00 16.32 ? 340 ARG A CZ 1 ATOM 2638 N NH1 . ARG A 1 340 ? 58.778 34.619 3.890 1.00 16.76 ? 340 ARG A NH1 1 ATOM 2639 N NH2 . ARG A 1 340 ? 58.403 34.613 1.608 1.00 14.60 ? 340 ARG A NH2 1 ATOM 2640 N N . ALA A 1 341 ? 53.014 33.282 6.720 1.00 13.73 ? 341 ALA A N 1 ATOM 2641 C CA . ALA A 1 341 ? 52.007 34.314 6.506 1.00 13.87 ? 341 ALA A CA 1 ATOM 2642 C C . ALA A 1 341 ? 52.338 35.571 7.310 1.00 13.87 ? 341 ALA A C 1 ATOM 2643 O O . ALA A 1 341 ? 52.171 36.682 6.820 1.00 14.58 ? 341 ALA A O 1 ATOM 2644 C CB . ALA A 1 341 ? 50.619 33.780 6.844 1.00 13.44 ? 341 ALA A CB 1 ATOM 2645 N N . GLY A 1 342 ? 52.858 35.411 8.522 1.00 14.02 ? 342 GLY A N 1 ATOM 2646 C CA . GLY A 1 342 ? 53.230 36.576 9.347 1.00 13.85 ? 342 GLY A CA 1 ATOM 2647 C C . GLY A 1 342 ? 54.365 37.380 8.730 1.00 14.55 ? 342 GLY A C 1 ATOM 2648 O O . GLY A 1 342 ? 54.470 38.574 8.960 1.00 14.55 ? 342 GLY A O 1 ATOM 2649 N N . GLN A 1 343 ? 55.209 36.724 7.929 1.00 14.98 ? 343 GLN A N 1 ATOM 2650 C CA . GLN A 1 343 ? 56.299 37.403 7.239 1.00 15.69 ? 343 GLN A CA 1 ATOM 2651 C C . GLN A 1 343 ? 55.782 38.215 6.056 1.00 16.53 ? 343 GLN A C 1 ATOM 2652 O O . GLN A 1 343 ? 56.371 39.228 5.681 1.00 16.95 ? 343 GLN A O 1 ATOM 2653 C CB . GLN A 1 343 ? 57.338 36.400 6.765 1.00 15.51 ? 343 GLN A CB 1 ATOM 2654 C CG . GLN A 1 343 ? 58.130 35.793 7.912 1.00 17.02 ? 343 GLN A CG 1 ATOM 2655 C CD . GLN A 1 343 ? 59.055 34.703 7.442 1.00 18.78 ? 343 GLN A CD 1 ATOM 2656 O OE1 . GLN A 1 343 ? 58.676 33.842 6.640 1.00 19.04 ? 343 GLN A OE1 1 ATOM 2657 N NE2 . GLN A 1 343 ? 60.273 34.721 7.942 1.00 20.86 ? 343 GLN A NE2 1 ATOM 2658 N N . LEU A 1 344 ? 54.679 37.753 5.478 1.00 16.81 ? 344 LEU A N 1 ATOM 2659 C CA . LEU A 1 344 ? 54.180 38.294 4.236 1.00 16.95 ? 344 LEU A CA 1 ATOM 2660 C C . LEU A 1 344 ? 53.060 39.288 4.454 1.00 17.50 ? 344 LEU A C 1 ATOM 2661 O O . LEU A 1 344 ? 52.563 39.863 3.503 1.00 18.10 ? 344 LEU A O 1 ATOM 2662 C CB . LEU A 1 344 ? 53.700 37.171 3.312 1.00 16.94 ? 344 LEU A CB 1 ATOM 2663 C CG . LEU A 1 344 ? 54.819 36.302 2.743 1.00 16.86 ? 344 LEU A CG 1 ATOM 2664 C CD1 . LEU A 1 344 ? 54.233 35.146 1.953 1.00 17.97 ? 344 LEU A CD1 1 ATOM 2665 C CD2 . LEU A 1 344 ? 55.750 37.135 1.893 1.00 17.85 ? 344 LEU A CD2 1 ATOM 2666 N N . THR A 1 345 ? 52.661 39.487 5.703 1.00 17.17 ? 345 THR A N 1 ATOM 2667 C CA . THR A 1 345 ? 51.561 40.394 6.015 1.00 16.88 ? 345 THR A CA 1 ATOM 2668 C C . THR A 1 345 ? 51.945 41.239 7.206 1.00 17.24 ? 345 THR A C 1 ATOM 2669 O O . THR A 1 345 ? 52.868 40.903 7.953 1.00 16.81 ? 345 THR A O 1 ATOM 2670 C CB . THR A 1 345 ? 50.246 39.640 6.333 1.00 16.59 ? 345 THR A CB 1 ATOM 2671 O OG1 . THR A 1 345 ? 50.468 38.722 7.411 1.00 17.03 ? 345 THR A OG1 1 ATOM 2672 C CG2 . THR A 1 345 ? 49.696 38.891 5.086 1.00 17.10 ? 345 THR A CG2 1 ATOM 2673 N N . SER A 1 346 ? 51.223 42.330 7.405 1.00 17.71 ? 346 SER A N 1 ATOM 2674 C CA . SER A 1 346 ? 51.525 43.211 8.506 1.00 17.58 ? 346 SER A CA 1 ATOM 2675 C C . SER A 1 346 ? 50.454 43.090 9.576 1.00 17.51 ? 346 SER A C 1 ATOM 2676 O O . SER A 1 346 ? 49.269 43.145 9.271 1.00 17.28 ? 346 SER A O 1 ATOM 2677 C CB . SER A 1 346 ? 51.608 44.650 8.017 1.00 17.80 ? 346 SER A CB 1 ATOM 2678 O OG . SER A 1 346 ? 51.686 45.522 9.135 1.00 18.83 ? 346 SER A OG 1 ATOM 2679 N N . GLU A 1 347 ? 50.868 42.958 10.830 1.00 17.58 ? 347 GLU A N 1 ATOM 2680 C CA . GLU A 1 347 ? 49.902 42.942 11.924 1.00 18.46 ? 347 GLU A CA 1 ATOM 2681 C C . GLU A 1 347 ? 49.282 44.321 12.160 1.00 18.01 ? 347 GLU A C 1 ATOM 2682 O O . GLU A 1 347 ? 48.323 44.431 12.905 1.00 16.90 ? 347 GLU A O 1 ATOM 2683 C CB . GLU A 1 347 ? 50.501 42.365 13.212 1.00 18.72 ? 347 GLU A CB 1 ATOM 2684 C CG . GLU A 1 347 ? 51.401 43.306 13.973 1.00 20.71 ? 347 GLU A CG 1 ATOM 2685 C CD . GLU A 1 347 ? 51.982 42.674 15.240 1.00 21.41 ? 347 GLU A CD 1 ATOM 2686 O OE1 . GLU A 1 347 ? 51.316 41.830 15.886 1.00 23.39 ? 347 GLU A OE1 1 ATOM 2687 O OE2 . GLU A 1 347 ? 53.117 43.045 15.588 1.00 27.69 ? 347 GLU A OE2 1 ATOM 2688 N N . GLU A 1 348 ? 49.823 45.361 11.510 1.00 17.67 ? 348 GLU A N 1 ATOM 2689 C CA . GLU A 1 348 ? 49.186 46.683 11.522 1.00 18.61 ? 348 GLU A CA 1 ATOM 2690 C C . GLU A 1 348 ? 47.826 46.676 10.813 1.00 17.92 ? 348 GLU A C 1 ATOM 2691 O O . GLU A 1 348 ? 46.936 47.440 11.166 1.00 18.48 ? 348 GLU A O 1 ATOM 2692 C CB . GLU A 1 348 ? 50.084 47.743 10.868 1.00 19.27 ? 348 GLU A CB 1 ATOM 2693 C CG . GLU A 1 348 ? 51.386 48.030 11.624 1.00 24.84 ? 348 GLU A CG 1 ATOM 2694 C CD . GLU A 1 348 ? 51.169 48.313 13.104 1.00 30.77 ? 348 GLU A CD 1 ATOM 2695 O OE1 . GLU A 1 348 ? 51.860 47.677 13.928 1.00 34.76 ? 348 GLU A OE1 1 ATOM 2696 O OE2 . GLU A 1 348 ? 50.309 49.164 13.444 1.00 33.58 ? 348 GLU A OE2 1 ATOM 2697 N N . ASP A 1 349 ? 47.658 45.820 9.809 1.00 17.19 ? 349 ASP A N 1 ATOM 2698 C CA . ASP A 1 349 ? 46.411 45.843 9.053 1.00 16.46 ? 349 ASP A CA 1 ATOM 2699 C C . ASP A 1 349 ? 45.790 44.458 8.820 1.00 16.14 ? 349 ASP A C 1 ATOM 2700 O O . ASP A 1 349 ? 44.745 44.334 8.165 1.00 14.79 ? 349 ASP A O 1 ATOM 2701 C CB . ASP A 1 349 ? 46.597 46.638 7.737 1.00 16.82 ? 349 ASP A CB 1 ATOM 2702 C CG . ASP A 1 349 ? 47.431 45.898 6.702 1.00 17.51 ? 349 ASP A CG 1 ATOM 2703 O OD1 . ASP A 1 349 ? 47.576 46.426 5.579 1.00 18.33 ? 349 ASP A OD1 1 ATOM 2704 O OD2 . ASP A 1 349 ? 47.932 44.791 6.997 1.00 18.28 ? 349 ASP A OD2 1 ATOM 2705 N N . THR A 1 350 ? 46.427 43.426 9.375 1.00 15.15 ? 350 THR A N 1 ATOM 2706 C CA . THR A 1 350 ? 45.957 42.052 9.188 1.00 14.99 ? 350 THR A CA 1 ATOM 2707 C C . THR A 1 350 ? 45.583 41.435 10.518 1.00 14.26 ? 350 THR A C 1 ATOM 2708 O O . THR A 1 350 ? 46.416 41.318 11.420 1.00 15.32 ? 350 THR A O 1 ATOM 2709 C CB . THR A 1 350 ? 47.030 41.175 8.478 1.00 14.37 ? 350 THR A CB 1 ATOM 2710 O OG1 . THR A 1 350 ? 47.398 41.800 7.247 1.00 15.78 ? 350 THR A OG1 1 ATOM 2711 C CG2 . THR A 1 350 ? 46.530 39.744 8.203 1.00 14.73 ? 350 THR A CG2 1 ATOM 2712 N N . LEU A 1 351 ? 44.325 41.049 10.656 1.00 13.30 ? 351 LEU A N 1 ATOM 2713 C CA . LEU A 1 351 ? 43.946 40.258 11.818 1.00 13.33 ? 351 LEU A CA 1 ATOM 2714 C C . LEU A 1 351 ? 44.150 38.785 11.493 1.00 13.09 ? 351 LEU A C 1 ATOM 2715 O O . LEU A 1 351 ? 43.582 38.269 10.525 1.00 13.64 ? 351 LEU A O 1 ATOM 2716 C CB . LEU A 1 351 ? 42.501 40.526 12.219 1.00 12.78 ? 351 LEU A CB 1 ATOM 2717 C CG . LEU A 1 351 ? 41.943 39.657 13.345 1.00 13.02 ? 351 LEU A CG 1 ATOM 2718 C CD1 . LEU A 1 351 ? 42.722 39.829 14.660 1.00 11.47 ? 351 LEU A CD1 1 ATOM 2719 C CD2 . LEU A 1 351 ? 40.456 39.970 13.565 1.00 14.29 ? 351 LEU A CD2 1 ATOM 2720 N N . SER A 1 352 ? 44.990 38.118 12.275 1.00 12.78 ? 352 SER A N 1 ATOM 2721 C CA . SER A 1 352 ? 45.257 36.714 12.049 1.00 12.93 ? 352 SER A CA 1 ATOM 2722 C C . SER A 1 352 ? 44.762 35.965 13.267 1.00 12.63 ? 352 SER A C 1 ATOM 2723 O O . SER A 1 352 ? 45.120 36.319 14.387 1.00 12.30 ? 352 SER A O 1 ATOM 2724 C CB . SER A 1 352 ? 46.750 36.460 11.885 1.00 12.66 ? 352 SER A CB 1 ATOM 2725 O OG . SER A 1 352 ? 47.277 37.174 10.777 1.00 14.09 ? 352 SER A OG 1 ATOM 2726 N N . LEU A 1 353 ? 43.921 34.958 13.051 1.00 12.57 ? 353 LEU A N 1 ATOM 2727 C CA . LEU A 1 353 ? 43.577 34.029 14.118 1.00 12.92 ? 353 LEU A CA 1 ATOM 2728 C C . LEU A 1 353 ? 44.053 32.623 13.792 1.00 12.82 ? 353 LEU A C 1 ATOM 2729 O O . LEU A 1 353 ? 43.883 32.140 12.673 1.00 12.07 ? 353 LEU A O 1 ATOM 2730 C CB . LEU A 1 353 ? 42.068 33.959 14.378 1.00 13.94 ? 353 LEU A CB 1 ATOM 2731 C CG . LEU A 1 353 ? 41.105 35.135 14.604 1.00 17.53 ? 353 LEU A CG 1 ATOM 2732 C CD1 . LEU A 1 353 ? 39.935 34.657 15.468 1.00 16.29 ? 353 LEU A CD1 1 ATOM 2733 C CD2 . LEU A 1 353 ? 41.724 36.355 15.189 1.00 18.89 ? 353 LEU A CD2 1 ATOM 2734 N N . VAL A 1 354 ? 44.620 31.961 14.798 1.00 12.47 ? 354 VAL A N 1 ATOM 2735 C CA . VAL A 1 354 ? 44.992 30.563 14.703 1.00 11.61 ? 354 VAL A CA 1 ATOM 2736 C C . VAL A 1 354 ? 44.077 29.834 15.663 1.00 12.12 ? 354 VAL A C 1 ATOM 2737 O O . VAL A 1 354 ? 43.949 30.231 16.833 1.00 12.78 ? 354 VAL A O 1 ATOM 2738 C CB . VAL A 1 354 ? 46.446 30.332 15.135 1.00 11.92 ? 354 VAL A CB 1 ATOM 2739 C CG1 . VAL A 1 354 ? 46.784 28.831 15.082 1.00 10.81 ? 354 VAL A CG1 1 ATOM 2740 C CG2 . VAL A 1 354 ? 47.392 31.153 14.247 1.00 9.71 ? 354 VAL A CG2 1 ATOM 2741 N N . THR A 1 355 ? 43.431 28.777 15.192 1.00 11.42 ? 355 THR A N 1 ATOM 2742 C CA . THR A 1 355 ? 42.630 27.964 16.112 1.00 11.86 ? 355 THR A CA 1 ATOM 2743 C C . THR A 1 355 ? 42.526 26.539 15.623 1.00 11.79 ? 355 THR A C 1 ATOM 2744 O O . THR A 1 355 ? 43.133 26.178 14.611 1.00 11.94 ? 355 THR A O 1 ATOM 2745 C CB . THR A 1 355 ? 41.226 28.603 16.394 1.00 12.20 ? 355 THR A CB 1 ATOM 2746 O OG1 . THR A 1 355 ? 40.660 28.019 17.567 1.00 12.83 ? 355 THR A OG1 1 ATOM 2747 C CG2 . THR A 1 355 ? 40.258 28.438 15.200 1.00 13.02 ? 355 THR A CG2 1 ATOM 2748 N N . ALA A 1 356 ? 41.766 25.734 16.354 1.00 11.39 ? 356 ALA A N 1 ATOM 2749 C CA . ALA A 1 356 ? 41.471 24.382 15.945 1.00 11.04 ? 356 ALA A CA 1 ATOM 2750 C C . ALA A 1 356 ? 39.968 24.288 15.858 1.00 11.15 ? 356 ALA A C 1 ATOM 2751 O O . ALA A 1 356 ? 39.271 25.049 16.523 1.00 11.61 ? 356 ALA A O 1 ATOM 2752 C CB . ALA A 1 356 ? 41.998 23.388 16.964 1.00 10.62 ? 356 ALA A CB 1 ATOM 2753 N N . ASP A 1 357 ? 39.464 23.368 15.048 1.00 10.39 ? 357 ASP A N 1 ATOM 2754 C CA . ASP A 1 357 ? 38.029 23.138 15.058 1.00 10.16 ? 357 ASP A CA 1 ATOM 2755 C C . ASP A 1 357 ? 37.616 22.349 16.294 1.00 10.26 ? 357 ASP A C 1 ATOM 2756 O O . ASP A 1 357 ? 36.523 22.527 16.789 1.00 10.27 ? 357 ASP A O 1 ATOM 2757 C CB . ASP A 1 357 ? 37.518 22.489 13.754 1.00 10.16 ? 357 ASP A CB 1 ATOM 2758 C CG . ASP A 1 357 ? 38.251 21.212 13.376 1.00 10.47 ? 357 ASP A CG 1 ATOM 2759 O OD1 . ASP A 1 357 ? 39.313 20.883 13.954 1.00 9.70 ? 357 ASP A OD1 1 ATOM 2760 O OD2 . ASP A 1 357 ? 37.732 20.511 12.477 1.00 11.66 ? 357 ASP A OD2 1 ATOM 2761 N N . HIS A 1 358 ? 38.519 21.509 16.806 1.00 10.04 ? 358 HIS A N 1 ATOM 2762 C CA . HIS A 1 358 ? 38.249 20.687 17.972 1.00 10.28 ? 358 HIS A CA 1 ATOM 2763 C C . HIS A 1 358 ? 39.528 19.922 18.230 1.00 10.42 ? 358 HIS A C 1 ATOM 2764 O O . HIS A 1 358 ? 40.499 20.015 17.461 1.00 10.39 ? 358 HIS A O 1 ATOM 2765 C CB . HIS A 1 358 ? 37.137 19.671 17.677 1.00 10.14 ? 358 HIS A CB 1 ATOM 2766 C CG . HIS A 1 358 ? 37.441 18.864 16.474 1.00 11.25 ? 358 HIS A CG 1 ATOM 2767 N ND1 . HIS A 1 358 ? 38.365 17.836 16.491 1.00 11.34 ? 358 HIS A ND1 1 ATOM 2768 C CD2 . HIS A 1 358 ? 37.073 19.028 15.184 1.00 11.46 ? 358 HIS A CD2 1 ATOM 2769 C CE1 . HIS A 1 358 ? 38.525 17.380 15.264 1.00 11.87 ? 358 HIS A CE1 1 ATOM 2770 N NE2 . HIS A 1 358 ? 37.743 18.079 14.454 1.00 12.00 ? 358 HIS A NE2 1 ATOM 2771 N N . SER A 1 359 ? 39.525 19.151 19.306 1.00 9.80 ? 359 SER A N 1 ATOM 2772 C CA . SER A 1 359 ? 40.692 18.374 19.696 1.00 10.69 ? 359 SER A CA 1 ATOM 2773 C C . SER A 1 359 ? 40.517 16.864 19.391 1.00 10.12 ? 359 SER A C 1 ATOM 2774 O O . SER A 1 359 ? 39.642 16.477 18.615 1.00 10.33 ? 359 SER A O 1 ATOM 2775 C CB . SER A 1 359 ? 40.936 18.633 21.195 1.00 9.88 ? 359 SER A CB 1 ATOM 2776 O OG . SER A 1 359 ? 42.121 18.011 21.668 1.00 12.28 ? 359 SER A OG 1 ATOM 2777 N N . HIS A 1 360 ? 41.362 16.046 20.011 1.00 10.27 ? 360 HIS A N 1 ATOM 2778 C CA . HIS A 1 360 ? 41.391 14.581 19.884 1.00 10.42 ? 360 HIS A CA 1 ATOM 2779 C C . HIS A 1 360 ? 41.722 14.065 21.250 1.00 10.92 ? 360 HIS A C 1 ATOM 2780 O O . HIS A 1 360 ? 42.220 14.826 22.077 1.00 11.02 ? 360 HIS A O 1 ATOM 2781 C CB . HIS A 1 360 ? 42.507 14.132 18.957 1.00 9.73 ? 360 HIS A CB 1 ATOM 2782 C CG . HIS A 1 360 ? 42.168 14.326 17.525 1.00 10.87 ? 360 HIS A CG 1 ATOM 2783 N ND1 . HIS A 1 360 ? 41.588 13.354 16.733 1.00 11.49 ? 360 HIS A ND1 1 ATOM 2784 C CD2 . HIS A 1 360 ? 42.255 15.434 16.761 1.00 9.51 ? 360 HIS A CD2 1 ATOM 2785 C CE1 . HIS A 1 360 ? 41.380 13.852 15.522 1.00 10.89 ? 360 HIS A CE1 1 ATOM 2786 N NE2 . HIS A 1 360 ? 41.760 15.114 15.522 1.00 11.03 ? 360 HIS A NE2 1 ATOM 2787 N N . VAL A 1 361 ? 41.501 12.770 21.456 1.00 10.58 ? 361 VAL A N 1 ATOM 2788 C CA . VAL A 1 361 ? 41.753 12.111 22.742 1.00 11.30 ? 361 VAL A CA 1 ATOM 2789 C C . VAL A 1 361 ? 43.235 11.728 22.881 1.00 11.77 ? 361 VAL A C 1 ATOM 2790 O O . VAL A 1 361 ? 43.590 10.659 23.360 1.00 12.09 ? 361 VAL A O 1 ATOM 2791 C CB . VAL A 1 361 ? 40.805 10.922 22.940 1.00 10.86 ? 361 VAL A CB 1 ATOM 2792 C CG1 . VAL A 1 361 ? 39.360 11.431 22.982 1.00 9.13 ? 361 VAL A CG1 1 ATOM 2793 C CG2 . VAL A 1 361 ? 40.963 9.887 21.822 1.00 10.85 ? 361 VAL A CG2 1 ATOM 2794 N N . PHE A 1 362 ? 44.076 12.668 22.472 1.00 11.90 ? 362 PHE A N 1 ATOM 2795 C CA . PHE A 1 362 ? 45.515 12.539 22.444 1.00 11.77 ? 362 PHE A CA 1 ATOM 2796 C C . PHE A 1 362 ? 46.098 13.078 23.747 1.00 12.44 ? 362 PHE A C 1 ATOM 2797 O O . PHE A 1 362 ? 45.802 14.206 24.164 1.00 13.17 ? 362 PHE A O 1 ATOM 2798 C CB . PHE A 1 362 ? 45.998 13.355 21.249 1.00 12.28 ? 362 PHE A CB 1 ATOM 2799 C CG . PHE A 1 362 ? 47.475 13.514 21.146 1.00 12.35 ? 362 PHE A CG 1 ATOM 2800 C CD1 . PHE A 1 362 ? 48.295 12.419 20.862 1.00 13.42 ? 362 PHE A CD1 1 ATOM 2801 C CD2 . PHE A 1 362 ? 48.050 14.785 21.266 1.00 12.95 ? 362 PHE A CD2 1 ATOM 2802 C CE1 . PHE A 1 362 ? 49.663 12.576 20.729 1.00 11.08 ? 362 PHE A CE1 1 ATOM 2803 C CE2 . PHE A 1 362 ? 49.418 14.949 21.143 1.00 12.74 ? 362 PHE A CE2 1 ATOM 2804 C CZ . PHE A 1 362 ? 50.229 13.844 20.868 1.00 12.18 ? 362 PHE A CZ 1 ATOM 2805 N N . SER A 1 363 ? 46.939 12.283 24.392 1.00 11.74 ? 363 SER A N 1 ATOM 2806 C CA . SER A 1 363 ? 47.540 12.729 25.646 1.00 11.90 ? 363 SER A CA 1 ATOM 2807 C C . SER A 1 363 ? 49.047 12.569 25.637 1.00 12.05 ? 363 SER A C 1 ATOM 2808 O O . SER A 1 363 ? 49.604 11.683 24.984 1.00 11.97 ? 363 SER A O 1 ATOM 2809 C CB . SER A 1 363 ? 46.931 12.017 26.863 1.00 11.06 ? 363 SER A CB 1 ATOM 2810 O OG . SER A 1 363 ? 47.187 10.606 26.821 1.00 12.74 ? 363 SER A OG 1 ATOM 2811 N N . PHE A 1 364 ? 49.683 13.430 26.413 1.00 11.93 ? 364 PHE A N 1 ATOM 2812 C CA . PHE A 1 364 ? 51.099 13.452 26.530 1.00 13.13 ? 364 PHE A CA 1 ATOM 2813 C C . PHE A 1 364 ? 51.406 13.284 28.027 1.00 12.98 ? 364 PHE A C 1 ATOM 2814 O O . PHE A 1 364 ? 51.205 14.200 28.809 1.00 12.84 ? 364 PHE A O 1 ATOM 2815 C CB . PHE A 1 364 ? 51.601 14.775 25.966 1.00 13.79 ? 364 PHE A CB 1 ATOM 2816 C CG . PHE A 1 364 ? 53.014 15.104 26.335 1.00 15.23 ? 364 PHE A CG 1 ATOM 2817 C CD1 . PHE A 1 364 ? 54.001 14.133 26.291 1.00 15.77 ? 364 PHE A CD1 1 ATOM 2818 C CD2 . PHE A 1 364 ? 53.359 16.407 26.694 1.00 17.06 ? 364 PHE A CD2 1 ATOM 2819 C CE1 . PHE A 1 364 ? 55.316 14.439 26.633 1.00 19.06 ? 364 PHE A CE1 1 ATOM 2820 C CE2 . PHE A 1 364 ? 54.676 16.720 27.028 1.00 17.33 ? 364 PHE A CE2 1 ATOM 2821 C CZ . PHE A 1 364 ? 55.646 15.728 26.991 1.00 17.15 ? 364 PHE A CZ 1 ATOM 2822 N N . GLY A 1 365 ? 51.855 12.091 28.407 1.00 13.36 ? 365 GLY A N 1 ATOM 2823 C CA . GLY A 1 365 ? 52.010 11.738 29.821 1.00 13.10 ? 365 GLY A CA 1 ATOM 2824 C C . GLY A 1 365 ? 53.230 10.888 30.095 1.00 14.31 ? 365 GLY A C 1 ATOM 2825 O O . GLY A 1 365 ? 54.236 10.977 29.374 1.00 13.86 ? 365 GLY A O 1 ATOM 2826 N N . GLY A 1 366 ? 53.148 10.063 31.145 1.00 14.31 ? 366 GLY A N 1 ATOM 2827 C CA . GLY A 1 366 ? 54.347 9.417 31.687 1.00 14.41 ? 366 GLY A CA 1 ATOM 2828 C C . GLY A 1 366 ? 55.166 10.558 32.266 1.00 15.44 ? 366 GLY A C 1 ATOM 2829 O O . GLY A 1 366 ? 54.703 11.705 32.327 1.00 16.13 ? 366 GLY A O 1 ATOM 2830 N N . TYR A 1 367 ? 56.377 10.288 32.695 1.00 15.02 ? 367 TYR A N 1 ATOM 2831 C CA . TYR A 1 367 ? 57.186 11.383 33.249 1.00 14.86 ? 367 TYR A CA 1 ATOM 2832 C C . TYR A 1 367 ? 58.518 11.464 32.531 1.00 15.27 ? 367 TYR A C 1 ATOM 2833 O O . TYR A 1 367 ? 59.569 11.236 33.146 1.00 15.48 ? 367 TYR A O 1 ATOM 2834 C CB . TYR A 1 367 ? 57.338 11.236 34.772 1.00 14.08 ? 367 TYR A CB 1 ATOM 2835 C CG . TYR A 1 367 ? 56.002 11.335 35.475 1.00 14.45 ? 367 TYR A CG 1 ATOM 2836 C CD1 . TYR A 1 367 ? 55.402 12.580 35.686 1.00 13.38 ? 367 TYR A CD1 1 ATOM 2837 C CD2 . TYR A 1 367 ? 55.306 10.192 35.864 1.00 14.65 ? 367 TYR A CD2 1 ATOM 2838 C CE1 . TYR A 1 367 ? 54.170 12.689 36.314 1.00 13.21 ? 367 TYR A CE1 1 ATOM 2839 C CE2 . TYR A 1 367 ? 54.055 10.291 36.482 1.00 13.65 ? 367 TYR A CE2 1 ATOM 2840 C CZ . TYR A 1 367 ? 53.503 11.545 36.702 1.00 13.17 ? 367 TYR A CZ 1 ATOM 2841 O OH . TYR A 1 367 ? 52.286 11.658 37.313 1.00 13.34 ? 367 TYR A OH 1 ATOM 2842 N N . PRO A 1 368 ? 58.476 11.793 31.220 1.00 15.21 ? 368 PRO A N 1 ATOM 2843 C CA . PRO A 1 368 ? 59.694 11.809 30.419 1.00 15.51 ? 368 PRO A CA 1 ATOM 2844 C C . PRO A 1 368 ? 60.620 12.938 30.826 1.00 15.85 ? 368 PRO A C 1 ATOM 2845 O O . PRO A 1 368 ? 60.172 14.008 31.235 1.00 15.11 ? 368 PRO A O 1 ATOM 2846 C CB . PRO A 1 368 ? 59.191 12.100 29.006 1.00 15.35 ? 368 PRO A CB 1 ATOM 2847 C CG . PRO A 1 368 ? 57.899 12.838 29.199 1.00 16.03 ? 368 PRO A CG 1 ATOM 2848 C CD . PRO A 1 368 ? 57.294 12.165 30.416 1.00 15.23 ? 368 PRO A CD 1 ATOM 2849 N N . LEU A 1 369 ? 61.903 12.690 30.643 1.00 16.33 ? 369 LEU A N 1 ATOM 2850 C CA . LEU A 1 369 ? 62.930 13.653 30.958 1.00 17.03 ? 369 LEU A CA 1 ATOM 2851 C C . LEU A 1 369 ? 62.947 14.782 29.946 1.00 16.84 ? 369 LEU A C 1 ATOM 2852 O O . LEU A 1 369 ? 62.652 14.588 28.762 1.00 16.33 ? 369 LEU A O 1 ATOM 2853 C CB . LEU A 1 369 ? 64.291 12.976 30.977 1.00 17.07 ? 369 LEU A CB 1 ATOM 2854 C CG . LEU A 1 369 ? 64.488 11.876 32.027 1.00 18.59 ? 369 LEU A CG 1 ATOM 2855 C CD1 . LEU A 1 369 ? 65.940 11.418 31.993 1.00 20.56 ? 369 LEU A CD1 1 ATOM 2856 C CD2 . LEU A 1 369 ? 64.095 12.328 33.424 1.00 19.50 ? 369 LEU A CD2 1 ATOM 2857 N N . ARG A 1 370 ? 63.319 15.960 30.428 1.00 16.73 ? 370 ARG A N 1 ATOM 2858 C CA . ARG A 1 370 ? 63.539 17.101 29.566 1.00 16.99 ? 370 ARG A CA 1 ATOM 2859 C C . ARG A 1 370 ? 64.471 16.699 28.415 1.00 17.82 ? 370 ARG A C 1 ATOM 2860 O O . ARG A 1 370 ? 65.498 16.051 28.631 1.00 17.36 ? 370 ARG A O 1 ATOM 2861 C CB . ARG A 1 370 ? 64.180 18.230 30.368 1.00 17.19 ? 370 ARG A CB 1 ATOM 2862 C CG . ARG A 1 370 ? 64.346 19.532 29.578 1.00 16.54 ? 370 ARG A CG 1 ATOM 2863 C CD . ARG A 1 370 ? 63.036 20.284 29.471 1.00 15.70 ? 370 ARG A CD 1 ATOM 2864 N NE . ARG A 1 370 ? 63.240 21.579 28.809 1.00 17.48 ? 370 ARG A NE 1 ATOM 2865 C CZ . ARG A 1 370 ? 63.716 22.661 29.419 1.00 17.02 ? 370 ARG A CZ 1 ATOM 2866 N NH1 . ARG A 1 370 ? 64.049 22.613 30.707 1.00 16.11 ? 370 ARG A NH1 1 ATOM 2867 N NH2 . ARG A 1 370 ? 63.885 23.783 28.739 1.00 16.63 ? 370 ARG A NH2 1 ATOM 2868 N N . GLY A 1 371 ? 64.069 17.059 27.201 1.00 17.78 ? 371 GLY A N 1 ATOM 2869 C CA . GLY A 1 371 ? 64.843 16.779 26.007 1.00 18.59 ? 371 GLY A CA 1 ATOM 2870 C C . GLY A 1 371 ? 64.581 15.432 25.381 1.00 19.17 ? 371 GLY A C 1 ATOM 2871 O O . GLY A 1 371 ? 65.065 15.168 24.292 1.00 19.16 ? 371 GLY A O 1 ATOM 2872 N N . SER A 1 372 ? 63.808 14.575 26.042 1.00 19.02 ? 372 SER A N 1 ATOM 2873 C CA . SER A 1 372 ? 63.518 13.270 25.468 1.00 19.54 ? 372 SER A CA 1 ATOM 2874 C C . SER A 1 372 ? 62.510 13.399 24.327 1.00 18.73 ? 372 SER A C 1 ATOM 2875 O O . SER A 1 372 ? 61.692 14.326 24.299 1.00 19.17 ? 372 SER A O 1 ATOM 2876 C CB . SER A 1 372 ? 63.024 12.309 26.536 1.00 19.88 ? 372 SER A CB 1 ATOM 2877 O OG . SER A 1 372 ? 61.826 12.821 27.095 1.00 24.72 ? 372 SER A OG 1 ATOM 2878 N N . SER A 1 373 ? 62.598 12.486 23.372 1.00 17.63 ? 373 SER A N 1 ATOM 2879 C CA . SER A 1 373 ? 61.741 12.511 22.190 1.00 16.76 ? 373 SER A CA 1 ATOM 2880 C C . SER A 1 373 ? 60.285 12.346 22.591 1.00 16.71 ? 373 SER A C 1 ATOM 2881 O O . SER A 1 373 ? 59.952 11.475 23.397 1.00 16.61 ? 373 SER A O 1 ATOM 2882 C CB . SER A 1 373 ? 62.100 11.360 21.249 1.00 16.55 ? 373 SER A CB 1 ATOM 2883 O OG . SER A 1 373 ? 61.141 11.275 20.207 1.00 14.93 ? 373 SER A OG 1 ATOM 2884 N N . ILE A 1 374 ? 59.424 13.170 21.999 1.00 16.36 ? 374 ILE A N 1 ATOM 2885 C CA . ILE A 1 374 ? 57.982 13.087 22.210 1.00 15.90 ? 374 ILE A CA 1 ATOM 2886 C C . ILE A 1 374 ? 57.462 11.698 21.786 1.00 15.41 ? 374 ILE A C 1 ATOM 2887 O O . ILE A 1 374 ? 56.429 11.247 22.266 1.00 15.03 ? 374 ILE A O 1 ATOM 2888 C CB . ILE A 1 374 ? 57.241 14.240 21.450 1.00 16.11 ? 374 ILE A CB 1 ATOM 2889 C CG1 . ILE A 1 374 ? 55.823 14.464 21.988 1.00 17.19 ? 374 ILE A CG1 1 ATOM 2890 C CG2 . ILE A 1 374 ? 57.177 13.965 19.952 1.00 16.63 ? 374 ILE A CG2 1 ATOM 2891 C CD1 . ILE A 1 374 ? 55.765 15.233 23.269 1.00 16.80 ? 374 ILE A CD1 1 ATOM 2892 N N . PHE A 1 375 ? 58.188 11.004 20.904 1.00 14.89 ? 375 PHE A N 1 ATOM 2893 C CA . PHE A 1 375 ? 57.731 9.681 20.440 1.00 15.39 ? 375 PHE A CA 1 ATOM 2894 C C . PHE A 1 375 ? 58.331 8.530 21.249 1.00 15.50 ? 375 PHE A C 1 ATOM 2895 O O . PHE A 1 375 ? 58.156 7.351 20.915 1.00 15.80 ? 375 PHE A O 1 ATOM 2896 C CB . PHE A 1 375 ? 57.999 9.512 18.941 1.00 14.41 ? 375 PHE A CB 1 ATOM 2897 C CG . PHE A 1 375 ? 57.403 10.612 18.121 1.00 15.61 ? 375 PHE A CG 1 ATOM 2898 C CD1 . PHE A 1 375 ? 56.016 10.747 18.029 1.00 13.93 ? 375 PHE A CD1 1 ATOM 2899 C CD2 . PHE A 1 375 ? 58.219 11.531 17.467 1.00 14.67 ? 375 PHE A CD2 1 ATOM 2900 C CE1 . PHE A 1 375 ? 55.452 11.783 17.297 1.00 14.45 ? 375 PHE A CE1 1 ATOM 2901 C CE2 . PHE A 1 375 ? 57.668 12.565 16.717 1.00 15.25 ? 375 PHE A CE2 1 ATOM 2902 C CZ . PHE A 1 375 ? 56.283 12.698 16.633 1.00 14.06 ? 375 PHE A CZ 1 ATOM 2903 N N . GLY A 1 376 ? 59.002 8.876 22.339 1.00 15.65 ? 376 GLY A N 1 ATOM 2904 C CA . GLY A 1 376 ? 59.684 7.884 23.133 1.00 15.69 ? 376 GLY A CA 1 ATOM 2905 C C . GLY A 1 376 ? 58.818 7.174 24.159 1.00 15.86 ? 376 GLY A C 1 ATOM 2906 O O . GLY A 1 376 ? 57.602 7.433 24.301 1.00 14.95 ? 376 GLY A O 1 ATOM 2907 N N . LEU A 1 377 ? 59.472 6.278 24.882 1.00 15.66 ? 377 LEU A N 1 ATOM 2908 C CA . LEU A 1 377 ? 58.840 5.522 25.950 1.00 16.01 ? 377 LEU A CA 1 ATOM 2909 C C . LEU A 1 377 ? 58.830 6.316 27.245 1.00 16.23 ? 377 LEU A C 1 ATOM 2910 O O . LEU A 1 377 ? 59.798 6.996 27.575 1.00 16.25 ? 377 LEU A O 1 ATOM 2911 C CB . LEU A 1 377 ? 59.581 4.195 26.171 1.00 15.92 ? 377 LEU A CB 1 ATOM 2912 C CG . LEU A 1 377 ? 59.718 3.258 24.964 1.00 16.81 ? 377 LEU A CG 1 ATOM 2913 C CD1 . LEU A 1 377 ? 60.457 1.966 25.375 1.00 14.61 ? 377 LEU A CD1 1 ATOM 2914 C CD2 . LEU A 1 377 ? 58.359 2.946 24.384 1.00 15.63 ? 377 LEU A CD2 1 ATOM 2915 N N . ALA A 1 378 ? 57.743 6.200 27.997 1.00 16.67 ? 378 ALA A N 1 ATOM 2916 C CA . ALA A 1 378 ? 57.707 6.749 29.342 1.00 17.08 ? 378 ALA A CA 1 ATOM 2917 C C . ALA A 1 378 ? 58.744 5.983 30.156 1.00 17.96 ? 378 ALA A C 1 ATOM 2918 O O . ALA A 1 378 ? 58.953 4.801 29.918 1.00 18.38 ? 378 ALA A O 1 ATOM 2919 C CB . ALA A 1 378 ? 56.355 6.574 29.936 1.00 17.02 ? 378 ALA A CB 1 ATOM 2920 N N . PRO A 1 379 ? 59.449 6.674 31.060 1.00 18.49 ? 379 PRO A N 1 ATOM 2921 C CA . PRO A 1 379 ? 60.348 5.983 31.986 1.00 19.29 ? 379 PRO A CA 1 ATOM 2922 C C . PRO A 1 379 ? 59.574 5.003 32.850 1.00 20.11 ? 379 PRO A C 1 ATOM 2923 O O . PRO A 1 379 ? 58.473 5.308 33.308 1.00 20.76 ? 379 PRO A O 1 ATOM 2924 C CB . PRO A 1 379 ? 60.904 7.119 32.839 1.00 19.16 ? 379 PRO A CB 1 ATOM 2925 C CG . PRO A 1 379 ? 60.839 8.319 31.925 1.00 18.97 ? 379 PRO A CG 1 ATOM 2926 C CD . PRO A 1 379 ? 59.516 8.136 31.220 1.00 18.15 ? 379 PRO A CD 1 ATOM 2927 N N . GLY A 1 380 ? 60.128 3.823 33.055 1.00 20.85 ? 380 GLY A N 1 ATOM 2928 C CA . GLY A 1 380 ? 59.486 2.858 33.936 1.00 21.28 ? 380 GLY A CA 1 ATOM 2929 C C . GLY A 1 380 ? 58.452 1.983 33.256 1.00 21.60 ? 380 GLY A C 1 ATOM 2930 O O . GLY A 1 380 ? 57.721 2.415 32.342 1.00 22.76 ? 380 GLY A O 1 ATOM 2931 N N . LYS A 1 381 ? 58.368 0.746 33.716 1.00 21.20 ? 381 LYS A N 1 ATOM 2932 C CA . LYS A 1 381 ? 57.430 -0.201 33.148 1.00 20.54 ? 381 LYS A CA 1 ATOM 2933 C C . LYS A 1 381 ? 56.030 0.034 33.685 1.00 19.52 ? 381 LYS A C 1 ATOM 2934 O O . LYS A 1 381 ? 55.853 0.581 34.780 1.00 19.61 ? 381 LYS A O 1 ATOM 2935 C CB . LYS A 1 381 ? 57.880 -1.634 33.441 1.00 21.06 ? 381 LYS A CB 1 ATOM 2936 C CG . LYS A 1 381 ? 59.248 -1.991 32.855 1.00 23.89 ? 381 LYS A CG 1 ATOM 2937 C CD . LYS A 1 381 ? 59.317 -1.843 31.335 1.00 28.14 ? 381 LYS A CD 1 ATOM 2938 C CE . LYS A 1 381 ? 60.631 -2.415 30.803 1.00 31.72 ? 381 LYS A CE 1 ATOM 2939 N NZ . LYS A 1 381 ? 61.083 -1.713 29.574 1.00 32.77 ? 381 LYS A NZ 1 ATOM 2940 N N . ALA A 1 382 ? 55.040 -0.378 32.901 1.00 18.58 ? 382 ALA A N 1 ATOM 2941 C CA . ALA A 1 382 ? 53.653 -0.401 33.344 1.00 18.01 ? 382 ALA A CA 1 ATOM 2942 C C . ALA A 1 382 ? 53.404 -1.584 34.284 1.00 18.12 ? 382 ALA A C 1 ATOM 2943 O O . ALA A 1 382 ? 54.292 -2.413 34.517 1.00 17.39 ? 382 ALA A O 1 ATOM 2944 C CB . ALA A 1 382 ? 52.722 -0.466 32.150 1.00 17.66 ? 382 ALA A CB 1 ATOM 2945 N N . ARG A 1 383 ? 52.196 -1.660 34.830 1.00 18.51 ? 383 ARG A N 1 ATOM 2946 C CA . ARG A 1 383 ? 51.878 -2.703 35.785 1.00 19.31 ? 383 ARG A CA 1 ATOM 2947 C C . ARG A 1 383 ? 51.921 -4.100 35.166 1.00 19.71 ? 383 ARG A C 1 ATOM 2948 O O . ARG A 1 383 ? 52.038 -5.075 35.882 1.00 20.36 ? 383 ARG A O 1 ATOM 2949 C CB . ARG A 1 383 ? 50.525 -2.441 36.432 1.00 19.35 ? 383 ARG A CB 1 ATOM 2950 C CG . ARG A 1 383 ? 50.342 -3.096 37.767 1.00 21.63 ? 383 ARG A CG 1 ATOM 2951 C CD . ARG A 1 383 ? 51.314 -2.551 38.832 1.00 25.82 ? 383 ARG A CD 1 ATOM 2952 N NE . ARG A 1 383 ? 50.831 -2.897 40.165 1.00 27.22 ? 383 ARG A NE 1 ATOM 2953 C CZ . ARG A 1 383 ? 51.074 -4.049 40.787 1.00 28.27 ? 383 ARG A CZ 1 ATOM 2954 N NH1 . ARG A 1 383 ? 50.567 -4.265 41.991 1.00 27.55 ? 383 ARG A NH1 1 ATOM 2955 N NH2 . ARG A 1 383 ? 51.826 -4.982 40.217 1.00 30.06 ? 383 ARG A NH2 1 ATOM 2956 N N . ASP A 1 384 ? 51.821 -4.196 33.840 1.00 20.02 ? 384 ASP A N 1 ATOM 2957 C CA . ASP A 1 384 ? 51.913 -5.488 33.155 1.00 20.25 ? 384 ASP A CA 1 ATOM 2958 C C . ASP A 1 384 ? 53.351 -5.798 32.744 1.00 20.85 ? 384 ASP A C 1 ATOM 2959 O O . ASP A 1 384 ? 53.599 -6.689 31.917 1.00 21.38 ? 384 ASP A O 1 ATOM 2960 C CB . ASP A 1 384 ? 50.987 -5.511 31.940 1.00 20.36 ? 384 ASP A CB 1 ATOM 2961 C CG . ASP A 1 384 ? 51.263 -4.365 30.958 1.00 19.06 ? 384 ASP A CG 1 ATOM 2962 O OD1 . ASP A 1 384 ? 52.298 -3.670 31.066 1.00 19.16 ? 384 ASP A OD1 1 ATOM 2963 O OD2 . ASP A 1 384 ? 50.429 -4.167 30.060 1.00 18.65 ? 384 ASP A OD2 1 ATOM 2964 N N . ARG A 1 385 ? 54.278 -5.029 33.316 1.00 21.07 ? 385 ARG A N 1 ATOM 2965 C CA . ARG A 1 385 ? 55.722 -5.220 33.176 1.00 21.93 ? 385 ARG A CA 1 ATOM 2966 C C . ARG A 1 385 ? 56.259 -4.869 31.797 1.00 21.46 ? 385 ARG A C 1 ATOM 2967 O O . ARG A 1 385 ? 57.409 -5.156 31.484 1.00 21.80 ? 385 ARG A O 1 ATOM 2968 C CB . ARG A 1 385 ? 56.153 -6.641 33.589 1.00 22.79 ? 385 ARG A CB 1 ATOM 2969 C CG . ARG A 1 385 ? 55.825 -7.015 35.039 1.00 25.74 ? 385 ARG A CG 1 ATOM 2970 C CD . ARG A 1 385 ? 56.155 -5.870 36.007 1.00 33.38 ? 385 ARG A CD 1 ATOM 2971 N NE . ARG A 1 385 ? 57.544 -5.389 35.912 1.00 37.74 ? 385 ARG A NE 1 ATOM 2972 C CZ . ARG A 1 385 ? 57.944 -4.175 36.291 1.00 41.42 ? 385 ARG A CZ 1 ATOM 2973 N NH1 . ARG A 1 385 ? 59.224 -3.824 36.165 1.00 42.33 ? 385 ARG A NH1 1 ATOM 2974 N NH2 . ARG A 1 385 ? 57.061 -3.300 36.782 1.00 43.94 ? 385 ARG A NH2 1 ATOM 2975 N N . LYS A 1 386 ? 55.441 -4.216 30.981 1.00 20.53 ? 386 LYS A N 1 ATOM 2976 C CA . LYS A 1 386 ? 55.887 -3.828 29.654 1.00 20.12 ? 386 LYS A CA 1 ATOM 2977 C C . LYS A 1 386 ? 55.978 -2.318 29.550 1.00 18.95 ? 386 LYS A C 1 ATOM 2978 O O . LYS A 1 386 ? 55.361 -1.580 30.340 1.00 18.03 ? 386 LYS A O 1 ATOM 2979 C CB . LYS A 1 386 ? 54.965 -4.404 28.581 1.00 20.53 ? 386 LYS A CB 1 ATOM 2980 C CG . LYS A 1 386 ? 54.927 -5.951 28.639 1.00 23.33 ? 386 LYS A CG 1 ATOM 2981 C CD . LYS A 1 386 ? 54.145 -6.532 27.498 1.00 27.90 ? 386 LYS A CD 1 ATOM 2982 C CE . LYS A 1 386 ? 53.367 -7.749 27.943 1.00 32.34 ? 386 LYS A CE 1 ATOM 2983 N NZ . LYS A 1 386 ? 52.087 -7.335 28.615 1.00 35.12 ? 386 LYS A NZ 1 ATOM 2984 N N . ALA A 1 387 ? 56.763 -1.867 28.584 1.00 17.66 ? 387 ALA A N 1 ATOM 2985 C CA . ALA A 1 387 ? 56.948 -0.446 28.366 1.00 17.46 ? 387 ALA A CA 1 ATOM 2986 C C . ALA A 1 387 ? 55.665 0.209 27.842 1.00 16.87 ? 387 ALA A C 1 ATOM 2987 O O . ALA A 1 387 ? 54.724 -0.469 27.402 1.00 16.73 ? 387 ALA A O 1 ATOM 2988 C CB . ALA A 1 387 ? 58.087 -0.213 27.407 1.00 17.51 ? 387 ALA A CB 1 ATOM 2989 N N . TYR A 1 388 ? 55.626 1.536 27.921 1.00 15.62 ? 388 TYR A N 1 ATOM 2990 C CA . TYR A 1 388 ? 54.559 2.291 27.305 1.00 15.43 ? 388 TYR A CA 1 ATOM 2991 C C . TYR A 1 388 ? 55.099 3.622 26.827 1.00 14.83 ? 388 TYR A C 1 ATOM 2992 O O . TYR A 1 388 ? 56.166 4.030 27.239 1.00 16.00 ? 388 TYR A O 1 ATOM 2993 C CB . TYR A 1 388 ? 53.363 2.468 28.253 1.00 15.22 ? 388 TYR A CB 1 ATOM 2994 C CG . TYR A 1 388 ? 53.619 3.310 29.493 1.00 16.28 ? 388 TYR A CG 1 ATOM 2995 C CD1 . TYR A 1 388 ? 54.348 2.804 30.586 1.00 17.14 ? 388 TYR A CD1 1 ATOM 2996 C CD2 . TYR A 1 388 ? 53.098 4.599 29.593 1.00 16.87 ? 388 TYR A CD2 1 ATOM 2997 C CE1 . TYR A 1 388 ? 54.552 3.575 31.723 1.00 17.39 ? 388 TYR A CE1 1 ATOM 2998 C CE2 . TYR A 1 388 ? 53.294 5.366 30.719 1.00 16.68 ? 388 TYR A CE2 1 ATOM 2999 C CZ . TYR A 1 388 ? 54.023 4.856 31.781 1.00 18.00 ? 388 TYR A CZ 1 ATOM 3000 O OH . TYR A 1 388 ? 54.217 5.658 32.892 1.00 19.81 ? 388 TYR A OH 1 ATOM 3001 N N . THR A 1 389 ? 54.350 4.281 25.952 1.00 14.36 ? 389 THR A N 1 ATOM 3002 C CA . THR A 1 389 ? 54.787 5.521 25.314 1.00 13.67 ? 389 THR A CA 1 ATOM 3003 C C . THR A 1 389 ? 54.282 6.758 26.073 1.00 13.64 ? 389 THR A C 1 ATOM 3004 O O . THR A 1 389 ? 53.260 6.704 26.770 1.00 13.20 ? 389 THR A O 1 ATOM 3005 C CB . THR A 1 389 ? 54.294 5.598 23.856 1.00 13.61 ? 389 THR A CB 1 ATOM 3006 O OG1 . THR A 1 389 ? 52.890 5.314 23.820 1.00 13.25 ? 389 THR A OG1 1 ATOM 3007 C CG2 . THR A 1 389 ? 55.042 4.570 22.972 1.00 12.58 ? 389 THR A CG2 1 ATOM 3008 N N . VAL A 1 390 ? 54.998 7.874 25.936 1.00 13.36 ? 390 VAL A N 1 ATOM 3009 C CA . VAL A 1 390 ? 54.531 9.121 26.550 1.00 13.48 ? 390 VAL A CA 1 ATOM 3010 C C . VAL A 1 390 ? 53.269 9.622 25.833 1.00 13.02 ? 390 VAL A C 1 ATOM 3011 O O . VAL A 1 390 ? 52.409 10.247 26.443 1.00 13.10 ? 390 VAL A O 1 ATOM 3012 C CB . VAL A 1 390 ? 55.639 10.215 26.675 1.00 14.17 ? 390 VAL A CB 1 ATOM 3013 C CG1 . VAL A 1 390 ? 56.864 9.645 27.396 1.00 13.53 ? 390 VAL A CG1 1 ATOM 3014 C CG2 . VAL A 1 390 ? 56.016 10.815 25.347 1.00 16.17 ? 390 VAL A CG2 1 ATOM 3015 N N . LEU A 1 391 ? 53.162 9.314 24.545 1.00 12.47 ? 391 LEU A N 1 ATOM 3016 C CA . LEU A 1 391 ? 51.973 9.685 23.766 1.00 11.82 ? 391 LEU A CA 1 ATOM 3017 C C . LEU A 1 391 ? 51.025 8.506 23.717 1.00 11.96 ? 391 LEU A C 1 ATOM 3018 O O . LEU A 1 391 ? 51.432 7.374 23.425 1.00 11.94 ? 391 LEU A O 1 ATOM 3019 C CB . LEU A 1 391 ? 52.348 10.136 22.355 1.00 11.13 ? 391 LEU A CB 1 ATOM 3020 C CG . LEU A 1 391 ? 53.283 11.335 22.270 1.00 9.58 ? 391 LEU A CG 1 ATOM 3021 C CD1 . LEU A 1 391 ? 53.511 11.713 20.780 1.00 9.85 ? 391 LEU A CD1 1 ATOM 3022 C CD2 . LEU A 1 391 ? 52.718 12.524 23.059 1.00 8.78 ? 391 LEU A CD2 1 ATOM 3023 N N . LEU A 1 392 ? 49.769 8.772 24.063 1.00 11.99 ? 392 LEU A N 1 ATOM 3024 C CA . LEU A 1 392 ? 48.733 7.752 24.063 1.00 11.95 ? 392 LEU A CA 1 ATOM 3025 C C . LEU A 1 392 ? 47.431 8.364 23.584 1.00 11.89 ? 392 LEU A C 1 ATOM 3026 O O . LEU A 1 392 ? 47.295 9.579 23.516 1.00 11.60 ? 392 LEU A O 1 ATOM 3027 C CB . LEU A 1 392 ? 48.561 7.144 25.462 1.00 11.73 ? 392 LEU A CB 1 ATOM 3028 C CG . LEU A 1 392 ? 49.723 6.283 25.969 1.00 11.42 ? 392 LEU A CG 1 ATOM 3029 C CD1 . LEU A 1 392 ? 49.575 6.056 27.472 1.00 11.69 ? 392 LEU A CD1 1 ATOM 3030 C CD2 . LEU A 1 392 ? 49.794 4.944 25.201 1.00 12.04 ? 392 LEU A CD2 1 ATOM 3031 N N . TYR A 1 393 ? 46.483 7.509 23.237 1.00 11.67 ? 393 TYR A N 1 ATOM 3032 C CA . TYR A 1 393 ? 45.161 7.958 22.828 1.00 12.13 ? 393 TYR A CA 1 ATOM 3033 C C . TYR A 1 393 ? 44.141 7.292 23.705 1.00 12.29 ? 393 TYR A C 1 ATOM 3034 O O . TYR A 1 393 ? 44.380 6.199 24.205 1.00 12.16 ? 393 TYR A O 1 ATOM 3035 C CB . TYR A 1 393 ? 44.890 7.592 21.373 1.00 11.48 ? 393 TYR A CB 1 ATOM 3036 C CG . TYR A 1 393 ? 45.694 8.398 20.395 1.00 11.59 ? 393 TYR A CG 1 ATOM 3037 C CD1 . TYR A 1 393 ? 45.227 9.634 19.938 1.00 10.48 ? 393 TYR A CD1 1 ATOM 3038 C CD2 . TYR A 1 393 ? 46.932 7.937 19.924 1.00 10.41 ? 393 TYR A CD2 1 ATOM 3039 C CE1 . TYR A 1 393 ? 45.946 10.374 19.021 1.00 9.65 ? 393 TYR A CE1 1 ATOM 3040 C CE2 . TYR A 1 393 ? 47.674 8.694 19.009 1.00 11.70 ? 393 TYR A CE2 1 ATOM 3041 C CZ . TYR A 1 393 ? 47.165 9.907 18.567 1.00 10.31 ? 393 TYR A CZ 1 ATOM 3042 O OH . TYR A 1 393 ? 47.871 10.662 17.670 1.00 11.12 ? 393 TYR A OH 1 ATOM 3043 N N . GLY A 1 394 ? 43.020 7.957 23.933 1.00 12.40 ? 394 GLY A N 1 ATOM 3044 C CA . GLY A 1 394 ? 41.959 7.339 24.737 1.00 12.92 ? 394 GLY A CA 1 ATOM 3045 C C . GLY A 1 394 ? 41.389 6.140 23.976 1.00 13.13 ? 394 GLY A C 1 ATOM 3046 O O . GLY A 1 394 ? 41.124 5.078 24.545 1.00 13.15 ? 394 GLY A O 1 ATOM 3047 N N . ASN A 1 395 ? 41.210 6.314 22.676 1.00 12.10 ? 395 ASN A N 1 ATOM 3048 C CA . ASN A 1 395 ? 40.647 5.257 21.844 1.00 12.55 ? 395 ASN A CA 1 ATOM 3049 C C . ASN A 1 395 ? 41.331 5.312 20.486 1.00 13.33 ? 395 ASN A C 1 ATOM 3050 O O . ASN A 1 395 ? 42.078 6.252 20.205 1.00 13.11 ? 395 ASN A O 1 ATOM 3051 C CB . ASN A 1 395 ? 39.128 5.443 21.722 1.00 11.75 ? 395 ASN A CB 1 ATOM 3052 C CG . ASN A 1 395 ? 38.757 6.818 21.181 1.00 12.50 ? 395 ASN A CG 1 ATOM 3053 O OD1 . ASN A 1 395 ? 39.278 7.227 20.153 1.00 10.45 ? 395 ASN A OD1 1 ATOM 3054 N ND2 . ASN A 1 395 ? 37.871 7.539 21.884 1.00 12.73 ? 395 ASN A ND2 1 ATOM 3055 N N . GLY A 1 396 ? 41.068 4.324 19.641 1.00 12.98 ? 396 GLY A N 1 ATOM 3056 C CA . GLY A 1 396 ? 41.620 4.342 18.296 1.00 13.51 ? 396 GLY A CA 1 ATOM 3057 C C . GLY A 1 396 ? 42.333 3.058 17.920 1.00 13.50 ? 396 GLY A C 1 ATOM 3058 O O . GLY A 1 396 ? 42.374 2.106 18.706 1.00 13.80 ? 396 GLY A O 1 ATOM 3059 N N . PRO A 1 397 ? 42.900 3.029 16.705 1.00 14.06 ? 397 PRO A N 1 ATOM 3060 C CA . PRO A 1 397 ? 43.399 1.813 16.080 1.00 14.57 ? 397 PRO A CA 1 ATOM 3061 C C . PRO A 1 397 ? 44.779 1.364 16.549 1.00 14.73 ? 397 PRO A C 1 ATOM 3062 O O . PRO A 1 397 ? 45.301 0.394 16.005 1.00 15.92 ? 397 PRO A O 1 ATOM 3063 C CB . PRO A 1 397 ? 43.401 2.170 14.590 1.00 14.24 ? 397 PRO A CB 1 ATOM 3064 C CG . PRO A 1 397 ? 43.617 3.649 14.556 1.00 14.60 ? 397 PRO A CG 1 ATOM 3065 C CD . PRO A 1 397 ? 43.025 4.206 15.820 1.00 13.71 ? 397 PRO A CD 1 ATOM 3066 N N . GLY A 1 398 ? 45.342 2.062 17.540 1.00 15.13 ? 398 GLY A N 1 ATOM 3067 C CA . GLY A 1 398 ? 46.579 1.642 18.216 1.00 15.33 ? 398 GLY A CA 1 ATOM 3068 C C . GLY A 1 398 ? 46.346 0.602 19.298 1.00 16.00 ? 398 GLY A C 1 ATOM 3069 O O . GLY A 1 398 ? 47.302 0.043 19.855 1.00 16.17 ? 398 GLY A O 1 ATOM 3070 N N . TYR A 1 399 ? 45.084 0.318 19.610 1.00 16.35 ? 399 TYR A N 1 ATOM 3071 C CA . TYR A 1 399 ? 44.803 -0.688 20.618 1.00 17.25 ? 399 TYR A CA 1 ATOM 3072 C C . TYR A 1 399 ? 45.184 -2.045 20.047 1.00 18.35 ? 399 TYR A C 1 ATOM 3073 O O . TYR A 1 399 ? 44.754 -2.404 18.943 1.00 17.77 ? 399 TYR A O 1 ATOM 3074 C CB . TYR A 1 399 ? 43.326 -0.679 21.025 1.00 17.27 ? 399 TYR A CB 1 ATOM 3075 C CG . TYR A 1 399 ? 42.971 -1.706 22.085 1.00 16.93 ? 399 TYR A CG 1 ATOM 3076 C CD1 . TYR A 1 399 ? 42.726 -3.037 21.741 1.00 16.65 ? 399 TYR A CD1 1 ATOM 3077 C CD2 . TYR A 1 399 ? 42.860 -1.343 23.429 1.00 16.79 ? 399 TYR A CD2 1 ATOM 3078 C CE1 . TYR A 1 399 ? 42.394 -3.986 22.710 1.00 19.00 ? 399 TYR A CE1 1 ATOM 3079 C CE2 . TYR A 1 399 ? 42.531 -2.283 24.408 1.00 16.14 ? 399 TYR A CE2 1 ATOM 3080 C CZ . TYR A 1 399 ? 42.297 -3.600 24.038 1.00 18.35 ? 399 TYR A CZ 1 ATOM 3081 O OH . TYR A 1 399 ? 41.965 -4.542 24.993 1.00 19.05 ? 399 TYR A OH 1 ATOM 3082 N N . VAL A 1 400 ? 46.013 -2.775 20.777 1.00 19.94 ? 400 VAL A N 1 ATOM 3083 C CA . VAL A 1 400 ? 46.454 -4.089 20.326 1.00 22.80 ? 400 VAL A CA 1 ATOM 3084 C C . VAL A 1 400 ? 46.511 -5.055 21.481 1.00 25.02 ? 400 VAL A C 1 ATOM 3085 O O . VAL A 1 400 ? 46.892 -4.694 22.593 1.00 23.78 ? 400 VAL A O 1 ATOM 3086 C CB . VAL A 1 400 ? 47.866 -4.074 19.648 1.00 23.14 ? 400 VAL A CB 1 ATOM 3087 C CG1 . VAL A 1 400 ? 48.248 -5.490 19.138 1.00 24.14 ? 400 VAL A CG1 1 ATOM 3088 C CG2 . VAL A 1 400 ? 47.903 -3.150 18.502 1.00 23.04 ? 400 VAL A CG2 1 ATOM 3089 N N . LEU A 1 401 ? 46.118 -6.292 21.193 1.00 27.98 ? 401 LEU A N 1 ATOM 3090 C CA . LEU A 1 401 ? 46.481 -7.429 22.017 1.00 31.59 ? 401 LEU A CA 1 ATOM 3091 C C . LEU A 1 401 ? 47.232 -8.434 21.155 1.00 33.80 ? 401 LEU A C 1 ATOM 3092 O O . LEU A 1 401 ? 46.717 -8.886 20.124 1.00 34.92 ? 401 LEU A O 1 ATOM 3093 C CB . LEU A 1 401 ? 45.243 -8.063 22.632 1.00 31.53 ? 401 LEU A CB 1 ATOM 3094 C CG . LEU A 1 401 ? 44.484 -7.112 23.564 1.00 31.89 ? 401 LEU A CG 1 ATOM 3095 C CD1 . LEU A 1 401 ? 43.113 -7.666 23.882 1.00 32.70 ? 401 LEU A CD1 1 ATOM 3096 C CD2 . LEU A 1 401 ? 45.273 -6.861 24.851 1.00 32.79 ? 401 LEU A CD2 1 ATOM 3097 N N . LYS A 1 402 ? 48.469 -8.727 21.555 1.00 35.98 ? 402 LYS A N 1 ATOM 3098 C CA . LYS A 1 402 ? 49.250 -9.811 20.978 1.00 37.85 ? 402 LYS A CA 1 ATOM 3099 C C . LYS A 1 402 ? 49.285 -10.937 22.002 1.00 38.74 ? 402 LYS A C 1 ATOM 3100 O O . LYS A 1 402 ? 49.665 -10.718 23.169 1.00 39.01 ? 402 LYS A O 1 ATOM 3101 C CB . LYS A 1 402 ? 50.681 -9.359 20.662 1.00 38.22 ? 402 LYS A CB 1 ATOM 3102 C CG . LYS A 1 402 ? 50.796 -8.293 19.584 1.00 40.72 ? 402 LYS A CG 1 ATOM 3103 C CD . LYS A 1 402 ? 51.994 -8.580 18.686 1.00 43.87 ? 402 LYS A CD 1 ATOM 3104 C CE . LYS A 1 402 ? 52.536 -7.322 18.051 1.00 45.65 ? 402 LYS A CE 1 ATOM 3105 N NZ . LYS A 1 402 ? 53.458 -6.635 18.999 1.00 48.53 ? 402 LYS A NZ 1 ATOM 3106 N N . ASP A 1 403 ? 48.884 -12.134 21.569 1.00 39.27 ? 403 ASP A N 1 ATOM 3107 C CA . ASP A 1 403 ? 48.771 -13.299 22.456 1.00 39.82 ? 403 ASP A CA 1 ATOM 3108 C C . ASP A 1 403 ? 47.994 -12.974 23.747 1.00 39.17 ? 403 ASP A C 1 ATOM 3109 O O . ASP A 1 403 ? 48.413 -13.333 24.851 1.00 39.66 ? 403 ASP A O 1 ATOM 3110 C CB . ASP A 1 403 ? 50.160 -13.878 22.758 1.00 40.35 ? 403 ASP A CB 1 ATOM 3111 C CG . ASP A 1 403 ? 50.867 -14.369 21.510 1.00 42.24 ? 403 ASP A CG 1 ATOM 3112 O OD1 . ASP A 1 403 ? 52.000 -13.902 21.237 1.00 44.28 ? 403 ASP A OD1 1 ATOM 3113 O OD2 . ASP A 1 403 ? 50.281 -15.215 20.792 1.00 45.11 ? 403 ASP A OD2 1 ATOM 3114 N N . GLY A 1 404 ? 46.868 -12.276 23.590 1.00 38.01 ? 404 GLY A N 1 ATOM 3115 C CA . GLY A 1 404 ? 46.017 -11.886 24.718 1.00 36.24 ? 404 GLY A CA 1 ATOM 3116 C C . GLY A 1 404 ? 46.579 -10.808 25.645 1.00 34.86 ? 404 GLY A C 1 ATOM 3117 O O . GLY A 1 404 ? 45.982 -10.500 26.681 1.00 35.05 ? 404 GLY A O 1 ATOM 3118 N N . ALA A 1 405 ? 47.721 -10.232 25.286 1.00 33.19 ? 405 ALA A N 1 ATOM 3119 C CA . ALA A 1 405 ? 48.396 -9.259 26.159 1.00 31.04 ? 405 ALA A CA 1 ATOM 3120 C C . ALA A 1 405 ? 48.670 -7.938 25.447 1.00 29.11 ? 405 ALA A C 1 ATOM 3121 O O . ALA A 1 405 ? 48.762 -7.913 24.235 1.00 28.98 ? 405 ALA A O 1 ATOM 3122 C CB . ALA A 1 405 ? 49.699 -9.850 26.669 1.00 31.32 ? 405 ALA A CB 1 ATOM 3123 N N . ARG A 1 406 ? 48.821 -6.852 26.206 1.00 26.78 ? 406 ARG A N 1 ATOM 3124 C CA . ARG A 1 406 ? 49.264 -5.574 25.639 1.00 24.45 ? 406 ARG A CA 1 ATOM 3125 C C . ARG A 1 406 ? 50.680 -5.778 25.112 1.00 24.58 ? 406 ARG A C 1 ATOM 3126 O O . ARG A 1 406 ? 51.509 -6.389 25.790 1.00 24.86 ? 406 ARG A O 1 ATOM 3127 C CB . ARG A 1 406 ? 49.240 -4.464 26.698 1.00 23.83 ? 406 ARG A CB 1 ATOM 3128 C CG . ARG A 1 406 ? 49.452 -3.072 26.130 1.00 21.93 ? 406 ARG A CG 1 ATOM 3129 C CD . ARG A 1 406 ? 49.372 -1.991 27.223 1.00 21.59 ? 406 ARG A CD 1 ATOM 3130 N NE . ARG A 1 406 ? 50.483 -2.114 28.167 1.00 17.57 ? 406 ARG A NE 1 ATOM 3131 C CZ . ARG A 1 406 ? 51.676 -1.537 28.009 1.00 16.06 ? 406 ARG A CZ 1 ATOM 3132 N NH1 . ARG A 1 406 ? 51.930 -0.777 26.941 1.00 13.51 ? 406 ARG A NH1 1 ATOM 3133 N NH2 . ARG A 1 406 ? 52.621 -1.727 28.924 1.00 15.57 ? 406 ARG A NH2 1 ATOM 3134 N N . PRO A 1 407 ? 50.960 -5.318 23.883 1.00 24.43 ? 407 PRO A N 1 ATOM 3135 C CA . PRO A 1 407 ? 52.308 -5.554 23.412 1.00 24.21 ? 407 PRO A CA 1 ATOM 3136 C C . PRO A 1 407 ? 53.293 -4.620 24.096 1.00 24.15 ? 407 PRO A C 1 ATOM 3137 O O . PRO A 1 407 ? 52.940 -3.500 24.501 1.00 23.84 ? 407 PRO A O 1 ATOM 3138 C CB . PRO A 1 407 ? 52.239 -5.232 21.914 1.00 24.83 ? 407 PRO A CB 1 ATOM 3139 C CG . PRO A 1 407 ? 50.837 -4.876 21.627 1.00 25.14 ? 407 PRO A CG 1 ATOM 3140 C CD . PRO A 1 407 ? 50.140 -4.596 22.900 1.00 23.98 ? 407 PRO A CD 1 ATOM 3141 N N . ASP A 1 408 ? 54.518 -5.104 24.243 1.00 23.42 ? 408 ASP A N 1 ATOM 3142 C CA . ASP A 1 408 ? 55.602 -4.283 24.687 1.00 23.73 ? 408 ASP A CA 1 ATOM 3143 C C . ASP A 1 408 ? 55.895 -3.339 23.531 1.00 23.50 ? 408 ASP A C 1 ATOM 3144 O O . ASP A 1 408 ? 55.406 -3.535 22.412 1.00 24.02 ? 408 ASP A O 1 ATOM 3145 C CB . ASP A 1 408 ? 56.800 -5.158 24.986 1.00 23.94 ? 408 ASP A CB 1 ATOM 3146 C CG . ASP A 1 408 ? 57.666 -4.598 26.084 1.00 25.60 ? 408 ASP A CG 1 ATOM 3147 O OD1 . ASP A 1 408 ? 57.678 -3.371 26.294 1.00 25.30 ? 408 ASP A OD1 1 ATOM 3148 O OD2 . ASP A 1 408 ? 58.333 -5.400 26.761 1.00 29.38 ? 408 ASP A OD2 1 ATOM 3149 N N . VAL A 1 409 ? 56.664 -2.303 23.785 1.00 22.57 ? 409 VAL A N 1 ATOM 3150 C CA . VAL A 1 409 ? 57.013 -1.383 22.716 1.00 22.27 ? 409 VAL A CA 1 ATOM 3151 C C . VAL A 1 409 ? 58.449 -0.966 22.950 1.00 22.29 ? 409 VAL A C 1 ATOM 3152 O O . VAL A 1 409 ? 58.878 -0.818 24.095 1.00 21.88 ? 409 VAL A O 1 ATOM 3153 C CB . VAL A 1 409 ? 56.000 -0.172 22.614 1.00 22.40 ? 409 VAL A CB 1 ATOM 3154 C CG1 . VAL A 1 409 ? 55.758 0.477 23.957 1.00 23.68 ? 409 VAL A CG1 1 ATOM 3155 C CG2 . VAL A 1 409 ? 56.449 0.856 21.588 1.00 21.33 ? 409 VAL A CG2 1 ATOM 3156 N N . THR A 1 410 ? 59.195 -0.812 21.866 1.00 22.31 ? 410 THR A N 1 ATOM 3157 C CA . THR A 1 410 ? 60.570 -0.349 21.943 1.00 22.43 ? 410 THR A CA 1 ATOM 3158 C C . THR A 1 410 ? 60.636 1.081 21.434 1.00 22.66 ? 410 THR A C 1 ATOM 3159 O O . THR A 1 410 ? 59.733 1.528 20.720 1.00 21.88 ? 410 THR A O 1 ATOM 3160 C CB . THR A 1 410 ? 61.488 -1.230 21.080 1.00 23.07 ? 410 THR A CB 1 ATOM 3161 O OG1 . THR A 1 410 ? 61.142 -1.057 19.697 1.00 23.06 ? 410 THR A OG1 1 ATOM 3162 C CG2 . THR A 1 410 ? 61.337 -2.713 21.475 1.00 23.31 ? 410 THR A CG2 1 ATOM 3163 N N . GLU A 1 411 ? 61.711 1.788 21.787 1.00 23.04 ? 411 GLU A N 1 ATOM 3164 C CA . GLU A 1 411 ? 61.956 3.138 21.277 1.00 23.69 ? 411 GLU A CA 1 ATOM 3165 C C . GLU A 1 411 ? 62.014 3.164 19.756 1.00 23.56 ? 411 GLU A C 1 ATOM 3166 O O . GLU A 1 411 ? 61.522 4.098 19.127 1.00 23.45 ? 411 GLU A O 1 ATOM 3167 C CB . GLU A 1 411 ? 63.246 3.729 21.858 1.00 23.60 ? 411 GLU A CB 1 ATOM 3168 C CG . GLU A 1 411 ? 63.108 4.205 23.296 1.00 24.75 ? 411 GLU A CG 1 ATOM 3169 C CD . GLU A 1 411 ? 62.573 5.638 23.450 1.00 24.66 ? 411 GLU A CD 1 ATOM 3170 O OE1 . GLU A 1 411 ? 62.227 6.005 24.593 1.00 23.65 ? 411 GLU A OE1 1 ATOM 3171 O OE2 . GLU A 1 411 ? 62.525 6.417 22.466 1.00 26.90 ? 411 GLU A OE2 1 ATOM 3172 N N . SER A 1 412 ? 62.614 2.130 19.167 1.00 23.59 ? 412 SER A N 1 ATOM 3173 C CA . SER A 1 412 ? 62.685 2.034 17.720 1.00 23.80 ? 412 SER A CA 1 ATOM 3174 C C . SER A 1 412 ? 61.288 1.959 17.094 1.00 22.93 ? 412 SER A C 1 ATOM 3175 O O . SER A 1 412 ? 60.998 2.665 16.117 1.00 22.83 ? 412 SER A O 1 ATOM 3176 C CB . SER A 1 412 ? 63.537 0.836 17.291 1.00 24.02 ? 412 SER A CB 1 ATOM 3177 O OG . SER A 1 412 ? 63.532 0.754 15.887 1.00 28.48 ? 412 SER A OG 1 ATOM 3178 N N . GLU A 1 413 ? 60.433 1.113 17.661 1.00 21.50 ? 413 GLU A N 1 ATOM 3179 C CA . GLU A 1 413 ? 59.046 0.991 17.206 1.00 21.81 ? 413 GLU A CA 1 ATOM 3180 C C . GLU A 1 413 ? 58.281 2.288 17.396 1.00 20.19 ? 413 GLU A C 1 ATOM 3181 O O . GLU A 1 413 ? 57.619 2.769 16.478 1.00 19.26 ? 413 GLU A O 1 ATOM 3182 C CB . GLU A 1 413 ? 58.302 -0.082 17.996 1.00 22.07 ? 413 GLU A CB 1 ATOM 3183 C CG . GLU A 1 413 ? 58.805 -1.469 17.767 1.00 27.49 ? 413 GLU A CG 1 ATOM 3184 C CD . GLU A 1 413 ? 58.408 -2.422 18.880 1.00 33.01 ? 413 GLU A CD 1 ATOM 3185 O OE1 . GLU A 1 413 ? 57.449 -2.128 19.627 1.00 35.29 ? 413 GLU A OE1 1 ATOM 3186 O OE2 . GLU A 1 413 ? 59.051 -3.479 18.989 1.00 37.62 ? 413 GLU A OE2 1 ATOM 3187 N N . SER A 1 414 ? 58.362 2.830 18.605 1.00 19.17 ? 414 SER A N 1 ATOM 3188 C CA . SER A 1 414 ? 57.558 3.992 18.994 1.00 18.90 ? 414 SER A CA 1 ATOM 3189 C C . SER A 1 414 ? 57.886 5.268 18.202 1.00 18.82 ? 414 SER A C 1 ATOM 3190 O O . SER A 1 414 ? 57.039 6.161 18.069 1.00 18.20 ? 414 SER A O 1 ATOM 3191 C CB . SER A 1 414 ? 57.635 4.230 20.513 1.00 18.27 ? 414 SER A CB 1 ATOM 3192 O OG . SER A 1 414 ? 58.892 4.734 20.904 1.00 19.08 ? 414 SER A OG 1 ATOM 3193 N N . GLY A 1 415 ? 59.100 5.321 17.659 1.00 19.13 ? 415 GLY A N 1 ATOM 3194 C CA . GLY A 1 415 ? 59.592 6.486 16.925 1.00 19.55 ? 415 GLY A CA 1 ATOM 3195 C C . GLY A 1 415 ? 59.311 6.441 15.436 1.00 20.28 ? 415 GLY A C 1 ATOM 3196 O O . GLY A 1 415 ? 59.593 7.401 14.724 1.00 19.70 ? 415 GLY A O 1 ATOM 3197 N N . SER A 1 416 ? 58.733 5.336 14.965 1.00 20.67 ? 416 SER A N 1 ATOM 3198 C CA . SER A 1 416 ? 58.471 5.150 13.535 1.00 21.31 ? 416 SER A CA 1 ATOM 3199 C C . SER A 1 416 ? 57.317 6.035 13.042 1.00 21.55 ? 416 SER A C 1 ATOM 3200 O O . SER A 1 416 ? 56.329 6.199 13.755 1.00 21.72 ? 416 SER A O 1 ATOM 3201 C CB . SER A 1 416 ? 58.146 3.687 13.246 1.00 21.55 ? 416 SER A CB 1 ATOM 3202 O OG . SER A 1 416 ? 57.477 3.586 11.998 1.00 22.76 ? 416 SER A OG 1 ATOM 3203 N N . PRO A 1 417 ? 57.434 6.607 11.818 1.00 21.52 ? 417 PRO A N 1 ATOM 3204 C CA . PRO A 1 417 ? 56.345 7.420 11.270 1.00 21.37 ? 417 PRO A CA 1 ATOM 3205 C C . PRO A 1 417 ? 55.035 6.644 11.097 1.00 20.93 ? 417 PRO A C 1 ATOM 3206 O O . PRO A 1 417 ? 53.983 7.257 10.983 1.00 21.10 ? 417 PRO A O 1 ATOM 3207 C CB . PRO A 1 417 ? 56.890 7.880 9.901 1.00 21.58 ? 417 PRO A CB 1 ATOM 3208 C CG . PRO A 1 417 ? 58.382 7.730 10.021 1.00 22.25 ? 417 PRO A CG 1 ATOM 3209 C CD . PRO A 1 417 ? 58.580 6.535 10.890 1.00 22.48 ? 417 PRO A CD 1 ATOM 3210 N N . GLU A 1 418 ? 55.105 5.312 11.083 1.00 20.33 ? 418 GLU A N 1 ATOM 3211 C CA . GLU A 1 418 ? 53.922 4.479 10.956 1.00 20.33 ? 418 GLU A CA 1 ATOM 3212 C C . GLU A 1 418 ? 53.377 3.993 12.287 1.00 19.41 ? 418 GLU A C 1 ATOM 3213 O O . GLU A 1 418 ? 52.315 3.359 12.320 1.00 19.07 ? 418 GLU A O 1 ATOM 3214 C CB . GLU A 1 418 ? 54.210 3.251 10.074 1.00 20.97 ? 418 GLU A CB 1 ATOM 3215 C CG . GLU A 1 418 ? 54.191 3.577 8.600 1.00 25.44 ? 418 GLU A CG 1 ATOM 3216 C CD . GLU A 1 418 ? 55.270 4.556 8.240 1.00 29.58 ? 418 GLU A CD 1 ATOM 3217 O OE1 . GLU A 1 418 ? 56.458 4.183 8.330 1.00 32.01 ? 418 GLU A OE1 1 ATOM 3218 O OE2 . GLU A 1 418 ? 54.923 5.707 7.891 1.00 33.38 ? 418 GLU A OE2 1 ATOM 3219 N N . TYR A 1 419 ? 54.103 4.257 13.379 1.00 17.94 ? 419 TYR A N 1 ATOM 3220 C CA . TYR A 1 419 ? 53.691 3.739 14.673 1.00 16.81 ? 419 TYR A CA 1 ATOM 3221 C C . TYR A 1 419 ? 52.335 4.278 15.128 1.00 16.36 ? 419 TYR A C 1 ATOM 3222 O O . TYR A 1 419 ? 52.088 5.479 15.082 1.00 16.16 ? 419 TYR A O 1 ATOM 3223 C CB . TYR A 1 419 ? 54.751 3.993 15.752 1.00 16.33 ? 419 TYR A CB 1 ATOM 3224 C CG . TYR A 1 419 ? 54.347 3.397 17.081 1.00 15.86 ? 419 TYR A CG 1 ATOM 3225 C CD1 . TYR A 1 419 ? 54.282 2.004 17.244 1.00 14.85 ? 419 TYR A CD1 1 ATOM 3226 C CD2 . TYR A 1 419 ? 54.010 4.207 18.166 1.00 15.06 ? 419 TYR A CD2 1 ATOM 3227 C CE1 . TYR A 1 419 ? 53.914 1.431 18.463 1.00 15.53 ? 419 TYR A CE1 1 ATOM 3228 C CE2 . TYR A 1 419 ? 53.636 3.641 19.398 1.00 14.26 ? 419 TYR A CE2 1 ATOM 3229 C CZ . TYR A 1 419 ? 53.582 2.254 19.527 1.00 14.76 ? 419 TYR A CZ 1 ATOM 3230 O OH . TYR A 1 419 ? 53.213 1.678 20.713 1.00 15.07 ? 419 TYR A OH 1 ATOM 3231 N N . ARG A 1 420 ? 51.470 3.380 15.583 1.00 15.31 ? 420 ARG A N 1 ATOM 3232 C CA . ARG A 1 420 ? 50.214 3.787 16.178 1.00 14.31 ? 420 ARG A CA 1 ATOM 3233 C C . ARG A 1 420 ? 50.330 3.705 17.687 1.00 13.91 ? 420 ARG A C 1 ATOM 3234 O O . ARG A 1 420 ? 50.533 2.624 18.249 1.00 13.55 ? 420 ARG A O 1 ATOM 3235 C CB . ARG A 1 420 ? 49.060 2.903 15.711 1.00 14.38 ? 420 ARG A CB 1 ATOM 3236 C CG . ARG A 1 420 ? 48.798 2.900 14.205 1.00 14.02 ? 420 ARG A CG 1 ATOM 3237 C CD . ARG A 1 420 ? 47.535 2.079 13.960 1.00 15.05 ? 420 ARG A CD 1 ATOM 3238 N NE . ARG A 1 420 ? 47.313 1.664 12.580 1.00 15.85 ? 420 ARG A NE 1 ATOM 3239 C CZ . ARG A 1 420 ? 46.564 2.324 11.694 1.00 18.72 ? 420 ARG A CZ 1 ATOM 3240 N NH1 . ARG A 1 420 ? 45.987 3.484 12.002 1.00 17.36 ? 420 ARG A NH1 1 ATOM 3241 N NH2 . ARG A 1 420 ? 46.393 1.816 10.480 1.00 19.86 ? 420 ARG A NH2 1 ATOM 3242 N N . GLN A 1 421 ? 50.212 4.846 18.358 1.00 13.27 ? 421 GLN A N 1 ATOM 3243 C CA . GLN A 1 421 ? 50.193 4.831 19.822 1.00 12.54 ? 421 GLN A CA 1 ATOM 3244 C C . GLN A 1 421 ? 48.991 4.034 20.335 1.00 12.74 ? 421 GLN A C 1 ATOM 3245 O O . GLN A 1 421 ? 47.903 4.037 19.742 1.00 13.09 ? 421 GLN A O 1 ATOM 3246 C CB . GLN A 1 421 ? 50.213 6.249 20.400 1.00 11.16 ? 421 GLN A CB 1 ATOM 3247 C CG . GLN A 1 421 ? 51.593 6.931 20.233 1.00 11.20 ? 421 GLN A CG 1 ATOM 3248 C CD . GLN A 1 421 ? 51.788 7.523 18.858 1.00 10.56 ? 421 GLN A CD 1 ATOM 3249 O OE1 . GLN A 1 421 ? 50.827 7.748 18.118 1.00 11.52 ? 421 GLN A OE1 1 ATOM 3250 N NE2 . GLN A 1 421 ? 53.032 7.795 18.507 1.00 12.18 ? 421 GLN A NE2 1 ATOM 3251 N N . GLN A 1 422 ? 49.215 3.323 21.425 1.00 12.59 ? 422 GLN A N 1 ATOM 3252 C CA . GLN A 1 422 ? 48.172 2.523 22.042 1.00 13.27 ? 422 GLN A CA 1 ATOM 3253 C C . GLN A 1 422 ? 47.021 3.377 22.587 1.00 13.21 ? 422 GLN A C 1 ATOM 3254 O O . GLN A 1 422 ? 47.172 4.575 22.853 1.00 13.04 ? 422 GLN A O 1 ATOM 3255 C CB . GLN A 1 422 ? 48.771 1.641 23.134 1.00 12.22 ? 422 GLN A CB 1 ATOM 3256 C CG . GLN A 1 422 ? 49.726 0.569 22.586 1.00 12.38 ? 422 GLN A CG 1 ATOM 3257 C CD . GLN A 1 422 ? 50.420 -0.224 23.676 1.00 14.10 ? 422 GLN A CD 1 ATOM 3258 O OE1 . GLN A 1 422 ? 50.179 -0.009 24.867 1.00 15.12 ? 422 GLN A OE1 1 ATOM 3259 N NE2 . GLN A 1 422 ? 51.283 -1.167 23.272 1.00 17.08 ? 422 GLN A NE2 1 ATOM 3260 N N . SER A 1 423 ? 45.867 2.740 22.740 1.00 13.71 ? 423 SER A N 1 ATOM 3261 C CA . SER A 1 423 ? 44.699 3.408 23.261 1.00 13.41 ? 423 SER A CA 1 ATOM 3262 C C . SER A 1 423 ? 44.024 2.450 24.229 1.00 13.74 ? 423 SER A C 1 ATOM 3263 O O . SER A 1 423 ? 44.404 1.267 24.305 1.00 13.90 ? 423 SER A O 1 ATOM 3264 C CB . SER A 1 423 ? 43.744 3.728 22.122 1.00 13.82 ? 423 SER A CB 1 ATOM 3265 O OG . SER A 1 423 ? 43.195 2.527 21.592 1.00 13.41 ? 423 SER A OG 1 ATOM 3266 N N . ALA A 1 424 ? 43.021 2.959 24.942 1.00 13.12 ? 424 ALA A N 1 ATOM 3267 C CA . ALA A 1 424 ? 42.220 2.158 25.873 1.00 13.53 ? 424 ALA A CA 1 ATOM 3268 C C . ALA A 1 424 ? 41.197 1.285 25.162 1.00 13.75 ? 424 ALA A C 1 ATOM 3269 O O . ALA A 1 424 ? 40.758 0.263 25.712 1.00 13.84 ? 424 ALA A O 1 ATOM 3270 C CB . ALA A 1 424 ? 41.491 3.080 26.850 1.00 12.48 ? 424 ALA A CB 1 ATOM 3271 N N . VAL A 1 425 ? 40.779 1.719 23.971 1.00 13.96 ? 425 VAL A N 1 ATOM 3272 C CA . VAL A 1 425 ? 39.591 1.168 23.293 1.00 14.31 ? 425 VAL A CA 1 ATOM 3273 C C . VAL A 1 425 ? 39.853 1.080 21.782 1.00 14.37 ? 425 VAL A C 1 ATOM 3274 O O . VAL A 1 425 ? 40.146 2.101 21.151 1.00 14.31 ? 425 VAL A O 1 ATOM 3275 C CB . VAL A 1 425 ? 38.361 2.090 23.531 1.00 14.47 ? 425 VAL A CB 1 ATOM 3276 C CG1 . VAL A 1 425 ? 37.129 1.560 22.808 1.00 13.92 ? 425 VAL A CG1 1 ATOM 3277 C CG2 . VAL A 1 425 ? 38.091 2.255 25.036 1.00 13.40 ? 425 VAL A CG2 1 ATOM 3278 N N . PRO A 1 426 ? 39.740 -0.135 21.196 1.00 14.69 ? 426 PRO A N 1 ATOM 3279 C CA . PRO A 1 426 ? 40.007 -0.264 19.761 1.00 14.89 ? 426 PRO A CA 1 ATOM 3280 C C . PRO A 1 426 ? 38.884 0.359 18.938 1.00 14.18 ? 426 PRO A C 1 ATOM 3281 O O . PRO A 1 426 ? 37.717 0.027 19.130 1.00 15.38 ? 426 PRO A O 1 ATOM 3282 C CB . PRO A 1 426 ? 40.065 -1.794 19.536 1.00 14.70 ? 426 PRO A CB 1 ATOM 3283 C CG . PRO A 1 426 ? 39.224 -2.374 20.653 1.00 14.41 ? 426 PRO A CG 1 ATOM 3284 C CD . PRO A 1 426 ? 39.351 -1.426 21.816 1.00 14.17 ? 426 PRO A CD 1 ATOM 3285 N N . LEU A 1 427 ? 39.245 1.277 18.054 1.00 13.89 ? 427 LEU A N 1 ATOM 3286 C CA . LEU A 1 427 ? 38.312 1.814 17.066 1.00 13.96 ? 427 LEU A CA 1 ATOM 3287 C C . LEU A 1 427 ? 39.085 1.928 15.791 1.00 15.12 ? 427 LEU A C 1 ATOM 3288 O O . LEU A 1 427 ? 40.288 2.177 15.827 1.00 15.46 ? 427 LEU A O 1 ATOM 3289 C CB . LEU A 1 427 ? 37.820 3.209 17.473 1.00 13.89 ? 427 LEU A CB 1 ATOM 3290 C CG . LEU A 1 427 ? 36.949 3.392 18.727 1.00 13.65 ? 427 LEU A CG 1 ATOM 3291 C CD1 . LEU A 1 427 ? 36.731 4.869 19.012 1.00 12.77 ? 427 LEU A CD1 1 ATOM 3292 C CD2 . LEU A 1 427 ? 35.603 2.670 18.628 1.00 15.19 ? 427 LEU A CD2 1 ATOM 3293 N N . ASP A 1 428 ? 38.415 1.758 14.658 1.00 15.81 ? 428 ASP A N 1 ATOM 3294 C CA . ASP A 1 428 ? 39.061 1.969 13.371 1.00 16.75 ? 428 ASP A CA 1 ATOM 3295 C C . ASP A 1 428 ? 39.698 3.339 13.261 1.00 16.53 ? 428 ASP A C 1 ATOM 3296 O O . ASP A 1 428 ? 40.770 3.474 12.690 1.00 16.17 ? 428 ASP A O 1 ATOM 3297 C CB . ASP A 1 428 ? 38.052 1.805 12.245 1.00 17.84 ? 428 ASP A CB 1 ATOM 3298 C CG . ASP A 1 428 ? 37.751 0.364 11.955 1.00 19.86 ? 428 ASP A CG 1 ATOM 3299 O OD1 . ASP A 1 428 ? 36.764 0.137 11.253 1.00 23.52 ? 428 ASP A OD1 1 ATOM 3300 O OD2 . ASP A 1 428 ? 38.493 -0.536 12.416 1.00 24.27 ? 428 ASP A OD2 1 ATOM 3301 N N . GLU A 1 429 ? 39.012 4.347 13.797 1.00 15.79 ? 429 GLU A N 1 ATOM 3302 C CA . GLU A 1 429 ? 39.551 5.695 13.861 1.00 16.11 ? 429 GLU A CA 1 ATOM 3303 C C . GLU A 1 429 ? 39.425 6.212 15.264 1.00 14.83 ? 429 GLU A C 1 ATOM 3304 O O . GLU A 1 429 ? 38.380 6.068 15.910 1.00 14.84 ? 429 GLU A O 1 ATOM 3305 C CB . GLU A 1 429 ? 38.829 6.658 12.915 1.00 17.01 ? 429 GLU A CB 1 ATOM 3306 C CG . GLU A 1 429 ? 38.995 6.320 11.460 1.00 22.07 ? 429 GLU A CG 1 ATOM 3307 C CD . GLU A 1 429 ? 39.018 7.555 10.581 1.00 28.07 ? 429 GLU A CD 1 ATOM 3308 O OE1 . GLU A 1 429 ? 38.283 8.523 10.855 1.00 32.18 ? 429 GLU A OE1 1 ATOM 3309 O OE2 . GLU A 1 429 ? 39.787 7.559 9.606 1.00 33.44 ? 429 GLU A OE2 1 ATOM 3310 N N . GLU A 1 430 ? 40.499 6.829 15.727 1.00 13.39 ? 430 GLU A N 1 ATOM 3311 C CA . GLU A 1 430 ? 40.482 7.526 16.999 1.00 12.66 ? 430 GLU A CA 1 ATOM 3312 C C . GLU A 1 430 ? 39.452 8.659 16.894 1.00 12.44 ? 430 GLU A C 1 ATOM 3313 O O . GLU A 1 430 ? 39.176 9.152 15.791 1.00 12.85 ? 430 GLU A O 1 ATOM 3314 C CB . GLU A 1 430 ? 41.900 8.029 17.301 1.00 11.83 ? 430 GLU A CB 1 ATOM 3315 C CG . GLU A 1 430 ? 42.056 8.850 18.583 1.00 11.27 ? 430 GLU A CG 1 ATOM 3316 C CD . GLU A 1 430 ? 42.036 10.345 18.325 1.00 11.53 ? 430 GLU A CD 1 ATOM 3317 O OE1 . GLU A 1 430 ? 41.615 10.767 17.217 1.00 12.39 ? 430 GLU A OE1 1 ATOM 3318 O OE2 . GLU A 1 430 ? 42.436 11.104 19.231 1.00 12.05 ? 430 GLU A OE2 1 ATOM 3319 N N . THR A 1 431 ? 38.884 9.068 18.021 1.00 12.11 ? 431 THR A N 1 ATOM 3320 C CA . THR A 1 431 ? 37.828 10.078 17.986 1.00 11.89 ? 431 THR A CA 1 ATOM 3321 C C . THR A 1 431 ? 38.346 11.476 18.275 1.00 11.99 ? 431 THR A C 1 ATOM 3322 O O . THR A 1 431 ? 39.353 11.667 18.974 1.00 10.74 ? 431 THR A O 1 ATOM 3323 C CB . THR A 1 431 ? 36.658 9.784 18.979 1.00 11.78 ? 431 THR A CB 1 ATOM 3324 O OG1 . THR A 1 431 ? 37.086 10.029 20.329 1.00 11.09 ? 431 THR A OG1 1 ATOM 3325 C CG2 . THR A 1 431 ? 36.153 8.348 18.846 1.00 12.83 ? 431 THR A CG2 1 ATOM 3326 N N . HIS A 1 432 ? 37.625 12.458 17.739 1.00 11.72 ? 432 HIS A N 1 ATOM 3327 C CA . HIS A 1 432 ? 37.726 13.820 18.229 1.00 12.07 ? 432 HIS A CA 1 ATOM 3328 C C . HIS A 1 432 ? 37.531 13.852 19.749 1.00 11.61 ? 432 HIS A C 1 ATOM 3329 O O . HIS A 1 432 ? 37.000 12.892 20.367 1.00 11.49 ? 432 HIS A O 1 ATOM 3330 C CB . HIS A 1 432 ? 36.666 14.706 17.572 1.00 11.51 ? 432 HIS A CB 1 ATOM 3331 C CG . HIS A 1 432 ? 36.791 14.802 16.079 1.00 13.13 ? 432 HIS A CG 1 ATOM 3332 N ND1 . HIS A 1 432 ? 35.801 15.351 15.295 1.00 11.07 ? 432 HIS A ND1 1 ATOM 3333 C CD2 . HIS A 1 432 ? 37.767 14.397 15.224 1.00 11.96 ? 432 HIS A CD2 1 ATOM 3334 C CE1 . HIS A 1 432 ? 36.169 15.309 14.026 1.00 13.85 ? 432 HIS A CE1 1 ATOM 3335 N NE2 . HIS A 1 432 ? 37.356 14.730 13.953 1.00 11.97 ? 432 HIS A NE2 1 ATOM 3336 N N . ALA A 1 433 ? 37.985 14.944 20.352 1.00 10.73 ? 433 ALA A N 1 ATOM 3337 C CA . ALA A 1 433 ? 37.722 15.199 21.753 1.00 10.85 ? 433 ALA A CA 1 ATOM 3338 C C . ALA A 1 433 ? 36.998 16.527 21.888 1.00 10.59 ? 433 ALA A C 1 ATOM 3339 O O . ALA A 1 433 ? 37.077 17.378 20.995 1.00 11.04 ? 433 ALA A O 1 ATOM 3340 C CB . ALA A 1 433 ? 39.010 15.183 22.566 1.00 10.18 ? 433 ALA A CB 1 ATOM 3341 N N . GLY A 1 434 ? 36.267 16.686 22.988 1.00 10.44 ? 434 GLY A N 1 ATOM 3342 C CA . GLY A 1 434 ? 35.360 17.806 23.135 1.00 11.09 ? 434 GLY A CA 1 ATOM 3343 C C . GLY A 1 434 ? 35.864 18.947 23.991 1.00 10.94 ? 434 GLY A C 1 ATOM 3344 O O . GLY A 1 434 ? 35.134 19.905 24.206 1.00 11.98 ? 434 GLY A O 1 ATOM 3345 N N . GLU A 1 435 ? 37.097 18.870 24.490 1.00 11.71 ? 435 GLU A N 1 ATOM 3346 C CA . GLU A 1 435 ? 37.575 19.934 25.370 1.00 11.37 ? 435 GLU A CA 1 ATOM 3347 C C . GLU A 1 435 ? 37.888 21.217 24.585 1.00 11.28 ? 435 GLU A C 1 ATOM 3348 O O . GLU A 1 435 ? 38.078 21.176 23.363 1.00 11.11 ? 435 GLU A O 1 ATOM 3349 C CB . GLU A 1 435 ? 38.767 19.485 26.210 1.00 11.25 ? 435 GLU A CB 1 ATOM 3350 C CG . GLU A 1 435 ? 40.141 19.705 25.576 1.00 11.81 ? 435 GLU A CG 1 ATOM 3351 C CD . GLU A 1 435 ? 40.520 18.639 24.553 1.00 13.39 ? 435 GLU A CD 1 ATOM 3352 O OE1 . GLU A 1 435 ? 39.697 17.743 24.238 1.00 14.42 ? 435 GLU A OE1 1 ATOM 3353 O OE2 . GLU A 1 435 ? 41.662 18.704 24.063 1.00 15.48 ? 435 GLU A OE2 1 ATOM 3354 N N . ASP A 1 436 ? 37.926 22.338 25.296 1.00 10.55 ? 436 ASP A N 1 ATOM 3355 C CA . ASP A 1 436 ? 38.163 23.637 24.662 1.00 11.36 ? 436 ASP A CA 1 ATOM 3356 C C . ASP A 1 436 ? 39.456 23.620 23.891 1.00 11.18 ? 436 ASP A C 1 ATOM 3357 O O . ASP A 1 436 ? 40.425 22.944 24.279 1.00 11.12 ? 436 ASP A O 1 ATOM 3358 C CB . ASP A 1 436 ? 38.259 24.745 25.697 1.00 11.18 ? 436 ASP A CB 1 ATOM 3359 C CG . ASP A 1 436 ? 37.029 24.839 26.561 1.00 13.05 ? 436 ASP A CG 1 ATOM 3360 O OD1 . ASP A 1 436 ? 35.998 24.188 26.243 1.00 14.65 ? 436 ASP A OD1 1 ATOM 3361 O OD2 . ASP A 1 436 ? 37.105 25.564 27.570 1.00 17.25 ? 436 ASP A OD2 1 ATOM 3362 N N . VAL A 1 437 ? 39.471 24.380 22.809 1.00 10.76 ? 437 VAL A N 1 ATOM 3363 C CA . VAL A 1 437 ? 40.697 24.555 22.052 1.00 10.69 ? 437 VAL A CA 1 ATOM 3364 C C . VAL A 1 437 ? 41.136 25.993 22.173 1.00 11.12 ? 437 VAL A C 1 ATOM 3365 O O . VAL A 1 437 ? 40.350 26.863 22.578 1.00 11.55 ? 437 VAL A O 1 ATOM 3366 C CB . VAL A 1 437 ? 40.551 24.132 20.582 1.00 10.63 ? 437 VAL A CB 1 ATOM 3367 C CG1 . VAL A 1 437 ? 40.121 22.654 20.505 1.00 9.58 ? 437 VAL A CG1 1 ATOM 3368 C CG2 . VAL A 1 437 ? 39.558 25.049 19.847 1.00 10.42 ? 437 VAL A CG2 1 ATOM 3369 N N . ALA A 1 438 ? 42.392 26.237 21.836 1.00 11.09 ? 438 ALA A N 1 ATOM 3370 C CA . ALA A 1 438 ? 42.941 27.576 21.921 1.00 11.85 ? 438 ALA A CA 1 ATOM 3371 C C . ALA A 1 438 ? 42.568 28.389 20.704 1.00 11.92 ? 438 ALA A C 1 ATOM 3372 O O . ALA A 1 438 ? 42.380 27.851 19.604 1.00 11.61 ? 438 ALA A O 1 ATOM 3373 C CB . ALA A 1 438 ? 44.470 27.521 22.071 1.00 12.41 ? 438 ALA A CB 1 ATOM 3374 N N . VAL A 1 439 ? 42.453 29.692 20.915 1.00 11.62 ? 439 VAL A N 1 ATOM 3375 C CA . VAL A 1 439 ? 42.437 30.646 19.824 1.00 12.48 ? 439 VAL A CA 1 ATOM 3376 C C . VAL A 1 439 ? 43.608 31.579 20.076 1.00 12.72 ? 439 VAL A C 1 ATOM 3377 O O . VAL A 1 439 ? 43.772 32.059 21.197 1.00 13.77 ? 439 VAL A O 1 ATOM 3378 C CB . VAL A 1 439 ? 41.130 31.485 19.787 1.00 12.93 ? 439 VAL A CB 1 ATOM 3379 C CG1 . VAL A 1 439 ? 41.077 32.341 18.499 1.00 12.50 ? 439 VAL A CG1 1 ATOM 3380 C CG2 . VAL A 1 439 ? 39.914 30.593 19.880 1.00 12.82 ? 439 VAL A CG2 1 ATOM 3381 N N . PHE A 1 440 ? 44.436 31.795 19.056 1.00 12.11 ? 440 PHE A N 1 ATOM 3382 C CA . PHE A 1 440 ? 45.545 32.733 19.145 1.00 12.48 ? 440 PHE A CA 1 ATOM 3383 C C . PHE A 1 440 ? 45.199 33.848 18.182 1.00 12.71 ? 440 PHE A C 1 ATOM 3384 O O . PHE A 1 440 ? 44.708 33.572 17.086 1.00 12.71 ? 440 PHE A O 1 ATOM 3385 C CB . PHE A 1 440 ? 46.857 32.087 18.689 1.00 12.50 ? 440 PHE A CB 1 ATOM 3386 C CG . PHE A 1 440 ? 47.175 30.783 19.364 1.00 12.63 ? 440 PHE A CG 1 ATOM 3387 C CD1 . PHE A 1 440 ? 46.645 29.583 18.895 1.00 13.42 ? 440 PHE A CD1 1 ATOM 3388 C CD2 . PHE A 1 440 ? 48.070 30.742 20.429 1.00 13.97 ? 440 PHE A CD2 1 ATOM 3389 C CE1 . PHE A 1 440 ? 46.963 28.371 19.508 1.00 13.39 ? 440 PHE A CE1 1 ATOM 3390 C CE2 . PHE A 1 440 ? 48.398 29.525 21.043 1.00 14.15 ? 440 PHE A CE2 1 ATOM 3391 C CZ . PHE A 1 440 ? 47.840 28.342 20.578 1.00 13.79 ? 440 PHE A CZ 1 ATOM 3392 N N . ALA A 1 441 ? 45.470 35.099 18.564 1.00 12.01 ? 441 ALA A N 1 ATOM 3393 C CA . ALA A 1 441 ? 45.123 36.224 17.698 1.00 12.51 ? 441 ALA A CA 1 ATOM 3394 C C . ALA A 1 441 ? 46.160 37.324 17.731 1.00 13.05 ? 441 ALA A C 1 ATOM 3395 O O . ALA A 1 441 ? 46.747 37.601 18.782 1.00 13.09 ? 441 ALA A O 1 ATOM 3396 C CB . ALA A 1 441 ? 43.735 36.797 18.065 1.00 12.29 ? 441 ALA A CB 1 ATOM 3397 N N . ARG A 1 442 ? 46.372 37.938 16.572 1.00 13.19 ? 442 ARG A N 1 ATOM 3398 C CA . ARG A 1 442 ? 47.192 39.136 16.464 1.00 14.34 ? 442 ARG A CA 1 ATOM 3399 C C . ARG A 1 442 ? 46.656 40.053 15.364 1.00 14.22 ? 442 ARG A C 1 ATOM 3400 O O . ARG A 1 442 ? 45.994 39.596 14.423 1.00 14.36 ? 442 ARG A O 1 ATOM 3401 C CB . ARG A 1 442 ? 48.658 38.800 16.194 1.00 14.60 ? 442 ARG A CB 1 ATOM 3402 C CG . ARG A 1 442 ? 48.955 38.355 14.800 1.00 17.51 ? 442 ARG A CG 1 ATOM 3403 C CD . ARG A 1 442 ? 50.420 38.621 14.445 1.00 18.74 ? 442 ARG A CD 1 ATOM 3404 N NE . ARG A 1 442 ? 51.314 37.633 15.029 1.00 21.56 ? 442 ARG A NE 1 ATOM 3405 C CZ . ARG A 1 442 ? 52.152 37.865 16.037 1.00 22.74 ? 442 ARG A CZ 1 ATOM 3406 N NH1 . ARG A 1 442 ? 52.930 36.890 16.472 1.00 22.65 ? 442 ARG A NH1 1 ATOM 3407 N NH2 . ARG A 1 442 ? 52.229 39.062 16.600 1.00 23.56 ? 442 ARG A NH2 1 ATOM 3408 N N . GLY A 1 443 ? 46.961 41.341 15.485 1.00 14.29 ? 443 GLY A N 1 ATOM 3409 C CA . GLY A 1 443 ? 46.523 42.321 14.512 1.00 14.66 ? 443 GLY A CA 1 ATOM 3410 C C . GLY A 1 443 ? 45.371 43.156 15.017 1.00 14.88 ? 443 GLY A C 1 ATOM 3411 O O . GLY A 1 443 ? 45.028 43.095 16.201 1.00 15.25 ? 443 GLY A O 1 ATOM 3412 N N . PRO A 1 444 ? 44.766 43.958 14.125 1.00 15.48 ? 444 PRO A N 1 ATOM 3413 C CA . PRO A 1 444 ? 43.737 44.896 14.543 1.00 15.54 ? 444 PRO A CA 1 ATOM 3414 C C . PRO A 1 444 ? 42.542 44.186 15.162 1.00 15.65 ? 444 PRO A C 1 ATOM 3415 O O . PRO A 1 444 ? 41.983 43.270 14.552 1.00 15.18 ? 444 PRO A O 1 ATOM 3416 C CB . PRO A 1 444 ? 43.338 45.587 13.228 1.00 16.11 ? 444 PRO A CB 1 ATOM 3417 C CG . PRO A 1 444 ? 44.533 45.432 12.349 1.00 15.82 ? 444 PRO A CG 1 ATOM 3418 C CD . PRO A 1 444 ? 45.047 44.065 12.681 1.00 14.92 ? 444 PRO A CD 1 ATOM 3419 N N . GLN A 1 445 ? 42.184 44.602 16.378 1.00 14.87 ? 445 GLN A N 1 ATOM 3420 C CA . GLN A 1 445 ? 41.050 44.047 17.123 1.00 15.24 ? 445 GLN A CA 1 ATOM 3421 C C . GLN A 1 445 ? 41.309 42.658 17.717 1.00 14.84 ? 445 GLN A C 1 ATOM 3422 O O . GLN A 1 445 ? 40.407 42.046 18.290 1.00 15.31 ? 445 GLN A O 1 ATOM 3423 C CB . GLN A 1 445 ? 39.753 44.096 16.287 1.00 15.00 ? 445 GLN A CB 1 ATOM 3424 C CG . GLN A 1 445 ? 39.474 45.490 15.676 1.00 16.21 ? 445 GLN A CG 1 ATOM 3425 C CD . GLN A 1 445 ? 39.609 46.600 16.702 1.00 18.26 ? 445 GLN A CD 1 ATOM 3426 O OE1 . GLN A 1 445 ? 38.997 46.540 17.777 1.00 20.64 ? 445 GLN A OE1 1 ATOM 3427 N NE2 . GLN A 1 445 ? 40.432 47.606 16.397 1.00 16.11 ? 445 GLN A NE2 1 ATOM 3428 N N . ALA A 1 446 ? 42.546 42.169 17.601 1.00 13.89 ? 446 ALA A N 1 ATOM 3429 C CA . ALA A 1 446 ? 42.913 40.866 18.176 1.00 13.64 ? 446 ALA A CA 1 ATOM 3430 C C . ALA A 1 446 ? 42.717 40.831 19.699 1.00 13.42 ? 446 ALA A C 1 ATOM 3431 O O . ALA A 1 446 ? 42.421 39.780 20.261 1.00 12.78 ? 446 ALA A O 1 ATOM 3432 C CB . ALA A 1 446 ? 44.345 40.517 17.825 1.00 12.63 ? 446 ALA A CB 1 ATOM 3433 N N . HIS A 1 447 ? 42.847 41.987 20.350 1.00 14.02 ? 447 HIS A N 1 ATOM 3434 C CA . HIS A 1 447 ? 42.656 42.096 21.796 1.00 14.66 ? 447 HIS A CA 1 ATOM 3435 C C . HIS A 1 447 ? 41.220 41.718 22.207 1.00 14.88 ? 447 HIS A C 1 ATOM 3436 O O . HIS A 1 447 ? 40.963 41.455 23.387 1.00 15.20 ? 447 HIS A O 1 ATOM 3437 C CB . HIS A 1 447 ? 42.998 43.515 22.290 1.00 14.96 ? 447 HIS A CB 1 ATOM 3438 C CG . HIS A 1 447 ? 42.010 44.547 21.847 1.00 16.73 ? 447 HIS A CG 1 ATOM 3439 N ND1 . HIS A 1 447 ? 42.022 45.087 20.580 1.00 18.89 ? 447 HIS A ND1 1 ATOM 3440 C CD2 . HIS A 1 447 ? 40.956 45.107 22.486 1.00 17.34 ? 447 HIS A CD2 1 ATOM 3441 C CE1 . HIS A 1 447 ? 41.026 45.948 20.460 1.00 18.01 ? 447 HIS A CE1 1 ATOM 3442 N NE2 . HIS A 1 447 ? 40.374 45.989 21.607 1.00 18.17 ? 447 HIS A NE2 1 ATOM 3443 N N . LEU A 1 448 ? 40.294 41.696 21.244 1.00 14.17 ? 448 LEU A N 1 ATOM 3444 C CA . LEU A 1 448 ? 38.922 41.254 21.517 1.00 13.95 ? 448 LEU A CA 1 ATOM 3445 C C . LEU A 1 448 ? 38.815 39.743 21.725 1.00 13.87 ? 448 LEU A C 1 ATOM 3446 O O . LEU A 1 448 ? 37.848 39.254 22.327 1.00 13.46 ? 448 LEU A O 1 ATOM 3447 C CB . LEU A 1 448 ? 37.964 41.720 20.419 1.00 14.26 ? 448 LEU A CB 1 ATOM 3448 C CG . LEU A 1 448 ? 37.871 43.240 20.249 1.00 14.57 ? 448 LEU A CG 1 ATOM 3449 C CD1 . LEU A 1 448 ? 36.829 43.561 19.206 1.00 14.64 ? 448 LEU A CD1 1 ATOM 3450 C CD2 . LEU A 1 448 ? 37.580 43.949 21.582 1.00 13.82 ? 448 LEU A CD2 1 ATOM 3451 N N . VAL A 1 449 ? 39.802 39.006 21.212 1.00 13.39 ? 449 VAL A N 1 ATOM 3452 C CA . VAL A 1 449 ? 39.882 37.560 21.430 1.00 13.15 ? 449 VAL A CA 1 ATOM 3453 C C . VAL A 1 449 ? 40.416 37.356 22.852 1.00 13.22 ? 449 VAL A C 1 ATOM 3454 O O . VAL A 1 449 ? 41.596 37.553 23.107 1.00 13.24 ? 449 VAL A O 1 ATOM 3455 C CB . VAL A 1 449 ? 40.784 36.875 20.369 1.00 13.02 ? 449 VAL A CB 1 ATOM 3456 C CG1 . VAL A 1 449 ? 40.954 35.364 20.663 1.00 12.76 ? 449 VAL A CG1 1 ATOM 3457 C CG2 . VAL A 1 449 ? 40.192 37.087 18.969 1.00 12.94 ? 449 VAL A CG2 1 ATOM 3458 N N . HIS A 1 450 ? 39.534 36.997 23.783 1.00 13.10 ? 450 HIS A N 1 ATOM 3459 C CA . HIS A 1 450 ? 39.937 36.866 25.184 1.00 13.15 ? 450 HIS A CA 1 ATOM 3460 C C . HIS A 1 450 ? 39.013 35.905 25.912 1.00 13.25 ? 450 HIS A C 1 ATOM 3461 O O . HIS A 1 450 ? 37.903 35.624 25.448 1.00 13.75 ? 450 HIS A O 1 ATOM 3462 C CB . HIS A 1 450 ? 39.836 38.228 25.870 1.00 12.69 ? 450 HIS A CB 1 ATOM 3463 C CG . HIS A 1 450 ? 38.426 38.601 26.164 1.00 13.59 ? 450 HIS A CG 1 ATOM 3464 N ND1 . HIS A 1 450 ? 37.842 38.397 27.398 1.00 15.26 ? 450 HIS A ND1 1 ATOM 3465 C CD2 . HIS A 1 450 ? 37.438 39.027 25.344 1.00 14.83 ? 450 HIS A CD2 1 ATOM 3466 C CE1 . HIS A 1 450 ? 36.566 38.740 27.337 1.00 14.95 ? 450 HIS A CE1 1 ATOM 3467 N NE2 . HIS A 1 450 ? 36.295 39.117 26.100 1.00 16.77 ? 450 HIS A NE2 1 ATOM 3468 N N . GLY A 1 451 ? 39.473 35.424 27.061 1.00 13.26 ? 451 GLY A N 1 ATOM 3469 C CA . GLY A 1 451 ? 38.637 34.680 27.987 1.00 12.96 ? 451 GLY A CA 1 ATOM 3470 C C . GLY A 1 451 ? 38.212 33.345 27.415 1.00 13.47 ? 451 GLY A C 1 ATOM 3471 O O . GLY A 1 451 ? 38.955 32.715 26.660 1.00 13.41 ? 451 GLY A O 1 ATOM 3472 N N . VAL A 1 452 ? 37.017 32.914 27.793 1.00 13.02 ? 452 VAL A N 1 ATOM 3473 C CA . VAL A 1 452 ? 36.442 31.662 27.289 1.00 12.70 ? 452 VAL A CA 1 ATOM 3474 C C . VAL A 1 452 ? 35.243 32.057 26.456 1.00 13.24 ? 452 VAL A C 1 ATOM 3475 O O . VAL A 1 452 ? 34.316 32.695 26.964 1.00 12.57 ? 452 VAL A O 1 ATOM 3476 C CB . VAL A 1 452 ? 36.005 30.727 28.465 1.00 12.67 ? 452 VAL A CB 1 ATOM 3477 C CG1 . VAL A 1 452 ? 35.409 29.400 27.947 1.00 12.16 ? 452 VAL A CG1 1 ATOM 3478 C CG2 . VAL A 1 452 ? 37.187 30.479 29.383 1.00 12.30 ? 452 VAL A CG2 1 ATOM 3479 N N . GLN A 1 453 ? 35.276 31.680 25.181 1.00 12.95 ? 453 GLN A N 1 ATOM 3480 C CA . GLN A 1 453 ? 34.272 32.084 24.211 1.00 13.95 ? 453 GLN A CA 1 ATOM 3481 C C . GLN A 1 453 ? 33.670 30.884 23.491 1.00 13.47 ? 453 GLN A C 1 ATOM 3482 O O . GLN A 1 453 ? 34.286 29.828 23.379 1.00 13.46 ? 453 GLN A O 1 ATOM 3483 C CB . GLN A 1 453 ? 34.886 33.074 23.201 1.00 13.56 ? 453 GLN A CB 1 ATOM 3484 C CG . GLN A 1 453 ? 35.431 34.295 23.935 1.00 16.98 ? 453 GLN A CG 1 ATOM 3485 C CD . GLN A 1 453 ? 36.268 35.252 23.122 1.00 21.86 ? 453 GLN A CD 1 ATOM 3486 O OE1 . GLN A 1 453 ? 37.180 34.855 22.385 1.00 24.82 ? 453 GLN A OE1 1 ATOM 3487 N NE2 . GLN A 1 453 ? 35.995 36.555 23.301 1.00 24.31 ? 453 GLN A NE2 1 ATOM 3488 N N . GLU A 1 454 ? 32.445 31.056 23.015 1.00 13.50 ? 454 GLU A N 1 ATOM 3489 C CA . GLU A 1 454 ? 31.891 30.133 22.042 1.00 13.00 ? 454 GLU A CA 1 ATOM 3490 C C . GLU A 1 454 ? 32.730 30.186 20.784 1.00 12.56 ? 454 GLU A C 1 ATOM 3491 O O . GLU A 1 454 ? 33.250 31.236 20.434 1.00 12.41 ? 454 GLU A O 1 ATOM 3492 C CB . GLU A 1 454 ? 30.459 30.532 21.704 1.00 12.93 ? 454 GLU A CB 1 ATOM 3493 C CG . GLU A 1 454 ? 29.480 30.309 22.847 1.00 13.70 ? 454 GLU A CG 1 ATOM 3494 C CD . GLU A 1 454 ? 29.172 28.847 23.066 1.00 14.32 ? 454 GLU A CD 1 ATOM 3495 O OE1 . GLU A 1 454 ? 29.693 27.996 22.302 1.00 14.35 ? 454 GLU A OE1 1 ATOM 3496 O OE2 . GLU A 1 454 ? 28.406 28.549 24.008 1.00 16.06 ? 454 GLU A OE2 1 ATOM 3497 N N . GLN A 1 455 ? 32.855 29.054 20.103 1.00 12.11 ? 455 GLN A N 1 ATOM 3498 C CA . GLN A 1 455 ? 33.617 28.985 18.852 1.00 12.16 ? 455 GLN A CA 1 ATOM 3499 C C . GLN A 1 455 ? 33.133 29.975 17.792 1.00 12.27 ? 455 GLN A C 1 ATOM 3500 O O . GLN A 1 455 ? 33.897 30.385 16.927 1.00 12.50 ? 455 GLN A O 1 ATOM 3501 C CB . GLN A 1 455 ? 33.549 27.573 18.292 1.00 12.73 ? 455 GLN A CB 1 ATOM 3502 C CG . GLN A 1 455 ? 34.468 27.329 17.113 1.00 11.91 ? 455 GLN A CG 1 ATOM 3503 C CD . GLN A 1 455 ? 34.608 25.856 16.861 1.00 13.05 ? 455 GLN A CD 1 ATOM 3504 O OE1 . GLN A 1 455 ? 33.600 25.149 16.734 1.00 14.03 ? 455 GLN A OE1 1 ATOM 3505 N NE2 . GLN A 1 455 ? 35.843 25.369 16.817 1.00 10.38 ? 455 GLN A NE2 1 ATOM 3506 N N . THR A 1 456 ? 31.867 30.373 17.882 1.00 11.99 ? 456 THR A N 1 ATOM 3507 C CA . THR A 1 456 ? 31.279 31.308 16.929 1.00 12.56 ? 456 THR A CA 1 ATOM 3508 C C . THR A 1 456 ? 31.949 32.673 17.007 1.00 12.84 ? 456 THR A C 1 ATOM 3509 O O . THR A 1 456 ? 31.945 33.411 16.019 1.00 13.15 ? 456 THR A O 1 ATOM 3510 C CB . THR A 1 456 ? 29.802 31.525 17.213 1.00 12.18 ? 456 THR A CB 1 ATOM 3511 O OG1 . THR A 1 456 ? 29.670 31.848 18.598 1.00 13.54 ? 456 THR A OG1 1 ATOM 3512 C CG2 . THR A 1 456 ? 28.991 30.248 16.897 1.00 10.95 ? 456 THR A CG2 1 ATOM 3513 N N . PHE A 1 457 ? 32.519 33.001 18.170 1.00 12.61 ? 457 PHE A N 1 ATOM 3514 C CA . PHE A 1 457 ? 33.208 34.280 18.359 1.00 13.88 ? 457 PHE A CA 1 ATOM 3515 C C . PHE A 1 457 ? 34.288 34.514 17.306 1.00 13.41 ? 457 PHE A C 1 ATOM 3516 O O . PHE A 1 457 ? 34.547 35.649 16.917 1.00 13.00 ? 457 PHE A O 1 ATOM 3517 C CB . PHE A 1 457 ? 33.831 34.365 19.753 1.00 13.81 ? 457 PHE A CB 1 ATOM 3518 C CG . PHE A 1 457 ? 34.308 35.734 20.108 1.00 14.92 ? 457 PHE A CG 1 ATOM 3519 C CD1 . PHE A 1 457 ? 33.406 36.698 20.570 1.00 14.79 ? 457 PHE A CD1 1 ATOM 3520 C CD2 . PHE A 1 457 ? 35.649 36.074 19.963 1.00 15.96 ? 457 PHE A CD2 1 ATOM 3521 C CE1 . PHE A 1 457 ? 33.840 37.988 20.902 1.00 17.85 ? 457 PHE A CE1 1 ATOM 3522 C CE2 . PHE A 1 457 ? 36.106 37.364 20.296 1.00 17.49 ? 457 PHE A CE2 1 ATOM 3523 C CZ . PHE A 1 457 ? 35.193 38.325 20.762 1.00 16.56 ? 457 PHE A CZ 1 ATOM 3524 N N . ILE A 1 458 ? 34.924 33.434 16.866 1.00 13.60 ? 458 ILE A N 1 ATOM 3525 C CA . ILE A 1 458 ? 35.989 33.523 15.866 1.00 13.67 ? 458 ILE A CA 1 ATOM 3526 C C . ILE A 1 458 ? 35.489 34.232 14.603 1.00 13.59 ? 458 ILE A C 1 ATOM 3527 O O . ILE A 1 458 ? 36.117 35.171 14.120 1.00 13.52 ? 458 ILE A O 1 ATOM 3528 C CB . ILE A 1 458 ? 36.551 32.129 15.555 1.00 13.46 ? 458 ILE A CB 1 ATOM 3529 C CG1 . ILE A 1 458 ? 37.322 31.631 16.789 1.00 14.42 ? 458 ILE A CG1 1 ATOM 3530 C CG2 . ILE A 1 458 ? 37.471 32.173 14.332 1.00 13.34 ? 458 ILE A CG2 1 ATOM 3531 C CD1 . ILE A 1 458 ? 37.301 30.132 16.928 1.00 16.99 ? 458 ILE A CD1 1 ATOM 3532 N N . ALA A 1 459 ? 34.365 33.770 14.067 1.00 13.23 ? 459 ALA A N 1 ATOM 3533 C CA . ALA A 1 459 ? 33.800 34.403 12.889 1.00 13.01 ? 459 ALA A CA 1 ATOM 3534 C C . ALA A 1 459 ? 33.435 35.854 13.183 1.00 13.40 ? 459 ALA A C 1 ATOM 3535 O O . ALA A 1 459 ? 33.726 36.746 12.389 1.00 13.58 ? 459 ALA A O 1 ATOM 3536 C CB . ALA A 1 459 ? 32.592 33.642 12.408 1.00 13.00 ? 459 ALA A CB 1 ATOM 3537 N N . HIS A 1 460 ? 32.802 36.087 14.326 1.00 13.49 ? 460 HIS A N 1 ATOM 3538 C CA . HIS A 1 460 ? 32.264 37.416 14.624 1.00 13.58 ? 460 HIS A CA 1 ATOM 3539 C C . HIS A 1 460 ? 33.339 38.469 14.822 1.00 13.38 ? 460 HIS A C 1 ATOM 3540 O O . HIS A 1 460 ? 33.189 39.597 14.351 1.00 13.43 ? 460 HIS A O 1 ATOM 3541 C CB . HIS A 1 460 ? 31.324 37.355 15.816 1.00 13.22 ? 460 HIS A CB 1 ATOM 3542 C CG . HIS A 1 460 ? 30.006 36.729 15.484 1.00 13.29 ? 460 HIS A CG 1 ATOM 3543 N ND1 . HIS A 1 460 ? 28.910 37.471 15.092 1.00 14.24 ? 460 HIS A ND1 1 ATOM 3544 C CD2 . HIS A 1 460 ? 29.618 35.430 15.449 1.00 12.69 ? 460 HIS A CD2 1 ATOM 3545 C CE1 . HIS A 1 460 ? 27.898 36.658 14.842 1.00 13.35 ? 460 HIS A CE1 1 ATOM 3546 N NE2 . HIS A 1 460 ? 28.297 35.413 15.060 1.00 13.91 ? 460 HIS A NE2 1 ATOM 3547 N N . VAL A 1 461 ? 34.407 38.112 15.526 1.00 12.86 ? 461 VAL A N 1 ATOM 3548 C CA . VAL A 1 461 ? 35.494 39.077 15.746 1.00 13.43 ? 461 VAL A CA 1 ATOM 3549 C C . VAL A 1 461 ? 36.174 39.427 14.413 1.00 14.05 ? 461 VAL A C 1 ATOM 3550 O O . VAL A 1 461 ? 36.583 40.578 14.190 1.00 14.03 ? 461 VAL A O 1 ATOM 3551 C CB . VAL A 1 461 ? 36.495 38.585 16.839 1.00 13.42 ? 461 VAL A CB 1 ATOM 3552 C CG1 . VAL A 1 461 ? 37.361 37.414 16.329 1.00 12.99 ? 461 VAL A CG1 1 ATOM 3553 C CG2 . VAL A 1 461 ? 37.358 39.739 17.343 1.00 14.71 ? 461 VAL A CG2 1 ATOM 3554 N N . MET A 1 462 ? 36.270 38.444 13.521 1.00 13.64 ? 462 MET A N 1 ATOM 3555 C CA . MET A 1 462 ? 36.831 38.685 12.195 1.00 14.93 ? 462 MET A CA 1 ATOM 3556 C C . MET A 1 462 ? 35.944 39.631 11.376 1.00 14.63 ? 462 MET A C 1 ATOM 3557 O O . MET A 1 462 ? 36.447 40.588 10.776 1.00 13.81 ? 462 MET A O 1 ATOM 3558 C CB . MET A 1 462 ? 37.060 37.362 11.468 1.00 14.13 ? 462 MET A CB 1 ATOM 3559 C CG . MET A 1 462 ? 38.138 36.517 12.177 1.00 15.67 ? 462 MET A CG 1 ATOM 3560 S SD . MET A 1 462 ? 38.510 34.984 11.327 1.00 17.37 ? 462 MET A SD 1 ATOM 3561 C CE . MET A 1 462 ? 39.537 35.584 9.982 1.00 18.89 ? 462 MET A CE 1 ATOM 3562 N N . ALA A 1 463 ? 34.633 39.371 11.365 1.00 14.63 ? 463 ALA A N 1 ATOM 3563 C CA . ALA A 1 463 ? 33.702 40.254 10.666 1.00 14.82 ? 463 ALA A CA 1 ATOM 3564 C C . ALA A 1 463 ? 33.763 41.650 11.272 1.00 15.77 ? 463 ALA A C 1 ATOM 3565 O O . ALA A 1 463 ? 33.810 42.664 10.548 1.00 16.12 ? 463 ALA A O 1 ATOM 3566 C CB . ALA A 1 463 ? 32.297 39.703 10.719 1.00 14.92 ? 463 ALA A CB 1 ATOM 3567 N N . PHE A 1 464 ? 33.775 41.709 12.600 1.00 15.69 ? 464 PHE A N 1 ATOM 3568 C CA . PHE A 1 464 ? 33.839 42.994 13.281 1.00 15.41 ? 464 PHE A CA 1 ATOM 3569 C C . PHE A 1 464 ? 35.106 43.774 12.906 1.00 15.73 ? 464 PHE A C 1 ATOM 3570 O O . PHE A 1 464 ? 35.049 44.957 12.559 1.00 15.09 ? 464 PHE A O 1 ATOM 3571 C CB . PHE A 1 464 ? 33.787 42.822 14.803 1.00 15.19 ? 464 PHE A CB 1 ATOM 3572 C CG . PHE A 1 464 ? 34.046 44.100 15.538 1.00 15.25 ? 464 PHE A CG 1 ATOM 3573 C CD1 . PHE A 1 464 ? 33.053 45.071 15.632 1.00 18.11 ? 464 PHE A CD1 1 ATOM 3574 C CD2 . PHE A 1 464 ? 35.299 44.371 16.074 1.00 15.97 ? 464 PHE A CD2 1 ATOM 3575 C CE1 . PHE A 1 464 ? 33.298 46.287 16.289 1.00 17.16 ? 464 PHE A CE1 1 ATOM 3576 C CE2 . PHE A 1 464 ? 35.549 45.595 16.729 1.00 16.82 ? 464 PHE A CE2 1 ATOM 3577 C CZ . PHE A 1 464 ? 34.556 46.538 16.836 1.00 17.25 ? 464 PHE A CZ 1 ATOM 3578 N N . ALA A 1 465 ? 36.248 43.103 12.988 1.00 15.38 ? 465 ALA A N 1 ATOM 3579 C CA . ALA A 1 465 ? 37.533 43.760 12.750 1.00 15.77 ? 465 ALA A CA 1 ATOM 3580 C C . ALA A 1 465 ? 37.632 44.372 11.358 1.00 16.07 ? 465 ALA A C 1 ATOM 3581 O O . ALA A 1 465 ? 38.228 45.440 11.186 1.00 16.66 ? 465 ALA A O 1 ATOM 3582 C CB . ALA A 1 465 ? 38.680 42.780 12.981 1.00 15.07 ? 465 ALA A CB 1 ATOM 3583 N N . ALA A 1 466 ? 37.061 43.696 10.363 1.00 15.80 ? 466 ALA A N 1 ATOM 3584 C CA . ALA A 1 466 ? 37.083 44.199 8.990 1.00 16.45 ? 466 ALA A CA 1 ATOM 3585 C C . ALA A 1 466 ? 35.832 45.001 8.626 1.00 17.40 ? 466 ALA A C 1 ATOM 3586 O O . ALA A 1 466 ? 35.639 45.355 7.451 1.00 17.47 ? 466 ALA A O 1 ATOM 3587 C CB . ALA A 1 466 ? 37.279 43.023 7.999 1.00 16.48 ? 466 ALA A CB 1 ATOM 3588 N N . CYS A 1 467 ? 34.992 45.296 9.624 1.00 18.40 ? 467 CYS A N 1 ATOM 3589 C CA . CYS A 1 467 ? 33.735 46.055 9.434 1.00 19.79 ? 467 CYS A CA 1 ATOM 3590 C C . CYS A 1 467 ? 32.831 45.451 8.376 1.00 19.99 ? 467 CYS A C 1 ATOM 3591 O O . CYS A 1 467 ? 32.245 46.155 7.548 1.00 20.62 ? 467 CYS A O 1 ATOM 3592 C CB . CYS A 1 467 ? 34.021 47.540 9.151 1.00 20.89 ? 467 CYS A CB 1 ATOM 3593 S SG . CYS A 1 467 ? 35.146 48.214 10.396 1.00 26.03 ? 467 CYS A SG 1 ATOM 3594 N N . LEU A 1 468 ? 32.717 44.131 8.413 1.00 19.14 ? 468 LEU A N 1 ATOM 3595 C CA . LEU A 1 468 ? 31.864 43.400 7.500 1.00 19.69 ? 468 LEU A CA 1 ATOM 3596 C C . LEU A 1 468 ? 30.538 43.180 8.198 1.00 20.05 ? 468 LEU A C 1 ATOM 3597 O O . LEU A 1 468 ? 30.479 43.193 9.428 1.00 19.07 ? 468 LEU A O 1 ATOM 3598 C CB . LEU A 1 468 ? 32.504 42.043 7.176 1.00 19.27 ? 468 LEU A CB 1 ATOM 3599 C CG . LEU A 1 468 ? 33.908 42.048 6.563 1.00 19.69 ? 468 LEU A CG 1 ATOM 3600 C CD1 . LEU A 1 468 ? 34.479 40.631 6.448 1.00 17.17 ? 468 LEU A CD1 1 ATOM 3601 C CD2 . LEU A 1 468 ? 33.885 42.750 5.198 1.00 21.20 ? 468 LEU A CD2 1 ATOM 3602 N N . GLU A 1 469 ? 29.480 42.976 7.420 1.00 21.08 ? 469 GLU A N 1 ATOM 3603 C CA . GLU A 1 469 ? 28.189 42.538 7.956 1.00 23.19 ? 469 GLU A CA 1 ATOM 3604 C C . GLU A 1 469 ? 28.414 41.453 8.993 1.00 22.04 ? 469 GLU A C 1 ATOM 3605 O O . GLU A 1 469 ? 29.216 40.556 8.757 1.00 22.31 ? 469 GLU A O 1 ATOM 3606 C CB . GLU A 1 469 ? 27.342 41.901 6.848 1.00 22.84 ? 469 GLU A CB 1 ATOM 3607 C CG . GLU A 1 469 ? 27.098 42.750 5.640 1.00 27.19 ? 469 GLU A CG 1 ATOM 3608 C CD . GLU A 1 469 ? 26.280 42.013 4.572 1.00 27.88 ? 469 GLU A CD 1 ATOM 3609 O OE1 . GLU A 1 469 ? 25.849 42.674 3.597 1.00 35.40 ? 469 GLU A OE1 1 ATOM 3610 O OE2 . GLU A 1 469 ? 26.069 40.778 4.708 1.00 35.17 ? 469 GLU A OE2 1 ATOM 3611 N N . PRO A 1 470 ? 27.689 41.498 10.126 1.00 22.08 ? 470 PRO A N 1 ATOM 3612 C CA . PRO A 1 470 ? 26.712 42.515 10.525 1.00 21.78 ? 470 PRO A CA 1 ATOM 3613 C C . PRO A 1 470 ? 27.315 43.729 11.247 1.00 21.77 ? 470 PRO A C 1 ATOM 3614 O O . PRO A 1 470 ? 26.594 44.445 11.932 1.00 22.01 ? 470 PRO A O 1 ATOM 3615 C CB . PRO A 1 470 ? 25.806 41.742 11.484 1.00 22.05 ? 470 PRO A CB 1 ATOM 3616 C CG . PRO A 1 470 ? 26.737 40.778 12.159 1.00 21.61 ? 470 PRO A CG 1 ATOM 3617 C CD . PRO A 1 470 ? 27.748 40.384 11.098 1.00 21.62 ? 470 PRO A CD 1 ATOM 3618 N N . TYR A 1 471 ? 28.615 43.958 11.090 1.00 20.93 ? 471 TYR A N 1 ATOM 3619 C CA . TYR A 1 471 ? 29.304 45.011 11.841 1.00 21.39 ? 471 TYR A CA 1 ATOM 3620 C C . TYR A 1 471 ? 29.828 46.127 10.943 1.00 22.06 ? 471 TYR A C 1 ATOM 3621 O O . TYR A 1 471 ? 30.927 46.642 11.158 1.00 22.08 ? 471 TYR A O 1 ATOM 3622 C CB . TYR A 1 471 ? 30.435 44.408 12.687 1.00 20.22 ? 471 TYR A CB 1 ATOM 3623 C CG . TYR A 1 471 ? 29.965 43.248 13.531 1.00 19.50 ? 471 TYR A CG 1 ATOM 3624 C CD1 . TYR A 1 471 ? 30.383 41.952 13.260 1.00 18.31 ? 471 TYR A CD1 1 ATOM 3625 C CD2 . TYR A 1 471 ? 29.059 43.446 14.574 1.00 18.96 ? 471 TYR A CD2 1 ATOM 3626 C CE1 . TYR A 1 471 ? 29.941 40.880 14.035 1.00 18.75 ? 471 TYR A CE1 1 ATOM 3627 C CE2 . TYR A 1 471 ? 28.606 42.382 15.350 1.00 18.62 ? 471 TYR A CE2 1 ATOM 3628 C CZ . TYR A 1 471 ? 29.045 41.113 15.072 1.00 17.86 ? 471 TYR A CZ 1 ATOM 3629 O OH . TYR A 1 471 ? 28.582 40.073 15.826 1.00 18.21 ? 471 TYR A OH 1 ATOM 3630 N N . THR A 1 472 ? 29.047 46.511 9.939 1.00 23.45 ? 472 THR A N 1 ATOM 3631 C CA . THR A 1 472 ? 29.495 47.601 9.061 1.00 25.06 ? 472 THR A CA 1 ATOM 3632 C C . THR A 1 472 ? 29.594 48.918 9.839 1.00 26.11 ? 472 THR A C 1 ATOM 3633 O O . THR A 1 472 ? 30.365 49.802 9.466 1.00 26.63 ? 472 THR A O 1 ATOM 3634 C CB . THR A 1 472 ? 28.598 47.779 7.810 1.00 25.06 ? 472 THR A CB 1 ATOM 3635 O OG1 . THR A 1 472 ? 27.258 48.019 8.226 1.00 25.99 ? 472 THR A OG1 1 ATOM 3636 C CG2 . THR A 1 472 ? 28.620 46.542 6.950 1.00 24.37 ? 472 THR A CG2 1 ATOM 3637 N N . ALA A 1 473 ? 28.834 49.029 10.928 1.00 27.22 ? 473 ALA A N 1 ATOM 3638 C CA . ALA A 1 473 ? 28.923 50.179 11.841 1.00 28.58 ? 473 ALA A CA 1 ATOM 3639 C C . ALA A 1 473 ? 29.877 49.862 12.990 1.00 29.34 ? 473 ALA A C 1 ATOM 3640 O O . ALA A 1 473 ? 29.575 50.101 14.167 1.00 29.91 ? 473 ALA A O 1 ATOM 3641 C CB . ALA A 1 473 ? 27.536 50.552 12.371 1.00 28.66 ? 473 ALA A CB 1 ATOM 3642 N N . CYS A 1 474 ? 31.035 49.317 12.631 1.00 29.86 ? 474 CYS A N 1 ATOM 3643 C CA . CYS A 1 474 ? 32.065 48.880 13.577 1.00 30.39 ? 474 CYS A CA 1 ATOM 3644 C C . CYS A 1 474 ? 32.615 50.053 14.393 1.00 30.48 ? 474 CYS A C 1 ATOM 3645 O O . CYS A 1 474 ? 33.123 49.866 15.493 1.00 30.43 ? 474 CYS A O 1 ATOM 3646 C CB . CYS A 1 474 ? 33.220 48.241 12.800 1.00 29.96 ? 474 CYS A CB 1 ATOM 3647 S SG . CYS A 1 474 ? 33.945 49.393 11.575 1.00 30.92 ? 474 CYS A SG 1 ATOM 3648 N N . ASP A 1 475 ? 32.534 51.257 13.833 1.00 31.01 ? 475 ASP A N 1 ATOM 3649 C CA . ASP A 1 475 ? 33.077 52.462 14.479 1.00 31.49 ? 475 ASP A CA 1 ATOM 3650 C C . ASP A 1 475 ? 34.592 52.430 14.637 1.00 30.53 ? 475 ASP A C 1 ATOM 3651 O O . ASP A 1 475 ? 35.144 53.052 15.539 1.00 31.17 ? 475 ASP A O 1 ATOM 3652 C CB . ASP A 1 475 ? 32.409 52.717 15.833 1.00 32.48 ? 475 ASP A CB 1 ATOM 3653 C CG . ASP A 1 475 ? 31.250 53.672 15.726 1.00 36.40 ? 475 ASP A CG 1 ATOM 3654 O OD1 . ASP A 1 475 ? 30.133 53.315 16.178 1.00 40.80 ? 475 ASP A OD1 1 ATOM 3655 O OD2 . ASP A 1 475 ? 31.462 54.784 15.176 1.00 42.53 ? 475 ASP A OD2 1 ATOM 3656 N N . LEU A 1 476 ? 35.261 51.701 13.757 1.00 28.96 ? 476 LEU A N 1 ATOM 3657 C CA . LEU A 1 476 ? 36.714 51.660 13.757 1.00 27.71 ? 476 LEU A CA 1 ATOM 3658 C C . LEU A 1 476 ? 37.226 52.632 12.706 1.00 27.45 ? 476 LEU A C 1 ATOM 3659 O O . LEU A 1 476 ? 36.546 52.891 11.718 1.00 27.45 ? 476 LEU A O 1 ATOM 3660 C CB . LEU A 1 476 ? 37.202 50.239 13.450 1.00 26.96 ? 476 LEU A CB 1 ATOM 3661 C CG . LEU A 1 476 ? 36.667 49.140 14.376 1.00 25.55 ? 476 LEU A CG 1 ATOM 3662 C CD1 . LEU A 1 476 ? 37.035 47.761 13.835 1.00 23.77 ? 476 LEU A CD1 1 ATOM 3663 C CD2 . LEU A 1 476 ? 37.199 49.338 15.780 1.00 24.57 ? 476 LEU A CD2 1 ATOM 3664 N N . ALA A 1 477 ? 38.420 53.165 12.929 1.00 27.28 ? 477 ALA A N 1 ATOM 3665 C CA . ALA A 1 477 ? 39.104 53.989 11.941 1.00 27.42 ? 477 ALA A CA 1 ATOM 3666 C C . ALA A 1 477 ? 39.580 53.091 10.795 1.00 28.06 ? 477 ALA A C 1 ATOM 3667 O O . ALA A 1 477 ? 39.666 51.863 10.970 1.00 27.33 ? 477 ALA A O 1 ATOM 3668 C CB . ALA A 1 477 ? 40.283 54.709 12.587 1.00 27.13 ? 477 ALA A CB 1 ATOM 3669 N N . PRO A 1 478 ? 39.890 53.684 9.619 1.00 28.64 ? 478 PRO A N 1 ATOM 3670 C CA . PRO A 1 478 ? 40.373 52.865 8.500 1.00 29.01 ? 478 PRO A CA 1 ATOM 3671 C C . PRO A 1 478 ? 41.623 52.093 8.885 1.00 29.60 ? 478 PRO A C 1 ATOM 3672 O O . PRO A 1 478 ? 42.342 52.512 9.805 1.00 29.61 ? 478 PRO A O 1 ATOM 3673 C CB . PRO A 1 478 ? 40.731 53.903 7.434 1.00 29.34 ? 478 PRO A CB 1 ATOM 3674 C CG . PRO A 1 478 ? 39.894 55.084 7.764 1.00 28.97 ? 478 PRO A CG 1 ATOM 3675 C CD . PRO A 1 478 ? 39.818 55.115 9.253 1.00 29.01 ? 478 PRO A CD 1 ATOM 3676 N N . PRO A 1 479 ? 41.887 50.961 8.200 1.00 29.91 ? 479 PRO A N 1 ATOM 3677 C CA . PRO A 1 479 ? 43.085 50.205 8.515 1.00 29.96 ? 479 PRO A CA 1 ATOM 3678 C C . PRO A 1 479 ? 44.316 51.088 8.482 1.00 30.71 ? 479 PRO A C 1 ATOM 3679 O O . PRO A 1 479 ? 44.431 51.985 7.625 1.00 29.78 ? 479 PRO A O 1 ATOM 3680 C CB . PRO A 1 479 ? 43.141 49.166 7.396 1.00 29.91 ? 479 PRO A CB 1 ATOM 3681 C CG . PRO A 1 479 ? 41.710 48.935 7.066 1.00 29.18 ? 479 PRO A CG 1 ATOM 3682 C CD . PRO A 1 479 ? 41.098 50.307 7.140 1.00 29.91 ? 479 PRO A CD 1 ATOM 3683 N N . ALA A 1 480 ? 45.202 50.848 9.442 1.00 31.22 ? 480 ALA A N 1 ATOM 3684 C CA . ALA A 1 480 ? 46.499 51.492 9.482 1.00 32.97 ? 480 ALA A CA 1 ATOM 3685 C C . ALA A 1 480 ? 47.267 51.200 8.198 1.00 34.30 ? 480 ALA A C 1 ATOM 3686 O O . ALA A 1 480 ? 47.132 50.122 7.599 1.00 33.93 ? 480 ALA A O 1 ATOM 3687 C CB . ALA A 1 480 ? 47.290 51.013 10.690 1.00 32.57 ? 480 ALA A CB 1 ATOM 3688 N N . GLY A 1 481 ? 48.057 52.177 7.762 1.00 35.73 ? 481 GLY A N 1 ATOM 3689 C CA . GLY A 1 481 ? 49.054 51.930 6.734 1.00 37.83 ? 481 GLY A CA 1 ATOM 3690 C C . GLY A 1 481 ? 50.084 50.930 7.257 1.00 39.11 ? 481 GLY A C 1 ATOM 3691 O O . GLY A 1 481 ? 50.282 50.757 8.476 1.00 39.85 ? 481 GLY A O 1 HETATM 3692 N N A PHE B 2 . ? 36.962 13.737 10.972 0.80 43.10 ? 912 PHE A N 1 HETATM 3693 C CA A PHE B 2 . ? 37.298 12.386 10.453 0.80 44.36 ? 912 PHE A CA 1 HETATM 3694 C C A PHE B 2 . ? 37.618 12.435 8.973 0.80 44.39 ? 912 PHE A C 1 HETATM 3695 O O A PHE B 2 . ? 38.744 12.126 8.586 0.80 44.46 ? 912 PHE A O 1 HETATM 3696 C CB A PHE B 2 . ? 36.255 11.285 10.794 0.80 44.42 ? 912 PHE A CB 1 HETATM 3697 C CG A PHE B 2 . ? 34.932 11.780 11.346 0.80 44.69 ? 912 PHE A CG 1 HETATM 3698 C CD1 A PHE B 2 . ? 34.781 13.050 11.874 0.80 44.87 ? 912 PHE A CD1 1 HETATM 3699 C CD2 A PHE B 2 . ? 33.841 10.917 11.393 0.80 45.88 ? 912 PHE A CD2 1 HETATM 3700 C CE1 A PHE B 2 . ? 33.571 13.470 12.390 0.80 44.79 ? 912 PHE A CE1 1 HETATM 3701 C CE2 A PHE B 2 . ? 32.621 11.333 11.913 0.80 46.10 ? 912 PHE A CE2 1 HETATM 3702 C CZ A PHE B 2 . ? 32.490 12.613 12.410 0.80 45.47 ? 912 PHE A CZ 1 HETATM 3703 O OXT A PHE B 2 . ? 36.786 12.812 8.152 0.80 44.50 ? 912 PHE A OXT 1 HETATM 3704 N N B PHE C 2 . ? 57.087 29.710 0.047 0.80 48.90 ? 923 PHE A N 1 HETATM 3705 C CA B PHE C 2 . ? 57.169 28.839 -1.162 0.80 49.07 ? 923 PHE A CA 1 HETATM 3706 C C B PHE C 2 . ? 58.465 28.003 -1.230 0.80 49.24 ? 923 PHE A C 1 HETATM 3707 O O B PHE C 2 . ? 58.796 27.398 -2.255 0.80 49.17 ? 923 PHE A O 1 HETATM 3708 C CB B PHE C 2 . ? 56.962 29.657 -2.439 0.80 48.68 ? 923 PHE A CB 1 HETATM 3709 C CG B PHE C 2 . ? 56.088 28.987 -3.447 0.80 48.33 ? 923 PHE A CG 1 HETATM 3710 C CD1 B PHE C 2 . ? 54.937 29.612 -3.902 0.80 46.95 ? 923 PHE A CD1 1 HETATM 3711 C CD2 B PHE C 2 . ? 56.399 27.718 -3.931 0.80 48.32 ? 923 PHE A CD2 1 HETATM 3712 C CE1 B PHE C 2 . ? 54.124 28.996 -4.833 0.80 46.52 ? 923 PHE A CE1 1 HETATM 3713 C CE2 B PHE C 2 . ? 55.582 27.096 -4.847 0.80 47.69 ? 923 PHE A CE2 1 HETATM 3714 C CZ B PHE C 2 . ? 54.442 27.737 -5.298 0.80 46.90 ? 923 PHE A CZ 1 HETATM 3715 O OXT B PHE C 2 . ? 59.202 27.873 -0.245 0.80 49.26 ? 923 PHE A OXT 1 HETATM 3716 C C1 . NAG D 3 . ? 12.172 15.463 4.305 1.00 32.00 ? 801 NAG A C1 1 HETATM 3717 C C2 . NAG D 3 . ? 10.859 15.943 4.950 1.00 33.64 ? 801 NAG A C2 1 HETATM 3718 C C3 . NAG D 3 . ? 10.158 14.838 5.754 1.00 36.38 ? 801 NAG A C3 1 HETATM 3719 C C4 . NAG D 3 . ? 10.129 13.502 4.994 1.00 39.10 ? 801 NAG A C4 1 HETATM 3720 C C5 . NAG D 3 . ? 11.445 13.194 4.277 1.00 39.09 ? 801 NAG A C5 1 HETATM 3721 C C6 . NAG D 3 . ? 11.222 12.074 3.276 1.00 40.40 ? 801 NAG A C6 1 HETATM 3722 C C7 . NAG D 3 . ? 10.676 18.343 5.341 1.00 30.04 ? 801 NAG A C7 1 HETATM 3723 C C8 . NAG D 3 . ? 11.160 19.532 6.124 1.00 27.42 ? 801 NAG A C8 1 HETATM 3724 N N2 . NAG D 3 . ? 11.058 17.131 5.769 1.00 30.32 ? 801 NAG A N2 1 HETATM 3725 O O3 . NAG D 3 . ? 8.831 15.243 6.068 1.00 35.26 ? 801 NAG A O3 1 HETATM 3726 O O4 . NAG D 3 . ? 9.879 12.435 5.886 1.00 43.34 ? 801 NAG A O4 1 HETATM 3727 O O5 . NAG D 3 . ? 11.915 14.299 3.545 1.00 34.78 ? 801 NAG A O5 1 HETATM 3728 O O6 . NAG D 3 . ? 11.967 10.965 3.721 1.00 45.22 ? 801 NAG A O6 1 HETATM 3729 O O7 . NAG D 3 . ? 9.974 18.527 4.345 1.00 27.76 ? 801 NAG A O7 1 HETATM 3730 C C1 . NAG E 3 . ? 8.588 11.854 5.622 1.00 45.90 ? 802 NAG A C1 1 HETATM 3731 C C2 . NAG E 3 . ? 8.692 10.360 5.964 1.00 48.24 ? 802 NAG A C2 1 HETATM 3732 C C3 . NAG E 3 . ? 7.332 9.664 6.013 1.00 48.02 ? 802 NAG A C3 1 HETATM 3733 C C4 . NAG E 3 . ? 6.357 10.479 6.853 1.00 47.15 ? 802 NAG A C4 1 HETATM 3734 C C5 . NAG E 3 . ? 6.279 11.916 6.311 1.00 47.00 ? 802 NAG A C5 1 HETATM 3735 C C6 . NAG E 3 . ? 5.317 12.757 7.134 1.00 46.23 ? 802 NAG A C6 1 HETATM 3736 C C7 . NAG E 3 . ? 10.644 9.014 5.330 1.00 52.68 ? 802 NAG A C7 1 HETATM 3737 C C8 . NAG E 3 . ? 11.018 7.881 4.412 1.00 52.97 ? 802 NAG A C8 1 HETATM 3738 N N2 . NAG E 3 . ? 9.543 9.697 4.990 1.00 50.74 ? 802 NAG A N2 1 HETATM 3739 O O3 . NAG E 3 . ? 7.481 8.366 6.548 1.00 48.69 ? 802 NAG A O3 1 HETATM 3740 O O4 . NAG E 3 . ? 5.093 9.852 6.846 1.00 47.55 ? 802 NAG A O4 1 HETATM 3741 O O5 . NAG E 3 . ? 7.560 12.541 6.321 1.00 45.91 ? 802 NAG A O5 1 HETATM 3742 O O6 . NAG E 3 . ? 5.939 13.165 8.334 1.00 45.51 ? 802 NAG A O6 1 HETATM 3743 O O7 . NAG E 3 . ? 11.347 9.283 6.318 1.00 52.93 ? 802 NAG A O7 1 HETATM 3744 C C1 . NAG F 3 . ? 52.695 20.374 -14.223 1.00 29.68 ? 803 NAG A C1 1 HETATM 3745 C C2 . NAG F 3 . ? 53.516 19.288 -14.916 1.00 33.47 ? 803 NAG A C2 1 HETATM 3746 C C3 . NAG F 3 . ? 53.831 19.621 -16.380 1.00 35.88 ? 803 NAG A C3 1 HETATM 3747 C C4 . NAG F 3 . ? 52.565 20.044 -17.121 1.00 36.81 ? 803 NAG A C4 1 HETATM 3748 C C5 . NAG F 3 . ? 51.856 21.126 -16.310 1.00 34.51 ? 803 NAG A C5 1 HETATM 3749 C C6 . NAG F 3 . ? 50.575 21.614 -16.962 1.00 34.36 ? 803 NAG A C6 1 HETATM 3750 C C7 . NAG F 3 . ? 54.981 17.706 -13.844 1.00 36.15 ? 803 NAG A C7 1 HETATM 3751 C C8 . NAG F 3 . ? 56.254 17.417 -13.097 1.00 36.52 ? 803 NAG A C8 1 HETATM 3752 N N2 . NAG F 3 . ? 54.725 18.973 -14.179 1.00 34.61 ? 803 NAG A N2 1 HETATM 3753 O O3 . NAG F 3 . ? 54.397 18.483 -16.996 1.00 36.76 ? 803 NAG A O3 1 HETATM 3754 O O4 . NAG F 3 . ? 52.896 20.568 -18.383 1.00 42.30 ? 803 NAG A O4 1 HETATM 3755 O O5 . NAG F 3 . ? 51.555 20.610 -15.024 1.00 31.81 ? 803 NAG A O5 1 HETATM 3756 O O6 . NAG F 3 . ? 49.699 20.521 -17.126 1.00 34.83 ? 803 NAG A O6 1 HETATM 3757 O O7 . NAG F 3 . ? 54.219 16.783 -14.131 1.00 38.02 ? 803 NAG A O7 1 HETATM 3758 C C1 . NAG G 3 . ? 52.480 19.686 -19.443 1.00 48.18 ? 804 NAG A C1 1 HETATM 3759 C C2 . NAG G 3 . ? 52.473 20.535 -20.714 1.00 50.62 ? 804 NAG A C2 1 HETATM 3760 C C3 . NAG G 3 . ? 52.363 19.725 -22.000 1.00 51.93 ? 804 NAG A C3 1 HETATM 3761 C C4 . NAG G 3 . ? 53.293 18.513 -21.959 1.00 52.09 ? 804 NAG A C4 1 HETATM 3762 C C5 . NAG G 3 . ? 53.071 17.719 -20.672 1.00 51.39 ? 804 NAG A C5 1 HETATM 3763 C C6 . NAG G 3 . ? 54.017 16.534 -20.585 1.00 51.53 ? 804 NAG A C6 1 HETATM 3764 C C7 . NAG G 3 . ? 51.790 22.805 -20.310 1.00 52.89 ? 804 NAG A C7 1 HETATM 3765 C C8 . NAG G 3 . ? 50.697 23.834 -20.249 1.00 53.17 ? 804 NAG A C8 1 HETATM 3766 N N2 . NAG G 3 . ? 51.439 21.560 -20.638 1.00 51.79 ? 804 NAG A N2 1 HETATM 3767 O O3 . NAG G 3 . ? 52.754 20.567 -23.054 1.00 53.64 ? 804 NAG A O3 1 HETATM 3768 O O4 . NAG G 3 . ? 53.112 17.686 -23.094 1.00 53.39 ? 804 NAG A O4 1 HETATM 3769 O O5 . NAG G 3 . ? 53.336 18.561 -19.565 1.00 50.20 ? 804 NAG A O5 1 HETATM 3770 O O6 . NAG G 3 . ? 55.329 17.038 -20.447 1.00 52.24 ? 804 NAG A O6 1 HETATM 3771 O O7 . NAG G 3 . ? 52.961 23.115 -20.058 1.00 53.38 ? 804 NAG A O7 1 HETATM 3772 ZN ZN . ZN H 4 . ? 38.502 14.425 12.322 1.00 13.82 ? 901 ZN A ZN 1 HETATM 3773 ZN ZN . ZN I 4 . ? 38.200 18.452 12.426 1.00 13.75 ? 902 ZN A ZN 1 HETATM 3774 MG MG . MG J 5 . ? 39.412 19.893 8.145 1.00 10.76 ? 903 MG A MG 1 HETATM 3775 CA CA . CA K 6 . ? 50.161 15.817 -6.457 1.00 15.99 ? 904 CA A CA 1 HETATM 3776 C C . ACT L 7 . ? 61.322 1.865 29.959 1.00 49.63 ? 933 ACT A C 1 HETATM 3777 O O . ACT L 7 . ? 60.375 1.281 29.384 1.00 49.00 ? 933 ACT A O 1 HETATM 3778 O OXT . ACT L 7 . ? 61.863 2.800 29.323 1.00 49.73 ? 933 ACT A OXT 1 HETATM 3779 C CH3 . ACT L 7 . ? 61.788 1.467 31.332 1.00 49.46 ? 933 ACT A CH3 1 HETATM 3780 C C . ACT M 7 . ? 58.959 16.220 2.107 1.00 53.47 ? 934 ACT A C 1 HETATM 3781 O O . ACT M 7 . ? 58.841 16.529 0.898 1.00 53.39 ? 934 ACT A O 1 HETATM 3782 O OXT . ACT M 7 . ? 58.700 15.034 2.412 1.00 53.57 ? 934 ACT A OXT 1 HETATM 3783 C CH3 . ACT M 7 . ? 59.394 17.213 3.140 1.00 53.34 ? 934 ACT A CH3 1 HETATM 3784 C C . ACT N 7 . ? 40.828 21.274 -17.447 1.00 49.99 ? 935 ACT A C 1 HETATM 3785 O O . ACT N 7 . ? 40.133 20.244 -17.591 1.00 49.70 ? 935 ACT A O 1 HETATM 3786 O OXT . ACT N 7 . ? 40.210 22.360 -17.489 1.00 49.93 ? 935 ACT A OXT 1 HETATM 3787 C CH3 . ACT N 7 . ? 42.316 21.212 -17.255 1.00 49.82 ? 935 ACT A CH3 1 HETATM 3788 C C1 . GOL O 8 . ? 46.523 9.946 -4.479 1.00 35.09 ? 936 GOL A C1 1 HETATM 3789 O O1 . GOL O 8 . ? 46.851 10.709 -3.335 1.00 32.03 ? 936 GOL A O1 1 HETATM 3790 C C2 . GOL O 8 . ? 46.863 8.476 -4.294 1.00 37.02 ? 936 GOL A C2 1 HETATM 3791 O O2 . GOL O 8 . ? 47.872 8.326 -3.328 1.00 37.29 ? 936 GOL A O2 1 HETATM 3792 C C3 . GOL O 8 . ? 47.290 7.853 -5.623 1.00 36.94 ? 936 GOL A C3 1 HETATM 3793 O O3 . GOL O 8 . ? 48.366 6.961 -5.420 1.00 38.18 ? 936 GOL A O3 1 HETATM 3794 C C1 . GOL P 8 . ? 39.952 5.991 -18.392 1.00 49.36 ? 937 GOL A C1 1 HETATM 3795 O O1 . GOL P 8 . ? 39.969 5.301 -17.158 1.00 49.69 ? 937 GOL A O1 1 HETATM 3796 C C2 . GOL P 8 . ? 41.137 5.593 -19.284 1.00 49.29 ? 937 GOL A C2 1 HETATM 3797 O O2 . GOL P 8 . ? 42.307 5.439 -18.513 1.00 48.98 ? 937 GOL A O2 1 HETATM 3798 C C3 . GOL P 8 . ? 41.431 6.659 -20.338 1.00 48.96 ? 937 GOL A C3 1 HETATM 3799 O O3 . GOL P 8 . ? 40.288 6.963 -21.112 1.00 47.21 ? 937 GOL A O3 1 HETATM 3800 O O . HOH Q 9 . ? 39.522 15.838 8.781 1.00 12.43 ? 1001 HOH A O 1 HETATM 3801 O O . HOH Q 9 . ? 32.991 18.018 3.189 1.00 14.12 ? 1002 HOH A O 1 HETATM 3802 O O . HOH Q 9 . ? 40.663 18.173 8.024 1.00 11.21 ? 1003 HOH A O 1 HETATM 3803 O O . HOH Q 9 . ? 32.465 19.835 24.403 1.00 15.01 ? 1004 HOH A O 1 HETATM 3804 O O . HOH Q 9 . ? 43.173 17.722 -13.628 1.00 23.89 ? 1005 HOH A O 1 HETATM 3805 O O . HOH Q 9 . ? 28.975 24.262 15.768 1.00 15.80 ? 1006 HOH A O 1 HETATM 3806 O O . HOH Q 9 . ? 46.091 -0.798 25.221 1.00 15.48 ? 1007 HOH A O 1 HETATM 3807 O O . HOH Q 9 . ? 56.107 23.619 26.300 1.00 16.53 ? 1008 HOH A O 1 HETATM 3808 O O . HOH Q 9 . ? 65.744 27.317 38.486 1.00 13.42 ? 1009 HOH A O 1 HETATM 3809 O O . HOH Q 9 . ? 31.031 24.524 17.478 1.00 13.29 ? 1010 HOH A O 1 HETATM 3810 O O . HOH Q 9 . ? 49.789 0.173 18.935 1.00 15.33 ? 1011 HOH A O 1 HETATM 3811 O O . HOH Q 9 . ? 52.175 2.229 25.153 1.00 15.58 ? 1012 HOH A O 1 HETATM 3812 O O . HOH Q 9 . ? 22.052 20.594 1.852 1.00 14.07 ? 1013 HOH A O 1 HETATM 3813 O O . HOH Q 9 . ? 35.063 22.724 24.086 1.00 11.98 ? 1014 HOH A O 1 HETATM 3814 O O . HOH Q 9 . ? 26.220 23.617 9.848 1.00 14.48 ? 1015 HOH A O 1 HETATM 3815 O O . HOH Q 9 . ? 28.818 31.147 3.046 1.00 16.13 ? 1016 HOH A O 1 HETATM 3816 O O . HOH Q 9 . ? 37.206 20.078 21.073 1.00 10.46 ? 1017 HOH A O 1 HETATM 3817 O O . HOH Q 9 . ? 44.992 17.721 21.087 1.00 12.33 ? 1018 HOH A O 1 HETATM 3818 O O . HOH Q 9 . ? 47.425 -1.917 23.104 1.00 15.74 ? 1019 HOH A O 1 HETATM 3819 O O . HOH Q 9 . ? 22.984 22.129 11.163 1.00 13.84 ? 1020 HOH A O 1 HETATM 3820 O O . HOH Q 9 . ? 62.465 10.235 29.253 1.00 20.94 ? 1021 HOH A O 1 HETATM 3821 O O . HOH Q 9 . ? 23.763 15.911 13.031 1.00 13.33 ? 1022 HOH A O 1 HETATM 3822 O O . HOH Q 9 . ? 57.079 7.629 33.532 1.00 22.04 ? 1023 HOH A O 1 HETATM 3823 O O . HOH Q 9 . ? 51.350 17.050 0.461 1.00 15.45 ? 1024 HOH A O 1 HETATM 3824 O O . HOH Q 9 . ? 59.219 34.751 -1.762 1.00 16.97 ? 1025 HOH A O 1 HETATM 3825 O O . HOH Q 9 . ? 55.599 8.524 22.762 1.00 13.43 ? 1026 HOH A O 1 HETATM 3826 O O . HOH Q 9 . ? 52.413 20.378 3.649 1.00 20.20 ? 1027 HOH A O 1 HETATM 3827 O O . HOH Q 9 . ? 32.351 22.512 24.335 1.00 14.79 ? 1028 HOH A O 1 HETATM 3828 O O . HOH Q 9 . ? 45.068 4.261 19.296 1.00 15.21 ? 1029 HOH A O 1 HETATM 3829 O O . HOH Q 9 . ? 52.896 14.625 -3.176 1.00 28.32 ? 1030 HOH A O 1 HETATM 3830 O O . HOH Q 9 . ? 42.194 21.249 23.230 1.00 10.63 ? 1031 HOH A O 1 HETATM 3831 O O . HOH Q 9 . ? 49.614 21.063 7.938 1.00 16.68 ? 1032 HOH A O 1 HETATM 3832 O O . HOH Q 9 . ? 49.625 43.459 5.341 1.00 20.71 ? 1033 HOH A O 1 HETATM 3833 O O . HOH Q 9 . ? 39.271 20.041 6.089 1.00 13.12 ? 1034 HOH A O 1 HETATM 3834 O O . HOH Q 9 . ? 53.367 7.950 15.595 1.00 16.07 ? 1035 HOH A O 1 HETATM 3835 O O . HOH Q 9 . ? 21.347 16.746 12.295 1.00 14.97 ? 1036 HOH A O 1 HETATM 3836 O O . HOH Q 9 . ? 39.795 15.712 25.926 1.00 13.61 ? 1037 HOH A O 1 HETATM 3837 O O . HOH Q 9 . ? 34.349 16.133 4.716 1.00 13.59 ? 1038 HOH A O 1 HETATM 3838 O O . HOH Q 9 . ? 51.843 3.242 22.536 1.00 12.57 ? 1039 HOH A O 1 HETATM 3839 O O . HOH Q 9 . ? 47.826 19.091 7.224 1.00 12.16 ? 1040 HOH A O 1 HETATM 3840 O O . HOH Q 9 . ? 36.578 22.165 10.629 1.00 11.70 ? 1041 HOH A O 1 HETATM 3841 O O . HOH Q 9 . ? 38.384 46.101 6.029 1.00 26.79 ? 1042 HOH A O 1 HETATM 3842 O O . HOH Q 9 . ? 49.900 9.730 27.456 1.00 12.79 ? 1043 HOH A O 1 HETATM 3843 O O . HOH Q 9 . ? 42.334 36.305 27.124 1.00 11.53 ? 1044 HOH A O 1 HETATM 3844 O O . HOH Q 9 . ? 60.229 32.845 33.713 1.00 15.33 ? 1045 HOH A O 1 HETATM 3845 O O . HOH Q 9 . ? 24.310 19.897 -0.534 1.00 16.66 ? 1046 HOH A O 1 HETATM 3846 O O . HOH Q 9 . ? 29.516 28.733 4.097 1.00 14.26 ? 1047 HOH A O 1 HETATM 3847 O O . HOH Q 9 . ? 37.868 27.164 17.841 1.00 12.60 ? 1048 HOH A O 1 HETATM 3848 O O . HOH Q 9 . ? 51.150 19.827 6.070 1.00 18.08 ? 1049 HOH A O 1 HETATM 3849 O O . HOH Q 9 . ? 56.060 28.980 23.750 1.00 20.63 ? 1050 HOH A O 1 HETATM 3850 O O . HOH Q 9 . ? 36.165 8.047 24.238 1.00 13.28 ? 1051 HOH A O 1 HETATM 3851 O O . HOH Q 9 . ? 23.533 10.723 1.674 1.00 21.25 ? 1052 HOH A O 1 HETATM 3852 O O . HOH Q 9 . ? 37.751 18.669 7.750 1.00 12.62 ? 1053 HOH A O 1 HETATM 3853 O O . HOH Q 9 . ? 44.718 42.509 -0.609 1.00 19.04 ? 1054 HOH A O 1 HETATM 3854 O O . HOH Q 9 . ? 63.373 27.699 29.186 1.00 19.49 ? 1055 HOH A O 1 HETATM 3855 O O . HOH Q 9 . ? 51.111 19.764 1.339 1.00 28.93 ? 1056 HOH A O 1 HETATM 3856 O O . HOH Q 9 . ? 44.640 48.565 11.222 1.00 23.36 ? 1057 HOH A O 1 HETATM 3857 O O . HOH Q 9 . ? 53.952 34.358 15.175 1.00 18.06 ? 1058 HOH A O 1 HETATM 3858 O O . HOH Q 9 . ? 55.171 7.089 20.266 1.00 14.09 ? 1059 HOH A O 1 HETATM 3859 O O . HOH Q 9 . ? 35.395 10.451 -1.959 1.00 20.10 ? 1060 HOH A O 1 HETATM 3860 O O . HOH Q 9 . ? 57.255 34.231 32.712 1.00 15.69 ? 1061 HOH A O 1 HETATM 3861 O O . HOH Q 9 . ? 31.688 29.078 -4.006 1.00 14.32 ? 1062 HOH A O 1 HETATM 3862 O O . HOH Q 9 . ? 19.238 13.526 10.201 1.00 28.34 ? 1063 HOH A O 1 HETATM 3863 O O . HOH Q 9 . ? 22.916 22.287 -0.181 1.00 17.72 ? 1064 HOH A O 1 HETATM 3864 O O . HOH Q 9 . ? 57.871 29.329 8.116 1.00 20.34 ? 1065 HOH A O 1 HETATM 3865 O O . HOH Q 9 . ? 50.969 34.734 11.141 1.00 20.06 ? 1066 HOH A O 1 HETATM 3866 O O . HOH Q 9 . ? 56.107 7.604 15.997 1.00 15.24 ? 1067 HOH A O 1 HETATM 3867 O O . HOH Q 9 . ? 13.877 26.560 6.648 1.00 25.75 ? 1068 HOH A O 1 HETATM 3868 O O . HOH Q 9 . ? 44.355 26.912 -16.702 1.00 22.45 ? 1069 HOH A O 1 HETATM 3869 O O . HOH Q 9 . ? 49.617 -1.111 16.574 1.00 23.74 ? 1070 HOH A O 1 HETATM 3870 O O . HOH Q 9 . ? 40.245 13.348 -13.191 1.00 22.36 ? 1071 HOH A O 1 HETATM 3871 O O . HOH Q 9 . ? 24.032 34.445 7.280 1.00 31.65 ? 1072 HOH A O 1 HETATM 3872 O O . HOH Q 9 . ? 50.385 15.993 -1.885 1.00 19.97 ? 1073 HOH A O 1 HETATM 3873 O O . HOH Q 9 . ? 49.017 46.016 28.144 1.00 26.86 ? 1074 HOH A O 1 HETATM 3874 O O . HOH Q 9 . ? 25.930 39.511 15.663 1.00 19.69 ? 1075 HOH A O 1 HETATM 3875 O O . HOH Q 9 . ? 49.538 22.079 -13.387 1.00 23.71 ? 1076 HOH A O 1 HETATM 3876 O O . HOH Q 9 . ? 44.560 -6.787 18.836 1.00 30.24 ? 1077 HOH A O 1 HETATM 3877 O O . HOH Q 9 . ? 51.519 9.481 38.567 1.00 21.43 ? 1078 HOH A O 1 HETATM 3878 O O . HOH Q 9 . ? 52.994 39.765 10.872 1.00 21.79 ? 1079 HOH A O 1 HETATM 3879 O O . HOH Q 9 . ? 54.057 38.831 27.783 1.00 19.56 ? 1080 HOH A O 1 HETATM 3880 O O . HOH Q 9 . ? 32.441 11.594 -5.188 1.00 17.86 ? 1081 HOH A O 1 HETATM 3881 O O . HOH Q 9 . ? 44.209 18.843 25.088 1.00 17.03 ? 1082 HOH A O 1 HETATM 3882 O O . HOH Q 9 . ? 46.385 43.155 1.157 1.00 32.72 ? 1083 HOH A O 1 HETATM 3883 O O . HOH Q 9 . ? 44.949 9.649 25.794 1.00 15.50 ? 1084 HOH A O 1 HETATM 3884 O O . HOH Q 9 . ? 11.899 21.504 1.953 1.00 17.44 ? 1085 HOH A O 1 HETATM 3885 O O . HOH Q 9 . ? 51.396 3.129 -16.334 1.00 29.53 ? 1086 HOH A O 1 HETATM 3886 O O . HOH Q 9 . ? 42.118 -3.490 27.491 1.00 20.27 ? 1087 HOH A O 1 HETATM 3887 O O . HOH Q 9 . ? 48.330 39.385 11.615 1.00 15.01 ? 1088 HOH A O 1 HETATM 3888 O O . HOH Q 9 . ? 49.457 36.418 9.514 1.00 18.24 ? 1089 HOH A O 1 HETATM 3889 O O . HOH Q 9 . ? 41.725 11.277 0.041 1.00 23.65 ? 1090 HOH A O 1 HETATM 3890 O O . HOH Q 9 . ? 61.617 9.071 18.821 1.00 22.13 ? 1091 HOH A O 1 HETATM 3891 O O . HOH Q 9 . ? 36.523 40.741 -4.926 1.00 31.45 ? 1092 HOH A O 1 HETATM 3892 O O . HOH Q 9 . ? 34.560 32.678 7.071 1.00 21.08 ? 1093 HOH A O 1 HETATM 3893 O O . HOH Q 9 . ? 34.412 30.009 -6.872 1.00 17.05 ? 1094 HOH A O 1 HETATM 3894 O O . HOH Q 9 . ? 51.925 -0.784 20.349 1.00 22.03 ? 1095 HOH A O 1 HETATM 3895 O O . HOH Q 9 . ? 47.751 9.647 3.383 1.00 33.26 ? 1096 HOH A O 1 HETATM 3896 O O . HOH Q 9 . ? 60.871 9.379 27.080 1.00 24.63 ? 1097 HOH A O 1 HETATM 3897 O O . HOH Q 9 . ? 56.133 35.276 11.230 1.00 19.58 ? 1098 HOH A O 1 HETATM 3898 O O . HOH Q 9 . ? 18.181 14.210 1.790 1.00 21.46 ? 1099 HOH A O 1 HETATM 3899 O O . HOH Q 9 . ? 64.439 41.125 31.830 1.00 36.25 ? 1100 HOH A O 1 HETATM 3900 O O . HOH Q 9 . ? 42.822 10.102 6.268 1.00 40.22 ? 1101 HOH A O 1 HETATM 3901 O O . HOH Q 9 . ? 41.041 12.869 -10.575 1.00 18.44 ? 1102 HOH A O 1 HETATM 3902 O O . HOH Q 9 . ? 51.916 34.663 23.370 1.00 14.45 ? 1103 HOH A O 1 HETATM 3903 O O . HOH Q 9 . ? 56.357 20.337 -12.586 1.00 95.64 ? 1104 HOH A O 1 HETATM 3904 O O . HOH Q 9 . ? 57.913 2.466 29.547 1.00 15.15 ? 1105 HOH A O 1 HETATM 3905 O O . HOH Q 9 . ? 60.493 36.042 0.395 1.00 27.78 ? 1106 HOH A O 1 HETATM 3906 O O . HOH Q 9 . ? 53.444 14.613 7.895 1.00 19.11 ? 1107 HOH A O 1 HETATM 3907 O O . HOH Q 9 . ? 59.080 44.484 33.351 1.00 46.60 ? 1108 HOH A O 1 HETATM 3908 O O . HOH Q 9 . ? 61.322 13.433 18.341 1.00 25.59 ? 1109 HOH A O 1 HETATM 3909 O O . HOH Q 9 . ? 60.310 15.085 20.196 1.00 20.88 ? 1110 HOH A O 1 HETATM 3910 O O . HOH Q 9 . ? 47.203 45.983 14.822 1.00 32.95 ? 1111 HOH A O 1 HETATM 3911 O O . HOH Q 9 . ? 48.576 42.377 17.482 1.00 27.76 ? 1112 HOH A O 1 HETATM 3912 O O . HOH Q 9 . ? 36.003 33.233 9.977 1.00 18.85 ? 1113 HOH A O 1 HETATM 3913 O O . HOH Q 9 . ? 66.263 15.556 33.071 1.00 22.57 ? 1114 HOH A O 1 HETATM 3914 O O . HOH Q 9 . ? 57.613 45.567 35.253 1.00 47.38 ? 1115 HOH A O 1 HETATM 3915 O O . HOH Q 9 . ? 56.564 33.689 29.846 1.00 20.95 ? 1116 HOH A O 1 HETATM 3916 O O . HOH Q 9 . ? 26.809 47.226 12.044 1.00 25.41 ? 1117 HOH A O 1 HETATM 3917 O O . HOH Q 9 . ? 55.380 20.258 -10.258 1.00 23.81 ? 1118 HOH A O 1 HETATM 3918 O O . HOH Q 9 . ? 21.712 14.801 15.846 1.00 30.36 ? 1119 HOH A O 1 HETATM 3919 O O . HOH Q 9 . ? 60.974 35.302 41.264 1.00 25.14 ? 1120 HOH A O 1 HETATM 3920 O O . HOH Q 9 . ? 20.549 14.251 18.040 1.00 32.53 ? 1121 HOH A O 1 HETATM 3921 O O . HOH Q 9 . ? 28.967 31.058 0.191 1.00 22.81 ? 1122 HOH A O 1 HETATM 3922 O O . HOH Q 9 . ? 44.410 10.294 1.489 1.00 34.71 ? 1123 HOH A O 1 HETATM 3923 O O . HOH Q 9 . ? 59.458 11.604 25.985 1.00 21.74 ? 1124 HOH A O 1 HETATM 3924 O O . HOH Q 9 . ? 44.286 24.432 20.652 1.00 16.81 ? 1125 HOH A O 1 HETATM 3925 O O . HOH Q 9 . ? 50.401 39.545 10.033 1.00 22.54 ? 1126 HOH A O 1 HETATM 3926 O O . HOH Q 9 . ? 31.770 8.138 -9.161 1.00 28.63 ? 1127 HOH A O 1 HETATM 3927 O O . HOH Q 9 . ? 26.258 10.188 4.654 1.00 24.81 ? 1128 HOH A O 1 HETATM 3928 O O . HOH Q 9 . ? 17.354 8.872 -3.398 1.00 31.25 ? 1129 HOH A O 1 HETATM 3929 O O . HOH Q 9 . ? 49.017 42.859 2.032 1.00 39.54 ? 1130 HOH A O 1 HETATM 3930 O O . HOH Q 9 . ? 35.598 1.339 14.929 1.00 20.44 ? 1131 HOH A O 1 HETATM 3931 O O . HOH Q 9 . ? 45.745 45.246 24.388 1.00 34.50 ? 1132 HOH A O 1 HETATM 3932 O O . HOH Q 9 . ? 29.871 12.021 -15.851 1.00 26.07 ? 1133 HOH A O 1 HETATM 3933 O O . HOH Q 9 . ? 10.140 19.691 1.408 1.00 29.14 ? 1134 HOH A O 1 HETATM 3934 O O . HOH Q 9 . ? 58.385 18.655 11.277 1.00 45.21 ? 1135 HOH A O 1 HETATM 3935 O O . HOH Q 9 . ? 29.603 36.494 11.905 1.00 25.81 ? 1136 HOH A O 1 HETATM 3936 O O . HOH Q 9 . ? 48.267 -5.623 29.897 1.00 26.10 ? 1137 HOH A O 1 HETATM 3937 O O . HOH Q 9 . ? 41.542 38.330 -7.692 1.00 39.23 ? 1138 HOH A O 1 HETATM 3938 O O . HOH Q 9 . ? 36.818 45.825 2.085 1.00 29.87 ? 1139 HOH A O 1 HETATM 3939 O O . HOH Q 9 . ? 28.617 29.750 26.394 1.00 31.26 ? 1140 HOH A O 1 HETATM 3940 O O . HOH Q 9 . ? 36.061 4.212 14.151 1.00 24.39 ? 1141 HOH A O 1 HETATM 3941 O O . HOH Q 9 . ? 62.204 5.906 28.714 1.00 32.92 ? 1142 HOH A O 1 HETATM 3942 O O . HOH Q 9 . ? 57.721 24.062 2.277 1.00 28.55 ? 1143 HOH A O 1 HETATM 3943 O O . HOH Q 9 . ? 61.113 9.498 15.866 1.00 31.70 ? 1144 HOH A O 1 HETATM 3944 O O . HOH Q 9 . ? 27.272 10.153 0.347 1.00 36.59 ? 1145 HOH A O 1 HETATM 3945 O O . HOH Q 9 . ? 54.355 43.695 23.456 1.00 30.02 ? 1146 HOH A O 1 HETATM 3946 O O . HOH Q 9 . ? 53.877 45.892 13.958 1.00 49.43 ? 1147 HOH A O 1 HETATM 3947 O O . HOH Q 9 . ? 58.163 21.701 -8.295 1.00 27.29 ? 1148 HOH A O 1 HETATM 3948 O O . HOH Q 9 . ? 33.257 35.236 24.560 1.00 37.53 ? 1149 HOH A O 1 HETATM 3949 O O . HOH Q 9 . ? 31.436 10.613 0.693 1.00 15.91 ? 1150 HOH A O 1 HETATM 3950 O O . HOH Q 9 . ? 71.194 31.414 33.663 1.00 27.66 ? 1151 HOH A O 1 HETATM 3951 O O . HOH Q 9 . ? 23.652 13.252 12.818 1.00 29.65 ? 1152 HOH A O 1 HETATM 3952 O O . HOH Q 9 . ? 41.513 15.435 -14.322 1.00 28.81 ? 1153 HOH A O 1 HETATM 3953 O O . HOH Q 9 . ? 56.765 0.825 14.651 1.00 25.78 ? 1154 HOH A O 1 HETATM 3954 O O . HOH Q 9 . ? 15.397 15.399 1.723 1.00 26.66 ? 1155 HOH A O 1 HETATM 3955 O O . HOH Q 9 . ? 26.230 31.289 -0.202 1.00 24.41 ? 1156 HOH A O 1 HETATM 3956 O O . HOH Q 9 . ? 43.214 29.303 -17.919 1.00 49.01 ? 1157 HOH A O 1 HETATM 3957 O O . HOH Q 9 . ? 14.571 27.322 9.045 1.00 27.12 ? 1158 HOH A O 1 HETATM 3958 O O . HOH Q 9 . ? 43.287 0.962 -11.856 1.00 30.51 ? 1159 HOH A O 1 HETATM 3959 O O . HOH Q 9 . ? 52.468 35.809 12.995 1.00 29.49 ? 1160 HOH A O 1 HETATM 3960 O O . HOH Q 9 . ? 54.147 -0.080 36.877 1.00 28.33 ? 1161 HOH A O 1 HETATM 3961 O O . HOH Q 9 . ? 46.680 45.592 -1.206 1.00 31.48 ? 1162 HOH A O 1 HETATM 3962 O O . HOH Q 9 . ? 63.491 0.535 23.635 1.00 36.06 ? 1163 HOH A O 1 HETATM 3963 O O . HOH Q 9 . ? 37.688 48.005 19.511 1.00 29.40 ? 1164 HOH A O 1 HETATM 3964 O O . HOH Q 9 . ? 58.656 21.944 -1.385 1.00 25.16 ? 1165 HOH A O 1 HETATM 3965 O O . HOH Q 9 . ? 46.700 25.291 22.249 1.00 22.47 ? 1166 HOH A O 1 HETATM 3966 O O . HOH Q 9 . ? 53.656 42.547 11.214 1.00 19.89 ? 1167 HOH A O 1 HETATM 3967 O O . HOH Q 9 . ? 32.651 8.906 -5.844 1.00 32.36 ? 1168 HOH A O 1 HETATM 3968 O O . HOH Q 9 . ? 42.469 11.024 3.392 1.00 35.89 ? 1169 HOH A O 1 HETATM 3969 O O . HOH Q 9 . ? 26.916 10.172 18.041 1.00 31.35 ? 1170 HOH A O 1 HETATM 3970 O O . HOH Q 9 . ? 60.038 14.876 -2.312 1.00 73.26 ? 1171 HOH A O 1 HETATM 3971 O O . HOH Q 9 . ? 44.490 12.043 -2.734 1.00 16.15 ? 1172 HOH A O 1 HETATM 3972 O O . HOH Q 9 . ? 59.162 25.442 0.703 1.00 39.92 ? 1173 HOH A O 1 HETATM 3973 O O . HOH Q 9 . ? 31.047 20.983 -17.887 1.00 31.93 ? 1174 HOH A O 1 HETATM 3974 O O . HOH Q 9 . ? 48.190 44.685 3.539 1.00 24.96 ? 1175 HOH A O 1 HETATM 3975 O O . HOH Q 9 . ? 19.802 15.384 13.982 1.00 35.34 ? 1176 HOH A O 1 HETATM 3976 O O . HOH Q 9 . ? 17.800 28.844 10.601 1.00 19.87 ? 1177 HOH A O 1 HETATM 3977 O O . HOH Q 9 . ? 18.017 22.976 -2.273 1.00 36.30 ? 1178 HOH A O 1 HETATM 3978 O O . HOH Q 9 . ? 45.557 44.177 18.779 1.00 30.91 ? 1179 HOH A O 1 HETATM 3979 O O . HOH Q 9 . ? 38.360 47.601 22.442 1.00 50.37 ? 1180 HOH A O 1 HETATM 3980 O O . HOH Q 9 . ? 73.244 22.327 40.341 1.00 40.72 ? 1181 HOH A O 1 HETATM 3981 O O . HOH Q 9 . ? 30.860 10.261 13.879 1.00 87.74 ? 1182 HOH A O 1 HETATM 3982 O O . HOH Q 9 . ? 42.502 40.757 25.447 1.00 31.89 ? 1183 HOH A O 1 HETATM 3983 O O . HOH Q 9 . ? 30.887 36.083 -5.220 1.00 29.94 ? 1184 HOH A O 1 HETATM 3984 O O . HOH Q 9 . ? 59.331 31.292 6.891 1.00 28.49 ? 1185 HOH A O 1 HETATM 3985 O O . HOH Q 9 . ? 38.958 6.722 -13.536 1.00 26.25 ? 1186 HOH A O 1 HETATM 3986 O O . HOH Q 9 . ? 13.475 25.014 13.329 1.00 39.45 ? 1187 HOH A O 1 HETATM 3987 O O . HOH Q 9 . ? 43.697 45.669 18.436 1.00 25.61 ? 1188 HOH A O 1 HETATM 3988 O O . HOH Q 9 . ? 23.883 7.881 -2.720 1.00 90.35 ? 1189 HOH A O 1 HETATM 3989 O O . HOH Q 9 . ? 73.228 22.588 30.129 1.00 60.95 ? 1190 HOH A O 1 HETATM 3990 O O . HOH Q 9 . ? 46.961 48.883 5.298 1.00 32.04 ? 1191 HOH A O 1 HETATM 3991 O O . HOH Q 9 . ? 43.314 38.053 25.113 1.00 22.14 ? 1192 HOH A O 1 HETATM 3992 O O . HOH Q 9 . ? 63.361 29.860 27.864 1.00 57.76 ? 1193 HOH A O 1 HETATM 3993 O O . HOH Q 9 . ? 47.076 7.457 5.728 1.00 28.78 ? 1194 HOH A O 1 HETATM 3994 O O . HOH Q 9 . ? 44.573 3.998 9.755 1.00 42.18 ? 1195 HOH A O 1 HETATM 3995 O O . HOH Q 9 . ? 64.515 32.632 28.374 1.00 36.04 ? 1196 HOH A O 1 HETATM 3996 O O . HOH Q 9 . ? 63.201 8.931 34.607 1.00 38.82 ? 1197 HOH A O 1 HETATM 3997 O O . HOH Q 9 . ? 51.144 0.974 11.354 1.00 34.29 ? 1198 HOH A O 1 HETATM 3998 O O . HOH Q 9 . ? 62.792 8.644 25.211 1.00 32.96 ? 1199 HOH A O 1 HETATM 3999 O O . HOH Q 9 . ? 42.134 14.897 24.963 1.00 25.38 ? 1200 HOH A O 1 HETATM 4000 O O . HOH Q 9 . ? 45.420 52.235 16.711 1.00 38.88 ? 1201 HOH A O 1 HETATM 4001 O O . HOH Q 9 . ? 20.866 26.098 -0.410 1.00 30.75 ? 1202 HOH A O 1 HETATM 4002 O O . HOH Q 9 . ? 57.302 37.555 11.079 1.00 36.57 ? 1203 HOH A O 1 HETATM 4003 O O . HOH Q 9 . ? 35.992 6.701 15.427 1.00 24.85 ? 1204 HOH A O 1 HETATM 4004 O O . HOH Q 9 . ? 67.416 38.273 37.113 1.00 50.03 ? 1205 HOH A O 1 HETATM 4005 O O . HOH Q 9 . ? 48.630 24.367 23.949 1.00 25.53 ? 1206 HOH A O 1 HETATM 4006 O O . HOH Q 9 . ? 71.854 26.123 29.378 1.00 36.59 ? 1207 HOH A O 1 HETATM 4007 O O . HOH Q 9 . ? 49.286 -2.153 43.126 1.00 30.86 ? 1208 HOH A O 1 HETATM 4008 O O . HOH Q 9 . ? 42.812 13.995 -17.734 1.00 46.26 ? 1209 HOH A O 1 HETATM 4009 O O . HOH Q 9 . ? 61.295 6.738 20.016 1.00 26.46 ? 1210 HOH A O 1 HETATM 4010 O O . HOH Q 9 . ? 49.265 17.264 4.222 1.00 26.31 ? 1211 HOH A O 1 HETATM 4011 O O . HOH Q 9 . ? 32.693 9.819 -1.715 1.00 29.43 ? 1212 HOH A O 1 HETATM 4012 O O . HOH Q 9 . ? 48.268 43.165 27.944 1.00 35.16 ? 1213 HOH A O 1 HETATM 4013 O O . HOH Q 9 . ? 43.181 8.358 -12.906 1.00 26.08 ? 1214 HOH A O 1 HETATM 4014 O O . HOH Q 9 . ? 73.092 28.315 35.880 1.00 28.58 ? 1215 HOH A O 1 HETATM 4015 O O . HOH Q 9 . ? 64.567 0.436 20.378 1.00 33.71 ? 1216 HOH A O 1 HETATM 4016 O O . HOH Q 9 . ? 64.865 -2.096 19.305 1.00 54.95 ? 1217 HOH A O 1 HETATM 4017 O O . HOH Q 9 . ? 58.718 8.114 36.078 1.00 35.18 ? 1218 HOH A O 1 HETATM 4018 O O . HOH Q 9 . ? 53.313 45.542 21.778 1.00 36.71 ? 1219 HOH A O 1 HETATM 4019 O O . HOH Q 9 . ? 34.349 36.603 28.730 1.00 38.72 ? 1220 HOH A O 1 HETATM 4020 O O . HOH Q 9 . ? 26.338 33.967 9.426 1.00 31.79 ? 1221 HOH A O 1 HETATM 4021 O O . HOH Q 9 . ? 17.707 15.555 -10.579 1.00 79.98 ? 1222 HOH A O 1 HETATM 4022 O O . HOH Q 9 . ? 21.001 18.922 -7.647 1.00 31.95 ? 1223 HOH A O 1 HETATM 4023 O O . HOH Q 9 . ? 61.229 12.240 15.733 1.00 36.24 ? 1224 HOH A O 1 HETATM 4024 O O . HOH Q 9 . ? 20.674 7.615 -5.130 1.00 64.18 ? 1225 HOH A O 1 HETATM 4025 O O . HOH Q 9 . ? 41.773 1.065 11.140 1.00 63.51 ? 1226 HOH A O 1 HETATM 4026 O O . HOH Q 9 . ? 61.750 13.663 13.402 1.00 64.64 ? 1227 HOH A O 1 HETATM 4027 O O . HOH Q 9 . ? 28.608 10.305 15.229 1.00 92.76 ? 1228 HOH A O 1 HETATM 4028 O O . HOH Q 9 . ? 35.195 46.456 4.634 1.00 51.34 ? 1229 HOH A O 1 HETATM 4029 O O . HOH Q 9 . ? 20.927 12.067 12.584 1.00 86.68 ? 1230 HOH A O 1 HETATM 4030 O O . HOH Q 9 . ? 56.775 49.179 35.888 1.00 56.86 ? 1231 HOH A O 1 HETATM 4031 O O . HOH Q 9 . ? 51.693 0.569 15.081 1.00 27.23 ? 1232 HOH A O 1 HETATM 4032 O O . HOH Q 9 . ? 54.265 6.670 36.822 1.00 32.98 ? 1233 HOH A O 1 HETATM 4033 O O . HOH Q 9 . ? 64.598 7.825 32.663 1.00 44.72 ? 1234 HOH A O 1 HETATM 4034 O O . HOH Q 9 . ? 64.411 10.402 23.679 1.00 26.33 ? 1235 HOH A O 1 HETATM 4035 O O . HOH Q 9 . ? 29.263 8.414 -1.052 1.00 55.65 ? 1237 HOH A O 1 HETATM 4036 O O . HOH Q 9 . ? 65.881 34.124 30.474 1.00 28.26 ? 1238 HOH A O 1 HETATM 4037 O O . HOH Q 9 . ? 59.089 26.635 17.202 1.00 29.79 ? 1239 HOH A O 1 HETATM 4038 O O . HOH Q 9 . ? 36.961 26.665 -19.530 1.00 40.29 ? 1240 HOH A O 1 HETATM 4039 O O . HOH Q 9 . ? 32.023 29.113 -11.829 1.00 49.47 ? 1241 HOH A O 1 HETATM 4040 O O . HOH Q 9 . ? 65.150 13.654 21.292 1.00 45.03 ? 1242 HOH A O 1 HETATM 4041 O O . HOH Q 9 . ? 27.858 23.412 -12.688 1.00 32.45 ? 1243 HOH A O 1 HETATM 4042 O O . HOH Q 9 . ? 35.694 4.872 11.594 1.00 40.04 ? 1244 HOH A O 1 HETATM 4043 O O . HOH Q 9 . ? 55.481 -1.795 18.196 1.00 61.38 ? 1245 HOH A O 1 HETATM 4044 O O . HOH Q 9 . ? 50.630 17.669 -7.806 1.00 22.17 ? 1246 HOH A O 1 HETATM 4045 O O . HOH Q 9 . ? 26.210 45.659 9.122 1.00 32.66 ? 1247 HOH A O 1 HETATM 4046 O O . HOH Q 9 . ? 10.422 16.976 0.583 1.00 42.76 ? 1248 HOH A O 1 HETATM 4047 O O . HOH Q 9 . ? 43.281 45.903 25.169 1.00 37.24 ? 1249 HOH A O 1 HETATM 4048 O O . HOH Q 9 . ? 67.116 18.173 20.368 1.00 60.45 ? 1250 HOH A O 1 HETATM 4049 O O . HOH Q 9 . ? 49.872 6.108 -10.519 1.00 43.47 ? 1251 HOH A O 1 HETATM 4050 O O . HOH Q 9 . ? 24.220 25.572 -3.190 1.00 31.34 ? 1252 HOH A O 1 HETATM 4051 O O . HOH Q 9 . ? 37.714 8.168 -8.372 1.00 30.25 ? 1253 HOH A O 1 HETATM 4052 O O . HOH Q 9 . ? 69.745 38.292 35.497 1.00 78.77 ? 1254 HOH A O 1 HETATM 4053 O O . HOH Q 9 . ? 45.177 0.602 -13.500 1.00 30.47 ? 1255 HOH A O 1 HETATM 4054 O O . HOH Q 9 . ? 30.349 36.571 -1.939 1.00 37.31 ? 1256 HOH A O 1 HETATM 4055 O O . HOH Q 9 . ? 46.889 -1.597 16.106 1.00 32.18 ? 1257 HOH A O 1 HETATM 4056 O O . HOH Q 9 . ? 63.884 34.291 42.698 1.00 27.88 ? 1258 HOH A O 1 HETATM 4057 O O . HOH Q 9 . ? 26.046 36.138 0.088 1.00 39.65 ? 1259 HOH A O 1 HETATM 4058 O O . HOH Q 9 . ? 53.252 28.870 -16.407 1.00 67.25 ? 1260 HOH A O 1 HETATM 4059 O O . HOH Q 9 . ? 43.514 39.827 -5.389 1.00 33.16 ? 1261 HOH A O 1 HETATM 4060 O O . HOH Q 9 . ? 46.317 51.108 14.517 1.00 31.75 ? 1262 HOH A O 1 HETATM 4061 O O . HOH Q 9 . ? 56.935 47.566 28.848 1.00 58.62 ? 1263 HOH A O 1 HETATM 4062 O O . HOH Q 9 . ? 44.178 38.926 -16.373 1.00 56.48 ? 1264 HOH A O 1 HETATM 4063 O O . HOH Q 9 . ? 53.697 -4.954 38.036 1.00 31.47 ? 1265 HOH A O 1 HETATM 4064 O O . HOH Q 9 . ? 66.954 37.039 39.912 1.00 35.97 ? 1266 HOH A O 1 HETATM 4065 O O . HOH Q 9 . ? 63.939 8.141 30.117 1.00 35.77 ? 1267 HOH A O 1 HETATM 4066 O O . HOH Q 9 . ? 70.738 34.023 34.454 1.00 51.88 ? 1268 HOH A O 1 HETATM 4067 O O . HOH Q 9 . ? 43.498 8.253 7.593 1.00 43.14 ? 1269 HOH A O 1 HETATM 4068 O O . HOH Q 9 . ? 60.852 -1.525 25.430 1.00 34.27 ? 1270 HOH A O 1 HETATM 4069 O O . HOH Q 9 . ? 43.308 54.863 10.168 1.00 38.17 ? 1271 HOH A O 1 HETATM 4070 O O . HOH Q 9 . ? 61.211 8.932 12.366 1.00 83.89 ? 1272 HOH A O 1 HETATM 4071 O O . HOH Q 9 . ? 41.496 47.709 25.948 1.00 67.41 ? 1273 HOH A O 1 HETATM 4072 O O . HOH Q 9 . ? 24.223 40.896 14.927 1.00 38.73 ? 1274 HOH A O 1 HETATM 4073 O O . HOH Q 9 . ? 54.801 31.825 -16.338 1.00 75.06 ? 1275 HOH A O 1 HETATM 4074 O O . HOH Q 9 . ? 23.630 26.817 -1.066 1.00 60.75 ? 1276 HOH A O 1 HETATM 4075 O O . HOH Q 9 . ? 59.486 15.687 6.034 1.00 66.45 ? 1277 HOH A O 1 HETATM 4076 O O . HOH Q 9 . ? 49.477 24.869 -15.339 1.00 68.12 ? 1278 HOH A O 1 HETATM 4077 O O . HOH Q 9 . ? 24.500 13.560 -10.966 1.00 56.17 ? 1279 HOH A O 1 HETATM 4078 O O . HOH Q 9 . ? 58.765 24.932 19.288 1.00 23.57 ? 1280 HOH A O 1 HETATM 4079 O O . HOH Q 9 . ? 25.041 29.844 -2.102 1.00 34.93 ? 1281 HOH A O 1 HETATM 4080 O O . HOH Q 9 . ? 36.235 31.169 20.178 1.00 33.95 ? 1282 HOH A O 1 HETATM 4081 O O . HOH Q 9 . ? 38.082 12.587 5.949 1.00 38.59 ? 1283 HOH A O 1 HETATM 4082 O O . HOH Q 9 . ? 32.327 31.617 28.623 1.00 20.88 ? 1284 HOH A O 1 HETATM 4083 O O . HOH Q 9 . ? 25.394 44.566 6.867 1.00 87.67 ? 1285 HOH A O 1 HETATM 4084 O O . HOH Q 9 . ? 35.919 10.089 0.966 1.00 54.52 ? 1286 HOH A O 1 HETATM 4085 O O . HOH Q 9 . ? 42.592 4.918 11.132 1.00 30.58 ? 1287 HOH A O 1 HETATM 4086 O O . HOH Q 9 . ? 23.031 39.804 12.729 1.00 34.96 ? 1288 HOH A O 1 HETATM 4087 O O . HOH Q 9 . ? 36.667 7.642 -13.154 1.00 35.58 ? 1289 HOH A O 1 HETATM 4088 O O . HOH Q 9 . ? 30.553 7.957 -4.423 1.00 36.48 ? 1290 HOH A O 1 HETATM 4089 O O . HOH Q 9 . ? 20.268 32.004 8.033 1.00 43.34 ? 1291 HOH A O 1 HETATM 4090 O O . HOH Q 9 . ? 47.295 48.645 14.467 1.00 62.65 ? 1292 HOH A O 1 HETATM 4091 O O . HOH Q 9 . ? 22.629 23.334 -2.924 1.00 26.67 ? 1293 HOH A O 1 HETATM 4092 O O . HOH Q 9 . ? 29.683 6.414 -8.721 1.00 31.53 ? 1294 HOH A O 1 HETATM 4093 O O . HOH Q 9 . ? 59.666 28.444 -12.388 1.00 28.65 ? 1295 HOH A O 1 HETATM 4094 O O . HOH Q 9 . ? 41.481 16.349 -16.735 1.00 42.54 ? 1296 HOH A O 1 HETATM 4095 O O . HOH Q 9 . ? 46.254 54.536 11.027 1.00 70.52 ? 1297 HOH A O 1 HETATM 4096 O O . HOH Q 9 . ? 63.477 4.646 26.663 1.00 35.91 ? 1298 HOH A O 1 HETATM 4097 O O . HOH Q 9 . ? 51.533 -6.519 43.263 1.00 49.03 ? 1299 HOH A O 1 HETATM 4098 O O . HOH Q 9 . ? 59.751 36.431 27.781 1.00 38.32 ? 1300 HOH A O 1 HETATM 4099 O O . HOH Q 9 . ? 67.002 26.654 28.241 1.00 40.53 ? 1301 HOH A O 1 HETATM 4100 O O . HOH Q 9 . ? 52.374 31.631 -15.634 1.00 71.93 ? 1302 HOH A O 1 HETATM 4101 O O . HOH Q 9 . ? 46.315 9.080 1.133 1.00 54.48 ? 1303 HOH A O 1 HETATM 4102 O O . HOH Q 9 . ? 55.688 41.599 5.066 1.00 37.64 ? 1304 HOH A O 1 HETATM 4103 O O . HOH Q 9 . ? 47.848 44.571 20.481 1.00 34.80 ? 1305 HOH A O 1 HETATM 4104 O O . HOH Q 9 . ? 35.079 16.058 -16.761 1.00 40.78 ? 1306 HOH A O 1 HETATM 4105 O O . HOH Q 9 . ? 56.064 7.169 6.495 1.00 36.91 ? 1307 HOH A O 1 HETATM 4106 O O . HOH Q 9 . ? 70.840 16.216 33.827 1.00 72.70 ? 1308 HOH A O 1 HETATM 4107 O O . HOH Q 9 . ? 67.065 16.737 23.541 1.00 87.69 ? 1309 HOH A O 1 HETATM 4108 O O . HOH Q 9 . ? 65.827 28.819 26.293 1.00 55.26 ? 1310 HOH A O 1 HETATM 4109 O O . HOH Q 9 . ? 55.657 41.414 8.382 1.00 40.73 ? 1311 HOH A O 1 HETATM 4110 O O . HOH Q 9 . ? 16.865 19.846 -9.373 1.00 46.34 ? 1312 HOH A O 1 HETATM 4111 O O . HOH Q 9 . ? 58.238 8.503 6.419 1.00 44.86 ? 1313 HOH A O 1 HETATM 4112 O O . HOH Q 9 . ? 26.788 9.275 -15.235 1.00 45.79 ? 1314 HOH A O 1 HETATM 4113 O O . HOH Q 9 . ? 65.221 36.092 29.155 1.00 46.77 ? 1315 HOH A O 1 HETATM 4114 O O . HOH Q 9 . ? 27.620 34.736 -2.850 1.00 36.12 ? 1316 HOH A O 1 HETATM 4115 O O . HOH Q 9 . ? 57.086 37.354 -12.595 1.00 71.08 ? 1317 HOH A O 1 HETATM 4116 O O . HOH Q 9 . ? 33.956 11.844 4.160 1.00 37.34 ? 1318 HOH A O 1 HETATM 4117 O O . HOH Q 9 . ? 72.484 21.091 34.659 1.00 57.63 ? 1319 HOH A O 1 HETATM 4118 O O . HOH Q 9 . ? 58.291 37.987 26.341 1.00 32.66 ? 1320 HOH A O 1 HETATM 4119 O O . HOH Q 9 . ? 17.366 32.487 6.193 1.00 52.25 ? 1321 HOH A O 1 HETATM 4120 O O . HOH Q 9 . ? 48.063 1.593 7.355 1.00 80.80 ? 1322 HOH A O 1 HETATM 4121 O O . HOH Q 9 . ? 32.991 17.092 -19.102 1.00 43.63 ? 1323 HOH A O 1 HETATM 4122 O O . HOH Q 9 . ? 70.344 33.178 43.062 1.00 43.01 ? 1324 HOH A O 1 HETATM 4123 O O . HOH Q 9 . ? 50.634 -16.079 18.180 1.00 55.56 ? 1325 HOH A O 1 HETATM 4124 O O . HOH Q 9 . ? 58.031 26.302 -17.982 1.00 47.05 ? 1326 HOH A O 1 HETATM 4125 O O . HOH Q 9 . ? 27.269 20.661 -11.048 1.00 41.95 ? 1327 HOH A O 1 HETATM 4126 O O . HOH Q 9 . ? 59.300 10.458 7.895 1.00 44.08 ? 1328 HOH A O 1 HETATM 4127 O O . HOH Q 9 . ? 54.405 38.662 18.614 1.00 48.99 ? 1329 HOH A O 1 HETATM 4128 O O . HOH Q 9 . ? 36.451 37.870 -9.552 1.00 60.16 ? 1330 HOH A O 1 HETATM 4129 O O . HOH Q 9 . ? 50.653 50.285 26.800 1.00 56.93 ? 1331 HOH A O 1 HETATM 4130 O O . HOH Q 9 . ? 52.600 -10.952 27.741 1.00 97.87 ? 1332 HOH A O 1 HETATM 4131 O O . HOH Q 9 . ? 62.015 32.280 7.217 1.00 76.52 ? 1333 HOH A O 1 HETATM 4132 O O . HOH Q 9 . ? 56.409 2.849 36.273 1.00 48.12 ? 1334 HOH A O 1 HETATM 4133 O O . HOH Q 9 . ? 46.921 11.355 -0.080 1.00 37.99 ? 1335 HOH A O 1 HETATM 4134 O O . HOH Q 9 . ? 25.144 33.574 -0.210 1.00 37.87 ? 1336 HOH A O 1 HETATM 4135 O O . HOH Q 9 . ? 52.764 15.802 -16.806 1.00 76.00 ? 1337 HOH A O 1 HETATM 4136 O O . HOH Q 9 . ? 25.425 27.353 -6.320 1.00 35.32 ? 1338 HOH A O 1 HETATM 4137 O O . HOH Q 9 . ? 56.808 38.674 -10.163 1.00 51.89 ? 1339 HOH A O 1 HETATM 4138 O O . HOH Q 9 . ? 37.426 12.256 -24.173 1.00 82.35 ? 1340 HOH A O 1 HETATM 4139 O O . HOH Q 9 . ? 25.118 19.331 -7.903 1.00 38.44 ? 1341 HOH A O 1 HETATM 4140 O O . HOH Q 9 . ? 57.735 30.561 -11.624 1.00 44.95 ? 1342 HOH A O 1 HETATM 4141 O O . HOH Q 9 . ? 44.443 18.544 -16.015 1.00 41.03 ? 1343 HOH A O 1 HETATM 4142 O O . HOH Q 9 . ? 71.156 33.766 40.921 1.00 46.50 ? 1344 HOH A O 1 HETATM 4143 O O . HOH Q 9 . ? 22.884 17.718 -6.592 1.00 39.77 ? 1345 HOH A O 1 HETATM 4144 O O . HOH Q 9 . ? 42.614 6.722 -15.012 1.00 37.10 ? 1346 HOH A O 1 HETATM 4145 O O . HOH Q 9 . ? 62.091 -0.095 27.582 1.00 52.97 ? 1347 HOH A O 1 HETATM 4146 O O . HOH Q 9 . ? 60.016 42.781 27.035 1.00 31.85 ? 1348 HOH A O 1 HETATM 4147 O O . HOH Q 9 . ? 50.464 46.823 21.026 1.00 37.34 ? 1349 HOH A O 1 HETATM 4148 O O . HOH Q 9 . ? 46.275 4.298 7.597 1.00 78.19 ? 1350 HOH A O 1 HETATM 4149 O O . HOH Q 9 . ? 51.423 4.090 5.826 1.00 60.13 ? 1351 HOH A O 1 HETATM 4150 O O . HOH Q 9 . ? 54.968 33.428 -13.744 1.00 38.61 ? 1352 HOH A O 1 HETATM 4151 O O . HOH Q 9 . ? 34.373 36.339 -11.534 1.00 50.59 ? 1353 HOH A O 1 HETATM 4152 O O . HOH Q 9 . ? 46.452 44.346 26.810 1.00 37.91 ? 1354 HOH A O 1 HETATM 4153 O O . HOH Q 9 . ? 19.840 12.269 1.794 1.00 27.54 ? 1355 HOH A O 1 HETATM 4154 O O . HOH Q 9 . ? 49.508 6.180 4.961 1.00 88.44 ? 1357 HOH A O 1 HETATM 4155 O O . HOH Q 9 . ? 39.282 10.166 -0.774 1.00 67.22 ? 1359 HOH A O 1 HETATM 4156 O O . HOH Q 9 . ? 56.958 21.100 8.063 1.00 49.09 ? 1360 HOH A O 1 HETATM 4157 O O . HOH Q 9 . ? 18.818 9.841 1.653 1.00 37.86 ? 1361 HOH A O 1 HETATM 4158 O O . HOH Q 9 . ? 36.910 44.926 -5.179 1.00 52.53 ? 1362 HOH A O 1 HETATM 4159 O O . HOH Q 9 . ? 56.345 34.324 14.072 1.00 35.01 ? 1363 HOH A O 1 HETATM 4160 O O . HOH Q 9 . ? 50.449 9.050 0.410 1.00 47.79 ? 1364 HOH A O 1 HETATM 4161 O O . HOH Q 9 . ? 46.559 52.317 4.906 1.00 77.33 ? 1365 HOH A O 1 HETATM 4162 O O . HOH Q 9 . ? 23.801 16.120 -10.371 1.00 85.22 ? 1366 HOH A O 1 HETATM 4163 O O . HOH Q 9 . ? 16.200 13.297 0.193 1.00 94.07 ? 1367 HOH A O 1 HETATM 4164 O O . HOH Q 9 . ? 17.466 9.098 -0.855 1.00 54.08 ? 1368 HOH A O 1 HETATM 4165 O O . HOH Q 9 . ? 55.940 4.743 34.744 1.00 44.40 ? 1369 HOH A O 1 HETATM 4166 O O . HOH Q 9 . ? 55.988 33.259 22.909 1.00 37.10 ? 1370 HOH A O 1 HETATM 4167 O O . HOH Q 9 . ? 24.544 18.245 -11.830 1.00 42.65 ? 1371 HOH A O 1 HETATM 4168 O O . HOH Q 9 . ? 29.535 47.255 15.240 1.00 51.97 ? 1372 HOH A O 1 HETATM 4169 O O . HOH Q 9 . ? 64.551 8.420 21.655 1.00 57.02 ? 1373 HOH A O 1 HETATM 4170 O O . HOH Q 9 . ? 20.020 23.908 -6.293 1.00 71.55 ? 1375 HOH A O 1 HETATM 4171 O O . HOH Q 9 . ? 53.805 38.079 12.610 1.00 34.75 ? 1376 HOH A O 1 HETATM 4172 O O . HOH Q 9 . ? 31.929 49.858 7.317 1.00 56.17 ? 1377 HOH A O 1 HETATM 4173 O O . HOH Q 9 . ? 30.524 31.612 26.718 1.00 77.44 ? 1378 HOH A O 1 HETATM 4174 O O . HOH Q 9 . ? 49.480 -7.579 28.903 1.00 50.75 ? 1379 HOH A O 1 HETATM 4175 O O . HOH Q 9 . ? 59.005 14.117 25.571 1.00 28.05 ? 1380 HOH A O 1 HETATM 4176 O O . HOH Q 9 . ? 31.697 31.573 -9.076 1.00 39.74 ? 1381 HOH A O 1 HETATM 4177 O O . HOH Q 9 . ? 58.792 12.583 0.861 1.00 62.43 ? 1382 HOH A O 1 HETATM 4178 O O . HOH Q 9 . ? 70.757 32.780 31.391 1.00 102.43 ? 1383 HOH A O 1 HETATM 4179 O O . HOH Q 9 . ? 29.578 33.093 -8.221 1.00 80.49 ? 1384 HOH A O 1 HETATM 4180 O O . HOH Q 9 . ? 21.665 32.445 3.305 1.00 94.17 ? 1385 HOH A O 1 HETATM 4181 O O . HOH Q 9 . ? 38.099 39.522 -6.933 1.00 44.58 ? 1386 HOH A O 1 HETATM 4182 O O . HOH Q 9 . ? 43.423 52.228 5.241 1.00 43.93 ? 1387 HOH A O 1 HETATM 4183 O O . HOH Q 9 . ? 59.544 0.254 36.111 1.00 45.11 ? 1388 HOH A O 1 HETATM 4184 O O . HOH Q 9 . ? 22.851 12.026 15.772 1.00 54.60 ? 1389 HOH A O 1 HETATM 4185 O O . HOH Q 9 . ? 59.529 26.862 7.256 1.00 50.49 ? 1390 HOH A O 1 HETATM 4186 O O . HOH Q 9 . ? 33.108 -2.102 12.818 1.00 99.21 ? 1392 HOH A O 1 HETATM 4187 O O . HOH Q 9 . ? 45.187 49.420 0.275 1.00 56.47 ? 1393 HOH A O 1 HETATM 4188 O O . HOH Q 9 . ? 53.593 -2.737 20.030 1.00 41.34 ? 1394 HOH A O 1 HETATM 4189 O O . HOH Q 9 . ? 40.149 47.592 3.492 1.00 43.83 ? 1395 HOH A O 1 HETATM 4190 O O . HOH Q 9 . ? 12.402 16.904 8.361 1.00 59.59 ? 1396 HOH A O 1 HETATM 4191 O O . HOH Q 9 . ? 54.631 0.568 13.170 1.00 60.00 ? 1397 HOH A O 1 HETATM 4192 O O . HOH Q 9 . ? 21.123 21.205 -8.854 1.00 42.83 ? 1398 HOH A O 1 HETATM 4193 O O . HOH Q 9 . ? 41.540 1.235 -9.833 1.00 46.44 ? 1399 HOH A O 1 HETATM 4194 O O . HOH Q 9 . ? 56.468 18.990 9.399 1.00 32.24 ? 1400 HOH A O 1 HETATM 4195 O O . HOH Q 9 . ? 74.868 21.367 37.185 1.00 53.69 ? 1401 HOH A O 1 HETATM 4196 O O . HOH Q 9 . ? 65.540 41.636 34.202 1.00 48.56 ? 1402 HOH A O 1 HETATM 4197 O O . HOH Q 9 . ? 52.111 8.560 -10.707 1.00 90.51 ? 1403 HOH A O 1 HETATM 4198 O O . HOH Q 9 . ? 58.823 11.186 -2.119 1.00 80.51 ? 1404 HOH A O 1 HETATM 4199 O O . HOH Q 9 . ? 37.812 48.610 1.270 1.00 65.41 ? 1405 HOH A O 1 HETATM 4200 O O . HOH Q 9 . ? 48.137 9.781 -1.124 1.00 48.33 ? 1406 HOH A O 1 HETATM 4201 O O . HOH Q 9 . ? 39.109 11.936 -20.441 1.00 53.41 ? 1407 HOH A O 1 HETATM 4202 O O . HOH Q 9 . ? 39.312 46.133 -5.233 1.00 35.54 ? 1408 HOH A O 1 HETATM 4203 O O . HOH Q 9 . ? 53.884 43.006 5.102 1.00 37.58 ? 1409 HOH A O 1 HETATM 4204 O O . HOH Q 9 . ? 19.656 32.297 5.007 1.00 58.59 ? 1410 HOH A O 1 HETATM 4205 O O . HOH Q 9 . ? 41.205 13.553 -20.116 1.00 58.85 ? 1411 HOH A O 1 HETATM 4206 O O . HOH Q 9 . ? 58.565 31.287 16.373 1.00 58.66 ? 1412 HOH A O 1 HETATM 4207 O O . HOH Q 9 . ? 51.371 39.537 -6.841 1.00 57.68 ? 1413 HOH A O 1 HETATM 4208 O O . HOH Q 9 . ? 51.006 28.411 -14.192 1.00 57.01 ? 1414 HOH A O 1 HETATM 4209 O O . HOH Q 9 . ? 57.979 9.972 0.363 1.00 65.44 ? 1415 HOH A O 1 HETATM 4210 O O . HOH Q 9 . ? 13.711 17.375 -9.769 1.00 51.00 ? 1416 HOH A O 1 HETATM 4211 O O . HOH Q 9 . ? 58.758 29.062 -14.804 1.00 38.70 ? 1417 HOH A O 1 HETATM 4212 O O . HOH Q 9 . ? 45.047 -11.353 21.029 1.00 86.97 ? 1418 HOH A O 1 HETATM 4213 O O . HOH Q 9 . ? 41.502 9.411 -4.346 1.00 51.39 ? 1419 HOH A O 1 HETATM 4214 O O . HOH Q 9 . ? 36.628 52.520 8.971 1.00 56.19 ? 1420 HOH A O 1 HETATM 4215 O O . HOH Q 9 . ? 36.255 17.750 -19.661 1.00 81.66 ? 1421 HOH A O 1 HETATM 4216 O O . HOH Q 9 . ? 37.582 50.616 7.451 1.00 56.19 ? 1422 HOH A O 1 HETATM 4217 O O . HOH Q 9 . ? 42.051 6.706 9.366 1.00 44.72 ? 1423 HOH A O 1 HETATM 4218 O O . HOH Q 9 . ? 45.386 3.362 -5.310 1.00 56.55 ? 1424 HOH A O 1 HETATM 4219 O O . HOH Q 9 . ? 32.784 22.202 -19.219 1.00 47.53 ? 1425 HOH A O 1 HETATM 4220 O O . HOH Q 9 . ? 52.474 12.174 -7.316 1.00 48.96 ? 1426 HOH A O 1 HETATM 4221 O O . HOH Q 9 . ? 51.913 -4.348 18.493 1.00 51.11 ? 1427 HOH A O 1 HETATM 4222 O O . HOH Q 9 . ? 60.499 21.329 -3.612 1.00 49.01 ? 1428 HOH A O 1 HETATM 4223 O O . HOH Q 9 . ? 57.152 44.127 23.411 1.00 60.67 ? 1429 HOH A O 1 HETATM 4224 O O . HOH Q 9 . ? 55.105 -6.010 15.462 1.00 65.70 ? 1430 HOH A O 1 HETATM 4225 O O . HOH Q 9 . ? 63.496 14.881 18.812 1.00 61.42 ? 1431 HOH A O 1 HETATM 4226 O O . HOH Q 9 . ? 66.814 25.288 24.725 1.00 50.83 ? 1432 HOH A O 1 HETATM 4227 O O . HOH Q 9 . ? 57.767 12.871 -8.943 1.00 40.57 ? 1433 HOH A O 1 HETATM 4228 O O . HOH Q 9 . ? 67.238 37.728 28.348 1.00 87.24 ? 1434 HOH A O 1 HETATM 4229 O O . HOH Q 9 . ? 32.534 25.371 -19.411 1.00 60.96 ? 1435 HOH A O 1 HETATM 4230 O O . HOH Q 9 . ? 47.303 23.519 -15.588 1.00 36.68 ? 1436 HOH A O 1 HETATM 4231 O O . HOH Q 9 . ? 58.887 44.427 25.485 1.00 75.44 ? 1437 HOH A O 1 HETATM 4232 O O . HOH Q 9 . ? 26.365 44.142 16.437 1.00 80.88 ? 1438 HOH A O 1 HETATM 4233 O O . HOH Q 9 . ? 59.921 23.539 10.673 1.00 48.79 ? 1439 HOH A O 1 HETATM 4234 O O . HOH Q 9 . ? 42.960 9.949 -2.195 1.00 34.79 ? 1440 HOH A O 1 HETATM 4235 O O . HOH Q 9 . ? 51.672 40.260 -4.511 1.00 37.14 ? 1441 HOH A O 1 HETATM 4236 O O . HOH Q 9 . ? 59.192 -0.581 13.821 1.00 56.80 ? 1442 HOH A O 1 HETATM 4237 O O . HOH Q 9 . ? 24.761 11.054 14.301 1.00 55.45 ? 1443 HOH A O 1 HETATM 4238 O O . HOH Q 9 . ? 27.409 7.121 -7.094 1.00 48.16 ? 1444 HOH A O 1 HETATM 4239 O O . HOH Q 9 . ? 52.948 50.154 23.565 1.00 76.33 ? 1445 HOH A O 1 HETATM 4240 O O . HOH Q 9 . ? 58.145 34.652 23.418 1.00 79.09 ? 1446 HOH A O 1 HETATM 4241 O O . HOH Q 9 . ? 20.326 24.136 -1.988 1.00 40.00 ? 1447 HOH A O 1 HETATM 4242 O O . HOH Q 9 . ? 51.091 7.904 -4.728 1.00 52.39 ? 1448 HOH A O 1 HETATM 4243 O O . HOH Q 9 . ? 65.402 39.986 36.374 1.00 40.12 ? 1449 HOH A O 1 HETATM 4244 O O . HOH Q 9 . ? 33.191 10.125 2.658 1.00 41.08 ? 1450 HOH A O 1 HETATM 4245 O O . HOH Q 9 . ? 20.778 14.062 -10.888 1.00 59.69 ? 1451 HOH A O 1 HETATM 4246 O O . HOH Q 9 . ? 50.789 43.281 -3.506 1.00 65.96 ? 1452 HOH A O 1 HETATM 4247 O O . HOH Q 9 . ? 47.180 -1.494 10.367 1.00 67.86 ? 1454 HOH A O 1 HETATM 4248 O O . HOH Q 9 . ? 32.221 45.807 -3.418 1.00 60.54 ? 1455 HOH A O 1 HETATM 4249 O O . HOH Q 9 . ? 19.928 9.887 7.651 1.00 71.63 ? 1456 HOH A O 1 HETATM 4250 O O . HOH Q 9 . ? 25.828 9.606 2.231 1.00 68.55 ? 1457 HOH A O 1 HETATM 4251 O O . HOH Q 9 . ? 66.202 6.757 26.342 1.00 102.48 ? 1458 HOH A O 1 HETATM 4252 O O . HOH Q 9 . ? 51.541 47.826 6.415 1.00 75.22 ? 1459 HOH A O 1 HETATM 4253 O O . HOH Q 9 . ? 27.331 38.799 2.231 1.00 83.28 ? 1460 HOH A O 1 HETATM 4254 O O . HOH Q 9 . ? 31.438 38.485 -6.329 1.00 48.19 ? 1461 HOH A O 1 HETATM 4255 O O . HOH Q 9 . ? 58.001 17.256 8.252 1.00 56.65 ? 1462 HOH A O 1 HETATM 4256 O O . HOH Q 9 . ? 32.988 7.046 -1.575 1.00 40.49 ? 1463 HOH A O 1 HETATM 4257 O O . HOH Q 9 . ? 59.746 12.289 4.781 1.00 90.73 ? 1464 HOH A O 1 HETATM 4258 O O . HOH Q 9 . ? 33.819 50.209 17.653 1.00 55.94 ? 1465 HOH A O 1 HETATM 4259 O O . HOH Q 9 . ? 62.388 -2.720 18.013 1.00 44.10 ? 1466 HOH A O 1 HETATM 4260 O O . HOH Q 9 . ? 61.914 44.015 30.082 1.00 68.14 ? 1467 HOH A O 1 HETATM 4261 O O . HOH Q 9 . ? 66.176 34.346 43.896 1.00 79.48 ? 1468 HOH A O 1 HETATM 4262 O O . HOH Q 9 . ? 31.627 46.131 4.727 1.00 50.55 ? 1469 HOH A O 1 HETATM 4263 O O . HOH Q 9 . ? 52.399 12.769 -4.794 1.00 75.64 ? 1470 HOH A O 1 HETATM 4264 O O . HOH Q 9 . ? 33.990 3.417 15.652 1.00 86.52 ? 1471 HOH A O 1 HETATM 4265 O O . HOH Q 9 . ? 32.239 47.430 0.672 1.00 75.62 ? 1472 HOH A O 1 HETATM 4266 O O . HOH Q 9 . ? 34.420 10.093 -19.328 1.00 49.37 ? 1474 HOH A O 1 HETATM 4267 O O . HOH Q 9 . ? 49.017 42.010 -11.261 1.00 74.73 ? 1475 HOH A O 1 HETATM 4268 O O . HOH Q 9 . ? 34.940 47.965 -0.237 1.00 81.78 ? 1476 HOH A O 1 HETATM 4269 O O . HOH Q 9 . ? 48.065 5.324 -7.662 1.00 47.23 ? 1477 HOH A O 1 HETATM 4270 O O . HOH Q 9 . ? 60.421 30.280 18.063 1.00 61.65 ? 1478 HOH A O 1 HETATM 4271 O O . HOH Q 9 . ? 29.885 8.768 1.574 1.00 58.00 ? 1479 HOH A O 1 HETATM 4272 O O . HOH Q 9 . ? 41.059 10.081 9.147 1.00 40.82 ? 1480 HOH A O 1 HETATM 4273 O O . HOH Q 9 . ? 10.894 10.938 0.162 1.00 89.26 ? 1481 HOH A O 1 HETATM 4274 O O . HOH Q 9 . ? 36.860 15.065 -18.687 1.00 72.58 ? 1482 HOH A O 1 HETATM 4275 O O . HOH Q 9 . ? 39.361 16.822 -18.699 1.00 49.97 ? 1483 HOH A O 1 HETATM 4276 O O . HOH Q 9 . ? 54.799 49.917 28.777 1.00 67.38 ? 1484 HOH A O 1 HETATM 4277 O O . HOH Q 9 . ? 8.156 14.357 8.439 1.00 84.87 ? 1485 HOH A O 1 HETATM 4278 O O . HOH Q 9 . ? 31.418 52.380 11.458 1.00 48.32 ? 1486 HOH A O 1 HETATM 4279 O O . HOH Q 9 . ? 55.329 38.075 25.615 1.00 56.34 ? 1487 HOH A O 1 HETATM 4280 O O . HOH Q 9 . ? 52.442 41.228 19.934 1.00 74.43 ? 1488 HOH A O 1 HETATM 4281 O O . HOH Q 9 . ? 54.806 45.036 9.388 1.00 67.48 ? 1489 HOH A O 1 HETATM 4282 O O . HOH Q 9 . ? 44.280 50.014 4.134 1.00 61.55 ? 1490 HOH A O 1 HETATM 4283 O O . HOH Q 9 . ? 27.835 52.562 15.430 1.00 77.83 ? 1491 HOH A O 1 HETATM 4284 O O . HOH Q 9 . ? 36.763 8.102 -5.864 1.00 40.02 ? 1492 HOH A O 1 HETATM 4285 O O . HOH Q 9 . ? 48.950 -0.589 12.457 1.00 65.26 ? 1493 HOH A O 1 HETATM 4286 O O . HOH Q 9 . ? 50.307 51.398 11.981 1.00 77.97 ? 1494 HOH A O 1 HETATM 4287 O O . HOH Q 9 . ? 54.054 39.357 23.587 1.00 74.37 ? 1495 HOH A O 1 HETATM 4288 O O . HOH Q 9 . ? 47.121 49.062 2.159 1.00 49.98 ? 1496 HOH A O 1 HETATM 4289 O O . HOH Q 9 . ? 17.374 11.415 5.028 1.00 48.54 ? 1497 HOH A O 1 HETATM 4290 O O . HOH Q 9 . ? 66.739 13.867 27.476 1.00 47.26 ? 1498 HOH A O 1 HETATM 4291 O O . HOH Q 9 . ? 31.046 10.272 -17.442 1.00 72.08 ? 1499 HOH A O 1 HETATM 4292 O O . HOH Q 9 . ? 38.186 21.063 -20.461 1.00 69.93 ? 1500 HOH A O 1 HETATM 4293 O O . HOH Q 9 . ? 24.161 8.565 -5.360 1.00 65.67 ? 1501 HOH A O 1 HETATM 4294 O O . HOH Q 9 . ? 26.733 25.359 -11.181 1.00 59.99 ? 1502 HOH A O 1 HETATM 4295 O O . HOH Q 9 . ? 24.855 16.833 -7.275 1.00 83.74 ? 1503 HOH A O 1 HETATM 4296 O O . HOH Q 9 . ? 58.771 14.546 -11.167 1.00 62.63 ? 1504 HOH A O 1 HETATM 4297 O O . HOH Q 9 . ? 72.272 35.816 35.680 1.00 85.90 ? 1505 HOH A O 1 HETATM 4298 O O . HOH Q 9 . ? 18.121 31.045 9.191 1.00 40.37 ? 1506 HOH A O 1 HETATM 4299 O O . HOH Q 9 . ? 8.682 10.835 1.592 1.00 48.19 ? 1507 HOH A O 1 HETATM 4300 O O . HOH Q 9 . ? 52.046 49.649 33.985 1.00 54.81 ? 1508 HOH A O 1 HETATM 4301 O O . HOH Q 9 . ? 63.374 29.405 24.670 1.00 55.67 ? 1509 HOH A O 1 HETATM 4302 O O . HOH Q 9 . ? 33.650 38.782 -7.716 1.00 53.31 ? 1510 HOH A O 1 HETATM 4303 O O . HOH Q 9 . ? 38.020 10.442 4.044 1.00 44.12 ? 1511 HOH A O 1 HETATM 4304 O O . HOH Q 9 . ? 59.980 15.580 8.999 1.00 62.52 ? 1512 HOH A O 1 HETATM 4305 O O . HOH Q 9 . ? 66.963 11.345 35.528 1.00 65.92 ? 1513 HOH A O 1 HETATM 4306 O O . HOH Q 9 . ? 62.957 37.981 42.300 1.00 52.75 ? 1514 HOH A O 1 HETATM 4307 O O . HOH Q 9 . ? 13.005 13.898 -4.406 1.00 43.95 ? 1515 HOH A O 1 HETATM 4308 O O . HOH Q 9 . ? 39.921 35.380 -13.355 1.00 89.10 ? 1516 HOH A O 1 HETATM 4309 O O . HOH Q 9 . ? 62.107 5.270 35.899 1.00 77.40 ? 1517 HOH A O 1 HETATM 4310 O O . HOH Q 9 . ? 62.466 36.439 27.594 1.00 53.52 ? 1518 HOH A O 1 HETATM 4311 O O . HOH Q 9 . ? 52.094 -8.883 31.747 1.00 49.86 ? 1519 HOH A O 1 HETATM 4312 O O . HOH Q 9 . ? 37.715 32.411 21.867 1.00 40.90 ? 1520 HOH A O 1 HETATM 4313 O O . HOH Q 9 . ? 59.867 27.265 11.170 1.00 62.10 ? 1521 HOH A O 1 HETATM 4314 O O . HOH Q 9 . ? 58.218 24.450 6.515 1.00 54.03 ? 1523 HOH A O 1 HETATM 4315 O O . HOH Q 9 . ? 53.838 38.963 -10.139 1.00 56.66 ? 1524 HOH A O 1 HETATM 4316 O O . HOH Q 9 . ? 29.263 8.395 -16.683 1.00 56.10 ? 1525 HOH A O 1 HETATM 4317 O O . HOH Q 9 . ? 60.440 20.559 1.047 1.00 108.84 ? 1526 HOH A O 1 HETATM 4318 O O . HOH Q 9 . ? 68.033 13.043 29.675 1.00 58.76 ? 1527 HOH A O 1 HETATM 4319 O O . HOH Q 9 . ? 40.139 31.859 -18.242 1.00 55.57 ? 1528 HOH A O 1 HETATM 4320 O O . HOH Q 9 . ? 59.051 19.661 5.443 1.00 88.28 ? 1529 HOH A O 1 HETATM 4321 O O . HOH Q 9 . ? 63.513 4.195 32.239 1.00 86.77 ? 1530 HOH A O 1 HETATM 4322 O O . HOH Q 9 . ? 53.053 38.105 21.971 1.00 46.54 ? 1532 HOH A O 1 HETATM 4323 O O . HOH Q 9 . ? 39.500 52.016 4.757 1.00 83.46 ? 1534 HOH A O 1 HETATM 4324 O O . HOH Q 9 . ? 47.140 -10.161 29.002 1.00 93.88 ? 1535 HOH A O 1 HETATM 4325 O O . HOH Q 9 . ? 25.681 11.844 11.969 1.00 53.47 ? 1536 HOH A O 1 HETATM 4326 O O . HOH Q 9 . ? 33.607 41.597 -5.427 1.00 65.63 ? 1537 HOH A O 1 HETATM 4327 O O . HOH Q 9 . ? 32.060 35.830 26.744 1.00 40.24 ? 1538 HOH A O 1 HETATM 4328 O O . HOH Q 9 . ? 41.290 9.588 -21.665 1.00 47.20 ? 1539 HOH A O 1 HETATM 4329 O O . HOH Q 9 . ? 45.648 33.916 -16.941 1.00 58.83 ? 1540 HOH A O 1 HETATM 4330 O O . HOH Q 9 . ? 21.852 30.273 -0.327 1.00 57.38 ? 1541 HOH A O 1 HETATM 4331 O O . HOH Q 9 . ? 57.307 -9.008 27.168 1.00 128.95 ? 1542 HOH A O 1 HETATM 4332 O O . HOH Q 9 . ? 42.164 44.176 -6.962 1.00 48.10 ? 1543 HOH A O 1 HETATM 4333 O O . HOH Q 9 . ? 29.050 19.749 -19.537 1.00 48.84 ? 1544 HOH A O 1 HETATM 4334 O O . HOH Q 9 . ? 11.159 16.337 -1.901 1.00 84.77 ? 1545 HOH A O 1 HETATM 4335 O O . HOH Q 9 . ? 23.568 22.365 -14.663 1.00 103.19 ? 1546 HOH A O 1 HETATM 4336 O O . HOH Q 9 . ? 35.250 12.135 6.554 1.00 46.65 ? 1547 HOH A O 1 HETATM 4337 O O . HOH Q 9 . ? 61.684 28.152 -0.442 1.00 33.47 ? 1548 HOH A O 1 HETATM 4338 O O . HOH Q 9 . ? 18.135 31.424 3.056 1.00 61.54 ? 1549 HOH A O 1 HETATM 4339 O O . HOH Q 9 . ? 57.932 29.192 2.091 1.00 66.71 ? 1550 HOH A O 1 HETATM 4340 O O . HOH Q 9 . ? 52.896 12.941 -12.393 1.00 79.60 ? 1552 HOH A O 1 HETATM 4341 O O . HOH Q 9 . ? 52.015 37.669 -8.411 1.00 27.51 ? 1553 HOH A O 1 HETATM 4342 O O . HOH Q 9 . ? 35.709 11.330 3.011 1.00 66.28 ? 1554 HOH A O 1 HETATM 4343 O O . HOH Q 9 . ? 33.770 6.690 11.808 1.00 83.03 ? 1555 HOH A O 1 HETATM 4344 O O . HOH Q 9 . ? 39.161 48.770 -5.209 1.00 42.82 ? 1556 HOH A O 1 HETATM 4345 O O . HOH Q 9 . ? 23.186 14.010 -14.286 1.00 97.84 ? 1557 HOH A O 1 HETATM 4346 O O . HOH Q 9 . ? 37.499 3.638 9.226 1.00 78.21 ? 1558 HOH A O 1 HETATM 4347 O O . HOH Q 9 . ? 40.246 10.637 6.275 1.00 82.76 ? 1559 HOH A O 1 HETATM 4348 O O . HOH Q 9 . ? 31.788 12.270 7.404 1.00 66.55 ? 1560 HOH A O 1 HETATM 4349 O O . HOH Q 9 . ? 36.516 9.136 12.493 1.00 44.69 ? 1561 HOH A O 1 HETATM 4350 O O . HOH Q 9 . ? 42.217 48.924 2.895 1.00 101.87 ? 1562 HOH A O 1 HETATM 4351 O O . HOH Q 9 . ? 50.195 10.589 2.682 1.00 16.14 ? 1563 HOH A O 1 HETATM 4352 O O . HOH Q 9 . ? 44.055 42.968 26.058 0.50 24.19 ? 1564 HOH A O 1 HETATM 4353 O O . HOH Q 9 . ? 44.509 15.945 26.036 0.50 19.56 ? 1565 HOH A O 1 HETATM 4354 O O . HOH Q 9 . ? 43.996 13.726 26.479 0.25 47.64 ? 1566 HOH A O 1 HETATM 4355 O O . HOH Q 9 . ? 54.954 9.356 -0.921 1.00 87.40 ? 1567 HOH A O 1 HETATM 4356 O O . HOH Q 9 . ? 8.076 18.714 -0.058 1.00 79.54 ? 1568 HOH A O 1 HETATM 4357 O O . HOH Q 9 . ? 21.445 8.661 1.770 1.00 66.34 ? 1569 HOH A O 1 HETATM 4358 O O . HOH Q 9 . ? 38.907 24.869 -19.751 1.00 87.24 ? 1570 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . ILE A 1 ? 0.3179 0.3510 0.3304 -0.0002 -0.0019 -0.0154 1 ILE A N 2 C CA . ILE A 1 ? 0.3328 0.3526 0.3432 -0.0017 0.0000 -0.0130 1 ILE A CA 3 C C . ILE A 1 ? 0.3173 0.3456 0.3375 -0.0008 -0.0030 -0.0104 1 ILE A C 4 O O . ILE A 1 ? 0.3102 0.3556 0.3285 0.0007 -0.0082 -0.0116 1 ILE A O 5 C CB . ILE A 1 ? 0.3481 0.3579 0.3559 -0.0022 0.0000 -0.0160 1 ILE A CB 6 C CG1 . ILE A 1 ? 0.3707 0.3725 0.3625 -0.0084 -0.0001 -0.0009 1 ILE A CG1 7 C CG2 . ILE A 1 ? 0.3783 0.3701 0.3815 -0.0073 0.0053 -0.0201 1 ILE A CG2 8 C CD1 . ILE A 1 ? 0.4215 0.4093 0.3931 -0.0160 -0.0096 -0.0265 1 ILE A CD1 9 N N . ILE A 2 ? 0.2960 0.3307 0.3258 -0.0035 -0.0030 -0.0059 2 ILE A N 10 C CA . ILE A 2 ? 0.2753 0.3230 0.3201 -0.0041 0.0022 -0.0034 2 ILE A CA 11 C C . ILE A 2 ? 0.2717 0.3172 0.3195 -0.0068 0.0018 0.0033 2 ILE A C 12 O O . ILE A 2 ? 0.2629 0.3157 0.3269 -0.0077 -0.0003 0.0056 2 ILE A O 13 C CB . ILE A 2 ? 0.2802 0.3227 0.3195 -0.0020 0.0080 -0.0025 2 ILE A CB 14 C CG1 . ILE A 2 ? 0.2631 0.3114 0.3176 -0.0138 0.0122 0.0075 2 ILE A CG1 15 C CG2 . ILE A 2 ? 0.2666 0.3262 0.3174 -0.0008 0.0130 -0.0160 2 ILE A CG2 16 C CD1 . ILE A 2 ? 0.2693 0.3355 0.2891 -0.0262 0.0245 0.0034 2 ILE A CD1 17 N N . PRO A 3 ? 0.2598 0.3141 0.3154 -0.0119 0.0011 0.0027 3 PRO A N 18 C CA . PRO A 3 ? 0.2565 0.3085 0.3117 -0.0140 0.0024 0.0069 3 PRO A CA 19 C C . PRO A 3 ? 0.2487 0.3102 0.3096 -0.0177 0.0033 0.0067 3 PRO A C 20 O O . PRO A 3 ? 0.2400 0.3047 0.3026 -0.0182 0.0045 0.0059 3 PRO A O 21 C CB . PRO A 3 ? 0.2565 0.3075 0.3156 -0.0146 0.0028 0.0037 3 PRO A CB 22 C CG . PRO A 3 ? 0.2604 0.3038 0.3224 -0.0170 0.0023 0.0046 3 PRO A CG 23 C CD . PRO A 3 ? 0.2615 0.3155 0.3191 -0.0046 0.0046 0.0097 3 PRO A CD 24 N N . VAL A 4 ? 0.2511 0.3175 0.3081 -0.0195 0.0032 0.0078 4 VAL A N 25 C CA . VAL A 4 ? 0.2472 0.3202 0.3090 -0.0206 0.0044 0.0084 4 VAL A CA 26 C C . VAL A 4 ? 0.2330 0.3141 0.3020 -0.0223 0.0080 0.0122 4 VAL A C 27 O O . VAL A 4 ? 0.2218 0.2996 0.2868 -0.0297 0.0087 0.0208 4 VAL A O 28 C CB . VAL A 4 ? 0.2480 0.3327 0.3091 -0.0177 0.0047 0.0090 4 VAL A CB 29 C CG1 . VAL A 4 ? 0.2677 0.3346 0.3425 -0.0137 0.0073 0.0154 4 VAL A CG1 30 C CG2 . VAL A 4 ? 0.2714 0.3453 0.3268 -0.0063 -0.0038 -0.0072 4 VAL A CG2 31 N N . GLU A 5 ? 0.2282 0.3119 0.2897 -0.0227 0.0126 0.0127 5 GLU A N 32 C CA . GLU A 5 ? 0.2505 0.3186 0.2993 -0.0227 0.0122 0.0128 5 GLU A CA 33 C C . GLU A 5 ? 0.2256 0.3024 0.2759 -0.0170 0.0112 0.0119 5 GLU A C 34 O O . GLU A 5 ? 0.2115 0.2981 0.2710 -0.0148 0.0133 0.0037 5 GLU A O 35 C CB . GLU A 5 ? 0.2464 0.3186 0.2972 -0.0216 0.0115 0.0117 5 GLU A CB 36 C CG . GLU A 5 ? 0.3122 0.3574 0.3269 -0.0279 0.0155 0.0123 5 GLU A CG 37 C CD . GLU A 5 ? 0.3354 0.3682 0.3639 -0.0408 0.0019 0.0101 5 GLU A CD 38 O OE1 . GLU A 5 ? 0.4351 0.4227 0.4734 -0.0647 0.0077 0.0244 5 GLU A OE1 39 O OE2 . GLU A 5 ? 0.4233 0.4174 0.4339 -0.0866 -0.0430 -0.0328 5 GLU A OE2 40 N N . GLU A 6 ? 0.2046 0.2809 0.2504 -0.0159 0.0038 0.0080 6 GLU A N 41 C CA . GLU A 6 ? 0.1969 0.2681 0.2423 -0.0122 0.0013 0.0090 6 GLU A CA 42 C C . GLU A 6 ? 0.1921 0.2565 0.2442 -0.0113 -0.0006 0.0105 6 GLU A C 43 O O . GLU A 6 ? 0.1921 0.2476 0.2400 -0.0004 -0.0026 0.0029 6 GLU A O 44 C CB . GLU A 6 ? 0.1916 0.2687 0.2294 -0.0096 -0.0048 0.0061 6 GLU A CB 45 C CG . GLU A 6 ? 0.2094 0.2793 0.2193 -0.0154 -0.0065 0.0118 6 GLU A CG 46 C CD . GLU A 6 ? 0.2147 0.3097 0.2006 -0.0072 -0.0246 0.0083 6 GLU A CD 47 O OE1 . GLU A 6 ? 0.2460 0.3164 0.2176 -0.0051 -0.0331 -0.0026 6 GLU A OE1 48 O OE2 . GLU A 6 ? 0.2107 0.2955 0.1866 -0.0017 -0.0284 0.0071 6 GLU A OE2 49 N N . GLU A 7 ? 0.1932 0.2467 0.2472 -0.0040 0.0019 0.0158 7 GLU A N 50 C CA . GLU A 7 ? 0.1950 0.2466 0.2582 -0.0068 -0.0010 0.0179 7 GLU A CA 51 C C . GLU A 7 ? 0.1914 0.2405 0.2573 -0.0129 -0.0012 0.0176 7 GLU A C 52 O O . GLU A 7 ? 0.2045 0.2381 0.2530 -0.0235 -0.0057 0.0147 7 GLU A O 53 C CB . GLU A 7 ? 0.1752 0.2366 0.2551 0.0054 -0.0027 0.0237 7 GLU A CB 54 C CG . GLU A 7 ? 0.2026 0.2834 0.3142 0.0235 -0.0049 0.0361 7 GLU A CG 55 C CD . GLU A 7 ? 0.2285 0.3379 0.3783 0.0371 0.0249 0.0656 7 GLU A CD 56 O OE1 . GLU A 7 ? 0.2527 0.4020 0.3832 0.0707 0.0172 0.0949 7 GLU A OE1 57 O OE2 . GLU A 7 ? 0.3261 0.4063 0.4595 0.0581 0.0041 0.0483 7 GLU A OE2 58 N N . ASN A 8 ? 0.1883 0.2443 0.2646 -0.0240 0.0017 0.0195 8 ASN A N 59 C CA . ASN A 8 ? 0.1911 0.2464 0.2679 -0.0226 0.0078 0.0248 8 ASN A CA 60 C C . ASN A 8 ? 0.1929 0.2518 0.2599 -0.0262 0.0050 0.0214 8 ASN A C 61 O O . ASN A 8 ? 0.1938 0.2552 0.2605 -0.0253 0.0078 0.0274 8 ASN A O 62 C CB . ASN A 8 ? 0.1896 0.2487 0.2869 -0.0279 0.0031 0.0211 8 ASN A CB 63 C CG . ASN A 8 ? 0.1889 0.2648 0.3213 -0.0275 0.0132 0.0220 8 ASN A CG 64 O OD1 . ASN A 8 ? 0.1954 0.2679 0.3405 -0.0281 0.0017 0.0178 8 ASN A OD1 65 N ND2 . ASN A 8 ? 0.1889 0.2487 0.3643 -0.0469 0.0052 0.0401 8 ASN A ND2 66 N N . PRO A 9 ? 0.1999 0.2577 0.2544 -0.0235 0.0051 0.0220 9 PRO A N 67 C CA . PRO A 9 ? 0.2124 0.2667 0.2526 -0.0226 0.0021 0.0170 9 PRO A CA 68 C C . PRO A 9 ? 0.2108 0.2683 0.2547 -0.0280 0.0038 0.0127 9 PRO A C 69 O O . PRO A 9 ? 0.2109 0.2639 0.2540 -0.0274 -0.0018 0.0098 9 PRO A O 70 C CB . PRO A 9 ? 0.2209 0.2665 0.2540 -0.0207 -0.0008 0.0162 9 PRO A CB 71 C CG . PRO A 9 ? 0.2245 0.2833 0.2604 -0.0118 -0.0057 0.0185 9 PRO A CG 72 C CD . PRO A 9 ? 0.2008 0.2647 0.2530 -0.0233 0.0060 0.0190 9 PRO A CD 73 N N . ASP A 10 ? 0.2126 0.2749 0.2613 -0.0382 0.0004 0.0097 10 ASP A N 74 C CA . ASP A 10 ? 0.2135 0.2847 0.2674 -0.0389 0.0042 0.0098 10 ASP A CA 75 C C . ASP A 10 ? 0.1941 0.2697 0.2633 -0.0396 -0.0004 0.0059 10 ASP A C 76 O O . ASP A 10 ? 0.1938 0.2662 0.2666 -0.0338 0.0003 0.0150 10 ASP A O 77 C CB . ASP A 10 ? 0.2219 0.2985 0.2770 -0.0546 -0.0031 0.0091 10 ASP A CB 78 C CG . ASP A 10 ? 0.2786 0.3557 0.3338 -0.0563 0.0162 0.0057 10 ASP A CG 79 O OD1 . ASP A 10 ? 0.3512 0.4298 0.4158 -0.0632 -0.0190 -0.0042 10 ASP A OD1 80 O OD2 . ASP A 10 ? 0.3540 0.4077 0.3335 -0.0697 0.0380 -0.0013 10 ASP A OD2 81 N N . PHE A 11 ? 0.1735 0.2424 0.2435 -0.0350 0.0044 -0.0001 11 PHE A N 82 C CA . PHE A 11 ? 0.1721 0.2295 0.2389 -0.0326 0.0060 -0.0028 11 PHE A CA 83 C C . PHE A 11 ? 0.1585 0.2088 0.2230 -0.0297 0.0078 -0.0051 11 PHE A C 84 O O . PHE A 11 ? 0.1470 0.1910 0.2208 -0.0344 0.0173 -0.0036 11 PHE A O 85 C CB . PHE A 11 ? 0.1747 0.2287 0.2272 -0.0288 0.0062 -0.0058 11 PHE A CB 86 C CG . PHE A 11 ? 0.1974 0.2391 0.2363 -0.0300 0.0030 0.0018 11 PHE A CG 87 C CD1 . PHE A 11 ? 0.2338 0.2688 0.2339 -0.0314 -0.0034 -0.0067 11 PHE A CD1 88 C CD2 . PHE A 11 ? 0.2069 0.2300 0.2317 -0.0162 -0.0029 0.0146 11 PHE A CD2 89 C CE1 . PHE A 11 ? 0.2451 0.2838 0.2600 -0.0347 -0.0035 0.0044 11 PHE A CE1 90 C CE2 . PHE A 11 ? 0.2269 0.2272 0.2213 -0.0263 -0.0002 0.0017 11 PHE A CE2 91 C CZ . PHE A 11 ? 0.2240 0.2598 0.2435 -0.0431 -0.0094 0.0046 11 PHE A CZ 92 N N . TRP A 12 ? 0.1625 0.1976 0.2115 -0.0269 0.0086 -0.0052 12 TRP A N 93 C CA . TRP A 12 ? 0.1630 0.1928 0.2083 -0.0273 0.0050 0.0012 12 TRP A CA 94 C C . TRP A 12 ? 0.1750 0.2007 0.2094 -0.0325 0.0027 0.0020 12 TRP A C 95 O O . TRP A 12 ? 0.1811 0.1926 0.2138 -0.0330 -0.0011 0.0076 12 TRP A O 96 C CB . TRP A 12 ? 0.1594 0.1859 0.1995 -0.0218 0.0109 0.0040 12 TRP A CB 97 C CG . TRP A 12 ? 0.1691 0.1806 0.1932 -0.0157 0.0110 0.0053 12 TRP A CG 98 C CD1 . TRP A 12 ? 0.1896 0.1668 0.2020 -0.0147 0.0244 0.0087 12 TRP A CD1 99 C CD2 . TRP A 12 ? 0.1699 0.1730 0.2023 -0.0131 0.0187 0.0095 12 TRP A CD2 100 N NE1 . TRP A 12 ? 0.1995 0.1608 0.1940 -0.0083 0.0153 0.0144 12 TRP A NE1 101 C CE2 . TRP A 12 ? 0.1937 0.1600 0.2042 -0.0232 0.0145 0.0065 12 TRP A CE2 102 C CE3 . TRP A 12 ? 0.1614 0.1805 0.1881 -0.0279 0.0050 -0.0029 12 TRP A CE3 103 C CZ2 . TRP A 12 ? 0.1911 0.1765 0.1996 -0.0185 0.0138 0.0074 12 TRP A CZ2 104 C CZ3 . TRP A 12 ? 0.1850 0.1590 0.1972 -0.0200 0.0278 0.0087 12 TRP A CZ3 105 C CH2 . TRP A 12 ? 0.1767 0.1733 0.2006 -0.0122 0.0181 0.0108 12 TRP A CH2 106 N N . ASN A 13 ? 0.1897 0.2051 0.2006 -0.0356 0.0031 0.0012 13 ASN A N 107 C CA . ASN A 13 ? 0.2024 0.2236 0.2039 -0.0385 0.0000 0.0020 13 ASN A CA 108 C C . ASN A 13 ? 0.2052 0.2271 0.2105 -0.0367 0.0020 0.0013 13 ASN A C 109 O O . ASN A 13 ? 0.2153 0.2372 0.2086 -0.0384 -0.0012 0.0071 13 ASN A O 110 C CB . ASN A 13 ? 0.2099 0.2235 0.2093 -0.0382 -0.0042 -0.0020 13 ASN A CB 111 C CG . ASN A 13 ? 0.2100 0.2486 0.2111 -0.0349 -0.0037 -0.0031 13 ASN A CG 112 O OD1 . ASN A 13 ? 0.2011 0.2417 0.2453 -0.0273 -0.0053 -0.0241 13 ASN A OD1 113 N ND2 . ASN A 13 ? 0.2230 0.2884 0.2119 -0.0293 -0.0176 -0.0048 13 ASN A ND2 114 N N . ARG A 14 ? 0.2095 0.2458 0.2198 -0.0404 0.0072 0.0110 14 ARG A N 115 C CA . ARG A 14 ? 0.2196 0.2620 0.2355 -0.0322 0.0152 0.0147 14 ARG A CA 116 C C . ARG A 14 ? 0.2110 0.2544 0.2267 -0.0328 0.0183 0.0128 14 ARG A C 117 O O . ARG A 14 ? 0.1921 0.2426 0.2257 -0.0302 0.0165 0.0124 14 ARG A O 118 C CB . ARG A 14 ? 0.2258 0.2702 0.2462 -0.0356 0.0224 0.0235 14 ARG A CB 119 C CG . ARG A 14 ? 0.2712 0.3456 0.3158 -0.0288 0.0273 0.0216 14 ARG A CG 120 C CD . ARG A 14 ? 0.3187 0.4600 0.4245 -0.0299 0.0318 0.0554 14 ARG A CD 121 N NE . ARG A 14 ? 0.3823 0.5213 0.4936 -0.0416 0.0344 0.0616 14 ARG A NE 122 C CZ . ARG A 14 ? 0.4025 0.5477 0.5149 -0.0404 0.0437 0.0657 14 ARG A CZ 123 N NH1 . ARG A 14 ? 0.4238 0.5796 0.5308 -0.0332 0.0459 0.0703 14 ARG A NH1 124 N NH2 . ARG A 14 ? 0.4150 0.5631 0.5399 -0.0544 0.0692 0.0553 14 ARG A NH2 125 N N . GLU A 15 ? 0.2116 0.2478 0.2200 -0.0318 0.0218 0.0097 15 GLU A N 126 C CA . GLU A 15 ? 0.2129 0.2520 0.2212 -0.0302 0.0189 0.0073 15 GLU A CA 127 C C . GLU A 15 ? 0.2150 0.2470 0.2179 -0.0318 0.0167 0.0096 15 GLU A C 128 O O . GLU A 15 ? 0.2163 0.2693 0.2060 -0.0335 0.0116 0.0139 15 GLU A O 129 C CB . GLU A 15 ? 0.2165 0.2453 0.2201 -0.0232 0.0162 0.0030 15 GLU A CB 130 C CG . GLU A 15 ? 0.2450 0.2814 0.2626 -0.0209 0.0213 0.0019 15 GLU A CG 131 C CD . GLU A 15 ? 0.2852 0.2900 0.2807 -0.0140 0.0122 -0.0060 15 GLU A CD 132 O OE1 . GLU A 15 ? 0.2925 0.3080 0.2837 -0.0172 -0.0033 0.0037 15 GLU A OE1 133 O OE2 . GLU A 15 ? 0.3218 0.3135 0.2963 -0.0187 0.0305 -0.0276 15 GLU A OE2 134 N N . ALA A 16 ? 0.2100 0.2378 0.2113 -0.0357 0.0186 0.0085 16 ALA A N 135 C CA . ALA A 16 ? 0.2052 0.2300 0.2150 -0.0335 0.0199 0.0072 16 ALA A CA 136 C C . ALA A 16 ? 0.2031 0.2283 0.2196 -0.0367 0.0193 0.0068 16 ALA A C 137 O O . ALA A 16 ? 0.1990 0.2183 0.2143 -0.0369 0.0224 0.0029 16 ALA A O 138 C CB . ALA A 16 ? 0.2053 0.2337 0.2112 -0.0315 0.0231 0.0082 16 ALA A CB 139 N N . ALA A 17 ? 0.2065 0.2239 0.2312 -0.0396 0.0156 0.0062 17 ALA A N 140 C CA . ALA A 17 ? 0.2043 0.2191 0.2469 -0.0404 0.0128 0.0111 17 ALA A CA 141 C C . ALA A 17 ? 0.2062 0.2254 0.2609 -0.0420 0.0145 0.0098 17 ALA A C 142 O O . ALA A 17 ? 0.2179 0.2116 0.2645 -0.0400 0.0068 0.0215 17 ALA A O 143 C CB . ALA A 17 ? 0.2031 0.2170 0.2553 -0.0421 0.0108 0.0051 17 ALA A CB 144 N N . GLU A 18 ? 0.1980 0.2247 0.2639 -0.0412 0.0186 0.0105 18 GLU A N 145 C CA . GLU A 18 ? 0.2075 0.2425 0.2707 -0.0373 0.0261 0.0129 18 GLU A CA 146 C C . GLU A 18 ? 0.1975 0.2332 0.2510 -0.0387 0.0297 0.0177 18 GLU A C 147 O O . GLU A 18 ? 0.1811 0.2343 0.2426 -0.0431 0.0348 0.0310 18 GLU A O 148 C CB . GLU A 18 ? 0.2124 0.2521 0.2864 -0.0381 0.0314 0.0126 18 GLU A CB 149 C CG . GLU A 18 ? 0.2637 0.3251 0.3660 -0.0290 0.0264 -0.0083 18 GLU A CG 150 C CD . GLU A 18 ? 0.3479 0.4008 0.4798 -0.0371 0.0270 -0.0352 18 GLU A CD 151 O OE1 . GLU A 18 ? 0.3992 0.4811 0.5150 -0.0280 0.0305 -0.0292 18 GLU A OE1 152 O OE2 . GLU A 18 ? 0.3833 0.4427 0.5053 -0.0444 0.0350 -0.0457 18 GLU A OE2 153 N N . ALA A 19 ? 0.1987 0.2173 0.2345 -0.0380 0.0237 0.0165 19 ALA A N 154 C CA . ALA A 19 ? 0.2022 0.2191 0.2217 -0.0356 0.0251 0.0155 19 ALA A CA 155 C C . ALA A 19 ? 0.2091 0.2187 0.2236 -0.0392 0.0205 0.0188 19 ALA A C 156 O O . ALA A 19 ? 0.2191 0.2325 0.2163 -0.0335 0.0156 0.0100 19 ALA A O 157 C CB . ALA A 19 ? 0.1926 0.2072 0.2285 -0.0359 0.0201 0.0125 19 ALA A CB 158 N N . LEU A 20 ? 0.2126 0.2145 0.2032 -0.0407 0.0237 0.0201 20 LEU A N 159 C CA . LEU A 20 ? 0.2312 0.2245 0.2121 -0.0423 0.0150 0.0227 20 LEU A CA 160 C C . LEU A 20 ? 0.2320 0.2215 0.2146 -0.0400 0.0123 0.0186 20 LEU A C 161 O O . LEU A 20 ? 0.2283 0.2122 0.2162 -0.0431 0.0084 0.0138 20 LEU A O 162 C CB . LEU A 20 ? 0.2361 0.2294 0.2073 -0.0388 0.0152 0.0297 20 LEU A CB 163 C CG . LEU A 20 ? 0.2260 0.2612 0.2129 -0.0366 0.0220 0.0291 20 LEU A CG 164 C CD1 . LEU A 20 ? 0.2524 0.2701 0.1469 -0.0271 0.0158 0.0486 20 LEU A CD1 165 C CD2 . LEU A 20 ? 0.2411 0.2689 0.2350 -0.0227 0.0263 0.0306 20 LEU A CD2 166 N N . GLY A 21 ? 0.2312 0.2238 0.2152 -0.0397 0.0131 0.0164 21 GLY A N 167 C CA . GLY A 21 ? 0.2321 0.2238 0.2236 -0.0330 0.0142 0.0150 21 GLY A CA 168 C C . GLY A 21 ? 0.2269 0.2265 0.2387 -0.0295 0.0134 0.0156 21 GLY A C 169 O O . GLY A 21 ? 0.2342 0.2268 0.2566 -0.0285 0.0126 0.0194 21 GLY A O 170 N N . ALA A 22 ? 0.2210 0.2227 0.2320 -0.0303 0.0137 0.0104 22 ALA A N 171 C CA . ALA A 22 ? 0.2221 0.2286 0.2348 -0.0277 0.0089 0.0063 22 ALA A CA 172 C C . ALA A 22 ? 0.2327 0.2345 0.2360 -0.0219 0.0069 0.0059 22 ALA A C 173 O O . ALA A 22 ? 0.2419 0.2483 0.2438 -0.0177 0.0063 0.0059 22 ALA A O 174 C CB . ALA A 22 ? 0.2238 0.2340 0.2275 -0.0266 0.0100 0.0029 22 ALA A CB 175 N N . ALA A 23 ? 0.2275 0.2333 0.2363 -0.0271 0.0100 0.0030 23 ALA A N 176 C CA . ALA A 23 ? 0.2328 0.2320 0.2424 -0.0292 0.0051 0.0038 23 ALA A CA 177 C C . ALA A 23 ? 0.2398 0.2381 0.2435 -0.0283 0.0047 0.0081 23 ALA A C 178 O O . ALA A 23 ? 0.2446 0.2366 0.2397 -0.0273 -0.0005 0.0167 23 ALA A O 179 C CB . ALA A 23 ? 0.2215 0.2202 0.2262 -0.0361 0.0074 0.0037 23 ALA A CB 180 N N . LYS A 24 ? 0.2532 0.2398 0.2565 -0.0287 0.0001 0.0056 24 LYS A N 181 C CA . LYS A 24 ? 0.2722 0.2571 0.2873 -0.0240 -0.0093 0.0010 24 LYS A CA 182 C C . LYS A 24 ? 0.2837 0.2637 0.3092 -0.0230 -0.0110 0.0031 24 LYS A C 183 O O . LYS A 24 ? 0.2912 0.2664 0.3292 -0.0175 -0.0203 0.0019 24 LYS A O 184 C CB . LYS A 24 ? 0.2741 0.2512 0.2814 -0.0205 -0.0099 -0.0084 24 LYS A CB 185 C CG . LYS A 24 ? 0.2993 0.2833 0.3042 -0.0307 -0.0292 -0.0098 24 LYS A CG 186 C CD . LYS A 24 ? 0.3625 0.3581 0.3340 -0.0497 -0.0462 -0.0286 24 LYS A CD 187 C CE . LYS A 24 ? 0.3997 0.4244 0.3655 -0.0539 -0.0671 -0.0234 24 LYS A CE 188 N NZ . LYS A 24 ? 0.4366 0.4959 0.4372 -0.0519 -0.0655 -0.0303 24 LYS A NZ 189 N N . LYS A 25 ? 0.2952 0.2747 0.3176 -0.0221 -0.0062 0.0057 25 LYS A N 190 C CA . LYS A 25 ? 0.3134 0.2854 0.3401 -0.0228 -0.0048 0.0137 25 LYS A CA 191 C C . LYS A 25 ? 0.3202 0.2811 0.3347 -0.0167 -0.0007 0.0179 25 LYS A C 192 O O . LYS A 25 ? 0.3316 0.2839 0.3394 -0.0258 0.0034 0.0287 25 LYS A O 193 C CB . LYS A 25 ? 0.3230 0.2959 0.3488 -0.0252 -0.0010 0.0136 25 LYS A CB 194 C CG . LYS A 25 ? 0.3551 0.3499 0.4009 -0.0220 -0.0049 0.0135 25 LYS A CG 195 C CD . LYS A 25 ? 0.4447 0.4497 0.4737 -0.0339 -0.0063 0.0132 25 LYS A CD 196 C CE . LYS A 25 ? 0.4820 0.5110 0.5011 -0.0346 -0.0264 0.0114 25 LYS A CE 197 N NZ . LYS A 25 ? 0.5466 0.5568 0.5470 -0.0310 -0.0212 0.0088 25 LYS A NZ 198 N N . LEU A 26 ? 0.3116 0.2571 0.3316 -0.0191 -0.0018 0.0173 26 LEU A N 199 C CA . LEU A 26 ? 0.3197 0.2595 0.3342 -0.0129 0.0000 0.0184 26 LEU A CA 200 C C . LEU A 26 ? 0.3335 0.2671 0.3453 -0.0159 -0.0060 0.0148 26 LEU A C 201 O O . LEU A 26 ? 0.3238 0.2574 0.3494 -0.0060 -0.0081 0.0115 26 LEU A O 202 C CB . LEU A 26 ? 0.3114 0.2438 0.3233 -0.0169 0.0015 0.0230 26 LEU A CB 203 C CG . LEU A 26 ? 0.2966 0.2297 0.2995 -0.0081 0.0130 0.0289 26 LEU A CG 204 C CD1 . LEU A 26 ? 0.2864 0.2133 0.2537 0.0042 0.0184 0.0501 26 LEU A CD1 205 C CD2 . LEU A 26 ? 0.3029 0.2140 0.2728 0.0032 0.0113 0.0461 26 LEU A CD2 206 N N . GLN A 27 ? 0.3523 0.2840 0.3563 -0.0169 -0.0118 0.0114 27 GLN A N 207 C CA . GLN A 27 ? 0.3824 0.3122 0.3688 -0.0179 -0.0139 0.0034 27 GLN A CA 208 C C . GLN A 27 ? 0.3806 0.3144 0.3608 -0.0161 -0.0177 -0.0015 27 GLN A C 209 O O . GLN A 27 ? 0.3878 0.3253 0.3617 -0.0175 -0.0268 -0.0011 27 GLN A O 210 C CB . GLN A 27 ? 0.3924 0.3187 0.3772 -0.0193 -0.0168 -0.0016 27 GLN A CB 211 C CG . GLN A 27 ? 0.4533 0.3706 0.4249 -0.0287 -0.0189 0.0026 27 GLN A CG 212 C CD . GLN A 27 ? 0.5482 0.4439 0.4692 -0.0342 -0.0179 -0.0108 27 GLN A CD 213 O OE1 . GLN A 27 ? 0.5825 0.4837 0.4862 -0.0454 -0.0094 -0.0077 27 GLN A OE1 214 N NE2 . GLN A 27 ? 0.5869 0.4833 0.4909 -0.0306 -0.0238 -0.0162 27 GLN A NE2 215 N N . PRO A 28 ? 0.3947 0.3213 0.3584 -0.0191 -0.0151 -0.0041 28 PRO A N 216 C CA . PRO A 28 ? 0.3935 0.3176 0.3528 -0.0156 -0.0187 -0.0056 28 PRO A CA 217 C C . PRO A 28 ? 0.3979 0.3099 0.3500 -0.0100 -0.0218 -0.0064 28 PRO A C 218 O O . PRO A 28 ? 0.4051 0.3079 0.3563 -0.0156 -0.0250 -0.0038 28 PRO A O 219 C CB . PRO A 28 ? 0.3989 0.3211 0.3539 -0.0187 -0.0179 -0.0096 28 PRO A CB 220 C CG . PRO A 28 ? 0.4040 0.3351 0.3635 -0.0181 -0.0129 -0.0086 28 PRO A CG 221 C CD . PRO A 28 ? 0.3915 0.3282 0.3620 -0.0195 -0.0160 -0.0063 28 PRO A CD 222 N N . ALA A 29 ? 0.3907 0.3012 0.3425 -0.0037 -0.0257 -0.0067 29 ALA A N 223 C CA . ALA A 29 ? 0.3849 0.2835 0.3331 0.0082 -0.0265 -0.0054 29 ALA A CA 224 C C . ALA A 29 ? 0.3824 0.2782 0.3323 0.0122 -0.0282 -0.0085 29 ALA A C 225 O O . ALA A 29 ? 0.3692 0.2519 0.3139 0.0185 -0.0287 -0.0072 29 ALA A O 226 C CB . ALA A 29 ? 0.3834 0.2794 0.3293 0.0079 -0.0250 -0.0069 29 ALA A CB 227 N N . GLN A 30 ? 0.3847 0.2781 0.3382 0.0169 -0.0327 -0.0091 30 GLN A N 228 C CA . GLN A 30 ? 0.3920 0.2811 0.3482 0.0219 -0.0269 -0.0153 30 GLN A CA 229 C C . GLN A 30 ? 0.3698 0.2752 0.3382 0.0274 -0.0230 -0.0117 30 GLN A C 230 O O . GLN A 30 ? 0.3894 0.2917 0.3433 0.0320 -0.0215 -0.0188 30 GLN A O 231 C CB . GLN A 30 ? 0.4104 0.2957 0.3623 0.0213 -0.0318 -0.0128 30 GLN A CB 232 C CG . GLN A 30 ? 0.4741 0.3252 0.4020 0.0153 -0.0412 -0.0205 30 GLN A CG 233 C CD . GLN A 30 ? 0.5494 0.4195 0.4566 0.0271 -0.0494 -0.0048 30 GLN A CD 234 O OE1 . GLN A 30 ? 0.5994 0.4465 0.5076 0.0212 -0.0476 0.0049 30 GLN A OE1 235 N NE2 . GLN A 30 ? 0.5811 0.4583 0.4851 0.0124 -0.0449 -0.0122 30 GLN A NE2 236 N N . THR A 31 ? 0.3455 0.2589 0.3222 0.0220 -0.0171 -0.0066 31 THR A N 237 C CA . THR A 31 ? 0.3147 0.2285 0.2996 0.0200 -0.0079 0.0076 31 THR A CA 238 C C . THR A 31 ? 0.2939 0.2143 0.2800 0.0190 -0.0070 0.0084 31 THR A C 239 O O . THR A 31 ? 0.2933 0.1877 0.2672 0.0288 -0.0030 0.0030 31 THR A O 240 C CB . THR A 31 ? 0.3117 0.2271 0.3074 0.0193 -0.0083 0.0092 31 THR A CB 241 O OG1 . THR A 31 ? 0.3151 0.2564 0.3146 0.0032 0.0087 0.0335 31 THR A OG1 242 C CG2 . THR A 31 ? 0.3137 0.2417 0.3117 0.0055 -0.0066 0.0184 31 THR A CG2 243 N N . ALA A 32 ? 0.2772 0.1914 0.2581 0.0171 -0.0047 0.0162 32 ALA A N 244 C CA . ALA A 32 ? 0.2587 0.1825 0.2453 0.0135 -0.0081 0.0207 32 ALA A CA 245 C C . ALA A 32 ? 0.2524 0.1786 0.2373 0.0113 -0.0087 0.0218 32 ALA A C 246 O O . ALA A 32 ? 0.2486 0.1710 0.2491 0.0158 -0.0151 0.0171 32 ALA A O 247 C CB . ALA A 32 ? 0.2586 0.1739 0.2475 0.0123 -0.0126 0.0264 32 ALA A CB 248 N N . ALA A 33 ? 0.2384 0.1658 0.2232 0.0068 -0.0076 0.0291 33 ALA A N 249 C CA . ALA A 33 ? 0.2310 0.1744 0.2131 0.0005 -0.0015 0.0310 33 ALA A CA 250 C C . ALA A 33 ? 0.2325 0.1812 0.2118 -0.0050 0.0025 0.0269 33 ALA A C 251 O O . ALA A 33 ? 0.2314 0.1937 0.2061 -0.0024 0.0003 0.0329 33 ALA A O 252 C CB . ALA A 33 ? 0.2186 0.1583 0.2265 0.0071 -0.0004 0.0339 33 ALA A CB 253 N N . LYS A 34 ? 0.2326 0.1815 0.1922 -0.0126 0.0106 0.0265 34 LYS A N 254 C CA . LYS A 34 ? 0.2309 0.1792 0.1927 -0.0188 0.0147 0.0258 34 LYS A CA 255 C C . LYS A 34 ? 0.2178 0.1653 0.1885 -0.0169 0.0152 0.0277 34 LYS A C 256 O O . LYS A 34 ? 0.2255 0.1560 0.1907 -0.0199 0.0127 0.0256 34 LYS A O 257 C CB . LYS A 34 ? 0.2258 0.1860 0.1884 -0.0261 0.0179 0.0255 34 LYS A CB 258 C CG . LYS A 34 ? 0.2468 0.2039 0.1900 -0.0354 0.0316 0.0278 34 LYS A CG 259 C CD . LYS A 34 ? 0.2358 0.2337 0.2171 -0.0329 0.0471 0.0419 34 LYS A CD 260 C CE . LYS A 34 ? 0.2523 0.2479 0.2218 -0.0291 0.0551 0.0369 34 LYS A CE 261 N NZ . LYS A 34 ? 0.2390 0.2278 0.2683 -0.0525 0.0513 0.0452 34 LYS A NZ 262 N N . ASN A 35 ? 0.2098 0.1584 0.1833 -0.0133 0.0202 0.0348 35 ASN A N 263 C CA . ASN A 35 ? 0.1978 0.1550 0.1774 -0.0077 0.0196 0.0306 35 ASN A CA 264 C C . ASN A 35 ? 0.1877 0.1523 0.1690 -0.0076 0.0194 0.0299 35 ASN A C 265 O O . ASN A 35 ? 0.2003 0.1592 0.1808 -0.0072 0.0257 0.0313 35 ASN A O 266 C CB . ASN A 35 ? 0.1867 0.1587 0.1758 -0.0095 0.0200 0.0325 35 ASN A CB 267 C CG . ASN A 35 ? 0.1841 0.1492 0.1877 -0.0097 0.0082 0.0339 35 ASN A CG 268 O OD1 . ASN A 35 ? 0.1829 0.1341 0.1815 -0.0090 0.0072 0.0477 35 ASN A OD1 269 N ND2 . ASN A 35 ? 0.1682 0.2022 0.2129 -0.0058 -0.0065 0.0450 35 ASN A ND2 270 N N . LEU A 36 ? 0.1763 0.1470 0.1625 -0.0013 0.0139 0.0257 36 LEU A N 271 C CA . LEU A 36 ? 0.1615 0.1441 0.1775 0.0048 0.0144 0.0146 36 LEU A CA 272 C C . LEU A 36 ? 0.1633 0.1510 0.1807 0.0009 0.0113 0.0242 36 LEU A C 273 O O . LEU A 36 ? 0.1670 0.1540 0.1844 0.0026 0.0096 0.0230 36 LEU A O 274 C CB . LEU A 36 ? 0.1486 0.1335 0.1749 0.0008 0.0141 0.0065 36 LEU A CB 275 C CG . LEU A 36 ? 0.1364 0.1482 0.1778 0.0234 0.0079 -0.0055 36 LEU A CG 276 C CD1 . LEU A 36 ? 0.1193 0.1404 0.2060 0.0195 0.0019 -0.0277 36 LEU A CD1 277 C CD2 . LEU A 36 ? 0.1544 0.1545 0.1809 0.0317 0.0043 -0.0384 36 LEU A CD2 278 N N . ILE A 37 ? 0.1614 0.1590 0.1879 0.0024 0.0093 0.0285 37 ILE A N 279 C CA . ILE A 37 ? 0.1560 0.1523 0.1792 0.0008 0.0141 0.0314 37 ILE A CA 280 C C . ILE A 37 ? 0.1626 0.1564 0.1761 0.0015 0.0135 0.0296 37 ILE A C 281 O O . ILE A 37 ? 0.1719 0.1619 0.1773 0.0068 0.0121 0.0399 37 ILE A O 282 C CB . ILE A 37 ? 0.1544 0.1543 0.1779 0.0034 0.0187 0.0304 37 ILE A CB 283 C CG1 . ILE A 37 ? 0.1478 0.1465 0.1669 -0.0079 0.0240 0.0361 37 ILE A CG1 284 C CG2 . ILE A 37 ? 0.1501 0.1432 0.1838 0.0018 0.0049 0.0262 37 ILE A CG2 285 C CD1 . ILE A 37 ? 0.1398 0.1639 0.1794 0.0008 0.0125 0.0390 37 ILE A CD1 286 N N . ILE A 38 ? 0.1665 0.1476 0.1720 0.0069 0.0146 0.0238 38 ILE A N 287 C CA . ILE A 38 ? 0.1681 0.1430 0.1860 0.0068 0.0068 0.0213 38 ILE A CA 288 C C . ILE A 38 ? 0.1661 0.1448 0.1831 0.0098 0.0012 0.0129 38 ILE A C 289 O O . ILE A 38 ? 0.1682 0.1365 0.1865 0.0101 -0.0110 0.0092 38 ILE A O 290 C CB . ILE A 38 ? 0.1742 0.1543 0.1858 0.0098 0.0109 0.0193 38 ILE A CB 291 C CG1 . ILE A 38 ? 0.1770 0.1324 0.2124 0.0017 0.0282 0.0320 38 ILE A CG1 292 C CG2 . ILE A 38 ? 0.1696 0.1541 0.1954 0.0039 0.0029 0.0239 38 ILE A CG2 293 C CD1 . ILE A 38 ? 0.2233 0.2113 0.2494 0.0052 0.0298 0.0349 38 ILE A CD1 294 N N . PHE A 39 ? 0.1545 0.1406 0.1731 0.0059 -0.0075 0.0137 39 PHE A N 295 C CA . PHE A 39 ? 0.1519 0.1423 0.1707 -0.0030 -0.0050 0.0201 39 PHE A CA 296 C C . PHE A 39 ? 0.1489 0.1446 0.1685 -0.0044 -0.0018 0.0194 39 PHE A C 297 O O . PHE A 39 ? 0.1671 0.1496 0.1579 -0.0104 0.0012 0.0239 39 PHE A O 298 C CB . PHE A 39 ? 0.1521 0.1496 0.1773 -0.0061 -0.0066 0.0221 39 PHE A CB 299 C CG . PHE A 39 ? 0.1473 0.1649 0.1695 -0.0130 -0.0080 0.0158 39 PHE A CG 300 C CD1 . PHE A 39 ? 0.1710 0.1487 0.1720 -0.0172 -0.0131 0.0214 39 PHE A CD1 301 C CD2 . PHE A 39 ? 0.1340 0.1819 0.1704 -0.0029 -0.0087 0.0152 39 PHE A CD2 302 C CE1 . PHE A 39 ? 0.1762 0.1803 0.1674 -0.0110 0.0042 0.0272 39 PHE A CE1 303 C CE2 . PHE A 39 ? 0.1443 0.1462 0.1626 -0.0095 -0.0087 0.0394 39 PHE A CE2 304 C CZ . PHE A 39 ? 0.1510 0.1822 0.1697 -0.0044 0.0092 0.0211 39 PHE A CZ 305 N N . LEU A 40 ? 0.1436 0.1243 0.1639 -0.0075 -0.0002 0.0146 40 LEU A N 306 C CA . LEU A 40 ? 0.1437 0.1279 0.1639 -0.0045 0.0013 0.0152 40 LEU A CA 307 C C . LEU A 40 ? 0.1408 0.1239 0.1628 -0.0083 0.0001 0.0145 40 LEU A C 308 O O . LEU A 40 ? 0.1453 0.1189 0.1478 -0.0101 -0.0034 0.0169 40 LEU A O 309 C CB . LEU A 40 ? 0.1419 0.1236 0.1721 -0.0022 0.0052 0.0156 40 LEU A CB 310 C CG . LEU A 40 ? 0.1430 0.1362 0.1936 0.0031 0.0076 0.0152 40 LEU A CG 311 C CD1 . LEU A 40 ? 0.1226 0.1092 0.2266 0.0087 0.0197 0.0314 40 LEU A CD1 312 C CD2 . LEU A 40 ? 0.1565 0.1596 0.1914 0.0126 0.0139 -0.0182 40 LEU A CD2 313 N N . GLY A 41 ? 0.1445 0.1237 0.1557 -0.0074 0.0015 0.0147 41 GLY A N 314 C CA . GLY A 41 ? 0.1443 0.1214 0.1544 -0.0015 0.0031 0.0079 41 GLY A CA 315 C C . GLY A 41 ? 0.1500 0.1278 0.1457 -0.0006 -0.0044 0.0028 41 GLY A C 316 O O . GLY A 41 ? 0.1619 0.1333 0.1519 -0.0032 -0.0070 0.0030 41 GLY A O 317 N N . ASP A 42 ? 0.1467 0.1304 0.1439 0.0011 -0.0045 -0.0019 42 ASP A N 318 C CA . ASP A 42 ? 0.1492 0.1329 0.1270 -0.0061 -0.0025 0.0003 42 ASP A CA 319 C C . ASP A 42 ? 0.1419 0.1309 0.1194 -0.0017 0.0003 0.0032 42 ASP A C 320 O O . ASP A 42 ? 0.1409 0.1347 0.1115 -0.0013 0.0140 0.0132 42 ASP A O 321 C CB . ASP A 42 ? 0.1493 0.1428 0.1370 -0.0038 -0.0131 0.0010 42 ASP A CB 322 C CG . ASP A 42 ? 0.1476 0.1180 0.1370 -0.0053 -0.0118 0.0072 42 ASP A CG 323 O OD1 . ASP A 42 ? 0.1458 0.0878 0.1968 0.0000 -0.0293 0.0229 42 ASP A OD1 324 O OD2 . ASP A 42 ? 0.1699 0.0988 0.1817 0.0149 -0.0200 0.0531 42 ASP A OD2 325 N N . GLY A 43 ? 0.1472 0.1382 0.1208 -0.0015 -0.0026 0.0045 43 GLY A N 326 C CA . GLY A 43 ? 0.1414 0.1404 0.1213 0.0060 -0.0027 0.0023 43 GLY A CA 327 C C . GLY A 43 ? 0.1367 0.1418 0.1255 0.0052 -0.0006 -0.0016 43 GLY A C 328 O O . GLY A 43 ? 0.1394 0.1470 0.1435 0.0152 -0.0134 0.0017 43 GLY A O 329 N N . MET A 44 ? 0.1238 0.1381 0.1271 -0.0020 0.0038 -0.0062 44 MET A N 330 C CA . MET A 44 ? 0.1343 0.1502 0.1399 -0.0024 0.0073 -0.0014 44 MET A CA 331 C C . MET A 44 ? 0.1351 0.1450 0.1443 0.0000 0.0010 -0.0046 44 MET A C 332 O O . MET A 44 ? 0.1288 0.1543 0.1562 -0.0016 0.0027 -0.0034 44 MET A O 333 C CB . MET A 44 ? 0.1287 0.1412 0.1387 -0.0098 0.0070 -0.0015 44 MET A CB 334 C CG . MET A 44 ? 0.1211 0.1637 0.1546 -0.0107 0.0048 0.0047 44 MET A CG 335 S SD . MET A 44 ? 0.1508 0.1562 0.1579 -0.0049 0.0044 -0.0015 44 MET A SD 336 C CE . MET A 44 ? 0.1368 0.1211 0.1663 0.0143 -0.0038 -0.0260 44 MET A CE 337 N N . GLY A 45 ? 0.1344 0.1515 0.1313 0.0012 0.0082 -0.0042 45 GLY A N 338 C CA . GLY A 45 ? 0.1401 0.1364 0.1356 0.0060 -0.0061 -0.0144 45 GLY A CA 339 C C . GLY A 45 ? 0.1414 0.1349 0.1375 0.0073 -0.0042 -0.0187 45 GLY A C 340 O O . GLY A 45 ? 0.1385 0.1133 0.1310 0.0114 -0.0050 -0.0265 45 GLY A O 341 N N . VAL A 46 ? 0.1395 0.1365 0.1322 0.0132 -0.0143 -0.0295 46 VAL A N 342 C CA . VAL A 46 ? 0.1420 0.1471 0.1396 0.0075 -0.0150 -0.0303 46 VAL A CA 343 C C . VAL A 46 ? 0.1442 0.1438 0.1352 0.0063 -0.0141 -0.0232 46 VAL A C 344 O O . VAL A 46 ? 0.1309 0.1358 0.1264 -0.0057 -0.0055 -0.0273 46 VAL A O 345 C CB . VAL A 46 ? 0.1451 0.1559 0.1429 0.0132 -0.0235 -0.0409 46 VAL A CB 346 C CG1 . VAL A 46 ? 0.1401 0.1816 0.1622 -0.0161 -0.0377 -0.0395 46 VAL A CG1 347 C CG2 . VAL A 46 ? 0.1334 0.1436 0.1461 0.0189 -0.0315 -0.0323 46 VAL A CG2 348 N N . SER A 47 ? 0.1455 0.1319 0.1318 0.0018 -0.0137 -0.0123 47 SER A N 349 C CA . SER A 47 ? 0.1562 0.1340 0.1390 -0.0043 -0.0043 -0.0123 47 SER A CA 350 C C . SER A 47 ? 0.1540 0.1291 0.1411 0.0000 -0.0086 -0.0139 47 SER A C 351 O O . SER A 47 ? 0.1568 0.1367 0.1407 0.0019 -0.0099 -0.0121 47 SER A O 352 C CB . SER A 47 ? 0.1567 0.1181 0.1385 -0.0087 -0.0182 -0.0135 47 SER A CB 353 O OG . SER A 47 ? 0.1716 0.1579 0.1913 -0.0162 0.0133 -0.0059 47 SER A OG 354 N N . THR A 48 ? 0.1494 0.1228 0.1218 0.0026 -0.0087 -0.0066 48 THR A N 355 C CA . THR A 48 ? 0.1496 0.1340 0.1288 -0.0028 -0.0131 -0.0049 48 THR A CA 356 C C . THR A 48 ? 0.1449 0.1345 0.1312 -0.0036 -0.0117 -0.0053 48 THR A C 357 O O . THR A 48 ? 0.1592 0.1509 0.1202 -0.0008 -0.0085 -0.0062 48 THR A O 358 C CB . THR A 48 ? 0.1464 0.1293 0.1210 -0.0021 -0.0120 -0.0008 48 THR A CB 359 O OG1 . THR A 48 ? 0.1295 0.1308 0.1314 0.0019 -0.0139 -0.0146 48 THR A OG1 360 C CG2 . THR A 48 ? 0.1422 0.1365 0.1036 0.0052 -0.0115 -0.0017 48 THR A CG2 361 N N . VAL A 49 ? 0.1317 0.1230 0.1332 -0.0078 -0.0119 -0.0056 49 VAL A N 362 C CA . VAL A 49 ? 0.1349 0.1176 0.1477 -0.0044 -0.0127 -0.0037 49 VAL A CA 363 C C . VAL A 49 ? 0.1366 0.1154 0.1473 -0.0030 -0.0086 -0.0052 49 VAL A C 364 O O . VAL A 49 ? 0.1240 0.1119 0.1406 0.0030 -0.0030 0.0021 49 VAL A O 365 C CB . VAL A 49 ? 0.1331 0.1102 0.1478 -0.0099 -0.0162 -0.0038 49 VAL A CB 366 C CG1 . VAL A 49 ? 0.1297 0.1099 0.1943 -0.0115 -0.0106 0.0056 49 VAL A CG1 367 C CG2 . VAL A 49 ? 0.1075 0.1231 0.1758 -0.0134 -0.0175 -0.0088 49 VAL A CG2 368 N N . THR A 50 ? 0.1364 0.1196 0.1468 0.0020 -0.0020 -0.0062 50 THR A N 369 C CA . THR A 50 ? 0.1384 0.1357 0.1508 0.0022 0.0026 -0.0075 50 THR A CA 370 C C . THR A 50 ? 0.1453 0.1359 0.1487 -0.0016 0.0027 -0.0103 50 THR A C 371 O O . THR A 50 ? 0.1447 0.1401 0.1450 -0.0083 0.0094 -0.0152 50 THR A O 372 C CB . THR A 50 ? 0.1365 0.1335 0.1501 0.0031 0.0037 -0.0100 50 THR A CB 373 O OG1 . THR A 50 ? 0.1405 0.1420 0.1791 0.0149 0.0341 -0.0029 50 THR A OG1 374 C CG2 . THR A 50 ? 0.1294 0.1686 0.1381 0.0063 0.0166 0.0010 50 THR A CG2 375 N N . ALA A 51 ? 0.1507 0.1299 0.1470 -0.0046 0.0007 -0.0104 51 ALA A N 376 C CA . ALA A 51 ? 0.1498 0.1398 0.1501 -0.0027 0.0035 -0.0059 51 ALA A CA 377 C C . ALA A 51 ? 0.1537 0.1419 0.1557 -0.0045 0.0025 -0.0012 51 ALA A C 378 O O . ALA A 51 ? 0.1479 0.1509 0.1521 -0.0034 0.0135 0.0088 51 ALA A O 379 C CB . ALA A 51 ? 0.1453 0.1134 0.1521 -0.0077 0.0067 -0.0086 51 ALA A CB 380 N N . ALA A 52 ? 0.1631 0.1429 0.1491 0.0004 -0.0024 0.0007 52 ALA A N 381 C CA . ALA A 52 ? 0.1671 0.1611 0.1650 0.0029 -0.0064 0.0003 52 ALA A CA 382 C C . ALA A 52 ? 0.1697 0.1732 0.1653 0.0063 -0.0083 -0.0024 52 ALA A C 383 O O . ALA A 52 ? 0.1764 0.1860 0.1805 0.0000 -0.0063 -0.0063 52 ALA A O 384 C CB . ALA A 52 ? 0.1631 0.1671 0.1555 0.0083 -0.0144 0.0082 52 ALA A CB 385 N N . ARG A 53 ? 0.1709 0.1655 0.1637 0.0081 -0.0142 -0.0033 53 ARG A N 386 C CA . ARG A 53 ? 0.1657 0.1711 0.1652 0.0120 -0.0057 -0.0082 53 ARG A CA 387 C C . ARG A 53 ? 0.1659 0.1712 0.1643 0.0151 -0.0007 -0.0064 53 ARG A C 388 O O . ARG A 53 ? 0.1537 0.1732 0.1799 0.0210 -0.0063 -0.0039 53 ARG A O 389 C CB . ARG A 53 ? 0.1539 0.1579 0.1556 0.0121 -0.0059 -0.0128 53 ARG A CB 390 C CG . ARG A 53 ? 0.1551 0.1729 0.1557 0.0292 0.0050 -0.0315 53 ARG A CG 391 C CD . ARG A 53 ? 0.1591 0.1900 0.1530 0.0321 0.0065 -0.0332 53 ARG A CD 392 N NE . ARG A 53 ? 0.1414 0.1478 0.1878 0.0119 -0.0158 -0.0306 53 ARG A NE 393 C CZ . ARG A 53 ? 0.1579 0.1685 0.2178 0.0100 -0.0172 -0.0276 53 ARG A CZ 394 N NH1 . ARG A 53 ? 0.1219 0.1598 0.2237 -0.0012 -0.0471 -0.0290 53 ARG A NH1 395 N NH2 . ARG A 53 ? 0.1613 0.1751 0.2172 0.0067 -0.0234 -0.0380 53 ARG A NH2 396 N N . ILE A 54 ? 0.1727 0.1742 0.1577 0.0140 0.0040 -0.0092 54 ILE A N 397 C CA . ILE A 54 ? 0.1705 0.1786 0.1600 0.0111 0.0109 -0.0058 54 ILE A CA 398 C C . ILE A 54 ? 0.1719 0.1794 0.1697 0.0049 0.0079 -0.0055 54 ILE A C 399 O O . ILE A 54 ? 0.1619 0.1939 0.1616 -0.0040 0.0088 -0.0110 54 ILE A O 400 C CB . ILE A 54 ? 0.1697 0.1760 0.1642 0.0111 0.0051 -0.0058 54 ILE A CB 401 C CG1 . ILE A 54 ? 0.1751 0.1902 0.1616 0.0229 0.0290 0.0045 54 ILE A CG1 402 C CG2 . ILE A 54 ? 0.1706 0.1656 0.1937 0.0143 0.0158 -0.0110 54 ILE A CG2 403 C CD1 . ILE A 54 ? 0.1818 0.1724 0.1590 0.0086 0.0254 0.0100 54 ILE A CD1 404 N N . LEU A 55 ? 0.1727 0.1828 0.1671 -0.0028 0.0060 -0.0067 55 LEU A N 405 C CA . LEU A 55 ? 0.1745 0.1971 0.1923 -0.0021 0.0128 -0.0184 55 LEU A CA 406 C C . LEU A 55 ? 0.1858 0.2069 0.2021 -0.0050 0.0156 -0.0114 55 LEU A C 407 O O . LEU A 55 ? 0.1835 0.1987 0.2306 0.0027 0.0240 -0.0176 55 LEU A O 408 C CB . LEU A 55 ? 0.1821 0.1870 0.1810 -0.0061 0.0088 -0.0191 55 LEU A CB 409 C CG . LEU A 55 ? 0.1719 0.1937 0.1885 -0.0089 0.0088 -0.0264 55 LEU A CG 410 C CD1 . LEU A 55 ? 0.1811 0.1945 0.1660 -0.0008 -0.0154 0.0007 55 LEU A CD1 411 C CD2 . LEU A 55 ? 0.1721 0.2053 0.1902 -0.0081 0.0090 -0.0367 55 LEU A CD2 412 N N . LYS A 56 ? 0.1966 0.2421 0.2201 -0.0046 0.0160 -0.0002 56 LYS A N 413 C CA . LYS A 56 ? 0.2248 0.2659 0.2459 -0.0060 0.0196 0.0171 56 LYS A CA 414 C C . LYS A 56 ? 0.2403 0.2919 0.2583 -0.0041 0.0180 0.0106 56 LYS A C 415 O O . LYS A 56 ? 0.2307 0.3035 0.2577 -0.0014 0.0179 0.0115 56 LYS A O 416 C CB . LYS A 56 ? 0.2256 0.2615 0.2419 -0.0051 0.0209 0.0242 56 LYS A CB 417 C CG . LYS A 56 ? 0.2371 0.2763 0.2605 -0.0048 0.0202 0.0451 56 LYS A CG 418 C CD . LYS A 56 ? 0.2624 0.2654 0.2663 -0.0048 0.0290 0.0450 56 LYS A CD 419 C CE . LYS A 56 ? 0.2892 0.3114 0.2624 0.0213 0.0206 0.0561 56 LYS A CE 420 N NZ . LYS A 56 ? 0.2827 0.3210 0.2842 0.0455 0.0277 0.0450 56 LYS A NZ 421 N N . GLY A 57 ? 0.2602 0.3259 0.2781 -0.0018 0.0172 0.0123 57 GLY A N 422 C CA . GLY A 57 ? 0.2870 0.3653 0.3006 0.0043 0.0157 0.0086 57 GLY A CA 423 C C . GLY A 57 ? 0.3084 0.3909 0.3223 0.0096 0.0141 0.0096 57 GLY A C 424 O O . GLY A 57 ? 0.3213 0.3991 0.3409 0.0133 0.0133 0.0115 57 GLY A O 425 N N . GLN A 58 ? 0.3261 0.4160 0.3285 0.0145 0.0141 0.0054 58 GLN A N 426 C CA . GLN A 58 ? 0.3458 0.4438 0.3454 0.0220 0.0147 0.0026 58 GLN A CA 427 C C . GLN A 58 ? 0.3656 0.4669 0.3610 0.0227 0.0145 -0.0023 58 GLN A C 428 O O . GLN A 58 ? 0.3669 0.4790 0.3606 0.0268 0.0157 -0.0063 58 GLN A O 429 C CB . GLN A 58 ? 0.3375 0.4381 0.3433 0.0246 0.0139 0.0025 58 GLN A CB 430 C CG . GLN A 58 ? 0.3322 0.4295 0.3411 0.0350 0.0147 0.0071 58 GLN A CG 431 C CD . GLN A 58 ? 0.3076 0.3885 0.3519 0.0471 0.0099 0.0081 58 GLN A CD 432 O OE1 . GLN A 58 ? 0.3261 0.4000 0.3338 0.0651 0.0052 -0.0119 58 GLN A OE1 433 N NE2 . GLN A 58 ? 0.2769 0.3726 0.2984 0.0655 0.0146 0.0081 58 GLN A NE2 434 N N . LYS A 59 ? 0.3891 0.4896 0.3814 0.0224 0.0157 -0.0050 59 LYS A N 435 C CA . LYS A 59 ? 0.4136 0.5037 0.4058 0.0173 0.0144 -0.0070 59 LYS A CA 436 C C . LYS A 59 ? 0.4243 0.5050 0.4167 0.0170 0.0160 -0.0077 59 LYS A C 437 O O . LYS A 59 ? 0.4278 0.5111 0.4232 0.0210 0.0184 -0.0103 59 LYS A O 438 C CB . LYS A 59 ? 0.4108 0.5047 0.4054 0.0137 0.0122 -0.0078 59 LYS A CB 439 C CG . LYS A 59 ? 0.4307 0.5333 0.4283 0.0052 0.0115 -0.0138 59 LYS A CG 440 C CD . LYS A 59 ? 0.4606 0.5672 0.4838 -0.0189 0.0186 -0.0186 59 LYS A CD 441 C CE . LYS A 59 ? 0.4815 0.5899 0.5025 -0.0267 0.0237 -0.0226 59 LYS A CE 442 N NZ . LYS A 59 ? 0.4810 0.6012 0.5297 -0.0377 0.0317 -0.0335 59 LYS A NZ 443 N N . LYS A 60 ? 0.4400 0.5097 0.4311 0.0174 0.0180 -0.0095 60 LYS A N 444 C CA . LYS A 60 ? 0.4477 0.5176 0.4486 0.0136 0.0188 -0.0106 60 LYS A CA 445 C C . LYS A 60 ? 0.4507 0.5187 0.4483 0.0078 0.0211 -0.0097 60 LYS A C 446 O O . LYS A 60 ? 0.4560 0.5323 0.4566 0.0072 0.0242 -0.0077 60 LYS A O 447 C CB . LYS A 60 ? 0.4536 0.5158 0.4548 0.0171 0.0185 -0.0112 60 LYS A CB 448 C CG . LYS A 60 ? 0.4700 0.5271 0.4946 0.0325 0.0185 -0.0231 60 LYS A CG 449 C CD . LYS A 60 ? 0.4919 0.5518 0.5723 0.0484 0.0163 -0.0175 60 LYS A CD 450 C CE . LYS A 60 ? 0.5224 0.5566 0.6077 0.0563 0.0264 -0.0207 60 LYS A CE 451 N NZ . LYS A 60 ? 0.5116 0.5499 0.6089 0.0778 0.0498 -0.0407 60 LYS A NZ 452 N N . ASP A 61 ? 0.4535 0.5245 0.4491 0.0008 0.0238 -0.0083 61 ASP A N 453 C CA . ASP A 61 ? 0.4590 0.5239 0.4504 -0.0028 0.0235 -0.0089 61 ASP A CA 454 C C . ASP A 61 ? 0.4457 0.5138 0.4393 -0.0053 0.0192 -0.0067 61 ASP A C 455 O O . ASP A 61 ? 0.4452 0.5197 0.4410 -0.0107 0.0133 -0.0076 61 ASP A O 456 C CB . ASP A 61 ? 0.4771 0.5365 0.4633 -0.0040 0.0255 -0.0085 61 ASP A CB 457 C CG . ASP A 61 ? 0.5301 0.5544 0.5009 -0.0065 0.0348 -0.0043 61 ASP A CG 458 O OD1 . ASP A 61 ? 0.5723 0.5625 0.5582 -0.0087 0.0432 -0.0005 61 ASP A OD1 459 O OD2 . ASP A 61 ? 0.6083 0.5857 0.5491 -0.0037 0.0272 0.0109 61 ASP A OD2 460 N N . LYS A 62 ? 0.4208 0.4849 0.4157 -0.0043 0.0194 -0.0057 62 LYS A N 461 C CA . LYS A 62 ? 0.4030 0.4631 0.3961 -0.0060 0.0176 -0.0009 62 LYS A CA 462 C C . LYS A 62 ? 0.3813 0.4413 0.3794 -0.0063 0.0120 -0.0022 62 LYS A C 463 O O . LYS A 62 ? 0.3900 0.4370 0.3772 -0.0056 0.0155 -0.0002 62 LYS A O 464 C CB . LYS A 62 ? 0.4061 0.4576 0.3978 -0.0072 0.0202 -0.0030 62 LYS A CB 465 C CG . LYS A 62 ? 0.4416 0.4879 0.4183 -0.0002 0.0251 0.0001 62 LYS A CG 466 C CD . LYS A 62 ? 0.4940 0.5212 0.4575 -0.0034 0.0424 0.0094 62 LYS A CD 467 C CE . LYS A 62 ? 0.5432 0.5706 0.4889 0.0140 0.0598 -0.0004 62 LYS A CE 468 N NZ . LYS A 62 ? 0.5862 0.5944 0.5268 0.0197 0.0530 0.0030 62 LYS A NZ 469 N N . LEU A 63 ? 0.3444 0.4181 0.3507 -0.0075 0.0085 -0.0022 63 LEU A N 470 C CA . LEU A 63 ? 0.3190 0.3952 0.3283 -0.0009 0.0014 -0.0032 63 LEU A CA 471 C C . LEU A 63 ? 0.3000 0.3797 0.3110 0.0009 0.0042 -0.0042 63 LEU A C 472 O O . LEU A 63 ? 0.2918 0.3693 0.3076 0.0103 0.0038 -0.0033 63 LEU A O 473 C CB . LEU A 63 ? 0.3181 0.3968 0.3269 -0.0033 -0.0002 -0.0062 63 LEU A CB 474 C CG . LEU A 63 ? 0.3199 0.3967 0.3325 0.0005 -0.0156 -0.0087 63 LEU A CG 475 C CD1 . LEU A 63 ? 0.3317 0.3956 0.3168 -0.0034 0.0000 -0.0131 63 LEU A CD1 476 C CD2 . LEU A 63 ? 0.3238 0.4161 0.3409 -0.0058 -0.0355 -0.0108 63 LEU A CD2 477 N N . GLY A 64 ? 0.2847 0.3606 0.2895 0.0012 0.0066 -0.0030 64 GLY A N 478 C CA . GLY A 64 ? 0.2737 0.3467 0.2827 0.0051 0.0040 -0.0064 64 GLY A CA 479 C C . GLY A 64 ? 0.2690 0.3252 0.2712 0.0045 0.0029 -0.0140 64 GLY A C 480 O O . GLY A 64 ? 0.2759 0.3306 0.2723 -0.0038 0.0044 -0.0138 64 GLY A O 481 N N . PRO A 65 ? 0.2635 0.3119 0.2624 0.0050 0.0004 -0.0171 65 PRO A N 482 C CA . PRO A 65 ? 0.2611 0.3028 0.2585 0.0055 0.0016 -0.0192 65 PRO A CA 483 C C . PRO A 65 ? 0.2608 0.2978 0.2581 -0.0001 -0.0025 -0.0236 65 PRO A C 484 O O . PRO A 65 ? 0.2491 0.2799 0.2494 0.0013 -0.0085 -0.0274 65 PRO A O 485 C CB . PRO A 65 ? 0.2626 0.3150 0.2559 0.0114 0.0000 -0.0234 65 PRO A CB 486 C CG . PRO A 65 ? 0.2568 0.3237 0.2584 0.0188 0.0041 -0.0164 65 PRO A CG 487 C CD . PRO A 65 ? 0.2648 0.3209 0.2566 0.0108 -0.0015 -0.0186 65 PRO A CD 488 N N . GLU A 66 ? 0.2648 0.2919 0.2691 -0.0042 -0.0036 -0.0203 66 GLU A N 489 C CA . GLU A 66 ? 0.2728 0.2960 0.2760 -0.0119 -0.0043 -0.0185 66 GLU A CA 490 C C . GLU A 66 ? 0.2743 0.2975 0.2846 -0.0135 -0.0098 -0.0169 66 GLU A C 491 O O . GLU A 66 ? 0.2852 0.2924 0.2873 -0.0201 -0.0093 -0.0274 66 GLU A O 492 C CB . GLU A 66 ? 0.2626 0.2934 0.2754 -0.0064 -0.0023 -0.0156 66 GLU A CB 493 C CG . GLU A 66 ? 0.2747 0.2989 0.2791 -0.0035 0.0164 -0.0143 66 GLU A CG 494 C CD . GLU A 66 ? 0.2843 0.3361 0.2983 0.0127 0.0255 -0.0040 66 GLU A CD 495 O OE1 . GLU A 66 ? 0.2134 0.3008 0.2820 0.0045 0.0139 0.0071 66 GLU A OE1 496 O OE2 . GLU A 66 ? 0.2945 0.3458 0.3095 0.0196 0.0736 -0.0169 66 GLU A OE2 497 N N . ILE A 67 ? 0.2680 0.2989 0.2842 -0.0166 -0.0087 -0.0182 67 ILE A N 498 C CA . ILE A 67 ? 0.2605 0.2970 0.2903 -0.0191 -0.0158 -0.0121 67 ILE A CA 499 C C . ILE A 67 ? 0.2569 0.2859 0.2917 -0.0195 -0.0134 -0.0129 67 ILE A C 500 O O . ILE A 67 ? 0.2574 0.2774 0.3025 -0.0297 -0.0178 -0.0170 67 ILE A O 501 C CB . ILE A 67 ? 0.2550 0.3072 0.2956 -0.0179 -0.0147 -0.0105 67 ILE A CB 502 C CG1 . ILE A 67 ? 0.2786 0.3359 0.3202 -0.0263 -0.0174 -0.0119 67 ILE A CG1 503 C CG2 . ILE A 67 ? 0.2643 0.3095 0.2876 -0.0207 -0.0263 -0.0027 67 ILE A CG2 504 C CD1 . ILE A 67 ? 0.2817 0.3189 0.3430 -0.0456 -0.0333 -0.0256 67 ILE A CD1 505 N N . PRO A 68 ? 0.2465 0.2730 0.2802 -0.0226 -0.0130 -0.0107 68 PRO A N 506 C CA . PRO A 68 ? 0.2308 0.2667 0.2627 -0.0229 -0.0106 -0.0085 68 PRO A CA 507 C C . PRO A 68 ? 0.2181 0.2572 0.2446 -0.0255 -0.0065 -0.0018 68 PRO A C 508 O O . PRO A 68 ? 0.2109 0.2573 0.2402 -0.0308 0.0006 0.0013 68 PRO A O 509 C CB . PRO A 68 ? 0.2292 0.2655 0.2637 -0.0258 -0.0126 -0.0104 68 PRO A CB 510 C CG . PRO A 68 ? 0.2481 0.2816 0.2817 -0.0227 -0.0086 -0.0102 68 PRO A CG 511 C CD . PRO A 68 ? 0.2465 0.2718 0.2900 -0.0175 -0.0171 -0.0127 68 PRO A CD 512 N N . LEU A 69 ? 0.1928 0.2290 0.2168 -0.0273 -0.0041 0.0059 69 LEU A N 513 C CA . LEU A 69 ? 0.1826 0.2142 0.1894 -0.0287 0.0041 0.0120 69 LEU A CA 514 C C . LEU A 69 ? 0.1742 0.2049 0.1766 -0.0221 0.0073 0.0138 69 LEU A C 515 O O . LEU A 69 ? 0.1740 0.2042 0.1547 -0.0141 0.0122 0.0150 69 LEU A O 516 C CB . LEU A 69 ? 0.1762 0.2092 0.1846 -0.0370 0.0010 0.0133 69 LEU A CB 517 C CG . LEU A 69 ? 0.1817 0.2057 0.1745 -0.0449 0.0088 0.0229 69 LEU A CG 518 C CD1 . LEU A 69 ? 0.1681 0.2298 0.1796 -0.0718 -0.0052 0.0460 69 LEU A CD1 519 C CD2 . LEU A 69 ? 0.2235 0.1762 0.1583 -0.0541 -0.0164 0.0365 69 LEU A CD2 520 N N . ALA A 70 ? 0.1728 0.1997 0.1698 -0.0156 0.0114 0.0120 70 ALA A N 521 C CA . ALA A 70 ? 0.1673 0.1795 0.1651 -0.0094 0.0174 0.0075 70 ALA A CA 522 C C . ALA A 70 ? 0.1696 0.1822 0.1664 -0.0120 0.0176 0.0068 70 ALA A C 523 O O . ALA A 70 ? 0.1579 0.1624 0.1585 0.0027 0.0308 -0.0083 70 ALA A O 524 C CB . ALA A 70 ? 0.1821 0.1874 0.1698 -0.0106 0.0141 0.0115 70 ALA A CB 525 N N . MET A 71 ? 0.1634 0.1721 0.1618 -0.0162 0.0160 0.0077 71 MET A N 526 C CA . MET A 71 ? 0.1593 0.1717 0.1785 -0.0152 0.0096 0.0097 71 MET A CA 527 C C . MET A 71 ? 0.1639 0.1752 0.1871 -0.0127 0.0108 0.0108 71 MET A C 528 O O . MET A 71 ? 0.1600 0.1720 0.1868 0.0009 -0.0013 0.0086 71 MET A O 529 C CB . MET A 71 ? 0.1589 0.1732 0.1786 -0.0122 0.0124 0.0091 71 MET A CB 530 C CG . MET A 71 ? 0.1643 0.1647 0.1756 -0.0418 0.0054 0.0255 71 MET A CG 531 S SD . MET A 71 ? 0.1873 0.1988 0.2050 -0.0231 0.0124 0.0088 71 MET A SD 532 C CE . MET A 71 ? 0.1759 0.2205 0.1253 -0.0540 0.0342 0.0040 71 MET A CE 533 N N . ASP A 72 ? 0.1637 0.1688 0.1841 -0.0190 0.0028 0.0129 72 ASP A N 534 C CA . ASP A 72 ? 0.1810 0.1729 0.1950 -0.0185 0.0035 0.0052 72 ASP A CA 535 C C . ASP A 72 ? 0.1866 0.1824 0.2022 -0.0121 0.0048 0.0033 72 ASP A C 536 O O . ASP A 72 ? 0.1990 0.1952 0.2054 -0.0188 0.0007 0.0023 72 ASP A O 537 C CB . ASP A 72 ? 0.1867 0.1670 0.1934 -0.0149 -0.0013 0.0054 72 ASP A CB 538 C CG . ASP A 72 ? 0.1995 0.1811 0.1896 -0.0110 -0.0051 0.0003 72 ASP A CG 539 O OD1 . ASP A 72 ? 0.2163 0.1896 0.1809 -0.0056 0.0101 -0.0075 72 ASP A OD1 540 O OD2 . ASP A 72 ? 0.2286 0.1535 0.2079 0.0062 -0.0271 0.0048 72 ASP A OD2 541 N N . ARG A 73 ? 0.1684 0.1874 0.2092 -0.0082 0.0134 0.0023 73 ARG A N 542 C CA . ARG A 73 ? 0.1621 0.1860 0.2235 0.0036 0.0118 -0.0003 73 ARG A CA 543 C C . ARG A 73 ? 0.1665 0.1899 0.2160 -0.0014 0.0087 -0.0032 73 ARG A C 544 O O . ARG A 73 ? 0.1523 0.1855 0.2349 0.0040 0.0012 -0.0138 73 ARG A O 545 C CB . ARG A 73 ? 0.1525 0.1956 0.2367 0.0023 0.0132 0.0035 73 ARG A CB 546 C CG . ARG A 73 ? 0.1785 0.2061 0.2943 0.0204 0.0290 -0.0032 73 ARG A CG 547 C CD . ARG A 73 ? 0.1572 0.2591 0.3934 0.0297 0.0323 0.0172 73 ARG A CD 548 N NE . ARG A 73 ? 0.2483 0.3315 0.4586 0.0218 0.0015 0.0209 73 ARG A NE 549 C CZ . ARG A 73 ? 0.2389 0.3480 0.5033 0.0228 -0.0043 0.0054 73 ARG A CZ 550 N NH1 . ARG A 73 ? 0.2533 0.3700 0.5335 0.0154 -0.0087 -0.0064 73 ARG A NH1 551 N NH2 . ARG A 73 ? 0.2758 0.3626 0.5491 0.0160 -0.0069 0.0259 73 ARG A NH2 552 N N . PHE A 74 ? 0.1613 0.1852 0.1954 -0.0009 -0.0051 -0.0090 74 PHE A N 553 C CA . PHE A 74 ? 0.1771 0.1702 0.1887 -0.0001 0.0005 -0.0049 74 PHE A CA 554 C C . PHE A 74 ? 0.1866 0.1650 0.1843 -0.0049 -0.0034 -0.0083 74 PHE A C 555 O O . PHE A 74 ? 0.1927 0.1699 0.1820 -0.0041 0.0011 -0.0118 74 PHE A O 556 C CB . PHE A 74 ? 0.1605 0.1560 0.1760 -0.0018 -0.0139 -0.0020 74 PHE A CB 557 C CG . PHE A 74 ? 0.1653 0.1623 0.1902 -0.0057 0.0055 0.0025 74 PHE A CG 558 C CD1 . PHE A 74 ? 0.1683 0.1864 0.1789 -0.0274 -0.0120 0.0041 74 PHE A CD1 559 C CD2 . PHE A 74 ? 0.1456 0.1497 0.1589 -0.0078 -0.0174 0.0134 74 PHE A CD2 560 C CE1 . PHE A 74 ? 0.1705 0.1588 0.1886 -0.0423 0.0066 0.0255 74 PHE A CE1 561 C CE2 . PHE A 74 ? 0.1770 0.1564 0.1943 -0.0173 0.0151 0.0252 74 PHE A CE2 562 C CZ . PHE A 74 ? 0.1771 0.1547 0.1854 -0.0251 0.0070 0.0302 74 PHE A CZ 563 N N . PRO A 75 ? 0.1971 0.1614 0.1862 -0.0030 -0.0025 -0.0057 75 PRO A N 564 C CA . PRO A 75 ? 0.2034 0.1623 0.1840 -0.0033 0.0039 -0.0029 75 PRO A CA 565 C C . PRO A 75 ? 0.2014 0.1607 0.1935 -0.0066 -0.0004 -0.0029 75 PRO A C 566 O O . PRO A 75 ? 0.2030 0.1676 0.1853 -0.0135 0.0017 0.0070 75 PRO A O 567 C CB . PRO A 75 ? 0.2085 0.1502 0.1826 -0.0032 -0.0024 -0.0060 75 PRO A CB 568 C CG . PRO A 75 ? 0.2178 0.1541 0.1904 -0.0049 0.0047 0.0009 75 PRO A CG 569 C CD . PRO A 75 ? 0.2001 0.1612 0.1721 -0.0025 -0.0010 -0.0044 75 PRO A CD 570 N N . TYR A 76 ? 0.1956 0.1481 0.1941 -0.0048 0.0003 -0.0054 76 TYR A N 571 C CA . TYR A 76 ? 0.1976 0.1451 0.2018 -0.0072 -0.0005 -0.0065 76 TYR A CA 572 C C . TYR A 76 ? 0.1996 0.1424 0.1998 -0.0042 0.0048 -0.0012 76 TYR A C 573 O O . TYR A 76 ? 0.2047 0.1341 0.1902 0.0020 -0.0011 0.0005 76 TYR A O 574 C CB . TYR A 76 ? 0.1954 0.1487 0.2170 -0.0067 0.0058 -0.0084 76 TYR A CB 575 C CG . TYR A 76 ? 0.1922 0.1567 0.2456 -0.0076 -0.0042 -0.0070 76 TYR A CG 576 C CD1 . TYR A 76 ? 0.1808 0.1264 0.2493 0.0028 -0.0025 -0.0197 76 TYR A CD1 577 C CD2 . TYR A 76 ? 0.1800 0.1414 0.2304 -0.0148 -0.0031 -0.0031 76 TYR A CD2 578 C CE1 . TYR A 76 ? 0.1770 0.2004 0.2855 -0.0175 -0.0101 -0.0141 76 TYR A CE1 579 C CE2 . TYR A 76 ? 0.1977 0.1881 0.2647 -0.0113 -0.0057 -0.0075 76 TYR A CE2 580 C CZ . TYR A 76 ? 0.1936 0.1647 0.2630 -0.0107 -0.0103 -0.0083 76 TYR A CZ 581 O OH . TYR A 76 ? 0.2016 0.2048 0.2982 -0.0276 -0.0115 -0.0185 76 TYR A OH 582 N N . VAL A 77 ? 0.1943 0.1446 0.1966 -0.0098 0.0151 -0.0035 77 VAL A N 583 C CA . VAL A 77 ? 0.1969 0.1448 0.1937 -0.0122 0.0203 0.0010 77 VAL A CA 584 C C . VAL A 77 ? 0.1908 0.1464 0.1843 -0.0171 0.0198 -0.0016 77 VAL A C 585 O O . VAL A 77 ? 0.1958 0.1545 0.1858 -0.0253 0.0231 0.0042 77 VAL A O 586 C CB . VAL A 77 ? 0.1984 0.1477 0.1949 -0.0125 0.0245 0.0021 77 VAL A CB 587 C CG1 . VAL A 77 ? 0.2274 0.1402 0.2104 -0.0225 0.0229 0.0161 77 VAL A CG1 588 C CG2 . VAL A 77 ? 0.2040 0.1548 0.1919 -0.0094 0.0225 0.0041 77 VAL A CG2 589 N N . ALA A 78 ? 0.1762 0.1425 0.1728 -0.0112 0.0155 -0.0035 78 ALA A N 590 C CA . ALA A 78 ? 0.1722 0.1463 0.1587 -0.0100 0.0104 0.0040 78 ALA A CA 591 C C . ALA A 78 ? 0.1689 0.1520 0.1548 -0.0057 0.0077 0.0041 78 ALA A C 592 O O . ALA A 78 ? 0.1732 0.1613 0.1494 -0.0121 0.0117 0.0112 78 ALA A O 593 C CB . ALA A 78 ? 0.1655 0.1341 0.1524 -0.0035 0.0144 0.0046 78 ALA A CB 594 N N . LEU A 79 ? 0.1512 0.1564 0.1377 -0.0038 0.0042 0.0080 79 LEU A N 595 C CA . LEU A 79 ? 0.1531 0.1652 0.1378 0.0036 -0.0055 -0.0004 79 LEU A CA 596 C C . LEU A 79 ? 0.1520 0.1654 0.1500 0.0022 -0.0073 -0.0096 79 LEU A C 597 O O . LEU A 79 ? 0.1657 0.1823 0.1628 -0.0010 -0.0155 -0.0214 79 LEU A O 598 C CB . LEU A 79 ? 0.1446 0.1646 0.1373 0.0019 0.0014 0.0098 79 LEU A CB 599 C CG . LEU A 79 ? 0.1562 0.1758 0.1434 0.0242 -0.0026 0.0100 79 LEU A CG 600 C CD1 . LEU A 79 ? 0.1634 0.2165 0.1557 0.0409 -0.0227 0.0191 79 LEU A CD1 601 C CD2 . LEU A 79 ? 0.1496 0.2092 0.1739 0.0517 -0.0107 -0.0029 79 LEU A CD2 602 N N . SER A 80 ? 0.1553 0.1672 0.1399 0.0046 -0.0114 -0.0109 80 SER A N 603 C CA . SER A 80 ? 0.1536 0.1651 0.1482 0.0095 -0.0103 -0.0106 80 SER A CA 604 C C . SER A 80 ? 0.1462 0.1620 0.1468 0.0106 -0.0051 -0.0104 80 SER A C 605 O O . SER A 80 ? 0.1495 0.1424 0.1674 0.0104 -0.0043 -0.0123 80 SER A O 606 C CB . SER A 80 ? 0.1518 0.1659 0.1284 0.0135 -0.0136 -0.0210 80 SER A CB 607 O OG . SER A 80 ? 0.1892 0.2061 0.1736 0.0261 -0.0181 -0.0108 80 SER A OG 608 N N . LYS A 81 ? 0.1418 0.1601 0.1431 0.0116 -0.0054 -0.0123 81 LYS A N 609 C CA . LYS A 81 ? 0.1327 0.1632 0.1392 0.0174 -0.0015 -0.0166 81 LYS A CA 610 C C . LYS A 81 ? 0.1330 0.1607 0.1337 0.0149 -0.0025 -0.0169 81 LYS A C 611 O O . LYS A 81 ? 0.1472 0.1609 0.1270 0.0308 -0.0120 -0.0118 81 LYS A O 612 C CB . LYS A 81 ? 0.1339 0.1602 0.1270 0.0199 0.0090 -0.0286 81 LYS A CB 613 C CG . LYS A 81 ? 0.1115 0.1899 0.1402 0.0331 0.0093 -0.0303 81 LYS A CG 614 C CD . LYS A 81 ? 0.1170 0.2238 0.1770 0.0564 0.0180 -0.0324 81 LYS A CD 615 C CE . LYS A 81 ? 0.0842 0.2674 0.2284 0.0582 0.0439 -0.0402 81 LYS A CE 616 N NZ . LYS A 81 ? 0.0996 0.2821 0.2669 0.0865 0.0320 -0.0646 81 LYS A NZ 617 N N . THR A 82 ? 0.1170 0.1491 0.1367 0.0112 -0.0034 -0.0074 82 THR A N 618 C CA . THR A 82 ? 0.1194 0.1526 0.1472 0.0007 0.0038 -0.0068 82 THR A CA 619 C C . THR A 82 ? 0.1271 0.1644 0.1539 0.0044 0.0005 -0.0071 82 THR A C 620 O O . THR A 82 ? 0.1338 0.1780 0.1559 -0.0045 0.0061 -0.0069 82 THR A O 621 C CB . THR A 82 ? 0.1097 0.1423 0.1490 0.0050 0.0032 -0.0093 82 THR A CB 622 O OG1 . THR A 82 ? 0.1287 0.1368 0.1130 -0.0086 0.0022 0.0054 82 THR A OG1 623 C CG2 . THR A 82 ? 0.0922 0.1359 0.1431 -0.0157 0.0157 -0.0111 82 THR A CG2 624 N N . TYR A 83 ? 0.1238 0.1646 0.1488 0.0069 0.0064 -0.0032 83 TYR A N 625 C CA . TYR A 83 ? 0.1371 0.1727 0.1592 0.0033 0.0114 0.0026 83 TYR A CA 626 C C . TYR A 83 ? 0.1303 0.1765 0.1628 0.0031 0.0091 0.0014 83 TYR A C 627 O O . TYR A 83 ? 0.1376 0.1816 0.1717 -0.0049 0.0167 0.0062 83 TYR A O 628 C CB . TYR A 83 ? 0.1480 0.1689 0.1625 0.0044 0.0151 -0.0039 83 TYR A CB 629 C CG . TYR A 83 ? 0.1559 0.1925 0.1705 0.0037 0.0178 0.0080 83 TYR A CG 630 C CD1 . TYR A 83 ? 0.1505 0.1632 0.1428 -0.0044 0.0140 -0.0233 83 TYR A CD1 631 C CD2 . TYR A 83 ? 0.1343 0.1843 0.1704 -0.0009 0.0344 0.0050 83 TYR A CD2 632 C CE1 . TYR A 83 ? 0.1647 0.1854 0.1465 0.0074 0.0161 -0.0022 83 TYR A CE1 633 C CE2 . TYR A 83 ? 0.1587 0.1916 0.1786 -0.0011 0.0221 0.0115 83 TYR A CE2 634 C CZ . TYR A 83 ? 0.1512 0.1850 0.1678 0.0035 0.0263 -0.0045 83 TYR A CZ 635 O OH . TYR A 83 ? 0.1557 0.1736 0.1810 -0.0123 0.0228 0.0048 83 TYR A OH 636 N N . ASN A 84 ? 0.1329 0.1762 0.1562 0.0049 0.0082 0.0010 84 ASN A N 637 C CA . ASN A 84 ? 0.1266 0.1889 0.1675 0.0097 -0.0088 -0.0006 84 ASN A CA 638 C C . ASN A 84 ? 0.1376 0.1899 0.1716 0.0060 -0.0102 0.0023 84 ASN A C 639 O O . ASN A 84 ? 0.1361 0.2079 0.1662 0.0078 -0.0220 0.0075 84 ASN A O 640 C CB . ASN A 84 ? 0.1274 0.1681 0.1570 0.0102 -0.0012 0.0012 84 ASN A CB 641 C CG . ASN A 84 ? 0.1445 0.1803 0.1717 0.0220 -0.0230 0.0043 84 ASN A CG 642 O OD1 . ASN A 84 ? 0.1704 0.1871 0.1684 0.0202 -0.0033 0.0067 84 ASN A OD1 643 N ND2 . ASN A 84 ? 0.1569 0.1536 0.1537 0.0158 -0.0078 0.0388 84 ASN A ND2 644 N N . VAL A 85 ? 0.1306 0.1833 0.1848 0.0072 -0.0164 0.0013 85 VAL A N 645 C CA . VAL A 85 ? 0.1354 0.1736 0.1898 -0.0001 -0.0128 -0.0018 85 VAL A CA 646 C C . VAL A 85 ? 0.1454 0.1844 0.1878 0.0018 -0.0151 0.0040 85 VAL A C 647 O O . VAL A 85 ? 0.1581 0.1841 0.1884 0.0023 -0.0153 0.0013 85 VAL A O 648 C CB . VAL A 85 ? 0.1339 0.1728 0.1957 -0.0021 -0.0120 -0.0030 85 VAL A CB 649 C CG1 . VAL A 85 ? 0.1193 0.1672 0.1915 0.0113 0.0031 -0.0314 85 VAL A CG1 650 C CG2 . VAL A 85 ? 0.1188 0.1588 0.1999 -0.0113 -0.0065 0.0100 85 VAL A CG2 651 N N . ASP A 86 ? 0.1409 0.1772 0.1856 0.0027 -0.0207 0.0015 86 ASP A N 652 C CA . ASP A 86 ? 0.1539 0.1906 0.1906 0.0018 -0.0193 0.0059 86 ASP A CA 653 C C . ASP A 86 ? 0.1602 0.1999 0.1906 -0.0022 -0.0148 0.0023 86 ASP A C 654 O O . ASP A 86 ? 0.1682 0.1814 0.1906 -0.0130 -0.0222 0.0162 86 ASP A O 655 C CB . ASP A 86 ? 0.1394 0.1852 0.1857 0.0014 -0.0196 0.0043 86 ASP A CB 656 C CG . ASP A 86 ? 0.1654 0.1894 0.2017 0.0085 -0.0258 0.0146 86 ASP A CG 657 O OD1 . ASP A 86 ? 0.1276 0.2129 0.2184 0.0031 -0.0162 0.0088 86 ASP A OD1 658 O OD2 . ASP A 86 ? 0.1646 0.2118 0.2264 0.0060 -0.0139 -0.0008 86 ASP A OD2 659 N N . LYS A 87 ? 0.1504 0.2046 0.1865 -0.0036 -0.0086 -0.0033 87 LYS A N 660 C CA . LYS A 87 ? 0.1632 0.2134 0.1956 0.0005 -0.0042 -0.0101 87 LYS A CA 661 C C . LYS A 87 ? 0.1517 0.2054 0.1872 0.0039 -0.0070 -0.0071 87 LYS A C 662 O O . LYS A 87 ? 0.1379 0.2156 0.1891 0.0123 -0.0175 -0.0066 87 LYS A O 663 C CB . LYS A 87 ? 0.1531 0.2104 0.1993 -0.0035 -0.0031 -0.0156 87 LYS A CB 664 C CG . LYS A 87 ? 0.1879 0.2411 0.2208 0.0050 0.0090 -0.0326 87 LYS A CG 665 C CD . LYS A 87 ? 0.1785 0.2280 0.2288 -0.0050 0.0068 -0.0203 87 LYS A CD 666 C CE . LYS A 87 ? 0.2079 0.2289 0.2218 0.0112 0.0230 -0.0416 87 LYS A CE 667 N NZ . LYS A 87 ? 0.2553 0.2402 0.3244 0.0087 0.0336 -0.0244 87 LYS A NZ 668 N N . HIS A 88 ? 0.1607 0.2121 0.1805 0.0050 -0.0045 -0.0150 88 HIS A N 669 C CA . HIS A 88 ? 0.1709 0.2166 0.1869 0.0063 -0.0008 -0.0020 88 HIS A CA 670 C C . HIS A 88 ? 0.1713 0.2049 0.1809 0.0071 0.0030 -0.0039 88 HIS A C 671 O O . HIS A 88 ? 0.1688 0.2054 0.1810 0.0080 0.0090 -0.0159 88 HIS A O 672 C CB . HIS A 88 ? 0.1790 0.2325 0.1823 0.0053 -0.0083 -0.0051 88 HIS A CB 673 C CG . HIS A 88 ? 0.2134 0.2532 0.2110 -0.0088 -0.0069 0.0091 88 HIS A CG 674 N ND1 . HIS A 88 ? 0.2449 0.3051 0.2455 -0.0225 -0.0051 0.0178 88 HIS A ND1 675 C CD2 . HIS A 88 ? 0.2440 0.2890 0.2456 -0.0083 0.0094 0.0246 88 HIS A CD2 676 C CE1 . HIS A 88 ? 0.2616 0.3055 0.2490 0.0001 0.0105 0.0202 88 HIS A CE1 677 N NE2 . HIS A 88 ? 0.2943 0.2926 0.2275 -0.0265 0.0097 0.0252 88 HIS A NE2 678 N N . VAL A 89 ? 0.1680 0.1884 0.1591 0.0112 -0.0002 -0.0007 89 VAL A N 679 C CA . VAL A 89 ? 0.1680 0.1713 0.1584 0.0150 -0.0069 0.0026 89 VAL A CA 680 C C . VAL A 89 ? 0.1668 0.1651 0.1663 0.0108 -0.0037 0.0003 89 VAL A C 681 O O . VAL A 89 ? 0.1727 0.1637 0.1700 0.0052 -0.0073 0.0023 89 VAL A O 682 C CB . VAL A 89 ? 0.1695 0.1686 0.1550 0.0175 -0.0034 0.0064 89 VAL A CB 683 C CG1 . VAL A 89 ? 0.1606 0.1409 0.1630 0.0147 -0.0104 0.0159 89 VAL A CG1 684 C CG2 . VAL A 89 ? 0.1676 0.1701 0.1535 0.0091 -0.0076 0.0004 89 VAL A CG2 685 N N . PRO A 90 ? 0.1604 0.1484 0.1658 0.0026 -0.0066 0.0017 90 PRO A N 686 C CA . PRO A 90 ? 0.1662 0.1473 0.1583 -0.0024 -0.0053 -0.0017 90 PRO A CA 687 C C . PRO A 90 ? 0.1639 0.1489 0.1582 -0.0070 -0.0079 -0.0006 90 PRO A C 688 O O . PRO A 90 ? 0.1628 0.1454 0.1662 0.0057 -0.0113 -0.0052 90 PRO A O 689 C CB . PRO A 90 ? 0.1611 0.1373 0.1528 -0.0112 -0.0068 -0.0018 90 PRO A CB 690 C CG . PRO A 90 ? 0.1620 0.1420 0.1734 -0.0030 -0.0164 0.0083 90 PRO A CG 691 C CD . PRO A 90 ? 0.1595 0.1573 0.1709 -0.0016 -0.0065 0.0035 90 PRO A CD 692 N N . ASP A 91 ? 0.1665 0.1622 0.1557 -0.0041 -0.0073 -0.0008 91 ASP A N 693 C CA . ASP A 91 ? 0.1649 0.1736 0.1454 0.0004 -0.0016 -0.0040 91 ASP A CA 694 C C . ASP A 91 ? 0.1602 0.1798 0.1468 0.0050 0.0024 -0.0048 91 ASP A C 695 O O . ASP A 91 ? 0.1610 0.1870 0.1490 0.0047 0.0063 -0.0098 91 ASP A O 696 C CB . ASP A 91 ? 0.1744 0.1791 0.1407 -0.0033 -0.0069 0.0013 91 ASP A CB 697 C CG . ASP A 91 ? 0.1948 0.2052 0.1547 0.0038 -0.0041 -0.0111 91 ASP A CG 698 O OD1 . ASP A 91 ? 0.1957 0.2191 0.1275 -0.0166 -0.0261 -0.0057 91 ASP A OD1 699 O OD2 . ASP A 91 ? 0.2070 0.2173 0.1786 0.0203 0.0021 -0.0093 91 ASP A OD2 700 N N . SEP A 92 ? 0.1656 0.1886 0.1409 0.0098 0.0014 -0.0034 92 SEP A N 701 C CA . SEP A 92 ? 0.1522 0.1797 0.1452 0.0137 0.0045 -0.0019 92 SEP A CA 702 C CB . SEP A 92 ? 0.1399 0.1790 0.1274 0.0198 0.0009 -0.0060 92 SEP A CB 703 O OG . SEP A 92 ? 0.1712 0.1819 0.1644 0.0323 0.0386 -0.0085 92 SEP A OG 704 C C . SEP A 92 ? 0.1437 0.1781 0.1380 0.0189 -0.0052 -0.0091 92 SEP A C 705 O O . SEP A 92 ? 0.1448 0.1869 0.1436 0.0200 -0.0174 -0.0074 92 SEP A O 706 P P . SEP A 92 ? 0.1513 0.1881 0.1705 0.0159 -0.0303 0.0143 92 SEP A P 707 O O1P . SEP A 92 ? 0.1429 0.2000 0.1904 0.0157 -0.0296 -0.0264 92 SEP A O1P 708 O O2P . SEP A 92 ? 0.1823 0.1778 0.1581 0.0124 0.0005 -0.0169 92 SEP A O2P 709 O O3P . SEP A 92 ? 0.1365 0.1844 0.1411 -0.0085 -0.0013 -0.0365 92 SEP A O3P 710 N N . GLY A 93 ? 0.1429 0.1751 0.1455 0.0190 -0.0014 -0.0122 93 GLY A N 711 C CA . GLY A 93 ? 0.1437 0.1768 0.1387 0.0139 -0.0064 -0.0189 93 GLY A CA 712 C C . GLY A 93 ? 0.1463 0.1712 0.1533 0.0104 -0.0065 -0.0165 93 GLY A C 713 O O . GLY A 93 ? 0.1427 0.1557 0.1381 0.0078 -0.0145 -0.0195 93 GLY A O 714 N N . ALA A 94 ? 0.1497 0.1689 0.1385 0.0103 -0.0025 -0.0174 94 ALA A N 715 C CA . ALA A 94 ? 0.1523 0.1706 0.1520 -0.0033 -0.0019 -0.0118 94 ALA A CA 716 C C . ALA A 94 ? 0.1394 0.1605 0.1488 -0.0027 -0.0046 -0.0102 94 ALA A C 717 O O . ALA A 94 ? 0.1278 0.1559 0.1760 -0.0068 -0.0151 -0.0019 94 ALA A O 718 C CB . ALA A 94 ? 0.1566 0.1848 0.1541 -0.0074 0.0057 -0.0230 94 ALA A CB 719 N N . THR A 95 ? 0.1493 0.1504 0.1438 -0.0045 -0.0039 -0.0016 95 THR A N 720 C CA . THR A 95 ? 0.1385 0.1445 0.1369 -0.0027 -0.0044 0.0042 95 THR A CA 721 C C . THR A 95 ? 0.1384 0.1455 0.1398 -0.0058 -0.0060 0.0080 95 THR A C 722 O O . THR A 95 ? 0.1440 0.1548 0.1530 0.0014 -0.0113 0.0197 95 THR A O 723 C CB . THR A 95 ? 0.1478 0.1435 0.1328 -0.0069 -0.0025 0.0028 95 THR A CB 724 O OG1 . THR A 95 ? 0.1613 0.1458 0.1372 0.0256 0.0049 0.0035 95 THR A OG1 725 C CG2 . THR A 95 ? 0.1101 0.1443 0.1189 -0.0033 0.0039 -0.0010 95 THR A CG2 726 N N . ALA A 96 ? 0.1466 0.1522 0.1362 -0.0075 -0.0105 0.0164 96 ALA A N 727 C CA . ALA A 96 ? 0.1517 0.1531 0.1363 -0.0050 -0.0146 0.0095 96 ALA A CA 728 C C . ALA A 96 ? 0.1537 0.1577 0.1413 -0.0034 -0.0171 0.0054 96 ALA A C 729 O O . ALA A 96 ? 0.1522 0.1610 0.1345 -0.0029 -0.0135 0.0155 96 ALA A O 730 C CB . ALA A 96 ? 0.1577 0.1520 0.1360 -0.0064 -0.0089 0.0152 96 ALA A CB 731 N N . THR A 97 ? 0.1556 0.1589 0.1446 0.0034 -0.0203 -0.0007 97 THR A N 732 C CA . THR A 97 ? 0.1557 0.1571 0.1609 0.0115 -0.0231 -0.0093 97 THR A CA 733 C C . THR A 97 ? 0.1553 0.1599 0.1578 0.0082 -0.0250 -0.0063 97 THR A C 734 O O . THR A 97 ? 0.1589 0.1485 0.1500 0.0078 -0.0262 -0.0153 97 THR A O 735 C CB . THR A 97 ? 0.1531 0.1527 0.1653 0.0121 -0.0282 -0.0036 97 THR A CB 736 O OG1 . THR A 97 ? 0.1702 0.1594 0.1763 0.0264 -0.0333 -0.0203 97 THR A OG1 737 C CG2 . THR A 97 ? 0.1419 0.1555 0.1736 0.0260 -0.0215 -0.0083 97 THR A CG2 738 N N . ALA A 98 ? 0.1459 0.1602 0.1577 0.0083 -0.0197 -0.0021 98 ALA A N 739 C CA . ALA A 98 ? 0.1442 0.1582 0.1600 0.0171 -0.0147 0.0001 98 ALA A CA 740 C C . ALA A 98 ? 0.1489 0.1611 0.1660 0.0179 -0.0168 0.0031 98 ALA A C 741 O O . ALA A 98 ? 0.1618 0.1496 0.1750 0.0290 -0.0128 0.0088 98 ALA A O 742 C CB . ALA A 98 ? 0.1327 0.1489 0.1510 0.0143 -0.0143 0.0007 98 ALA A CB 743 N N . TYR A 99 ? 0.1478 0.1628 0.1626 0.0216 -0.0059 0.0012 99 TYR A N 744 C CA . TYR A 99 ? 0.1487 0.1686 0.1624 0.0150 -0.0068 0.0019 99 TYR A CA 745 C C . TYR A 99 ? 0.1564 0.1685 0.1748 0.0157 -0.0081 0.0009 99 TYR A C 746 O O . TYR A 99 ? 0.1640 0.1729 0.1834 0.0145 -0.0070 -0.0005 99 TYR A O 747 C CB . TYR A 99 ? 0.1378 0.1638 0.1589 0.0244 -0.0003 0.0012 99 TYR A CB 748 C CG . TYR A 99 ? 0.1394 0.1803 0.1660 0.0111 -0.0054 -0.0029 99 TYR A CG 749 C CD1 . TYR A 99 ? 0.1287 0.1930 0.1703 0.0162 -0.0102 -0.0161 99 TYR A CD1 750 C CD2 . TYR A 99 ? 0.1035 0.1569 0.1643 0.0371 -0.0156 -0.0020 99 TYR A CD2 751 C CE1 . TYR A 99 ? 0.1099 0.1882 0.1791 0.0255 -0.0124 -0.0136 99 TYR A CE1 752 C CE2 . TYR A 99 ? 0.1065 0.1880 0.1823 0.0399 -0.0007 0.0004 99 TYR A CE2 753 C CZ . TYR A 99 ? 0.1224 0.1798 0.1735 0.0406 -0.0063 0.0049 99 TYR A CZ 754 O OH . TYR A 99 ? 0.1530 0.1943 0.1799 0.0183 0.0024 0.0004 99 TYR A OH 755 N N . LEU A 100 ? 0.1584 0.1666 0.1594 0.0156 -0.0094 -0.0047 100 LEU A N 756 C CA . LEU A 100 ? 0.1610 0.1607 0.1643 0.0156 -0.0061 -0.0086 100 LEU A CA 757 C C . LEU A 100 ? 0.1731 0.1605 0.1641 0.0156 -0.0105 -0.0108 100 LEU A C 758 O O . LEU A 100 ? 0.1833 0.1717 0.1772 0.0204 -0.0151 -0.0066 100 LEU A O 759 C CB . LEU A 100 ? 0.1641 0.1600 0.1593 0.0103 -0.0052 -0.0090 100 LEU A CB 760 C CG . LEU A 100 ? 0.1500 0.1404 0.1674 0.0121 0.0029 -0.0175 100 LEU A CG 761 C CD1 . LEU A 100 ? 0.1560 0.1601 0.1428 -0.0183 0.0060 -0.0346 100 LEU A CD1 762 C CD2 . LEU A 100 ? 0.1645 0.1707 0.1857 -0.0040 -0.0044 0.0020 100 LEU A CD2 763 N N . CYS A 101 ? 0.1547 0.1573 0.1599 0.0149 -0.0114 -0.0134 101 CYS A N 764 C CA . CYS A 101 ? 0.1631 0.1583 0.1627 0.0193 -0.0114 -0.0154 101 CYS A CA 765 C C . CYS A 101 ? 0.1620 0.1573 0.1682 0.0220 -0.0137 -0.0148 101 CYS A C 766 O O . CYS A 101 ? 0.1753 0.1829 0.1713 0.0304 -0.0199 -0.0153 101 CYS A O 767 C CB . CYS A 101 ? 0.1478 0.1508 0.1580 0.0199 -0.0094 -0.0165 101 CYS A CB 768 S SG . CYS A 101 ? 0.1910 0.1757 0.1734 0.0191 -0.0171 -0.0141 101 CYS A SG 769 N N . GLY A 102 ? 0.1564 0.1540 0.1695 0.0170 -0.0147 -0.0141 102 GLY A N 770 C CA . GLY A 102 ? 0.1491 0.1503 0.1797 0.0135 -0.0072 -0.0042 102 GLY A CA 771 C C . GLY A 102 ? 0.1469 0.1461 0.1760 0.0110 -0.0117 0.0029 102 GLY A C 772 O O . GLY A 102 ? 0.1514 0.1479 0.2051 0.0081 -0.0069 0.0059 102 GLY A O 773 N N . VAL A 103 ? 0.1421 0.1471 0.1760 0.0088 -0.0142 0.0027 103 VAL A N 774 C CA . VAL A 103 ? 0.1461 0.1490 0.1887 0.0047 -0.0212 0.0064 103 VAL A CA 775 C C . VAL A 103 ? 0.1479 0.1519 0.1822 0.0032 -0.0207 0.0040 103 VAL A C 776 O O . VAL A 103 ? 0.1329 0.1423 0.1799 0.0023 -0.0052 0.0025 103 VAL A O 777 C CB . VAL A 103 ? 0.1491 0.1512 0.1913 0.0053 -0.0235 0.0059 103 VAL A CB 778 C CG1 . VAL A 103 ? 0.1378 0.1629 0.2091 -0.0020 -0.0311 0.0072 103 VAL A CG1 779 C CG2 . VAL A 103 ? 0.1615 0.1591 0.1990 0.0036 -0.0315 0.0149 103 VAL A CG2 780 N N . LYS A 104 ? 0.1471 0.1533 0.1744 0.0068 -0.0245 0.0112 104 LYS A N 781 C CA . LYS A 104 ? 0.1579 0.1654 0.1708 0.0086 -0.0287 -0.0002 104 LYS A CA 782 C C . LYS A 104 ? 0.1608 0.1741 0.1754 0.0067 -0.0265 0.0041 104 LYS A C 783 O O . LYS A 104 ? 0.1593 0.1779 0.1792 0.0138 -0.0262 0.0033 104 LYS A O 784 C CB . LYS A 104 ? 0.1605 0.1595 0.1605 0.0189 -0.0373 0.0066 104 LYS A CB 785 C CG . LYS A 104 ? 0.1370 0.1882 0.1583 0.0153 -0.0566 0.0094 104 LYS A CG 786 C CD . LYS A 104 ? 0.1479 0.1889 0.1290 0.0153 -0.0657 0.0319 104 LYS A CD 787 C CE . LYS A 104 ? 0.1070 0.2102 0.1240 0.0255 -0.0828 0.0249 104 LYS A CE 788 N NZ . LYS A 104 ? 0.1124 0.2454 0.1108 0.0406 -0.0520 0.0120 104 LYS A NZ 789 N N . GLY A 105 ? 0.1674 0.1691 0.1762 0.0003 -0.0269 -0.0022 105 GLY A N 790 C CA . GLY A 105 ? 0.1577 0.1722 0.1844 -0.0098 -0.0260 0.0030 105 GLY A CA 791 C C . GLY A 105 ? 0.1585 0.1801 0.1888 -0.0083 -0.0246 0.0010 105 GLY A C 792 O O . GLY A 105 ? 0.1459 0.1699 0.1772 -0.0137 -0.0226 0.0069 105 GLY A O 793 N N . ASN A 106 ? 0.1490 0.1813 0.1915 -0.0123 -0.0268 0.0005 106 ASN A N 794 C CA . ASN A 106 ? 0.1508 0.1823 0.1870 0.0025 -0.0235 0.0055 106 ASN A CA 795 C C . ASN A 106 ? 0.1565 0.1830 0.1815 0.0007 -0.0218 0.0025 106 ASN A C 796 O O . ASN A 106 ? 0.1490 0.1798 0.1774 0.0044 -0.0243 0.0063 106 ASN A O 797 C CB . ASN A 106 ? 0.1485 0.1798 0.1962 -0.0015 -0.0207 0.0029 106 ASN A CB 798 C CG . ASN A 106 ? 0.1457 0.1951 0.1986 0.0156 -0.0149 0.0033 106 ASN A CG 799 O OD1 . ASN A 106 ? 0.1218 0.2135 0.1866 0.0415 0.0048 -0.0011 106 ASN A OD1 800 N ND2 . ASN A 106 ? 0.0993 0.1612 0.2167 0.0262 -0.0323 0.0308 106 ASN A ND2 801 N N . PHE A 107 ? 0.1544 0.1832 0.1682 0.0088 -0.0234 0.0053 107 PHE A N 802 C CA . PHE A 107 ? 0.1665 0.1877 0.1687 0.0101 -0.0222 0.0058 107 PHE A CA 803 C C . PHE A 107 ? 0.1709 0.1949 0.1779 0.0129 -0.0209 0.0093 107 PHE A C 804 O O . PHE A 107 ? 0.1854 0.2004 0.1635 0.0016 -0.0260 0.0037 107 PHE A O 805 C CB . PHE A 107 ? 0.1595 0.1832 0.1687 0.0194 -0.0246 0.0075 107 PHE A CB 806 C CG . PHE A 107 ? 0.1769 0.1996 0.1765 0.0152 -0.0156 0.0125 107 PHE A CG 807 C CD1 . PHE A 107 ? 0.1755 0.1843 0.1702 0.0400 -0.0147 -0.0003 107 PHE A CD1 808 C CD2 . PHE A 107 ? 0.1538 0.2100 0.1635 0.0277 -0.0101 0.0311 107 PHE A CD2 809 C CE1 . PHE A 107 ? 0.1594 0.1972 0.1941 0.0422 -0.0233 0.0094 107 PHE A CE1 810 C CE2 . PHE A 107 ? 0.1665 0.1965 0.1537 0.0476 0.0136 0.0106 107 PHE A CE2 811 C CZ . PHE A 107 ? 0.1713 0.1981 0.1839 0.0310 -0.0058 0.0123 107 PHE A CZ 812 N N . GLN A 108 ? 0.1809 0.1946 0.1853 0.0173 -0.0208 0.0164 108 GLN A N 813 C CA . GLN A 108 ? 0.1812 0.1904 0.1876 0.0136 -0.0217 0.0099 108 GLN A CA 814 C C . GLN A 108 ? 0.1805 0.1958 0.1898 0.0100 -0.0186 0.0057 108 GLN A C 815 O O . GLN A 108 ? 0.1773 0.1912 0.1693 0.0154 -0.0280 -0.0048 108 GLN A O 816 C CB . GLN A 108 ? 0.1937 0.2015 0.1966 0.0100 -0.0220 0.0140 108 GLN A CB 817 C CG . GLN A 108 ? 0.2574 0.2101 0.2643 0.0045 -0.0121 0.0135 108 GLN A CG 818 C CD . GLN A 108 ? 0.3268 0.2693 0.3522 -0.0119 -0.0028 0.0113 108 GLN A CD 819 O OE1 . GLN A 108 ? 0.3730 0.2716 0.3880 -0.0500 -0.0522 0.0412 108 GLN A OE1 820 N NE2 . GLN A 108 ? 0.3842 0.2759 0.4437 0.0116 -0.0003 -0.0039 108 GLN A NE2 821 N N . THR A 109 ? 0.1601 0.1795 0.1874 0.0112 -0.0166 0.0040 109 THR A N 822 C CA . THR A 109 ? 0.1506 0.1882 0.1935 -0.0032 -0.0079 0.0015 109 THR A CA 823 C C . THR A 109 ? 0.1521 0.1864 0.1878 -0.0052 -0.0034 0.0039 109 THR A C 824 O O . THR A 109 ? 0.1560 0.1976 0.1790 -0.0061 -0.0069 0.0107 109 THR A O 825 C CB . THR A 109 ? 0.1462 0.1901 0.1944 0.0009 -0.0084 -0.0010 109 THR A CB 826 O OG1 . THR A 109 ? 0.1268 0.1563 0.2107 0.0063 -0.0022 0.0014 109 THR A OG1 827 C CG2 . THR A 109 ? 0.1203 0.1663 0.2036 -0.0295 0.0075 -0.0021 109 THR A CG2 828 N N . ILE A 110 ? 0.1464 0.1829 0.1899 -0.0068 -0.0009 0.0019 110 ILE A N 829 C CA . ILE A 110 ? 0.1441 0.1613 0.1911 -0.0011 0.0071 -0.0045 110 ILE A CA 830 C C . ILE A 110 ? 0.1408 0.1683 0.1852 -0.0028 0.0087 -0.0043 110 ILE A C 831 O O . ILE A 110 ? 0.1327 0.1649 0.1910 -0.0022 0.0079 -0.0032 110 ILE A O 832 C CB . ILE A 110 ? 0.1390 0.1535 0.1903 0.0013 0.0121 -0.0087 110 ILE A CB 833 C CG1 . ILE A 110 ? 0.1530 0.1567 0.1873 0.0162 0.0045 -0.0145 110 ILE A CG1 834 C CG2 . ILE A 110 ? 0.1503 0.1544 0.2043 0.0035 0.0204 -0.0013 110 ILE A CG2 835 C CD1 . ILE A 110 ? 0.1399 0.1376 0.1949 0.0008 0.0155 -0.0210 110 ILE A CD1 836 N N . GLY A 111 ? 0.1454 0.1711 0.1840 -0.0083 0.0045 -0.0029 111 GLY A N 837 C CA . GLY A 111 ? 0.1429 0.1729 0.1878 -0.0028 -0.0024 -0.0055 111 GLY A CA 838 C C . GLY A 111 ? 0.1586 0.1824 0.1961 -0.0049 -0.0157 -0.0053 111 GLY A C 839 O O . GLY A 111 ? 0.1660 0.1922 0.2037 -0.0020 -0.0223 -0.0078 111 GLY A O 840 N N . LEU A 112 ? 0.1597 0.1920 0.1874 -0.0030 -0.0131 -0.0075 112 LEU A N 841 C CA . LEU A 112 ? 0.1549 0.1876 0.1859 0.0010 -0.0209 -0.0062 112 LEU A CA 842 C C . LEU A 112 ? 0.1562 0.1973 0.1931 0.0058 -0.0139 -0.0002 112 LEU A C 843 O O . LEU A 112 ? 0.1556 0.2056 0.1865 0.0004 -0.0163 0.0023 112 LEU A O 844 C CB . LEU A 112 ? 0.1538 0.1976 0.1874 0.0030 -0.0249 -0.0072 112 LEU A CB 845 C CG . LEU A 112 ? 0.1560 0.1735 0.1792 -0.0044 -0.0519 -0.0090 112 LEU A CG 846 C CD1 . LEU A 112 ? 0.1380 0.1954 0.1959 -0.0163 -0.0491 0.0003 112 LEU A CD1 847 C CD2 . LEU A 112 ? 0.1413 0.1740 0.1933 0.0164 -0.0579 0.0091 112 LEU A CD2 848 N N . SER A 113 ? 0.1501 0.1945 0.1978 0.0156 -0.0131 0.0017 113 SER A N 849 C CA . SER A 113 ? 0.1534 0.1977 0.2017 0.0181 -0.0159 0.0009 113 SER A CA 850 C C . SER A 113 ? 0.1483 0.2014 0.1994 0.0134 -0.0141 0.0040 113 SER A C 851 O O . SER A 113 ? 0.1474 0.1916 0.2004 0.0087 -0.0132 0.0050 113 SER A O 852 C CB . SER A 113 ? 0.1371 0.2002 0.2050 0.0228 -0.0152 -0.0041 113 SER A CB 853 O OG . SER A 113 ? 0.1618 0.2128 0.2279 0.0277 -0.0086 0.0049 113 SER A OG 854 N N . ALA A 114 ? 0.1514 0.2015 0.1903 0.0117 -0.0252 0.0086 114 ALA A N 855 C CA . ALA A 114 ? 0.1584 0.2075 0.1892 0.0038 -0.0255 0.0067 114 ALA A CA 856 C C . ALA A 114 ? 0.1642 0.2070 0.1907 -0.0009 -0.0296 0.0059 114 ALA A C 857 O O . ALA A 114 ? 0.1784 0.2159 0.1952 -0.0003 -0.0325 0.0048 114 ALA A O 858 C CB . ALA A 114 ? 0.1537 0.2083 0.1796 -0.0029 -0.0271 0.0074 114 ALA A CB 859 N N . ALA A 115 ? 0.1582 0.2059 0.1976 -0.0004 -0.0329 0.0068 115 ALA A N 860 C CA . ALA A 115 ? 0.1540 0.1985 0.2035 -0.0053 -0.0301 0.0046 115 ALA A CA 861 C C . ALA A 115 ? 0.1541 0.2024 0.2035 -0.0060 -0.0302 0.0089 115 ALA A C 862 O O . ALA A 115 ? 0.1365 0.1821 0.2060 -0.0096 -0.0384 0.0016 115 ALA A O 863 C CB . ALA A 115 ? 0.1552 0.2084 0.2074 -0.0036 -0.0394 0.0091 115 ALA A CB 864 N N . ALA A 116 ? 0.1536 0.2003 0.1964 -0.0080 -0.0190 0.0097 116 ALA A N 865 C CA . ALA A 116 ? 0.1575 0.1949 0.2017 -0.0125 -0.0197 0.0057 116 ALA A CA 866 C C . ALA A 116 ? 0.1557 0.1986 0.2033 -0.0102 -0.0154 0.0046 116 ALA A C 867 O O . ALA A 116 ? 0.1580 0.2005 0.2078 -0.0117 -0.0238 -0.0064 116 ALA A O 868 C CB . ALA A 116 ? 0.1496 0.1919 0.1779 -0.0178 -0.0117 0.0138 116 ALA A CB 869 N N . ARG A 117 ? 0.1531 0.1963 0.2135 -0.0172 -0.0165 0.0004 117 ARG A N 870 C CA . ARG A 117 ? 0.1568 0.1961 0.2173 -0.0114 -0.0120 0.0015 117 ARG A CA 871 C C . ARG A 117 ? 0.1662 0.1997 0.2171 -0.0101 -0.0186 0.0039 117 ARG A C 872 O O . ARG A 117 ? 0.1786 0.2100 0.2147 -0.0015 -0.0105 0.0018 117 ARG A O 873 C CB . ARG A 117 ? 0.1596 0.2044 0.2265 -0.0216 -0.0077 -0.0014 117 ARG A CB 874 C CG . ARG A 117 ? 0.1710 0.2281 0.2335 -0.0094 -0.0121 -0.0144 117 ARG A CG 875 C CD . ARG A 117 ? 0.1998 0.2576 0.2583 -0.0180 0.0039 -0.0141 117 ARG A CD 876 N NE . ARG A 117 ? 0.2051 0.2602 0.2680 -0.0444 0.0119 -0.0246 117 ARG A NE 877 C CZ . ARG A 117 ? 0.2030 0.2743 0.2615 -0.0357 0.0010 -0.0155 117 ARG A CZ 878 N NH1 . ARG A 117 ? 0.1839 0.2654 0.2243 -0.0587 -0.0111 0.0050 117 ARG A NH1 879 N NH2 . ARG A 117 ? 0.1931 0.2648 0.2611 -0.0418 0.0026 -0.0051 117 ARG A NH2 880 N N . PHE A 118 ? 0.1655 0.1980 0.2187 0.0019 -0.0230 0.0011 118 PHE A N 881 C CA . PHE A 118 ? 0.1731 0.2043 0.2201 0.0021 -0.0348 0.0068 118 PHE A CA 882 C C . PHE A 118 ? 0.1766 0.2053 0.2241 0.0028 -0.0333 0.0116 118 PHE A C 883 O O . PHE A 118 ? 0.1789 0.2043 0.2250 -0.0096 -0.0383 0.0177 118 PHE A O 884 C CB . PHE A 118 ? 0.1704 0.1943 0.2172 0.0064 -0.0338 0.0025 118 PHE A CB 885 C CG . PHE A 118 ? 0.1698 0.2066 0.2225 0.0168 -0.0502 -0.0042 118 PHE A CG 886 C CD1 . PHE A 118 ? 0.1523 0.1914 0.2050 0.0080 -0.0423 -0.0194 118 PHE A CD1 887 C CD2 . PHE A 118 ? 0.1792 0.1890 0.2128 0.0258 -0.0536 -0.0092 118 PHE A CD2 888 C CE1 . PHE A 118 ? 0.1847 0.1989 0.2181 0.0219 -0.0471 -0.0214 118 PHE A CE1 889 C CE2 . PHE A 118 ? 0.1861 0.2193 0.2056 0.0310 -0.0465 -0.0150 118 PHE A CE2 890 C CZ . PHE A 118 ? 0.1802 0.2037 0.2161 0.0139 -0.0504 -0.0043 118 PHE A CZ 891 N N . ASN A 119 ? 0.1800 0.2041 0.2221 0.0037 -0.0367 0.0216 119 ASN A N 892 C CA . ASN A 119 ? 0.1800 0.1934 0.2241 0.0073 -0.0410 0.0179 119 ASN A CA 893 C C . ASN A 119 ? 0.1797 0.2055 0.2266 0.0121 -0.0427 0.0204 119 ASN A C 894 O O . ASN A 119 ? 0.1765 0.2094 0.2309 0.0123 -0.0553 0.0196 119 ASN A O 895 C CB . ASN A 119 ? 0.1882 0.1891 0.2236 0.0090 -0.0347 0.0190 119 ASN A CB 896 C CG . ASN A 119 ? 0.2170 0.1807 0.2308 0.0013 -0.0405 0.0216 119 ASN A CG 897 O OD1 . ASN A 119 ? 0.2209 0.2082 0.2352 0.0260 -0.0571 0.0117 119 ASN A OD1 898 N ND2 . ASN A 119 ? 0.2595 0.1746 0.2500 -0.0027 -0.0226 -0.0087 119 ASN A ND2 899 N N . GLN A 120 ? 0.1735 0.2230 0.2234 0.0134 -0.0399 0.0249 120 GLN A N 900 C CA . GLN A 120 ? 0.1952 0.2441 0.2383 0.0199 -0.0343 0.0291 120 GLN A CA 901 C C . GLN A 120 ? 0.1888 0.2439 0.2280 0.0199 -0.0396 0.0248 120 GLN A C 902 O O . GLN A 120 ? 0.1850 0.2307 0.2235 0.0232 -0.0472 0.0231 120 GLN A O 903 C CB . GLN A 120 ? 0.1787 0.2411 0.2320 0.0159 -0.0342 0.0333 120 GLN A CB 904 C CG . GLN A 120 ? 0.2148 0.2779 0.2533 0.0238 -0.0243 0.0319 120 GLN A CG 905 C CD . GLN A 120 ? 0.2289 0.2892 0.2899 0.0231 -0.0276 0.0492 120 GLN A CD 906 O OE1 . GLN A 120 ? 0.3254 0.3764 0.4094 0.0106 0.0163 0.0589 120 GLN A OE1 907 N NE2 . GLN A 120 ? 0.3145 0.3736 0.3625 0.0055 -0.0155 0.0394 120 GLN A NE2 908 N N . CYS A 121 ? 0.1999 0.2542 0.2295 0.0200 -0.0420 0.0142 121 CYS A N 909 C CA . CYS A 121 ? 0.2059 0.2531 0.2240 0.0177 -0.0395 0.0090 121 CYS A CA 910 C C . CYS A 121 ? 0.2093 0.2518 0.2191 0.0107 -0.0345 0.0034 121 CYS A C 911 O O . CYS A 121 ? 0.2065 0.2486 0.2149 0.0111 -0.0314 0.0064 121 CYS A O 912 C CB . CYS A 121 ? 0.2168 0.2550 0.2329 0.0174 -0.0419 0.0088 121 CYS A CB 913 S SG . CYS A 121 ? 0.2565 0.2893 0.2482 0.0204 -0.0559 0.0000 121 CYS A SG 914 N N . ASN A 122 ? 0.1985 0.2469 0.2176 0.0081 -0.0335 -0.0031 122 ASN A N 915 C CA . ASN A 122 ? 0.2066 0.2483 0.2352 0.0029 -0.0282 -0.0018 122 ASN A CA 916 C C . ASN A 122 ? 0.1971 0.2380 0.2283 0.0040 -0.0275 -0.0029 122 ASN A C 917 O O . ASN A 122 ? 0.1952 0.2441 0.2399 0.0045 -0.0307 -0.0050 122 ASN A O 918 C CB . ASN A 122 ? 0.2134 0.2490 0.2475 -0.0017 -0.0271 -0.0008 122 ASN A CB 919 C CG . ASN A 122 ? 0.2493 0.2794 0.2953 -0.0086 -0.0081 0.0006 122 ASN A CG 920 O OD1 . ASN A 122 ? 0.2918 0.2620 0.2821 -0.0292 -0.0056 0.0155 122 ASN A OD1 921 N ND2 . ASN A 122 ? 0.3248 0.2690 0.3746 -0.0276 0.0174 -0.0068 122 ASN A ND2 922 N N . THR A 123 ? 0.1950 0.2316 0.2090 0.0128 -0.0269 0.0019 123 THR A N 923 C CA . THR A 123 ? 0.1914 0.2247 0.1967 0.0099 -0.0231 0.0023 123 THR A CA 924 C C . THR A 123 ? 0.1910 0.2227 0.1975 0.0136 -0.0192 0.0071 123 THR A C 925 O O . THR A 123 ? 0.1905 0.2185 0.1991 0.0145 -0.0135 0.0078 123 THR A O 926 C CB . THR A 123 ? 0.1900 0.2238 0.1885 0.0115 -0.0224 0.0019 123 THR A CB 927 O OG1 . THR A 123 ? 0.1861 0.2215 0.1580 -0.0001 -0.0357 0.0040 123 THR A OG1 928 C CG2 . THR A 123 ? 0.1859 0.2277 0.2003 0.0134 -0.0154 -0.0021 123 THR A CG2 929 N N . THR A 124 ? 0.1851 0.2202 0.1934 0.0158 -0.0198 0.0089 124 THR A N 930 C CA . THR A 124 ? 0.1836 0.2185 0.1977 0.0118 -0.0168 0.0104 124 THR A CA 931 C C . THR A 124 ? 0.1859 0.2311 0.1915 0.0091 -0.0204 0.0065 124 THR A C 932 O O . THR A 124 ? 0.1708 0.2391 0.1906 0.0080 -0.0293 0.0039 124 THR A O 933 C CB . THR A 124 ? 0.1811 0.2131 0.1962 0.0087 -0.0153 0.0102 124 THR A CB 934 O OG1 . THR A 124 ? 0.2045 0.2010 0.1990 0.0061 -0.0160 0.0214 124 THR A OG1 935 C CG2 . THR A 124 ? 0.1798 0.2207 0.2213 -0.0016 -0.0039 0.0104 124 THR A CG2 936 N N . ARG A 125 ? 0.1811 0.2341 0.1853 0.0115 -0.0238 0.0036 125 ARG A N 937 C CA . ARG A 125 ? 0.1945 0.2283 0.1824 0.0061 -0.0244 0.0019 125 ARG A CA 938 C C . ARG A 125 ? 0.1915 0.2298 0.1931 0.0062 -0.0282 0.0047 125 ARG A C 939 O O . ARG A 125 ? 0.1848 0.2344 0.1920 0.0029 -0.0218 0.0043 125 ARG A O 940 C CB . ARG A 125 ? 0.1899 0.2307 0.1787 0.0044 -0.0267 0.0016 125 ARG A CB 941 C CG . ARG A 125 ? 0.2406 0.2463 0.2020 0.0004 -0.0302 0.0000 125 ARG A CG 942 C CD . ARG A 125 ? 0.3071 0.3197 0.2481 -0.0118 -0.0171 -0.0090 125 ARG A CD 943 N NE . ARG A 125 ? 0.2914 0.3464 0.2791 -0.0216 -0.0144 -0.0137 125 ARG A NE 944 C CZ . ARG A 125 ? 0.3100 0.3577 0.3063 -0.0327 -0.0250 -0.0180 125 ARG A CZ 945 N NH1 . ARG A 125 ? 0.3465 0.4126 0.3307 -0.0457 -0.0224 -0.0134 125 ARG A NH1 946 N NH2 . ARG A 125 ? 0.3325 0.3620 0.3334 -0.0410 -0.0510 -0.0089 125 ARG A NH2 947 N N . GLY A 126 ? 0.1834 0.2148 0.1892 0.0044 -0.0353 0.0023 126 GLY A N 948 C CA . GLY A 126 ? 0.1862 0.2149 0.2011 0.0026 -0.0307 0.0058 126 GLY A CA 949 C C . GLY A 126 ? 0.1836 0.2065 0.1954 0.0002 -0.0315 0.0026 126 GLY A C 950 O O . GLY A 126 ? 0.1918 0.2052 0.2223 -0.0007 -0.0323 0.0059 126 GLY A O 951 N N . ASN A 127 ? 0.1810 0.2031 0.1962 -0.0039 -0.0281 0.0112 127 ASN A N 952 C CA . ASN A 127 ? 0.1855 0.2016 0.1869 -0.0024 -0.0270 0.0090 127 ASN A CA 953 C C . ASN A 127 ? 0.1899 0.2032 0.1962 0.0001 -0.0310 0.0080 127 ASN A C 954 O O . ASN A 127 ? 0.1903 0.2023 0.1985 -0.0007 -0.0286 0.0138 127 ASN A O 955 C CB . ASN A 127 ? 0.1875 0.2077 0.1875 -0.0071 -0.0317 0.0156 127 ASN A CB 956 C CG . ASN A 127 ? 0.2095 0.2293 0.1730 0.0004 -0.0211 0.0084 127 ASN A CG 957 O OD1 . ASN A 127 ? 0.2506 0.2694 0.2004 -0.0091 -0.0187 0.0172 127 ASN A OD1 958 N ND2 . ASN A 127 ? 0.2127 0.2172 0.1935 -0.0124 -0.0488 -0.0174 127 ASN A ND2 959 N N . GLU A 128 ? 0.1922 0.2076 0.1900 0.0035 -0.0255 0.0037 128 GLU A N 960 C CA . GLU A 128 ? 0.1893 0.2113 0.2015 0.0043 -0.0321 -0.0014 128 GLU A CA 961 C C . GLU A 128 ? 0.1981 0.2144 0.2147 0.0106 -0.0286 0.0029 128 GLU A C 962 O O . GLU A 128 ? 0.1892 0.2127 0.2169 0.0208 -0.0338 0.0060 128 GLU A O 963 C CB . GLU A 128 ? 0.1982 0.2217 0.2061 0.0031 -0.0281 -0.0037 128 GLU A CB 964 C CG . GLU A 128 ? 0.1965 0.2142 0.1984 -0.0081 -0.0334 -0.0215 128 GLU A CG 965 C CD . GLU A 128 ? 0.2475 0.2416 0.2175 0.0030 -0.0287 -0.0172 128 GLU A CD 966 O OE1 . GLU A 128 ? 0.2372 0.2105 0.2116 0.0160 -0.0215 -0.0037 128 GLU A OE1 967 O OE2 . GLU A 128 ? 0.2438 0.2555 0.2001 0.0023 -0.0487 -0.0093 128 GLU A OE2 968 N N . VAL A 129 ? 0.1781 0.2042 0.2154 0.0114 -0.0268 0.0065 129 VAL A N 969 C CA . VAL A 129 ? 0.1864 0.2078 0.2236 0.0122 -0.0212 0.0152 129 VAL A CA 970 C C . VAL A 129 ? 0.1821 0.2074 0.2276 0.0124 -0.0171 0.0171 129 VAL A C 971 O O . VAL A 129 ? 0.1893 0.2179 0.2449 0.0139 -0.0121 0.0236 129 VAL A O 972 C CB . VAL A 129 ? 0.1830 0.2071 0.2244 0.0171 -0.0192 0.0130 129 VAL A CB 973 C CG1 . VAL A 129 ? 0.2091 0.2209 0.2177 0.0012 -0.0180 0.0128 129 VAL A CG1 974 C CG2 . VAL A 129 ? 0.2194 0.1932 0.2286 0.0255 -0.0291 0.0158 129 VAL A CG2 975 N N . ILE A 130 ? 0.1801 0.1997 0.2273 0.0081 -0.0139 0.0237 130 ILE A N 976 C CA . ILE A 130 ? 0.1825 0.2112 0.2259 0.0069 -0.0086 0.0248 130 ILE A CA 977 C C . ILE A 130 ? 0.1800 0.1975 0.2166 0.0010 -0.0063 0.0221 130 ILE A C 978 O O . ILE A 130 ? 0.1773 0.2041 0.2058 -0.0003 -0.0003 0.0178 130 ILE A O 979 C CB . ILE A 130 ? 0.1839 0.2230 0.2341 0.0045 -0.0144 0.0346 130 ILE A CB 980 C CG1 . ILE A 130 ? 0.2071 0.2572 0.2442 0.0115 -0.0115 0.0142 130 ILE A CG1 981 C CG2 . ILE A 130 ? 0.1760 0.2389 0.2353 0.0118 0.0039 0.0427 130 ILE A CG2 982 C CD1 . ILE A 130 ? 0.2523 0.2749 0.2591 0.0229 -0.0185 -0.0043 130 ILE A CD1 983 N N . SER A 131 ? 0.1741 0.1830 0.2116 0.0010 -0.0045 0.0143 131 SER A N 984 C CA . SER A 131 ? 0.1739 0.1698 0.2065 -0.0065 0.0003 0.0052 131 SER A CA 985 C C . SER A 131 ? 0.1692 0.1667 0.2001 -0.0047 0.0053 0.0013 131 SER A C 986 O O . SER A 131 ? 0.1541 0.1553 0.2072 0.0055 0.0037 -0.0007 131 SER A O 987 C CB . SER A 131 ? 0.1653 0.1656 0.1935 -0.0080 0.0013 0.0032 131 SER A CB 988 O OG . SER A 131 ? 0.1984 0.1600 0.2292 -0.0154 0.0085 -0.0051 131 SER A OG 989 N N . VAL A 132 ? 0.1631 0.1624 0.1956 -0.0071 0.0070 -0.0025 132 VAL A N 990 C CA . VAL A 132 ? 0.1788 0.1668 0.1970 -0.0112 0.0105 -0.0019 132 VAL A CA 991 C C . VAL A 132 ? 0.1804 0.1641 0.1864 -0.0017 0.0051 0.0018 132 VAL A C 992 O O . VAL A 132 ? 0.1835 0.1576 0.1899 0.0041 0.0050 0.0042 132 VAL A O 993 C CB . VAL A 132 ? 0.1774 0.1675 0.1897 -0.0239 0.0056 0.0000 132 VAL A CB 994 C CG1 . VAL A 132 ? 0.1927 0.1753 0.2044 -0.0355 0.0119 -0.0095 132 VAL A CG1 995 C CG2 . VAL A 132 ? 0.1721 0.1808 0.2050 -0.0276 0.0236 -0.0081 132 VAL A CG2 996 N N . MET A 133 ? 0.1842 0.1664 0.1767 0.0104 0.0070 0.0006 133 MET A N 997 C CA . MET A 133 ? 0.1923 0.1664 0.1773 0.0181 0.0133 0.0108 133 MET A CA 998 C C . MET A 133 ? 0.1906 0.1721 0.1797 0.0154 0.0073 0.0073 133 MET A C 999 O O . MET A 133 ? 0.1905 0.1711 0.1654 0.0167 0.0077 0.0210 133 MET A O 1000 C CB . MET A 133 ? 0.1834 0.1611 0.1703 0.0229 0.0167 0.0071 133 MET A CB 1001 C CG . MET A 133 ? 0.1893 0.1558 0.1683 0.0338 0.0223 0.0150 133 MET A CG 1002 S SD . MET A 133 ? 0.2096 0.1599 0.1944 0.0272 0.0216 0.0179 133 MET A SD 1003 C CE . MET A 133 ? 0.1646 0.1528 0.1365 0.0187 -0.0027 -0.0004 133 MET A CE 1004 N N . ASN A 134 ? 0.1984 0.1711 0.1834 0.0136 0.0013 0.0045 134 ASN A N 1005 C CA . ASN A 134 ? 0.2039 0.1749 0.1862 0.0146 -0.0061 0.0053 134 ASN A CA 1006 C C . ASN A 134 ? 0.2010 0.1733 0.1888 0.0109 -0.0043 0.0071 134 ASN A C 1007 O O . ASN A 134 ? 0.2078 0.1646 0.1831 0.0125 -0.0047 0.0140 134 ASN A O 1008 C CB . ASN A 134 ? 0.2054 0.1913 0.1849 0.0194 -0.0214 -0.0019 134 ASN A CB 1009 C CG . ASN A 134 ? 0.2415 0.2077 0.2158 0.0245 -0.0350 -0.0100 134 ASN A CG 1010 O OD1 . ASN A 134 ? 0.2469 0.2402 0.2425 0.0417 -0.0688 -0.0222 134 ASN A OD1 1011 N ND2 . ASN A 134 ? 0.2693 0.2448 0.1675 0.0312 -0.0754 -0.0623 134 ASN A ND2 1012 N N . ARG A 135 ? 0.2023 0.1589 0.1898 0.0103 -0.0034 0.0010 135 ARG A N 1013 C CA . ARG A 135 ? 0.2091 0.1827 0.2011 0.0118 0.0008 0.0042 135 ARG A CA 1014 C C . ARG A 135 ? 0.2081 0.1818 0.2014 0.0114 -0.0001 0.0052 135 ARG A C 1015 O O . ARG A 135 ? 0.2033 0.1894 0.2171 0.0156 -0.0002 0.0084 135 ARG A O 1016 C CB . ARG A 135 ? 0.2057 0.1705 0.1953 0.0125 0.0056 -0.0052 135 ARG A CB 1017 C CG . ARG A 135 ? 0.2345 0.1781 0.2115 0.0213 0.0089 -0.0046 135 ARG A CG 1018 C CD . ARG A 135 ? 0.2774 0.1807 0.2066 0.0319 -0.0210 0.0295 135 ARG A CD 1019 N NE . ARG A 135 ? 0.2766 0.2071 0.2608 0.0230 -0.0336 0.0197 135 ARG A NE 1020 C CZ . ARG A 135 ? 0.2648 0.2178 0.2653 0.0267 -0.0270 0.0168 135 ARG A CZ 1021 N NH1 . ARG A 135 ? 0.2432 0.1629 0.2457 0.0030 -0.0199 0.0371 135 ARG A NH1 1022 N NH2 . ARG A 135 ? 0.2595 0.2323 0.2847 0.0244 -0.0349 0.0015 135 ARG A NH2 1023 N N . ALA A 136 ? 0.2051 0.1839 0.1882 0.0173 0.0000 0.0021 136 ALA A N 1024 C CA . ALA A 136 ? 0.2045 0.1911 0.1903 0.0188 0.0013 0.0003 136 ALA A CA 1025 C C . ALA A 136 ? 0.2050 0.1945 0.2023 0.0220 -0.0041 0.0033 136 ALA A C 1026 O O . ALA A 136 ? 0.2013 0.1893 0.1992 0.0206 -0.0032 -0.0003 136 ALA A O 1027 C CB . ALA A 136 ? 0.2037 0.1794 0.1762 0.0222 -0.0027 0.0083 136 ALA A CB 1028 N N . LYS A 137 ? 0.2059 0.2043 0.2093 0.0227 -0.0022 0.0007 137 LYS A N 1029 C CA . LYS A 137 ? 0.2195 0.2167 0.2282 0.0242 -0.0022 0.0058 137 LYS A CA 1030 C C . LYS A 137 ? 0.2314 0.2199 0.2401 0.0222 -0.0004 0.0076 137 LYS A C 1031 O O . LYS A 137 ? 0.2266 0.2158 0.2376 0.0257 0.0016 0.0122 137 LYS A O 1032 C CB . LYS A 137 ? 0.2214 0.2049 0.2229 0.0174 -0.0025 0.0016 137 LYS A CB 1033 C CG . LYS A 137 ? 0.2194 0.2334 0.2353 0.0202 0.0012 0.0180 137 LYS A CG 1034 C CD . LYS A 137 ? 0.2190 0.2568 0.2469 0.0476 0.0169 0.0054 137 LYS A CD 1035 C CE . LYS A 137 ? 0.2024 0.3043 0.2682 0.0531 0.0220 0.0298 137 LYS A CE 1036 N NZ . LYS A 137 ? 0.2138 0.3037 0.2328 0.0644 0.0242 0.0130 137 LYS A NZ 1037 N N . LYS A 138 ? 0.2407 0.2327 0.2529 0.0248 0.0054 0.0110 138 LYS A N 1038 C CA . LYS A 138 ? 0.2583 0.2493 0.2839 0.0245 0.0028 0.0205 138 LYS A CA 1039 C C . LYS A 138 ? 0.2620 0.2464 0.2824 0.0252 0.0029 0.0223 138 LYS A C 1040 O O . LYS A 138 ? 0.2629 0.2253 0.2879 0.0290 -0.0023 0.0384 138 LYS A O 1041 C CB . LYS A 138 ? 0.2701 0.2705 0.2930 0.0208 0.0076 0.0182 138 LYS A CB 1042 C CG . LYS A 138 ? 0.3040 0.3152 0.3495 0.0108 -0.0033 0.0081 138 LYS A CG 1043 C CD . LYS A 138 ? 0.3354 0.3206 0.3842 0.0173 0.0089 -0.0046 138 LYS A CD 1044 C CE . LYS A 138 ? 0.3182 0.2842 0.3574 0.0127 0.0039 -0.0056 138 LYS A CE 1045 N NZ . LYS A 138 ? 0.3333 0.3872 0.3950 -0.0138 -0.0207 0.0071 138 LYS A NZ 1046 N N . ALA A 139 ? 0.2668 0.2419 0.2790 0.0258 -0.0038 0.0249 139 ALA A N 1047 C CA . ALA A 139 ? 0.2746 0.2450 0.2774 0.0270 -0.0019 0.0252 139 ALA A CA 1048 C C . ALA A 139 ? 0.2741 0.2414 0.2745 0.0249 -0.0045 0.0260 139 ALA A C 1049 O O . ALA A 139 ? 0.2965 0.2568 0.2958 0.0297 -0.0021 0.0206 139 ALA A O 1050 C CB . ALA A 139 ? 0.2712 0.2420 0.2737 0.0244 -0.0084 0.0227 139 ALA A CB 1051 N N . GLY A 140 ? 0.2721 0.2398 0.2578 0.0278 -0.0067 0.0286 140 GLY A N 1052 C CA . GLY A 140 ? 0.2637 0.2328 0.2408 0.0243 -0.0041 0.0314 140 GLY A CA 1053 C C . GLY A 140 ? 0.2599 0.2282 0.2296 0.0191 -0.0031 0.0269 140 GLY A C 1054 O O . GLY A 140 ? 0.2642 0.2296 0.2381 0.0163 -0.0040 0.0396 140 GLY A O 1055 N N . LYS A 141 ? 0.2533 0.2133 0.2152 0.0156 -0.0074 0.0205 141 LYS A N 1056 C CA . LYS A 141 ? 0.2480 0.2020 0.1964 0.0131 -0.0035 0.0065 141 LYS A CA 1057 C C . LYS A 141 ? 0.2423 0.1957 0.1897 0.0095 0.0026 0.0138 141 LYS A C 1058 O O . LYS A 141 ? 0.2376 0.2002 0.1919 0.0059 -0.0034 0.0066 141 LYS A O 1059 C CB . LYS A 141 ? 0.2449 0.1946 0.1892 0.0095 -0.0004 0.0089 141 LYS A CB 1060 C CG . LYS A 141 ? 0.2630 0.2105 0.1822 0.0176 0.0031 -0.0031 141 LYS A CG 1061 C CD . LYS A 141 ? 0.2554 0.1920 0.1831 0.0129 -0.0088 -0.0116 141 LYS A CD 1062 C CE . LYS A 141 ? 0.2575 0.1799 0.1948 0.0212 0.0042 -0.0114 141 LYS A CE 1063 N NZ . LYS A 141 ? 0.2482 0.1874 0.2049 0.0127 -0.0209 -0.0397 141 LYS A NZ 1064 N N . SER A 142 ? 0.2330 0.1786 0.1785 0.0142 0.0059 0.0237 142 SER A N 1065 C CA . SER A 142 ? 0.2324 0.1687 0.1824 0.0074 0.0149 0.0266 142 SER A CA 1066 C C . SER A 142 ? 0.2186 0.1678 0.1763 0.0144 0.0156 0.0291 142 SER A C 1067 O O . SER A 142 ? 0.2253 0.1784 0.1734 0.0183 0.0199 0.0294 142 SER A O 1068 C CB . SER A 142 ? 0.2306 0.1660 0.1783 0.0081 0.0181 0.0298 142 SER A CB 1069 O OG . SER A 142 ? 0.2667 0.2040 0.1955 -0.0104 0.0212 0.0397 142 SER A OG 1070 N N . VAL A 143 ? 0.2013 0.1554 0.1789 0.0144 0.0170 0.0292 143 VAL A N 1071 C CA . VAL A 143 ? 0.2009 0.1465 0.1754 0.0206 0.0179 0.0321 143 VAL A CA 1072 C C . VAL A 143 ? 0.1905 0.1617 0.1794 0.0187 0.0198 0.0291 143 VAL A C 1073 O O . VAL A 143 ? 0.1983 0.1665 0.1667 0.0160 0.0227 0.0316 143 VAL A O 1074 C CB . VAL A 143 ? 0.1971 0.1390 0.1765 0.0254 0.0183 0.0272 143 VAL A CB 1075 C CG1 . VAL A 143 ? 0.2101 0.1285 0.1815 0.0152 0.0186 0.0421 143 VAL A CG1 1076 C CG2 . VAL A 143 ? 0.2149 0.1429 0.1825 0.0270 0.0199 0.0353 143 VAL A CG2 1077 N N . GLY A 144 ? 0.1762 0.1605 0.1728 0.0233 0.0154 0.0291 144 GLY A N 1078 C CA . GLY A 144 ? 0.1752 0.1589 0.1789 0.0172 0.0108 0.0252 144 GLY A CA 1079 C C . GLY A 144 ? 0.1691 0.1694 0.1827 0.0195 0.0085 0.0213 144 GLY A C 1080 O O . GLY A 144 ? 0.1709 0.1683 0.1664 0.0192 0.0091 0.0178 144 GLY A O 1081 N N . VAL A 145 ? 0.1680 0.1697 0.1778 0.0136 0.0084 0.0149 145 VAL A N 1082 C CA . VAL A 145 ? 0.1711 0.1683 0.1894 0.0210 0.0044 0.0142 145 VAL A CA 1083 C C . VAL A 145 ? 0.1797 0.1724 0.1807 0.0151 0.0057 0.0172 145 VAL A C 1084 O O . VAL A 145 ? 0.1911 0.1707 0.1750 0.0227 0.0045 0.0118 145 VAL A O 1085 C CB . VAL A 145 ? 0.1814 0.1780 0.2038 0.0173 0.0072 0.0174 145 VAL A CB 1086 C CG1 . VAL A 145 ? 0.1970 0.1873 0.2145 0.0202 0.0022 0.0175 145 VAL A CG1 1087 C CG2 . VAL A 145 ? 0.1610 0.1543 0.1990 0.0369 0.0124 -0.0083 145 VAL A CG2 1088 N N . VAL A 146 ? 0.1652 0.1700 0.1710 0.0123 0.0008 0.0200 146 VAL A N 1089 C CA . VAL A 146 ? 0.1719 0.1726 0.1640 0.0086 0.0006 0.0274 146 VAL A CA 1090 C C . VAL A 146 ? 0.1607 0.1667 0.1637 0.0082 -0.0001 0.0230 146 VAL A C 1091 O O . VAL A 146 ? 0.1624 0.1567 0.1510 0.0148 0.0034 0.0274 146 VAL A O 1092 C CB . VAL A 146 ? 0.1650 0.1771 0.1599 0.0006 -0.0064 0.0289 146 VAL A CB 1093 C CG1 . VAL A 146 ? 0.1714 0.1902 0.1771 0.0185 0.0127 0.0253 146 VAL A CG1 1094 C CG2 . VAL A 146 ? 0.1887 0.1907 0.1674 -0.0039 -0.0045 0.0320 146 VAL A CG2 1095 N N . THR A 147 ? 0.1461 0.1566 0.1562 0.0051 0.0012 0.0170 147 THR A N 1096 C CA . THR A 147 ? 0.1510 0.1665 0.1591 0.0073 0.0032 0.0094 147 THR A CA 1097 C C . THR A 147 ? 0.1459 0.1639 0.1603 0.0049 0.0026 0.0115 147 THR A C 1098 O O . THR A 147 ? 0.1533 0.1713 0.1602 0.0113 -0.0081 0.0133 147 THR A O 1099 C CB . THR A 147 ? 0.1480 0.1556 0.1516 -0.0002 0.0017 0.0077 147 THR A CB 1100 O OG1 . THR A 147 ? 0.1623 0.1760 0.1629 -0.0026 0.0036 -0.0049 147 THR A OG1 1101 C CG2 . THR A 147 ? 0.1445 0.1836 0.1653 0.0071 0.0096 0.0039 147 THR A CG2 1102 N N . THR A 148 ? 0.1388 0.1673 0.1648 0.0047 0.0011 0.0095 148 THR A N 1103 C CA . THR A 148 ? 0.1482 0.1774 0.1710 0.0017 0.0030 0.0128 148 THR A CA 1104 C C . THR A 148 ? 0.1489 0.1856 0.1720 0.0061 -0.0015 -0.0010 148 THR A C 1105 O O . THR A 148 ? 0.1501 0.1931 0.1970 0.0107 0.0051 0.0005 148 THR A O 1106 C CB . THR A 148 ? 0.1404 0.1823 0.1639 0.0024 -0.0028 0.0152 148 THR A CB 1107 O OG1 . THR A 148 ? 0.1576 0.1636 0.1544 -0.0080 0.0166 0.0139 148 THR A OG1 1108 C CG2 . THR A 148 ? 0.1380 0.1653 0.1696 0.0017 -0.0078 0.0202 148 THR A CG2 1109 N N . THR A 149 ? 0.1554 0.1861 0.1637 0.0096 0.0031 -0.0032 149 THR A N 1110 C CA . THR A 149 ? 0.1499 0.1814 0.1583 0.0049 0.0042 -0.0033 149 THR A CA 1111 C C . THR A 149 ? 0.1514 0.1791 0.1622 0.0050 0.0040 -0.0096 149 THR A C 1112 O O . THR A 149 ? 0.1552 0.1811 0.1610 0.0095 0.0054 -0.0189 149 THR A O 1113 C CB . THR A 149 ? 0.1539 0.1839 0.1543 0.0134 0.0040 -0.0046 149 THR A CB 1114 O OG1 . THR A 149 ? 0.1520 0.1619 0.1577 -0.0063 0.0114 -0.0005 149 THR A OG1 1115 C CG2 . THR A 149 ? 0.1466 0.2050 0.1344 0.0088 0.0092 0.0116 149 THR A CG2 1116 N N . ARG A 150 ? 0.1652 0.1775 0.1705 0.0039 -0.0004 -0.0076 150 ARG A N 1117 C CA . ARG A 150 ? 0.1588 0.1705 0.1753 -0.0034 -0.0030 -0.0075 150 ARG A CA 1118 C C . ARG A 150 ? 0.1665 0.1736 0.1779 -0.0044 -0.0007 0.0029 150 ARG A C 1119 O O . ARG A 150 ? 0.1660 0.1653 0.1534 -0.0112 0.0073 0.0003 150 ARG A O 1120 C CB . ARG A 150 ? 0.1712 0.1614 0.1833 -0.0030 0.0030 -0.0009 150 ARG A CB 1121 C CG . ARG A 150 ? 0.1651 0.1491 0.1768 0.0031 0.0084 -0.0258 150 ARG A CG 1122 C CD . ARG A 150 ? 0.1821 0.1641 0.1688 -0.0066 0.0174 -0.0008 150 ARG A CD 1123 N NE . ARG A 150 ? 0.2017 0.1823 0.1856 0.0056 0.0107 -0.0167 150 ARG A NE 1124 C CZ . ARG A 150 ? 0.2210 0.2262 0.1813 -0.0086 -0.0020 -0.0037 150 ARG A CZ 1125 N NH1 . ARG A 150 ? 0.2343 0.2393 0.1648 -0.0036 0.0033 -0.0197 150 ARG A NH1 1126 N NH2 . ARG A 150 ? 0.2091 0.2056 0.1703 -0.0120 -0.0156 -0.0255 150 ARG A NH2 1127 N N . VAL A 151 ? 0.1651 0.1838 0.1765 -0.0011 -0.0025 0.0060 151 VAL A N 1128 C CA . VAL A 151 ? 0.1602 0.1758 0.1801 -0.0021 -0.0046 0.0096 151 VAL A CA 1129 C C . VAL A 151 ? 0.1623 0.1744 0.1652 0.0013 -0.0078 0.0120 151 VAL A C 1130 O O . VAL A 151 ? 0.1641 0.1805 0.1638 -0.0029 -0.0045 0.0058 151 VAL A O 1131 C CB . VAL A 151 ? 0.1517 0.1733 0.1696 -0.0033 -0.0061 0.0105 151 VAL A CB 1132 C CG1 . VAL A 151 ? 0.1279 0.1495 0.1946 -0.0028 -0.0023 0.0132 151 VAL A CG1 1133 C CG2 . VAL A 151 ? 0.1645 0.1907 0.1858 0.0032 -0.0062 0.0123 151 VAL A CG2 1134 N N . GLN A 152 ? 0.1691 0.1775 0.1593 0.0032 -0.0150 0.0098 152 GLN A N 1135 C CA . GLN A 152 ? 0.1707 0.1715 0.1502 0.0075 -0.0100 0.0065 152 GLN A CA 1136 C C . GLN A 152 ? 0.1718 0.1693 0.1538 0.0079 -0.0106 -0.0037 152 GLN A C 1137 O O . GLN A 152 ? 0.1632 0.1821 0.1561 0.0142 -0.0030 -0.0059 152 GLN A O 1138 C CB . GLN A 152 ? 0.1747 0.1595 0.1418 0.0113 -0.0172 0.0121 152 GLN A CB 1139 C CG . GLN A 152 ? 0.1795 0.1979 0.1414 0.0188 0.0070 -0.0031 152 GLN A CG 1140 C CD . GLN A 152 ? 0.1951 0.2059 0.1644 0.0241 0.0000 0.0039 152 GLN A CD 1141 O OE1 . GLN A 152 ? 0.2142 0.2324 0.1608 0.0177 0.0052 -0.0056 152 GLN A OE1 1142 N NE2 . GLN A 152 ? 0.1774 0.1531 0.1398 0.0066 -0.0027 0.0022 152 GLN A NE2 1143 N N . HIS A 153 ? 0.1702 0.1546 0.1546 0.0112 -0.0105 -0.0074 153 HIS A N 1144 C CA . HIS A 153 ? 0.1649 0.1491 0.1489 0.0113 -0.0050 -0.0081 153 HIS A CA 1145 C C . HIS A 153 ? 0.1563 0.1391 0.1501 0.0056 -0.0045 -0.0121 153 HIS A C 1146 O O . HIS A 153 ? 0.1434 0.1466 0.1495 0.0066 -0.0036 -0.0099 153 HIS A O 1147 C CB . HIS A 153 ? 0.1610 0.1458 0.1527 0.0035 -0.0124 -0.0087 153 HIS A CB 1148 C CG . HIS A 153 ? 0.1839 0.1507 0.1650 0.0057 -0.0114 -0.0075 153 HIS A CG 1149 N ND1 . HIS A 153 ? 0.2196 0.1625 0.2011 -0.0154 -0.0276 0.0005 153 HIS A ND1 1150 C CD2 . HIS A 153 ? 0.2279 0.1453 0.1954 -0.0187 -0.0344 0.0187 153 HIS A CD2 1151 C CE1 . HIS A 153 ? 0.2181 0.1681 0.1891 -0.0170 -0.0206 0.0087 153 HIS A CE1 1152 N NE2 . HIS A 153 ? 0.2161 0.1710 0.2018 -0.0148 -0.0152 0.0027 153 HIS A NE2 1153 N N . ALA A 154 ? 0.1544 0.1361 0.1383 0.0046 -0.0067 -0.0138 154 ALA A N 1154 C CA . ALA A 154 ? 0.1504 0.1355 0.1473 -0.0044 -0.0085 -0.0087 154 ALA A CA 1155 C C . ALA A 154 ? 0.1593 0.1421 0.1566 -0.0045 -0.0087 -0.0028 154 ALA A C 1156 O O . ALA A 154 ? 0.1533 0.1361 0.1678 -0.0048 -0.0132 -0.0062 154 ALA A O 1157 C CB . ALA A 154 ? 0.1498 0.1455 0.1444 -0.0045 -0.0024 -0.0068 154 ALA A CB 1158 N N . SER A 155 ? 0.1495 0.1390 0.1582 -0.0082 -0.0115 -0.0007 155 SER A N 1159 C CA . SER A 155 ? 0.1629 0.1401 0.1453 0.0003 -0.0109 -0.0068 155 SER A CA 1160 C C . SER A 155 ? 0.1580 0.1479 0.1362 0.0026 -0.0110 -0.0056 155 SER A C 1161 O O . SER A 155 ? 0.1585 0.1545 0.1292 0.0074 -0.0021 -0.0093 155 SER A O 1162 C CB . SER A 155 ? 0.1493 0.1280 0.1389 0.0020 -0.0134 -0.0035 155 SER A CB 1163 O OG . SER A 155 ? 0.1630 0.1387 0.1411 0.0019 -0.0045 0.0102 155 SER A OG 1164 N N . PRO A 156 ? 0.1591 0.1532 0.1368 0.0093 -0.0071 -0.0064 156 PRO A N 1165 C CA . PRO A 156 ? 0.1576 0.1504 0.1389 0.0077 -0.0063 0.0004 156 PRO A CA 1166 C C . PRO A 156 ? 0.1696 0.1597 0.1545 0.0099 -0.0022 0.0021 156 PRO A C 1167 O O . PRO A 156 ? 0.1741 0.1613 0.1661 0.0193 -0.0112 0.0191 156 PRO A O 1168 C CB . PRO A 156 ? 0.1571 0.1511 0.1384 0.0110 -0.0001 -0.0005 156 PRO A CB 1169 C CG . PRO A 156 ? 0.1517 0.1407 0.1201 -0.0019 -0.0039 -0.0025 156 PRO A CG 1170 C CD . PRO A 156 ? 0.1612 0.1556 0.1298 0.0100 -0.0084 -0.0051 156 PRO A CD 1171 N N . ALA A 157 ? 0.1632 0.1603 0.1548 0.0010 -0.0092 0.0007 157 ALA A N 1172 C CA . ALA A 157 ? 0.1716 0.1628 0.1569 0.0013 -0.0065 0.0011 157 ALA A CA 1173 C C . ALA A 157 ? 0.1750 0.1547 0.1630 0.0016 -0.0129 0.0045 157 ALA A C 1174 O O . ALA A 157 ? 0.1705 0.1627 0.1650 0.0084 -0.0203 0.0055 157 ALA A O 1175 C CB . ALA A 157 ? 0.1602 0.1451 0.1505 -0.0069 -0.0139 -0.0072 157 ALA A CB 1176 N N . GLY A 158 ? 0.1774 0.1603 0.1576 -0.0025 -0.0139 -0.0004 158 GLY A N 1177 C CA . GLY A 158 ? 0.1705 0.1635 0.1592 0.0105 -0.0146 0.0048 158 GLY A CA 1178 C C . GLY A 158 ? 0.1718 0.1701 0.1507 0.0083 -0.0165 0.0060 158 GLY A C 1179 O O . GLY A 158 ? 0.1734 0.1700 0.1516 0.0165 -0.0134 0.0168 158 GLY A O 1180 N N . THR A 159 ? 0.1770 0.1743 0.1543 0.0077 -0.0252 0.0027 159 THR A N 1181 C CA . THR A 159 ? 0.1792 0.1817 0.1597 0.0059 -0.0226 0.0044 159 THR A CA 1182 C C . THR A 159 ? 0.1752 0.1806 0.1580 0.0093 -0.0244 0.0007 159 THR A C 1183 O O . THR A 159 ? 0.1936 0.1819 0.1724 0.0156 -0.0334 -0.0098 159 THR A O 1184 C CB . THR A 159 ? 0.1657 0.1800 0.1528 0.0028 -0.0201 0.0020 159 THR A CB 1185 O OG1 . THR A 159 ? 0.1854 0.1926 0.1697 -0.0180 -0.0179 0.0131 159 THR A OG1 1186 C CG2 . THR A 159 ? 0.1797 0.1945 0.1414 0.0014 -0.0362 0.0134 159 THR A CG2 1187 N N . TYR A 160 ? 0.1708 0.1801 0.1622 0.0093 -0.0125 0.0026 160 TYR A N 1188 C CA . TYR A 160 ? 0.1676 0.1816 0.1683 0.0131 -0.0091 0.0013 160 TYR A CA 1189 C C . TYR A 160 ? 0.1592 0.1801 0.1718 0.0150 -0.0121 0.0008 160 TYR A C 1190 O O . TYR A 160 ? 0.1738 0.1876 0.1943 0.0060 -0.0176 0.0140 160 TYR A O 1191 C CB . TYR A 160 ? 0.1793 0.1864 0.1699 0.0120 -0.0045 0.0049 160 TYR A CB 1192 C CG . TYR A 160 ? 0.1781 0.1729 0.1613 0.0163 -0.0079 -0.0023 160 TYR A CG 1193 C CD1 . TYR A 160 ? 0.1815 0.1597 0.1425 0.0273 -0.0146 0.0004 160 TYR A CD1 1194 C CD2 . TYR A 160 ? 0.1949 0.1675 0.1744 0.0106 0.0031 0.0067 160 TYR A CD2 1195 C CE1 . TYR A 160 ? 0.1905 0.1781 0.1523 0.0227 -0.0389 0.0084 160 TYR A CE1 1196 C CE2 . TYR A 160 ? 0.1787 0.1881 0.1589 0.0236 -0.0174 0.0198 160 TYR A CE2 1197 C CZ . TYR A 160 ? 0.1871 0.1921 0.1867 0.0165 -0.0030 0.0140 160 TYR A CZ 1198 O OH . TYR A 160 ? 0.1732 0.1615 0.1945 0.0123 -0.0211 0.0161 160 TYR A OH 1199 N N . ALA A 161 ? 0.1388 0.1684 0.1659 0.0159 -0.0129 -0.0004 161 ALA A N 1200 C CA . ALA A 161 ? 0.1445 0.1788 0.1695 0.0192 -0.0047 -0.0026 161 ALA A CA 1201 C C . ALA A 161 ? 0.1358 0.1763 0.1719 0.0200 -0.0061 -0.0042 161 ALA A C 1202 O O . ALA A 161 ? 0.1303 0.1685 0.1453 0.0292 -0.0081 -0.0107 161 ALA A O 1203 C CB . ALA A 161 ? 0.1306 0.1552 0.1803 0.0203 -0.0129 0.0071 161 ALA A CB 1204 N N . HIS A 162 ? 0.1461 0.1783 0.1695 0.0256 -0.0063 -0.0054 162 HIS A N 1205 C CA . HIS A 162 ? 0.1518 0.1681 0.1826 0.0197 -0.0111 0.0006 162 HIS A CA 1206 C C . HIS A 162 ? 0.1568 0.1650 0.1843 0.0228 -0.0130 -0.0005 162 HIS A C 1207 O O . HIS A 162 ? 0.1661 0.1626 0.1794 0.0183 -0.0107 -0.0055 162 HIS A O 1208 C CB . HIS A 162 ? 0.1476 0.1577 0.1747 0.0284 -0.0101 0.0041 162 HIS A CB 1209 C CG . HIS A 162 ? 0.1781 0.1470 0.1808 0.0240 -0.0156 0.0081 162 HIS A CG 1210 N ND1 . HIS A 162 ? 0.1971 0.1327 0.2046 0.0189 -0.0183 0.0054 162 HIS A ND1 1211 C CD2 . HIS A 162 ? 0.2053 0.1316 0.1861 0.0316 -0.0239 0.0113 162 HIS A CD2 1212 C CE1 . HIS A 162 ? 0.2042 0.1542 0.2113 0.0257 -0.0340 0.0290 162 HIS A CE1 1213 N NE2 . HIS A 162 ? 0.2151 0.1332 0.1898 0.0184 -0.0102 0.0389 162 HIS A NE2 1214 N N . THR A 163 ? 0.1590 0.1717 0.1799 0.0096 -0.0092 0.0016 163 THR A N 1215 C CA . THR A 163 ? 0.1601 0.1788 0.1829 0.0082 -0.0170 0.0006 163 THR A CA 1216 C C . THR A 163 ? 0.1646 0.1761 0.1833 0.0029 -0.0164 0.0011 163 THR A C 1217 O O . THR A 163 ? 0.1730 0.1804 0.1733 0.0022 -0.0220 -0.0015 163 THR A O 1218 C CB . THR A 163 ? 0.1567 0.1778 0.1841 0.0109 -0.0233 0.0000 163 THR A CB 1219 O OG1 . THR A 163 ? 0.1374 0.1983 0.1864 0.0107 -0.0070 0.0053 163 THR A OG1 1220 C CG2 . THR A 163 ? 0.1545 0.1788 0.1913 0.0134 -0.0287 0.0069 163 THR A CG2 1221 N N . VAL A 164 ? 0.1651 0.1762 0.1843 0.0033 -0.0163 -0.0023 164 VAL A N 1222 C CA . VAL A 164 ? 0.1615 0.1637 0.1852 -0.0001 -0.0182 -0.0020 164 VAL A CA 1223 C C . VAL A 164 ? 0.1685 0.1704 0.1878 -0.0014 -0.0197 -0.0009 164 VAL A C 1224 O O . VAL A 164 ? 0.1755 0.1509 0.1895 -0.0078 -0.0144 0.0179 164 VAL A O 1225 C CB . VAL A 164 ? 0.1722 0.1761 0.1879 0.0017 -0.0208 -0.0024 164 VAL A CB 1226 C CG1 . VAL A 164 ? 0.1426 0.1548 0.1959 0.0076 -0.0150 -0.0158 164 VAL A CG1 1227 C CG2 . VAL A 164 ? 0.1525 0.1577 0.1652 -0.0068 -0.0407 -0.0217 164 VAL A CG2 1228 N N . ASN A 165 ? 0.1588 0.1624 0.1915 -0.0009 -0.0208 -0.0011 165 ASN A N 1229 C CA . ASN A 165 ? 0.1616 0.1667 0.1989 -0.0010 -0.0219 -0.0053 165 ASN A CA 1230 C C . ASN A 165 ? 0.1617 0.1649 0.1944 -0.0001 -0.0238 -0.0038 165 ASN A C 1231 O O . ASN A 165 ? 0.1535 0.1435 0.1843 0.0029 -0.0279 -0.0018 165 ASN A O 1232 C CB . ASN A 165 ? 0.1701 0.1643 0.2134 -0.0025 -0.0160 -0.0035 165 ASN A CB 1233 C CG . ASN A 165 ? 0.1729 0.1712 0.2192 -0.0023 -0.0126 -0.0004 165 ASN A CG 1234 O OD1 . ASN A 165 ? 0.1792 0.1706 0.2104 0.0251 0.0154 -0.0096 165 ASN A OD1 1235 N ND2 . ASN A 165 ? 0.1964 0.1508 0.2280 -0.0192 -0.0078 0.0210 165 ASN A ND2 1236 N N . ARG A 166 ? 0.1606 0.1677 0.1775 -0.0014 -0.0331 -0.0091 166 ARG A N 1237 C CA . ARG A 166 ? 0.1702 0.1849 0.1699 0.0010 -0.0294 -0.0049 166 ARG A CA 1238 C C . ARG A 166 ? 0.1783 0.1861 0.1729 -0.0004 -0.0270 -0.0056 166 ARG A C 1239 O O . ARG A 166 ? 0.1797 0.2004 0.1688 -0.0003 -0.0159 -0.0134 166 ARG A O 1240 C CB . ARG A 166 ? 0.1656 0.1846 0.1661 0.0016 -0.0356 0.0017 166 ARG A CB 1241 C CG . ARG A 166 ? 0.1702 0.1835 0.1721 0.0132 -0.0412 0.0074 166 ARG A CG 1242 C CD . ARG A 166 ? 0.1512 0.2153 0.1689 0.0014 -0.0732 0.0039 166 ARG A CD 1243 N NE . ARG A 166 ? 0.1855 0.2054 0.1655 0.0052 -0.0552 0.0077 166 ARG A NE 1244 C CZ . ARG A 166 ? 0.1768 0.1959 0.1602 -0.0115 -0.0564 -0.0020 166 ARG A CZ 1245 N NH1 . ARG A 166 ? 0.1687 0.2133 0.1302 -0.0084 -0.0394 0.0054 166 ARG A NH1 1246 N NH2 . ARG A 166 ? 0.2022 0.1718 0.1560 0.0220 -0.0330 -0.0028 166 ARG A NH2 1247 N N . ASN A 167 ? 0.1940 0.1923 0.1738 0.0013 -0.0278 -0.0022 167 ASN A N 1248 C CA . ASN A 167 ? 0.2002 0.1940 0.1827 0.0032 -0.0263 0.0018 167 ASN A CA 1249 C C . ASN A 167 ? 0.1971 0.1960 0.1813 0.0027 -0.0256 0.0006 167 ASN A C 1250 O O . ASN A 167 ? 0.2073 0.1988 0.1761 -0.0011 -0.0302 -0.0040 167 ASN A O 1251 C CB . ASN A 167 ? 0.2074 0.2013 0.1828 0.0032 -0.0216 0.0088 167 ASN A CB 1252 C CG . ASN A 167 ? 0.2200 0.2327 0.2242 -0.0031 -0.0220 0.0115 167 ASN A CG 1253 O OD1 . ASN A 167 ? 0.2167 0.2614 0.2536 0.0077 -0.0492 0.0011 167 ASN A OD1 1254 N ND2 . ASN A 167 ? 0.2685 0.2708 0.2209 -0.0063 0.0079 0.0429 167 ASN A ND2 1255 N N . TRP A 168 ? 0.1921 0.1970 0.1814 0.0010 -0.0278 -0.0037 168 TRP A N 1256 C CA . TRP A 168 ? 0.1823 0.1988 0.1808 0.0016 -0.0317 -0.0075 168 TRP A CA 1257 C C . TRP A 168 ? 0.1777 0.2016 0.1876 0.0024 -0.0338 -0.0114 168 TRP A C 1258 O O . TRP A 168 ? 0.1634 0.1993 0.2063 0.0007 -0.0378 -0.0153 168 TRP A O 1259 C CB . TRP A 168 ? 0.1685 0.1950 0.1741 -0.0010 -0.0326 -0.0093 168 TRP A CB 1260 C CG . TRP A 168 ? 0.1951 0.2094 0.1814 0.0082 -0.0278 -0.0096 168 TRP A CG 1261 C CD1 . TRP A 168 ? 0.1750 0.1934 0.1672 0.0042 -0.0214 -0.0251 168 TRP A CD1 1262 C CD2 . TRP A 168 ? 0.1809 0.2051 0.1694 0.0162 -0.0203 -0.0040 168 TRP A CD2 1263 N NE1 . TRP A 168 ? 0.1830 0.2210 0.1697 0.0057 -0.0187 -0.0287 168 TRP A NE1 1264 C CE2 . TRP A 168 ? 0.1790 0.2006 0.1899 0.0108 -0.0350 -0.0186 168 TRP A CE2 1265 C CE3 . TRP A 168 ? 0.1728 0.1798 0.1724 0.0232 -0.0390 -0.0144 168 TRP A CE3 1266 C CZ2 . TRP A 168 ? 0.1838 0.2104 0.2052 0.0117 -0.0419 -0.0123 168 TRP A CZ2 1267 C CZ3 . TRP A 168 ? 0.1572 0.1895 0.1679 -0.0016 -0.0224 -0.0166 168 TRP A CZ3 1268 C CH2 . TRP A 168 ? 0.1919 0.1881 0.1963 0.0129 -0.0348 -0.0215 168 TRP A CH2 1269 N N . TYR A 169 ? 0.1833 0.2128 0.1867 0.0037 -0.0346 -0.0148 169 TYR A N 1270 C CA . TYR A 169 ? 0.1926 0.2091 0.1796 0.0029 -0.0316 -0.0170 169 TYR A CA 1271 C C . TYR A 169 ? 0.1967 0.2109 0.1819 0.0048 -0.0313 -0.0205 169 TYR A C 1272 O O . TYR A 169 ? 0.2037 0.2131 0.1777 0.0017 -0.0309 -0.0253 169 TYR A O 1273 C CB . TYR A 169 ? 0.1869 0.2014 0.1787 0.0078 -0.0319 -0.0180 169 TYR A CB 1274 C CG . TYR A 169 ? 0.1936 0.1931 0.1729 0.0135 -0.0335 -0.0183 169 TYR A CG 1275 C CD1 . TYR A 169 ? 0.1975 0.1818 0.1790 0.0003 -0.0383 -0.0144 169 TYR A CD1 1276 C CD2 . TYR A 169 ? 0.1899 0.1909 0.1878 0.0014 -0.0364 -0.0115 169 TYR A CD2 1277 C CE1 . TYR A 169 ? 0.2150 0.1700 0.1880 0.0109 -0.0339 -0.0183 169 TYR A CE1 1278 C CE2 . TYR A 169 ? 0.1984 0.1758 0.1726 0.0084 -0.0499 -0.0216 169 TYR A CE2 1279 C CZ . TYR A 169 ? 0.2063 0.1990 0.1787 0.0134 -0.0354 -0.0149 169 TYR A CZ 1280 O OH . TYR A 169 ? 0.2318 0.2183 0.1739 0.0074 -0.0386 -0.0298 169 TYR A OH 1281 N N . SER A 170 ? 0.2003 0.2172 0.1842 0.0055 -0.0307 -0.0266 170 SER A N 1282 C CA . SER A 170 ? 0.2029 0.2157 0.1935 0.0085 -0.0331 -0.0263 170 SER A CA 1283 C C . SER A 170 ? 0.2081 0.2121 0.1960 0.0082 -0.0300 -0.0263 170 SER A C 1284 O O . SER A 170 ? 0.2061 0.2008 0.1985 0.0100 -0.0340 -0.0300 170 SER A O 1285 C CB . SER A 170 ? 0.2124 0.2225 0.1998 0.0061 -0.0318 -0.0233 170 SER A CB 1286 O OG . SER A 170 ? 0.2007 0.2251 0.2146 -0.0054 -0.0523 -0.0406 170 SER A OG 1287 N N . ASP A 171 ? 0.2108 0.2203 0.1964 0.0086 -0.0275 -0.0245 171 ASP A N 1288 C CA . ASP A 171 ? 0.2252 0.2287 0.2065 0.0031 -0.0305 -0.0216 171 ASP A CA 1289 C C . ASP A 171 ? 0.2286 0.2153 0.2055 0.0051 -0.0290 -0.0179 171 ASP A C 1290 O O . ASP A 171 ? 0.2334 0.2083 0.2054 0.0037 -0.0386 -0.0094 171 ASP A O 1291 C CB . ASP A 171 ? 0.2201 0.2403 0.2028 0.0082 -0.0272 -0.0227 171 ASP A CB 1292 C CG . ASP A 171 ? 0.2361 0.2968 0.2165 -0.0045 -0.0280 -0.0266 171 ASP A CG 1293 O OD1 . ASP A 171 ? 0.2472 0.3108 0.2396 0.0429 -0.0262 -0.0230 171 ASP A OD1 1294 O OD2 . ASP A 171 ? 0.2989 0.4045 0.2334 -0.0110 0.0038 -0.0410 171 ASP A OD2 1295 N N . ALA A 172 ? 0.2345 0.2080 0.2063 0.0014 -0.0297 -0.0193 172 ALA A N 1296 C CA . ALA A 172 ? 0.2391 0.2130 0.2149 0.0047 -0.0249 -0.0248 172 ALA A CA 1297 C C . ALA A 172 ? 0.2355 0.2099 0.2203 0.0050 -0.0205 -0.0252 172 ALA A C 1298 O O . ALA A 172 ? 0.2473 0.2348 0.2253 -0.0055 -0.0182 -0.0364 172 ALA A O 1299 C CB . ALA A 172 ? 0.2291 0.1944 0.2086 0.0053 -0.0246 -0.0245 172 ALA A CB 1300 N N . ASP A 173 ? 0.2192 0.2098 0.2233 0.0075 -0.0259 -0.0319 173 ASP A N 1301 C CA . ASP A 173 ? 0.2139 0.2006 0.2318 0.0189 -0.0267 -0.0316 173 ASP A CA 1302 C C . ASP A 173 ? 0.2098 0.2052 0.2391 0.0192 -0.0245 -0.0303 173 ASP A C 1303 O O . ASP A 173 ? 0.2016 0.1995 0.2447 0.0292 -0.0264 -0.0281 173 ASP A O 1304 C CB . ASP A 173 ? 0.2130 0.1967 0.2289 0.0202 -0.0313 -0.0323 173 ASP A CB 1305 C CG . ASP A 173 ? 0.2280 0.1885 0.2410 0.0267 -0.0202 -0.0451 173 ASP A CG 1306 O OD1 . ASP A 173 ? 0.2697 0.1639 0.2567 0.0523 -0.0250 -0.0658 173 ASP A OD1 1307 O OD2 . ASP A 173 ? 0.2296 0.1822 0.2892 0.0504 -0.0191 -0.0682 173 ASP A OD2 1308 N N . VAL A 174 ? 0.2029 0.2099 0.2388 0.0211 -0.0302 -0.0334 174 VAL A N 1309 C CA . VAL A 174 ? 0.2061 0.2141 0.2498 0.0153 -0.0282 -0.0326 174 VAL A CA 1310 C C . VAL A 174 ? 0.2187 0.2183 0.2538 0.0118 -0.0303 -0.0286 174 VAL A C 1311 O O . VAL A 174 ? 0.2245 0.2149 0.2551 0.0111 -0.0385 -0.0303 174 VAL A O 1312 C CB . VAL A 174 ? 0.2023 0.2129 0.2471 0.0172 -0.0257 -0.0332 174 VAL A CB 1313 C CG1 . VAL A 174 ? 0.1826 0.2282 0.2503 0.0257 -0.0252 -0.0280 174 VAL A CG1 1314 C CG2 . VAL A 174 ? 0.1873 0.2105 0.2436 0.0123 -0.0159 -0.0374 174 VAL A CG2 1315 N N . PRO A 175 ? 0.2284 0.2277 0.2627 0.0020 -0.0347 -0.0240 175 PRO A N 1316 C CA . PRO A 175 ? 0.2307 0.2426 0.2648 -0.0033 -0.0415 -0.0227 175 PRO A CA 1317 C C . PRO A 175 ? 0.2387 0.2507 0.2784 -0.0050 -0.0449 -0.0246 175 PRO A C 1318 O O . PRO A 175 ? 0.2303 0.2320 0.2834 -0.0145 -0.0473 -0.0208 175 PRO A O 1319 C CB . PRO A 175 ? 0.2309 0.2500 0.2631 -0.0038 -0.0398 -0.0252 175 PRO A CB 1320 C CG . PRO A 175 ? 0.2335 0.2439 0.2630 -0.0010 -0.0339 -0.0213 175 PRO A CG 1321 C CD . PRO A 175 ? 0.2232 0.2288 0.2547 -0.0007 -0.0357 -0.0261 175 PRO A CD 1322 N N . ALA A 176 ? 0.2456 0.2522 0.2801 -0.0078 -0.0539 -0.0282 176 ALA A N 1323 C CA . ALA A 176 ? 0.2554 0.2608 0.2861 -0.0035 -0.0571 -0.0262 176 ALA A CA 1324 C C . ALA A 176 ? 0.2580 0.2728 0.2851 -0.0059 -0.0550 -0.0191 176 ALA A C 1325 O O . ALA A 176 ? 0.2604 0.2663 0.2870 -0.0021 -0.0574 -0.0211 176 ALA A O 1326 C CB . ALA A 176 ? 0.2652 0.2700 0.2907 -0.0054 -0.0621 -0.0288 176 ALA A CB 1327 N N . SER A 177 ? 0.2581 0.2815 0.2887 -0.0054 -0.0525 -0.0127 177 SER A N 1328 C CA . SER A 177 ? 0.2611 0.2919 0.2855 -0.0064 -0.0499 -0.0041 177 SER A CA 1329 C C . SER A 177 ? 0.2462 0.2848 0.2784 -0.0054 -0.0469 -0.0020 177 SER A C 1330 O O . SER A 177 ? 0.2321 0.2925 0.2837 -0.0107 -0.0424 0.0012 177 SER A O 1331 C CB . SER A 177 ? 0.2651 0.2968 0.2858 -0.0075 -0.0555 0.0006 177 SER A CB 1332 O OG . SER A 177 ? 0.3235 0.3315 0.3185 -0.0043 -0.0556 0.0169 177 SER A OG 1333 N N . ALA A 178 ? 0.2239 0.2787 0.2613 -0.0012 -0.0471 -0.0037 178 ALA A N 1334 C CA . ALA A 178 ? 0.2133 0.2729 0.2501 0.0041 -0.0469 -0.0039 178 ALA A CA 1335 C C . ALA A 178 ? 0.2103 0.2775 0.2503 0.0093 -0.0490 -0.0064 178 ALA A C 1336 O O . ALA A 178 ? 0.2052 0.2686 0.2403 0.0025 -0.0482 -0.0175 178 ALA A O 1337 C CB . ALA A 178 ? 0.2105 0.2656 0.2450 0.0018 -0.0474 -0.0071 178 ALA A CB 1338 N N . ARG A 179 ? 0.2131 0.2857 0.2481 0.0191 -0.0524 -0.0058 179 ARG A N 1339 C CA . ARG A 179 ? 0.2271 0.3027 0.2599 0.0243 -0.0460 -0.0049 179 ARG A CA 1340 C C . ARG A 179 ? 0.2350 0.3107 0.2602 0.0240 -0.0471 -0.0021 179 ARG A C 1341 O O . ARG A 179 ? 0.2184 0.2940 0.2531 0.0260 -0.0529 0.0028 179 ARG A O 1342 C CB . ARG A 179 ? 0.2246 0.3072 0.2634 0.0276 -0.0468 -0.0074 179 ARG A CB 1343 C CG . ARG A 179 ? 0.2821 0.3366 0.2977 0.0286 -0.0292 -0.0159 179 ARG A CG 1344 C CD . ARG A 179 ? 0.3558 0.3923 0.3482 0.0198 -0.0225 -0.0363 179 ARG A CD 1345 N NE . ARG A 179 ? 0.4200 0.4197 0.3925 0.0137 -0.0258 -0.0475 179 ARG A NE 1346 C CZ . ARG A 179 ? 0.4617 0.4567 0.4239 0.0045 -0.0468 -0.0487 179 ARG A CZ 1347 N NH1 . ARG A 179 ? 0.4934 0.4756 0.3934 0.0033 -0.0641 -0.0501 179 ARG A NH1 1348 N NH2 . ARG A 179 ? 0.4747 0.4741 0.4187 -0.0046 -0.0503 -0.0795 179 ARG A NH2 1349 N N . GLN A 180 ? 0.2524 0.3180 0.2666 0.0184 -0.0442 0.0008 180 GLN A N 1350 C CA . GLN A 180 ? 0.2824 0.3413 0.2947 0.0130 -0.0415 0.0022 180 GLN A CA 1351 C C . GLN A 180 ? 0.2693 0.3312 0.2835 0.0140 -0.0399 0.0066 180 GLN A C 1352 O O . GLN A 180 ? 0.2611 0.3162 0.2802 0.0214 -0.0409 0.0108 180 GLN A O 1353 C CB . GLN A 180 ? 0.2913 0.3463 0.2877 0.0102 -0.0425 0.0117 180 GLN A CB 1354 C CG . GLN A 180 ? 0.3373 0.3965 0.3480 0.0030 -0.0421 -0.0013 180 GLN A CG 1355 C CD . GLN A 180 ? 0.3474 0.4033 0.3420 -0.0008 -0.0320 -0.0061 180 GLN A CD 1356 O OE1 . GLN A 180 ? 0.4339 0.4960 0.4122 0.0047 -0.0145 -0.0140 180 GLN A OE1 1357 N NE2 . GLN A 180 ? 0.3974 0.4706 0.4223 -0.0230 -0.0270 -0.0093 180 GLN A NE2 1358 N N . GLU A 181 ? 0.2654 0.3227 0.2760 0.0119 -0.0419 0.0102 181 GLU A N 1359 C CA . GLU A 181 ? 0.2669 0.3251 0.2747 0.0093 -0.0429 0.0122 181 GLU A CA 1360 C C . GLU A 181 ? 0.2636 0.3136 0.2704 0.0108 -0.0420 0.0096 181 GLU A C 1361 O O . GLU A 181 ? 0.2734 0.3234 0.2699 0.0082 -0.0469 0.0096 181 GLU A O 1362 C CB . GLU A 181 ? 0.2689 0.3320 0.2763 0.0067 -0.0405 0.0091 181 GLU A CB 1363 C CG . GLU A 181 ? 0.2857 0.3759 0.2943 -0.0051 -0.0473 0.0213 181 GLU A CG 1364 C CD . GLU A 181 ? 0.3189 0.4545 0.3408 -0.0234 -0.0534 0.0330 181 GLU A CD 1365 O OE1 . GLU A 181 ? 0.3608 0.4930 0.3735 -0.0405 -0.0628 0.0489 181 GLU A OE1 1366 O OE2 . GLU A 181 ? 0.3574 0.4960 0.3351 -0.0301 -0.0606 0.0112 181 GLU A OE2 1367 N N . GLY A 182 ? 0.2536 0.3042 0.2753 0.0143 -0.0406 0.0089 182 GLY A N 1368 C CA . GLY A 182 ? 0.2477 0.2808 0.2767 0.0159 -0.0272 0.0127 182 GLY A CA 1369 C C . GLY A 182 ? 0.2475 0.2770 0.2871 0.0183 -0.0186 0.0090 182 GLY A C 1370 O O . GLY A 182 ? 0.2501 0.2667 0.2998 0.0218 -0.0221 0.0160 182 GLY A O 1371 N N . CYS A 183 ? 0.2429 0.2646 0.2782 0.0181 -0.0149 0.0111 183 CYS A N 1372 C CA . CYS A 183 ? 0.2334 0.2629 0.2801 0.0146 -0.0166 0.0018 183 CYS A CA 1373 C C . CYS A 183 ? 0.2328 0.2584 0.2800 0.0182 -0.0155 0.0027 183 CYS A C 1374 O O . CYS A 183 ? 0.2277 0.2630 0.2978 0.0162 -0.0076 -0.0025 183 CYS A O 1375 C CB . CYS A 183 ? 0.2307 0.2710 0.2780 0.0158 -0.0173 0.0046 183 CYS A CB 1376 S SG . CYS A 183 ? 0.2843 0.2893 0.2853 0.0102 -0.0330 -0.0248 183 CYS A SG 1377 N N . GLN A 184 ? 0.2187 0.2460 0.2591 0.0236 -0.0209 0.0098 184 GLN A N 1378 C CA . GLN A 184 ? 0.2190 0.2389 0.2453 0.0289 -0.0296 0.0127 184 GLN A CA 1379 C C . GLN A 184 ? 0.1983 0.2175 0.2367 0.0292 -0.0245 0.0095 184 GLN A C 1380 O O . GLN A 184 ? 0.1765 0.2103 0.2344 0.0398 -0.0336 0.0136 184 GLN A O 1381 C CB . GLN A 184 ? 0.2338 0.2470 0.2443 0.0282 -0.0294 0.0168 184 GLN A CB 1382 C CG . GLN A 184 ? 0.2840 0.2852 0.2627 0.0426 -0.0354 0.0342 184 GLN A CG 1383 C CD . GLN A 184 ? 0.3606 0.3831 0.2855 0.0262 -0.0363 0.0457 184 GLN A CD 1384 O OE1 . GLN A 184 ? 0.4164 0.4245 0.3275 0.0462 -0.0404 0.0713 184 GLN A OE1 1385 N NE2 . GLN A 184 ? 0.3861 0.3982 0.2927 0.0309 -0.0346 0.0416 184 GLN A NE2 1386 N N . ASP A 185 ? 0.1943 0.2014 0.2241 0.0259 -0.0262 0.0030 185 ASP A N 1387 C CA . ASP A 185 ? 0.1780 0.1909 0.2050 0.0264 -0.0275 -0.0057 185 ASP A CA 1388 C C . ASP A 185 ? 0.1767 0.1881 0.1927 0.0238 -0.0271 -0.0081 185 ASP A C 1389 O O . ASP A 185 ? 0.1656 0.1714 0.1820 0.0173 -0.0290 -0.0016 185 ASP A O 1390 C CB . ASP A 185 ? 0.1918 0.1987 0.2062 0.0327 -0.0264 -0.0095 185 ASP A CB 1391 C CG . ASP A 185 ? 0.1818 0.2097 0.2163 0.0354 -0.0248 -0.0193 185 ASP A CG 1392 O OD1 . ASP A 185 ? 0.1644 0.2329 0.2389 0.0357 -0.0525 -0.0525 185 ASP A OD1 1393 O OD2 . ASP A 185 ? 0.1973 0.2402 0.2134 0.0426 -0.0283 -0.0377 185 ASP A OD2 1394 N N . ILE A 186 ? 0.1681 0.1796 0.1810 0.0164 -0.0297 -0.0132 186 ILE A N 1395 C CA . ILE A 186 ? 0.1744 0.1797 0.1703 0.0156 -0.0298 -0.0134 186 ILE A CA 1396 C C . ILE A 186 ? 0.1798 0.1814 0.1754 0.0200 -0.0293 -0.0164 186 ILE A C 1397 O O . ILE A 186 ? 0.1774 0.1671 0.1644 0.0344 -0.0271 -0.0110 186 ILE A O 1398 C CB . ILE A 186 ? 0.1717 0.1779 0.1653 0.0155 -0.0351 -0.0104 186 ILE A CB 1399 C CG1 . ILE A 186 ? 0.1726 0.1706 0.1470 0.0062 -0.0329 0.0071 186 ILE A CG1 1400 C CG2 . ILE A 186 ? 0.1508 0.1667 0.1650 -0.0048 -0.0362 -0.0226 186 ILE A CG2 1401 C CD1 . ILE A 186 ? 0.2024 0.1928 0.1509 0.0307 -0.0416 0.0319 186 ILE A CD1 1402 N N . ALA A 187 ? 0.1782 0.1863 0.1732 0.0242 -0.0278 -0.0206 187 ALA A N 1403 C CA . ALA A 187 ? 0.1885 0.1897 0.1857 0.0187 -0.0241 -0.0241 187 ALA A CA 1404 C C . ALA A 187 ? 0.1883 0.1889 0.1892 0.0144 -0.0228 -0.0233 187 ALA A C 1405 O O . ALA A 187 ? 0.1984 0.1877 0.1882 0.0180 -0.0269 -0.0241 187 ALA A O 1406 C CB . ALA A 187 ? 0.1946 0.1845 0.1900 0.0230 -0.0182 -0.0285 187 ALA A CB 1407 N N . THR A 188 ? 0.1973 0.1972 0.1953 0.0147 -0.0234 -0.0242 188 THR A N 1408 C CA . THR A 188 ? 0.1991 0.1939 0.2001 0.0058 -0.0224 -0.0163 188 THR A CA 1409 C C . THR A 188 ? 0.1943 0.1932 0.1983 -0.0023 -0.0205 -0.0162 188 THR A C 1410 O O . THR A 188 ? 0.1930 0.2003 0.1950 -0.0103 -0.0196 -0.0179 188 THR A O 1411 C CB . THR A 188 ? 0.2001 0.1845 0.1993 0.0041 -0.0286 -0.0153 188 THR A CB 1412 O OG1 . THR A 188 ? 0.2239 0.2000 0.2077 0.0124 -0.0310 -0.0153 188 THR A OG1 1413 C CG2 . THR A 188 ? 0.1973 0.1917 0.2196 0.0058 -0.0215 -0.0020 188 THR A CG2 1414 N N . GLN A 189 ? 0.1839 0.1898 0.1843 -0.0045 -0.0134 -0.0167 189 GLN A N 1415 C CA . GLN A 189 ? 0.1872 0.1884 0.1875 0.0008 -0.0040 -0.0072 189 GLN A CA 1416 C C . GLN A 189 ? 0.1818 0.1869 0.1772 0.0042 -0.0050 -0.0061 189 GLN A C 1417 O O . GLN A 189 ? 0.1891 0.1995 0.1729 0.0064 -0.0034 0.0039 189 GLN A O 1418 C CB . GLN A 189 ? 0.1805 0.1839 0.1755 0.0005 -0.0086 -0.0064 189 GLN A CB 1419 C CG . GLN A 189 ? 0.1539 0.1702 0.1815 -0.0001 -0.0075 0.0003 189 GLN A CG 1420 C CD . GLN A 189 ? 0.1689 0.1768 0.1814 -0.0087 -0.0255 0.0100 189 GLN A CD 1421 O OE1 . GLN A 189 ? 0.1962 0.2082 0.1907 -0.0001 -0.0303 0.0399 189 GLN A OE1 1422 N NE2 . GLN A 189 ? 0.1771 0.1451 0.2058 0.0042 0.0048 0.0380 189 GLN A NE2 1423 N N . LEU A 190 ? 0.1964 0.1965 0.1771 0.0065 -0.0009 0.0023 190 LEU A N 1424 C CA . LEU A 190 ? 0.1904 0.1995 0.1739 0.0146 0.0002 -0.0002 190 LEU A CA 1425 C C . LEU A 190 ? 0.2009 0.2033 0.1705 0.0220 -0.0030 0.0007 190 LEU A C 1426 O O . LEU A 190 ? 0.2085 0.2007 0.1644 0.0270 -0.0014 0.0047 190 LEU A O 1427 C CB . LEU A 190 ? 0.1845 0.1946 0.1717 0.0186 -0.0010 -0.0006 190 LEU A CB 1428 C CG . LEU A 190 ? 0.1901 0.1922 0.1845 0.0089 0.0018 -0.0045 190 LEU A CG 1429 C CD1 . LEU A 190 ? 0.1785 0.2095 0.1651 -0.0137 0.0021 -0.0157 190 LEU A CD1 1430 C CD2 . LEU A 190 ? 0.1805 0.1989 0.1636 0.0211 0.0162 -0.0015 190 LEU A CD2 1431 N N . ILE A 191 ? 0.2190 0.2110 0.1720 0.0244 -0.0044 -0.0052 191 ILE A N 1432 C CA . ILE A 191 ? 0.2425 0.2021 0.1774 0.0231 -0.0145 -0.0051 191 ILE A CA 1433 C C . ILE A 191 ? 0.2504 0.2148 0.1860 0.0170 -0.0194 -0.0061 191 ILE A C 1434 O O . ILE A 191 ? 0.2580 0.2260 0.1930 0.0144 -0.0196 0.0005 191 ILE A O 1435 C CB . ILE A 191 ? 0.2405 0.2093 0.1732 0.0236 -0.0148 -0.0062 191 ILE A CB 1436 C CG1 . ILE A 191 ? 0.2662 0.1826 0.1495 0.0242 -0.0190 -0.0110 191 ILE A CG1 1437 C CG2 . ILE A 191 ? 0.2527 0.1893 0.1854 0.0343 -0.0242 -0.0150 191 ILE A CG2 1438 C CD1 . ILE A 191 ? 0.3287 0.2011 0.1414 0.0167 -0.0047 -0.0034 191 ILE A CD1 1439 N N . SER A 192 ? 0.2631 0.2177 0.1914 0.0173 -0.0216 -0.0092 192 SER A N 1440 C CA . SER A 192 ? 0.2753 0.2367 0.2115 0.0180 -0.0251 -0.0111 192 SER A CA 1441 C C . SER A 192 ? 0.2694 0.2289 0.2049 0.0181 -0.0219 -0.0076 192 SER A C 1442 O O . SER A 192 ? 0.2651 0.2266 0.1882 0.0278 -0.0266 0.0099 192 SER A O 1443 C CB . SER A 192 ? 0.2909 0.2357 0.2154 0.0182 -0.0260 -0.0226 192 SER A CB 1444 O OG . SER A 192 ? 0.3391 0.3089 0.2806 0.0207 -0.0374 -0.0282 192 SER A OG 1445 N N . ASN A 193 ? 0.2523 0.2197 0.1950 0.0145 -0.0288 -0.0013 193 ASN A N 1446 C CA . ASN A 193 ? 0.2417 0.2158 0.2064 0.0055 -0.0281 -0.0031 193 ASN A CA 1447 C C . ASN A 193 ? 0.2378 0.2165 0.2089 0.0056 -0.0238 -0.0003 193 ASN A C 1448 O O . ASN A 193 ? 0.2152 0.2126 0.2231 0.0035 -0.0291 0.0000 193 ASN A O 1449 C CB . ASN A 193 ? 0.2409 0.2089 0.1954 0.0061 -0.0279 0.0017 193 ASN A CB 1450 C CG . ASN A 193 ? 0.2399 0.2161 0.2123 0.0024 -0.0419 -0.0022 193 ASN A CG 1451 O OD1 . ASN A 193 ? 0.2570 0.2313 0.2296 0.0192 -0.0327 -0.0079 193 ASN A OD1 1452 N ND2 . ASN A 193 ? 0.2210 0.1652 0.1923 0.0056 -0.0487 0.0263 193 ASN A ND2 1453 N N . MET A 194 ? 0.2229 0.2140 0.2010 -0.0032 -0.0208 -0.0021 194 MET A N 1454 C CA . MET A 194 ? 0.2368 0.2271 0.2042 0.0002 -0.0141 0.0056 194 MET A CA 1455 C C . MET A 194 ? 0.2311 0.2245 0.2043 -0.0034 -0.0111 0.0086 194 MET A C 1456 O O . MET A 194 ? 0.2295 0.2278 0.2111 -0.0180 -0.0079 0.0123 194 MET A O 1457 C CB . MET A 194 ? 0.2284 0.2182 0.1901 0.0017 -0.0204 0.0002 194 MET A CB 1458 C CG . MET A 194 ? 0.2397 0.2341 0.1889 -0.0016 -0.0128 -0.0056 194 MET A CG 1459 S SD . MET A 194 ? 0.2433 0.2316 0.1995 -0.0005 -0.0160 0.0073 194 MET A SD 1460 C CE . MET A 194 ? 0.2289 0.2008 0.1745 -0.0313 -0.0005 0.0030 194 MET A CE 1461 N N . ASP A 195 ? 0.2411 0.2246 0.2058 -0.0014 -0.0105 0.0147 195 ASP A N 1462 C CA . ASP A 195 ? 0.2474 0.2302 0.2150 -0.0007 -0.0075 0.0130 195 ASP A CA 1463 C C . ASP A 195 ? 0.2410 0.2232 0.2101 0.0043 -0.0114 0.0103 195 ASP A C 1464 O O . ASP A 195 ? 0.2481 0.2438 0.2214 0.0153 -0.0200 0.0118 195 ASP A O 1465 C CB . ASP A 195 ? 0.2565 0.2377 0.2247 -0.0048 -0.0011 0.0159 195 ASP A CB 1466 C CG . ASP A 195 ? 0.2967 0.2645 0.2544 -0.0195 0.0038 0.0162 195 ASP A CG 1467 O OD1 . ASP A 195 ? 0.3130 0.2672 0.2452 -0.0046 0.0233 0.0212 195 ASP A OD1 1468 O OD2 . ASP A 195 ? 0.3702 0.3460 0.3103 -0.0339 -0.0054 0.0302 195 ASP A OD2 1469 N N . ILE A 196 ? 0.2300 0.2121 0.2037 0.0047 -0.0074 0.0091 196 ILE A N 1470 C CA . ILE A 196 ? 0.2146 0.2000 0.1987 0.0006 -0.0089 0.0071 196 ILE A CA 1471 C C . ILE A 196 ? 0.2245 0.2032 0.2010 0.0001 -0.0082 0.0090 196 ILE A C 1472 O O . ILE A 196 ? 0.2272 0.2176 0.2063 0.0016 -0.0106 0.0020 196 ILE A O 1473 C CB . ILE A 196 ? 0.2173 0.1937 0.1886 0.0025 -0.0049 0.0056 196 ILE A CB 1474 C CG1 . ILE A 196 ? 0.1994 0.1841 0.2087 -0.0035 -0.0134 0.0003 196 ILE A CG1 1475 C CG2 . ILE A 196 ? 0.2021 0.2048 0.1875 0.0042 0.0012 0.0036 196 ILE A CG2 1476 C CD1 . ILE A 196 ? 0.1933 0.1777 0.1910 -0.0044 -0.0178 0.0120 196 ILE A CD1 1477 N N . ASP A 197 ? 0.2126 0.1809 0.1961 -0.0017 -0.0100 0.0183 197 ASP A N 1478 C CA . ASP A 197 ? 0.2219 0.1790 0.1909 -0.0024 -0.0036 0.0209 197 ASP A CA 1479 C C . ASP A 197 ? 0.2132 0.1741 0.1877 -0.0071 0.0009 0.0167 197 ASP A C 1480 O O . ASP A 197 ? 0.2279 0.1728 0.1765 -0.0048 0.0090 0.0199 197 ASP A O 1481 C CB . ASP A 197 ? 0.2264 0.1703 0.1884 -0.0048 -0.0038 0.0219 197 ASP A CB 1482 C CG . ASP A 197 ? 0.2559 0.2095 0.2116 -0.0064 0.0008 0.0315 197 ASP A CG 1483 O OD1 . ASP A 197 ? 0.3119 0.2586 0.2437 0.0219 0.0053 0.0678 197 ASP A OD1 1484 O OD2 . ASP A 197 ? 0.2688 0.1966 0.2023 -0.0270 -0.0063 0.0112 197 ASP A OD2 1485 N N . VAL A 198 ? 0.1971 0.1652 0.1787 -0.0041 -0.0016 0.0259 198 VAL A N 1486 C CA . VAL A 198 ? 0.1913 0.1717 0.1868 -0.0037 0.0074 0.0214 198 VAL A CA 1487 C C . VAL A 198 ? 0.1865 0.1717 0.1833 -0.0053 0.0019 0.0179 198 VAL A C 1488 O O . VAL A 198 ? 0.1938 0.1683 0.1817 -0.0081 0.0004 0.0246 198 VAL A O 1489 C CB . VAL A 198 ? 0.1906 0.1638 0.1953 -0.0028 0.0049 0.0284 198 VAL A CB 1490 C CG1 . VAL A 198 ? 0.1755 0.1971 0.2104 0.0088 0.0168 0.0231 198 VAL A CG1 1491 C CG2 . VAL A 198 ? 0.1909 0.1840 0.1912 -0.0218 0.0309 0.0222 198 VAL A CG2 1492 N N . ILE A 199 ? 0.1742 0.1779 0.1714 -0.0055 -0.0051 0.0120 199 ILE A N 1493 C CA . ILE A 199 ? 0.1645 0.1841 0.1671 -0.0003 -0.0031 0.0093 199 ILE A CA 1494 C C . ILE A 199 ? 0.1611 0.1847 0.1658 -0.0017 0.0015 0.0083 199 ILE A C 1495 O O . ILE A 199 ? 0.1554 0.1881 0.1529 0.0018 0.0117 0.0032 199 ILE A O 1496 C CB . ILE A 199 ? 0.1580 0.1880 0.1726 -0.0047 -0.0078 0.0106 199 ILE A CB 1497 C CG1 . ILE A 199 ? 0.1571 0.1881 0.1756 0.0080 -0.0188 0.0030 199 ILE A CG1 1498 C CG2 . ILE A 199 ? 0.1757 0.1929 0.1767 0.0047 -0.0127 0.0044 199 ILE A CG2 1499 C CD1 . ILE A 199 ? 0.1708 0.2436 0.1953 0.0241 -0.0233 0.0025 199 ILE A CD1 1500 N N . LEU A 200 ? 0.1547 0.1634 0.1572 -0.0037 0.0097 0.0158 200 LEU A N 1501 C CA . LEU A 200 ? 0.1612 0.1547 0.1599 -0.0113 0.0086 0.0173 200 LEU A CA 1502 C C . LEU A 200 ? 0.1628 0.1528 0.1560 -0.0116 0.0049 0.0188 200 LEU A C 1503 O O . LEU A 200 ? 0.1634 0.1506 0.1464 -0.0121 0.0065 0.0091 200 LEU A O 1504 C CB . LEU A 200 ? 0.1523 0.1477 0.1496 -0.0142 0.0074 0.0156 200 LEU A CB 1505 C CG . LEU A 200 ? 0.1525 0.1426 0.1236 -0.0200 0.0153 0.0178 200 LEU A CG 1506 C CD1 . LEU A 200 ? 0.1835 0.1504 0.1147 -0.0427 0.0104 0.0184 200 LEU A CD1 1507 C CD2 . LEU A 200 ? 0.1337 0.1850 0.0982 -0.0177 0.0187 0.0342 200 LEU A CD2 1508 N N . GLY A 201 ? 0.1686 0.1499 0.1563 -0.0148 0.0027 0.0112 201 GLY A N 1509 C CA . GLY A 201 ? 0.1705 0.1443 0.1453 -0.0120 -0.0050 0.0145 201 GLY A CA 1510 C C . GLY A 201 ? 0.1729 0.1524 0.1560 -0.0156 -0.0080 0.0137 201 GLY A C 1511 O O . GLY A 201 ? 0.1906 0.1545 0.1698 -0.0170 -0.0112 0.0038 201 GLY A O 1512 N N . GLY A 202 ? 0.1837 0.1515 0.1535 -0.0123 -0.0119 0.0170 202 GLY A N 1513 C CA . GLY A 202 ? 0.1827 0.1673 0.1565 -0.0213 -0.0125 0.0137 202 GLY A CA 1514 C C . GLY A 202 ? 0.1928 0.1778 0.1567 -0.0144 -0.0122 0.0147 202 GLY A C 1515 O O . GLY A 202 ? 0.2005 0.1779 0.1610 -0.0237 -0.0073 0.0203 202 GLY A O 1516 N N . GLY A 203 ? 0.1947 0.1837 0.1556 -0.0136 -0.0109 0.0056 203 GLY A N 1517 C CA . GLY A 203 ? 0.1942 0.1933 0.1679 -0.0060 -0.0169 0.0003 203 GLY A CA 1518 C C . GLY A 203 ? 0.2041 0.2041 0.1901 0.0015 -0.0170 -0.0079 203 GLY A C 1519 O O . GLY A 203 ? 0.2070 0.2175 0.1959 0.0035 -0.0267 -0.0061 203 GLY A O 1520 N N . ARG A 204 ? 0.2112 0.2065 0.1940 0.0056 -0.0153 -0.0133 204 ARG A N 1521 C CA . ARG A 204 ? 0.2195 0.2142 0.2070 0.0097 -0.0115 -0.0230 204 ARG A CA 1522 C C . ARG A 204 ? 0.2159 0.2205 0.2115 0.0129 -0.0139 -0.0236 204 ARG A C 1523 O O . ARG A 204 ? 0.2133 0.2217 0.2143 0.0155 -0.0222 -0.0265 204 ARG A O 1524 C CB . ARG A 204 ? 0.2115 0.2241 0.2115 0.0152 -0.0048 -0.0223 204 ARG A CB 1525 C CG . ARG A 204 ? 0.2362 0.2107 0.2182 0.0128 -0.0005 -0.0268 204 ARG A CG 1526 C CD . ARG A 204 ? 0.2224 0.1825 0.1996 0.0398 0.0179 -0.0564 204 ARG A CD 1527 N NE . ARG A 204 ? 0.2501 0.1975 0.2087 0.0314 0.0186 -0.0474 204 ARG A NE 1528 C CZ . ARG A 204 ? 0.2732 0.2000 0.1890 0.0295 0.0134 -0.0475 204 ARG A CZ 1529 N NH1 . ARG A 204 ? 0.2683 0.1913 0.1700 0.0330 0.0377 -0.0325 204 ARG A NH1 1530 N NH2 . ARG A 204 ? 0.2833 0.1606 0.1916 0.0439 0.0197 -0.0784 204 ARG A NH2 1531 N N . LYS A 205 ? 0.2155 0.2098 0.2105 0.0147 -0.0113 -0.0264 205 LYS A N 1532 C CA . LYS A 205 ? 0.2368 0.2095 0.2124 0.0206 -0.0100 -0.0259 205 LYS A CA 1533 C C . LYS A 205 ? 0.2396 0.2140 0.2100 0.0162 -0.0121 -0.0256 205 LYS A C 1534 O O . LYS A 205 ? 0.2530 0.2047 0.2088 0.0219 -0.0128 -0.0383 205 LYS A O 1535 C CB . LYS A 205 ? 0.2400 0.2106 0.2114 0.0213 -0.0102 -0.0256 205 LYS A CB 1536 C CG . LYS A 205 ? 0.2674 0.2010 0.2093 0.0252 -0.0179 -0.0199 205 LYS A CG 1537 C CD . LYS A 205 ? 0.3211 0.1823 0.2265 0.0454 -0.0176 -0.0323 205 LYS A CD 1538 C CE . LYS A 205 ? 0.3511 0.2035 0.2869 0.0424 -0.0402 0.0002 205 LYS A CE 1539 N NZ . LYS A 205 ? 0.3687 0.2420 0.3242 0.0737 -0.0638 -0.0002 205 LYS A NZ 1540 N N . TYR A 206 ? 0.2382 0.2123 0.2002 0.0149 -0.0141 -0.0252 206 TYR A N 1541 C CA . TYR A 206 ? 0.2339 0.2224 0.1925 0.0078 -0.0168 -0.0217 206 TYR A CA 1542 C C . TYR A 206 ? 0.2299 0.2217 0.1917 0.0089 -0.0203 -0.0207 206 TYR A C 1543 O O . TYR A 206 ? 0.2386 0.2320 0.1992 -0.0027 -0.0192 -0.0188 206 TYR A O 1544 C CB . TYR A 206 ? 0.2251 0.2216 0.1813 0.0070 -0.0175 -0.0186 206 TYR A CB 1545 C CG . TYR A 206 ? 0.2225 0.2298 0.1661 0.0135 -0.0224 -0.0093 206 TYR A CG 1546 C CD1 . TYR A 206 ? 0.2180 0.2383 0.1503 -0.0009 -0.0334 0.0045 206 TYR A CD1 1547 C CD2 . TYR A 206 ? 0.2210 0.2291 0.1468 0.0127 -0.0223 -0.0253 206 TYR A CD2 1548 C CE1 . TYR A 206 ? 0.2247 0.2454 0.1535 0.0098 -0.0335 -0.0031 206 TYR A CE1 1549 C CE2 . TYR A 206 ? 0.2125 0.2256 0.1298 0.0221 -0.0301 -0.0159 206 TYR A CE2 1550 C CZ . TYR A 206 ? 0.2193 0.2154 0.1442 0.0171 -0.0315 -0.0159 206 TYR A CZ 1551 O OH . TYR A 206 ? 0.2196 0.2148 0.1701 0.0125 -0.0499 -0.0204 206 TYR A OH 1552 N N . MET A 207 ? 0.2295 0.2261 0.1843 0.0109 -0.0184 -0.0280 207 MET A N 1553 C CA . MET A 207 ? 0.2331 0.2348 0.1850 0.0097 -0.0216 -0.0246 207 MET A CA 1554 C C . MET A 207 ? 0.2439 0.2531 0.2005 0.0111 -0.0195 -0.0249 207 MET A C 1555 O O . MET A 207 ? 0.2593 0.2661 0.1978 0.0185 -0.0311 -0.0243 207 MET A O 1556 C CB . MET A 207 ? 0.2280 0.2321 0.1871 0.0122 -0.0226 -0.0209 207 MET A CB 1557 C CG . MET A 207 ? 0.2266 0.2204 0.1684 0.0080 -0.0203 -0.0189 207 MET A CG 1558 S SD . MET A 207 ? 0.2363 0.2551 0.1641 0.0078 -0.0230 -0.0195 207 MET A SD 1559 C CE . MET A 207 ? 0.2642 0.2454 0.1569 -0.0123 -0.0287 -0.0087 207 MET A CE 1560 N N . PHE A 208 ? 0.2477 0.2585 0.2098 0.0075 -0.0169 -0.0295 208 PHE A N 1561 C CA . PHE A 208 ? 0.2535 0.2748 0.2078 0.0073 -0.0183 -0.0364 208 PHE A CA 1562 C C . PHE A 208 ? 0.2709 0.2881 0.2224 0.0116 -0.0170 -0.0403 208 PHE A C 1563 O O . PHE A 208 ? 0.2544 0.2809 0.2001 0.0101 -0.0160 -0.0483 208 PHE A O 1564 C CB . PHE A 208 ? 0.2595 0.2809 0.2105 0.0064 -0.0146 -0.0313 208 PHE A CB 1565 C CG . PHE A 208 ? 0.2477 0.2752 0.2185 0.0007 -0.0049 -0.0309 208 PHE A CG 1566 C CD1 . PHE A 208 ? 0.2642 0.2990 0.2279 -0.0050 0.0028 -0.0263 208 PHE A CD1 1567 C CD2 . PHE A 208 ? 0.2578 0.2868 0.2193 -0.0028 0.0215 -0.0416 208 PHE A CD2 1568 C CE1 . PHE A 208 ? 0.2676 0.2680 0.2370 -0.0096 0.0049 -0.0401 208 PHE A CE1 1569 C CE2 . PHE A 208 ? 0.2590 0.2712 0.2320 -0.0184 0.0291 -0.0427 208 PHE A CE2 1570 C CZ . PHE A 208 ? 0.2561 0.2761 0.2268 -0.0002 -0.0021 -0.0300 208 PHE A CZ 1571 N N . ARG A 209 ? 0.2910 0.3057 0.2399 0.0075 -0.0230 -0.0477 209 ARG A N 1572 C CA . ARG A 209 ? 0.3304 0.3370 0.2704 0.0030 -0.0161 -0.0445 209 ARG A CA 1573 C C . ARG A 209 ? 0.3300 0.3302 0.2693 -0.0014 -0.0163 -0.0478 209 ARG A C 1574 O O . ARG A 209 ? 0.3176 0.3117 0.2542 0.0010 -0.0250 -0.0540 209 ARG A O 1575 C CB . ARG A 209 ? 0.3243 0.3409 0.2588 0.0019 -0.0175 -0.0496 209 ARG A CB 1576 C CG . ARG A 209 ? 0.3705 0.3838 0.3015 -0.0026 -0.0119 -0.0389 209 ARG A CG 1577 C CD . ARG A 209 ? 0.3864 0.3965 0.3092 0.0031 -0.0055 -0.0450 209 ARG A CD 1578 N NE . ARG A 209 ? 0.5223 0.5103 0.4365 -0.0221 0.0317 -0.0269 209 ARG A NE 1579 C CZ . ARG A 209 ? 0.5741 0.5387 0.4850 -0.0191 0.0404 -0.0308 209 ARG A CZ 1580 N NH1 . ARG A 209 ? 0.6114 0.5649 0.5324 -0.0216 0.0397 -0.0188 209 ARG A NH1 1581 N NH2 . ARG A 209 ? 0.6026 0.5773 0.5099 -0.0214 0.0431 -0.0273 209 ARG A NH2 1582 N N . MET A 210 ? 0.3396 0.3393 0.2909 -0.0096 -0.0151 -0.0456 210 MET A N 1583 C CA . MET A 210 ? 0.3635 0.3649 0.3324 -0.0155 -0.0061 -0.0376 210 MET A CA 1584 C C . MET A 210 ? 0.3543 0.3558 0.3299 -0.0073 -0.0025 -0.0458 210 MET A C 1585 O O . MET A 210 ? 0.3542 0.3605 0.3213 -0.0059 0.0015 -0.0491 210 MET A O 1586 C CB . MET A 210 ? 0.3702 0.3571 0.3358 -0.0144 -0.0081 -0.0356 210 MET A CB 1587 C CG . MET A 210 ? 0.3887 0.3939 0.3797 -0.0237 -0.0054 -0.0251 210 MET A CG 1588 S SD . MET A 210 ? 0.4287 0.4200 0.4002 -0.0440 0.0000 -0.0159 210 MET A SD 1589 C CE . MET A 210 ? 0.4424 0.4281 0.4282 -0.0506 -0.0013 -0.0203 210 MET A CE 1590 N N . GLY A 211 ? 0.3552 0.3504 0.3349 -0.0029 0.0039 -0.0509 211 GLY A N 1591 C CA . GLY A 211 ? 0.3545 0.3437 0.3297 0.0041 0.0128 -0.0599 211 GLY A CA 1592 C C . GLY A 211 ? 0.3500 0.3293 0.3237 0.0092 0.0170 -0.0595 211 GLY A C 1593 O O . GLY A 211 ? 0.3628 0.3318 0.3369 0.0098 0.0201 -0.0678 211 GLY A O 1594 N N . THR A 212 ? 0.3349 0.3183 0.3149 0.0175 0.0158 -0.0579 212 THR A N 1595 C CA . THR A 212 ? 0.3232 0.3079 0.2986 0.0243 0.0172 -0.0563 212 THR A CA 1596 C C . THR A 212 ? 0.3081 0.3116 0.2935 0.0266 0.0191 -0.0534 212 THR A C 1597 O O . THR A 212 ? 0.3027 0.3120 0.2970 0.0275 0.0080 -0.0447 212 THR A O 1598 C CB . THR A 212 ? 0.3198 0.2962 0.2941 0.0299 0.0179 -0.0614 212 THR A CB 1599 O OG1 . THR A 212 ? 0.3432 0.2973 0.2761 0.0242 0.0206 -0.0812 212 THR A OG1 1600 C CG2 . THR A 212 ? 0.3208 0.2810 0.2894 0.0366 0.0186 -0.0586 212 THR A CG2 1601 N N . PRO A 213 ? 0.3052 0.3215 0.2913 0.0272 0.0194 -0.0516 213 PRO A N 1602 C CA . PRO A 213 ? 0.2983 0.3206 0.2853 0.0281 0.0232 -0.0489 213 PRO A CA 1603 C C . PRO A 213 ? 0.2949 0.3174 0.2849 0.0254 0.0244 -0.0452 213 PRO A C 1604 O O . PRO A 213 ? 0.3037 0.3243 0.2799 0.0279 0.0265 -0.0451 213 PRO A O 1605 C CB . PRO A 213 ? 0.3044 0.3283 0.2902 0.0309 0.0201 -0.0537 213 PRO A CB 1606 C CG . PRO A 213 ? 0.3062 0.3376 0.2873 0.0330 0.0178 -0.0526 213 PRO A CG 1607 C CD . PRO A 213 ? 0.3013 0.3256 0.2881 0.0337 0.0232 -0.0533 213 PRO A CD 1608 N N . ASP A 214 ? 0.2863 0.3068 0.2889 0.0198 0.0275 -0.0413 214 ASP A N 1609 C CA . ASP A 214 ? 0.2844 0.3014 0.2884 0.0166 0.0262 -0.0406 214 ASP A CA 1610 C C . ASP A 214 ? 0.2885 0.2970 0.2901 0.0145 0.0274 -0.0388 214 ASP A C 1611 O O . ASP A 214 ? 0.2798 0.2873 0.2894 0.0230 0.0339 -0.0491 214 ASP A O 1612 C CB . ASP A 214 ? 0.2741 0.2933 0.2833 0.0119 0.0262 -0.0369 214 ASP A CB 1613 C CG . ASP A 214 ? 0.2764 0.2818 0.2784 0.0058 0.0241 -0.0339 214 ASP A CG 1614 O OD1 . ASP A 214 ? 0.2227 0.2407 0.2613 -0.0290 0.0167 -0.0094 214 ASP A OD1 1615 O OD2 . ASP A 214 ? 0.2964 0.2598 0.2900 -0.0196 0.0137 -0.0361 214 ASP A OD2 1616 N N . PRO A 215 ? 0.2966 0.2996 0.2895 0.0149 0.0285 -0.0362 215 PRO A N 1617 C CA . PRO A 215 ? 0.2996 0.3008 0.2877 0.0157 0.0280 -0.0378 215 PRO A CA 1618 C C . PRO A 215 ? 0.3017 0.3062 0.2816 0.0128 0.0253 -0.0396 215 PRO A C 1619 O O . PRO A 215 ? 0.3043 0.3153 0.2782 0.0168 0.0315 -0.0368 215 PRO A O 1620 C CB . PRO A 215 ? 0.3060 0.3006 0.2883 0.0104 0.0280 -0.0345 215 PRO A CB 1621 C CG . PRO A 215 ? 0.2971 0.2985 0.2795 0.0181 0.0317 -0.0401 215 PRO A CG 1622 C CD . PRO A 215 ? 0.2972 0.2881 0.2875 0.0142 0.0303 -0.0388 215 PRO A CD 1623 N N . GLU A 216 ? 0.2976 0.3034 0.2735 0.0141 0.0235 -0.0401 216 GLU A N 1624 C CA . GLU A 216 ? 0.3020 0.3096 0.2738 0.0143 0.0177 -0.0434 216 GLU A CA 1625 C C . GLU A 216 ? 0.3049 0.3070 0.2724 0.0174 0.0132 -0.0503 216 GLU A C 1626 O O . GLU A 216 ? 0.3204 0.3195 0.2845 0.0109 0.0126 -0.0524 216 GLU A O 1627 C CB . GLU A 216 ? 0.2946 0.3016 0.2695 0.0178 0.0147 -0.0499 216 GLU A CB 1628 C CG . GLU A 216 ? 0.2936 0.3139 0.2681 0.0190 0.0158 -0.0425 216 GLU A CG 1629 C CD . GLU A 216 ? 0.2752 0.3081 0.2555 0.0323 0.0136 -0.0401 216 GLU A CD 1630 O OE1 . GLU A 216 ? 0.2826 0.2966 0.2295 0.0397 0.0070 -0.0361 216 GLU A OE1 1631 O OE2 . GLU A 216 ? 0.2210 0.3022 0.2773 0.0415 0.0147 -0.0134 216 GLU A OE2 1632 N N . TYR A 217 ? 0.3119 0.3114 0.2659 0.0165 0.0104 -0.0554 217 TYR A N 1633 C CA . TYR A 217 ? 0.3211 0.3169 0.2791 0.0132 0.0036 -0.0566 217 TYR A CA 1634 C C . TYR A 217 ? 0.3332 0.3325 0.2954 0.0077 0.0011 -0.0581 217 TYR A C 1635 O O . TYR A 217 ? 0.3204 0.3170 0.2897 0.0013 -0.0020 -0.0664 217 TYR A O 1636 C CB . TYR A 217 ? 0.3137 0.3064 0.2760 0.0215 0.0033 -0.0576 217 TYR A CB 1637 C CG . TYR A 217 ? 0.3207 0.3031 0.2674 0.0390 0.0037 -0.0500 217 TYR A CG 1638 C CD1 . TYR A 217 ? 0.3276 0.3327 0.3029 0.0566 0.0008 -0.0666 217 TYR A CD1 1639 C CD2 . TYR A 217 ? 0.2886 0.2806 0.2583 0.0567 0.0272 -0.0592 217 TYR A CD2 1640 C CE1 . TYR A 217 ? 0.3343 0.3055 0.2810 0.0627 -0.0095 -0.0818 217 TYR A CE1 1641 C CE2 . TYR A 217 ? 0.2954 0.2930 0.2493 0.0779 0.0090 -0.0622 217 TYR A CE2 1642 C CZ . TYR A 217 ? 0.3175 0.3168 0.2798 0.0520 0.0083 -0.0680 217 TYR A CZ 1643 O OH . TYR A 217 ? 0.3220 0.2996 0.2493 0.0492 0.0029 -0.0699 217 TYR A OH 1644 N N . PRO A 218 ? 0.3476 0.3544 0.3149 0.0019 -0.0016 -0.0572 218 PRO A N 1645 C CA . PRO A 218 ? 0.3568 0.3658 0.3330 0.0015 -0.0033 -0.0571 218 PRO A CA 1646 C C . PRO A 218 ? 0.3615 0.3716 0.3510 0.0060 -0.0042 -0.0593 218 PRO A C 1647 O O . PRO A 218 ? 0.3655 0.3819 0.3583 0.0054 -0.0050 -0.0648 218 PRO A O 1648 C CB . PRO A 218 ? 0.3599 0.3724 0.3284 0.0002 -0.0013 -0.0551 218 PRO A CB 1649 C CG . PRO A 218 ? 0.3495 0.3759 0.3178 0.0022 -0.0011 -0.0554 218 PRO A CG 1650 C CD . PRO A 218 ? 0.3506 0.3606 0.3167 0.0012 0.0011 -0.0585 218 PRO A CD 1651 N N . ASP A 219 ? 0.3543 0.3680 0.3672 0.0153 -0.0061 -0.0603 219 ASP A N 1652 C CA . ASP A 219 ? 0.3602 0.3637 0.3874 0.0230 -0.0110 -0.0614 219 ASP A CA 1653 C C . ASP A 219 ? 0.3535 0.3458 0.3838 0.0210 -0.0146 -0.0572 219 ASP A C 1654 O O . ASP A 219 ? 0.3611 0.3513 0.4058 0.0183 -0.0124 -0.0620 219 ASP A O 1655 C CB . ASP A 219 ? 0.3687 0.3753 0.4056 0.0244 -0.0179 -0.0632 219 ASP A CB 1656 C CG . ASP A 219 ? 0.4021 0.4097 0.4651 0.0430 -0.0238 -0.0744 219 ASP A CG 1657 O OD1 . ASP A 219 ? 0.4742 0.4661 0.5422 0.0578 -0.0258 -0.0831 219 ASP A OD1 1658 O OD2 . ASP A 219 ? 0.4229 0.4403 0.5217 0.0626 -0.0178 -0.0924 219 ASP A OD2 1659 N N . ASP A 220 ? 0.3414 0.3235 0.3540 0.0190 -0.0153 -0.0571 220 ASP A N 1660 C CA . ASP A 220 ? 0.3356 0.3013 0.3350 0.0187 -0.0200 -0.0532 220 ASP A CA 1661 C C . ASP A 220 ? 0.3202 0.2836 0.3082 0.0141 -0.0156 -0.0524 220 ASP A C 1662 O O . ASP A 220 ? 0.3154 0.2715 0.2969 0.0140 -0.0091 -0.0633 220 ASP A O 1663 C CB . ASP A 220 ? 0.3385 0.3046 0.3406 0.0221 -0.0266 -0.0500 220 ASP A CB 1664 C CG . ASP A 220 ? 0.3628 0.3098 0.3619 0.0297 -0.0391 -0.0414 220 ASP A CG 1665 O OD1 . ASP A 220 ? 0.3689 0.3118 0.3986 0.0483 -0.0641 -0.0334 220 ASP A OD1 1666 O OD2 . ASP A 220 ? 0.3891 0.3113 0.3719 0.0266 -0.0758 -0.0362 220 ASP A OD2 1667 N N . TYR A 221 ? 0.3100 0.2555 0.2757 0.0083 -0.0081 -0.0542 221 TYR A N 1668 C CA . TYR A 221 ? 0.3061 0.2433 0.2473 0.0052 -0.0071 -0.0499 221 TYR A CA 1669 C C . TYR A 221 ? 0.3099 0.2462 0.2496 0.0058 -0.0045 -0.0467 221 TYR A C 1670 O O . TYR A 221 ? 0.3101 0.2474 0.2359 0.0028 -0.0017 -0.0452 221 TYR A O 1671 C CB . TYR A 221 ? 0.2989 0.2263 0.2336 0.0029 -0.0087 -0.0494 221 TYR A CB 1672 C CG . TYR A 221 ? 0.2767 0.1938 0.2106 0.0062 -0.0107 -0.0557 221 TYR A CG 1673 C CD1 . TYR A 221 ? 0.2817 0.1724 0.1760 0.0065 -0.0058 -0.0786 221 TYR A CD1 1674 C CD2 . TYR A 221 ? 0.2741 0.1536 0.1916 0.0003 -0.0177 -0.0457 221 TYR A CD2 1675 C CE1 . TYR A 221 ? 0.2691 0.1749 0.1994 0.0130 -0.0201 -0.0471 221 TYR A CE1 1676 C CE2 . TYR A 221 ? 0.2474 0.1803 0.1990 0.0125 -0.0025 -0.0385 221 TYR A CE2 1677 C CZ . TYR A 221 ? 0.2814 0.1710 0.2001 0.0176 -0.0174 -0.0417 221 TYR A CZ 1678 O OH . TYR A 221 ? 0.2735 0.1628 0.2092 0.0214 -0.0062 -0.0492 221 TYR A OH 1679 N N . SER A 222 ? 0.3150 0.2450 0.2465 0.0069 -0.0025 -0.0398 222 SER A N 1680 C CA . SER A 222 ? 0.3230 0.2558 0.2548 0.0101 -0.0040 -0.0322 222 SER A CA 1681 C C . SER A 222 ? 0.3162 0.2540 0.2486 0.0118 -0.0026 -0.0307 222 SER A C 1682 O O . SER A 222 ? 0.3256 0.2541 0.2552 0.0135 0.0027 -0.0266 222 SER A O 1683 C CB . SER A 222 ? 0.3164 0.2546 0.2552 0.0118 -0.0056 -0.0306 222 SER A CB 1684 O OG . SER A 222 ? 0.3604 0.2697 0.2774 0.0141 -0.0253 -0.0322 222 SER A OG 1685 N N . GLN A 223 ? 0.3041 0.2540 0.2432 0.0128 -0.0059 -0.0261 223 GLN A N 1686 C CA . GLN A 223 ? 0.3010 0.2613 0.2392 0.0129 -0.0062 -0.0258 223 GLN A CA 1687 C C . GLN A 223 ? 0.2928 0.2602 0.2339 0.0121 -0.0021 -0.0254 223 GLN A C 1688 O O . GLN A 223 ? 0.2951 0.2604 0.2284 0.0067 -0.0019 -0.0295 223 GLN A O 1689 C CB . GLN A 223 ? 0.3046 0.2608 0.2427 0.0117 -0.0084 -0.0242 223 GLN A CB 1690 C CG . GLN A 223 ? 0.3376 0.2865 0.2537 0.0122 -0.0220 -0.0253 223 GLN A CG 1691 C CD . GLN A 223 ? 0.3954 0.3108 0.2702 0.0180 -0.0300 -0.0258 223 GLN A CD 1692 O OE1 . GLN A 223 ? 0.4068 0.3418 0.2693 0.0306 -0.0389 -0.0439 223 GLN A OE1 1693 N NE2 . GLN A 223 ? 0.4203 0.3244 0.2686 0.0095 -0.0397 -0.0152 223 GLN A NE2 1694 N N . GLY A 224 ? 0.2820 0.2590 0.2262 0.0118 -0.0020 -0.0254 224 GLY A N 1695 C CA . GLY A 224 ? 0.2780 0.2516 0.2204 0.0116 -0.0040 -0.0275 224 GLY A CA 1696 C C . GLY A 224 ? 0.2844 0.2468 0.2219 0.0059 -0.0074 -0.0307 224 GLY A C 1697 O O . GLY A 224 ? 0.2847 0.2372 0.2130 0.0042 0.0000 -0.0321 224 GLY A O 1698 N N . GLY A 225 ? 0.2786 0.2449 0.2243 0.0059 -0.0120 -0.0350 225 GLY A N 1699 C CA . GLY A 225 ? 0.2683 0.2519 0.2258 0.0012 -0.0144 -0.0336 225 GLY A CA 1700 C C . GLY A 225 ? 0.2718 0.2600 0.2321 0.0052 -0.0200 -0.0374 225 GLY A C 1701 O O . GLY A 225 ? 0.2691 0.2583 0.2440 0.0058 -0.0169 -0.0353 225 GLY A O 1702 N N . THR A 226 ? 0.2661 0.2622 0.2219 0.0039 -0.0264 -0.0382 226 THR A N 1703 C CA . THR A 226 ? 0.2631 0.2573 0.2208 0.0002 -0.0290 -0.0437 226 THR A CA 1704 C C . THR A 226 ? 0.2611 0.2556 0.2145 -0.0071 -0.0349 -0.0439 226 THR A C 1705 O O . THR A 226 ? 0.2559 0.2527 0.2112 -0.0094 -0.0333 -0.0359 226 THR A O 1706 C CB . THR A 226 ? 0.2545 0.2567 0.2184 -0.0028 -0.0328 -0.0436 226 THR A CB 1707 O OG1 . THR A 226 ? 0.2818 0.2498 0.2112 0.0038 -0.0312 -0.0659 226 THR A OG1 1708 C CG2 . THR A 226 ? 0.2713 0.2735 0.2362 0.0076 -0.0308 -0.0446 226 THR A CG2 1709 N N . ARG A 227 ? 0.2651 0.2606 0.2196 -0.0109 -0.0391 -0.0459 227 ARG A N 1710 C CA . ARG A 227 ? 0.2709 0.2722 0.2329 -0.0128 -0.0365 -0.0436 227 ARG A CA 1711 C C . ARG A 227 ? 0.2768 0.2869 0.2422 -0.0149 -0.0372 -0.0406 227 ARG A C 1712 O O . ARG A 227 ? 0.2876 0.2976 0.2433 -0.0183 -0.0357 -0.0478 227 ARG A O 1713 C CB . ARG A 227 ? 0.2664 0.2668 0.2251 -0.0143 -0.0318 -0.0359 227 ARG A CB 1714 C CG . ARG A 227 ? 0.2596 0.2590 0.2220 -0.0084 -0.0361 -0.0453 227 ARG A CG 1715 C CD . ARG A 227 ? 0.2414 0.2403 0.2179 0.0154 -0.0237 -0.0306 227 ARG A CD 1716 N NE . ARG A 227 ? 0.2375 0.2181 0.2193 0.0162 -0.0209 -0.0189 227 ARG A NE 1717 C CZ . ARG A 227 ? 0.2381 0.1983 0.2041 0.0066 -0.0157 -0.0226 227 ARG A CZ 1718 N NH1 . ARG A 227 ? 0.2058 0.1402 0.1869 -0.0205 -0.0409 -0.0211 227 ARG A NH1 1719 N NH2 . ARG A 227 ? 0.2115 0.1847 0.2050 0.0058 -0.0034 -0.0373 227 ARG A NH2 1720 N N . LEU A 228 ? 0.2871 0.3004 0.2541 -0.0161 -0.0422 -0.0358 228 LEU A N 1721 C CA . LEU A 228 ? 0.2964 0.3197 0.2751 -0.0155 -0.0430 -0.0267 228 LEU A CA 1722 C C . LEU A 228 ? 0.2964 0.3197 0.2723 -0.0119 -0.0484 -0.0246 228 LEU A C 1723 O O . LEU A 228 ? 0.3024 0.3207 0.2644 -0.0118 -0.0606 -0.0286 228 LEU A O 1724 C CB . LEU A 228 ? 0.3020 0.3280 0.2863 -0.0224 -0.0431 -0.0235 228 LEU A CB 1725 C CG . LEU A 228 ? 0.3162 0.3437 0.3135 -0.0286 -0.0314 -0.0262 228 LEU A CG 1726 C CD1 . LEU A 228 ? 0.3880 0.3947 0.3625 -0.0354 -0.0279 -0.0244 228 LEU A CD1 1727 C CD2 . LEU A 228 ? 0.3440 0.3734 0.3496 -0.0282 -0.0357 -0.0313 228 LEU A CD2 1728 N N . ASP A 229 ? 0.2946 0.3157 0.2700 -0.0124 -0.0532 -0.0217 229 ASP A N 1729 C CA . ASP A 229 ? 0.2984 0.3210 0.2746 -0.0095 -0.0536 -0.0217 229 ASP A CA 1730 C C . ASP A 229 ? 0.3044 0.3171 0.2770 -0.0119 -0.0526 -0.0233 229 ASP A C 1731 O O . ASP A 229 ? 0.3079 0.3198 0.2859 -0.0078 -0.0617 -0.0180 229 ASP A O 1732 C CB . ASP A 229 ? 0.2882 0.3162 0.2715 -0.0081 -0.0559 -0.0227 229 ASP A CB 1733 C CG . ASP A 229 ? 0.2816 0.3265 0.2580 -0.0050 -0.0648 -0.0235 229 ASP A CG 1734 O OD1 . ASP A 229 ? 0.2690 0.3456 0.2125 -0.0302 -0.0477 -0.0196 229 ASP A OD1 1735 O OD2 . ASP A 229 ? 0.2676 0.3663 0.2675 0.0193 -0.0673 -0.0028 229 ASP A OD2 1736 N N . GLY A 230 ? 0.3009 0.3138 0.2696 -0.0116 -0.0430 -0.0314 230 GLY A N 1737 C CA . GLY A 230 ? 0.3141 0.3117 0.2653 -0.0134 -0.0353 -0.0315 230 GLY A CA 1738 C C . GLY A 230 ? 0.3159 0.3150 0.2586 -0.0131 -0.0269 -0.0358 230 GLY A C 1739 O O . GLY A 230 ? 0.3229 0.3190 0.2502 -0.0169 -0.0283 -0.0416 230 GLY A O 1740 N N . LYS A 231 ? 0.3128 0.3099 0.2514 -0.0068 -0.0195 -0.0381 231 LYS A N 1741 C CA . LYS A 231 ? 0.3082 0.3135 0.2476 0.0014 -0.0133 -0.0357 231 LYS A CA 1742 C C . LYS A 231 ? 0.3042 0.3092 0.2338 0.0000 -0.0114 -0.0366 231 LYS A C 1743 O O . LYS A 231 ? 0.3071 0.3176 0.2302 0.0005 -0.0199 -0.0352 231 LYS A O 1744 C CB . LYS A 231 ? 0.3113 0.3101 0.2516 0.0071 -0.0126 -0.0345 231 LYS A CB 1745 C CG . LYS A 231 ? 0.3341 0.3428 0.2961 0.0125 0.0026 -0.0325 231 LYS A CG 1746 C CD . LYS A 231 ? 0.3751 0.3836 0.3486 0.0356 0.0136 -0.0394 231 LYS A CD 1747 C CE . LYS A 231 ? 0.4023 0.4336 0.4094 0.0302 0.0202 -0.0478 231 LYS A CE 1748 N NZ . LYS A 231 ? 0.4437 0.4646 0.4677 0.0384 0.0125 -0.0448 231 LYS A NZ 1749 N N . ASN A 232 ? 0.2919 0.3039 0.2173 -0.0008 -0.0093 -0.0368 232 ASN A N 1750 C CA . ASN A 232 ? 0.2756 0.2981 0.2063 0.0012 -0.0073 -0.0342 232 ASN A CA 1751 C C . ASN A 232 ? 0.2617 0.2927 0.1970 0.0003 -0.0061 -0.0325 232 ASN A C 1752 O O . ASN A 232 ? 0.2591 0.2917 0.1887 0.0026 -0.0090 -0.0418 232 ASN A O 1753 C CB . ASN A 232 ? 0.2774 0.3017 0.1980 0.0063 -0.0083 -0.0302 232 ASN A CB 1754 C CG . ASN A 232 ? 0.2869 0.3070 0.2058 0.0070 -0.0080 -0.0288 232 ASN A CG 1755 O OD1 . ASN A 232 ? 0.2921 0.3198 0.2303 0.0143 -0.0307 -0.0237 232 ASN A OD1 1756 N ND2 . ASN A 232 ? 0.2954 0.3650 0.1924 0.0024 -0.0007 -0.0211 232 ASN A ND2 1757 N N . LEU A 233 ? 0.2526 0.2833 0.1881 -0.0007 -0.0076 -0.0284 233 LEU A N 1758 C CA . LEU A 233 ? 0.2517 0.2773 0.1860 0.0005 -0.0079 -0.0181 233 LEU A CA 1759 C C . LEU A 233 ? 0.2566 0.2777 0.1810 0.0003 -0.0071 -0.0113 233 LEU A C 1760 O O . LEU A 233 ? 0.2474 0.2762 0.1793 0.0062 -0.0088 -0.0127 233 LEU A O 1761 C CB . LEU A 233 ? 0.2519 0.2769 0.1791 -0.0030 -0.0009 -0.0174 233 LEU A CB 1762 C CG . LEU A 233 ? 0.2445 0.2721 0.1916 -0.0025 -0.0102 -0.0175 233 LEU A CG 1763 C CD1 . LEU A 233 ? 0.2433 0.2468 0.1651 -0.0068 -0.0019 0.0000 233 LEU A CD1 1764 C CD2 . LEU A 233 ? 0.2415 0.2828 0.1967 0.0187 -0.0157 -0.0035 233 LEU A CD2 1765 N N . VAL A 234 ? 0.2613 0.2758 0.1796 0.0033 -0.0050 -0.0088 234 VAL A N 1766 C CA . VAL A 234 ? 0.2792 0.2864 0.1939 -0.0016 -0.0099 -0.0026 234 VAL A CA 1767 C C . VAL A 234 ? 0.2933 0.2990 0.2083 0.0000 -0.0124 -0.0004 234 VAL A C 1768 O O . VAL A 234 ? 0.2942 0.2985 0.2063 0.0030 -0.0156 0.0041 234 VAL A O 1769 C CB . VAL A 234 ? 0.2740 0.2854 0.1932 -0.0040 -0.0043 0.0008 234 VAL A CB 1770 C CG1 . VAL A 234 ? 0.2744 0.2865 0.2144 -0.0150 -0.0077 0.0015 234 VAL A CG1 1771 C CG2 . VAL A 234 ? 0.2693 0.2736 0.1807 -0.0047 -0.0107 -0.0010 234 VAL A CG2 1772 N N . GLN A 235 ? 0.3188 0.3159 0.2165 0.0046 -0.0148 0.0029 235 GLN A N 1773 C CA . GLN A 235 ? 0.3592 0.3423 0.2453 -0.0020 -0.0197 0.0034 235 GLN A CA 1774 C C . GLN A 235 ? 0.3409 0.3334 0.2363 -0.0017 -0.0287 0.0022 235 GLN A C 1775 O O . GLN A 235 ? 0.3519 0.3348 0.2334 0.0000 -0.0293 -0.0027 235 GLN A O 1776 C CB . GLN A 235 ? 0.3569 0.3491 0.2407 -0.0025 -0.0205 0.0045 235 GLN A CB 1777 C CG . GLN A 235 ? 0.4227 0.3824 0.2733 -0.0066 -0.0150 0.0090 235 GLN A CG 1778 C CD . GLN A 235 ? 0.4345 0.3891 0.2859 -0.0125 -0.0073 0.0106 235 GLN A CD 1779 O OE1 . GLN A 235 ? 0.5459 0.4893 0.3839 -0.0137 0.0110 0.0072 235 GLN A OE1 1780 N NE2 . GLN A 235 ? 0.5248 0.4191 0.3416 -0.0345 0.0041 0.0315 235 GLN A NE2 1781 N N . GLU A 236 ? 0.3296 0.3291 0.2290 -0.0044 -0.0360 0.0024 236 GLU A N 1782 C CA . GLU A 236 ? 0.3211 0.3230 0.2509 -0.0021 -0.0378 0.0060 236 GLU A CA 1783 C C . GLU A 236 ? 0.3126 0.3123 0.2459 0.0023 -0.0388 0.0124 236 GLU A C 1784 O O . GLU A 236 ? 0.3039 0.3004 0.2509 0.0053 -0.0515 0.0114 236 GLU A O 1785 C CB . GLU A 236 ? 0.3266 0.3256 0.2469 -0.0051 -0.0363 0.0059 236 GLU A CB 1786 C CG . GLU A 236 ? 0.3208 0.3433 0.2695 -0.0031 -0.0296 0.0085 236 GLU A CG 1787 C CD . GLU A 236 ? 0.3475 0.3513 0.2894 -0.0005 -0.0325 -0.0019 236 GLU A CD 1788 O OE1 . GLU A 236 ? 0.3664 0.4001 0.3344 0.0232 -0.0058 -0.0218 236 GLU A OE1 1789 O OE2 . GLU A 236 ? 0.3776 0.3901 0.3526 0.0004 -0.0433 -0.0181 236 GLU A OE2 1790 N N . TRP A 237 ? 0.3067 0.3033 0.2434 0.0024 -0.0398 0.0204 237 TRP A N 1791 C CA . TRP A 237 ? 0.3042 0.2984 0.2479 0.0034 -0.0369 0.0320 237 TRP A CA 1792 C C . TRP A 237 ? 0.3103 0.3064 0.2510 0.0090 -0.0404 0.0352 237 TRP A C 1793 O O . TRP A 237 ? 0.3077 0.2926 0.2468 0.0100 -0.0340 0.0406 237 TRP A O 1794 C CB . TRP A 237 ? 0.2984 0.2844 0.2454 0.0012 -0.0349 0.0352 237 TRP A CB 1795 C CG . TRP A 237 ? 0.3034 0.2958 0.2532 0.0042 -0.0299 0.0413 237 TRP A CG 1796 C CD1 . TRP A 237 ? 0.3220 0.2821 0.2620 -0.0032 -0.0306 0.0402 237 TRP A CD1 1797 C CD2 . TRP A 237 ? 0.3035 0.2794 0.2656 0.0021 -0.0262 0.0519 237 TRP A CD2 1798 N NE1 . TRP A 237 ? 0.3085 0.2854 0.2749 -0.0123 -0.0412 0.0389 237 TRP A NE1 1799 C CE2 . TRP A 237 ? 0.2938 0.2699 0.2681 -0.0006 -0.0327 0.0550 237 TRP A CE2 1800 C CE3 . TRP A 237 ? 0.3112 0.2950 0.2732 -0.0040 -0.0257 0.0879 237 TRP A CE3 1801 C CZ2 . TRP A 237 ? 0.3099 0.2670 0.2712 -0.0023 -0.0350 0.0571 237 TRP A CZ2 1802 C CZ3 . TRP A 237 ? 0.3115 0.2588 0.2469 -0.0107 -0.0432 0.0669 237 TRP A CZ3 1803 C CH2 . TRP A 237 ? 0.2977 0.2737 0.2567 0.0022 -0.0237 0.0560 237 TRP A CH2 1804 N N . LEU A 238 ? 0.3145 0.3154 0.2647 0.0142 -0.0371 0.0406 238 LEU A N 1805 C CA . LEU A 238 ? 0.3281 0.3287 0.2843 0.0126 -0.0348 0.0447 238 LEU A CA 1806 C C . LEU A 238 ? 0.3475 0.3429 0.2964 0.0110 -0.0325 0.0399 238 LEU A C 1807 O O . LEU A 238 ? 0.3461 0.3381 0.2854 0.0054 -0.0335 0.0468 238 LEU A O 1808 C CB . LEU A 238 ? 0.3324 0.3201 0.2811 0.0119 -0.0288 0.0430 238 LEU A CB 1809 C CG . LEU A 238 ? 0.3175 0.3324 0.2824 0.0152 -0.0383 0.0443 238 LEU A CG 1810 C CD1 . LEU A 238 ? 0.3081 0.3521 0.2779 0.0250 -0.0330 0.0336 238 LEU A CD1 1811 C CD2 . LEU A 238 ? 0.3288 0.3302 0.3095 0.0046 -0.0244 0.0434 238 LEU A CD2 1812 N N . ALA A 239 ? 0.3632 0.3600 0.3219 0.0110 -0.0323 0.0371 239 ALA A N 1813 C CA . ALA A 239 ? 0.3899 0.3858 0.3552 0.0112 -0.0311 0.0294 239 ALA A CA 1814 C C . ALA A 239 ? 0.4085 0.4000 0.3799 0.0126 -0.0318 0.0243 239 ALA A C 1815 O O . ALA A 239 ? 0.4250 0.4117 0.3923 0.0066 -0.0295 0.0182 239 ALA A O 1816 C CB . ALA A 239 ? 0.3875 0.3780 0.3427 0.0125 -0.0354 0.0320 239 ALA A CB 1817 N N . LYS A 240 ? 0.4289 0.4230 0.4093 0.0141 -0.0314 0.0143 240 LYS A N 1818 C CA . LYS A 240 ? 0.4543 0.4492 0.4413 0.0144 -0.0285 0.0109 240 LYS A CA 1819 C C . LYS A 240 ? 0.4629 0.4554 0.4538 0.0176 -0.0300 0.0066 240 LYS A C 1820 O O . LYS A 240 ? 0.4740 0.4634 0.4626 0.0200 -0.0337 0.0033 240 LYS A O 1821 C CB . LYS A 240 ? 0.4498 0.4561 0.4457 0.0162 -0.0241 0.0109 240 LYS A CB 1822 C CG . LYS A 240 ? 0.4946 0.4957 0.4763 0.0079 -0.0145 0.0101 240 LYS A CG 1823 C CD . LYS A 240 ? 0.5302 0.5470 0.5211 0.0088 0.0061 0.0095 240 LYS A CD 1824 C CE . LYS A 240 ? 0.5606 0.5747 0.5442 -0.0021 0.0253 0.0068 240 LYS A CE 1825 N NZ . LYS A 240 ? 0.5838 0.5750 0.5276 0.0093 0.0407 0.0163 240 LYS A NZ 1826 N N . ARG A 241 ? 0.4743 0.4595 0.4633 0.0146 -0.0302 0.0078 241 ARG A N 1827 C CA . ARG A 241 ? 0.4772 0.4582 0.4634 0.0135 -0.0309 0.0101 241 ARG A CA 1828 C C . ARG A 241 ? 0.4803 0.4553 0.4675 0.0114 -0.0293 0.0134 241 ARG A C 1829 O O . ARG A 241 ? 0.4904 0.4581 0.4740 0.0125 -0.0320 0.0140 241 ARG A O 1830 C CB . ARG A 241 ? 0.4782 0.4583 0.4674 0.0154 -0.0339 0.0079 241 ARG A CB 1831 C CG . ARG A 241 ? 0.4806 0.4577 0.4600 0.0172 -0.0410 0.0051 241 ARG A CG 1832 C CD . ARG A 241 ? 0.4942 0.4466 0.4360 0.0250 -0.0578 -0.0042 241 ARG A CD 1833 N NE . ARG A 241 ? 0.5100 0.4211 0.4406 0.0256 -0.0726 -0.0044 241 ARG A NE 1834 C CZ . ARG A 241 ? 0.5297 0.4164 0.4299 0.0312 -0.0746 -0.0158 241 ARG A CZ 1835 N NH1 . ARG A 241 ? 0.5478 0.4136 0.3804 0.0268 -0.0768 -0.0458 241 ARG A NH1 1836 N NH2 . ARG A 241 ? 0.5302 0.3769 0.4065 0.0362 -0.0772 -0.0306 241 ARG A NH2 1837 N N . GLN A 242 ? 0.4789 0.4501 0.4652 0.0081 -0.0239 0.0192 242 GLN A N 1838 C CA . GLN A 242 ? 0.4814 0.4455 0.4597 0.0052 -0.0197 0.0231 242 GLN A CA 1839 C C . GLN A 242 ? 0.4602 0.4243 0.4329 0.0075 -0.0215 0.0265 242 GLN A C 1840 O O . GLN A 242 ? 0.4657 0.4312 0.4386 0.0081 -0.0289 0.0291 242 GLN A O 1841 C CB . GLN A 242 ? 0.4949 0.4572 0.4654 0.0017 -0.0148 0.0233 242 GLN A CB 1842 C CG . GLN A 242 ? 0.5526 0.4923 0.5126 -0.0072 0.0021 0.0176 242 GLN A CG 1843 C CD . GLN A 242 ? 0.6241 0.5493 0.5562 -0.0105 0.0223 0.0052 242 GLN A CD 1844 O OE1 . GLN A 242 ? 0.6585 0.5831 0.5885 -0.0048 0.0306 0.0000 242 GLN A OE1 1845 N NE2 . GLN A 242 ? 0.6506 0.5793 0.5764 -0.0142 0.0242 0.0079 242 GLN A NE2 1846 N N . GLY A 243 ? 0.4387 0.3987 0.4095 0.0065 -0.0226 0.0335 243 GLY A N 1847 C CA . GLY A 243 ? 0.4117 0.3737 0.3738 0.0111 -0.0165 0.0320 243 GLY A CA 1848 C C . GLY A 243 ? 0.3904 0.3500 0.3444 0.0141 -0.0134 0.0311 243 GLY A C 1849 O O . GLY A 243 ? 0.3896 0.3516 0.3546 0.0171 -0.0143 0.0339 243 GLY A O 1850 N N . ALA A 244 ? 0.3628 0.3273 0.3108 0.0171 -0.0072 0.0260 244 ALA A N 1851 C CA . ALA A 244 ? 0.3400 0.3033 0.2824 0.0229 -0.0048 0.0242 244 ALA A CA 1852 C C . ALA A 244 ? 0.3309 0.3024 0.2716 0.0190 -0.0017 0.0228 244 ALA A C 1853 O O . ALA A 244 ? 0.3293 0.2909 0.2448 0.0257 -0.0053 0.0220 244 ALA A O 1854 C CB . ALA A 244 ? 0.3392 0.3011 0.2834 0.0196 -0.0005 0.0246 244 ALA A CB 1855 N N . ARG A 245 ? 0.3023 0.2829 0.2444 0.0238 -0.0035 0.0232 245 ARG A N 1856 C CA . ARG A 245 ? 0.2926 0.2871 0.2370 0.0139 0.0074 0.0205 245 ARG A CA 1857 C C . ARG A 245 ? 0.2690 0.2667 0.2235 0.0120 0.0096 0.0190 245 ARG A C 1858 O O . ARG A 245 ? 0.2576 0.2561 0.2065 0.0122 0.0110 0.0225 245 ARG A O 1859 C CB . ARG A 245 ? 0.2955 0.2891 0.2505 0.0196 0.0047 0.0171 245 ARG A CB 1860 C CG . ARG A 245 ? 0.3572 0.3509 0.2732 0.0070 0.0143 0.0166 245 ARG A CG 1861 C CD . ARG A 245 ? 0.4463 0.4219 0.3120 -0.0054 0.0229 0.0217 245 ARG A CD 1862 N NE . ARG A 245 ? 0.5003 0.4571 0.3570 -0.0098 0.0226 0.0243 245 ARG A NE 1863 C CZ . ARG A 245 ? 0.5089 0.4967 0.3604 0.0033 0.0299 0.0225 245 ARG A CZ 1864 N NH1 . ARG A 245 ? 0.5168 0.5243 0.3250 0.0149 0.0298 0.0232 245 ARG A NH1 1865 N NH2 . ARG A 245 ? 0.5166 0.5058 0.3485 -0.0132 0.0501 0.0213 245 ARG A NH2 1866 N N . TYR A 246 ? 0.2457 0.2650 0.2062 0.0030 0.0142 0.0170 246 TYR A N 1867 C CA . TYR A 246 ? 0.2406 0.2594 0.2036 0.0000 0.0159 0.0107 246 TYR A CA 1868 C C . TYR A 246 ? 0.2411 0.2706 0.1964 0.0001 0.0160 0.0123 246 TYR A C 1869 O O . TYR A 246 ? 0.2381 0.2916 0.1889 -0.0053 0.0280 0.0105 246 TYR A O 1870 C CB . TYR A 246 ? 0.2446 0.2528 0.2119 -0.0017 0.0097 0.0179 246 TYR A CB 1871 C CG . TYR A 246 ? 0.2475 0.2416 0.2316 -0.0217 0.0029 0.0144 246 TYR A CG 1872 C CD1 . TYR A 246 ? 0.2571 0.2401 0.2094 -0.0273 -0.0194 0.0304 246 TYR A CD1 1873 C CD2 . TYR A 246 ? 0.2590 0.2402 0.2419 -0.0150 0.0028 0.0181 246 TYR A CD2 1874 C CE1 . TYR A 246 ? 0.2610 0.2275 0.2378 -0.0181 -0.0138 0.0234 246 TYR A CE1 1875 C CE2 . TYR A 246 ? 0.2556 0.2309 0.2276 -0.0225 -0.0039 0.0214 246 TYR A CE2 1876 C CZ . TYR A 246 ? 0.2559 0.2382 0.2284 -0.0160 -0.0100 0.0218 246 TYR A CZ 1877 O OH . TYR A 246 ? 0.2441 0.2201 0.2320 -0.0095 -0.0082 0.0303 246 TYR A OH 1878 N N . VAL A 247 ? 0.2391 0.2645 0.1873 0.0003 0.0235 0.0092 247 VAL A N 1879 C CA . VAL A 247 ? 0.2413 0.2546 0.1772 0.0055 0.0212 0.0122 247 VAL A CA 1880 C C . VAL A 247 ? 0.2414 0.2583 0.1809 0.0066 0.0222 0.0071 247 VAL A C 1881 O O . VAL A 247 ? 0.2310 0.2601 0.1666 0.0088 0.0200 0.0133 247 VAL A O 1882 C CB . VAL A 247 ? 0.2393 0.2526 0.1762 0.0023 0.0230 0.0150 247 VAL A CB 1883 C CG1 . VAL A 247 ? 0.2457 0.2364 0.1919 -0.0043 0.0152 0.0179 247 VAL A CG1 1884 C CG2 . VAL A 247 ? 0.2100 0.2251 0.1370 0.0180 0.0300 -0.0025 247 VAL A CG2 1885 N N . TRP A 248 ? 0.2396 0.2612 0.1785 0.0103 0.0230 -0.0034 248 TRP A N 1886 C CA . TRP A 248 ? 0.2468 0.2684 0.1914 0.0189 0.0315 -0.0087 248 TRP A CA 1887 C C . TRP A 248 ? 0.2357 0.2603 0.1860 0.0237 0.0372 -0.0129 248 TRP A C 1888 O O . TRP A 248 ? 0.2352 0.2637 0.1892 0.0351 0.0396 -0.0183 248 TRP A O 1889 C CB . TRP A 248 ? 0.2632 0.2747 0.1971 0.0214 0.0345 -0.0190 248 TRP A CB 1890 C CG . TRP A 248 ? 0.2878 0.3060 0.2248 0.0184 0.0334 -0.0153 248 TRP A CG 1891 C CD1 . TRP A 248 ? 0.3214 0.3329 0.2364 0.0224 0.0382 -0.0237 248 TRP A CD1 1892 C CD2 . TRP A 248 ? 0.3125 0.3053 0.2359 0.0226 0.0397 -0.0264 248 TRP A CD2 1893 N NE1 . TRP A 248 ? 0.3269 0.3455 0.2633 0.0349 0.0406 -0.0264 248 TRP A NE1 1894 C CE2 . TRP A 248 ? 0.3303 0.3248 0.2566 0.0259 0.0329 -0.0257 248 TRP A CE2 1895 C CE3 . TRP A 248 ? 0.2979 0.3082 0.2536 0.0336 0.0272 -0.0313 248 TRP A CE3 1896 C CZ2 . TRP A 248 ? 0.3103 0.3164 0.2393 0.0319 0.0320 -0.0259 248 TRP A CZ2 1897 C CZ3 . TRP A 248 ? 0.3225 0.3274 0.2462 0.0203 0.0415 -0.0254 248 TRP A CZ3 1898 C CH2 . TRP A 248 ? 0.3104 0.3134 0.2361 0.0202 0.0340 -0.0272 248 TRP A CH2 1899 N N . ASN A 249 ? 0.2263 0.2555 0.1845 0.0250 0.0386 -0.0180 249 ASN A N 1900 C CA . ASN A 249 ? 0.2233 0.2543 0.1903 0.0224 0.0385 -0.0123 249 ASN A CA 1901 C C . ASN A 249 ? 0.2182 0.2608 0.1978 0.0188 0.0421 -0.0039 249 ASN A C 1902 O O . ASN A 249 ? 0.2119 0.2518 0.2048 0.0178 0.0415 -0.0089 249 ASN A O 1903 C CB . ASN A 249 ? 0.2182 0.2606 0.1770 0.0218 0.0469 -0.0138 249 ASN A CB 1904 C CG . ASN A 249 ? 0.2609 0.2774 0.2117 0.0238 0.0538 -0.0051 249 ASN A CG 1905 O OD1 . ASN A 249 ? 0.2443 0.2609 0.2062 0.0231 0.0632 -0.0138 249 ASN A OD1 1906 N ND2 . ASN A 249 ? 0.3250 0.3460 0.2159 0.0327 0.0875 -0.0001 249 ASN A ND2 1907 N N . ARG A 250 ? 0.2170 0.2648 0.2030 0.0166 0.0397 0.0000 250 ARG A N 1908 C CA . ARG A 250 ? 0.2267 0.2755 0.2163 0.0158 0.0372 0.0091 250 ARG A CA 1909 C C . ARG A 250 ? 0.2427 0.2843 0.2261 0.0158 0.0366 0.0127 250 ARG A C 1910 O O . ARG A 250 ? 0.2488 0.2772 0.2350 0.0177 0.0333 0.0110 250 ARG A O 1911 C CB . ARG A 250 ? 0.2241 0.2766 0.2106 0.0155 0.0319 0.0098 250 ARG A CB 1912 C CG . ARG A 250 ? 0.1963 0.2805 0.2084 0.0264 0.0234 0.0173 250 ARG A CG 1913 C CD . ARG A 250 ? 0.2093 0.3293 0.2331 0.0180 0.0280 0.0025 250 ARG A CD 1914 N NE . ARG A 250 ? 0.1742 0.3077 0.2644 0.0251 0.0241 -0.0074 250 ARG A NE 1915 C CZ . ARG A 250 ? 0.2366 0.3435 0.2964 0.0149 0.0401 -0.0091 250 ARG A CZ 1916 N NH1 . ARG A 250 ? 0.2433 0.3475 0.2862 0.0135 0.0407 -0.0014 250 ARG A NH1 1917 N NH2 . ARG A 250 ? 0.1962 0.3422 0.2934 0.0000 0.0165 -0.0299 250 ARG A NH2 1918 N N . THR A 251 ? 0.2579 0.2993 0.2372 0.0098 0.0452 0.0154 251 THR A N 1919 C CA . THR A 251 ? 0.2843 0.3134 0.2530 0.0057 0.0564 0.0163 251 THR A CA 1920 C C . THR A 251 ? 0.2768 0.3154 0.2487 0.0009 0.0590 0.0158 251 THR A C 1921 O O . THR A 251 ? 0.2799 0.3068 0.2570 0.0030 0.0666 0.0259 251 THR A O 1922 C CB . THR A 251 ? 0.2832 0.3183 0.2680 0.0028 0.0525 0.0092 251 THR A CB 1923 O OG1 . THR A 251 ? 0.3556 0.3754 0.3328 0.0098 0.0673 -0.0033 251 THR A OG1 1924 C CG2 . THR A 251 ? 0.3136 0.3167 0.2574 0.0085 0.0753 0.0246 251 THR A CG2 1925 N N . GLU A 252 ? 0.2767 0.3189 0.2349 -0.0030 0.0589 0.0166 252 GLU A N 1926 C CA . GLU A 252 ? 0.2870 0.3257 0.2414 -0.0072 0.0513 0.0149 252 GLU A CA 1927 C C . GLU A 252 ? 0.2724 0.3133 0.2275 -0.0119 0.0429 0.0122 252 GLU A C 1928 O O . GLU A 252 ? 0.2706 0.3048 0.1970 -0.0114 0.0450 0.0184 252 GLU A O 1929 C CB . GLU A 252 ? 0.2954 0.3372 0.2528 -0.0062 0.0498 0.0122 252 GLU A CB 1930 C CG . GLU A 252 ? 0.3566 0.4114 0.3130 0.0037 0.0614 0.0251 252 GLU A CG 1931 C CD . GLU A 252 ? 0.4354 0.5028 0.4086 0.0298 0.0445 0.0584 252 GLU A CD 1932 O OE1 . GLU A 252 ? 0.4957 0.5649 0.4727 0.0428 0.0448 0.0694 252 GLU A OE1 1933 O OE2 . GLU A 252 ? 0.4712 0.5483 0.4387 0.0388 0.0582 0.0574 252 GLU A OE2 1934 N N . LEU A 253 ? 0.2595 0.3027 0.2255 -0.0184 0.0372 0.0121 253 LEU A N 1935 C CA . LEU A 253 ? 0.2563 0.3006 0.2283 -0.0196 0.0269 0.0104 253 LEU A CA 1936 C C . LEU A 253 ? 0.2635 0.3166 0.2565 -0.0174 0.0238 0.0168 253 LEU A C 1937 O O . LEU A 253 ? 0.2489 0.3159 0.2401 -0.0130 0.0215 0.0192 253 LEU A O 1938 C CB . LEU A 253 ? 0.2504 0.2862 0.2209 -0.0175 0.0303 0.0136 253 LEU A CB 1939 C CG . LEU A 253 ? 0.2532 0.2771 0.2059 -0.0241 0.0232 0.0106 253 LEU A CG 1940 C CD1 . LEU A 253 ? 0.2021 0.2400 0.1917 -0.0101 0.0244 -0.0005 253 LEU A CD1 1941 C CD2 . LEU A 253 ? 0.2637 0.2847 0.2055 -0.0224 0.0196 0.0063 253 LEU A CD2 1942 N N . MET A 254 ? 0.2641 0.3378 0.2956 -0.0139 0.0166 0.0160 254 MET A N 1943 C CA . MET A 254 ? 0.2932 0.3646 0.3530 -0.0133 0.0067 0.0160 254 MET A CA 1944 C C . MET A 254 ? 0.2789 0.3482 0.3384 -0.0133 0.0086 0.0158 254 MET A C 1945 O O . MET A 254 ? 0.2827 0.3443 0.3448 -0.0206 0.0077 0.0228 254 MET A O 1946 C CB . MET A 254 ? 0.2919 0.3597 0.3609 -0.0163 -0.0027 0.0191 254 MET A CB 1947 C CG . MET A 254 ? 0.3242 0.4136 0.4077 -0.0220 -0.0024 0.0214 254 MET A CG 1948 S SD . MET A 254 ? 0.3738 0.4624 0.4502 0.0096 -0.0103 0.0096 254 MET A SD 1949 C CE . MET A 254 ? 0.4023 0.4985 0.4303 -0.0154 0.0000 -0.0044 254 MET A CE 1950 N N . GLN A 255 ? 0.2850 0.3459 0.3342 -0.0133 0.0136 0.0177 255 GLN A N 1951 C CA . GLN A 255 ? 0.3019 0.3507 0.3320 -0.0111 0.0194 0.0125 255 GLN A CA 1952 C C . GLN A 255 ? 0.2883 0.3334 0.3076 -0.0105 0.0207 0.0164 255 GLN A C 1953 O O . GLN A 255 ? 0.3014 0.3271 0.2979 -0.0103 0.0287 0.0224 255 GLN A O 1954 C CB . GLN A 255 ? 0.2965 0.3497 0.3287 -0.0105 0.0232 0.0086 255 GLN A CB 1955 C CG . GLN A 255 ? 0.3327 0.3754 0.3547 -0.0124 0.0207 0.0069 255 GLN A CG 1956 C CD . GLN A 255 ? 0.3257 0.3868 0.3650 -0.0048 0.0245 0.0068 255 GLN A CD 1957 O OE1 . GLN A 255 ? 0.3661 0.4556 0.4131 -0.0041 0.0482 0.0085 255 GLN A OE1 1958 N NE2 . GLN A 255 ? 0.3827 0.4555 0.4040 0.0079 0.0250 0.0032 255 GLN A NE2 1959 N N . ALA A 256 ? 0.2846 0.3239 0.2984 -0.0079 0.0184 0.0180 256 ALA A N 1960 C CA . ALA A 256 ? 0.2645 0.3076 0.2895 -0.0083 0.0169 0.0246 256 ALA A CA 1961 C C . ALA A 256 ? 0.2565 0.2972 0.2827 -0.0102 0.0130 0.0288 256 ALA A C 1962 O O . ALA A 256 ? 0.2450 0.2912 0.2760 -0.0079 0.0151 0.0270 256 ALA A O 1963 C CB . ALA A 256 ? 0.2741 0.3167 0.2993 -0.0049 0.0131 0.0141 256 ALA A CB 1964 N N . SER A 257 ? 0.2478 0.2863 0.2843 -0.0116 0.0119 0.0344 257 SER A N 1965 C CA . SER A 257 ? 0.2479 0.2785 0.2789 -0.0074 0.0094 0.0402 257 SER A CA 1966 C C . SER A 257 ? 0.2551 0.2851 0.2914 -0.0058 0.0134 0.0456 257 SER A C 1967 O O . SER A 257 ? 0.2437 0.2682 0.2792 0.0014 0.0179 0.0410 257 SER A O 1968 C CB . SER A 257 ? 0.2432 0.2715 0.2682 -0.0080 0.0084 0.0373 257 SER A CB 1969 O OG . SER A 257 ? 0.2435 0.2542 0.2410 -0.0106 -0.0152 0.0519 257 SER A OG 1970 N N . LEU A 258 ? 0.2565 0.2946 0.3005 -0.0056 0.0166 0.0566 258 LEU A N 1971 C CA . LEU A 258 ? 0.2791 0.3217 0.3209 -0.0021 0.0152 0.0616 258 LEU A CA 1972 C C . LEU A 258 ? 0.2961 0.3283 0.3299 -0.0044 0.0139 0.0633 258 LEU A C 1973 O O . LEU A 258 ? 0.3074 0.3471 0.3457 -0.0045 0.0116 0.0664 258 LEU A O 1974 C CB . LEU A 258 ? 0.2540 0.3171 0.3144 -0.0035 0.0207 0.0650 258 LEU A CB 1975 C CG . LEU A 258 ? 0.2619 0.3428 0.3292 0.0101 0.0257 0.0685 258 LEU A CG 1976 C CD1 . LEU A 258 ? 0.1824 0.3619 0.3366 0.0137 0.0292 0.0822 258 LEU A CD1 1977 C CD2 . LEU A 258 ? 0.2384 0.3160 0.3325 -0.0104 0.0297 0.0664 258 LEU A CD2 1978 N N . ASP A 259 ? 0.3133 0.3417 0.3364 -0.0008 0.0138 0.0630 259 ASP A N 1979 C CA . ASP A 259 ? 0.3362 0.3439 0.3511 0.0012 0.0115 0.0644 259 ASP A CA 1980 C C . ASP A 259 ? 0.3522 0.3457 0.3648 -0.0020 0.0080 0.0647 259 ASP A C 1981 O O . ASP A 259 ? 0.3412 0.3373 0.3558 0.0064 0.0055 0.0680 259 ASP A O 1982 C CB . ASP A 259 ? 0.3465 0.3551 0.3379 0.0033 0.0113 0.0675 259 ASP A CB 1983 C CG . ASP A 259 ? 0.3719 0.3747 0.3507 0.0026 0.0255 0.0715 259 ASP A CG 1984 O OD1 . ASP A 259 ? 0.3970 0.4193 0.3261 -0.0005 0.0098 0.0556 259 ASP A OD1 1985 O OD2 . ASP A 259 ? 0.3842 0.3981 0.3167 -0.0058 0.0505 0.1270 259 ASP A OD2 1986 N N . PRO A 260 ? 0.3662 0.3524 0.3901 -0.0010 0.0069 0.0587 260 PRO A N 1987 C CA . PRO A 260 ? 0.3738 0.3488 0.3964 -0.0042 0.0069 0.0551 260 PRO A CA 1988 C C . PRO A 260 ? 0.3666 0.3463 0.3897 -0.0079 0.0083 0.0531 260 PRO A C 1989 O O . PRO A 260 ? 0.3829 0.3368 0.4048 -0.0029 0.0053 0.0481 260 PRO A O 1990 C CB . PRO A 260 ? 0.3708 0.3544 0.3977 -0.0055 0.0136 0.0522 260 PRO A CB 1991 C CG . PRO A 260 ? 0.3868 0.3574 0.4137 -0.0016 0.0034 0.0553 260 PRO A CG 1992 C CD . PRO A 260 ? 0.3718 0.3531 0.3906 -0.0037 0.0069 0.0618 260 PRO A CD 1993 N N . SER A 261 ? 0.3659 0.3425 0.3836 -0.0129 0.0077 0.0593 261 SER A N 1994 C CA . SER A 261 ? 0.3530 0.3423 0.3649 -0.0107 0.0061 0.0614 261 SER A CA 1995 C C . SER A 261 ? 0.3404 0.3375 0.3579 -0.0111 0.0083 0.0608 261 SER A C 1996 O O . SER A 261 ? 0.3385 0.3375 0.3590 -0.0110 0.0036 0.0709 261 SER A O 1997 C CB . SER A 261 ? 0.3638 0.3471 0.3701 -0.0091 0.0058 0.0628 261 SER A CB 1998 O OG . SER A 261 ? 0.3829 0.3785 0.3512 -0.0022 0.0112 0.0685 261 SER A OG 1999 N N . VAL A 262 ? 0.3242 0.3237 0.3362 -0.0133 0.0097 0.0586 262 VAL A N 2000 C CA . VAL A 262 ? 0.3121 0.3172 0.3233 -0.0091 0.0187 0.0485 262 VAL A CA 2001 C C . VAL A 262 ? 0.3157 0.3177 0.3306 -0.0094 0.0207 0.0432 262 VAL A C 2002 O O . VAL A 262 ? 0.3165 0.3272 0.3379 -0.0151 0.0320 0.0316 262 VAL A O 2003 C CB . VAL A 262 ? 0.3080 0.3103 0.3248 -0.0101 0.0195 0.0522 262 VAL A CB 2004 C CG1 . VAL A 262 ? 0.3025 0.3138 0.3102 -0.0019 0.0186 0.0645 262 VAL A CG1 2005 C CG2 . VAL A 262 ? 0.2949 0.3081 0.3078 -0.0009 0.0112 0.0480 262 VAL A CG2 2006 N N . THR A 263 ? 0.3149 0.3041 0.3236 -0.0037 0.0228 0.0426 263 THR A N 2007 C CA . THR A 263 ? 0.3206 0.3032 0.3314 0.0018 0.0187 0.0400 263 THR A CA 2008 C C . THR A 263 ? 0.3117 0.2908 0.3048 0.0012 0.0217 0.0367 263 THR A C 2009 O O . THR A 263 ? 0.3286 0.3000 0.3174 -0.0042 0.0173 0.0376 263 THR A O 2010 C CB . THR A 263 ? 0.3233 0.3040 0.3376 0.0014 0.0170 0.0441 263 THR A CB 2011 O OG1 . THR A 263 ? 0.3458 0.3285 0.3743 0.0224 -0.0060 0.0421 263 THR A OG1 2012 C CG2 . THR A 263 ? 0.3473 0.3231 0.3721 0.0185 0.0268 0.0500 263 THR A CG2 2013 N N . HIS A 264 ? 0.2921 0.2615 0.2790 0.0019 0.0193 0.0336 264 HIS A N 2014 C CA . HIS A 264 ? 0.2852 0.2492 0.2560 0.0074 0.0155 0.0301 264 HIS A CA 2015 C C . HIS A 264 ? 0.2721 0.2304 0.2366 0.0081 0.0139 0.0272 264 HIS A C 2016 O O . HIS A 264 ? 0.2798 0.2171 0.2243 0.0092 0.0128 0.0305 264 HIS A O 2017 C CB . HIS A 264 ? 0.2877 0.2546 0.2661 0.0089 0.0160 0.0311 264 HIS A CB 2018 C CG . HIS A 264 ? 0.3051 0.2714 0.2869 0.0095 0.0194 0.0344 264 HIS A CG 2019 N ND1 . HIS A 264 ? 0.3248 0.2989 0.3220 0.0165 0.0233 0.0404 264 HIS A ND1 2020 C CD2 . HIS A 264 ? 0.3019 0.2927 0.2913 0.0125 0.0176 0.0459 264 HIS A CD2 2021 C CE1 . HIS A 264 ? 0.3335 0.3238 0.3326 0.0046 0.0403 0.0411 264 HIS A CE1 2022 N NE2 . HIS A 264 ? 0.3418 0.3247 0.3123 -0.0111 0.0365 0.0423 264 HIS A NE2 2023 N N . LEU A 265 ? 0.2583 0.2193 0.2108 0.0053 0.0154 0.0238 265 LEU A N 2024 C CA . LEU A 265 ? 0.2444 0.2187 0.2025 0.0098 0.0102 0.0267 265 LEU A CA 2025 C C . LEU A 265 ? 0.2474 0.2226 0.2001 0.0106 0.0087 0.0239 265 LEU A C 2026 O O . LEU A 265 ? 0.2645 0.2321 0.1958 0.0062 0.0191 0.0368 265 LEU A O 2027 C CB . LEU A 265 ? 0.2534 0.2156 0.2080 0.0119 0.0085 0.0219 265 LEU A CB 2028 C CG . LEU A 265 ? 0.2400 0.2399 0.2163 0.0269 0.0086 0.0107 265 LEU A CG 2029 C CD1 . LEU A 265 ? 0.2432 0.2417 0.2180 0.0373 0.0259 -0.0128 265 LEU A CD1 2030 C CD2 . LEU A 265 ? 0.2612 0.2692 0.2412 0.0512 -0.0155 -0.0104 265 LEU A CD2 2031 N N . MET A 266 ? 0.2324 0.2085 0.1885 0.0128 0.0029 0.0190 266 MET A N 2032 C CA . MET A 266 ? 0.2373 0.2158 0.1952 0.0117 0.0009 0.0106 266 MET A CA 2033 C C . MET A 266 ? 0.2362 0.2060 0.1844 0.0140 -0.0003 0.0038 266 MET A C 2034 O O . MET A 266 ? 0.2515 0.2210 0.1755 0.0215 0.0024 -0.0023 266 MET A O 2035 C CB . MET A 266 ? 0.2261 0.2089 0.1889 0.0054 0.0018 0.0076 266 MET A CB 2036 C CG . MET A 266 ? 0.2292 0.2180 0.2017 0.0112 -0.0089 0.0248 266 MET A CG 2037 S SD . MET A 266 ? 0.2700 0.2268 0.2406 0.0071 -0.0075 0.0053 266 MET A SD 2038 C CE . MET A 266 ? 0.2453 0.2332 0.2302 0.0234 0.0262 0.0052 266 MET A CE 2039 N N . GLY A 267 ? 0.2261 0.1976 0.1736 0.0133 -0.0048 -0.0040 267 GLY A N 2040 C CA . GLY A 267 ? 0.2123 0.1839 0.1691 0.0075 -0.0035 -0.0011 267 GLY A CA 2041 C C . GLY A 267 ? 0.2041 0.1892 0.1706 0.0066 -0.0084 -0.0003 267 GLY A C 2042 O O . GLY A 267 ? 0.1889 0.1864 0.1709 0.0028 0.0003 -0.0012 267 GLY A O 2043 N N . LEU A 268 ? 0.1962 0.1835 0.1721 0.0061 -0.0075 -0.0022 268 LEU A N 2044 C CA . LEU A 268 ? 0.1874 0.1830 0.1672 0.0089 -0.0139 -0.0065 268 LEU A CA 2045 C C . LEU A 268 ? 0.1901 0.1890 0.1701 0.0063 -0.0122 -0.0099 268 LEU A C 2046 O O . LEU A 268 ? 0.1914 0.1902 0.1651 0.0192 -0.0200 -0.0116 268 LEU A O 2047 C CB . LEU A 268 ? 0.1859 0.1885 0.1675 0.0081 -0.0121 -0.0096 268 LEU A CB 2048 C CG . LEU A 268 ? 0.1852 0.1834 0.1598 0.0090 -0.0119 -0.0159 268 LEU A CG 2049 C CD1 . LEU A 268 ? 0.1493 0.2016 0.1573 -0.0055 -0.0319 -0.0431 268 LEU A CD1 2050 C CD2 . LEU A 268 ? 0.1834 0.1756 0.1568 -0.0007 0.0031 -0.0354 268 LEU A CD2 2051 N N . PHE A 269 ? 0.1808 0.1854 0.1654 0.0107 -0.0187 -0.0106 269 PHE A N 2052 C CA . PHE A 269 ? 0.1880 0.1969 0.1770 0.0057 -0.0116 -0.0186 269 PHE A CA 2053 C C . PHE A 269 ? 0.1848 0.1962 0.1708 0.0112 -0.0125 -0.0168 269 PHE A C 2054 O O . PHE A 269 ? 0.1975 0.2161 0.1770 0.0019 -0.0016 -0.0242 269 PHE A O 2055 C CB . PHE A 269 ? 0.1716 0.1865 0.1815 0.0020 -0.0115 -0.0166 269 PHE A CB 2056 C CG . PHE A 269 ? 0.1833 0.1785 0.2077 0.0051 -0.0081 -0.0231 269 PHE A CG 2057 C CD1 . PHE A 269 ? 0.1728 0.1831 0.2050 -0.0218 -0.0151 -0.0303 269 PHE A CD1 2058 C CD2 . PHE A 269 ? 0.1894 0.1719 0.1983 -0.0039 -0.0127 -0.0205 269 PHE A CD2 2059 C CE1 . PHE A 269 ? 0.1861 0.1285 0.1922 -0.0017 -0.0113 -0.0012 269 PHE A CE1 2060 C CE2 . PHE A 269 ? 0.2116 0.1930 0.2015 -0.0216 -0.0078 -0.0155 269 PHE A CE2 2061 C CZ . PHE A 269 ? 0.1797 0.1688 0.2060 -0.0022 -0.0007 -0.0297 269 PHE A CZ 2062 N N . GLU A 270 ? 0.1870 0.2010 0.1681 0.0150 -0.0103 -0.0191 270 GLU A N 2063 C CA . GLU A 270 ? 0.1891 0.2056 0.1789 0.0151 -0.0092 -0.0192 270 GLU A CA 2064 C C . GLU A 270 ? 0.1927 0.2023 0.1858 0.0146 -0.0075 -0.0205 270 GLU A C 2065 O O . GLU A 270 ? 0.1953 0.2007 0.1924 0.0065 -0.0069 -0.0203 270 GLU A O 2066 C CB . GLU A 270 ? 0.1916 0.2074 0.1693 0.0181 -0.0015 -0.0211 270 GLU A CB 2067 C CG . GLU A 270 ? 0.1866 0.2201 0.1788 0.0288 0.0005 -0.0192 270 GLU A CG 2068 C CD . GLU A 270 ? 0.2235 0.2504 0.2372 0.0179 0.0262 -0.0063 270 GLU A CD 2069 O OE1 . GLU A 270 ? 0.2455 0.2239 0.2474 0.0048 0.0401 -0.0313 270 GLU A OE1 2070 O OE2 . GLU A 270 ? 0.2411 0.2648 0.2881 0.0570 0.0380 -0.0091 270 GLU A OE2 2071 N N . PRO A 271 ? 0.1959 0.2015 0.1907 0.0177 -0.0073 -0.0294 271 PRO A N 2072 C CA . PRO A 271 ? 0.1982 0.2009 0.1892 0.0144 0.0013 -0.0243 271 PRO A CA 2073 C C . PRO A 271 ? 0.1969 0.1982 0.1843 0.0168 -0.0011 -0.0275 271 PRO A C 2074 O O . PRO A 271 ? 0.1990 0.1972 0.1838 0.0120 -0.0042 -0.0228 271 PRO A O 2075 C CB . PRO A 271 ? 0.1908 0.1954 0.1926 0.0179 0.0032 -0.0307 271 PRO A CB 2076 C CG . PRO A 271 ? 0.1977 0.2030 0.2006 0.0204 -0.0072 -0.0381 271 PRO A CG 2077 C CD . PRO A 271 ? 0.2018 0.1938 0.1981 0.0199 -0.0100 -0.0237 271 PRO A CD 2078 N N . GLY A 272 ? 0.1971 0.1995 0.1741 0.0144 -0.0003 -0.0204 272 GLY A N 2079 C CA . GLY A 272 ? 0.1948 0.1996 0.1677 0.0106 -0.0101 -0.0193 272 GLY A CA 2080 C C . GLY A 272 ? 0.1913 0.2050 0.1698 0.0082 -0.0062 -0.0122 272 GLY A C 2081 O O . GLY A 272 ? 0.1963 0.1954 0.1676 0.0085 -0.0096 -0.0109 272 GLY A O 2082 N N . ASP A 273 ? 0.1934 0.2103 0.1635 0.0049 -0.0023 -0.0162 273 ASP A N 2083 C CA . ASP A 273 ? 0.1861 0.2122 0.1623 0.0023 -0.0046 -0.0098 273 ASP A CA 2084 C C . ASP A 273 ? 0.1920 0.2093 0.1648 0.0040 -0.0031 -0.0059 273 ASP A C 2085 O O . ASP A 273 ? 0.1923 0.2059 0.1674 -0.0032 -0.0041 -0.0115 273 ASP A O 2086 C CB . ASP A 273 ? 0.1895 0.2094 0.1628 0.0025 -0.0015 -0.0095 273 ASP A CB 2087 C CG . ASP A 273 ? 0.1832 0.2178 0.1610 0.0102 0.0009 -0.0059 273 ASP A CG 2088 O OD1 . ASP A 273 ? 0.1968 0.2279 0.1479 0.0039 0.0040 -0.0175 273 ASP A OD1 2089 O OD2 . ASP A 273 ? 0.1822 0.1909 0.1654 0.0262 0.0083 0.0142 273 ASP A OD2 2090 N N . MET A 274 ? 0.1893 0.1959 0.1656 0.0069 0.0000 -0.0008 274 MET A N 2091 C CA . MET A 274 ? 0.1918 0.2055 0.1872 0.0181 0.0033 0.0018 274 MET A CA 2092 C C . MET A 274 ? 0.1834 0.2025 0.1728 0.0176 0.0048 -0.0044 274 MET A C 2093 O O . MET A 274 ? 0.1711 0.2033 0.1732 0.0232 0.0102 -0.0049 274 MET A O 2094 C CB . MET A 274 ? 0.1850 0.2057 0.1826 0.0162 -0.0031 0.0047 274 MET A CB 2095 C CG . MET A 274 ? 0.2163 0.1884 0.2132 0.0115 0.0009 0.0205 274 MET A CG 2096 S SD . MET A 274 ? 0.2332 0.2710 0.2420 0.0233 0.0164 0.0020 274 MET A SD 2097 C CE . MET A 274 ? 0.2164 0.2448 0.2289 0.0142 0.0270 0.0356 274 MET A CE 2098 N N . LYS A 275 ? 0.1760 0.1908 0.1615 0.0246 0.0094 -0.0175 275 LYS A N 2099 C CA . LYS A 275 ? 0.1777 0.1912 0.1590 0.0256 0.0110 -0.0206 275 LYS A CA 2100 C C . LYS A 275 ? 0.1808 0.1929 0.1576 0.0274 0.0111 -0.0139 275 LYS A C 2101 O O . LYS A 275 ? 0.1907 0.1714 0.1482 0.0202 0.0080 -0.0190 275 LYS A O 2102 C CB . LYS A 275 ? 0.1751 0.2038 0.1613 0.0245 0.0108 -0.0227 275 LYS A CB 2103 C CG . LYS A 275 ? 0.1994 0.2370 0.1786 0.0409 0.0270 -0.0521 275 LYS A CG 2104 C CD . LYS A 275 ? 0.2603 0.3090 0.2369 0.0508 0.0197 -0.0565 275 LYS A CD 2105 C CE . LYS A 275 ? 0.2895 0.3602 0.2608 0.0641 0.0363 -0.0796 275 LYS A CE 2106 N NZ . LYS A 275 ? 0.3102 0.4473 0.3121 0.0444 0.0358 -0.0642 275 LYS A NZ 2107 N N . TYR A 276 ? 0.1821 0.2028 0.1669 0.0227 0.0107 -0.0138 276 TYR A N 2108 C CA . TYR A 276 ? 0.1851 0.2152 0.1711 0.0250 0.0039 -0.0104 276 TYR A CA 2109 C C . TYR A 276 ? 0.1858 0.2297 0.1881 0.0261 -0.0012 -0.0135 276 TYR A C 2110 O O . TYR A 276 ? 0.1878 0.2358 0.1856 0.0214 -0.0056 -0.0176 276 TYR A O 2111 C CB . TYR A 276 ? 0.1836 0.2060 0.1680 0.0253 0.0061 -0.0068 276 TYR A CB 2112 C CG . TYR A 276 ? 0.1935 0.2165 0.1631 0.0370 0.0054 -0.0052 276 TYR A CG 2113 C CD1 . TYR A 276 ? 0.1809 0.1847 0.1749 0.0270 -0.0012 0.0035 276 TYR A CD1 2114 C CD2 . TYR A 276 ? 0.1817 0.2195 0.1845 0.0472 0.0093 -0.0044 276 TYR A CD2 2115 C CE1 . TYR A 276 ? 0.1661 0.1910 0.1552 0.0497 0.0112 0.0095 276 TYR A CE1 2116 C CE2 . TYR A 276 ? 0.1724 0.2163 0.1858 0.0454 0.0013 -0.0067 276 TYR A CE2 2117 C CZ . TYR A 276 ? 0.1682 0.1940 0.1656 0.0392 0.0007 -0.0021 276 TYR A CZ 2118 O OH . TYR A 276 ? 0.1930 0.1951 0.1411 0.0430 0.0086 -0.0030 276 TYR A OH 2119 N N . GLU A 277 ? 0.1855 0.2457 0.1982 0.0244 -0.0091 -0.0118 277 GLU A N 2120 C CA . GLU A 277 ? 0.2032 0.2621 0.2146 0.0270 -0.0039 -0.0096 277 GLU A CA 2121 C C . GLU A 277 ? 0.2105 0.2661 0.2189 0.0315 -0.0041 -0.0082 277 GLU A C 2122 O O . GLU A 277 ? 0.1908 0.2675 0.2147 0.0369 0.0084 -0.0069 277 GLU A O 2123 C CB . GLU A 277 ? 0.2077 0.2627 0.2166 0.0191 -0.0095 -0.0117 277 GLU A CB 2124 C CG . GLU A 277 ? 0.1875 0.2854 0.2142 0.0102 -0.0024 -0.0114 277 GLU A CG 2125 C CD . GLU A 277 ? 0.1820 0.3198 0.2417 0.0067 -0.0017 -0.0193 277 GLU A CD 2126 O OE1 . GLU A 277 ? 0.1831 0.3390 0.2547 0.0060 0.0077 -0.0134 277 GLU A OE1 2127 O OE2 . GLU A 277 ? 0.1201 0.3370 0.2477 0.0014 0.0085 -0.0075 277 GLU A OE2 2128 N N . ILE A 278 ? 0.2258 0.2781 0.2222 0.0349 -0.0007 -0.0065 278 ILE A N 2129 C CA . ILE A 278 ? 0.2472 0.2942 0.2365 0.0403 0.0021 0.0003 278 ILE A CA 2130 C C . ILE A 278 ? 0.2510 0.2865 0.2396 0.0390 0.0059 -0.0036 278 ILE A C 2131 O O . ILE A 278 ? 0.2545 0.2963 0.2458 0.0348 0.0053 -0.0027 278 ILE A O 2132 C CB . ILE A 278 ? 0.2418 0.2903 0.2389 0.0412 -0.0020 0.0002 278 ILE A CB 2133 C CG1 . ILE A 278 ? 0.2661 0.3080 0.2472 0.0457 0.0118 0.0187 278 ILE A CG1 2134 C CG2 . ILE A 278 ? 0.2537 0.3251 0.2276 0.0572 -0.0002 -0.0032 278 ILE A CG2 2135 C CD1 . ILE A 278 ? 0.2663 0.3070 0.2552 0.0459 0.0050 0.0126 278 ILE A CD1 2136 N N . HIS A 279 ? 0.2586 0.2820 0.2357 0.0359 0.0122 -0.0021 279 HIS A N 2137 C CA . HIS A 279 ? 0.2654 0.2758 0.2313 0.0376 0.0243 -0.0045 279 HIS A CA 2138 C C . HIS A 279 ? 0.2647 0.2690 0.2246 0.0334 0.0288 -0.0059 279 HIS A C 2139 O O . HIS A 279 ? 0.2663 0.2714 0.2174 0.0338 0.0275 -0.0093 279 HIS A O 2140 C CB . HIS A 279 ? 0.2613 0.2746 0.2385 0.0340 0.0274 0.0001 279 HIS A CB 2141 C CG . HIS A 279 ? 0.2887 0.3093 0.2539 0.0406 0.0313 0.0068 279 HIS A CG 2142 N ND1 . HIS A 279 ? 0.3293 0.3237 0.2928 0.0454 0.0359 0.0205 279 HIS A ND1 2143 C CD2 . HIS A 279 ? 0.3053 0.3339 0.2863 0.0356 0.0388 0.0024 279 HIS A CD2 2144 C CE1 . HIS A 279 ? 0.3402 0.3678 0.3147 0.0358 0.0325 0.0210 279 HIS A CE1 2145 N NE2 . HIS A 279 ? 0.3237 0.3522 0.2968 0.0443 0.0408 0.0108 279 HIS A NE2 2146 N N . ARG A 280 ? 0.2592 0.2546 0.2176 0.0310 0.0353 -0.0079 280 ARG A N 2147 C CA . ARG A 280 ? 0.2564 0.2540 0.2189 0.0278 0.0394 -0.0136 280 ARG A CA 2148 C C . ARG A 280 ? 0.2604 0.2558 0.2250 0.0248 0.0445 -0.0160 280 ARG A C 2149 O O . ARG A 280 ? 0.2564 0.2445 0.2216 0.0293 0.0496 -0.0187 280 ARG A O 2150 C CB . ARG A 280 ? 0.2514 0.2446 0.2216 0.0281 0.0335 -0.0114 280 ARG A CB 2151 C CG . ARG A 280 ? 0.2379 0.2446 0.1944 0.0126 0.0349 -0.0078 280 ARG A CG 2152 C CD . ARG A 280 ? 0.2388 0.2437 0.2140 0.0305 0.0276 -0.0083 280 ARG A CD 2153 N NE . ARG A 280 ? 0.2277 0.2316 0.2076 0.0322 -0.0039 -0.0132 280 ARG A NE 2154 C CZ . ARG A 280 ? 0.2214 0.2399 0.2024 0.0322 -0.0015 -0.0146 280 ARG A CZ 2155 N NH1 . ARG A 280 ? 0.2544 0.2448 0.2221 0.0147 0.0120 -0.0298 280 ARG A NH1 2156 N NH2 . ARG A 280 ? 0.2275 0.2518 0.2107 0.0303 0.0083 -0.0288 280 ARG A NH2 2157 N N . ASP A 281 ? 0.2692 0.2619 0.2258 0.0239 0.0560 -0.0248 281 ASP A N 2158 C CA . ASP A 281 ? 0.2874 0.2849 0.2391 0.0228 0.0567 -0.0284 281 ASP A CA 2159 C C . ASP A 281 ? 0.2829 0.2927 0.2419 0.0254 0.0561 -0.0307 281 ASP A C 2160 O O . ASP A 281 ? 0.2838 0.2900 0.2359 0.0288 0.0536 -0.0240 281 ASP A O 2161 C CB . ASP A 281 ? 0.2971 0.2900 0.2405 0.0238 0.0682 -0.0367 281 ASP A CB 2162 C CG . ASP A 281 ? 0.3481 0.3106 0.2481 0.0067 0.0821 -0.0427 281 ASP A CG 2163 O OD1 . ASP A 281 ? 0.3840 0.3555 0.2500 0.0015 0.1204 -0.0619 281 ASP A OD1 2164 O OD2 . ASP A 281 ? 0.4087 0.3375 0.2759 0.0069 0.0964 -0.0524 281 ASP A OD2 2165 N N . SER A 282 ? 0.2736 0.3047 0.2503 0.0267 0.0488 -0.0311 282 SER A N 2166 C CA . SER A 282 ? 0.2793 0.3240 0.2812 0.0241 0.0394 -0.0240 282 SER A CA 2167 C C . SER A 282 ? 0.2793 0.3237 0.2818 0.0228 0.0351 -0.0196 282 SER A C 2168 O O . SER A 282 ? 0.2854 0.3331 0.2940 0.0269 0.0316 -0.0177 282 SER A O 2169 C CB . SER A 282 ? 0.2738 0.3271 0.2846 0.0271 0.0357 -0.0302 282 SER A CB 2170 O OG . SER A 282 ? 0.2910 0.3618 0.3450 0.0163 0.0226 -0.0260 282 SER A OG 2171 N N . THR A 283 ? 0.2777 0.3312 0.2838 0.0227 0.0375 -0.0112 283 THR A N 2172 C CA . THR A 283 ? 0.2907 0.3328 0.2856 0.0218 0.0381 -0.0086 283 THR A CA 2173 C C . THR A 283 ? 0.2891 0.3198 0.2740 0.0163 0.0341 -0.0046 283 THR A C 2174 O O . THR A 283 ? 0.2985 0.3172 0.2807 0.0117 0.0345 0.0094 283 THR A O 2175 C CB . THR A 283 ? 0.2896 0.3278 0.2880 0.0180 0.0413 -0.0140 283 THR A CB 2176 O OG1 . THR A 283 ? 0.3501 0.3844 0.3217 0.0388 0.0523 -0.0254 283 THR A OG1 2177 C CG2 . THR A 283 ? 0.2732 0.3596 0.2902 0.0363 0.0430 -0.0164 283 THR A CG2 2178 N N . LEU A 284 ? 0.2774 0.2911 0.2466 0.0132 0.0370 -0.0080 284 LEU A N 2179 C CA . LEU A 284 ? 0.2782 0.2785 0.2346 0.0144 0.0418 -0.0148 284 LEU A CA 2180 C C . LEU A 284 ? 0.2605 0.2633 0.2226 0.0131 0.0416 -0.0125 284 LEU A C 2181 O O . LEU A 284 ? 0.2509 0.2565 0.2003 0.0170 0.0470 -0.0127 284 LEU A O 2182 C CB . LEU A 284 ? 0.2873 0.2852 0.2408 0.0160 0.0424 -0.0203 284 LEU A CB 2183 C CG . LEU A 284 ? 0.3434 0.3006 0.2596 0.0188 0.0239 -0.0197 284 LEU A CG 2184 C CD1 . LEU A 284 ? 0.3955 0.3430 0.3205 0.0140 0.0313 -0.0482 284 LEU A CD1 2185 C CD2 . LEU A 284 ? 0.3798 0.3719 0.2651 0.0080 0.0267 -0.0350 284 LEU A CD2 2186 N N . ASP A 285 ? 0.2450 0.2469 0.2142 0.0098 0.0343 -0.0180 285 ASP A N 2187 C CA . ASP A 285 ? 0.2385 0.2333 0.2115 0.0072 0.0309 -0.0182 285 ASP A CA 2188 C C . ASP A 285 ? 0.2196 0.2258 0.2044 0.0117 0.0295 -0.0107 285 ASP A C 2189 O O . ASP A 285 ? 0.2047 0.1990 0.1981 0.0216 0.0278 -0.0060 285 ASP A O 2190 C CB . ASP A 285 ? 0.2508 0.2439 0.2242 -0.0011 0.0256 -0.0285 285 ASP A CB 2191 C CG . ASP A 285 ? 0.2768 0.2673 0.2564 -0.0017 0.0279 -0.0423 285 ASP A CG 2192 O OD1 . ASP A 285 ? 0.2883 0.2762 0.3070 -0.0083 -0.0047 -0.0568 285 ASP A OD1 2193 O OD2 . ASP A 285 ? 0.3112 0.2581 0.2728 0.0051 0.0294 -0.1027 285 ASP A OD2 2194 N N . PRO A 286 ? 0.2046 0.2203 0.1973 0.0175 0.0259 -0.0038 286 PRO A N 2195 C CA . PRO A 286 ? 0.1982 0.2250 0.1927 0.0197 0.0239 -0.0065 286 PRO A CA 2196 C C . PRO A 286 ? 0.1968 0.2297 0.1888 0.0236 0.0201 -0.0031 286 PRO A C 2197 O O . PRO A 286 ? 0.1928 0.2301 0.1714 0.0163 0.0248 -0.0019 286 PRO A O 2198 C CB . PRO A 286 ? 0.1981 0.2283 0.1912 0.0242 0.0200 0.0017 286 PRO A CB 2199 C CG . PRO A 286 ? 0.1978 0.2117 0.2026 0.0161 0.0215 -0.0204 286 PRO A CG 2200 C CD . PRO A 286 ? 0.2017 0.2201 0.2033 0.0184 0.0223 -0.0001 286 PRO A CD 2201 N N . SER A 287 ? 0.1893 0.2293 0.1844 0.0255 0.0197 -0.0144 287 SER A N 2202 C CA . SER A 287 ? 0.1827 0.2384 0.1841 0.0241 0.0217 -0.0073 287 SER A CA 2203 C C . SER A 287 ? 0.1749 0.2318 0.1758 0.0204 0.0238 -0.0086 287 SER A C 2204 O O . SER A 287 ? 0.1703 0.2383 0.1809 0.0214 0.0300 -0.0122 287 SER A O 2205 C CB . SER A 287 ? 0.1840 0.2373 0.1854 0.0205 0.0159 -0.0134 287 SER A CB 2206 O OG . SER A 287 ? 0.1847 0.2438 0.1899 0.0289 0.0276 -0.0147 287 SER A OG 2207 N N . LEU A 288 ? 0.1685 0.2330 0.1652 0.0162 0.0253 -0.0101 288 LEU A N 2208 C CA . LEU A 288 ? 0.1674 0.2328 0.1579 0.0097 0.0247 0.0004 288 LEU A CA 2209 C C . LEU A 288 ? 0.1674 0.2403 0.1515 0.0039 0.0265 -0.0019 288 LEU A C 2210 O O . LEU A 288 ? 0.1601 0.2206 0.1252 0.0052 0.0278 0.0145 288 LEU A O 2211 C CB . LEU A 288 ? 0.1653 0.2288 0.1479 0.0064 0.0278 0.0019 288 LEU A CB 2212 C CG . LEU A 288 ? 0.1414 0.2247 0.1509 0.0048 0.0302 0.0003 288 LEU A CG 2213 C CD1 . LEU A 288 ? 0.1372 0.1817 0.1470 0.0195 0.0307 0.0004 288 LEU A CD1 2214 C CD2 . LEU A 288 ? 0.1570 0.2360 0.1598 0.0141 0.0184 0.0073 288 LEU A CD2 2215 N N . MET A 289 ? 0.1634 0.2478 0.1486 0.0031 0.0253 -0.0032 289 MET A N 2216 C CA . MET A 289 ? 0.1835 0.2850 0.1858 0.0012 0.0173 -0.0140 289 MET A CA 2217 C C . MET A 289 ? 0.1646 0.2565 0.1640 -0.0020 0.0179 -0.0129 289 MET A C 2218 O O . MET A 289 ? 0.1666 0.2679 0.1484 0.0016 0.0203 -0.0193 289 MET A O 2219 C CB . MET A 289 ? 0.1833 0.2690 0.1768 -0.0108 0.0105 -0.0097 289 MET A CB 2220 C CG . MET A 289 ? 0.2394 0.3334 0.2320 -0.0047 0.0016 -0.0107 289 MET A CG 2221 S SD . MET A 289 ? 0.2146 0.3966 0.2869 0.0140 0.0135 -0.0300 289 MET A SD 2222 C CE . MET A 289 ? 0.3005 0.4009 0.3339 0.0036 -0.0094 -0.0404 289 MET A CE 2223 N N . GLU A 290 ? 0.1630 0.2490 0.1641 -0.0038 0.0123 -0.0158 290 GLU A N 2224 C CA . GLU A 290 ? 0.1615 0.2318 0.1586 -0.0026 0.0162 -0.0094 290 GLU A CA 2225 C C . GLU A 290 ? 0.1556 0.2181 0.1542 -0.0044 0.0176 -0.0099 290 GLU A C 2226 O O . GLU A 290 ? 0.1597 0.2092 0.1480 -0.0125 0.0212 -0.0123 290 GLU A O 2227 C CB . GLU A 290 ? 0.1556 0.2372 0.1649 0.0035 0.0163 -0.0089 290 GLU A CB 2228 C CG . GLU A 290 ? 0.1818 0.2720 0.2043 0.0129 0.0149 -0.0134 290 GLU A CG 2229 C CD . GLU A 290 ? 0.1948 0.3041 0.2516 0.0122 0.0187 -0.0292 290 GLU A CD 2230 O OE1 . GLU A 290 ? 0.1847 0.2831 0.2898 0.0008 0.0158 -0.0455 290 GLU A OE1 2231 O OE2 . GLU A 290 ? 0.2158 0.3316 0.3025 0.0030 0.0222 -0.0264 290 GLU A OE2 2232 N N . MET A 291 ? 0.1657 0.2149 0.1577 -0.0082 0.0105 -0.0058 291 MET A N 2233 C CA . MET A 291 ? 0.1696 0.2092 0.1563 -0.0090 0.0096 -0.0026 291 MET A CA 2234 C C . MET A 291 ? 0.1771 0.2279 0.1625 -0.0161 0.0108 0.0053 291 MET A C 2235 O O . MET A 291 ? 0.1688 0.2183 0.1322 -0.0143 0.0065 0.0234 291 MET A O 2236 C CB . MET A 291 ? 0.1570 0.2061 0.1556 -0.0103 0.0062 0.0027 291 MET A CB 2237 C CG . MET A 291 ? 0.1663 0.1999 0.1540 -0.0168 0.0139 -0.0097 291 MET A CG 2238 S SD . MET A 291 ? 0.2068 0.2001 0.1855 0.0020 0.0015 0.0073 291 MET A SD 2239 C CE . MET A 291 ? 0.2289 0.2395 0.1534 -0.0130 0.0125 0.0118 291 MET A CE 2240 N N . THR A 292 ? 0.1752 0.2166 0.1241 -0.0197 0.0143 0.0084 292 THR A N 2241 C CA . THR A 292 ? 0.1721 0.2063 0.1397 -0.0245 0.0182 0.0140 292 THR A CA 2242 C C . THR A 292 ? 0.1705 0.2045 0.1462 -0.0211 0.0188 0.0147 292 THR A C 2243 O O . THR A 292 ? 0.1633 0.1872 0.1390 -0.0302 0.0209 0.0203 292 THR A O 2244 C CB . THR A 292 ? 0.1652 0.2019 0.1255 -0.0242 0.0217 0.0104 292 THR A CB 2245 O OG1 . THR A 292 ? 0.1786 0.2059 0.1143 -0.0193 0.0185 0.0038 292 THR A OG1 2246 C CG2 . THR A 292 ? 0.1690 0.1952 0.1388 -0.0262 0.0166 0.0204 292 THR A CG2 2247 N N . GLU A 293 ? 0.1739 0.2054 0.1608 -0.0254 0.0191 0.0171 293 GLU A N 2248 C CA . GLU A 293 ? 0.1760 0.2049 0.1749 -0.0204 0.0227 0.0152 293 GLU A CA 2249 C C . GLU A 293 ? 0.1759 0.2038 0.1768 -0.0163 0.0218 0.0144 293 GLU A C 2250 O O . GLU A 293 ? 0.1735 0.2028 0.1795 -0.0128 0.0226 0.0156 293 GLU A O 2251 C CB . GLU A 293 ? 0.1855 0.2149 0.1837 -0.0259 0.0222 0.0153 293 GLU A CB 2252 C CG . GLU A 293 ? 0.1845 0.1988 0.2048 -0.0467 0.0290 0.0172 293 GLU A CG 2253 C CD . GLU A 293 ? 0.1740 0.1977 0.2126 -0.0614 0.0104 -0.0025 293 GLU A CD 2254 O OE1 . GLU A 293 ? 0.2064 0.2054 0.2577 -0.0729 0.0376 0.0234 293 GLU A OE1 2255 O OE2 . GLU A 293 ? 0.1542 0.1708 0.2325 -0.0440 0.0028 -0.0278 293 GLU A OE2 2256 N N . ALA A 294 ? 0.1726 0.2028 0.1753 -0.0132 0.0245 0.0184 294 ALA A N 2257 C CA . ALA A 294 ? 0.1729 0.1983 0.1802 -0.0128 0.0233 0.0138 294 ALA A CA 2258 C C . ALA A 294 ? 0.1790 0.1929 0.1739 -0.0108 0.0260 0.0168 294 ALA A C 2259 O O . ALA A 294 ? 0.1768 0.1890 0.1761 -0.0169 0.0290 0.0143 294 ALA A O 2260 C CB . ALA A 294 ? 0.1736 0.2085 0.1882 -0.0070 0.0243 0.0131 294 ALA A CB 2261 N N . ALA A 295 ? 0.1755 0.1875 0.1740 -0.0148 0.0245 0.0189 295 ALA A N 2262 C CA . ALA A 295 ? 0.1793 0.1774 0.1626 -0.0084 0.0271 0.0232 295 ALA A CA 2263 C C . ALA A 295 ? 0.1832 0.1759 0.1604 -0.0094 0.0282 0.0258 295 ALA A C 2264 O O . ALA A 295 ? 0.1902 0.1718 0.1723 -0.0133 0.0282 0.0228 295 ALA A O 2265 C CB . ALA A 295 ? 0.1665 0.1857 0.1560 -0.0083 0.0233 0.0279 295 ALA A CB 2266 N N . LEU A 296 ? 0.1898 0.1695 0.1540 -0.0084 0.0296 0.0298 296 LEU A N 2267 C CA . LEU A 296 ? 0.2026 0.1747 0.1620 -0.0006 0.0178 0.0249 296 LEU A CA 2268 C C . LEU A 296 ? 0.2079 0.1849 0.1635 0.0015 0.0193 0.0230 296 LEU A C 2269 O O . LEU A 296 ? 0.2132 0.1775 0.1631 -0.0062 0.0139 0.0181 296 LEU A O 2270 C CB . LEU A 296 ? 0.2063 0.1656 0.1594 0.0027 0.0130 0.0276 296 LEU A CB 2271 C CG . LEU A 296 ? 0.1787 0.1478 0.1495 0.0098 0.0137 0.0156 296 LEU A CG 2272 C CD1 . LEU A 296 ? 0.2020 0.1624 0.1688 0.0354 -0.0106 0.0173 296 LEU A CD1 2273 C CD2 . LEU A 296 ? 0.1689 0.1337 0.1860 0.0367 -0.0015 0.0356 296 LEU A CD2 2274 N N . ARG A 297 ? 0.2030 0.2000 0.1751 0.0047 0.0167 0.0229 297 ARG A N 2275 C CA . ARG A 297 ? 0.2082 0.2055 0.1838 0.0108 0.0200 0.0170 297 ARG A CA 2276 C C . ARG A 297 ? 0.2202 0.2167 0.1937 0.0058 0.0220 0.0154 297 ARG A C 2277 O O . ARG A 297 ? 0.2276 0.2067 0.1984 0.0066 0.0179 0.0261 297 ARG A O 2278 C CB . ARG A 297 ? 0.2078 0.2102 0.1884 0.0104 0.0234 0.0168 297 ARG A CB 2279 C CG . ARG A 297 ? 0.1916 0.2069 0.1812 0.0291 0.0152 0.0078 297 ARG A CG 2280 C CD . ARG A 297 ? 0.1963 0.2408 0.2035 0.0284 0.0259 0.0226 297 ARG A CD 2281 N NE . ARG A 297 ? 0.1892 0.2254 0.2014 0.0312 0.0124 0.0277 297 ARG A NE 2282 C CZ . ARG A 297 ? 0.2024 0.2241 0.1823 0.0424 0.0220 0.0067 297 ARG A CZ 2283 N NH1 . ARG A 297 ? 0.1943 0.2256 0.2043 0.0323 0.0138 -0.0142 297 ARG A NH1 2284 N NH2 . ARG A 297 ? 0.1992 0.2352 0.2146 0.0200 0.0072 0.0062 297 ARG A NH2 2285 N N . LEU A 298 ? 0.2182 0.2241 0.1957 0.0030 0.0253 0.0114 298 LEU A N 2286 C CA . LEU A 298 ? 0.2333 0.2399 0.2046 -0.0011 0.0231 0.0139 298 LEU A CA 2287 C C . LEU A 298 ? 0.2267 0.2269 0.2027 0.0018 0.0230 0.0197 298 LEU A C 2288 O O . LEU A 298 ? 0.2306 0.2275 0.1999 0.0020 0.0269 0.0267 298 LEU A O 2289 C CB . LEU A 298 ? 0.2424 0.2438 0.2088 -0.0050 0.0234 0.0034 298 LEU A CB 2290 C CG . LEU A 298 ? 0.2976 0.3165 0.2732 -0.0304 0.0142 0.0189 298 LEU A CG 2291 C CD1 . LEU A 298 ? 0.3119 0.3365 0.2721 -0.0789 -0.0169 0.0078 298 LEU A CD1 2292 C CD2 . LEU A 298 ? 0.3048 0.3026 0.3466 -0.0510 -0.0205 0.0324 298 LEU A CD2 2293 N N . LEU A 299 ? 0.2131 0.2132 0.1857 0.0024 0.0217 0.0263 299 LEU A N 2294 C CA . LEU A 299 ? 0.2183 0.2105 0.1937 0.0004 0.0157 0.0317 299 LEU A CA 2295 C C . LEU A 299 ? 0.2227 0.2112 0.1956 0.0034 0.0161 0.0359 299 LEU A C 2296 O O . LEU A 299 ? 0.2234 0.2134 0.1927 0.0080 0.0148 0.0420 299 LEU A O 2297 C CB . LEU A 299 ? 0.2044 0.2017 0.1747 -0.0006 0.0183 0.0361 299 LEU A CB 2298 C CG . LEU A 299 ? 0.2135 0.1916 0.1844 0.0017 -0.0002 0.0319 299 LEU A CG 2299 C CD1 . LEU A 299 ? 0.2375 0.1684 0.1618 -0.0101 0.0140 0.0342 299 LEU A CD1 2300 C CD2 . LEU A 299 ? 0.2255 0.1902 0.1959 -0.0136 -0.0400 0.0291 299 LEU A CD2 2301 N N . SER A 300 ? 0.2287 0.2146 0.2078 0.0022 0.0161 0.0409 300 SER A N 2302 C CA . SER A 300 ? 0.2401 0.2247 0.2321 0.0030 0.0119 0.0383 300 SER A CA 2303 C C . SER A 300 ? 0.2419 0.2237 0.2315 0.0053 0.0180 0.0379 300 SER A C 2304 O O . SER A 300 ? 0.2497 0.2100 0.2278 -0.0046 0.0180 0.0387 300 SER A O 2305 C CB . SER A 300 ? 0.2335 0.2331 0.2381 0.0017 0.0140 0.0273 300 SER A CB 2306 O OG . SER A 300 ? 0.2677 0.2472 0.2981 -0.0039 0.0009 0.0514 300 SER A OG 2307 N N . ARG A 301 ? 0.2438 0.2249 0.2327 0.0121 0.0176 0.0383 301 ARG A N 2308 C CA . ARG A 301 ? 0.2577 0.2289 0.2418 0.0198 0.0165 0.0399 301 ARG A CA 2309 C C . ARG A 301 ? 0.2595 0.2359 0.2552 0.0127 0.0152 0.0436 301 ARG A C 2310 O O . ARG A 301 ? 0.2608 0.2391 0.2580 0.0138 0.0234 0.0537 301 ARG A O 2311 C CB . ARG A 301 ? 0.2692 0.2350 0.2486 0.0220 0.0140 0.0437 301 ARG A CB 2312 C CG . ARG A 301 ? 0.2939 0.2622 0.2542 0.0396 0.0188 0.0361 301 ARG A CG 2313 C CD . ARG A 301 ? 0.3843 0.3008 0.2891 0.0452 0.0020 0.0373 301 ARG A CD 2314 N NE . ARG A 301 ? 0.4189 0.3821 0.3078 0.0325 -0.0028 0.0328 301 ARG A NE 2315 C CZ . ARG A 301 ? 0.4553 0.3896 0.4001 0.0268 -0.0134 0.0279 301 ARG A CZ 2316 N NH1 . ARG A 301 ? 0.4838 0.3826 0.3891 0.0145 -0.0442 0.0485 301 ARG A NH1 2317 N NH2 . ARG A 301 ? 0.4667 0.3934 0.4388 0.0352 -0.0218 0.0310 301 ARG A NH2 2318 N N . ASN A 302 ? 0.2486 0.2327 0.2535 0.0072 0.0124 0.0413 302 ASN A N 2319 C CA . ASN A 302 ? 0.2488 0.2328 0.2581 0.0096 0.0077 0.0362 302 ASN A CA 2320 C C . ASN A 302 ? 0.2545 0.2373 0.2645 0.0064 0.0032 0.0395 302 ASN A C 2321 O O . ASN A 302 ? 0.2514 0.2418 0.2601 0.0057 0.0036 0.0371 302 ASN A O 2322 C CB . ASN A 302 ? 0.2334 0.2320 0.2624 0.0088 0.0098 0.0339 302 ASN A CB 2323 C CG . ASN A 302 ? 0.2317 0.2394 0.2729 0.0155 0.0013 0.0368 302 ASN A CG 2324 O OD1 . ASN A 302 ? 0.2210 0.2784 0.2658 0.0162 0.0023 0.0381 302 ASN A OD1 2325 N ND2 . ASN A 302 ? 0.1728 0.2507 0.2807 0.0123 0.0045 0.0317 302 ASN A ND2 2326 N N . PRO A 303 ? 0.2631 0.2448 0.2666 0.0077 -0.0010 0.0425 303 PRO A N 2327 C CA . PRO A 303 ? 0.2707 0.2375 0.2657 0.0074 -0.0033 0.0472 303 PRO A CA 2328 C C . PRO A 303 ? 0.2735 0.2344 0.2568 0.0056 -0.0050 0.0566 303 PRO A C 2329 O O . PRO A 303 ? 0.2798 0.2224 0.2578 0.0012 -0.0029 0.0641 303 PRO A O 2330 C CB . PRO A 303 ? 0.2755 0.2500 0.2636 0.0068 -0.0093 0.0501 303 PRO A CB 2331 C CG . PRO A 303 ? 0.2831 0.2543 0.2773 0.0076 -0.0065 0.0355 303 PRO A CG 2332 C CD . PRO A 303 ? 0.2721 0.2402 0.2729 0.0113 -0.0036 0.0432 303 PRO A CD 2333 N N . ARG A 304 ? 0.2735 0.2321 0.2542 0.0111 -0.0062 0.0609 304 ARG A N 2334 C CA . ARG A 304 ? 0.2730 0.2338 0.2601 0.0120 -0.0091 0.0597 304 ARG A CA 2335 C C . ARG A 304 ? 0.2672 0.2223 0.2504 0.0041 -0.0005 0.0534 304 ARG A C 2336 O O . ARG A 304 ? 0.2716 0.2297 0.2599 0.0070 -0.0042 0.0523 304 ARG A O 2337 C CB . ARG A 304 ? 0.2794 0.2389 0.2669 0.0107 -0.0083 0.0610 304 ARG A CB 2338 C CG . ARG A 304 ? 0.3259 0.2828 0.3160 0.0327 -0.0320 0.0654 304 ARG A CG 2339 C CD . ARG A 304 ? 0.4142 0.3271 0.3942 0.0445 -0.0691 0.0790 304 ARG A CD 2340 N NE . ARG A 304 ? 0.5294 0.4028 0.4847 0.0590 -0.0623 0.0505 304 ARG A NE 2341 C CZ . ARG A 304 ? 0.5725 0.4614 0.5114 0.0642 -0.0694 0.0467 304 ARG A CZ 2342 N NH1 . ARG A 304 ? 0.5980 0.4988 0.5354 0.0632 -0.0662 0.0266 304 ARG A NH1 2343 N NH2 . ARG A 304 ? 0.5937 0.4639 0.5388 0.0704 -0.0686 0.0591 304 ARG A NH2 2344 N N . GLY A 305 ? 0.2461 0.2002 0.2392 0.0054 -0.0004 0.0485 305 GLY A N 2345 C CA . GLY A 305 ? 0.2434 0.1871 0.2134 -0.0053 0.0089 0.0377 305 GLY A CA 2346 C C . GLY A 305 ? 0.2349 0.1886 0.2117 -0.0024 0.0107 0.0346 305 GLY A C 2347 O O . GLY A 305 ? 0.2378 0.1759 0.1963 -0.0033 0.0137 0.0299 305 GLY A O 2348 N N . PHE A 306 ? 0.2231 0.1812 0.2026 -0.0075 0.0153 0.0306 306 PHE A N 2349 C CA . PHE A 306 ? 0.2113 0.1825 0.1962 -0.0100 0.0182 0.0241 306 PHE A CA 2350 C C . PHE A 306 ? 0.2046 0.1820 0.1877 -0.0128 0.0186 0.0230 306 PHE A C 2351 O O . PHE A 306 ? 0.2017 0.1762 0.1814 -0.0233 0.0195 0.0204 306 PHE A O 2352 C CB . PHE A 306 ? 0.2135 0.1901 0.1925 -0.0059 0.0188 0.0164 306 PHE A CB 2353 C CG . PHE A 306 ? 0.2157 0.1843 0.1912 -0.0009 0.0182 0.0073 306 PHE A CG 2354 C CD1 . PHE A 306 ? 0.2196 0.1852 0.1882 0.0032 0.0078 -0.0039 306 PHE A CD1 2355 C CD2 . PHE A 306 ? 0.2223 0.2070 0.1898 0.0023 0.0243 -0.0040 306 PHE A CD2 2356 C CE1 . PHE A 306 ? 0.1912 0.1910 0.1926 -0.0012 0.0184 0.0081 306 PHE A CE1 2357 C CE2 . PHE A 306 ? 0.2207 0.1679 0.2049 0.0139 0.0199 -0.0061 306 PHE A CE2 2358 C CZ . PHE A 306 ? 0.2224 0.2065 0.1991 0.0155 0.0184 -0.0039 306 PHE A CZ 2359 N N . PHE A 307 ? 0.1896 0.1608 0.1835 -0.0143 0.0209 0.0244 307 PHE A N 2360 C CA . PHE A 307 ? 0.1914 0.1670 0.1832 -0.0041 0.0175 0.0232 307 PHE A CA 2361 C C . PHE A 307 ? 0.1846 0.1586 0.1865 0.0040 0.0163 0.0245 307 PHE A C 2362 O O . PHE A 307 ? 0.1875 0.1543 0.1628 0.0078 0.0116 0.0131 307 PHE A O 2363 C CB . PHE A 307 ? 0.1741 0.1587 0.1819 -0.0120 0.0243 0.0291 307 PHE A CB 2364 C CG . PHE A 307 ? 0.1864 0.1862 0.2036 -0.0194 0.0136 0.0375 307 PHE A CG 2365 C CD1 . PHE A 307 ? 0.1705 0.1666 0.2009 -0.0399 0.0225 0.0478 307 PHE A CD1 2366 C CD2 . PHE A 307 ? 0.1702 0.1932 0.1750 -0.0380 0.0323 0.0460 307 PHE A CD2 2367 C CE1 . PHE A 307 ? 0.1916 0.1877 0.2171 -0.0382 0.0351 0.0422 307 PHE A CE1 2368 C CE2 . PHE A 307 ? 0.1947 0.1912 0.2176 -0.0356 0.0095 0.0356 307 PHE A CE2 2369 C CZ . PHE A 307 ? 0.1910 0.1800 0.2066 -0.0339 0.0158 0.0444 307 PHE A CZ 2370 N N . LEU A 308 ? 0.1816 0.1618 0.1892 0.0068 0.0154 0.0259 308 LEU A N 2371 C CA . LEU A 308 ? 0.1711 0.1490 0.1870 0.0074 0.0179 0.0262 308 LEU A CA 2372 C C . LEU A 308 ? 0.1690 0.1475 0.1793 0.0041 0.0147 0.0286 308 LEU A C 2373 O O . LEU A 308 ? 0.1755 0.1455 0.1697 -0.0011 0.0174 0.0263 308 LEU A O 2374 C CB . LEU A 308 ? 0.1639 0.1535 0.1955 0.0091 0.0164 0.0224 308 LEU A CB 2375 C CG . LEU A 308 ? 0.1643 0.1522 0.2028 0.0181 0.0133 0.0216 308 LEU A CG 2376 C CD1 . LEU A 308 ? 0.1638 0.1354 0.2000 0.0090 0.0011 -0.0046 308 LEU A CD1 2377 C CD2 . LEU A 308 ? 0.1256 0.1523 0.2309 -0.0076 0.0094 0.0241 308 LEU A CD2 2378 N N . PHE A 309 ? 0.1638 0.1422 0.1707 0.0045 0.0159 0.0300 309 PHE A N 2379 C CA . PHE A 309 ? 0.1599 0.1491 0.1837 0.0038 0.0125 0.0197 309 PHE A CA 2380 C C . PHE A 309 ? 0.1542 0.1556 0.1787 0.0038 0.0121 0.0218 309 PHE A C 2381 O O . PHE A 309 ? 0.1487 0.1520 0.1560 0.0033 0.0090 0.0090 309 PHE A O 2382 C CB . PHE A 309 ? 0.1600 0.1519 0.1918 -0.0052 0.0087 0.0188 309 PHE A CB 2383 C CG . PHE A 309 ? 0.1580 0.1626 0.1845 -0.0111 0.0027 0.0215 309 PHE A CG 2384 C CD1 . PHE A 309 ? 0.1580 0.1516 0.1853 -0.0193 -0.0193 0.0093 309 PHE A CD1 2385 C CD2 . PHE A 309 ? 0.1647 0.1837 0.2156 -0.0157 0.0013 0.0124 309 PHE A CD2 2386 C CE1 . PHE A 309 ? 0.1314 0.1725 0.1552 -0.0169 -0.0320 0.0053 309 PHE A CE1 2387 C CE2 . PHE A 309 ? 0.1528 0.1618 0.2093 -0.0144 0.0072 0.0089 309 PHE A CE2 2388 C CZ . PHE A 309 ? 0.1432 0.1708 0.2029 -0.0196 -0.0005 0.0001 309 PHE A CZ 2389 N N . VAL A 310 ? 0.1421 0.1566 0.1639 0.0083 0.0066 0.0204 310 VAL A N 2390 C CA . VAL A 310 ? 0.1496 0.1492 0.1634 0.0078 0.0066 0.0270 310 VAL A CA 2391 C C . VAL A 310 ? 0.1458 0.1502 0.1618 0.0000 0.0081 0.0186 310 VAL A C 2392 O O . VAL A 310 ? 0.1536 0.1445 0.1555 0.0064 0.0038 0.0072 310 VAL A O 2393 C CB . VAL A 310 ? 0.1352 0.1395 0.1565 0.0071 0.0119 0.0277 310 VAL A CB 2394 C CG1 . VAL A 310 ? 0.1428 0.1436 0.1461 0.0092 0.0215 0.0487 310 VAL A CG1 2395 C CG2 . VAL A 310 ? 0.1326 0.1447 0.1509 0.0206 -0.0053 0.0532 310 VAL A CG2 2396 N N . GLU A 311 ? 0.1448 0.1438 0.1572 -0.0075 0.0055 0.0104 311 GLU A N 2397 C CA . GLU A 311 ? 0.1470 0.1518 0.1564 -0.0088 0.0021 0.0083 311 GLU A CA 2398 C C . GLU A 311 ? 0.1567 0.1584 0.1588 -0.0094 -0.0007 0.0045 311 GLU A C 2399 O O . GLU A 311 ? 0.1523 0.1605 0.1636 -0.0198 0.0061 0.0065 311 GLU A O 2400 C CB . GLU A 311 ? 0.1416 0.1526 0.1532 -0.0147 0.0067 0.0096 311 GLU A CB 2401 C CG . GLU A 311 ? 0.1447 0.1450 0.1546 -0.0202 -0.0127 0.0145 311 GLU A CG 2402 C CD . GLU A 311 ? 0.1330 0.1572 0.1606 -0.0079 -0.0022 0.0212 311 GLU A CD 2403 O OE1 . GLU A 311 ? 0.1395 0.1706 0.1384 0.0007 -0.0131 0.0391 311 GLU A OE1 2404 O OE2 . GLU A 311 ? 0.1152 0.1390 0.1384 0.0074 0.0072 0.0201 311 GLU A OE2 2405 N N . GLY A 312 ? 0.1594 0.1639 0.1522 -0.0065 -0.0093 -0.0009 312 GLY A N 2406 C CA . GLY A 312 ? 0.1633 0.1560 0.1433 0.0046 -0.0107 -0.0141 312 GLY A CA 2407 C C . GLY A 312 ? 0.1724 0.1615 0.1407 0.0049 -0.0144 -0.0181 312 GLY A C 2408 O O . GLY A 312 ? 0.1693 0.1754 0.1415 0.0009 -0.0204 -0.0248 312 GLY A O 2409 N N . GLY A 313 ? 0.1655 0.1545 0.1394 0.0071 -0.0150 -0.0246 313 GLY A N 2410 C CA . GLY A 313 ? 0.1688 0.1413 0.1357 0.0116 -0.0100 -0.0254 313 GLY A CA 2411 C C . GLY A 313 ? 0.1618 0.1411 0.1330 0.0132 -0.0046 -0.0197 313 GLY A C 2412 O O . GLY A 313 ? 0.1697 0.1356 0.1548 0.0147 -0.0053 -0.0203 313 GLY A O 2413 N N . ARG A 314 ? 0.1581 0.1332 0.1191 0.0165 0.0051 -0.0253 314 ARG A N 2414 C CA . ARG A 314 ? 0.1477 0.1290 0.1176 0.0122 0.0085 -0.0244 314 ARG A CA 2415 C C . ARG A 314 ? 0.1385 0.1279 0.1276 0.0106 0.0140 -0.0187 314 ARG A C 2416 O O . ARG A 314 ? 0.1344 0.1474 0.1358 0.0119 0.0121 -0.0127 314 ARG A O 2417 C CB . ARG A 314 ? 0.1563 0.1247 0.1182 0.0173 0.0172 -0.0227 314 ARG A CB 2418 C CG . ARG A 314 ? 0.1701 0.1356 0.1240 0.0202 0.0087 -0.0335 314 ARG A CG 2419 C CD . ARG A 314 ? 0.1757 0.1263 0.1447 0.0413 0.0285 -0.0169 314 ARG A CD 2420 N NE . ARG A 314 ? 0.1844 0.1277 0.1643 0.0534 0.0168 0.0036 314 ARG A NE 2421 C CZ . ARG A 314 ? 0.1853 0.1461 0.1745 0.0336 0.0145 0.0112 314 ARG A CZ 2422 N NH1 . ARG A 314 ? 0.1835 0.1611 0.1683 0.0584 0.0398 0.0368 314 ARG A NH1 2423 N NH2 . ARG A 314 ? 0.1856 0.1587 0.1897 0.0227 0.0222 0.0200 314 ARG A NH2 2424 N N . ILE A 315 ? 0.1229 0.1240 0.1200 -0.0037 0.0065 -0.0225 315 ILE A N 2425 C CA . ILE A 315 ? 0.1352 0.1152 0.1348 -0.0050 0.0014 -0.0294 315 ILE A CA 2426 C C . ILE A 315 ? 0.1459 0.1189 0.1404 -0.0031 -0.0003 -0.0269 315 ILE A C 2427 O O . ILE A 315 ? 0.1556 0.1126 0.1498 -0.0040 0.0015 -0.0264 315 ILE A O 2428 C CB . ILE A 315 ? 0.1247 0.1091 0.1184 -0.0028 -0.0034 -0.0259 315 ILE A CB 2429 C CG1 . ILE A 315 ? 0.1425 0.0980 0.1386 -0.0090 -0.0123 -0.0300 315 ILE A CG1 2430 C CG2 . ILE A 315 ? 0.1193 0.1174 0.1310 -0.0215 -0.0020 -0.0283 315 ILE A CG2 2431 C CD1 . ILE A 315 ? 0.1515 0.1010 0.1333 0.0081 0.0000 -0.0462 315 ILE A CD1 2432 N N . ASP A 316 ? 0.1448 0.1225 0.1480 -0.0040 -0.0034 -0.0308 316 ASP A N 2433 C CA . ASP A 316 ? 0.1469 0.1208 0.1516 -0.0037 -0.0054 -0.0271 316 ASP A CA 2434 C C . ASP A 316 ? 0.1439 0.1217 0.1439 0.0028 -0.0031 -0.0286 316 ASP A C 2435 O O . ASP A 316 ? 0.1563 0.1133 0.1447 0.0010 -0.0034 -0.0395 316 ASP A O 2436 C CB . ASP A 316 ? 0.1437 0.1139 0.1566 -0.0023 -0.0082 -0.0234 316 ASP A CB 2437 C CG . ASP A 316 ? 0.1630 0.1318 0.1732 0.0028 -0.0251 -0.0166 316 ASP A CG 2438 O OD1 . ASP A 316 ? 0.1815 0.0827 0.2042 -0.0161 -0.0418 -0.0114 316 ASP A OD1 2439 O OD2 . ASP A 316 ? 0.1493 0.1343 0.1492 -0.0140 -0.0269 -0.0145 316 ASP A OD2 2440 N N . HIS A 317 ? 0.1436 0.1319 0.1367 0.0053 -0.0039 -0.0249 317 HIS A N 2441 C CA . HIS A 317 ? 0.1507 0.1398 0.1398 0.0152 0.0000 -0.0206 317 HIS A CA 2442 C C . HIS A 317 ? 0.1617 0.1468 0.1425 0.0125 0.0023 -0.0247 317 HIS A C 2443 O O . HIS A 317 ? 0.1681 0.1530 0.1610 0.0087 -0.0023 -0.0269 317 HIS A O 2444 C CB . HIS A 317 ? 0.1609 0.1427 0.1455 0.0182 -0.0062 -0.0224 317 HIS A CB 2445 C CG . HIS A 317 ? 0.1737 0.1746 0.1727 0.0300 -0.0010 -0.0034 317 HIS A CG 2446 N ND1 . HIS A 317 ? 0.2068 0.1999 0.1927 0.0413 0.0019 -0.0031 317 HIS A ND1 2447 C CD2 . HIS A 317 ? 0.1813 0.1986 0.2106 0.0197 0.0184 0.0150 317 HIS A CD2 2448 C CE1 . HIS A 317 ? 0.2059 0.2042 0.2005 0.0272 0.0107 0.0019 317 HIS A CE1 2449 N NE2 . HIS A 317 ? 0.2060 0.1996 0.1989 0.0325 0.0054 0.0318 317 HIS A NE2 2450 N N . GLY A 318 ? 0.1539 0.1457 0.1311 0.0169 0.0087 -0.0274 318 GLY A N 2451 C CA . GLY A 318 ? 0.1654 0.1557 0.1266 0.0146 0.0056 -0.0260 318 GLY A CA 2452 C C . GLY A 318 ? 0.1649 0.1482 0.1380 0.0109 0.0039 -0.0230 318 GLY A C 2453 O O . GLY A 318 ? 0.1721 0.1557 0.1420 0.0093 -0.0001 -0.0362 318 GLY A O 2454 N N . HIS A 319 ? 0.1578 0.1458 0.1297 0.0090 0.0040 -0.0200 319 HIS A N 2455 C CA . HIS A 319 ? 0.1529 0.1502 0.1379 0.0074 -0.0015 -0.0181 319 HIS A CA 2456 C C . HIS A 319 ? 0.1587 0.1437 0.1355 0.0096 0.0006 -0.0202 319 HIS A C 2457 O O . HIS A 319 ? 0.1740 0.1499 0.1398 0.0133 -0.0108 -0.0129 319 HIS A O 2458 C CB . HIS A 319 ? 0.1582 0.1392 0.1279 -0.0001 -0.0035 -0.0208 319 HIS A CB 2459 C CG . HIS A 319 ? 0.1447 0.1493 0.1422 -0.0136 -0.0039 -0.0022 319 HIS A CG 2460 N ND1 . HIS A 319 ? 0.1405 0.1393 0.1439 -0.0364 0.0236 0.0192 319 HIS A ND1 2461 C CD2 . HIS A 319 ? 0.1314 0.1246 0.1450 -0.0289 0.0063 0.0086 319 HIS A CD2 2462 C CE1 . HIS A 319 ? 0.1539 0.1403 0.1341 -0.0239 0.0221 0.0139 319 HIS A CE1 2463 N NE2 . HIS A 319 ? 0.1603 0.1306 0.1675 -0.0274 0.0299 0.0014 319 HIS A NE2 2464 N N . HIS A 320 ? 0.1468 0.1424 0.1261 0.0099 0.0016 -0.0230 320 HIS A N 2465 C CA . HIS A 320 ? 0.1609 0.1429 0.1459 0.0084 -0.0063 -0.0134 320 HIS A CA 2466 C C . HIS A 320 ? 0.1593 0.1368 0.1474 0.0123 -0.0078 -0.0057 320 HIS A C 2467 O O . HIS A 320 ? 0.1593 0.1308 0.1551 0.0056 -0.0064 0.0002 320 HIS A O 2468 C CB . HIS A 320 ? 0.1479 0.1374 0.1462 0.0062 -0.0119 -0.0053 320 HIS A CB 2469 C CG . HIS A 320 ? 0.1564 0.1471 0.1510 0.0067 -0.0022 -0.0163 320 HIS A CG 2470 N ND1 . HIS A 320 ? 0.1600 0.1578 0.1650 0.0090 -0.0015 -0.0072 320 HIS A ND1 2471 C CD2 . HIS A 320 ? 0.1685 0.1475 0.1446 0.0033 -0.0063 -0.0127 320 HIS A CD2 2472 C CE1 . HIS A 320 ? 0.2085 0.1382 0.1562 0.0197 0.0037 -0.0157 320 HIS A CE1 2473 N NE2 . HIS A 320 ? 0.1743 0.1562 0.1528 0.0172 0.0071 -0.0084 320 HIS A NE2 2474 N N . GLU A 321 ? 0.1648 0.1417 0.1447 0.0137 -0.0062 -0.0017 321 GLU A N 2475 C CA . GLU A 321 ? 0.1736 0.1460 0.1488 0.0139 -0.0023 0.0045 321 GLU A CA 2476 C C . GLU A 321 ? 0.1703 0.1429 0.1538 0.0078 -0.0015 0.0061 321 GLU A C 2477 O O . GLU A 321 ? 0.1872 0.1533 0.1649 -0.0010 -0.0055 0.0107 321 GLU A O 2478 C CB . GLU A 321 ? 0.1652 0.1410 0.1403 0.0208 -0.0006 0.0105 321 GLU A CB 2479 C CG . GLU A 321 ? 0.1984 0.1853 0.1476 0.0060 0.0002 -0.0046 321 GLU A CG 2480 C CD . GLU A 321 ? 0.2087 0.1681 0.1524 -0.0013 0.0002 -0.0044 321 GLU A CD 2481 O OE1 . GLU A 321 ? 0.2158 0.1778 0.1567 -0.0103 -0.0081 -0.0063 321 GLU A OE1 2482 O OE2 . GLU A 321 ? 0.2429 0.2005 0.1528 0.0099 -0.0093 -0.0135 321 GLU A OE2 2483 N N . SER A 322 ? 0.1765 0.1483 0.1573 0.0004 0.0013 0.0068 322 SER A N 2484 C CA . SER A 322 ? 0.1848 0.1540 0.1688 -0.0039 0.0039 -0.0063 322 SER A CA 2485 C C . SER A 322 ? 0.1846 0.1518 0.1614 0.0047 0.0039 -0.0149 322 SER A C 2486 O O . SER A 322 ? 0.1977 0.1574 0.1669 0.0125 -0.0019 -0.0151 322 SER A O 2487 C CB . SER A 322 ? 0.1854 0.1570 0.1740 -0.0084 0.0084 -0.0088 322 SER A CB 2488 O OG . SER A 322 ? 0.2099 0.1902 0.2009 -0.0098 0.0265 -0.0192 322 SER A OG 2489 N N . ARG A 323 ? 0.1808 0.1484 0.1432 0.0084 -0.0007 -0.0189 323 ARG A N 2490 C CA . ARG A 323 ? 0.1811 0.1467 0.1392 0.0065 0.0017 -0.0247 323 ARG A CA 2491 C C . ARG A 323 ? 0.1663 0.1604 0.1397 0.0056 0.0008 -0.0207 323 ARG A C 2492 O O . ARG A 323 ? 0.1507 0.1517 0.1430 0.0121 -0.0116 -0.0180 323 ARG A O 2493 C CB . ARG A 323 ? 0.1900 0.1425 0.1357 0.0079 0.0002 -0.0263 323 ARG A CB 2494 C CG . ARG A 323 ? 0.2043 0.1389 0.1317 -0.0058 -0.0005 -0.0475 323 ARG A CG 2495 C CD . ARG A 323 ? 0.2625 0.1626 0.1257 0.0036 -0.0002 -0.0548 323 ARG A CD 2496 N NE . ARG A 323 ? 0.2655 0.1573 0.1655 0.0091 -0.0098 -0.0495 323 ARG A NE 2497 C CZ . ARG A 323 ? 0.2813 0.1855 0.2328 -0.0001 -0.0070 -0.0313 323 ARG A CZ 2498 N NH1 . ARG A 323 ? 0.2670 0.2311 0.2283 -0.0051 -0.0179 -0.0114 323 ARG A NH1 2499 N NH2 . ARG A 323 ? 0.2966 0.1574 0.2337 -0.0104 -0.0116 -0.0588 323 ARG A NH2 2500 N N . ALA A 324 ? 0.1609 0.1616 0.1377 0.0085 -0.0002 -0.0218 324 ALA A N 2501 C CA . ALA A 324 ? 0.1639 0.1683 0.1401 0.0144 0.0013 -0.0195 324 ALA A CA 2502 C C . ALA A 324 ? 0.1616 0.1708 0.1267 0.0189 0.0014 -0.0128 324 ALA A C 2503 O O . ALA A 324 ? 0.1553 0.1657 0.1210 0.0132 -0.0031 -0.0237 324 ALA A O 2504 C CB . ALA A 324 ? 0.1517 0.1655 0.1150 0.0193 -0.0005 -0.0195 324 ALA A CB 2505 N N . TYR A 325 ? 0.1667 0.1767 0.1366 0.0258 0.0017 -0.0082 325 TYR A N 2506 C CA . TYR A 325 ? 0.1723 0.1805 0.1576 0.0259 0.0114 -0.0036 325 TYR A CA 2507 C C . TYR A 325 ? 0.1655 0.1751 0.1578 0.0290 0.0126 -0.0050 325 TYR A C 2508 O O . TYR A 325 ? 0.1763 0.1798 0.1659 0.0401 0.0086 0.0059 325 TYR A O 2509 C CB . TYR A 325 ? 0.1868 0.2077 0.1838 0.0218 0.0176 0.0005 325 TYR A CB 2510 C CG . TYR A 325 ? 0.2129 0.2346 0.2185 0.0171 0.0235 0.0031 325 TYR A CG 2511 C CD1 . TYR A 325 ? 0.2204 0.2300 0.2408 0.0204 0.0226 0.0211 325 TYR A CD1 2512 C CD2 . TYR A 325 ? 0.2367 0.2595 0.2464 -0.0004 0.0303 -0.0028 325 TYR A CD2 2513 C CE1 . TYR A 325 ? 0.2231 0.2496 0.2616 0.0177 0.0276 0.0156 325 TYR A CE1 2514 C CE2 . TYR A 325 ? 0.2547 0.2881 0.2522 0.0037 0.0427 0.0099 325 TYR A CE2 2515 C CZ . TYR A 325 ? 0.2405 0.2839 0.2621 0.0010 0.0331 0.0179 325 TYR A CZ 2516 O OH . TYR A 325 ? 0.2651 0.3164 0.2832 -0.0046 0.0417 0.0182 325 TYR A OH 2517 N N . ARG A 326 ? 0.1717 0.1717 0.1564 0.0326 0.0127 -0.0067 326 ARG A N 2518 C CA . ARG A 326 ? 0.1694 0.1601 0.1529 0.0306 0.0156 -0.0067 326 ARG A CA 2519 C C . ARG A 326 ? 0.1609 0.1572 0.1532 0.0200 0.0117 -0.0091 326 ARG A C 2520 O O . ARG A 326 ? 0.1727 0.1709 0.1612 0.0234 0.0158 -0.0105 326 ARG A O 2521 C CB . ARG A 326 ? 0.1585 0.1455 0.1492 0.0313 0.0111 -0.0074 326 ARG A CB 2522 C CG . ARG A 326 ? 0.1976 0.1747 0.1765 0.0328 0.0263 -0.0128 326 ARG A CG 2523 C CD . ARG A 326 ? 0.2290 0.1571 0.1880 0.0357 0.0337 -0.0341 326 ARG A CD 2524 N NE . ARG A 326 ? 0.2371 0.1935 0.2203 0.0375 0.0403 -0.0348 326 ARG A NE 2525 C CZ . ARG A 326 ? 0.2522 0.1954 0.2155 0.0423 0.0327 -0.0440 326 ARG A CZ 2526 N NH1 . ARG A 326 ? 0.2670 0.2029 0.2224 0.0531 0.0194 -0.0459 326 ARG A NH1 2527 N NH2 . ARG A 326 ? 0.2632 0.1869 0.2031 0.0294 0.0243 -0.0285 326 ARG A NH2 2528 N N . ALA A 327 ? 0.1541 0.1506 0.1472 0.0126 0.0096 -0.0181 327 ALA A N 2529 C CA . ALA A 327 ? 0.1469 0.1540 0.1475 0.0117 0.0112 -0.0115 327 ALA A CA 2530 C C . ALA A 327 ? 0.1466 0.1474 0.1403 0.0142 0.0099 -0.0123 327 ALA A C 2531 O O . ALA A 327 ? 0.1429 0.1556 0.1460 0.0167 0.0031 -0.0030 327 ALA A O 2532 C CB . ALA A 327 ? 0.1493 0.1525 0.1334 0.0044 0.0101 -0.0122 327 ALA A CB 2533 N N . LEU A 328 ? 0.1439 0.1416 0.1369 0.0213 0.0115 -0.0069 328 LEU A N 2534 C CA . LEU A 328 ? 0.1402 0.1505 0.1495 0.0231 0.0104 -0.0061 328 LEU A CA 2535 C C . LEU A 328 ? 0.1439 0.1525 0.1545 0.0254 0.0037 -0.0059 328 LEU A C 2536 O O . LEU A 328 ? 0.1509 0.1386 0.1678 0.0246 0.0002 -0.0057 328 LEU A O 2537 C CB . LEU A 328 ? 0.1495 0.1443 0.1392 0.0282 0.0148 -0.0017 328 LEU A CB 2538 C CG . LEU A 328 ? 0.1460 0.1568 0.1599 0.0306 0.0223 -0.0010 328 LEU A CG 2539 C CD1 . LEU A 328 ? 0.1537 0.1630 0.1717 0.0399 0.0164 0.0130 328 LEU A CD1 2540 C CD2 . LEU A 328 ? 0.1625 0.1425 0.1532 0.0282 0.0096 -0.0081 328 LEU A CD2 2541 N N . THR A 329 ? 0.1345 0.1569 0.1534 0.0274 0.0064 -0.0141 329 THR A N 2542 C CA . THR A 329 ? 0.1384 0.1645 0.1603 0.0268 0.0080 -0.0123 329 THR A CA 2543 C C . THR A 329 ? 0.1278 0.1572 0.1600 0.0311 0.0114 -0.0197 329 THR A C 2544 O O . THR A 329 ? 0.1290 0.1563 0.1639 0.0258 0.0054 -0.0081 329 THR A O 2545 C CB . THR A 329 ? 0.1322 0.1591 0.1659 0.0341 0.0049 -0.0179 329 THR A CB 2546 O OG1 . THR A 329 ? 0.1320 0.1753 0.1649 0.0129 0.0260 -0.0100 329 THR A OG1 2547 C CG2 . THR A 329 ? 0.1581 0.1906 0.1885 0.0313 -0.0015 -0.0039 329 THR A CG2 2548 N N . GLU A 330 ? 0.1359 0.1510 0.1582 0.0246 0.0129 -0.0240 330 GLU A N 2549 C CA . GLU A 330 ? 0.1336 0.1525 0.1546 0.0298 0.0148 -0.0273 330 GLU A CA 2550 C C . GLU A 330 ? 0.1339 0.1483 0.1510 0.0201 0.0120 -0.0250 330 GLU A C 2551 O O . GLU A 330 ? 0.1323 0.1463 0.1422 0.0342 0.0199 -0.0329 330 GLU A O 2552 C CB . GLU A 330 ? 0.1438 0.1466 0.1604 0.0233 0.0060 -0.0271 330 GLU A CB 2553 C CG . GLU A 330 ? 0.1437 0.1809 0.1640 0.0363 0.0288 -0.0298 330 GLU A CG 2554 C CD . GLU A 330 ? 0.1645 0.2103 0.2119 0.0289 0.0258 -0.0170 330 GLU A CD 2555 O OE1 . GLU A 330 ? 0.1625 0.2527 0.2271 0.0250 0.0460 0.0023 330 GLU A OE1 2556 O OE2 . GLU A 330 ? 0.1887 0.1868 0.2062 0.0212 0.0334 -0.0014 330 GLU A OE2 2557 N N . THR A 331 ? 0.1274 0.1463 0.1471 0.0178 0.0169 -0.0170 331 THR A N 2558 C CA . THR A 331 ? 0.1443 0.1573 0.1465 0.0129 0.0142 -0.0109 331 THR A CA 2559 C C . THR A 331 ? 0.1392 0.1681 0.1535 0.0109 0.0134 -0.0026 331 THR A C 2560 O O . THR A 331 ? 0.1499 0.1769 0.1584 0.0144 0.0114 0.0047 331 THR A O 2561 C CB . THR A 331 ? 0.1504 0.1544 0.1517 0.0100 0.0219 -0.0178 331 THR A CB 2562 O OG1 . THR A 331 ? 0.1463 0.1474 0.1349 0.0227 0.0238 -0.0016 331 THR A OG1 2563 C CG2 . THR A 331 ? 0.1608 0.1357 0.1561 0.0262 0.0200 -0.0317 331 THR A CG2 2564 N N . ILE A 332 ? 0.1361 0.1794 0.1507 0.0064 0.0168 0.0042 332 ILE A N 2565 C CA . ILE A 332 ? 0.1340 0.2045 0.1678 0.0093 0.0098 0.0119 332 ILE A CA 2566 C C . ILE A 332 ? 0.1328 0.2017 0.1562 0.0099 0.0142 0.0084 332 ILE A C 2567 O O . ILE A 332 ? 0.1400 0.1984 0.1523 0.0081 0.0135 0.0025 332 ILE A O 2568 C CB . ILE A 332 ? 0.1284 0.2112 0.1696 0.0109 0.0070 0.0185 332 ILE A CB 2569 C CG1 . ILE A 332 ? 0.1202 0.2279 0.1872 0.0085 -0.0081 0.0286 332 ILE A CG1 2570 C CG2 . ILE A 332 ? 0.1400 0.2167 0.1868 0.0033 0.0089 0.0299 332 ILE A CG2 2571 C CD1 . ILE A 332 ? 0.1525 0.2275 0.2466 0.0444 -0.0272 0.0295 332 ILE A CD1 2572 N N . MET A 333 ? 0.1270 0.2058 0.1485 0.0052 0.0124 0.0025 333 MET A N 2573 C CA . MET A 333 ? 0.1486 0.1960 0.1547 0.0079 0.0119 0.0030 333 MET A CA 2574 C C . MET A 333 ? 0.1465 0.1882 0.1494 0.0060 0.0147 -0.0029 333 MET A C 2575 O O . MET A 333 ? 0.1531 0.1682 0.1532 0.0165 0.0141 -0.0004 333 MET A O 2576 C CB . MET A 333 ? 0.1634 0.2197 0.1454 0.0034 0.0118 0.0015 333 MET A CB 2577 C CG . MET A 333 ? 0.1933 0.2469 0.2086 0.0000 0.0231 0.0154 333 MET A CG 2578 S SD . MET A 333 ? 0.2666 0.3860 0.2836 -0.0191 0.0596 -0.0021 333 MET A SD 2579 C CE . MET A 333 ? 0.2410 0.3670 0.3153 -0.0020 0.0650 -0.0020 333 MET A CE 2580 N N . PHE A 334 ? 0.1418 0.1750 0.1392 0.0070 0.0120 -0.0091 334 PHE A N 2581 C CA . PHE A 334 ? 0.1461 0.1731 0.1470 0.0063 0.0192 -0.0077 334 PHE A CA 2582 C C . PHE A 334 ? 0.1368 0.1785 0.1439 -0.0005 0.0187 -0.0035 334 PHE A C 2583 O O . PHE A 334 ? 0.1454 0.1844 0.1345 -0.0022 0.0250 0.0112 334 PHE A O 2584 C CB . PHE A 334 ? 0.1309 0.1534 0.1420 0.0048 0.0202 -0.0096 334 PHE A CB 2585 C CG . PHE A 334 ? 0.1569 0.1398 0.1568 0.0045 0.0021 -0.0070 334 PHE A CG 2586 C CD1 . PHE A 334 ? 0.1467 0.1145 0.1695 0.0253 -0.0104 -0.0218 334 PHE A CD1 2587 C CD2 . PHE A 334 ? 0.1400 0.1368 0.1416 0.0039 0.0068 -0.0226 334 PHE A CD2 2588 C CE1 . PHE A 334 ? 0.1650 0.0808 0.1700 0.0176 -0.0235 -0.0151 334 PHE A CE1 2589 C CE2 . PHE A 334 ? 0.1473 0.0573 0.1730 0.0129 -0.0078 -0.0177 334 PHE A CE2 2590 C CZ . PHE A 334 ? 0.1335 0.0825 0.1596 0.0098 -0.0065 -0.0101 334 PHE A CZ 2591 N N . ASP A 335 ? 0.1398 0.1833 0.1401 0.0002 0.0237 -0.0030 335 ASP A N 2592 C CA . ASP A 335 ? 0.1417 0.1850 0.1400 -0.0048 0.0223 -0.0050 335 ASP A CA 2593 C C . ASP A 335 ? 0.1526 0.1810 0.1472 -0.0010 0.0197 -0.0050 335 ASP A C 2594 O O . ASP A 335 ? 0.1576 0.1885 0.1523 -0.0007 0.0281 -0.0113 335 ASP A O 2595 C CB . ASP A 335 ? 0.1447 0.1878 0.1390 -0.0119 0.0200 -0.0107 335 ASP A CB 2596 C CG . ASP A 335 ? 0.1700 0.2158 0.1625 -0.0231 0.0206 0.0027 335 ASP A CG 2597 O OD1 . ASP A 335 ? 0.1903 0.2093 0.1373 -0.0416 0.0410 -0.0116 335 ASP A OD1 2598 O OD2 . ASP A 335 ? 0.1539 0.2595 0.1820 -0.0517 0.0088 0.0346 335 ASP A OD2 2599 N N . ASP A 336 ? 0.1490 0.1817 0.1481 0.0054 0.0245 -0.0038 336 ASP A N 2600 C CA . ASP A 336 ? 0.1627 0.1780 0.1580 0.0031 0.0252 0.0009 336 ASP A CA 2601 C C . ASP A 336 ? 0.1525 0.1748 0.1570 0.0034 0.0202 0.0021 336 ASP A C 2602 O O . ASP A 336 ? 0.1398 0.1714 0.1511 0.0057 0.0286 0.0001 336 ASP A O 2603 C CB . ASP A 336 ? 0.1621 0.1868 0.1694 0.0082 0.0301 0.0125 336 ASP A CB 2604 C CG . ASP A 336 ? 0.1976 0.2124 0.2053 0.0066 0.0357 0.0090 336 ASP A CG 2605 O OD1 . ASP A 336 ? 0.2180 0.2281 0.2130 -0.0082 0.0178 0.0109 336 ASP A OD1 2606 O OD2 . ASP A 336 ? 0.2319 0.2329 0.2658 0.0503 0.0537 0.0221 336 ASP A OD2 2607 N N . ALA A 337 ? 0.1503 0.1668 0.1466 0.0016 0.0166 -0.0030 337 ALA A N 2608 C CA . ALA A 337 ? 0.1511 0.1663 0.1541 -0.0043 0.0118 -0.0007 337 ALA A CA 2609 C C . ALA A 337 ? 0.1541 0.1714 0.1519 -0.0071 0.0132 -0.0019 337 ALA A C 2610 O O . ALA A 337 ? 0.1669 0.1779 0.1525 -0.0197 0.0215 0.0053 337 ALA A O 2611 C CB . ALA A 337 ? 0.1532 0.1647 0.1442 -0.0056 0.0101 0.0023 337 ALA A CB 2612 N N . ILE A 338 ? 0.1531 0.1729 0.1547 -0.0062 0.0122 -0.0039 338 ILE A N 2613 C CA . ILE A 338 ? 0.1562 0.1702 0.1562 -0.0035 0.0160 -0.0084 338 ILE A CA 2614 C C . ILE A 338 ? 0.1636 0.1807 0.1625 -0.0011 0.0182 -0.0077 338 ILE A C 2615 O O . ILE A 338 ? 0.1668 0.1905 0.1717 -0.0007 0.0178 -0.0045 338 ILE A O 2616 C CB . ILE A 338 ? 0.1568 0.1580 0.1521 -0.0057 0.0219 -0.0096 338 ILE A CB 2617 C CG1 . ILE A 338 ? 0.1404 0.1557 0.1609 0.0026 0.0195 0.0009 338 ILE A CG1 2618 C CG2 . ILE A 338 ? 0.1758 0.1707 0.1434 -0.0114 0.0159 -0.0079 338 ILE A CG2 2619 C CD1 . ILE A 338 ? 0.1499 0.1078 0.1153 -0.0109 0.0375 0.0191 338 ILE A CD1 2620 N N . GLU A 339 ? 0.1628 0.1942 0.1609 -0.0025 0.0154 -0.0105 339 GLU A N 2621 C CA . GLU A 339 ? 0.1694 0.2119 0.1787 0.0013 0.0173 -0.0039 339 GLU A CA 2622 C C . GLU A 339 ? 0.1676 0.2088 0.1722 0.0012 0.0191 -0.0004 339 GLU A C 2623 O O . GLU A 339 ? 0.1747 0.2158 0.1710 0.0029 0.0199 -0.0009 339 GLU A O 2624 C CB . GLU A 339 ? 0.1742 0.2144 0.1908 0.0010 0.0127 -0.0136 339 GLU A CB 2625 C CG . GLU A 339 ? 0.2060 0.2778 0.2718 0.0261 -0.0047 -0.0109 339 GLU A CG 2626 C CD . GLU A 339 ? 0.2842 0.3692 0.3416 0.0292 -0.0316 -0.0355 339 GLU A CD 2627 O OE1 . GLU A 339 ? 0.3428 0.4321 0.4071 0.0383 -0.0551 -0.0305 339 GLU A OE1 2628 O OE2 . GLU A 339 ? 0.2948 0.3714 0.3949 0.0368 -0.0176 -0.0448 339 GLU A OE2 2629 N N . ARG A 340 ? 0.1660 0.2093 0.1582 0.0017 0.0270 0.0073 340 ARG A N 2630 C CA . ARG A 340 ? 0.1753 0.2079 0.1586 -0.0046 0.0309 0.0116 340 ARG A CA 2631 C C . ARG A 340 ? 0.1661 0.2085 0.1574 -0.0026 0.0331 0.0126 340 ARG A C 2632 O O . ARG A 340 ? 0.1721 0.2000 0.1622 -0.0064 0.0382 -0.0047 340 ARG A O 2633 C CB . ARG A 340 ? 0.1808 0.2172 0.1457 -0.0086 0.0341 0.0171 340 ARG A CB 2634 C CG . ARG A 340 ? 0.1828 0.2276 0.1584 -0.0299 0.0463 0.0297 340 ARG A CG 2635 C CD . ARG A 340 ? 0.1808 0.2291 0.1582 -0.0383 0.0309 0.0619 340 ARG A CD 2636 N NE . ARG A 340 ? 0.1784 0.2223 0.2065 -0.0280 0.0382 0.0642 340 ARG A NE 2637 C CZ . ARG A 340 ? 0.1867 0.2254 0.2077 -0.0297 0.0259 0.0751 340 ARG A CZ 2638 N NH1 . ARG A 340 ? 0.1735 0.2326 0.2307 -0.0282 -0.0006 0.0658 340 ARG A NH1 2639 N NH2 . ARG A 340 ? 0.1671 0.2036 0.1839 -0.0032 0.0349 0.1001 340 ARG A NH2 2640 N N . ALA A 341 ? 0.1563 0.2058 0.1593 0.0019 0.0292 0.0143 341 ALA A N 2641 C CA . ALA A 341 ? 0.1512 0.2031 0.1726 0.0009 0.0332 0.0169 341 ALA A CA 2642 C C . ALA A 341 ? 0.1522 0.1996 0.1751 0.0019 0.0343 0.0217 341 ALA A C 2643 O O . ALA A 341 ? 0.1655 0.2030 0.1852 0.0052 0.0298 0.0267 341 ALA A O 2644 C CB . ALA A 341 ? 0.1385 0.2000 0.1721 0.0014 0.0314 0.0199 341 ALA A CB 2645 N N . GLY A 342 ? 0.1528 0.1995 0.1800 -0.0006 0.0340 0.0216 342 GLY A N 2646 C CA . GLY A 342 ? 0.1572 0.1896 0.1795 -0.0080 0.0312 0.0202 342 GLY A CA 2647 C C . GLY A 342 ? 0.1753 0.1915 0.1860 -0.0058 0.0318 0.0191 342 GLY A C 2648 O O . GLY A 342 ? 0.1762 0.1850 0.1917 -0.0166 0.0387 0.0195 342 GLY A O 2649 N N . GLN A 343 ? 0.1762 0.1973 0.1956 -0.0056 0.0284 0.0230 343 GLN A N 2650 C CA . GLN A 343 ? 0.1921 0.2064 0.1975 -0.0006 0.0296 0.0202 343 GLN A CA 2651 C C . GLN A 343 ? 0.2053 0.2153 0.2072 -0.0060 0.0293 0.0164 343 GLN A C 2652 O O . GLN A 343 ? 0.2161 0.2124 0.2152 -0.0089 0.0265 0.0197 343 GLN A O 2653 C CB . GLN A 343 ? 0.1829 0.2093 0.1971 0.0004 0.0293 0.0302 343 GLN A CB 2654 C CG . GLN A 343 ? 0.1915 0.2463 0.2088 0.0097 0.0235 0.0006 343 GLN A CG 2655 C CD . GLN A 343 ? 0.2101 0.2718 0.2315 0.0271 0.0081 -0.0115 343 GLN A CD 2656 O OE1 . GLN A 343 ? 0.2295 0.2624 0.2313 0.0231 0.0292 -0.0276 343 GLN A OE1 2657 N NE2 . GLN A 343 ? 0.2026 0.3253 0.2644 0.0347 0.0094 -0.0354 343 GLN A NE2 2658 N N . LEU A 344 ? 0.2094 0.2181 0.2111 -0.0092 0.0242 0.0129 344 LEU A N 2659 C CA . LEU A 344 ? 0.2185 0.2175 0.2080 -0.0078 0.0242 0.0128 344 LEU A CA 2660 C C . LEU A 344 ? 0.2251 0.2263 0.2132 -0.0114 0.0208 0.0154 344 LEU A C 2661 O O . LEU A 344 ? 0.2419 0.2378 0.2079 -0.0031 0.0122 0.0179 344 LEU A O 2662 C CB . LEU A 344 ? 0.2170 0.2165 0.2101 -0.0118 0.0258 0.0104 344 LEU A CB 2663 C CG . LEU A 344 ? 0.2176 0.2169 0.2060 -0.0069 0.0291 -0.0030 344 LEU A CG 2664 C CD1 . LEU A 344 ? 0.2236 0.2137 0.2454 -0.0023 0.0295 -0.0384 344 LEU A CD1 2665 C CD2 . LEU A 344 ? 0.2220 0.2279 0.2283 -0.0027 0.0402 -0.0121 344 LEU A CD2 2666 N N . THR A 345 ? 0.2233 0.2180 0.2110 -0.0245 0.0182 0.0188 345 THR A N 2667 C CA . THR A 345 ? 0.2081 0.2182 0.2150 -0.0360 0.0175 0.0136 345 THR A CA 2668 C C . THR A 345 ? 0.2123 0.2120 0.2306 -0.0388 0.0196 0.0163 345 THR A C 2669 O O . THR A 345 ? 0.1998 0.2200 0.2186 -0.0434 0.0182 0.0190 345 THR A O 2670 C CB . THR A 345 ? 0.2092 0.2109 0.2102 -0.0375 0.0174 0.0119 345 THR A CB 2671 O OG1 . THR A 345 ? 0.1864 0.2349 0.2257 -0.0568 0.0099 0.0172 345 THR A OG1 2672 C CG2 . THR A 345 ? 0.2048 0.2206 0.2241 -0.0600 0.0171 0.0113 345 THR A CG2 2673 N N . SER A 346 ? 0.2191 0.2122 0.2414 -0.0397 0.0180 0.0153 346 SER A N 2674 C CA . SER A 346 ? 0.2265 0.2007 0.2405 -0.0449 0.0169 0.0101 346 SER A CA 2675 C C . SER A 346 ? 0.2273 0.1984 0.2394 -0.0414 0.0099 0.0177 346 SER A C 2676 O O . SER A 346 ? 0.2250 0.1957 0.2359 -0.0424 0.0193 0.0144 346 SER A O 2677 C CB . SER A 346 ? 0.2317 0.2036 0.2409 -0.0463 0.0199 0.0142 346 SER A CB 2678 O OG . SER A 346 ? 0.2505 0.1903 0.2746 -0.0743 0.0322 0.0031 346 SER A OG 2679 N N . GLU A 347 ? 0.2301 0.1981 0.2394 -0.0373 0.0000 0.0236 347 GLU A N 2680 C CA . GLU A 347 ? 0.2347 0.2188 0.2478 -0.0337 -0.0130 0.0335 347 GLU A CA 2681 C C . GLU A 347 ? 0.2313 0.2107 0.2423 -0.0339 -0.0122 0.0274 347 GLU A C 2682 O O . GLU A 347 ? 0.2083 0.1961 0.2375 -0.0322 -0.0012 0.0295 347 GLU A O 2683 C CB . GLU A 347 ? 0.2372 0.2266 0.2474 -0.0381 -0.0136 0.0298 347 GLU A CB 2684 C CG . GLU A 347 ? 0.2708 0.2531 0.2629 -0.0271 -0.0242 0.0469 347 GLU A CG 2685 C CD . GLU A 347 ? 0.2610 0.2744 0.2778 -0.0401 -0.0293 0.0474 347 GLU A CD 2686 O OE1 . GLU A 347 ? 0.2887 0.3023 0.2978 -0.0348 -0.0396 0.0722 347 GLU A OE1 2687 O OE2 . GLU A 347 ? 0.3318 0.3739 0.3462 -0.0387 -0.0382 0.0636 347 GLU A OE2 2688 N N . GLU A 348 ? 0.2244 0.2035 0.2434 -0.0352 -0.0145 0.0297 348 GLU A N 2689 C CA . GLU A 348 ? 0.2433 0.2137 0.2500 -0.0285 -0.0111 0.0276 348 GLU A CA 2690 C C . GLU A 348 ? 0.2436 0.1966 0.2407 -0.0223 -0.0040 0.0289 348 GLU A C 2691 O O . GLU A 348 ? 0.2533 0.2014 0.2472 -0.0217 -0.0063 0.0242 348 GLU A O 2692 C CB . GLU A 348 ? 0.2479 0.2183 0.2656 -0.0305 -0.0220 0.0240 348 GLU A CB 2693 C CG . GLU A 348 ? 0.3120 0.3090 0.3225 -0.0253 -0.0231 0.0160 348 GLU A CG 2694 C CD . GLU A 348 ? 0.3795 0.3876 0.4017 -0.0061 -0.0371 0.0140 348 GLU A CD 2695 O OE1 . GLU A 348 ? 0.4300 0.4413 0.4494 -0.0039 -0.0493 0.0261 348 GLU A OE1 2696 O OE2 . GLU A 348 ? 0.3998 0.4266 0.4494 -0.0257 -0.0372 -0.0093 348 GLU A OE2 2697 N N . ASP A 349 ? 0.2447 0.1857 0.2227 -0.0138 0.0028 0.0307 349 ASP A N 2698 C CA . ASP A 349 ? 0.2287 0.1771 0.2195 -0.0109 0.0134 0.0279 349 ASP A CA 2699 C C . ASP A 349 ? 0.2258 0.1755 0.2120 -0.0024 0.0232 0.0227 349 ASP A C 2700 O O . ASP A 349 ? 0.2023 0.1611 0.1985 -0.0039 0.0262 0.0297 349 ASP A O 2701 C CB . ASP A 349 ? 0.2327 0.1879 0.2182 -0.0063 0.0201 0.0249 349 ASP A CB 2702 C CG . ASP A 349 ? 0.2364 0.1981 0.2305 -0.0127 0.0166 0.0294 349 ASP A CG 2703 O OD1 . ASP A 349 ? 0.2380 0.2015 0.2569 -0.0228 0.0257 0.0378 349 ASP A OD1 2704 O OD2 . ASP A 349 ? 0.2374 0.2247 0.2323 -0.0412 0.0008 0.0162 349 ASP A OD2 2705 N N . THR A 350 ? 0.2131 0.1568 0.2056 0.0044 0.0281 0.0161 350 THR A N 2706 C CA . THR A 350 ? 0.2049 0.1601 0.2045 0.0055 0.0330 0.0086 350 THR A CA 2707 C C . THR A 350 ? 0.1928 0.1504 0.1986 0.0103 0.0314 0.0075 350 THR A C 2708 O O . THR A 350 ? 0.1994 0.1697 0.2128 0.0056 0.0331 -0.0001 350 THR A O 2709 C CB . THR A 350 ? 0.2022 0.1457 0.1980 0.0057 0.0359 0.0064 350 THR A CB 2710 O OG1 . THR A 350 ? 0.2305 0.1714 0.1977 -0.0012 0.0434 -0.0024 350 THR A OG1 2711 C CG2 . THR A 350 ? 0.2102 0.1576 0.1919 0.0115 0.0348 0.0037 350 THR A CG2 2712 N N . LEU A 351 ? 0.1755 0.1391 0.1905 0.0114 0.0321 0.0082 351 LEU A N 2713 C CA . LEU A 351 ? 0.1712 0.1533 0.1818 0.0118 0.0313 0.0104 351 LEU A CA 2714 C C . LEU A 351 ? 0.1723 0.1494 0.1755 0.0134 0.0316 0.0139 351 LEU A C 2715 O O . LEU A 351 ? 0.1783 0.1506 0.1890 0.0188 0.0280 0.0206 351 LEU A O 2716 C CB . LEU A 351 ? 0.1575 0.1507 0.1773 0.0079 0.0321 0.0098 351 LEU A CB 2717 C CG . LEU A 351 ? 0.1582 0.1574 0.1788 0.0089 0.0306 0.0160 351 LEU A CG 2718 C CD1 . LEU A 351 ? 0.1500 0.1451 0.1407 -0.0144 0.0249 0.0100 351 LEU A CD1 2719 C CD2 . LEU A 351 ? 0.1570 0.1863 0.1993 0.0045 0.0250 0.0090 351 LEU A CD2 2720 N N . SER A 352 ? 0.1799 0.1435 0.1619 0.0149 0.0353 0.0179 352 SER A N 2721 C CA . SER A 352 ? 0.1839 0.1478 0.1595 0.0098 0.0334 0.0208 352 SER A CA 2722 C C . SER A 352 ? 0.1776 0.1461 0.1562 0.0079 0.0317 0.0203 352 SER A C 2723 O O . SER A 352 ? 0.1832 0.1471 0.1368 0.0036 0.0354 0.0282 352 SER A O 2724 C CB . SER A 352 ? 0.1820 0.1398 0.1593 0.0072 0.0363 0.0182 352 SER A CB 2725 O OG . SER A 352 ? 0.2068 0.1714 0.1571 0.0357 0.0389 0.0380 352 SER A OG 2726 N N . LEU A 353 ? 0.1618 0.1524 0.1632 0.0082 0.0246 0.0105 353 LEU A N 2727 C CA . LEU A 353 ? 0.1590 0.1583 0.1733 0.0068 0.0267 0.0062 353 LEU A CA 2728 C C . LEU A 353 ? 0.1533 0.1614 0.1721 0.0074 0.0188 0.0089 353 LEU A C 2729 O O . LEU A 353 ? 0.1492 0.1484 0.1608 0.0118 0.0152 0.0082 353 LEU A O 2730 C CB . LEU A 353 ? 0.1617 0.1719 0.1959 0.0146 0.0230 0.0040 353 LEU A CB 2731 C CG . LEU A 353 ? 0.2009 0.2178 0.2472 0.0025 0.0462 -0.0371 353 LEU A CG 2732 C CD1 . LEU A 353 ? 0.1677 0.2036 0.2473 -0.0047 0.0869 -0.0521 353 LEU A CD1 2733 C CD2 . LEU A 353 ? 0.1977 0.2450 0.2748 -0.0142 0.0400 -0.0755 353 LEU A CD2 2734 N N . VAL A 354 ? 0.1479 0.1544 0.1715 -0.0006 0.0137 0.0114 354 VAL A N 2735 C CA . VAL A 354 ? 0.1404 0.1434 0.1571 -0.0071 0.0163 0.0073 354 VAL A CA 2736 C C . VAL A 354 ? 0.1508 0.1529 0.1565 -0.0041 0.0111 0.0106 354 VAL A C 2737 O O . VAL A 354 ? 0.1611 0.1628 0.1617 -0.0064 0.0203 -0.0029 354 VAL A O 2738 C CB . VAL A 354 ? 0.1501 0.1416 0.1609 -0.0027 0.0177 0.0116 354 VAL A CB 2739 C CG1 . VAL A 354 ? 0.1467 0.1142 0.1499 -0.0126 0.0139 0.0048 354 VAL A CG1 2740 C CG2 . VAL A 354 ? 0.1086 0.1196 0.1406 -0.0413 0.0293 0.0000 354 VAL A CG2 2741 N N . THR A 355 ? 0.1399 0.1521 0.1418 -0.0012 0.0038 0.0098 355 THR A N 2742 C CA . THR A 355 ? 0.1404 0.1523 0.1577 0.0002 0.0009 0.0078 355 THR A CA 2743 C C . THR A 355 ? 0.1377 0.1534 0.1568 0.0027 -0.0056 0.0108 355 THR A C 2744 O O . THR A 355 ? 0.1399 0.1525 0.1609 0.0038 0.0022 0.0010 355 THR A O 2745 C CB . THR A 355 ? 0.1429 0.1619 0.1585 -0.0049 0.0009 0.0138 355 THR A CB 2746 O OG1 . THR A 355 ? 0.1518 0.1820 0.1537 0.0028 0.0091 0.0107 355 THR A OG1 2747 C CG2 . THR A 355 ? 0.1600 0.1740 0.1608 0.0059 0.0014 0.0094 355 THR A CG2 2748 N N . ALA A 356 ? 0.1399 0.1370 0.1558 0.0054 -0.0165 0.0146 356 ALA A N 2749 C CA . ALA A 356 ? 0.1321 0.1381 0.1493 -0.0007 -0.0218 0.0074 356 ALA A CA 2750 C C . ALA A 356 ? 0.1376 0.1382 0.1479 0.0038 -0.0161 0.0111 356 ALA A C 2751 O O . ALA A 356 ? 0.1403 0.1387 0.1618 0.0081 -0.0160 0.0090 356 ALA A O 2752 C CB . ALA A 356 ? 0.1349 0.1212 0.1475 0.0058 -0.0239 0.0122 356 ALA A CB 2753 N N . ASP A 357 ? 0.1292 0.1316 0.1339 -0.0070 -0.0234 0.0103 357 ASP A N 2754 C CA . ASP A 357 ? 0.1277 0.1341 0.1239 0.0038 -0.0200 0.0069 357 ASP A CA 2755 C C . ASP A 357 ? 0.1302 0.1304 0.1291 0.0011 -0.0183 -0.0010 357 ASP A C 2756 O O . ASP A 357 ? 0.1199 0.1443 0.1258 0.0006 -0.0098 0.0091 357 ASP A O 2757 C CB . ASP A 357 ? 0.1364 0.1282 0.1213 0.0057 -0.0205 0.0011 357 ASP A CB 2758 C CG . ASP A 357 ? 0.1447 0.1297 0.1231 -0.0060 -0.0196 0.0029 357 ASP A CG 2759 O OD1 . ASP A 357 ? 0.1326 0.1027 0.1331 -0.0277 -0.0160 -0.0202 357 ASP A OD1 2760 O OD2 . ASP A 357 ? 0.1359 0.1592 0.1478 0.0077 -0.0140 -0.0030 357 ASP A OD2 2761 N N . HIS A 358 ? 0.1334 0.1262 0.1218 -0.0008 -0.0187 -0.0055 358 HIS A N 2762 C CA . HIS A 358 ? 0.1368 0.1213 0.1324 -0.0069 -0.0198 -0.0047 358 HIS A CA 2763 C C . HIS A 358 ? 0.1405 0.1189 0.1366 -0.0017 -0.0123 -0.0093 358 HIS A C 2764 O O . HIS A 358 ? 0.1404 0.1151 0.1391 0.0010 -0.0052 -0.0030 358 HIS A O 2765 C CB . HIS A 358 ? 0.1358 0.1271 0.1223 -0.0024 -0.0193 -0.0084 358 HIS A CB 2766 C CG . HIS A 358 ? 0.1533 0.1216 0.1524 -0.0172 -0.0262 0.0034 358 HIS A CG 2767 N ND1 . HIS A 358 ? 0.1590 0.1246 0.1471 -0.0147 -0.0317 -0.0058 358 HIS A ND1 2768 C CD2 . HIS A 358 ? 0.1696 0.1170 0.1488 -0.0310 -0.0273 -0.0069 358 HIS A CD2 2769 C CE1 . HIS A 358 ? 0.1523 0.1429 0.1555 -0.0353 -0.0574 0.0084 358 HIS A CE1 2770 N NE2 . HIS A 358 ? 0.1957 0.0970 0.1629 -0.0249 -0.0207 0.0221 358 HIS A NE2 2771 N N . SER A 359 ? 0.1333 0.1165 0.1224 -0.0029 -0.0181 -0.0090 359 SER A N 2772 C CA . SER A 359 ? 0.1449 0.1257 0.1355 -0.0020 -0.0171 -0.0112 359 SER A CA 2773 C C . SER A 359 ? 0.1391 0.1197 0.1254 0.0010 -0.0130 -0.0162 359 SER A C 2774 O O . SER A 359 ? 0.1387 0.1157 0.1378 0.0003 -0.0087 -0.0095 359 SER A O 2775 C CB . SER A 359 ? 0.1414 0.1210 0.1128 -0.0002 -0.0287 -0.0220 359 SER A CB 2776 O OG . SER A 359 ? 0.1475 0.1490 0.1701 -0.0032 -0.0217 -0.0248 359 SER A OG 2777 N N . HIS A 360 ? 0.1351 0.1232 0.1318 0.0019 -0.0110 -0.0067 360 HIS A N 2778 C CA . HIS A 360 ? 0.1402 0.1297 0.1259 0.0046 -0.0072 -0.0055 360 HIS A CA 2779 C C . HIS A 360 ? 0.1422 0.1422 0.1301 0.0055 -0.0135 -0.0006 360 HIS A C 2780 O O . HIS A 360 ? 0.1542 0.1275 0.1369 -0.0036 -0.0225 -0.0046 360 HIS A O 2781 C CB . HIS A 360 ? 0.1382 0.1255 0.1056 0.0013 -0.0081 -0.0123 360 HIS A CB 2782 C CG . HIS A 360 ? 0.1462 0.1494 0.1171 0.0267 0.0110 -0.0019 360 HIS A CG 2783 N ND1 . HIS A 360 ? 0.1469 0.1635 0.1260 0.0344 0.0171 -0.0229 360 HIS A ND1 2784 C CD2 . HIS A 360 ? 0.1448 0.1510 0.0654 0.0281 0.0183 -0.0017 360 HIS A CD2 2785 C CE1 . HIS A 360 ? 0.1401 0.1730 0.1006 0.0326 0.0102 0.0033 360 HIS A CE1 2786 N NE2 . HIS A 360 ? 0.1554 0.1476 0.1158 0.0286 0.0383 0.0172 360 HIS A NE2 2787 N N . VAL A 361 ? 0.1357 0.1337 0.1323 -0.0017 -0.0147 0.0070 361 VAL A N 2788 C CA . VAL A 361 ? 0.1322 0.1600 0.1372 0.0053 -0.0114 0.0092 361 VAL A CA 2789 C C . VAL A 361 ? 0.1460 0.1558 0.1452 0.0055 -0.0080 0.0108 361 VAL A C 2790 O O . VAL A 361 ? 0.1457 0.1657 0.1478 0.0062 -0.0089 0.0163 361 VAL A O 2791 C CB . VAL A 361 ? 0.1355 0.1428 0.1342 0.0032 -0.0114 0.0117 361 VAL A CB 2792 C CG1 . VAL A 361 ? 0.0833 0.1484 0.1151 0.0006 -0.0072 0.0030 361 VAL A CG1 2793 C CG2 . VAL A 361 ? 0.1149 0.1778 0.1195 0.0029 -0.0069 -0.0028 361 VAL A CG2 2794 N N . PHE A 362 ? 0.1542 0.1515 0.1461 0.0006 -0.0013 0.0137 362 PHE A N 2795 C CA . PHE A 362 ? 0.1551 0.1439 0.1481 0.0044 -0.0075 0.0172 362 PHE A CA 2796 C C . PHE A 362 ? 0.1656 0.1515 0.1554 0.0056 -0.0060 0.0211 362 PHE A C 2797 O O . PHE A 362 ? 0.1881 0.1600 0.1520 0.0245 -0.0010 0.0160 362 PHE A O 2798 C CB . PHE A 362 ? 0.1613 0.1516 0.1537 0.0080 -0.0038 0.0203 362 PHE A CB 2799 C CG . PHE A 362 ? 0.1577 0.1478 0.1637 -0.0070 0.0026 0.0154 362 PHE A CG 2800 C CD1 . PHE A 362 ? 0.1656 0.1776 0.1667 0.0061 -0.0123 0.0166 362 PHE A CD1 2801 C CD2 . PHE A 362 ? 0.1590 0.1650 0.1677 -0.0097 0.0093 0.0226 362 PHE A CD2 2802 C CE1 . PHE A 362 ? 0.1213 0.1565 0.1429 -0.0065 -0.0195 0.0238 362 PHE A CE1 2803 C CE2 . PHE A 362 ? 0.1455 0.1707 0.1677 -0.0144 0.0087 0.0362 362 PHE A CE2 2804 C CZ . PHE A 362 ? 0.1587 0.1474 0.1563 0.0105 -0.0080 0.0388 362 PHE A CZ 2805 N N . SER A 363 ? 0.1465 0.1504 0.1489 0.0005 -0.0115 0.0232 363 SER A N 2806 C CA . SER A 363 ? 0.1428 0.1551 0.1540 -0.0067 -0.0189 0.0171 363 SER A CA 2807 C C . SER A 363 ? 0.1395 0.1654 0.1527 -0.0078 -0.0129 0.0129 363 SER A C 2808 O O . SER A 363 ? 0.1296 0.1612 0.1640 -0.0110 -0.0170 0.0138 363 SER A O 2809 C CB . SER A 363 ? 0.1418 0.1455 0.1327 -0.0019 -0.0186 0.0187 363 SER A CB 2810 O OG . SER A 363 ? 0.1776 0.1489 0.1574 -0.0231 -0.0253 0.0266 363 SER A OG 2811 N N . PHE A 364 ? 0.1350 0.1667 0.1516 -0.0139 -0.0178 0.0163 364 PHE A N 2812 C CA . PHE A 364 ? 0.1512 0.1910 0.1566 -0.0092 -0.0155 0.0088 364 PHE A CA 2813 C C . PHE A 364 ? 0.1542 0.1864 0.1524 -0.0025 -0.0207 0.0070 364 PHE A C 2814 O O . PHE A 364 ? 0.1525 0.1819 0.1532 0.0108 -0.0246 0.0002 364 PHE A O 2815 C CB . PHE A 364 ? 0.1523 0.2073 0.1642 -0.0224 -0.0086 0.0114 364 PHE A CB 2816 C CG . PHE A 364 ? 0.1600 0.2443 0.1740 -0.0419 -0.0102 0.0080 364 PHE A CG 2817 C CD1 . PHE A 364 ? 0.1475 0.2650 0.1865 -0.0633 -0.0066 0.0256 364 PHE A CD1 2818 C CD2 . PHE A 364 ? 0.1679 0.2981 0.1820 -0.0706 0.0071 -0.0006 364 PHE A CD2 2819 C CE1 . PHE A 364 ? 0.2012 0.3147 0.2083 -0.0687 -0.0079 0.0182 364 PHE A CE1 2820 C CE2 . PHE A 364 ? 0.1725 0.3204 0.1655 -0.0545 -0.0042 0.0116 364 PHE A CE2 2821 C CZ . PHE A 364 ? 0.1806 0.2944 0.1766 -0.0660 -0.0007 0.0061 364 PHE A CZ 2822 N N . GLY A 365 ? 0.1552 0.1912 0.1611 0.0073 -0.0191 0.0010 365 GLY A N 2823 C CA . GLY A 365 ? 0.1604 0.1819 0.1554 0.0115 -0.0215 0.0066 365 GLY A CA 2824 C C . GLY A 365 ? 0.1775 0.1905 0.1755 0.0047 -0.0207 0.0000 365 GLY A C 2825 O O . GLY A 365 ? 0.1746 0.1848 0.1670 0.0142 -0.0179 -0.0185 365 GLY A O 2826 N N . GLY A 366 ? 0.1814 0.1879 0.1744 0.0065 -0.0283 0.0038 366 GLY A N 2827 C CA . GLY A 366 ? 0.1798 0.1820 0.1857 0.0089 -0.0269 -0.0015 366 GLY A CA 2828 C C . GLY A 366 ? 0.1896 0.2019 0.1948 0.0102 -0.0192 0.0035 366 GLY A C 2829 O O . GLY A 366 ? 0.2093 0.1878 0.2157 0.0028 -0.0192 0.0050 366 GLY A O 2830 N N . TYR A 367 ? 0.1769 0.2074 0.1862 0.0104 -0.0211 0.0026 367 TYR A N 2831 C CA . TYR A 367 ? 0.1812 0.1987 0.1845 0.0122 -0.0129 -0.0013 367 TYR A CA 2832 C C . TYR A 367 ? 0.1841 0.2078 0.1881 0.0115 -0.0134 -0.0058 367 TYR A C 2833 O O . TYR A 367 ? 0.1811 0.2152 0.1916 0.0119 -0.0161 -0.0057 367 TYR A O 2834 C CB . TYR A 367 ? 0.1641 0.2011 0.1697 0.0202 -0.0166 -0.0036 367 TYR A CB 2835 C CG . TYR A 367 ? 0.1726 0.2042 0.1721 0.0095 -0.0146 0.0085 367 TYR A CG 2836 C CD1 . TYR A 367 ? 0.1578 0.1825 0.1678 0.0299 -0.0051 -0.0107 367 TYR A CD1 2837 C CD2 . TYR A 367 ? 0.1879 0.1877 0.1809 0.0087 -0.0035 0.0049 367 TYR A CD2 2838 C CE1 . TYR A 367 ? 0.1457 0.1841 0.1717 0.0228 -0.0103 0.0137 367 TYR A CE1 2839 C CE2 . TYR A 367 ? 0.1600 0.1938 0.1648 0.0143 -0.0127 0.0138 367 TYR A CE2 2840 C CZ . TYR A 367 ? 0.1498 0.1934 0.1571 0.0163 -0.0097 0.0018 367 TYR A CZ 2841 O OH . TYR A 367 ? 0.1328 0.2122 0.1616 0.0112 -0.0226 -0.0012 367 TYR A OH 2842 N N . PRO A 368 ? 0.1884 0.2067 0.1827 0.0108 -0.0117 -0.0073 368 PRO A N 2843 C CA . PRO A 368 ? 0.1898 0.2107 0.1885 0.0078 -0.0117 -0.0125 368 PRO A CA 2844 C C . PRO A 368 ? 0.1925 0.2157 0.1939 0.0088 -0.0143 -0.0127 368 PRO A C 2845 O O . PRO A 368 ? 0.1891 0.2090 0.1759 0.0082 -0.0138 -0.0232 368 PRO A O 2846 C CB . PRO A 368 ? 0.1837 0.2129 0.1864 0.0109 -0.0158 -0.0105 368 PRO A CB 2847 C CG . PRO A 368 ? 0.2010 0.2145 0.1936 0.0189 -0.0025 -0.0061 368 PRO A CG 2848 C CD . PRO A 368 ? 0.1869 0.2111 0.1806 0.0126 -0.0038 -0.0053 368 PRO A CD 2849 N N . LEU A 369 ? 0.1939 0.2221 0.2045 0.0136 -0.0112 -0.0129 369 LEU A N 2850 C CA . LEU A 369 ? 0.2003 0.2280 0.2187 0.0119 -0.0094 -0.0099 369 LEU A CA 2851 C C . LEU A 369 ? 0.1931 0.2318 0.2148 0.0135 -0.0090 -0.0116 369 LEU A C 2852 O O . LEU A 369 ? 0.1837 0.2352 0.2015 0.0072 -0.0153 -0.0159 369 LEU A O 2853 C CB . LEU A 369 ? 0.1954 0.2246 0.2283 0.0254 -0.0106 -0.0056 369 LEU A CB 2854 C CG . LEU A 369 ? 0.2203 0.2475 0.2384 0.0287 -0.0051 0.0002 369 LEU A CG 2855 C CD1 . LEU A 369 ? 0.2203 0.2776 0.2832 0.0277 -0.0175 0.0049 369 LEU A CD1 2856 C CD2 . LEU A 369 ? 0.2284 0.2630 0.2492 0.0423 -0.0087 0.0000 369 LEU A CD2 2857 N N . ARG A 370 ? 0.2005 0.2245 0.2107 0.0120 -0.0044 -0.0192 370 ARG A N 2858 C CA . ARG A 370 ? 0.2098 0.2277 0.2077 0.0075 0.0006 -0.0196 370 ARG A CA 2859 C C . ARG A 370 ? 0.2167 0.2390 0.2211 0.0065 -0.0013 -0.0240 370 ARG A C 2860 O O . ARG A 370 ? 0.1976 0.2394 0.2223 0.0164 -0.0011 -0.0267 370 ARG A O 2861 C CB . ARG A 370 ? 0.2248 0.2225 0.2056 0.0103 -0.0068 -0.0224 370 ARG A CB 2862 C CG . ARG A 370 ? 0.2352 0.2167 0.1763 -0.0044 -0.0037 -0.0011 370 ARG A CG 2863 C CD . ARG A 370 ? 0.2566 0.1896 0.1503 0.0340 -0.0112 0.0063 370 ARG A CD 2864 N NE . ARG A 370 ? 0.2554 0.2154 0.1931 0.0230 -0.0234 0.0045 370 ARG A NE 2865 C CZ . ARG A 370 ? 0.2419 0.2135 0.1910 0.0409 -0.0272 0.0081 370 ARG A CZ 2866 N NH1 . ARG A 370 ? 0.2317 0.2101 0.1701 0.0479 0.0010 -0.0009 370 ARG A NH1 2867 N NH2 . ARG A 370 ? 0.2191 0.2325 0.1800 0.0292 -0.0413 0.0276 370 ARG A NH2 2868 N N . GLY A 371 ? 0.2149 0.2410 0.2194 0.0025 0.0042 -0.0177 371 GLY A N 2869 C CA . GLY A 371 ? 0.2226 0.2531 0.2303 0.0031 0.0048 -0.0262 371 GLY A CA 2870 C C . GLY A 371 ? 0.2296 0.2640 0.2347 0.0078 0.0105 -0.0224 371 GLY A C 2871 O O . GLY A 371 ? 0.2250 0.2709 0.2319 0.0084 0.0175 -0.0259 371 GLY A O 2872 N N . SER A 372 ? 0.2248 0.2638 0.2338 0.0074 0.0116 -0.0236 372 SER A N 2873 C CA . SER A 372 ? 0.2291 0.2677 0.2454 0.0097 0.0124 -0.0227 372 SER A CA 2874 C C . SER A 372 ? 0.2164 0.2586 0.2364 0.0060 0.0139 -0.0269 372 SER A C 2875 O O . SER A 372 ? 0.2181 0.2672 0.2430 0.0069 0.0067 -0.0322 372 SER A O 2876 C CB . SER A 372 ? 0.2315 0.2717 0.2519 0.0084 0.0304 -0.0268 372 SER A CB 2877 O OG . SER A 372 ? 0.2960 0.3257 0.3172 0.0087 0.0044 -0.0159 372 SER A OG 2878 N N . SER A 373 ? 0.2056 0.2441 0.2200 0.0081 0.0122 -0.0316 373 SER A N 2879 C CA . SER A 373 ? 0.1925 0.2365 0.2078 0.0098 0.0116 -0.0283 373 SER A CA 2880 C C . SER A 373 ? 0.1951 0.2313 0.2083 0.0097 0.0081 -0.0274 373 SER A C 2881 O O . SER A 373 ? 0.2003 0.2272 0.2033 0.0087 0.0039 -0.0147 373 SER A O 2882 C CB . SER A 373 ? 0.1928 0.2378 0.1980 0.0027 0.0144 -0.0339 373 SER A CB 2883 O OG . SER A 373 ? 0.1681 0.2259 0.1730 0.0075 0.0183 -0.0322 373 SER A OG 2884 N N . ILE A 374 ? 0.1940 0.2188 0.2086 0.0127 0.0080 -0.0270 374 ILE A N 2885 C CA . ILE A 374 ? 0.1882 0.2163 0.1995 0.0183 0.0083 -0.0296 374 ILE A CA 2886 C C . ILE A 374 ? 0.1863 0.2061 0.1928 0.0216 0.0058 -0.0244 374 ILE A C 2887 O O . ILE A 374 ? 0.1821 0.1999 0.1890 0.0350 0.0094 -0.0324 374 ILE A O 2888 C CB . ILE A 374 ? 0.1913 0.2161 0.2045 0.0184 0.0134 -0.0325 374 ILE A CB 2889 C CG1 . ILE A 374 ? 0.2068 0.2287 0.2175 0.0088 0.0171 -0.0472 374 ILE A CG1 2890 C CG2 . ILE A 374 ? 0.1959 0.2279 0.2078 0.0250 -0.0005 -0.0215 374 ILE A CG2 2891 C CD1 . ILE A 374 ? 0.2116 0.2265 0.2000 -0.0042 0.0426 -0.0620 374 ILE A CD1 2892 N N . PHE A 375 ? 0.1835 0.2002 0.1819 0.0226 -0.0015 -0.0208 375 PHE A N 2893 C CA . PHE A 375 ? 0.1906 0.2042 0.1899 0.0193 -0.0074 -0.0128 375 PHE A CA 2894 C C . PHE A 375 ? 0.1911 0.2049 0.1929 0.0154 -0.0111 -0.0083 375 PHE A C 2895 O O . PHE A 375 ? 0.1915 0.2140 0.1945 0.0128 -0.0207 -0.0102 375 PHE A O 2896 C CB . PHE A 375 ? 0.1797 0.1968 0.1709 0.0197 -0.0091 -0.0130 375 PHE A CB 2897 C CG . PHE A 375 ? 0.1892 0.2040 0.1999 0.0217 -0.0079 -0.0139 375 PHE A CG 2898 C CD1 . PHE A 375 ? 0.1688 0.1886 0.1718 0.0428 0.0039 -0.0241 375 PHE A CD1 2899 C CD2 . PHE A 375 ? 0.1859 0.1858 0.1857 0.0270 0.0074 -0.0071 375 PHE A CD2 2900 C CE1 . PHE A 375 ? 0.1813 0.1858 0.1819 0.0414 -0.0094 -0.0160 375 PHE A CE1 2901 C CE2 . PHE A 375 ? 0.1877 0.2014 0.1903 0.0311 -0.0098 -0.0101 375 PHE A CE2 2902 C CZ . PHE A 375 ? 0.1665 0.1890 0.1785 0.0335 0.0017 -0.0214 375 PHE A CZ 2903 N N . GLY A 376 ? 0.1863 0.2075 0.2005 0.0125 -0.0158 -0.0007 376 GLY A N 2904 C CA . GLY A 376 ? 0.1933 0.1956 0.2072 0.0091 -0.0118 0.0097 376 GLY A CA 2905 C C . GLY A 376 ? 0.2009 0.1963 0.2053 0.0139 -0.0123 0.0091 376 GLY A C 2906 O O . GLY A 376 ? 0.1886 0.1757 0.2035 0.0068 -0.0115 0.0120 376 GLY A O 2907 N N . LEU A 377 ? 0.1999 0.1851 0.2096 0.0220 -0.0154 0.0085 377 LEU A N 2908 C CA . LEU A 377 ? 0.2050 0.1904 0.2129 0.0238 -0.0189 0.0095 377 LEU A CA 2909 C C . LEU A 377 ? 0.2085 0.1896 0.2184 0.0263 -0.0197 0.0110 377 LEU A C 2910 O O . LEU A 377 ? 0.2081 0.1851 0.2240 0.0251 -0.0221 0.0087 377 LEU A O 2911 C CB . LEU A 377 ? 0.2034 0.1859 0.2153 0.0269 -0.0143 0.0003 377 LEU A CB 2912 C CG . LEU A 377 ? 0.2162 0.1937 0.2287 0.0250 -0.0276 0.0050 377 LEU A CG 2913 C CD1 . LEU A 377 ? 0.1870 0.1486 0.2194 0.0195 -0.0219 0.0318 377 LEU A CD1 2914 C CD2 . LEU A 377 ? 0.2055 0.1936 0.1948 0.0203 -0.0189 0.0040 377 LEU A CD2 2915 N N . ALA A 378 ? 0.2155 0.2035 0.2141 0.0245 -0.0207 0.0132 378 ALA A N 2916 C CA . ALA A 378 ? 0.2254 0.2149 0.2083 0.0201 -0.0276 0.0109 378 ALA A CA 2917 C C . ALA A 378 ? 0.2386 0.2241 0.2196 0.0178 -0.0231 0.0120 378 ALA A C 2918 O O . ALA A 378 ? 0.2492 0.2260 0.2232 0.0180 -0.0274 0.0175 378 ALA A O 2919 C CB . ALA A 378 ? 0.2231 0.2175 0.2057 0.0193 -0.0228 0.0037 378 ALA A CB 2920 N N . PRO A 379 ? 0.2464 0.2373 0.2186 0.0154 -0.0285 0.0134 379 PRO A N 2921 C CA . PRO A 379 ? 0.2597 0.2417 0.2316 0.0151 -0.0310 0.0150 379 PRO A CA 2922 C C . PRO A 379 ? 0.2713 0.2532 0.2392 0.0131 -0.0328 0.0183 379 PRO A C 2923 O O . PRO A 379 ? 0.2740 0.2666 0.2482 0.0062 -0.0269 0.0224 379 PRO A O 2924 C CB . PRO A 379 ? 0.2595 0.2397 0.2288 0.0161 -0.0366 0.0137 379 PRO A CB 2925 C CG . PRO A 379 ? 0.2613 0.2299 0.2295 0.0142 -0.0371 0.0177 379 PRO A CG 2926 C CD . PRO A 379 ? 0.2447 0.2252 0.2195 0.0183 -0.0268 0.0107 379 PRO A CD 2927 N N . GLY A 380 ? 0.2830 0.2590 0.2499 0.0109 -0.0356 0.0175 380 GLY A N 2928 C CA . GLY A 380 ? 0.2882 0.2639 0.2565 0.0058 -0.0350 0.0236 380 GLY A CA 2929 C C . GLY A 380 ? 0.2848 0.2656 0.2701 0.0083 -0.0349 0.0306 380 GLY A C 2930 O O . GLY A 380 ? 0.3083 0.2768 0.2794 -0.0028 -0.0375 0.0304 380 GLY A O 2931 N N . LYS A 381 ? 0.2745 0.2639 0.2669 0.0145 -0.0275 0.0315 381 LYS A N 2932 C CA . LYS A 381 ? 0.2512 0.2580 0.2712 0.0188 -0.0254 0.0316 381 LYS A CA 2933 C C . LYS A 381 ? 0.2406 0.2398 0.2613 0.0234 -0.0259 0.0323 381 LYS A C 2934 O O . LYS A 381 ? 0.2293 0.2451 0.2706 0.0246 -0.0313 0.0326 381 LYS A O 2935 C CB . LYS A 381 ? 0.2527 0.2669 0.2804 0.0233 -0.0187 0.0324 381 LYS A CB 2936 C CG . LYS A 381 ? 0.2676 0.3297 0.3104 0.0295 -0.0120 0.0320 381 LYS A CG 2937 C CD . LYS A 381 ? 0.2849 0.3994 0.3847 0.0383 0.0187 0.0388 381 LYS A CD 2938 C CE . LYS A 381 ? 0.3502 0.4505 0.4043 0.0354 0.0370 0.0271 381 LYS A CE 2939 N NZ . LYS A 381 ? 0.3564 0.4602 0.4284 0.0379 0.0511 0.0339 381 LYS A NZ 2940 N N . ALA A 382 ? 0.2256 0.2280 0.2523 0.0255 -0.0271 0.0344 382 ALA A N 2941 C CA . ALA A 382 ? 0.2210 0.2181 0.2450 0.0282 -0.0225 0.0323 382 ALA A CA 2942 C C . ALA A 382 ? 0.2209 0.2211 0.2461 0.0260 -0.0232 0.0324 382 ALA A C 2943 O O . ALA A 382 ? 0.2108 0.2108 0.2389 0.0260 -0.0306 0.0362 382 ALA A O 2944 C CB . ALA A 382 ? 0.2115 0.2145 0.2447 0.0354 -0.0268 0.0385 382 ALA A CB 2945 N N . ARG A 383 ? 0.2278 0.2264 0.2490 0.0219 -0.0213 0.0365 383 ARG A N 2946 C CA . ARG A 383 ? 0.2417 0.2396 0.2520 0.0233 -0.0192 0.0368 383 ARG A CA 2947 C C . ARG A 383 ? 0.2522 0.2392 0.2575 0.0228 -0.0144 0.0422 383 ARG A C 2948 O O . ARG A 383 ? 0.2600 0.2553 0.2579 0.0211 -0.0203 0.0433 383 ARG A O 2949 C CB . ARG A 383 ? 0.2405 0.2381 0.2564 0.0259 -0.0172 0.0438 383 ARG A CB 2950 C CG . ARG A 383 ? 0.2606 0.2953 0.2657 0.0267 -0.0264 0.0263 383 ARG A CG 2951 C CD . ARG A 383 ? 0.3230 0.3430 0.3148 0.0260 -0.0184 0.0116 383 ARG A CD 2952 N NE . ARG A 383 ? 0.3437 0.3701 0.3203 0.0272 -0.0207 0.0290 383 ARG A NE 2953 C CZ . ARG A 383 ? 0.3528 0.3794 0.3416 0.0441 -0.0290 0.0119 383 ARG A CZ 2954 N NH1 . ARG A 383 ? 0.3550 0.3700 0.3215 0.0359 -0.0057 0.0231 383 ARG A NH1 2955 N NH2 . ARG A 383 ? 0.3755 0.4031 0.3633 0.0463 -0.0370 0.0085 383 ARG A NH2 2956 N N . ASP A 384 ? 0.2626 0.2366 0.2614 0.0239 -0.0074 0.0401 384 ASP A N 2957 C CA . ASP A 384 ? 0.2750 0.2280 0.2660 0.0271 -0.0030 0.0451 384 ASP A CA 2958 C C . ASP A 384 ? 0.2851 0.2336 0.2732 0.0316 -0.0011 0.0475 384 ASP A C 2959 O O . ASP A 384 ? 0.2899 0.2436 0.2788 0.0346 0.0014 0.0524 384 ASP A O 2960 C CB . ASP A 384 ? 0.2828 0.2227 0.2680 0.0283 -0.0064 0.0424 384 ASP A CB 2961 C CG . ASP A 384 ? 0.2740 0.1875 0.2625 0.0239 0.0001 0.0395 384 ASP A CG 2962 O OD1 . ASP A 384 ? 0.2790 0.1706 0.2781 0.0534 0.0039 0.0014 384 ASP A OD1 2963 O OD2 . ASP A 384 ? 0.2801 0.1476 0.2806 0.0273 -0.0009 0.0353 384 ASP A OD2 2964 N N . ARG A 385 ? 0.2879 0.2350 0.2777 0.0338 0.0004 0.0533 385 ARG A N 2965 C CA . ARG A 385 ? 0.2955 0.2420 0.2954 0.0345 0.0048 0.0497 385 ARG A CA 2966 C C . ARG A 385 ? 0.2905 0.2342 0.2904 0.0349 0.0041 0.0455 385 ARG A C 2967 O O . ARG A 385 ? 0.2947 0.2395 0.2940 0.0456 0.0047 0.0483 385 ARG A O 2968 C CB . ARG A 385 ? 0.3035 0.2586 0.3037 0.0368 0.0027 0.0476 385 ARG A CB 2969 C CG . ARG A 385 ? 0.3356 0.2991 0.3431 0.0327 0.0070 0.0438 385 ARG A CG 2970 C CD . ARG A 385 ? 0.4222 0.4195 0.4265 0.0194 0.0096 0.0382 385 ARG A CD 2971 N NE . ARG A 385 ? 0.4811 0.4720 0.4807 0.0147 0.0087 0.0319 385 ARG A NE 2972 C CZ . ARG A 385 ? 0.5214 0.5280 0.5241 0.0219 0.0141 0.0284 385 ARG A CZ 2973 N NH1 . ARG A 385 ? 0.5134 0.5574 0.5374 0.0221 0.0125 0.0267 385 ARG A NH1 2974 N NH2 . ARG A 385 ? 0.5733 0.5520 0.5439 0.0284 0.0273 0.0221 385 ARG A NH2 2975 N N . LYS A 386 ? 0.2862 0.2068 0.2869 0.0308 0.0053 0.0402 386 LYS A N 2976 C CA . LYS A 386 ? 0.2856 0.1902 0.2885 0.0271 0.0038 0.0294 386 LYS A CA 2977 C C . LYS A 386 ? 0.2667 0.1776 0.2756 0.0276 0.0013 0.0322 386 LYS A C 2978 O O . LYS A 386 ? 0.2567 0.1636 0.2645 0.0389 0.0016 0.0314 386 LYS A O 2979 C CB . LYS A 386 ? 0.2925 0.1898 0.2974 0.0209 0.0013 0.0291 386 LYS A CB 2980 C CG . LYS A 386 ? 0.3389 0.2113 0.3362 0.0218 0.0016 0.0199 386 LYS A CG 2981 C CD . LYS A 386 ? 0.3762 0.2740 0.4099 0.0157 0.0064 0.0261 386 LYS A CD 2982 C CE . LYS A 386 ? 0.4273 0.3412 0.4602 0.0267 0.0303 0.0307 386 LYS A CE 2983 N NZ . LYS A 386 ? 0.4589 0.3801 0.4952 0.0418 0.0364 0.0283 386 LYS A NZ 2984 N N . ALA A 387 ? 0.2430 0.1699 0.2579 0.0299 0.0036 0.0251 387 ALA A N 2985 C CA . ALA A 387 ? 0.2352 0.1724 0.2555 0.0230 0.0010 0.0256 387 ALA A CA 2986 C C . ALA A 387 ? 0.2238 0.1727 0.2443 0.0176 0.0023 0.0223 387 ALA A C 2987 O O . ALA A 387 ? 0.2278 0.1696 0.2382 0.0245 -0.0034 0.0211 387 ALA A O 2988 C CB . ALA A 387 ? 0.2242 0.1839 0.2568 0.0194 0.0054 0.0248 387 ALA A CB 2989 N N . TYR A 388 ? 0.2066 0.1655 0.2210 0.0139 0.0075 0.0202 388 TYR A N 2990 C CA . TYR A 388 ? 0.2050 0.1731 0.2081 0.0031 0.0025 0.0214 388 TYR A CA 2991 C C . TYR A 388 ? 0.1951 0.1677 0.2006 -0.0010 0.0009 0.0180 388 TYR A C 2992 O O . TYR A 388 ? 0.2157 0.1839 0.2083 0.0006 -0.0114 0.0280 388 TYR A O 2993 C CB . TYR A 388 ? 0.1936 0.1821 0.2025 -0.0056 0.0122 0.0241 388 TYR A CB 2994 C CG . TYR A 388 ? 0.1971 0.2028 0.2185 -0.0118 0.0132 0.0317 388 TYR A CG 2995 C CD1 . TYR A 388 ? 0.2096 0.2197 0.2219 -0.0239 0.0114 0.0293 388 TYR A CD1 2996 C CD2 . TYR A 388 ? 0.1916 0.2261 0.2233 -0.0178 0.0165 0.0267 388 TYR A CD2 2997 C CE1 . TYR A 388 ? 0.2088 0.2374 0.2144 -0.0271 0.0005 0.0378 388 TYR A CE1 2998 C CE2 . TYR A 388 ? 0.1867 0.2359 0.2111 -0.0237 0.0154 0.0242 388 TYR A CE2 2999 C CZ . TYR A 388 ? 0.2164 0.2453 0.2222 -0.0198 0.0224 0.0171 388 TYR A CZ 3000 O OH . TYR A 388 ? 0.2396 0.2721 0.2407 -0.0352 0.0228 0.0225 388 TYR A OH 3001 N N . THR A 389 ? 0.1953 0.1581 0.1922 0.0040 -0.0004 0.0106 389 THR A N 3002 C CA . THR A 389 ? 0.1896 0.1498 0.1800 0.0042 0.0000 -0.0005 389 THR A CA 3003 C C . THR A 389 ? 0.1854 0.1536 0.1791 0.0038 -0.0055 0.0022 389 THR A C 3004 O O . THR A 389 ? 0.1770 0.1417 0.1827 0.0053 -0.0086 -0.0003 389 THR A O 3005 C CB . THR A 389 ? 0.1851 0.1481 0.1838 0.0055 -0.0010 -0.0056 389 THR A CB 3006 O OG1 . THR A 389 ? 0.1812 0.1498 0.1724 0.0246 0.0064 0.0035 389 THR A OG1 3007 C CG2 . THR A 389 ? 0.1708 0.1471 0.1600 0.0139 0.0047 -0.0265 389 THR A CG2 3008 N N . VAL A 390 ? 0.1776 0.1634 0.1666 -0.0021 -0.0125 0.0032 390 VAL A N 3009 C CA . VAL A 390 ? 0.1703 0.1724 0.1692 -0.0025 -0.0209 0.0051 390 VAL A CA 3010 C C . VAL A 390 ? 0.1648 0.1658 0.1638 -0.0044 -0.0184 0.0072 390 VAL A C 3011 O O . VAL A 390 ? 0.1636 0.1671 0.1669 -0.0060 -0.0190 0.0050 390 VAL A O 3012 C CB . VAL A 390 ? 0.1766 0.1935 0.1682 -0.0033 -0.0224 0.0051 390 VAL A CB 3013 C CG1 . VAL A 390 ? 0.1485 0.1883 0.1773 0.0089 -0.0234 -0.0141 390 VAL A CG1 3014 C CG2 . VAL A 390 ? 0.1868 0.2305 0.1971 -0.0146 -0.0256 0.0088 390 VAL A CG2 3015 N N . LEU A 391 ? 0.1597 0.1612 0.1526 -0.0018 -0.0245 0.0070 391 LEU A N 3016 C CA . LEU A 391 ? 0.1566 0.1487 0.1436 -0.0021 -0.0189 0.0060 391 LEU A CA 3017 C C . LEU A 391 ? 0.1634 0.1505 0.1404 -0.0022 -0.0190 0.0042 391 LEU A C 3018 O O . LEU A 391 ? 0.1673 0.1470 0.1390 -0.0034 -0.0094 -0.0029 391 LEU A O 3019 C CB . LEU A 391 ? 0.1527 0.1335 0.1364 0.0025 -0.0169 0.0071 391 LEU A CB 3020 C CG . LEU A 391 ? 0.1399 0.1126 0.1115 -0.0040 -0.0088 -0.0011 391 LEU A CG 3021 C CD1 . LEU A 391 ? 0.1494 0.1138 0.1108 -0.0092 0.0082 -0.0076 391 LEU A CD1 3022 C CD2 . LEU A 391 ? 0.1356 0.0799 0.1179 0.0044 0.0055 0.0098 391 LEU A CD2 3023 N N . LEU A 392 ? 0.1648 0.1480 0.1426 -0.0046 -0.0245 0.0045 392 LEU A N 3024 C CA . LEU A 392 ? 0.1659 0.1458 0.1421 -0.0054 -0.0284 -0.0036 392 LEU A CA 3025 C C . LEU A 392 ? 0.1624 0.1480 0.1411 -0.0068 -0.0250 -0.0045 392 LEU A C 3026 O O . LEU A 392 ? 0.1514 0.1438 0.1455 -0.0115 -0.0265 -0.0148 392 LEU A O 3027 C CB . LEU A 392 ? 0.1670 0.1394 0.1392 -0.0038 -0.0300 -0.0056 392 LEU A CB 3028 C CG . LEU A 392 ? 0.1865 0.1227 0.1246 -0.0014 -0.0431 -0.0213 392 LEU A CG 3029 C CD1 . LEU A 392 ? 0.1933 0.1433 0.1074 -0.0201 -0.0537 -0.0272 392 LEU A CD1 3030 C CD2 . LEU A 392 ? 0.2093 0.1240 0.1239 0.0090 -0.0358 -0.0445 392 LEU A CD2 3031 N N . TYR A 393 ? 0.1610 0.1439 0.1383 -0.0115 -0.0263 -0.0113 393 TYR A N 3032 C CA . TYR A 393 ? 0.1718 0.1420 0.1470 -0.0043 -0.0204 -0.0054 393 TYR A CA 3033 C C . TYR A 393 ? 0.1643 0.1476 0.1547 -0.0053 -0.0163 -0.0098 393 TYR A C 3034 O O . TYR A 393 ? 0.1612 0.1353 0.1656 -0.0002 -0.0096 -0.0045 393 TYR A O 3035 C CB . TYR A 393 ? 0.1713 0.1375 0.1274 -0.0034 -0.0196 -0.0089 393 TYR A CB 3036 C CG . TYR A 393 ? 0.1730 0.1454 0.1218 -0.0045 -0.0208 0.0035 393 TYR A CG 3037 C CD1 . TYR A 393 ? 0.1591 0.1278 0.1111 0.0034 -0.0259 0.0067 393 TYR A CD1 3038 C CD2 . TYR A 393 ? 0.1631 0.1442 0.0881 -0.0057 -0.0189 0.0075 393 TYR A CD2 3039 C CE1 . TYR A 393 ? 0.1619 0.1156 0.0891 -0.0063 -0.0195 0.0026 393 TYR A CE1 3040 C CE2 . TYR A 393 ? 0.1800 0.1496 0.1149 -0.0102 -0.0290 -0.0004 393 TYR A CE2 3041 C CZ . TYR A 393 ? 0.1688 0.1280 0.0947 -0.0014 -0.0255 0.0049 393 TYR A CZ 3042 O OH . TYR A 393 ? 0.1678 0.1383 0.1160 -0.0049 -0.0069 -0.0003 393 TYR A OH 3043 N N . GLY A 394 ? 0.1552 0.1486 0.1673 0.0000 -0.0264 -0.0077 394 GLY A N 3044 C CA . GLY A 394 ? 0.1687 0.1487 0.1733 -0.0090 -0.0219 -0.0072 394 GLY A CA 3045 C C . GLY A 394 ? 0.1719 0.1462 0.1808 -0.0035 -0.0180 -0.0082 394 GLY A C 3046 O O . GLY A 394 ? 0.1691 0.1427 0.1878 -0.0055 -0.0193 -0.0034 394 GLY A O 3047 N N . ASN A 395 ? 0.1586 0.1366 0.1645 -0.0016 -0.0203 -0.0077 395 ASN A N 3048 C CA . ASN A 395 ? 0.1659 0.1475 0.1633 -0.0060 -0.0116 -0.0049 395 ASN A CA 3049 C C . ASN A 395 ? 0.1754 0.1556 0.1755 -0.0055 -0.0097 -0.0060 395 ASN A C 3050 O O . ASN A 395 ? 0.1617 0.1592 0.1769 -0.0242 -0.0023 -0.0011 395 ASN A O 3051 C CB . ASN A 395 ? 0.1580 0.1374 0.1510 -0.0065 -0.0260 -0.0025 395 ASN A CB 3052 C CG . ASN A 395 ? 0.1699 0.1473 0.1576 -0.0038 -0.0225 -0.0064 395 ASN A CG 3053 O OD1 . ASN A 395 ? 0.1518 0.1076 0.1375 -0.0171 -0.0224 0.0076 395 ASN A OD1 3054 N ND2 . ASN A 395 ? 0.1661 0.1784 0.1391 -0.0100 -0.0433 -0.0234 395 ASN A ND2 3055 N N . GLY A 396 ? 0.1777 0.1451 0.1704 0.0005 0.0005 -0.0144 396 GLY A N 3056 C CA . GLY A 396 ? 0.1958 0.1427 0.1748 0.0028 0.0084 -0.0054 396 GLY A CA 3057 C C . GLY A 396 ? 0.2055 0.1375 0.1697 0.0031 0.0090 -0.0069 396 GLY A C 3058 O O . GLY A 396 ? 0.2062 0.1401 0.1780 0.0069 0.0150 -0.0100 396 GLY A O 3059 N N . PRO A 397 ? 0.2137 0.1385 0.1817 0.0028 0.0077 -0.0080 397 PRO A N 3060 C CA . PRO A 397 ? 0.2233 0.1425 0.1876 0.0023 0.0053 -0.0041 397 PRO A CA 3061 C C . PRO A 397 ? 0.2231 0.1426 0.1938 0.0060 -0.0003 0.0009 397 PRO A C 3062 O O . PRO A 397 ? 0.2305 0.1711 0.2032 0.0057 -0.0058 0.0011 397 PRO A O 3063 C CB . PRO A 397 ? 0.2298 0.1321 0.1791 -0.0007 0.0083 -0.0043 397 PRO A CB 3064 C CG . PRO A 397 ? 0.2350 0.1331 0.1865 -0.0009 0.0142 -0.0151 397 PRO A CG 3065 C CD . PRO A 397 ? 0.2212 0.1298 0.1698 -0.0023 0.0177 -0.0046 397 PRO A CD 3066 N N . GLY A 398 ? 0.2254 0.1495 0.1997 0.0034 -0.0035 0.0067 398 GLY A N 3067 C CA . GLY A 398 ? 0.2275 0.1424 0.2124 0.0053 -0.0070 -0.0014 398 GLY A CA 3068 C C . GLY A 398 ? 0.2360 0.1492 0.2227 0.0031 -0.0082 -0.0104 398 GLY A C 3069 O O . GLY A 398 ? 0.2341 0.1495 0.2308 -0.0002 -0.0158 -0.0044 398 GLY A O 3070 N N . TYR A 399 ? 0.2470 0.1452 0.2289 0.0035 -0.0046 -0.0159 399 TYR A N 3071 C CA . TYR A 399 ? 0.2630 0.1474 0.2450 0.0029 -0.0027 -0.0179 399 TYR A CA 3072 C C . TYR A 399 ? 0.2744 0.1591 0.2636 0.0101 0.0007 -0.0189 399 TYR A C 3073 O O . TYR A 399 ? 0.2713 0.1429 0.2608 0.0171 0.0012 -0.0230 399 TYR A O 3074 C CB . TYR A 399 ? 0.2608 0.1487 0.2466 0.0009 0.0015 -0.0141 399 TYR A CB 3075 C CG . TYR A 399 ? 0.2649 0.1424 0.2360 -0.0112 -0.0063 -0.0089 399 TYR A CG 3076 C CD1 . TYR A 399 ? 0.2790 0.1303 0.2231 0.0039 -0.0117 0.0002 399 TYR A CD1 3077 C CD2 . TYR A 399 ? 0.2575 0.1344 0.2459 -0.0164 -0.0181 -0.0097 399 TYR A CD2 3078 C CE1 . TYR A 399 ? 0.2948 0.1754 0.2516 -0.0118 -0.0026 -0.0127 399 TYR A CE1 3079 C CE2 . TYR A 399 ? 0.2493 0.1318 0.2321 -0.0190 -0.0123 -0.0055 399 TYR A CE2 3080 C CZ . TYR A 399 ? 0.2940 0.1635 0.2397 -0.0137 -0.0034 -0.0021 399 TYR A CZ 3081 O OH . TYR A 399 ? 0.3086 0.1374 0.2777 -0.0325 0.0204 -0.0020 399 TYR A OH 3082 N N . VAL A 400 ? 0.2975 0.1764 0.2838 0.0119 -0.0013 -0.0165 400 VAL A N 3083 C CA . VAL A 400 ? 0.3359 0.2045 0.3258 0.0157 -0.0036 -0.0145 400 VAL A CA 3084 C C . VAL A 400 ? 0.3665 0.2329 0.3510 0.0172 -0.0089 -0.0135 400 VAL A C 3085 O O . VAL A 400 ? 0.3600 0.2002 0.3432 0.0121 -0.0154 -0.0176 400 VAL A O 3086 C CB . VAL A 400 ? 0.3402 0.2039 0.3349 0.0221 -0.0017 -0.0161 400 VAL A CB 3087 C CG1 . VAL A 400 ? 0.3513 0.2069 0.3587 0.0203 -0.0028 -0.0339 400 VAL A CG1 3088 C CG2 . VAL A 400 ? 0.3347 0.2073 0.3333 0.0135 0.0087 -0.0079 400 VAL A CG2 3089 N N . LEU A 401 ? 0.4058 0.2726 0.3846 0.0114 -0.0171 -0.0114 401 LEU A N 3090 C CA . LEU A 401 ? 0.4483 0.3282 0.4238 0.0137 -0.0189 -0.0112 401 LEU A CA 3091 C C . LEU A 401 ? 0.4778 0.3578 0.4485 0.0114 -0.0234 -0.0087 401 LEU A C 3092 O O . LEU A 401 ? 0.4980 0.3689 0.4598 0.0169 -0.0265 -0.0044 401 LEU A O 3093 C CB . LEU A 401 ? 0.4452 0.3278 0.4249 0.0093 -0.0206 -0.0091 401 LEU A CB 3094 C CG . LEU A 401 ? 0.4558 0.3221 0.4336 0.0127 -0.0254 -0.0268 401 LEU A CG 3095 C CD1 . LEU A 401 ? 0.4537 0.3380 0.4506 0.0038 -0.0336 -0.0462 401 LEU A CD1 3096 C CD2 . LEU A 401 ? 0.4626 0.3174 0.4657 0.0092 -0.0344 -0.0430 401 LEU A CD2 3097 N N . LYS A 402 ? 0.5024 0.3936 0.4708 0.0101 -0.0205 -0.0049 402 LYS A N 3098 C CA . LYS A 402 ? 0.5264 0.4206 0.4911 0.0037 -0.0181 -0.0027 402 LYS A CA 3099 C C . LYS A 402 ? 0.5380 0.4318 0.5018 -0.0001 -0.0197 -0.0024 402 LYS A C 3100 O O . LYS A 402 ? 0.5501 0.4297 0.5022 0.0023 -0.0223 -0.0049 402 LYS A O 3101 C CB . LYS A 402 ? 0.5311 0.4279 0.4928 0.0012 -0.0145 -0.0006 402 LYS A CB 3102 C CG . LYS A 402 ? 0.5594 0.4588 0.5289 -0.0018 -0.0119 -0.0100 402 LYS A CG 3103 C CD . LYS A 402 ? 0.5973 0.5061 0.5634 -0.0223 -0.0022 -0.0137 402 LYS A CD 3104 C CE . LYS A 402 ? 0.6264 0.5176 0.5903 -0.0286 -0.0157 -0.0317 402 LYS A CE 3105 N NZ . LYS A 402 ? 0.6675 0.5506 0.6256 -0.0319 -0.0061 -0.0354 402 LYS A NZ 3106 N N . ASP A 403 ? 0.5455 0.4378 0.5086 -0.0037 -0.0206 -0.0009 403 ASP A N 3107 C CA . ASP A 403 ? 0.5487 0.4471 0.5170 -0.0058 -0.0214 0.0005 403 ASP A CA 3108 C C . ASP A 403 ? 0.5440 0.4381 0.5062 -0.0086 -0.0215 0.0003 403 ASP A C 3109 O O . ASP A 403 ? 0.5570 0.4392 0.5106 -0.0109 -0.0262 0.0017 403 ASP A O 3110 C CB . ASP A 403 ? 0.5536 0.4546 0.5247 -0.0054 -0.0226 0.0023 403 ASP A CB 3111 C CG . ASP A 403 ? 0.5741 0.4695 0.5612 -0.0113 -0.0304 0.0036 403 ASP A CG 3112 O OD1 . ASP A 403 ? 0.5941 0.4788 0.6094 -0.0242 -0.0326 0.0093 403 ASP A OD1 3113 O OD2 . ASP A 403 ? 0.6039 0.4946 0.6155 -0.0265 -0.0456 0.0067 403 ASP A OD2 3114 N N . GLY A 404 ? 0.5292 0.4186 0.4962 -0.0107 -0.0196 -0.0031 404 GLY A N 3115 C CA . GLY A 404 ? 0.5105 0.3924 0.4739 -0.0193 -0.0162 -0.0029 404 GLY A CA 3116 C C . GLY A 404 ? 0.4946 0.3730 0.4568 -0.0197 -0.0167 -0.0017 404 GLY A C 3117 O O . GLY A 404 ? 0.5020 0.3621 0.4673 -0.0181 -0.0112 -0.0001 404 GLY A O 3118 N N . ALA A 405 ? 0.4739 0.3521 0.4350 -0.0233 -0.0210 -0.0011 405 ALA A N 3119 C CA . ALA A 405 ? 0.4480 0.3251 0.4060 -0.0229 -0.0269 -0.0021 405 ALA A CA 3120 C C . ALA A 405 ? 0.4287 0.3015 0.3759 -0.0188 -0.0276 -0.0036 405 ALA A C 3121 O O . ALA A 405 ? 0.4362 0.2926 0.3723 -0.0207 -0.0373 -0.0131 405 ALA A O 3122 C CB . ALA A 405 ? 0.4495 0.3291 0.4113 -0.0241 -0.0278 0.0076 405 ALA A CB 3123 N N . ARG A 406 ? 0.3985 0.2781 0.3408 -0.0198 -0.0301 -0.0091 406 ARG A N 3124 C CA . ARG A 406 ? 0.3558 0.2584 0.3146 -0.0121 -0.0317 -0.0194 406 ARG A CA 3125 C C . ARG A 406 ? 0.3574 0.2653 0.3109 -0.0103 -0.0324 -0.0163 406 ARG A C 3126 O O . ARG A 406 ? 0.3654 0.2634 0.3156 -0.0094 -0.0326 -0.0224 406 ARG A O 3127 C CB . ARG A 406 ? 0.3446 0.2491 0.3114 -0.0124 -0.0345 -0.0208 406 ARG A CB 3128 C CG . ARG A 406 ? 0.3185 0.2320 0.2827 -0.0129 -0.0343 -0.0281 406 ARG A CG 3129 C CD . ARG A 406 ? 0.3156 0.2260 0.2787 -0.0086 -0.0363 -0.0278 406 ARG A CD 3130 N NE . ARG A 406 ? 0.2460 0.1927 0.2285 0.0007 -0.0305 -0.0355 406 ARG A NE 3131 C CZ . ARG A 406 ? 0.2183 0.1797 0.2120 0.0087 -0.0257 -0.0163 406 ARG A CZ 3132 N NH1 . ARG A 406 ? 0.1830 0.1568 0.1734 0.0397 -0.0228 -0.0066 406 ARG A NH1 3133 N NH2 . ARG A 406 ? 0.2204 0.1783 0.1928 0.0117 -0.0183 -0.0032 406 ARG A NH2 3134 N N . PRO A 407 ? 0.3490 0.2674 0.3118 -0.0041 -0.0291 -0.0099 407 PRO A N 3135 C CA . PRO A 407 ? 0.3393 0.2737 0.3065 0.0003 -0.0274 -0.0049 407 PRO A CA 3136 C C . PRO A 407 ? 0.3382 0.2735 0.3060 0.0065 -0.0222 -0.0020 407 PRO A C 3137 O O . PRO A 407 ? 0.3276 0.2669 0.3112 0.0073 -0.0229 0.0010 407 PRO A O 3138 C CB . PRO A 407 ? 0.3441 0.2872 0.3121 0.0036 -0.0303 -0.0082 407 PRO A CB 3139 C CG . PRO A 407 ? 0.3441 0.2878 0.3232 0.0043 -0.0325 -0.0067 407 PRO A CG 3140 C CD . PRO A 407 ? 0.3424 0.2724 0.2963 -0.0053 -0.0332 -0.0097 407 PRO A CD 3141 N N . ASP A 408 ? 0.3267 0.2640 0.2989 0.0120 -0.0200 0.0002 408 ASP A N 3142 C CA . ASP A 408 ? 0.3266 0.2700 0.3047 0.0174 -0.0158 0.0060 408 ASP A CA 3143 C C . ASP A 408 ? 0.3242 0.2671 0.3014 0.0208 -0.0105 0.0053 408 ASP A C 3144 O O . ASP A 408 ? 0.3371 0.2727 0.3028 0.0191 -0.0098 0.0055 408 ASP A O 3145 C CB . ASP A 408 ? 0.3227 0.2751 0.3118 0.0191 -0.0223 0.0037 408 ASP A CB 3146 C CG . ASP A 408 ? 0.3402 0.2764 0.3561 0.0238 -0.0340 0.0068 408 ASP A CG 3147 O OD1 . ASP A 408 ? 0.3241 0.2547 0.3825 0.0313 -0.0398 -0.0091 408 ASP A OD1 3148 O OD2 . ASP A 408 ? 0.3534 0.3307 0.4323 0.0245 -0.0534 0.0003 408 ASP A OD2 3149 N N . VAL A 409 ? 0.3125 0.2544 0.2906 0.0271 -0.0028 0.0050 409 VAL A N 3150 C CA . VAL A 409 ? 0.3076 0.2468 0.2917 0.0314 0.0046 0.0095 409 VAL A CA 3151 C C . VAL A 409 ? 0.3056 0.2479 0.2931 0.0372 0.0118 0.0066 409 VAL A C 3152 O O . VAL A 409 ? 0.2932 0.2524 0.2858 0.0355 0.0069 0.0121 409 VAL A O 3153 C CB . VAL A 409 ? 0.3149 0.2504 0.2857 0.0310 0.0020 0.0106 409 VAL A CB 3154 C CG1 . VAL A 409 ? 0.3365 0.2451 0.3181 0.0270 0.0231 0.0169 409 VAL A CG1 3155 C CG2 . VAL A 409 ? 0.2857 0.2315 0.2932 0.0271 -0.0006 0.0282 409 VAL A CG2 3156 N N . THR A 410 ? 0.3091 0.2471 0.2915 0.0463 0.0179 -0.0012 410 THR A N 3157 C CA . THR A 410 ? 0.3019 0.2543 0.2958 0.0481 0.0231 -0.0082 410 THR A CA 3158 C C . THR A 410 ? 0.2989 0.2649 0.2970 0.0472 0.0267 -0.0132 410 THR A C 3159 O O . THR A 410 ? 0.2876 0.2544 0.2893 0.0482 0.0304 -0.0118 410 THR A O 3160 C CB . THR A 410 ? 0.3157 0.2571 0.3036 0.0479 0.0219 -0.0059 410 THR A CB 3161 O OG1 . THR A 410 ? 0.3144 0.2496 0.3120 0.0562 0.0234 -0.0148 410 THR A OG1 3162 C CG2 . THR A 410 ? 0.3178 0.2455 0.3223 0.0541 0.0250 -0.0046 410 THR A CG2 3163 N N . GLU A 411 ? 0.2940 0.2790 0.3023 0.0490 0.0271 -0.0179 411 GLU A N 3164 C CA . GLU A 411 ? 0.2963 0.2941 0.3095 0.0499 0.0297 -0.0226 411 GLU A CA 3165 C C . GLU A 411 ? 0.2936 0.2929 0.3086 0.0562 0.0341 -0.0252 411 GLU A C 3166 O O . GLU A 411 ? 0.2926 0.2848 0.3133 0.0610 0.0399 -0.0268 411 GLU A O 3167 C CB . GLU A 411 ? 0.2869 0.2984 0.3113 0.0505 0.0293 -0.0219 411 GLU A CB 3168 C CG . GLU A 411 ? 0.2927 0.3291 0.3183 0.0332 0.0286 -0.0210 411 GLU A CG 3169 C CD . GLU A 411 ? 0.2778 0.3463 0.3128 0.0319 0.0450 -0.0058 411 GLU A CD 3170 O OE1 . GLU A 411 ? 0.2287 0.3367 0.3329 -0.0046 0.0647 0.0088 411 GLU A OE1 3171 O OE2 . GLU A 411 ? 0.3039 0.3925 0.3254 0.0319 0.0450 -0.0285 411 GLU A OE2 3172 N N . SER A 412 ? 0.2967 0.2914 0.3082 0.0602 0.0355 -0.0273 412 SER A N 3173 C CA . SER A 412 ? 0.2982 0.2974 0.3088 0.0649 0.0356 -0.0293 412 SER A CA 3174 C C . SER A 412 ? 0.2910 0.2844 0.2958 0.0651 0.0361 -0.0254 412 SER A C 3175 O O . SER A 412 ? 0.2862 0.2913 0.2898 0.0645 0.0432 -0.0247 412 SER A O 3176 C CB . SER A 412 ? 0.3055 0.3089 0.2979 0.0704 0.0357 -0.0339 412 SER A CB 3177 O OG . SER A 412 ? 0.3412 0.3616 0.3793 0.0730 0.0455 -0.0334 412 SER A OG 3178 N N . GLU A 413 ? 0.2802 0.2607 0.2758 0.0648 0.0407 -0.0227 413 GLU A N 3179 C CA . GLU A 413 ? 0.2937 0.2563 0.2786 0.0558 0.0356 -0.0175 413 GLU A CA 3180 C C . GLU A 413 ? 0.2728 0.2316 0.2627 0.0545 0.0306 -0.0189 413 GLU A C 3181 O O . GLU A 413 ? 0.2688 0.2221 0.2407 0.0538 0.0303 -0.0192 413 GLU A O 3182 C CB . GLU A 413 ? 0.3062 0.2500 0.2821 0.0587 0.0377 -0.0125 413 GLU A CB 3183 C CG . GLU A 413 ? 0.3823 0.3162 0.3458 0.0542 0.0586 -0.0071 413 GLU A CG 3184 C CD . GLU A 413 ? 0.4583 0.3635 0.4324 0.0693 0.0768 0.0064 413 GLU A CD 3185 O OE1 . GLU A 413 ? 0.5189 0.3965 0.4254 0.0546 0.1066 -0.0178 413 GLU A OE1 3186 O OE2 . GLU A 413 ? 0.5021 0.4110 0.5160 0.0818 0.0600 0.0190 413 GLU A OE2 3187 N N . SER A 414 ? 0.2588 0.2237 0.2459 0.0489 0.0221 -0.0161 414 SER A N 3188 C CA . SER A 414 ? 0.2592 0.2135 0.2452 0.0440 0.0172 -0.0156 414 SER A CA 3189 C C . SER A 414 ? 0.2595 0.2118 0.2435 0.0332 0.0172 -0.0150 414 SER A C 3190 O O . SER A 414 ? 0.2542 0.1991 0.2382 0.0377 0.0143 -0.0107 414 SER A O 3191 C CB . SER A 414 ? 0.2516 0.2054 0.2370 0.0424 0.0182 -0.0156 414 SER A CB 3192 O OG . SER A 414 ? 0.2639 0.2294 0.2316 0.0579 0.0046 -0.0240 414 SER A OG 3193 N N . GLY A 415 ? 0.2682 0.2125 0.2461 0.0299 0.0162 -0.0180 415 GLY A N 3194 C CA . GLY A 415 ? 0.2770 0.2197 0.2459 0.0177 0.0169 -0.0173 415 GLY A CA 3195 C C . GLY A 415 ? 0.2889 0.2273 0.2542 0.0142 0.0185 -0.0189 415 GLY A C 3196 O O . GLY A 415 ? 0.2823 0.2166 0.2495 0.0032 0.0261 -0.0209 415 GLY A O 3197 N N . SER A 416 ? 0.2952 0.2313 0.2585 0.0084 0.0155 -0.0166 416 SER A N 3198 C CA . SER A 416 ? 0.3067 0.2447 0.2584 0.0136 0.0126 -0.0119 416 SER A CA 3199 C C . SER A 416 ? 0.3093 0.2539 0.2554 0.0092 0.0184 -0.0057 416 SER A C 3200 O O . SER A 416 ? 0.3111 0.2544 0.2596 0.0092 0.0217 0.0058 416 SER A O 3201 C CB . SER A 416 ? 0.3144 0.2498 0.2542 0.0147 0.0071 -0.0194 416 SER A CB 3202 O OG . SER A 416 ? 0.3168 0.2561 0.2916 0.0379 0.0108 -0.0272 416 SER A OG 3203 N N . PRO A 417 ? 0.3067 0.2633 0.2476 0.0091 0.0225 -0.0031 417 PRO A N 3204 C CA . PRO A 417 ? 0.3135 0.2614 0.2369 0.0083 0.0226 -0.0021 417 PRO A CA 3205 C C . PRO A 417 ? 0.3071 0.2614 0.2266 0.0127 0.0254 -0.0048 417 PRO A C 3206 O O . PRO A 417 ? 0.3194 0.2596 0.2226 0.0130 0.0291 -0.0029 417 PRO A O 3207 C CB . PRO A 417 ? 0.3043 0.2696 0.2460 0.0051 0.0286 -0.0058 417 PRO A CB 3208 C CG . PRO A 417 ? 0.3155 0.2741 0.2555 0.0061 0.0193 0.0130 417 PRO A CG 3209 C CD . PRO A 417 ? 0.3218 0.2697 0.2624 0.0058 0.0193 0.0003 417 PRO A CD 3210 N N . GLU A 418 ? 0.3067 0.2506 0.2151 0.0134 0.0222 -0.0208 418 GLU A N 3211 C CA . GLU A 418 ? 0.3029 0.2497 0.2199 0.0167 0.0116 -0.0275 418 GLU A CA 3212 C C . GLU A 418 ? 0.2869 0.2369 0.2136 0.0183 0.0003 -0.0279 418 GLU A C 3213 O O . GLU A 418 ? 0.2757 0.2328 0.2159 0.0246 -0.0094 -0.0290 418 GLU A O 3214 C CB . GLU A 418 ? 0.3163 0.2616 0.2188 0.0133 0.0147 -0.0290 418 GLU A CB 3215 C CG . GLU A 418 ? 0.3710 0.3097 0.2856 0.0187 0.0149 -0.0277 418 GLU A CG 3216 C CD . GLU A 418 ? 0.4156 0.3705 0.3376 0.0341 0.0138 -0.0293 418 GLU A CD 3217 O OE1 . GLU A 418 ? 0.4225 0.4155 0.3780 0.0501 0.0039 -0.0335 418 GLU A OE1 3218 O OE2 . GLU A 418 ? 0.4575 0.4210 0.3897 0.0508 0.0125 -0.0359 418 GLU A OE2 3219 N N . TYR A 419 ? 0.2655 0.2120 0.2041 0.0216 -0.0116 -0.0265 419 TYR A N 3220 C CA . TYR A 419 ? 0.2434 0.2003 0.1947 0.0263 -0.0147 -0.0288 419 TYR A CA 3221 C C . TYR A 419 ? 0.2366 0.1913 0.1936 0.0227 -0.0178 -0.0283 419 TYR A C 3222 O O . TYR A 419 ? 0.2314 0.1816 0.2008 0.0379 -0.0231 -0.0191 419 TYR A O 3223 C CB . TYR A 419 ? 0.2334 0.1971 0.1899 0.0322 -0.0160 -0.0243 419 TYR A CB 3224 C CG . TYR A 419 ? 0.2166 0.1992 0.1866 0.0365 -0.0081 -0.0269 419 TYR A CG 3225 C CD1 . TYR A 419 ? 0.1956 0.1815 0.1869 0.0462 0.0021 -0.0073 419 TYR A CD1 3226 C CD2 . TYR A 419 ? 0.1894 0.1965 0.1861 0.0550 -0.0055 -0.0294 419 TYR A CD2 3227 C CE1 . TYR A 419 ? 0.1938 0.2004 0.1959 0.0486 0.0123 -0.0171 419 TYR A CE1 3228 C CE2 . TYR A 419 ? 0.1894 0.1821 0.1700 0.0474 0.0057 -0.0161 419 TYR A CE2 3229 C CZ . TYR A 419 ? 0.2018 0.1895 0.1691 0.0456 0.0005 -0.0259 419 TYR A CZ 3230 O OH . TYR A 419 ? 0.2024 0.1844 0.1854 0.0514 0.0038 -0.0314 419 TYR A OH 3231 N N . ARG A 420 ? 0.2243 0.1794 0.1779 0.0167 -0.0152 -0.0279 420 ARG A N 3232 C CA . ARG A 420 ? 0.2103 0.1647 0.1685 0.0139 -0.0119 -0.0307 420 ARG A CA 3233 C C . ARG A 420 ? 0.2027 0.1562 0.1696 0.0125 -0.0073 -0.0249 420 ARG A C 3234 O O . ARG A 420 ? 0.2049 0.1429 0.1670 0.0129 0.0056 -0.0301 420 ARG A O 3235 C CB . ARG A 420 ? 0.2138 0.1562 0.1763 0.0095 -0.0159 -0.0304 420 ARG A CB 3236 C CG . ARG A 420 ? 0.2045 0.1762 0.1517 -0.0002 -0.0150 -0.0419 420 ARG A CG 3237 C CD . ARG A 420 ? 0.2419 0.1718 0.1581 -0.0263 -0.0374 -0.0447 420 ARG A CD 3238 N NE . ARG A 420 ? 0.2442 0.1766 0.1813 -0.0147 -0.0349 -0.0403 420 ARG A NE 3239 C CZ . ARG A 420 ? 0.2869 0.2166 0.2078 -0.0171 -0.0259 -0.0423 420 ARG A CZ 3240 N NH1 . ARG A 420 ? 0.2501 0.1898 0.2195 -0.0057 -0.0298 -0.0538 420 ARG A NH1 3241 N NH2 . ARG A 420 ? 0.2976 0.2468 0.2100 -0.0003 -0.0269 -0.0205 420 ARG A NH2 3242 N N . GLN A 421 ? 0.1984 0.1472 0.1586 0.0047 -0.0075 -0.0215 421 GLN A N 3243 C CA . GLN A 421 ? 0.1847 0.1396 0.1521 -0.0003 -0.0136 -0.0058 421 GLN A CA 3244 C C . GLN A 421 ? 0.1858 0.1387 0.1594 0.0006 -0.0162 -0.0007 421 GLN A C 3245 O O . GLN A 421 ? 0.1976 0.1370 0.1629 0.0034 -0.0198 0.0170 421 GLN A O 3246 C CB . GLN A 421 ? 0.1687 0.1185 0.1368 -0.0040 -0.0168 -0.0148 421 GLN A CB 3247 C CG . GLN A 421 ? 0.1728 0.1077 0.1449 -0.0040 -0.0083 -0.0146 421 GLN A CG 3248 C CD . GLN A 421 ? 0.1527 0.1077 0.1404 -0.0049 -0.0116 -0.0399 421 GLN A CD 3249 O OE1 . GLN A 421 ? 0.1552 0.1359 0.1467 -0.0019 -0.0267 -0.0259 421 GLN A OE1 3250 N NE2 . GLN A 421 ? 0.1864 0.1367 0.1395 -0.0049 0.0000 -0.0235 421 GLN A NE2 3251 N N . GLN A 422 ? 0.1774 0.1412 0.1598 0.0030 -0.0165 0.0074 422 GLN A N 3252 C CA . GLN A 422 ? 0.1859 0.1472 0.1711 0.0102 -0.0147 0.0026 422 GLN A CA 3253 C C . GLN A 422 ? 0.1808 0.1555 0.1657 0.0043 -0.0175 0.0061 422 GLN A C 3254 O O . GLN A 422 ? 0.1834 0.1495 0.1624 0.0071 -0.0224 0.0064 422 GLN A O 3255 C CB . GLN A 422 ? 0.1724 0.1428 0.1490 0.0132 -0.0218 0.0070 422 GLN A CB 3256 C CG . GLN A 422 ? 0.1958 0.1275 0.1470 0.0164 -0.0156 0.0000 422 GLN A CG 3257 C CD . GLN A 422 ? 0.1988 0.1493 0.1875 0.0221 -0.0126 -0.0090 422 GLN A CD 3258 O OE1 . GLN A 422 ? 0.2098 0.1562 0.2085 0.0166 -0.0109 -0.0149 422 GLN A OE1 3259 N NE2 . GLN A 422 ? 0.2159 0.1795 0.2535 0.0437 -0.0020 -0.0115 422 GLN A NE2 3260 N N . SER A 423 ? 0.1820 0.1721 0.1665 0.0028 -0.0215 0.0045 423 SER A N 3261 C CA . SER A 423 ? 0.1803 0.1632 0.1659 -0.0017 -0.0200 0.0055 423 SER A CA 3262 C C . SER A 423 ? 0.1861 0.1624 0.1736 -0.0031 -0.0173 0.0061 423 SER A C 3263 O O . SER A 423 ? 0.1842 0.1668 0.1769 0.0041 -0.0121 0.0034 423 SER A O 3264 C CB . SER A 423 ? 0.1870 0.1702 0.1678 -0.0014 -0.0258 0.0081 423 SER A CB 3265 O OG . SER A 423 ? 0.1911 0.1679 0.1505 -0.0092 -0.0378 0.0166 423 SER A OG 3266 N N . ALA A 424 ? 0.1783 0.1483 0.1717 -0.0061 -0.0093 0.0016 424 ALA A N 3267 C CA . ALA A 424 ? 0.1859 0.1435 0.1847 -0.0069 -0.0130 0.0059 424 ALA A CA 3268 C C . ALA A 424 ? 0.1910 0.1367 0.1947 -0.0062 -0.0118 0.0018 424 ALA A C 3269 O O . ALA A 424 ? 0.1935 0.1203 0.2120 -0.0067 -0.0126 0.0113 424 ALA A O 3270 C CB . ALA A 424 ? 0.1780 0.1322 0.1637 -0.0032 -0.0107 0.0032 424 ALA A CB 3271 N N . VAL A 425 ? 0.1957 0.1372 0.1975 -0.0108 -0.0148 0.0007 425 VAL A N 3272 C CA . VAL A 425 ? 0.1975 0.1427 0.2033 -0.0048 -0.0160 -0.0047 425 VAL A CA 3273 C C . VAL A 425 ? 0.2051 0.1412 0.1997 -0.0073 -0.0167 -0.0025 425 VAL A C 3274 O O . VAL A 425 ? 0.1981 0.1463 0.1991 -0.0101 -0.0191 -0.0050 425 VAL A O 3275 C CB . VAL A 425 ? 0.1961 0.1446 0.2090 -0.0040 -0.0159 -0.0016 425 VAL A CB 3276 C CG1 . VAL A 425 ? 0.1926 0.1363 0.2000 0.0040 -0.0260 -0.0057 425 VAL A CG1 3277 C CG2 . VAL A 425 ? 0.1826 0.1191 0.2071 -0.0142 -0.0147 -0.0097 425 VAL A CG2 3278 N N . PRO A 426 ? 0.2161 0.1476 0.1943 -0.0105 -0.0123 -0.0034 426 PRO A N 3279 C CA . PRO A 426 ? 0.2230 0.1446 0.1981 -0.0076 -0.0124 -0.0031 426 PRO A CA 3280 C C . PRO A 426 ? 0.2110 0.1394 0.1884 -0.0052 -0.0161 -0.0082 426 PRO A C 3281 O O . PRO A 426 ? 0.2373 0.1489 0.1981 0.0027 -0.0108 0.0066 426 PRO A O 3282 C CB . PRO A 426 ? 0.2186 0.1376 0.2020 -0.0102 -0.0104 -0.0003 426 PRO A CB 3283 C CG . PRO A 426 ? 0.2183 0.1365 0.1928 -0.0147 -0.0070 0.0089 426 PRO A CG 3284 C CD . PRO A 426 ? 0.2204 0.1268 0.1911 -0.0079 -0.0148 -0.0005 426 PRO A CD 3285 N N . LEU A 427 ? 0.2069 0.1409 0.1799 -0.0087 -0.0134 -0.0206 427 LEU A N 3286 C CA . LEU A 427 ? 0.2023 0.1478 0.1801 -0.0125 -0.0172 -0.0243 427 LEU A CA 3287 C C . LEU A 427 ? 0.2176 0.1623 0.1945 -0.0133 -0.0260 -0.0222 427 LEU A C 3288 O O . LEU A 427 ? 0.2090 0.1837 0.1946 -0.0181 -0.0245 -0.0268 427 LEU A O 3289 C CB . LEU A 427 ? 0.2053 0.1430 0.1794 -0.0204 -0.0204 -0.0269 427 LEU A CB 3290 C CG . LEU A 427 ? 0.1951 0.1405 0.1831 -0.0324 -0.0110 -0.0487 427 LEU A CG 3291 C CD1 . LEU A 427 ? 0.2007 0.1198 0.1645 -0.0156 -0.0060 -0.0530 427 LEU A CD1 3292 C CD2 . LEU A 427 ? 0.2046 0.1772 0.1954 -0.0554 -0.0255 -0.0702 427 LEU A CD2 3293 N N . ASP A 428 ? 0.2276 0.1718 0.2012 -0.0173 -0.0301 -0.0264 428 ASP A N 3294 C CA . ASP A 428 ? 0.2492 0.1806 0.2067 -0.0189 -0.0338 -0.0177 428 ASP A CA 3295 C C . ASP A 428 ? 0.2433 0.1836 0.2012 -0.0135 -0.0300 -0.0129 428 ASP A C 3296 O O . ASP A 428 ? 0.2393 0.1766 0.1984 -0.0110 -0.0273 -0.0016 428 ASP A O 3297 C CB . ASP A 428 ? 0.2614 0.1923 0.2240 -0.0227 -0.0383 -0.0208 428 ASP A CB 3298 C CG . ASP A 428 ? 0.2979 0.1990 0.2574 -0.0248 -0.0636 -0.0228 428 ASP A CG 3299 O OD1 . ASP A 428 ? 0.3713 0.2015 0.3209 -0.0595 -0.1025 -0.0375 428 ASP A OD1 3300 O OD2 . ASP A 428 ? 0.3857 0.2406 0.2957 -0.0178 -0.0754 -0.0235 428 ASP A OD2 3301 N N . GLU A 429 ? 0.2389 0.1761 0.1848 -0.0069 -0.0291 -0.0099 429 GLU A N 3302 C CA . GLU A 429 ? 0.2398 0.1925 0.1796 -0.0008 -0.0273 -0.0093 429 GLU A CA 3303 C C . GLU A 429 ? 0.2241 0.1702 0.1689 -0.0013 -0.0272 -0.0108 429 GLU A C 3304 O O . GLU A 429 ? 0.2312 0.1730 0.1594 -0.0092 -0.0275 -0.0113 429 GLU A O 3305 C CB . GLU A 429 ? 0.2594 0.1982 0.1887 -0.0019 -0.0235 -0.0080 429 GLU A CB 3306 C CG . GLU A 429 ? 0.3216 0.2756 0.2410 0.0245 -0.0137 0.0057 429 GLU A CG 3307 C CD . GLU A 429 ? 0.4037 0.3505 0.3121 0.0598 0.0144 0.0058 429 GLU A CD 3308 O OE1 . GLU A 429 ? 0.4371 0.4157 0.3698 0.0745 0.0002 -0.0010 429 GLU A OE1 3309 O OE2 . GLU A 429 ? 0.4817 0.4264 0.3624 0.0645 -0.0009 0.0063 429 GLU A OE2 3310 N N . GLU A 430 ? 0.1995 0.1592 0.1498 0.0023 -0.0353 -0.0090 430 GLU A N 3311 C CA . GLU A 430 ? 0.1865 0.1474 0.1470 0.0037 -0.0266 -0.0136 430 GLU A CA 3312 C C . GLU A 430 ? 0.1777 0.1432 0.1518 0.0008 -0.0237 -0.0100 430 GLU A C 3313 O O . GLU A 430 ? 0.1688 0.1510 0.1682 0.0104 -0.0313 -0.0142 430 GLU A O 3314 C CB . GLU A 430 ? 0.1741 0.1434 0.1317 -0.0016 -0.0311 -0.0143 430 GLU A CB 3315 C CG . GLU A 430 ? 0.1695 0.1422 0.1163 -0.0026 -0.0262 -0.0103 430 GLU A CG 3316 C CD . GLU A 430 ? 0.1487 0.1589 0.1303 0.0158 -0.0219 -0.0089 430 GLU A CD 3317 O OE1 . GLU A 430 ? 0.1609 0.1546 0.1553 0.0086 -0.0235 0.0022 430 GLU A OE1 3318 O OE2 . GLU A 430 ? 0.1745 0.1450 0.1380 0.0047 -0.0343 0.0176 430 GLU A OE2 3319 N N . THR A 431 ? 0.1723 0.1340 0.1538 0.0019 -0.0133 -0.0090 431 THR A N 3320 C CA . THR A 431 ? 0.1711 0.1320 0.1486 0.0040 -0.0137 -0.0056 431 THR A CA 3321 C C . THR A 431 ? 0.1705 0.1392 0.1457 0.0078 -0.0103 -0.0036 431 THR A C 3322 O O . THR A 431 ? 0.1463 0.1274 0.1343 0.0130 -0.0094 0.0086 431 THR A O 3323 C CB . THR A 431 ? 0.1771 0.1284 0.1420 0.0013 -0.0114 -0.0071 431 THR A CB 3324 O OG1 . THR A 431 ? 0.1608 0.1202 0.1401 0.0065 -0.0188 -0.0106 431 THR A OG1 3325 C CG2 . THR A 431 ? 0.1945 0.1358 0.1572 -0.0025 -0.0141 -0.0085 431 THR A CG2 3326 N N . HIS A 432 ? 0.1671 0.1372 0.1409 0.0120 -0.0089 -0.0045 432 HIS A N 3327 C CA . HIS A 432 ? 0.1669 0.1475 0.1439 0.0037 -0.0096 -0.0034 432 HIS A CA 3328 C C . HIS A 432 ? 0.1521 0.1491 0.1399 0.0075 -0.0117 -0.0034 432 HIS A C 3329 O O . HIS A 432 ? 0.1447 0.1469 0.1447 0.0050 -0.0050 -0.0014 432 HIS A O 3330 C CB . HIS A 432 ? 0.1618 0.1458 0.1296 0.0103 -0.0177 -0.0036 432 HIS A CB 3331 C CG . HIS A 432 ? 0.1861 0.1580 0.1544 -0.0183 -0.0050 0.0016 432 HIS A CG 3332 N ND1 . HIS A 432 ? 0.1363 0.1657 0.1185 -0.0102 -0.0264 0.0025 432 HIS A ND1 3333 C CD2 . HIS A 432 ? 0.1816 0.1285 0.1440 -0.0265 -0.0148 -0.0050 432 HIS A CD2 3334 C CE1 . HIS A 432 ? 0.1770 0.1950 0.1539 -0.0259 -0.0178 -0.0176 432 HIS A CE1 3335 N NE2 . HIS A 432 ? 0.1499 0.1699 0.1348 -0.0368 -0.0356 -0.0197 432 HIS A NE2 3336 N N . ALA A 433 ? 0.1381 0.1383 0.1314 0.0089 -0.0129 -0.0077 433 ALA A N 3337 C CA . ALA A 433 ? 0.1355 0.1495 0.1273 0.0075 -0.0111 -0.0072 433 ALA A CA 3338 C C . ALA A 433 ? 0.1293 0.1446 0.1281 0.0012 -0.0089 -0.0074 433 ALA A C 3339 O O . ALA A 433 ? 0.1323 0.1659 0.1211 0.0053 -0.0056 -0.0084 433 ALA A O 3340 C CB . ALA A 433 ? 0.1246 0.1490 0.1130 0.0069 -0.0218 -0.0128 433 ALA A CB 3341 N N . GLY A 434 ? 0.1251 0.1422 0.1293 -0.0006 -0.0085 -0.0086 434 GLY A N 3342 C CA . GLY A 434 ? 0.1266 0.1489 0.1459 -0.0072 0.0020 -0.0106 434 GLY A CA 3343 C C . GLY A 434 ? 0.1272 0.1509 0.1375 -0.0046 0.0013 -0.0087 434 GLY A C 3344 O O . GLY A 434 ? 0.1361 0.1653 0.1538 -0.0089 0.0022 -0.0084 434 GLY A O 3345 N N . GLU A 435 ? 0.1436 0.1542 0.1468 -0.0071 0.0045 -0.0107 435 GLU A N 3346 C CA . GLU A 435 ? 0.1391 0.1435 0.1494 -0.0112 0.0037 -0.0047 435 GLU A CA 3347 C C . GLU A 435 ? 0.1313 0.1460 0.1513 -0.0070 0.0049 -0.0023 435 GLU A C 3348 O O . GLU A 435 ? 0.1336 0.1412 0.1470 -0.0107 0.0062 0.0068 435 GLU A O 3349 C CB . GLU A 435 ? 0.1388 0.1403 0.1482 -0.0049 0.0009 -0.0112 435 GLU A CB 3350 C CG . GLU A 435 ? 0.1571 0.1462 0.1452 -0.0137 0.0134 -0.0022 435 GLU A CG 3351 C CD . GLU A 435 ? 0.1594 0.1827 0.1664 -0.0025 0.0043 -0.0025 435 GLU A CD 3352 O OE1 . GLU A 435 ? 0.2118 0.1635 0.1726 -0.0062 0.0177 0.0026 435 GLU A OE1 3353 O OE2 . GLU A 435 ? 0.1932 0.2157 0.1790 -0.0049 0.0149 -0.0072 435 GLU A OE2 3354 N N . ASP A 436 ? 0.1204 0.1328 0.1473 -0.0098 0.0080 -0.0078 436 ASP A N 3355 C CA . ASP A 436 ? 0.1340 0.1472 0.1503 -0.0041 0.0086 -0.0125 436 ASP A CA 3356 C C . ASP A 436 ? 0.1396 0.1453 0.1397 -0.0040 0.0113 -0.0122 436 ASP A C 3357 O O . ASP A 436 ? 0.1424 0.1427 0.1371 0.0056 0.0145 -0.0101 436 ASP A O 3358 C CB . ASP A 436 ? 0.1339 0.1441 0.1466 -0.0061 0.0100 -0.0212 436 ASP A CB 3359 C CG . ASP A 436 ? 0.1527 0.1654 0.1777 -0.0116 0.0115 -0.0268 436 ASP A CG 3360 O OD1 . ASP A 436 ? 0.1599 0.1882 0.2084 0.0055 -0.0122 -0.0293 436 ASP A OD1 3361 O OD2 . ASP A 436 ? 0.2087 0.2161 0.2304 -0.0321 0.0232 -0.0603 436 ASP A OD2 3362 N N . VAL A 437 ? 0.1414 0.1297 0.1374 -0.0042 0.0075 -0.0075 437 VAL A N 3363 C CA . VAL A 437 ? 0.1374 0.1301 0.1384 -0.0106 0.0056 -0.0046 437 VAL A CA 3364 C C . VAL A 437 ? 0.1399 0.1419 0.1406 -0.0114 0.0023 -0.0041 437 VAL A C 3365 O O . VAL A 437 ? 0.1419 0.1371 0.1598 -0.0126 -0.0057 -0.0041 437 VAL A O 3366 C CB . VAL A 437 ? 0.1384 0.1274 0.1381 -0.0154 0.0006 -0.0065 437 VAL A CB 3367 C CG1 . VAL A 437 ? 0.1466 0.0857 0.1318 0.0009 0.0172 -0.0012 437 VAL A CG1 3368 C CG2 . VAL A 437 ? 0.1547 0.1240 0.1170 -0.0084 0.0094 -0.0021 437 VAL A CG2 3369 N N . ALA A 438 ? 0.1186 0.1535 0.1490 -0.0199 -0.0100 -0.0039 438 ALA A N 3370 C CA . ALA A 438 ? 0.1318 0.1597 0.1586 -0.0104 0.0018 -0.0026 438 ALA A CA 3371 C C . ALA A 438 ? 0.1316 0.1627 0.1586 -0.0152 0.0071 -0.0016 438 ALA A C 3372 O O . ALA A 438 ? 0.1467 0.1365 0.1575 -0.0088 0.0151 -0.0095 438 ALA A O 3373 C CB . ALA A 438 ? 0.1262 0.1798 0.1653 -0.0219 -0.0029 -0.0054 438 ALA A CB 3374 N N . VAL A 439 ? 0.1279 0.1550 0.1586 -0.0120 0.0117 0.0013 439 VAL A N 3375 C CA . VAL A 439 ? 0.1483 0.1683 0.1575 -0.0165 0.0136 0.0041 439 VAL A CA 3376 C C . VAL A 439 ? 0.1575 0.1664 0.1591 -0.0193 0.0151 0.0012 439 VAL A C 3377 O O . VAL A 439 ? 0.1712 0.1856 0.1663 -0.0308 0.0196 -0.0071 439 VAL A O 3378 C CB . VAL A 439 ? 0.1540 0.1685 0.1688 -0.0127 0.0138 0.0106 439 VAL A CB 3379 C CG1 . VAL A 439 ? 0.1655 0.1720 0.1372 -0.0024 0.0015 0.0179 439 VAL A CG1 3380 C CG2 . VAL A 439 ? 0.1542 0.1643 0.1686 -0.0251 0.0155 -0.0004 439 VAL A CG2 3381 N N . PHE A 440 ? 0.1513 0.1560 0.1527 -0.0156 0.0152 0.0071 440 PHE A N 3382 C CA . PHE A 440 ? 0.1653 0.1525 0.1561 -0.0039 0.0211 0.0115 440 PHE A CA 3383 C C . PHE A 440 ? 0.1698 0.1534 0.1595 -0.0073 0.0164 0.0131 440 PHE A C 3384 O O . PHE A 440 ? 0.1839 0.1477 0.1513 -0.0204 0.0126 0.0176 440 PHE A O 3385 C CB . PHE A 440 ? 0.1567 0.1648 0.1533 0.0007 0.0188 0.0131 440 PHE A CB 3386 C CG . PHE A 440 ? 0.1649 0.1620 0.1529 0.0035 0.0328 0.0125 440 PHE A CG 3387 C CD1 . PHE A 440 ? 0.1665 0.1827 0.1606 -0.0053 0.0183 0.0164 440 PHE A CD1 3388 C CD2 . PHE A 440 ? 0.1885 0.1911 0.1510 -0.0039 0.0282 0.0256 440 PHE A CD2 3389 C CE1 . PHE A 440 ? 0.1772 0.1658 0.1657 0.0258 0.0149 0.0137 440 PHE A CE1 3390 C CE2 . PHE A 440 ? 0.1850 0.1673 0.1852 0.0161 0.0319 0.0188 440 PHE A CE2 3391 C CZ . PHE A 440 ? 0.1849 0.1771 0.1618 0.0058 0.0266 -0.0053 440 PHE A CZ 3392 N N . ALA A 441 ? 0.1558 0.1394 0.1608 0.0005 0.0227 0.0098 441 ALA A N 3393 C CA . ALA A 441 ? 0.1541 0.1448 0.1760 -0.0016 0.0221 0.0102 441 ALA A CA 3394 C C . ALA A 441 ? 0.1623 0.1522 0.1813 0.0029 0.0169 0.0104 441 ALA A C 3395 O O . ALA A 441 ? 0.1763 0.1482 0.1728 -0.0136 0.0202 0.0067 441 ALA A O 3396 C CB . ALA A 441 ? 0.1442 0.1393 0.1832 0.0063 0.0236 0.0052 441 ALA A CB 3397 N N . ARG A 442 ? 0.1693 0.1566 0.1750 0.0070 0.0134 0.0154 442 ARG A N 3398 C CA . ARG A 442 ? 0.1832 0.1730 0.1885 0.0137 0.0043 0.0191 442 ARG A CA 3399 C C . ARG A 442 ? 0.1881 0.1677 0.1842 0.0145 -0.0010 0.0199 442 ARG A C 3400 O O . ARG A 442 ? 0.1963 0.1685 0.1806 0.0114 -0.0028 0.0270 442 ARG A O 3401 C CB . ARG A 442 ? 0.1825 0.1777 0.1944 0.0205 0.0022 0.0134 442 ARG A CB 3402 C CG . ARG A 442 ? 0.2115 0.2303 0.2235 0.0189 0.0037 0.0364 442 ARG A CG 3403 C CD . ARG A 442 ? 0.2065 0.2400 0.2656 0.0120 0.0063 0.0491 442 ARG A CD 3404 N NE . ARG A 442 ? 0.2441 0.2875 0.2873 -0.0102 -0.0015 0.0432 442 ARG A NE 3405 C CZ . ARG A 442 ? 0.2793 0.2879 0.2966 -0.0057 -0.0021 0.0387 442 ARG A CZ 3406 N NH1 . ARG A 442 ? 0.2744 0.2837 0.3025 0.0018 -0.0226 0.0394 442 ARG A NH1 3407 N NH2 . ARG A 442 ? 0.2814 0.2850 0.3288 -0.0096 0.0089 0.0373 442 ARG A NH2 3408 N N . GLY A 443 ? 0.1981 0.1609 0.1837 0.0154 -0.0071 0.0187 443 GLY A N 3409 C CA . GLY A 443 ? 0.2062 0.1598 0.1907 0.0155 -0.0090 0.0198 443 GLY A CA 3410 C C . GLY A 443 ? 0.2107 0.1590 0.1954 0.0197 -0.0111 0.0247 443 GLY A C 3411 O O . GLY A 443 ? 0.2145 0.1550 0.2098 0.0130 -0.0120 0.0222 443 GLY A O 3412 N N . PRO A 444 ? 0.2173 0.1642 0.2065 0.0258 -0.0106 0.0249 444 PRO A N 3413 C CA . PRO A 444 ? 0.2166 0.1701 0.2036 0.0363 -0.0076 0.0274 444 PRO A CA 3414 C C . PRO A 444 ? 0.2205 0.1689 0.2050 0.0402 -0.0111 0.0250 444 PRO A C 3415 O O . PRO A 444 ? 0.2129 0.1679 0.1960 0.0440 -0.0123 0.0200 444 PRO A O 3416 C CB . PRO A 444 ? 0.2321 0.1770 0.2027 0.0399 -0.0060 0.0322 444 PRO A CB 3417 C CG . PRO A 444 ? 0.2253 0.1625 0.2131 0.0296 0.0024 0.0304 444 PRO A CG 3418 C CD . PRO A 444 ? 0.2110 0.1600 0.1957 0.0367 -0.0068 0.0278 444 PRO A CD 3419 N N . GLN A 445 ? 0.2093 0.1595 0.1963 0.0451 -0.0062 0.0151 445 GLN A N 3420 C CA . GLN A 445 ? 0.2146 0.1636 0.2006 0.0467 -0.0080 0.0097 445 GLN A CA 3421 C C . GLN A 445 ? 0.2095 0.1595 0.1948 0.0415 -0.0062 0.0073 445 GLN A C 3422 O O . GLN A 445 ? 0.2088 0.1805 0.1922 0.0495 0.0012 0.0013 445 GLN A O 3423 C CB . GLN A 445 ? 0.2106 0.1586 0.2008 0.0452 -0.0133 0.0133 445 GLN A CB 3424 C CG . GLN A 445 ? 0.2369 0.1584 0.2203 0.0415 -0.0094 0.0079 445 GLN A CG 3425 C CD . GLN A 445 ? 0.2606 0.1792 0.2540 0.0402 -0.0143 0.0252 445 GLN A CD 3426 O OE1 . GLN A 445 ? 0.3037 0.1986 0.2820 0.0456 -0.0231 0.0202 445 GLN A OE1 3427 N NE2 . GLN A 445 ? 0.2503 0.1101 0.2515 0.0276 -0.0248 0.0318 445 GLN A NE2 3428 N N . ALA A 446 ? 0.1993 0.1455 0.1828 0.0474 -0.0048 0.0060 446 ALA A N 3429 C CA . ALA A 446 ? 0.2014 0.1338 0.1830 0.0382 -0.0027 0.0014 446 ALA A CA 3430 C C . ALA A 446 ? 0.1976 0.1322 0.1801 0.0355 -0.0059 0.0009 446 ALA A C 3431 O O . ALA A 446 ? 0.1892 0.1248 0.1714 0.0390 -0.0084 -0.0037 446 ALA A O 3432 C CB . ALA A 446 ? 0.1892 0.1152 0.1754 0.0419 -0.0093 0.0039 446 ALA A CB 3433 N N . HIS A 447 ? 0.1994 0.1428 0.1904 0.0246 -0.0086 -0.0025 447 HIS A N 3434 C CA . HIS A 447 ? 0.2058 0.1483 0.2027 0.0218 -0.0084 -0.0082 447 HIS A CA 3435 C C . HIS A 447 ? 0.2121 0.1530 0.2002 0.0167 -0.0092 -0.0032 447 HIS A C 3436 O O . HIS A 447 ? 0.2218 0.1669 0.1887 0.0144 -0.0015 -0.0035 447 HIS A O 3437 C CB . HIS A 447 ? 0.2057 0.1477 0.2150 0.0205 -0.0170 -0.0088 447 HIS A CB 3438 C CG . HIS A 447 ? 0.2327 0.1629 0.2400 0.0248 -0.0145 -0.0319 447 HIS A CG 3439 N ND1 . HIS A 447 ? 0.2546 0.1899 0.2732 0.0293 -0.0106 -0.0300 447 HIS A ND1 3440 C CD2 . HIS A 447 ? 0.2228 0.1901 0.2458 0.0209 -0.0232 -0.0432 447 HIS A CD2 3441 C CE1 . HIS A 447 ? 0.2242 0.1911 0.2689 0.0337 -0.0060 -0.0493 447 HIS A CE1 3442 N NE2 . HIS A 447 ? 0.2300 0.1895 0.2707 0.0237 -0.0117 -0.0339 447 HIS A NE2 3443 N N . LEU A 448 ? 0.2074 0.1451 0.1857 0.0196 -0.0130 0.0038 448 LEU A N 3444 C CA . LEU A 448 ? 0.2010 0.1428 0.1861 0.0229 -0.0148 0.0061 448 LEU A CA 3445 C C . LEU A 448 ? 0.1982 0.1485 0.1800 0.0252 -0.0118 0.0062 448 LEU A C 3446 O O . LEU A 448 ? 0.1938 0.1402 0.1772 0.0312 -0.0126 0.0077 448 LEU A O 3447 C CB . LEU A 448 ? 0.2090 0.1422 0.1906 0.0124 -0.0159 0.0105 448 LEU A CB 3448 C CG . LEU A 448 ? 0.2204 0.1281 0.2049 0.0295 -0.0195 0.0029 448 LEU A CG 3449 C CD1 . LEU A 448 ? 0.2393 0.1141 0.2027 0.0291 -0.0162 0.0240 448 LEU A CD1 3450 C CD2 . LEU A 448 ? 0.2229 0.1038 0.1981 -0.0140 -0.0158 0.0090 448 LEU A CD2 3451 N N . VAL A 449 ? 0.1943 0.1488 0.1657 0.0288 -0.0085 0.0052 449 VAL A N 3452 C CA . VAL A 449 ? 0.1933 0.1511 0.1551 0.0259 -0.0035 0.0061 449 VAL A CA 3453 C C . VAL A 449 ? 0.1863 0.1595 0.1563 0.0218 -0.0028 0.0079 449 VAL A C 3454 O O . VAL A 449 ? 0.1883 0.1643 0.1502 0.0159 -0.0068 0.0147 449 VAL A O 3455 C CB . VAL A 449 ? 0.2004 0.1424 0.1516 0.0244 -0.0073 0.0099 449 VAL A CB 3456 C CG1 . VAL A 449 ? 0.1908 0.1447 0.1491 0.0382 0.0023 0.0009 449 VAL A CG1 3457 C CG2 . VAL A 449 ? 0.2067 0.1475 0.1375 0.0239 -0.0039 0.0136 449 VAL A CG2 3458 N N . HIS A 450 ? 0.1799 0.1568 0.1610 0.0196 -0.0010 -0.0028 450 HIS A N 3459 C CA . HIS A 450 ? 0.1717 0.1554 0.1723 0.0198 0.0079 -0.0096 450 HIS A CA 3460 C C . HIS A 450 ? 0.1693 0.1570 0.1768 0.0191 0.0054 -0.0123 450 HIS A C 3461 O O . HIS A 450 ? 0.1777 0.1547 0.1899 0.0238 0.0016 -0.0167 450 HIS A O 3462 C CB . HIS A 450 ? 0.1650 0.1517 0.1653 0.0213 0.0122 -0.0178 450 HIS A CB 3463 C CG . HIS A 450 ? 0.1756 0.1619 0.1786 0.0272 0.0171 -0.0254 450 HIS A CG 3464 N ND1 . HIS A 450 ? 0.1853 0.1818 0.2126 0.0303 0.0315 -0.0178 450 HIS A ND1 3465 C CD2 . HIS A 450 ? 0.1705 0.1788 0.2140 0.0593 0.0417 -0.0256 450 HIS A CD2 3466 C CE1 . HIS A 450 ? 0.1780 0.1786 0.2111 0.0336 0.0375 0.0040 450 HIS A CE1 3467 N NE2 . HIS A 450 ? 0.2028 0.2123 0.2217 0.0316 0.0259 -0.0191 450 HIS A NE2 3468 N N . GLY A 451 ? 0.1693 0.1604 0.1741 0.0162 0.0083 -0.0111 451 GLY A N 3469 C CA . GLY A 451 ? 0.1662 0.1482 0.1779 0.0048 0.0043 -0.0074 451 GLY A CA 3470 C C . GLY A 451 ? 0.1732 0.1607 0.1779 0.0040 0.0041 -0.0055 451 GLY A C 3471 O O . GLY A 451 ? 0.1717 0.1529 0.1846 -0.0006 0.0152 -0.0105 451 GLY A O 3472 N N . VAL A 452 ? 0.1586 0.1643 0.1715 0.0037 -0.0004 -0.0010 452 VAL A N 3473 C CA . VAL A 452 ? 0.1577 0.1599 0.1649 0.0136 -0.0042 -0.0028 452 VAL A CA 3474 C C . VAL A 452 ? 0.1629 0.1708 0.1691 0.0176 -0.0077 -0.0065 452 VAL A C 3475 O O . VAL A 452 ? 0.1508 0.1724 0.1541 0.0425 -0.0136 -0.0142 452 VAL A O 3476 C CB . VAL A 452 ? 0.1613 0.1588 0.1610 0.0107 -0.0039 0.0011 452 VAL A CB 3477 C CG1 . VAL A 452 ? 0.1529 0.1520 0.1569 0.0152 0.0080 -0.0042 452 VAL A CG1 3478 C CG2 . VAL A 452 ? 0.1420 0.1587 0.1663 0.0127 -0.0026 0.0013 452 VAL A CG2 3479 N N . GLN A 453 ? 0.1599 0.1701 0.1618 0.0194 -0.0069 -0.0088 453 GLN A N 3480 C CA . GLN A 453 ? 0.1675 0.1767 0.1857 0.0133 -0.0075 -0.0113 453 GLN A CA 3481 C C . GLN A 453 ? 0.1571 0.1793 0.1752 0.0149 -0.0042 -0.0115 453 GLN A C 3482 O O . GLN A 453 ? 0.1480 0.1775 0.1858 0.0099 -0.0009 -0.0114 453 GLN A O 3483 C CB . GLN A 453 ? 0.1643 0.1780 0.1726 0.0241 -0.0121 -0.0119 453 GLN A CB 3484 C CG . GLN A 453 ? 0.2275 0.1972 0.2201 0.0025 -0.0077 0.0063 453 GLN A CG 3485 C CD . GLN A 453 ? 0.2881 0.2635 0.2789 0.0367 -0.0197 -0.0301 453 GLN A CD 3486 O OE1 . GLN A 453 ? 0.3123 0.3094 0.3212 0.0458 -0.0124 -0.0497 453 GLN A OE1 3487 N NE2 . GLN A 453 ? 0.3560 0.2411 0.3265 0.0472 -0.0481 -0.0370 453 GLN A NE2 3488 N N . GLU A 454 ? 0.1486 0.1815 0.1827 0.0069 -0.0021 -0.0164 454 GLU A N 3489 C CA . GLU A 454 ? 0.1458 0.1683 0.1797 0.0090 0.0000 -0.0217 454 GLU A CA 3490 C C . GLU A 454 ? 0.1391 0.1617 0.1761 0.0125 -0.0023 -0.0219 454 GLU A C 3491 O O . GLU A 454 ? 0.1465 0.1477 0.1771 0.0119 -0.0021 -0.0257 454 GLU A O 3492 C CB . GLU A 454 ? 0.1387 0.1689 0.1835 0.0144 -0.0018 -0.0173 454 GLU A CB 3493 C CG . GLU A 454 ? 0.1503 0.1666 0.2036 0.0092 0.0129 -0.0180 454 GLU A CG 3494 C CD . GLU A 454 ? 0.1518 0.1833 0.2087 0.0133 0.0018 -0.0203 454 GLU A CD 3495 O OE1 . GLU A 454 ? 0.1436 0.1976 0.2037 0.0091 0.0207 -0.0046 454 GLU A OE1 3496 O OE2 . GLU A 454 ? 0.1869 0.1691 0.2539 0.0202 0.0040 -0.0411 454 GLU A OE2 3497 N N . GLN A 455 ? 0.1394 0.1518 0.1688 0.0157 -0.0026 -0.0254 455 GLN A N 3498 C CA . GLN A 455 ? 0.1451 0.1457 0.1712 0.0162 0.0008 -0.0264 455 GLN A CA 3499 C C . GLN A 455 ? 0.1444 0.1492 0.1724 0.0126 0.0003 -0.0242 455 GLN A C 3500 O O . GLN A 455 ? 0.1405 0.1567 0.1776 0.0163 -0.0058 -0.0273 455 GLN A O 3501 C CB . GLN A 455 ? 0.1595 0.1502 0.1738 0.0187 0.0070 -0.0283 455 GLN A CB 3502 C CG . GLN A 455 ? 0.1623 0.1223 0.1677 0.0156 0.0221 -0.0347 455 GLN A CG 3503 C CD . GLN A 455 ? 0.1820 0.1218 0.1918 -0.0008 0.0354 -0.0260 455 GLN A CD 3504 O OE1 . GLN A 455 ? 0.2086 0.1453 0.1789 0.0090 0.0115 -0.0373 455 GLN A OE1 3505 N NE2 . GLN A 455 ? 0.1107 0.1202 0.1632 0.0079 0.0231 -0.0025 455 GLN A NE2 3506 N N . THR A 456 ? 0.1415 0.1403 0.1737 0.0136 -0.0064 -0.0239 456 THR A N 3507 C CA . THR A 456 ? 0.1481 0.1547 0.1743 0.0128 -0.0047 -0.0196 456 THR A CA 3508 C C . THR A 456 ? 0.1531 0.1572 0.1774 0.0113 -0.0026 -0.0142 456 THR A C 3509 O O . THR A 456 ? 0.1608 0.1603 0.1783 0.0138 -0.0092 -0.0120 456 THR A O 3510 C CB . THR A 456 ? 0.1381 0.1519 0.1727 0.0168 0.0009 -0.0192 456 THR A CB 3511 O OG1 . THR A 456 ? 0.1580 0.1817 0.1747 0.0288 0.0002 -0.0239 456 THR A OG1 3512 C CG2 . THR A 456 ? 0.1072 0.1505 0.1583 0.0221 -0.0212 -0.0164 456 THR A CG2 3513 N N . PHE A 457 ? 0.1530 0.1511 0.1747 0.0080 -0.0032 -0.0194 457 PHE A N 3514 C CA . PHE A 457 ? 0.1712 0.1780 0.1780 0.0095 -0.0077 -0.0134 457 PHE A CA 3515 C C . PHE A 457 ? 0.1685 0.1689 0.1719 0.0111 -0.0076 -0.0099 457 PHE A C 3516 O O . PHE A 457 ? 0.1656 0.1615 0.1668 0.0061 -0.0063 -0.0023 457 PHE A O 3517 C CB . PHE A 457 ? 0.1764 0.1739 0.1742 0.0117 -0.0148 -0.0206 457 PHE A CB 3518 C CG . PHE A 457 ? 0.1938 0.1901 0.1830 0.0137 -0.0277 -0.0234 457 PHE A CG 3519 C CD1 . PHE A 457 ? 0.2033 0.1706 0.1878 0.0301 -0.0314 -0.0539 457 PHE A CD1 3520 C CD2 . PHE A 457 ? 0.2064 0.1837 0.2160 0.0247 -0.0196 -0.0393 457 PHE A CD2 3521 C CE1 . PHE A 457 ? 0.2182 0.2152 0.2446 0.0146 -0.0309 -0.0373 457 PHE A CE1 3522 C CE2 . PHE A 457 ? 0.2258 0.2077 0.2308 0.0198 -0.0438 -0.0395 457 PHE A CE2 3523 C CZ . PHE A 457 ? 0.1907 0.2010 0.2374 0.0159 -0.0223 -0.0537 457 PHE A CZ 3524 N N . ILE A 458 ? 0.1750 0.1696 0.1720 0.0100 -0.0070 -0.0073 458 ILE A N 3525 C CA . ILE A 458 ? 0.1879 0.1614 0.1699 0.0150 -0.0097 -0.0027 458 ILE A CA 3526 C C . ILE A 458 ? 0.1811 0.1588 0.1764 0.0156 -0.0119 -0.0030 458 ILE A C 3527 O O . ILE A 458 ? 0.1911 0.1438 0.1787 0.0118 -0.0199 -0.0030 458 ILE A O 3528 C CB . ILE A 458 ? 0.1811 0.1629 0.1673 0.0216 -0.0081 0.0029 458 ILE A CB 3529 C CG1 . ILE A 458 ? 0.2169 0.1456 0.1852 0.0265 -0.0059 0.0128 458 ILE A CG1 3530 C CG2 . ILE A 458 ? 0.1960 0.1530 0.1577 0.0136 -0.0132 -0.0077 458 ILE A CG2 3531 C CD1 . ILE A 458 ? 0.2591 0.1210 0.2652 -0.0131 -0.0038 0.0210 458 ILE A CD1 3532 N N . ALA A 459 ? 0.1691 0.1587 0.1746 0.0174 -0.0076 -0.0080 459 ALA A N 3533 C CA . ALA A 459 ? 0.1650 0.1548 0.1745 0.0200 -0.0082 -0.0053 459 ALA A CA 3534 C C . ALA A 459 ? 0.1660 0.1653 0.1778 0.0164 -0.0061 -0.0088 459 ALA A C 3535 O O . ALA A 459 ? 0.1742 0.1574 0.1843 0.0214 -0.0089 -0.0058 459 ALA A O 3536 C CB . ALA A 459 ? 0.1594 0.1659 0.1687 0.0151 -0.0015 -0.0048 459 ALA A CB 3537 N N . HIS A 460 ? 0.1593 0.1632 0.1900 0.0220 -0.0068 -0.0133 460 HIS A N 3538 C CA . HIS A 460 ? 0.1570 0.1682 0.1907 0.0179 -0.0017 -0.0116 460 HIS A CA 3539 C C . HIS A 460 ? 0.1532 0.1662 0.1889 0.0173 -0.0009 -0.0133 460 HIS A C 3540 O O . HIS A 460 ? 0.1483 0.1745 0.1872 0.0112 -0.0004 -0.0081 460 HIS A O 3541 C CB . HIS A 460 ? 0.1531 0.1668 0.1821 0.0200 0.0040 -0.0042 460 HIS A CB 3542 C CG . HIS A 460 ? 0.1430 0.1781 0.1838 0.0125 0.0016 -0.0017 460 HIS A CG 3543 N ND1 . HIS A 460 ? 0.1735 0.1756 0.1920 0.0128 0.0250 0.0093 460 HIS A ND1 3544 C CD2 . HIS A 460 ? 0.1423 0.1723 0.1672 0.0094 0.0174 -0.0122 460 HIS A CD2 3545 C CE1 . HIS A 460 ? 0.1364 0.1843 0.1864 0.0049 0.0004 -0.0019 460 HIS A CE1 3546 N NE2 . HIS A 460 ? 0.1521 0.1715 0.2048 0.0207 -0.0056 -0.0163 460 HIS A NE2 3547 N N . VAL A 461 ? 0.1427 0.1607 0.1849 0.0250 -0.0024 -0.0174 461 VAL A N 3548 C CA . VAL A 461 ? 0.1570 0.1580 0.1951 0.0265 -0.0072 -0.0110 461 VAL A CA 3549 C C . VAL A 461 ? 0.1718 0.1589 0.2030 0.0258 -0.0005 -0.0108 461 VAL A C 3550 O O . VAL A 461 ? 0.1853 0.1521 0.1953 0.0304 0.0035 -0.0064 461 VAL A O 3551 C CB . VAL A 461 ? 0.1516 0.1543 0.2039 0.0225 -0.0161 -0.0133 461 VAL A CB 3552 C CG1 . VAL A 461 ? 0.1279 0.1568 0.2089 0.0421 -0.0198 -0.0062 461 VAL A CG1 3553 C CG2 . VAL A 461 ? 0.1704 0.1720 0.2165 0.0349 -0.0405 -0.0063 461 VAL A CG2 3554 N N . MET A 462 ? 0.1719 0.1558 0.1905 0.0327 0.0045 -0.0107 462 MET A N 3555 C CA . MET A 462 ? 0.1865 0.1625 0.2180 0.0355 0.0091 -0.0055 462 MET A CA 3556 C C . MET A 462 ? 0.1813 0.1690 0.2055 0.0329 0.0042 -0.0043 462 MET A C 3557 O O . MET A 462 ? 0.1770 0.1442 0.2031 0.0180 0.0008 -0.0005 462 MET A O 3558 C CB . MET A 462 ? 0.1808 0.1573 0.1988 0.0416 0.0120 -0.0075 462 MET A CB 3559 C CG . MET A 462 ? 0.1993 0.1647 0.2312 0.0539 0.0243 -0.0104 462 MET A CG 3560 S SD . MET A 462 ? 0.2096 0.1690 0.2814 0.0340 0.0278 -0.0074 462 MET A SD 3561 C CE . MET A 462 ? 0.2760 0.2068 0.2346 0.0567 0.0485 -0.0125 462 MET A CE 3562 N N . ALA A 463 ? 0.1739 0.1823 0.1993 0.0288 0.0023 -0.0042 463 ALA A N 3563 C CA . ALA A 463 ? 0.1771 0.1787 0.2069 0.0335 0.0013 -0.0018 463 ALA A CA 3564 C C . ALA A 463 ? 0.1892 0.1967 0.2131 0.0305 -0.0011 -0.0023 463 ALA A C 3565 O O . ALA A 463 ? 0.1947 0.1927 0.2250 0.0395 -0.0028 -0.0063 463 ALA A O 3566 C CB . ALA A 463 ? 0.1724 0.1904 0.2039 0.0369 -0.0075 0.0032 463 ALA A CB 3567 N N . PHE A 464 ? 0.1805 0.1961 0.2192 0.0286 -0.0103 -0.0057 464 PHE A N 3568 C CA . PHE A 464 ? 0.1866 0.1758 0.2230 0.0257 -0.0076 -0.0021 464 PHE A CA 3569 C C . PHE A 464 ? 0.1916 0.1780 0.2278 0.0257 -0.0092 0.0017 464 PHE A C 3570 O O . PHE A 464 ? 0.1953 0.1503 0.2277 0.0244 -0.0056 0.0131 464 PHE A O 3571 C CB . PHE A 464 ? 0.1804 0.1806 0.2158 0.0255 -0.0095 -0.0066 464 PHE A CB 3572 C CG . PHE A 464 ? 0.1932 0.1619 0.2241 0.0190 -0.0196 -0.0084 464 PHE A CG 3573 C CD1 . PHE A 464 ? 0.2301 0.2095 0.2483 0.0143 -0.0116 -0.0278 464 PHE A CD1 3574 C CD2 . PHE A 464 ? 0.2101 0.1693 0.2273 -0.0007 -0.0304 -0.0248 464 PHE A CD2 3575 C CE1 . PHE A 464 ? 0.2290 0.1719 0.2508 -0.0032 -0.0430 -0.0321 464 PHE A CE1 3576 C CE2 . PHE A 464 ? 0.2277 0.1740 0.2371 0.0112 -0.0216 -0.0191 464 PHE A CE2 3577 C CZ . PHE A 464 ? 0.2118 0.1887 0.2549 0.0097 -0.0184 -0.0156 464 PHE A CZ 3578 N N . ALA A 465 ? 0.1870 0.1692 0.2282 0.0299 -0.0086 0.0018 465 ALA A N 3579 C CA . ALA A 465 ? 0.1980 0.1711 0.2300 0.0226 -0.0115 -0.0029 465 ALA A CA 3580 C C . ALA A 465 ? 0.2073 0.1705 0.2325 0.0269 -0.0130 -0.0010 465 ALA A C 3581 O O . ALA A 465 ? 0.2258 0.1720 0.2352 0.0141 -0.0103 -0.0059 465 ALA A O 3582 C CB . ALA A 465 ? 0.1863 0.1580 0.2281 0.0326 -0.0139 -0.0072 465 ALA A CB 3583 N N . ALA A 466 ? 0.2085 0.1675 0.2243 0.0297 -0.0124 -0.0054 466 ALA A N 3584 C CA . ALA A 466 ? 0.2266 0.1720 0.2263 0.0294 -0.0087 0.0042 466 ALA A CA 3585 C C . ALA A 466 ? 0.2439 0.1809 0.2361 0.0304 -0.0116 0.0080 466 ALA A C 3586 O O . ALA A 466 ? 0.2480 0.1851 0.2306 0.0360 -0.0071 0.0129 466 ALA A O 3587 C CB . ALA A 466 ? 0.2333 0.1770 0.2159 0.0267 -0.0052 0.0011 466 ALA A CB 3588 N N . CYS A 467 ? 0.2556 0.1914 0.2521 0.0308 -0.0167 0.0186 467 CYS A N 3589 C CA . CYS A 467 ? 0.2778 0.1948 0.2791 0.0297 -0.0201 0.0176 467 CYS A CA 3590 C C . CYS A 467 ? 0.2776 0.2038 0.2781 0.0341 -0.0172 0.0264 467 CYS A C 3591 O O . CYS A 467 ? 0.2909 0.2041 0.2882 0.0386 -0.0182 0.0360 467 CYS A O 3592 C CB . CYS A 467 ? 0.2862 0.2150 0.2923 0.0315 -0.0248 0.0184 467 CYS A CB 3593 S SG . CYS A 467 ? 0.3669 0.2497 0.3723 0.0353 -0.0450 -0.0031 467 CYS A SG 3594 N N . LEU A 468 ? 0.2694 0.1859 0.2716 0.0290 -0.0158 0.0243 468 LEU A N 3595 C CA . LEU A 468 ? 0.2728 0.2004 0.2748 0.0267 -0.0140 0.0234 468 LEU A CA 3596 C C . LEU A 468 ? 0.2726 0.2069 0.2822 0.0206 -0.0193 0.0200 468 LEU A C 3597 O O . LEU A 468 ? 0.2551 0.2008 0.2685 0.0175 -0.0204 0.0124 468 LEU A O 3598 C CB . LEU A 468 ? 0.2669 0.1920 0.2732 0.0309 -0.0127 0.0185 468 LEU A CB 3599 C CG . LEU A 468 ? 0.2812 0.1902 0.2764 0.0303 -0.0073 0.0263 468 LEU A CG 3600 C CD1 . LEU A 468 ? 0.2089 0.1654 0.2778 0.0511 -0.0076 0.0012 468 LEU A CD1 3601 C CD2 . LEU A 468 ? 0.3163 0.2306 0.2587 0.0358 0.0025 0.0148 468 LEU A CD2 3602 N N . GLU A 469 ? 0.2888 0.2291 0.2831 0.0161 -0.0270 0.0209 469 GLU A N 3603 C CA . GLU A 469 ? 0.3122 0.2610 0.3075 0.0057 -0.0307 0.0206 469 GLU A CA 3604 C C . GLU A 469 ? 0.2920 0.2528 0.2926 0.0077 -0.0221 0.0144 469 GLU A C 3605 O O . GLU A 469 ? 0.3070 0.2522 0.2885 0.0106 -0.0164 0.0044 469 GLU A O 3606 C CB . GLU A 469 ? 0.3128 0.2604 0.2946 0.0071 -0.0355 0.0221 469 GLU A CB 3607 C CG . GLU A 469 ? 0.3611 0.3175 0.3544 -0.0088 -0.0438 0.0238 469 GLU A CG 3608 C CD . GLU A 469 ? 0.3882 0.3121 0.3588 -0.0073 -0.0482 0.0290 469 GLU A CD 3609 O OE1 . GLU A 469 ? 0.4717 0.4114 0.4617 -0.0067 -0.0631 0.0490 469 GLU A OE1 3610 O OE2 . GLU A 469 ? 0.4961 0.3900 0.4501 -0.0209 -0.0521 0.0309 469 GLU A OE2 3611 N N . PRO A 470 ? 0.2884 0.2523 0.2980 0.0104 -0.0137 0.0103 470 PRO A N 3612 C CA . PRO A 470 ? 0.2829 0.2448 0.2998 0.0124 -0.0093 0.0099 470 PRO A CA 3613 C C . PRO A 470 ? 0.2849 0.2400 0.3022 0.0191 -0.0065 0.0111 470 PRO A C 3614 O O . PRO A 470 ? 0.2830 0.2421 0.3113 0.0219 -0.0020 0.0094 470 PRO A O 3615 C CB . PRO A 470 ? 0.2867 0.2491 0.3019 0.0144 -0.0065 0.0138 470 PRO A CB 3616 C CG . PRO A 470 ? 0.2744 0.2494 0.2970 0.0067 -0.0096 0.0127 470 PRO A CG 3617 C CD . PRO A 470 ? 0.2837 0.2437 0.2938 0.0106 -0.0095 0.0112 470 PRO A CD 3618 N N . TYR A 471 ? 0.2735 0.2246 0.2970 0.0251 -0.0136 0.0152 471 TYR A N 3619 C CA . TYR A 471 ? 0.2807 0.2391 0.2928 0.0302 -0.0142 0.0177 471 TYR A CA 3620 C C . TYR A 471 ? 0.2967 0.2363 0.3049 0.0363 -0.0177 0.0202 471 TYR A C 3621 O O . TYR A 471 ? 0.2944 0.2364 0.3080 0.0352 -0.0139 0.0280 471 TYR A O 3622 C CB . TYR A 471 ? 0.2659 0.2234 0.2788 0.0309 -0.0186 0.0180 471 TYR A CB 3623 C CG . TYR A 471 ? 0.2497 0.2241 0.2668 0.0278 -0.0267 0.0131 471 TYR A CG 3624 C CD1 . TYR A 471 ? 0.2169 0.2128 0.2660 0.0217 -0.0248 0.0064 471 TYR A CD1 3625 C CD2 . TYR A 471 ? 0.2607 0.2209 0.2386 0.0192 -0.0226 0.0084 471 TYR A CD2 3626 C CE1 . TYR A 471 ? 0.2238 0.2251 0.2632 0.0147 -0.0227 0.0143 471 TYR A CE1 3627 C CE2 . TYR A 471 ? 0.2490 0.2047 0.2538 0.0060 -0.0264 -0.0045 471 TYR A CE2 3628 C CZ . TYR A 471 ? 0.2314 0.2068 0.2402 0.0297 -0.0230 0.0073 471 TYR A CZ 3629 O OH . TYR A 471 ? 0.2456 0.1931 0.2531 0.0540 -0.0229 0.0099 471 TYR A OH 3630 N N . THR A 472 ? 0.3165 0.2579 0.3166 0.0429 -0.0192 0.0196 472 THR A N 3631 C CA . THR A 472 ? 0.3366 0.2792 0.3362 0.0451 -0.0222 0.0202 472 THR A CA 3632 C C . THR A 472 ? 0.3457 0.2966 0.3497 0.0446 -0.0211 0.0161 472 THR A C 3633 O O . THR A 472 ? 0.3574 0.2930 0.3612 0.0473 -0.0267 0.0227 472 THR A O 3634 C CB . THR A 472 ? 0.3322 0.2834 0.3362 0.0460 -0.0214 0.0237 472 THR A CB 3635 O OG1 . THR A 472 ? 0.3500 0.2784 0.3590 0.0633 -0.0352 0.0386 472 THR A OG1 3636 C CG2 . THR A 472 ? 0.3369 0.2732 0.3156 0.0467 -0.0289 0.0129 472 THR A CG2 3637 N N . ALA A 473 ? 0.3571 0.3147 0.3622 0.0497 -0.0200 0.0076 473 ALA A N 3638 C CA . ALA A 473 ? 0.3716 0.3384 0.3757 0.0436 -0.0141 -0.0048 473 ALA A CA 3639 C C . ALA A 473 ? 0.3816 0.3489 0.3840 0.0397 -0.0087 -0.0119 473 ALA A C 3640 O O . ALA A 473 ? 0.3890 0.3576 0.3898 0.0417 -0.0040 -0.0161 473 ALA A O 3641 C CB . ALA A 473 ? 0.3706 0.3385 0.3795 0.0454 -0.0113 -0.0037 473 ALA A CB 3642 N N . CYS A 474 ? 0.3837 0.3599 0.3907 0.0353 -0.0050 -0.0187 474 CYS A N 3643 C CA . CYS A 474 ? 0.3943 0.3625 0.3978 0.0313 -0.0046 -0.0198 474 CYS A CA 3644 C C . CYS A 474 ? 0.3956 0.3625 0.4000 0.0290 0.0032 -0.0181 474 CYS A C 3645 O O . CYS A 474 ? 0.3961 0.3591 0.4008 0.0294 0.0038 -0.0120 474 CYS A O 3646 C CB . CYS A 474 ? 0.3901 0.3585 0.3895 0.0339 -0.0064 -0.0230 474 CYS A CB 3647 S SG . CYS A 474 ? 0.4115 0.3487 0.4145 0.0399 -0.0154 -0.0397 474 CYS A SG 3648 N N . ASP A 475 ? 0.4018 0.3665 0.4098 0.0259 0.0074 -0.0158 475 ASP A N 3649 C CA . ASP A 475 ? 0.4109 0.3695 0.4158 0.0207 0.0118 -0.0157 475 ASP A CA 3650 C C . ASP A 475 ? 0.3998 0.3596 0.4004 0.0182 0.0105 -0.0179 475 ASP A C 3651 O O . ASP A 475 ? 0.4080 0.3739 0.4024 0.0179 0.0131 -0.0265 475 ASP A O 3652 C CB . ASP A 475 ? 0.4214 0.3799 0.4326 0.0234 0.0165 -0.0115 475 ASP A CB 3653 C CG . ASP A 475 ? 0.4770 0.4160 0.4898 0.0169 0.0252 0.0025 475 ASP A CG 3654 O OD1 . ASP A 475 ? 0.5326 0.4644 0.5532 0.0133 0.0321 0.0037 475 ASP A OD1 3655 O OD2 . ASP A 475 ? 0.5662 0.4919 0.5577 0.0220 0.0332 0.0119 475 ASP A OD2 3656 N N . LEU A 476 ? 0.3858 0.3337 0.3806 0.0197 0.0116 -0.0147 476 LEU A N 3657 C CA . LEU A 476 ? 0.3746 0.3156 0.3626 0.0199 0.0044 -0.0086 476 LEU A CA 3658 C C . LEU A 476 ? 0.3765 0.3088 0.3574 0.0179 0.0064 -0.0050 476 LEU A C 3659 O O . LEU A 476 ? 0.3781 0.3079 0.3570 0.0168 0.0050 0.0034 476 LEU A O 3660 C CB . LEU A 476 ? 0.3641 0.3027 0.3574 0.0226 0.0027 -0.0082 476 LEU A CB 3661 C CG . LEU A 476 ? 0.3477 0.2857 0.3370 0.0286 -0.0037 -0.0044 476 LEU A CG 3662 C CD1 . LEU A 476 ? 0.3203 0.2518 0.3310 0.0368 -0.0182 0.0072 476 LEU A CD1 3663 C CD2 . LEU A 476 ? 0.3376 0.2919 0.3040 0.0378 0.0035 0.0079 476 LEU A CD2 3664 N N . ALA A 477 ? 0.3787 0.3077 0.3500 0.0188 0.0062 -0.0050 477 ALA A N 3665 C CA . ALA A 477 ? 0.3869 0.3037 0.3510 0.0193 0.0094 -0.0024 477 ALA A CA 3666 C C . ALA A 477 ? 0.3974 0.3144 0.3542 0.0143 0.0089 -0.0001 477 ALA A C 3667 O O . ALA A 477 ? 0.3940 0.2939 0.3501 0.0213 0.0118 -0.0012 477 ALA A O 3668 C CB . ALA A 477 ? 0.3803 0.3061 0.3442 0.0214 0.0056 -0.0031 477 ALA A CB 3669 N N . PRO A 478 ? 0.4086 0.3174 0.3622 0.0119 0.0106 0.0024 478 PRO A N 3670 C CA . PRO A 478 ? 0.4170 0.3215 0.3638 0.0087 0.0122 0.0013 478 PRO A CA 3671 C C . PRO A 478 ? 0.4268 0.3261 0.3716 0.0027 0.0119 0.0002 478 PRO A C 3672 O O . PRO A 478 ? 0.4341 0.3232 0.3674 0.0039 0.0139 0.0022 478 PRO A O 3673 C CB . PRO A 478 ? 0.4255 0.3245 0.3647 0.0112 0.0122 0.0049 478 PRO A CB 3674 C CG . PRO A 478 ? 0.4203 0.3179 0.3624 0.0157 0.0149 0.0055 478 PRO A CG 3675 C CD . PRO A 478 ? 0.4145 0.3242 0.3634 0.0120 0.0114 0.0034 478 PRO A CD 3676 N N . PRO A 479 ? 0.4301 0.3294 0.3768 0.0004 0.0126 -0.0021 479 PRO A N 3677 C CA . PRO A 479 ? 0.4279 0.3292 0.3811 -0.0035 0.0123 -0.0009 479 PRO A CA 3678 C C . PRO A 479 ? 0.4376 0.3359 0.3931 -0.0071 0.0148 -0.0049 479 PRO A C 3679 O O . PRO A 479 ? 0.4386 0.3136 0.3791 -0.0086 0.0133 -0.0028 479 PRO A O 3680 C CB . PRO A 479 ? 0.4305 0.3261 0.3798 -0.0012 0.0105 -0.0008 479 PRO A CB 3681 C CG . PRO A 479 ? 0.4189 0.3186 0.3709 -0.0009 0.0124 0.0030 479 PRO A CG 3682 C CD . PRO A 479 ? 0.4294 0.3315 0.3754 -0.0013 0.0101 -0.0042 479 PRO A CD 3683 N N . ALA A 480 ? 0.4374 0.3448 0.4040 -0.0101 0.0147 -0.0029 480 ALA A N 3684 C CA . ALA A 480 ? 0.4503 0.3712 0.4311 -0.0164 0.0213 -0.0037 480 ALA A CA 3685 C C . ALA A 480 ? 0.4621 0.3916 0.4494 -0.0180 0.0223 -0.0049 480 ALA A C 3686 O O . ALA A 480 ? 0.4590 0.3732 0.4568 -0.0215 0.0290 -0.0062 480 ALA A O 3687 C CB . ALA A 480 ? 0.4431 0.3676 0.4268 -0.0191 0.0177 0.0021 480 ALA A CB 3688 N N . GLY A 481 ? 0.4759 0.4133 0.4683 -0.0148 0.0230 -0.0067 481 GLY A N 3689 C CA . GLY A 481 ? 0.4952 0.4567 0.4852 -0.0078 0.0175 -0.0042 481 GLY A CA 3690 C C . GLY A 481 ? 0.5106 0.4803 0.4948 -0.0040 0.0129 -0.0049 481 GLY A C 3691 O O . GLY A 481 ? 0.5222 0.4940 0.4977 -0.0053 0.0124 -0.0072 481 GLY A O 3692 N N A PHE B . ? 0.5293 0.5836 0.5245 0.0183 -0.0023 -0.0113 912 PHE A N 3693 C CA A PHE B . ? 0.5435 0.6010 0.5407 0.0146 -0.0032 -0.0099 912 PHE A CA 3694 C C A PHE B . ? 0.5444 0.6016 0.5404 0.0159 -0.0025 -0.0104 912 PHE A C 3695 O O A PHE B . ? 0.5426 0.6055 0.5412 0.0146 -0.0035 -0.0100 912 PHE A O 3696 C CB A PHE B . ? 0.5450 0.5957 0.5467 0.0122 -0.0022 -0.0114 912 PHE A CB 3697 C CG A PHE B . ? 0.5514 0.5901 0.5564 0.0104 0.0015 -0.0151 912 PHE A CG 3698 C CD1 A PHE B . ? 0.5541 0.5850 0.5655 0.0070 0.0000 -0.0174 912 PHE A CD1 3699 C CD2 A PHE B . ? 0.5631 0.6015 0.5785 0.0152 0.0038 -0.0217 912 PHE A CD2 3700 C CE1 A PHE B . ? 0.5509 0.5816 0.5692 0.0090 0.0106 -0.0264 912 PHE A CE1 3701 C CE2 A PHE B . ? 0.5750 0.5944 0.5820 0.0159 0.0089 -0.0235 912 PHE A CE2 3702 C CZ A PHE B . ? 0.5682 0.5874 0.5719 0.0167 0.0115 -0.0277 912 PHE A CZ 3703 O OXT A PHE B . ? 0.5447 0.6058 0.5402 0.0182 -0.0034 -0.0111 912 PHE A OXT 3704 N N B PHE C . ? 0.6149 0.6100 0.6331 -0.0499 0.0247 0.0142 923 PHE A N 3705 C CA B PHE C . ? 0.6172 0.6129 0.6342 -0.0517 0.0262 0.0163 923 PHE A CA 3706 C C B PHE C . ? 0.6183 0.6159 0.6365 -0.0518 0.0274 0.0135 923 PHE A C 3707 O O B PHE C . ? 0.6178 0.6167 0.6335 -0.0557 0.0314 0.0143 923 PHE A O 3708 C CB B PHE C . ? 0.6141 0.6099 0.6256 -0.0556 0.0292 0.0191 923 PHE A CB 3709 C CG B PHE C . ? 0.6151 0.6037 0.6174 -0.0623 0.0380 0.0274 923 PHE A CG 3710 C CD1 B PHE C . ? 0.5961 0.5873 0.6002 -0.0700 0.0423 0.0410 923 PHE A CD1 3711 C CD2 B PHE C . ? 0.6164 0.6088 0.6106 -0.0691 0.0434 0.0301 923 PHE A CD2 3712 C CE1 B PHE C . ? 0.5883 0.5876 0.5915 -0.0778 0.0488 0.0381 923 PHE A CE1 3713 C CE2 B PHE C . ? 0.6108 0.6009 0.6001 -0.0785 0.0403 0.0259 923 PHE A CE2 3714 C CZ B PHE C . ? 0.5913 0.5955 0.5951 -0.0688 0.0405 0.0313 923 PHE A CZ 3715 O OXT B PHE C . ? 0.6169 0.6147 0.6400 -0.0506 0.0254 0.0133 923 PHE A OXT 3716 C C1 . NAG D . ? 0.3971 0.3330 0.4857 -0.0202 0.0382 -0.0011 801 NAG A C1 3717 C C2 . NAG D . ? 0.4173 0.3373 0.5235 -0.0269 0.0481 0.0046 801 NAG A C2 3718 C C3 . NAG D . ? 0.4575 0.3610 0.5636 -0.0281 0.0517 0.0070 801 NAG A C3 3719 C C4 . NAG D . ? 0.4902 0.3953 0.5999 -0.0229 0.0548 0.0144 801 NAG A C4 3720 C C5 . NAG D . ? 0.4957 0.3980 0.5912 -0.0151 0.0556 0.0135 801 NAG A C5 3721 C C6 . NAG D . ? 0.5285 0.3909 0.6154 -0.0064 0.0594 0.0190 801 NAG A C6 3722 C C7 . NAG D . ? 0.3330 0.3300 0.4781 -0.0455 0.0266 -0.0118 801 NAG A C7 3723 C C8 . NAG D . ? 0.3054 0.2821 0.4541 -0.0438 0.0127 -0.0209 801 NAG A C8 3724 N N2 . NAG D . ? 0.3562 0.3145 0.4811 -0.0456 0.0372 -0.0017 801 NAG A N2 3725 O O3 . NAG D . ? 0.4769 0.3088 0.5539 -0.0306 0.0219 0.0222 801 NAG A O3 3726 O O4 . NAG D . ? 0.5373 0.4493 0.6599 -0.0213 0.0381 0.0238 801 NAG A O4 3727 O O5 . NAG D . ? 0.4367 0.3435 0.5413 -0.0286 0.0495 -0.0036 801 NAG A O5 3728 O O6 . NAG D . ? 0.5882 0.4741 0.6557 -0.0111 0.0380 0.0522 801 NAG A O6 3729 O O7 . NAG D . ? 0.2739 0.3176 0.4631 -0.0553 0.0162 -0.0045 801 NAG A O7 3730 C C1 . NAG E . ? 0.5581 0.4896 0.6960 -0.0319 0.0308 0.0279 802 NAG A C1 3731 C C2 . NAG E . ? 0.5823 0.5253 0.7252 -0.0232 0.0241 0.0280 802 NAG A C2 3732 C C3 . NAG E . ? 0.5783 0.5238 0.7222 -0.0249 0.0252 0.0372 802 NAG A C3 3733 C C4 . NAG E . ? 0.5729 0.5144 0.7040 -0.0232 0.0255 0.0360 802 NAG A C4 3734 C C5 . NAG E . ? 0.5695 0.5157 0.7003 -0.0205 0.0241 0.0285 802 NAG A C5 3735 C C6 . NAG E . ? 0.5605 0.5012 0.6945 -0.0085 0.0268 0.0304 802 NAG A C6 3736 C C7 . NAG E . ? 0.6499 0.5892 0.7623 -0.0156 0.0004 0.0250 802 NAG A C7 3737 C C8 . NAG E . ? 0.6583 0.5905 0.7636 -0.0112 -0.0043 0.0155 802 NAG A C8 3738 N N2 . NAG E . ? 0.6115 0.5681 0.7482 -0.0166 0.0119 0.0211 802 NAG A N2 3739 O O3 . NAG E . ? 0.5763 0.5348 0.7388 -0.0388 0.0340 0.0478 802 NAG A O3 3740 O O4 . NAG E . ? 0.5710 0.5251 0.7104 -0.0152 0.0108 0.0337 802 NAG A O4 3741 O O5 . NAG E . ? 0.5598 0.4867 0.6976 -0.0323 0.0328 0.0313 802 NAG A O5 3742 O O6 . NAG E . ? 0.5407 0.4989 0.6895 -0.0141 0.0255 0.0251 802 NAG A O6 3743 O O7 . NAG E . ? 0.6603 0.5900 0.7604 -0.0291 -0.0056 0.0388 802 NAG A O7 3744 C C1 . NAG F . ? 0.4319 0.4241 0.2715 0.0539 0.0821 -0.0014 803 NAG A C1 3745 C C2 . NAG F . ? 0.4876 0.4809 0.3031 0.0470 0.0913 0.0013 803 NAG A C2 3746 C C3 . NAG F . ? 0.5284 0.4931 0.3417 0.0561 0.0818 -0.0112 803 NAG A C3 3747 C C4 . NAG F . ? 0.5461 0.5012 0.3513 0.0574 0.0726 -0.0082 803 NAG A C4 3748 C C5 . NAG F . ? 0.5160 0.4683 0.3268 0.0572 0.0705 0.0001 803 NAG A C5 3749 C C6 . NAG F . ? 0.5269 0.4560 0.3224 0.0608 0.0528 0.0255 803 NAG A C6 3750 C C7 . NAG F . ? 0.4935 0.5191 0.3608 0.0052 0.0852 0.0304 803 NAG A C7 3751 C C8 . NAG F . ? 0.4702 0.5355 0.3817 0.0063 0.0943 0.0327 803 NAG A C8 3752 N N2 . NAG F . ? 0.4782 0.5052 0.3316 0.0258 0.0923 0.0087 803 NAG A N2 3753 O O3 . NAG F . ? 0.5429 0.5234 0.3305 0.0630 0.1055 -0.0148 803 NAG A O3 3754 O O4 . NAG F . ? 0.6255 0.5444 0.4372 0.0527 0.0567 -0.0118 803 NAG A O4 3755 O O5 . NAG F . ? 0.4700 0.4408 0.2978 0.0518 0.0864 -0.0102 803 NAG A O5 3756 O O6 . NAG F . ? 0.5581 0.4477 0.3176 0.0750 0.0527 0.0506 803 NAG A O6 3757 O O7 . NAG F . ? 0.5017 0.5533 0.3895 -0.0116 0.0852 0.0504 803 NAG A O7 3758 C C1 . NAG G . ? 0.7019 0.6199 0.5089 0.0452 0.0424 -0.0056 804 NAG A C1 3759 C C2 . NAG G . ? 0.7426 0.6454 0.5352 0.0385 0.0378 -0.0012 804 NAG A C2 3760 C C3 . NAG G . ? 0.7610 0.6651 0.5467 0.0374 0.0365 -0.0060 804 NAG A C3 3761 C C4 . NAG G . ? 0.7551 0.6755 0.5485 0.0385 0.0345 -0.0133 804 NAG A C4 3762 C C5 . NAG G . ? 0.7404 0.6746 0.5375 0.0432 0.0343 -0.0197 804 NAG A C5 3763 C C6 . NAG G . ? 0.7364 0.6852 0.5363 0.0438 0.0366 -0.0242 804 NAG A C6 3764 C C7 . NAG G . ? 0.7654 0.6727 0.5713 0.0180 0.0369 0.0122 804 NAG A C7 3765 C C8 . NAG G . ? 0.7572 0.6775 0.5854 0.0194 0.0359 0.0234 804 NAG A C8 3766 N N2 . NAG G . ? 0.7572 0.6598 0.5506 0.0272 0.0377 0.0091 804 NAG A N2 3767 O O3 . NAG G . ? 0.7907 0.6886 0.5587 0.0338 0.0382 -0.0101 804 NAG A O3 3768 O O4 . NAG G . ? 0.7661 0.6960 0.5662 0.0283 0.0245 -0.0157 804 NAG A O4 3769 O O5 . NAG G . ? 0.7247 0.6488 0.5338 0.0490 0.0405 -0.0173 804 NAG A O5 3770 O O6 . NAG G . ? 0.7336 0.7173 0.5336 0.0431 0.0428 -0.0355 804 NAG A O6 3771 O O7 . NAG G . ? 0.7692 0.6815 0.5775 0.0017 0.0380 0.0166 804 NAG A O7 3772 ZN ZN . ZN H . ? 0.1680 0.1581 0.1989 0.0147 -0.0027 0.0112 901 ZN A ZN 3773 ZN ZN . ZN I . ? 0.1471 0.2044 0.1709 0.0070 -0.0127 0.0052 902 ZN A ZN 3774 MG MG . MG J . ? 0.1545 0.1515 0.1028 -0.0447 -0.0055 0.0469 903 MG A MG 3775 CA CA . CA K . ? 0.1875 0.2273 0.1924 -0.0160 0.0340 -0.0172 904 CA A CA 3776 C C . ACT L . ? 0.5752 0.6426 0.6677 0.0601 -0.0082 0.0029 933 ACT A C 3777 O O . ACT L . ? 0.5647 0.6360 0.6611 0.0611 -0.0126 -0.0020 933 ACT A O 3778 O OXT . ACT L . ? 0.5760 0.6446 0.6689 0.0627 -0.0076 0.0065 933 ACT A OXT 3779 C CH3 . ACT L . ? 0.5709 0.6438 0.6644 0.0570 -0.0118 0.0031 933 ACT A CH3 3780 C C . ACT M . ? 0.6336 0.6679 0.7302 -0.0142 -0.0155 0.0148 934 ACT A C 3781 O O . ACT M . ? 0.6326 0.6653 0.7307 -0.0151 -0.0144 0.0154 934 ACT A O 3782 O OXT . ACT M . ? 0.6336 0.6697 0.7322 -0.0136 -0.0169 0.0171 934 ACT A OXT 3783 C CH3 . ACT M . ? 0.6333 0.6643 0.7287 -0.0130 -0.0141 0.0130 934 ACT A CH3 3784 C C . ACT N . ? 0.6341 0.6563 0.6087 0.0074 0.0288 -0.0284 935 ACT A C 3785 O O . ACT N . ? 0.6304 0.6533 0.6045 0.0052 0.0320 -0.0261 935 ACT A O 3786 O OXT . ACT N . ? 0.6350 0.6536 0.6084 0.0097 0.0311 -0.0335 935 ACT A OXT 3787 C CH3 . ACT N . ? 0.6282 0.6580 0.6068 0.0071 0.0227 -0.0286 935 ACT A CH3 3788 C C1 . GOL O . ? 0.4774 0.3986 0.4570 0.0877 -0.0820 -0.1011 936 GOL A C1 3789 O O1 . GOL O . ? 0.4394 0.3760 0.4016 0.0893 -0.0723 -0.0866 936 GOL A O1 3790 C C2 . GOL O . ? 0.5003 0.4274 0.4787 0.0816 -0.0873 -0.1106 936 GOL A C2 3791 O O2 . GOL O . ? 0.4861 0.4372 0.4933 0.0804 -0.1015 -0.1232 936 GOL A O2 3792 C C3 . GOL O . ? 0.4938 0.4121 0.4975 0.0876 -0.0808 -0.1167 936 GOL A C3 3793 O O3 . GOL O . ? 0.5348 0.4110 0.5045 0.0623 -0.0827 -0.1415 936 GOL A O3 3794 C C1 . GOL P . ? 0.6709 0.5784 0.6261 0.0501 0.0019 -0.0413 937 GOL A C1 3795 O O1 . GOL P . ? 0.6710 0.5875 0.6293 0.0371 -0.0143 -0.0170 937 GOL A O1 3796 C C2 . GOL P . ? 0.6719 0.5726 0.6280 0.0594 0.0001 -0.0498 937 GOL A C2 3797 O O2 . GOL P . ? 0.6678 0.5607 0.6321 0.0660 -0.0061 -0.0604 937 GOL A O2 3798 C C3 . GOL P . ? 0.6663 0.5799 0.6138 0.0593 0.0104 -0.0557 937 GOL A C3 3799 O O3 . GOL P . ? 0.6258 0.5740 0.5939 0.0624 0.0109 -0.0633 937 GOL A O3 3800 O O . HOH Q . ? 0.1526 0.1428 0.1766 0.0469 -0.0439 -0.0596 1001 HOH A O 3801 O O . HOH Q . ? 0.1717 0.1730 0.1914 0.0267 -0.0365 0.0003 1002 HOH A O 3802 O O . HOH Q . ? 0.1249 0.1588 0.1421 0.0357 -0.0150 -0.0297 1003 HOH A O 3803 O O . HOH Q . ? 0.1344 0.2344 0.2015 -0.0011 0.0005 0.0431 1004 HOH A O 3804 O O . HOH Q . ? 0.3038 0.3787 0.2249 0.1303 -0.0358 -0.1145 1005 HOH A O 3805 O O . HOH Q . ? 0.1454 0.1844 0.2705 -0.0031 0.0252 -0.0095 1006 HOH A O 3806 O O . HOH Q . ? 0.2024 0.1349 0.2506 -0.0078 -0.0196 -0.0351 1007 HOH A O 3807 O O . HOH Q . ? 0.1468 0.2862 0.1951 -0.0367 0.0295 0.0606 1008 HOH A O 3808 O O . HOH Q . ? 0.1929 0.1857 0.1312 0.0076 0.0209 -0.0376 1009 HOH A O 3809 O O . HOH Q . ? 0.1790 0.1747 0.1511 -0.0153 0.0677 -0.0580 1010 HOH A O 3810 O O . HOH Q . ? 0.1734 0.1398 0.2690 0.0035 -0.0066 0.0238 1011 HOH A O 3811 O O . HOH Q . ? 0.1725 0.2325 0.1867 -0.0762 -0.0332 -0.0276 1012 HOH A O 3812 O O . HOH Q . ? 0.1274 0.2049 0.2021 0.0352 -0.0223 0.0383 1013 HOH A O 3813 O O . HOH Q . ? 0.1023 0.1501 0.2025 0.0031 0.0184 -0.0138 1014 HOH A O 3814 O O . HOH Q . ? 0.1576 0.1677 0.2247 0.0107 0.0114 -0.0193 1015 HOH A O 3815 O O . HOH Q . ? 0.1320 0.2292 0.2515 -0.0005 -0.0322 0.0221 1016 HOH A O 3816 O O . HOH Q . ? 0.1774 0.1061 0.1137 -0.0742 0.0177 -0.0048 1017 HOH A O 3817 O O . HOH Q . ? 0.1448 0.1323 0.1912 -0.0234 0.0071 0.0203 1018 HOH A O 3818 O O . HOH Q . ? 0.1884 0.2071 0.2023 0.0040 -0.0197 0.0347 1019 HOH A O 3819 O O . HOH Q . ? 0.1781 0.1718 0.1757 0.0245 0.0070 0.0317 1020 HOH A O 3820 O O . HOH Q . ? 0.3073 0.2516 0.2367 0.1159 -0.0002 0.0214 1021 HOH A O 3821 O O . HOH Q . ? 0.1266 0.1832 0.1964 0.0120 -0.0342 -0.0166 1022 HOH A O 3822 O O . HOH Q . ? 0.2103 0.3960 0.2308 -0.0355 0.0733 -0.0378 1023 HOH A O 3823 O O . HOH Q . ? 0.1671 0.2305 0.1893 0.0086 0.0241 -0.0007 1024 HOH A O 3824 O O . HOH Q . ? 0.1790 0.2160 0.2498 0.0118 0.0863 0.0109 1025 HOH A O 3825 O O . HOH Q . ? 0.1590 0.1796 0.1717 0.0438 0.0224 -0.0358 1026 HOH A O 3826 O O . HOH Q . ? 0.3024 0.2815 0.1836 0.1093 0.1075 0.1309 1027 HOH A O 3827 O O . HOH Q . ? 0.1720 0.2359 0.1537 0.0080 -0.0477 0.0145 1028 HOH A O 3828 O O . HOH Q . ? 0.3611 0.1475 0.0693 -0.1319 0.0675 -0.0622 1029 HOH A O 3829 O O . HOH Q . ? 0.2663 0.5501 0.2593 0.0200 0.0159 -0.0889 1030 HOH A O 3830 O O . HOH Q . ? 0.1250 0.1731 0.1058 -0.0509 0.0396 0.0238 1031 HOH A O 3831 O O . HOH Q . ? 0.2433 0.2198 0.1704 0.0071 -0.0423 0.0082 1032 HOH A O 3832 O O . HOH Q . ? 0.2608 0.2839 0.2422 0.0485 -0.0878 -0.0417 1033 HOH A O 3833 O O . HOH Q . ? 0.1501 0.1720 0.1762 0.0699 -0.0358 0.0374 1034 HOH A O 3834 O O . HOH Q . ? 0.2210 0.1934 0.1959 0.0286 0.0570 -0.0005 1035 HOH A O 3835 O O . HOH Q . ? 0.1774 0.1620 0.2294 0.0164 -0.0422 -0.0433 1036 HOH A O 3836 O O . HOH Q . ? 0.2331 0.1262 0.1575 -0.0411 -0.0281 -0.0329 1037 HOH A O 3837 O O . HOH Q . ? 0.1942 0.1349 0.1873 -0.0152 -0.0380 -0.0055 1038 HOH A O 3838 O O . HOH Q . ? 0.1341 0.1877 0.1559 0.0138 -0.0163 -0.0017 1039 HOH A O 3839 O O . HOH Q . ? 0.1534 0.1491 0.1594 -0.0196 0.0027 0.0209 1040 HOH A O 3840 O O . HOH Q . ? 0.1712 0.1438 0.1294 -0.0341 0.0012 -0.0206 1041 HOH A O 3841 O O . HOH Q . ? 0.4875 0.2748 0.2556 0.1340 0.0235 0.0146 1042 HOH A O 3842 O O . HOH Q . ? 0.1931 0.0935 0.1994 0.0277 -0.0511 -0.0243 1043 HOH A O 3843 O O . HOH Q . ? 0.1390 0.1395 0.1594 0.0083 0.0272 -0.0229 1044 HOH A O 3844 O O . HOH Q . ? 0.1943 0.2077 0.1801 -0.0135 -0.0311 0.0097 1045 HOH A O 3845 O O . HOH Q . ? 0.1984 0.1636 0.2709 -0.0274 -0.0502 -0.0188 1046 HOH A O 3846 O O . HOH Q . ? 0.1766 0.1173 0.2477 -0.0076 -0.0153 -0.0494 1047 HOH A O 3847 O O . HOH Q . ? 0.2333 0.1349 0.1103 0.0240 -0.0274 0.0127 1048 HOH A O 3848 O O . HOH Q . ? 0.1865 0.2315 0.2687 0.0528 -0.0536 0.0854 1049 HOH A O 3849 O O . HOH Q . ? 0.2573 0.2795 0.2470 -0.0077 0.0004 0.0594 1050 HOH A O 3850 O O . HOH Q . ? 0.1971 0.1789 0.1283 -0.0347 0.0282 -0.0024 1051 HOH A O 3851 O O . HOH Q . ? 0.3884 0.2336 0.1852 0.0030 -0.0089 0.0467 1052 HOH A O 3852 O O . HOH Q . ? 0.1713 0.1364 0.1716 0.0581 0.0523 0.0505 1053 HOH A O 3853 O O . HOH Q . ? 0.2496 0.2755 0.1980 0.0459 -0.0071 -0.0011 1054 HOH A O 3854 O O . HOH Q . ? 0.1708 0.2743 0.2951 -0.0103 0.0252 0.0721 1055 HOH A O 3855 O O . HOH Q . ? 0.3442 0.4027 0.3522 -0.1725 0.0811 -0.1798 1056 HOH A O 3856 O O . HOH Q . ? 0.3809 0.1967 0.3099 0.0399 -0.0292 -0.0399 1057 HOH A O 3857 O O . HOH Q . ? 0.3333 0.1570 0.1957 -0.0545 0.0292 0.0653 1058 HOH A O 3858 O O . HOH Q . ? 0.1457 0.2231 0.1665 0.0401 -0.0661 -0.0436 1059 HOH A O 3859 O O . HOH Q . ? 0.2941 0.1319 0.3375 0.0368 -0.1093 -0.0090 1060 HOH A O 3860 O O . HOH Q . ? 0.1810 0.1982 0.2168 0.0113 -0.0180 0.0259 1061 HOH A O 3861 O O . HOH Q . ? 0.1318 0.1579 0.2543 -0.0074 -0.0011 -0.0141 1062 HOH A O 3862 O O . HOH Q . ? 0.4974 0.3254 0.2538 -0.0402 0.0083 0.0680 1063 HOH A O 3863 O O . HOH Q . ? 0.1845 0.2499 0.2387 -0.0024 -0.0293 0.0097 1064 HOH A O 3864 O O . HOH Q . ? 0.1787 0.3094 0.2844 0.0218 0.0467 -0.0118 1065 HOH A O 3865 O O . HOH Q . ? 0.2452 0.1723 0.3444 0.0533 0.1669 0.0107 1066 HOH A O 3866 O O . HOH Q . ? 0.2350 0.1831 0.1608 -0.0316 0.0154 -0.0616 1067 HOH A O 3867 O O . HOH Q . ? 0.2161 0.4922 0.2699 0.0278 0.0884 -0.1004 1068 HOH A O 3868 O O . HOH Q . ? 0.3694 0.3240 0.1594 0.0135 0.0126 0.0769 1069 HOH A O 3869 O O . HOH Q . ? 0.3735 0.1853 0.3431 -0.0168 -0.0470 -0.0462 1070 HOH A O 3870 O O . HOH Q . ? 0.4044 0.2008 0.2442 0.1035 -0.0676 -0.0979 1071 HOH A O 3871 O O . HOH Q . ? 0.4901 0.2606 0.4519 0.0906 0.2547 0.0657 1072 HOH A O 3872 O O . HOH Q . ? 0.2771 0.2434 0.2381 -0.0721 0.0169 -0.0478 1073 HOH A O 3873 O O . HOH Q . ? 0.2087 0.4930 0.3186 -0.0886 0.0624 -0.1486 1074 HOH A O 3874 O O . HOH Q . ? 0.1842 0.2788 0.2852 0.0682 -0.0031 -0.0117 1075 HOH A O 3875 O O . HOH Q . ? 0.3933 0.2214 0.2861 -0.0364 0.0793 0.0220 1076 HOH A O 3876 O O . HOH Q . ? 0.3772 0.2563 0.5151 -0.0773 -0.0238 -0.1652 1077 HOH A O 3877 O O . HOH Q . ? 0.3222 0.3093 0.1827 0.0946 0.0751 0.0953 1078 HOH A O 3878 O O . HOH Q . ? 0.2397 0.2496 0.3383 0.0724 0.0200 -0.0478 1079 HOH A O 3879 O O . HOH Q . ? 0.1965 0.2188 0.3277 -0.0379 0.0104 -0.1105 1080 HOH A O 3880 O O . HOH Q . ? 0.2289 0.1945 0.2552 -0.0019 0.0091 -0.0400 1081 HOH A O 3881 O O . HOH Q . ? 0.1075 0.2560 0.2836 -0.0322 0.0197 0.0044 1082 HOH A O 3882 O O . HOH Q . ? 0.6951 0.1533 0.3946 -0.0039 0.0435 0.0616 1083 HOH A O 3883 O O . HOH Q . ? 0.1635 0.2016 0.2238 -0.0165 0.0000 0.0020 1084 HOH A O 3884 O O . HOH Q . ? 0.1738 0.2294 0.2595 -0.0245 -0.0427 0.0721 1085 HOH A O 3885 O O . HOH Q . ? 0.3312 0.3580 0.4326 -0.0465 -0.0644 -0.1227 1086 HOH A O 3886 O O . HOH Q . ? 0.2856 0.1985 0.2861 -0.0070 -0.0055 -0.0095 1087 HOH A O 3887 O O . HOH Q . ? 0.2346 0.1487 0.1870 -0.0268 0.0276 0.0167 1088 HOH A O 3888 O O . HOH Q . ? 0.2138 0.2106 0.2688 -0.0446 0.0579 -0.0344 1089 HOH A O 3889 O O . HOH Q . ? 0.5200 0.2183 0.1602 -0.0298 -0.0441 -0.0327 1090 HOH A O 3890 O O . HOH Q . ? 0.2236 0.3276 0.2896 0.0052 0.0184 -0.0514 1091 HOH A O 3891 O O . HOH Q . ? 0.4156 0.3669 0.4122 0.0424 -0.0848 -0.0451 1092 HOH A O 3892 O O . HOH Q . ? 0.2359 0.2708 0.2940 -0.0325 -0.0380 0.0985 1093 HOH A O 3893 O O . HOH Q . ? 0.2954 0.2257 0.1267 0.0488 -0.0023 -0.0028 1094 HOH A O 3894 O O . HOH Q . ? 0.3162 0.2083 0.3125 0.0869 0.0963 -0.0293 1095 HOH A O 3895 O O . HOH Q . ? 0.6081 0.3217 0.3338 0.4129 -0.4021 -0.2958 1096 HOH A O 3896 O O . HOH Q . ? 0.1948 0.2286 0.5123 0.0044 -0.0271 -0.1474 1097 HOH A O 3897 O O . HOH Q . ? 0.2981 0.2061 0.2395 -0.0094 -0.0085 -0.0638 1098 HOH A O 3898 O O . HOH Q . ? 0.4304 0.1699 0.2148 0.0824 -0.1028 -0.0331 1099 HOH A O 3899 O O . HOH Q . ? 0.4908 0.4279 0.4585 0.1633 -0.0282 0.0872 1100 HOH A O 3900 O O . HOH Q . ? 0.7039 0.3134 0.5108 0.0515 -0.0859 -0.0036 1101 HOH A O 3901 O O . HOH Q . ? 0.2592 0.2292 0.2119 0.0206 0.0325 -0.0278 1102 HOH A O 3902 O O . HOH Q . ? 0.1932 0.1850 0.1709 0.0225 0.0184 -0.0005 1103 HOH A O 3903 O O . HOH Q . ? 0.6169 1.2098 1.8071 0.0948 0.3982 0.6435 1104 HOH A O 3904 O O . HOH Q . ? 0.1624 0.2111 0.2019 0.0215 -0.0513 0.0066 1105 HOH A O 3905 O O . HOH Q . ? 0.5070 0.3309 0.2174 -0.2125 0.0580 -0.0802 1106 HOH A O 3906 O O . HOH Q . ? 0.2526 0.2692 0.2043 0.0254 0.0050 -0.0132 1107 HOH A O 3907 O O . HOH Q . ? 0.4464 0.5634 0.7605 -0.0184 -0.2911 -0.3397 1108 HOH A O 3908 O O . HOH Q . ? 0.3230 0.2991 0.3498 0.0520 -0.0382 0.0029 1109 HOH A O 3909 O O . HOH Q . ? 0.2469 0.2802 0.2661 0.0348 -0.0167 -0.0425 1110 HOH A O 3910 O O . HOH Q . ? 0.3240 0.4812 0.4465 -0.0991 0.1287 -0.0910 1111 HOH A O 3911 O O . HOH Q . ? 0.4080 0.2311 0.4154 0.0835 -0.1663 -0.0527 1112 HOH A O 3912 O O . HOH Q . ? 0.2651 0.1666 0.2843 0.0357 0.0638 0.0321 1113 HOH A O 3913 O O . HOH Q . ? 0.2485 0.3167 0.2923 0.0419 0.0104 -0.0213 1114 HOH A O 3914 O O . HOH Q . ? 0.4239 0.9669 0.4093 0.0213 0.0474 -0.0353 1115 HOH A O 3915 O O . HOH Q . ? 0.1245 0.2048 0.4665 -0.0419 -0.0527 0.1330 1116 HOH A O 3916 O O . HOH Q . ? 0.2967 0.2572 0.4115 0.0784 -0.0350 -0.0466 1117 HOH A O 3917 O O . HOH Q . ? 0.2777 0.4294 0.1974 0.0267 0.1189 -0.0114 1118 HOH A O 3918 O O . HOH Q . ? 0.3831 0.4565 0.3137 -0.2512 0.1241 -0.2240 1119 HOH A O 3919 O O . HOH Q . ? 0.3086 0.4197 0.2269 0.1256 0.0122 0.0574 1120 HOH A O 3920 O O . HOH Q . ? 0.3412 0.6249 0.2696 -0.3036 -0.0225 0.0839 1121 HOH A O 3921 O O . HOH Q . ? 0.3066 0.3115 0.2484 0.0246 -0.0447 0.0967 1122 HOH A O 3922 O O . HOH Q . ? 0.4918 0.2977 0.5291 0.1674 -0.0418 -0.1267 1123 HOH A O 3923 O O . HOH Q . ? 0.1070 0.4357 0.2831 -0.0315 0.0037 0.0265 1124 HOH A O 3924 O O . HOH Q . ? 0.1837 0.1688 0.2861 0.0055 0.0300 -0.0785 1125 HOH A O 3925 O O . HOH Q . ? 0.1878 0.3363 0.3322 -0.0171 0.0579 0.0718 1126 HOH A O 3926 O O . HOH Q . ? 0.3057 0.2607 0.5213 0.1323 0.0938 -0.0127 1127 HOH A O 3927 O O . HOH Q . ? 0.3575 0.2485 0.3367 0.0707 -0.0438 -0.0276 1128 HOH A O 3928 O O . HOH Q . ? 0.3588 0.2590 0.5693 0.0058 -0.2346 -0.0979 1129 HOH A O 3929 O O . HOH Q . ? 0.2219 0.5754 0.7050 -0.0462 0.2400 0.1056 1130 HOH A O 3930 O O . HOH Q . ? 0.2303 0.2896 0.2565 -0.0709 -0.0427 -0.0476 1131 HOH A O 3931 O O . HOH Q . ? 0.3785 0.5824 0.3498 -0.0901 0.0185 -0.1989 1132 HOH A O 3932 O O . HOH Q . ? 0.3410 0.4173 0.2321 -0.0372 -0.0508 -0.0795 1133 HOH A O 3933 O O . HOH Q . ? 0.2616 0.4490 0.3963 0.0000 -0.0218 0.0032 1134 HOH A O 3934 O O . HOH Q . ? 0.5463 0.4019 0.7694 -0.0779 -0.0028 -0.1998 1135 HOH A O 3935 O O . HOH Q . ? 0.4429 0.3898 0.1476 0.0652 -0.0091 -0.0239 1136 HOH A O 3936 O O . HOH Q . ? 0.3108 0.2520 0.4287 0.0448 0.1099 0.1332 1137 HOH A O 3937 O O . HOH Q . ? 0.6444 0.2821 0.5639 0.1034 0.3467 0.1457 1138 HOH A O 3938 O O . HOH Q . ? 0.6018 0.1183 0.4146 0.0318 -0.0354 -0.0181 1139 HOH A O 3939 O O . HOH Q . ? 0.4494 0.3618 0.3765 -0.0975 0.1188 -0.1088 1140 HOH A O 3940 O O . HOH Q . ? 0.2582 0.3338 0.3346 0.0415 -0.0633 0.0811 1141 HOH A O 3941 O O . HOH Q . ? 0.3080 0.5918 0.3507 0.0904 -0.0619 0.0222 1142 HOH A O 3942 O O . HOH Q . ? 0.2663 0.3937 0.4248 -0.0215 -0.1193 0.1454 1143 HOH A O 3943 O O . HOH Q . ? 0.4007 0.4341 0.3695 0.0852 0.0136 0.0916 1144 HOH A O 3944 O O . HOH Q . ? 0.4323 0.3668 0.5909 0.0590 0.0408 0.1833 1145 HOH A O 3945 O O . HOH Q . ? 0.3477 0.6285 0.1642 0.0137 0.0077 0.1698 1146 HOH A O 3946 O O . HOH Q . ? 0.3725 0.7604 0.7452 -0.2779 -0.0744 -0.0674 1147 HOH A O 3947 O O . HOH Q . ? 0.3135 0.5037 0.2195 -0.0858 0.0608 -0.1601 1148 HOH A O 3948 O O . HOH Q . ? 0.8370 0.1898 0.3989 0.0776 -0.1245 0.0085 1149 HOH A O 3949 O O . HOH Q . ? 0.2503 0.1199 0.2341 -0.0271 -0.0353 -0.0009 1150 HOH A O 3950 O O . HOH Q . ? 0.2595 0.4429 0.3485 0.0328 0.1118 0.1501 1151 HOH A O 3951 O O . HOH Q . ? 0.5741 0.3390 0.2134 -0.0998 -0.0749 0.0937 1152 HOH A O 3952 O O . HOH Q . ? 0.3562 0.3649 0.3733 -0.0288 0.0517 -0.0598 1153 HOH A O 3953 O O . HOH Q . ? 0.4262 0.2375 0.3158 0.0740 0.1578 -0.0298 1154 HOH A O 3954 O O . HOH Q . ? 0.2005 0.5094 0.3029 0.0689 -0.0550 -0.0539 1155 HOH A O 3955 O O . HOH Q . ? 0.2854 0.2085 0.4334 0.0324 0.1058 -0.0120 1156 HOH A O 3956 O O . HOH Q . ? 0.7492 0.5816 0.5314 0.1622 0.2165 0.2681 1157 HOH A O 3957 O O . HOH Q . ? 0.2130 0.5384 0.2788 0.0874 -0.0445 -0.1623 1158 HOH A O 3958 O O . HOH Q . ? 0.3981 0.3774 0.3836 0.1859 -0.0702 -0.2097 1159 HOH A O 3959 O O . HOH Q . ? 0.3752 0.3656 0.3796 -0.1884 -0.0306 0.1301 1160 HOH A O 3960 O O . HOH Q . ? 0.5212 0.2890 0.2659 0.0553 -0.0501 -0.0672 1161 HOH A O 3961 O O . HOH Q . ? 0.4233 0.3525 0.4202 -0.0320 -0.0284 0.0306 1162 HOH A O 3962 O O . HOH Q . ? 0.2601 0.6050 0.5049 0.1621 -0.0464 0.1082 1163 HOH A O 3963 O O . HOH Q . ? 0.4411 0.3795 0.2965 0.2238 0.0990 -0.1663 1164 HOH A O 3964 O O . HOH Q . ? 0.2732 0.3379 0.3445 0.0219 0.0076 0.0352 1165 HOH A O 3965 O O . HOH Q . ? 0.2985 0.3365 0.2185 0.0112 -0.0021 0.0011 1166 HOH A O 3966 O O . HOH Q . ? 0.2321 0.2153 0.3082 0.0369 0.0302 -0.0706 1167 HOH A O 3967 O O . HOH Q . ? 0.4266 0.2901 0.5125 0.1119 0.1858 0.0065 1168 HOH A O 3968 O O . HOH Q . ? 0.4016 0.2590 0.7028 0.1042 -0.1744 0.0668 1169 HOH A O 3969 O O . HOH Q . ? 0.3549 0.3112 0.5250 0.0443 -0.2256 -0.0890 1170 HOH A O 3970 O O . HOH Q . ? 0.5851 1.0915 1.1069 0.1455 0.1947 0.3525 1171 HOH A O 3971 O O . HOH Q . ? 0.2347 0.1981 0.1808 0.0562 0.0432 0.0368 1172 HOH A O 3972 O O . HOH Q . ? 0.3003 0.6338 0.5824 0.0994 0.0034 -0.2268 1173 HOH A O 3973 O O . HOH Q . ? 0.3739 0.3943 0.4447 -0.0414 -0.0699 -0.1045 1174 HOH A O 3974 O O . HOH Q . ? 0.5586 0.2507 0.1391 -0.1168 0.0279 -0.0037 1175 HOH A O 3975 O O . HOH Q . ? 0.2577 0.5858 0.4991 -0.0798 -0.0170 0.2230 1176 HOH A O 3976 O O . HOH Q . ? 0.2059 0.1807 0.3681 -0.0244 -0.0300 -0.1387 1177 HOH A O 3977 O O . HOH Q . ? 0.4636 0.3903 0.5252 0.0726 0.1539 -0.0013 1178 HOH A O 3978 O O . HOH Q . ? 0.5692 0.2462 0.3591 -0.0049 -0.1057 -0.0340 1179 HOH A O 3979 O O . HOH Q . ? 0.5951 0.4507 0.8678 -0.1170 0.2550 -0.1887 1180 HOH A O 3980 O O . HOH Q . ? 0.3874 0.5588 0.6006 0.0039 -0.1332 -0.1793 1181 HOH A O 3981 O O . HOH Q . ? 1.5163 0.6261 1.1913 0.3282 -0.2636 -0.4462 1182 HOH A O 3982 O O . HOH Q . ? 0.1936 0.5597 0.4583 -0.0617 -0.0403 0.2101 1183 HOH A O 3983 O O . HOH Q . ? 0.3767 0.1871 0.5736 0.0365 -0.0069 0.1753 1184 HOH A O 3984 O O . HOH Q . ? 0.3920 0.3987 0.2917 0.1414 0.0676 -0.0741 1185 HOH A O 3985 O O . HOH Q . ? 0.3548 0.3810 0.2613 0.0039 -0.0003 -0.0988 1186 HOH A O 3986 O O . HOH Q . ? 0.1918 0.7731 0.5339 0.2772 0.0769 0.3860 1187 HOH A O 3987 O O . HOH Q . ? 0.2277 0.3532 0.3921 -0.0424 -0.0070 -0.1165 1188 HOH A O 3988 O O . HOH Q . ? 0.7354 0.9626 1.7348 0.4311 0.4908 0.4236 1189 HOH A O 3989 O O . HOH Q . ? 0.5246 1.1563 0.6349 -0.0622 -0.0107 0.0591 1190 HOH A O 3990 O O . HOH Q . ? 0.6926 0.2062 0.3184 -0.0579 0.0533 0.0297 1191 HOH A O 3991 O O . HOH Q . ? 0.2459 0.2000 0.3950 -0.0112 0.0461 0.0571 1192 HOH A O 3992 O O . HOH Q . ? 0.6644 0.6543 0.8758 -0.5180 -0.6032 0.4324 1193 HOH A O 3993 O O . HOH Q . ? 0.3338 0.5482 0.2115 -0.0163 0.0192 -0.1212 1194 HOH A O 3994 O O . HOH Q . ? 0.7287 0.2611 0.6127 0.0320 -0.3661 0.0425 1195 HOH A O 3995 O O . HOH Q . ? 0.4416 0.6214 0.3062 0.0873 0.1171 0.0671 1196 HOH A O 3996 O O . HOH Q . ? 0.4226 0.6219 0.4302 -0.0736 -0.1911 -0.1081 1197 HOH A O 3997 O O . HOH Q . ? 0.5031 0.2489 0.5506 0.1858 -0.2177 -0.1352 1198 HOH A O 3998 O O . HOH Q . ? 0.3289 0.4389 0.4843 -0.0818 0.1222 0.1191 1199 HOH A O 3999 O O . HOH Q . ? 0.3891 0.4018 0.1732 -0.0014 -0.0845 -0.0519 1200 HOH A O 4000 O O . HOH Q . ? 0.5636 0.4984 0.4152 -0.0206 0.0213 -0.1166 1201 HOH A O 4001 O O . HOH Q . ? 0.5102 0.3958 0.2624 -0.0325 -0.0323 -0.0198 1202 HOH A O 4002 O O . HOH Q . ? 0.6420 0.5514 0.1959 -0.4184 0.0045 -0.1484 1203 HOH A O 4003 O O . HOH Q . ? 0.2630 0.4765 0.2045 0.0215 -0.0156 0.0003 1204 HOH A O 4004 O O . HOH Q . ? 0.4922 0.7710 0.6378 -0.5113 0.0572 -0.0015 1205 HOH A O 4005 O O . HOH Q . ? 0.3920 0.3848 0.1932 0.0696 0.0167 -0.0786 1206 HOH A O 4006 O O . HOH Q . ? 0.6154 0.4309 0.3439 -0.0718 0.0989 0.0898 1207 HOH A O 4007 O O . HOH Q . ? 0.3967 0.2824 0.4931 -0.0115 -0.0008 0.0945 1208 HOH A O 4008 O O . HOH Q . ? 0.9185 0.4049 0.4342 -0.2212 0.2447 -0.1421 1209 HOH A O 4009 O O . HOH Q . ? 0.3941 0.2569 0.3542 0.0035 0.0803 -0.0285 1210 HOH A O 4010 O O . HOH Q . ? 0.4423 0.2991 0.2580 0.1425 -0.0976 -0.1049 1211 HOH A O 4011 O O . HOH Q . ? 0.2802 0.4413 0.3965 0.0004 -0.1041 0.0235 1212 HOH A O 4012 O O . HOH Q . ? 0.6146 0.4909 0.2303 0.1124 -0.0750 0.0203 1213 HOH A O 4013 O O . HOH Q . ? 0.3611 0.3601 0.2695 -0.0233 -0.0303 -0.1348 1214 HOH A O 4014 O O . HOH Q . ? 0.3550 0.4232 0.3076 -0.0824 0.0654 -0.1113 1215 HOH A O 4015 O O . HOH Q . ? 0.2509 0.5023 0.5274 0.0611 -0.0395 0.1248 1216 HOH A O 4016 O O . HOH Q . ? 0.7559 0.5764 0.7554 0.1684 0.0588 0.0046 1217 HOH A O 4017 O O . HOH Q . ? 0.4059 0.4433 0.4872 0.1070 0.0394 0.0047 1218 HOH A O 4018 O O . HOH Q . ? 0.5184 0.4490 0.4272 -0.1843 0.0211 0.0655 1219 HOH A O 4019 O O . HOH Q . ? 0.4994 0.3676 0.6038 0.0232 0.1870 0.2004 1220 HOH A O 4020 O O . HOH Q . ? 0.3812 0.3934 0.4332 -0.0082 -0.0307 -0.0343 1221 HOH A O 4021 O O . HOH Q . ? 0.8482 1.6515 0.5391 0.2332 0.1269 -0.6818 1222 HOH A O 4022 O O . HOH Q . ? 0.2381 0.6230 0.3528 0.0945 -0.0234 0.0582 1223 HOH A O 4023 O O . HOH Q . ? 0.3607 0.6297 0.3863 -0.1877 0.0792 -0.0627 1224 HOH A O 4024 O O . HOH Q . ? 0.8750 0.4014 1.1620 0.4116 -0.8396 -0.5414 1225 HOH A O 4025 O O . HOH Q . ? 0.6940 1.2393 0.4795 -0.1032 -0.0776 -0.0781 1226 HOH A O 4026 O O . HOH Q . ? 1.4575 0.4991 0.4993 -0.0969 -0.1522 0.1356 1227 HOH A O 4027 O O . HOH Q . ? 0.9463 0.1907 2.3871 0.1735 -0.0047 0.0593 1228 HOH A O 4028 O O . HOH Q . ? 0.4324 1.1883 0.3298 -0.3066 0.0237 -0.2090 1229 HOH A O 4029 O O . HOH Q . ? 1.3772 1.0771 0.8389 -0.4089 -0.1454 0.1501 1230 HOH A O 4030 O O . HOH Q . ? 0.9759 0.4765 0.7078 -0.0200 0.0398 -0.1248 1231 HOH A O 4031 O O . HOH Q . ? 0.5340 0.1853 0.3151 -0.0125 -0.0550 -0.0020 1232 HOH A O 4032 O O . HOH Q . ? 0.7005 0.2697 0.2827 0.1087 0.1046 -0.0130 1233 HOH A O 4033 O O . HOH Q . ? 0.2765 0.8068 0.6156 0.0195 -0.1617 0.3299 1234 HOH A O 4034 O O . HOH Q . ? 0.3028 0.4185 0.2788 0.1195 -0.0566 -0.1530 1235 HOH A O 4035 O O . HOH Q . ? 0.5108 0.5314 1.0722 -0.0953 -0.1229 0.1865 1237 HOH A O 4036 O O . HOH Q . ? 0.3686 0.3693 0.3356 0.0623 0.1251 0.1537 1238 HOH A O 4037 O O . HOH Q . ? 0.3044 0.5306 0.2968 0.0416 -0.0055 -0.0154 1239 HOH A O 4038 O O . HOH Q . ? 0.4593 0.7268 0.3448 -0.0579 0.0253 0.1290 1240 HOH A O 4039 O O . HOH Q . ? 0.5731 0.9002 0.4060 0.0118 0.0430 0.1199 1241 HOH A O 4040 O O . HOH Q . ? 0.4362 0.6309 0.6435 -0.1043 0.2849 0.1323 1242 HOH A O 4041 O O . HOH Q . ? 0.3874 0.4124 0.4329 -0.0484 0.1081 0.0166 1243 HOH A O 4042 O O . HOH Q . ? 0.5672 0.4399 0.5140 0.0725 -0.1188 0.0886 1244 HOH A O 4043 O O . HOH Q . ? 1.2000 0.5211 0.6110 0.2174 0.1175 -0.0662 1245 HOH A O 4044 O O . HOH Q . ? 0.2576 0.3118 0.2727 0.0051 0.0580 -0.0306 1246 HOH A O 4045 O O . HOH Q . ? 0.2431 0.4181 0.5797 0.0354 -0.0685 0.1347 1247 HOH A O 4046 O O . HOH Q . ? 0.6331 0.6509 0.3406 0.2203 -0.0451 -0.0769 1248 HOH A O 4047 O O . HOH Q . ? 0.3909 0.4406 0.5832 0.0548 -0.0544 -0.0501 1249 HOH A O 4048 O O . HOH Q . ? 0.1286 1.0229 1.1451 0.1185 -0.1402 -0.2903 1250 HOH A O 4049 O O . HOH Q . ? 0.5404 0.4070 0.7043 0.2818 -0.1187 -0.4500 1251 HOH A O 4050 O O . HOH Q . ? 0.2289 0.7090 0.2526 0.0748 -0.0317 0.1643 1252 HOH A O 4051 O O . HOH Q . ? 0.5319 0.3634 0.2538 0.1375 0.0618 -0.0435 1253 HOH A O 4052 O O . HOH Q . ? 0.3762 1.4963 1.1202 0.0024 -0.0498 -0.4636 1254 HOH A O 4053 O O . HOH Q . ? 0.4745 0.3121 0.3711 -0.1545 -0.1132 -0.0109 1255 HOH A O 4054 O O . HOH Q . ? 0.3574 0.6440 0.4160 -0.0279 -0.0934 0.1017 1256 HOH A O 4055 O O . HOH Q . ? 0.3506 0.3603 0.5116 0.1398 -0.1486 -0.2266 1257 HOH A O 4056 O O . HOH Q . ? 0.5037 0.3258 0.2296 -0.0980 0.0358 0.0083 1258 HOH A O 4057 O O . HOH Q . ? 0.6826 0.4247 0.3990 0.2501 0.0270 -0.0197 1259 HOH A O 4058 O O . HOH Q . ? 0.6919 1.0219 0.8412 0.2533 0.6013 0.4685 1260 HOH A O 4059 O O . HOH Q . ? 0.5944 0.3081 0.3572 0.1785 0.1070 0.1468 1261 HOH A O 4060 O O . HOH Q . ? 0.4746 0.2377 0.4939 -0.0480 -0.1145 0.0331 1262 HOH A O 4061 O O . HOH Q . ? 0.8439 0.3754 1.0078 0.0094 0.2537 0.1542 1263 HOH A O 4062 O O . HOH Q . ? 0.4134 0.9718 0.7605 -0.1146 -0.0225 0.3992 1264 HOH A O 4063 O O . HOH Q . ? 0.3386 0.4837 0.3735 0.0459 0.0033 0.1263 1265 HOH A O 4064 O O . HOH Q . ? 0.3215 0.7539 0.2912 -0.1075 -0.0109 -0.0131 1266 HOH A O 4065 O O . HOH Q . ? 0.3324 0.3646 0.6620 0.0621 0.1334 0.1788 1267 HOH A O 4066 O O . HOH Q . ? 0.5609 0.3788 1.0313 0.0165 0.1678 -0.0442 1268 HOH A O 4067 O O . HOH Q . ? 0.2668 0.6600 0.7121 -0.2065 -0.2627 0.2452 1269 HOH A O 4068 O O . HOH Q . ? 0.5119 0.4777 0.3123 0.2645 -0.1266 -0.0971 1270 HOH A O 4069 O O . HOH Q . ? 0.7689 0.2502 0.4309 -0.0646 0.0508 0.0182 1271 HOH A O 4070 O O . HOH Q . ? 1.2956 0.8753 1.0165 0.3206 -0.4874 -0.2279 1272 HOH A O 4071 O O . HOH Q . ? 0.8928 1.2299 0.4385 -0.0670 0.0405 -0.0136 1273 HOH A O 4072 O O . HOH Q . ? 0.6413 0.2913 0.5389 0.2049 -0.0900 0.1007 1274 HOH A O 4073 O O . HOH Q . ? 0.6658 1.6752 0.5108 -0.5625 0.0847 0.5012 1275 HOH A O 4074 O O . HOH Q . ? 0.4191 1.2530 0.6358 -0.0139 0.1689 -0.1499 1276 HOH A O 4075 O O . HOH Q . ? 0.4255 0.7509 1.3481 -0.4236 -0.5039 0.5819 1277 HOH A O 4076 O O . HOH Q . ? 0.5109 1.3873 0.6898 0.3255 -0.4962 -0.7571 1278 HOH A O 4077 O O . HOH Q . ? 0.5141 1.1410 0.4791 -0.1569 0.0307 -0.1870 1279 HOH A O 4078 O O . HOH Q . ? 0.3691 0.2500 0.2762 -0.0779 0.1438 -0.0544 1280 HOH A O 4079 O O . HOH Q . ? 0.4175 0.5613 0.3483 0.1894 -0.1132 -0.1626 1281 HOH A O 4080 O O . HOH Q . ? 0.4939 0.4337 0.3622 -0.0414 -0.0187 -0.0316 1282 HOH A O 4081 O O . HOH Q . ? 0.8122 0.2315 0.4226 0.0815 0.1082 0.0862 1283 HOH A O 4082 O O . HOH Q . ? 0.1959 0.2756 0.3216 0.0079 0.0042 0.0422 1284 HOH A O 4083 O O . HOH Q . ? 0.6963 1.2592 1.3755 0.2781 -0.1150 -0.4464 1285 HOH A O 4084 O O . HOH Q . ? 0.5704 0.4140 1.0870 0.0136 0.2042 -0.0173 1286 HOH A O 4085 O O . HOH Q . ? 0.4114 0.3806 0.3698 -0.1633 -0.1062 0.0837 1287 HOH A O 4086 O O . HOH Q . ? 0.3613 0.5541 0.4129 -0.0231 0.0244 0.1442 1288 HOH A O 4087 O O . HOH Q . ? 0.4115 0.3095 0.6307 -0.0068 -0.0187 -0.2275 1289 HOH A O 4088 O O . HOH Q . ? 0.5642 0.4111 0.4107 0.1065 -0.1060 -0.0506 1290 HOH A O 4089 O O . HOH Q . ? 0.5799 0.6848 0.3817 0.1640 0.0000 -0.0571 1291 HOH A O 4090 O O . HOH Q . ? 0.9465 0.8592 0.5746 0.3165 0.1022 0.1091 1292 HOH A O 4091 O O . HOH Q . ? 0.2417 0.4175 0.3540 0.1084 -0.0427 -0.1017 1293 HOH A O 4092 O O . HOH Q . ? 0.4460 0.2646 0.4871 -0.0305 0.0246 -0.1896 1294 HOH A O 4093 O O . HOH Q . ? 0.2921 0.4611 0.3351 -0.0696 0.1471 -0.0498 1295 HOH A O 4094 O O . HOH Q . ? 0.5467 0.6618 0.4076 -0.0523 0.0221 -0.1734 1296 HOH A O 4095 O O . HOH Q . ? 1.6722 0.3618 0.6450 -0.3799 -0.5892 0.2820 1297 HOH A O 4096 O O . HOH Q . ? 0.4537 0.5058 0.4046 0.2230 -0.1590 -0.0928 1298 HOH A O 4097 O O . HOH Q . ? 0.5264 0.3872 0.9494 -0.0260 0.0372 0.1964 1299 HOH A O 4098 O O . HOH Q . ? 0.4413 0.5603 0.4541 0.0712 0.1684 0.2325 1300 HOH A O 4099 O O . HOH Q . ? 0.3825 0.8548 0.3026 -0.1136 0.0166 0.1355 1301 HOH A O 4100 O O . HOH Q . ? 1.0917 0.8495 0.7915 0.1382 -0.0826 -0.1856 1302 HOH A O 4101 O O . HOH Q . ? 0.5172 0.6846 0.8682 -0.2178 0.2421 -0.3615 1303 HOH A O 4102 O O . HOH Q . ? 0.0883 0.3216 1.0201 -0.0560 0.0187 0.1006 1304 HOH A O 4103 O O . HOH Q . ? 0.5339 0.2671 0.5212 -0.0996 -0.0004 0.0727 1305 HOH A O 4104 O O . HOH Q . ? 0.6068 0.5117 0.4308 0.0292 -0.2415 -0.1825 1306 HOH A O 4105 O O . HOH Q . ? 0.6902 0.3669 0.3452 0.0940 -0.0845 0.0653 1307 HOH A O 4106 O O . HOH Q . ? 0.7221 0.8403 1.1998 0.1739 -0.2441 -0.4356 1308 HOH A O 4107 O O . HOH Q . ? 1.5811 0.8776 0.8729 -0.8246 0.5377 -0.1358 1309 HOH A O 4108 O O . HOH Q . ? 0.5638 0.6580 0.8776 -0.1482 0.0158 -0.1004 1310 HOH A O 4109 O O . HOH Q . ? 0.5586 0.6182 0.3706 -0.1165 0.0326 -0.1274 1311 HOH A O 4110 O O . HOH Q . ? 0.8492 0.4877 0.4237 0.2622 0.1774 0.0471 1312 HOH A O 4111 O O . HOH Q . ? 0.4839 0.5927 0.6278 0.1216 0.0995 0.0838 1313 HOH A O 4112 O O . HOH Q . ? 0.5447 0.6806 0.5142 -0.0369 0.0152 -0.0785 1314 HOH A O 4113 O O . HOH Q . ? 0.4855 0.8891 0.4021 -0.3185 0.0495 0.2871 1315 HOH A O 4114 O O . HOH Q . ? 0.4655 0.6011 0.3056 0.1985 -0.0424 0.0219 1316 HOH A O 4115 O O . HOH Q . ? 0.9335 0.5682 1.1989 0.0159 0.3716 -0.1922 1317 HOH A O 4116 O O . HOH Q . ? 0.7498 0.2402 0.4285 -0.0291 0.0738 0.0445 1318 HOH A O 4117 O O . HOH Q . ? 0.4638 1.2496 0.4760 -0.1723 -0.0360 -0.0509 1319 HOH A O 4118 O O . HOH Q . ? 0.4451 0.4491 0.3466 -0.0235 0.0606 -0.1205 1320 HOH A O 4119 O O . HOH Q . ? 0.2852 0.4522 1.2477 0.0403 0.0316 0.4125 1321 HOH A O 4120 O O . HOH Q . ? 0.7444 1.4327 0.8927 -0.0278 0.0921 -0.4027 1322 HOH A O 4121 O O . HOH Q . ? 0.5865 0.4821 0.5891 0.0217 -0.2293 -0.2148 1323 HOH A O 4122 O O . HOH Q . ? 0.5205 0.5004 0.6129 -0.3234 0.0769 -0.3294 1324 HOH A O 4123 O O . HOH Q . ? 1.1131 0.5991 0.3986 0.2006 -0.1234 -0.0854 1325 HOH A O 4124 O O . HOH Q . ? 0.4945 0.7154 0.5778 -0.0412 0.0074 -0.2503 1326 HOH A O 4125 O O . HOH Q . ? 0.5321 0.6098 0.4518 0.2089 -0.2548 -0.2069 1327 HOH A O 4126 O O . HOH Q . ? 0.6009 0.6242 0.4496 0.3352 0.1837 0.1669 1328 HOH A O 4127 O O . HOH Q . ? 0.9710 0.2672 0.6230 -0.1277 -0.2840 0.0218 1329 HOH A O 4128 O O . HOH Q . ? 0.5043 1.2747 0.5064 0.0830 -0.0661 -0.0021 1330 HOH A O 4129 O O . HOH Q . ? 1.1225 0.2021 0.8383 0.1253 -0.0829 0.0711 1331 HOH A O 4130 O O . HOH Q . ? 0.5724 0.6762 2.4698 -0.1319 0.0248 0.2789 1332 HOH A O 4131 O O . HOH Q . ? 0.7937 1.4273 0.6862 0.2902 -0.0886 0.1768 1333 HOH A O 4132 O O . HOH Q . ? 0.6868 0.8075 0.3339 -0.2987 0.0329 -0.1261 1334 HOH A O 4133 O O . HOH Q . ? 0.2855 0.5492 0.6088 -0.0431 -0.0411 -0.1955 1335 HOH A O 4134 O O . HOH Q . ? 0.4347 0.3903 0.6138 0.1286 -0.1642 -0.0744 1336 HOH A O 4135 O O . HOH Q . ? 0.9289 1.3682 0.5903 0.0621 -0.0746 -0.2047 1337 HOH A O 4136 O O . HOH Q . ? 0.4712 0.5831 0.2874 -0.1851 -0.1836 0.0835 1338 HOH A O 4137 O O . HOH Q . ? 0.4228 0.9351 0.6136 0.3259 -0.0251 0.1368 1339 HOH A O 4138 O O . HOH Q . ? 0.7998 0.8711 1.4576 0.0167 -0.0104 -0.2988 1340 HOH A O 4139 O O . HOH Q . ? 0.5232 0.5360 0.4010 0.1219 -0.0938 0.0183 1341 HOH A O 4140 O O . HOH Q . ? 0.4253 0.8839 0.3985 -0.2985 -0.0440 0.0996 1342 HOH A O 4141 O O . HOH Q . ? 0.6585 0.5857 0.3148 0.0475 0.0496 -0.0332 1343 HOH A O 4142 O O . HOH Q . ? 0.6485 0.5674 0.5507 -0.1892 0.0650 -0.0405 1344 HOH A O 4143 O O . HOH Q . ? 0.4824 0.3100 0.7186 -0.1047 0.1036 -0.1154 1345 HOH A O 4144 O O . HOH Q . ? 0.5827 0.2695 0.5574 -0.0762 -0.0648 0.0124 1346 HOH A O 4145 O O . HOH Q . ? 0.5097 1.0810 0.4219 0.5394 -0.2109 -0.3586 1347 HOH A O 4146 O O . HOH Q . ? 0.2672 0.5294 0.4133 -0.0706 0.0193 0.2268 1348 HOH A O 4147 O O . HOH Q . ? 0.7707 0.3497 0.2984 0.0344 0.0418 0.0927 1349 HOH A O 4148 O O . HOH Q . ? 1.3012 0.8362 0.8334 0.3639 -0.3316 -0.1181 1350 HOH A O 4149 O O . HOH Q . ? 0.3992 0.8902 0.9950 -0.3934 0.3030 -0.6821 1351 HOH A O 4150 O O . HOH Q . ? 0.5611 0.6880 0.2180 -0.1233 0.0912 -0.0088 1352 HOH A O 4151 O O . HOH Q . ? 1.1575 0.4140 0.3504 0.3772 -0.2043 -0.1178 1353 HOH A O 4152 O O . HOH Q . ? 0.3087 0.3843 0.7473 -0.0063 0.1391 0.0392 1354 HOH A O 4153 O O . HOH Q . ? 0.3177 0.3410 0.3874 -0.0829 -0.0549 -0.1520 1355 HOH A O 4154 O O . HOH Q . ? 0.8465 1.6678 0.8458 0.1873 -0.0005 -0.3116 1357 HOH A O 4155 O O . HOH Q . ? 0.6257 1.1947 0.7334 0.5465 0.2770 -0.1577 1359 HOH A O 4156 O O . HOH Q . ? 0.7008 0.4711 0.6932 0.2181 0.4781 0.5060 1360 HOH A O 4157 O O . HOH Q . ? 0.4265 0.5910 0.4208 0.1137 -0.0214 -0.0586 1361 HOH A O 4158 O O . HOH Q . ? 0.3543 1.1022 0.5393 -0.1117 0.0210 -0.0354 1362 HOH A O 4159 O O . HOH Q . ? 0.3957 0.4752 0.4592 -0.1232 0.1011 0.0724 1363 HOH A O 4160 O O . HOH Q . ? 0.8745 0.5570 0.3840 0.2337 0.0446 -0.0194 1364 HOH A O 4161 O O . HOH Q . ? 1.3785 0.6525 0.9070 -0.1522 0.3245 0.1236 1365 HOH A O 4162 O O . HOH Q . ? 0.9480 1.4344 0.8553 0.0383 0.0949 0.3229 1366 HOH A O 4163 O O . HOH Q . ? 1.5700 0.4111 1.5929 -0.2752 -0.4268 -0.0445 1367 HOH A O 4164 O O . HOH Q . ? 0.8979 0.9014 0.2552 -0.5051 -0.1195 0.0991 1368 HOH A O 4165 O O . HOH Q . ? 0.6000 0.7859 0.3011 -0.5394 -0.3704 0.2919 1369 HOH A O 4166 O O . HOH Q . ? 0.5027 0.4283 0.4784 0.2055 0.0364 0.0689 1370 HOH A O 4167 O O . HOH Q . ? 0.5652 0.4679 0.5872 0.0816 -0.2628 -0.2762 1371 HOH A O 4168 O O . HOH Q . ? 0.7073 0.4017 0.8655 -0.0099 0.3694 -0.0846 1372 HOH A O 4169 O O . HOH Q . ? 0.6789 0.7011 0.7864 0.3871 -0.4007 -0.0921 1373 HOH A O 4170 O O . HOH Q . ? 0.7221 0.6393 1.3569 -0.0679 -0.2809 0.6599 1375 HOH A O 4171 O O . HOH Q . ? 0.5855 0.3878 0.3467 0.0015 0.0270 -0.1042 1376 HOH A O 4172 O O . HOH Q . ? 0.5579 0.9156 0.6606 0.0759 -0.1082 0.4570 1377 HOH A O 4173 O O . HOH Q . ? 2.1000 0.5519 0.2903 -0.6675 0.2888 -0.1969 1378 HOH A O 4174 O O . HOH Q . ? 0.4608 0.8152 0.6522 0.0304 -0.0560 0.2843 1379 HOH A O 4175 O O . HOH Q . ? 0.2614 0.5027 0.3017 -0.0261 0.0028 -0.0547 1380 HOH A O 4176 O O . HOH Q . ? 0.6872 0.4759 0.3467 -0.0280 -0.0009 0.0658 1381 HOH A O 4177 O O . HOH Q . ? 0.8539 0.8066 0.7114 -0.0575 -0.1365 0.2104 1382 HOH A O 4178 O O . HOH Q . ? 1.1418 1.2980 1.4517 -0.1760 -0.5054 0.7713 1383 HOH A O 4179 O O . HOH Q . ? 0.8060 1.2974 0.9546 -0.5453 -0.2124 0.4155 1384 HOH A O 4180 O O . HOH Q . ? 1.5783 0.6418 1.3575 -0.2779 -0.6380 0.2230 1385 HOH A O 4181 O O . HOH Q . ? 0.5550 0.6383 0.5003 0.4446 0.1726 0.4617 1386 HOH A O 4182 O O . HOH Q . ? 0.4202 0.6717 0.5769 -0.0189 -0.0692 0.1840 1387 HOH A O 4183 O O . HOH Q . ? 0.7053 0.6414 0.3670 -0.1218 -0.1896 0.1403 1388 HOH A O 4184 O O . HOH Q . ? 0.4634 0.7821 0.8291 0.0135 0.0169 -0.4983 1389 HOH A O 4185 O O . HOH Q . ? 0.4191 1.1300 0.3692 0.1058 -0.0696 0.2730 1390 HOH A O 4186 O O . HOH Q . ? 0.8669 0.6634 2.2390 0.1012 -0.3594 0.3043 1392 HOH A O 4187 O O . HOH Q . ? 1.2073 0.4575 0.4806 -0.0746 -0.0176 -0.0734 1393 HOH A O 4188 O O . HOH Q . ? 0.3635 0.5230 0.6841 -0.0424 0.2480 -0.2113 1394 HOH A O 4189 O O . HOH Q . ? 0.4640 0.5441 0.6570 0.0465 0.1318 -0.2407 1395 HOH A O 4190 O O . HOH Q . ? 0.6418 0.4909 1.1313 -0.0573 -0.1558 0.1409 1396 HOH A O 4191 O O . HOH Q . ? 0.8206 0.6934 0.7656 0.5071 -0.5065 -0.5224 1397 HOH A O 4192 O O . HOH Q . ? 0.5510 0.7177 0.3585 -0.3303 0.1160 0.1176 1398 HOH A O 4193 O O . HOH Q . ? 0.8784 0.4519 0.4339 -0.2267 0.0476 0.0895 1399 HOH A O 4194 O O . HOH Q . ? 0.3811 0.4114 0.4322 -0.0654 0.0242 -0.0821 1400 HOH A O 4195 O O . HOH Q . ? 0.2934 1.1344 0.6119 -0.0728 0.1252 -0.0349 1401 HOH A O 4196 O O . HOH Q . ? 0.4453 0.6144 0.7851 -0.1030 0.1563 0.0619 1402 HOH A O 4197 O O . HOH Q . ? 0.5205 1.7939 1.1245 0.0880 -0.2766 -0.2855 1403 HOH A O 4198 O O . HOH Q . ? 0.2966 1.2536 1.5085 0.2016 -0.0948 -0.3314 1404 HOH A O 4199 O O . HOH Q . ? 0.9746 1.0978 0.4126 0.7667 0.3286 0.2958 1405 HOH A O 4200 O O . HOH Q . ? 0.8399 0.5485 0.4477 0.3545 -0.1681 -0.0094 1406 HOH A O 4201 O O . HOH Q . ? 0.6225 0.8392 0.5674 -0.1410 -0.1857 0.0725 1407 HOH A O 4202 O O . HOH Q . ? 0.3326 0.5491 0.4686 0.1163 0.0632 0.1066 1408 HOH A O 4203 O O . HOH Q . ? 0.4713 0.4359 0.5205 0.0090 0.0741 0.1943 1409 HOH A O 4204 O O . HOH Q . ? 0.7140 1.0198 0.4924 -0.2415 -0.2877 0.4023 1410 HOH A O 4205 O O . HOH Q . ? 1.3152 0.6593 0.2613 0.0017 0.2846 0.0022 1411 HOH A O 4206 O O . HOH Q . ? 0.4607 1.1532 0.6147 -0.4654 -0.1781 0.0325 1412 HOH A O 4207 O O . HOH Q . ? 0.5169 0.7194 0.9551 0.2427 0.1157 0.2218 1413 HOH A O 4208 O O . HOH Q . ? 1.1946 0.3812 0.5902 0.0368 0.2249 -0.0121 1414 HOH A O 4209 O O . HOH Q . ? 0.7404 1.1156 0.6303 0.4469 0.2295 0.2716 1415 HOH A O 4210 O O . HOH Q . ? 0.4557 0.6241 0.8580 0.0464 0.1224 -0.1920 1416 HOH A O 4211 O O . HOH Q . ? 0.4911 0.4955 0.4837 0.1843 0.0623 0.0361 1417 HOH A O 4212 O O . HOH Q . ? 1.8549 0.7203 0.7292 -0.3200 -0.1706 -0.0674 1418 HOH A O 4213 O O . HOH Q . ? 0.9509 0.4609 0.5406 0.0742 0.2890 0.2212 1419 HOH A O 4214 O O . HOH Q . ? 0.7029 1.1617 0.2700 0.0226 -0.0242 0.3322 1420 HOH A O 4215 O O . HOH Q . ? 0.9088 1.3417 0.8521 0.6487 -0.2173 -0.4673 1421 HOH A O 4216 O O . HOH Q . ? 0.6460 1.0218 0.4671 -0.2298 -0.2764 0.3249 1422 HOH A O 4217 O O . HOH Q . ? 0.4661 0.7321 0.5007 -0.3168 -0.1615 0.1316 1423 HOH A O 4218 O O . HOH Q . ? 0.7695 0.6098 0.7691 -0.1058 -0.1508 0.2272 1424 HOH A O 4219 O O . HOH Q . ? 0.5315 0.6739 0.6005 -0.1237 -0.2457 0.0286 1425 HOH A O 4220 O O . HOH Q . ? 0.5170 0.3327 1.0105 0.0816 -0.1263 0.0144 1426 HOH A O 4221 O O . HOH Q . ? 0.8655 0.3786 0.6976 0.0532 0.4759 0.0471 1427 HOH A O 4222 O O . HOH Q . ? 0.8380 0.3408 0.6833 0.0053 -0.1460 0.2066 1428 HOH A O 4223 O O . HOH Q . ? 0.4816 1.3777 0.4457 0.0521 -0.1957 0.5093 1429 HOH A O 4224 O O . HOH Q . ? 1.0786 0.9386 0.4790 -0.4119 0.3335 -0.1400 1430 HOH A O 4225 O O . HOH Q . ? 0.9057 0.6611 0.7668 -0.3022 0.5996 -0.3187 1431 HOH A O 4226 O O . HOH Q . ? 0.2026 0.9415 0.7872 -0.3076 0.1363 -0.0427 1432 HOH A O 4227 O O . HOH Q . ? 0.6226 0.3665 0.5521 -0.1088 0.0735 -0.2025 1433 HOH A O 4228 O O . HOH Q . ? 0.4636 1.4710 1.3800 -0.2046 0.1292 0.8688 1434 HOH A O 4229 O O . HOH Q . ? 0.9333 0.9611 0.4214 -0.3570 -0.0889 -0.0112 1435 HOH A O 4230 O O . HOH Q . ? 0.7557 0.3856 0.2524 0.1162 0.2814 -0.0638 1436 HOH A O 4231 O O . HOH Q . ? 0.6427 1.1077 1.1160 -0.0198 -0.1451 0.3205 1437 HOH A O 4232 O O . HOH Q . ? 0.6717 0.6842 1.7169 0.1772 0.8209 -0.2972 1438 HOH A O 4233 O O . HOH Q . ? 0.2924 0.7634 0.7978 0.0079 0.3588 0.4735 1439 HOH A O 4234 O O . HOH Q . ? 0.5153 0.2209 0.5856 -0.0260 -0.0829 0.1303 1440 HOH A O 4235 O O . HOH Q . ? 0.5150 0.2873 0.6087 0.0531 -0.0811 0.1070 1441 HOH A O 4236 O O . HOH Q . ? 0.8929 0.7026 0.5624 -0.0484 0.0731 -0.4919 1442 HOH A O 4237 O O . HOH Q . ? 0.9713 0.4711 0.6645 0.2515 -0.2148 -0.1494 1443 HOH A O 4238 O O . HOH Q . ? 0.8522 0.3721 0.6054 -0.1754 0.1137 -0.0056 1444 HOH A O 4239 O O . HOH Q . ? 1.1438 0.7883 0.9678 -0.1380 -0.3716 0.2321 1445 HOH A O 4240 O O . HOH Q . ? 1.5245 0.4711 1.0094 -0.2354 0.9723 -0.4447 1446 HOH A O 4241 O O . HOH Q . ? 0.4918 0.6161 0.4116 -0.3740 0.0070 -0.3038 1447 HOH A O 4242 O O . HOH Q . ? 1.0916 0.5401 0.3587 0.0950 -0.4460 -0.0187 1448 HOH A O 4243 O O . HOH Q . ? 0.3760 0.6536 0.4946 -0.2183 0.0867 -0.1436 1449 HOH A O 4244 O O . HOH Q . ? 0.5187 0.3384 0.7038 -0.1857 -0.1339 0.1864 1450 HOH A O 4245 O O . HOH Q . ? 0.4351 0.9125 0.9201 0.0956 0.0494 0.3290 1451 HOH A O 4246 O O . HOH Q . ? 0.2276 1.5923 0.6859 -0.1456 0.0728 0.6708 1452 HOH A O 4247 O O . HOH Q . ? 1.2108 0.5856 0.7817 -0.1775 -0.0376 0.0053 1454 HOH A O 4248 O O . HOH Q . ? 0.5720 0.8173 0.9108 -0.2064 -0.4937 0.7121 1455 HOH A O 4249 O O . HOH Q . ? 1.3496 0.6104 0.7615 -0.2019 -0.1847 0.0362 1456 HOH A O 4250 O O . HOH Q . ? 1.6887 0.2854 0.6302 -0.1647 0.4174 -0.1719 1457 HOH A O 4251 O O . HOH Q . ? 0.7075 2.2625 0.9237 -0.3420 -0.0766 0.0378 1458 HOH A O 4252 O O . HOH Q . ? 0.4528 0.6817 1.7235 -0.2521 0.0919 0.8632 1459 HOH A O 4253 O O . HOH Q . ? 1.1941 0.7330 1.2369 -0.2034 0.0886 -0.0904 1460 HOH A O 4254 O O . HOH Q . ? 0.4616 0.4778 0.8915 -0.0130 -0.2302 0.0157 1461 HOH A O 4255 O O . HOH Q . ? 0.4698 0.7895 0.8928 0.1191 -0.1057 -0.1421 1462 HOH A O 4256 O O . HOH Q . ? 0.5299 0.2525 0.7558 0.1325 -0.0081 0.0926 1463 HOH A O 4257 O O . HOH Q . ? 0.4644 2.0260 0.9568 0.1344 -0.1073 -0.1715 1464 HOH A O 4258 O O . HOH Q . ? 0.8152 0.6760 0.6340 0.5639 -0.4709 -0.3954 1465 HOH A O 4259 O O . HOH Q . ? 0.3986 0.8151 0.4617 0.1233 0.0584 -0.2452 1466 HOH A O 4260 O O . HOH Q . ? 0.8229 0.6100 1.1560 -0.5102 0.5190 -0.2572 1467 HOH A O 4261 O O . HOH Q . ? 0.9663 1.2091 0.8443 0.5185 -0.2893 -0.2559 1468 HOH A O 4262 O O . HOH Q . ? 1.2037 0.3471 0.3697 0.2474 -0.0659 -0.1416 1469 HOH A O 4263 O O . HOH Q . ? 0.8689 1.1003 0.9046 -0.1880 0.0398 -0.3233 1470 HOH A O 4264 O O . HOH Q . ? 1.2686 1.7217 0.2969 0.6357 -0.3423 -0.3889 1471 HOH A O 4265 O O . HOH Q . ? 1.4694 0.2310 1.1729 0.4840 0.3189 0.1113 1472 HOH A O 4266 O O . HOH Q . ? 0.7247 0.5330 0.6182 0.0638 0.0887 -0.1256 1474 HOH A O 4267 O O . HOH Q . ? 1.4893 0.8080 0.5417 -0.6813 -0.0462 0.3942 1475 HOH A O 4268 O O . HOH Q . ? 1.8962 0.3877 0.8232 -0.2594 -0.7292 -0.0676 1476 HOH A O 4269 O O . HOH Q . ? 0.5103 0.4559 0.8281 -0.3641 -0.5239 0.2433 1477 HOH A O 4270 O O . HOH Q . ? 0.4368 0.6530 1.2524 0.0193 0.0340 -0.0345 1478 HOH A O 4271 O O . HOH Q . ? 0.4408 0.4632 1.2996 -0.0340 -0.1699 -0.4639 1479 HOH A O 4272 O O . HOH Q . ? 1.1975 0.2354 0.1180 -0.3062 -0.1824 -0.0336 1480 HOH A O 4273 O O . HOH Q . ? 1.7029 0.2986 1.3898 -0.1214 0.0491 -0.4789 1481 HOH A O 4274 O O . HOH Q . ? 0.5444 1.6336 0.5796 0.2059 0.2249 0.0706 1482 HOH A O 4275 O O . HOH Q . ? 0.7562 0.6132 0.5291 0.2735 0.2724 0.0324 1483 HOH A O 4276 O O . HOH Q . ? 0.7033 0.7307 1.1259 -0.3133 0.1807 0.1006 1484 HOH A O 4277 O O . HOH Q . ? 1.7811 0.8425 0.6008 0.1231 -0.2654 0.1514 1485 HOH A O 4278 O O . HOH Q . ? 0.6838 0.3815 0.7705 0.1469 -0.4193 -0.0420 1486 HOH A O 4279 O O . HOH Q . ? 0.4646 0.6710 1.0051 -0.2671 0.3967 -0.7161 1487 HOH A O 4280 O O . HOH Q . ? 0.6455 1.2999 0.8826 -0.2237 0.1267 -0.4207 1488 HOH A O 4281 O O . HOH Q . ? 0.4042 1.3760 0.7836 -0.5642 -0.1936 -0.0252 1489 HOH A O 4282 O O . HOH Q . ? 1.4636 0.1403 0.7346 0.2142 0.2980 0.2113 1490 HOH A O 4283 O O . HOH Q . ? 0.9689 1.2750 0.7131 0.1447 -0.1583 -0.6759 1491 HOH A O 4284 O O . HOH Q . ? 0.5427 0.4208 0.5571 -0.0845 0.0050 0.1580 1492 HOH A O 4285 O O . HOH Q . ? 0.9717 0.3604 1.1474 0.3762 0.7080 0.1360 1493 HOH A O 4286 O O . HOH Q . ? 0.9428 0.4122 1.6073 -0.0354 0.0381 -0.1208 1494 HOH A O 4287 O O . HOH Q . ? 1.5295 0.8785 0.4174 -0.3910 -0.0641 -0.1636 1495 HOH A O 4288 O O . HOH Q . ? 0.8165 0.5618 0.5205 -0.4315 -0.0402 0.1792 1496 HOH A O 4289 O O . HOH Q . ? 0.6980 0.2378 0.9082 -0.1449 0.4622 -0.2288 1497 HOH A O 4290 O O . HOH Q . ? 0.8012 0.5728 0.4215 0.2613 -0.2226 -0.0431 1498 HOH A O 4291 O O . HOH Q . ? 0.6582 0.7700 1.3105 0.0636 -0.1442 -0.0421 1499 HOH A O 4292 O O . HOH Q . ? 0.9954 1.0772 0.5842 -0.0953 -0.1130 0.1237 1500 HOH A O 4293 O O . HOH Q . ? 0.7078 0.5603 1.2269 0.1367 0.4072 -0.1871 1501 HOH A O 4294 O O . HOH Q . ? 1.3206 0.3513 0.6073 -0.0263 -0.5082 0.1436 1502 HOH A O 4295 O O . HOH Q . ? 0.8514 1.2004 1.1299 0.3493 -0.0810 -0.3391 1503 HOH A O 4296 O O . HOH Q . ? 0.6853 0.5175 1.1768 0.0528 0.0240 -0.1545 1504 HOH A O 4297 O O . HOH Q . ? 0.9124 1.0116 1.3396 -0.2382 -0.4077 0.2102 1505 HOH A O 4298 O O . HOH Q . ? 0.3962 0.6420 0.4958 0.0471 -0.1912 -0.1841 1506 HOH A O 4299 O O . HOH Q . ? 1.0074 0.3118 0.5117 0.0779 -0.2475 -0.1009 1507 HOH A O 4300 O O . HOH Q . ? 0.8512 0.5654 0.6657 0.2492 0.2963 0.2772 1508 HOH A O 4301 O O . HOH Q . ? 0.6140 0.5891 0.9121 -0.1339 -0.0869 0.2281 1509 HOH A O 4302 O O . HOH Q . ? 0.7596 0.9749 0.2911 -0.1795 -0.1451 0.2063 1510 HOH A O 4303 O O . HOH Q . ? 0.6897 0.1696 0.8171 -0.0470 0.3650 0.2080 1511 HOH A O 4304 O O . HOH Q . ? 0.8952 0.6593 0.8207 -0.0520 0.0111 0.0598 1512 HOH A O 4305 O O . HOH Q . ? 0.9129 0.9207 0.6708 0.6974 -0.6084 -0.6750 1513 HOH A O 4306 O O . HOH Q . ? 0.9571 0.6672 0.3798 0.3625 0.0120 0.0218 1514 HOH A O 4307 O O . HOH Q . ? 0.7366 0.4430 0.4901 -0.1987 -0.3444 0.1432 1515 HOH A O 4308 O O . HOH Q . ? 1.5633 0.2706 1.5515 0.2659 -0.1762 -0.3045 1516 HOH A O 4309 O O . HOH Q . ? 1.2186 1.1699 0.5521 -0.2855 -0.1172 0.0645 1517 HOH A O 4310 O O . HOH Q . ? 0.9455 0.4867 0.6013 -0.2253 0.2851 -0.1494 1518 HOH A O 4311 O O . HOH Q . ? 0.8507 0.3766 0.6671 0.0125 0.2600 0.0378 1519 HOH A O 4312 O O . HOH Q . ? 0.5275 0.4056 0.6208 0.1836 0.0163 -0.0659 1520 HOH A O 4313 O O . HOH Q . ? 0.7297 0.7464 0.8834 -0.1948 -0.0447 0.2660 1521 HOH A O 4314 O O . HOH Q . ? 1.4230 0.2527 0.3772 0.1157 0.4210 0.1329 1523 HOH A O 4315 O O . HOH Q . ? 0.9405 0.4593 0.7527 0.0285 0.2865 0.2296 1524 HOH A O 4316 O O . HOH Q . ? 0.5813 0.9053 0.6449 -0.0890 -0.1522 -0.0007 1525 HOH A O 4317 O O . HOH Q . ? 0.5439 2.2742 1.3172 -0.1930 0.1575 -0.6517 1526 HOH A O 4318 O O . HOH Q . ? 0.8148 0.3686 1.0491 -0.0347 0.4226 0.1143 1527 HOH A O 4319 O O . HOH Q . ? 0.4870 1.2564 0.3677 0.3135 0.2517 0.3650 1528 HOH A O 4320 O O . HOH Q . ? 0.6008 1.8606 0.8927 -0.0508 0.4176 0.8076 1529 HOH A O 4321 O O . HOH Q . ? 1.0476 0.9965 1.2524 0.2397 0.5858 0.4350 1530 HOH A O 4322 O O . HOH Q . ? 0.7320 0.4107 0.6253 -0.1229 -0.1850 0.0189 1532 HOH A O 4323 O O . HOH Q . ? 1.5077 0.9221 0.7413 0.6275 -0.6609 -0.3990 1534 HOH A O 4324 O O . HOH Q . ? 2.5566 0.4249 0.5852 0.4746 0.7616 -0.1045 1535 HOH A O 4325 O O . HOH Q . ? 0.7437 1.0706 0.2172 -0.2714 -0.1963 0.0452 1536 HOH A O 4326 O O . HOH Q . ? 1.7092 0.3500 0.4343 0.1109 -0.5771 0.1482 1537 HOH A O 4327 O O . HOH Q . ? 0.4189 0.5872 0.5229 0.0738 0.2301 0.0934 1538 HOH A O 4328 O O . HOH Q . ? 0.6832 0.5143 0.5960 -0.2388 -0.1534 -0.0311 1539 HOH A O 4329 O O . HOH Q . ? 0.5993 1.3749 0.2612 -0.1307 -0.0749 0.1681 1540 HOH A O 4330 O O . HOH Q . ? 0.9413 0.3704 0.8684 -0.1655 0.3883 0.1659 1541 HOH A O 4331 O O . HOH Q . ? 1.4091 0.5481 2.9420 0.2853 -0.3152 0.3805 1542 HOH A O 4332 O O . HOH Q . ? 0.7899 0.4701 0.5673 0.2406 -0.2486 -0.0938 1543 HOH A O 4333 O O . HOH Q . ? 0.6263 1.0690 0.1601 -0.0552 -0.0205 0.0545 1544 HOH A O 4334 O O . HOH Q . ? 1.9143 0.5778 0.7287 0.2563 -0.0377 -0.0786 1545 HOH A O 4335 O O . HOH Q . ? 0.3601 0.6318 2.9286 -0.0919 0.1470 -0.8620 1546 HOH A O 4336 O O . HOH Q . ? 0.6342 0.7951 0.3431 -0.1803 -0.0169 -0.0448 1547 HOH A O 4337 O O . HOH Q . ? 0.4077 0.3055 0.5584 0.0401 -0.0080 0.0400 1548 HOH A O 4338 O O . HOH Q . ? 0.5049 0.9676 0.8655 -0.0700 -0.1013 0.4180 1549 HOH A O 4339 O O . HOH Q . ? 0.9834 0.6200 0.9310 -0.2908 0.3696 -0.0039 1550 HOH A O 4340 O O . HOH Q . ? 0.7736 1.3977 0.8532 -0.0450 0.2383 -0.2862 1552 HOH A O 4341 O O . HOH Q . ? 0.4669 0.2544 0.3240 0.0561 0.0158 0.0129 1553 HOH A O 4342 O O . HOH Q . ? 0.6663 0.9373 0.9148 -0.2111 -0.0789 0.2800 1554 HOH A O 4343 O O . HOH Q . ? 1.6197 0.9665 0.5683 0.3820 0.0876 -0.0798 1555 HOH A O 4344 O O . HOH Q . ? 0.7975 0.3391 0.4905 0.0783 -0.0822 0.2482 1556 HOH A O 4345 O O . HOH Q . ? 0.6318 1.9390 1.1465 -0.0816 0.3330 -0.5355 1557 HOH A O 4346 O O . HOH Q . ? 0.5723 1.6491 0.7499 0.3354 -0.3682 0.3678 1558 HOH A O 4347 O O . HOH Q . ? 0.6447 1.1775 1.3220 0.0325 0.0602 0.1075 1559 HOH A O 4348 O O . HOH Q . ? 1.2890 0.6428 0.5965 -0.1862 -0.2713 -0.0636 1560 HOH A O 4349 O O . HOH Q . ? 0.6230 0.4172 0.6575 0.1435 -0.2917 -0.1519 1561 HOH A O 4350 O O . HOH Q . ? 0.6824 0.4979 2.6900 0.1558 -0.5293 0.0237 1562 HOH A O 4351 O O . HOH Q . ? 0.1996 0.1996 0.2137 0.0156 0.0233 -0.0030 1563 HOH A O 4352 O O . HOH Q . ? 0.1925 0.6362 0.0904 0.1259 0.0652 -0.0939 1564 HOH A O 4353 O O . HOH Q . ? 0.2100 0.1838 0.3494 0.0685 0.1461 0.0889 1565 HOH A O 4354 O O . HOH Q . ? 0.5983 0.7738 0.4379 -0.5934 0.4807 -0.4625 1566 HOH A O 4355 O O . HOH Q . ? 0.9569 1.1487 1.2148 -0.3769 0.3857 -0.5226 1567 HOH A O 4356 O O . HOH Q . ? 0.7951 1.0515 1.1754 0.4562 0.3533 0.2714 1568 HOH A O 4357 O O . HOH Q . ? 1.4795 0.1468 0.8941 -0.0887 -0.3332 0.0482 1569 HOH A O 4358 O O . HOH Q . ? 1.4618 1.2670 0.5859 0.7893 -0.3069 -0.5461 1570 HOH A O # 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 ILE 1 1 1 ILE ILE A . n A 1 2 ILE 2 2 2 ILE ILE A . n A 1 3 PRO 3 3 3 PRO PRO A . n A 1 4 VAL 4 4 4 VAL VAL A . n A 1 5 GLU 5 5 5 GLU GLU A . n A 1 6 GLU 6 6 6 GLU GLU A . n A 1 7 GLU 7 7 7 GLU GLU A . n A 1 8 ASN 8 8 8 ASN ASN A . n A 1 9 PRO 9 9 9 PRO PRO A . n A 1 10 ASP 10 10 10 ASP ASP A . n A 1 11 PHE 11 11 11 PHE PHE A . n A 1 12 TRP 12 12 12 TRP TRP A . n A 1 13 ASN 13 13 13 ASN ASN A . n A 1 14 ARG 14 14 14 ARG ARG A . n A 1 15 GLU 15 15 15 GLU GLU A . n A 1 16 ALA 16 16 16 ALA ALA A . n A 1 17 ALA 17 17 17 ALA ALA A . n A 1 18 GLU 18 18 18 GLU GLU A . n A 1 19 ALA 19 19 19 ALA ALA A . n A 1 20 LEU 20 20 20 LEU LEU A . n A 1 21 GLY 21 21 21 GLY GLY A . n A 1 22 ALA 22 22 22 ALA ALA A . n A 1 23 ALA 23 23 23 ALA ALA A . n A 1 24 LYS 24 24 24 LYS LYS A . n A 1 25 LYS 25 25 25 LYS LYS A . n A 1 26 LEU 26 26 26 LEU LEU A . n A 1 27 GLN 27 27 27 GLN GLN A . n A 1 28 PRO 28 28 28 PRO PRO A . n A 1 29 ALA 29 29 29 ALA ALA A . n A 1 30 GLN 30 30 30 GLN GLN A . n A 1 31 THR 31 31 31 THR THR A . n A 1 32 ALA 32 32 32 ALA ALA A . n A 1 33 ALA 33 33 33 ALA ALA A . n A 1 34 LYS 34 34 34 LYS LYS A . n A 1 35 ASN 35 35 35 ASN ASN A . n A 1 36 LEU 36 36 36 LEU LEU A . n A 1 37 ILE 37 37 37 ILE ILE A . n A 1 38 ILE 38 38 38 ILE ILE A . n A 1 39 PHE 39 39 39 PHE PHE A . n A 1 40 LEU 40 40 40 LEU LEU A . n A 1 41 GLY 41 41 41 GLY GLY A . n A 1 42 ASP 42 42 42 ASP ASP A . n A 1 43 GLY 43 43 43 GLY GLY A . n A 1 44 MET 44 44 44 MET MET A . n A 1 45 GLY 45 45 45 GLY GLY A . n A 1 46 VAL 46 46 46 VAL VAL A . n A 1 47 SER 47 47 47 SER SER A . n A 1 48 THR 48 48 48 THR THR A . n A 1 49 VAL 49 49 49 VAL VAL A . n A 1 50 THR 50 50 50 THR THR A . n A 1 51 ALA 51 51 51 ALA ALA A . n A 1 52 ALA 52 52 52 ALA ALA A . n A 1 53 ARG 53 53 53 ARG ARG A . n A 1 54 ILE 54 54 54 ILE ILE A . n A 1 55 LEU 55 55 55 LEU LEU A . n A 1 56 LYS 56 56 56 LYS LYS A . n A 1 57 GLY 57 57 57 GLY GLY A . n A 1 58 GLN 58 58 58 GLN GLN A . n A 1 59 LYS 59 59 59 LYS LYS A . n A 1 60 LYS 60 60 60 LYS LYS A . n A 1 61 ASP 61 61 61 ASP ASP A . n A 1 62 LYS 62 62 62 LYS LYS A . n A 1 63 LEU 63 63 63 LEU LEU A . n A 1 64 GLY 64 64 64 GLY GLY A . n A 1 65 PRO 65 65 65 PRO PRO A . n A 1 66 GLU 66 66 66 GLU GLU A . n A 1 67 ILE 67 67 67 ILE ILE A . n A 1 68 PRO 68 68 68 PRO PRO A . n A 1 69 LEU 69 69 69 LEU LEU A . n A 1 70 ALA 70 70 70 ALA ALA A . n A 1 71 MET 71 71 71 MET MET A . n A 1 72 ASP 72 72 72 ASP ASP A . n A 1 73 ARG 73 73 73 ARG ARG A . n A 1 74 PHE 74 74 74 PHE PHE A . n A 1 75 PRO 75 75 75 PRO PRO A . n A 1 76 TYR 76 76 76 TYR TYR A . n A 1 77 VAL 77 77 77 VAL VAL A . n A 1 78 ALA 78 78 78 ALA ALA A . n A 1 79 LEU 79 79 79 LEU LEU A . n A 1 80 SER 80 80 80 SER SER A . n A 1 81 LYS 81 81 81 LYS LYS A . n A 1 82 THR 82 82 82 THR THR A . n A 1 83 TYR 83 83 83 TYR TYR A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 VAL 85 85 85 VAL VAL A . n A 1 86 ASP 86 86 86 ASP ASP A . n A 1 87 LYS 87 87 87 LYS LYS A . n A 1 88 HIS 88 88 88 HIS HIS A . n A 1 89 VAL 89 89 89 VAL VAL A . n A 1 90 PRO 90 90 90 PRO PRO A . n A 1 91 ASP 91 91 91 ASP ASP A . n A 1 92 SEP 92 92 92 SEP SEP A . n A 1 93 GLY 93 93 93 GLY GLY A . n A 1 94 ALA 94 94 94 ALA ALA A . n A 1 95 THR 95 95 95 THR THR A . n A 1 96 ALA 96 96 96 ALA ALA A . n A 1 97 THR 97 97 97 THR THR A . n A 1 98 ALA 98 98 98 ALA ALA A . n A 1 99 TYR 99 99 99 TYR TYR A . n A 1 100 LEU 100 100 100 LEU LEU A . n A 1 101 CYS 101 101 101 CYS CYS A . n A 1 102 GLY 102 102 102 GLY GLY A . n A 1 103 VAL 103 103 103 VAL VAL A . n A 1 104 LYS 104 104 104 LYS LYS A . n A 1 105 GLY 105 105 105 GLY GLY A . n A 1 106 ASN 106 106 106 ASN ASN A . n A 1 107 PHE 107 107 107 PHE PHE A . n A 1 108 GLN 108 108 108 GLN GLN A . n A 1 109 THR 109 109 109 THR THR A . n A 1 110 ILE 110 110 110 ILE ILE A . n A 1 111 GLY 111 111 111 GLY GLY A . n A 1 112 LEU 112 112 112 LEU LEU A . n A 1 113 SER 113 113 113 SER SER A . n A 1 114 ALA 114 114 114 ALA ALA A . n A 1 115 ALA 115 115 115 ALA ALA A . n A 1 116 ALA 116 116 116 ALA ALA A . n A 1 117 ARG 117 117 117 ARG ARG A . n A 1 118 PHE 118 118 118 PHE PHE A . n A 1 119 ASN 119 119 119 ASN ASN A . n A 1 120 GLN 120 120 120 GLN GLN A . n A 1 121 CYS 121 121 121 CYS CYS A . n A 1 122 ASN 122 122 122 ASN ASN A . n A 1 123 THR 123 123 123 THR THR A . n A 1 124 THR 124 124 124 THR THR A . n A 1 125 ARG 125 125 125 ARG ARG A . n A 1 126 GLY 126 126 126 GLY GLY A . n A 1 127 ASN 127 127 127 ASN ASN A . n A 1 128 GLU 128 128 128 GLU GLU A . n A 1 129 VAL 129 129 129 VAL VAL A . n A 1 130 ILE 130 130 130 ILE ILE A . n A 1 131 SER 131 131 131 SER SER A . n A 1 132 VAL 132 132 132 VAL VAL A . n A 1 133 MET 133 133 133 MET MET A . n A 1 134 ASN 134 134 134 ASN ASN A . n A 1 135 ARG 135 135 135 ARG ARG A . n A 1 136 ALA 136 136 136 ALA ALA A . n A 1 137 LYS 137 137 137 LYS LYS A . n A 1 138 LYS 138 138 138 LYS LYS A . n A 1 139 ALA 139 139 139 ALA ALA A . n A 1 140 GLY 140 140 140 GLY GLY A . n A 1 141 LYS 141 141 141 LYS LYS A . n A 1 142 SER 142 142 142 SER SER A . n A 1 143 VAL 143 143 143 VAL VAL A . n A 1 144 GLY 144 144 144 GLY GLY A . n A 1 145 VAL 145 145 145 VAL VAL A . n A 1 146 VAL 146 146 146 VAL VAL A . n A 1 147 THR 147 147 147 THR THR A . n A 1 148 THR 148 148 148 THR THR A . n A 1 149 THR 149 149 149 THR THR A . n A 1 150 ARG 150 150 150 ARG ARG A . n A 1 151 VAL 151 151 151 VAL VAL A . n A 1 152 GLN 152 152 152 GLN GLN A . n A 1 153 HIS 153 153 153 HIS HIS A . n A 1 154 ALA 154 154 154 ALA ALA A . n A 1 155 SER 155 155 155 SER SER A . n A 1 156 PRO 156 156 156 PRO PRO A . n A 1 157 ALA 157 157 157 ALA ALA A . n A 1 158 GLY 158 158 158 GLY GLY A . n A 1 159 THR 159 159 159 THR THR A . n A 1 160 TYR 160 160 160 TYR TYR A . n A 1 161 ALA 161 161 161 ALA ALA A . n A 1 162 HIS 162 162 162 HIS HIS A . n A 1 163 THR 163 163 163 THR THR A . n A 1 164 VAL 164 164 164 VAL VAL A . n A 1 165 ASN 165 165 165 ASN ASN A . n A 1 166 ARG 166 166 166 ARG ARG A . n A 1 167 ASN 167 167 167 ASN ASN A . n A 1 168 TRP 168 168 168 TRP TRP A . n A 1 169 TYR 169 169 169 TYR TYR A . n A 1 170 SER 170 170 170 SER SER A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 ALA 172 172 172 ALA ALA A . n A 1 173 ASP 173 173 173 ASP ASP A . n A 1 174 VAL 174 174 174 VAL VAL A . n A 1 175 PRO 175 175 175 PRO PRO A . n A 1 176 ALA 176 176 176 ALA ALA A . n A 1 177 SER 177 177 177 SER SER A . n A 1 178 ALA 178 178 178 ALA ALA A . n A 1 179 ARG 179 179 179 ARG ARG A . n A 1 180 GLN 180 180 180 GLN GLN A . n A 1 181 GLU 181 181 181 GLU GLU A . n A 1 182 GLY 182 182 182 GLY GLY A . n A 1 183 CYS 183 183 183 CYS CYS A . n A 1 184 GLN 184 184 184 GLN GLN A . n A 1 185 ASP 185 185 185 ASP ASP A . n A 1 186 ILE 186 186 186 ILE ILE A . n A 1 187 ALA 187 187 187 ALA ALA A . n A 1 188 THR 188 188 188 THR THR A . n A 1 189 GLN 189 189 189 GLN GLN A . n A 1 190 LEU 190 190 190 LEU LEU A . n A 1 191 ILE 191 191 191 ILE ILE A . n A 1 192 SER 192 192 192 SER SER A . n A 1 193 ASN 193 193 193 ASN ASN A . n A 1 194 MET 194 194 194 MET MET A . n A 1 195 ASP 195 195 195 ASP ASP A . n A 1 196 ILE 196 196 196 ILE ILE A . n A 1 197 ASP 197 197 197 ASP ASP A . n A 1 198 VAL 198 198 198 VAL VAL A . n A 1 199 ILE 199 199 199 ILE ILE A . n A 1 200 LEU 200 200 200 LEU LEU A . n A 1 201 GLY 201 201 201 GLY GLY A . n A 1 202 GLY 202 202 202 GLY GLY A . n A 1 203 GLY 203 203 203 GLY GLY A . n A 1 204 ARG 204 204 204 ARG ARG A . n A 1 205 LYS 205 205 205 LYS LYS A . n A 1 206 TYR 206 206 206 TYR TYR A . n A 1 207 MET 207 207 207 MET MET A . n A 1 208 PHE 208 208 208 PHE PHE A . n A 1 209 ARG 209 209 209 ARG ARG A . n A 1 210 MET 210 210 210 MET MET A . n A 1 211 GLY 211 211 211 GLY GLY A . n A 1 212 THR 212 212 212 THR THR A . n A 1 213 PRO 213 213 213 PRO PRO A . n A 1 214 ASP 214 214 214 ASP ASP A . n A 1 215 PRO 215 215 215 PRO PRO A . n A 1 216 GLU 216 216 216 GLU GLU A . n A 1 217 TYR 217 217 217 TYR TYR A . n A 1 218 PRO 218 218 218 PRO PRO A . n A 1 219 ASP 219 219 219 ASP ASP A . n A 1 220 ASP 220 220 220 ASP ASP A . n A 1 221 TYR 221 221 221 TYR TYR A . n A 1 222 SER 222 222 222 SER SER A . n A 1 223 GLN 223 223 223 GLN GLN A . n A 1 224 GLY 224 224 224 GLY GLY A . n A 1 225 GLY 225 225 225 GLY GLY A . n A 1 226 THR 226 226 226 THR THR A . n A 1 227 ARG 227 227 227 ARG ARG A . n A 1 228 LEU 228 228 228 LEU LEU A . n A 1 229 ASP 229 229 229 ASP ASP A . n A 1 230 GLY 230 230 230 GLY GLY A . n A 1 231 LYS 231 231 231 LYS LYS A . n A 1 232 ASN 232 232 232 ASN ASN A . n A 1 233 LEU 233 233 233 LEU LEU A . n A 1 234 VAL 234 234 234 VAL VAL A . n A 1 235 GLN 235 235 235 GLN GLN A . n A 1 236 GLU 236 236 236 GLU GLU A . n A 1 237 TRP 237 237 237 TRP TRP A . n A 1 238 LEU 238 238 238 LEU LEU A . n A 1 239 ALA 239 239 239 ALA ALA A . n A 1 240 LYS 240 240 240 LYS LYS A . n A 1 241 ARG 241 241 241 ARG ARG A . n A 1 242 GLN 242 242 242 GLN GLN A . n A 1 243 GLY 243 243 243 GLY GLY A . n A 1 244 ALA 244 244 244 ALA ALA A . n A 1 245 ARG 245 245 245 ARG ARG A . n A 1 246 TYR 246 246 246 TYR TYR A . n A 1 247 VAL 247 247 247 VAL VAL A . n A 1 248 TRP 248 248 248 TRP TRP A . n A 1 249 ASN 249 249 249 ASN ASN A . n A 1 250 ARG 250 250 250 ARG ARG A . n A 1 251 THR 251 251 251 THR THR A . n A 1 252 GLU 252 252 252 GLU GLU A . n A 1 253 LEU 253 253 253 LEU LEU A . n A 1 254 MET 254 254 254 MET MET A . n A 1 255 GLN 255 255 255 GLN GLN A . n A 1 256 ALA 256 256 256 ALA ALA A . n A 1 257 SER 257 257 257 SER SER A . n A 1 258 LEU 258 258 258 LEU LEU A . n A 1 259 ASP 259 259 259 ASP ASP A . n A 1 260 PRO 260 260 260 PRO PRO A . n A 1 261 SER 261 261 261 SER SER A . n A 1 262 VAL 262 262 262 VAL VAL A . n A 1 263 THR 263 263 263 THR THR A . n A 1 264 HIS 264 264 264 HIS HIS A . n A 1 265 LEU 265 265 265 LEU LEU A . n A 1 266 MET 266 266 266 MET MET A . n A 1 267 GLY 267 267 267 GLY GLY A . n A 1 268 LEU 268 268 268 LEU LEU A . n A 1 269 PHE 269 269 269 PHE PHE A . n A 1 270 GLU 270 270 270 GLU GLU A . n A 1 271 PRO 271 271 271 PRO PRO A . n A 1 272 GLY 272 272 272 GLY GLY A . n A 1 273 ASP 273 273 273 ASP ASP A . n A 1 274 MET 274 274 274 MET MET A . n A 1 275 LYS 275 275 275 LYS LYS A . n A 1 276 TYR 276 276 276 TYR TYR A . n A 1 277 GLU 277 277 277 GLU GLU A . n A 1 278 ILE 278 278 278 ILE ILE A . n A 1 279 HIS 279 279 279 HIS HIS A . n A 1 280 ARG 280 280 280 ARG ARG A . n A 1 281 ASP 281 281 281 ASP ASP A . n A 1 282 SER 282 282 282 SER SER A . n A 1 283 THR 283 283 283 THR THR A . n A 1 284 LEU 284 284 284 LEU LEU A . n A 1 285 ASP 285 285 285 ASP ASP A . n A 1 286 PRO 286 286 286 PRO PRO A . n A 1 287 SER 287 287 287 SER SER A . n A 1 288 LEU 288 288 288 LEU LEU A . n A 1 289 MET 289 289 289 MET MET A . n A 1 290 GLU 290 290 290 GLU GLU A . n A 1 291 MET 291 291 291 MET MET A . n A 1 292 THR 292 292 292 THR THR A . n A 1 293 GLU 293 293 293 GLU GLU A . n A 1 294 ALA 294 294 294 ALA ALA A . n A 1 295 ALA 295 295 295 ALA ALA A . n A 1 296 LEU 296 296 296 LEU LEU A . n A 1 297 ARG 297 297 297 ARG ARG A . n A 1 298 LEU 298 298 298 LEU LEU A . n A 1 299 LEU 299 299 299 LEU LEU A . n A 1 300 SER 300 300 300 SER SER A . n A 1 301 ARG 301 301 301 ARG ARG A . n A 1 302 ASN 302 302 302 ASN ASN A . n A 1 303 PRO 303 303 303 PRO PRO A . n A 1 304 ARG 304 304 304 ARG ARG A . n A 1 305 GLY 305 305 305 GLY GLY A . n A 1 306 PHE 306 306 306 PHE PHE A . n A 1 307 PHE 307 307 307 PHE PHE A . n A 1 308 LEU 308 308 308 LEU LEU A . n A 1 309 PHE 309 309 309 PHE PHE A . n A 1 310 VAL 310 310 310 VAL VAL A . n A 1 311 GLU 311 311 311 GLU GLU A . n A 1 312 GLY 312 312 312 GLY GLY A . n A 1 313 GLY 313 313 313 GLY GLY A . n A 1 314 ARG 314 314 314 ARG ARG A . n A 1 315 ILE 315 315 315 ILE ILE A . n A 1 316 ASP 316 316 316 ASP ASP A . n A 1 317 HIS 317 317 317 HIS HIS A . n A 1 318 GLY 318 318 318 GLY GLY A . n A 1 319 HIS 319 319 319 HIS HIS A . n A 1 320 HIS 320 320 320 HIS HIS A . n A 1 321 GLU 321 321 321 GLU GLU A . n A 1 322 SER 322 322 322 SER SER A . n A 1 323 ARG 323 323 323 ARG ARG A . n A 1 324 ALA 324 324 324 ALA ALA A . n A 1 325 TYR 325 325 325 TYR TYR A . n A 1 326 ARG 326 326 326 ARG ARG A . n A 1 327 ALA 327 327 327 ALA ALA A . n A 1 328 LEU 328 328 328 LEU LEU A . n A 1 329 THR 329 329 329 THR THR A . n A 1 330 GLU 330 330 330 GLU GLU A . n A 1 331 THR 331 331 331 THR THR A . n A 1 332 ILE 332 332 332 ILE ILE A . n A 1 333 MET 333 333 333 MET MET A . n A 1 334 PHE 334 334 334 PHE PHE A . n A 1 335 ASP 335 335 335 ASP ASP A . n A 1 336 ASP 336 336 336 ASP ASP A . n A 1 337 ALA 337 337 337 ALA ALA A . n A 1 338 ILE 338 338 338 ILE ILE A . n A 1 339 GLU 339 339 339 GLU GLU A . n A 1 340 ARG 340 340 340 ARG ARG A . n A 1 341 ALA 341 341 341 ALA ALA A . n A 1 342 GLY 342 342 342 GLY GLY A . n A 1 343 GLN 343 343 343 GLN GLN A . n A 1 344 LEU 344 344 344 LEU LEU A . n A 1 345 THR 345 345 345 THR THR A . n A 1 346 SER 346 346 346 SER SER A . n A 1 347 GLU 347 347 347 GLU GLU A . n A 1 348 GLU 348 348 348 GLU GLU A . n A 1 349 ASP 349 349 349 ASP ASP A . n A 1 350 THR 350 350 350 THR THR A . n A 1 351 LEU 351 351 351 LEU LEU A . n A 1 352 SER 352 352 352 SER SER A . n A 1 353 LEU 353 353 353 LEU LEU A . n A 1 354 VAL 354 354 354 VAL VAL A . n A 1 355 THR 355 355 355 THR THR A . n A 1 356 ALA 356 356 356 ALA ALA A . n A 1 357 ASP 357 357 357 ASP ASP A . n A 1 358 HIS 358 358 358 HIS HIS A . n A 1 359 SER 359 359 359 SER SER A . n A 1 360 HIS 360 360 360 HIS HIS A . n A 1 361 VAL 361 361 361 VAL VAL A . n A 1 362 PHE 362 362 362 PHE PHE A . n A 1 363 SER 363 363 363 SER SER A . n A 1 364 PHE 364 364 364 PHE PHE A . n A 1 365 GLY 365 365 365 GLY GLY A . n A 1 366 GLY 366 366 366 GLY GLY A . n A 1 367 TYR 367 367 367 TYR TYR A . n A 1 368 PRO 368 368 368 PRO PRO A . n A 1 369 LEU 369 369 369 LEU LEU A . n A 1 370 ARG 370 370 370 ARG ARG A . n A 1 371 GLY 371 371 371 GLY GLY A . n A 1 372 SER 372 372 372 SER SER A . n A 1 373 SER 373 373 373 SER SER A . n A 1 374 ILE 374 374 374 ILE ILE A . n A 1 375 PHE 375 375 375 PHE PHE A . n A 1 376 GLY 376 376 376 GLY GLY A . n A 1 377 LEU 377 377 377 LEU LEU A . n A 1 378 ALA 378 378 378 ALA ALA A . n A 1 379 PRO 379 379 379 PRO PRO A . n A 1 380 GLY 380 380 380 GLY GLY A . n A 1 381 LYS 381 381 381 LYS LYS A . n A 1 382 ALA 382 382 382 ALA ALA A . n A 1 383 ARG 383 383 383 ARG ARG A . n A 1 384 ASP 384 384 384 ASP ASP A . n A 1 385 ARG 385 385 385 ARG ARG A . n A 1 386 LYS 386 386 386 LYS LYS A . n A 1 387 ALA 387 387 387 ALA ALA A . n A 1 388 TYR 388 388 388 TYR TYR A . n A 1 389 THR 389 389 389 THR THR A . n A 1 390 VAL 390 390 390 VAL VAL A . n A 1 391 LEU 391 391 391 LEU LEU A . n A 1 392 LEU 392 392 392 LEU LEU A . n A 1 393 TYR 393 393 393 TYR TYR A . n A 1 394 GLY 394 394 394 GLY GLY A . n A 1 395 ASN 395 395 395 ASN ASN A . n A 1 396 GLY 396 396 396 GLY GLY A . n A 1 397 PRO 397 397 397 PRO PRO A . n A 1 398 GLY 398 398 398 GLY GLY A . n A 1 399 TYR 399 399 399 TYR TYR A . n A 1 400 VAL 400 400 400 VAL VAL A . n A 1 401 LEU 401 401 401 LEU LEU A . n A 1 402 LYS 402 402 402 LYS LYS A . n A 1 403 ASP 403 403 403 ASP ASP A . n A 1 404 GLY 404 404 404 GLY GLY A . n A 1 405 ALA 405 405 405 ALA ALA A . n A 1 406 ARG 406 406 406 ARG ARG A . n A 1 407 PRO 407 407 407 PRO PRO A . n A 1 408 ASP 408 408 408 ASP ASP A . n A 1 409 VAL 409 409 409 VAL VAL A . n A 1 410 THR 410 410 410 THR THR A . n A 1 411 GLU 411 411 411 GLU GLU A . n A 1 412 SER 412 412 412 SER SER A . n A 1 413 GLU 413 413 413 GLU GLU A . n A 1 414 SER 414 414 414 SER SER A . n A 1 415 GLY 415 415 415 GLY GLY A . n A 1 416 SER 416 416 416 SER SER A . n A 1 417 PRO 417 417 417 PRO PRO A . n A 1 418 GLU 418 418 418 GLU GLU A . n A 1 419 TYR 419 419 419 TYR TYR A . n A 1 420 ARG 420 420 420 ARG ARG A . n A 1 421 GLN 421 421 421 GLN GLN A . n A 1 422 GLN 422 422 422 GLN GLN A . n A 1 423 SER 423 423 423 SER SER A . n A 1 424 ALA 424 424 424 ALA ALA A . n A 1 425 VAL 425 425 425 VAL VAL A . n A 1 426 PRO 426 426 426 PRO PRO A . n A 1 427 LEU 427 427 427 LEU LEU A . n A 1 428 ASP 428 428 428 ASP ASP A . n A 1 429 GLU 429 429 429 GLU GLU A . n A 1 430 GLU 430 430 430 GLU GLU A . n A 1 431 THR 431 431 431 THR THR A . n A 1 432 HIS 432 432 432 HIS HIS A . n A 1 433 ALA 433 433 433 ALA ALA A . n A 1 434 GLY 434 434 434 GLY GLY A . n A 1 435 GLU 435 435 435 GLU GLU A . n A 1 436 ASP 436 436 436 ASP ASP A . n A 1 437 VAL 437 437 437 VAL VAL A . n A 1 438 ALA 438 438 438 ALA ALA A . n A 1 439 VAL 439 439 439 VAL VAL A . n A 1 440 PHE 440 440 440 PHE PHE A . n A 1 441 ALA 441 441 441 ALA ALA A . n A 1 442 ARG 442 442 442 ARG ARG A . n A 1 443 GLY 443 443 443 GLY GLY A . n A 1 444 PRO 444 444 444 PRO PRO A . n A 1 445 GLN 445 445 445 GLN GLN A . n A 1 446 ALA 446 446 446 ALA ALA A . n A 1 447 HIS 447 447 447 HIS HIS A . n A 1 448 LEU 448 448 448 LEU LEU A . n A 1 449 VAL 449 449 449 VAL VAL A . n A 1 450 HIS 450 450 450 HIS HIS A . n A 1 451 GLY 451 451 451 GLY GLY A . n A 1 452 VAL 452 452 452 VAL VAL A . n A 1 453 GLN 453 453 453 GLN GLN A . n A 1 454 GLU 454 454 454 GLU GLU A . n A 1 455 GLN 455 455 455 GLN GLN A . n A 1 456 THR 456 456 456 THR THR A . n A 1 457 PHE 457 457 457 PHE PHE A . n A 1 458 ILE 458 458 458 ILE ILE A . n A 1 459 ALA 459 459 459 ALA ALA A . n A 1 460 HIS 460 460 460 HIS HIS A . n A 1 461 VAL 461 461 461 VAL VAL A . n A 1 462 MET 462 462 462 MET MET A . n A 1 463 ALA 463 463 463 ALA ALA A . n A 1 464 PHE 464 464 464 PHE PHE A . n A 1 465 ALA 465 465 465 ALA ALA A . n A 1 466 ALA 466 466 466 ALA ALA A . n A 1 467 CYS 467 467 467 CYS CYS A . n A 1 468 LEU 468 468 468 LEU LEU A . n A 1 469 GLU 469 469 469 GLU GLU A . n A 1 470 PRO 470 470 470 PRO PRO A . n A 1 471 TYR 471 471 471 TYR TYR A . n A 1 472 THR 472 472 472 THR THR A . n A 1 473 ALA 473 473 473 ALA ALA A . n A 1 474 CYS 474 474 474 CYS CYS A . n A 1 475 ASP 475 475 475 ASP ASP A . n A 1 476 LEU 476 476 476 LEU LEU A . n A 1 477 ALA 477 477 477 ALA ALA A . n A 1 478 PRO 478 478 478 PRO PRO A . n A 1 479 PRO 479 479 479 PRO PRO A . n A 1 480 ALA 480 480 480 ALA ALA A . n A 1 481 GLY 481 481 481 GLY GLY A . n A 1 482 THR 482 482 ? ? ? A . n A 1 483 THR 483 483 ? ? ? A . n A 1 484 ASP 484 484 ? ? ? 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 PHE 1 912 912 PHE PHE A . C 2 PHE 1 923 923 PHE PHE A . D 3 NAG 1 801 801 NAG NAG A . E 3 NAG 2 802 802 NAG NAG A . F 3 NAG 1 803 803 NAG NAG A . G 3 NAG 2 804 804 NAG NAG A . H 4 ZN 1 901 901 ZN ZN A . I 4 ZN 1 902 902 ZN ZN A . J 5 MG 1 903 903 MG MG A . K 6 CA 1 904 904 CA CA A . L 7 ACT 1 933 933 ACT ACT A . M 7 ACT 1 934 934 ACT ACT A . N 7 ACT 1 935 935 ACT ACT A . O 8 GOL 1 936 936 GOL GOL A . P 8 GOL 1 937 937 GOL GOL A . Q 9 HOH 1 1001 1001 HOH HOH A . Q 9 HOH 2 1002 1002 HOH HOH A . Q 9 HOH 3 1003 1003 HOH HOH A . Q 9 HOH 4 1004 1004 HOH HOH A . Q 9 HOH 5 1005 1005 HOH HOH A . Q 9 HOH 6 1006 1006 HOH HOH A . Q 9 HOH 7 1007 1007 HOH HOH A . Q 9 HOH 8 1008 1008 HOH HOH A . Q 9 HOH 9 1009 1009 HOH HOH A . Q 9 HOH 10 1010 1010 HOH HOH A . Q 9 HOH 11 1011 1011 HOH HOH A . Q 9 HOH 12 1012 1012 HOH HOH A . Q 9 HOH 13 1013 1013 HOH HOH A . Q 9 HOH 14 1014 1014 HOH HOH A . Q 9 HOH 15 1015 1015 HOH HOH A . Q 9 HOH 16 1016 1016 HOH HOH A . Q 9 HOH 17 1017 1017 HOH HOH A . Q 9 HOH 18 1018 1018 HOH HOH A . Q 9 HOH 19 1019 1019 HOH HOH A . Q 9 HOH 20 1020 1020 HOH HOH A . Q 9 HOH 21 1021 1021 HOH HOH A . Q 9 HOH 22 1022 1022 HOH HOH A . Q 9 HOH 23 1023 1023 HOH HOH A . Q 9 HOH 24 1024 1024 HOH HOH A . Q 9 HOH 25 1025 1025 HOH HOH A . Q 9 HOH 26 1026 1026 HOH HOH A . Q 9 HOH 27 1027 1027 HOH HOH A . Q 9 HOH 28 1028 1028 HOH HOH A . Q 9 HOH 29 1029 1029 HOH HOH A . Q 9 HOH 30 1030 1030 HOH HOH A . Q 9 HOH 31 1031 1031 HOH HOH A . Q 9 HOH 32 1032 1032 HOH HOH A . Q 9 HOH 33 1033 1033 HOH HOH A . Q 9 HOH 34 1034 1034 HOH HOH A . Q 9 HOH 35 1035 1035 HOH HOH A . Q 9 HOH 36 1036 1036 HOH HOH A . Q 9 HOH 37 1037 1037 HOH HOH A . Q 9 HOH 38 1038 1038 HOH HOH A . Q 9 HOH 39 1039 1039 HOH HOH A . Q 9 HOH 40 1040 1040 HOH HOH A . Q 9 HOH 41 1041 1041 HOH HOH A . Q 9 HOH 42 1042 1042 HOH HOH A . Q 9 HOH 43 1043 1043 HOH HOH A . Q 9 HOH 44 1044 1044 HOH HOH A . Q 9 HOH 45 1045 1045 HOH HOH A . Q 9 HOH 46 1046 1046 HOH HOH A . Q 9 HOH 47 1047 1047 HOH HOH A . Q 9 HOH 48 1048 1048 HOH HOH A . Q 9 HOH 49 1049 1049 HOH HOH A . Q 9 HOH 50 1050 1050 HOH HOH A . Q 9 HOH 51 1051 1051 HOH HOH A . Q 9 HOH 52 1052 1052 HOH HOH A . Q 9 HOH 53 1053 1053 HOH HOH A . Q 9 HOH 54 1054 1054 HOH HOH A . Q 9 HOH 55 1055 1055 HOH HOH A . Q 9 HOH 56 1056 1056 HOH HOH A . Q 9 HOH 57 1057 1057 HOH HOH A . Q 9 HOH 58 1058 1058 HOH HOH A . Q 9 HOH 59 1059 1059 HOH HOH A . Q 9 HOH 60 1060 1060 HOH HOH A . Q 9 HOH 61 1061 1061 HOH HOH A . Q 9 HOH 62 1062 1062 HOH HOH A . Q 9 HOH 63 1063 1063 HOH HOH A . Q 9 HOH 64 1064 1064 HOH HOH A . Q 9 HOH 65 1065 1065 HOH HOH A . Q 9 HOH 66 1066 1066 HOH HOH A . Q 9 HOH 67 1067 1067 HOH HOH A . Q 9 HOH 68 1068 1068 HOH HOH A . Q 9 HOH 69 1069 1069 HOH HOH A . Q 9 HOH 70 1070 1070 HOH HOH A . Q 9 HOH 71 1071 1071 HOH HOH A . Q 9 HOH 72 1072 1072 HOH HOH A . Q 9 HOH 73 1073 1073 HOH HOH A . Q 9 HOH 74 1074 1074 HOH HOH A . Q 9 HOH 75 1075 1075 HOH HOH A . Q 9 HOH 76 1076 1076 HOH HOH A . Q 9 HOH 77 1077 1077 HOH HOH A . Q 9 HOH 78 1078 1078 HOH HOH A . Q 9 HOH 79 1079 1079 HOH HOH A . Q 9 HOH 80 1080 1080 HOH HOH A . Q 9 HOH 81 1081 1081 HOH HOH A . Q 9 HOH 82 1082 1082 HOH HOH A . Q 9 HOH 83 1083 1083 HOH HOH A . Q 9 HOH 84 1084 1084 HOH HOH A . Q 9 HOH 85 1085 1085 HOH HOH A . Q 9 HOH 86 1086 1086 HOH HOH A . Q 9 HOH 87 1087 1087 HOH HOH A . Q 9 HOH 88 1088 1088 HOH HOH A . Q 9 HOH 89 1089 1089 HOH HOH A . Q 9 HOH 90 1090 1090 HOH HOH A . Q 9 HOH 91 1091 1091 HOH HOH A . Q 9 HOH 92 1092 1092 HOH HOH A . Q 9 HOH 93 1093 1093 HOH HOH A . Q 9 HOH 94 1094 1094 HOH HOH A . Q 9 HOH 95 1095 1095 HOH HOH A . Q 9 HOH 96 1096 1096 HOH HOH A . Q 9 HOH 97 1097 1097 HOH HOH A . Q 9 HOH 98 1098 1098 HOH HOH A . Q 9 HOH 99 1099 1099 HOH HOH A . Q 9 HOH 100 1100 1100 HOH HOH A . Q 9 HOH 101 1101 1101 HOH HOH A . Q 9 HOH 102 1102 1102 HOH HOH A . Q 9 HOH 103 1103 1103 HOH HOH A . Q 9 HOH 104 1104 1104 HOH HOH A . Q 9 HOH 105 1105 1105 HOH HOH A . Q 9 HOH 106 1106 1106 HOH HOH A . Q 9 HOH 107 1107 1107 HOH HOH A . Q 9 HOH 108 1108 1108 HOH HOH A . Q 9 HOH 109 1109 1109 HOH HOH A . Q 9 HOH 110 1110 1110 HOH HOH A . Q 9 HOH 111 1111 1111 HOH HOH A . Q 9 HOH 112 1112 1112 HOH HOH A . Q 9 HOH 113 1113 1113 HOH HOH A . Q 9 HOH 114 1114 1114 HOH HOH A . Q 9 HOH 115 1115 1115 HOH HOH A . Q 9 HOH 116 1116 1116 HOH HOH A . Q 9 HOH 117 1117 1117 HOH HOH A . Q 9 HOH 118 1118 1118 HOH HOH A . Q 9 HOH 119 1119 1119 HOH HOH A . Q 9 HOH 120 1120 1120 HOH HOH A . Q 9 HOH 121 1121 1121 HOH HOH A . Q 9 HOH 122 1122 1122 HOH HOH A . Q 9 HOH 123 1123 1123 HOH HOH A . Q 9 HOH 124 1124 1124 HOH HOH A . Q 9 HOH 125 1125 1125 HOH HOH A . Q 9 HOH 126 1126 1126 HOH HOH A . Q 9 HOH 127 1127 1127 HOH HOH A . Q 9 HOH 128 1128 1128 HOH HOH A . Q 9 HOH 129 1129 1129 HOH HOH A . Q 9 HOH 130 1130 1130 HOH HOH A . Q 9 HOH 131 1131 1131 HOH HOH A . Q 9 HOH 132 1132 1132 HOH HOH A . Q 9 HOH 133 1133 1133 HOH HOH A . Q 9 HOH 134 1134 1134 HOH HOH A . Q 9 HOH 135 1135 1135 HOH HOH A . Q 9 HOH 136 1136 1136 HOH HOH A . Q 9 HOH 137 1137 1137 HOH HOH A . Q 9 HOH 138 1138 1138 HOH HOH A . Q 9 HOH 139 1139 1139 HOH HOH A . Q 9 HOH 140 1140 1140 HOH HOH A . Q 9 HOH 141 1141 1141 HOH HOH A . Q 9 HOH 142 1142 1142 HOH HOH A . Q 9 HOH 143 1143 1143 HOH HOH A . Q 9 HOH 144 1144 1144 HOH HOH A . Q 9 HOH 145 1145 1145 HOH HOH A . Q 9 HOH 146 1146 1146 HOH HOH A . Q 9 HOH 147 1147 1147 HOH HOH A . Q 9 HOH 148 1148 1148 HOH HOH A . Q 9 HOH 149 1149 1149 HOH HOH A . Q 9 HOH 150 1150 1150 HOH HOH A . Q 9 HOH 151 1151 1151 HOH HOH A . Q 9 HOH 152 1152 1152 HOH HOH A . Q 9 HOH 153 1153 1153 HOH HOH A . Q 9 HOH 154 1154 1154 HOH HOH A . Q 9 HOH 155 1155 1155 HOH HOH A . Q 9 HOH 156 1156 1156 HOH HOH A . Q 9 HOH 157 1157 1157 HOH HOH A . Q 9 HOH 158 1158 1158 HOH HOH A . Q 9 HOH 159 1159 1159 HOH HOH A . Q 9 HOH 160 1160 1160 HOH HOH A . Q 9 HOH 161 1161 1161 HOH HOH A . Q 9 HOH 162 1162 1162 HOH HOH A . Q 9 HOH 163 1163 1163 HOH HOH A . Q 9 HOH 164 1164 1164 HOH HOH A . Q 9 HOH 165 1165 1165 HOH HOH A . Q 9 HOH 166 1166 1166 HOH HOH A . Q 9 HOH 167 1167 1167 HOH HOH A . Q 9 HOH 168 1168 1168 HOH HOH A . Q 9 HOH 169 1169 1169 HOH HOH A . Q 9 HOH 170 1170 1170 HOH HOH A . Q 9 HOH 171 1171 1171 HOH HOH A . Q 9 HOH 172 1172 1172 HOH HOH A . Q 9 HOH 173 1173 1173 HOH HOH A . Q 9 HOH 174 1174 1174 HOH HOH A . Q 9 HOH 175 1175 1175 HOH HOH A . Q 9 HOH 176 1176 1176 HOH HOH A . Q 9 HOH 177 1177 1177 HOH HOH A . Q 9 HOH 178 1178 1178 HOH HOH A . Q 9 HOH 179 1179 1179 HOH HOH A . Q 9 HOH 180 1180 1180 HOH HOH A . Q 9 HOH 181 1181 1181 HOH HOH A . Q 9 HOH 182 1182 1182 HOH HOH A . Q 9 HOH 183 1183 1183 HOH HOH A . Q 9 HOH 184 1184 1184 HOH HOH A . Q 9 HOH 185 1185 1185 HOH HOH A . Q 9 HOH 186 1186 1186 HOH HOH A . Q 9 HOH 187 1187 1187 HOH HOH A . Q 9 HOH 188 1188 1188 HOH HOH A . Q 9 HOH 189 1189 1189 HOH HOH A . Q 9 HOH 190 1190 1190 HOH HOH A . Q 9 HOH 191 1191 1191 HOH HOH A . Q 9 HOH 192 1192 1192 HOH HOH A . Q 9 HOH 193 1193 1193 HOH HOH A . Q 9 HOH 194 1194 1194 HOH HOH A . Q 9 HOH 195 1195 1195 HOH HOH A . Q 9 HOH 196 1196 1196 HOH HOH A . Q 9 HOH 197 1197 1197 HOH HOH A . Q 9 HOH 198 1198 1198 HOH HOH A . Q 9 HOH 199 1199 1199 HOH HOH A . Q 9 HOH 200 1200 1200 HOH HOH A . Q 9 HOH 201 1201 1201 HOH HOH A . Q 9 HOH 202 1202 1202 HOH HOH A . Q 9 HOH 203 1203 1203 HOH HOH A . Q 9 HOH 204 1204 1204 HOH HOH A . Q 9 HOH 205 1205 1205 HOH HOH A . Q 9 HOH 206 1206 1206 HOH HOH A . Q 9 HOH 207 1207 1207 HOH HOH A . Q 9 HOH 208 1208 1208 HOH HOH A . Q 9 HOH 209 1209 1209 HOH HOH A . Q 9 HOH 210 1210 1210 HOH HOH A . Q 9 HOH 211 1211 1211 HOH HOH A . Q 9 HOH 212 1212 1212 HOH HOH A . Q 9 HOH 213 1213 1213 HOH HOH A . Q 9 HOH 214 1214 1214 HOH HOH A . Q 9 HOH 215 1215 1215 HOH HOH A . Q 9 HOH 216 1216 1216 HOH HOH A . Q 9 HOH 217 1217 1217 HOH HOH A . Q 9 HOH 218 1218 1218 HOH HOH A . Q 9 HOH 219 1219 1219 HOH HOH A . Q 9 HOH 220 1220 1220 HOH HOH A . Q 9 HOH 221 1221 1221 HOH HOH A . Q 9 HOH 222 1222 1222 HOH HOH A . Q 9 HOH 223 1223 1223 HOH HOH A . Q 9 HOH 224 1224 1224 HOH HOH A . Q 9 HOH 225 1225 1225 HOH HOH A . Q 9 HOH 226 1226 1226 HOH HOH A . Q 9 HOH 227 1227 1227 HOH HOH A . Q 9 HOH 228 1228 1228 HOH HOH A . Q 9 HOH 229 1229 1229 HOH HOH A . Q 9 HOH 230 1230 1230 HOH HOH A . Q 9 HOH 231 1231 1231 HOH HOH A . Q 9 HOH 232 1232 1232 HOH HOH A . Q 9 HOH 233 1233 1233 HOH HOH A . Q 9 HOH 234 1234 1234 HOH HOH A . Q 9 HOH 235 1235 1235 HOH HOH A . Q 9 HOH 236 1237 1237 HOH HOH A . Q 9 HOH 237 1238 1238 HOH HOH A . Q 9 HOH 238 1239 1239 HOH HOH A . Q 9 HOH 239 1240 1240 HOH HOH A . Q 9 HOH 240 1241 1241 HOH HOH A . Q 9 HOH 241 1242 1242 HOH HOH A . Q 9 HOH 242 1243 1243 HOH HOH A . Q 9 HOH 243 1244 1244 HOH HOH A . Q 9 HOH 244 1245 1245 HOH HOH A . Q 9 HOH 245 1246 1246 HOH HOH A . Q 9 HOH 246 1247 1247 HOH HOH A . Q 9 HOH 247 1248 1248 HOH HOH A . Q 9 HOH 248 1249 1249 HOH HOH A . Q 9 HOH 249 1250 1250 HOH HOH A . Q 9 HOH 250 1251 1251 HOH HOH A . Q 9 HOH 251 1252 1252 HOH HOH A . Q 9 HOH 252 1253 1253 HOH HOH A . Q 9 HOH 253 1254 1254 HOH HOH A . Q 9 HOH 254 1255 1255 HOH HOH A . Q 9 HOH 255 1256 1256 HOH HOH A . Q 9 HOH 256 1257 1257 HOH HOH A . Q 9 HOH 257 1258 1258 HOH HOH A . Q 9 HOH 258 1259 1259 HOH HOH A . Q 9 HOH 259 1260 1260 HOH HOH A . Q 9 HOH 260 1261 1261 HOH HOH A . Q 9 HOH 261 1262 1262 HOH HOH A . Q 9 HOH 262 1263 1263 HOH HOH A . Q 9 HOH 263 1264 1264 HOH HOH A . Q 9 HOH 264 1265 1265 HOH HOH A . Q 9 HOH 265 1266 1266 HOH HOH A . Q 9 HOH 266 1267 1267 HOH HOH A . Q 9 HOH 267 1268 1268 HOH HOH A . Q 9 HOH 268 1269 1269 HOH HOH A . Q 9 HOH 269 1270 1270 HOH HOH A . Q 9 HOH 270 1271 1271 HOH HOH A . Q 9 HOH 271 1272 1272 HOH HOH A . Q 9 HOH 272 1273 1273 HOH HOH A . Q 9 HOH 273 1274 1274 HOH HOH A . Q 9 HOH 274 1275 1275 HOH HOH A . Q 9 HOH 275 1276 1276 HOH HOH A . Q 9 HOH 276 1277 1277 HOH HOH A . Q 9 HOH 277 1278 1278 HOH HOH A . Q 9 HOH 278 1279 1279 HOH HOH A . Q 9 HOH 279 1280 1280 HOH HOH A . Q 9 HOH 280 1281 1281 HOH HOH A . Q 9 HOH 281 1282 1282 HOH HOH A . Q 9 HOH 282 1283 1283 HOH HOH A . Q 9 HOH 283 1284 1284 HOH HOH A . Q 9 HOH 284 1285 1285 HOH HOH A . Q 9 HOH 285 1286 1286 HOH HOH A . Q 9 HOH 286 1287 1287 HOH HOH A . Q 9 HOH 287 1288 1288 HOH HOH A . Q 9 HOH 288 1289 1289 HOH HOH A . Q 9 HOH 289 1290 1290 HOH HOH A . Q 9 HOH 290 1291 1291 HOH HOH A . Q 9 HOH 291 1292 1292 HOH HOH A . Q 9 HOH 292 1293 1293 HOH HOH A . Q 9 HOH 293 1294 1294 HOH HOH A . Q 9 HOH 294 1295 1295 HOH HOH A . Q 9 HOH 295 1296 1296 HOH HOH A . Q 9 HOH 296 1297 1297 HOH HOH A . Q 9 HOH 297 1298 1298 HOH HOH A . Q 9 HOH 298 1299 1299 HOH HOH A . Q 9 HOH 299 1300 1300 HOH HOH A . Q 9 HOH 300 1301 1301 HOH HOH A . Q 9 HOH 301 1302 1302 HOH HOH A . Q 9 HOH 302 1303 1303 HOH HOH A . Q 9 HOH 303 1304 1304 HOH HOH A . Q 9 HOH 304 1305 1305 HOH HOH A . Q 9 HOH 305 1306 1306 HOH HOH A . Q 9 HOH 306 1307 1307 HOH HOH A . Q 9 HOH 307 1308 1308 HOH HOH A . Q 9 HOH 308 1309 1309 HOH HOH A . Q 9 HOH 309 1310 1310 HOH HOH A . Q 9 HOH 310 1311 1311 HOH HOH A . Q 9 HOH 311 1312 1312 HOH HOH A . Q 9 HOH 312 1313 1313 HOH HOH A . Q 9 HOH 313 1314 1314 HOH HOH A . Q 9 HOH 314 1315 1315 HOH HOH A . Q 9 HOH 315 1316 1316 HOH HOH A . Q 9 HOH 316 1317 1317 HOH HOH A . Q 9 HOH 317 1318 1318 HOH HOH A . Q 9 HOH 318 1319 1319 HOH HOH A . Q 9 HOH 319 1320 1320 HOH HOH A . Q 9 HOH 320 1321 1321 HOH HOH A . Q 9 HOH 321 1322 1322 HOH HOH A . Q 9 HOH 322 1323 1323 HOH HOH A . Q 9 HOH 323 1324 1324 HOH HOH A . Q 9 HOH 324 1325 1325 HOH HOH A . Q 9 HOH 325 1326 1326 HOH HOH A . Q 9 HOH 326 1327 1327 HOH HOH A . Q 9 HOH 327 1328 1328 HOH HOH A . Q 9 HOH 328 1329 1329 HOH HOH A . Q 9 HOH 329 1330 1330 HOH HOH A . Q 9 HOH 330 1331 1331 HOH HOH A . Q 9 HOH 331 1332 1332 HOH HOH A . Q 9 HOH 332 1333 1333 HOH HOH A . Q 9 HOH 333 1334 1334 HOH HOH A . Q 9 HOH 334 1335 1335 HOH HOH A . Q 9 HOH 335 1336 1336 HOH HOH A . Q 9 HOH 336 1337 1337 HOH HOH A . Q 9 HOH 337 1338 1338 HOH HOH A . Q 9 HOH 338 1339 1339 HOH HOH A . Q 9 HOH 339 1340 1340 HOH HOH A . Q 9 HOH 340 1341 1341 HOH HOH A . Q 9 HOH 341 1342 1342 HOH HOH A . Q 9 HOH 342 1343 1343 HOH HOH A . Q 9 HOH 343 1344 1344 HOH HOH A . Q 9 HOH 344 1345 1345 HOH HOH A . Q 9 HOH 345 1346 1346 HOH HOH A . Q 9 HOH 346 1347 1347 HOH HOH A . Q 9 HOH 347 1348 1348 HOH HOH A . Q 9 HOH 348 1349 1349 HOH HOH A . Q 9 HOH 349 1350 1350 HOH HOH A . Q 9 HOH 350 1351 1351 HOH HOH A . Q 9 HOH 351 1352 1352 HOH HOH A . Q 9 HOH 352 1353 1353 HOH HOH A . Q 9 HOH 353 1354 1354 HOH HOH A . Q 9 HOH 354 1355 1355 HOH HOH A . Q 9 HOH 355 1357 1357 HOH HOH A . Q 9 HOH 356 1359 1359 HOH HOH A . Q 9 HOH 357 1360 1360 HOH HOH A . Q 9 HOH 358 1361 1361 HOH HOH A . Q 9 HOH 359 1362 1362 HOH HOH A . Q 9 HOH 360 1363 1363 HOH HOH A . Q 9 HOH 361 1364 1364 HOH HOH A . Q 9 HOH 362 1365 1365 HOH HOH A . Q 9 HOH 363 1366 1366 HOH HOH A . Q 9 HOH 364 1367 1367 HOH HOH A . Q 9 HOH 365 1368 1368 HOH HOH A . Q 9 HOH 366 1369 1369 HOH HOH A . Q 9 HOH 367 1370 1370 HOH HOH A . Q 9 HOH 368 1371 1371 HOH HOH A . Q 9 HOH 369 1372 1372 HOH HOH A . Q 9 HOH 370 1373 1373 HOH HOH A . Q 9 HOH 371 1375 1375 HOH HOH A . Q 9 HOH 372 1376 1376 HOH HOH A . Q 9 HOH 373 1377 1377 HOH HOH A . Q 9 HOH 374 1378 1378 HOH HOH A . Q 9 HOH 375 1379 1379 HOH HOH A . Q 9 HOH 376 1380 1380 HOH HOH A . Q 9 HOH 377 1381 1381 HOH HOH A . Q 9 HOH 378 1382 1382 HOH HOH A . Q 9 HOH 379 1383 1383 HOH HOH A . Q 9 HOH 380 1384 1384 HOH HOH A . Q 9 HOH 381 1385 1385 HOH HOH A . Q 9 HOH 382 1386 1386 HOH HOH A . Q 9 HOH 383 1387 1387 HOH HOH A . Q 9 HOH 384 1388 1388 HOH HOH A . Q 9 HOH 385 1389 1389 HOH HOH A . Q 9 HOH 386 1390 1390 HOH HOH A . Q 9 HOH 387 1392 1392 HOH HOH A . Q 9 HOH 388 1393 1393 HOH HOH A . Q 9 HOH 389 1394 1394 HOH HOH A . Q 9 HOH 390 1395 1395 HOH HOH A . Q 9 HOH 391 1396 1396 HOH HOH A . Q 9 HOH 392 1397 1397 HOH HOH A . Q 9 HOH 393 1398 1398 HOH HOH A . Q 9 HOH 394 1399 1399 HOH HOH A . Q 9 HOH 395 1400 1400 HOH HOH A . Q 9 HOH 396 1401 1401 HOH HOH A . Q 9 HOH 397 1402 1402 HOH HOH A . Q 9 HOH 398 1403 1403 HOH HOH A . Q 9 HOH 399 1404 1404 HOH HOH A . Q 9 HOH 400 1405 1405 HOH HOH A . Q 9 HOH 401 1406 1406 HOH HOH A . Q 9 HOH 402 1407 1407 HOH HOH A . Q 9 HOH 403 1408 1408 HOH HOH A . Q 9 HOH 404 1409 1409 HOH HOH A . Q 9 HOH 405 1410 1410 HOH HOH A . Q 9 HOH 406 1411 1411 HOH HOH A . Q 9 HOH 407 1412 1412 HOH HOH A . Q 9 HOH 408 1413 1413 HOH HOH A . Q 9 HOH 409 1414 1414 HOH HOH A . Q 9 HOH 410 1415 1415 HOH HOH A . Q 9 HOH 411 1416 1416 HOH HOH A . Q 9 HOH 412 1417 1417 HOH HOH A . Q 9 HOH 413 1418 1418 HOH HOH A . Q 9 HOH 414 1419 1419 HOH HOH A . Q 9 HOH 415 1420 1420 HOH HOH A . Q 9 HOH 416 1421 1421 HOH HOH A . Q 9 HOH 417 1422 1422 HOH HOH A . Q 9 HOH 418 1423 1423 HOH HOH A . Q 9 HOH 419 1424 1424 HOH HOH A . Q 9 HOH 420 1425 1425 HOH HOH A . Q 9 HOH 421 1426 1426 HOH HOH A . Q 9 HOH 422 1427 1427 HOH HOH A . Q 9 HOH 423 1428 1428 HOH HOH A . Q 9 HOH 424 1429 1429 HOH HOH A . Q 9 HOH 425 1430 1430 HOH HOH A . Q 9 HOH 426 1431 1431 HOH HOH A . Q 9 HOH 427 1432 1432 HOH HOH A . Q 9 HOH 428 1433 1433 HOH HOH A . Q 9 HOH 429 1434 1434 HOH HOH A . Q 9 HOH 430 1435 1435 HOH HOH A . Q 9 HOH 431 1436 1436 HOH HOH A . Q 9 HOH 432 1437 1437 HOH HOH A . Q 9 HOH 433 1438 1438 HOH HOH A . Q 9 HOH 434 1439 1439 HOH HOH A . Q 9 HOH 435 1440 1440 HOH HOH A . Q 9 HOH 436 1441 1441 HOH HOH A . Q 9 HOH 437 1442 1442 HOH HOH A . Q 9 HOH 438 1443 1443 HOH HOH A . Q 9 HOH 439 1444 1444 HOH HOH A . Q 9 HOH 440 1445 1445 HOH HOH A . Q 9 HOH 441 1446 1446 HOH HOH A . Q 9 HOH 442 1447 1447 HOH HOH A . Q 9 HOH 443 1448 1448 HOH HOH A . Q 9 HOH 444 1449 1449 HOH HOH A . Q 9 HOH 445 1450 1450 HOH HOH A . Q 9 HOH 446 1451 1451 HOH HOH A . Q 9 HOH 447 1452 1452 HOH HOH A . Q 9 HOH 448 1454 1454 HOH HOH A . Q 9 HOH 449 1455 1455 HOH HOH A . Q 9 HOH 450 1456 1456 HOH HOH A . Q 9 HOH 451 1457 1457 HOH HOH A . Q 9 HOH 452 1458 1458 HOH HOH A . Q 9 HOH 453 1459 1459 HOH HOH A . Q 9 HOH 454 1460 1460 HOH HOH A . Q 9 HOH 455 1461 1461 HOH HOH A . Q 9 HOH 456 1462 1462 HOH HOH A . Q 9 HOH 457 1463 1463 HOH HOH A . Q 9 HOH 458 1464 1464 HOH HOH A . Q 9 HOH 459 1465 1465 HOH HOH A . Q 9 HOH 460 1466 1466 HOH HOH A . Q 9 HOH 461 1467 1467 HOH HOH A . Q 9 HOH 462 1468 1468 HOH HOH A . Q 9 HOH 463 1469 1469 HOH HOH A . Q 9 HOH 464 1470 1470 HOH HOH A . Q 9 HOH 465 1471 1471 HOH HOH A . Q 9 HOH 466 1472 1472 HOH HOH A . Q 9 HOH 467 1474 1474 HOH HOH A . Q 9 HOH 468 1475 1475 HOH HOH A . Q 9 HOH 469 1476 1476 HOH HOH A . Q 9 HOH 470 1477 1477 HOH HOH A . Q 9 HOH 471 1478 1478 HOH HOH A . Q 9 HOH 472 1479 1479 HOH HOH A . Q 9 HOH 473 1480 1480 HOH HOH A . Q 9 HOH 474 1481 1481 HOH HOH A . Q 9 HOH 475 1482 1482 HOH HOH A . Q 9 HOH 476 1483 1483 HOH HOH A . Q 9 HOH 477 1484 1484 HOH HOH A . Q 9 HOH 478 1485 1485 HOH HOH A . Q 9 HOH 479 1486 1486 HOH HOH A . Q 9 HOH 480 1487 1487 HOH HOH A . Q 9 HOH 481 1488 1488 HOH HOH A . Q 9 HOH 482 1489 1489 HOH HOH A . Q 9 HOH 483 1490 1490 HOH HOH A . Q 9 HOH 484 1491 1491 HOH HOH A . Q 9 HOH 485 1492 1492 HOH HOH A . Q 9 HOH 486 1493 1493 HOH HOH A . Q 9 HOH 487 1494 1494 HOH HOH A . Q 9 HOH 488 1495 1495 HOH HOH A . Q 9 HOH 489 1496 1496 HOH HOH A . Q 9 HOH 490 1497 1497 HOH HOH A . Q 9 HOH 491 1498 1498 HOH HOH A . Q 9 HOH 492 1499 1499 HOH HOH A . Q 9 HOH 493 1500 1500 HOH HOH A . Q 9 HOH 494 1501 1501 HOH HOH A . Q 9 HOH 495 1502 1502 HOH HOH A . Q 9 HOH 496 1503 1503 HOH HOH A . Q 9 HOH 497 1504 1504 HOH HOH A . Q 9 HOH 498 1505 1505 HOH HOH A . Q 9 HOH 499 1506 1506 HOH HOH A . Q 9 HOH 500 1507 1507 HOH HOH A . Q 9 HOH 501 1508 1508 HOH HOH A . Q 9 HOH 502 1509 1509 HOH HOH A . Q 9 HOH 503 1510 1510 HOH HOH A . Q 9 HOH 504 1511 1511 HOH HOH A . Q 9 HOH 505 1512 1512 HOH HOH A . Q 9 HOH 506 1513 1513 HOH HOH A . Q 9 HOH 507 1514 1514 HOH HOH A . Q 9 HOH 508 1515 1515 HOH HOH A . Q 9 HOH 509 1516 1516 HOH HOH A . Q 9 HOH 510 1517 1517 HOH HOH A . Q 9 HOH 511 1518 1518 HOH HOH A . Q 9 HOH 512 1519 1519 HOH HOH A . Q 9 HOH 513 1520 1520 HOH HOH A . Q 9 HOH 514 1521 1521 HOH HOH A . Q 9 HOH 515 1523 1523 HOH HOH A . Q 9 HOH 516 1524 1524 HOH HOH A . Q 9 HOH 517 1525 1525 HOH HOH A . Q 9 HOH 518 1526 1526 HOH HOH A . Q 9 HOH 519 1527 1527 HOH HOH A . Q 9 HOH 520 1528 1528 HOH HOH A . Q 9 HOH 521 1529 1529 HOH HOH A . Q 9 HOH 522 1530 1530 HOH HOH A . Q 9 HOH 523 1532 1532 HOH HOH A . Q 9 HOH 524 1534 1534 HOH HOH A . Q 9 HOH 525 1535 1535 HOH HOH A . Q 9 HOH 526 1536 1536 HOH HOH A . Q 9 HOH 527 1537 1537 HOH HOH A . Q 9 HOH 528 1538 1538 HOH HOH A . Q 9 HOH 529 1539 1539 HOH HOH A . Q 9 HOH 530 1540 1540 HOH HOH A . Q 9 HOH 531 1541 1541 HOH HOH A . Q 9 HOH 532 1542 1542 HOH HOH A . Q 9 HOH 533 1543 1543 HOH HOH A . Q 9 HOH 534 1544 1544 HOH HOH A . Q 9 HOH 535 1545 1545 HOH HOH A . Q 9 HOH 536 1546 1546 HOH HOH A . Q 9 HOH 537 1547 1547 HOH HOH A . Q 9 HOH 538 1548 1548 HOH HOH A . Q 9 HOH 539 1549 1549 HOH HOH A . Q 9 HOH 540 1550 1550 HOH HOH A . Q 9 HOH 541 1552 1552 HOH HOH A . Q 9 HOH 542 1553 1553 HOH HOH A . Q 9 HOH 543 1554 1554 HOH HOH A . Q 9 HOH 544 1555 1555 HOH HOH A . Q 9 HOH 545 1556 1556 HOH HOH A . Q 9 HOH 546 1557 1557 HOH HOH A . Q 9 HOH 547 1558 1558 HOH HOH A . Q 9 HOH 548 1559 1559 HOH HOH A . Q 9 HOH 549 1560 1560 HOH HOH A . Q 9 HOH 550 1561 1561 HOH HOH A . Q 9 HOH 551 1562 1562 HOH HOH A . Q 9 HOH 552 1563 1563 HOH HOH A . Q 9 HOH 553 1564 1564 HOH HOH A . Q 9 HOH 554 1565 1565 HOH HOH A . Q 9 HOH 555 1566 1566 HOH HOH A . Q 9 HOH 556 1567 1567 HOH HOH A . Q 9 HOH 557 1568 1568 HOH HOH A . Q 9 HOH 558 1569 1569 HOH HOH A . Q 9 HOH 559 1570 1570 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 122 A ASN 122 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 249 A ASN 249 ? ASN 'GLYCOSYLATION SITE' 3 A SEP 92 A SEP 92 ? SER PHOSPHOSERINE # _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 dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 12330 ? 1 MORE -117 ? 1 'SSA (A^2)' 31930 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 3_655 -x+1,y,-z+1/2 -1.0000000000 0.0000000000 0.0000000000 87.7910000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 53.1705000000 # _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 1566 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id Q _pdbx_struct_special_symmetry.label_comp_id HOH _pdbx_struct_special_symmetry.label_seq_id . # loop_ _pdbx_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 42 ? A ASP 42 ? 1_555 ZN ? I ZN . ? A ZN 902 ? 1_555 OG ? A SEP 92 ? A SEP 92 ? 1_555 119.1 ? 2 OD1 ? A ASP 42 ? A ASP 42 ? 1_555 ZN ? I ZN . ? A ZN 902 ? 1_555 NE2 ? A HIS 358 ? A HIS 358 ? 1_555 119.4 ? 3 OG ? A SEP 92 ? A SEP 92 ? 1_555 ZN ? I ZN . ? A ZN 902 ? 1_555 NE2 ? A HIS 358 ? A HIS 358 ? 1_555 121.3 ? 4 OD1 ? A ASP 42 ? A ASP 42 ? 1_555 ZN ? I ZN . ? A ZN 902 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 96.2 ? 5 OG ? A SEP 92 ? A SEP 92 ? 1_555 ZN ? I ZN . ? A ZN 902 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 83.6 ? 6 NE2 ? A HIS 358 ? A HIS 358 ? 1_555 ZN ? I ZN . ? A ZN 902 ? 1_555 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 95.8 ? 7 OD1 ? A ASP 42 ? A ASP 42 ? 1_555 ZN ? I ZN . ? A ZN 902 ? 1_555 O3P ? A SEP 92 ? A SEP 92 ? 1_555 97.8 ? 8 OG ? A SEP 92 ? A SEP 92 ? 1_555 ZN ? I ZN . ? A ZN 902 ? 1_555 O3P ? A SEP 92 ? A SEP 92 ? 1_555 68.8 ? 9 NE2 ? A HIS 358 ? A HIS 358 ? 1_555 ZN ? I ZN . ? A ZN 902 ? 1_555 O3P ? A SEP 92 ? A SEP 92 ? 1_555 97.8 ? 10 OD2 ? A ASP 357 ? A ASP 357 ? 1_555 ZN ? I ZN . ? A ZN 902 ? 1_555 O3P ? A SEP 92 ? A SEP 92 ? 1_555 152.4 ? 11 OD2 ? A ASP 42 ? A ASP 42 ? 1_555 MG ? J MG . ? A MG 903 ? 1_555 OE2 ? A GLU 311 ? A GLU 311 ? 1_555 97.9 ? 12 OD2 ? A ASP 42 ? A ASP 42 ? 1_555 MG ? J MG . ? A MG 903 ? 1_555 O ? Q HOH . ? A HOH 1034 ? 1_555 175.6 ? 13 OE2 ? A GLU 311 ? A GLU 311 ? 1_555 MG ? J MG . ? A MG 903 ? 1_555 O ? Q HOH . ? A HOH 1034 ? 1_555 86.5 ? 14 OD2 ? A ASP 42 ? A ASP 42 ? 1_555 MG ? J MG . ? A MG 903 ? 1_555 O ? Q HOH . ? A HOH 1053 ? 1_555 97.1 ? 15 OE2 ? A GLU 311 ? A GLU 311 ? 1_555 MG ? J MG . ? A MG 903 ? 1_555 O ? Q HOH . ? A HOH 1053 ? 1_555 163.7 ? 16 O ? Q HOH . ? A HOH 1034 ? 1_555 MG ? J MG . ? A MG 903 ? 1_555 O ? Q HOH . ? A HOH 1053 ? 1_555 78.5 ? 17 OD2 ? A ASP 42 ? A ASP 42 ? 1_555 MG ? J MG . ? A MG 903 ? 1_555 O ? Q HOH . ? A HOH 1003 ? 1_555 87.0 ? 18 OE2 ? A GLU 311 ? A GLU 311 ? 1_555 MG ? J MG . ? A MG 903 ? 1_555 O ? Q HOH . ? A HOH 1003 ? 1_555 98.2 ? 19 O ? Q HOH . ? A HOH 1034 ? 1_555 MG ? J MG . ? A MG 903 ? 1_555 O ? Q HOH . ? A HOH 1003 ? 1_555 92.4 ? 20 O ? Q HOH . ? A HOH 1053 ? 1_555 MG ? J MG . ? A MG 903 ? 1_555 O ? Q HOH . ? A HOH 1003 ? 1_555 89.0 ? 21 OD2 ? A ASP 42 ? A ASP 42 ? 1_555 MG ? J MG . ? A MG 903 ? 1_555 OG ? A SER 155 ? A SER 155 ? 1_555 87.7 ? 22 OE2 ? A GLU 311 ? A GLU 311 ? 1_555 MG ? J MG . ? A MG 903 ? 1_555 OG ? A SER 155 ? A SER 155 ? 1_555 87.7 ? 23 O ? Q HOH . ? A HOH 1034 ? 1_555 MG ? J MG . ? A MG 903 ? 1_555 OG ? A SER 155 ? A SER 155 ? 1_555 92.5 ? 24 O ? Q HOH . ? A HOH 1053 ? 1_555 MG ? J MG . ? A MG 903 ? 1_555 OG ? A SER 155 ? A SER 155 ? 1_555 86.4 ? 25 O ? Q HOH . ? A HOH 1003 ? 1_555 MG ? J MG . ? A MG 903 ? 1_555 OG ? A SER 155 ? A SER 155 ? 1_555 172.5 ? 26 NE2 ? A HIS 432 ? A HIS 432 ? 1_555 ZN ? H ZN . ? A ZN 901 ? 1_555 OD1 ? A ASP 316 ? A ASP 316 ? 1_555 150.4 ? 27 NE2 ? A HIS 432 ? A HIS 432 ? 1_555 ZN ? H ZN . ? A ZN 901 ? 1_555 NE2 ? A HIS 320 ? A HIS 320 ? 1_555 99.6 ? 28 OD1 ? A ASP 316 ? A ASP 316 ? 1_555 ZN ? H ZN . ? A ZN 901 ? 1_555 NE2 ? A HIS 320 ? A HIS 320 ? 1_555 91.8 ? 29 NE2 ? A HIS 432 ? A HIS 432 ? 1_555 ZN ? H ZN . ? A ZN 901 ? 1_555 O3P ? A SEP 92 ? A SEP 92 ? 1_555 87.4 ? 30 OD1 ? A ASP 316 ? A ASP 316 ? 1_555 ZN ? H ZN . ? A ZN 901 ? 1_555 O3P ? A SEP 92 ? A SEP 92 ? 1_555 80.7 ? 31 NE2 ? A HIS 320 ? A HIS 320 ? 1_555 ZN ? H ZN . ? A ZN 901 ? 1_555 O3P ? A SEP 92 ? A SEP 92 ? 1_555 172.5 ? 32 NE2 ? A HIS 432 ? A HIS 432 ? 1_555 ZN ? H ZN . ? A ZN 901 ? 1_555 N A B PHE . ? A PHE 912 ? 1_555 98.5 ? 33 OD1 ? A ASP 316 ? A ASP 316 ? 1_555 ZN ? H ZN . ? A ZN 901 ? 1_555 N A B PHE . ? A PHE 912 ? 1_555 107.1 ? 34 NE2 ? A HIS 320 ? A HIS 320 ? 1_555 ZN ? H ZN . ? A ZN 901 ? 1_555 N A B PHE . ? A PHE 912 ? 1_555 97.3 ? 35 O3P ? A SEP 92 ? A SEP 92 ? 1_555 ZN ? H ZN . ? A ZN 901 ? 1_555 N A B PHE . ? A PHE 912 ? 1_555 84.4 ? 36 NE2 ? A HIS 432 ? A HIS 432 ? 1_555 ZN ? H ZN . ? A ZN 901 ? 1_555 OD2 ? A ASP 316 ? A ASP 316 ? 1_555 93.5 ? 37 OD1 ? A ASP 316 ? A ASP 316 ? 1_555 ZN ? H ZN . ? A ZN 901 ? 1_555 OD2 ? A ASP 316 ? A ASP 316 ? 1_555 58.4 ? 38 NE2 ? A HIS 320 ? A HIS 320 ? 1_555 ZN ? H ZN . ? A ZN 901 ? 1_555 OD2 ? A ASP 316 ? A ASP 316 ? 1_555 93.3 ? 39 O3P ? A SEP 92 ? A SEP 92 ? 1_555 ZN ? H ZN . ? A ZN 901 ? 1_555 OD2 ? A ASP 316 ? A ASP 316 ? 1_555 83.4 ? 40 N A B PHE . ? A PHE 912 ? 1_555 ZN ? H ZN . ? A ZN 901 ? 1_555 OD2 ? A ASP 316 ? A ASP 316 ? 1_555 162.4 ? 41 OE2 ? A GLU 270 ? A GLU 270 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 O ? A PHE 269 ? A PHE 269 ? 1_555 85.0 ? 42 OE2 ? A GLU 270 ? A GLU 270 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OD2 ? A ASP 285 ? A ASP 285 ? 1_555 95.9 ? 43 O ? A PHE 269 ? A PHE 269 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OD2 ? A ASP 285 ? A ASP 285 ? 1_555 130.8 ? 44 OE2 ? A GLU 270 ? A GLU 270 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OE1 ? A GLU 216 ? A GLU 216 ? 1_555 96.8 ? 45 O ? A PHE 269 ? A PHE 269 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OE1 ? A GLU 216 ? A GLU 216 ? 1_555 83.8 ? 46 OD2 ? A ASP 285 ? A ASP 285 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OE1 ? A GLU 216 ? A GLU 216 ? 1_555 144.0 ? 47 OE2 ? A GLU 270 ? A GLU 270 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 O ? Q HOH . ? A HOH 1246 ? 1_555 170.9 ? 48 O ? A PHE 269 ? A PHE 269 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 O ? Q HOH . ? A HOH 1246 ? 1_555 86.2 ? 49 OD2 ? A ASP 285 ? A ASP 285 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 O ? Q HOH . ? A HOH 1246 ? 1_555 87.9 ? 50 OE1 ? A GLU 216 ? A GLU 216 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 O ? Q HOH . ? A HOH 1246 ? 1_555 84.7 ? 51 OE2 ? A GLU 270 ? A GLU 270 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OE2 ? A GLU 216 ? A GLU 216 ? 1_555 96.0 ? 52 O ? A PHE 269 ? A PHE 269 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OE2 ? A GLU 216 ? A GLU 216 ? 1_555 138.6 ? 53 OD2 ? A ASP 285 ? A ASP 285 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OE2 ? A GLU 216 ? A GLU 216 ? 1_555 90.4 ? 54 OE1 ? A GLU 216 ? A GLU 216 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OE2 ? A GLU 216 ? A GLU 216 ? 1_555 54.9 ? 55 O ? Q HOH . ? A HOH 1246 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OE2 ? A GLU 216 ? A GLU 216 ? 1_555 92.2 ? 56 OE2 ? A GLU 270 ? A GLU 270 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OD1 ? A ASP 285 ? A ASP 285 ? 1_555 85.1 ? 57 O ? A PHE 269 ? A PHE 269 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OD1 ? A ASP 285 ? A ASP 285 ? 1_555 78.1 ? 58 OD2 ? A ASP 285 ? A ASP 285 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OD1 ? A ASP 285 ? A ASP 285 ? 1_555 53.2 ? 59 OE1 ? A GLU 216 ? A GLU 216 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OD1 ? A ASP 285 ? A ASP 285 ? 1_555 161.5 ? 60 O ? Q HOH . ? A HOH 1246 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OD1 ? A ASP 285 ? A ASP 285 ? 1_555 90.5 ? 61 OE2 ? A GLU 216 ? A GLU 216 ? 1_555 CA ? K CA . ? A CA 904 ? 1_555 OD1 ? A ASP 285 ? A ASP 285 ? 1_555 143.3 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2011-01-19 2 'Structure model' 1 1 2011-07-13 3 'Structure model' 1 2 2011-10-05 # _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' 'Version format compliance' 2 3 'Structure model' 'Database references' # _software.name REFMAC _software.classification refinement _software.version 5.2.0019 _software.citation_id ? _software.pdbx_ordinal 1 # _pdbx_database_remark.id 0 _pdbx_database_remark.text ;THIS ENTRY 3MK2 REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA R1ZEFSF DETERMINED BY AUTHORS OF THE PDB ENTRY 1ZEF: P.LLINAS,E.A.STURA,A.MENEZ,Z.KISS,T.STIGBRAND,J.L.MILLAN,M.H.LE DU ; # _pdbx_validate_close_contact.id 1 _pdbx_validate_close_contact.PDB_model_num 1 _pdbx_validate_close_contact.auth_atom_id_1 O _pdbx_validate_close_contact.auth_asym_id_1 A _pdbx_validate_close_contact.auth_comp_id_1 HOH _pdbx_validate_close_contact.auth_seq_id_1 1318 _pdbx_validate_close_contact.PDB_ins_code_1 ? _pdbx_validate_close_contact.label_alt_id_1 ? _pdbx_validate_close_contact.auth_atom_id_2 O _pdbx_validate_close_contact.auth_asym_id_2 A _pdbx_validate_close_contact.auth_comp_id_2 HOH _pdbx_validate_close_contact.auth_seq_id_2 1554 _pdbx_validate_close_contact.PDB_ins_code_2 ? _pdbx_validate_close_contact.label_alt_id_2 ? _pdbx_validate_close_contact.dist 2.16 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 O _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 HOH _pdbx_validate_symm_contact.auth_seq_id_1 1078 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 HOH _pdbx_validate_symm_contact.auth_seq_id_2 1561 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 3_655 _pdbx_validate_symm_contact.dist 2.15 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 PHE A 107 ? ? -30.92 123.48 2 1 SER A 359 ? ? -105.40 -163.40 3 1 VAL A 361 ? ? -82.81 42.88 4 1 ALA A 473 ? ? -94.14 46.83 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A THR 482 ? A THR 482 2 1 Y 1 A THR 483 ? A THR 483 3 1 Y 1 A ASP 484 ? A ASP 484 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 PHENYLALANINE PHE 3 N-ACETYL-D-GLUCOSAMINE NAG 4 'ZINC ION' ZN 5 'MAGNESIUM ION' MG 6 'CALCIUM ION' CA 7 'ACETATE ION' ACT 8 GLYCEROL GOL 9 water HOH #