data_2GUY # _entry.id 2GUY # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.286 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 2GUY RCSB RCSB037580 WWPDB D_1000037580 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 7TAA 'Crystal structure of family 13 alpha amylase from Aspergillus oryzae in complex with acarbose' unspecified PDB 6TAA 'Crystal structure of the same protein in a different crystal form' unspecified PDB 2TAA 'Crystal structure of the same protein in a different crystal form' unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 2GUY _pdbx_database_status.recvd_initial_deposition_date 2006-05-02 _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.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # _audit_author.name 'Vujicic Zagar, A.' _audit_author.pdbx_ordinal 1 # _citation.id primary _citation.title 'Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with maltose at 1.8 angstroms resolution.' _citation.journal_abbrev 'Acta Crystallogr.,Sect.F' _citation.journal_volume 62 _citation.page_first 716 _citation.page_last 721 _citation.year 2006 _citation.journal_id_ASTM ? _citation.country DK _citation.journal_id_ISSN 1744-3091 _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 16880540 _citation.pdbx_database_id_DOI 10.1107/S1744309106024729 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Vujicic-Zagar, A.' 1 primary 'Dijkstra, B.W.' 2 # _cell.entry_id 2GUY _cell.length_a 102.799 _cell.length_b 63.228 _cell.length_c 74.456 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 2GUY _symmetry.space_group_name_H-M 'P 21 21 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 18 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat 'Alpha-amylase A' 52525.973 1 3.2.1.1 ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 4 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 5 water nat water 18.015 564 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'Taka-amylase A, TAA, 1,4- alpha-D-glucan glucanohydrolase' # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;ATPADWRSQSIYFLLTDRFARTDGSTTATCNTADQKYCGGTWQGIIDKLDYIQGMGFTAIWITPVTAQLPQTTAYGDAYH GYWQQDIYSLNENYGTADDLKALSSALHERGMYLMVDVVANHMGYDGAGSSVDYSVFKPFSSQDYFHPFCFIQNYEDQTQ VEDCWLGDNTVSLPDLDTTKDVVKNEWYDWVGSLVSNYSIDGLRIDTVKHVQKDFWPGYNKAAGVYCIGEVLDGDPAYTC PYQNVMDGVLNYPIYYPLLNAFKSTSGSMDDLYNMINTVKSDCPDSTLLGTFVENHDNPRFASYTNDIALAKNVAAFIIL NDGIPIIYAGQEQHYAGGNDPANREATWLSGYPTDSELYKLIASANAIRNYAISKDTGFVTYKNWPIYKDDTTIAMRKGT DGSQIVTILSNKGASGDSYTLSLSGAGYTAGQQLTEVIGCTTVTVGSDGNVPVPMAGGLPRVLYPTEKLAGSKICSSS ; _entity_poly.pdbx_seq_one_letter_code_can ;ATPADWRSQSIYFLLTDRFARTDGSTTATCNTADQKYCGGTWQGIIDKLDYIQGMGFTAIWITPVTAQLPQTTAYGDAYH GYWQQDIYSLNENYGTADDLKALSSALHERGMYLMVDVVANHMGYDGAGSSVDYSVFKPFSSQDYFHPFCFIQNYEDQTQ VEDCWLGDNTVSLPDLDTTKDVVKNEWYDWVGSLVSNYSIDGLRIDTVKHVQKDFWPGYNKAAGVYCIGEVLDGDPAYTC PYQNVMDGVLNYPIYYPLLNAFKSTSGSMDDLYNMINTVKSDCPDSTLLGTFVENHDNPRFASYTNDIALAKNVAAFIIL NDGIPIIYAGQEQHYAGGNDPANREATWLSGYPTDSELYKLIASANAIRNYAISKDTGFVTYKNWPIYKDDTTIAMRKGT DGSQIVTILSNKGASGDSYTLSLSGAGYTAGQQLTEVIGCTTVTVGSDGNVPVPMAGGLPRVLYPTEKLAGSKICSSS ; _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 ALA n 1 2 THR n 1 3 PRO n 1 4 ALA n 1 5 ASP n 1 6 TRP n 1 7 ARG n 1 8 SER n 1 9 GLN n 1 10 SER n 1 11 ILE n 1 12 TYR n 1 13 PHE n 1 14 LEU n 1 15 LEU n 1 16 THR n 1 17 ASP n 1 18 ARG n 1 19 PHE n 1 20 ALA n 1 21 ARG n 1 22 THR n 1 23 ASP n 1 24 GLY n 1 25 SER n 1 26 THR n 1 27 THR n 1 28 ALA n 1 29 THR n 1 30 CYS n 1 31 ASN n 1 32 THR n 1 33 ALA n 1 34 ASP n 1 35 GLN n 1 36 LYS n 1 37 TYR n 1 38 CYS n 1 39 GLY n 1 40 GLY n 1 41 THR n 1 42 TRP n 1 43 GLN n 1 44 GLY n 1 45 ILE n 1 46 ILE n 1 47 ASP n 1 48 LYS n 1 49 LEU n 1 50 ASP n 1 51 TYR n 1 52 ILE n 1 53 GLN n 1 54 GLY n 1 55 MET n 1 56 GLY n 1 57 PHE n 1 58 THR n 1 59 ALA n 1 60 ILE n 1 61 TRP n 1 62 ILE n 1 63 THR n 1 64 PRO n 1 65 VAL n 1 66 THR n 1 67 ALA n 1 68 GLN n 1 69 LEU n 1 70 PRO n 1 71 GLN n 1 72 THR n 1 73 THR n 1 74 ALA n 1 75 TYR n 1 76 GLY n 1 77 ASP n 1 78 ALA n 1 79 TYR n 1 80 HIS n 1 81 GLY n 1 82 TYR n 1 83 TRP n 1 84 GLN n 1 85 GLN n 1 86 ASP n 1 87 ILE n 1 88 TYR n 1 89 SER n 1 90 LEU n 1 91 ASN n 1 92 GLU n 1 93 ASN n 1 94 TYR n 1 95 GLY n 1 96 THR n 1 97 ALA n 1 98 ASP n 1 99 ASP n 1 100 LEU n 1 101 LYS n 1 102 ALA n 1 103 LEU n 1 104 SER n 1 105 SER n 1 106 ALA n 1 107 LEU n 1 108 HIS n 1 109 GLU n 1 110 ARG n 1 111 GLY n 1 112 MET n 1 113 TYR n 1 114 LEU n 1 115 MET n 1 116 VAL n 1 117 ASP n 1 118 VAL n 1 119 VAL n 1 120 ALA n 1 121 ASN n 1 122 HIS n 1 123 MET n 1 124 GLY n 1 125 TYR n 1 126 ASP n 1 127 GLY n 1 128 ALA n 1 129 GLY n 1 130 SER n 1 131 SER n 1 132 VAL n 1 133 ASP n 1 134 TYR n 1 135 SER n 1 136 VAL n 1 137 PHE n 1 138 LYS n 1 139 PRO n 1 140 PHE n 1 141 SER n 1 142 SER n 1 143 GLN n 1 144 ASP n 1 145 TYR n 1 146 PHE n 1 147 HIS n 1 148 PRO n 1 149 PHE n 1 150 CYS n 1 151 PHE n 1 152 ILE n 1 153 GLN n 1 154 ASN n 1 155 TYR n 1 156 GLU n 1 157 ASP n 1 158 GLN n 1 159 THR n 1 160 GLN n 1 161 VAL n 1 162 GLU n 1 163 ASP n 1 164 CYS n 1 165 TRP n 1 166 LEU n 1 167 GLY n 1 168 ASP n 1 169 ASN n 1 170 THR n 1 171 VAL n 1 172 SER n 1 173 LEU n 1 174 PRO n 1 175 ASP n 1 176 LEU n 1 177 ASP n 1 178 THR n 1 179 THR n 1 180 LYS n 1 181 ASP n 1 182 VAL n 1 183 VAL n 1 184 LYS n 1 185 ASN n 1 186 GLU n 1 187 TRP n 1 188 TYR n 1 189 ASP n 1 190 TRP n 1 191 VAL n 1 192 GLY n 1 193 SER n 1 194 LEU n 1 195 VAL n 1 196 SER n 1 197 ASN n 1 198 TYR n 1 199 SER n 1 200 ILE n 1 201 ASP n 1 202 GLY n 1 203 LEU n 1 204 ARG n 1 205 ILE n 1 206 ASP n 1 207 THR n 1 208 VAL n 1 209 LYS n 1 210 HIS n 1 211 VAL n 1 212 GLN n 1 213 LYS n 1 214 ASP n 1 215 PHE n 1 216 TRP n 1 217 PRO n 1 218 GLY n 1 219 TYR n 1 220 ASN n 1 221 LYS n 1 222 ALA n 1 223 ALA n 1 224 GLY n 1 225 VAL n 1 226 TYR n 1 227 CYS n 1 228 ILE n 1 229 GLY n 1 230 GLU n 1 231 VAL n 1 232 LEU n 1 233 ASP n 1 234 GLY n 1 235 ASP n 1 236 PRO n 1 237 ALA n 1 238 TYR n 1 239 THR n 1 240 CYS n 1 241 PRO n 1 242 TYR n 1 243 GLN n 1 244 ASN n 1 245 VAL n 1 246 MET n 1 247 ASP n 1 248 GLY n 1 249 VAL n 1 250 LEU n 1 251 ASN n 1 252 TYR n 1 253 PRO n 1 254 ILE n 1 255 TYR n 1 256 TYR n 1 257 PRO n 1 258 LEU n 1 259 LEU n 1 260 ASN n 1 261 ALA n 1 262 PHE n 1 263 LYS n 1 264 SER n 1 265 THR n 1 266 SER n 1 267 GLY n 1 268 SER n 1 269 MET n 1 270 ASP n 1 271 ASP n 1 272 LEU n 1 273 TYR n 1 274 ASN n 1 275 MET n 1 276 ILE n 1 277 ASN n 1 278 THR n 1 279 VAL n 1 280 LYS n 1 281 SER n 1 282 ASP n 1 283 CYS n 1 284 PRO n 1 285 ASP n 1 286 SER n 1 287 THR n 1 288 LEU n 1 289 LEU n 1 290 GLY n 1 291 THR n 1 292 PHE n 1 293 VAL n 1 294 GLU n 1 295 ASN n 1 296 HIS n 1 297 ASP n 1 298 ASN n 1 299 PRO n 1 300 ARG n 1 301 PHE n 1 302 ALA n 1 303 SER n 1 304 TYR n 1 305 THR n 1 306 ASN n 1 307 ASP n 1 308 ILE n 1 309 ALA n 1 310 LEU n 1 311 ALA n 1 312 LYS n 1 313 ASN n 1 314 VAL n 1 315 ALA n 1 316 ALA n 1 317 PHE n 1 318 ILE n 1 319 ILE n 1 320 LEU n 1 321 ASN n 1 322 ASP n 1 323 GLY n 1 324 ILE n 1 325 PRO n 1 326 ILE n 1 327 ILE n 1 328 TYR n 1 329 ALA n 1 330 GLY n 1 331 GLN n 1 332 GLU n 1 333 GLN n 1 334 HIS n 1 335 TYR n 1 336 ALA n 1 337 GLY n 1 338 GLY n 1 339 ASN n 1 340 ASP n 1 341 PRO n 1 342 ALA n 1 343 ASN n 1 344 ARG n 1 345 GLU n 1 346 ALA n 1 347 THR n 1 348 TRP n 1 349 LEU n 1 350 SER n 1 351 GLY n 1 352 TYR n 1 353 PRO n 1 354 THR n 1 355 ASP n 1 356 SER n 1 357 GLU n 1 358 LEU n 1 359 TYR n 1 360 LYS n 1 361 LEU n 1 362 ILE n 1 363 ALA n 1 364 SER n 1 365 ALA n 1 366 ASN n 1 367 ALA n 1 368 ILE n 1 369 ARG n 1 370 ASN n 1 371 TYR n 1 372 ALA n 1 373 ILE n 1 374 SER n 1 375 LYS n 1 376 ASP n 1 377 THR n 1 378 GLY n 1 379 PHE n 1 380 VAL n 1 381 THR n 1 382 TYR n 1 383 LYS n 1 384 ASN n 1 385 TRP n 1 386 PRO n 1 387 ILE n 1 388 TYR n 1 389 LYS n 1 390 ASP n 1 391 ASP n 1 392 THR n 1 393 THR n 1 394 ILE n 1 395 ALA n 1 396 MET n 1 397 ARG n 1 398 LYS n 1 399 GLY n 1 400 THR n 1 401 ASP n 1 402 GLY n 1 403 SER n 1 404 GLN n 1 405 ILE n 1 406 VAL n 1 407 THR n 1 408 ILE n 1 409 LEU n 1 410 SER n 1 411 ASN n 1 412 LYS n 1 413 GLY n 1 414 ALA n 1 415 SER n 1 416 GLY n 1 417 ASP n 1 418 SER n 1 419 TYR n 1 420 THR n 1 421 LEU n 1 422 SER n 1 423 LEU n 1 424 SER n 1 425 GLY n 1 426 ALA n 1 427 GLY n 1 428 TYR n 1 429 THR n 1 430 ALA n 1 431 GLY n 1 432 GLN n 1 433 GLN n 1 434 LEU n 1 435 THR n 1 436 GLU n 1 437 VAL n 1 438 ILE n 1 439 GLY n 1 440 CYS n 1 441 THR n 1 442 THR n 1 443 VAL n 1 444 THR n 1 445 VAL n 1 446 GLY n 1 447 SER n 1 448 ASP n 1 449 GLY n 1 450 ASN n 1 451 VAL n 1 452 PRO n 1 453 VAL n 1 454 PRO n 1 455 MET n 1 456 ALA n 1 457 GLY n 1 458 GLY n 1 459 LEU n 1 460 PRO n 1 461 ARG n 1 462 VAL n 1 463 LEU n 1 464 TYR n 1 465 PRO n 1 466 THR n 1 467 GLU n 1 468 LYS n 1 469 LEU n 1 470 ALA n 1 471 GLY n 1 472 SER n 1 473 LYS n 1 474 ILE n 1 475 CYS n 1 476 SER n 1 477 SER n 1 478 SER 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 ? _entity_src_nat.pdbx_organism_scientific 'Aspergillus oryzae' _entity_src_nat.pdbx_ncbi_taxonomy_id 5062 _entity_src_nat.genus Aspergillus _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 AMYA1_ASPOR _struct_ref.pdbx_db_accession P0C1B3 _struct_ref.entity_id 1 _struct_ref.pdbx_align_begin 22 _struct_ref.pdbx_db_isoform ? _struct_ref.pdbx_seq_one_letter_code ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 2GUY _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 478 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P0C1B3 _struct_ref_seq.db_align_beg 22 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 499 _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 478 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 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 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 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 2GUY _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.30 _exptl_crystal.density_percent_sol 46.58 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 296 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 6.8 _exptl_crystal_grow.pdbx_details '30% PEG 8000, 0.2M Na-acetate, 0.1M Na-cacodylate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 296K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC QUANTUM 315' _diffrn_detector.pdbx_collection_date 2005-08-30 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'Si(111)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.91835 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID23-1' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID23-1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.91835 # _reflns.entry_id 2GUY _reflns.observed_criterion_sigma_I 0 _reflns.observed_criterion_sigma_F 0 _reflns.d_resolution_low 40 _reflns.d_resolution_high 1.59 _reflns.number_obs 65130 _reflns.number_all 65130 _reflns.percent_possible_obs 98.6 _reflns.pdbx_Rmerge_I_obs 0.079 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy ? _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.59 _reflns_shell.d_res_low 1.66 _reflns_shell.percent_possible_all 90.1 _reflns_shell.Rmerge_I_obs 0.556 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 2GUY _refine.ls_number_reflns_obs 60711 _refine.ls_number_reflns_all 60711 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 20.00 _refine.ls_d_res_high 1.59 _refine.ls_percent_reflns_obs 96.88 _refine.ls_R_factor_obs 0.16527 _refine.ls_R_factor_all 0.16527 _refine.ls_R_factor_R_work 0.16362 _refine.ls_R_factor_R_free 0.19623 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 3245 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.970 _refine.correlation_coeff_Fo_to_Fc_free 0.956 _refine.B_iso_mean 26.310 _refine.aniso_B[1][1] -0.79 _refine.aniso_B[2][2] 1.08 _refine.aniso_B[3][3] -0.29 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 'PDB ENTRY 7TAA' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.084 _refine.pdbx_overall_ESU_R_Free 0.085 _refine.overall_SU_ML 0.059 _refine.overall_SU_B 3.205 _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_TLS_residual_ADP_flag 'LIKELY RESIDUAL' _refine.pdbx_diffrn_id 1 _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3686 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 40 _refine_hist.number_atoms_solvent 564 _refine_hist.number_atoms_total 4290 _refine_hist.d_res_high 1.59 _refine_hist.d_res_low 20.00 # 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 0.014 0.022 ? 3828 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.483 1.952 ? 5234 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.772 5.000 ? 475 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 35.711 25.115 ? 174 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 13.725 15.000 ? 567 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 10.104 15.000 ? 10 'X-RAY DIFFRACTION' ? r_chiral_restr 0.110 0.200 ? 579 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.007 0.020 ? 2950 'X-RAY DIFFRACTION' ? r_nbd_refined 0.217 0.300 ? 1903 'X-RAY DIFFRACTION' ? r_nbtor_refined 0.324 0.500 ? 2703 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.172 0.500 ? 815 'X-RAY DIFFRACTION' ? r_metal_ion_refined 0.030 0.500 ? 2 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.235 0.300 ? 48 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.279 0.500 ? 98 'X-RAY DIFFRACTION' ? r_mcbond_it 1.158 2.000 ? 2394 'X-RAY DIFFRACTION' ? r_mcangle_it 1.726 3.000 ? 3805 'X-RAY DIFFRACTION' ? r_scbond_it 1.482 2.000 ? 1659 'X-RAY DIFFRACTION' ? r_scangle_it 2.129 3.000 ? 1429 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.59 _refine_ls_shell.d_res_low 1.630 _refine_ls_shell.number_reflns_R_work 3418 _refine_ls_shell.R_factor_R_work 0.252 _refine_ls_shell.percent_reflns_obs 74.80 _refine_ls_shell.R_factor_R_free 0.272 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 183 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 2GUY _struct.title 'Orthorhombic crystal structure (space group P21212) of Aspergillus niger alpha-amylase at 1.6 A resolution' _struct.pdbx_descriptor 'Alpha-amylase A (E.C.3.2.1.1)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 2GUY _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text '(beta-alpha) 8 barrel, 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 4 ? F N N 5 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 THR A 2 ? ARG A 7 ? THR A 2 ARG A 7 1 ? 6 HELX_P HELX_P2 2 LEU A 15 ? ALA A 20 ? LEU A 15 ALA A 20 1 ? 6 HELX_P HELX_P3 3 ASN A 31 ? GLN A 35 ? ASN A 31 GLN A 35 5 ? 5 HELX_P HELX_P4 4 THR A 41 ? LYS A 48 ? THR A 41 LYS A 48 1 ? 8 HELX_P HELX_P5 5 LYS A 48 ? GLY A 54 ? LYS A 48 GLY A 54 1 ? 7 HELX_P HELX_P6 6 THR A 96 ? ARG A 110 ? THR A 96 ARG A 110 1 ? 15 HELX_P HELX_P7 7 ALA A 128 ? VAL A 132 ? ALA A 128 VAL A 132 5 ? 5 HELX_P HELX_P8 8 ASP A 133 ? PHE A 137 ? ASP A 133 PHE A 137 5 ? 5 HELX_P HELX_P9 9 SER A 142 ? PHE A 146 ? SER A 142 PHE A 146 5 ? 5 HELX_P HELX_P10 10 ASP A 157 ? CYS A 164 ? ASP A 157 CYS A 164 1 ? 8 HELX_P HELX_P11 11 LYS A 180 ? SER A 199 ? LYS A 180 SER A 199 1 ? 20 HELX_P HELX_P12 12 THR A 207 ? VAL A 211 ? THR A 207 VAL A 211 5 ? 5 HELX_P HELX_P13 13 GLN A 212 ? ASP A 214 ? GLN A 212 ASP A 214 5 ? 3 HELX_P HELX_P14 14 PHE A 215 ? GLY A 224 ? PHE A 215 GLY A 224 1 ? 10 HELX_P HELX_P15 15 ASP A 235 ? CYS A 240 ? ASP A 235 CYS A 240 1 ? 6 HELX_P HELX_P16 16 PRO A 241 ? VAL A 245 ? PRO A 241 VAL A 245 5 ? 5 HELX_P HELX_P17 17 ASN A 251 ? LYS A 263 ? ASN A 251 LYS A 263 1 ? 13 HELX_P HELX_P18 18 SER A 268 ? CYS A 283 ? SER A 268 CYS A 283 1 ? 16 HELX_P HELX_P19 19 ASP A 285 ? LEU A 288 ? ASP A 285 LEU A 288 5 ? 4 HELX_P HELX_P20 20 ARG A 300 ? TYR A 304 ? ARG A 300 TYR A 304 5 ? 5 HELX_P HELX_P21 21 ASP A 307 ? ASN A 321 ? ASP A 307 ASN A 321 1 ? 15 HELX_P HELX_P22 22 GLY A 330 ? HIS A 334 ? GLY A 330 HIS A 334 5 ? 5 HELX_P HELX_P23 23 ALA A 346 ? GLY A 351 ? ALA A 346 GLY A 351 5 ? 6 HELX_P HELX_P24 24 SER A 356 ? ASP A 376 ? SER A 356 ASP A 376 1 ? 21 HELX_P HELX_P25 25 GLU A 467 ? ALA A 470 ? GLU A 467 ALA A 470 5 ? 4 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 30 SG ? ? ? 1_555 A CYS 38 SG ? ? A CYS 30 A CYS 38 1_555 ? ? ? ? ? ? ? 2.129 ? disulf2 disulf ? ? A CYS 150 SG ? ? ? 1_555 A CYS 164 SG ? ? A CYS 150 A CYS 164 1_555 ? ? ? ? ? ? ? 2.490 ? disulf3 disulf ? ? A CYS 240 SG ? ? ? 1_555 A CYS 283 SG ? ? A CYS 240 A CYS 283 1_555 ? ? ? ? ? ? ? 2.041 ? disulf4 disulf ? ? A CYS 440 SG A ? ? 1_555 A CYS 475 SG ? ? A CYS 440 A CYS 475 1_555 ? ? ? ? ? ? ? 2.048 ? covale1 covale ? ? A ASN 197 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 197 A NAG 1000 1_555 ? ? ? ? ? ? ? 1.448 ? covale2 covale ? ? B NAG . O4 ? ? ? 1_555 C NAG . C1 ? ? A NAG 1000 A NAG 1001 1_555 ? ? ? ? ? ? ? 1.444 ? covale3 covale ? ? C NAG . O4 ? ? ? 1_555 D BMA . C1 ? ? A NAG 1001 A BMA 1002 1_555 ? ? ? ? ? ? ? 1.463 ? metalc1 metalc ? ? E CA . CA ? ? ? 1_555 F HOH . O ? ? A CA 601 A HOH 1050 1_555 ? ? ? ? ? ? ? 2.512 ? metalc2 metalc ? ? E CA . CA ? ? ? 1_555 A GLU 162 O ? ? A CA 601 A GLU 162 1_555 ? ? ? ? ? ? ? 2.441 ? metalc3 metalc ? ? E CA . CA ? ? ? 1_555 A ASP 175 OD2 ? ? A CA 601 A ASP 175 1_555 ? ? ? ? ? ? ? 2.504 ? metalc4 metalc ? ? E CA . CA ? ? ? 1_555 F HOH . O ? ? A CA 601 A HOH 1026 1_555 ? ? ? ? ? ? ? 2.482 ? metalc5 metalc ? ? E CA . CA ? ? ? 1_555 F HOH . O ? ? A CA 601 A HOH 1194 1_555 ? ? ? ? ? ? ? 2.425 ? metalc6 metalc ? ? E CA . CA ? ? ? 1_555 A ASP 175 OD1 ? ? A CA 601 A ASP 175 1_555 ? ? ? ? ? ? ? 2.608 ? metalc7 metalc ? ? E CA . CA ? ? ? 1_555 A ASN 121 OD1 ? ? A CA 601 A ASN 121 1_555 ? ? ? ? ? ? ? 2.378 ? metalc8 metalc ? ? E CA . CA ? ? ? 1_555 A HIS 210 O ? ? A CA 601 A HIS 210 1_555 ? ? ? ? ? ? ? 2.409 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 LYS 138 A . ? LYS 138 A PRO 139 A ? PRO 139 A 1 4.88 2 ASP 340 A . ? ASP 340 A PRO 341 A ? PRO 341 A 1 5.20 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 8 ? B ? 2 ? C ? 3 ? D ? 6 ? E ? 2 ? # 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 ? parallel B 1 2 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel D 4 5 ? anti-parallel D 5 6 ? anti-parallel E 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 GLY A 248 ? VAL A 249 ? GLY A 248 VAL A 249 A 2 TYR A 226 ? GLY A 229 ? TYR A 226 GLY A 229 A 3 GLY A 202 ? ILE A 205 ? GLY A 202 ILE A 205 A 4 TYR A 113 ? VAL A 118 ? TYR A 113 VAL A 118 A 5 ALA A 59 ? ILE A 62 ? ALA A 59 ILE A 62 A 6 ILE A 11 ? LEU A 14 ? ILE A 11 LEU A 14 A 7 ILE A 324 ? TYR A 328 ? ILE A 324 TYR A 328 A 8 GLY A 290 ? THR A 291 ? GLY A 290 THR A 291 B 1 THR A 66 ? GLN A 68 ? THR A 66 GLN A 68 B 2 GLN A 84 ? LEU A 90 ? GLN A 84 LEU A 90 C 1 TYR A 125 ? ASP A 126 ? TYR A 125 ASP A 126 C 2 VAL A 171 ? LEU A 173 ? VAL A 171 LEU A 173 C 3 LEU A 166 ? GLY A 167 ? LEU A 166 GLY A 167 D 1 TRP A 385 ? ASP A 390 ? TRP A 385 ASP A 390 D 2 THR A 393 ? LYS A 398 ? THR A 393 LYS A 398 D 3 ILE A 405 ? SER A 410 ? ILE A 405 SER A 410 D 4 ARG A 461 ? PRO A 465 ? ARG A 461 PRO A 465 D 5 GLN A 433 ? GLU A 436 ? GLN A 433 GLU A 436 D 6 THR A 441 ? THR A 444 ? THR A 441 THR A 444 E 1 TYR A 419 ? LEU A 423 ? TYR A 419 LEU A 423 E 2 VAL A 451 ? MET A 455 ? VAL A 451 MET A 455 # 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 O GLY A 248 ? O GLY A 248 N GLY A 229 ? N GLY A 229 A 2 3 O ILE A 228 ? O ILE A 228 N ILE A 205 ? N ILE A 205 A 3 4 O ARG A 204 ? O ARG A 204 N VAL A 118 ? N VAL A 118 A 4 5 O MET A 115 ? O MET A 115 N ILE A 60 ? N ILE A 60 A 5 6 O TRP A 61 ? O TRP A 61 N LEU A 14 ? N LEU A 14 A 6 7 N ILE A 11 ? N ILE A 11 O PRO A 325 ? O PRO A 325 A 7 8 O ILE A 326 ? O ILE A 326 N THR A 291 ? N THR A 291 B 1 2 N ALA A 67 ? N ALA A 67 O GLN A 85 ? O GLN A 85 C 1 2 N TYR A 125 ? N TYR A 125 O SER A 172 ? O SER A 172 C 2 3 O LEU A 173 ? O LEU A 173 N LEU A 166 ? N LEU A 166 D 1 2 N TYR A 388 ? N TYR A 388 O ALA A 395 ? O ALA A 395 D 2 3 N ILE A 394 ? N ILE A 394 O LEU A 409 ? O LEU A 409 D 3 4 N VAL A 406 ? N VAL A 406 O LEU A 463 ? O LEU A 463 D 4 5 O TYR A 464 ? O TYR A 464 N THR A 435 ? N THR A 435 D 5 6 N LEU A 434 ? N LEU A 434 O VAL A 443 ? O VAL A 443 E 1 2 N TYR A 419 ? N TYR A 419 O MET A 455 ? O MET A 455 # 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 ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 1000' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 1001' AC3 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE BMA A 1002' AC4 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE CA A 601' # 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 7 TYR A 88 ? TYR A 88 . ? 1_555 ? 2 AC1 7 TRP A 190 ? TRP A 190 . ? 1_555 ? 3 AC1 7 SER A 193 ? SER A 193 . ? 1_555 ? 4 AC1 7 ASN A 197 ? ASN A 197 . ? 1_555 ? 5 AC1 7 NAG C . ? NAG A 1001 . ? 1_555 ? 6 AC1 7 HOH F . ? HOH A 1080 . ? 1_555 ? 7 AC1 7 HOH F . ? HOH A 1246 . ? 1_555 ? 8 AC2 3 NAG B . ? NAG A 1000 . ? 1_555 ? 9 AC2 3 BMA D . ? BMA A 1002 . ? 1_555 ? 10 AC2 3 HOH F . ? HOH A 1367 . ? 1_555 ? 11 AC3 1 NAG C . ? NAG A 1001 . ? 1_555 ? 12 AC4 7 ASN A 121 ? ASN A 121 . ? 1_555 ? 13 AC4 7 GLU A 162 ? GLU A 162 . ? 1_555 ? 14 AC4 7 ASP A 175 ? ASP A 175 . ? 1_555 ? 15 AC4 7 HIS A 210 ? HIS A 210 . ? 1_555 ? 16 AC4 7 HOH F . ? HOH A 1026 . ? 1_555 ? 17 AC4 7 HOH F . ? HOH A 1050 . ? 1_555 ? 18 AC4 7 HOH F . ? HOH A 1194 . ? 1_555 ? # _database_PDB_matrix.entry_id 2GUY _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 2GUY _atom_sites.fract_transf_matrix[1][1] 0.009728 _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] 0.015816 _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] 0.013431 _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 N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ALA A 1 1 ? 19.277 -7.950 9.452 1.00 21.90 ? 1 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? 18.815 -7.051 8.360 1.00 23.43 ? 1 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? 19.984 -6.249 7.786 1.00 24.21 ? 1 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? 20.956 -5.927 8.499 1.00 25.09 ? 1 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? 17.712 -6.126 8.858 1.00 22.74 ? 1 ALA A CB 1 ATOM 6 N N . THR A 1 2 ? 19.888 -5.939 6.490 1.00 23.90 ? 2 THR A N 1 ATOM 7 C CA . THR A 1 2 ? 20.992 -5.333 5.762 1.00 23.47 ? 2 THR A CA 1 ATOM 8 C C . THR A 1 2 ? 21.081 -3.835 5.981 1.00 22.03 ? 2 THR A C 1 ATOM 9 O O . THR A 1 2 ? 20.124 -3.197 6.393 1.00 24.36 ? 2 THR A O 1 ATOM 10 C CB . THR A 1 2 ? 20.832 -5.560 4.231 1.00 22.07 ? 2 THR A CB 1 ATOM 11 O OG1 . THR A 1 2 ? 19.649 -4.900 3.786 1.00 24.35 ? 2 THR A OG1 1 ATOM 12 C CG2 . THR A 1 2 ? 20.737 -7.043 3.921 1.00 24.10 ? 2 THR A CG2 1 ATOM 13 N N . PRO A 1 3 ? 22.239 -3.245 5.670 1.00 22.33 ? 3 PRO A N 1 ATOM 14 C CA . PRO A 1 3 ? 22.260 -1.786 5.685 1.00 22.98 ? 3 PRO A CA 1 ATOM 15 C C . PRO A 1 3 ? 21.118 -1.143 4.872 1.00 22.68 ? 3 PRO A C 1 ATOM 16 O O . PRO A 1 3 ? 20.522 -0.170 5.334 1.00 23.34 ? 3 PRO A O 1 ATOM 17 C CB . PRO A 1 3 ? 23.630 -1.444 5.107 1.00 23.28 ? 3 PRO A CB 1 ATOM 18 C CG . PRO A 1 3 ? 24.516 -2.641 5.503 1.00 22.19 ? 3 PRO A CG 1 ATOM 19 C CD . PRO A 1 3 ? 23.554 -3.830 5.339 1.00 22.32 ? 3 PRO A CD 1 ATOM 20 N N . ALA A 1 4 ? 20.789 -1.679 3.696 1.00 23.54 ? 4 ALA A N 1 ATOM 21 C CA . ALA A 1 4 ? 19.676 -1.125 2.911 1.00 23.43 ? 4 ALA A CA 1 ATOM 22 C C . ALA A 1 4 ? 18.338 -1.219 3.651 1.00 23.83 ? 4 ALA A C 1 ATOM 23 O O . ALA A 1 4 ? 17.530 -0.283 3.605 1.00 24.42 ? 4 ALA A O 1 ATOM 24 C CB . ALA A 1 4 ? 19.598 -1.814 1.528 1.00 22.76 ? 4 ALA A CB 1 ATOM 25 N N . ASP A 1 5 ? 18.110 -2.328 4.356 1.00 23.90 ? 5 ASP A N 1 ATOM 26 C CA . ASP A 1 5 ? 16.903 -2.487 5.191 1.00 24.84 ? 5 ASP A CA 1 ATOM 27 C C . ASP A 1 5 ? 16.863 -1.467 6.323 1.00 22.59 ? 5 ASP A C 1 ATOM 28 O O . ASP A 1 5 ? 15.778 -1.008 6.747 1.00 22.81 ? 5 ASP A O 1 ATOM 29 C CB . ASP A 1 5 ? 16.861 -3.867 5.863 1.00 25.69 ? 5 ASP A CB 1 ATOM 30 C CG . ASP A 1 5 ? 16.688 -5.016 4.897 1.00 27.83 ? 5 ASP A CG 1 ATOM 31 O OD1 . ASP A 1 5 ? 16.051 -4.876 3.824 1.00 28.27 ? 5 ASP A OD1 1 ATOM 32 O OD2 . ASP A 1 5 ? 17.201 -6.097 5.248 1.00 27.82 ? 5 ASP A OD2 1 ATOM 33 N N . TRP A 1 6 ? 18.034 -1.136 6.853 1.00 21.81 ? 6 TRP A N 1 ATOM 34 C CA . TRP A 1 6 ? 18.121 -0.189 7.980 1.00 20.49 ? 6 TRP A CA 1 ATOM 35 C C . TRP A 1 6 ? 17.915 1.302 7.645 1.00 21.96 ? 6 TRP A C 1 ATOM 36 O O . TRP A 1 6 ? 17.598 2.099 8.540 1.00 21.21 ? 6 TRP A O 1 ATOM 37 C CB . TRP A 1 6 ? 19.424 -0.392 8.779 1.00 21.98 ? 6 TRP A CB 1 ATOM 38 C CG . TRP A 1 6 ? 19.295 -1.473 9.825 1.00 21.68 ? 6 TRP A CG 1 ATOM 39 C CD1 . TRP A 1 6 ? 19.587 -2.816 9.672 1.00 21.35 ? 6 TRP A CD1 1 ATOM 40 C CD2 . TRP A 1 6 ? 18.819 -1.317 11.177 1.00 22.25 ? 6 TRP A CD2 1 ATOM 41 N NE1 . TRP A 1 6 ? 19.335 -3.486 10.860 1.00 21.48 ? 6 TRP A NE1 1 ATOM 42 C CE2 . TRP A 1 6 ? 18.840 -2.596 11.780 1.00 20.67 ? 6 TRP A CE2 1 ATOM 43 C CE3 . TRP A 1 6 ? 18.320 -0.222 11.919 1.00 20.49 ? 6 TRP A CE3 1 ATOM 44 C CZ2 . TRP A 1 6 ? 18.426 -2.808 13.113 1.00 21.39 ? 6 TRP A CZ2 1 ATOM 45 C CZ3 . TRP A 1 6 ? 17.917 -0.425 13.227 1.00 21.14 ? 6 TRP A CZ3 1 ATOM 46 C CH2 . TRP A 1 6 ? 17.983 -1.711 13.822 1.00 20.48 ? 6 TRP A CH2 1 ATOM 47 N N . ARG A 1 7 ? 18.127 1.700 6.392 1.00 21.17 ? 7 ARG A N 1 ATOM 48 C CA . ARG A 1 7 ? 17.996 3.140 6.040 1.00 23.00 ? 7 ARG A CA 1 ATOM 49 C C . ARG A 1 7 ? 16.659 3.719 6.447 1.00 22.52 ? 7 ARG A C 1 ATOM 50 O O . ARG A 1 7 ? 16.570 4.874 6.896 1.00 24.11 ? 7 ARG A O 1 ATOM 51 C CB . ARG A 1 7 ? 18.185 3.369 4.546 1.00 21.87 ? 7 ARG A CB 1 ATOM 52 C CG . ARG A 1 7 ? 19.648 3.284 4.085 1.00 23.76 ? 7 ARG A CG 1 ATOM 53 C CD . ARG A 1 7 ? 19.821 4.050 2.752 1.00 23.93 ? 7 ARG A CD 1 ATOM 54 N NE . ARG A 1 7 ? 21.211 4.038 2.301 1.00 24.17 ? 7 ARG A NE 1 ATOM 55 C CZ . ARG A 1 7 ? 21.753 3.019 1.638 1.00 25.06 ? 7 ARG A CZ 1 ATOM 56 N NH1 . ARG A 1 7 ? 21.008 1.951 1.351 1.00 25.04 ? 7 ARG A NH1 1 ATOM 57 N NH2 . ARG A 1 7 ? 23.035 3.054 1.249 1.00 25.85 ? 7 ARG A NH2 1 ATOM 58 N N . SER A 1 8 ? 15.611 2.918 6.321 1.00 21.67 ? 8 SER A N 1 ATOM 59 C CA . SER A 1 8 ? 14.265 3.456 6.563 1.00 21.53 ? 8 SER A CA 1 ATOM 60 C C . SER A 1 8 ? 13.936 3.489 8.065 1.00 23.04 ? 8 SER A C 1 ATOM 61 O O . SER A 1 8 ? 12.883 3.974 8.448 1.00 23.33 ? 8 SER A O 1 ATOM 62 C CB . SER A 1 8 ? 13.224 2.603 5.850 1.00 24.40 ? 8 SER A CB 1 ATOM 63 O OG . SER A 1 8 ? 13.349 1.259 6.276 1.00 25.98 ? 8 SER A OG 1 ATOM 64 N N . GLN A 1 9 ? 14.821 2.954 8.908 1.00 22.89 ? 9 GLN A N 1 ATOM 65 C CA . GLN A 1 9 ? 14.432 2.720 10.316 1.00 21.64 ? 9 GLN A CA 1 ATOM 66 C C . GLN A 1 9 ? 14.556 3.987 11.166 1.00 21.24 ? 9 GLN A C 1 ATOM 67 O O . GLN A 1 9 ? 15.243 4.939 10.745 1.00 21.46 ? 9 GLN A O 1 ATOM 68 C CB . GLN A 1 9 ? 15.306 1.616 10.915 1.00 21.69 ? 9 GLN A CB 1 ATOM 69 C CG . GLN A 1 9 ? 15.243 0.330 10.134 1.00 22.78 ? 9 GLN A CG 1 ATOM 70 C CD . GLN A 1 9 ? 13.858 -0.310 10.160 1.00 25.21 ? 9 GLN A CD 1 ATOM 71 O OE1 . GLN A 1 9 ? 13.276 -0.532 11.222 1.00 26.82 ? 9 GLN A OE1 1 ATOM 72 N NE2 . GLN A 1 9 ? 13.331 -0.613 8.974 1.00 28.27 ? 9 GLN A NE2 1 ATOM 73 N N . SER A 1 10 ? 13.906 3.996 12.339 1.00 21.74 ? 10 SER A N 1 ATOM 74 C CA . SER A 1 10 ? 13.990 5.098 13.286 1.00 21.13 ? 10 SER A CA 1 ATOM 75 C C . SER A 1 10 ? 14.149 4.395 14.636 1.00 22.38 ? 10 SER A C 1 ATOM 76 O O . SER A 1 10 ? 13.331 3.518 14.953 1.00 22.46 ? 10 SER A O 1 ATOM 77 C CB . SER A 1 10 ? 12.683 5.927 13.275 1.00 22.11 ? 10 SER A CB 1 ATOM 78 O OG . SER A 1 10 ? 12.845 7.036 14.178 1.00 23.41 ? 10 SER A OG 1 ATOM 79 N N . ILE A 1 11 ? 15.212 4.732 15.388 1.00 20.84 ? 11 ILE A N 1 ATOM 80 C CA . ILE A 1 11 ? 15.602 3.953 16.585 1.00 20.82 ? 11 ILE A CA 1 ATOM 81 C C . ILE A 1 11 ? 15.303 4.700 17.886 1.00 22.18 ? 11 ILE A C 1 ATOM 82 O O . ILE A 1 11 ? 15.611 5.872 18.032 1.00 21.55 ? 11 ILE A O 1 ATOM 83 C CB . ILE A 1 11 ? 17.120 3.657 16.535 1.00 20.28 ? 11 ILE A CB 1 ATOM 84 C CG1 . ILE A 1 11 ? 17.448 2.773 15.324 1.00 21.21 ? 11 ILE A CG1 1 ATOM 85 C CG2 . ILE A 1 11 ? 17.621 2.977 17.798 1.00 23.17 ? 11 ILE A CG2 1 ATOM 86 C CD1 . ILE A 1 11 ? 18.983 2.629 15.152 1.00 22.20 ? 11 ILE A CD1 1 ATOM 87 N N . TYR A 1 12 ? 14.717 3.988 18.821 1.00 19.75 ? 12 TYR A N 1 ATOM 88 C CA . TYR A 1 12 ? 14.596 4.443 20.206 1.00 20.84 ? 12 TYR A CA 1 ATOM 89 C C . TYR A 1 12 ? 15.660 3.699 20.991 1.00 21.65 ? 12 TYR A C 1 ATOM 90 O O . TYR A 1 12 ? 15.633 2.480 21.065 1.00 20.70 ? 12 TYR A O 1 ATOM 91 C CB . TYR A 1 12 ? 13.206 4.087 20.713 1.00 21.08 ? 12 TYR A CB 1 ATOM 92 C CG . TYR A 1 12 ? 12.872 4.578 22.084 1.00 20.84 ? 12 TYR A CG 1 ATOM 93 C CD1 . TYR A 1 12 ? 12.409 5.891 22.276 1.00 20.79 ? 12 TYR A CD1 1 ATOM 94 C CD2 . TYR A 1 12 ? 12.915 3.729 23.183 1.00 20.79 ? 12 TYR A CD2 1 ATOM 95 C CE1 . TYR A 1 12 ? 12.030 6.367 23.552 1.00 22.10 ? 12 TYR A CE1 1 ATOM 96 C CE2 . TYR A 1 12 ? 12.557 4.177 24.475 1.00 21.83 ? 12 TYR A CE2 1 ATOM 97 C CZ . TYR A 1 12 ? 12.116 5.506 24.649 1.00 19.98 ? 12 TYR A CZ 1 ATOM 98 O OH . TYR A 1 12 ? 11.725 5.930 25.896 1.00 20.88 ? 12 TYR A OH 1 ATOM 99 N N . PHE A 1 13 ? 16.628 4.446 21.532 1.00 20.78 ? 13 PHE A N 1 ATOM 100 C CA . PHE A 1 13 ? 17.743 3.851 22.251 1.00 19.28 ? 13 PHE A CA 1 ATOM 101 C C . PHE A 1 13 ? 17.378 3.933 23.750 1.00 20.15 ? 13 PHE A C 1 ATOM 102 O O . PHE A 1 13 ? 17.000 4.998 24.250 1.00 21.38 ? 13 PHE A O 1 ATOM 103 C CB . PHE A 1 13 ? 18.996 4.668 21.944 1.00 20.61 ? 13 PHE A CB 1 ATOM 104 C CG . PHE A 1 13 ? 20.077 4.550 22.993 1.00 20.59 ? 13 PHE A CG 1 ATOM 105 C CD1 . PHE A 1 13 ? 20.528 3.302 23.420 1.00 21.67 ? 13 PHE A CD1 1 ATOM 106 C CD2 . PHE A 1 13 ? 20.686 5.725 23.495 1.00 21.30 ? 13 PHE A CD2 1 ATOM 107 C CE1 . PHE A 1 13 ? 21.527 3.232 24.402 1.00 22.71 ? 13 PHE A CE1 1 ATOM 108 C CE2 . PHE A 1 13 ? 21.669 5.660 24.442 1.00 22.51 ? 13 PHE A CE2 1 ATOM 109 C CZ . PHE A 1 13 ? 22.116 4.404 24.884 1.00 20.56 ? 13 PHE A CZ 1 ATOM 110 N N . LEU A 1 14 ? 17.563 2.824 24.459 1.00 20.95 ? 14 LEU A N 1 ATOM 111 C CA . LEU A 1 14 ? 17.221 2.769 25.866 1.00 20.45 ? 14 LEU A CA 1 ATOM 112 C C . LEU A 1 14 ? 18.270 1.978 26.624 1.00 21.53 ? 14 LEU A C 1 ATOM 113 O O . LEU A 1 14 ? 18.966 1.148 26.071 1.00 21.24 ? 14 LEU A O 1 ATOM 114 C CB . LEU A 1 14 ? 15.835 2.120 26.033 1.00 19.36 ? 14 LEU A CB 1 ATOM 115 C CG . LEU A 1 14 ? 15.621 0.674 25.504 1.00 20.50 ? 14 LEU A CG 1 ATOM 116 C CD1 . LEU A 1 14 ? 15.986 -0.348 26.610 1.00 21.27 ? 14 LEU A CD1 1 ATOM 117 C CD2 . LEU A 1 14 ? 14.169 0.505 25.083 1.00 21.14 ? 14 LEU A CD2 1 ATOM 118 N N . LEU A 1 15 ? 18.383 2.268 27.910 1.00 22.08 ? 15 LEU A N 1 ATOM 119 C CA . LEU A 1 15 ? 19.150 1.440 28.812 1.00 22.68 ? 15 LEU A CA 1 ATOM 120 C C . LEU A 1 15 ? 18.265 0.369 29.414 1.00 21.94 ? 15 LEU A C 1 ATOM 121 O O . LEU A 1 15 ? 17.268 0.664 30.044 1.00 22.43 ? 15 LEU A O 1 ATOM 122 C CB . LEU A 1 15 ? 19.746 2.286 29.932 1.00 23.45 ? 15 LEU A CB 1 ATOM 123 C CG . LEU A 1 15 ? 21.186 2.746 29.745 1.00 31.85 ? 15 LEU A CG 1 ATOM 124 C CD1 . LEU A 1 15 ? 21.327 3.681 28.556 1.00 27.64 ? 15 LEU A CD1 1 ATOM 125 C CD2 . LEU A 1 15 ? 21.695 3.398 31.002 1.00 30.19 ? 15 LEU A CD2 1 ATOM 126 N N . THR A 1 16 ? 18.635 -0.888 29.233 1.00 21.84 ? 16 THR A N 1 ATOM 127 C CA . THR A 1 16 ? 17.748 -1.918 29.708 1.00 21.17 ? 16 THR A CA 1 ATOM 128 C C . THR A 1 16 ? 17.463 -1.806 31.202 1.00 21.47 ? 16 THR A C 1 ATOM 129 O O . THR A 1 16 ? 16.346 -2.085 31.646 1.00 22.14 ? 16 THR A O 1 ATOM 130 C CB . THR A 1 16 ? 18.344 -3.272 29.395 1.00 21.92 ? 16 THR A CB 1 ATOM 131 O OG1 . THR A 1 16 ? 18.558 -3.316 27.975 1.00 21.50 ? 16 THR A OG1 1 ATOM 132 C CG2 . THR A 1 16 ? 17.390 -4.401 29.810 1.00 23.15 ? 16 THR A CG2 1 ATOM 133 N N . ASP A 1 17 ? 18.466 -1.419 31.990 1.00 20.89 ? 17 ASP A N 1 ATOM 134 C CA . ASP A 1 17 ? 18.233 -1.341 33.444 1.00 21.26 ? 17 ASP A CA 1 ATOM 135 C C . ASP A 1 17 ? 17.291 -0.192 33.821 1.00 21.78 ? 17 ASP A C 1 ATOM 136 O O . ASP A 1 17 ? 16.796 -0.142 34.973 1.00 21.34 ? 17 ASP A O 1 ATOM 137 C CB . ASP A 1 17 ? 19.561 -1.156 34.195 1.00 21.56 ? 17 ASP A CB 1 ATOM 138 C CG . ASP A 1 17 ? 19.361 -1.138 35.698 1.00 22.86 ? 17 ASP A CG 1 ATOM 139 O OD1 . ASP A 1 17 ? 18.876 -2.143 36.240 1.00 22.36 ? 17 ASP A OD1 1 ATOM 140 O OD2 . ASP A 1 17 ? 19.638 -0.116 36.339 1.00 23.28 ? 17 ASP A OD2 1 ATOM 141 N N . ARG A 1 18 ? 17.087 0.764 32.900 1.00 20.27 ? 18 ARG A N 1 ATOM 142 C CA . ARG A 1 18 ? 16.474 2.038 33.278 1.00 22.30 ? 18 ARG A CA 1 ATOM 143 C C . ARG A 1 18 ? 15.172 2.306 32.541 1.00 23.48 ? 18 ARG A C 1 ATOM 144 O O . ARG A 1 18 ? 14.511 3.314 32.825 1.00 24.08 ? 18 ARG A O 1 ATOM 145 C CB . ARG A 1 18 ? 17.471 3.199 33.054 1.00 23.12 ? 18 ARG A CB 1 ATOM 146 C CG . ARG A 1 18 ? 18.788 3.087 33.839 1.00 22.61 ? 18 ARG A CG 1 ATOM 147 C CD . ARG A 1 18 ? 18.500 3.111 35.357 1.00 22.69 ? 18 ARG A CD 1 ATOM 148 N NE . ARG A 1 18 ? 19.589 2.699 36.236 1.00 23.81 ? 18 ARG A NE 1 ATOM 149 C CZ . ARG A 1 18 ? 20.536 3.529 36.687 1.00 22.61 ? 18 ARG A CZ 1 ATOM 150 N NH1 . ARG A 1 18 ? 20.558 4.801 36.310 1.00 20.99 ? 18 ARG A NH1 1 ATOM 151 N NH2 . ARG A 1 18 ? 21.462 3.077 37.540 1.00 22.76 ? 18 ARG A NH2 1 ATOM 152 N N . PHE A 1 19 ? 14.795 1.425 31.618 1.00 22.70 ? 19 PHE A N 1 ATOM 153 C CA . PHE A 1 19 ? 13.595 1.712 30.856 1.00 21.86 ? 19 PHE A CA 1 ATOM 154 C C . PHE A 1 19 ? 12.271 1.213 31.443 1.00 21.87 ? 19 PHE A C 1 ATOM 155 O O . PHE A 1 19 ? 11.300 1.992 31.581 1.00 20.43 ? 19 PHE A O 1 ATOM 156 C CB . PHE A 1 19 ? 13.731 1.219 29.401 1.00 22.15 ? 19 PHE A CB 1 ATOM 157 C CG . PHE A 1 19 ? 12.501 1.447 28.611 1.00 21.09 ? 19 PHE A CG 1 ATOM 158 C CD1 . PHE A 1 19 ? 12.156 2.725 28.221 1.00 22.55 ? 19 PHE A CD1 1 ATOM 159 C CD2 . PHE A 1 19 ? 11.668 0.374 28.258 1.00 22.23 ? 19 PHE A CD2 1 ATOM 160 C CE1 . PHE A 1 19 ? 10.991 2.956 27.489 1.00 22.08 ? 19 PHE A CE1 1 ATOM 161 C CE2 . PHE A 1 19 ? 10.521 0.583 27.520 1.00 21.80 ? 19 PHE A CE2 1 ATOM 162 C CZ . PHE A 1 19 ? 10.153 1.858 27.146 1.00 22.65 ? 19 PHE A CZ 1 ATOM 163 N N . ALA A 1 20 ? 12.199 -0.073 31.774 1.00 21.78 ? 20 ALA A N 1 ATOM 164 C CA . ALA A 1 20 ? 10.910 -0.624 32.287 1.00 20.54 ? 20 ALA A CA 1 ATOM 165 C C . ALA A 1 20 ? 11.186 -1.862 33.125 1.00 22.82 ? 20 ALA A C 1 ATOM 166 O O . ALA A 1 20 ? 11.896 -2.764 32.667 1.00 20.99 ? 20 ALA A O 1 ATOM 167 C CB . ALA A 1 20 ? 10.038 -0.981 31.117 1.00 20.76 ? 20 ALA A CB 1 ATOM 168 N N . ARG A 1 21 ? 10.633 -1.884 34.343 1.00 21.10 ? 21 ARG A N 1 ATOM 169 C CA . ARG A 1 21 ? 10.731 -3.050 35.230 1.00 22.00 ? 21 ARG A CA 1 ATOM 170 C C . ARG A 1 21 ? 9.681 -4.095 34.869 1.00 23.63 ? 21 ARG A C 1 ATOM 171 O O . ARG A 1 21 ? 8.618 -3.790 34.280 1.00 24.13 ? 21 ARG A O 1 ATOM 172 C CB . ARG A 1 21 ? 10.503 -2.637 36.700 1.00 23.11 ? 21 ARG A CB 1 ATOM 173 C CG . ARG A 1 21 ? 11.471 -1.581 37.218 1.00 23.32 ? 21 ARG A CG 1 ATOM 174 C CD . ARG A 1 21 ? 11.013 -0.972 38.584 1.00 23.91 ? 21 ARG A CD 1 ATOM 175 N NE . ARG A 1 21 ? 10.606 -2.026 39.528 1.00 22.50 ? 21 ARG A NE 1 ATOM 176 C CZ . ARG A 1 21 ? 11.456 -2.695 40.297 1.00 23.54 ? 21 ARG A CZ 1 ATOM 177 N NH1 . ARG A 1 21 ? 12.762 -2.399 40.288 1.00 23.79 ? 21 ARG A NH1 1 ATOM 178 N NH2 . ARG A 1 21 ? 10.989 -3.644 41.095 1.00 24.50 ? 21 ARG A NH2 1 ATOM 179 N N . THR A 1 22 ? 9.957 -5.337 35.250 1.00 21.90 ? 22 THR A N 1 ATOM 180 C CA . THR A 1 22 ? 8.986 -6.405 35.016 1.00 24.14 ? 22 THR A CA 1 ATOM 181 C C . THR A 1 22 ? 7.642 -6.067 35.659 1.00 23.96 ? 22 THR A C 1 ATOM 182 O O . THR A 1 22 ? 6.570 -6.282 35.058 1.00 24.44 ? 22 THR A O 1 ATOM 183 C CB . THR A 1 22 ? 9.530 -7.739 35.539 1.00 24.67 ? 22 THR A CB 1 ATOM 184 O OG1 . THR A 1 22 ? 10.693 -8.075 34.772 1.00 25.93 ? 22 THR A OG1 1 ATOM 185 C CG2 . THR A 1 22 ? 8.490 -8.854 35.397 1.00 24.01 ? 22 THR A CG2 1 ATOM 186 N N . ASP A 1 23 ? 7.694 -5.503 36.859 1.00 24.01 ? 23 ASP A N 1 ATOM 187 C CA . ASP A 1 23 ? 6.449 -5.182 37.574 1.00 24.60 ? 23 ASP A CA 1 ATOM 188 C C . ASP A 1 23 ? 5.708 -3.937 37.050 1.00 24.85 ? 23 ASP A C 1 ATOM 189 O O . ASP A 1 23 ? 4.606 -3.631 37.518 1.00 24.86 ? 23 ASP A O 1 ATOM 190 C CB . ASP A 1 23 ? 6.653 -5.137 39.112 1.00 24.22 ? 23 ASP A CB 1 ATOM 191 C CG . ASP A 1 23 ? 7.557 -3.986 39.590 1.00 24.78 ? 23 ASP A CG 1 ATOM 192 O OD1 . ASP A 1 23 ? 7.856 -3.019 38.828 1.00 23.39 ? 23 ASP A OD1 1 ATOM 193 O OD2 . ASP A 1 23 ? 7.932 -4.034 40.785 1.00 25.11 ? 23 ASP A OD2 1 ATOM 194 N N . GLY A 1 24 ? 6.302 -3.233 36.091 1.00 23.15 ? 24 GLY A N 1 ATOM 195 C CA . GLY A 1 24 ? 5.623 -2.073 35.475 1.00 22.97 ? 24 GLY A CA 1 ATOM 196 C C . GLY A 1 24 ? 5.456 -0.873 36.384 1.00 24.74 ? 24 GLY A C 1 ATOM 197 O O . GLY A 1 24 ? 4.664 0.054 36.080 1.00 23.92 ? 24 GLY A O 1 ATOM 198 N N . SER A 1 25 ? 6.186 -0.867 37.497 1.00 24.28 ? 25 SER A N 1 ATOM 199 C CA . SER A 1 25 ? 6.081 0.260 38.436 1.00 24.05 ? 25 SER A CA 1 ATOM 200 C C . SER A 1 25 ? 6.494 1.542 37.763 1.00 24.54 ? 25 SER A C 1 ATOM 201 O O . SER A 1 25 ? 7.476 1.567 37.009 1.00 24.50 ? 25 SER A O 1 ATOM 202 C CB . SER A 1 25 ? 6.981 0.045 39.643 1.00 24.62 ? 25 SER A CB 1 ATOM 203 O OG . SER A 1 25 ? 6.887 1.149 40.529 1.00 24.49 ? 25 SER A OG 1 ATOM 204 N N . THR A 1 26 ? 5.749 2.620 38.028 1.00 21.74 ? 26 THR A N 1 ATOM 205 C CA . THR A 1 26 ? 6.205 3.948 37.607 1.00 21.73 ? 26 THR A CA 1 ATOM 206 C C . THR A 1 26 ? 6.683 4.759 38.802 1.00 23.61 ? 26 THR A C 1 ATOM 207 O O . THR A 1 26 ? 6.916 5.961 38.683 1.00 24.56 ? 26 THR A O 1 ATOM 208 C CB . THR A 1 26 ? 5.098 4.742 36.896 1.00 24.23 ? 26 THR A CB 1 ATOM 209 O OG1 . THR A 1 26 ? 3.946 4.829 37.757 1.00 23.98 ? 26 THR A OG1 1 ATOM 210 C CG2 . THR A 1 26 ? 4.759 4.094 35.555 1.00 23.82 ? 26 THR A CG2 1 ATOM 211 N N . THR A 1 27 ? 6.824 4.115 39.957 1.00 22.57 ? 27 THR A N 1 ATOM 212 C CA . THR A 1 27 ? 7.254 4.835 41.153 1.00 25.25 ? 27 THR A CA 1 ATOM 213 C C . THR A 1 27 ? 8.500 4.237 41.822 1.00 24.66 ? 27 THR A C 1 ATOM 214 O O . THR A 1 27 ? 9.066 4.846 42.733 1.00 25.80 ? 27 THR A O 1 ATOM 215 C CB . THR A 1 27 ? 6.120 4.903 42.194 1.00 27.17 ? 27 THR A CB 1 ATOM 216 O OG1 . THR A 1 27 ? 5.731 3.578 42.544 1.00 28.29 ? 27 THR A OG1 1 ATOM 217 C CG2 . THR A 1 27 ? 4.917 5.633 41.624 1.00 27.47 ? 27 THR A CG2 1 ATOM 218 N N . ALA A 1 28 ? 8.894 3.038 41.441 1.00 23.98 ? 28 ALA A N 1 ATOM 219 C CA . ALA A 1 28 ? 10.103 2.435 42.010 1.00 24.35 ? 28 ALA A CA 1 ATOM 220 C C . ALA A 1 28 ? 11.307 3.381 41.928 1.00 24.39 ? 28 ALA A C 1 ATOM 221 O O . ALA A 1 28 ? 11.595 3.954 40.871 1.00 23.59 ? 28 ALA A O 1 ATOM 222 C CB . ALA A 1 28 ? 10.424 1.120 41.309 1.00 25.11 ? 28 ALA A CB 1 ATOM 223 N N . THR A 1 29 ? 12.005 3.522 43.054 1.00 26.18 ? 29 THR A N 1 ATOM 224 C CA . THR A 1 29 ? 13.203 4.364 43.176 1.00 27.84 ? 29 THR A CA 1 ATOM 225 C C . THR A 1 29 ? 14.288 4.066 42.164 1.00 26.19 ? 29 THR A C 1 ATOM 226 O O . THR A 1 29 ? 14.607 2.901 41.929 1.00 24.78 ? 29 THR A O 1 ATOM 227 C CB . THR A 1 29 ? 13.855 4.116 44.569 1.00 30.07 ? 29 THR A CB 1 ATOM 228 O OG1 . THR A 1 29 ? 12.919 4.443 45.577 1.00 33.95 ? 29 THR A OG1 1 ATOM 229 C CG2 . THR A 1 29 ? 15.115 4.953 44.764 1.00 32.66 ? 29 THR A CG2 1 ATOM 230 N N . CYS A 1 30 ? 14.891 5.105 41.591 1.00 25.80 ? 30 CYS A N 1 ATOM 231 C CA . CYS A 1 30 ? 16.117 4.906 40.830 1.00 25.54 ? 30 CYS A CA 1 ATOM 232 C C . CYS A 1 30 ? 16.967 6.154 40.985 1.00 25.60 ? 30 CYS A C 1 ATOM 233 O O . CYS A 1 30 ? 16.743 7.166 40.310 1.00 26.00 ? 30 CYS A O 1 ATOM 234 C CB . CYS A 1 30 ? 15.825 4.669 39.371 1.00 26.42 ? 30 CYS A CB 1 ATOM 235 S SG . CYS A 1 30 ? 17.393 4.269 38.477 1.00 28.89 ? 30 CYS A SG 1 ATOM 236 N N . ASN A 1 31 ? 17.916 6.084 41.914 1.00 23.56 ? 31 ASN A N 1 ATOM 237 C CA . ASN A 1 31 ? 18.730 7.237 42.257 1.00 24.31 ? 31 ASN A CA 1 ATOM 238 C C . ASN A 1 31 ? 19.944 7.138 41.376 1.00 24.35 ? 31 ASN A C 1 ATOM 239 O O . ASN A 1 31 ? 20.740 6.191 41.537 1.00 23.45 ? 31 ASN A O 1 ATOM 240 C CB . ASN A 1 31 ? 19.116 7.181 43.739 1.00 26.13 ? 31 ASN A CB 1 ATOM 241 C CG . ASN A 1 31 ? 20.125 8.260 44.129 1.00 28.69 ? 31 ASN A CG 1 ATOM 242 O OD1 . ASN A 1 31 ? 20.927 8.678 43.305 1.00 30.41 ? 31 ASN A OD1 1 ATOM 243 N ND2 . ASN A 1 31 ? 20.110 8.680 45.392 1.00 28.95 ? 31 ASN A ND2 1 ATOM 244 N N . THR A 1 32 ? 20.046 8.040 40.389 1.00 22.77 ? 32 THR A N 1 ATOM 245 C CA . THR A 1 32 ? 21.101 7.871 39.380 1.00 23.68 ? 32 THR A CA 1 ATOM 246 C C . THR A 1 32 ? 22.480 7.985 40.012 1.00 21.82 ? 32 THR A C 1 ATOM 247 O O . THR A 1 32 ? 23.426 7.300 39.599 1.00 22.41 ? 32 THR A O 1 ATOM 248 C CB . THR A 1 32 ? 21.005 8.848 38.218 1.00 23.78 ? 32 THR A CB 1 ATOM 249 O OG1 . THR A 1 32 ? 20.984 10.169 38.747 1.00 24.61 ? 32 THR A OG1 1 ATOM 250 C CG2 . THR A 1 32 ? 19.705 8.606 37.415 1.00 24.06 ? 32 THR A CG2 1 ATOM 251 N N . ALA A 1 33 ? 22.606 8.815 41.059 1.00 23.18 ? 33 ALA A N 1 ATOM 252 C CA . ALA A 1 33 ? 23.917 9.034 41.654 1.00 22.08 ? 33 ALA A CA 1 ATOM 253 C C . ALA A 1 33 ? 24.480 7.756 42.282 1.00 23.07 ? 33 ALA A C 1 ATOM 254 O O . ALA A 1 33 ? 25.696 7.586 42.365 1.00 25.76 ? 33 ALA A O 1 ATOM 255 C CB . ALA A 1 33 ? 23.856 10.167 42.697 1.00 24.29 ? 33 ALA A CB 1 ATOM 256 N N . ASP A 1 34 ? 23.601 6.855 42.714 1.00 22.34 ? 34 ASP A N 1 ATOM 257 C CA . ASP A 1 34 ? 24.029 5.623 43.378 1.00 24.74 ? 34 ASP A CA 1 ATOM 258 C C . ASP A 1 34 ? 24.638 4.632 42.392 1.00 24.63 ? 34 ASP A C 1 ATOM 259 O O . ASP A 1 34 ? 25.398 3.741 42.767 1.00 25.44 ? 34 ASP A O 1 ATOM 260 C CB . ASP A 1 34 ? 22.828 4.948 44.051 1.00 28.85 ? 34 ASP A CB 1 ATOM 261 C CG . ASP A 1 34 ? 22.377 5.660 45.326 1.00 32.46 ? 34 ASP A CG 1 ATOM 262 O OD1 . ASP A 1 34 ? 23.049 6.596 45.802 1.00 35.32 ? 34 ASP A OD1 1 ATOM 263 O OD2 . ASP A 1 34 ? 21.324 5.260 45.854 1.00 35.69 ? 34 ASP A OD2 1 ATOM 264 N N . GLN A 1 35 ? 24.300 4.800 41.121 1.00 23.05 ? 35 GLN A N 1 ATOM 265 C CA . GLN A 1 35 ? 24.899 3.966 40.061 1.00 23.39 ? 35 GLN A CA 1 ATOM 266 C C . GLN A 1 35 ? 24.669 2.483 40.269 1.00 23.40 ? 35 GLN A C 1 ATOM 267 O O . GLN A 1 35 ? 25.508 1.679 39.912 1.00 25.51 ? 35 GLN A O 1 ATOM 268 C CB . GLN A 1 35 ? 26.387 4.231 39.956 1.00 22.42 ? 35 GLN A CB 1 ATOM 269 C CG . GLN A 1 35 ? 26.633 5.611 39.393 1.00 24.72 ? 35 GLN A CG 1 ATOM 270 C CD . GLN A 1 35 ? 28.087 5.948 39.370 1.00 26.16 ? 35 GLN A CD 1 ATOM 271 O OE1 . GLN A 1 35 ? 28.715 6.051 40.412 1.00 27.54 ? 35 GLN A OE1 1 ATOM 272 N NE2 . GLN A 1 35 ? 28.636 6.100 38.186 1.00 25.97 ? 35 GLN A NE2 1 ATOM 273 N N . LYS A 1 36 ? 23.502 2.114 40.778 1.00 23.54 ? 36 LYS A N 1 ATOM 274 C CA . LYS A 1 36 ? 23.217 0.685 41.006 1.00 25.77 ? 36 LYS A CA 1 ATOM 275 C C . LYS A 1 36 ? 22.146 0.165 40.045 1.00 24.87 ? 36 LYS A C 1 ATOM 276 O O . LYS A 1 36 ? 21.453 0.954 39.415 1.00 25.57 ? 36 LYS A O 1 ATOM 277 C CB . LYS A 1 36 ? 22.799 0.451 42.467 1.00 29.25 ? 36 LYS A CB 1 ATOM 278 C CG . LYS A 1 36 ? 23.956 0.662 43.453 1.00 31.27 ? 36 LYS A CG 1 ATOM 279 C CD . LYS A 1 36 ? 23.502 0.487 44.918 1.00 32.93 ? 36 LYS A CD 1 ATOM 280 C CE . LYS A 1 36 ? 24.670 0.538 45.899 1.00 34.06 ? 36 LYS A CE 1 ATOM 281 N NZ . LYS A 1 36 ? 24.141 0.752 47.273 1.00 38.50 ? 36 LYS A NZ 1 ATOM 282 N N . TYR A 1 37 ? 22.010 -1.152 39.927 1.00 23.18 ? 37 TYR A N 1 ATOM 283 C CA . TYR A 1 37 ? 20.879 -1.701 39.190 1.00 23.55 ? 37 TYR A CA 1 ATOM 284 C C . TYR A 1 37 ? 19.581 -1.207 39.799 1.00 26.12 ? 37 TYR A C 1 ATOM 285 O O . TYR A 1 37 ? 19.362 -1.347 41.037 1.00 26.21 ? 37 TYR A O 1 ATOM 286 C CB . TYR A 1 37 ? 20.888 -3.230 39.255 1.00 23.79 ? 37 TYR A CB 1 ATOM 287 C CG . TYR A 1 37 ? 21.918 -3.888 38.386 1.00 23.43 ? 37 TYR A CG 1 ATOM 288 C CD1 . TYR A 1 37 ? 21.659 -4.119 37.025 1.00 23.03 ? 37 TYR A CD1 1 ATOM 289 C CD2 . TYR A 1 37 ? 23.129 -4.360 38.922 1.00 24.08 ? 37 TYR A CD2 1 ATOM 290 C CE1 . TYR A 1 37 ? 22.589 -4.764 36.221 1.00 23.56 ? 37 TYR A CE1 1 ATOM 291 C CE2 . TYR A 1 37 ? 24.054 -5.016 38.123 1.00 22.98 ? 37 TYR A CE2 1 ATOM 292 C CZ . TYR A 1 37 ? 23.788 -5.191 36.774 1.00 23.90 ? 37 TYR A CZ 1 ATOM 293 O OH . TYR A 1 37 ? 24.669 -5.869 35.957 1.00 24.53 ? 37 TYR A OH 1 ATOM 294 N N . CYS A 1 38 ? 18.710 -0.676 38.945 1.00 22.76 ? 38 CYS A N 1 ATOM 295 C CA . CYS A 1 38 ? 17.385 -0.172 39.363 1.00 22.94 ? 38 CYS A CA 1 ATOM 296 C C . CYS A 1 38 ? 16.263 -1.144 39.009 1.00 22.65 ? 38 CYS A C 1 ATOM 297 O O . CYS A 1 38 ? 15.105 -0.966 39.441 1.00 22.99 ? 38 CYS A O 1 ATOM 298 C CB . CYS A 1 38 ? 17.115 1.174 38.711 1.00 24.73 ? 38 CYS A CB 1 ATOM 299 S SG . CYS A 1 38 ? 18.106 2.503 39.428 1.00 27.70 ? 38 CYS A SG 1 ATOM 300 N N . GLY A 1 39 ? 16.594 -2.146 38.188 1.00 21.22 ? 39 GLY A N 1 ATOM 301 C CA . GLY A 1 39 ? 15.673 -3.272 37.934 1.00 22.15 ? 39 GLY A CA 1 ATOM 302 C C . GLY A 1 39 ? 14.975 -3.348 36.572 1.00 22.21 ? 39 GLY A C 1 ATOM 303 O O . GLY A 1 39 ? 14.039 -4.122 36.383 1.00 22.45 ? 39 GLY A O 1 ATOM 304 N N . GLY A 1 40 ? 15.397 -2.548 35.609 1.00 20.91 ? 40 GLY A N 1 ATOM 305 C CA . GLY A 1 40 ? 14.834 -2.675 34.272 1.00 19.93 ? 40 GLY A CA 1 ATOM 306 C C . GLY A 1 40 ? 15.118 -4.027 33.656 1.00 21.24 ? 40 GLY A C 1 ATOM 307 O O . GLY A 1 40 ? 16.179 -4.569 33.865 1.00 20.21 ? 40 GLY A O 1 ATOM 308 N N . THR A 1 41 ? 14.186 -4.565 32.866 1.00 21.08 ? 41 THR A N 1 ATOM 309 C CA . THR A 1 41 ? 14.360 -5.916 32.274 1.00 20.40 ? 41 THR A CA 1 ATOM 310 C C . THR A 1 41 ? 13.899 -5.992 30.833 1.00 21.22 ? 41 THR A C 1 ATOM 311 O O . THR A 1 41 ? 13.157 -5.103 30.358 1.00 20.52 ? 41 THR A O 1 ATOM 312 C CB . THR A 1 41 ? 13.538 -6.956 33.023 1.00 22.20 ? 41 THR A CB 1 ATOM 313 O OG1 . THR A 1 41 ? 12.144 -6.582 32.916 1.00 22.93 ? 41 THR A OG1 1 ATOM 314 C CG2 . THR A 1 41 ? 13.956 -7.003 34.493 1.00 21.61 ? 41 THR A CG2 1 ATOM 315 N N . TRP A 1 42 ? 14.269 -7.080 30.146 1.00 22.13 ? 42 TRP A N 1 ATOM 316 C CA . TRP A 1 42 ? 13.774 -7.318 28.793 1.00 21.08 ? 42 TRP A CA 1 ATOM 317 C C . TRP A 1 42 ? 12.258 -7.508 28.783 1.00 21.56 ? 42 TRP A C 1 ATOM 318 O O . TRP A 1 42 ? 11.581 -6.988 27.900 1.00 21.46 ? 42 TRP A O 1 ATOM 319 C CB . TRP A 1 42 ? 14.475 -8.512 28.152 1.00 21.64 ? 42 TRP A CB 1 ATOM 320 C CG . TRP A 1 42 ? 15.951 -8.299 28.019 1.00 21.87 ? 42 TRP A CG 1 ATOM 321 C CD1 . TRP A 1 42 ? 16.572 -7.162 27.568 1.00 21.43 ? 42 TRP A CD1 1 ATOM 322 C CD2 . TRP A 1 42 ? 17.004 -9.242 28.314 1.00 22.59 ? 42 TRP A CD2 1 ATOM 323 N NE1 . TRP A 1 42 ? 17.948 -7.344 27.569 1.00 21.43 ? 42 TRP A NE1 1 ATOM 324 C CE2 . TRP A 1 42 ? 18.233 -8.598 28.037 1.00 20.70 ? 42 TRP A CE2 1 ATOM 325 C CE3 . TRP A 1 42 ? 17.029 -10.552 28.814 1.00 21.80 ? 42 TRP A CE3 1 ATOM 326 C CZ2 . TRP A 1 42 ? 19.490 -9.229 28.234 1.00 22.18 ? 42 TRP A CZ2 1 ATOM 327 C CZ3 . TRP A 1 42 ? 18.287 -11.190 29.005 1.00 20.84 ? 42 TRP A CZ3 1 ATOM 328 C CH2 . TRP A 1 42 ? 19.492 -10.513 28.723 1.00 20.72 ? 42 TRP A CH2 1 ATOM 329 N N . GLN A 1 43 ? 11.713 -8.225 29.763 1.00 21.11 ? 43 GLN A N 1 ATOM 330 C CA . GLN A 1 43 ? 10.258 -8.372 29.826 1.00 22.37 ? 43 GLN A CA 1 ATOM 331 C C . GLN A 1 43 ? 9.597 -7.000 29.992 1.00 20.91 ? 43 GLN A C 1 ATOM 332 O O . GLN A 1 43 ? 8.539 -6.738 29.420 1.00 21.66 ? 43 GLN A O 1 ATOM 333 C CB . GLN A 1 43 ? 9.852 -9.278 30.993 1.00 23.24 ? 43 GLN A CB 1 ATOM 334 C CG . GLN A 1 43 ? 8.357 -9.503 31.091 1.00 28.74 ? 43 GLN A CG 1 ATOM 335 C CD . GLN A 1 43 ? 7.758 -10.062 29.783 1.00 30.68 ? 43 GLN A CD 1 ATOM 336 O OE1 . GLN A 1 43 ? 6.766 -9.516 29.251 1.00 34.60 ? 43 GLN A OE1 1 ATOM 337 N NE2 . GLN A 1 43 ? 8.343 -11.135 29.276 1.00 28.09 ? 43 GLN A NE2 1 ATOM 338 N N . GLY A 1 44 ? 10.215 -6.130 30.800 1.00 21.49 ? 44 GLY A N 1 ATOM 339 C CA . GLY A 1 44 ? 9.708 -4.782 30.972 1.00 21.03 ? 44 GLY A CA 1 ATOM 340 C C . GLY A 1 44 ? 9.585 -4.067 29.640 1.00 22.19 ? 44 GLY A C 1 ATOM 341 O O . GLY A 1 44 ? 8.590 -3.393 29.371 1.00 21.84 ? 44 GLY A O 1 ATOM 342 N N . ILE A 1 45 ? 10.619 -4.196 28.799 1.00 21.55 ? 45 ILE A N 1 ATOM 343 C CA . ILE A 1 45 ? 10.596 -3.533 27.488 1.00 21.13 ? 45 ILE A CA 1 ATOM 344 C C . ILE A 1 45 ? 9.404 -4.070 26.669 1.00 21.61 ? 45 ILE A C 1 ATOM 345 O O . ILE A 1 45 ? 8.652 -3.319 26.054 1.00 21.00 ? 45 ILE A O 1 ATOM 346 C CB . ILE A 1 45 ? 11.915 -3.795 26.693 1.00 21.67 ? 45 ILE A CB 1 ATOM 347 C CG1 . ILE A 1 45 ? 13.141 -3.244 27.428 1.00 22.82 ? 45 ILE A CG1 1 ATOM 348 C CG2 . ILE A 1 45 ? 11.836 -3.172 25.290 1.00 22.78 ? 45 ILE A CG2 1 ATOM 349 C CD1 . ILE A 1 45 ? 14.468 -3.840 26.812 1.00 22.51 ? 45 ILE A CD1 1 ATOM 350 N N . ILE A 1 46 ? 9.218 -5.381 26.671 1.00 20.58 ? 46 ILE A N 1 ATOM 351 C CA . ILE A 1 46 ? 8.149 -5.958 25.858 1.00 21.22 ? 46 ILE A CA 1 ATOM 352 C C . ILE A 1 46 ? 6.830 -5.296 26.211 1.00 21.84 ? 46 ILE A C 1 ATOM 353 O O . ILE A 1 46 ? 6.045 -4.931 25.344 1.00 23.69 ? 46 ILE A O 1 ATOM 354 C CB . ILE A 1 46 ? 8.046 -7.469 26.119 1.00 22.15 ? 46 ILE A CB 1 ATOM 355 C CG1 . ILE A 1 46 ? 9.310 -8.179 25.590 1.00 22.53 ? 46 ILE A CG1 1 ATOM 356 C CG2 . ILE A 1 46 ? 6.701 -8.056 25.514 1.00 21.81 ? 46 ILE A CG2 1 ATOM 357 C CD1 . ILE A 1 46 ? 9.372 -9.705 25.930 1.00 22.00 ? 46 ILE A CD1 1 ATOM 358 N N . ASP A 1 47 ? 6.591 -5.124 27.502 1.00 22.07 ? 47 ASP A N 1 ATOM 359 C CA . ASP A 1 47 ? 5.297 -4.585 27.931 1.00 24.34 ? 47 ASP A CA 1 ATOM 360 C C . ASP A 1 47 ? 5.102 -3.097 27.622 1.00 23.30 ? 47 ASP A C 1 ATOM 361 O O . ASP A 1 47 ? 3.961 -2.585 27.704 1.00 22.87 ? 47 ASP A O 1 ATOM 362 C CB . ASP A 1 47 ? 5.114 -4.874 29.407 1.00 26.23 ? 47 ASP A CB 1 ATOM 363 C CG . ASP A 1 47 ? 4.851 -6.346 29.662 1.00 29.51 ? 47 ASP A CG 1 ATOM 364 O OD1 . ASP A 1 47 ? 4.293 -7.032 28.754 1.00 30.34 ? 47 ASP A OD1 1 ATOM 365 O OD2 . ASP A 1 47 ? 5.189 -6.815 30.762 1.00 30.47 ? 47 ASP A OD2 1 ATOM 366 N N . LYS A 1 48 ? 6.178 -2.403 27.262 1.00 22.10 ? 48 LYS A N 1 ATOM 367 C CA . LYS A 1 48 ? 6.081 -1.000 26.884 1.00 22.23 ? 48 LYS A CA 1 ATOM 368 C C . LYS A 1 48 ? 6.383 -0.754 25.409 1.00 21.19 ? 48 LYS A C 1 ATOM 369 O O . LYS A 1 48 ? 6.599 0.401 24.980 1.00 22.62 ? 48 LYS A O 1 ATOM 370 C CB . LYS A 1 48 ? 6.979 -0.130 27.787 1.00 23.78 ? 48 LYS A CB 1 ATOM 371 C CG . LYS A 1 48 ? 6.532 -0.073 29.230 1.00 24.69 ? 48 LYS A CG 1 ATOM 372 C CD . LYS A 1 48 ? 5.074 0.340 29.397 1.00 27.73 ? 48 LYS A CD 1 ATOM 373 C CE . LYS A 1 48 ? 4.839 1.811 29.061 1.00 28.22 ? 48 LYS A CE 1 ATOM 374 N NZ . LYS A 1 48 ? 3.410 2.179 29.388 1.00 29.19 ? 48 LYS A NZ 1 ATOM 375 N N . LEU A 1 49 ? 6.354 -1.801 24.592 1.00 20.71 ? 49 LEU A N 1 ATOM 376 C CA . LEU A 1 49 ? 6.567 -1.587 23.165 1.00 21.48 ? 49 LEU A CA 1 ATOM 377 C C . LEU A 1 49 ? 5.531 -0.673 22.526 1.00 21.24 ? 49 LEU A C 1 ATOM 378 O O . LEU A 1 49 ? 5.843 0.012 21.539 1.00 22.63 ? 49 LEU A O 1 ATOM 379 C CB . LEU A 1 49 ? 6.686 -2.902 22.396 1.00 21.38 ? 49 LEU A CB 1 ATOM 380 C CG . LEU A 1 49 ? 7.986 -3.628 22.687 1.00 22.63 ? 49 LEU A CG 1 ATOM 381 C CD1 . LEU A 1 49 ? 7.904 -5.023 22.023 1.00 22.93 ? 49 LEU A CD1 1 ATOM 382 C CD2 . LEU A 1 49 ? 9.202 -2.820 22.173 1.00 22.84 ? 49 LEU A CD2 1 ATOM 383 N N . ASP A 1 50 ? 4.291 -0.688 23.032 1.00 21.98 ? 50 ASP A N 1 ATOM 384 C CA . ASP A 1 50 ? 3.276 0.209 22.470 1.00 22.85 ? 50 ASP A CA 1 ATOM 385 C C . ASP A 1 50 ? 3.630 1.683 22.645 1.00 21.63 ? 50 ASP A C 1 ATOM 386 O O . ASP A 1 50 ? 3.352 2.509 21.767 1.00 22.50 ? 50 ASP A O 1 ATOM 387 C CB . ASP A 1 50 ? 1.925 -0.034 23.122 1.00 23.24 ? 50 ASP A CB 1 ATOM 388 C CG . ASP A 1 50 ? 1.320 -1.384 22.766 1.00 25.07 ? 50 ASP A CG 1 ATOM 389 O OD1 . ASP A 1 50 ? 1.368 -1.802 21.586 1.00 28.35 ? 50 ASP A OD1 1 ATOM 390 O OD2 . ASP A 1 50 ? 0.730 -1.980 23.671 1.00 27.72 ? 50 ASP A OD2 1 ATOM 391 N N . TYR A 1 51 ? 4.222 2.012 23.791 1.00 22.66 ? 51 TYR A N 1 ATOM 392 C CA . TYR A 1 51 ? 4.671 3.368 24.083 1.00 22.06 ? 51 TYR A CA 1 ATOM 393 C C . TYR A 1 51 ? 5.703 3.783 23.042 1.00 21.66 ? 51 TYR A C 1 ATOM 394 O O . TYR A 1 51 ? 5.671 4.899 22.526 1.00 23.83 ? 51 TYR A O 1 ATOM 395 C CB . TYR A 1 51 ? 5.270 3.400 25.480 1.00 21.93 ? 51 TYR A CB 1 ATOM 396 C CG . TYR A 1 51 ? 5.990 4.664 25.852 1.00 21.24 ? 51 TYR A CG 1 ATOM 397 C CD1 . TYR A 1 51 ? 5.282 5.774 26.318 1.00 21.18 ? 51 TYR A CD1 1 ATOM 398 C CD2 . TYR A 1 51 ? 7.377 4.728 25.807 1.00 20.17 ? 51 TYR A CD2 1 ATOM 399 C CE1 . TYR A 1 51 ? 5.936 6.948 26.675 1.00 21.47 ? 51 TYR A CE1 1 ATOM 400 C CE2 . TYR A 1 51 ? 8.054 5.888 26.182 1.00 22.01 ? 51 TYR A CE2 1 ATOM 401 C CZ . TYR A 1 51 ? 7.308 7.002 26.624 1.00 22.50 ? 51 TYR A CZ 1 ATOM 402 O OH . TYR A 1 51 ? 7.940 8.161 26.984 1.00 22.84 ? 51 TYR A OH 1 ATOM 403 N N . ILE A 1 52 ? 6.631 2.876 22.733 1.00 22.71 ? 52 ILE A N 1 ATOM 404 C CA . ILE A 1 52 ? 7.705 3.217 21.806 1.00 22.03 ? 52 ILE A CA 1 ATOM 405 C C . ILE A 1 52 ? 7.160 3.297 20.409 1.00 22.25 ? 52 ILE A C 1 ATOM 406 O O . ILE A 1 52 ? 7.440 4.259 19.689 1.00 23.33 ? 52 ILE A O 1 ATOM 407 C CB . ILE A 1 52 ? 8.849 2.167 21.890 1.00 21.59 ? 52 ILE A CB 1 ATOM 408 C CG1 . ILE A 1 52 ? 9.461 2.229 23.290 1.00 21.79 ? 52 ILE A CG1 1 ATOM 409 C CG2 . ILE A 1 52 ? 9.884 2.342 20.748 1.00 21.79 ? 52 ILE A CG2 1 ATOM 410 C CD1 . ILE A 1 52 ? 10.403 1.031 23.622 1.00 22.46 ? 52 ILE A CD1 1 ATOM 411 N N . GLN A 1 53 ? 6.396 2.278 20.004 1.00 22.58 ? 53 GLN A N 1 ATOM 412 C CA . GLN A 1 53 ? 5.911 2.233 18.632 1.00 21.61 ? 53 GLN A CA 1 ATOM 413 C C . GLN A 1 53 ? 4.902 3.375 18.350 1.00 21.82 ? 53 GLN A C 1 ATOM 414 O O . GLN A 1 53 ? 4.790 3.856 17.200 1.00 22.27 ? 53 GLN A O 1 ATOM 415 C CB . GLN A 1 53 ? 5.338 0.842 18.294 1.00 23.30 ? 53 GLN A CB 1 ATOM 416 C CG . GLN A 1 53 ? 4.999 0.675 16.833 1.00 24.08 ? 53 GLN A CG 1 ATOM 417 C CD . GLN A 1 53 ? 4.724 -0.764 16.445 1.00 24.83 ? 53 GLN A CD 1 ATOM 418 O OE1 . GLN A 1 53 ? 4.158 -1.567 17.232 1.00 25.80 ? 53 GLN A OE1 1 ATOM 419 N NE2 . GLN A 1 53 ? 5.116 -1.108 15.219 1.00 24.49 ? 53 GLN A NE2 1 ATOM 420 N N . GLY A 1 54 ? 4.216 3.826 19.396 1.00 21.99 ? 54 GLY A N 1 ATOM 421 C CA . GLY A 1 54 ? 3.274 4.973 19.314 1.00 22.74 ? 54 GLY A CA 1 ATOM 422 C C . GLY A 1 54 ? 3.944 6.282 18.937 1.00 22.02 ? 54 GLY A C 1 ATOM 423 O O . GLY A 1 54 ? 3.246 7.256 18.524 1.00 24.34 ? 54 GLY A O 1 ATOM 424 N N . MET A 1 55 ? 5.274 6.337 19.092 1.00 21.78 ? 55 MET A N 1 ATOM 425 C CA . MET A 1 55 ? 5.996 7.545 18.672 1.00 23.39 ? 55 MET A CA 1 ATOM 426 C C . MET A 1 55 ? 6.481 7.396 17.261 1.00 21.53 ? 55 MET A C 1 ATOM 427 O O . MET A 1 55 ? 7.185 8.305 16.744 1.00 22.86 ? 55 MET A O 1 ATOM 428 C CB . MET A 1 55 ? 7.197 7.869 19.563 1.00 22.84 ? 55 MET A CB 1 ATOM 429 C CG . MET A 1 55 ? 6.853 8.748 20.761 1.00 24.29 ? 55 MET A CG 1 ATOM 430 S SD . MET A 1 55 ? 8.342 8.977 21.782 1.00 24.34 ? 55 MET A SD 1 ATOM 431 C CE . MET A 1 55 ? 8.510 7.385 22.587 1.00 24.74 ? 55 MET A CE 1 ATOM 432 N N . GLY A 1 56 ? 6.221 6.234 16.673 1.00 21.68 ? 56 GLY A N 1 ATOM 433 C CA . GLY A 1 56 ? 6.552 6.043 15.265 1.00 20.55 ? 56 GLY A CA 1 ATOM 434 C C . GLY A 1 56 ? 7.944 5.440 15.044 1.00 20.40 ? 56 GLY A C 1 ATOM 435 O O . GLY A 1 56 ? 8.410 5.332 13.905 1.00 22.02 ? 56 GLY A O 1 ATOM 436 N N . PHE A 1 57 ? 8.600 5.019 16.135 1.00 20.73 ? 57 PHE A N 1 ATOM 437 C CA . PHE A 1 57 ? 9.830 4.231 16.001 1.00 22.68 ? 57 PHE A CA 1 ATOM 438 C C . PHE A 1 57 ? 9.619 2.845 15.380 1.00 21.43 ? 57 PHE A C 1 ATOM 439 O O . PHE A 1 57 ? 8.594 2.209 15.568 1.00 22.79 ? 57 PHE A O 1 ATOM 440 C CB . PHE A 1 57 ? 10.526 4.103 17.336 1.00 23.10 ? 57 PHE A CB 1 ATOM 441 C CG . PHE A 1 57 ? 10.977 5.419 17.852 1.00 22.34 ? 57 PHE A CG 1 ATOM 442 C CD1 . PHE A 1 57 ? 12.040 6.074 17.261 1.00 22.18 ? 57 PHE A CD1 1 ATOM 443 C CD2 . PHE A 1 57 ? 10.286 6.052 18.887 1.00 22.76 ? 57 PHE A CD2 1 ATOM 444 C CE1 . PHE A 1 57 ? 12.449 7.354 17.738 1.00 21.89 ? 57 PHE A CE1 1 ATOM 445 C CE2 . PHE A 1 57 ? 10.681 7.318 19.373 1.00 22.89 ? 57 PHE A CE2 1 ATOM 446 C CZ . PHE A 1 57 ? 11.767 7.978 18.787 1.00 22.19 ? 57 PHE A CZ 1 ATOM 447 N N . THR A 1 58 ? 10.631 2.378 14.655 1.00 21.19 ? 58 THR A N 1 ATOM 448 C CA . THR A 1 58 ? 10.553 1.092 13.996 1.00 20.92 ? 58 THR A CA 1 ATOM 449 C C . THR A 1 58 ? 11.588 0.103 14.541 1.00 20.19 ? 58 THR A C 1 ATOM 450 O O . THR A 1 58 ? 11.665 -1.048 14.089 1.00 20.92 ? 58 THR A O 1 ATOM 451 C CB . THR A 1 58 ? 10.817 1.246 12.467 1.00 23.09 ? 58 THR A CB 1 ATOM 452 O OG1 . THR A 1 58 ? 12.193 1.626 12.250 1.00 23.96 ? 58 THR A OG1 1 ATOM 453 C CG2 . THR A 1 58 ? 9.880 2.284 11.849 1.00 22.75 ? 58 THR A CG2 1 ATOM 454 N N . ALA A 1 59 ? 12.382 0.558 15.505 1.00 19.46 ? 59 ALA A N 1 ATOM 455 C CA . ALA A 1 59 ? 13.476 -0.256 16.033 1.00 20.26 ? 59 ALA A CA 1 ATOM 456 C C . ALA A 1 59 ? 13.883 0.223 17.406 1.00 20.89 ? 59 ALA A C 1 ATOM 457 O O . ALA A 1 59 ? 13.657 1.381 17.746 1.00 19.71 ? 59 ALA A O 1 ATOM 458 C CB . ALA A 1 59 ? 14.682 -0.172 15.113 1.00 21.33 ? 59 ALA A CB 1 ATOM 459 N N . ILE A 1 60 ? 14.503 -0.667 18.186 1.00 21.01 ? 60 ILE A N 1 ATOM 460 C CA . ILE A 1 60 ? 15.099 -0.208 19.430 1.00 19.83 ? 60 ILE A CA 1 ATOM 461 C C . ILE A 1 60 ? 16.548 -0.654 19.500 1.00 20.97 ? 60 ILE A C 1 ATOM 462 O O . ILE A 1 60 ? 16.911 -1.645 18.891 1.00 20.77 ? 60 ILE A O 1 ATOM 463 C CB . ILE A 1 60 ? 14.399 -0.741 20.694 1.00 20.49 ? 60 ILE A CB 1 ATOM 464 C CG1 . ILE A 1 60 ? 14.617 -2.254 20.836 1.00 22.91 ? 60 ILE A CG1 1 ATOM 465 C CG2 . ILE A 1 60 ? 12.886 -0.405 20.686 1.00 21.71 ? 60 ILE A CG2 1 ATOM 466 C CD1 . ILE A 1 60 ? 13.916 -2.883 22.069 1.00 23.24 ? 60 ILE A CD1 1 ATOM 467 N N . TRP A 1 61 ? 17.364 0.133 20.197 1.00 20.57 ? 61 TRP A N 1 ATOM 468 C CA . TRP A 1 61 ? 18.767 -0.203 20.485 1.00 20.52 ? 61 TRP A CA 1 ATOM 469 C C . TRP A 1 61 ? 18.828 -0.384 21.979 1.00 20.72 ? 61 TRP A C 1 ATOM 470 O O . TRP A 1 61 ? 18.462 0.543 22.707 1.00 20.88 ? 61 TRP A O 1 ATOM 471 C CB . TRP A 1 61 ? 19.684 0.912 19.948 1.00 22.18 ? 61 TRP A CB 1 ATOM 472 C CG . TRP A 1 61 ? 20.974 1.160 20.672 1.00 21.72 ? 61 TRP A CG 1 ATOM 473 C CD1 . TRP A 1 61 ? 21.604 0.359 21.605 1.00 21.98 ? 61 TRP A CD1 1 ATOM 474 C CD2 . TRP A 1 61 ? 21.779 2.332 20.528 1.00 22.25 ? 61 TRP A CD2 1 ATOM 475 N NE1 . TRP A 1 61 ? 22.753 1.019 22.091 1.00 22.26 ? 61 TRP A NE1 1 ATOM 476 C CE2 . TRP A 1 61 ? 22.886 2.206 21.410 1.00 22.83 ? 61 TRP A CE2 1 ATOM 477 C CE3 . TRP A 1 61 ? 21.677 3.476 19.710 1.00 22.54 ? 61 TRP A CE3 1 ATOM 478 C CZ2 . TRP A 1 61 ? 23.826 3.201 21.554 1.00 22.69 ? 61 TRP A CZ2 1 ATOM 479 C CZ3 . TRP A 1 61 ? 22.651 4.465 19.823 1.00 21.74 ? 61 TRP A CZ3 1 ATOM 480 C CH2 . TRP A 1 61 ? 23.710 4.320 20.746 1.00 21.71 ? 61 TRP A CH2 1 ATOM 481 N N . ILE A 1 62 ? 19.193 -1.590 22.428 1.00 20.25 ? 62 ILE A N 1 ATOM 482 C CA . ILE A 1 62 ? 19.301 -1.827 23.880 1.00 20.50 ? 62 ILE A CA 1 ATOM 483 C C . ILE A 1 62 ? 20.776 -1.998 24.254 1.00 21.63 ? 62 ILE A C 1 ATOM 484 O O . ILE A 1 62 ? 21.581 -2.375 23.421 1.00 20.14 ? 62 ILE A O 1 ATOM 485 C CB . ILE A 1 62 ? 18.504 -3.075 24.300 1.00 20.53 ? 62 ILE A CB 1 ATOM 486 C CG1 . ILE A 1 62 ? 19.161 -4.370 23.749 1.00 21.14 ? 62 ILE A CG1 1 ATOM 487 C CG2 . ILE A 1 62 ? 17.054 -2.957 23.793 1.00 21.53 ? 62 ILE A CG2 1 ATOM 488 C CD1 . ILE A 1 62 ? 18.431 -5.680 24.195 1.00 21.94 ? 62 ILE A CD1 1 ATOM 489 N N . THR A 1 63 ? 21.092 -1.758 25.538 1.00 21.19 ? 63 THR A N 1 ATOM 490 C CA . THR A 1 63 ? 22.489 -1.788 25.996 1.00 20.57 ? 63 THR A CA 1 ATOM 491 C C . THR A 1 63 ? 22.960 -3.258 26.082 1.00 20.18 ? 63 THR A C 1 ATOM 492 O O . THR A 1 63 ? 22.164 -4.176 25.868 1.00 20.65 ? 63 THR A O 1 ATOM 493 C CB . THR A 1 63 ? 22.620 -1.017 27.338 1.00 20.92 ? 63 THR A CB 1 ATOM 494 O OG1 . THR A 1 63 ? 21.511 -1.389 28.220 1.00 21.23 ? 63 THR A OG1 1 ATOM 495 C CG2 . THR A 1 63 ? 22.566 0.490 27.036 1.00 21.10 ? 63 THR A CG2 1 ATOM 496 N N . PRO A 1 64 ? 24.271 -3.485 26.246 1.00 20.57 ? 64 PRO A N 1 ATOM 497 C CA . PRO A 1 64 ? 24.826 -4.837 26.062 1.00 20.82 ? 64 PRO A CA 1 ATOM 498 C C . PRO A 1 64 ? 24.205 -5.900 26.942 1.00 19.73 ? 64 PRO A C 1 ATOM 499 O O . PRO A 1 64 ? 23.787 -5.589 28.079 1.00 21.77 ? 64 PRO A O 1 ATOM 500 C CB . PRO A 1 64 ? 26.304 -4.653 26.450 1.00 20.56 ? 64 PRO A CB 1 ATOM 501 C CG . PRO A 1 64 ? 26.610 -3.250 25.957 1.00 20.97 ? 64 PRO A CG 1 ATOM 502 C CD . PRO A 1 64 ? 25.344 -2.493 26.461 1.00 20.71 ? 64 PRO A CD 1 ATOM 503 N N . VAL A 1 65 ? 24.194 -7.134 26.440 1.00 21.21 ? 65 VAL A N 1 ATOM 504 C CA . VAL A 1 65 ? 23.481 -8.210 27.091 1.00 20.40 ? 65 VAL A CA 1 ATOM 505 C C . VAL A 1 65 ? 24.352 -9.220 27.851 1.00 21.22 ? 65 VAL A C 1 ATOM 506 O O . VAL A 1 65 ? 23.806 -10.088 28.536 1.00 22.05 ? 65 VAL A O 1 ATOM 507 C CB . VAL A 1 65 ? 22.627 -8.981 26.050 1.00 20.63 ? 65 VAL A CB 1 ATOM 508 C CG1 . VAL A 1 65 ? 21.660 -8.006 25.332 1.00 21.60 ? 65 VAL A CG1 1 ATOM 509 C CG2 . VAL A 1 65 ? 23.536 -9.728 25.051 1.00 22.50 ? 65 VAL A CG2 1 ATOM 510 N N . THR A 1 66 ? 25.675 -9.141 27.698 1.00 20.94 ? 66 THR A N 1 ATOM 511 C CA . THR A 1 66 ? 26.586 -10.132 28.235 1.00 21.07 ? 66 THR A CA 1 ATOM 512 C C . THR A 1 66 ? 26.695 -10.035 29.766 1.00 19.74 ? 66 THR A C 1 ATOM 513 O O . THR A 1 66 ? 26.482 -8.946 30.343 1.00 21.09 ? 66 THR A O 1 ATOM 514 C CB . THR A 1 66 ? 27.990 -9.964 27.637 1.00 20.10 ? 66 THR A CB 1 ATOM 515 O OG1 . THR A 1 66 ? 28.367 -8.573 27.713 1.00 21.11 ? 66 THR A OG1 1 ATOM 516 C CG2 . THR A 1 66 ? 27.986 -10.424 26.167 1.00 19.97 ? 66 THR A CG2 1 ATOM 517 N N . ALA A 1 67 ? 27.056 -11.149 30.397 1.00 19.86 ? 67 ALA A N 1 ATOM 518 C CA . ALA A 1 67 ? 27.238 -11.199 31.858 1.00 20.46 ? 67 ALA A CA 1 ATOM 519 C C . ALA A 1 67 ? 28.382 -10.256 32.209 1.00 21.84 ? 67 ALA A C 1 ATOM 520 O O . ALA A 1 67 ? 29.432 -10.244 31.536 1.00 21.69 ? 67 ALA A O 1 ATOM 521 C CB . ALA A 1 67 ? 27.543 -12.599 32.343 1.00 21.50 ? 67 ALA A CB 1 ATOM 522 N N . GLN A 1 68 ? 28.166 -9.512 33.284 1.00 19.80 ? 68 GLN A N 1 ATOM 523 C CA . GLN A 1 68 ? 29.069 -8.445 33.687 1.00 20.90 ? 68 GLN A CA 1 ATOM 524 C C . GLN A 1 68 ? 29.868 -8.807 34.918 1.00 20.74 ? 68 GLN A C 1 ATOM 525 O O . GLN A 1 68 ? 29.656 -9.861 35.564 1.00 22.03 ? 68 GLN A O 1 ATOM 526 C CB . GLN A 1 68 ? 28.229 -7.196 34.030 1.00 21.89 ? 68 GLN A CB 1 ATOM 527 C CG . GLN A 1 68 ? 27.354 -6.759 32.872 1.00 22.26 ? 68 GLN A CG 1 ATOM 528 C CD . GLN A 1 68 ? 28.137 -6.030 31.832 1.00 22.44 ? 68 GLN A CD 1 ATOM 529 O OE1 . GLN A 1 68 ? 28.687 -4.955 32.100 1.00 21.16 ? 68 GLN A OE1 1 ATOM 530 N NE2 . GLN A 1 68 ? 28.228 -6.615 30.624 1.00 22.08 ? 68 GLN A NE2 1 ATOM 531 N N . LEU A 1 69 ? 30.824 -7.945 35.248 1.00 20.92 ? 69 LEU A N 1 ATOM 532 C CA . LEU A 1 69 ? 31.405 -8.087 36.563 1.00 22.29 ? 69 LEU A CA 1 ATOM 533 C C . LEU A 1 69 ? 30.280 -7.989 37.616 1.00 21.81 ? 69 LEU A C 1 ATOM 534 O O . LEU A 1 69 ? 29.370 -7.183 37.471 1.00 21.21 ? 69 LEU A O 1 ATOM 535 C CB . LEU A 1 69 ? 32.501 -7.041 36.763 1.00 21.99 ? 69 LEU A CB 1 ATOM 536 C CG . LEU A 1 69 ? 32.138 -5.555 36.862 1.00 22.66 ? 69 LEU A CG 1 ATOM 537 C CD1 . LEU A 1 69 ? 31.684 -5.150 38.293 1.00 22.66 ? 69 LEU A CD1 1 ATOM 538 C CD2 . LEU A 1 69 ? 33.379 -4.754 36.496 1.00 23.44 ? 69 LEU A CD2 1 ATOM 539 N N . PRO A 1 70 ? 30.327 -8.825 38.672 1.00 21.12 ? 70 PRO A N 1 ATOM 540 C CA . PRO A 1 70 ? 29.202 -8.903 39.614 1.00 21.55 ? 70 PRO A CA 1 ATOM 541 C C . PRO A 1 70 ? 29.274 -7.894 40.779 1.00 21.69 ? 70 PRO A C 1 ATOM 542 O O . PRO A 1 70 ? 28.263 -7.630 41.425 1.00 21.59 ? 70 PRO A O 1 ATOM 543 C CB . PRO A 1 70 ? 29.303 -10.343 40.152 1.00 21.29 ? 70 PRO A CB 1 ATOM 544 C CG . PRO A 1 70 ? 30.780 -10.629 40.107 1.00 21.86 ? 70 PRO A CG 1 ATOM 545 C CD . PRO A 1 70 ? 31.383 -9.812 38.957 1.00 21.19 ? 70 PRO A CD 1 ATOM 546 N N . GLN A 1 71 ? 30.449 -7.322 41.012 1.00 20.64 ? 71 GLN A N 1 ATOM 547 C CA . GLN A 1 71 ? 30.642 -6.466 42.191 1.00 18.49 ? 71 GLN A CA 1 ATOM 548 C C . GLN A 1 71 ? 29.902 -5.131 42.160 1.00 20.50 ? 71 GLN A C 1 ATOM 549 O O . GLN A 1 71 ? 29.619 -4.608 41.113 1.00 20.98 ? 71 GLN A O 1 ATOM 550 C CB . GLN A 1 71 ? 32.144 -6.171 42.361 1.00 18.84 ? 71 GLN A CB 1 ATOM 551 C CG . GLN A 1 71 ? 32.996 -7.391 42.715 1.00 18.08 ? 71 GLN A CG 1 ATOM 552 C CD . GLN A 1 71 ? 33.478 -8.148 41.465 1.00 19.58 ? 71 GLN A CD 1 ATOM 553 O OE1 . GLN A 1 71 ? 33.298 -7.678 40.311 1.00 20.90 ? 71 GLN A OE1 1 ATOM 554 N NE2 . GLN A 1 71 ? 34.067 -9.344 41.680 1.00 21.64 ? 71 GLN A NE2 1 ATOM 555 N N . THR A 1 72 ? 29.623 -4.597 43.340 1.00 19.71 ? 72 THR A N 1 ATOM 556 C CA . THR A 1 72 ? 29.280 -3.192 43.434 1.00 20.07 ? 72 THR A CA 1 ATOM 557 C C . THR A 1 72 ? 30.631 -2.550 43.741 1.00 22.48 ? 72 THR A C 1 ATOM 558 O O . THR A 1 72 ? 31.275 -2.874 44.738 1.00 21.97 ? 72 THR A O 1 ATOM 559 C CB . THR A 1 72 ? 28.328 -2.953 44.591 1.00 21.24 ? 72 THR A CB 1 ATOM 560 O OG1 . THR A 1 72 ? 27.083 -3.615 44.314 1.00 22.65 ? 72 THR A OG1 1 ATOM 561 C CG2 . THR A 1 72 ? 28.052 -1.453 44.731 1.00 22.47 ? 72 THR A CG2 1 ATOM 562 N N . THR A 1 73 ? 31.058 -1.671 42.834 1.00 23.21 ? 73 THR A N 1 ATOM 563 C CA . THR A 1 73 ? 32.354 -1.028 42.958 1.00 25.05 ? 73 THR A CA 1 ATOM 564 C C . THR A 1 73 ? 32.153 0.384 43.484 1.00 25.41 ? 73 THR A C 1 ATOM 565 O O . THR A 1 73 ? 31.015 0.837 43.728 1.00 24.06 ? 73 THR A O 1 ATOM 566 C CB . THR A 1 73 ? 33.015 -0.890 41.576 1.00 25.65 ? 73 THR A CB 1 ATOM 567 O OG1 . THR A 1 73 ? 32.343 0.154 40.845 1.00 24.74 ? 73 THR A OG1 1 ATOM 568 C CG2 . THR A 1 73 ? 32.930 -2.201 40.762 1.00 27.15 ? 73 THR A CG2 1 ATOM 569 N N . ALA A 1 74 ? 33.259 1.128 43.662 1.00 26.30 ? 74 ALA A N 1 ATOM 570 C CA . ALA A 1 74 ? 33.124 2.500 44.081 1.00 27.45 ? 74 ALA A CA 1 ATOM 571 C C . ALA A 1 74 ? 32.432 3.364 43.027 1.00 27.07 ? 74 ALA A C 1 ATOM 572 O O . ALA A 1 74 ? 31.960 4.470 43.327 1.00 27.04 ? 74 ALA A O 1 ATOM 573 C CB . ALA A 1 74 ? 34.493 3.106 44.476 1.00 28.27 ? 74 ALA A CB 1 ATOM 574 N N . TYR A 1 75 ? 32.361 2.857 41.793 1.00 24.46 ? 75 TYR A N 1 ATOM 575 C CA . TYR A 1 75 ? 31.582 3.513 40.740 1.00 24.18 ? 75 TYR A CA 1 ATOM 576 C C . TYR A 1 75 ? 30.228 2.827 40.499 1.00 23.02 ? 75 TYR A C 1 ATOM 577 O O . TYR A 1 75 ? 29.627 2.965 39.418 1.00 24.44 ? 75 TYR A O 1 ATOM 578 C CB . TYR A 1 75 ? 32.340 3.552 39.397 1.00 24.53 ? 75 TYR A CB 1 ATOM 579 C CG . TYR A 1 75 ? 33.671 4.246 39.413 1.00 24.56 ? 75 TYR A CG 1 ATOM 580 C CD1 . TYR A 1 75 ? 33.945 5.223 40.359 1.00 25.59 ? 75 TYR A CD1 1 ATOM 581 C CD2 . TYR A 1 75 ? 34.634 3.948 38.460 1.00 24.86 ? 75 TYR A CD2 1 ATOM 582 C CE1 . TYR A 1 75 ? 35.192 5.883 40.375 1.00 24.67 ? 75 TYR A CE1 1 ATOM 583 C CE2 . TYR A 1 75 ? 35.864 4.593 38.432 1.00 25.48 ? 75 TYR A CE2 1 ATOM 584 C CZ . TYR A 1 75 ? 36.146 5.548 39.423 1.00 25.78 ? 75 TYR A CZ 1 ATOM 585 O OH . TYR A 1 75 ? 37.374 6.209 39.436 1.00 26.65 ? 75 TYR A OH 1 ATOM 586 N N . GLY A 1 76 ? 29.775 2.041 41.471 1.00 21.71 ? 76 GLY A N 1 ATOM 587 C CA . GLY A 1 76 ? 28.502 1.331 41.328 1.00 22.12 ? 76 GLY A CA 1 ATOM 588 C C . GLY A 1 76 ? 28.581 -0.017 40.620 1.00 22.27 ? 76 GLY A C 1 ATOM 589 O O . GLY A 1 76 ? 29.631 -0.662 40.555 1.00 21.99 ? 76 GLY A O 1 ATOM 590 N N . ASP A 1 77 ? 27.433 -0.457 40.130 1.00 21.64 ? 77 ASP A N 1 ATOM 591 C CA . ASP A 1 77 ? 27.262 -1.757 39.489 1.00 22.09 ? 77 ASP A CA 1 ATOM 592 C C . ASP A 1 77 ? 27.388 -1.619 37.981 1.00 22.11 ? 77 ASP A C 1 ATOM 593 O O . ASP A 1 77 ? 27.327 -0.502 37.434 1.00 23.12 ? 77 ASP A O 1 ATOM 594 C CB . ASP A 1 77 ? 25.799 -2.192 39.716 1.00 23.60 ? 77 ASP A CB 1 ATOM 595 C CG . ASP A 1 77 ? 25.498 -2.508 41.139 1.00 26.32 ? 77 ASP A CG 1 ATOM 596 O OD1 . ASP A 1 77 ? 26.419 -2.914 41.871 1.00 28.22 ? 77 ASP A OD1 1 ATOM 597 O OD2 . ASP A 1 77 ? 24.312 -2.349 41.519 1.00 26.84 ? 77 ASP A OD2 1 ATOM 598 N N . ALA A 1 78 ? 27.513 -2.757 37.305 1.00 20.68 ? 78 ALA A N 1 ATOM 599 C CA . ALA A 1 78 ? 27.580 -2.765 35.837 1.00 20.41 ? 78 ALA A CA 1 ATOM 600 C C . ALA A 1 78 ? 26.200 -2.628 35.182 1.00 21.44 ? 78 ALA A C 1 ATOM 601 O O . ALA A 1 78 ? 25.891 -3.320 34.190 1.00 21.24 ? 78 ALA A O 1 ATOM 602 C CB . ALA A 1 78 ? 28.239 -4.080 35.371 1.00 20.23 ? 78 ALA A CB 1 ATOM 603 N N . TYR A 1 79 ? 25.383 -1.694 35.665 1.00 21.19 ? 79 TYR A N 1 ATOM 604 C CA . TYR A 1 79 ? 23.985 -1.659 35.230 1.00 21.49 ? 79 TYR A CA 1 ATOM 605 C C . TYR A 1 79 ? 23.848 -1.304 33.749 1.00 21.13 ? 79 TYR A C 1 ATOM 606 O O . TYR A 1 79 ? 22.832 -1.624 33.126 1.00 23.76 ? 79 TYR A O 1 ATOM 607 C CB . TYR A 1 79 ? 23.222 -0.630 36.075 1.00 21.89 ? 79 TYR A CB 1 ATOM 608 C CG . TYR A 1 79 ? 23.651 0.784 35.842 1.00 22.49 ? 79 TYR A CG 1 ATOM 609 C CD1 . TYR A 1 79 ? 24.666 1.376 36.625 1.00 21.59 ? 79 TYR A CD1 1 ATOM 610 C CD2 . TYR A 1 79 ? 23.065 1.550 34.830 1.00 22.12 ? 79 TYR A CD2 1 ATOM 611 C CE1 . TYR A 1 79 ? 25.077 2.702 36.398 1.00 21.60 ? 79 TYR A CE1 1 ATOM 612 C CE2 . TYR A 1 79 ? 23.470 2.891 34.614 1.00 21.77 ? 79 TYR A CE2 1 ATOM 613 C CZ . TYR A 1 79 ? 24.480 3.434 35.380 1.00 22.95 ? 79 TYR A CZ 1 ATOM 614 O OH . TYR A 1 79 ? 24.869 4.725 35.163 1.00 22.82 ? 79 TYR A OH 1 ATOM 615 N N . HIS A 1 80 ? 24.875 -0.635 33.231 1.00 20.85 ? 80 HIS A N 1 ATOM 616 C CA . HIS A 1 80 ? 24.931 -0.128 31.856 1.00 21.66 ? 80 HIS A CA 1 ATOM 617 C C . HIS A 1 80 ? 25.385 -1.165 30.836 1.00 22.86 ? 80 HIS A C 1 ATOM 618 O O . HIS A 1 80 ? 25.189 -0.960 29.645 1.00 24.25 ? 80 HIS A O 1 ATOM 619 C CB . HIS A 1 80 ? 25.891 1.073 31.823 1.00 22.87 ? 80 HIS A CB 1 ATOM 620 C CG . HIS A 1 80 ? 27.157 0.822 32.573 1.00 22.92 ? 80 HIS A CG 1 ATOM 621 N ND1 . HIS A 1 80 ? 28.120 -0.048 32.108 1.00 21.73 ? 80 HIS A ND1 1 ATOM 622 C CD2 . HIS A 1 80 ? 27.614 1.297 33.763 1.00 23.97 ? 80 HIS A CD2 1 ATOM 623 C CE1 . HIS A 1 80 ? 29.108 -0.112 32.981 1.00 23.02 ? 80 HIS A CE1 1 ATOM 624 N NE2 . HIS A 1 80 ? 28.843 0.725 33.976 1.00 23.73 ? 80 HIS A NE2 1 ATOM 625 N N . GLY A 1 81 ? 25.978 -2.277 31.276 1.00 21.71 ? 81 GLY A N 1 ATOM 626 C CA . GLY A 1 81 ? 26.336 -3.362 30.342 1.00 21.25 ? 81 GLY A CA 1 ATOM 627 C C . GLY A 1 81 ? 27.729 -3.296 29.735 1.00 21.83 ? 81 GLY A C 1 ATOM 628 O O . GLY A 1 81 ? 28.082 -4.171 28.943 1.00 20.98 ? 81 GLY A O 1 ATOM 629 N N . TYR A 1 82 ? 28.521 -2.268 30.063 1.00 21.14 ? 82 TYR A N 1 ATOM 630 C CA . TYR A 1 82 ? 29.787 -2.088 29.327 1.00 21.50 ? 82 TYR A CA 1 ATOM 631 C C . TYR A 1 82 ? 31.023 -2.699 29.997 1.00 21.43 ? 82 TYR A C 1 ATOM 632 O O . TYR A 1 82 ? 32.154 -2.433 29.557 1.00 21.40 ? 82 TYR A O 1 ATOM 633 C CB . TYR A 1 82 ? 30.035 -0.598 29.024 1.00 22.82 ? 82 TYR A CB 1 ATOM 634 C CG . TYR A 1 82 ? 28.979 -0.003 28.108 1.00 22.15 ? 82 TYR A CG 1 ATOM 635 C CD1 . TYR A 1 82 ? 28.917 -0.334 26.751 1.00 21.91 ? 82 TYR A CD1 1 ATOM 636 C CD2 . TYR A 1 82 ? 28.001 0.874 28.592 1.00 23.61 ? 82 TYR A CD2 1 ATOM 637 C CE1 . TYR A 1 82 ? 27.926 0.189 25.912 1.00 22.77 ? 82 TYR A CE1 1 ATOM 638 C CE2 . TYR A 1 82 ? 27.026 1.417 27.734 1.00 25.62 ? 82 TYR A CE2 1 ATOM 639 C CZ . TYR A 1 82 ? 27.000 1.085 26.396 1.00 23.74 ? 82 TYR A CZ 1 ATOM 640 O OH . TYR A 1 82 ? 26.040 1.617 25.573 1.00 24.24 ? 82 TYR A OH 1 ATOM 641 N N . TRP A 1 83 ? 30.798 -3.465 31.070 1.00 20.60 ? 83 TRP A N 1 ATOM 642 C CA . TRP A 1 83 ? 31.854 -4.084 31.876 1.00 20.91 ? 83 TRP A CA 1 ATOM 643 C C . TRP A 1 83 ? 31.724 -5.617 31.883 1.00 20.51 ? 83 TRP A C 1 ATOM 644 O O . TRP A 1 83 ? 31.570 -6.221 32.948 1.00 20.87 ? 83 TRP A O 1 ATOM 645 C CB . TRP A 1 83 ? 31.731 -3.593 33.332 1.00 22.05 ? 83 TRP A CB 1 ATOM 646 C CG . TRP A 1 83 ? 31.967 -2.076 33.507 1.00 21.28 ? 83 TRP A CG 1 ATOM 647 C CD1 . TRP A 1 83 ? 32.527 -1.187 32.609 1.00 21.61 ? 83 TRP A CD1 1 ATOM 648 C CD2 . TRP A 1 83 ? 31.688 -1.319 34.696 1.00 21.98 ? 83 TRP A CD2 1 ATOM 649 N NE1 . TRP A 1 83 ? 32.572 0.101 33.172 1.00 22.43 ? 83 TRP A NE1 1 ATOM 650 C CE2 . TRP A 1 83 ? 32.068 0.023 34.449 1.00 21.98 ? 83 TRP A CE2 1 ATOM 651 C CE3 . TRP A 1 83 ? 31.135 -1.649 35.939 1.00 22.55 ? 83 TRP A CE3 1 ATOM 652 C CZ2 . TRP A 1 83 ? 31.924 1.029 35.412 1.00 23.20 ? 83 TRP A CZ2 1 ATOM 653 C CZ3 . TRP A 1 83 ? 30.952 -0.626 36.892 1.00 22.61 ? 83 TRP A CZ3 1 ATOM 654 C CH2 . TRP A 1 83 ? 31.354 0.672 36.626 1.00 22.32 ? 83 TRP A CH2 1 ATOM 655 N N . GLN A 1 84 ? 31.826 -6.245 30.717 1.00 20.72 ? 84 GLN A N 1 ATOM 656 C CA . GLN A 1 84 ? 31.499 -7.655 30.614 1.00 19.97 ? 84 GLN A CA 1 ATOM 657 C C . GLN A 1 84 ? 32.631 -8.509 31.189 1.00 20.48 ? 84 GLN A C 1 ATOM 658 O O . GLN A 1 84 ? 33.810 -8.091 31.230 1.00 21.01 ? 84 GLN A O 1 ATOM 659 C CB . GLN A 1 84 ? 31.203 -8.005 29.133 1.00 20.64 ? 84 GLN A CB 1 ATOM 660 C CG . GLN A 1 84 ? 32.446 -8.006 28.245 1.00 21.07 ? 84 GLN A CG 1 ATOM 661 C CD . GLN A 1 84 ? 32.047 -7.972 26.777 1.00 21.47 ? 84 GLN A CD 1 ATOM 662 O OE1 . GLN A 1 84 ? 30.938 -8.411 26.416 1.00 22.23 ? 84 GLN A OE1 1 ATOM 663 N NE2 . GLN A 1 84 ? 32.910 -7.398 25.932 1.00 21.91 ? 84 GLN A NE2 1 ATOM 664 N N . GLN A 1 85 ? 32.270 -9.720 31.607 1.00 21.13 ? 85 GLN A N 1 ATOM 665 C CA . GLN A 1 85 ? 33.227 -10.727 32.031 1.00 21.59 ? 85 GLN A CA 1 ATOM 666 C C . GLN A 1 85 ? 33.035 -12.090 31.405 1.00 22.50 ? 85 GLN A C 1 ATOM 667 O O . GLN A 1 85 ? 34.021 -12.773 31.223 1.00 23.93 ? 85 GLN A O 1 ATOM 668 C CB . GLN A 1 85 ? 33.320 -10.875 33.549 1.00 23.58 ? 85 GLN A CB 1 ATOM 669 C CG . GLN A 1 85 ? 33.977 -9.644 34.155 1.00 23.80 ? 85 GLN A CG 1 ATOM 670 C CD . GLN A 1 85 ? 34.373 -9.819 35.640 1.00 24.54 ? 85 GLN A CD 1 ATOM 671 O OE1 . GLN A 1 85 ? 33.845 -10.708 36.342 1.00 23.87 ? 85 GLN A OE1 1 ATOM 672 N NE2 . GLN A 1 85 ? 35.315 -8.948 36.122 1.00 21.99 ? 85 GLN A NE2 1 ATOM 673 N N . ASP A 1 86 ? 31.783 -12.505 31.149 1.00 22.82 ? 86 ASP A N 1 ATOM 674 C CA . ASP A 1 86 ? 31.519 -13.838 30.559 1.00 22.25 ? 86 ASP A CA 1 ATOM 675 C C . ASP A 1 86 ? 30.638 -13.684 29.339 1.00 23.03 ? 86 ASP A C 1 ATOM 676 O O . ASP A 1 86 ? 29.417 -13.480 29.471 1.00 23.24 ? 86 ASP A O 1 ATOM 677 C CB . ASP A 1 86 ? 30.810 -14.703 31.582 1.00 25.13 ? 86 ASP A CB 1 ATOM 678 C CG . ASP A 1 86 ? 30.406 -16.084 31.028 1.00 26.36 ? 86 ASP A CG 1 ATOM 679 O OD1 . ASP A 1 86 ? 30.614 -16.370 29.823 1.00 27.45 ? 86 ASP A OD1 1 ATOM 680 O OD2 . ASP A 1 86 ? 29.845 -16.874 31.816 1.00 29.23 ? 86 ASP A OD2 1 ATOM 681 N N . ILE A 1 87 ? 31.231 -13.732 28.137 1.00 22.87 ? 87 ILE A N 1 ATOM 682 C CA . ILE A 1 87 ? 30.496 -13.306 26.940 1.00 22.36 ? 87 ILE A CA 1 ATOM 683 C C . ILE A 1 87 ? 29.497 -14.374 26.456 1.00 22.43 ? 87 ILE A C 1 ATOM 684 O O . ILE A 1 87 ? 28.620 -14.095 25.636 1.00 22.23 ? 87 ILE A O 1 ATOM 685 C CB . ILE A 1 87 ? 31.443 -12.943 25.787 1.00 22.56 ? 87 ILE A CB 1 ATOM 686 C CG1 . ILE A 1 87 ? 32.154 -14.201 25.270 1.00 22.71 ? 87 ILE A CG1 1 ATOM 687 C CG2 . ILE A 1 87 ? 32.472 -11.884 26.234 1.00 23.92 ? 87 ILE A CG2 1 ATOM 688 C CD1 . ILE A 1 87 ? 33.062 -13.920 24.075 1.00 24.45 ? 87 ILE A CD1 1 ATOM 689 N N . TYR A 1 88 ? 29.629 -15.592 26.989 1.00 20.07 ? 88 TYR A N 1 ATOM 690 C CA . TYR A 1 88 ? 28.720 -16.667 26.638 1.00 20.58 ? 88 TYR A CA 1 ATOM 691 C C . TYR A 1 88 ? 27.584 -16.840 27.622 1.00 22.10 ? 88 TYR A C 1 ATOM 692 O O . TYR A 1 88 ? 26.796 -17.768 27.472 1.00 21.91 ? 88 TYR A O 1 ATOM 693 C CB . TYR A 1 88 ? 29.474 -17.990 26.418 1.00 22.62 ? 88 TYR A CB 1 ATOM 694 C CG . TYR A 1 88 ? 30.211 -17.935 25.108 1.00 24.02 ? 88 TYR A CG 1 ATOM 695 C CD1 . TYR A 1 88 ? 29.530 -18.000 23.900 1.00 23.23 ? 88 TYR A CD1 1 ATOM 696 C CD2 . TYR A 1 88 ? 31.586 -17.816 25.088 1.00 24.88 ? 88 TYR A CD2 1 ATOM 697 C CE1 . TYR A 1 88 ? 30.202 -17.912 22.718 1.00 24.21 ? 88 TYR A CE1 1 ATOM 698 C CE2 . TYR A 1 88 ? 32.271 -17.721 23.906 1.00 26.13 ? 88 TYR A CE2 1 ATOM 699 C CZ . TYR A 1 88 ? 31.565 -17.752 22.726 1.00 24.88 ? 88 TYR A CZ 1 ATOM 700 O OH . TYR A 1 88 ? 32.259 -17.665 21.531 1.00 27.32 ? 88 TYR A OH 1 ATOM 701 N N . SER A 1 89 ? 27.495 -15.942 28.610 1.00 22.73 ? 89 SER A N 1 ATOM 702 C CA . SER A 1 89 ? 26.344 -15.918 29.522 1.00 23.53 ? 89 SER A CA 1 ATOM 703 C C . SER A 1 89 ? 25.678 -14.571 29.373 1.00 22.00 ? 89 SER A C 1 ATOM 704 O O . SER A 1 89 ? 26.293 -13.609 28.883 1.00 21.81 ? 89 SER A O 1 ATOM 705 C CB . SER A 1 89 ? 26.789 -16.083 30.979 1.00 23.85 ? 89 SER A CB 1 ATOM 706 O OG . SER A 1 89 ? 27.233 -17.423 31.205 1.00 25.08 ? 89 SER A OG 1 ATOM 707 N N . LEU A 1 90 ? 24.418 -14.503 29.788 1.00 21.87 ? 90 LEU A N 1 ATOM 708 C CA . LEU A 1 90 ? 23.691 -13.225 29.753 1.00 20.26 ? 90 LEU A CA 1 ATOM 709 C C . LEU A 1 90 ? 23.645 -12.594 31.116 1.00 22.84 ? 90 LEU A C 1 ATOM 710 O O . LEU A 1 90 ? 23.837 -13.256 32.121 1.00 23.18 ? 90 LEU A O 1 ATOM 711 C CB . LEU A 1 90 ? 22.253 -13.467 29.276 1.00 21.97 ? 90 LEU A CB 1 ATOM 712 C CG . LEU A 1 90 ? 22.074 -13.996 27.854 1.00 21.96 ? 90 LEU A CG 1 ATOM 713 C CD1 . LEU A 1 90 ? 20.599 -14.365 27.657 1.00 24.60 ? 90 LEU A CD1 1 ATOM 714 C CD2 . LEU A 1 90 ? 22.538 -12.970 26.793 1.00 23.61 ? 90 LEU A CD2 1 ATOM 715 N N . ASN A 1 91 ? 23.375 -11.290 31.143 1.00 20.32 ? 91 ASN A N 1 ATOM 716 C CA . ASN A 1 91 ? 23.244 -10.544 32.393 1.00 21.34 ? 91 ASN A CA 1 ATOM 717 C C . ASN A 1 91 ? 21.891 -10.890 33.028 1.00 22.47 ? 91 ASN A C 1 ATOM 718 O O . ASN A 1 91 ? 20.840 -10.422 32.577 1.00 24.07 ? 91 ASN A O 1 ATOM 719 C CB . ASN A 1 91 ? 23.354 -9.035 32.115 1.00 20.08 ? 91 ASN A CB 1 ATOM 720 C CG . ASN A 1 91 ? 23.400 -8.225 33.397 1.00 21.67 ? 91 ASN A CG 1 ATOM 721 O OD1 . ASN A 1 91 ? 22.966 -8.717 34.441 1.00 22.21 ? 91 ASN A OD1 1 ATOM 722 N ND2 . ASN A 1 91 ? 23.957 -6.999 33.339 1.00 20.46 ? 91 ASN A ND2 1 ATOM 723 N N . GLU A 1 92 ? 21.936 -11.716 34.080 1.00 22.04 ? 92 GLU A N 1 ATOM 724 C CA . GLU A 1 92 ? 20.743 -12.219 34.756 1.00 24.62 ? 92 GLU A CA 1 ATOM 725 C C . GLU A 1 92 ? 19.829 -11.132 35.316 1.00 23.88 ? 92 GLU A C 1 ATOM 726 O O . GLU A 1 92 ? 18.661 -11.380 35.619 1.00 24.20 ? 92 GLU A O 1 ATOM 727 C CB . GLU A 1 92 ? 21.174 -13.123 35.916 1.00 28.47 ? 92 GLU A CB 1 ATOM 728 C CG . GLU A 1 92 ? 20.023 -13.920 36.530 1.00 35.28 ? 92 GLU A CG 1 ATOM 729 C CD . GLU A 1 92 ? 20.125 -15.421 36.263 1.00 39.05 ? 92 GLU A CD 1 ATOM 730 O OE1 . GLU A 1 92 ? 19.476 -15.922 35.285 1.00 40.63 ? 92 GLU A OE1 1 ATOM 731 O OE2 . GLU A 1 92 ? 20.862 -16.092 37.050 1.00 40.61 ? 92 GLU A OE2 1 ATOM 732 N N . ASN A 1 93 ? 20.377 -9.937 35.512 1.00 23.49 ? 93 ASN A N 1 ATOM 733 C CA . ASN A 1 93 ? 19.556 -8.855 35.990 1.00 22.51 ? 93 ASN A CA 1 ATOM 734 C C . ASN A 1 93 ? 18.423 -8.558 35.023 1.00 24.10 ? 93 ASN A C 1 ATOM 735 O O . ASN A 1 93 ? 17.349 -8.080 35.442 1.00 24.73 ? 93 ASN A O 1 ATOM 736 C CB . ASN A 1 93 ? 20.417 -7.614 36.160 1.00 23.18 ? 93 ASN A CB 1 ATOM 737 C CG . ASN A 1 93 ? 21.297 -7.713 37.363 1.00 23.70 ? 93 ASN A CG 1 ATOM 738 O OD1 . ASN A 1 93 ? 22.484 -8.127 37.262 1.00 25.82 ? 93 ASN A OD1 1 ATOM 739 N ND2 . ASN A 1 93 ? 20.753 -7.352 38.526 1.00 22.39 ? 93 ASN A ND2 1 ATOM 740 N N . TYR A 1 94 ? 18.668 -8.782 33.724 1.00 22.14 ? 94 TYR A N 1 ATOM 741 C CA . TYR A 1 94 ? 17.659 -8.380 32.730 1.00 21.62 ? 94 TYR A CA 1 ATOM 742 C C . TYR A 1 94 ? 16.671 -9.453 32.382 1.00 23.17 ? 94 TYR A C 1 ATOM 743 O O . TYR A 1 94 ? 15.669 -9.181 31.721 1.00 21.02 ? 94 TYR A O 1 ATOM 744 C CB . TYR A 1 94 ? 18.321 -7.903 31.433 1.00 22.48 ? 94 TYR A CB 1 ATOM 745 C CG . TYR A 1 94 ? 19.424 -6.902 31.632 1.00 21.42 ? 94 TYR A CG 1 ATOM 746 C CD1 . TYR A 1 94 ? 19.300 -5.846 32.540 1.00 21.16 ? 94 TYR A CD1 1 ATOM 747 C CD2 . TYR A 1 94 ? 20.576 -6.981 30.842 1.00 22.52 ? 94 TYR A CD2 1 ATOM 748 C CE1 . TYR A 1 94 ? 20.353 -4.896 32.697 1.00 21.45 ? 94 TYR A CE1 1 ATOM 749 C CE2 . TYR A 1 94 ? 21.615 -6.065 30.985 1.00 22.07 ? 94 TYR A CE2 1 ATOM 750 C CZ . TYR A 1 94 ? 21.495 -5.017 31.886 1.00 22.17 ? 94 TYR A CZ 1 ATOM 751 O OH . TYR A 1 94 ? 22.544 -4.129 32.001 1.00 21.60 ? 94 TYR A OH 1 ATOM 752 N N . GLY A 1 95 ? 16.957 -10.684 32.809 1.00 22.11 ? 95 GLY A N 1 ATOM 753 C CA . GLY A 1 95 ? 16.128 -11.854 32.462 1.00 23.37 ? 95 GLY A CA 1 ATOM 754 C C . GLY A 1 95 ? 16.961 -13.036 31.997 1.00 24.00 ? 95 GLY A C 1 ATOM 755 O O . GLY A 1 95 ? 18.144 -13.127 32.267 1.00 24.83 ? 95 GLY A O 1 ATOM 756 N N . THR A 1 96 ? 16.323 -13.940 31.274 1.00 24.62 ? 96 THR A N 1 ATOM 757 C CA . THR A 1 96 ? 16.933 -15.170 30.831 1.00 24.70 ? 96 THR A CA 1 ATOM 758 C C . THR A 1 96 ? 17.092 -15.147 29.318 1.00 24.84 ? 96 THR A C 1 ATOM 759 O O . THR A 1 96 ? 16.584 -14.239 28.630 1.00 22.69 ? 96 THR A O 1 ATOM 760 C CB . THR A 1 96 ? 16.003 -16.376 31.126 1.00 26.44 ? 96 THR A CB 1 ATOM 761 O OG1 . THR A 1 96 ? 14.789 -16.200 30.394 1.00 26.38 ? 96 THR A OG1 1 ATOM 762 C CG2 . THR A 1 96 ? 15.661 -16.476 32.623 1.00 26.91 ? 96 THR A CG2 1 ATOM 763 N N . ALA A 1 97 ? 17.740 -16.180 28.787 1.00 23.80 ? 97 ALA A N 1 ATOM 764 C CA . ALA A 1 97 ? 17.842 -16.302 27.330 1.00 23.64 ? 97 ALA A CA 1 ATOM 765 C C . ALA A 1 97 ? 16.460 -16.282 26.699 1.00 23.09 ? 97 ALA A C 1 ATOM 766 O O . ALA A 1 97 ? 16.241 -15.662 25.643 1.00 23.32 ? 97 ALA A O 1 ATOM 767 C CB . ALA A 1 97 ? 18.625 -17.551 26.927 1.00 25.63 ? 97 ALA A CB 1 ATOM 768 N N . ASP A 1 98 ? 15.514 -16.943 27.345 1.00 24.45 ? 98 ASP A N 1 ATOM 769 C CA . ASP A 1 98 ? 14.176 -17.015 26.800 1.00 25.38 ? 98 ASP A CA 1 ATOM 770 C C . ASP A 1 98 ? 13.535 -15.634 26.749 1.00 24.06 ? 98 ASP A C 1 ATOM 771 O O . ASP A 1 98 ? 12.783 -15.328 25.837 1.00 23.37 ? 98 ASP A O 1 ATOM 772 C CB . ASP A 1 98 ? 13.316 -17.988 27.597 1.00 27.50 ? 98 ASP A CB 1 ATOM 773 C CG . ASP A 1 98 ? 13.704 -19.437 27.356 1.00 31.94 ? 98 ASP A CG 1 ATOM 774 O OD1 . ASP A 1 98 ? 14.462 -19.693 26.408 1.00 33.26 ? 98 ASP A OD1 1 ATOM 775 O OD2 . ASP A 1 98 ? 13.295 -20.375 28.062 1.00 32.90 ? 98 ASP A OD2 1 ATOM 776 N N . ASP A 1 99 ? 13.863 -14.794 27.725 1.00 23.86 ? 99 ASP A N 1 ATOM 777 C CA . ASP A 1 99 ? 13.299 -13.436 27.751 1.00 22.88 ? 99 ASP A CA 1 ATOM 778 C C . ASP A 1 99 ? 13.875 -12.590 26.608 1.00 22.77 ? 99 ASP A C 1 ATOM 779 O O . ASP A 1 99 ? 13.164 -11.799 25.982 1.00 23.37 ? 99 ASP A O 1 ATOM 780 C CB . ASP A 1 99 ? 13.598 -12.755 29.089 1.00 24.19 ? 99 ASP A CB 1 ATOM 781 C CG . ASP A 1 99 ? 12.868 -13.402 30.273 1.00 26.63 ? 99 ASP A CG 1 ATOM 782 O OD1 . ASP A 1 99 ? 11.742 -13.984 30.098 1.00 25.76 ? 99 ASP A OD1 1 ATOM 783 O OD2 . ASP A 1 99 ? 13.399 -13.282 31.410 1.00 29.08 ? 99 ASP A OD2 1 ATOM 784 N N . LEU A 1 100 ? 15.166 -12.737 26.333 1.00 21.63 ? 100 LEU A N 1 ATOM 785 C CA . LEU A 1 100 ? 15.787 -11.937 25.255 1.00 22.42 ? 100 LEU A CA 1 ATOM 786 C C . LEU A 1 100 ? 15.225 -12.393 23.927 1.00 21.92 ? 100 LEU A C 1 ATOM 787 O O . LEU A 1 100 ? 14.930 -11.562 23.077 1.00 24.14 ? 100 LEU A O 1 ATOM 788 C CB . LEU A 1 100 ? 17.321 -12.047 25.285 1.00 21.97 ? 100 LEU A CB 1 ATOM 789 C CG . LEU A 1 100 ? 18.076 -11.214 24.244 1.00 21.70 ? 100 LEU A CG 1 ATOM 790 C CD1 . LEU A 1 100 ? 17.698 -9.741 24.219 1.00 21.21 ? 100 LEU A CD1 1 ATOM 791 C CD2 . LEU A 1 100 ? 19.562 -11.369 24.483 1.00 20.64 ? 100 LEU A CD2 1 ATOM 792 N N . LYS A 1 101 ? 15.066 -13.706 23.743 1.00 22.65 ? 101 LYS A N 1 ATOM 793 C CA . LYS A 1 101 ? 14.410 -14.220 22.537 1.00 21.96 ? 101 LYS A CA 1 ATOM 794 C C . LYS A 1 101 ? 12.956 -13.725 22.433 1.00 21.39 ? 101 LYS A C 1 ATOM 795 O O . LYS A 1 101 ? 12.480 -13.450 21.353 1.00 22.40 ? 101 LYS A O 1 ATOM 796 C CB . LYS A 1 101 ? 14.449 -15.754 22.467 1.00 23.33 ? 101 LYS A CB 1 ATOM 797 C CG . LYS A 1 101 ? 15.877 -16.284 22.402 1.00 24.10 ? 101 LYS A CG 1 ATOM 798 C CD . LYS A 1 101 ? 15.900 -17.793 22.517 1.00 26.09 ? 101 LYS A CD 1 ATOM 799 C CE . LYS A 1 101 ? 17.339 -18.293 22.441 1.00 27.85 ? 101 LYS A CE 1 ATOM 800 N NZ . LYS A 1 101 ? 17.360 -19.760 22.467 1.00 30.48 ? 101 LYS A NZ 1 ATOM 801 N N . ALA A 1 102 ? 12.261 -13.626 23.556 1.00 21.80 ? 102 ALA A N 1 ATOM 802 C CA . ALA A 1 102 ? 10.888 -13.105 23.571 1.00 22.63 ? 102 ALA A CA 1 ATOM 803 C C . ALA A 1 102 ? 10.799 -11.655 23.142 1.00 22.41 ? 102 ALA A C 1 ATOM 804 O O . ALA A 1 102 ? 9.817 -11.246 22.495 1.00 22.22 ? 102 ALA A O 1 ATOM 805 C CB . ALA A 1 102 ? 10.238 -13.292 24.962 1.00 25.35 ? 102 ALA A CB 1 ATOM 806 N N . LEU A 1 103 ? 11.805 -10.879 23.532 1.00 20.25 ? 103 LEU A N 1 ATOM 807 C CA . LEU A 1 103 ? 11.879 -9.466 23.140 1.00 21.86 ? 103 LEU A CA 1 ATOM 808 C C . LEU A 1 103 ? 12.055 -9.364 21.621 1.00 20.76 ? 103 LEU A C 1 ATOM 809 O O . LEU A 1 103 ? 11.334 -8.626 20.962 1.00 20.94 ? 103 LEU A O 1 ATOM 810 C CB . LEU A 1 103 ? 13.018 -8.756 23.893 1.00 20.84 ? 103 LEU A CB 1 ATOM 811 C CG . LEU A 1 103 ? 13.325 -7.337 23.453 1.00 21.54 ? 103 LEU A CG 1 ATOM 812 C CD1 . LEU A 1 103 ? 12.076 -6.447 23.545 1.00 21.11 ? 103 LEU A CD1 1 ATOM 813 C CD2 . LEU A 1 103 ? 14.517 -6.772 24.287 1.00 21.66 ? 103 LEU A CD2 1 ATOM 814 N N . SER A 1 104 ? 13.003 -10.104 21.053 1.00 22.13 ? 104 SER A N 1 ATOM 815 C CA . SER A 1 104 ? 13.223 -10.030 19.604 1.00 21.70 ? 104 SER A CA 1 ATOM 816 C C . SER A 1 104 ? 11.955 -10.467 18.866 1.00 22.00 ? 104 SER A C 1 ATOM 817 O O . SER A 1 104 ? 11.541 -9.827 17.897 1.00 22.38 ? 104 SER A O 1 ATOM 818 C CB . SER A 1 104 ? 14.434 -10.878 19.172 1.00 25.84 ? 104 SER A CB 1 ATOM 819 O OG . SER A 1 104 ? 14.248 -12.200 19.578 1.00 30.08 ? 104 SER A OG 1 ATOM 820 N N . SER A 1 105 ? 11.339 -11.539 19.356 1.00 20.27 ? 105 SER A N 1 ATOM 821 C CA . SER A 1 105 ? 10.078 -12.021 18.795 1.00 21.60 ? 105 SER A CA 1 ATOM 822 C C . SER A 1 105 ? 8.983 -10.957 18.840 1.00 20.78 ? 105 SER A C 1 ATOM 823 O O . SER A 1 105 ? 8.256 -10.733 17.878 1.00 22.98 ? 105 SER A O 1 ATOM 824 C CB . SER A 1 105 ? 9.597 -13.265 19.552 1.00 22.52 ? 105 SER A CB 1 ATOM 825 O OG . SER A 1 105 ? 8.468 -13.794 18.914 1.00 28.14 ? 105 SER A OG 1 ATOM 826 N N . ALA A 1 106 ? 8.833 -10.329 19.990 1.00 20.87 ? 106 ALA A N 1 ATOM 827 C CA . ALA A 1 106 ? 7.791 -9.310 20.131 1.00 20.39 ? 106 ALA A CA 1 ATOM 828 C C . ALA A 1 106 ? 8.009 -8.155 19.158 1.00 21.90 ? 106 ALA A C 1 ATOM 829 O O . ALA A 1 106 ? 7.050 -7.593 18.621 1.00 22.31 ? 106 ALA A O 1 ATOM 830 C CB . ALA A 1 106 ? 7.777 -8.777 21.562 1.00 20.65 ? 106 ALA A CB 1 ATOM 831 N N . LEU A 1 107 ? 9.264 -7.757 18.970 1.00 19.97 ? 107 LEU A N 1 ATOM 832 C CA . LEU A 1 107 ? 9.540 -6.671 18.038 1.00 20.56 ? 107 LEU A CA 1 ATOM 833 C C . LEU A 1 107 ? 9.195 -7.094 16.621 1.00 20.29 ? 107 LEU A C 1 ATOM 834 O O . LEU A 1 107 ? 8.568 -6.349 15.827 1.00 20.91 ? 107 LEU A O 1 ATOM 835 C CB . LEU A 1 107 ? 11.018 -6.250 18.123 1.00 20.45 ? 107 LEU A CB 1 ATOM 836 C CG . LEU A 1 107 ? 11.350 -5.443 19.380 1.00 19.18 ? 107 LEU A CG 1 ATOM 837 C CD1 . LEU A 1 107 ? 12.827 -5.623 19.741 1.00 20.96 ? 107 LEU A CD1 1 ATOM 838 C CD2 . LEU A 1 107 ? 11.035 -3.973 19.065 1.00 22.07 ? 107 LEU A CD2 1 ATOM 839 N N . HIS A 1 108 ? 9.566 -8.329 16.294 1.00 18.53 ? 108 HIS A N 1 ATOM 840 C CA . HIS A 1 108 ? 9.294 -8.831 14.957 1.00 19.76 ? 108 HIS A CA 1 ATOM 841 C C . HIS A 1 108 ? 7.818 -8.920 14.627 1.00 20.80 ? 108 HIS A C 1 ATOM 842 O O . HIS A 1 108 ? 7.417 -8.661 13.486 1.00 22.99 ? 108 HIS A O 1 ATOM 843 C CB . HIS A 1 108 ? 10.010 -10.151 14.766 1.00 20.43 ? 108 HIS A CB 1 ATOM 844 C CG . HIS A 1 108 ? 11.491 -9.993 14.835 1.00 21.52 ? 108 HIS A CG 1 ATOM 845 N ND1 . HIS A 1 108 ? 12.355 -11.050 15.035 1.00 23.33 ? 108 HIS A ND1 1 ATOM 846 C CD2 . HIS A 1 108 ? 12.259 -8.887 14.708 1.00 22.83 ? 108 HIS A CD2 1 ATOM 847 C CE1 . HIS A 1 108 ? 13.596 -10.588 15.072 1.00 23.37 ? 108 HIS A CE1 1 ATOM 848 N NE2 . HIS A 1 108 ? 13.564 -9.284 14.852 1.00 22.54 ? 108 HIS A NE2 1 ATOM 849 N N . GLU A 1 109 ? 6.995 -9.275 15.609 1.00 22.14 ? 109 GLU A N 1 ATOM 850 C CA . GLU A 1 109 ? 5.550 -9.369 15.394 1.00 24.27 ? 109 GLU A CA 1 ATOM 851 C C . GLU A 1 109 ? 4.939 -8.002 15.088 1.00 24.68 ? 109 GLU A C 1 ATOM 852 O O . GLU A 1 109 ? 3.845 -7.902 14.532 1.00 23.82 ? 109 GLU A O 1 ATOM 853 C CB . GLU A 1 109 ? 4.866 -9.990 16.614 1.00 26.59 ? 109 GLU A CB 1 ATOM 854 C CG . GLU A 1 109 ? 5.207 -11.454 16.839 1.00 31.50 ? 109 GLU A CG 1 ATOM 855 C CD . GLU A 1 109 ? 4.554 -12.019 18.085 1.00 34.75 ? 109 GLU A CD 1 ATOM 856 O OE1 . GLU A 1 109 ? 3.868 -11.256 18.797 1.00 38.17 ? 109 GLU A OE1 1 ATOM 857 O OE2 . GLU A 1 109 ? 4.727 -13.226 18.353 1.00 36.17 ? 109 GLU A OE2 1 ATOM 858 N N . ARG A 1 110 ? 5.666 -6.956 15.460 1.00 22.36 ? 110 ARG A N 1 ATOM 859 C CA . ARG A 1 110 ? 5.242 -5.552 15.277 1.00 23.72 ? 110 ARG A CA 1 ATOM 860 C C . ARG A 1 110 ? 5.906 -4.928 14.050 1.00 23.84 ? 110 ARG A C 1 ATOM 861 O O . ARG A 1 110 ? 5.736 -3.730 13.780 1.00 23.71 ? 110 ARG A O 1 ATOM 862 C CB . ARG A 1 110 ? 5.618 -4.695 16.498 1.00 24.16 ? 110 ARG A CB 1 ATOM 863 C CG . ARG A 1 110 ? 4.843 -5.029 17.792 1.00 23.72 ? 110 ARG A CG 1 ATOM 864 C CD . ARG A 1 110 ? 5.487 -4.393 19.005 1.00 25.25 ? 110 ARG A CD 1 ATOM 865 N NE . ARG A 1 110 ? 4.687 -4.653 20.198 1.00 24.90 ? 110 ARG A NE 1 ATOM 866 C CZ . ARG A 1 110 ? 3.727 -3.844 20.622 1.00 26.07 ? 110 ARG A CZ 1 ATOM 867 N NH1 . ARG A 1 110 ? 3.490 -2.711 19.978 1.00 26.95 ? 110 ARG A NH1 1 ATOM 868 N NH2 . ARG A 1 110 ? 3.034 -4.149 21.703 1.00 25.43 ? 110 ARG A NH2 1 ATOM 869 N N . GLY A 1 111 ? 6.667 -5.741 13.322 1.00 21.91 ? 111 GLY A N 1 ATOM 870 C CA . GLY A 1 111 ? 7.402 -5.260 12.159 1.00 23.88 ? 111 GLY A CA 1 ATOM 871 C C . GLY A 1 111 ? 8.523 -4.290 12.552 1.00 25.20 ? 111 GLY A C 1 ATOM 872 O O . GLY A 1 111 ? 8.870 -3.376 11.776 1.00 26.64 ? 111 GLY A O 1 ATOM 873 N N . MET A 1 112 ? 9.081 -4.506 13.744 1.00 24.10 ? 112 MET A N 1 ATOM 874 C CA . MET A 1 112 ? 10.188 -3.704 14.270 1.00 21.31 ? 112 MET A CA 1 ATOM 875 C C . MET A 1 112 ? 11.484 -4.523 14.322 1.00 21.26 ? 112 MET A C 1 ATOM 876 O O . MET A 1 112 ? 11.461 -5.755 14.185 1.00 22.73 ? 112 MET A O 1 ATOM 877 C CB . MET A 1 112 ? 9.853 -3.161 15.665 1.00 21.24 ? 112 MET A CB 1 ATOM 878 C CG . MET A 1 112 ? 8.607 -2.261 15.685 1.00 20.28 ? 112 MET A CG 1 ATOM 879 S SD . MET A 1 112 ? 8.144 -1.730 17.366 1.00 23.69 ? 112 MET A SD 1 ATOM 880 C CE . MET A 1 112 ? 9.456 -0.542 17.727 1.00 22.04 ? 112 MET A CE 1 ATOM 881 N N . TYR A 1 113 ? 12.612 -3.815 14.485 1.00 20.91 ? 113 TYR A N 1 ATOM 882 C CA . TYR A 1 113 ? 13.915 -4.461 14.566 1.00 21.16 ? 113 TYR A CA 1 ATOM 883 C C . TYR A 1 113 ? 14.486 -4.320 15.968 1.00 20.34 ? 113 TYR A C 1 ATOM 884 O O . TYR A 1 113 ? 14.200 -3.357 16.703 1.00 21.05 ? 113 TYR A O 1 ATOM 885 C CB . TYR A 1 113 ? 14.922 -3.810 13.617 1.00 22.29 ? 113 TYR A CB 1 ATOM 886 C CG . TYR A 1 113 ? 14.745 -4.085 12.142 1.00 22.30 ? 113 TYR A CG 1 ATOM 887 C CD1 . TYR A 1 113 ? 14.024 -5.172 11.686 1.00 23.63 ? 113 TYR A CD1 1 ATOM 888 C CD2 . TYR A 1 113 ? 15.395 -3.285 11.215 1.00 23.32 ? 113 TYR A CD2 1 ATOM 889 C CE1 . TYR A 1 113 ? 13.922 -5.445 10.303 1.00 22.54 ? 113 TYR A CE1 1 ATOM 890 C CE2 . TYR A 1 113 ? 15.286 -3.501 9.885 1.00 22.80 ? 113 TYR A CE2 1 ATOM 891 C CZ . TYR A 1 113 ? 14.543 -4.585 9.418 1.00 22.52 ? 113 TYR A CZ 1 ATOM 892 O OH . TYR A 1 113 ? 14.424 -4.816 8.066 1.00 24.91 ? 113 TYR A OH 1 ATOM 893 N N . LEU A 1 114 ? 15.334 -5.291 16.308 1.00 20.17 ? 114 LEU A N 1 ATOM 894 C CA . LEU A 1 114 ? 16.107 -5.236 17.550 1.00 21.17 ? 114 LEU A CA 1 ATOM 895 C C . LEU A 1 114 ? 17.559 -4.962 17.186 1.00 20.43 ? 114 LEU A C 1 ATOM 896 O O . LEU A 1 114 ? 18.148 -5.690 16.379 1.00 21.73 ? 114 LEU A O 1 ATOM 897 C CB . LEU A 1 114 ? 16.044 -6.601 18.240 1.00 22.24 ? 114 LEU A CB 1 ATOM 898 C CG . LEU A 1 114 ? 16.987 -6.720 19.461 1.00 22.07 ? 114 LEU A CG 1 ATOM 899 C CD1 . LEU A 1 114 ? 16.675 -5.659 20.522 1.00 23.86 ? 114 LEU A CD1 1 ATOM 900 C CD2 . LEU A 1 114 ? 16.878 -8.162 20.074 1.00 22.80 ? 114 LEU A CD2 1 ATOM 901 N N . MET A 1 115 ? 18.113 -3.909 17.763 1.00 19.90 ? 115 MET A N 1 ATOM 902 C CA . MET A 1 115 ? 19.544 -3.636 17.673 1.00 19.53 ? 115 MET A CA 1 ATOM 903 C C . MET A 1 115 ? 20.128 -3.820 19.074 1.00 20.01 ? 115 MET A C 1 ATOM 904 O O . MET A 1 115 ? 19.584 -3.307 20.040 1.00 20.05 ? 115 MET A O 1 ATOM 905 C CB . MET A 1 115 ? 19.757 -2.205 17.181 1.00 21.24 ? 115 MET A CB 1 ATOM 906 C CG . MET A 1 115 ? 21.196 -1.728 17.263 1.00 21.16 ? 115 MET A CG 1 ATOM 907 S SD . MET A 1 115 ? 21.490 -0.121 16.441 1.00 22.89 ? 115 MET A SD 1 ATOM 908 C CE . MET A 1 115 ? 21.506 -0.637 14.723 1.00 21.84 ? 115 MET A CE 1 ATOM 909 N N . VAL A 1 116 ? 21.236 -4.550 19.150 1.00 20.61 ? 116 VAL A N 1 ATOM 910 C CA . VAL A 1 116 ? 21.913 -4.810 20.415 1.00 20.97 ? 116 VAL A CA 1 ATOM 911 C C . VAL A 1 116 ? 23.309 -4.181 20.432 1.00 20.68 ? 116 VAL A C 1 ATOM 912 O O . VAL A 1 116 ? 24.041 -4.256 19.456 1.00 20.02 ? 116 VAL A O 1 ATOM 913 C CB . VAL A 1 116 ? 22.010 -6.299 20.646 1.00 21.25 ? 116 VAL A CB 1 ATOM 914 C CG1 . VAL A 1 116 ? 22.954 -6.658 21.821 1.00 22.12 ? 116 VAL A CG1 1 ATOM 915 C CG2 . VAL A 1 116 ? 20.594 -6.865 20.856 1.00 21.58 ? 116 VAL A CG2 1 ATOM 916 N N . ASP A 1 117 ? 23.612 -3.530 21.559 1.00 19.73 ? 117 ASP A N 1 ATOM 917 C CA . ASP A 1 117 ? 24.898 -2.887 21.789 1.00 19.26 ? 117 ASP A CA 1 ATOM 918 C C . ASP A 1 117 ? 25.930 -4.002 22.109 1.00 20.49 ? 117 ASP A C 1 ATOM 919 O O . ASP A 1 117 ? 25.650 -4.892 22.959 1.00 21.60 ? 117 ASP A O 1 ATOM 920 C CB . ASP A 1 117 ? 24.702 -1.963 23.006 1.00 20.37 ? 117 ASP A CB 1 ATOM 921 C CG . ASP A 1 117 ? 25.687 -0.812 23.073 1.00 24.88 ? 117 ASP A CG 1 ATOM 922 O OD1 . ASP A 1 117 ? 26.876 -0.945 22.705 1.00 25.31 ? 117 ASP A OD1 1 ATOM 923 O OD2 . ASP A 1 117 ? 25.220 0.239 23.588 1.00 24.53 ? 117 ASP A OD2 1 ATOM 924 N N . VAL A 1 118 ? 27.116 -3.952 21.488 1.00 19.90 ? 118 VAL A N 1 ATOM 925 C CA . VAL A 1 118 ? 28.149 -4.960 21.774 1.00 19.08 ? 118 VAL A CA 1 ATOM 926 C C . VAL A 1 118 ? 29.487 -4.280 21.977 1.00 20.39 ? 118 VAL A C 1 ATOM 927 O O . VAL A 1 118 ? 29.778 -3.260 21.343 1.00 20.10 ? 118 VAL A O 1 ATOM 928 C CB . VAL A 1 118 ? 28.276 -6.004 20.632 1.00 21.02 ? 118 VAL A CB 1 ATOM 929 C CG1 . VAL A 1 118 ? 26.957 -6.851 20.524 1.00 20.44 ? 118 VAL A CG1 1 ATOM 930 C CG2 . VAL A 1 118 ? 28.566 -5.308 19.302 1.00 19.97 ? 118 VAL A CG2 1 ATOM 931 N N . VAL A 1 119 ? 30.292 -4.854 22.869 1.00 20.27 ? 119 VAL A N 1 ATOM 932 C CA . VAL A 1 119 ? 31.643 -4.356 23.116 1.00 19.18 ? 119 VAL A CA 1 ATOM 933 C C . VAL A 1 119 ? 32.637 -5.457 22.688 1.00 20.56 ? 119 VAL A C 1 ATOM 934 O O . VAL A 1 119 ? 32.474 -6.594 23.086 1.00 20.60 ? 119 VAL A O 1 ATOM 935 C CB . VAL A 1 119 ? 31.856 -4.120 24.636 1.00 20.61 ? 119 VAL A CB 1 ATOM 936 C CG1 . VAL A 1 119 ? 33.286 -3.683 24.881 1.00 22.57 ? 119 VAL A CG1 1 ATOM 937 C CG2 . VAL A 1 119 ? 30.905 -2.998 25.188 1.00 20.57 ? 119 VAL A CG2 1 ATOM 938 N N . ALA A 1 120 ? 33.636 -5.090 21.889 1.00 20.30 ? 120 ALA A N 1 ATOM 939 C CA . ALA A 1 120 ? 34.710 -6.027 21.520 1.00 20.70 ? 120 ALA A CA 1 ATOM 940 C C . ALA A 1 120 ? 36.023 -5.570 22.141 1.00 20.12 ? 120 ALA A C 1 ATOM 941 O O . ALA A 1 120 ? 36.952 -6.362 22.274 1.00 19.66 ? 120 ALA A O 1 ATOM 942 C CB . ALA A 1 120 ? 34.859 -6.079 20.003 1.00 21.84 ? 120 ALA A CB 1 ATOM 943 N N . ASN A 1 121 ? 36.096 -4.283 22.481 1.00 18.76 ? 121 ASN A N 1 ATOM 944 C CA . ASN A 1 121 ? 37.376 -3.702 22.908 1.00 18.77 ? 121 ASN A CA 1 ATOM 945 C C . ASN A 1 121 ? 37.889 -4.246 24.248 1.00 20.79 ? 121 ASN A C 1 ATOM 946 O O . ASN A 1 121 ? 39.106 -4.405 24.426 1.00 19.04 ? 121 ASN A O 1 ATOM 947 C CB . ASN A 1 121 ? 37.205 -2.180 23.012 1.00 19.31 ? 121 ASN A CB 1 ATOM 948 C CG . ASN A 1 121 ? 38.476 -1.479 23.390 1.00 20.77 ? 121 ASN A CG 1 ATOM 949 O OD1 . ASN A 1 121 ? 39.443 -1.435 22.604 1.00 20.59 ? 121 ASN A OD1 1 ATOM 950 N ND2 . ASN A 1 121 ? 38.490 -0.904 24.599 1.00 20.42 ? 121 ASN A ND2 1 ATOM 951 N N . HIS A 1 122 ? 36.987 -4.505 25.198 1.00 19.08 ? 122 HIS A N 1 ATOM 952 C CA . HIS A 1 122 ? 37.426 -4.677 26.588 1.00 19.88 ? 122 HIS A CA 1 ATOM 953 C C . HIS A 1 122 ? 36.477 -5.533 27.418 1.00 19.64 ? 122 HIS A C 1 ATOM 954 O O . HIS A 1 122 ? 35.251 -5.668 27.109 1.00 20.70 ? 122 HIS A O 1 ATOM 955 C CB . HIS A 1 122 ? 37.627 -3.295 27.243 1.00 19.97 ? 122 HIS A CB 1 ATOM 956 C CG . HIS A 1 122 ? 36.370 -2.464 27.289 1.00 20.94 ? 122 HIS A CG 1 ATOM 957 N ND1 . HIS A 1 122 ? 36.078 -1.509 26.332 1.00 21.92 ? 122 HIS A ND1 1 ATOM 958 C CD2 . HIS A 1 122 ? 35.334 -2.454 28.165 1.00 21.24 ? 122 HIS A CD2 1 ATOM 959 C CE1 . HIS A 1 122 ? 34.905 -0.955 26.619 1.00 22.74 ? 122 HIS A CE1 1 ATOM 960 N NE2 . HIS A 1 122 ? 34.432 -1.518 27.722 1.00 21.47 ? 122 HIS A NE2 1 ATOM 961 N N . MET A 1 123 ? 37.046 -6.070 28.490 1.00 19.53 ? 123 MET A N 1 ATOM 962 C CA . MET A 1 123 ? 36.271 -6.639 29.595 1.00 20.51 ? 123 MET A CA 1 ATOM 963 C C . MET A 1 123 ? 36.229 -5.561 30.684 1.00 21.51 ? 123 MET A C 1 ATOM 964 O O . MET A 1 123 ? 36.787 -4.469 30.515 1.00 22.58 ? 123 MET A O 1 ATOM 965 C CB . MET A 1 123 ? 36.963 -7.907 30.088 1.00 21.89 ? 123 MET A CB 1 ATOM 966 C CG . MET A 1 123 ? 37.398 -8.851 28.928 1.00 23.31 ? 123 MET A CG 1 ATOM 967 S SD . MET A 1 123 ? 36.023 -9.474 27.885 1.00 29.76 ? 123 MET A SD 1 ATOM 968 C CE . MET A 1 123 ? 35.389 -10.395 29.153 1.00 24.91 ? 123 MET A CE 1 ATOM 969 N N . GLY A 1 124 ? 35.523 -5.825 31.781 1.00 22.12 ? 124 GLY A N 1 ATOM 970 C CA . GLY A 1 124 ? 35.557 -4.903 32.941 1.00 20.86 ? 124 GLY A CA 1 ATOM 971 C C . GLY A 1 124 ? 36.060 -5.622 34.180 1.00 21.02 ? 124 GLY A C 1 ATOM 972 O O . GLY A 1 124 ? 35.869 -6.830 34.299 1.00 21.99 ? 124 GLY A O 1 ATOM 973 N N . TYR A 1 125 ? 36.738 -4.904 35.090 1.00 21.67 ? 125 TYR A N 1 ATOM 974 C CA . TYR A 1 125 ? 37.268 -5.553 36.290 1.00 21.16 ? 125 TYR A CA 1 ATOM 975 C C . TYR A 1 125 ? 37.179 -4.615 37.509 1.00 21.47 ? 125 TYR A C 1 ATOM 976 O O . TYR A 1 125 ? 37.516 -3.433 37.424 1.00 23.23 ? 125 TYR A O 1 ATOM 977 C CB . TYR A 1 125 ? 38.712 -5.985 36.071 1.00 23.01 ? 125 TYR A CB 1 ATOM 978 C CG . TYR A 1 125 ? 39.231 -6.878 37.159 1.00 24.01 ? 125 TYR A CG 1 ATOM 979 C CD1 . TYR A 1 125 ? 38.884 -8.213 37.182 1.00 24.19 ? 125 TYR A CD1 1 ATOM 980 C CD2 . TYR A 1 125 ? 40.005 -6.362 38.188 1.00 25.68 ? 125 TYR A CD2 1 ATOM 981 C CE1 . TYR A 1 125 ? 39.347 -9.055 38.190 1.00 24.08 ? 125 TYR A CE1 1 ATOM 982 C CE2 . TYR A 1 125 ? 40.475 -7.192 39.209 1.00 25.53 ? 125 TYR A CE2 1 ATOM 983 C CZ . TYR A 1 125 ? 40.126 -8.524 39.202 1.00 25.25 ? 125 TYR A CZ 1 ATOM 984 O OH . TYR A 1 125 ? 40.598 -9.373 40.205 1.00 27.67 ? 125 TYR A OH 1 ATOM 985 N N . ASP A 1 126 ? 36.712 -5.145 38.631 1.00 22.34 ? 126 ASP A N 1 ATOM 986 C CA . ASP A 1 126 ? 36.693 -4.371 39.874 1.00 22.13 ? 126 ASP A CA 1 ATOM 987 C C . ASP A 1 126 ? 38.083 -4.329 40.522 1.00 22.99 ? 126 ASP A C 1 ATOM 988 O O . ASP A 1 126 ? 38.462 -5.201 41.312 1.00 23.32 ? 126 ASP A O 1 ATOM 989 C CB . ASP A 1 126 ? 35.663 -4.984 40.851 1.00 22.27 ? 126 ASP A CB 1 ATOM 990 C CG . ASP A 1 126 ? 35.638 -4.286 42.197 1.00 24.13 ? 126 ASP A CG 1 ATOM 991 O OD1 . ASP A 1 126 ? 36.205 -3.164 42.340 1.00 25.71 ? 126 ASP A OD1 1 ATOM 992 O OD2 . ASP A 1 126 ? 35.045 -4.850 43.137 1.00 21.40 ? 126 ASP A OD2 1 ATOM 993 N N . GLY A 1 127 ? 38.850 -3.300 40.200 1.00 23.72 ? 127 GLY A N 1 ATOM 994 C CA . GLY A 1 127 ? 40.149 -3.139 40.834 1.00 24.11 ? 127 GLY A CA 1 ATOM 995 C C . GLY A 1 127 ? 41.266 -2.676 39.927 1.00 25.51 ? 127 GLY A C 1 ATOM 996 O O . GLY A 1 127 ? 41.058 -2.427 38.744 1.00 24.42 ? 127 GLY A O 1 ATOM 997 N N . ALA A 1 128 ? 42.471 -2.597 40.490 1.00 26.01 ? 128 ALA A N 1 ATOM 998 C CA . ALA A 1 128 ? 43.621 -2.022 39.795 1.00 26.38 ? 128 ALA A CA 1 ATOM 999 C C . ALA A 1 128 ? 44.051 -2.853 38.597 1.00 26.47 ? 128 ALA A C 1 ATOM 1000 O O . ALA A 1 128 ? 43.981 -4.081 38.625 1.00 26.29 ? 128 ALA A O 1 ATOM 1001 C CB . ALA A 1 128 ? 44.795 -1.885 40.762 1.00 25.30 ? 128 ALA A CB 1 ATOM 1002 N N . GLY A 1 129 ? 44.510 -2.172 37.548 1.00 28.06 ? 129 GLY A N 1 ATOM 1003 C CA . GLY A 1 129 ? 44.964 -2.852 36.339 1.00 29.23 ? 129 GLY A CA 1 ATOM 1004 C C . GLY A 1 129 ? 46.069 -3.866 36.590 1.00 31.06 ? 129 GLY A C 1 ATOM 1005 O O . GLY A 1 129 ? 46.116 -4.911 35.957 1.00 30.78 ? 129 GLY A O 1 ATOM 1006 N N . SER A 1 130 ? 46.942 -3.556 37.539 1.00 33.18 ? 130 SER A N 1 ATOM 1007 C CA . SER A 1 130 ? 48.028 -4.439 37.912 1.00 36.21 ? 130 SER A CA 1 ATOM 1008 C C . SER A 1 130 ? 47.568 -5.682 38.648 1.00 36.46 ? 130 SER A C 1 ATOM 1009 O O . SER A 1 130 ? 48.302 -6.658 38.727 1.00 38.83 ? 130 SER A O 1 ATOM 1010 C CB . SER A 1 130 ? 49.008 -3.687 38.802 1.00 36.94 ? 130 SER A CB 1 ATOM 1011 O OG . SER A 1 130 ? 49.869 -2.943 37.987 1.00 40.42 ? 130 SER A OG 1 ATOM 1012 N N . SER A 1 131 ? 46.370 -5.644 39.216 1.00 36.44 ? 131 SER A N 1 ATOM 1013 C CA . SER A 1 131 ? 45.947 -6.735 40.091 1.00 36.04 ? 131 SER A CA 1 ATOM 1014 C C . SER A 1 131 ? 44.960 -7.654 39.403 1.00 34.31 ? 131 SER A C 1 ATOM 1015 O O . SER A 1 131 ? 44.370 -8.531 40.037 1.00 34.93 ? 131 SER A O 1 ATOM 1016 C CB . SER A 1 131 ? 45.291 -6.188 41.355 1.00 37.19 ? 131 SER A CB 1 ATOM 1017 O OG . SER A 1 131 ? 45.985 -5.046 41.820 1.00 38.85 ? 131 SER A OG 1 ATOM 1018 N N . VAL A 1 132 ? 44.757 -7.453 38.108 1.00 31.89 ? 132 VAL A N 1 ATOM 1019 C CA . VAL A 1 132 ? 43.673 -8.170 37.458 1.00 29.88 ? 132 VAL A CA 1 ATOM 1020 C C . VAL A 1 132 ? 43.894 -9.668 37.512 1.00 29.42 ? 132 VAL A C 1 ATOM 1021 O O . VAL A 1 132 ? 44.962 -10.155 37.149 1.00 30.37 ? 132 VAL A O 1 ATOM 1022 C CB . VAL A 1 132 ? 43.511 -7.743 35.993 1.00 28.25 ? 132 VAL A CB 1 ATOM 1023 C CG1 . VAL A 1 132 ? 42.585 -8.714 35.242 1.00 28.53 ? 132 VAL A CG1 1 ATOM 1024 C CG2 . VAL A 1 132 ? 43.001 -6.324 35.940 1.00 26.87 ? 132 VAL A CG2 1 ATOM 1025 N N . ASP A 1 133 ? 42.869 -10.378 37.973 1.00 30.00 ? 133 ASP A N 1 ATOM 1026 C CA . ASP A 1 133 ? 42.829 -11.839 37.907 1.00 30.73 ? 133 ASP A CA 1 ATOM 1027 C C . ASP A 1 133 ? 42.167 -12.279 36.606 1.00 29.03 ? 133 ASP A C 1 ATOM 1028 O O . ASP A 1 133 ? 40.932 -12.375 36.529 1.00 28.81 ? 133 ASP A O 1 ATOM 1029 C CB . ASP A 1 133 ? 42.055 -12.411 39.089 1.00 33.52 ? 133 ASP A CB 1 ATOM 1030 C CG . ASP A 1 133 ? 42.008 -13.930 39.073 1.00 35.59 ? 133 ASP A CG 1 ATOM 1031 O OD1 . ASP A 1 133 ? 42.463 -14.537 38.074 1.00 34.99 ? 133 ASP A OD1 1 ATOM 1032 O OD2 . ASP A 1 133 ? 41.527 -14.518 40.078 1.00 37.81 ? 133 ASP A OD2 1 ATOM 1033 N N . TYR A 1 134 ? 42.980 -12.577 35.592 1.00 26.80 ? 134 TYR A N 1 ATOM 1034 C CA . TYR A 1 134 ? 42.439 -12.905 34.268 1.00 25.89 ? 134 TYR A CA 1 ATOM 1035 C C . TYR A 1 134 ? 41.577 -14.168 34.204 1.00 26.98 ? 134 TYR A C 1 ATOM 1036 O O . TYR A 1 134 ? 40.814 -14.348 33.256 1.00 27.14 ? 134 TYR A O 1 ATOM 1037 C CB . TYR A 1 134 ? 43.540 -12.932 33.206 1.00 25.64 ? 134 TYR A CB 1 ATOM 1038 C CG . TYR A 1 134 ? 44.205 -11.576 33.001 1.00 24.12 ? 134 TYR A CG 1 ATOM 1039 C CD1 . TYR A 1 134 ? 43.722 -10.674 32.034 1.00 25.34 ? 134 TYR A CD1 1 ATOM 1040 C CD2 . TYR A 1 134 ? 45.285 -11.180 33.785 1.00 23.88 ? 134 TYR A CD2 1 ATOM 1041 C CE1 . TYR A 1 134 ? 44.301 -9.443 31.855 1.00 25.04 ? 134 TYR A CE1 1 ATOM 1042 C CE2 . TYR A 1 134 ? 45.894 -9.947 33.611 1.00 23.92 ? 134 TYR A CE2 1 ATOM 1043 C CZ . TYR A 1 134 ? 45.385 -9.075 32.643 1.00 25.03 ? 134 TYR A CZ 1 ATOM 1044 O OH . TYR A 1 134 ? 45.953 -7.866 32.443 1.00 24.63 ? 134 TYR A OH 1 ATOM 1045 N N . SER A 1 135 ? 41.679 -15.041 35.200 1.00 27.45 ? 135 SER A N 1 ATOM 1046 C CA . SER A 1 135 ? 40.920 -16.278 35.148 1.00 28.96 ? 135 SER A CA 1 ATOM 1047 C C . SER A 1 135 ? 39.418 -16.039 35.277 1.00 28.88 ? 135 SER A C 1 ATOM 1048 O O . SER A 1 135 ? 38.623 -16.949 35.019 1.00 30.92 ? 135 SER A O 1 ATOM 1049 C CB . SER A 1 135 ? 41.414 -17.252 36.226 1.00 30.61 ? 135 SER A CB 1 ATOM 1050 O OG . SER A 1 135 ? 40.970 -16.805 37.492 1.00 32.64 ? 135 SER A OG 1 ATOM 1051 N N . VAL A 1 136 ? 39.006 -14.821 35.647 1.00 27.50 ? 136 VAL A N 1 ATOM 1052 C CA . VAL A 1 136 ? 37.577 -14.576 35.824 1.00 26.39 ? 136 VAL A CA 1 ATOM 1053 C C . VAL A 1 136 ? 36.902 -14.315 34.490 1.00 25.81 ? 136 VAL A C 1 ATOM 1054 O O . VAL A 1 136 ? 35.667 -14.316 34.424 1.00 27.84 ? 136 VAL A O 1 ATOM 1055 C CB . VAL A 1 136 ? 37.230 -13.373 36.745 1.00 26.53 ? 136 VAL A CB 1 ATOM 1056 C CG1 . VAL A 1 136 ? 37.751 -13.578 38.180 1.00 27.04 ? 136 VAL A CG1 1 ATOM 1057 C CG2 . VAL A 1 136 ? 37.723 -12.083 36.121 1.00 26.82 ? 136 VAL A CG2 1 ATOM 1058 N N . PHE A 1 137 ? 37.681 -14.025 33.437 1.00 22.45 ? 137 PHE A N 1 ATOM 1059 C CA . PHE A 1 137 ? 37.078 -13.764 32.126 1.00 22.33 ? 137 PHE A CA 1 ATOM 1060 C C . PHE A 1 137 ? 36.821 -15.048 31.380 1.00 23.38 ? 137 PHE A C 1 ATOM 1061 O O . PHE A 1 137 ? 37.644 -15.936 31.433 1.00 22.37 ? 137 PHE A O 1 ATOM 1062 C CB . PHE A 1 137 ? 37.971 -12.855 31.271 1.00 21.69 ? 137 PHE A CB 1 ATOM 1063 C CG . PHE A 1 137 ? 38.352 -11.571 31.964 1.00 20.97 ? 137 PHE A CG 1 ATOM 1064 C CD1 . PHE A 1 137 ? 37.363 -10.735 32.487 1.00 21.20 ? 137 PHE A CD1 1 ATOM 1065 C CD2 . PHE A 1 137 ? 39.681 -11.203 32.121 1.00 22.55 ? 137 PHE A CD2 1 ATOM 1066 C CE1 . PHE A 1 137 ? 37.710 -9.568 33.146 1.00 22.24 ? 137 PHE A CE1 1 ATOM 1067 C CE2 . PHE A 1 137 ? 40.015 -10.029 32.782 1.00 22.51 ? 137 PHE A CE2 1 ATOM 1068 C CZ . PHE A 1 137 ? 39.043 -9.210 33.287 1.00 22.46 ? 137 PHE A CZ 1 ATOM 1069 N N . LYS A 1 138 ? 35.660 -15.142 30.738 1.00 24.00 ? 138 LYS A N 1 ATOM 1070 C CA . LYS A 1 138 ? 35.312 -16.291 29.909 1.00 24.94 ? 138 LYS A CA 1 ATOM 1071 C C . LYS A 1 138 ? 34.898 -15.804 28.531 1.00 24.20 ? 138 LYS A C 1 ATOM 1072 O O . LYS A 1 138 ? 33.974 -15.002 28.405 1.00 24.28 ? 138 LYS A O 1 ATOM 1073 C CB . LYS A 1 138 ? 34.154 -17.066 30.521 1.00 27.41 ? 138 LYS A CB 1 ATOM 1074 C CG . LYS A 1 138 ? 34.351 -17.426 31.991 1.00 31.46 ? 138 LYS A CG 1 ATOM 1075 C CD . LYS A 1 138 ? 33.229 -18.360 32.423 1.00 35.55 ? 138 LYS A CD 1 ATOM 1076 C CE . LYS A 1 138 ? 33.329 -18.653 33.910 1.00 38.24 ? 138 LYS A CE 1 ATOM 1077 N NZ . LYS A 1 138 ? 32.041 -19.207 34.514 1.00 40.21 ? 138 LYS A NZ 1 ATOM 1078 N N . PRO A 1 139 ? 35.551 -16.304 27.487 1.00 23.07 ? 139 PRO A N 1 ATOM 1079 C CA . PRO A 1 139 ? 36.579 -17.363 27.494 1.00 23.36 ? 139 PRO A CA 1 ATOM 1080 C C . PRO A 1 139 ? 38.022 -16.856 27.546 1.00 22.56 ? 139 PRO A C 1 ATOM 1081 O O . PRO A 1 139 ? 38.962 -17.667 27.509 1.00 23.94 ? 139 PRO A O 1 ATOM 1082 C CB . PRO A 1 139 ? 36.351 -18.052 26.144 1.00 24.27 ? 139 PRO A CB 1 ATOM 1083 C CG . PRO A 1 139 ? 36.014 -16.878 25.252 1.00 24.66 ? 139 PRO A CG 1 ATOM 1084 C CD . PRO A 1 139 ? 35.249 -15.849 26.116 1.00 23.88 ? 139 PRO A CD 1 ATOM 1085 N N . PHE A 1 140 ? 38.197 -15.542 27.655 1.00 23.18 ? 140 PHE A N 1 ATOM 1086 C CA . PHE A 1 140 ? 39.530 -14.919 27.591 1.00 21.99 ? 140 PHE A CA 1 ATOM 1087 C C . PHE A 1 140 ? 40.253 -15.008 28.926 1.00 23.59 ? 140 PHE A C 1 ATOM 1088 O O . PHE A 1 140 ? 40.637 -13.994 29.495 1.00 22.89 ? 140 PHE A O 1 ATOM 1089 C CB . PHE A 1 140 ? 39.363 -13.440 27.153 1.00 23.28 ? 140 PHE A CB 1 ATOM 1090 C CG . PHE A 1 140 ? 38.746 -13.295 25.781 1.00 23.20 ? 140 PHE A CG 1 ATOM 1091 C CD1 . PHE A 1 140 ? 39.338 -13.897 24.683 1.00 24.87 ? 140 PHE A CD1 1 ATOM 1092 C CD2 . PHE A 1 140 ? 37.563 -12.554 25.598 1.00 24.20 ? 140 PHE A CD2 1 ATOM 1093 C CE1 . PHE A 1 140 ? 38.796 -13.760 23.386 1.00 24.36 ? 140 PHE A CE1 1 ATOM 1094 C CE2 . PHE A 1 140 ? 37.004 -12.424 24.294 1.00 24.24 ? 140 PHE A CE2 1 ATOM 1095 C CZ . PHE A 1 140 ? 37.623 -13.031 23.207 1.00 23.82 ? 140 PHE A CZ 1 ATOM 1096 N N . SER A 1 141 ? 40.505 -16.245 29.387 1.00 20.92 ? 141 SER A N 1 ATOM 1097 C CA . SER A 1 141 ? 40.871 -16.478 30.793 1.00 22.01 ? 141 SER A CA 1 ATOM 1098 C C . SER A 1 141 ? 42.366 -16.417 31.046 1.00 22.72 ? 141 SER A C 1 ATOM 1099 O O . SER A 1 141 ? 42.883 -17.060 31.978 1.00 23.27 ? 141 SER A O 1 ATOM 1100 C CB . SER A 1 141 ? 40.324 -17.821 31.255 1.00 22.29 ? 141 SER A CB 1 ATOM 1101 O OG . SER A 1 141 ? 40.729 -18.824 30.332 1.00 23.40 ? 141 SER A OG 1 ATOM 1102 N N . SER A 1 142 ? 43.072 -15.613 30.253 1.00 21.57 ? 142 SER A N 1 ATOM 1103 C CA . SER A 1 142 ? 44.520 -15.550 30.389 1.00 21.68 ? 142 SER A CA 1 ATOM 1104 C C . SER A 1 142 ? 45.006 -14.173 29.960 1.00 22.17 ? 142 SER A C 1 ATOM 1105 O O . SER A 1 142 ? 44.442 -13.572 29.047 1.00 21.01 ? 142 SER A O 1 ATOM 1106 C CB . SER A 1 142 ? 45.181 -16.596 29.504 1.00 22.76 ? 142 SER A CB 1 ATOM 1107 O OG . SER A 1 142 ? 46.566 -16.343 29.411 1.00 24.36 ? 142 SER A OG 1 ATOM 1108 N N . GLN A 1 143 ? 46.021 -13.684 30.661 1.00 22.26 ? 143 GLN A N 1 ATOM 1109 C CA . GLN A 1 143 ? 46.677 -12.419 30.310 1.00 24.35 ? 143 GLN A CA 1 ATOM 1110 C C . GLN A 1 143 ? 47.114 -12.437 28.837 1.00 23.43 ? 143 GLN A C 1 ATOM 1111 O O . GLN A 1 143 ? 47.169 -11.382 28.182 1.00 23.75 ? 143 GLN A O 1 ATOM 1112 C CB . GLN A 1 143 ? 47.881 -12.215 31.210 1.00 26.09 ? 143 GLN A CB 1 ATOM 1113 C CG . GLN A 1 143 ? 48.420 -10.795 31.274 1.00 28.56 ? 143 GLN A CG 1 ATOM 1114 C CD . GLN A 1 143 ? 49.487 -10.655 32.366 1.00 30.55 ? 143 GLN A CD 1 ATOM 1115 O OE1 . GLN A 1 143 ? 49.367 -11.236 33.463 1.00 33.39 ? 143 GLN A OE1 1 ATOM 1116 N NE2 . GLN A 1 143 ? 50.530 -9.899 32.072 1.00 32.67 ? 143 GLN A NE2 1 ATOM 1117 N N . ASP A 1 144 ? 47.425 -13.621 28.305 1.00 24.24 ? 144 ASP A N 1 ATOM 1118 C CA . ASP A 1 144 ? 47.859 -13.741 26.917 1.00 25.12 ? 144 ASP A CA 1 ATOM 1119 C C . ASP A 1 144 ? 46.873 -13.217 25.884 1.00 24.65 ? 144 ASP A C 1 ATOM 1120 O O . ASP A 1 144 ? 47.266 -12.972 24.745 1.00 25.26 ? 144 ASP A O 1 ATOM 1121 C CB . ASP A 1 144 ? 48.231 -15.183 26.564 1.00 27.05 ? 144 ASP A CB 1 ATOM 1122 C CG . ASP A 1 144 ? 49.378 -15.695 27.389 1.00 30.96 ? 144 ASP A CG 1 ATOM 1123 O OD1 . ASP A 1 144 ? 50.078 -14.874 28.019 1.00 32.48 ? 144 ASP A OD1 1 ATOM 1124 O OD2 . ASP A 1 144 ? 49.561 -16.923 27.415 1.00 32.25 ? 144 ASP A OD2 1 ATOM 1125 N N . TYR A 1 145 ? 45.601 -13.054 26.256 1.00 22.31 ? 145 TYR A N 1 ATOM 1126 C CA . TYR A 1 145 ? 44.640 -12.535 25.314 1.00 21.98 ? 145 TYR A CA 1 ATOM 1127 C C . TYR A 1 145 ? 44.626 -11.006 25.280 1.00 20.60 ? 145 TYR A C 1 ATOM 1128 O O . TYR A 1 145 ? 43.932 -10.430 24.462 1.00 21.85 ? 145 TYR A O 1 ATOM 1129 C CB . TYR A 1 145 ? 43.234 -12.989 25.679 1.00 23.12 ? 145 TYR A CB 1 ATOM 1130 C CG . TYR A 1 145 ? 42.997 -14.470 25.475 1.00 23.15 ? 145 TYR A CG 1 ATOM 1131 C CD1 . TYR A 1 145 ? 42.824 -14.979 24.185 1.00 22.32 ? 145 TYR A CD1 1 ATOM 1132 C CD2 . TYR A 1 145 ? 42.883 -15.326 26.553 1.00 23.02 ? 145 TYR A CD2 1 ATOM 1133 C CE1 . TYR A 1 145 ? 42.589 -16.337 23.971 1.00 24.99 ? 145 TYR A CE1 1 ATOM 1134 C CE2 . TYR A 1 145 ? 42.642 -16.690 26.342 1.00 24.44 ? 145 TYR A CE2 1 ATOM 1135 C CZ . TYR A 1 145 ? 42.487 -17.170 25.049 1.00 24.03 ? 145 TYR A CZ 1 ATOM 1136 O OH . TYR A 1 145 ? 42.256 -18.533 24.841 1.00 25.11 ? 145 TYR A OH 1 ATOM 1137 N N . PHE A 1 146 ? 45.369 -10.376 26.187 1.00 19.07 ? 146 PHE A N 1 ATOM 1138 C CA . PHE A 1 146 ? 45.231 -8.936 26.368 1.00 19.95 ? 146 PHE A CA 1 ATOM 1139 C C . PHE A 1 146 ? 46.473 -8.105 26.008 1.00 19.14 ? 146 PHE A C 1 ATOM 1140 O O . PHE A 1 146 ? 47.610 -8.556 26.116 1.00 19.20 ? 146 PHE A O 1 ATOM 1141 C CB . PHE A 1 146 ? 44.849 -8.639 27.831 1.00 21.34 ? 146 PHE A CB 1 ATOM 1142 C CG . PHE A 1 146 ? 43.508 -9.197 28.210 1.00 19.96 ? 146 PHE A CG 1 ATOM 1143 C CD1 . PHE A 1 146 ? 43.350 -10.565 28.532 1.00 20.24 ? 146 PHE A CD1 1 ATOM 1144 C CD2 . PHE A 1 146 ? 42.403 -8.381 28.195 1.00 20.16 ? 146 PHE A CD2 1 ATOM 1145 C CE1 . PHE A 1 146 ? 42.099 -11.075 28.864 1.00 20.00 ? 146 PHE A CE1 1 ATOM 1146 C CE2 . PHE A 1 146 ? 41.123 -8.886 28.537 1.00 20.95 ? 146 PHE A CE2 1 ATOM 1147 C CZ . PHE A 1 146 ? 40.981 -10.232 28.870 1.00 21.21 ? 146 PHE A CZ 1 ATOM 1148 N N . HIS A 1 147 ? 46.233 -6.838 25.674 1.00 18.81 ? 147 HIS A N 1 ATOM 1149 C CA . HIS A 1 147 ? 47.334 -5.889 25.572 1.00 19.50 ? 147 HIS A CA 1 ATOM 1150 C C . HIS A 1 147 ? 47.928 -5.666 26.971 1.00 21.03 ? 147 HIS A C 1 ATOM 1151 O O . HIS A 1 147 ? 47.195 -5.681 27.977 1.00 20.41 ? 147 HIS A O 1 ATOM 1152 C CB . HIS A 1 147 ? 46.822 -4.542 25.044 1.00 21.07 ? 147 HIS A CB 1 ATOM 1153 C CG . HIS A 1 147 ? 46.582 -4.503 23.565 1.00 20.70 ? 147 HIS A CG 1 ATOM 1154 N ND1 . HIS A 1 147 ? 45.422 -3.991 23.009 1.00 21.33 ? 147 HIS A ND1 1 ATOM 1155 C CD2 . HIS A 1 147 ? 47.365 -4.884 22.529 1.00 22.93 ? 147 HIS A CD2 1 ATOM 1156 C CE1 . HIS A 1 147 ? 45.504 -4.068 21.690 1.00 21.14 ? 147 HIS A CE1 1 ATOM 1157 N NE2 . HIS A 1 147 ? 46.691 -4.567 21.372 1.00 21.35 ? 147 HIS A NE2 1 ATOM 1158 N N . PRO A 1 148 ? 49.250 -5.437 27.039 1.00 20.43 ? 148 PRO A N 1 ATOM 1159 C CA . PRO A 1 148 ? 49.890 -5.173 28.324 1.00 21.01 ? 148 PRO A CA 1 ATOM 1160 C C . PRO A 1 148 ? 49.226 -4.020 29.037 1.00 20.96 ? 148 PRO A C 1 ATOM 1161 O O . PRO A 1 148 ? 48.742 -3.086 28.397 1.00 20.68 ? 148 PRO A O 1 ATOM 1162 C CB . PRO A 1 148 ? 51.336 -4.767 27.946 1.00 22.11 ? 148 PRO A CB 1 ATOM 1163 C CG . PRO A 1 148 ? 51.561 -5.322 26.582 1.00 22.24 ? 148 PRO A CG 1 ATOM 1164 C CD . PRO A 1 148 ? 50.189 -5.381 25.909 1.00 20.76 ? 148 PRO A CD 1 ATOM 1165 N N . PHE A 1 149 ? 49.226 -4.058 30.365 1.00 22.95 ? 149 PHE A N 1 ATOM 1166 C CA . PHE A 1 149 ? 48.500 -3.038 31.105 1.00 21.02 ? 149 PHE A CA 1 ATOM 1167 C C . PHE A 1 149 ? 49.171 -1.666 31.070 1.00 22.33 ? 149 PHE A C 1 ATOM 1168 O O . PHE A 1 149 ? 50.310 -1.514 31.518 1.00 22.15 ? 149 PHE A O 1 ATOM 1169 C CB . PHE A 1 149 ? 48.273 -3.488 32.554 1.00 23.86 ? 149 PHE A CB 1 ATOM 1170 C CG . PHE A 1 149 ? 47.898 -2.365 33.459 1.00 24.03 ? 149 PHE A CG 1 ATOM 1171 C CD1 . PHE A 1 149 ? 46.805 -1.573 33.164 1.00 25.04 ? 149 PHE A CD1 1 ATOM 1172 C CD2 . PHE A 1 149 ? 48.662 -2.080 34.577 1.00 26.38 ? 149 PHE A CD2 1 ATOM 1173 C CE1 . PHE A 1 149 ? 46.461 -0.496 33.979 1.00 26.30 ? 149 PHE A CE1 1 ATOM 1174 C CE2 . PHE A 1 149 ? 48.322 -1.022 35.401 1.00 26.52 ? 149 PHE A CE2 1 ATOM 1175 C CZ . PHE A 1 149 ? 47.238 -0.221 35.098 1.00 25.66 ? 149 PHE A CZ 1 ATOM 1176 N N . CYS A 1 150 ? 48.443 -0.701 30.498 1.00 23.68 ? 150 CYS A N 1 ATOM 1177 C CA . CYS A 1 150 ? 48.791 0.709 30.570 1.00 24.47 ? 150 CYS A CA 1 ATOM 1178 C C . CYS A 1 150 ? 47.499 1.451 30.342 1.00 24.67 ? 150 CYS A C 1 ATOM 1179 O O . CYS A 1 150 ? 46.615 0.953 29.658 1.00 24.45 ? 150 CYS A O 1 ATOM 1180 C CB . CYS A 1 150 ? 49.828 1.097 29.513 1.00 27.54 ? 150 CYS A CB 1 ATOM 1181 S SG . CYS A 1 150 ? 49.399 0.575 27.836 1.00 31.55 ? 150 CYS A SG 1 ATOM 1182 N N . PHE A 1 151 ? 47.344 2.605 30.962 1.00 22.92 ? 151 PHE A N 1 ATOM 1183 C CA . PHE A 1 151 ? 46.134 3.387 30.722 1.00 22.53 ? 151 PHE A CA 1 ATOM 1184 C C . PHE A 1 151 ? 46.412 4.405 29.645 1.00 21.81 ? 151 PHE A C 1 ATOM 1185 O O . PHE A 1 151 ? 47.504 4.977 29.561 1.00 22.56 ? 151 PHE A O 1 ATOM 1186 C CB . PHE A 1 151 ? 45.663 4.084 32.004 1.00 25.74 ? 151 PHE A CB 1 ATOM 1187 C CG . PHE A 1 151 ? 45.049 3.156 33.019 1.00 26.23 ? 151 PHE A CG 1 ATOM 1188 C CD1 . PHE A 1 151 ? 43.937 2.393 32.707 1.00 27.89 ? 151 PHE A CD1 1 ATOM 1189 C CD2 . PHE A 1 151 ? 45.557 3.097 34.307 1.00 28.38 ? 151 PHE A CD2 1 ATOM 1190 C CE1 . PHE A 1 151 ? 43.361 1.555 33.660 1.00 27.79 ? 151 PHE A CE1 1 ATOM 1191 C CE2 . PHE A 1 151 ? 44.990 2.293 35.244 1.00 27.54 ? 151 PHE A CE2 1 ATOM 1192 C CZ . PHE A 1 151 ? 43.903 1.499 34.925 1.00 27.48 ? 151 PHE A CZ 1 ATOM 1193 N N . ILE A 1 152 ? 45.415 4.632 28.796 1.00 22.20 ? 152 ILE A N 1 ATOM 1194 C CA . ILE A 1 152 ? 45.545 5.652 27.753 1.00 23.62 ? 152 ILE A CA 1 ATOM 1195 C C . ILE A 1 152 ? 45.842 7.016 28.388 1.00 26.20 ? 152 ILE A C 1 ATOM 1196 O O . ILE A 1 152 ? 45.133 7.424 29.318 1.00 26.64 ? 152 ILE A O 1 ATOM 1197 C CB . ILE A 1 152 ? 44.245 5.762 26.942 1.00 23.44 ? 152 ILE A CB 1 ATOM 1198 C CG1 . ILE A 1 152 ? 43.915 4.434 26.244 1.00 23.77 ? 152 ILE A CG1 1 ATOM 1199 C CG2 . ILE A 1 152 ? 44.390 6.837 25.894 1.00 23.21 ? 152 ILE A CG2 1 ATOM 1200 C CD1 . ILE A 1 152 ? 42.524 4.395 25.698 1.00 23.83 ? 152 ILE A CD1 1 ATOM 1201 N N . GLN A 1 153 ? 46.859 7.703 27.868 1.00 26.19 ? 153 GLN A N 1 ATOM 1202 C CA . GLN A 1 153 ? 47.329 8.999 28.401 1.00 28.43 ? 153 GLN A CA 1 ATOM 1203 C C . GLN A 1 153 ? 47.009 10.138 27.447 1.00 29.97 ? 153 GLN A C 1 ATOM 1204 O O . GLN A 1 153 ? 46.660 11.256 27.868 1.00 30.86 ? 153 GLN A O 1 ATOM 1205 C CB . GLN A 1 153 ? 48.848 8.975 28.572 1.00 31.26 ? 153 GLN A CB 1 ATOM 1206 C CG . GLN A 1 153 ? 49.324 7.890 29.506 1.00 34.53 ? 153 GLN A CG 1 ATOM 1207 C CD . GLN A 1 153 ? 48.944 8.202 30.933 1.00 36.05 ? 153 GLN A CD 1 ATOM 1208 O OE1 . GLN A 1 153 ? 49.053 9.351 31.374 1.00 38.03 ? 153 GLN A OE1 1 ATOM 1209 N NE2 . GLN A 1 153 ? 48.508 7.185 31.672 1.00 36.36 ? 153 GLN A NE2 1 ATOM 1210 N N . ASN A 1 154 ? 47.174 9.865 26.157 1.00 28.36 ? 154 ASN A N 1 ATOM 1211 C CA . ASN A 1 154 ? 47.058 10.881 25.115 1.00 29.52 ? 154 ASN A CA 1 ATOM 1212 C C . ASN A 1 154 ? 46.066 10.446 24.031 1.00 29.57 ? 154 ASN A C 1 ATOM 1213 O O . ASN A 1 154 ? 46.371 9.606 23.180 1.00 29.50 ? 154 ASN A O 1 ATOM 1214 C CB . ASN A 1 154 ? 48.440 11.122 24.507 1.00 28.64 ? 154 ASN A CB 1 ATOM 1215 C CG . ASN A 1 154 ? 48.442 12.239 23.510 1.00 29.75 ? 154 ASN A CG 1 ATOM 1216 O OD1 . ASN A 1 154 ? 47.403 12.854 23.241 1.00 28.39 ? 154 ASN A OD1 1 ATOM 1217 N ND2 . ASN A 1 154 ? 49.609 12.511 22.944 1.00 30.05 ? 154 ASN A ND2 1 ATOM 1218 N N . TYR A 1 155 ? 44.871 11.014 24.047 1.00 28.16 ? 155 TYR A N 1 ATOM 1219 C CA . TYR A 1 155 ? 43.858 10.567 23.113 1.00 29.48 ? 155 TYR A CA 1 ATOM 1220 C C . TYR A 1 155 ? 44.116 11.056 21.677 1.00 31.24 ? 155 TYR A C 1 ATOM 1221 O O . TYR A 1 155 ? 43.421 10.666 20.750 1.00 31.91 ? 155 TYR A O 1 ATOM 1222 C CB . TYR A 1 155 ? 42.443 10.907 23.616 1.00 30.49 ? 155 TYR A CB 1 ATOM 1223 C CG . TYR A 1 155 ? 41.972 10.020 24.759 1.00 29.78 ? 155 TYR A CG 1 ATOM 1224 C CD1 . TYR A 1 155 ? 42.479 10.178 26.037 1.00 30.85 ? 155 TYR A CD1 1 ATOM 1225 C CD2 . TYR A 1 155 ? 41.033 9.025 24.554 1.00 30.28 ? 155 TYR A CD2 1 ATOM 1226 C CE1 . TYR A 1 155 ? 42.070 9.374 27.076 1.00 31.63 ? 155 TYR A CE1 1 ATOM 1227 C CE2 . TYR A 1 155 ? 40.610 8.215 25.593 1.00 30.63 ? 155 TYR A CE2 1 ATOM 1228 C CZ . TYR A 1 155 ? 41.131 8.393 26.853 1.00 31.63 ? 155 TYR A CZ 1 ATOM 1229 O OH . TYR A 1 155 ? 40.724 7.596 27.899 1.00 32.32 ? 155 TYR A OH 1 ATOM 1230 N N . GLU A 1 156 ? 45.146 11.884 21.507 1.00 32.23 ? 156 GLU A N 1 ATOM 1231 C CA . GLU A 1 156 ? 45.594 12.310 20.184 1.00 33.98 ? 156 GLU A CA 1 ATOM 1232 C C . GLU A 1 156 ? 46.502 11.297 19.530 1.00 32.73 ? 156 GLU A C 1 ATOM 1233 O O . GLU A 1 156 ? 46.819 11.428 18.351 1.00 32.18 ? 156 GLU A O 1 ATOM 1234 C CB . GLU A 1 156 ? 46.411 13.596 20.259 1.00 36.94 ? 156 GLU A CB 1 ATOM 1235 C CG . GLU A 1 156 ? 45.641 14.823 20.665 1.00 40.63 ? 156 GLU A CG 1 ATOM 1236 C CD . GLU A 1 156 ? 46.539 16.007 20.758 1.00 42.80 ? 156 GLU A CD 1 ATOM 1237 O OE1 . GLU A 1 156 ? 47.766 15.837 20.542 1.00 44.20 ? 156 GLU A OE1 1 ATOM 1238 O OE2 . GLU A 1 156 ? 46.014 17.110 21.027 1.00 43.78 ? 156 GLU A OE2 1 ATOM 1239 N N . ASP A 1 157 ? 46.974 10.325 20.311 1.00 30.08 ? 157 ASP A N 1 ATOM 1240 C CA . ASP A 1 157 ? 47.905 9.324 19.812 1.00 28.84 ? 157 ASP A CA 1 ATOM 1241 C C . ASP A 1 157 ? 47.116 8.048 19.523 1.00 27.15 ? 157 ASP A C 1 ATOM 1242 O O . ASP A 1 157 ? 46.807 7.293 20.424 1.00 25.51 ? 157 ASP A O 1 ATOM 1243 C CB . ASP A 1 157 ? 48.969 9.045 20.872 1.00 30.16 ? 157 ASP A CB 1 ATOM 1244 C CG . ASP A 1 157 ? 49.847 7.842 20.532 1.00 32.72 ? 157 ASP A CG 1 ATOM 1245 O OD1 . ASP A 1 157 ? 49.882 7.433 19.357 1.00 32.94 ? 157 ASP A OD1 1 ATOM 1246 O OD2 . ASP A 1 157 ? 50.504 7.291 21.450 1.00 35.84 ? 157 ASP A OD2 1 ATOM 1247 N N . GLN A 1 158 ? 46.812 7.807 18.259 1.00 25.67 ? 158 GLN A N 1 ATOM 1248 C CA . GLN A 1 158 ? 45.914 6.712 17.895 1.00 25.17 ? 158 GLN A CA 1 ATOM 1249 C C . GLN A 1 158 ? 46.473 5.340 18.283 1.00 23.97 ? 158 GLN A C 1 ATOM 1250 O O . GLN A 1 158 ? 45.717 4.422 18.534 1.00 23.33 ? 158 GLN A O 1 ATOM 1251 C CB . GLN A 1 158 ? 45.625 6.751 16.398 1.00 25.78 ? 158 GLN A CB 1 ATOM 1252 C CG . GLN A 1 158 ? 44.563 5.768 15.916 1.00 25.99 ? 158 GLN A CG 1 ATOM 1253 C CD . GLN A 1 158 ? 43.217 6.000 16.564 1.00 25.63 ? 158 GLN A CD 1 ATOM 1254 O OE1 . GLN A 1 158 ? 42.906 7.118 16.998 1.00 24.47 ? 158 GLN A OE1 1 ATOM 1255 N NE2 . GLN A 1 158 ? 42.425 4.933 16.675 1.00 24.85 ? 158 GLN A NE2 1 ATOM 1256 N N . THR A 1 159 ? 47.789 5.195 18.319 1.00 23.05 ? 159 THR A N 1 ATOM 1257 C CA . THR A 1 159 ? 48.351 3.895 18.726 1.00 22.10 ? 159 THR A CA 1 ATOM 1258 C C . THR A 1 159 ? 47.971 3.599 20.165 1.00 21.92 ? 159 THR A C 1 ATOM 1259 O O . THR A 1 159 ? 47.570 2.476 20.513 1.00 22.75 ? 159 THR A O 1 ATOM 1260 C CB . THR A 1 159 ? 49.889 3.898 18.601 1.00 23.14 ? 159 THR A CB 1 ATOM 1261 O OG1 . THR A 1 159 ? 50.226 4.127 17.227 1.00 25.61 ? 159 THR A OG1 1 ATOM 1262 C CG2 . THR A 1 159 ? 50.478 2.555 19.048 1.00 24.24 ? 159 THR A CG2 1 ATOM 1263 N N . GLN A 1 160 ? 48.119 4.602 21.020 1.00 21.63 ? 160 GLN A N 1 ATOM 1264 C CA . GLN A 1 160 ? 47.774 4.470 22.440 1.00 23.39 ? 160 GLN A CA 1 ATOM 1265 C C . GLN A 1 160 ? 46.268 4.239 22.571 1.00 21.42 ? 160 GLN A C 1 ATOM 1266 O O . GLN A 1 160 ? 45.793 3.488 23.415 1.00 20.80 ? 160 GLN A O 1 ATOM 1267 C CB . GLN A 1 160 ? 48.011 5.804 23.177 1.00 26.21 ? 160 GLN A CB 1 ATOM 1268 C CG . GLN A 1 160 ? 49.401 6.106 23.580 1.00 29.28 ? 160 GLN A CG 1 ATOM 1269 C CD . GLN A 1 160 ? 49.418 7.246 24.571 1.00 27.32 ? 160 GLN A CD 1 ATOM 1270 O OE1 . GLN A 1 160 ? 48.493 7.376 25.413 1.00 26.44 ? 160 GLN A OE1 1 ATOM 1271 N NE2 . GLN A 1 160 ? 50.466 8.040 24.523 1.00 27.85 ? 160 GLN A NE2 1 ATOM 1272 N N . VAL A 1 161 ? 45.502 4.988 21.801 1.00 21.87 ? 161 VAL A N 1 ATOM 1273 C CA . VAL A 1 161 ? 44.051 4.866 21.847 1.00 21.27 ? 161 VAL A CA 1 ATOM 1274 C C . VAL A 1 161 ? 43.605 3.435 21.579 1.00 21.64 ? 161 VAL A C 1 ATOM 1275 O O . VAL A 1 161 ? 42.605 2.959 22.159 1.00 21.63 ? 161 VAL A O 1 ATOM 1276 C CB . VAL A 1 161 ? 43.418 5.840 20.834 1.00 23.01 ? 161 VAL A CB 1 ATOM 1277 C CG1 . VAL A 1 161 ? 41.960 5.496 20.527 1.00 22.41 ? 161 VAL A CG1 1 ATOM 1278 C CG2 . VAL A 1 161 ? 43.547 7.277 21.378 1.00 23.87 ? 161 VAL A CG2 1 ATOM 1279 N N . GLU A 1 162 ? 44.326 2.741 20.704 1.00 21.44 ? 162 GLU A N 1 ATOM 1280 C CA . GLU A 1 162 ? 43.944 1.370 20.382 1.00 21.22 ? 162 GLU A CA 1 ATOM 1281 C C . GLU A 1 162 ? 44.588 0.341 21.316 1.00 21.10 ? 162 GLU A C 1 ATOM 1282 O O . GLU A 1 162 ? 43.960 -0.663 21.667 1.00 20.81 ? 162 GLU A O 1 ATOM 1283 C CB . GLU A 1 162 ? 44.290 0.997 18.931 1.00 22.50 ? 162 GLU A CB 1 ATOM 1284 C CG . GLU A 1 162 ? 43.607 1.926 17.911 1.00 23.28 ? 162 GLU A CG 1 ATOM 1285 C CD . GLU A 1 162 ? 44.124 1.761 16.472 1.00 24.32 ? 162 GLU A CD 1 ATOM 1286 O OE1 . GLU A 1 162 ? 45.223 1.166 16.245 1.00 23.53 ? 162 GLU A OE1 1 ATOM 1287 O OE2 . GLU A 1 162 ? 43.408 2.243 15.566 1.00 25.17 ? 162 GLU A OE2 1 ATOM 1288 N N . ASP A 1 163 ? 45.852 0.574 21.677 1.00 18.99 ? 163 ASP A N 1 ATOM 1289 C CA . ASP A 1 163 ? 46.624 -0.434 22.404 1.00 20.22 ? 163 ASP A CA 1 ATOM 1290 C C . ASP A 1 163 ? 46.583 -0.344 23.939 1.00 20.69 ? 163 ASP A C 1 ATOM 1291 O O . ASP A 1 163 ? 46.895 -1.346 24.616 1.00 21.28 ? 163 ASP A O 1 ATOM 1292 C CB . ASP A 1 163 ? 48.084 -0.436 21.907 1.00 22.74 ? 163 ASP A CB 1 ATOM 1293 C CG . ASP A 1 163 ? 48.207 -0.883 20.452 1.00 26.25 ? 163 ASP A CG 1 ATOM 1294 O OD1 . ASP A 1 163 ? 47.185 -1.314 19.847 1.00 28.49 ? 163 ASP A OD1 1 ATOM 1295 O OD2 . ASP A 1 163 ? 49.317 -0.777 19.896 1.00 25.64 ? 163 ASP A OD2 1 ATOM 1296 N N . CYS A 1 164 ? 46.272 0.831 24.500 1.00 20.60 ? 164 CYS A N 1 ATOM 1297 C CA . CYS A 1 164 ? 46.244 0.946 25.963 1.00 20.57 ? 164 CYS A CA 1 ATOM 1298 C C . CYS A 1 164 ? 44.806 0.836 26.473 1.00 21.67 ? 164 CYS A C 1 ATOM 1299 O O . CYS A 1 164 ? 43.866 0.768 25.684 1.00 21.26 ? 164 CYS A O 1 ATOM 1300 C CB . CYS A 1 164 ? 46.868 2.240 26.447 0.65 19.51 ? 164 CYS A CB 1 ATOM 1301 S SG . CYS A 1 164 ? 48.649 2.276 26.180 0.65 22.13 ? 164 CYS A SG 1 ATOM 1302 N N . TRP A 1 165 ? 44.651 0.797 27.799 1.00 21.46 ? 165 TRP A N 1 ATOM 1303 C CA . TRP A 1 165 ? 43.387 0.451 28.395 1.00 19.49 ? 165 TRP A CA 1 ATOM 1304 C C . TRP A 1 165 ? 42.551 1.676 28.766 1.00 20.99 ? 165 TRP A C 1 ATOM 1305 O O . TRP A 1 165 ? 43.067 2.703 29.240 1.00 20.21 ? 165 TRP A O 1 ATOM 1306 C CB . TRP A 1 165 ? 43.636 -0.274 29.717 1.00 21.12 ? 165 TRP A CB 1 ATOM 1307 C CG . TRP A 1 165 ? 44.273 -1.639 29.682 1.00 20.45 ? 165 TRP A CG 1 ATOM 1308 C CD1 . TRP A 1 165 ? 45.043 -2.201 28.708 1.00 22.31 ? 165 TRP A CD1 1 ATOM 1309 C CD2 . TRP A 1 165 ? 44.208 -2.590 30.745 1.00 20.20 ? 165 TRP A CD2 1 ATOM 1310 N NE1 . TRP A 1 165 ? 45.442 -3.473 29.093 1.00 20.73 ? 165 TRP A NE1 1 ATOM 1311 C CE2 . TRP A 1 165 ? 44.939 -3.734 30.342 1.00 21.65 ? 165 TRP A CE2 1 ATOM 1312 C CE3 . TRP A 1 165 ? 43.567 -2.596 31.990 1.00 20.99 ? 165 TRP A CE3 1 ATOM 1313 C CZ2 . TRP A 1 165 ? 45.059 -4.857 31.150 1.00 20.62 ? 165 TRP A CZ2 1 ATOM 1314 C CZ3 . TRP A 1 165 ? 43.690 -3.683 32.787 1.00 22.26 ? 165 TRP A CZ3 1 ATOM 1315 C CH2 . TRP A 1 165 ? 44.429 -4.822 32.368 1.00 21.44 ? 165 TRP A CH2 1 ATOM 1316 N N . LEU A 1 166 ? 41.247 1.529 28.585 1.00 21.23 ? 166 LEU A N 1 ATOM 1317 C CA . LEU A 1 166 ? 40.302 2.445 29.182 1.00 21.55 ? 166 LEU A CA 1 ATOM 1318 C C . LEU A 1 166 ? 40.159 2.182 30.676 1.00 21.42 ? 166 LEU A C 1 ATOM 1319 O O . LEU A 1 166 ? 40.699 1.188 31.213 1.00 22.06 ? 166 LEU A O 1 ATOM 1320 C CB . LEU A 1 166 ? 38.948 2.270 28.514 1.00 21.94 ? 166 LEU A CB 1 ATOM 1321 C CG . LEU A 1 166 ? 38.933 2.775 27.068 1.00 23.60 ? 166 LEU A CG 1 ATOM 1322 C CD1 . LEU A 1 166 ? 37.681 2.266 26.352 1.00 24.13 ? 166 LEU A CD1 1 ATOM 1323 C CD2 . LEU A 1 166 ? 38.985 4.317 26.995 1.00 23.47 ? 166 LEU A CD2 1 ATOM 1324 N N . GLY A 1 167 ? 39.406 3.068 31.336 1.00 22.61 ? 167 GLY A N 1 ATOM 1325 C CA . GLY A 1 167 ? 39.126 2.909 32.747 1.00 21.30 ? 167 GLY A CA 1 ATOM 1326 C C . GLY A 1 167 ? 40.264 3.439 33.606 1.00 22.78 ? 167 GLY A C 1 ATOM 1327 O O . GLY A 1 167 ? 41.111 4.256 33.161 1.00 23.37 ? 167 GLY A O 1 ATOM 1328 N N . ASP A 1 168 ? 40.262 3.035 34.871 1.00 23.22 ? 168 ASP A N 1 ATOM 1329 C CA . ASP A 1 168 ? 41.288 3.507 35.799 1.00 23.82 ? 168 ASP A CA 1 ATOM 1330 C C . ASP A 1 168 ? 41.525 2.413 36.830 1.00 24.23 ? 168 ASP A C 1 ATOM 1331 O O . ASP A 1 168 ? 41.142 1.256 36.594 1.00 23.55 ? 168 ASP A O 1 ATOM 1332 C CB . ASP A 1 168 ? 40.878 4.854 36.439 1.00 23.56 ? 168 ASP A CB 1 ATOM 1333 C CG . ASP A 1 168 ? 39.561 4.780 37.217 1.00 26.80 ? 168 ASP A CG 1 ATOM 1334 O OD1 . ASP A 1 168 ? 39.127 3.663 37.619 1.00 26.92 ? 168 ASP A OD1 1 ATOM 1335 O OD2 . ASP A 1 168 ? 38.950 5.864 37.420 1.00 26.70 ? 168 ASP A OD2 1 ATOM 1336 N N . ASN A 1 169 ? 42.172 2.731 37.941 1.00 25.71 ? 169 ASN A N 1 ATOM 1337 C CA . ASN A 1 169 ? 42.458 1.684 38.926 1.00 25.37 ? 169 ASN A CA 1 ATOM 1338 C C . ASN A 1 169 ? 41.304 1.391 39.896 1.00 24.65 ? 169 ASN A C 1 ATOM 1339 O O . ASN A 1 169 ? 41.437 0.530 40.787 1.00 27.12 ? 169 ASN A O 1 ATOM 1340 C CB . ASN A 1 169 ? 43.771 1.984 39.672 1.00 25.59 ? 169 ASN A CB 1 ATOM 1341 C CG . ASN A 1 169 ? 45.019 1.701 38.826 1.00 27.66 ? 169 ASN A CG 1 ATOM 1342 O OD1 . ASN A 1 169 ? 45.115 0.681 38.162 1.00 28.85 ? 169 ASN A OD1 1 ATOM 1343 N ND2 . ASN A 1 169 ? 46.018 2.590 38.915 1.00 28.52 ? 169 ASN A ND2 1 ATOM 1344 N N . THR A 1 170 ? 40.171 2.061 39.728 1.00 22.45 ? 170 THR A N 1 ATOM 1345 C CA . THR A 1 170 ? 38.969 1.692 40.489 1.00 23.34 ? 170 THR A CA 1 ATOM 1346 C C . THR A 1 170 ? 38.153 0.684 39.692 1.00 22.59 ? 170 THR A C 1 ATOM 1347 O O . THR A 1 170 ? 37.805 -0.385 40.203 1.00 24.16 ? 170 THR A O 1 ATOM 1348 C CB . THR A 1 170 ? 38.148 2.935 40.833 1.00 25.94 ? 170 THR A CB 1 ATOM 1349 O OG1 . THR A 1 170 ? 38.934 3.758 41.704 1.00 28.46 ? 170 THR A OG1 1 ATOM 1350 C CG2 . THR A 1 170 ? 36.800 2.541 41.507 1.00 27.44 ? 170 THR A CG2 1 ATOM 1351 N N . VAL A 1 171 ? 37.852 1.017 38.441 1.00 22.01 ? 171 VAL A N 1 ATOM 1352 C CA . VAL A 1 171 ? 37.269 0.000 37.555 1.00 20.90 ? 171 VAL A CA 1 ATOM 1353 C C . VAL A 1 171 ? 38.124 0.022 36.302 1.00 20.63 ? 171 VAL A C 1 ATOM 1354 O O . VAL A 1 171 ? 38.174 1.016 35.593 1.00 22.15 ? 171 VAL A O 1 ATOM 1355 C CB . VAL A 1 171 ? 35.803 0.272 37.254 1.00 21.36 ? 171 VAL A CB 1 ATOM 1356 C CG1 . VAL A 1 171 ? 35.301 -0.654 36.145 1.00 23.42 ? 171 VAL A CG1 1 ATOM 1357 C CG2 . VAL A 1 171 ? 35.010 0.059 38.538 1.00 24.67 ? 171 VAL A CG2 1 ATOM 1358 N N . SER A 1 172 ? 38.868 -1.061 36.092 1.00 21.39 ? 172 SER A N 1 ATOM 1359 C CA . SER A 1 172 ? 39.772 -1.107 34.941 1.00 21.08 ? 172 SER A CA 1 ATOM 1360 C C . SER A 1 172 ? 39.091 -1.852 33.827 1.00 21.55 ? 172 SER A C 1 ATOM 1361 O O . SER A 1 172 ? 38.194 -2.661 34.078 1.00 21.46 ? 172 SER A O 1 ATOM 1362 C CB . SER A 1 172 ? 41.090 -1.786 35.322 1.00 21.39 ? 172 SER A CB 1 ATOM 1363 O OG . SER A 1 172 ? 40.875 -3.038 35.943 1.00 23.01 ? 172 SER A OG 1 ATOM 1364 N N . LEU A 1 173 ? 39.464 -1.559 32.580 1.00 20.61 ? 173 LEU A N 1 ATOM 1365 C CA . LEU A 1 173 ? 38.802 -2.202 31.439 1.00 20.85 ? 173 LEU A CA 1 ATOM 1366 C C . LEU A 1 173 ? 39.836 -2.967 30.608 1.00 20.30 ? 173 LEU A C 1 ATOM 1367 O O . LEU A 1 173 ? 40.355 -2.455 29.607 1.00 20.81 ? 173 LEU A O 1 ATOM 1368 C CB . LEU A 1 173 ? 38.106 -1.128 30.582 1.00 22.13 ? 173 LEU A CB 1 ATOM 1369 C CG . LEU A 1 173 ? 37.016 -0.348 31.338 1.00 22.82 ? 173 LEU A CG 1 ATOM 1370 C CD1 . LEU A 1 173 ? 36.310 0.686 30.418 1.00 22.40 ? 173 LEU A CD1 1 ATOM 1371 C CD2 . LEU A 1 173 ? 36.033 -1.318 31.991 1.00 23.94 ? 173 LEU A CD2 1 ATOM 1372 N N . PRO A 1 174 ? 40.188 -4.193 31.035 1.00 20.47 ? 174 PRO A N 1 ATOM 1373 C CA . PRO A 1 174 ? 41.275 -4.879 30.345 1.00 20.11 ? 174 PRO A CA 1 ATOM 1374 C C . PRO A 1 174 ? 41.077 -4.957 28.832 1.00 20.48 ? 174 PRO A C 1 ATOM 1375 O O . PRO A 1 174 ? 40.011 -5.359 28.346 1.00 20.91 ? 174 PRO A O 1 ATOM 1376 C CB . PRO A 1 174 ? 41.295 -6.265 30.994 1.00 20.15 ? 174 PRO A CB 1 ATOM 1377 C CG . PRO A 1 174 ? 40.769 -5.991 32.425 1.00 20.16 ? 174 PRO A CG 1 ATOM 1378 C CD . PRO A 1 174 ? 39.705 -4.939 32.214 1.00 20.25 ? 174 PRO A CD 1 ATOM 1379 N N . ASP A 1 175 ? 42.107 -4.532 28.114 1.00 20.13 ? 175 ASP A N 1 ATOM 1380 C CA . ASP A 1 175 ? 42.008 -4.293 26.657 1.00 18.50 ? 175 ASP A CA 1 ATOM 1381 C C . ASP A 1 175 ? 42.405 -5.534 25.866 1.00 19.96 ? 175 ASP A C 1 ATOM 1382 O O . ASP A 1 175 ? 43.560 -5.977 25.905 1.00 20.04 ? 175 ASP A O 1 ATOM 1383 C CB . ASP A 1 175 ? 42.916 -3.108 26.291 1.00 19.09 ? 175 ASP A CB 1 ATOM 1384 C CG . ASP A 1 175 ? 42.551 -2.493 24.959 1.00 19.23 ? 175 ASP A CG 1 ATOM 1385 O OD1 . ASP A 1 175 ? 41.436 -1.894 24.890 1.00 19.17 ? 175 ASP A OD1 1 ATOM 1386 O OD2 . ASP A 1 175 ? 43.341 -2.636 23.999 1.00 20.64 ? 175 ASP A OD2 1 ATOM 1387 N N . LEU A 1 176 ? 41.453 -6.122 25.160 1.00 19.81 ? 176 LEU A N 1 ATOM 1388 C CA . LEU A 1 176 ? 41.753 -7.344 24.379 1.00 21.40 ? 176 LEU A CA 1 ATOM 1389 C C . LEU A 1 176 ? 42.740 -7.042 23.254 1.00 20.80 ? 176 LEU A C 1 ATOM 1390 O O . LEU A 1 176 ? 42.689 -5.977 22.644 1.00 22.00 ? 176 LEU A O 1 ATOM 1391 C CB . LEU A 1 176 ? 40.462 -7.949 23.802 1.00 23.47 ? 176 LEU A CB 1 ATOM 1392 C CG . LEU A 1 176 ? 39.641 -8.694 24.866 1.00 23.93 ? 176 LEU A CG 1 ATOM 1393 C CD1 . LEU A 1 176 ? 38.185 -8.830 24.457 1.00 26.70 ? 176 LEU A CD1 1 ATOM 1394 C CD2 . LEU A 1 176 ? 40.251 -10.051 25.149 1.00 23.24 ? 176 LEU A CD2 1 ATOM 1395 N N . ASP A 1 177 ? 43.681 -7.965 23.009 1.00 20.80 ? 177 ASP A N 1 ATOM 1396 C CA . ASP A 1 177 ? 44.576 -7.750 21.879 1.00 21.09 ? 177 ASP A CA 1 ATOM 1397 C C . ASP A 1 177 ? 43.896 -8.203 20.588 1.00 20.47 ? 177 ASP A C 1 ATOM 1398 O O . ASP A 1 177 ? 44.027 -9.357 20.155 1.00 21.89 ? 177 ASP A O 1 ATOM 1399 C CB . ASP A 1 177 ? 45.904 -8.466 22.064 1.00 21.57 ? 177 ASP A CB 1 ATOM 1400 C CG . ASP A 1 177 ? 46.888 -8.108 20.971 1.00 23.85 ? 177 ASP A CG 1 ATOM 1401 O OD1 . ASP A 1 177 ? 46.454 -7.537 19.940 1.00 22.61 ? 177 ASP A OD1 1 ATOM 1402 O OD2 . ASP A 1 177 ? 48.096 -8.412 21.159 1.00 26.03 ? 177 ASP A OD2 1 ATOM 1403 N N . THR A 1 178 ? 43.139 -7.272 19.999 1.00 20.68 ? 178 THR A N 1 ATOM 1404 C CA . THR A 1 178 ? 42.338 -7.533 18.837 1.00 21.89 ? 178 THR A CA 1 ATOM 1405 C C . THR A 1 178 ? 43.164 -7.727 17.561 1.00 23.58 ? 178 THR A C 1 ATOM 1406 O O . THR A 1 178 ? 42.602 -7.889 16.457 1.00 22.06 ? 178 THR A O 1 ATOM 1407 C CB . THR A 1 178 ? 41.304 -6.405 18.682 1.00 21.78 ? 178 THR A CB 1 ATOM 1408 O OG1 . THR A 1 178 ? 41.989 -5.156 18.762 1.00 21.43 ? 178 THR A OG1 1 ATOM 1409 C CG2 . THR A 1 178 ? 40.291 -6.476 19.813 1.00 22.98 ? 178 THR A CG2 1 ATOM 1410 N N . THR A 1 179 ? 44.499 -7.714 17.692 1.00 21.39 ? 179 THR A N 1 ATOM 1411 C CA . THR A 1 179 ? 45.344 -8.004 16.530 1.00 22.72 ? 179 THR A CA 1 ATOM 1412 C C . THR A 1 179 ? 45.668 -9.492 16.478 1.00 22.63 ? 179 THR A C 1 ATOM 1413 O O . THR A 1 179 ? 46.207 -9.964 15.475 1.00 24.99 ? 179 THR A O 1 ATOM 1414 C CB . THR A 1 179 ? 46.673 -7.212 16.486 1.00 22.93 ? 179 THR A CB 1 ATOM 1415 O OG1 . THR A 1 179 ? 47.568 -7.700 17.506 1.00 22.25 ? 179 THR A OG1 1 ATOM 1416 C CG2 . THR A 1 179 ? 46.433 -5.703 16.600 1.00 22.54 ? 179 THR A CG2 1 ATOM 1417 N N . LYS A 1 180 ? 45.370 -10.236 17.547 1.00 21.43 ? 180 LYS A N 1 ATOM 1418 C CA . LYS A 1 180 ? 45.670 -11.679 17.570 1.00 22.74 ? 180 LYS A CA 1 ATOM 1419 C C . LYS A 1 180 ? 44.604 -12.491 16.872 1.00 22.41 ? 180 LYS A C 1 ATOM 1420 O O . LYS A 1 180 ? 43.416 -12.288 17.081 1.00 22.24 ? 180 LYS A O 1 ATOM 1421 C CB . LYS A 1 180 ? 45.792 -12.207 18.998 1.00 23.57 ? 180 LYS A CB 1 ATOM 1422 C CG . LYS A 1 180 ? 46.926 -11.597 19.796 1.00 26.24 ? 180 LYS A CG 1 ATOM 1423 C CD . LYS A 1 180 ? 47.005 -12.239 21.163 1.00 27.79 ? 180 LYS A CD 1 ATOM 1424 C CE . LYS A 1 180 ? 48.076 -11.560 22.008 1.00 29.90 ? 180 LYS A CE 1 ATOM 1425 N NZ . LYS A 1 180 ? 49.429 -11.911 21.478 1.00 30.41 ? 180 LYS A NZ 1 ATOM 1426 N N . ASP A 1 181 ? 45.016 -13.464 16.078 1.00 22.29 ? 181 ASP A N 1 ATOM 1427 C CA . ASP A 1 181 ? 44.050 -14.328 15.445 1.00 23.90 ? 181 ASP A CA 1 ATOM 1428 C C . ASP A 1 181 ? 43.135 -15.053 16.429 1.00 23.11 ? 181 ASP A C 1 ATOM 1429 O O . ASP A 1 181 ? 41.957 -15.222 16.131 1.00 26.28 ? 181 ASP A O 1 ATOM 1430 C CB . ASP A 1 181 ? 44.773 -15.377 14.593 1.00 25.92 ? 181 ASP A CB 1 ATOM 1431 C CG . ASP A 1 181 ? 45.396 -14.787 13.346 1.00 29.56 ? 181 ASP A CG 1 ATOM 1432 O OD1 . ASP A 1 181 ? 45.117 -13.627 13.012 1.00 32.33 ? 181 ASP A OD1 1 ATOM 1433 O OD2 . ASP A 1 181 ? 46.176 -15.503 12.687 1.00 33.05 ? 181 ASP A OD2 1 ATOM 1434 N N . VAL A 1 182 ? 43.640 -15.495 17.579 1.00 23.58 ? 182 VAL A N 1 ATOM 1435 C CA . VAL A 1 182 ? 42.769 -16.232 18.491 1.00 24.81 ? 182 VAL A CA 1 ATOM 1436 C C . VAL A 1 182 ? 41.667 -15.310 19.016 1.00 24.36 ? 182 VAL A C 1 ATOM 1437 O O . VAL A 1 182 ? 40.532 -15.758 19.212 1.00 25.45 ? 182 VAL A O 1 ATOM 1438 C CB . VAL A 1 182 ? 43.486 -16.922 19.679 1.00 25.56 ? 182 VAL A CB 1 ATOM 1439 C CG1 . VAL A 1 182 ? 44.321 -18.100 19.194 1.00 26.98 ? 182 VAL A CG1 1 ATOM 1440 C CG2 . VAL A 1 182 ? 44.309 -15.919 20.463 1.00 26.49 ? 182 VAL A CG2 1 ATOM 1441 N N . VAL A 1 183 ? 41.999 -14.032 19.224 1.00 22.50 ? 183 VAL A N 1 ATOM 1442 C CA . VAL A 1 183 ? 40.996 -13.060 19.659 1.00 22.40 ? 183 VAL A CA 1 ATOM 1443 C C . VAL A 1 183 ? 40.001 -12.752 18.567 1.00 22.98 ? 183 VAL A C 1 ATOM 1444 O O . VAL A 1 183 ? 38.787 -12.795 18.807 1.00 22.74 ? 183 VAL A O 1 ATOM 1445 C CB . VAL A 1 183 ? 41.599 -11.764 20.209 1.00 21.80 ? 183 VAL A CB 1 ATOM 1446 C CG1 . VAL A 1 183 ? 40.466 -10.743 20.486 1.00 21.51 ? 183 VAL A CG1 1 ATOM 1447 C CG2 . VAL A 1 183 ? 42.419 -12.074 21.477 1.00 22.86 ? 183 VAL A CG2 1 ATOM 1448 N N . LYS A 1 184 ? 40.493 -12.447 17.371 1.00 22.99 ? 184 LYS A N 1 ATOM 1449 C CA . LYS A 1 184 ? 39.600 -12.204 16.240 1.00 23.41 ? 184 LYS A CA 1 ATOM 1450 C C . LYS A 1 184 ? 38.665 -13.370 16.015 1.00 23.34 ? 184 LYS A C 1 ATOM 1451 O O . LYS A 1 184 ? 37.451 -13.197 15.891 1.00 22.64 ? 184 LYS A O 1 ATOM 1452 C CB . LYS A 1 184 ? 40.381 -11.943 14.949 1.00 23.90 ? 184 LYS A CB 1 ATOM 1453 C CG . LYS A 1 184 ? 41.158 -10.656 14.944 1.00 28.00 ? 184 LYS A CG 1 ATOM 1454 C CD . LYS A 1 184 ? 42.292 -10.747 13.944 1.00 31.34 ? 184 LYS A CD 1 ATOM 1455 C CE . LYS A 1 184 ? 42.034 -9.890 12.743 1.00 34.59 ? 184 LYS A CE 1 ATOM 1456 N NZ . LYS A 1 184 ? 42.307 -8.463 13.070 1.00 36.70 ? 184 LYS A NZ 1 ATOM 1457 N N . ASN A 1 185 ? 39.226 -14.569 15.938 1.00 22.82 ? 185 ASN A N 1 ATOM 1458 C CA . ASN A 1 185 ? 38.403 -15.736 15.610 1.00 23.91 ? 185 ASN A CA 1 ATOM 1459 C C . ASN A 1 185 ? 37.348 -15.972 16.692 1.00 23.23 ? 185 ASN A C 1 ATOM 1460 O O . ASN A 1 185 ? 36.207 -16.331 16.397 1.00 23.21 ? 185 ASN A O 1 ATOM 1461 C CB . ASN A 1 185 ? 39.288 -16.957 15.403 1.00 25.51 ? 185 ASN A CB 1 ATOM 1462 C CG . ASN A 1 185 ? 40.170 -16.827 14.146 1.00 27.26 ? 185 ASN A CG 1 ATOM 1463 O OD1 . ASN A 1 185 ? 39.884 -16.008 13.266 1.00 28.61 ? 185 ASN A OD1 1 ATOM 1464 N ND2 . ASN A 1 185 ? 41.230 -17.608 14.076 1.00 29.68 ? 185 ASN A ND2 1 ATOM 1465 N N . GLU A 1 186 ? 37.724 -15.748 17.946 1.00 22.72 ? 186 GLU A N 1 ATOM 1466 C CA . GLU A 1 186 ? 36.779 -15.968 19.021 1.00 21.48 ? 186 GLU A CA 1 ATOM 1467 C C . GLU A 1 186 ? 35.640 -14.935 18.919 1.00 21.23 ? 186 GLU A C 1 ATOM 1468 O O . GLU A 1 186 ? 34.463 -15.290 19.023 1.00 22.73 ? 186 GLU A O 1 ATOM 1469 C CB . GLU A 1 186 ? 37.440 -15.870 20.389 1.00 25.75 ? 186 GLU A CB 1 ATOM 1470 C CG . GLU A 1 186 ? 36.467 -16.186 21.538 1.00 28.71 ? 186 GLU A CG 1 ATOM 1471 C CD . GLU A 1 186 ? 36.138 -17.674 21.623 1.00 30.74 ? 186 GLU A CD 1 ATOM 1472 O OE1 . GLU A 1 186 ? 37.064 -18.476 21.464 1.00 32.58 ? 186 GLU A OE1 1 ATOM 1473 O OE2 . GLU A 1 186 ? 34.966 -18.035 21.880 1.00 32.80 ? 186 GLU A OE2 1 ATOM 1474 N N . TRP A 1 187 ? 35.981 -13.658 18.741 1.00 20.51 ? 187 TRP A N 1 ATOM 1475 C CA . TRP A 1 187 ? 34.932 -12.637 18.632 1.00 19.83 ? 187 TRP A CA 1 ATOM 1476 C C . TRP A 1 187 ? 34.046 -12.859 17.398 1.00 20.23 ? 187 TRP A C 1 ATOM 1477 O O . TRP A 1 187 ? 32.844 -12.602 17.463 1.00 22.62 ? 187 TRP A O 1 ATOM 1478 C CB . TRP A 1 187 ? 35.524 -11.229 18.544 1.00 20.67 ? 187 TRP A CB 1 ATOM 1479 C CG . TRP A 1 187 ? 35.770 -10.522 19.856 1.00 20.81 ? 187 TRP A CG 1 ATOM 1480 C CD1 . TRP A 1 187 ? 36.882 -9.774 20.190 1.00 21.52 ? 187 TRP A CD1 1 ATOM 1481 C CD2 . TRP A 1 187 ? 34.883 -10.438 20.986 1.00 20.31 ? 187 TRP A CD2 1 ATOM 1482 N NE1 . TRP A 1 187 ? 36.716 -9.229 21.453 1.00 21.46 ? 187 TRP A NE1 1 ATOM 1483 C CE2 . TRP A 1 187 ? 35.493 -9.601 21.946 1.00 21.70 ? 187 TRP A CE2 1 ATOM 1484 C CE3 . TRP A 1 187 ? 33.608 -10.951 21.260 1.00 21.07 ? 187 TRP A CE3 1 ATOM 1485 C CZ2 . TRP A 1 187 ? 34.894 -9.314 23.176 1.00 22.13 ? 187 TRP A CZ2 1 ATOM 1486 C CZ3 . TRP A 1 187 ? 33.022 -10.658 22.486 1.00 21.21 ? 187 TRP A CZ3 1 ATOM 1487 C CH2 . TRP A 1 187 ? 33.648 -9.839 23.417 1.00 20.85 ? 187 TRP A CH2 1 ATOM 1488 N N . TYR A 1 188 ? 34.637 -13.278 16.279 1.00 22.32 ? 188 TYR A N 1 ATOM 1489 C CA . TYR A 1 188 ? 33.859 -13.459 15.050 1.00 22.27 ? 188 TYR A CA 1 ATOM 1490 C C . TYR A 1 188 ? 32.871 -14.627 15.221 1.00 22.08 ? 188 TYR A C 1 ATOM 1491 O O . TYR A 1 188 ? 31.708 -14.546 14.780 1.00 22.66 ? 188 TYR A O 1 ATOM 1492 C CB . TYR A 1 188 ? 34.770 -13.669 13.829 1.00 21.35 ? 188 TYR A CB 1 ATOM 1493 C CG . TYR A 1 188 ? 35.688 -12.496 13.494 1.00 21.33 ? 188 TYR A CG 1 ATOM 1494 C CD1 . TYR A 1 188 ? 35.568 -11.253 14.110 1.00 21.38 ? 188 TYR A CD1 1 ATOM 1495 C CD2 . TYR A 1 188 ? 36.652 -12.623 12.500 1.00 20.64 ? 188 TYR A CD2 1 ATOM 1496 C CE1 . TYR A 1 188 ? 36.428 -10.186 13.771 1.00 20.69 ? 188 TYR A CE1 1 ATOM 1497 C CE2 . TYR A 1 188 ? 37.489 -11.585 12.171 1.00 20.67 ? 188 TYR A CE2 1 ATOM 1498 C CZ . TYR A 1 188 ? 37.368 -10.362 12.779 1.00 20.89 ? 188 TYR A CZ 1 ATOM 1499 O OH . TYR A 1 188 ? 38.251 -9.382 12.382 1.00 21.76 ? 188 TYR A OH 1 ATOM 1500 N N . ASP A 1 189 ? 33.313 -15.707 15.857 1.00 22.41 ? 189 ASP A N 1 ATOM 1501 C CA . ASP A 1 189 ? 32.406 -16.827 16.175 1.00 23.86 ? 189 ASP A CA 1 ATOM 1502 C C . ASP A 1 189 ? 31.268 -16.341 17.083 1.00 22.76 ? 189 ASP A C 1 ATOM 1503 O O . ASP A 1 189 ? 30.098 -16.589 16.816 1.00 23.01 ? 189 ASP A O 1 ATOM 1504 C CB . ASP A 1 189 ? 33.152 -17.942 16.884 1.00 25.99 ? 189 ASP A CB 1 ATOM 1505 C CG . ASP A 1 189 ? 33.978 -18.770 15.945 1.00 30.05 ? 189 ASP A CG 1 ATOM 1506 O OD1 . ASP A 1 189 ? 33.899 -18.555 14.707 1.00 31.48 ? 189 ASP A OD1 1 ATOM 1507 O OD2 . ASP A 1 189 ? 34.703 -19.666 16.449 1.00 32.67 ? 189 ASP A OD2 1 ATOM 1508 N N . TRP A 1 190 ? 31.636 -15.631 18.140 1.00 20.85 ? 190 TRP A N 1 ATOM 1509 C CA . TRP A 1 190 ? 30.699 -15.112 19.101 1.00 20.81 ? 190 TRP A CA 1 ATOM 1510 C C . TRP A 1 190 ? 29.625 -14.253 18.453 1.00 20.96 ? 190 TRP A C 1 ATOM 1511 O O . TRP A 1 190 ? 28.433 -14.442 18.704 1.00 23.21 ? 190 TRP A O 1 ATOM 1512 C CB . TRP A 1 190 ? 31.445 -14.282 20.175 1.00 21.42 ? 190 TRP A CB 1 ATOM 1513 C CG . TRP A 1 190 ? 30.539 -13.715 21.183 1.00 21.58 ? 190 TRP A CG 1 ATOM 1514 C CD1 . TRP A 1 190 ? 30.052 -14.334 22.293 1.00 21.82 ? 190 TRP A CD1 1 ATOM 1515 C CD2 . TRP A 1 190 ? 30.002 -12.382 21.196 1.00 22.12 ? 190 TRP A CD2 1 ATOM 1516 N NE1 . TRP A 1 190 ? 29.227 -13.483 22.985 1.00 22.21 ? 190 TRP A NE1 1 ATOM 1517 C CE2 . TRP A 1 190 ? 29.201 -12.265 22.348 1.00 21.07 ? 190 TRP A CE2 1 ATOM 1518 C CE3 . TRP A 1 190 ? 30.130 -11.271 20.338 1.00 21.52 ? 190 TRP A CE3 1 ATOM 1519 C CZ2 . TRP A 1 190 ? 28.507 -11.080 22.661 1.00 21.52 ? 190 TRP A CZ2 1 ATOM 1520 C CZ3 . TRP A 1 190 ? 29.451 -10.097 20.654 1.00 22.31 ? 190 TRP A CZ3 1 ATOM 1521 C CH2 . TRP A 1 190 ? 28.660 -10.008 21.805 1.00 21.77 ? 190 TRP A CH2 1 ATOM 1522 N N . VAL A 1 191 ? 30.023 -13.267 17.657 1.00 20.04 ? 191 VAL A N 1 ATOM 1523 C CA . VAL A 1 191 ? 29.019 -12.271 17.219 1.00 20.32 ? 191 VAL A CA 1 ATOM 1524 C C . VAL A 1 191 ? 28.056 -12.922 16.223 1.00 20.38 ? 191 VAL A C 1 ATOM 1525 O O . VAL A 1 191 ? 26.848 -12.646 16.242 1.00 20.60 ? 191 VAL A O 1 ATOM 1526 C CB . VAL A 1 191 ? 29.659 -10.965 16.650 1.00 20.99 ? 191 VAL A CB 1 ATOM 1527 C CG1 . VAL A 1 191 ? 30.282 -11.183 15.277 1.00 20.56 ? 191 VAL A CG1 1 ATOM 1528 C CG2 . VAL A 1 191 ? 28.591 -9.828 16.573 1.00 22.05 ? 191 VAL A CG2 1 ATOM 1529 N N . GLY A 1 192 ? 28.558 -13.831 15.382 1.00 20.74 ? 192 GLY A N 1 ATOM 1530 C CA . GLY A 1 192 ? 27.667 -14.531 14.452 1.00 20.88 ? 192 GLY A CA 1 ATOM 1531 C C . GLY A 1 192 ? 26.669 -15.371 15.225 1.00 21.92 ? 192 GLY A C 1 ATOM 1532 O O . GLY A 1 192 ? 25.453 -15.352 14.928 1.00 22.61 ? 192 GLY A O 1 ATOM 1533 N N . SER A 1 193 ? 27.145 -16.061 16.250 1.00 21.05 ? 193 SER A N 1 ATOM 1534 C CA . SER A 1 193 ? 26.247 -16.912 17.046 1.00 22.61 ? 193 SER A CA 1 ATOM 1535 C C . SER A 1 193 ? 25.292 -16.113 17.958 1.00 21.95 ? 193 SER A C 1 ATOM 1536 O O . SER A 1 193 ? 24.164 -16.550 18.223 1.00 22.54 ? 193 SER A O 1 ATOM 1537 C CB . SER A 1 193 ? 27.006 -18.032 17.799 1.00 24.83 ? 193 SER A CB 1 ATOM 1538 O OG . SER A 1 193 ? 27.664 -17.520 18.921 1.00 26.86 ? 193 SER A OG 1 ATOM 1539 N N . LEU A 1 194 ? 25.727 -14.932 18.412 1.00 20.60 ? 194 LEU A N 1 ATOM 1540 C CA . LEU A 1 194 ? 24.865 -14.067 19.201 1.00 20.48 ? 194 LEU A CA 1 ATOM 1541 C C . LEU A 1 194 ? 23.693 -13.628 18.336 1.00 21.37 ? 194 LEU A C 1 ATOM 1542 O O . LEU A 1 194 ? 22.538 -13.696 18.748 1.00 21.52 ? 194 LEU A O 1 ATOM 1543 C CB . LEU A 1 194 ? 25.631 -12.817 19.685 1.00 20.41 ? 194 LEU A CB 1 ATOM 1544 C CG . LEU A 1 194 ? 24.737 -11.849 20.485 1.00 22.19 ? 194 LEU A CG 1 ATOM 1545 C CD1 . LEU A 1 194 ? 24.729 -12.259 21.985 1.00 23.26 ? 194 LEU A CD1 1 ATOM 1546 C CD2 . LEU A 1 194 ? 25.278 -10.460 20.376 1.00 23.44 ? 194 LEU A CD2 1 ATOM 1547 N N . VAL A 1 195 ? 24.008 -13.178 17.114 1.00 21.65 ? 195 VAL A N 1 ATOM 1548 C CA . VAL A 1 195 ? 22.990 -12.686 16.202 1.00 22.50 ? 195 VAL A CA 1 ATOM 1549 C C . VAL A 1 195 ? 21.991 -13.783 15.858 1.00 22.23 ? 195 VAL A C 1 ATOM 1550 O O . VAL A 1 195 ? 20.777 -13.542 15.833 1.00 21.79 ? 195 VAL A O 1 ATOM 1551 C CB . VAL A 1 195 ? 23.665 -12.047 14.967 1.00 23.12 ? 195 VAL A CB 1 ATOM 1552 C CG1 . VAL A 1 195 ? 22.681 -11.849 13.796 1.00 24.67 ? 195 VAL A CG1 1 ATOM 1553 C CG2 . VAL A 1 195 ? 24.308 -10.724 15.405 1.00 22.19 ? 195 VAL A CG2 1 ATOM 1554 N N . SER A 1 196 ? 22.512 -14.983 15.605 1.00 23.06 ? 196 SER A N 1 ATOM 1555 C CA . SER A 1 196 ? 21.694 -16.138 15.267 1.00 24.06 ? 196 SER A CA 1 ATOM 1556 C C . SER A 1 196 ? 20.811 -16.530 16.451 1.00 24.11 ? 196 SER A C 1 ATOM 1557 O O . SER A 1 196 ? 19.602 -16.721 16.286 1.00 24.01 ? 196 SER A O 1 ATOM 1558 C CB . SER A 1 196 ? 22.587 -17.326 14.858 1.00 24.91 ? 196 SER A CB 1 ATOM 1559 O OG . SER A 1 196 ? 21.802 -18.495 14.755 1.00 28.83 ? 196 SER A OG 1 ATOM 1560 N N . ASN A 1 197 ? 21.407 -16.679 17.633 1.00 22.52 ? 197 ASN A N 1 ATOM 1561 C CA . ASN A 1 197 ? 20.656 -17.195 18.768 1.00 23.13 ? 197 ASN A CA 1 ATOM 1562 C C . ASN A 1 197 ? 19.503 -16.302 19.162 1.00 23.64 ? 197 ASN A C 1 ATOM 1563 O O . ASN A 1 197 ? 18.446 -16.796 19.547 1.00 24.71 ? 197 ASN A O 1 ATOM 1564 C CB . ASN A 1 197 ? 21.538 -17.429 19.981 1.00 23.14 ? 197 ASN A CB 1 ATOM 1565 C CG . ASN A 1 197 ? 22.538 -18.555 19.777 1.00 23.33 ? 197 ASN A CG 1 ATOM 1566 O OD1 . ASN A 1 197 ? 22.580 -19.214 18.719 1.00 22.40 ? 197 ASN A OD1 1 ATOM 1567 N ND2 . ASN A 1 197 ? 23.331 -18.799 20.828 1.00 25.14 ? 197 ASN A ND2 1 ATOM 1568 N N . TYR A 1 198 ? 19.697 -14.987 19.083 1.00 22.03 ? 198 TYR A N 1 ATOM 1569 C CA . TYR A 1 198 ? 18.662 -14.068 19.547 1.00 23.05 ? 198 TYR A CA 1 ATOM 1570 C C . TYR A 1 198 ? 17.910 -13.354 18.418 1.00 23.54 ? 198 TYR A C 1 ATOM 1571 O O . TYR A 1 198 ? 17.108 -12.438 18.691 1.00 25.66 ? 198 TYR A O 1 ATOM 1572 C CB . TYR A 1 198 ? 19.245 -13.088 20.583 1.00 24.77 ? 198 TYR A CB 1 ATOM 1573 C CG . TYR A 1 198 ? 19.893 -13.845 21.717 1.00 25.49 ? 198 TYR A CG 1 ATOM 1574 C CD1 . TYR A 1 198 ? 19.108 -14.563 22.617 1.00 25.87 ? 198 TYR A CD1 1 ATOM 1575 C CD2 . TYR A 1 198 ? 21.280 -13.914 21.852 1.00 26.85 ? 198 TYR A CD2 1 ATOM 1576 C CE1 . TYR A 1 198 ? 19.661 -15.291 23.644 1.00 25.80 ? 198 TYR A CE1 1 ATOM 1577 C CE2 . TYR A 1 198 ? 21.864 -14.668 22.890 1.00 26.16 ? 198 TYR A CE2 1 ATOM 1578 C CZ . TYR A 1 198 ? 21.044 -15.351 23.773 1.00 26.39 ? 198 TYR A CZ 1 ATOM 1579 O OH . TYR A 1 198 ? 21.548 -16.112 24.806 1.00 27.30 ? 198 TYR A OH 1 ATOM 1580 N N . SER A 1 199 ? 18.128 -13.791 17.173 1.00 24.02 ? 199 SER A N 1 ATOM 1581 C CA . SER A 1 199 ? 17.483 -13.154 16.023 1.00 23.41 ? 199 SER A CA 1 ATOM 1582 C C . SER A 1 199 ? 17.621 -11.644 16.046 1.00 23.85 ? 199 SER A C 1 ATOM 1583 O O . SER A 1 199 ? 16.632 -10.917 15.935 1.00 23.56 ? 199 SER A O 1 ATOM 1584 C CB . SER A 1 199 ? 16.006 -13.521 15.973 1.00 25.52 ? 199 SER A CB 1 ATOM 1585 O OG . SER A 1 199 ? 15.866 -14.930 15.884 1.00 28.68 ? 199 SER A OG 1 ATOM 1586 N N . ILE A 1 200 ? 18.856 -11.172 16.211 1.00 22.01 ? 200 ILE A N 1 ATOM 1587 C CA . ILE A 1 200 ? 19.154 -9.747 16.266 1.00 22.08 ? 200 ILE A CA 1 ATOM 1588 C C . ILE A 1 200 ? 19.238 -9.162 14.849 1.00 22.17 ? 200 ILE A C 1 ATOM 1589 O O . ILE A 1 200 ? 19.802 -9.770 13.957 1.00 22.94 ? 200 ILE A O 1 ATOM 1590 C CB . ILE A 1 200 ? 20.471 -9.527 17.022 1.00 22.69 ? 200 ILE A CB 1 ATOM 1591 C CG1 . ILE A 1 200 ? 20.266 -9.930 18.488 1.00 23.86 ? 200 ILE A CG1 1 ATOM 1592 C CG2 . ILE A 1 200 ? 20.898 -8.086 16.888 1.00 22.63 ? 200 ILE A CG2 1 ATOM 1593 C CD1 . ILE A 1 200 ? 21.536 -10.211 19.265 1.00 24.56 ? 200 ILE A CD1 1 ATOM 1594 N N . ASP A 1 201 ? 18.668 -7.977 14.655 1.00 20.40 ? 201 ASP A N 1 ATOM 1595 C CA . ASP A 1 201 ? 18.566 -7.383 13.327 1.00 20.85 ? 201 ASP A CA 1 ATOM 1596 C C . ASP A 1 201 ? 19.677 -6.425 12.982 1.00 21.53 ? 201 ASP A C 1 ATOM 1597 O O . ASP A 1 201 ? 19.914 -6.169 11.809 1.00 21.07 ? 201 ASP A O 1 ATOM 1598 C CB . ASP A 1 201 ? 17.242 -6.660 13.201 1.00 21.42 ? 201 ASP A CB 1 ATOM 1599 C CG . ASP A 1 201 ? 16.069 -7.595 13.435 1.00 21.94 ? 201 ASP A CG 1 ATOM 1600 O OD1 . ASP A 1 201 ? 15.887 -8.547 12.645 1.00 24.67 ? 201 ASP A OD1 1 ATOM 1601 O OD2 . ASP A 1 201 ? 15.373 -7.427 14.433 1.00 22.43 ? 201 ASP A OD2 1 ATOM 1602 N N . GLY A 1 202 ? 20.356 -5.900 14.009 1.00 21.37 ? 202 GLY A N 1 ATOM 1603 C CA . GLY A 1 202 ? 21.423 -4.920 13.793 1.00 22.71 ? 202 GLY A CA 1 ATOM 1604 C C . GLY A 1 202 ? 22.243 -4.825 15.056 1.00 22.67 ? 202 GLY A C 1 ATOM 1605 O O . GLY A 1 202 ? 21.768 -5.234 16.117 1.00 21.77 ? 202 GLY A O 1 ATOM 1606 N N . LEU A 1 203 ? 23.472 -4.285 14.953 1.00 20.07 ? 203 LEU A N 1 ATOM 1607 C CA . LEU A 1 203 ? 24.272 -4.064 16.145 1.00 19.20 ? 203 LEU A CA 1 ATOM 1608 C C . LEU A 1 203 ? 24.745 -2.634 16.231 1.00 20.29 ? 203 LEU A C 1 ATOM 1609 O O . LEU A 1 203 ? 25.013 -2.012 15.194 1.00 20.48 ? 203 LEU A O 1 ATOM 1610 C CB . LEU A 1 203 ? 25.540 -4.931 16.072 1.00 19.30 ? 203 LEU A CB 1 ATOM 1611 C CG . LEU A 1 203 ? 25.291 -6.448 16.015 1.00 17.85 ? 203 LEU A CG 1 ATOM 1612 C CD1 . LEU A 1 203 ? 26.659 -7.183 15.904 1.00 20.09 ? 203 LEU A CD1 1 ATOM 1613 C CD2 . LEU A 1 203 ? 24.566 -6.913 17.263 1.00 20.39 ? 203 LEU A CD2 1 ATOM 1614 N N . ARG A 1 204 ? 24.859 -2.132 17.462 1.00 19.13 ? 204 ARG A N 1 ATOM 1615 C CA . ARG A 1 204 ? 25.565 -0.879 17.706 1.00 21.08 ? 204 ARG A CA 1 ATOM 1616 C C . ARG A 1 204 ? 26.843 -1.302 18.363 1.00 22.07 ? 204 ARG A C 1 ATOM 1617 O O . ARG A 1 204 ? 26.802 -2.037 19.373 1.00 20.75 ? 204 ARG A O 1 ATOM 1618 C CB . ARG A 1 204 ? 24.745 0.017 18.641 1.00 21.49 ? 204 ARG A CB 1 ATOM 1619 C CG . ARG A 1 204 ? 25.378 1.372 18.992 1.00 22.50 ? 204 ARG A CG 1 ATOM 1620 C CD . ARG A 1 204 ? 26.262 1.249 20.264 1.00 22.10 ? 204 ARG A CD 1 ATOM 1621 N NE . ARG A 1 204 ? 26.673 2.567 20.751 1.00 22.11 ? 204 ARG A NE 1 ATOM 1622 C CZ . ARG A 1 204 ? 27.425 2.755 21.825 1.00 22.47 ? 204 ARG A CZ 1 ATOM 1623 N NH1 . ARG A 1 204 ? 27.908 1.701 22.484 1.00 22.84 ? 204 ARG A NH1 1 ATOM 1624 N NH2 . ARG A 1 204 ? 27.690 3.998 22.237 1.00 22.20 ? 204 ARG A NH2 1 ATOM 1625 N N . ILE A 1 205 ? 27.957 -0.851 17.805 1.00 21.32 ? 205 ILE A N 1 ATOM 1626 C CA . ILE A 1 205 ? 29.264 -1.321 18.274 1.00 20.82 ? 205 ILE A CA 1 ATOM 1627 C C . ILE A 1 205 ? 29.937 -0.222 19.097 1.00 20.25 ? 205 ILE A C 1 ATOM 1628 O O . ILE A 1 205 ? 30.163 0.895 18.632 1.00 21.28 ? 205 ILE A O 1 ATOM 1629 C CB . ILE A 1 205 ? 30.130 -1.753 17.101 1.00 20.99 ? 205 ILE A CB 1 ATOM 1630 C CG1 . ILE A 1 205 ? 29.423 -2.856 16.298 1.00 21.05 ? 205 ILE A CG1 1 ATOM 1631 C CG2 . ILE A 1 205 ? 31.500 -2.236 17.596 1.00 22.12 ? 205 ILE A CG2 1 ATOM 1632 C CD1 . ILE A 1 205 ? 30.268 -3.388 15.147 1.00 24.32 ? 205 ILE A CD1 1 ATOM 1633 N N . ASP A 1 206 ? 30.225 -0.547 20.347 1.00 20.25 ? 206 ASP A N 1 ATOM 1634 C CA . ASP A 1 206 ? 30.796 0.382 21.288 1.00 19.68 ? 206 ASP A CA 1 ATOM 1635 C C . ASP A 1 206 ? 32.274 0.590 20.969 1.00 20.04 ? 206 ASP A C 1 ATOM 1636 O O . ASP A 1 206 ? 32.929 -0.292 20.331 1.00 20.26 ? 206 ASP A O 1 ATOM 1637 C CB . ASP A 1 206 ? 30.707 -0.290 22.670 1.00 21.22 ? 206 ASP A CB 1 ATOM 1638 C CG . ASP A 1 206 ? 31.135 0.624 23.786 1.00 24.61 ? 206 ASP A CG 1 ATOM 1639 O OD1 . ASP A 1 206 ? 30.444 1.663 23.904 1.00 22.83 ? 206 ASP A OD1 1 ATOM 1640 O OD2 . ASP A 1 206 ? 32.094 0.304 24.557 1.00 24.18 ? 206 ASP A OD2 1 ATOM 1641 N N . THR A 1 207 ? 32.803 1.743 21.401 1.00 20.74 ? 207 THR A N 1 ATOM 1642 C CA . THR A 1 207 ? 34.275 1.974 21.456 1.00 20.64 ? 207 THR A CA 1 ATOM 1643 C C . THR A 1 207 ? 35.052 1.581 20.202 1.00 21.32 ? 207 THR A C 1 ATOM 1644 O O . THR A 1 207 ? 36.187 1.069 20.273 1.00 20.72 ? 207 THR A O 1 ATOM 1645 C CB . THR A 1 207 ? 34.941 1.309 22.731 1.00 21.15 ? 207 THR A CB 1 ATOM 1646 O OG1 . THR A 1 207 ? 34.411 -0.004 22.944 1.00 21.82 ? 207 THR A OG1 1 ATOM 1647 C CG2 . THR A 1 207 ? 34.668 2.152 24.006 1.00 21.47 ? 207 THR A CG2 1 ATOM 1648 N N . VAL A 1 208 ? 34.493 1.918 19.045 1.00 19.68 ? 208 VAL A N 1 ATOM 1649 C CA . VAL A 1 208 ? 35.094 1.472 17.788 1.00 20.11 ? 208 VAL A CA 1 ATOM 1650 C C . VAL A 1 208 ? 36.519 2.028 17.555 1.00 20.50 ? 208 VAL A C 1 ATOM 1651 O O . VAL A 1 208 ? 37.388 1.316 17.025 1.00 21.98 ? 208 VAL A O 1 ATOM 1652 C CB . VAL A 1 208 ? 34.155 1.833 16.646 1.00 20.02 ? 208 VAL A CB 1 ATOM 1653 C CG1 . VAL A 1 208 ? 34.923 1.784 15.296 1.00 21.16 ? 208 VAL A CG1 1 ATOM 1654 C CG2 . VAL A 1 208 ? 32.936 0.872 16.690 1.00 21.43 ? 208 VAL A CG2 1 ATOM 1655 N N . LYS A 1 209 ? 36.741 3.283 17.935 1.00 20.59 ? 209 LYS A N 1 ATOM 1656 C CA . LYS A 1 209 ? 38.040 3.941 17.674 1.00 20.33 ? 209 LYS A CA 1 ATOM 1657 C C . LYS A 1 209 ? 39.150 3.312 18.522 1.00 19.99 ? 209 LYS A C 1 ATOM 1658 O O . LYS A 1 209 ? 40.338 3.589 18.306 1.00 20.28 ? 209 LYS A O 1 ATOM 1659 C CB . LYS A 1 209 ? 38.013 5.457 17.947 1.00 20.69 ? 209 LYS A CB 1 ATOM 1660 C CG . LYS A 1 209 ? 37.966 5.875 19.421 1.00 21.97 ? 209 LYS A CG 1 ATOM 1661 C CD . LYS A 1 209 ? 37.726 7.383 19.563 1.00 22.24 ? 209 LYS A CD 1 ATOM 1662 C CE . LYS A 1 209 ? 37.838 7.814 21.003 1.00 25.11 ? 209 LYS A CE 1 ATOM 1663 N NZ . LYS A 1 209 ? 37.784 9.343 21.116 1.00 26.57 ? 209 LYS A NZ 1 ATOM 1664 N N . HIS A 1 210 ? 38.764 2.511 19.532 1.00 20.22 ? 210 HIS A N 1 ATOM 1665 C CA . HIS A 1 210 ? 39.753 1.922 20.416 1.00 20.32 ? 210 HIS A CA 1 ATOM 1666 C C . HIS A 1 210 ? 40.207 0.551 19.951 1.00 20.52 ? 210 HIS A C 1 ATOM 1667 O O . HIS A 1 210 ? 41.021 -0.066 20.630 1.00 20.07 ? 210 HIS A O 1 ATOM 1668 C CB . HIS A 1 210 ? 39.170 1.823 21.840 1.00 21.61 ? 210 HIS A CB 1 ATOM 1669 C CG . HIS A 1 210 ? 39.001 3.157 22.487 1.00 20.63 ? 210 HIS A CG 1 ATOM 1670 N ND1 . HIS A 1 210 ? 40.065 3.875 23.003 1.00 22.19 ? 210 HIS A ND1 1 ATOM 1671 C CD2 . HIS A 1 210 ? 37.896 3.937 22.658 1.00 20.99 ? 210 HIS A CD2 1 ATOM 1672 C CE1 . HIS A 1 210 ? 39.618 5.038 23.467 1.00 20.75 ? 210 HIS A CE1 1 ATOM 1673 N NE2 . HIS A 1 210 ? 38.308 5.090 23.281 1.00 22.44 ? 210 HIS A NE2 1 ATOM 1674 N N . VAL A 1 211 ? 39.726 0.106 18.783 1.00 19.85 ? 211 VAL A N 1 ATOM 1675 C CA . VAL A 1 211 ? 40.128 -1.187 18.166 1.00 20.89 ? 211 VAL A CA 1 ATOM 1676 C C . VAL A 1 211 ? 40.634 -0.900 16.768 1.00 21.26 ? 211 VAL A C 1 ATOM 1677 O O . VAL A 1 211 ? 40.005 -0.130 16.034 1.00 21.72 ? 211 VAL A O 1 ATOM 1678 C CB . VAL A 1 211 ? 38.923 -2.171 18.082 1.00 21.58 ? 211 VAL A CB 1 ATOM 1679 C CG1 . VAL A 1 211 ? 39.295 -3.421 17.277 1.00 22.01 ? 211 VAL A CG1 1 ATOM 1680 C CG2 . VAL A 1 211 ? 38.463 -2.564 19.536 1.00 20.35 ? 211 VAL A CG2 1 ATOM 1681 N N . GLN A 1 212 ? 41.776 -1.485 16.392 1.00 21.10 ? 212 GLN A N 1 ATOM 1682 C CA . GLN A 1 212 ? 42.381 -1.187 15.081 1.00 20.88 ? 212 GLN A CA 1 ATOM 1683 C C . GLN A 1 212 ? 41.428 -1.484 13.921 1.00 21.39 ? 212 GLN A C 1 ATOM 1684 O O . GLN A 1 212 ? 40.619 -2.408 13.957 1.00 22.27 ? 212 GLN A O 1 ATOM 1685 C CB . GLN A 1 212 ? 43.740 -1.929 14.920 1.00 22.13 ? 212 GLN A CB 1 ATOM 1686 C CG . GLN A 1 212 ? 43.634 -3.334 14.320 1.00 22.26 ? 212 GLN A CG 1 ATOM 1687 C CD . GLN A 1 212 ? 43.199 -4.384 15.302 1.00 22.18 ? 212 GLN A CD 1 ATOM 1688 O OE1 . GLN A 1 212 ? 43.091 -4.129 16.501 1.00 21.30 ? 212 GLN A OE1 1 ATOM 1689 N NE2 . GLN A 1 212 ? 42.997 -5.597 14.815 1.00 21.85 ? 212 GLN A NE2 1 ATOM 1690 N N . LYS A 1 213 ? 41.513 -0.656 12.888 1.00 23.25 ? 213 LYS A N 1 ATOM 1691 C CA . LYS A 1 213 ? 40.536 -0.686 11.823 1.00 23.66 ? 213 LYS A CA 1 ATOM 1692 C C . LYS A 1 213 ? 40.390 -2.053 11.179 1.00 23.71 ? 213 LYS A C 1 ATOM 1693 O O . LYS A 1 213 ? 39.275 -2.427 10.833 1.00 25.62 ? 213 LYS A O 1 ATOM 1694 C CB . LYS A 1 213 ? 40.871 0.393 10.756 1.00 22.48 ? 213 LYS A CB 1 ATOM 1695 C CG . LYS A 1 213 ? 40.419 1.781 11.201 1.00 22.82 ? 213 LYS A CG 1 ATOM 1696 C CD . LYS A 1 213 ? 40.779 2.853 10.196 1.00 23.25 ? 213 LYS A CD 1 ATOM 1697 C CE . LYS A 1 213 ? 40.152 4.207 10.576 1.00 24.15 ? 213 LYS A CE 1 ATOM 1698 N NZ . LYS A 1 213 ? 40.680 5.318 9.708 1.00 25.19 ? 213 LYS A NZ 1 ATOM 1699 N N . ASP A 1 214 ? 41.485 -2.795 11.048 1.00 23.07 ? 214 ASP A N 1 ATOM 1700 C CA . ASP A 1 214 ? 41.471 -4.059 10.316 1.00 23.64 ? 214 ASP A CA 1 ATOM 1701 C C . ASP A 1 214 ? 40.835 -5.198 11.114 1.00 22.46 ? 214 ASP A C 1 ATOM 1702 O O . ASP A 1 214 ? 40.886 -6.358 10.704 1.00 24.11 ? 214 ASP A O 1 ATOM 1703 C CB . ASP A 1 214 ? 42.888 -4.445 9.886 1.00 23.07 ? 214 ASP A CB 1 ATOM 1704 C CG . ASP A 1 214 ? 43.692 -5.059 11.015 1.00 24.95 ? 214 ASP A CG 1 ATOM 1705 O OD1 . ASP A 1 214 ? 43.080 -5.640 11.936 1.00 26.02 ? 214 ASP A OD1 1 ATOM 1706 O OD2 . ASP A 1 214 ? 44.939 -5.010 11.067 1.00 27.99 ? 214 ASP A OD2 1 ATOM 1707 N N . PHE A 1 215 ? 40.239 -4.860 12.253 1.00 21.94 ? 215 PHE A N 1 ATOM 1708 C CA . PHE A 1 215 ? 39.418 -5.806 13.017 1.00 21.06 ? 215 PHE A CA 1 ATOM 1709 C C . PHE A 1 215 ? 37.983 -5.769 12.505 1.00 21.15 ? 215 PHE A C 1 ATOM 1710 O O . PHE A 1 215 ? 37.276 -6.793 12.490 1.00 21.95 ? 215 PHE A O 1 ATOM 1711 C CB . PHE A 1 215 ? 39.434 -5.437 14.513 1.00 19.73 ? 215 PHE A CB 1 ATOM 1712 C CG . PHE A 1 215 ? 38.611 -6.363 15.386 1.00 19.58 ? 215 PHE A CG 1 ATOM 1713 C CD1 . PHE A 1 215 ? 37.300 -6.043 15.687 1.00 18.66 ? 215 PHE A CD1 1 ATOM 1714 C CD2 . PHE A 1 215 ? 39.142 -7.537 15.883 1.00 19.88 ? 215 PHE A CD2 1 ATOM 1715 C CE1 . PHE A 1 215 ? 36.527 -6.853 16.503 1.00 21.21 ? 215 PHE A CE1 1 ATOM 1716 C CE2 . PHE A 1 215 ? 38.398 -8.355 16.700 1.00 20.43 ? 215 PHE A CE2 1 ATOM 1717 C CZ . PHE A 1 215 ? 37.071 -8.031 17.007 1.00 19.68 ? 215 PHE A CZ 1 ATOM 1718 N N . TRP A 1 216 ? 37.550 -4.583 12.074 1.00 21.12 ? 216 TRP A N 1 ATOM 1719 C CA . TRP A 1 216 ? 36.120 -4.359 11.909 1.00 20.29 ? 216 TRP A CA 1 ATOM 1720 C C . TRP A 1 216 ? 35.461 -5.045 10.692 1.00 20.97 ? 216 TRP A C 1 ATOM 1721 O O . TRP A 1 216 ? 34.352 -5.546 10.832 1.00 23.24 ? 216 TRP A O 1 ATOM 1722 C CB . TRP A 1 216 ? 35.799 -2.857 12.012 1.00 20.66 ? 216 TRP A CB 1 ATOM 1723 C CG . TRP A 1 216 ? 36.083 -2.340 13.403 1.00 19.43 ? 216 TRP A CG 1 ATOM 1724 C CD1 . TRP A 1 216 ? 36.963 -1.361 13.766 1.00 20.42 ? 216 TRP A CD1 1 ATOM 1725 C CD2 . TRP A 1 216 ? 35.492 -2.815 14.618 1.00 20.26 ? 216 TRP A CD2 1 ATOM 1726 N NE1 . TRP A 1 216 ? 36.965 -1.201 15.130 1.00 20.57 ? 216 TRP A NE1 1 ATOM 1727 C CE2 . TRP A 1 216 ? 36.051 -2.075 15.674 1.00 19.98 ? 216 TRP A CE2 1 ATOM 1728 C CE3 . TRP A 1 216 ? 34.506 -3.770 14.903 1.00 21.46 ? 216 TRP A CE3 1 ATOM 1729 C CZ2 . TRP A 1 216 ? 35.679 -2.278 17.019 1.00 20.19 ? 216 TRP A CZ2 1 ATOM 1730 C CZ3 . TRP A 1 216 ? 34.138 -3.969 16.254 1.00 20.97 ? 216 TRP A CZ3 1 ATOM 1731 C CH2 . TRP A 1 216 ? 34.721 -3.226 17.281 1.00 21.12 ? 216 TRP A CH2 1 ATOM 1732 N N . PRO A 1 217 ? 36.105 -5.065 9.500 1.00 21.86 ? 217 PRO A N 1 ATOM 1733 C CA . PRO A 1 217 ? 35.407 -5.700 8.368 1.00 21.60 ? 217 PRO A CA 1 ATOM 1734 C C . PRO A 1 217 ? 35.011 -7.156 8.647 1.00 22.92 ? 217 PRO A C 1 ATOM 1735 O O . PRO A 1 217 ? 33.863 -7.562 8.326 1.00 22.44 ? 217 PRO A O 1 ATOM 1736 C CB . PRO A 1 217 ? 36.431 -5.609 7.223 1.00 23.40 ? 217 PRO A CB 1 ATOM 1737 C CG . PRO A 1 217 ? 37.214 -4.423 7.560 1.00 22.37 ? 217 PRO A CG 1 ATOM 1738 C CD . PRO A 1 217 ? 37.400 -4.523 9.077 1.00 22.22 ? 217 PRO A CD 1 ATOM 1739 N N . GLY A 1 218 ? 35.931 -7.933 9.247 1.00 22.11 ? 218 GLY A N 1 ATOM 1740 C CA . GLY A 1 218 ? 35.637 -9.324 9.606 1.00 21.33 ? 218 GLY A CA 1 ATOM 1741 C C . GLY A 1 218 ? 34.548 -9.467 10.654 1.00 22.02 ? 218 GLY A C 1 ATOM 1742 O O . GLY A 1 218 ? 33.740 -10.388 10.613 1.00 22.33 ? 218 GLY A O 1 ATOM 1743 N N . TYR A 1 219 ? 34.511 -8.527 11.601 1.00 20.64 ? 219 TYR A N 1 ATOM 1744 C CA . TYR A 1 219 ? 33.482 -8.544 12.634 1.00 20.63 ? 219 TYR A CA 1 ATOM 1745 C C . TYR A 1 219 ? 32.101 -8.228 12.005 1.00 20.43 ? 219 TYR A C 1 ATOM 1746 O O . TYR A 1 219 ? 31.129 -8.919 12.279 1.00 21.79 ? 219 TYR A O 1 ATOM 1747 C CB . TYR A 1 219 ? 33.840 -7.502 13.699 1.00 20.94 ? 219 TYR A CB 1 ATOM 1748 C CG . TYR A 1 219 ? 33.003 -7.548 14.968 1.00 20.08 ? 219 TYR A CG 1 ATOM 1749 C CD1 . TYR A 1 219 ? 31.808 -6.821 15.059 1.00 21.02 ? 219 TYR A CD1 1 ATOM 1750 C CD2 . TYR A 1 219 ? 33.438 -8.271 16.086 1.00 21.13 ? 219 TYR A CD2 1 ATOM 1751 C CE1 . TYR A 1 219 ? 31.066 -6.852 16.214 1.00 20.35 ? 219 TYR A CE1 1 ATOM 1752 C CE2 . TYR A 1 219 ? 32.724 -8.304 17.228 1.00 20.39 ? 219 TYR A CE2 1 ATOM 1753 C CZ . TYR A 1 219 ? 31.512 -7.581 17.305 1.00 21.87 ? 219 TYR A CZ 1 ATOM 1754 O OH . TYR A 1 219 ? 30.772 -7.582 18.478 1.00 22.91 ? 219 TYR A OH 1 ATOM 1755 N N . ASN A 1 220 ? 32.039 -7.189 11.163 1.00 21.34 ? 220 ASN A N 1 ATOM 1756 C CA . ASN A 1 220 ? 30.785 -6.760 10.505 1.00 22.07 ? 220 ASN A CA 1 ATOM 1757 C C . ASN A 1 220 ? 30.298 -7.919 9.614 1.00 22.25 ? 220 ASN A C 1 ATOM 1758 O O . ASN A 1 220 ? 29.106 -8.203 9.578 1.00 21.90 ? 220 ASN A O 1 ATOM 1759 C CB . ASN A 1 220 ? 31.076 -5.475 9.683 1.00 22.36 ? 220 ASN A CB 1 ATOM 1760 C CG . ASN A 1 220 ? 29.851 -4.639 9.336 1.00 24.76 ? 220 ASN A CG 1 ATOM 1761 O OD1 . ASN A 1 220 ? 29.993 -3.407 9.171 1.00 25.39 ? 220 ASN A OD1 1 ATOM 1762 N ND2 . ASN A 1 220 ? 28.680 -5.257 9.191 1.00 24.92 ? 220 ASN A ND2 1 ATOM 1763 N N . LYS A 1 221 ? 31.205 -8.619 8.914 1.00 20.65 ? 221 LYS A N 1 ATOM 1764 C CA . LYS A 1 221 ? 30.797 -9.752 8.068 1.00 23.75 ? 221 LYS A CA 1 ATOM 1765 C C . LYS A 1 221 ? 30.275 -10.885 8.929 1.00 22.93 ? 221 LYS A C 1 ATOM 1766 O O . LYS A 1 221 ? 29.229 -11.452 8.642 1.00 21.13 ? 221 LYS A O 1 ATOM 1767 C CB . LYS A 1 221 ? 31.960 -10.282 7.208 1.00 24.90 ? 221 LYS A CB 1 ATOM 1768 C CG . LYS A 1 221 ? 31.505 -11.315 6.137 1.00 26.02 ? 221 LYS A CG 1 ATOM 1769 C CD . LYS A 1 221 ? 32.564 -12.362 5.774 1.00 29.87 ? 221 LYS A CD 1 ATOM 1770 C CE . LYS A 1 221 ? 31.934 -13.437 4.856 1.00 29.22 ? 221 LYS A CE 1 ATOM 1771 N NZ . LYS A 1 221 ? 32.583 -14.780 4.890 1.00 33.66 ? 221 LYS A NZ 1 ATOM 1772 N N . ALA A 1 222 ? 31.002 -11.198 10.007 1.00 23.53 ? 222 ALA A N 1 ATOM 1773 C CA . ALA A 1 222 ? 30.592 -12.294 10.894 1.00 23.84 ? 222 ALA A CA 1 ATOM 1774 C C . ALA A 1 222 ? 29.215 -12.026 11.509 1.00 22.83 ? 222 ALA A C 1 ATOM 1775 O O . ALA A 1 222 ? 28.431 -12.959 11.666 1.00 22.13 ? 222 ALA A O 1 ATOM 1776 C CB . ALA A 1 222 ? 31.624 -12.534 11.987 1.00 24.08 ? 222 ALA A CB 1 ATOM 1777 N N . ALA A 1 223 ? 28.927 -10.757 11.838 1.00 19.93 ? 223 ALA A N 1 ATOM 1778 C CA . ALA A 1 223 ? 27.638 -10.383 12.438 1.00 21.08 ? 223 ALA A CA 1 ATOM 1779 C C . ALA A 1 223 ? 26.532 -10.702 11.439 1.00 22.13 ? 223 ALA A C 1 ATOM 1780 O O . ALA A 1 223 ? 25.474 -11.226 11.815 1.00 23.65 ? 223 ALA A O 1 ATOM 1781 C CB . ALA A 1 223 ? 27.642 -8.897 12.785 1.00 20.47 ? 223 ALA A CB 1 ATOM 1782 N N . GLY A 1 224 ? 26.792 -10.385 10.171 1.00 21.62 ? 224 GLY A N 1 ATOM 1783 C CA . GLY A 1 224 ? 25.845 -10.651 9.081 1.00 21.41 ? 224 GLY A CA 1 ATOM 1784 C C . GLY A 1 224 ? 24.669 -9.705 9.007 1.00 22.53 ? 224 GLY A C 1 ATOM 1785 O O . GLY A 1 224 ? 23.682 -9.978 8.317 1.00 23.48 ? 224 GLY A O 1 ATOM 1786 N N . VAL A 1 225 ? 24.766 -8.606 9.756 1.00 20.20 ? 225 VAL A N 1 ATOM 1787 C CA . VAL A 1 225 ? 23.719 -7.597 9.841 1.00 21.46 ? 225 VAL A CA 1 ATOM 1788 C C . VAL A 1 225 ? 24.363 -6.213 9.801 1.00 20.90 ? 225 VAL A C 1 ATOM 1789 O O . VAL A 1 225 ? 25.591 -6.074 9.936 1.00 21.78 ? 225 VAL A O 1 ATOM 1790 C CB . VAL A 1 225 ? 22.894 -7.709 11.155 1.00 22.78 ? 225 VAL A CB 1 ATOM 1791 C CG1 . VAL A 1 225 ? 22.226 -9.079 11.253 1.00 22.60 ? 225 VAL A CG1 1 ATOM 1792 C CG2 . VAL A 1 225 ? 23.785 -7.484 12.409 1.00 23.35 ? 225 VAL A CG2 1 ATOM 1793 N N . TYR A 1 226 ? 23.533 -5.186 9.619 1.00 20.06 ? 226 TYR A N 1 ATOM 1794 C CA . TYR A 1 226 ? 23.999 -3.811 9.683 1.00 20.26 ? 226 TYR A CA 1 ATOM 1795 C C . TYR A 1 226 ? 24.650 -3.550 11.037 1.00 21.52 ? 226 TYR A C 1 ATOM 1796 O O . TYR A 1 226 ? 24.094 -3.907 12.068 1.00 22.52 ? 226 TYR A O 1 ATOM 1797 C CB . TYR A 1 226 ? 22.800 -2.895 9.536 1.00 20.59 ? 226 TYR A CB 1 ATOM 1798 C CG . TYR A 1 226 ? 23.061 -1.443 9.769 1.00 20.69 ? 226 TYR A CG 1 ATOM 1799 C CD1 . TYR A 1 226 ? 23.843 -0.703 8.877 1.00 20.75 ? 226 TYR A CD1 1 ATOM 1800 C CD2 . TYR A 1 226 ? 22.482 -0.777 10.852 1.00 22.20 ? 226 TYR A CD2 1 ATOM 1801 C CE1 . TYR A 1 226 ? 24.076 0.660 9.079 1.00 22.14 ? 226 TYR A CE1 1 ATOM 1802 C CE2 . TYR A 1 226 ? 22.691 0.561 11.047 1.00 21.88 ? 226 TYR A CE2 1 ATOM 1803 C CZ . TYR A 1 226 ? 23.481 1.287 10.179 1.00 21.35 ? 226 TYR A CZ 1 ATOM 1804 O OH . TYR A 1 226 ? 23.661 2.631 10.473 1.00 22.51 ? 226 TYR A OH 1 ATOM 1805 N N . CYS A 1 227 ? 25.839 -2.940 11.005 1.00 22.43 ? 227 CYS A N 1 ATOM 1806 C CA . CYS A 1 227 ? 26.499 -2.477 12.223 1.00 19.79 ? 227 CYS A CA 1 ATOM 1807 C C . CYS A 1 227 ? 26.723 -0.989 12.163 1.00 21.56 ? 227 CYS A C 1 ATOM 1808 O O . CYS A 1 227 ? 27.253 -0.480 11.164 1.00 21.09 ? 227 CYS A O 1 ATOM 1809 C CB . CYS A 1 227 ? 27.861 -3.155 12.390 1.00 21.93 ? 227 CYS A CB 1 ATOM 1810 S SG . CYS A 1 227 ? 27.780 -4.959 12.611 1.00 23.16 ? 227 CYS A SG 1 ATOM 1811 N N . ILE A 1 228 ? 26.373 -0.322 13.258 1.00 19.61 ? 228 ILE A N 1 ATOM 1812 C CA . ILE A 1 228 ? 26.633 1.115 13.395 1.00 21.60 ? 228 ILE A CA 1 ATOM 1813 C C . ILE A 1 228 ? 27.602 1.291 14.541 1.00 22.03 ? 228 ILE A C 1 ATOM 1814 O O . ILE A 1 228 ? 27.361 0.827 15.663 1.00 21.78 ? 228 ILE A O 1 ATOM 1815 C CB . ILE A 1 228 ? 25.333 1.946 13.581 1.00 21.28 ? 228 ILE A CB 1 ATOM 1816 C CG1 . ILE A 1 228 ? 25.640 3.457 13.577 1.00 22.05 ? 228 ILE A CG1 1 ATOM 1817 C CG2 . ILE A 1 228 ? 24.556 1.533 14.856 1.00 21.35 ? 228 ILE A CG2 1 ATOM 1818 C CD1 . ILE A 1 228 ? 24.334 4.321 13.488 1.00 21.80 ? 228 ILE A CD1 1 ATOM 1819 N N . GLY A 1 229 ? 28.701 1.966 14.257 1.00 21.92 ? 229 GLY A N 1 ATOM 1820 C CA . GLY A 1 229 ? 29.768 2.092 15.252 1.00 23.67 ? 229 GLY A CA 1 ATOM 1821 C C . GLY A 1 229 ? 29.778 3.417 16.012 1.00 22.82 ? 229 GLY A C 1 ATOM 1822 O O . GLY A 1 229 ? 29.563 4.515 15.421 1.00 23.53 ? 229 GLY A O 1 ATOM 1823 N N . GLU A 1 230 ? 30.080 3.325 17.311 1.00 21.38 ? 230 GLU A N 1 ATOM 1824 C CA . GLU A 1 230 ? 30.334 4.536 18.128 1.00 21.42 ? 230 GLU A CA 1 ATOM 1825 C C . GLU A 1 230 ? 31.772 4.959 17.920 1.00 21.86 ? 230 GLU A C 1 ATOM 1826 O O . GLU A 1 230 ? 32.696 4.339 18.480 1.00 21.33 ? 230 GLU A O 1 ATOM 1827 C CB . GLU A 1 230 ? 30.106 4.244 19.612 1.00 22.36 ? 230 GLU A CB 1 ATOM 1828 C CG . GLU A 1 230 ? 30.336 5.505 20.439 1.00 24.20 ? 230 GLU A CG 1 ATOM 1829 C CD . GLU A 1 230 ? 30.996 5.280 21.801 1.00 27.34 ? 230 GLU A CD 1 ATOM 1830 O OE1 . GLU A 1 230 ? 31.571 4.190 22.069 1.00 26.25 ? 230 GLU A OE1 1 ATOM 1831 O OE2 . GLU A 1 230 ? 31.001 6.236 22.605 1.00 26.71 ? 230 GLU A OE2 1 ATOM 1832 N N . VAL A 1 231 ? 31.972 5.969 17.069 1.00 21.90 ? 231 VAL A N 1 ATOM 1833 C CA . VAL A 1 231 ? 33.305 6.590 16.930 1.00 22.47 ? 231 VAL A CA 1 ATOM 1834 C C . VAL A 1 231 ? 33.240 7.971 17.570 1.00 21.61 ? 231 VAL A C 1 ATOM 1835 O O . VAL A 1 231 ? 32.688 8.928 17.021 1.00 22.78 ? 231 VAL A O 1 ATOM 1836 C CB . VAL A 1 231 ? 33.765 6.664 15.477 1.00 21.58 ? 231 VAL A CB 1 ATOM 1837 C CG1 . VAL A 1 231 ? 35.081 7.375 15.399 1.00 22.32 ? 231 VAL A CG1 1 ATOM 1838 C CG2 . VAL A 1 231 ? 33.881 5.252 14.914 1.00 23.62 ? 231 VAL A CG2 1 ATOM 1839 N N . LEU A 1 232 ? 33.746 8.052 18.790 1.00 22.78 ? 232 LEU A N 1 ATOM 1840 C CA . LEU A 1 232 ? 33.508 9.241 19.605 1.00 24.63 ? 232 LEU A CA 1 ATOM 1841 C C . LEU A 1 232 ? 34.479 10.369 19.207 1.00 24.60 ? 232 LEU A C 1 ATOM 1842 O O . LEU A 1 232 ? 35.498 10.604 19.855 1.00 24.84 ? 232 LEU A O 1 ATOM 1843 C CB . LEU A 1 232 ? 33.614 8.859 21.086 1.00 26.86 ? 232 LEU A CB 1 ATOM 1844 C CG . LEU A 1 232 ? 32.905 9.747 22.133 1.00 31.68 ? 232 LEU A CG 1 ATOM 1845 C CD1 . LEU A 1 232 ? 33.543 9.451 23.500 1.00 33.20 ? 232 LEU A CD1 1 ATOM 1846 C CD2 . LEU A 1 232 ? 32.918 11.217 21.815 1.00 33.34 ? 232 LEU A CD2 1 ATOM 1847 N N . ASP A 1 233 ? 34.140 11.076 18.132 1.00 23.44 ? 233 ASP A N 1 ATOM 1848 C CA . ASP A 1 233 ? 34.991 12.176 17.651 1.00 24.06 ? 233 ASP A CA 1 ATOM 1849 C C . ASP A 1 233 ? 34.137 13.042 16.736 1.00 23.54 ? 233 ASP A C 1 ATOM 1850 O O . ASP A 1 233 ? 33.453 12.533 15.848 1.00 23.11 ? 233 ASP A O 1 ATOM 1851 C CB . ASP A 1 233 ? 36.198 11.639 16.879 1.00 25.08 ? 233 ASP A CB 1 ATOM 1852 C CG . ASP A 1 233 ? 37.312 12.672 16.733 1.00 26.16 ? 233 ASP A CG 1 ATOM 1853 O OD1 . ASP A 1 233 ? 37.059 13.740 16.161 1.00 27.81 ? 233 ASP A OD1 1 ATOM 1854 O OD2 . ASP A 1 233 ? 38.454 12.390 17.177 1.00 29.56 ? 233 ASP A OD2 1 ATOM 1855 N N . GLY A 1 234 ? 34.181 14.352 16.954 1.00 23.80 ? 234 GLY A N 1 ATOM 1856 C CA . GLY A 1 234 ? 33.390 15.286 16.166 1.00 22.54 ? 234 GLY A CA 1 ATOM 1857 C C . GLY A 1 234 ? 33.998 15.701 14.834 1.00 23.22 ? 234 GLY A C 1 ATOM 1858 O O . GLY A 1 234 ? 33.342 16.382 14.041 1.00 22.33 ? 234 GLY A O 1 ATOM 1859 N N . ASP A 1 235 ? 35.234 15.260 14.567 1.00 23.41 ? 235 ASP A N 1 ATOM 1860 C CA . ASP A 1 235 ? 35.890 15.629 13.317 1.00 23.59 ? 235 ASP A CA 1 ATOM 1861 C C . ASP A 1 235 ? 35.508 14.657 12.232 1.00 24.23 ? 235 ASP A C 1 ATOM 1862 O O . ASP A 1 235 ? 35.853 13.471 12.318 1.00 23.38 ? 235 ASP A O 1 ATOM 1863 C CB . ASP A 1 235 ? 37.412 15.594 13.496 1.00 25.05 ? 235 ASP A CB 1 ATOM 1864 C CG . ASP A 1 235 ? 38.151 16.118 12.271 1.00 26.73 ? 235 ASP A CG 1 ATOM 1865 O OD1 . ASP A 1 235 ? 37.539 16.238 11.172 1.00 26.92 ? 235 ASP A OD1 1 ATOM 1866 O OD2 . ASP A 1 235 ? 39.368 16.396 12.409 1.00 28.20 ? 235 ASP A OD2 1 ATOM 1867 N N . PRO A 1 236 ? 34.805 15.119 11.194 1.00 25.07 ? 236 PRO A N 1 ATOM 1868 C CA . PRO A 1 236 ? 34.383 14.183 10.129 1.00 24.57 ? 236 PRO A CA 1 ATOM 1869 C C . PRO A 1 236 ? 35.555 13.484 9.422 1.00 23.70 ? 236 PRO A C 1 ATOM 1870 O O . PRO A 1 236 ? 35.392 12.373 8.904 1.00 23.99 ? 236 PRO A O 1 ATOM 1871 C CB . PRO A 1 236 ? 33.576 15.063 9.154 1.00 25.93 ? 236 PRO A CB 1 ATOM 1872 C CG . PRO A 1 236 ? 33.939 16.479 9.516 1.00 24.25 ? 236 PRO A CG 1 ATOM 1873 C CD . PRO A 1 236 ? 34.331 16.499 10.962 1.00 24.11 ? 236 PRO A CD 1 ATOM 1874 N N . ALA A 1 237 ? 36.718 14.131 9.411 1.00 23.01 ? 237 ALA A N 1 ATOM 1875 C CA . ALA A 1 237 ? 37.932 13.572 8.764 1.00 23.27 ? 237 ALA A CA 1 ATOM 1876 C C . ALA A 1 237 ? 38.478 12.374 9.537 1.00 24.52 ? 237 ALA A C 1 ATOM 1877 O O . ALA A 1 237 ? 39.216 11.547 8.961 1.00 25.32 ? 237 ALA A O 1 ATOM 1878 C CB . ALA A 1 237 ? 38.986 14.630 8.636 1.00 24.66 ? 237 ALA A CB 1 ATOM 1879 N N . TYR A 1 238 ? 38.150 12.310 10.823 1.00 23.62 ? 238 TYR A N 1 ATOM 1880 C CA . TYR A 1 238 ? 38.570 11.193 11.691 1.00 22.15 ? 238 TYR A CA 1 ATOM 1881 C C . TYR A 1 238 ? 37.481 10.146 11.719 1.00 21.61 ? 238 TYR A C 1 ATOM 1882 O O . TYR A 1 238 ? 37.745 8.943 11.613 1.00 24.52 ? 238 TYR A O 1 ATOM 1883 C CB . TYR A 1 238 ? 38.826 11.686 13.109 1.00 22.24 ? 238 TYR A CB 1 ATOM 1884 C CG . TYR A 1 238 ? 39.231 10.613 14.112 1.00 22.02 ? 238 TYR A CG 1 ATOM 1885 C CD1 . TYR A 1 238 ? 38.266 9.918 14.818 1.00 22.88 ? 238 TYR A CD1 1 ATOM 1886 C CD2 . TYR A 1 238 ? 40.564 10.354 14.394 1.00 22.14 ? 238 TYR A CD2 1 ATOM 1887 C CE1 . TYR A 1 238 ? 38.623 8.934 15.766 1.00 22.32 ? 238 TYR A CE1 1 ATOM 1888 C CE2 . TYR A 1 238 ? 40.945 9.365 15.337 1.00 22.89 ? 238 TYR A CE2 1 ATOM 1889 C CZ . TYR A 1 238 ? 39.957 8.675 16.023 1.00 22.51 ? 238 TYR A CZ 1 ATOM 1890 O OH . TYR A 1 238 ? 40.308 7.711 16.953 1.00 23.33 ? 238 TYR A OH 1 ATOM 1891 N N . THR A 1 239 ? 36.238 10.604 11.844 1.00 22.16 ? 239 THR A N 1 ATOM 1892 C CA . THR A 1 239 ? 35.122 9.694 12.039 1.00 23.36 ? 239 THR A CA 1 ATOM 1893 C C . THR A 1 239 ? 34.546 9.036 10.796 1.00 25.05 ? 239 THR A C 1 ATOM 1894 O O . THR A 1 239 ? 34.290 7.829 10.798 1.00 24.97 ? 239 THR A O 1 ATOM 1895 C CB . THR A 1 239 ? 34.033 10.436 12.810 1.00 22.57 ? 239 THR A CB 1 ATOM 1896 O OG1 . THR A 1 239 ? 34.560 10.693 14.113 1.00 22.53 ? 239 THR A OG1 1 ATOM 1897 C CG2 . THR A 1 239 ? 32.784 9.593 12.947 1.00 23.17 ? 239 THR A CG2 1 ATOM 1898 N N . CYS A 1 240 ? 34.341 9.804 9.727 1.00 25.34 ? 240 CYS A N 1 ATOM 1899 C CA . CYS A 1 240 ? 33.738 9.202 8.532 1.00 27.26 ? 240 CYS A CA 1 ATOM 1900 C C . CYS A 1 240 ? 34.520 8.058 7.875 1.00 26.30 ? 240 CYS A C 1 ATOM 1901 O O . CYS A 1 240 ? 33.905 7.148 7.339 1.00 26.84 ? 240 CYS A O 1 ATOM 1902 C CB . CYS A 1 240 ? 33.328 10.262 7.519 1.00 30.35 ? 240 CYS A CB 1 ATOM 1903 S SG . CYS A 1 240 ? 31.808 11.028 8.152 1.00 37.18 ? 240 CYS A SG 1 ATOM 1904 N N . PRO A 1 241 ? 35.867 8.130 7.861 1.00 25.14 ? 241 PRO A N 1 ATOM 1905 C CA . PRO A 1 241 ? 36.633 7.000 7.320 1.00 24.45 ? 241 PRO A CA 1 ATOM 1906 C C . PRO A 1 241 ? 36.353 5.667 8.009 1.00 23.31 ? 241 PRO A C 1 ATOM 1907 O O . PRO A 1 241 ? 36.623 4.615 7.429 1.00 23.13 ? 241 PRO A O 1 ATOM 1908 C CB . PRO A 1 241 ? 38.077 7.410 7.548 1.00 24.94 ? 241 PRO A CB 1 ATOM 1909 C CG . PRO A 1 241 ? 38.047 8.934 7.492 1.00 26.06 ? 241 PRO A CG 1 ATOM 1910 C CD . PRO A 1 241 ? 36.735 9.269 8.221 1.00 25.99 ? 241 PRO A CD 1 ATOM 1911 N N . TYR A 1 242 ? 35.814 5.674 9.223 1.00 22.96 ? 242 TYR A N 1 ATOM 1912 C CA . TYR A 1 242 ? 35.466 4.378 9.796 1.00 23.62 ? 242 TYR A CA 1 ATOM 1913 C C . TYR A 1 242 ? 34.328 3.720 9.006 1.00 23.58 ? 242 TYR A C 1 ATOM 1914 O O . TYR A 1 242 ? 34.103 2.519 9.116 1.00 24.34 ? 242 TYR A O 1 ATOM 1915 C CB . TYR A 1 242 ? 35.112 4.508 11.292 1.00 22.49 ? 242 TYR A CB 1 ATOM 1916 C CG . TYR A 1 242 ? 36.333 4.578 12.170 1.00 22.84 ? 242 TYR A CG 1 ATOM 1917 C CD1 . TYR A 1 242 ? 36.859 3.409 12.784 1.00 21.47 ? 242 TYR A CD1 1 ATOM 1918 C CD2 . TYR A 1 242 ? 36.967 5.797 12.414 1.00 22.70 ? 242 TYR A CD2 1 ATOM 1919 C CE1 . TYR A 1 242 ? 37.975 3.475 13.572 1.00 21.27 ? 242 TYR A CE1 1 ATOM 1920 C CE2 . TYR A 1 242 ? 38.074 5.875 13.221 1.00 23.13 ? 242 TYR A CE2 1 ATOM 1921 C CZ . TYR A 1 242 ? 38.588 4.701 13.802 1.00 22.30 ? 242 TYR A CZ 1 ATOM 1922 O OH . TYR A 1 242 ? 39.709 4.757 14.615 1.00 22.69 ? 242 TYR A OH 1 ATOM 1923 N N . GLN A 1 243 ? 33.613 4.498 8.186 1.00 23.30 ? 243 GLN A N 1 ATOM 1924 C CA . GLN A 1 243 ? 32.620 3.887 7.325 1.00 25.12 ? 243 GLN A CA 1 ATOM 1925 C C . GLN A 1 243 ? 33.210 3.006 6.211 1.00 25.11 ? 243 GLN A C 1 ATOM 1926 O O . GLN A 1 243 ? 32.473 2.308 5.510 1.00 25.75 ? 243 GLN A O 1 ATOM 1927 C CB . GLN A 1 243 ? 31.672 4.928 6.721 1.00 27.31 ? 243 GLN A CB 1 ATOM 1928 C CG . GLN A 1 243 ? 30.280 4.396 6.595 1.00 28.78 ? 243 GLN A CG 1 ATOM 1929 C CD . GLN A 1 243 ? 29.297 5.455 6.174 1.00 28.08 ? 243 GLN A CD 1 ATOM 1930 O OE1 . GLN A 1 243 ? 29.685 6.574 5.809 1.00 29.25 ? 243 GLN A OE1 1 ATOM 1931 N NE2 . GLN A 1 243 ? 28.023 5.099 6.176 1.00 27.12 ? 243 GLN A NE2 1 ATOM 1932 N N . ASN A 1 244 ? 34.530 3.052 6.041 1.00 23.83 ? 244 ASN A N 1 ATOM 1933 C CA . ASN A 1 244 ? 35.196 2.169 5.089 1.00 25.82 ? 244 ASN A CA 1 ATOM 1934 C C . ASN A 1 244 ? 35.376 0.767 5.681 1.00 25.14 ? 244 ASN A C 1 ATOM 1935 O O . ASN A 1 244 ? 35.677 -0.190 4.948 1.00 27.73 ? 244 ASN A O 1 ATOM 1936 C CB . ASN A 1 244 ? 36.540 2.751 4.720 1.00 27.14 ? 244 ASN A CB 1 ATOM 1937 C CG . ASN A 1 244 ? 36.419 4.045 3.934 1.00 30.05 ? 244 ASN A CG 1 ATOM 1938 O OD1 . ASN A 1 244 ? 35.515 4.222 3.113 1.00 30.76 ? 244 ASN A OD1 1 ATOM 1939 N ND2 . ASN A 1 244 ? 37.345 4.956 4.178 1.00 33.32 ? 244 ASN A ND2 1 ATOM 1940 N N . VAL A 1 245 ? 35.212 0.640 7.005 1.00 24.34 ? 245 VAL A N 1 ATOM 1941 C CA . VAL A 1 245 ? 35.432 -0.659 7.658 1.00 23.02 ? 245 VAL A CA 1 ATOM 1942 C C . VAL A 1 245 ? 34.145 -1.191 8.320 1.00 24.07 ? 245 VAL A C 1 ATOM 1943 O O . VAL A 1 245 ? 34.085 -2.339 8.746 1.00 24.83 ? 245 VAL A O 1 ATOM 1944 C CB . VAL A 1 245 ? 36.637 -0.636 8.674 1.00 21.56 ? 245 VAL A CB 1 ATOM 1945 C CG1 . VAL A 1 245 ? 37.989 -0.359 7.941 1.00 21.80 ? 245 VAL A CG1 1 ATOM 1946 C CG2 . VAL A 1 245 ? 36.436 0.358 9.810 1.00 21.25 ? 245 VAL A CG2 1 ATOM 1947 N N . MET A 1 246 ? 33.107 -0.357 8.395 1.00 22.94 ? 246 MET A N 1 ATOM 1948 C CA . MET A 1 246 ? 31.890 -0.728 9.069 1.00 23.85 ? 246 MET A CA 1 ATOM 1949 C C . MET A 1 246 ? 30.736 -0.033 8.346 1.00 22.19 ? 246 MET A C 1 ATOM 1950 O O . MET A 1 246 ? 30.915 1.043 7.794 1.00 23.05 ? 246 MET A O 1 ATOM 1951 C CB . MET A 1 246 ? 32.004 -0.216 10.518 1.00 25.56 ? 246 MET A CB 1 ATOM 1952 C CG . MET A 1 246 ? 30.867 -0.418 11.389 1.00 27.20 ? 246 MET A CG 1 ATOM 1953 S SD . MET A 1 246 ? 31.330 -0.047 13.101 1.00 26.19 ? 246 MET A SD 1 ATOM 1954 C CE . MET A 1 246 ? 32.742 -1.143 13.369 1.00 23.24 ? 246 MET A CE 1 ATOM 1955 N N . ASP A 1 247 ? 29.548 -0.614 8.360 1.00 21.54 ? 247 ASP A N 1 ATOM 1956 C CA . ASP A 1 247 ? 28.434 -0.059 7.564 1.00 21.68 ? 247 ASP A CA 1 ATOM 1957 C C . ASP A 1 247 ? 28.096 1.393 7.863 1.00 21.85 ? 247 ASP A C 1 ATOM 1958 O O . ASP A 1 247 ? 27.919 2.210 6.953 1.00 22.60 ? 247 ASP A O 1 ATOM 1959 C CB . ASP A 1 247 ? 27.172 -0.895 7.752 1.00 21.89 ? 247 ASP A CB 1 ATOM 1960 C CG . ASP A 1 247 ? 27.362 -2.343 7.361 1.00 24.11 ? 247 ASP A CG 1 ATOM 1961 O OD1 . ASP A 1 247 ? 27.941 -2.632 6.278 1.00 24.06 ? 247 ASP A OD1 1 ATOM 1962 O OD2 . ASP A 1 247 ? 26.863 -3.204 8.122 1.00 24.63 ? 247 ASP A OD2 1 ATOM 1963 N N . GLY A 1 248 ? 27.990 1.697 9.146 1.00 22.40 ? 248 GLY A N 1 ATOM 1964 C CA . GLY A 1 248 ? 27.644 3.061 9.563 1.00 21.72 ? 248 GLY A CA 1 ATOM 1965 C C . GLY A 1 248 ? 28.406 3.475 10.808 1.00 21.05 ? 248 GLY A C 1 ATOM 1966 O O . GLY A 1 248 ? 29.004 2.632 11.494 1.00 20.54 ? 248 GLY A O 1 ATOM 1967 N N . VAL A 1 249 ? 28.347 4.781 11.117 1.00 21.18 ? 249 VAL A N 1 ATOM 1968 C CA . VAL A 1 249 ? 28.807 5.237 12.418 1.00 20.74 ? 249 VAL A CA 1 ATOM 1969 C C . VAL A 1 249 ? 27.794 6.230 12.971 1.00 20.95 ? 249 VAL A C 1 ATOM 1970 O O . VAL A 1 249 ? 27.024 6.835 12.207 1.00 22.26 ? 249 VAL A O 1 ATOM 1971 C CB . VAL A 1 249 ? 30.223 5.873 12.369 1.00 21.30 ? 249 VAL A CB 1 ATOM 1972 C CG1 . VAL A 1 249 ? 31.319 4.786 11.991 1.00 20.58 ? 249 VAL A CG1 1 ATOM 1973 C CG2 . VAL A 1 249 ? 30.262 7.079 11.396 1.00 22.88 ? 249 VAL A CG2 1 ATOM 1974 N N . LEU A 1 250 ? 27.797 6.399 14.292 1.00 19.79 ? 250 LEU A N 1 ATOM 1975 C CA . LEU A 1 250 ? 26.969 7.456 14.887 1.00 18.77 ? 250 LEU A CA 1 ATOM 1976 C C . LEU A 1 250 ? 27.455 8.809 14.418 1.00 20.49 ? 250 LEU A C 1 ATOM 1977 O O . LEU A 1 250 ? 28.669 9.044 14.284 1.00 21.09 ? 250 LEU A O 1 ATOM 1978 C CB . LEU A 1 250 ? 27.033 7.347 16.425 1.00 21.11 ? 250 LEU A CB 1 ATOM 1979 C CG . LEU A 1 250 ? 26.485 6.028 16.973 1.00 21.80 ? 250 LEU A CG 1 ATOM 1980 C CD1 . LEU A 1 250 ? 26.811 5.909 18.454 1.00 23.67 ? 250 LEU A CD1 1 ATOM 1981 C CD2 . LEU A 1 250 ? 24.987 6.014 16.754 1.00 25.41 ? 250 LEU A CD2 1 ATOM 1982 N N . ASN A 1 251 ? 26.503 9.704 14.184 1.00 20.86 ? 251 ASN A N 1 ATOM 1983 C CA . ASN A 1 251 ? 26.869 10.995 13.572 1.00 21.09 ? 251 ASN A CA 1 ATOM 1984 C C . ASN A 1 251 ? 27.379 12.008 14.597 1.00 21.34 ? 251 ASN A C 1 ATOM 1985 O O . ASN A 1 251 ? 26.771 13.066 14.807 1.00 19.75 ? 251 ASN A O 1 ATOM 1986 C CB . ASN A 1 251 ? 25.711 11.560 12.733 1.00 21.86 ? 251 ASN A CB 1 ATOM 1987 C CG . ASN A 1 251 ? 26.192 12.513 11.675 1.00 22.31 ? 251 ASN A CG 1 ATOM 1988 O OD1 . ASN A 1 251 ? 27.290 13.084 11.785 1.00 21.17 ? 251 ASN A OD1 1 ATOM 1989 N ND2 . ASN A 1 251 ? 25.361 12.728 10.644 1.00 22.66 ? 251 ASN A ND2 1 ATOM 1990 N N . TYR A 1 252 ? 28.514 11.691 15.239 1.00 20.07 ? 252 TYR A N 1 ATOM 1991 C CA . TYR A 1 252 ? 29.134 12.649 16.133 1.00 21.11 ? 252 TYR A CA 1 ATOM 1992 C C . TYR A 1 252 ? 29.544 13.967 15.446 1.00 20.80 ? 252 TYR A C 1 ATOM 1993 O O . TYR A 1 252 ? 29.509 15.013 16.077 1.00 21.91 ? 252 TYR A O 1 ATOM 1994 C CB . TYR A 1 252 ? 30.304 11.979 16.874 1.00 21.63 ? 252 TYR A CB 1 ATOM 1995 C CG . TYR A 1 252 ? 29.874 11.541 18.267 1.00 20.89 ? 252 TYR A CG 1 ATOM 1996 C CD1 . TYR A 1 252 ? 29.667 12.492 19.271 1.00 22.43 ? 252 TYR A CD1 1 ATOM 1997 C CD2 . TYR A 1 252 ? 29.636 10.205 18.570 1.00 21.56 ? 252 TYR A CD2 1 ATOM 1998 C CE1 . TYR A 1 252 ? 29.267 12.144 20.547 1.00 23.26 ? 252 TYR A CE1 1 ATOM 1999 C CE2 . TYR A 1 252 ? 29.222 9.816 19.862 1.00 21.94 ? 252 TYR A CE2 1 ATOM 2000 C CZ . TYR A 1 252 ? 29.028 10.793 20.862 1.00 22.39 ? 252 TYR A CZ 1 ATOM 2001 O OH . TYR A 1 252 ? 28.637 10.443 22.161 1.00 22.17 ? 252 TYR A OH 1 ATOM 2002 N N . PRO A 1 253 ? 30.007 13.912 14.183 1.00 20.35 ? 253 PRO A N 1 ATOM 2003 C CA . PRO A 1 253 ? 30.246 15.227 13.513 1.00 19.85 ? 253 PRO A CA 1 ATOM 2004 C C . PRO A 1 253 ? 29.065 16.218 13.511 1.00 20.38 ? 253 PRO A C 1 ATOM 2005 O O . PRO A 1 253 ? 29.280 17.411 13.752 1.00 20.54 ? 253 PRO A O 1 ATOM 2006 C CB . PRO A 1 253 ? 30.630 14.822 12.092 1.00 19.74 ? 253 PRO A CB 1 ATOM 2007 C CG . PRO A 1 253 ? 31.354 13.410 12.315 1.00 19.84 ? 253 PRO A CG 1 ATOM 2008 C CD . PRO A 1 253 ? 30.482 12.763 13.374 1.00 20.95 ? 253 PRO A CD 1 ATOM 2009 N N . ILE A 1 254 ? 27.856 15.734 13.254 1.00 18.38 ? 254 ILE A N 1 ATOM 2010 C CA . ILE A 1 254 ? 26.655 16.591 13.261 1.00 19.25 ? 254 ILE A CA 1 ATOM 2011 C C . ILE A 1 254 ? 26.248 16.941 14.694 1.00 20.35 ? 254 ILE A C 1 ATOM 2012 O O . ILE A 1 254 ? 25.777 18.060 14.938 1.00 20.42 ? 254 ILE A O 1 ATOM 2013 C CB . ILE A 1 254 ? 25.466 15.949 12.471 1.00 20.28 ? 254 ILE A CB 1 ATOM 2014 C CG1 . ILE A 1 254 ? 25.679 16.126 10.957 1.00 20.19 ? 254 ILE A CG1 1 ATOM 2015 C CG2 . ILE A 1 254 ? 24.062 16.558 12.889 1.00 20.38 ? 254 ILE A CG2 1 ATOM 2016 C CD1 . ILE A 1 254 ? 25.415 17.601 10.488 1.00 21.80 ? 254 ILE A CD1 1 ATOM 2017 N N . TYR A 1 255 ? 26.436 16.003 15.621 1.00 21.76 ? 255 TYR A N 1 ATOM 2018 C CA . TYR A 1 255 ? 26.085 16.222 17.031 1.00 22.23 ? 255 TYR A CA 1 ATOM 2019 C C . TYR A 1 255 ? 26.472 17.599 17.552 1.00 22.10 ? 255 TYR A C 1 ATOM 2020 O O . TYR A 1 255 ? 25.629 18.359 18.071 1.00 22.62 ? 255 TYR A O 1 ATOM 2021 C CB . TYR A 1 255 ? 26.710 15.120 17.911 1.00 22.18 ? 255 TYR A CB 1 ATOM 2022 C CG . TYR A 1 255 ? 26.484 15.392 19.374 1.00 22.19 ? 255 TYR A CG 1 ATOM 2023 C CD1 . TYR A 1 255 ? 25.199 15.488 19.888 1.00 23.52 ? 255 TYR A CD1 1 ATOM 2024 C CD2 . TYR A 1 255 ? 27.550 15.647 20.217 1.00 22.05 ? 255 TYR A CD2 1 ATOM 2025 C CE1 . TYR A 1 255 ? 24.990 15.786 21.260 1.00 22.45 ? 255 TYR A CE1 1 ATOM 2026 C CE2 . TYR A 1 255 ? 27.372 15.931 21.566 1.00 21.32 ? 255 TYR A CE2 1 ATOM 2027 C CZ . TYR A 1 255 ? 26.067 16.025 22.073 1.00 22.65 ? 255 TYR A CZ 1 ATOM 2028 O OH . TYR A 1 255 ? 25.843 16.325 23.418 1.00 22.78 ? 255 TYR A OH 1 ATOM 2029 N N . TYR A 1 256 ? 27.750 17.920 17.456 1.00 21.21 ? 256 TYR A N 1 ATOM 2030 C CA . TYR A 1 256 ? 28.255 19.161 18.078 1.00 21.51 ? 256 TYR A CA 1 ATOM 2031 C C . TYR A 1 256 ? 27.615 20.447 17.550 1.00 21.94 ? 256 TYR A C 1 ATOM 2032 O O . TYR A 1 256 ? 27.083 21.241 18.340 1.00 22.49 ? 256 TYR A O 1 ATOM 2033 C CB . TYR A 1 256 ? 29.808 19.208 18.114 1.00 22.31 ? 256 TYR A CB 1 ATOM 2034 C CG . TYR A 1 256 ? 30.369 18.035 18.901 1.00 22.09 ? 256 TYR A CG 1 ATOM 2035 C CD1 . TYR A 1 256 ? 30.288 17.998 20.298 1.00 24.21 ? 256 TYR A CD1 1 ATOM 2036 C CD2 . TYR A 1 256 ? 30.951 16.944 18.256 1.00 21.77 ? 256 TYR A CD2 1 ATOM 2037 C CE1 . TYR A 1 256 ? 30.769 16.893 21.032 1.00 22.56 ? 256 TYR A CE1 1 ATOM 2038 C CE2 . TYR A 1 256 ? 31.430 15.836 18.982 1.00 22.46 ? 256 TYR A CE2 1 ATOM 2039 C CZ . TYR A 1 256 ? 31.353 15.825 20.365 1.00 22.03 ? 256 TYR A CZ 1 ATOM 2040 O OH . TYR A 1 256 ? 31.830 14.722 21.051 1.00 24.34 ? 256 TYR A OH 1 ATOM 2041 N N . PRO A 1 257 ? 27.678 20.688 16.237 1.00 21.12 ? 257 PRO A N 1 ATOM 2042 C CA . PRO A 1 257 ? 26.999 21.891 15.692 1.00 21.17 ? 257 PRO A CA 1 ATOM 2043 C C . PRO A 1 257 ? 25.454 21.881 15.813 1.00 21.52 ? 257 PRO A C 1 ATOM 2044 O O . PRO A 1 257 ? 24.821 22.943 15.931 1.00 21.40 ? 257 PRO A O 1 ATOM 2045 C CB . PRO A 1 257 ? 27.450 21.911 14.222 1.00 22.02 ? 257 PRO A CB 1 ATOM 2046 C CG . PRO A 1 257 ? 27.884 20.495 13.919 1.00 22.54 ? 257 PRO A CG 1 ATOM 2047 C CD . PRO A 1 257 ? 28.435 19.946 15.196 1.00 22.07 ? 257 PRO A CD 1 ATOM 2048 N N . LEU A 1 258 ? 24.854 20.695 15.756 1.00 20.60 ? 258 LEU A N 1 ATOM 2049 C CA . LEU A 1 258 ? 23.414 20.572 15.971 1.00 21.47 ? 258 LEU A CA 1 ATOM 2050 C C . LEU A 1 258 ? 23.052 21.029 17.381 1.00 20.39 ? 258 LEU A C 1 ATOM 2051 O O . LEU A 1 258 ? 22.156 21.868 17.566 1.00 22.12 ? 258 LEU A O 1 ATOM 2052 C CB . LEU A 1 258 ? 22.984 19.114 15.806 1.00 21.82 ? 258 LEU A CB 1 ATOM 2053 C CG . LEU A 1 258 ? 21.490 18.871 16.118 1.00 22.06 ? 258 LEU A CG 1 ATOM 2054 C CD1 . LEU A 1 258 ? 20.574 19.696 15.192 1.00 23.19 ? 258 LEU A CD1 1 ATOM 2055 C CD2 . LEU A 1 258 ? 21.142 17.381 16.040 1.00 22.30 ? 258 LEU A CD2 1 ATOM 2056 N N . LEU A 1 259 ? 23.739 20.478 18.386 1.00 22.19 ? 259 LEU A N 1 ATOM 2057 C CA . LEU A 1 259 ? 23.491 20.893 19.760 1.00 23.04 ? 259 LEU A CA 1 ATOM 2058 C C . LEU A 1 259 ? 23.744 22.394 19.922 1.00 24.13 ? 259 LEU A C 1 ATOM 2059 O O . LEU A 1 259 ? 22.927 23.119 20.520 1.00 22.59 ? 259 LEU A O 1 ATOM 2060 C CB . LEU A 1 259 ? 24.386 20.088 20.739 1.00 23.60 ? 259 LEU A CB 1 ATOM 2061 C CG . LEU A 1 259 ? 24.379 20.598 22.192 1.00 22.04 ? 259 LEU A CG 1 ATOM 2062 C CD1 . LEU A 1 259 ? 23.014 20.408 22.832 1.00 23.88 ? 259 LEU A CD1 1 ATOM 2063 C CD2 . LEU A 1 259 ? 25.431 19.835 23.034 1.00 23.23 ? 259 LEU A CD2 1 ATOM 2064 N N . ASN A 1 260 ? 24.846 22.890 19.374 1.00 22.91 ? 260 ASN A N 1 ATOM 2065 C CA . ASN A 1 260 ? 25.121 24.316 19.557 1.00 24.67 ? 260 ASN A CA 1 ATOM 2066 C C . ASN A 1 260 ? 24.096 25.226 18.897 1.00 24.53 ? 260 ASN A C 1 ATOM 2067 O O . ASN A 1 260 ? 23.794 26.311 19.414 1.00 23.98 ? 260 ASN A O 1 ATOM 2068 C CB . ASN A 1 260 ? 26.530 24.665 19.106 1.00 27.95 ? 260 ASN A CB 1 ATOM 2069 C CG . ASN A 1 260 ? 27.599 24.073 20.039 1.00 30.84 ? 260 ASN A CG 1 ATOM 2070 O OD1 . ASN A 1 260 ? 27.351 23.810 21.218 1.00 30.74 ? 260 ASN A OD1 1 ATOM 2071 N ND2 . ASN A 1 260 ? 28.810 23.882 19.504 1.00 34.04 ? 260 ASN A ND2 1 ATOM 2072 N N . ALA A 1 261 ? 23.581 24.806 17.744 1.00 22.99 ? 261 ALA A N 1 ATOM 2073 C CA . ALA A 1 261 ? 22.619 25.668 17.020 1.00 22.62 ? 261 ALA A CA 1 ATOM 2074 C C . ALA A 1 261 ? 21.359 25.908 17.811 1.00 22.33 ? 261 ALA A C 1 ATOM 2075 O O . ALA A 1 261 ? 20.732 26.990 17.658 1.00 23.76 ? 261 ALA A O 1 ATOM 2076 C CB . ALA A 1 261 ? 22.249 25.038 15.719 1.00 22.42 ? 261 ALA A CB 1 ATOM 2077 N N . PHE A 1 262 ? 20.926 24.885 18.576 1.00 22.73 ? 262 PHE A N 1 ATOM 2078 C CA . PHE A 1 262 ? 19.591 24.950 19.212 1.00 23.36 ? 262 PHE A CA 1 ATOM 2079 C C . PHE A 1 262 ? 19.597 25.023 20.721 1.00 23.66 ? 262 PHE A C 1 ATOM 2080 O O . PHE A 1 262 ? 18.537 25.209 21.347 1.00 22.97 ? 262 PHE A O 1 ATOM 2081 C CB . PHE A 1 262 ? 18.713 23.773 18.795 1.00 23.30 ? 262 PHE A CB 1 ATOM 2082 C CG . PHE A 1 262 ? 18.359 23.799 17.336 1.00 24.12 ? 262 PHE A CG 1 ATOM 2083 C CD1 . PHE A 1 262 ? 17.337 24.617 16.874 1.00 23.66 ? 262 PHE A CD1 1 ATOM 2084 C CD2 . PHE A 1 262 ? 19.073 23.030 16.432 1.00 25.34 ? 262 PHE A CD2 1 ATOM 2085 C CE1 . PHE A 1 262 ? 17.031 24.664 15.524 1.00 23.64 ? 262 PHE A CE1 1 ATOM 2086 C CE2 . PHE A 1 262 ? 18.780 23.075 15.084 1.00 24.15 ? 262 PHE A CE2 1 ATOM 2087 C CZ . PHE A 1 262 ? 17.748 23.879 14.634 1.00 23.77 ? 262 PHE A CZ 1 ATOM 2088 N N . LYS A 1 263 ? 20.760 24.870 21.320 1.00 22.23 ? 263 LYS A N 1 ATOM 2089 C CA . LYS A 1 263 ? 20.776 24.868 22.784 1.00 24.11 ? 263 LYS A CA 1 ATOM 2090 C C . LYS A 1 263 ? 20.575 26.263 23.361 1.00 25.04 ? 263 LYS A C 1 ATOM 2091 O O . LYS A 1 263 ? 20.343 26.416 24.567 1.00 24.94 ? 263 LYS A O 1 ATOM 2092 C CB . LYS A 1 263 ? 22.037 24.200 23.318 1.00 25.31 ? 263 LYS A CB 1 ATOM 2093 C CG . LYS A 1 263 ? 23.251 25.084 23.284 1.00 26.05 ? 263 LYS A CG 1 ATOM 2094 C CD . LYS A 1 263 ? 24.463 24.297 23.797 1.00 28.79 ? 263 LYS A CD 1 ATOM 2095 C CE . LYS A 1 263 ? 25.529 25.251 24.247 1.00 31.62 ? 263 LYS A CE 1 ATOM 2096 N NZ . LYS A 1 263 ? 26.061 26.083 23.157 1.00 34.06 ? 263 LYS A NZ 1 ATOM 2097 N N . SER A 1 264 ? 20.624 27.280 22.512 1.00 24.03 ? 264 SER A N 1 ATOM 2098 C CA . SER A 1 264 ? 20.296 28.642 22.966 1.00 26.56 ? 264 SER A CA 1 ATOM 2099 C C . SER A 1 264 ? 19.829 29.458 21.782 1.00 27.70 ? 264 SER A C 1 ATOM 2100 O O . SER A 1 264 ? 20.044 29.074 20.639 1.00 26.57 ? 264 SER A O 1 ATOM 2101 C CB . SER A 1 264 ? 21.508 29.317 23.585 1.00 28.94 ? 264 SER A CB 1 ATOM 2102 O OG . SER A 1 264 ? 22.425 29.672 22.558 1.00 31.18 ? 264 SER A OG 1 ATOM 2103 N N . THR A 1 265 ? 19.209 30.599 22.064 1.00 27.74 ? 265 THR A N 1 ATOM 2104 C CA . THR A 1 265 ? 18.657 31.421 21.008 1.00 29.29 ? 265 THR A CA 1 ATOM 2105 C C . THR A 1 265 ? 19.769 32.139 20.232 1.00 30.64 ? 265 THR A C 1 ATOM 2106 O O . THR A 1 265 ? 19.503 32.838 19.270 1.00 32.05 ? 265 THR A O 1 ATOM 2107 C CB . THR A 1 265 ? 17.634 32.431 21.587 1.00 29.87 ? 265 THR A CB 1 ATOM 2108 O OG1 . THR A 1 265 ? 18.279 33.192 22.616 1.00 29.69 ? 265 THR A OG1 1 ATOM 2109 C CG2 . THR A 1 265 ? 16.466 31.664 22.201 1.00 30.03 ? 265 THR A CG2 1 ATOM 2110 N N . SER A 1 266 ? 21.018 31.959 20.632 1.00 31.33 ? 266 SER A N 1 ATOM 2111 C CA . SER A 1 266 ? 22.104 32.580 19.870 1.00 32.78 ? 266 SER A CA 1 ATOM 2112 C C . SER A 1 266 ? 23.034 31.550 19.222 1.00 33.33 ? 266 SER A C 1 ATOM 2113 O O . SER A 1 266 ? 24.165 31.870 18.825 1.00 32.20 ? 266 SER A O 1 ATOM 2114 C CB . SER A 1 266 ? 22.878 33.560 20.747 1.00 34.36 ? 266 SER A CB 1 ATOM 2115 O OG . SER A 1 266 ? 23.530 32.866 21.788 1.00 35.58 ? 266 SER A OG 1 ATOM 2116 N N . GLY A 1 267 ? 22.553 30.310 19.110 1.00 32.28 ? 267 GLY A N 1 ATOM 2117 C CA . GLY A 1 267 ? 23.354 29.240 18.492 1.00 32.31 ? 267 GLY A CA 1 ATOM 2118 C C . GLY A 1 267 ? 23.635 29.510 17.020 1.00 30.88 ? 267 GLY A C 1 ATOM 2119 O O . GLY A 1 267 ? 22.901 30.263 16.389 1.00 32.14 ? 267 GLY A O 1 ATOM 2120 N N . SER A 1 268 ? 24.675 28.884 16.463 1.00 31.20 ? 268 SER A N 1 ATOM 2121 C CA . SER A 1 268 ? 25.099 29.172 15.074 1.00 30.64 ? 268 SER A CA 1 ATOM 2122 C C . SER A 1 268 ? 24.425 28.254 14.081 1.00 28.82 ? 268 SER A C 1 ATOM 2123 O O . SER A 1 268 ? 24.721 27.053 14.022 1.00 30.08 ? 268 SER A O 1 ATOM 2124 C CB . SER A 1 268 ? 26.632 29.060 14.905 1.00 31.59 ? 268 SER A CB 1 ATOM 2125 O OG . SER A 1 268 ? 27.029 28.915 13.526 1.00 32.24 ? 268 SER A OG 1 ATOM 2126 N N . MET A 1 269 ? 23.529 28.817 13.278 1.00 28.31 ? 269 MET A N 1 ATOM 2127 C CA . MET A 1 269 ? 22.971 28.079 12.149 1.00 27.58 ? 269 MET A CA 1 ATOM 2128 C C . MET A 1 269 ? 24.021 27.774 11.062 1.00 27.43 ? 269 MET A C 1 ATOM 2129 O O . MET A 1 269 ? 23.977 26.720 10.457 1.00 24.98 ? 269 MET A O 1 ATOM 2130 C CB . MET A 1 269 ? 21.771 28.807 11.543 1.00 27.65 ? 269 MET A CB 1 ATOM 2131 C CG . MET A 1 269 ? 20.554 28.889 12.481 1.00 26.73 ? 269 MET A CG 1 ATOM 2132 S SD . MET A 1 269 ? 20.025 27.246 13.033 1.00 26.25 ? 269 MET A SD 1 ATOM 2133 C CE . MET A 1 269 ? 18.499 27.673 13.876 1.00 27.96 ? 269 MET A CE 1 ATOM 2134 N N . ASP A 1 270 ? 24.938 28.712 10.803 1.00 26.89 ? 270 ASP A N 1 ATOM 2135 C CA . ASP A 1 270 ? 26.020 28.506 9.833 1.00 28.54 ? 270 ASP A CA 1 ATOM 2136 C C . ASP A 1 270 ? 26.786 27.194 10.071 1.00 27.73 ? 270 ASP A C 1 ATOM 2137 O O . ASP A 1 270 ? 27.005 26.412 9.126 1.00 26.65 ? 270 ASP A O 1 ATOM 2138 C CB . ASP A 1 270 ? 27.023 29.657 9.891 1.00 31.62 ? 270 ASP A CB 1 ATOM 2139 C CG . ASP A 1 270 ? 26.578 30.870 9.103 1.00 35.04 ? 270 ASP A CG 1 ATOM 2140 O OD1 . ASP A 1 270 ? 25.406 30.919 8.674 1.00 35.73 ? 270 ASP A OD1 1 ATOM 2141 O OD2 . ASP A 1 270 ? 27.420 31.778 8.912 1.00 36.32 ? 270 ASP A OD2 1 ATOM 2142 N N . ASP A 1 271 ? 27.236 26.969 11.306 1.00 26.56 ? 271 ASP A N 1 ATOM 2143 C CA . ASP A 1 271 ? 28.014 25.757 11.598 1.00 26.87 ? 271 ASP A CA 1 ATOM 2144 C C . ASP A 1 271 ? 27.252 24.475 11.262 1.00 24.65 ? 271 ASP A C 1 ATOM 2145 O O . ASP A 1 271 ? 27.854 23.525 10.751 1.00 24.80 ? 271 ASP A O 1 ATOM 2146 C CB . ASP A 1 271 ? 28.519 25.705 13.045 1.00 28.75 ? 271 ASP A CB 1 ATOM 2147 C CG . ASP A 1 271 ? 29.561 26.752 13.328 1.00 32.02 ? 271 ASP A CG 1 ATOM 2148 O OD1 . ASP A 1 271 ? 30.073 27.355 12.355 1.00 32.05 ? 271 ASP A OD1 1 ATOM 2149 O OD2 . ASP A 1 271 ? 29.856 26.978 14.520 1.00 33.62 ? 271 ASP A OD2 1 ATOM 2150 N N . LEU A 1 272 ? 25.947 24.449 11.539 1.00 23.70 ? 272 LEU A N 1 ATOM 2151 C CA . LEU A 1 272 ? 25.121 23.258 11.275 1.00 21.83 ? 272 LEU A CA 1 ATOM 2152 C C . LEU A 1 272 ? 24.926 23.073 9.779 1.00 22.09 ? 272 LEU A C 1 ATOM 2153 O O . LEU A 1 272 ? 25.130 21.984 9.258 1.00 22.17 ? 272 LEU A O 1 ATOM 2154 C CB . LEU A 1 272 ? 23.758 23.364 11.953 1.00 21.14 ? 272 LEU A CB 1 ATOM 2155 C CG . LEU A 1 272 ? 22.766 22.192 11.777 1.00 22.10 ? 272 LEU A CG 1 ATOM 2156 C CD1 . LEU A 1 272 ? 23.397 20.840 12.156 1.00 22.79 ? 272 LEU A CD1 1 ATOM 2157 C CD2 . LEU A 1 272 ? 21.507 22.422 12.572 1.00 22.51 ? 272 LEU A CD2 1 ATOM 2158 N N . TYR A 1 273 ? 24.508 24.151 9.097 1.00 20.70 ? 273 TYR A N 1 ATOM 2159 C CA . TYR A 1 273 ? 24.386 24.154 7.648 1.00 21.88 ? 273 TYR A CA 1 ATOM 2160 C C . TYR A 1 273 ? 25.663 23.586 6.992 1.00 21.46 ? 273 TYR A C 1 ATOM 2161 O O . TYR A 1 273 ? 25.608 22.694 6.140 1.00 22.70 ? 273 TYR A O 1 ATOM 2162 C CB . TYR A 1 273 ? 24.138 25.607 7.209 1.00 23.96 ? 273 TYR A CB 1 ATOM 2163 C CG . TYR A 1 273 ? 23.879 25.871 5.740 1.00 25.68 ? 273 TYR A CG 1 ATOM 2164 C CD1 . TYR A 1 273 ? 24.920 25.884 4.833 1.00 26.82 ? 273 TYR A CD1 1 ATOM 2165 C CD2 . TYR A 1 273 ? 22.599 26.211 5.285 1.00 25.78 ? 273 TYR A CD2 1 ATOM 2166 C CE1 . TYR A 1 273 ? 24.709 26.157 3.482 1.00 26.25 ? 273 TYR A CE1 1 ATOM 2167 C CE2 . TYR A 1 273 ? 22.373 26.512 3.905 1.00 25.93 ? 273 TYR A CE2 1 ATOM 2168 C CZ . TYR A 1 273 ? 23.447 26.468 3.030 1.00 26.60 ? 273 TYR A CZ 1 ATOM 2169 O OH . TYR A 1 273 ? 23.285 26.744 1.676 1.00 26.67 ? 273 TYR A OH 1 ATOM 2170 N N . ASN A 1 274 ? 26.822 24.103 7.389 1.00 22.80 ? 274 ASN A N 1 ATOM 2171 C CA . ASN A 1 274 ? 28.070 23.689 6.777 1.00 22.79 ? 274 ASN A CA 1 ATOM 2172 C C . ASN A 1 274 ? 28.428 22.236 7.078 1.00 22.48 ? 274 ASN A C 1 ATOM 2173 O O . ASN A 1 274 ? 28.968 21.539 6.203 1.00 23.26 ? 274 ASN A O 1 ATOM 2174 C CB . ASN A 1 274 ? 29.198 24.611 7.213 1.00 25.10 ? 274 ASN A CB 1 ATOM 2175 C CG . ASN A 1 274 ? 29.083 25.984 6.600 1.00 26.21 ? 274 ASN A CG 1 ATOM 2176 O OD1 . ASN A 1 274 ? 28.480 26.148 5.544 1.00 26.77 ? 274 ASN A OD1 1 ATOM 2177 N ND2 . ASN A 1 274 ? 29.663 26.981 7.260 1.00 28.02 ? 274 ASN A ND2 1 ATOM 2178 N N . MET A 1 275 ? 28.117 21.769 8.287 1.00 21.77 ? 275 MET A N 1 ATOM 2179 C CA . MET A 1 275 ? 28.429 20.383 8.623 1.00 22.51 ? 275 MET A CA 1 ATOM 2180 C C . MET A 1 275 ? 27.549 19.408 7.861 1.00 20.72 ? 275 MET A C 1 ATOM 2181 O O . MET A 1 275 ? 28.014 18.326 7.479 1.00 22.90 ? 275 MET A O 1 ATOM 2182 C CB . MET A 1 275 ? 28.323 20.118 10.122 1.00 22.05 ? 275 MET A CB 1 ATOM 2183 C CG . MET A 1 275 ? 28.829 18.736 10.477 1.00 22.82 ? 275 MET A CG 1 ATOM 2184 S SD . MET A 1 275 ? 30.578 18.428 10.055 1.00 24.86 ? 275 MET A SD 1 ATOM 2185 C CE . MET A 1 275 ? 31.379 19.409 11.323 1.00 25.93 ? 275 MET A CE 1 ATOM 2186 N N . ILE A 1 276 ? 26.288 19.784 7.629 1.00 22.63 ? 276 ILE A N 1 ATOM 2187 C CA . ILE A 1 276 ? 25.412 18.926 6.840 1.00 20.91 ? 276 ILE A CA 1 ATOM 2188 C C . ILE A 1 276 ? 26.087 18.700 5.475 1.00 21.57 ? 276 ILE A C 1 ATOM 2189 O O . ILE A 1 276 ? 26.191 17.562 5.002 1.00 22.59 ? 276 ILE A O 1 ATOM 2190 C CB . ILE A 1 276 ? 24.024 19.536 6.661 1.00 21.89 ? 276 ILE A CB 1 ATOM 2191 C CG1 . ILE A 1 276 ? 23.297 19.495 8.002 1.00 20.42 ? 276 ILE A CG1 1 ATOM 2192 C CG2 . ILE A 1 276 ? 23.214 18.766 5.628 1.00 22.30 ? 276 ILE A CG2 1 ATOM 2193 C CD1 . ILE A 1 276 ? 22.050 20.427 7.982 1.00 21.29 ? 276 ILE A CD1 1 ATOM 2194 N N . ASN A 1 277 ? 26.593 19.781 4.866 1.00 21.04 ? 277 ASN A N 1 ATOM 2195 C CA . ASN A 1 277 ? 27.179 19.682 3.544 1.00 21.47 ? 277 ASN A CA 1 ATOM 2196 C C . ASN A 1 277 ? 28.521 18.946 3.591 1.00 22.97 ? 277 ASN A C 1 ATOM 2197 O O . ASN A 1 277 ? 28.845 18.175 2.687 1.00 25.16 ? 277 ASN A O 1 ATOM 2198 C CB . ASN A 1 277 ? 27.333 21.067 2.906 1.00 23.41 ? 277 ASN A CB 1 ATOM 2199 C CG . ASN A 1 277 ? 26.016 21.614 2.433 1.00 26.15 ? 277 ASN A CG 1 ATOM 2200 O OD1 . ASN A 1 277 ? 25.109 20.843 2.075 1.00 26.38 ? 277 ASN A OD1 1 ATOM 2201 N ND2 . ASN A 1 277 ? 25.876 22.946 2.458 1.00 26.92 ? 277 ASN A ND2 1 ATOM 2202 N N . THR A 1 278 ? 29.254 19.133 4.685 1.00 22.53 ? 278 THR A N 1 ATOM 2203 C CA . THR A 1 278 ? 30.563 18.518 4.810 1.00 23.49 ? 278 THR A CA 1 ATOM 2204 C C . THR A 1 278 ? 30.409 17.011 4.902 1.00 24.34 ? 278 THR A C 1 ATOM 2205 O O . THR A 1 278 ? 31.127 16.240 4.228 1.00 24.75 ? 278 THR A O 1 ATOM 2206 C CB . THR A 1 278 ? 31.310 19.097 6.024 1.00 23.94 ? 278 THR A CB 1 ATOM 2207 O OG1 . THR A 1 278 ? 31.735 20.430 5.692 1.00 24.50 ? 278 THR A OG1 1 ATOM 2208 C CG2 . THR A 1 278 ? 32.535 18.250 6.374 1.00 24.64 ? 278 THR A CG2 1 ATOM 2209 N N . VAL A 1 279 ? 29.441 16.582 5.714 1.00 24.09 ? 279 VAL A N 1 ATOM 2210 C CA . VAL A 1 279 ? 29.192 15.145 5.890 1.00 24.63 ? 279 VAL A CA 1 ATOM 2211 C C . VAL A 1 279 ? 28.626 14.521 4.614 1.00 25.92 ? 279 VAL A C 1 ATOM 2212 O O . VAL A 1 279 ? 28.979 13.394 4.245 1.00 25.81 ? 279 VAL A O 1 ATOM 2213 C CB . VAL A 1 279 ? 28.237 14.898 7.082 1.00 25.87 ? 279 VAL A CB 1 ATOM 2214 C CG1 . VAL A 1 279 ? 27.716 13.440 7.084 1.00 25.77 ? 279 VAL A CG1 1 ATOM 2215 C CG2 . VAL A 1 279 ? 28.939 15.226 8.371 1.00 23.92 ? 279 VAL A CG2 1 ATOM 2216 N N . LYS A 1 280 ? 27.745 15.259 3.936 1.00 26.20 ? 280 LYS A N 1 ATOM 2217 C CA . LYS A 1 280 ? 27.154 14.786 2.699 1.00 28.26 ? 280 LYS A CA 1 ATOM 2218 C C . LYS A 1 280 ? 28.230 14.439 1.680 1.00 27.06 ? 280 LYS A C 1 ATOM 2219 O O . LYS A 1 280 ? 28.146 13.420 1.002 1.00 26.33 ? 280 LYS A O 1 ATOM 2220 C CB . LYS A 1 280 ? 26.239 15.857 2.106 1.00 28.89 ? 280 LYS A CB 1 ATOM 2221 C CG . LYS A 1 280 ? 25.739 15.552 0.665 1.00 32.26 ? 280 LYS A CG 1 ATOM 2222 C CD . LYS A 1 280 ? 24.463 16.340 0.317 1.00 33.07 ? 280 LYS A CD 1 ATOM 2223 C CE . LYS A 1 280 ? 24.709 17.454 -0.706 1.00 36.09 ? 280 LYS A CE 1 ATOM 2224 N NZ . LYS A 1 280 ? 25.940 18.260 -0.399 1.00 38.52 ? 280 LYS A NZ 1 ATOM 2225 N N . SER A 1 281 ? 29.236 15.290 1.572 1.00 27.18 ? 281 SER A N 1 ATOM 2226 C CA . SER A 1 281 ? 30.198 15.120 0.492 1.00 29.57 ? 281 SER A CA 1 ATOM 2227 C C . SER A 1 281 ? 31.399 14.276 0.904 1.00 30.12 ? 281 SER A C 1 ATOM 2228 O O . SER A 1 281 ? 32.038 13.662 0.053 1.00 30.45 ? 281 SER A O 1 ATOM 2229 C CB . SER A 1 281 ? 30.672 16.484 -0.010 1.00 32.02 ? 281 SER A CB 1 ATOM 2230 O OG . SER A 1 281 ? 31.281 17.228 1.043 1.00 34.19 ? 281 SER A OG 1 ATOM 2231 N N . ASP A 1 282 ? 31.720 14.268 2.190 1.00 30.23 ? 282 ASP A N 1 ATOM 2232 C CA . ASP A 1 282 ? 32.952 13.633 2.666 1.00 31.65 ? 282 ASP A CA 1 ATOM 2233 C C . ASP A 1 282 ? 32.784 12.224 3.258 1.00 31.80 ? 282 ASP A C 1 ATOM 2234 O O . ASP A 1 282 ? 33.735 11.429 3.283 1.00 31.86 ? 282 ASP A O 1 ATOM 2235 C CB . ASP A 1 282 ? 33.632 14.543 3.688 1.00 32.31 ? 282 ASP A CB 1 ATOM 2236 C CG . ASP A 1 282 ? 34.163 15.818 3.065 1.00 32.63 ? 282 ASP A CG 1 ATOM 2237 O OD1 . ASP A 1 282 ? 34.074 15.975 1.824 1.00 34.43 ? 282 ASP A OD1 1 ATOM 2238 O OD2 . ASP A 1 282 ? 34.696 16.660 3.810 1.00 33.87 ? 282 ASP A OD2 1 ATOM 2239 N N . CYS A 1 283 ? 31.592 11.902 3.736 1.00 30.75 ? 283 CYS A N 1 ATOM 2240 C CA . CYS A 1 283 ? 31.380 10.584 4.296 1.00 30.85 ? 283 CYS A CA 1 ATOM 2241 C C . CYS A 1 283 ? 30.954 9.597 3.240 1.00 29.21 ? 283 CYS A C 1 ATOM 2242 O O . CYS A 1 283 ? 30.187 9.924 2.333 1.00 27.88 ? 283 CYS A O 1 ATOM 2243 C CB . CYS A 1 283 ? 30.381 10.659 5.443 1.00 34.44 ? 283 CYS A CB 1 ATOM 2244 S SG . CYS A 1 283 ? 30.933 11.963 6.563 1.00 40.34 ? 283 CYS A SG 1 ATOM 2245 N N . PRO A 1 284 ? 31.493 8.374 3.316 1.00 27.18 ? 284 PRO A N 1 ATOM 2246 C CA . PRO A 1 284 ? 31.140 7.374 2.319 1.00 26.44 ? 284 PRO A CA 1 ATOM 2247 C C . PRO A 1 284 ? 29.631 7.332 2.047 1.00 26.12 ? 284 PRO A C 1 ATOM 2248 O O . PRO A 1 284 ? 29.215 7.334 0.884 1.00 25.47 ? 284 PRO A O 1 ATOM 2249 C CB . PRO A 1 284 ? 31.636 6.081 2.964 1.00 26.80 ? 284 PRO A CB 1 ATOM 2250 C CG . PRO A 1 284 ? 32.896 6.545 3.655 1.00 26.34 ? 284 PRO A CG 1 ATOM 2251 C CD . PRO A 1 284 ? 32.463 7.847 4.301 1.00 26.95 ? 284 PRO A CD 1 ATOM 2252 N N . ASP A 1 285 ? 28.820 7.334 3.096 1.00 24.71 ? 285 ASP A N 1 ATOM 2253 C CA . ASP A 1 285 ? 27.376 7.419 2.873 1.00 24.36 ? 285 ASP A CA 1 ATOM 2254 C C . ASP A 1 285 ? 26.635 7.978 4.067 1.00 23.84 ? 285 ASP A C 1 ATOM 2255 O O . ASP A 1 285 ? 26.354 7.255 5.007 1.00 23.42 ? 285 ASP A O 1 ATOM 2256 C CB . ASP A 1 285 ? 26.793 6.055 2.488 1.00 24.18 ? 285 ASP A CB 1 ATOM 2257 C CG . ASP A 1 285 ? 25.362 6.145 2.006 1.00 25.68 ? 285 ASP A CG 1 ATOM 2258 O OD1 . ASP A 1 285 ? 24.741 7.227 2.100 1.00 27.04 ? 285 ASP A OD1 1 ATOM 2259 O OD2 . ASP A 1 285 ? 24.839 5.119 1.534 1.00 26.52 ? 285 ASP A OD2 1 ATOM 2260 N N . SER A 1 286 ? 26.299 9.266 3.992 1.00 23.10 ? 286 SER A N 1 ATOM 2261 C CA . SER A 1 286 ? 25.540 9.954 5.041 1.00 21.94 ? 286 SER A CA 1 ATOM 2262 C C . SER A 1 286 ? 24.255 9.244 5.392 1.00 21.75 ? 286 SER A C 1 ATOM 2263 O O . SER A 1 286 ? 23.778 9.363 6.542 1.00 23.99 ? 286 SER A O 1 ATOM 2264 C CB . SER A 1 286 ? 25.225 11.382 4.589 1.00 22.77 ? 286 SER A CB 1 ATOM 2265 O OG . SER A 1 286 ? 24.557 11.366 3.342 1.00 23.41 ? 286 SER A OG 1 ATOM 2266 N N . THR A 1 287 ? 23.680 8.503 4.444 1.00 21.99 ? 287 THR A N 1 ATOM 2267 C CA . THR A 1 287 ? 22.391 7.860 4.708 1.00 22.67 ? 287 THR A CA 1 ATOM 2268 C C . THR A 1 287 ? 22.467 6.598 5.545 1.00 23.05 ? 287 THR A C 1 ATOM 2269 O O . THR A 1 287 ? 21.423 6.023 5.874 1.00 22.98 ? 287 THR A O 1 ATOM 2270 C CB . THR A 1 287 ? 21.551 7.598 3.458 1.00 23.71 ? 287 THR A CB 1 ATOM 2271 O OG1 . THR A 1 287 ? 22.186 6.614 2.633 1.00 23.40 ? 287 THR A OG1 1 ATOM 2272 C CG2 . THR A 1 287 ? 21.316 8.894 2.704 1.00 25.18 ? 287 THR A CG2 1 ATOM 2273 N N . LEU A 1 288 ? 23.686 6.177 5.884 1.00 22.53 ? 288 LEU A N 1 ATOM 2274 C CA . LEU A 1 288 ? 23.866 5.041 6.784 1.00 21.95 ? 288 LEU A CA 1 ATOM 2275 C C . LEU A 1 288 ? 24.371 5.443 8.180 1.00 21.93 ? 288 LEU A C 1 ATOM 2276 O O . LEU A 1 288 ? 24.773 4.560 8.962 1.00 22.27 ? 288 LEU A O 1 ATOM 2277 C CB . LEU A 1 288 ? 24.828 4.000 6.197 1.00 22.03 ? 288 LEU A CB 1 ATOM 2278 C CG . LEU A 1 288 ? 24.205 3.286 4.989 1.00 21.75 ? 288 LEU A CG 1 ATOM 2279 C CD1 . LEU A 1 288 ? 25.291 2.448 4.304 1.00 21.79 ? 288 LEU A CD1 1 ATOM 2280 C CD2 . LEU A 1 288 ? 23.046 2.425 5.453 1.00 22.68 ? 288 LEU A CD2 1 ATOM 2281 N N . LEU A 1 289 ? 24.417 6.744 8.463 1.00 20.88 ? 289 LEU A N 1 ATOM 2282 C CA . LEU A 1 289 ? 24.859 7.226 9.776 1.00 21.22 ? 289 LEU A CA 1 ATOM 2283 C C . LEU A 1 289 ? 23.648 7.356 10.656 1.00 23.75 ? 289 LEU A C 1 ATOM 2284 O O . LEU A 1 289 ? 22.512 7.320 10.169 1.00 24.05 ? 289 LEU A O 1 ATOM 2285 C CB . LEU A 1 289 ? 25.523 8.593 9.642 1.00 22.03 ? 289 LEU A CB 1 ATOM 2286 C CG . LEU A 1 289 ? 26.591 8.713 8.575 1.00 21.61 ? 289 LEU A CG 1 ATOM 2287 C CD1 . LEU A 1 289 ? 27.129 10.113 8.626 1.00 24.67 ? 289 LEU A CD1 1 ATOM 2288 C CD2 . LEU A 1 289 ? 27.714 7.689 8.845 1.00 22.65 ? 289 LEU A CD2 1 ATOM 2289 N N . GLY A 1 290 ? 23.885 7.545 11.949 1.00 21.69 ? 290 GLY A N 1 ATOM 2290 C CA . GLY A 1 290 ? 22.787 7.648 12.908 1.00 22.83 ? 290 GLY A CA 1 ATOM 2291 C C . GLY A 1 290 ? 22.756 9.037 13.521 1.00 22.39 ? 290 GLY A C 1 ATOM 2292 O O . GLY A 1 290 ? 23.754 9.454 14.085 1.00 22.03 ? 290 GLY A O 1 ATOM 2293 N N . THR A 1 291 ? 21.654 9.786 13.368 1.00 20.38 ? 291 THR A N 1 ATOM 2294 C CA . THR A 1 291 ? 21.611 11.158 13.867 1.00 21.66 ? 291 THR A CA 1 ATOM 2295 C C . THR A 1 291 ? 21.063 11.201 15.285 1.00 21.22 ? 291 THR A C 1 ATOM 2296 O O . THR A 1 291 ? 20.028 10.582 15.579 1.00 21.17 ? 291 THR A O 1 ATOM 2297 C CB . THR A 1 291 ? 20.694 12.044 12.976 1.00 21.58 ? 291 THR A CB 1 ATOM 2298 O OG1 . THR A 1 291 ? 21.030 11.835 11.581 1.00 21.18 ? 291 THR A OG1 1 ATOM 2299 C CG2 . THR A 1 291 ? 20.862 13.529 13.320 1.00 24.10 ? 291 THR A CG2 1 ATOM 2300 N N . PHE A 1 292 ? 21.694 11.993 16.135 1.00 21.24 ? 292 PHE A N 1 ATOM 2301 C CA . PHE A 1 292 ? 21.246 12.100 17.517 1.00 20.82 ? 292 PHE A CA 1 ATOM 2302 C C . PHE A 1 292 ? 21.643 13.462 18.113 1.00 20.18 ? 292 PHE A C 1 ATOM 2303 O O . PHE A 1 292 ? 22.597 14.138 17.600 1.00 21.55 ? 292 PHE A O 1 ATOM 2304 C CB . PHE A 1 292 ? 21.859 10.957 18.325 1.00 20.53 ? 292 PHE A CB 1 ATOM 2305 C CG . PHE A 1 292 ? 23.339 11.103 18.508 1.00 20.71 ? 292 PHE A CG 1 ATOM 2306 C CD1 . PHE A 1 292 ? 24.220 10.618 17.535 1.00 21.18 ? 292 PHE A CD1 1 ATOM 2307 C CD2 . PHE A 1 292 ? 23.838 11.760 19.634 1.00 20.93 ? 292 PHE A CD2 1 ATOM 2308 C CE1 . PHE A 1 292 ? 25.622 10.796 17.694 1.00 21.47 ? 292 PHE A CE1 1 ATOM 2309 C CE2 . PHE A 1 292 ? 25.228 11.956 19.782 1.00 22.27 ? 292 PHE A CE2 1 ATOM 2310 C CZ . PHE A 1 292 ? 26.108 11.465 18.832 1.00 20.50 ? 292 PHE A CZ 1 ATOM 2311 N N . VAL A 1 293 ? 20.956 13.878 19.169 1.00 20.67 ? 293 VAL A N 1 ATOM 2312 C CA . VAL A 1 293 ? 21.419 15.007 19.959 1.00 21.50 ? 293 VAL A CA 1 ATOM 2313 C C . VAL A 1 293 ? 21.454 14.710 21.454 1.00 22.71 ? 293 VAL A C 1 ATOM 2314 O O . VAL A 1 293 ? 21.777 15.565 22.256 1.00 22.40 ? 293 VAL A O 1 ATOM 2315 C CB . VAL A 1 293 ? 20.577 16.266 19.710 1.00 23.28 ? 293 VAL A CB 1 ATOM 2316 C CG1 . VAL A 1 293 ? 19.365 16.260 20.602 1.00 24.03 ? 293 VAL A CG1 1 ATOM 2317 C CG2 . VAL A 1 293 ? 21.409 17.505 19.959 1.00 25.46 ? 293 VAL A CG2 1 ATOM 2318 N N . GLU A 1 294 ? 21.118 13.483 21.811 1.00 21.30 ? 294 GLU A N 1 ATOM 2319 C CA . GLU A 1 294 ? 21.022 13.116 23.210 1.00 21.42 ? 294 GLU A CA 1 ATOM 2320 C C . GLU A 1 294 ? 21.433 11.660 23.351 1.00 23.39 ? 294 GLU A C 1 ATOM 2321 O O . GLU A 1 294 ? 21.007 10.819 22.572 1.00 21.54 ? 294 GLU A O 1 ATOM 2322 C CB . GLU A 1 294 ? 19.584 13.317 23.691 1.00 24.03 ? 294 GLU A CB 1 ATOM 2323 C CG . GLU A 1 294 ? 19.375 13.144 25.178 1.00 25.53 ? 294 GLU A CG 1 ATOM 2324 C CD . GLU A 1 294 ? 18.179 13.933 25.684 1.00 23.59 ? 294 GLU A CD 1 ATOM 2325 O OE1 . GLU A 1 294 ? 17.359 13.353 26.403 1.00 24.92 ? 294 GLU A OE1 1 ATOM 2326 O OE2 . GLU A 1 294 ? 18.082 15.130 25.361 1.00 24.33 ? 294 GLU A OE2 1 ATOM 2327 N N . ASN A 1 295 ? 22.285 11.375 24.326 1.00 21.79 ? 295 ASN A N 1 ATOM 2328 C CA . ASN A 1 295 ? 22.644 9.969 24.631 1.00 21.12 ? 295 ASN A CA 1 ATOM 2329 C C . ASN A 1 295 ? 23.124 9.878 26.069 1.00 21.57 ? 295 ASN A C 1 ATOM 2330 O O . ASN A 1 295 ? 22.974 10.840 26.825 1.00 23.04 ? 295 ASN A O 1 ATOM 2331 C CB . ASN A 1 295 ? 23.654 9.340 23.622 1.00 21.85 ? 295 ASN A CB 1 ATOM 2332 C CG . ASN A 1 295 ? 25.001 10.048 23.607 1.00 22.27 ? 295 ASN A CG 1 ATOM 2333 O OD1 . ASN A 1 295 ? 25.430 10.623 24.607 1.00 23.27 ? 295 ASN A OD1 1 ATOM 2334 N ND2 . ASN A 1 295 ? 25.676 10.008 22.459 1.00 21.98 ? 295 ASN A ND2 1 ATOM 2335 N N . HIS A 1 296 ? 23.684 8.714 26.428 1.00 21.15 ? 296 HIS A N 1 ATOM 2336 C CA . HIS A 1 296 ? 24.015 8.438 27.800 1.00 21.51 ? 296 HIS A CA 1 ATOM 2337 C C . HIS A 1 296 ? 25.450 8.852 28.132 1.00 22.42 ? 296 HIS A C 1 ATOM 2338 O O . HIS A 1 296 ? 25.942 8.596 29.237 1.00 22.11 ? 296 HIS A O 1 ATOM 2339 C CB . HIS A 1 296 ? 23.824 6.943 28.073 1.00 22.88 ? 296 HIS A CB 1 ATOM 2340 C CG . HIS A 1 296 ? 24.556 6.035 27.123 1.00 23.64 ? 296 HIS A CG 1 ATOM 2341 N ND1 . HIS A 1 296 ? 24.809 6.359 25.800 1.00 24.01 ? 296 HIS A ND1 1 ATOM 2342 C CD2 . HIS A 1 296 ? 25.078 4.800 27.308 1.00 23.90 ? 296 HIS A CD2 1 ATOM 2343 C CE1 . HIS A 1 296 ? 25.429 5.351 25.208 1.00 25.98 ? 296 HIS A CE1 1 ATOM 2344 N NE2 . HIS A 1 296 ? 25.611 4.390 26.102 1.00 24.56 ? 296 HIS A NE2 1 ATOM 2345 N N . ASP A 1 297 ? 26.120 9.497 27.178 1.00 21.57 ? 297 ASP A N 1 ATOM 2346 C CA . ASP A 1 297 ? 27.535 9.890 27.343 1.00 21.64 ? 297 ASP A CA 1 ATOM 2347 C C . ASP A 1 297 ? 27.741 11.400 27.225 1.00 22.18 ? 297 ASP A C 1 ATOM 2348 O O . ASP A 1 297 ? 28.882 11.870 27.147 1.00 21.97 ? 297 ASP A O 1 ATOM 2349 C CB . ASP A 1 297 ? 28.389 9.196 26.283 1.00 22.86 ? 297 ASP A CB 1 ATOM 2350 C CG . ASP A 1 297 ? 28.404 7.676 26.444 1.00 24.69 ? 297 ASP A CG 1 ATOM 2351 O OD1 . ASP A 1 297 ? 28.339 7.156 27.605 1.00 24.77 ? 297 ASP A OD1 1 ATOM 2352 O OD2 . ASP A 1 297 ? 28.514 7.029 25.382 1.00 25.97 ? 297 ASP A OD2 1 ATOM 2353 N N . ASN A 1 298 ? 26.642 12.156 27.194 1.00 21.83 ? 298 ASN A N 1 ATOM 2354 C CA . ASN A 1 298 ? 26.700 13.612 27.140 1.00 21.58 ? 298 ASN A CA 1 ATOM 2355 C C . ASN A 1 298 ? 25.510 14.178 27.953 1.00 21.48 ? 298 ASN A C 1 ATOM 2356 O O . ASN A 1 298 ? 24.531 13.486 28.192 1.00 21.36 ? 298 ASN A O 1 ATOM 2357 C CB . ASN A 1 298 ? 26.555 14.074 25.688 1.00 21.95 ? 298 ASN A CB 1 ATOM 2358 C CG . ASN A 1 298 ? 27.723 13.655 24.826 1.00 22.21 ? 298 ASN A CG 1 ATOM 2359 O OD1 . ASN A 1 298 ? 28.759 14.345 24.783 1.00 24.03 ? 298 ASN A OD1 1 ATOM 2360 N ND2 . ASN A 1 298 ? 27.566 12.548 24.142 1.00 23.33 ? 298 ASN A ND2 1 ATOM 2361 N N . PRO A 1 299 ? 25.609 15.428 28.377 1.00 20.10 ? 299 PRO A N 1 ATOM 2362 C CA . PRO A 1 299 ? 24.445 16.027 29.084 1.00 20.94 ? 299 PRO A CA 1 ATOM 2363 C C . PRO A 1 299 ? 23.234 15.969 28.150 1.00 22.26 ? 299 PRO A C 1 ATOM 2364 O O . PRO A 1 299 ? 23.398 16.172 26.928 1.00 21.56 ? 299 PRO A O 1 ATOM 2365 C CB . PRO A 1 299 ? 24.898 17.469 29.302 1.00 21.90 ? 299 PRO A CB 1 ATOM 2366 C CG . PRO A 1 299 ? 26.413 17.394 29.331 1.00 21.07 ? 299 PRO A CG 1 ATOM 2367 C CD . PRO A 1 299 ? 26.718 16.385 28.215 1.00 22.05 ? 299 PRO A CD 1 ATOM 2368 N N . ARG A 1 300 ? 22.028 15.723 28.676 1.00 22.64 ? 300 ARG A N 1 ATOM 2369 C CA . ARG A 1 300 ? 20.827 15.750 27.814 1.00 20.93 ? 300 ARG A CA 1 ATOM 2370 C C . ARG A 1 300 ? 20.552 17.132 27.226 1.00 22.10 ? 300 ARG A C 1 ATOM 2371 O O . ARG A 1 300 ? 21.013 18.143 27.756 1.00 21.08 ? 300 ARG A O 1 ATOM 2372 C CB . ARG A 1 300 ? 19.598 15.324 28.627 1.00 20.67 ? 300 ARG A CB 1 ATOM 2373 C CG . ARG A 1 300 ? 19.694 13.824 29.004 1.00 20.40 ? 300 ARG A CG 1 ATOM 2374 C CD . ARG A 1 300 ? 18.357 13.332 29.429 1.00 21.96 ? 300 ARG A CD 1 ATOM 2375 N NE . ARG A 1 300 ? 18.324 11.952 29.909 1.00 21.16 ? 300 ARG A NE 1 ATOM 2376 C CZ . ARG A 1 300 ? 17.754 10.946 29.240 1.00 21.56 ? 300 ARG A CZ 1 ATOM 2377 N NH1 . ARG A 1 300 ? 17.262 11.152 28.005 1.00 21.97 ? 300 ARG A NH1 1 ATOM 2378 N NH2 . ARG A 1 300 ? 17.679 9.744 29.805 1.00 21.81 ? 300 ARG A NH2 1 ATOM 2379 N N . PHE A 1 301 ? 19.772 17.177 26.143 1.00 20.24 ? 301 PHE A N 1 ATOM 2380 C CA . PHE A 1 301 ? 19.547 18.465 25.495 1.00 21.27 ? 301 PHE A CA 1 ATOM 2381 C C . PHE A 1 301 ? 18.955 19.481 26.501 1.00 20.18 ? 301 PHE A C 1 ATOM 2382 O O . PHE A 1 301 ? 19.427 20.637 26.593 1.00 20.76 ? 301 PHE A O 1 ATOM 2383 C CB . PHE A 1 301 ? 18.617 18.328 24.290 1.00 21.35 ? 301 PHE A CB 1 ATOM 2384 C CG . PHE A 1 301 ? 18.341 19.645 23.632 1.00 20.52 ? 301 PHE A CG 1 ATOM 2385 C CD1 . PHE A 1 301 ? 19.284 20.194 22.759 1.00 21.07 ? 301 PHE A CD1 1 ATOM 2386 C CD2 . PHE A 1 301 ? 17.195 20.382 23.971 1.00 20.74 ? 301 PHE A CD2 1 ATOM 2387 C CE1 . PHE A 1 301 ? 19.072 21.456 22.177 1.00 20.86 ? 301 PHE A CE1 1 ATOM 2388 C CE2 . PHE A 1 301 ? 16.959 21.644 23.407 1.00 21.82 ? 301 PHE A CE2 1 ATOM 2389 C CZ . PHE A 1 301 ? 17.903 22.188 22.497 1.00 21.76 ? 301 PHE A CZ 1 ATOM 2390 N N . ALA A 1 302 ? 17.933 19.042 27.230 1.00 20.92 ? 302 ALA A N 1 ATOM 2391 C CA . ALA A 1 302 ? 17.221 19.926 28.182 1.00 20.23 ? 302 ALA A CA 1 ATOM 2392 C C . ALA A 1 302 ? 18.079 20.318 29.397 1.00 21.89 ? 302 ALA A C 1 ATOM 2393 O O . ALA A 1 302 ? 17.718 21.214 30.147 1.00 21.91 ? 302 ALA A O 1 ATOM 2394 C CB . ALA A 1 302 ? 15.909 19.316 28.633 1.00 22.73 ? 302 ALA A CB 1 ATOM 2395 N N . SER A 1 303 ? 19.230 19.659 29.570 1.00 20.22 ? 303 SER A N 1 ATOM 2396 C CA . SER A 1 303 ? 20.172 20.128 30.595 1.00 20.88 ? 303 SER A CA 1 ATOM 2397 C C . SER A 1 303 ? 20.802 21.478 30.249 1.00 20.01 ? 303 SER A C 1 ATOM 2398 O O . SER A 1 303 ? 21.322 22.146 31.127 1.00 20.75 ? 303 SER A O 1 ATOM 2399 C CB . SER A 1 303 ? 21.296 19.096 30.836 1.00 21.37 ? 303 SER A CB 1 ATOM 2400 O OG . SER A 1 303 ? 22.296 19.169 29.842 1.00 21.50 ? 303 SER A OG 1 ATOM 2401 N N . TYR A 1 304 ? 20.792 21.850 28.961 1.00 19.42 ? 304 TYR A N 1 ATOM 2402 C CA . TYR A 1 304 ? 21.340 23.124 28.494 1.00 19.87 ? 304 TYR A CA 1 ATOM 2403 C C . TYR A 1 304 ? 20.293 24.245 28.522 1.00 19.51 ? 304 TYR A C 1 ATOM 2404 O O . TYR A 1 304 ? 20.603 25.384 28.825 1.00 20.30 ? 304 TYR A O 1 ATOM 2405 C CB . TYR A 1 304 ? 21.845 23.007 27.051 1.00 21.06 ? 304 TYR A CB 1 ATOM 2406 C CG . TYR A 1 304 ? 23.077 22.123 26.951 1.00 21.06 ? 304 TYR A CG 1 ATOM 2407 C CD1 . TYR A 1 304 ? 24.354 22.653 27.153 1.00 20.71 ? 304 TYR A CD1 1 ATOM 2408 C CD2 . TYR A 1 304 ? 22.952 20.763 26.687 1.00 21.58 ? 304 TYR A CD2 1 ATOM 2409 C CE1 . TYR A 1 304 ? 25.500 21.824 27.095 1.00 21.20 ? 304 TYR A CE1 1 ATOM 2410 C CE2 . TYR A 1 304 ? 24.068 19.944 26.603 1.00 22.22 ? 304 TYR A CE2 1 ATOM 2411 C CZ . TYR A 1 304 ? 25.335 20.489 26.798 1.00 22.00 ? 304 TYR A CZ 1 ATOM 2412 O OH . TYR A 1 304 ? 26.439 19.655 26.711 1.00 23.61 ? 304 TYR A OH 1 ATOM 2413 N N . THR A 1 305 ? 19.071 23.890 28.144 1.00 20.60 ? 305 THR A N 1 ATOM 2414 C CA . THR A 1 305 ? 17.964 24.835 28.138 1.00 19.65 ? 305 THR A CA 1 ATOM 2415 C C . THR A 1 305 ? 16.660 24.096 28.324 1.00 20.78 ? 305 THR A C 1 ATOM 2416 O O . THR A 1 305 ? 16.498 23.006 27.796 1.00 19.92 ? 305 THR A O 1 ATOM 2417 C CB . THR A 1 305 ? 17.883 25.619 26.817 1.00 20.51 ? 305 THR A CB 1 ATOM 2418 O OG1 . THR A 1 305 ? 16.742 26.477 26.900 1.00 22.30 ? 305 THR A OG1 1 ATOM 2419 C CG2 . THR A 1 305 ? 17.730 24.656 25.598 1.00 21.39 ? 305 THR A CG2 1 ATOM 2420 N N . ASN A 1 306 ? 15.740 24.687 29.080 1.00 21.62 ? 306 ASN A N 1 ATOM 2421 C CA . ASN A 1 306 ? 14.442 24.074 29.324 1.00 22.43 ? 306 ASN A CA 1 ATOM 2422 C C . ASN A 1 306 ? 13.402 24.502 28.301 1.00 21.93 ? 306 ASN A C 1 ATOM 2423 O O . ASN A 1 306 ? 12.235 24.167 28.419 1.00 21.53 ? 306 ASN A O 1 ATOM 2424 C CB . ASN A 1 306 ? 13.934 24.410 30.726 1.00 25.18 ? 306 ASN A CB 1 ATOM 2425 C CG . ASN A 1 306 ? 13.862 23.207 31.633 1.00 27.33 ? 306 ASN A CG 1 ATOM 2426 O OD1 . ASN A 1 306 ? 13.740 23.345 32.847 1.00 29.01 ? 306 ASN A OD1 1 ATOM 2427 N ND2 . ASN A 1 306 ? 13.948 22.028 31.060 1.00 30.57 ? 306 ASN A ND2 1 ATOM 2428 N N . ASP A 1 307 ? 13.834 25.248 27.294 1.00 21.17 ? 307 ASP A N 1 ATOM 2429 C CA . ASP A 1 307 ? 12.878 25.819 26.330 1.00 21.87 ? 307 ASP A CA 1 ATOM 2430 C C . ASP A 1 307 ? 12.286 24.688 25.478 1.00 20.84 ? 307 ASP A C 1 ATOM 2431 O O . ASP A 1 307 ? 13.010 23.983 24.780 1.00 20.72 ? 307 ASP A O 1 ATOM 2432 C CB . ASP A 1 307 ? 13.573 26.879 25.495 1.00 22.23 ? 307 ASP A CB 1 ATOM 2433 C CG . ASP A 1 307 ? 12.632 27.572 24.523 1.00 23.78 ? 307 ASP A CG 1 ATOM 2434 O OD1 . ASP A 1 307 ? 12.092 26.883 23.657 1.00 24.19 ? 307 ASP A OD1 1 ATOM 2435 O OD2 . ASP A 1 307 ? 12.464 28.799 24.609 1.00 24.73 ? 307 ASP A OD2 1 ATOM 2436 N N . ILE A 1 308 ? 10.966 24.494 25.594 1.00 20.85 ? 308 ILE A N 1 ATOM 2437 C CA . ILE A 1 308 ? 10.320 23.377 24.901 1.00 21.84 ? 308 ILE A CA 1 ATOM 2438 C C . ILE A 1 308 ? 10.364 23.535 23.373 1.00 20.10 ? 308 ILE A C 1 ATOM 2439 O O . ILE A 1 308 ? 10.527 22.526 22.681 1.00 20.89 ? 308 ILE A O 1 ATOM 2440 C CB . ILE A 1 308 ? 8.862 23.179 25.412 1.00 23.50 ? 308 ILE A CB 1 ATOM 2441 C CG1 . ILE A 1 308 ? 8.278 21.866 24.920 1.00 27.14 ? 308 ILE A CG1 1 ATOM 2442 C CG2 . ILE A 1 308 ? 7.967 24.333 25.029 1.00 24.26 ? 308 ILE A CG2 1 ATOM 2443 C CD1 . ILE A 1 308 ? 8.967 20.669 25.618 1.00 29.30 ? 308 ILE A CD1 1 ATOM 2444 N N . ALA A 1 309 ? 10.271 24.765 22.861 1.00 20.35 ? 309 ALA A N 1 ATOM 2445 C CA . ALA A 1 309 ? 10.356 24.954 21.385 1.00 21.40 ? 309 ALA A CA 1 ATOM 2446 C C . ALA A 1 309 ? 11.729 24.537 20.854 1.00 20.35 ? 309 ALA A C 1 ATOM 2447 O O . ALA A 1 309 ? 11.832 23.887 19.804 1.00 21.20 ? 309 ALA A O 1 ATOM 2448 C CB . ALA A 1 309 ? 10.057 26.406 20.988 1.00 21.81 ? 309 ALA A CB 1 ATOM 2449 N N . LEU A 1 310 ? 12.793 24.951 21.543 1.00 20.78 ? 310 LEU A N 1 ATOM 2450 C CA . LEU A 1 310 ? 14.145 24.505 21.124 1.00 20.60 ? 310 LEU A CA 1 ATOM 2451 C C . LEU A 1 310 ? 14.236 22.994 21.114 1.00 21.30 ? 310 LEU A C 1 ATOM 2452 O O . LEU A 1 310 ? 14.843 22.416 20.200 1.00 21.77 ? 310 LEU A O 1 ATOM 2453 C CB . LEU A 1 310 ? 15.241 25.088 22.009 1.00 22.57 ? 310 LEU A CB 1 ATOM 2454 C CG . LEU A 1 310 ? 15.342 26.617 21.900 1.00 20.98 ? 310 LEU A CG 1 ATOM 2455 C CD1 . LEU A 1 310 ? 16.363 27.189 22.873 1.00 21.50 ? 310 LEU A CD1 1 ATOM 2456 C CD2 . LEU A 1 310 ? 15.666 27.059 20.433 1.00 19.92 ? 310 LEU A CD2 1 ATOM 2457 N N . ALA A 1 311 ? 13.647 22.327 22.109 1.00 20.20 ? 311 ALA A N 1 ATOM 2458 C CA . ALA A 1 311 ? 13.734 20.842 22.165 1.00 20.23 ? 311 ALA A CA 1 ATOM 2459 C C . ALA A 1 311 ? 12.932 20.226 21.018 1.00 19.82 ? 311 ALA A C 1 ATOM 2460 O O . ALA A 1 311 ? 13.286 19.149 20.507 1.00 21.52 ? 311 ALA A O 1 ATOM 2461 C CB . ALA A 1 311 ? 13.195 20.318 23.510 1.00 19.90 ? 311 ALA A CB 1 ATOM 2462 N N . LYS A 1 312 ? 11.815 20.879 20.649 1.00 19.77 ? 312 LYS A N 1 ATOM 2463 C CA . LYS A 1 312 ? 11.019 20.400 19.516 1.00 21.53 ? 312 LYS A CA 1 ATOM 2464 C C . LYS A 1 312 ? 11.788 20.516 18.203 1.00 19.83 ? 312 LYS A C 1 ATOM 2465 O O . LYS A 1 312 ? 11.705 19.626 17.336 1.00 21.72 ? 312 LYS A O 1 ATOM 2466 C CB . LYS A 1 312 ? 9.684 21.139 19.373 1.00 19.60 ? 312 LYS A CB 1 ATOM 2467 C CG . LYS A 1 312 ? 8.693 20.865 20.490 1.00 21.62 ? 312 LYS A CG 1 ATOM 2468 C CD . LYS A 1 312 ? 7.420 21.718 20.297 1.00 22.45 ? 312 LYS A CD 1 ATOM 2469 C CE . LYS A 1 312 ? 6.226 21.161 21.062 1.00 26.06 ? 312 LYS A CE 1 ATOM 2470 N NZ . LYS A 1 312 ? 5.042 22.110 20.865 1.00 27.62 ? 312 LYS A NZ 1 ATOM 2471 N N . ASN A 1 313 ? 12.471 21.650 17.999 1.00 19.75 ? 313 ASN A N 1 ATOM 2472 C CA . ASN A 1 313 ? 13.257 21.790 16.777 1.00 18.74 ? 313 ASN A CA 1 ATOM 2473 C C . ASN A 1 313 ? 14.387 20.765 16.638 1.00 19.76 ? 313 ASN A C 1 ATOM 2474 O O . ASN A 1 313 ? 14.573 20.197 15.554 1.00 20.75 ? 313 ASN A O 1 ATOM 2475 C CB . ASN A 1 313 ? 13.824 23.199 16.687 1.00 20.47 ? 313 ASN A CB 1 ATOM 2476 C CG . ASN A 1 313 ? 12.798 24.188 16.173 1.00 20.97 ? 313 ASN A CG 1 ATOM 2477 O OD1 . ASN A 1 313 ? 12.651 24.358 14.951 1.00 21.62 ? 313 ASN A OD1 1 ATOM 2478 N ND2 . ASN A 1 313 ? 12.036 24.806 17.086 1.00 20.57 ? 313 ASN A ND2 1 ATOM 2479 N N . VAL A 1 314 ? 15.127 20.507 17.714 1.00 20.31 ? 314 VAL A N 1 ATOM 2480 C CA . VAL A 1 314 ? 16.235 19.596 17.572 1.00 21.34 ? 314 VAL A CA 1 ATOM 2481 C C . VAL A 1 314 ? 15.709 18.172 17.350 1.00 21.07 ? 314 VAL A C 1 ATOM 2482 O O . VAL A 1 314 ? 16.327 17.394 16.599 1.00 21.70 ? 314 VAL A O 1 ATOM 2483 C CB . VAL A 1 314 ? 17.217 19.726 18.779 1.00 23.45 ? 314 VAL A CB 1 ATOM 2484 C CG1 . VAL A 1 314 ? 16.647 19.076 20.053 1.00 21.75 ? 314 VAL A CG1 1 ATOM 2485 C CG2 . VAL A 1 314 ? 18.562 19.203 18.435 1.00 26.32 ? 314 VAL A CG2 1 ATOM 2486 N N . ALA A 1 315 ? 14.573 17.824 17.987 1.00 21.58 ? 315 ALA A N 1 ATOM 2487 C CA . ALA A 1 315 ? 13.987 16.499 17.745 1.00 21.71 ? 315 ALA A CA 1 ATOM 2488 C C . ALA A 1 315 ? 13.523 16.362 16.294 1.00 20.93 ? 315 ALA A C 1 ATOM 2489 O O . ALA A 1 315 ? 13.772 15.333 15.660 1.00 21.50 ? 315 ALA A O 1 ATOM 2490 C CB . ALA A 1 315 ? 12.840 16.200 18.697 1.00 22.93 ? 315 ALA A CB 1 ATOM 2491 N N . ALA A 1 316 ? 12.858 17.389 15.774 1.00 20.55 ? 316 ALA A N 1 ATOM 2492 C CA . ALA A 1 316 ? 12.505 17.365 14.354 1.00 21.36 ? 316 ALA A CA 1 ATOM 2493 C C . ALA A 1 316 ? 13.737 17.169 13.454 1.00 21.10 ? 316 ALA A C 1 ATOM 2494 O O . ALA A 1 316 ? 13.685 16.437 12.455 1.00 21.80 ? 316 ALA A O 1 ATOM 2495 C CB . ALA A 1 316 ? 11.740 18.666 13.972 1.00 20.30 ? 316 ALA A CB 1 ATOM 2496 N N . PHE A 1 317 ? 14.830 17.862 13.746 1.00 21.84 ? 317 PHE A N 1 ATOM 2497 C CA . PHE A 1 317 ? 16.001 17.727 12.902 1.00 20.85 ? 317 PHE A CA 1 ATOM 2498 C C . PHE A 1 317 ? 16.509 16.269 12.863 1.00 19.99 ? 317 PHE A C 1 ATOM 2499 O O . PHE A 1 317 ? 16.833 15.699 11.796 1.00 21.87 ? 317 PHE A O 1 ATOM 2500 C CB . PHE A 1 317 ? 17.154 18.604 13.410 1.00 22.09 ? 317 PHE A CB 1 ATOM 2501 C CG . PHE A 1 317 ? 18.378 18.503 12.542 1.00 21.99 ? 317 PHE A CG 1 ATOM 2502 C CD1 . PHE A 1 317 ? 19.309 17.480 12.732 1.00 22.88 ? 317 PHE A CD1 1 ATOM 2503 C CD2 . PHE A 1 317 ? 18.564 19.395 11.483 1.00 23.92 ? 317 PHE A CD2 1 ATOM 2504 C CE1 . PHE A 1 317 ? 20.402 17.376 11.893 1.00 23.47 ? 317 PHE A CE1 1 ATOM 2505 C CE2 . PHE A 1 317 ? 19.638 19.286 10.647 1.00 23.66 ? 317 PHE A CE2 1 ATOM 2506 C CZ . PHE A 1 317 ? 20.561 18.302 10.844 1.00 22.38 ? 317 PHE A CZ 1 ATOM 2507 N N . ILE A 1 318 ? 16.586 15.671 14.050 1.00 21.48 ? 318 ILE A N 1 ATOM 2508 C CA . ILE A 1 318 ? 17.090 14.311 14.183 1.00 22.97 ? 318 ILE A CA 1 ATOM 2509 C C . ILE A 1 318 ? 16.265 13.374 13.310 1.00 23.01 ? 318 ILE A C 1 ATOM 2510 O O . ILE A 1 318 ? 16.796 12.484 12.627 1.00 22.74 ? 318 ILE A O 1 ATOM 2511 C CB . ILE A 1 318 ? 17.029 13.878 15.663 1.00 24.34 ? 318 ILE A CB 1 ATOM 2512 C CG1 . ILE A 1 318 ? 18.089 14.675 16.422 1.00 26.09 ? 318 ILE A CG1 1 ATOM 2513 C CG2 . ILE A 1 318 ? 17.251 12.350 15.823 1.00 27.11 ? 318 ILE A CG2 1 ATOM 2514 C CD1 . ILE A 1 318 ? 17.796 14.693 17.943 1.00 28.51 ? 318 ILE A CD1 1 ATOM 2515 N N . ILE A 1 319 ? 14.952 13.596 13.296 1.00 22.29 ? 319 ILE A N 1 ATOM 2516 C CA . ILE A 1 319 ? 14.102 12.660 12.563 1.00 23.05 ? 319 ILE A CA 1 ATOM 2517 C C . ILE A 1 319 ? 14.199 12.873 11.046 1.00 21.45 ? 319 ILE A C 1 ATOM 2518 O O . ILE A 1 319 ? 14.119 11.920 10.248 1.00 23.15 ? 319 ILE A O 1 ATOM 2519 C CB . ILE A 1 319 ? 12.662 12.720 13.109 1.00 23.11 ? 319 ILE A CB 1 ATOM 2520 C CG1 . ILE A 1 319 ? 12.684 12.093 14.524 1.00 25.54 ? 319 ILE A CG1 1 ATOM 2521 C CG2 . ILE A 1 319 ? 11.685 11.950 12.214 1.00 23.63 ? 319 ILE A CG2 1 ATOM 2522 C CD1 . ILE A 1 319 ? 11.606 12.451 15.366 1.00 27.92 ? 319 ILE A CD1 1 ATOM 2523 N N . LEU A 1 320 ? 14.441 14.113 10.631 1.00 22.30 ? 320 LEU A N 1 ATOM 2524 C CA . LEU A 1 320 ? 14.340 14.432 9.204 1.00 23.63 ? 320 LEU A CA 1 ATOM 2525 C C . LEU A 1 320 ? 15.697 14.543 8.483 1.00 24.92 ? 320 LEU A C 1 ATOM 2526 O O . LEU A 1 320 ? 15.739 14.726 7.261 1.00 24.95 ? 320 LEU A O 1 ATOM 2527 C CB . LEU A 1 320 ? 13.474 15.677 9.012 1.00 25.79 ? 320 LEU A CB 1 ATOM 2528 C CG . LEU A 1 320 ? 12.034 15.381 9.449 1.00 28.23 ? 320 LEU A CG 1 ATOM 2529 C CD1 . LEU A 1 320 ? 11.199 16.653 9.597 1.00 29.49 ? 320 LEU A CD1 1 ATOM 2530 C CD2 . LEU A 1 320 ? 11.383 14.369 8.505 1.00 29.46 ? 320 LEU A CD2 1 ATOM 2531 N N . ASN A 1 321 ? 16.799 14.465 9.231 1.00 23.63 ? 321 ASN A N 1 ATOM 2532 C CA . ASN A 1 321 ? 18.151 14.483 8.644 1.00 24.21 ? 321 ASN A CA 1 ATOM 2533 C C . ASN A 1 321 ? 18.437 13.187 7.848 1.00 25.03 ? 321 ASN A C 1 ATOM 2534 O O . ASN A 1 321 ? 17.750 12.168 8.021 1.00 24.48 ? 321 ASN A O 1 ATOM 2535 C CB . ASN A 1 321 ? 19.206 14.615 9.768 1.00 24.69 ? 321 ASN A CB 1 ATOM 2536 C CG . ASN A 1 321 ? 20.595 14.934 9.233 1.00 23.74 ? 321 ASN A CG 1 ATOM 2537 O OD1 . ASN A 1 321 ? 20.735 15.748 8.328 1.00 24.96 ? 321 ASN A OD1 1 ATOM 2538 N ND2 . ASN A 1 321 ? 21.629 14.263 9.755 1.00 24.50 ? 321 ASN A ND2 1 ATOM 2539 N N . ASP A 1 322 ? 19.458 13.208 7.000 1.00 23.53 ? 322 ASP A N 1 ATOM 2540 C CA . ASP A 1 322 ? 19.931 11.950 6.393 1.00 23.85 ? 322 ASP A CA 1 ATOM 2541 C C . ASP A 1 322 ? 20.173 10.908 7.461 1.00 23.96 ? 322 ASP A C 1 ATOM 2542 O O . ASP A 1 322 ? 20.598 11.255 8.565 1.00 24.73 ? 322 ASP A O 1 ATOM 2543 C CB . ASP A 1 322 ? 21.275 12.172 5.704 1.00 25.43 ? 322 ASP A CB 1 ATOM 2544 C CG . ASP A 1 322 ? 21.131 12.540 4.241 1.00 27.51 ? 322 ASP A CG 1 ATOM 2545 O OD1 . ASP A 1 322 ? 19.978 12.758 3.783 1.00 28.59 ? 322 ASP A OD1 1 ATOM 2546 O OD2 . ASP A 1 322 ? 22.186 12.623 3.555 1.00 25.97 ? 322 ASP A OD2 1 ATOM 2547 N N . GLY A 1 323 ? 19.961 9.643 7.124 1.00 24.62 ? 323 GLY A N 1 ATOM 2548 C CA . GLY A 1 323 ? 20.409 8.568 8.008 1.00 22.66 ? 323 GLY A CA 1 ATOM 2549 C C . GLY A 1 323 ? 19.303 8.168 8.967 1.00 24.09 ? 323 GLY A C 1 ATOM 2550 O O . GLY A 1 323 ? 18.130 8.560 8.804 1.00 24.23 ? 323 GLY A O 1 ATOM 2551 N N . ILE A 1 324 ? 19.686 7.425 9.989 1.00 22.14 ? 324 ILE A N 1 ATOM 2552 C CA . ILE A 1 324 ? 18.731 6.773 10.847 1.00 20.43 ? 324 ILE A CA 1 ATOM 2553 C C . ILE A 1 324 ? 18.556 7.640 12.112 1.00 21.08 ? 324 ILE A C 1 ATOM 2554 O O . ILE A 1 324 ? 19.504 7.841 12.846 1.00 22.48 ? 324 ILE A O 1 ATOM 2555 C CB . ILE A 1 324 ? 19.277 5.392 11.257 1.00 21.42 ? 324 ILE A CB 1 ATOM 2556 C CG1 . ILE A 1 324 ? 19.486 4.525 10.019 1.00 22.50 ? 324 ILE A CG1 1 ATOM 2557 C CG2 . ILE A 1 324 ? 18.351 4.696 12.213 1.00 23.17 ? 324 ILE A CG2 1 ATOM 2558 C CD1 . ILE A 1 324 ? 20.327 3.289 10.300 1.00 24.67 ? 324 ILE A CD1 1 ATOM 2559 N N . PRO A 1 325 ? 17.356 8.168 12.341 1.00 21.14 ? 325 PRO A N 1 ATOM 2560 C CA . PRO A 1 325 ? 17.162 8.946 13.585 1.00 20.43 ? 325 PRO A CA 1 ATOM 2561 C C . PRO A 1 325 ? 17.369 8.072 14.826 1.00 21.23 ? 325 PRO A C 1 ATOM 2562 O O . PRO A 1 325 ? 16.974 6.911 14.831 1.00 21.90 ? 325 PRO A O 1 ATOM 2563 C CB . PRO A 1 325 ? 15.665 9.340 13.545 1.00 21.47 ? 325 PRO A CB 1 ATOM 2564 C CG . PRO A 1 325 ? 15.284 9.247 12.067 1.00 21.07 ? 325 PRO A CG 1 ATOM 2565 C CD . PRO A 1 325 ? 16.146 8.100 11.499 1.00 22.27 ? 325 PRO A CD 1 ATOM 2566 N N . ILE A 1 326 ? 17.923 8.652 15.887 1.00 20.56 ? 326 ILE A N 1 ATOM 2567 C CA . ILE A 1 326 ? 18.107 7.926 17.145 1.00 18.93 ? 326 ILE A CA 1 ATOM 2568 C C . ILE A 1 326 ? 17.755 8.853 18.316 1.00 20.15 ? 326 ILE A C 1 ATOM 2569 O O . ILE A 1 326 ? 18.421 9.870 18.544 1.00 20.99 ? 326 ILE A O 1 ATOM 2570 C CB . ILE A 1 326 ? 19.548 7.395 17.324 1.00 19.76 ? 326 ILE A CB 1 ATOM 2571 C CG1 . ILE A 1 326 ? 20.028 6.662 16.064 1.00 20.79 ? 326 ILE A CG1 1 ATOM 2572 C CG2 . ILE A 1 326 ? 19.607 6.487 18.566 1.00 20.83 ? 326 ILE A CG2 1 ATOM 2573 C CD1 . ILE A 1 326 ? 21.470 6.274 16.170 1.00 23.29 ? 326 ILE A CD1 1 ATOM 2574 N N . ILE A 1 327 ? 16.647 8.534 18.985 1.00 19.76 ? 327 ILE A N 1 ATOM 2575 C CA . ILE A 1 327 ? 16.183 9.269 20.145 1.00 19.90 ? 327 ILE A CA 1 ATOM 2576 C C . ILE A 1 327 ? 16.490 8.449 21.390 1.00 21.94 ? 327 ILE A C 1 ATOM 2577 O O . ILE A 1 327 ? 16.276 7.249 21.400 1.00 21.33 ? 327 ILE A O 1 ATOM 2578 C CB . ILE A 1 327 ? 14.651 9.482 20.029 1.00 21.19 ? 327 ILE A CB 1 ATOM 2579 C CG1 . ILE A 1 327 ? 14.332 10.406 18.822 1.00 22.19 ? 327 ILE A CG1 1 ATOM 2580 C CG2 . ILE A 1 327 ? 14.063 9.924 21.359 1.00 22.96 ? 327 ILE A CG2 1 ATOM 2581 C CD1 . ILE A 1 327 ? 14.787 11.837 19.034 1.00 25.75 ? 327 ILE A CD1 1 ATOM 2582 N N . TYR A 1 328 ? 17.010 9.107 22.433 1.00 20.72 ? 328 TYR A N 1 ATOM 2583 C CA . TYR A 1 328 ? 17.431 8.403 23.662 1.00 20.48 ? 328 TYR A CA 1 ATOM 2584 C C . TYR A 1 328 ? 16.310 8.479 24.705 1.00 20.29 ? 328 TYR A C 1 ATOM 2585 O O . TYR A 1 328 ? 15.843 9.585 25.076 1.00 21.24 ? 328 TYR A O 1 ATOM 2586 C CB . TYR A 1 328 ? 18.718 9.047 24.210 1.00 20.90 ? 328 TYR A CB 1 ATOM 2587 C CG . TYR A 1 328 ? 19.123 8.533 25.578 1.00 20.91 ? 328 TYR A CG 1 ATOM 2588 C CD1 . TYR A 1 328 ? 18.927 7.194 25.951 1.00 22.15 ? 328 TYR A CD1 1 ATOM 2589 C CD2 . TYR A 1 328 ? 19.727 9.406 26.504 1.00 21.71 ? 328 TYR A CD2 1 ATOM 2590 C CE1 . TYR A 1 328 ? 19.272 6.749 27.267 1.00 22.16 ? 328 TYR A CE1 1 ATOM 2591 C CE2 . TYR A 1 328 ? 20.094 8.988 27.772 1.00 22.20 ? 328 TYR A CE2 1 ATOM 2592 C CZ . TYR A 1 328 ? 19.894 7.651 28.141 1.00 22.25 ? 328 TYR A CZ 1 ATOM 2593 O OH . TYR A 1 328 ? 20.250 7.270 29.417 1.00 22.55 ? 328 TYR A OH 1 ATOM 2594 N N . ALA A 1 329 ? 15.864 7.303 25.150 1.00 20.53 ? 329 ALA A N 1 ATOM 2595 C CA . ALA A 1 329 ? 14.787 7.183 26.154 1.00 20.88 ? 329 ALA A CA 1 ATOM 2596 C C . ALA A 1 329 ? 14.844 8.288 27.205 1.00 20.88 ? 329 ALA A C 1 ATOM 2597 O O . ALA A 1 329 ? 15.844 8.422 27.896 1.00 21.02 ? 329 ALA A O 1 ATOM 2598 C CB . ALA A 1 329 ? 14.881 5.797 26.845 1.00 21.62 ? 329 ALA A CB 1 ATOM 2599 N N . GLY A 1 330 ? 13.761 9.055 27.318 1.00 21.33 ? 330 GLY A N 1 ATOM 2600 C CA . GLY A 1 330 ? 13.730 10.194 28.245 1.00 20.23 ? 330 GLY A CA 1 ATOM 2601 C C . GLY A 1 330 ? 13.703 11.513 27.490 1.00 21.58 ? 330 GLY A C 1 ATOM 2602 O O . GLY A 1 330 ? 13.122 12.485 27.971 1.00 21.15 ? 330 GLY A O 1 ATOM 2603 N N . GLN A 1 331 ? 14.291 11.546 26.300 1.00 21.32 ? 331 GLN A N 1 ATOM 2604 C CA . GLN A 1 331 ? 14.333 12.789 25.535 1.00 20.79 ? 331 GLN A CA 1 ATOM 2605 C C . GLN A 1 331 ? 12.905 13.217 25.279 1.00 20.40 ? 331 GLN A C 1 ATOM 2606 O O . GLN A 1 331 ? 12.565 14.423 25.320 1.00 21.72 ? 331 GLN A O 1 ATOM 2607 C CB . GLN A 1 331 ? 15.048 12.529 24.214 1.00 20.48 ? 331 GLN A CB 1 ATOM 2608 C CG . GLN A 1 331 ? 15.322 13.824 23.466 1.00 23.34 ? 331 GLN A CG 1 ATOM 2609 C CD . GLN A 1 331 ? 16.064 13.559 22.144 1.00 22.90 ? 331 GLN A CD 1 ATOM 2610 O OE1 . GLN A 1 331 ? 16.674 12.469 21.919 1.00 21.65 ? 331 GLN A OE1 1 ATOM 2611 N NE2 . GLN A 1 331 ? 16.054 14.557 21.285 1.00 25.42 ? 331 GLN A NE2 1 ATOM 2612 N N . GLU A 1 332 ? 12.043 12.239 25.030 1.00 19.13 ? 332 GLU A N 1 ATOM 2613 C CA . GLU A 1 332 ? 10.639 12.543 24.741 1.00 21.08 ? 332 GLU A CA 1 ATOM 2614 C C . GLU A 1 332 ? 9.832 13.008 25.951 1.00 20.66 ? 332 GLU A C 1 ATOM 2615 O O . GLU A 1 332 ? 8.691 13.465 25.793 1.00 22.22 ? 332 GLU A O 1 ATOM 2616 C CB . GLU A 1 332 ? 9.962 11.334 24.079 1.00 22.26 ? 332 GLU A CB 1 ATOM 2617 C CG . GLU A 1 332 ? 9.540 10.206 25.050 1.00 23.02 ? 332 GLU A CG 1 ATOM 2618 C CD . GLU A 1 332 ? 10.676 9.269 25.483 1.00 23.13 ? 332 GLU A CD 1 ATOM 2619 O OE1 . GLU A 1 332 ? 11.861 9.556 25.198 1.00 21.53 ? 332 GLU A OE1 1 ATOM 2620 O OE2 . GLU A 1 332 ? 10.348 8.236 26.137 1.00 22.36 ? 332 GLU A OE2 1 ATOM 2621 N N . GLN A 1 333 ? 10.388 12.841 27.145 1.00 19.48 ? 333 GLN A N 1 ATOM 2622 C CA . GLN A 1 333 ? 9.782 13.361 28.370 1.00 20.40 ? 333 GLN A CA 1 ATOM 2623 C C . GLN A 1 333 ? 10.571 14.558 28.901 1.00 20.54 ? 333 GLN A C 1 ATOM 2624 O O . GLN A 1 333 ? 10.419 14.973 30.063 1.00 21.44 ? 333 GLN A O 1 ATOM 2625 C CB . GLN A 1 333 ? 9.668 12.242 29.423 1.00 22.60 ? 333 GLN A CB 1 ATOM 2626 C CG . GLN A 1 333 ? 8.787 11.061 28.956 1.00 22.71 ? 333 GLN A CG 1 ATOM 2627 C CD . GLN A 1 333 ? 7.367 11.444 28.585 1.00 24.18 ? 333 GLN A CD 1 ATOM 2628 O OE1 . GLN A 1 333 ? 6.867 12.527 28.924 1.00 24.78 ? 333 GLN A OE1 1 ATOM 2629 N NE2 . GLN A 1 333 ? 6.698 10.533 27.865 1.00 23.76 ? 333 GLN A NE2 1 ATOM 2630 N N . HIS A 1 334 ? 11.402 15.121 28.026 1.00 20.42 ? 334 HIS A N 1 ATOM 2631 C CA . HIS A 1 334 ? 12.125 16.365 28.337 1.00 21.48 ? 334 HIS A CA 1 ATOM 2632 C C . HIS A 1 334 ? 13.035 16.200 29.568 1.00 21.36 ? 334 HIS A C 1 ATOM 2633 O O . HIS A 1 334 ? 13.213 17.106 30.401 1.00 21.19 ? 334 HIS A O 1 ATOM 2634 C CB . HIS A 1 334 ? 11.136 17.509 28.523 1.00 20.12 ? 334 HIS A CB 1 ATOM 2635 C CG . HIS A 1 334 ? 11.718 18.861 28.217 1.00 22.05 ? 334 HIS A CG 1 ATOM 2636 N ND1 . HIS A 1 334 ? 11.427 19.989 28.960 1.00 25.17 ? 334 HIS A ND1 1 ATOM 2637 C CD2 . HIS A 1 334 ? 12.559 19.263 27.232 1.00 23.54 ? 334 HIS A CD2 1 ATOM 2638 C CE1 . HIS A 1 334 ? 12.081 21.028 28.446 1.00 23.85 ? 334 HIS A CE1 1 ATOM 2639 N NE2 . HIS A 1 334 ? 12.767 20.614 27.395 1.00 24.36 ? 334 HIS A NE2 1 ATOM 2640 N N . TYR A 1 335 ? 13.664 15.026 29.657 1.00 21.92 ? 335 TYR A N 1 ATOM 2641 C CA . TYR A 1 335 ? 14.614 14.776 30.723 1.00 22.18 ? 335 TYR A CA 1 ATOM 2642 C C . TYR A 1 335 ? 15.811 15.710 30.571 1.00 21.20 ? 335 TYR A C 1 ATOM 2643 O O . TYR A 1 335 ? 16.208 16.056 29.449 1.00 21.80 ? 335 TYR A O 1 ATOM 2644 C CB . TYR A 1 335 ? 15.070 13.307 30.680 1.00 21.01 ? 335 TYR A CB 1 ATOM 2645 C CG . TYR A 1 335 ? 14.148 12.294 31.387 1.00 21.37 ? 335 TYR A CG 1 ATOM 2646 C CD1 . TYR A 1 335 ? 12.842 12.623 31.770 1.00 20.30 ? 335 TYR A CD1 1 ATOM 2647 C CD2 . TYR A 1 335 ? 14.593 11.012 31.666 1.00 21.64 ? 335 TYR A CD2 1 ATOM 2648 C CE1 . TYR A 1 335 ? 12.018 11.698 32.425 1.00 20.76 ? 335 TYR A CE1 1 ATOM 2649 C CE2 . TYR A 1 335 ? 13.772 10.087 32.309 1.00 20.91 ? 335 TYR A CE2 1 ATOM 2650 C CZ . TYR A 1 335 ? 12.476 10.456 32.696 1.00 22.06 ? 335 TYR A CZ 1 ATOM 2651 O OH . TYR A 1 335 ? 11.608 9.624 33.388 1.00 22.17 ? 335 TYR A OH 1 ATOM 2652 N N . ALA A 1 336 ? 16.368 16.092 31.721 1.00 20.43 ? 336 ALA A N 1 ATOM 2653 C CA . ALA A 1 336 ? 17.338 17.179 31.788 1.00 20.95 ? 336 ALA A CA 1 ATOM 2654 C C . ALA A 1 336 ? 18.619 16.814 32.543 1.00 22.47 ? 336 ALA A C 1 ATOM 2655 O O . ALA A 1 336 ? 19.360 17.713 32.947 1.00 22.40 ? 336 ALA A O 1 ATOM 2656 C CB . ALA A 1 336 ? 16.687 18.397 32.441 1.00 21.66 ? 336 ALA A CB 1 ATOM 2657 N N . GLY A 1 337 ? 18.894 15.518 32.711 1.00 21.40 ? 337 GLY A N 1 ATOM 2658 C CA . GLY A 1 337 ? 20.131 15.131 33.426 1.00 21.82 ? 337 GLY A CA 1 ATOM 2659 C C . GLY A 1 337 ? 21.399 15.548 32.681 1.00 20.87 ? 337 GLY A C 1 ATOM 2660 O O . GLY A 1 337 ? 21.428 15.515 31.429 1.00 21.26 ? 337 GLY A O 1 ATOM 2661 N N . GLY A 1 338 ? 22.423 15.933 33.451 1.00 22.66 ? 338 GLY A N 1 ATOM 2662 C CA . GLY A 1 338 ? 23.757 16.224 32.925 1.00 21.80 ? 338 GLY A CA 1 ATOM 2663 C C . GLY A 1 338 ? 24.591 14.964 32.697 1.00 22.70 ? 338 GLY A C 1 ATOM 2664 O O . GLY A 1 338 ? 24.049 13.843 32.446 1.00 22.73 ? 338 GLY A O 1 ATOM 2665 N N . ASN A 1 339 ? 25.915 15.099 32.793 1.00 23.10 ? 339 ASN A N 1 ATOM 2666 C CA . ASN A 1 339 ? 26.791 13.966 32.474 1.00 22.42 ? 339 ASN A CA 1 ATOM 2667 C C . ASN A 1 339 ? 26.641 12.747 33.399 1.00 23.52 ? 339 ASN A C 1 ATOM 2668 O O . ASN A 1 339 ? 26.224 12.875 34.563 1.00 23.73 ? 339 ASN A O 1 ATOM 2669 C CB . ASN A 1 339 ? 28.291 14.389 32.390 1.00 23.57 ? 339 ASN A CB 1 ATOM 2670 C CG . ASN A 1 339 ? 28.654 15.008 31.045 1.00 24.12 ? 339 ASN A CG 1 ATOM 2671 O OD1 . ASN A 1 339 ? 28.383 14.423 29.981 1.00 24.87 ? 339 ASN A OD1 1 ATOM 2672 N ND2 . ASN A 1 339 ? 29.282 16.184 31.083 1.00 26.62 ? 339 ASN A ND2 1 ATOM 2673 N N . ASP A 1 340 ? 26.948 11.582 32.834 1.00 23.16 ? 340 ASP A N 1 ATOM 2674 C CA . ASP A 1 340 ? 26.976 10.289 33.510 1.00 24.00 ? 340 ASP A CA 1 ATOM 2675 C C . ASP A 1 340 ? 27.435 10.473 34.977 1.00 24.08 ? 340 ASP A C 1 ATOM 2676 O O . ASP A 1 340 ? 28.540 10.997 35.206 1.00 25.34 ? 340 ASP A O 1 ATOM 2677 C CB . ASP A 1 340 ? 27.995 9.414 32.720 1.00 24.99 ? 340 ASP A CB 1 ATOM 2678 C CG . ASP A 1 340 ? 28.125 7.994 33.248 1.00 28.07 ? 340 ASP A CG 1 ATOM 2679 O OD1 . ASP A 1 340 ? 27.552 7.675 34.312 1.00 28.32 ? 340 ASP A OD1 1 ATOM 2680 O OD2 . ASP A 1 340 ? 28.810 7.175 32.574 1.00 28.45 ? 340 ASP A OD2 1 ATOM 2681 N N . PRO A 1 341 ? 26.657 9.965 35.952 1.00 23.01 ? 341 PRO A N 1 ATOM 2682 C CA . PRO A 1 341 ? 25.437 9.141 35.815 1.00 22.66 ? 341 PRO A CA 1 ATOM 2683 C C . PRO A 1 341 ? 24.095 9.880 35.703 1.00 21.67 ? 341 PRO A C 1 ATOM 2684 O O . PRO A 1 341 ? 23.043 9.223 35.653 1.00 21.78 ? 341 PRO A O 1 ATOM 2685 C CB . PRO A 1 341 ? 25.443 8.347 37.137 1.00 23.86 ? 341 PRO A CB 1 ATOM 2686 C CG . PRO A 1 341 ? 25.964 9.360 38.126 1.00 24.49 ? 341 PRO A CG 1 ATOM 2687 C CD . PRO A 1 341 ? 27.014 10.157 37.386 1.00 25.13 ? 341 PRO A CD 1 ATOM 2688 N N . ALA A 1 342 ? 24.099 11.215 35.665 1.00 20.56 ? 342 ALA A N 1 ATOM 2689 C CA . ALA A 1 342 ? 22.832 11.954 35.776 1.00 20.11 ? 342 ALA A CA 1 ATOM 2690 C C . ALA A 1 342 ? 21.924 11.797 34.555 1.00 20.19 ? 342 ALA A C 1 ATOM 2691 O O . ALA A 1 342 ? 20.704 12.114 34.609 1.00 21.66 ? 342 ALA A O 1 ATOM 2692 C CB . ALA A 1 342 ? 23.092 13.422 36.088 1.00 21.95 ? 342 ALA A CB 1 ATOM 2693 N N . ASN A 1 343 ? 22.516 11.358 33.449 1.00 20.19 ? 343 ASN A N 1 ATOM 2694 C CA . ASN A 1 343 ? 21.783 11.134 32.206 1.00 20.33 ? 343 ASN A CA 1 ATOM 2695 C C . ASN A 1 343 ? 21.273 9.705 32.019 1.00 22.34 ? 343 ASN A C 1 ATOM 2696 O O . ASN A 1 343 ? 20.877 9.335 30.909 1.00 22.67 ? 343 ASN A O 1 ATOM 2697 C CB . ASN A 1 343 ? 22.609 11.595 30.980 1.00 21.72 ? 343 ASN A CB 1 ATOM 2698 C CG . ASN A 1 343 ? 23.977 10.926 30.914 1.00 22.49 ? 343 ASN A CG 1 ATOM 2699 O OD1 . ASN A 1 343 ? 24.244 9.993 31.690 1.00 21.74 ? 343 ASN A OD1 1 ATOM 2700 N ND2 . ASN A 1 343 ? 24.848 11.376 29.978 1.00 21.63 ? 343 ASN A ND2 1 ATOM 2701 N N . ARG A 1 344 ? 21.305 8.919 33.088 1.00 21.86 ? 344 ARG A N 1 ATOM 2702 C CA . ARG A 1 344 ? 20.744 7.578 33.049 1.00 21.90 ? 344 ARG A CA 1 ATOM 2703 C C . ARG A 1 344 ? 19.463 7.485 33.915 1.00 21.76 ? 344 ARG A C 1 ATOM 2704 O O . ARG A 1 344 ? 19.189 6.443 34.544 1.00 21.37 ? 344 ARG A O 1 ATOM 2705 C CB . ARG A 1 344 ? 21.765 6.496 33.447 1.00 21.76 ? 344 ARG A CB 1 ATOM 2706 C CG . ARG A 1 344 ? 22.922 6.364 32.394 1.00 23.10 ? 344 ARG A CG 1 ATOM 2707 C CD . ARG A 1 344 ? 24.156 7.166 32.851 1.00 25.72 ? 344 ARG A CD 1 ATOM 2708 N NE . ARG A 1 344 ? 25.141 7.145 31.772 1.00 25.15 ? 344 ARG A NE 1 ATOM 2709 C CZ . ARG A 1 344 ? 25.971 6.123 31.535 1.00 27.29 ? 344 ARG A CZ 1 ATOM 2710 N NH1 . ARG A 1 344 ? 25.967 5.056 32.328 1.00 24.57 ? 344 ARG A NH1 1 ATOM 2711 N NH2 . ARG A 1 344 ? 26.784 6.164 30.479 1.00 26.75 ? 344 ARG A NH2 1 ATOM 2712 N N . GLU A 1 345 ? 18.631 8.533 33.876 1.00 20.57 ? 345 GLU A N 1 ATOM 2713 C CA . GLU A 1 345 ? 17.355 8.504 34.569 1.00 21.50 ? 345 GLU A CA 1 ATOM 2714 C C . GLU A 1 345 ? 16.452 7.378 34.108 1.00 21.88 ? 345 GLU A C 1 ATOM 2715 O O . GLU A 1 345 ? 16.433 7.038 32.912 1.00 21.93 ? 345 GLU A O 1 ATOM 2716 C CB . GLU A 1 345 ? 16.599 9.819 34.403 1.00 21.73 ? 345 GLU A CB 1 ATOM 2717 C CG . GLU A 1 345 ? 17.458 11.095 34.590 1.00 23.07 ? 345 GLU A CG 1 ATOM 2718 C CD . GLU A 1 345 ? 17.942 11.650 33.241 1.00 23.50 ? 345 GLU A CD 1 ATOM 2719 O OE1 . GLU A 1 345 ? 18.563 10.893 32.469 1.00 23.97 ? 345 GLU A OE1 1 ATOM 2720 O OE2 . GLU A 1 345 ? 17.677 12.870 32.973 1.00 23.55 ? 345 GLU A OE2 1 ATOM 2721 N N . ALA A 1 346 ? 15.705 6.800 35.067 1.00 22.15 ? 346 ALA A N 1 ATOM 2722 C CA . ALA A 1 346 ? 14.730 5.766 34.706 1.00 21.77 ? 346 ALA A CA 1 ATOM 2723 C C . ALA A 1 346 ? 13.541 6.354 33.936 1.00 22.04 ? 346 ALA A C 1 ATOM 2724 O O . ALA A 1 346 ? 12.922 7.314 34.348 1.00 22.03 ? 346 ALA A O 1 ATOM 2725 C CB . ALA A 1 346 ? 14.239 5.011 35.958 1.00 22.44 ? 346 ALA A CB 1 ATOM 2726 N N . THR A 1 347 ? 13.216 5.757 32.794 1.00 22.03 ? 347 THR A N 1 ATOM 2727 C CA . THR A 1 347 ? 12.092 6.275 32.009 1.00 21.58 ? 347 THR A CA 1 ATOM 2728 C C . THR A 1 347 ? 10.760 6.072 32.721 1.00 22.15 ? 347 THR A C 1 ATOM 2729 O O . THR A 1 347 ? 9.832 6.879 32.560 1.00 23.31 ? 347 THR A O 1 ATOM 2730 C CB . THR A 1 347 ? 12.023 5.525 30.658 1.00 22.82 ? 347 THR A CB 1 ATOM 2731 O OG1 . THR A 1 347 ? 13.354 5.255 30.170 1.00 23.92 ? 347 THR A OG1 1 ATOM 2732 C CG2 . THR A 1 347 ? 11.232 6.347 29.621 1.00 23.05 ? 347 THR A CG2 1 ATOM 2733 N N . TRP A 1 348 ? 10.651 4.997 33.511 1.00 22.43 ? 348 TRP A N 1 ATOM 2734 C CA . TRP A 1 348 ? 9.362 4.716 34.168 1.00 22.01 ? 348 TRP A CA 1 ATOM 2735 C C . TRP A 1 348 ? 8.922 5.819 35.112 1.00 21.29 ? 348 TRP A C 1 ATOM 2736 O O . TRP A 1 348 ? 7.725 5.992 35.332 1.00 22.16 ? 348 TRP A O 1 ATOM 2737 C CB . TRP A 1 348 ? 9.348 3.374 34.902 1.00 22.61 ? 348 TRP A CB 1 ATOM 2738 C CG . TRP A 1 348 ? 10.319 3.206 36.058 1.00 22.21 ? 348 TRP A CG 1 ATOM 2739 C CD1 . TRP A 1 348 ? 10.175 3.655 37.354 1.00 22.90 ? 348 TRP A CD1 1 ATOM 2740 C CD2 . TRP A 1 348 ? 11.546 2.457 36.030 1.00 21.24 ? 348 TRP A CD2 1 ATOM 2741 N NE1 . TRP A 1 348 ? 11.239 3.248 38.126 1.00 22.45 ? 348 TRP A NE1 1 ATOM 2742 C CE2 . TRP A 1 348 ? 12.095 2.498 37.347 1.00 22.03 ? 348 TRP A CE2 1 ATOM 2743 C CE3 . TRP A 1 348 ? 12.225 1.740 35.033 1.00 22.01 ? 348 TRP A CE3 1 ATOM 2744 C CZ2 . TRP A 1 348 ? 13.309 1.859 37.671 1.00 21.63 ? 348 TRP A CZ2 1 ATOM 2745 C CZ3 . TRP A 1 348 ? 13.430 1.120 35.363 1.00 22.11 ? 348 TRP A CZ3 1 ATOM 2746 C CH2 . TRP A 1 348 ? 13.953 1.175 36.664 1.00 22.33 ? 348 TRP A CH2 1 ATOM 2747 N N . LEU A 1 349 ? 9.869 6.560 35.681 1.00 20.72 ? 349 LEU A N 1 ATOM 2748 C CA . LEU A 1 349 ? 9.486 7.591 36.665 1.00 21.05 ? 349 LEU A CA 1 ATOM 2749 C C . LEU A 1 349 ? 8.658 8.695 36.036 1.00 21.55 ? 349 LEU A C 1 ATOM 2750 O O . LEU A 1 349 ? 8.005 9.484 36.759 1.00 24.14 ? 349 LEU A O 1 ATOM 2751 C CB . LEU A 1 349 ? 10.712 8.156 37.389 1.00 22.19 ? 349 LEU A CB 1 ATOM 2752 C CG . LEU A 1 349 ? 11.362 7.148 38.355 1.00 22.27 ? 349 LEU A CG 1 ATOM 2753 C CD1 . LEU A 1 349 ? 12.704 7.647 38.834 1.00 23.63 ? 349 LEU A CD1 1 ATOM 2754 C CD2 . LEU A 1 349 ? 10.459 6.921 39.531 1.00 23.48 ? 349 LEU A CD2 1 ATOM 2755 N N . SER A 1 350 ? 8.691 8.780 34.701 1.00 20.96 ? 350 SER A N 1 ATOM 2756 C CA . SER A 1 350 ? 7.902 9.826 34.013 1.00 21.24 ? 350 SER A CA 1 ATOM 2757 C C . SER A 1 350 ? 6.428 9.445 34.027 1.00 22.56 ? 350 SER A C 1 ATOM 2758 O O . SER A 1 350 ? 5.585 10.282 33.766 1.00 23.40 ? 350 SER A O 1 ATOM 2759 C CB . SER A 1 350 ? 8.355 9.969 32.560 1.00 20.79 ? 350 SER A CB 1 ATOM 2760 O OG . SER A 1 350 ? 8.076 8.792 31.803 1.00 21.63 ? 350 SER A OG 1 ATOM 2761 N N . GLY A 1 351 ? 6.124 8.172 34.271 1.00 22.31 ? 351 GLY A N 1 ATOM 2762 C CA . GLY A 1 351 ? 4.739 7.661 34.082 1.00 23.39 ? 351 GLY A CA 1 ATOM 2763 C C . GLY A 1 351 ? 4.404 7.321 32.622 1.00 23.10 ? 351 GLY A C 1 ATOM 2764 O O . GLY A 1 351 ? 3.260 6.923 32.322 1.00 24.01 ? 351 GLY A O 1 ATOM 2765 N N . TYR A 1 352 ? 5.373 7.496 31.734 1.00 22.83 ? 352 TYR A N 1 ATOM 2766 C CA . TYR A 1 352 ? 5.191 7.244 30.315 1.00 22.36 ? 352 TYR A CA 1 ATOM 2767 C C . TYR A 1 352 ? 3.987 7.944 29.657 1.00 23.18 ? 352 TYR A C 1 ATOM 2768 O O . TYR A 1 352 ? 3.239 7.309 28.930 1.00 24.41 ? 352 TYR A O 1 ATOM 2769 C CB . TYR A 1 352 ? 5.050 5.749 30.038 1.00 22.86 ? 352 TYR A CB 1 ATOM 2770 C CG . TYR A 1 352 ? 6.090 4.787 30.584 1.00 21.29 ? 352 TYR A CG 1 ATOM 2771 C CD1 . TYR A 1 352 ? 7.288 4.574 29.936 1.00 21.31 ? 352 TYR A CD1 1 ATOM 2772 C CD2 . TYR A 1 352 ? 5.817 4.023 31.693 1.00 20.99 ? 352 TYR A CD2 1 ATOM 2773 C CE1 . TYR A 1 352 ? 8.202 3.656 30.414 1.00 20.00 ? 352 TYR A CE1 1 ATOM 2774 C CE2 . TYR A 1 352 ? 6.714 3.112 32.172 1.00 20.90 ? 352 TYR A CE2 1 ATOM 2775 C CZ . TYR A 1 352 ? 7.905 2.925 31.533 1.00 22.22 ? 352 TYR A CZ 1 ATOM 2776 O OH . TYR A 1 352 ? 8.782 2.004 32.034 1.00 22.11 ? 352 TYR A OH 1 ATOM 2777 N N . PRO A 1 353 ? 3.798 9.238 29.882 1.00 24.01 ? 353 PRO A N 1 ATOM 2778 C CA . PRO A 1 353 ? 2.618 9.889 29.294 1.00 23.17 ? 353 PRO A CA 1 ATOM 2779 C C . PRO A 1 353 ? 2.766 10.049 27.783 1.00 23.50 ? 353 PRO A C 1 ATOM 2780 O O . PRO A 1 353 ? 3.788 10.533 27.299 1.00 23.76 ? 353 PRO A O 1 ATOM 2781 C CB . PRO A 1 353 ? 2.591 11.255 30.003 1.00 24.01 ? 353 PRO A CB 1 ATOM 2782 C CG . PRO A 1 353 ? 4.023 11.514 30.333 1.00 23.73 ? 353 PRO A CG 1 ATOM 2783 C CD . PRO A 1 353 ? 4.619 10.177 30.674 1.00 24.26 ? 353 PRO A CD 1 ATOM 2784 N N . THR A 1 354 ? 1.737 9.673 27.042 1.00 23.61 ? 354 THR A N 1 ATOM 2785 C CA . THR A 1 354 ? 1.779 9.746 25.581 1.00 22.41 ? 354 THR A CA 1 ATOM 2786 C C . THR A 1 354 ? 1.264 11.079 25.065 1.00 24.04 ? 354 THR A C 1 ATOM 2787 O O . THR A 1 354 ? 1.191 11.283 23.840 1.00 25.40 ? 354 THR A O 1 ATOM 2788 C CB . THR A 1 354 ? 0.949 8.614 24.979 1.00 22.47 ? 354 THR A CB 1 ATOM 2789 O OG1 . THR A 1 354 ? -0.411 8.743 25.427 1.00 23.68 ? 354 THR A OG1 1 ATOM 2790 C CG2 . THR A 1 354 ? 1.507 7.253 25.425 1.00 24.41 ? 354 THR A CG2 1 ATOM 2791 N N . ASP A 1 355 ? 0.861 11.950 25.987 1.00 24.02 ? 355 ASP A N 1 ATOM 2792 C CA . ASP A 1 355 ? 0.465 13.294 25.596 1.00 24.56 ? 355 ASP A CA 1 ATOM 2793 C C . ASP A 1 355 ? 1.479 14.361 25.977 1.00 23.72 ? 355 ASP A C 1 ATOM 2794 O O . ASP A 1 355 ? 1.132 15.528 26.040 1.00 25.95 ? 355 ASP A O 1 ATOM 2795 C CB . ASP A 1 355 ? -0.915 13.656 26.175 1.00 26.47 ? 355 ASP A CB 1 ATOM 2796 C CG . ASP A 1 355 ? -0.953 13.586 27.692 1.00 28.11 ? 355 ASP A CG 1 ATOM 2797 O OD1 . ASP A 1 355 ? 0.058 13.178 28.327 1.00 28.50 ? 355 ASP A OD1 1 ATOM 2798 O OD2 . ASP A 1 355 ? -2.013 13.966 28.279 1.00 30.99 ? 355 ASP A OD2 1 ATOM 2799 N N . SER A 1 356 ? 2.725 13.988 26.245 1.00 23.05 ? 356 SER A N 1 ATOM 2800 C CA . SER A 1 356 ? 3.702 15.045 26.535 1.00 23.79 ? 356 SER A CA 1 ATOM 2801 C C . SER A 1 356 ? 4.011 15.789 25.241 1.00 23.05 ? 356 SER A C 1 ATOM 2802 O O . SER A 1 356 ? 3.818 15.248 24.123 1.00 22.45 ? 356 SER A O 1 ATOM 2803 C CB . SER A 1 356 ? 4.967 14.480 27.164 1.00 25.80 ? 356 SER A CB 1 ATOM 2804 O OG . SER A 1 356 ? 5.731 13.769 26.218 1.00 27.97 ? 356 SER A OG 1 ATOM 2805 N N . GLU A 1 357 ? 4.463 17.037 25.365 1.00 23.67 ? 357 GLU A N 1 ATOM 2806 C CA . GLU A 1 357 ? 4.706 17.830 24.154 1.00 24.54 ? 357 GLU A CA 1 ATOM 2807 C C . GLU A 1 357 ? 5.689 17.160 23.185 1.00 24.16 ? 357 GLU A C 1 ATOM 2808 O O . GLU A 1 357 ? 5.480 17.146 21.955 1.00 23.78 ? 357 GLU A O 1 ATOM 2809 C CB . GLU A 1 357 ? 5.193 19.228 24.516 1.00 28.37 ? 357 GLU A CB 1 ATOM 2810 C CG . GLU A 1 357 ? 4.107 20.046 25.200 1.00 31.72 ? 357 GLU A CG 1 ATOM 2811 C CD . GLU A 1 357 ? 2.894 20.239 24.326 1.00 36.28 ? 357 GLU A CD 1 ATOM 2812 O OE1 . GLU A 1 357 ? 3.043 20.692 23.163 1.00 38.65 ? 357 GLU A OE1 1 ATOM 2813 O OE2 . GLU A 1 357 ? 1.779 19.931 24.793 1.00 39.70 ? 357 GLU A OE2 1 ATOM 2814 N N . LEU A 1 358 ? 6.765 16.597 23.725 1.00 22.56 ? 358 LEU A N 1 ATOM 2815 C CA . LEU A 1 358 ? 7.768 15.999 22.847 1.00 22.84 ? 358 LEU A CA 1 ATOM 2816 C C . LEU A 1 358 ? 7.358 14.624 22.314 1.00 21.58 ? 358 LEU A C 1 ATOM 2817 O O . LEU A 1 358 ? 7.741 14.248 21.200 1.00 21.59 ? 358 LEU A O 1 ATOM 2818 C CB . LEU A 1 358 ? 9.128 15.960 23.537 1.00 23.68 ? 358 LEU A CB 1 ATOM 2819 C CG . LEU A 1 358 ? 9.716 17.374 23.663 1.00 25.75 ? 358 LEU A CG 1 ATOM 2820 C CD1 . LEU A 1 358 ? 10.883 17.434 24.640 1.00 26.67 ? 358 LEU A CD1 1 ATOM 2821 C CD2 . LEU A 1 358 ? 10.176 17.849 22.262 1.00 27.52 ? 358 LEU A CD2 1 ATOM 2822 N N . TYR A 1 359 ? 6.597 13.854 23.096 1.00 20.80 ? 359 TYR A N 1 ATOM 2823 C CA . TYR A 1 359 ? 6.035 12.613 22.559 1.00 21.36 ? 359 TYR A CA 1 ATOM 2824 C C . TYR A 1 359 ? 5.227 12.911 21.280 1.00 22.05 ? 359 TYR A C 1 ATOM 2825 O O . TYR A 1 359 ? 5.415 12.289 20.250 1.00 21.52 ? 359 TYR A O 1 ATOM 2826 C CB . TYR A 1 359 ? 5.144 11.930 23.609 1.00 21.96 ? 359 TYR A CB 1 ATOM 2827 C CG . TYR A 1 359 ? 4.735 10.498 23.250 1.00 21.67 ? 359 TYR A CG 1 ATOM 2828 C CD1 . TYR A 1 359 ? 3.708 10.258 22.310 1.00 21.87 ? 359 TYR A CD1 1 ATOM 2829 C CD2 . TYR A 1 359 ? 5.353 9.411 23.858 1.00 21.07 ? 359 TYR A CD2 1 ATOM 2830 C CE1 . TYR A 1 359 ? 3.331 8.964 21.974 1.00 22.72 ? 359 TYR A CE1 1 ATOM 2831 C CE2 . TYR A 1 359 ? 4.972 8.106 23.536 1.00 23.24 ? 359 TYR A CE2 1 ATOM 2832 C CZ . TYR A 1 359 ? 3.972 7.891 22.609 1.00 22.93 ? 359 TYR A CZ 1 ATOM 2833 O OH . TYR A 1 359 ? 3.633 6.585 22.273 1.00 23.25 ? 359 TYR A OH 1 ATOM 2834 N N . LYS A 1 360 ? 4.339 13.899 21.369 1.00 21.37 ? 360 LYS A N 1 ATOM 2835 C CA . LYS A 1 360 ? 3.496 14.251 20.235 1.00 21.30 ? 360 LYS A CA 1 ATOM 2836 C C . LYS A 1 360 ? 4.328 14.800 19.092 1.00 22.12 ? 360 LYS A C 1 ATOM 2837 O O . LYS A 1 360 ? 4.069 14.500 17.902 1.00 21.77 ? 360 LYS A O 1 ATOM 2838 C CB . LYS A 1 360 ? 2.453 15.272 20.662 1.00 23.49 ? 360 LYS A CB 1 ATOM 2839 C CG . LYS A 1 360 ? 1.440 14.682 21.603 1.00 27.03 ? 360 LYS A CG 1 ATOM 2840 C CD . LYS A 1 360 ? 0.348 15.735 21.793 1.00 30.55 ? 360 LYS A CD 1 ATOM 2841 C CE . LYS A 1 360 ? -0.739 15.289 22.729 1.00 33.70 ? 360 LYS A CE 1 ATOM 2842 N NZ . LYS A 1 360 ? -1.594 16.492 23.094 1.00 36.81 ? 360 LYS A NZ 1 ATOM 2843 N N . LEU A 1 361 ? 5.346 15.604 19.411 1.00 21.20 ? 361 LEU A N 1 ATOM 2844 C CA . LEU A 1 361 ? 6.171 16.146 18.315 1.00 21.97 ? 361 LEU A CA 1 ATOM 2845 C C . LEU A 1 361 ? 6.892 15.013 17.592 1.00 21.97 ? 361 LEU A C 1 ATOM 2846 O O . LEU A 1 361 ? 6.857 14.912 16.351 1.00 24.10 ? 361 LEU A O 1 ATOM 2847 C CB . LEU A 1 361 ? 7.201 17.150 18.840 1.00 22.33 ? 361 LEU A CB 1 ATOM 2848 C CG . LEU A 1 361 ? 8.266 17.797 17.932 1.00 22.34 ? 361 LEU A CG 1 ATOM 2849 C CD1 . LEU A 1 361 ? 9.300 16.842 17.349 1.00 23.56 ? 361 LEU A CD1 1 ATOM 2850 C CD2 . LEU A 1 361 ? 7.582 18.650 16.851 1.00 22.63 ? 361 LEU A CD2 1 ATOM 2851 N N . ILE A 1 362 ? 7.577 14.164 18.362 1.00 20.66 ? 362 ILE A N 1 ATOM 2852 C CA . ILE A 1 362 ? 8.266 13.001 17.802 1.00 21.24 ? 362 ILE A CA 1 ATOM 2853 C C . ILE A 1 362 ? 7.329 12.100 16.984 1.00 19.99 ? 362 ILE A C 1 ATOM 2854 O O . ILE A 1 362 ? 7.665 11.729 15.824 1.00 21.11 ? 362 ILE A O 1 ATOM 2855 C CB . ILE A 1 362 ? 8.997 12.240 18.881 1.00 22.37 ? 362 ILE A CB 1 ATOM 2856 C CG1 . ILE A 1 362 ? 10.161 13.108 19.403 1.00 22.52 ? 362 ILE A CG1 1 ATOM 2857 C CG2 . ILE A 1 362 ? 9.615 10.987 18.342 1.00 22.58 ? 362 ILE A CG2 1 ATOM 2858 C CD1 . ILE A 1 362 ? 10.796 12.563 20.710 1.00 25.60 ? 362 ILE A CD1 1 ATOM 2859 N N . ALA A 1 363 ? 6.134 11.824 17.514 1.00 21.91 ? 363 ALA A N 1 ATOM 2860 C CA . ALA A 1 363 ? 5.155 11.022 16.762 1.00 22.50 ? 363 ALA A CA 1 ATOM 2861 C C . ALA A 1 363 ? 4.837 11.655 15.410 1.00 22.80 ? 363 ALA A C 1 ATOM 2862 O O . ALA A 1 363 ? 4.765 10.952 14.384 1.00 23.58 ? 363 ALA A O 1 ATOM 2863 C CB . ALA A 1 363 ? 3.881 10.846 17.566 1.00 24.07 ? 363 ALA A CB 1 ATOM 2864 N N . SER A 1 364 ? 4.580 12.967 15.421 1.00 20.97 ? 364 SER A N 1 ATOM 2865 C CA . SER A 1 364 ? 4.226 13.673 14.188 1.00 22.10 ? 364 SER A CA 1 ATOM 2866 C C . SER A 1 364 ? 5.365 13.625 13.173 1.00 22.81 ? 364 SER A C 1 ATOM 2867 O O . SER A 1 364 ? 5.141 13.452 11.968 1.00 22.53 ? 364 SER A O 1 ATOM 2868 C CB . SER A 1 364 ? 3.866 15.121 14.513 1.00 22.79 ? 364 SER A CB 1 ATOM 2869 O OG . SER A 1 364 ? 2.582 15.166 15.128 1.00 21.07 ? 364 SER A OG 1 ATOM 2870 N N . ALA A 1 365 ? 6.596 13.778 13.654 1.00 21.68 ? 365 ALA A N 1 ATOM 2871 C CA . ALA A 1 365 ? 7.748 13.783 12.733 1.00 22.01 ? 365 ALA A CA 1 ATOM 2872 C C . ALA A 1 365 ? 8.045 12.390 12.192 1.00 20.86 ? 365 ALA A C 1 ATOM 2873 O O . ALA A 1 365 ? 8.275 12.217 10.977 1.00 21.38 ? 365 ALA A O 1 ATOM 2874 C CB . ALA A 1 365 ? 8.977 14.374 13.395 1.00 21.38 ? 365 ALA A CB 1 ATOM 2875 N N . ASN A 1 366 ? 8.067 11.379 13.068 1.00 20.97 ? 366 ASN A N 1 ATOM 2876 C CA . ASN A 1 366 ? 8.233 10.016 12.553 1.00 21.61 ? 366 ASN A CA 1 ATOM 2877 C C . ASN A 1 366 ? 7.072 9.685 11.613 1.00 22.13 ? 366 ASN A C 1 ATOM 2878 O O . ASN A 1 366 ? 7.255 8.971 10.629 1.00 21.36 ? 366 ASN A O 1 ATOM 2879 C CB . ASN A 1 366 ? 8.287 8.981 13.666 1.00 21.16 ? 366 ASN A CB 1 ATOM 2880 C CG . ASN A 1 366 ? 9.701 8.775 14.217 1.00 22.49 ? 366 ASN A CG 1 ATOM 2881 O OD1 . ASN A 1 366 ? 10.682 8.763 13.462 1.00 23.11 ? 366 ASN A OD1 1 ATOM 2882 N ND2 . ASN A 1 366 ? 9.803 8.570 15.531 1.00 22.89 ? 366 ASN A ND2 1 ATOM 2883 N N . ALA A 1 367 ? 5.866 10.179 11.912 1.00 20.34 ? 367 ALA A N 1 ATOM 2884 C CA . ALA A 1 367 ? 4.713 9.816 11.085 1.00 21.49 ? 367 ALA A CA 1 ATOM 2885 C C . ALA A 1 367 ? 4.936 10.252 9.643 1.00 20.19 ? 367 ALA A C 1 ATOM 2886 O O . ALA A 1 367 ? 4.721 9.479 8.689 1.00 21.83 ? 367 ALA A O 1 ATOM 2887 C CB . ALA A 1 367 ? 3.415 10.443 11.614 1.00 20.38 ? 367 ALA A CB 1 ATOM 2888 N N . ILE A 1 368 ? 5.413 11.481 9.461 1.00 20.24 ? 368 ILE A N 1 ATOM 2889 C CA . ILE A 1 368 ? 5.574 11.971 8.073 1.00 21.06 ? 368 ILE A CA 1 ATOM 2890 C C . ILE A 1 368 ? 6.790 11.319 7.376 1.00 20.76 ? 368 ILE A C 1 ATOM 2891 O O . ILE A 1 368 ? 6.732 11.027 6.162 1.00 21.58 ? 368 ILE A O 1 ATOM 2892 C CB . ILE A 1 368 ? 5.638 13.518 7.969 1.00 20.82 ? 368 ILE A CB 1 ATOM 2893 C CG1 . ILE A 1 368 ? 5.651 13.946 6.485 1.00 22.19 ? 368 ILE A CG1 1 ATOM 2894 C CG2 . ILE A 1 368 ? 6.863 14.053 8.712 1.00 21.90 ? 368 ILE A CG2 1 ATOM 2895 C CD1 . ILE A 1 368 ? 4.371 13.562 5.767 1.00 24.72 ? 368 ILE A CD1 1 ATOM 2896 N N . ARG A 1 369 ? 7.869 11.089 8.124 1.00 21.00 ? 369 ARG A N 1 ATOM 2897 C CA . ARG A 1 369 ? 9.041 10.372 7.570 1.00 21.23 ? 369 ARG A CA 1 ATOM 2898 C C . ARG A 1 369 ? 8.630 8.966 7.116 1.00 21.52 ? 369 ARG A C 1 ATOM 2899 O O . ARG A 1 369 ? 8.901 8.541 5.971 1.00 22.19 ? 369 ARG A O 1 ATOM 2900 C CB . ARG A 1 369 ? 10.165 10.306 8.605 1.00 21.43 ? 369 ARG A CB 1 ATOM 2901 C CG . ARG A 1 369 ? 11.305 9.367 8.175 1.00 21.16 ? 369 ARG A CG 1 ATOM 2902 C CD . ARG A 1 369 ? 12.531 9.585 9.035 1.00 21.71 ? 369 ARG A CD 1 ATOM 2903 N NE . ARG A 1 369 ? 13.680 8.824 8.538 1.00 22.31 ? 369 ARG A NE 1 ATOM 2904 C CZ . ARG A 1 369 ? 13.852 7.515 8.738 1.00 23.67 ? 369 ARG A CZ 1 ATOM 2905 N NH1 . ARG A 1 369 ? 12.950 6.813 9.435 1.00 23.00 ? 369 ARG A NH1 1 ATOM 2906 N NH2 . ARG A 1 369 ? 14.924 6.906 8.233 1.00 21.28 ? 369 ARG A NH2 1 ATOM 2907 N N . ASN A 1 370 ? 7.944 8.234 7.996 1.00 21.51 ? 370 ASN A N 1 ATOM 2908 C CA . ASN A 1 370 ? 7.518 6.880 7.655 1.00 21.37 ? 370 ASN A CA 1 ATOM 2909 C C . ASN A 1 370 ? 6.591 6.875 6.443 1.00 21.62 ? 370 ASN A C 1 ATOM 2910 O O . ASN A 1 370 ? 6.722 6.059 5.538 1.00 21.62 ? 370 ASN A O 1 ATOM 2911 C CB . ASN A 1 370 ? 6.816 6.205 8.837 1.00 20.48 ? 370 ASN A CB 1 ATOM 2912 C CG . ASN A 1 370 ? 7.759 5.896 9.997 1.00 22.35 ? 370 ASN A CG 1 ATOM 2913 O OD1 . ASN A 1 370 ? 8.983 5.821 9.818 1.00 22.43 ? 370 ASN A OD1 1 ATOM 2914 N ND2 . ASN A 1 370 ? 7.197 5.710 11.197 1.00 22.98 ? 370 ASN A ND2 1 ATOM 2915 N N . TYR A 1 371 ? 5.633 7.794 6.441 1.00 21.57 ? 371 TYR A N 1 ATOM 2916 C CA . TYR A 1 371 ? 4.729 7.883 5.309 1.00 21.22 ? 371 TYR A CA 1 ATOM 2917 C C . TYR A 1 371 ? 5.470 8.224 4.009 1.00 20.48 ? 371 TYR A C 1 ATOM 2918 O O . TYR A 1 371 ? 5.252 7.603 2.977 1.00 20.67 ? 371 TYR A O 1 ATOM 2919 C CB . TYR A 1 371 ? 3.649 8.912 5.601 1.00 23.50 ? 371 TYR A CB 1 ATOM 2920 C CG . TYR A 1 371 ? 2.615 8.970 4.505 1.00 25.33 ? 371 TYR A CG 1 ATOM 2921 C CD1 . TYR A 1 371 ? 1.540 8.088 4.496 1.00 25.48 ? 371 TYR A CD1 1 ATOM 2922 C CD2 . TYR A 1 371 ? 2.713 9.905 3.479 1.00 25.78 ? 371 TYR A CD2 1 ATOM 2923 C CE1 . TYR A 1 371 ? 0.578 8.135 3.480 1.00 25.81 ? 371 TYR A CE1 1 ATOM 2924 C CE2 . TYR A 1 371 ? 1.759 9.951 2.457 1.00 27.00 ? 371 TYR A CE2 1 ATOM 2925 C CZ . TYR A 1 371 ? 0.696 9.059 2.471 1.00 26.23 ? 371 TYR A CZ 1 ATOM 2926 O OH . TYR A 1 371 ? -0.272 9.105 1.480 1.00 27.28 ? 371 TYR A OH 1 ATOM 2927 N N . ALA A 1 372 ? 6.346 9.219 4.065 1.00 21.73 ? 372 ALA A N 1 ATOM 2928 C CA . ALA A 1 372 ? 7.074 9.645 2.883 1.00 21.71 ? 372 ALA A CA 1 ATOM 2929 C C . ALA A 1 372 ? 7.888 8.485 2.298 1.00 22.71 ? 372 ALA A C 1 ATOM 2930 O O . ALA A 1 372 ? 7.888 8.260 1.097 1.00 23.74 ? 372 ALA A O 1 ATOM 2931 C CB . ALA A 1 372 ? 7.962 10.844 3.202 1.00 21.96 ? 372 ALA A CB 1 ATOM 2932 N N . ILE A 1 373 ? 8.552 7.737 3.172 1.00 23.23 ? 373 ILE A N 1 ATOM 2933 C CA . ILE A 1 373 ? 9.304 6.567 2.763 1.00 22.78 ? 373 ILE A CA 1 ATOM 2934 C C . ILE A 1 373 ? 8.386 5.564 2.062 1.00 23.38 ? 373 ILE A C 1 ATOM 2935 O O . ILE A 1 373 ? 8.758 4.975 1.037 1.00 25.71 ? 373 ILE A O 1 ATOM 2936 C CB . ILE A 1 373 ? 10.015 5.911 3.967 1.00 22.41 ? 373 ILE A CB 1 ATOM 2937 C CG1 . ILE A 1 373 ? 11.195 6.793 4.421 1.00 22.42 ? 373 ILE A CG1 1 ATOM 2938 C CG2 . ILE A 1 373 ? 10.523 4.516 3.599 1.00 23.39 ? 373 ILE A CG2 1 ATOM 2939 C CD1 . ILE A 1 373 ? 11.715 6.493 5.862 1.00 22.75 ? 373 ILE A CD1 1 ATOM 2940 N N . SER A 1 374 ? 7.185 5.367 2.587 1.00 24.93 ? 374 SER A N 1 ATOM 2941 C CA . SER A 1 374 ? 6.278 4.387 1.986 1.00 25.46 ? 374 SER A CA 1 ATOM 2942 C C . SER A 1 374 ? 5.853 4.791 0.576 1.00 25.88 ? 374 SER A C 1 ATOM 2943 O O . SER A 1 374 ? 5.502 3.931 -0.243 1.00 27.04 ? 374 SER A O 1 ATOM 2944 C CB . SER A 1 374 ? 5.054 4.120 2.862 1.00 25.02 ? 374 SER A CB 1 ATOM 2945 O OG . SER A 1 374 ? 4.129 5.201 2.805 1.00 23.71 ? 374 SER A OG 1 ATOM 2946 N N . LYS A 1 375 ? 5.932 6.082 0.274 1.00 26.90 ? 375 LYS A N 1 ATOM 2947 C CA . LYS A 1 375 ? 5.512 6.573 -1.060 1.00 27.51 ? 375 LYS A CA 1 ATOM 2948 C C . LYS A 1 375 ? 6.653 6.944 -2.021 1.00 27.48 ? 375 LYS A C 1 ATOM 2949 O O . LYS A 1 375 ? 6.409 7.156 -3.212 1.00 27.92 ? 375 LYS A O 1 ATOM 2950 C CB . LYS A 1 375 ? 4.562 7.758 -0.915 1.00 28.54 ? 375 LYS A CB 1 ATOM 2951 C CG . LYS A 1 375 ? 3.286 7.403 -0.197 1.00 29.76 ? 375 LYS A CG 1 ATOM 2952 C CD . LYS A 1 375 ? 2.439 6.423 -1.006 1.00 30.18 ? 375 LYS A CD 1 ATOM 2953 C CE . LYS A 1 375 ? 1.127 6.137 -0.284 1.00 31.93 ? 375 LYS A CE 1 ATOM 2954 N NZ . LYS A 1 375 ? 0.258 5.145 -0.988 1.00 31.48 ? 375 LYS A NZ 1 ATOM 2955 N N . ASP A 1 376 ? 7.883 7.029 -1.512 1.00 26.68 ? 376 ASP A N 1 ATOM 2956 C CA . ASP A 1 376 ? 9.012 7.546 -2.290 1.00 26.03 ? 376 ASP A CA 1 ATOM 2957 C C . ASP A 1 376 ? 10.212 6.648 -2.053 1.00 27.09 ? 376 ASP A C 1 ATOM 2958 O O . ASP A 1 376 ? 10.886 6.774 -1.028 1.00 26.06 ? 376 ASP A O 1 ATOM 2959 C CB . ASP A 1 376 ? 9.333 8.989 -1.871 1.00 26.18 ? 376 ASP A CB 1 ATOM 2960 C CG . ASP A 1 376 ? 10.523 9.593 -2.630 1.00 26.87 ? 376 ASP A CG 1 ATOM 2961 O OD1 . ASP A 1 376 ? 11.003 8.986 -3.614 1.00 27.27 ? 376 ASP A OD1 1 ATOM 2962 O OD2 . ASP A 1 376 ? 10.984 10.685 -2.223 1.00 27.29 ? 376 ASP A OD2 1 ATOM 2963 N N . THR A 1 377 ? 10.467 5.732 -2.991 1.00 27.87 ? 377 THR A N 1 ATOM 2964 C CA . THR A 1 377 ? 11.565 4.767 -2.832 1.00 27.55 ? 377 THR A CA 1 ATOM 2965 C C . THR A 1 377 ? 12.913 5.484 -2.845 1.00 27.62 ? 377 THR A C 1 ATOM 2966 O O . THR A 1 377 ? 13.950 4.911 -2.491 1.00 28.94 ? 377 THR A O 1 ATOM 2967 C CB . THR A 1 377 ? 11.549 3.720 -3.970 1.00 29.00 ? 377 THR A CB 1 ATOM 2968 O OG1 . THR A 1 377 ? 11.514 4.402 -5.228 1.00 29.08 ? 377 THR A OG1 1 ATOM 2969 C CG2 . THR A 1 377 ? 10.327 2.798 -3.859 1.00 28.54 ? 377 THR A CG2 1 ATOM 2970 N N . GLY A 1 378 ? 12.903 6.741 -3.262 1.00 26.87 ? 378 GLY A N 1 ATOM 2971 C CA . GLY A 1 378 ? 14.125 7.511 -3.331 1.00 27.04 ? 378 GLY A CA 1 ATOM 2972 C C . GLY A 1 378 ? 14.430 8.270 -2.056 1.00 26.16 ? 378 GLY A C 1 ATOM 2973 O O . GLY A 1 378 ? 15.502 8.845 -1.913 1.00 25.76 ? 378 GLY A O 1 ATOM 2974 N N . PHE A 1 379 ? 13.482 8.306 -1.127 1.00 25.36 ? 379 PHE A N 1 ATOM 2975 C CA . PHE A 1 379 ? 13.633 9.201 0.015 1.00 25.19 ? 379 PHE A CA 1 ATOM 2976 C C . PHE A 1 379 ? 14.868 8.855 0.838 1.00 24.66 ? 379 PHE A C 1 ATOM 2977 O O . PHE A 1 379 ? 15.656 9.731 1.182 1.00 25.42 ? 379 PHE A O 1 ATOM 2978 C CB . PHE A 1 379 ? 12.415 9.159 0.915 1.00 24.84 ? 379 PHE A CB 1 ATOM 2979 C CG . PHE A 1 379 ? 12.526 10.073 2.130 1.00 24.32 ? 379 PHE A CG 1 ATOM 2980 C CD1 . PHE A 1 379 ? 12.158 11.421 2.043 1.00 24.91 ? 379 PHE A CD1 1 ATOM 2981 C CD2 . PHE A 1 379 ? 12.993 9.579 3.349 1.00 25.60 ? 379 PHE A CD2 1 ATOM 2982 C CE1 . PHE A 1 379 ? 12.247 12.262 3.174 1.00 24.74 ? 379 PHE A CE1 1 ATOM 2983 C CE2 . PHE A 1 379 ? 13.072 10.392 4.488 1.00 25.16 ? 379 PHE A CE2 1 ATOM 2984 C CZ . PHE A 1 379 ? 12.713 11.742 4.394 1.00 25.31 ? 379 PHE A CZ 1 ATOM 2985 N N . VAL A 1 380 ? 15.046 7.579 1.147 1.00 24.66 ? 380 VAL A N 1 ATOM 2986 C CA . VAL A 1 380 ? 16.124 7.239 2.072 1.00 24.81 ? 380 VAL A CA 1 ATOM 2987 C C . VAL A 1 380 ? 17.514 7.430 1.497 1.00 25.50 ? 380 VAL A C 1 ATOM 2988 O O . VAL A 1 380 ? 18.465 7.552 2.279 1.00 26.93 ? 380 VAL A O 1 ATOM 2989 C CB . VAL A 1 380 ? 16.026 5.808 2.644 1.00 25.73 ? 380 VAL A CB 1 ATOM 2990 C CG1 . VAL A 1 380 ? 14.801 5.688 3.560 1.00 25.31 ? 380 VAL A CG1 1 ATOM 2991 C CG2 . VAL A 1 380 ? 16.076 4.756 1.533 1.00 26.12 ? 380 VAL A CG2 1 ATOM 2992 N N . THR A 1 381 ? 17.653 7.420 0.155 1.00 24.56 ? 381 THR A N 1 ATOM 2993 C CA . THR A 1 381 ? 18.959 7.616 -0.453 1.00 25.43 ? 381 THR A CA 1 ATOM 2994 C C . THR A 1 381 ? 19.140 9.046 -0.949 1.00 25.41 ? 381 THR A C 1 ATOM 2995 O O . THR A 1 381 ? 20.245 9.462 -1.304 1.00 24.88 ? 381 THR A O 1 ATOM 2996 C CB . THR A 1 381 ? 19.205 6.618 -1.595 1.00 26.94 ? 381 THR A CB 1 ATOM 2997 O OG1 . THR A 1 381 ? 18.083 6.648 -2.486 1.00 27.61 ? 381 THR A OG1 1 ATOM 2998 C CG2 . THR A 1 381 ? 19.395 5.181 -1.025 1.00 27.98 ? 381 THR A CG2 1 ATOM 2999 N N . TYR A 1 382 ? 18.057 9.823 -0.926 1.00 25.85 ? 382 TYR A N 1 ATOM 3000 C CA . TYR A 1 382 ? 18.121 11.215 -1.335 1.00 26.23 ? 382 TYR A CA 1 ATOM 3001 C C . TYR A 1 382 ? 18.936 12.024 -0.327 1.00 26.94 ? 382 TYR A C 1 ATOM 3002 O O . TYR A 1 382 ? 18.630 12.006 0.872 1.00 27.44 ? 382 TYR A O 1 ATOM 3003 C CB . TYR A 1 382 ? 16.696 11.777 -1.473 1.00 26.27 ? 382 TYR A CB 1 ATOM 3004 C CG . TYR A 1 382 ? 16.646 13.123 -2.147 1.00 25.19 ? 382 TYR A CG 1 ATOM 3005 C CD1 . TYR A 1 382 ? 16.997 14.258 -1.450 1.00 25.32 ? 382 TYR A CD1 1 ATOM 3006 C CD2 . TYR A 1 382 ? 16.281 13.249 -3.484 1.00 25.29 ? 382 TYR A CD2 1 ATOM 3007 C CE1 . TYR A 1 382 ? 16.977 15.486 -2.040 1.00 26.06 ? 382 TYR A CE1 1 ATOM 3008 C CE2 . TYR A 1 382 ? 16.251 14.480 -4.088 1.00 25.49 ? 382 TYR A CE2 1 ATOM 3009 C CZ . TYR A 1 382 ? 16.588 15.602 -3.348 1.00 25.94 ? 382 TYR A CZ 1 ATOM 3010 O OH . TYR A 1 382 ? 16.591 16.856 -3.912 1.00 26.56 ? 382 TYR A OH 1 ATOM 3011 N N . LYS A 1 383 ? 19.981 12.727 -0.781 1.00 27.13 ? 383 LYS A N 1 ATOM 3012 C CA . LYS A 1 383 ? 20.798 13.494 0.181 1.00 26.69 ? 383 LYS A CA 1 ATOM 3013 C C . LYS A 1 383 ? 20.113 14.760 0.701 1.00 25.59 ? 383 LYS A C 1 ATOM 3014 O O . LYS A 1 383 ? 19.788 15.668 -0.066 1.00 22.95 ? 383 LYS A O 1 ATOM 3015 C CB . LYS A 1 383 ? 22.151 13.899 -0.417 1.00 28.07 ? 383 LYS A CB 1 ATOM 3016 C CG . LYS A 1 383 ? 22.959 12.770 -1.011 1.00 28.25 ? 383 LYS A CG 1 ATOM 3017 C CD . LYS A 1 383 ? 23.260 11.693 0.002 1.00 27.56 ? 383 LYS A CD 1 ATOM 3018 C CE . LYS A 1 383 ? 24.481 10.882 -0.453 1.00 27.55 ? 383 LYS A CE 1 ATOM 3019 N NZ . LYS A 1 383 ? 24.971 10.056 0.692 1.00 26.67 ? 383 LYS A NZ 1 ATOM 3020 N N . ASN A 1 384 ? 19.970 14.869 2.020 1.00 25.38 ? 384 ASN A N 1 ATOM 3021 C CA . ASN A 1 384 ? 19.392 16.050 2.643 1.00 26.17 ? 384 ASN A CA 1 ATOM 3022 C C . ASN A 1 384 ? 20.191 17.292 2.259 1.00 27.26 ? 384 ASN A C 1 ATOM 3023 O O . ASN A 1 384 ? 21.434 17.292 2.284 1.00 28.53 ? 384 ASN A O 1 ATOM 3024 C CB . ASN A 1 384 ? 19.391 15.852 4.163 1.00 25.66 ? 384 ASN A CB 1 ATOM 3025 C CG . ASN A 1 384 ? 18.743 17.006 4.943 1.00 26.75 ? 384 ASN A CG 1 ATOM 3026 O OD1 . ASN A 1 384 ? 17.772 17.644 4.496 1.00 26.36 ? 384 ASN A OD1 1 ATOM 3027 N ND2 . ASN A 1 384 ? 19.266 17.253 6.148 1.00 25.45 ? 384 ASN A ND2 1 ATOM 3028 N N . TRP A 1 385 ? 19.459 18.346 1.934 1.00 28.47 ? 385 TRP A N 1 ATOM 3029 C CA . TRP A 1 385 ? 20.000 19.512 1.260 1.00 30.45 ? 385 TRP A CA 1 ATOM 3030 C C . TRP A 1 385 ? 19.567 20.786 1.989 1.00 28.56 ? 385 TRP A C 1 ATOM 3031 O O . TRP A 1 385 ? 18.391 21.153 1.976 1.00 28.06 ? 385 TRP A O 1 ATOM 3032 C CB . TRP A 1 385 ? 19.510 19.478 -0.203 1.00 34.20 ? 385 TRP A CB 1 ATOM 3033 C CG . TRP A 1 385 ? 19.707 20.711 -1.036 1.00 35.90 ? 385 TRP A CG 1 ATOM 3034 C CD1 . TRP A 1 385 ? 20.690 21.653 -0.914 1.00 37.06 ? 385 TRP A CD1 1 ATOM 3035 C CD2 . TRP A 1 385 ? 18.912 21.105 -2.158 1.00 36.93 ? 385 TRP A CD2 1 ATOM 3036 N NE1 . TRP A 1 385 ? 20.544 22.623 -1.891 1.00 37.73 ? 385 TRP A NE1 1 ATOM 3037 C CE2 . TRP A 1 385 ? 19.452 22.313 -2.656 1.00 37.07 ? 385 TRP A CE2 1 ATOM 3038 C CE3 . TRP A 1 385 ? 17.784 20.558 -2.788 1.00 36.77 ? 385 TRP A CE3 1 ATOM 3039 C CZ2 . TRP A 1 385 ? 18.919 22.967 -3.763 1.00 37.19 ? 385 TRP A CZ2 1 ATOM 3040 C CZ3 . TRP A 1 385 ? 17.253 21.215 -3.891 1.00 36.85 ? 385 TRP A CZ3 1 ATOM 3041 C CH2 . TRP A 1 385 ? 17.814 22.410 -4.360 1.00 36.85 ? 385 TRP A CH2 1 ATOM 3042 N N . PRO A 1 386 ? 20.519 21.477 2.634 1.00 26.36 ? 386 PRO A N 1 ATOM 3043 C CA . PRO A 1 386 ? 20.125 22.755 3.247 1.00 25.47 ? 386 PRO A CA 1 ATOM 3044 C C . PRO A 1 386 ? 19.813 23.775 2.162 1.00 24.71 ? 386 PRO A C 1 ATOM 3045 O O . PRO A 1 386 ? 20.628 23.988 1.261 1.00 23.86 ? 386 PRO A O 1 ATOM 3046 C CB . PRO A 1 386 ? 21.377 23.195 4.023 1.00 25.42 ? 386 PRO A CB 1 ATOM 3047 C CG . PRO A 1 386 ? 22.301 21.962 4.038 1.00 25.74 ? 386 PRO A CG 1 ATOM 3048 C CD . PRO A 1 386 ? 21.939 21.142 2.862 1.00 26.50 ? 386 PRO A CD 1 ATOM 3049 N N . ILE A 1 387 ? 18.638 24.396 2.242 1.00 23.58 ? 387 ILE A N 1 ATOM 3050 C CA . ILE A 1 387 ? 18.187 25.298 1.180 1.00 25.22 ? 387 ILE A CA 1 ATOM 3051 C C . ILE A 1 387 ? 18.111 26.748 1.614 1.00 25.07 ? 387 ILE A C 1 ATOM 3052 O O . ILE A 1 387 ? 17.972 27.639 0.777 1.00 26.61 ? 387 ILE A O 1 ATOM 3053 C CB . ILE A 1 387 ? 16.798 24.925 0.682 1.00 24.51 ? 387 ILE A CB 1 ATOM 3054 C CG1 . ILE A 1 387 ? 15.781 25.045 1.822 1.00 24.22 ? 387 ILE A CG1 1 ATOM 3055 C CG2 . ILE A 1 387 ? 16.787 23.538 0.140 1.00 26.02 ? 387 ILE A CG2 1 ATOM 3056 C CD1 . ILE A 1 387 ? 14.360 24.996 1.332 1.00 22.17 ? 387 ILE A CD1 1 ATOM 3057 N N . TYR A 1 388 ? 18.179 26.987 2.919 1.00 25.57 ? 388 TYR A N 1 ATOM 3058 C CA . TYR A 1 388 ? 18.068 28.331 3.469 1.00 27.05 ? 388 TYR A CA 1 ATOM 3059 C C . TYR A 1 388 ? 18.665 28.437 4.869 1.00 27.46 ? 388 TYR A C 1 ATOM 3060 O O . TYR A 1 388 ? 18.642 27.471 5.652 1.00 26.67 ? 388 TYR A O 1 ATOM 3061 C CB . TYR A 1 388 ? 16.599 28.753 3.503 1.00 29.43 ? 388 TYR A CB 1 ATOM 3062 C CG . TYR A 1 388 ? 16.361 30.111 4.113 1.00 29.92 ? 388 TYR A CG 1 ATOM 3063 C CD1 . TYR A 1 388 ? 16.464 31.263 3.338 1.00 30.68 ? 388 TYR A CD1 1 ATOM 3064 C CD2 . TYR A 1 388 ? 16.025 30.248 5.459 1.00 30.57 ? 388 TYR A CD2 1 ATOM 3065 C CE1 . TYR A 1 388 ? 16.258 32.508 3.891 1.00 31.24 ? 388 TYR A CE1 1 ATOM 3066 C CE2 . TYR A 1 388 ? 15.807 31.488 6.018 1.00 30.48 ? 388 TYR A CE2 1 ATOM 3067 C CZ . TYR A 1 388 ? 15.920 32.615 5.230 1.00 31.22 ? 388 TYR A CZ 1 ATOM 3068 O OH . TYR A 1 388 ? 15.696 33.853 5.778 1.00 30.43 ? 388 TYR A OH 1 ATOM 3069 N N . LYS A 1 389 ? 19.249 29.589 5.173 1.00 28.22 ? 389 LYS A N 1 ATOM 3070 C CA . LYS A 1 389 ? 19.608 29.905 6.546 1.00 29.80 ? 389 LYS A CA 1 ATOM 3071 C C . LYS A 1 389 ? 19.601 31.402 6.775 1.00 30.92 ? 389 LYS A C 1 ATOM 3072 O O . LYS A 1 389 ? 19.914 32.178 5.867 1.00 30.16 ? 389 LYS A O 1 ATOM 3073 C CB . LYS A 1 389 ? 20.959 29.322 6.955 1.00 30.26 ? 389 LYS A CB 1 ATOM 3074 C CG . LYS A 1 389 ? 22.145 29.890 6.184 1.00 31.58 ? 389 LYS A CG 1 ATOM 3075 C CD . LYS A 1 389 ? 23.443 29.281 6.665 1.00 31.54 ? 389 LYS A CD 1 ATOM 3076 C CE . LYS A 1 389 ? 24.546 29.579 5.686 1.00 31.58 ? 389 LYS A CE 1 ATOM 3077 N NZ . LYS A 1 389 ? 24.907 31.010 5.774 1.00 31.92 ? 389 LYS A NZ 1 ATOM 3078 N N . ASP A 1 390 ? 19.210 31.802 7.980 1.00 30.69 ? 390 ASP A N 1 ATOM 3079 C CA . ASP A 1 390 ? 19.450 33.165 8.447 1.00 32.07 ? 390 ASP A CA 1 ATOM 3080 C C . ASP A 1 390 ? 19.883 33.079 9.906 1.00 32.25 ? 390 ASP A C 1 ATOM 3081 O O . ASP A 1 390 ? 20.188 31.993 10.383 1.00 32.45 ? 390 ASP A O 1 ATOM 3082 C CB . ASP A 1 390 ? 18.239 34.084 8.223 1.00 31.94 ? 390 ASP A CB 1 ATOM 3083 C CG . ASP A 1 390 ? 16.996 33.615 8.957 1.00 33.55 ? 390 ASP A CG 1 ATOM 3084 O OD1 . ASP A 1 390 ? 17.120 33.147 10.117 1.00 31.89 ? 390 ASP A OD1 1 ATOM 3085 O OD2 . ASP A 1 390 ? 15.895 33.720 8.363 1.00 34.19 ? 390 ASP A OD2 1 ATOM 3086 N N . ASP A 1 391 ? 19.926 34.211 10.602 1.00 32.18 ? 391 ASP A N 1 ATOM 3087 C CA . ASP A 1 391 ? 20.456 34.258 11.958 1.00 31.76 ? 391 ASP A CA 1 ATOM 3088 C C . ASP A 1 391 ? 19.794 33.240 12.881 1.00 30.01 ? 391 ASP A C 1 ATOM 3089 O O . ASP A 1 391 ? 20.418 32.746 13.814 1.00 30.69 ? 391 ASP A O 1 ATOM 3090 C CB . ASP A 1 391 ? 20.244 35.642 12.558 1.00 35.07 ? 391 ASP A CB 1 ATOM 3091 C CG . ASP A 1 391 ? 21.169 36.667 11.967 1.00 37.16 ? 391 ASP A CG 1 ATOM 3092 O OD1 . ASP A 1 391 ? 22.247 36.261 11.464 1.00 38.88 ? 391 ASP A OD1 1 ATOM 3093 O OD2 . ASP A 1 391 ? 20.822 37.867 12.011 1.00 39.63 ? 391 ASP A OD2 1 ATOM 3094 N N . THR A 1 392 ? 18.522 32.949 12.635 1.00 28.69 ? 392 THR A N 1 ATOM 3095 C CA . THR A 1 392 ? 17.752 32.148 13.602 1.00 26.95 ? 392 THR A CA 1 ATOM 3096 C C . THR A 1 392 ? 17.021 30.974 12.942 1.00 25.72 ? 392 THR A C 1 ATOM 3097 O O . THR A 1 392 ? 16.151 30.353 13.545 1.00 24.39 ? 392 THR A O 1 ATOM 3098 C CB . THR A 1 392 ? 16.697 33.018 14.342 1.00 27.31 ? 392 THR A CB 1 ATOM 3099 O OG1 . THR A 1 392 ? 15.705 33.431 13.409 1.00 27.48 ? 392 THR A OG1 1 ATOM 3100 C CG2 . THR A 1 392 ? 17.332 34.274 14.942 1.00 29.01 ? 392 THR A CG2 1 ATOM 3101 N N . THR A 1 393 ? 17.370 30.663 11.697 1.00 25.47 ? 393 THR A N 1 ATOM 3102 C CA . THR A 1 393 ? 16.572 29.713 10.934 1.00 23.35 ? 393 THR A CA 1 ATOM 3103 C C . THR A 1 393 ? 17.443 28.855 10.025 1.00 22.89 ? 393 THR A C 1 ATOM 3104 O O . THR A 1 393 ? 18.385 29.352 9.398 1.00 22.85 ? 393 THR A O 1 ATOM 3105 C CB . THR A 1 393 ? 15.620 30.445 9.975 1.00 24.53 ? 393 THR A CB 1 ATOM 3106 O OG1 . THR A 1 393 ? 14.968 31.512 10.677 1.00 25.03 ? 393 THR A OG1 1 ATOM 3107 C CG2 . THR A 1 393 ? 14.574 29.485 9.410 1.00 24.45 ? 393 THR A CG2 1 ATOM 3108 N N . ILE A 1 394 ? 17.102 27.587 9.928 1.00 23.11 ? 394 ILE A N 1 ATOM 3109 C CA . ILE A 1 394 ? 17.712 26.742 8.924 1.00 22.92 ? 394 ILE A CA 1 ATOM 3110 C C . ILE A 1 394 ? 16.596 25.940 8.278 1.00 23.19 ? 394 ILE A C 1 ATOM 3111 O O . ILE A 1 394 ? 15.698 25.487 8.958 1.00 23.99 ? 394 ILE A O 1 ATOM 3112 C CB . ILE A 1 394 ? 18.779 25.809 9.504 1.00 22.69 ? 394 ILE A CB 1 ATOM 3113 C CG1 . ILE A 1 394 ? 19.485 25.082 8.358 1.00 23.44 ? 394 ILE A CG1 1 ATOM 3114 C CG2 . ILE A 1 394 ? 18.156 24.812 10.455 1.00 22.90 ? 394 ILE A CG2 1 ATOM 3115 C CD1 . ILE A 1 394 ? 20.836 24.402 8.797 1.00 23.20 ? 394 ILE A CD1 1 ATOM 3116 N N . ALA A 1 395 ? 16.631 25.805 6.959 1.00 23.04 ? 395 ALA A N 1 ATOM 3117 C CA . ALA A 1 395 ? 15.636 24.996 6.287 1.00 22.26 ? 395 ALA A CA 1 ATOM 3118 C C . ALA A 1 395 ? 16.378 24.001 5.406 1.00 23.81 ? 395 ALA A C 1 ATOM 3119 O O . ALA A 1 395 ? 17.475 24.293 4.895 1.00 23.94 ? 395 ALA A O 1 ATOM 3120 C CB . ALA A 1 395 ? 14.712 25.856 5.447 1.00 23.56 ? 395 ALA A CB 1 ATOM 3121 N N . MET A 1 396 ? 15.767 22.842 5.219 1.00 23.03 ? 396 MET A N 1 ATOM 3122 C CA . MET A 1 396 ? 16.393 21.779 4.467 1.00 25.48 ? 396 MET A CA 1 ATOM 3123 C C . MET A 1 396 ? 15.327 20.974 3.736 1.00 24.38 ? 396 MET A C 1 ATOM 3124 O O . MET A 1 396 ? 14.154 21.019 4.086 1.00 25.06 ? 396 MET A O 1 ATOM 3125 C CB . MET A 1 396 ? 17.240 20.891 5.398 1.00 25.60 ? 396 MET A CB 1 ATOM 3126 C CG . MET A 1 396 ? 16.451 20.229 6.477 1.00 26.62 ? 396 MET A CG 1 ATOM 3127 S SD . MET A 1 396 ? 17.481 19.681 7.858 1.00 28.73 ? 396 MET A SD 1 ATOM 3128 C CE . MET A 1 396 ? 16.290 18.682 8.765 1.00 27.89 ? 396 MET A CE 1 ATOM 3129 N N . ARG A 1 397 ? 15.742 20.236 2.712 1.00 25.01 ? 397 ARG A N 1 ATOM 3130 C CA . ARG A 1 397 ? 14.797 19.546 1.841 1.00 24.15 ? 397 ARG A CA 1 ATOM 3131 C C . ARG A 1 397 ? 15.296 18.154 1.472 1.00 24.41 ? 397 ARG A C 1 ATOM 3132 O O . ARG A 1 397 ? 16.440 17.989 1.048 1.00 22.76 ? 397 ARG A O 1 ATOM 3133 C CB . ARG A 1 397 ? 14.539 20.365 0.575 1.00 24.81 ? 397 ARG A CB 1 ATOM 3134 C CG . ARG A 1 397 ? 13.901 19.574 -0.556 1.00 25.89 ? 397 ARG A CG 1 ATOM 3135 C CD . ARG A 1 397 ? 14.898 18.859 -1.453 1.00 25.65 ? 397 ARG A CD 1 ATOM 3136 N NE . ARG A 1 397 ? 14.236 18.004 -2.434 1.00 26.49 ? 397 ARG A NE 1 ATOM 3137 C CZ . ARG A 1 397 ? 13.840 18.412 -3.632 1.00 28.16 ? 397 ARG A CZ 1 ATOM 3138 N NH1 . ARG A 1 397 ? 14.037 19.669 -4.005 1.00 27.89 ? 397 ARG A NH1 1 ATOM 3139 N NH2 . ARG A 1 397 ? 13.245 17.564 -4.460 1.00 28.33 ? 397 ARG A NH2 1 ATOM 3140 N N . LYS A 1 398 ? 14.435 17.154 1.636 1.00 21.76 ? 398 LYS A N 1 ATOM 3141 C CA . LYS A 1 398 ? 14.831 15.774 1.406 1.00 23.20 ? 398 LYS A CA 1 ATOM 3142 C C . LYS A 1 398 ? 13.672 15.060 0.754 1.00 24.45 ? 398 LYS A C 1 ATOM 3143 O O . LYS A 1 398 ? 12.528 15.201 1.221 1.00 24.94 ? 398 LYS A O 1 ATOM 3144 C CB . LYS A 1 398 ? 15.130 15.089 2.739 1.00 23.40 ? 398 LYS A CB 1 ATOM 3145 C CG . LYS A 1 398 ? 15.688 13.670 2.621 1.00 25.08 ? 398 LYS A CG 1 ATOM 3146 C CD . LYS A 1 398 ? 16.147 13.174 4.020 1.00 24.04 ? 398 LYS A CD 1 ATOM 3147 C CE . LYS A 1 398 ? 16.442 11.664 4.018 1.00 25.00 ? 398 LYS A CE 1 ATOM 3148 N NZ . LYS A 1 398 ? 17.632 11.250 3.190 1.00 24.39 ? 398 LYS A NZ 1 ATOM 3149 N N . GLY A 1 399 ? 13.948 14.346 -0.342 1.00 24.18 ? 399 GLY A N 1 ATOM 3150 C CA . GLY A 1 399 ? 12.909 13.631 -1.045 1.00 22.28 ? 399 GLY A CA 1 ATOM 3151 C C . GLY A 1 399 ? 12.855 13.981 -2.525 1.00 22.54 ? 399 GLY A C 1 ATOM 3152 O O . GLY A 1 399 ? 13.215 15.087 -2.935 1.00 23.75 ? 399 GLY A O 1 ATOM 3153 N N . THR A 1 400 ? 12.382 13.032 -3.311 1.00 22.71 ? 400 THR A N 1 ATOM 3154 C CA . THR A 1 400 ? 12.269 13.185 -4.754 1.00 23.29 ? 400 THR A CA 1 ATOM 3155 C C . THR A 1 400 ? 11.352 14.353 -5.144 1.00 24.92 ? 400 THR A C 1 ATOM 3156 O O . THR A 1 400 ? 10.389 14.634 -4.436 1.00 24.61 ? 400 THR A O 1 ATOM 3157 C CB . THR A 1 400 ? 11.723 11.870 -5.344 1.00 23.02 ? 400 THR A CB 1 ATOM 3158 O OG1 . THR A 1 400 ? 12.592 10.789 -4.938 1.00 24.42 ? 400 THR A OG1 1 ATOM 3159 C CG2 . THR A 1 400 ? 11.624 11.947 -6.877 1.00 22.60 ? 400 THR A CG2 1 ATOM 3160 N N . ASP A 1 401 ? 11.663 15.037 -6.256 1.00 25.48 ? 401 ASP A N 1 ATOM 3161 C CA . ASP A 1 401 ? 10.825 16.133 -6.727 1.00 25.71 ? 401 ASP A CA 1 ATOM 3162 C C . ASP A 1 401 ? 9.378 15.676 -6.748 1.00 24.52 ? 401 ASP A C 1 ATOM 3163 O O . ASP A 1 401 ? 9.071 14.587 -7.264 1.00 22.85 ? 401 ASP A O 1 ATOM 3164 C CB . ASP A 1 401 ? 11.176 16.559 -8.162 1.00 28.61 ? 401 ASP A CB 1 ATOM 3165 C CG . ASP A 1 401 ? 12.421 17.448 -8.254 1.00 30.61 ? 401 ASP A CG 1 ATOM 3166 O OD1 . ASP A 1 401 ? 12.815 18.071 -7.249 1.00 32.35 ? 401 ASP A OD1 1 ATOM 3167 O OD2 . ASP A 1 401 ? 12.988 17.553 -9.371 1.00 30.74 ? 401 ASP A OD2 1 ATOM 3168 N N . GLY A 1 402 ? 8.503 16.527 -6.223 1.00 22.96 ? 402 GLY A N 1 ATOM 3169 C CA . GLY A 1 402 ? 7.071 16.279 -6.185 1.00 23.32 ? 402 GLY A CA 1 ATOM 3170 C C . GLY A 1 402 ? 6.620 15.644 -4.888 1.00 23.80 ? 402 GLY A C 1 ATOM 3171 O O . GLY A 1 402 ? 5.419 15.656 -4.569 1.00 22.52 ? 402 GLY A O 1 ATOM 3172 N N . SER A 1 403 ? 7.586 15.126 -4.129 1.00 23.02 ? 403 SER A N 1 ATOM 3173 C CA . SER A 1 403 ? 7.310 14.415 -2.883 1.00 23.20 ? 403 SER A CA 1 ATOM 3174 C C . SER A 1 403 ? 8.231 14.853 -1.729 1.00 22.26 ? 403 SER A C 1 ATOM 3175 O O . SER A 1 403 ? 8.305 14.172 -0.714 1.00 22.37 ? 403 SER A O 1 ATOM 3176 C CB . SER A 1 403 ? 7.503 12.912 -3.086 1.00 24.73 ? 403 SER A CB 1 ATOM 3177 O OG . SER A 1 403 ? 6.720 12.466 -4.175 1.00 26.75 ? 403 SER A OG 1 ATOM 3178 N N . GLN A 1 404 ? 8.957 15.953 -1.887 1.00 21.27 ? 404 GLN A N 1 ATOM 3179 C CA . GLN A 1 404 ? 9.986 16.280 -0.928 1.00 20.96 ? 404 GLN A CA 1 ATOM 3180 C C . GLN A 1 404 ? 9.369 16.825 0.370 1.00 21.80 ? 404 GLN A C 1 ATOM 3181 O O . GLN A 1 404 ? 8.332 17.507 0.363 1.00 20.92 ? 404 GLN A O 1 ATOM 3182 C CB . GLN A 1 404 ? 11.020 17.271 -1.493 1.00 20.19 ? 404 GLN A CB 1 ATOM 3183 C CG . GLN A 1 404 ? 10.455 18.654 -1.809 1.00 20.85 ? 404 GLN A CG 1 ATOM 3184 C CD . GLN A 1 404 ? 10.046 18.780 -3.244 1.00 21.16 ? 404 GLN A CD 1 ATOM 3185 O OE1 . GLN A 1 404 ? 9.450 17.867 -3.804 1.00 23.26 ? 404 GLN A OE1 1 ATOM 3186 N NE2 . GLN A 1 404 ? 10.318 19.944 -3.847 1.00 21.97 ? 404 GLN A NE2 1 ATOM 3187 N N . ILE A 1 405 ? 10.011 16.474 1.474 1.00 21.74 ? 405 ILE A N 1 ATOM 3188 C CA . ILE A 1 405 ? 9.689 17.063 2.757 1.00 22.26 ? 405 ILE A CA 1 ATOM 3189 C C . ILE A 1 405 ? 10.597 18.269 2.908 1.00 22.56 ? 405 ILE A C 1 ATOM 3190 O O . ILE A 1 405 ? 11.815 18.161 2.704 1.00 23.07 ? 405 ILE A O 1 ATOM 3191 C CB . ILE A 1 405 ? 9.975 16.115 3.918 1.00 23.25 ? 405 ILE A CB 1 ATOM 3192 C CG1 . ILE A 1 405 ? 9.041 14.912 3.877 1.00 23.60 ? 405 ILE A CG1 1 ATOM 3193 C CG2 . ILE A 1 405 ? 9.772 16.843 5.259 1.00 23.13 ? 405 ILE A CG2 1 ATOM 3194 C CD1 . ILE A 1 405 ? 9.325 13.888 4.990 1.00 23.89 ? 405 ILE A CD1 1 ATOM 3195 N N . VAL A 1 406 ? 10.010 19.414 3.227 1.00 21.35 ? 406 VAL A N 1 ATOM 3196 C CA . VAL A 1 406 ? 10.805 20.620 3.438 1.00 22.18 ? 406 VAL A CA 1 ATOM 3197 C C . VAL A 1 406 ? 10.607 21.079 4.875 1.00 22.45 ? 406 VAL A C 1 ATOM 3198 O O . VAL A 1 406 ? 9.462 21.318 5.303 1.00 22.80 ? 406 VAL A O 1 ATOM 3199 C CB . VAL A 1 406 ? 10.444 21.704 2.442 1.00 21.77 ? 406 VAL A CB 1 ATOM 3200 C CG1 . VAL A 1 406 ? 11.059 23.028 2.842 1.00 23.75 ? 406 VAL A CG1 1 ATOM 3201 C CG2 . VAL A 1 406 ? 10.937 21.290 1.050 1.00 22.86 ? 406 VAL A CG2 1 ATOM 3202 N N . THR A 1 407 ? 11.723 21.185 5.604 1.00 24.00 ? 407 THR A N 1 ATOM 3203 C CA . THR A 1 407 ? 11.673 21.412 7.067 1.00 23.08 ? 407 THR A CA 1 ATOM 3204 C C . THR A 1 407 ? 12.300 22.744 7.394 1.00 23.87 ? 407 THR A C 1 ATOM 3205 O O . THR A 1 407 ? 13.409 23.032 6.937 1.00 23.50 ? 407 THR A O 1 ATOM 3206 C CB . THR A 1 407 ? 12.437 20.309 7.796 1.00 25.00 ? 407 THR A CB 1 ATOM 3207 O OG1 . THR A 1 407 ? 11.853 19.040 7.487 1.00 25.54 ? 407 THR A OG1 1 ATOM 3208 C CG2 . THR A 1 407 ? 12.450 20.510 9.326 1.00 23.57 ? 407 THR A CG2 1 ATOM 3209 N N . ILE A 1 408 ? 11.606 23.550 8.196 1.00 21.16 ? 408 ILE A N 1 ATOM 3210 C CA . ILE A 1 408 ? 12.098 24.861 8.582 1.00 20.19 ? 408 ILE A CA 1 ATOM 3211 C C . ILE A 1 408 ? 12.230 24.840 10.113 1.00 21.07 ? 408 ILE A C 1 ATOM 3212 O O . ILE A 1 408 ? 11.216 24.651 10.828 1.00 22.78 ? 408 ILE A O 1 ATOM 3213 C CB . ILE A 1 408 ? 11.135 25.999 8.192 1.00 19.83 ? 408 ILE A CB 1 ATOM 3214 C CG1 . ILE A 1 408 ? 10.885 25.992 6.680 1.00 19.55 ? 408 ILE A CG1 1 ATOM 3215 C CG2 . ILE A 1 408 ? 11.732 27.324 8.593 1.00 22.11 ? 408 ILE A CG2 1 ATOM 3216 C CD1 . ILE A 1 408 ? 9.686 25.163 6.275 1.00 19.55 ? 408 ILE A CD1 1 ATOM 3217 N N . LEU A 1 409 ? 13.455 25.073 10.597 1.00 19.29 ? 409 LEU A N 1 ATOM 3218 C CA . LEU A 1 409 ? 13.724 25.026 12.035 1.00 19.78 ? 409 LEU A CA 1 ATOM 3219 C C . LEU A 1 409 ? 14.180 26.379 12.500 1.00 22.04 ? 409 LEU A C 1 ATOM 3220 O O . LEU A 1 409 ? 14.799 27.138 11.741 1.00 21.26 ? 409 LEU A O 1 ATOM 3221 C CB . LEU A 1 409 ? 14.811 23.983 12.347 1.00 20.18 ? 409 LEU A CB 1 ATOM 3222 C CG . LEU A 1 409 ? 14.504 22.601 11.805 1.00 21.72 ? 409 LEU A CG 1 ATOM 3223 C CD1 . LEU A 1 409 ? 15.696 21.655 12.074 1.00 22.73 ? 409 LEU A CD1 1 ATOM 3224 C CD2 . LEU A 1 409 ? 13.224 22.069 12.424 1.00 22.19 ? 409 LEU A CD2 1 ATOM 3225 N N . SER A 1 410 ? 13.866 26.687 13.752 1.00 22.03 ? 410 SER A N 1 ATOM 3226 C CA . SER A 1 410 ? 14.127 28.006 14.295 1.00 23.00 ? 410 SER A CA 1 ATOM 3227 C C . SER A 1 410 ? 14.794 27.856 15.653 1.00 21.79 ? 410 SER A C 1 ATOM 3228 O O . SER A 1 410 ? 14.520 26.894 16.381 1.00 23.29 ? 410 SER A O 1 ATOM 3229 C CB . SER A 1 410 ? 12.805 28.770 14.454 1.00 23.30 ? 410 SER A CB 1 ATOM 3230 O OG . SER A 1 410 ? 13.019 30.039 15.058 1.00 24.29 ? 410 SER A OG 1 ATOM 3231 N N . ASN A 1 411 ? 15.708 28.766 15.975 1.00 22.52 ? 411 ASN A N 1 ATOM 3232 C CA . ASN A 1 411 ? 16.213 28.824 17.347 1.00 21.47 ? 411 ASN A CA 1 ATOM 3233 C C . ASN A 1 411 ? 15.685 30.045 18.121 1.00 22.62 ? 411 ASN A C 1 ATOM 3234 O O . ASN A 1 411 ? 16.223 30.424 19.159 1.00 23.17 ? 411 ASN A O 1 ATOM 3235 C CB . ASN A 1 411 ? 17.741 28.629 17.454 1.00 22.48 ? 411 ASN A CB 1 ATOM 3236 C CG . ASN A 1 411 ? 18.544 29.788 16.883 1.00 23.83 ? 411 ASN A CG 1 ATOM 3237 O OD1 . ASN A 1 411 ? 17.992 30.835 16.510 1.00 23.91 ? 411 ASN A OD1 1 ATOM 3238 N ND2 . ASN A 1 411 ? 19.866 29.597 16.810 1.00 23.73 ? 411 ASN A ND2 1 ATOM 3239 N N . LYS A 1 412 ? 14.595 30.633 17.633 1.00 21.92 ? 412 LYS A N 1 ATOM 3240 C CA . LYS A 1 412 ? 13.966 31.749 18.358 1.00 22.37 ? 412 LYS A CA 1 ATOM 3241 C C . LYS A 1 412 ? 13.444 31.376 19.752 1.00 22.94 ? 412 LYS A C 1 ATOM 3242 O O . LYS A 1 412 ? 13.349 32.248 20.635 1.00 23.89 ? 412 LYS A O 1 ATOM 3243 C CB . LYS A 1 412 ? 12.832 32.396 17.552 1.00 24.01 ? 412 LYS A CB 1 ATOM 3244 C CG . LYS A 1 412 ? 13.337 33.106 16.314 1.00 25.91 ? 412 LYS A CG 1 ATOM 3245 C CD . LYS A 1 412 ? 12.204 33.741 15.555 1.00 27.78 ? 412 LYS A CD 1 ATOM 3246 C CE . LYS A 1 412 ? 12.763 34.417 14.330 1.00 29.30 ? 412 LYS A CE 1 ATOM 3247 N NZ . LYS A 1 412 ? 11.639 35.010 13.614 1.00 30.23 ? 412 LYS A NZ 1 ATOM 3248 N N . GLY A 1 413 ? 13.074 30.111 19.931 1.00 22.13 ? 413 GLY A N 1 ATOM 3249 C CA . GLY A 1 413 ? 12.589 29.626 21.235 1.00 21.89 ? 413 GLY A CA 1 ATOM 3250 C C . GLY A 1 413 ? 11.136 29.987 21.475 1.00 22.22 ? 413 GLY A C 1 ATOM 3251 O O . GLY A 1 413 ? 10.507 30.621 20.626 1.00 23.01 ? 413 GLY A O 1 ATOM 3252 N N . ALA A 1 414 ? 10.632 29.646 22.663 1.00 23.56 ? 414 ALA A N 1 ATOM 3253 C CA . ALA A 1 414 ? 9.207 29.726 22.970 1.00 24.03 ? 414 ALA A CA 1 ATOM 3254 C C . ALA A 1 414 ? 8.645 31.135 22.932 1.00 24.61 ? 414 ALA A C 1 ATOM 3255 O O . ALA A 1 414 ? 7.423 31.323 22.796 1.00 26.57 ? 414 ALA A O 1 ATOM 3256 C CB . ALA A 1 414 ? 8.915 29.094 24.344 1.00 24.51 ? 414 ALA A CB 1 ATOM 3257 N N . SER A 1 415 ? 9.521 32.127 23.047 1.00 24.96 ? 415 SER A N 1 ATOM 3258 C CA . SER A 1 415 ? 9.121 33.535 23.006 1.00 26.65 ? 415 SER A CA 1 ATOM 3259 C C . SER A 1 415 ? 9.189 34.140 21.611 1.00 26.47 ? 415 SER A C 1 ATOM 3260 O O . SER A 1 415 ? 9.046 35.343 21.441 1.00 26.08 ? 415 SER A O 1 ATOM 3261 C CB . SER A 1 415 ? 9.984 34.354 23.952 1.00 28.73 ? 415 SER A CB 1 ATOM 3262 O OG . SER A 1 415 ? 9.612 34.108 25.293 1.00 31.29 ? 415 SER A OG 1 ATOM 3263 N N . GLY A 1 416 ? 9.412 33.293 20.619 1.00 25.21 ? 416 GLY A N 1 ATOM 3264 C CA . GLY A 1 416 ? 9.559 33.737 19.233 1.00 25.51 ? 416 GLY A CA 1 ATOM 3265 C C . GLY A 1 416 ? 8.362 34.555 18.771 1.00 25.90 ? 416 GLY A C 1 ATOM 3266 O O . GLY A 1 416 ? 7.234 34.286 19.174 1.00 25.63 ? 416 GLY A O 1 ATOM 3267 N N . ASP A 1 417 ? 8.610 35.540 17.922 1.00 28.86 ? 417 ASP A N 1 ATOM 3268 C CA . ASP A 1 417 ? 7.526 36.366 17.385 1.00 29.46 ? 417 ASP A CA 1 ATOM 3269 C C . ASP A 1 417 ? 6.753 35.647 16.269 1.00 29.27 ? 417 ASP A C 1 ATOM 3270 O O . ASP A 1 417 ? 7.179 34.596 15.767 1.00 28.82 ? 417 ASP A O 1 ATOM 3271 C CB . ASP A 1 417 ? 8.062 37.718 16.885 1.00 31.58 ? 417 ASP A CB 1 ATOM 3272 C CG . ASP A 1 417 ? 9.234 37.563 15.923 1.00 34.02 ? 417 ASP A CG 1 ATOM 3273 O OD1 . ASP A 1 417 ? 9.977 36.552 16.015 1.00 35.10 ? 417 ASP A OD1 1 ATOM 3274 O OD2 . ASP A 1 417 ? 9.428 38.454 15.071 1.00 34.50 ? 417 ASP A OD2 1 ATOM 3275 N N . SER A 1 418 ? 5.609 36.209 15.884 1.00 27.43 ? 418 SER A N 1 ATOM 3276 C CA . SER A 1 418 ? 4.837 35.670 14.784 1.00 26.63 ? 418 SER A CA 1 ATOM 3277 C C . SER A 1 418 ? 5.128 36.504 13.537 1.00 26.75 ? 418 SER A C 1 ATOM 3278 O O . SER A 1 418 ? 4.871 37.702 13.522 1.00 27.00 ? 418 SER A O 1 ATOM 3279 C CB . SER A 1 418 ? 3.350 35.719 15.103 1.00 27.21 ? 418 SER A CB 1 ATOM 3280 O OG . SER A 1 418 ? 3.008 34.834 16.161 1.00 27.64 ? 418 SER A OG 1 ATOM 3281 N N . TYR A 1 419 ? 5.678 35.868 12.503 1.00 25.28 ? 419 TYR A N 1 ATOM 3282 C CA . TYR A 1 419 ? 6.044 36.559 11.279 1.00 24.86 ? 419 TYR A CA 1 ATOM 3283 C C . TYR A 1 419 ? 5.957 35.593 10.110 1.00 24.35 ? 419 TYR A C 1 ATOM 3284 O O . TYR A 1 419 ? 5.731 34.399 10.303 1.00 23.57 ? 419 TYR A O 1 ATOM 3285 C CB . TYR A 1 419 ? 7.453 37.152 11.375 1.00 25.47 ? 419 TYR A CB 1 ATOM 3286 C CG . TYR A 1 419 ? 8.566 36.118 11.365 1.00 26.06 ? 419 TYR A CG 1 ATOM 3287 C CD1 . TYR A 1 419 ? 8.964 35.499 12.530 1.00 25.32 ? 419 TYR A CD1 1 ATOM 3288 C CD2 . TYR A 1 419 ? 9.218 35.792 10.186 1.00 25.68 ? 419 TYR A CD2 1 ATOM 3289 C CE1 . TYR A 1 419 ? 9.991 34.545 12.537 1.00 25.56 ? 419 TYR A CE1 1 ATOM 3290 C CE2 . TYR A 1 419 ? 10.243 34.844 10.169 1.00 26.30 ? 419 TYR A CE2 1 ATOM 3291 C CZ . TYR A 1 419 ? 10.628 34.226 11.350 1.00 25.75 ? 419 TYR A CZ 1 ATOM 3292 O OH . TYR A 1 419 ? 11.652 33.267 11.346 1.00 26.70 ? 419 TYR A OH 1 ATOM 3293 N N . THR A 1 420 ? 6.108 36.116 8.894 1.00 24.35 ? 420 THR A N 1 ATOM 3294 C CA . THR A 1 420 ? 6.029 35.256 7.725 1.00 25.86 ? 420 THR A CA 1 ATOM 3295 C C . THR A 1 420 ? 7.400 35.109 7.121 1.00 25.88 ? 420 THR A C 1 ATOM 3296 O O . THR A 1 420 ? 8.022 36.113 6.779 1.00 25.26 ? 420 THR A O 1 ATOM 3297 C CB . THR A 1 420 ? 5.146 35.834 6.626 1.00 26.57 ? 420 THR A CB 1 ATOM 3298 O OG1 . THR A 1 420 ? 3.874 36.203 7.172 1.00 27.64 ? 420 THR A OG1 1 ATOM 3299 C CG2 . THR A 1 420 ? 4.963 34.788 5.544 1.00 27.34 ? 420 THR A CG2 1 ATOM 3300 N N . LEU A 1 421 ? 7.874 33.872 6.979 1.00 24.96 ? 421 LEU A N 1 ATOM 3301 C CA . LEU A 1 421 ? 9.156 33.653 6.333 1.00 25.50 ? 421 LEU A CA 1 ATOM 3302 C C . LEU A 1 421 ? 8.977 33.434 4.836 1.00 25.62 ? 421 LEU A C 1 ATOM 3303 O O . LEU A 1 421 ? 8.216 32.555 4.431 1.00 26.02 ? 421 LEU A O 1 ATOM 3304 C CB . LEU A 1 421 ? 9.857 32.436 6.952 1.00 25.88 ? 421 LEU A CB 1 ATOM 3305 C CG . LEU A 1 421 ? 11.081 31.948 6.169 1.00 25.63 ? 421 LEU A CG 1 ATOM 3306 C CD1 . LEU A 1 421 ? 12.221 32.941 6.350 1.00 27.16 ? 421 LEU A CD1 1 ATOM 3307 C CD2 . LEU A 1 421 ? 11.534 30.550 6.611 1.00 25.96 ? 421 LEU A CD2 1 ATOM 3308 N N . SER A 1 422 ? 9.651 34.247 4.017 1.00 25.42 ? 422 SER A N 1 ATOM 3309 C CA . SER A 1 422 ? 9.597 34.072 2.582 1.00 24.55 ? 422 SER A CA 1 ATOM 3310 C C . SER A 1 422 ? 10.661 33.043 2.172 1.00 24.99 ? 422 SER A C 1 ATOM 3311 O O . SER A 1 422 ? 11.833 33.386 1.984 1.00 26.35 ? 422 SER A O 1 ATOM 3312 C CB . SER A 1 422 ? 9.814 35.410 1.876 1.00 26.97 ? 422 SER A CB 1 ATOM 3313 O OG . SER A 1 422 ? 9.706 35.247 0.480 1.00 29.54 ? 422 SER A OG 1 ATOM 3314 N N . LEU A 1 423 ? 10.264 31.781 2.063 1.00 23.09 ? 423 LEU A N 1 ATOM 3315 C CA . LEU A 1 423 ? 11.245 30.706 1.899 1.00 24.34 ? 423 LEU A CA 1 ATOM 3316 C C . LEU A 1 423 ? 11.508 30.427 0.431 1.00 26.07 ? 423 LEU A C 1 ATOM 3317 O O . LEU A 1 423 ? 10.586 30.092 -0.319 1.00 24.95 ? 423 LEU A O 1 ATOM 3318 C CB . LEU A 1 423 ? 10.770 29.419 2.570 1.00 23.13 ? 423 LEU A CB 1 ATOM 3319 C CG . LEU A 1 423 ? 11.687 28.195 2.372 1.00 23.57 ? 423 LEU A CG 1 ATOM 3320 C CD1 . LEU A 1 423 ? 13.011 28.387 3.106 1.00 25.49 ? 423 LEU A CD1 1 ATOM 3321 C CD2 . LEU A 1 423 ? 11.023 26.899 2.815 1.00 22.73 ? 423 LEU A CD2 1 ATOM 3322 N N . SER A 1 424 ? 12.770 30.577 0.032 1.00 29.12 ? 424 SER A N 1 ATOM 3323 C CA . SER A 1 424 ? 13.204 30.256 -1.324 1.00 28.92 ? 424 SER A CA 1 ATOM 3324 C C . SER A 1 424 ? 14.005 28.964 -1.318 1.00 27.94 ? 424 SER A C 1 ATOM 3325 O O . SER A 1 424 ? 14.641 28.618 -0.321 1.00 29.08 ? 424 SER A O 1 ATOM 3326 C CB . SER A 1 424 ? 14.057 31.393 -1.911 1.00 31.32 ? 424 SER A CB 1 ATOM 3327 O OG . SER A 1 424 ? 15.383 31.302 -1.410 1.00 35.64 ? 424 SER A OG 1 ATOM 3328 N N . GLY A 1 425 ? 13.973 28.245 -2.438 1.00 26.96 ? 425 GLY A N 1 ATOM 3329 C CA . GLY A 1 425 ? 14.800 27.060 -2.612 1.00 26.77 ? 425 GLY A CA 1 ATOM 3330 C C . GLY A 1 425 ? 14.117 25.726 -2.377 1.00 25.13 ? 425 GLY A C 1 ATOM 3331 O O . GLY A 1 425 ? 14.751 24.689 -2.535 1.00 24.98 ? 425 GLY A O 1 ATOM 3332 N N . ALA A 1 426 ? 12.828 25.747 -2.016 1.00 25.96 ? 426 ALA A N 1 ATOM 3333 C CA . ALA A 1 426 ? 12.102 24.500 -1.618 1.00 24.72 ? 426 ALA A CA 1 ATOM 3334 C C . ALA A 1 426 ? 11.817 23.576 -2.813 1.00 25.44 ? 426 ALA A C 1 ATOM 3335 O O . ALA A 1 426 ? 11.694 22.355 -2.659 1.00 26.47 ? 426 ALA A O 1 ATOM 3336 C CB . ALA A 1 426 ? 10.787 24.835 -0.851 1.00 25.82 ? 426 ALA A CB 1 ATOM 3337 N N . GLY A 1 427 ? 11.716 24.158 -4.003 1.00 24.09 ? 427 GLY A N 1 ATOM 3338 C CA . GLY A 1 427 ? 11.633 23.364 -5.220 1.00 23.98 ? 427 GLY A CA 1 ATOM 3339 C C . GLY A 1 427 ? 10.278 22.773 -5.547 1.00 23.42 ? 427 GLY A C 1 ATOM 3340 O O . GLY A 1 427 ? 10.162 21.895 -6.394 1.00 23.73 ? 427 GLY A O 1 ATOM 3341 N N . TYR A 1 428 ? 9.247 23.253 -4.877 1.00 22.99 ? 428 TYR A N 1 ATOM 3342 C CA . TYR A 1 428 ? 7.873 22.900 -5.240 1.00 23.34 ? 428 TYR A CA 1 ATOM 3343 C C . TYR A 1 428 ? 7.406 23.686 -6.480 1.00 25.02 ? 428 TYR A C 1 ATOM 3344 O O . TYR A 1 428 ? 8.079 24.636 -6.922 1.00 26.19 ? 428 TYR A O 1 ATOM 3345 C CB . TYR A 1 428 ? 6.937 23.212 -4.075 1.00 23.14 ? 428 TYR A CB 1 ATOM 3346 C CG . TYR A 1 428 ? 7.181 22.400 -2.822 1.00 22.43 ? 428 TYR A CG 1 ATOM 3347 C CD1 . TYR A 1 428 ? 7.063 21.010 -2.817 1.00 22.79 ? 428 TYR A CD1 1 ATOM 3348 C CD2 . TYR A 1 428 ? 7.496 23.028 -1.622 1.00 22.97 ? 428 TYR A CD2 1 ATOM 3349 C CE1 . TYR A 1 428 ? 7.295 20.265 -1.653 1.00 23.56 ? 428 TYR A CE1 1 ATOM 3350 C CE2 . TYR A 1 428 ? 7.691 22.308 -0.467 1.00 22.83 ? 428 TYR A CE2 1 ATOM 3351 C CZ . TYR A 1 428 ? 7.583 20.935 -0.476 1.00 23.15 ? 428 TYR A CZ 1 ATOM 3352 O OH . TYR A 1 428 ? 7.788 20.233 0.700 1.00 23.48 ? 428 TYR A OH 1 ATOM 3353 N N . THR A 1 429 ? 6.249 23.316 -7.030 1.00 24.13 ? 429 THR A N 1 ATOM 3354 C CA . THR A 1 429 ? 5.735 23.996 -8.221 1.00 24.96 ? 429 THR A CA 1 ATOM 3355 C C . THR A 1 429 ? 4.783 25.124 -7.833 1.00 23.67 ? 429 THR A C 1 ATOM 3356 O O . THR A 1 429 ? 4.105 25.039 -6.801 1.00 24.18 ? 429 THR A O 1 ATOM 3357 C CB . THR A 1 429 ? 4.989 23.036 -9.165 1.00 26.40 ? 429 THR A CB 1 ATOM 3358 O OG1 . THR A 1 429 ? 3.789 22.568 -8.533 1.00 28.36 ? 429 THR A OG1 1 ATOM 3359 C CG2 . THR A 1 429 ? 5.874 21.850 -9.534 1.00 26.19 ? 429 THR A CG2 1 ATOM 3360 N N . ALA A 1 430 ? 4.739 26.179 -8.645 1.00 22.30 ? 430 ALA A N 1 ATOM 3361 C CA . ALA A 1 430 ? 3.891 27.324 -8.357 1.00 23.52 ? 430 ALA A CA 1 ATOM 3362 C C . ALA A 1 430 ? 2.454 26.872 -8.106 1.00 23.82 ? 430 ALA A C 1 ATOM 3363 O O . ALA A 1 430 ? 1.942 26.007 -8.810 1.00 24.26 ? 430 ALA A O 1 ATOM 3364 C CB . ALA A 1 430 ? 3.937 28.343 -9.519 1.00 23.20 ? 430 ALA A CB 1 ATOM 3365 N N . GLY A 1 431 ? 1.825 27.432 -7.079 1.00 25.21 ? 431 GLY A N 1 ATOM 3366 C CA . GLY A 1 431 ? 0.422 27.120 -6.780 1.00 25.57 ? 431 GLY A CA 1 ATOM 3367 C C . GLY A 1 431 ? 0.153 25.834 -6.011 1.00 26.13 ? 431 GLY A C 1 ATOM 3368 O O . GLY A 1 431 ? -0.981 25.583 -5.613 1.00 27.04 ? 431 GLY A O 1 ATOM 3369 N N . GLN A 1 432 ? 1.184 25.020 -5.790 1.00 27.00 ? 432 GLN A N 1 ATOM 3370 C CA . GLN A 1 432 ? 1.011 23.739 -5.096 1.00 26.76 ? 432 GLN A CA 1 ATOM 3371 C C . GLN A 1 432 ? 0.615 23.920 -3.626 1.00 27.27 ? 432 GLN A C 1 ATOM 3372 O O . GLN A 1 432 ? 1.200 24.746 -2.923 1.00 27.64 ? 432 GLN A O 1 ATOM 3373 C CB . GLN A 1 432 ? 2.304 22.914 -5.185 1.00 28.06 ? 432 GLN A CB 1 ATOM 3374 C CG . GLN A 1 432 ? 2.195 21.506 -4.617 1.00 29.72 ? 432 GLN A CG 1 ATOM 3375 C CD . GLN A 1 432 ? 3.304 20.591 -5.099 1.00 30.41 ? 432 GLN A CD 1 ATOM 3376 O OE1 . GLN A 1 432 ? 4.411 21.037 -5.430 1.00 32.07 ? 432 GLN A OE1 1 ATOM 3377 N NE2 . GLN A 1 432 ? 3.020 19.302 -5.133 1.00 31.15 ? 432 GLN A NE2 1 ATOM 3378 N N . GLN A 1 433 ? -0.374 23.151 -3.168 1.00 25.27 ? 433 GLN A N 1 ATOM 3379 C CA . GLN A 1 433 ? -0.749 23.200 -1.758 1.00 25.99 ? 433 GLN A CA 1 ATOM 3380 C C . GLN A 1 433 ? 0.127 22.294 -0.919 1.00 24.57 ? 433 GLN A C 1 ATOM 3381 O O . GLN A 1 433 ? 0.389 21.144 -1.282 1.00 24.04 ? 433 GLN A O 1 ATOM 3382 C CB . GLN A 1 433 ? -2.206 22.807 -1.547 1.00 27.58 ? 433 GLN A CB 1 ATOM 3383 C CG . GLN A 1 433 ? -2.655 22.903 -0.064 1.00 30.41 ? 433 GLN A CG 1 ATOM 3384 C CD . GLN A 1 433 ? -4.167 22.914 0.081 1.00 32.18 ? 433 GLN A CD 1 ATOM 3385 O OE1 . GLN A 1 433 ? -4.719 23.651 0.897 1.00 35.10 ? 433 GLN A OE1 1 ATOM 3386 N NE2 . GLN A 1 433 ? -4.846 22.129 -0.743 1.00 33.47 ? 433 GLN A NE2 1 ATOM 3387 N N . LEU A 1 434 ? 0.587 22.809 0.211 1.00 24.15 ? 434 LEU A N 1 ATOM 3388 C CA . LEU A 1 434 ? 1.386 21.993 1.108 1.00 24.18 ? 434 LEU A CA 1 ATOM 3389 C C . LEU A 1 434 ? 0.696 21.922 2.449 1.00 23.80 ? 434 LEU A C 1 ATOM 3390 O O . LEU A 1 434 ? -0.058 22.837 2.835 1.00 22.41 ? 434 LEU A O 1 ATOM 3391 C CB . LEU A 1 434 ? 2.774 22.592 1.289 1.00 25.31 ? 434 LEU A CB 1 ATOM 3392 C CG . LEU A 1 434 ? 3.508 23.067 0.035 1.00 25.24 ? 434 LEU A CG 1 ATOM 3393 C CD1 . LEU A 1 434 ? 4.734 23.873 0.455 1.00 25.10 ? 434 LEU A CD1 1 ATOM 3394 C CD2 . LEU A 1 434 ? 3.903 21.886 -0.844 1.00 24.63 ? 434 LEU A CD2 1 ATOM 3395 N N . THR A 1 435 ? 0.946 20.833 3.144 1.00 21.19 ? 435 THR A N 1 ATOM 3396 C CA . THR A 1 435 ? 0.491 20.685 4.514 1.00 22.02 ? 435 THR A CA 1 ATOM 3397 C C . THR A 1 435 ? 1.664 20.838 5.466 1.00 21.69 ? 435 THR A C 1 ATOM 3398 O O . THR A 1 435 ? 2.703 20.218 5.276 1.00 22.55 ? 435 THR A O 1 ATOM 3399 C CB . THR A 1 435 ? -0.135 19.308 4.719 1.00 22.43 ? 435 THR A CB 1 ATOM 3400 O OG1 . THR A 1 435 ? -1.283 19.214 3.869 1.00 22.95 ? 435 THR A OG1 1 ATOM 3401 C CG2 . THR A 1 435 ? -0.559 19.110 6.158 1.00 23.81 ? 435 THR A CG2 1 ATOM 3402 N N . GLU A 1 436 ? 1.487 21.673 6.488 1.00 20.80 ? 436 GLU A N 1 ATOM 3403 C CA . GLU A 1 436 ? 2.443 21.758 7.573 1.00 20.73 ? 436 GLU A CA 1 ATOM 3404 C C . GLU A 1 436 ? 2.034 20.674 8.576 1.00 21.06 ? 436 GLU A C 1 ATOM 3405 O O . GLU A 1 436 ? 1.009 20.784 9.252 1.00 21.70 ? 436 GLU A O 1 ATOM 3406 C CB . GLU A 1 436 ? 2.388 23.129 8.226 1.00 21.36 ? 436 GLU A CB 1 ATOM 3407 C CG . GLU A 1 436 ? 3.601 23.447 9.049 1.00 22.10 ? 436 GLU A CG 1 ATOM 3408 C CD . GLU A 1 436 ? 3.657 22.655 10.340 1.00 22.47 ? 436 GLU A CD 1 ATOM 3409 O OE1 . GLU A 1 436 ? 2.899 22.997 11.293 1.00 23.41 ? 436 GLU A OE1 1 ATOM 3410 O OE2 . GLU A 1 436 ? 4.479 21.712 10.391 1.00 21.96 ? 436 GLU A OE2 1 ATOM 3411 N N . VAL A 1 437 ? 2.795 19.602 8.620 1.00 20.20 ? 437 VAL A N 1 ATOM 3412 C CA . VAL A 1 437 ? 2.298 18.377 9.235 1.00 20.44 ? 437 VAL A CA 1 ATOM 3413 C C . VAL A 1 437 ? 2.488 18.307 10.747 1.00 23.52 ? 437 VAL A C 1 ATOM 3414 O O . VAL A 1 437 ? 2.050 17.331 11.367 1.00 24.99 ? 437 VAL A O 1 ATOM 3415 C CB . VAL A 1 437 ? 2.903 17.102 8.594 1.00 22.10 ? 437 VAL A CB 1 ATOM 3416 C CG1 . VAL A 1 437 ? 2.639 17.074 7.076 1.00 21.66 ? 437 VAL A CG1 1 ATOM 3417 C CG2 . VAL A 1 437 ? 4.401 16.952 8.959 1.00 20.95 ? 437 VAL A CG2 1 ATOM 3418 N N . ILE A 1 438 ? 3.182 19.281 11.343 1.00 22.77 ? 438 ILE A N 1 ATOM 3419 C CA . ILE A 1 438 ? 3.312 19.272 12.818 1.00 23.26 ? 438 ILE A CA 1 ATOM 3420 C C . ILE A 1 438 ? 2.060 19.895 13.466 1.00 23.58 ? 438 ILE A C 1 ATOM 3421 O O . ILE A 1 438 ? 1.510 19.365 14.454 1.00 23.67 ? 438 ILE A O 1 ATOM 3422 C CB . ILE A 1 438 ? 4.554 20.035 13.307 1.00 23.45 ? 438 ILE A CB 1 ATOM 3423 C CG1 . ILE A 1 438 ? 5.835 19.452 12.694 1.00 24.07 ? 438 ILE A CG1 1 ATOM 3424 C CG2 . ILE A 1 438 ? 4.666 19.918 14.836 1.00 24.49 ? 438 ILE A CG2 1 ATOM 3425 C CD1 . ILE A 1 438 ? 5.992 17.972 12.922 1.00 26.62 ? 438 ILE A CD1 1 ATOM 3426 N N . GLY A 1 439 ? 1.615 21.024 12.921 1.00 21.97 ? 439 GLY A N 1 ATOM 3427 C CA . GLY A 1 439 ? 0.468 21.775 13.489 1.00 22.40 ? 439 GLY A CA 1 ATOM 3428 C C . GLY A 1 439 ? -0.800 21.591 12.685 1.00 24.16 ? 439 GLY A C 1 ATOM 3429 O O . GLY A 1 439 ? -1.869 22.095 13.058 1.00 24.23 ? 439 GLY A O 1 ATOM 3430 N N . CYS A 1 440 ? -0.680 20.880 11.563 1.00 22.94 ? 440 CYS A N 1 ATOM 3431 C CA . CYS A 1 440 ? -1.789 20.591 10.647 1.00 25.21 ? 440 CYS A CA 1 ATOM 3432 C C . CYS A 1 440 ? -2.477 21.844 10.169 1.00 24.81 ? 440 CYS A C 1 ATOM 3433 O O . CYS A 1 440 ? -3.644 22.091 10.494 1.00 27.92 ? 440 CYS A O 1 ATOM 3434 C CB A CYS A 1 440 ? -2.743 19.554 11.229 0.65 26.23 ? 440 CYS A CB 1 ATOM 3435 C CB B CYS A 1 440 ? -2.854 19.728 11.341 0.35 26.00 ? 440 CYS A CB 1 ATOM 3436 S SG A CYS A 1 440 ? -1.879 17.967 11.464 0.65 27.92 ? 440 CYS A SG 1 ATOM 3437 S SG B CYS A 1 440 ? -2.252 18.380 12.385 0.35 28.90 ? 440 CYS A SG 1 ATOM 3438 N N . THR A 1 441 ? -1.744 22.660 9.419 1.00 23.71 ? 441 THR A N 1 ATOM 3439 C CA . THR A 1 441 ? -2.335 23.792 8.726 1.00 22.74 ? 441 THR A CA 1 ATOM 3440 C C . THR A 1 441 ? -1.878 23.669 7.293 1.00 24.13 ? 441 THR A C 1 ATOM 3441 O O . THR A 1 441 ? -1.104 22.747 6.972 1.00 23.44 ? 441 THR A O 1 ATOM 3442 C CB . THR A 1 441 ? -1.844 25.117 9.305 1.00 24.17 ? 441 THR A CB 1 ATOM 3443 O OG1 . THR A 1 441 ? -0.410 25.153 9.215 1.00 23.97 ? 441 THR A OG1 1 ATOM 3444 C CG2 . THR A 1 441 ? -2.301 25.250 10.806 1.00 25.16 ? 441 THR A CG2 1 ATOM 3445 N N . THR A 1 442 ? -2.337 24.564 6.427 1.00 23.90 ? 442 THR A N 1 ATOM 3446 C CA . THR A 1 442 ? -1.865 24.486 5.048 1.00 25.45 ? 442 THR A CA 1 ATOM 3447 C C . THR A 1 442 ? -1.232 25.768 4.523 1.00 26.24 ? 442 THR A C 1 ATOM 3448 O O . THR A 1 442 ? -1.553 26.866 4.982 1.00 24.51 ? 442 THR A O 1 ATOM 3449 C CB . THR A 1 442 ? -2.913 23.907 4.086 1.00 27.58 ? 442 THR A CB 1 ATOM 3450 O OG1 . THR A 1 442 ? -4.084 24.705 4.106 1.00 26.95 ? 442 THR A OG1 1 ATOM 3451 C CG2 . THR A 1 442 ? -3.264 22.488 4.485 1.00 28.62 ? 442 THR A CG2 1 ATOM 3452 N N . VAL A 1 443 ? -0.289 25.600 3.593 1.00 26.76 ? 443 VAL A N 1 ATOM 3453 C CA . VAL A 1 443 ? 0.350 26.729 2.936 1.00 29.49 ? 443 VAL A CA 1 ATOM 3454 C C . VAL A 1 443 ? 0.334 26.459 1.427 1.00 29.63 ? 443 VAL A C 1 ATOM 3455 O O . VAL A 1 443 ? 0.357 25.302 0.992 1.00 30.50 ? 443 VAL A O 1 ATOM 3456 C CB . VAL A 1 443 ? 1.813 26.951 3.431 1.00 30.86 ? 443 VAL A CB 1 ATOM 3457 C CG1 . VAL A 1 443 ? 1.944 26.676 4.946 1.00 31.55 ? 443 VAL A CG1 1 ATOM 3458 C CG2 . VAL A 1 443 ? 2.755 26.071 2.706 1.00 30.93 ? 443 VAL A CG2 1 ATOM 3459 N N . THR A 1 444 ? 0.326 27.521 0.639 1.00 28.98 ? 444 THR A N 1 ATOM 3460 C CA . THR A 1 444 ? 0.344 27.376 -0.809 1.00 28.16 ? 444 THR A CA 1 ATOM 3461 C C . THR A 1 444 ? 1.598 28.040 -1.379 1.00 28.62 ? 444 THR A C 1 ATOM 3462 O O . THR A 1 444 ? 1.934 29.157 -1.002 1.00 28.26 ? 444 THR A O 1 ATOM 3463 C CB . THR A 1 444 ? -0.930 27.995 -1.424 1.00 29.91 ? 444 THR A CB 1 ATOM 3464 O OG1 . THR A 1 444 ? -2.087 27.421 -0.790 1.00 29.92 ? 444 THR A OG1 1 ATOM 3465 C CG2 . THR A 1 444 ? -0.991 27.760 -2.942 1.00 29.20 ? 444 THR A CG2 1 ATOM 3466 N N . VAL A 1 445 ? 2.276 27.342 -2.293 1.00 28.97 ? 445 VAL A N 1 ATOM 3467 C CA . VAL A 1 445 ? 3.483 27.849 -2.950 1.00 28.47 ? 445 VAL A CA 1 ATOM 3468 C C . VAL A 1 445 ? 3.082 28.995 -3.875 1.00 29.79 ? 445 VAL A C 1 ATOM 3469 O O . VAL A 1 445 ? 2.048 28.928 -4.545 1.00 31.36 ? 445 VAL A O 1 ATOM 3470 C CB . VAL A 1 445 ? 4.195 26.705 -3.702 1.00 28.19 ? 445 VAL A CB 1 ATOM 3471 C CG1 . VAL A 1 445 ? 5.440 27.203 -4.459 1.00 27.47 ? 445 VAL A CG1 1 ATOM 3472 C CG2 . VAL A 1 445 ? 4.567 25.599 -2.706 1.00 28.75 ? 445 VAL A CG2 1 ATOM 3473 N N . GLY A 1 446 ? 3.865 30.071 -3.870 1.00 30.05 ? 446 GLY A N 1 ATOM 3474 C CA . GLY A 1 446 ? 3.604 31.225 -4.739 1.00 31.37 ? 446 GLY A CA 1 ATOM 3475 C C . GLY A 1 446 ? 3.983 30.971 -6.185 1.00 31.67 ? 446 GLY A C 1 ATOM 3476 O O . GLY A 1 446 ? 4.688 30.003 -6.504 1.00 31.99 ? 446 GLY A O 1 ATOM 3477 N N . SER A 1 447 ? 3.518 31.859 -7.057 1.00 33.43 ? 447 SER A N 1 ATOM 3478 C CA . SER A 1 447 ? 3.767 31.745 -8.488 1.00 34.32 ? 447 SER A CA 1 ATOM 3479 C C . SER A 1 447 ? 5.233 31.962 -8.823 1.00 34.67 ? 447 SER A C 1 ATOM 3480 O O . SER A 1 447 ? 5.666 31.710 -9.947 1.00 36.72 ? 447 SER A O 1 ATOM 3481 C CB . SER A 1 447 ? 2.926 32.763 -9.236 1.00 34.61 ? 447 SER A CB 1 ATOM 3482 O OG . SER A 1 447 ? 2.905 33.981 -8.516 1.00 35.26 ? 447 SER A OG 1 ATOM 3483 N N . ASP A 1 448 ? 5.997 32.448 -7.856 1.00 33.71 ? 448 ASP A N 1 ATOM 3484 C CA . ASP A 1 448 ? 7.417 32.633 -8.054 1.00 33.17 ? 448 ASP A CA 1 ATOM 3485 C C . ASP A 1 448 ? 8.223 31.519 -7.380 1.00 32.72 ? 448 ASP A C 1 ATOM 3486 O O . ASP A 1 448 ? 9.438 31.611 -7.262 1.00 32.05 ? 448 ASP A O 1 ATOM 3487 C CB . ASP A 1 448 ? 7.866 34.018 -7.579 1.00 34.14 ? 448 ASP A CB 1 ATOM 3488 C CG . ASP A 1 448 ? 7.605 34.260 -6.097 1.00 36.67 ? 448 ASP A CG 1 ATOM 3489 O OD1 . ASP A 1 448 ? 7.036 33.380 -5.382 1.00 36.06 ? 448 ASP A OD1 1 ATOM 3490 O OD2 . ASP A 1 448 ? 7.989 35.359 -5.641 1.00 37.76 ? 448 ASP A OD2 1 ATOM 3491 N N . GLY A 1 449 ? 7.531 30.463 -6.957 1.00 32.07 ? 449 GLY A N 1 ATOM 3492 C CA . GLY A 1 449 ? 8.180 29.341 -6.290 1.00 30.64 ? 449 GLY A CA 1 ATOM 3493 C C . GLY A 1 449 ? 8.385 29.523 -4.792 1.00 30.69 ? 449 GLY A C 1 ATOM 3494 O O . GLY A 1 449 ? 8.608 28.556 -4.071 1.00 31.36 ? 449 GLY A O 1 ATOM 3495 N N . ASN A 1 450 ? 8.322 30.762 -4.322 1.00 29.91 ? 450 ASN A N 1 ATOM 3496 C CA . ASN A 1 450 ? 8.526 31.054 -2.915 1.00 29.97 ? 450 ASN A CA 1 ATOM 3497 C C . ASN A 1 450 ? 7.441 30.401 -2.062 1.00 28.30 ? 450 ASN A C 1 ATOM 3498 O O . ASN A 1 450 ? 6.296 30.309 -2.481 1.00 26.50 ? 450 ASN A O 1 ATOM 3499 C CB . ASN A 1 450 ? 8.492 32.563 -2.700 1.00 32.63 ? 450 ASN A CB 1 ATOM 3500 C CG . ASN A 1 450 ? 9.617 33.041 -1.810 1.00 35.08 ? 450 ASN A CG 1 ATOM 3501 O OD1 . ASN A 1 450 ? 10.799 33.095 -2.228 1.00 36.03 ? 450 ASN A OD1 1 ATOM 3502 N ND2 . ASN A 1 450 ? 9.266 33.404 -0.573 1.00 34.60 ? 450 ASN A ND2 1 ATOM 3503 N N . VAL A 1 451 ? 7.806 29.947 -0.864 1.00 26.46 ? 451 VAL A N 1 ATOM 3504 C CA . VAL A 1 451 ? 6.819 29.412 0.064 1.00 27.10 ? 451 VAL A CA 1 ATOM 3505 C C . VAL A 1 451 ? 6.667 30.383 1.238 1.00 26.26 ? 451 VAL A C 1 ATOM 3506 O O . VAL A 1 451 ? 7.617 30.621 1.966 1.00 25.32 ? 451 VAL A O 1 ATOM 3507 C CB . VAL A 1 451 ? 7.248 28.014 0.584 1.00 27.88 ? 451 VAL A CB 1 ATOM 3508 C CG1 . VAL A 1 451 ? 6.130 27.390 1.442 1.00 30.54 ? 451 VAL A CG1 1 ATOM 3509 C CG2 . VAL A 1 451 ? 7.589 27.099 -0.575 1.00 28.55 ? 451 VAL A CG2 1 ATOM 3510 N N . PRO A 1 452 ? 5.472 30.984 1.404 1.00 25.22 ? 452 PRO A N 1 ATOM 3511 C CA . PRO A 1 452 ? 5.276 31.799 2.599 1.00 26.08 ? 452 PRO A CA 1 ATOM 3512 C C . PRO A 1 452 ? 4.995 30.886 3.800 1.00 27.68 ? 452 PRO A C 1 ATOM 3513 O O . PRO A 1 452 ? 3.920 30.264 3.888 1.00 29.43 ? 452 PRO A O 1 ATOM 3514 C CB . PRO A 1 452 ? 4.047 32.645 2.257 1.00 25.78 ? 452 PRO A CB 1 ATOM 3515 C CG . PRO A 1 452 ? 3.284 31.805 1.285 1.00 26.72 ? 452 PRO A CG 1 ATOM 3516 C CD . PRO A 1 452 ? 4.290 30.957 0.530 1.00 26.58 ? 452 PRO A CD 1 ATOM 3517 N N . VAL A 1 453 ? 5.947 30.798 4.715 1.00 26.82 ? 453 VAL A N 1 ATOM 3518 C CA . VAL A 1 453 ? 5.769 29.916 5.873 1.00 27.28 ? 453 VAL A CA 1 ATOM 3519 C C . VAL A 1 453 ? 5.414 30.710 7.134 1.00 27.20 ? 453 VAL A C 1 ATOM 3520 O O . VAL A 1 453 ? 6.216 31.545 7.564 1.00 27.04 ? 453 VAL A O 1 ATOM 3521 C CB . VAL A 1 453 ? 7.037 29.156 6.153 1.00 26.03 ? 453 VAL A CB 1 ATOM 3522 C CG1 . VAL A 1 453 ? 6.775 28.126 7.268 1.00 26.57 ? 453 VAL A CG1 1 ATOM 3523 C CG2 . VAL A 1 453 ? 7.558 28.503 4.861 1.00 27.99 ? 453 VAL A CG2 1 ATOM 3524 N N . PRO A 1 454 ? 4.197 30.515 7.668 1.00 28.35 ? 454 PRO A N 1 ATOM 3525 C CA . PRO A 1 454 ? 3.852 31.244 8.894 1.00 27.92 ? 454 PRO A CA 1 ATOM 3526 C C . PRO A 1 454 ? 4.685 30.731 10.047 1.00 27.77 ? 454 PRO A C 1 ATOM 3527 O O . PRO A 1 454 ? 4.619 29.538 10.358 1.00 28.23 ? 454 PRO A O 1 ATOM 3528 C CB . PRO A 1 454 ? 2.374 30.878 9.115 1.00 29.42 ? 454 PRO A CB 1 ATOM 3529 C CG . PRO A 1 454 ? 1.852 30.543 7.730 1.00 30.15 ? 454 PRO A CG 1 ATOM 3530 C CD . PRO A 1 454 ? 3.037 29.744 7.179 1.00 29.48 ? 454 PRO A CD 1 ATOM 3531 N N . MET A 1 455 ? 5.481 31.614 10.642 1.00 25.82 ? 455 MET A N 1 ATOM 3532 C CA . MET A 1 455 ? 6.321 31.266 11.778 1.00 25.49 ? 455 MET A CA 1 ATOM 3533 C C . MET A 1 455 ? 5.700 31.790 13.079 1.00 26.12 ? 455 MET A C 1 ATOM 3534 O O . MET A 1 455 ? 5.126 32.879 13.081 1.00 25.64 ? 455 MET A O 1 ATOM 3535 C CB . MET A 1 455 ? 7.702 31.872 11.578 1.00 25.94 ? 455 MET A CB 1 ATOM 3536 C CG . MET A 1 455 ? 8.373 31.421 10.269 1.00 25.37 ? 455 MET A CG 1 ATOM 3537 S SD . MET A 1 455 ? 9.035 29.717 10.362 1.00 26.57 ? 455 MET A SD 1 ATOM 3538 C CE . MET A 1 455 ? 10.605 30.029 11.090 1.00 27.68 ? 455 MET A CE 1 ATOM 3539 N N . ALA A 1 456 ? 5.806 31.023 14.164 1.00 24.98 ? 456 ALA A N 1 ATOM 3540 C CA . ALA A 1 456 ? 5.269 31.443 15.475 1.00 25.95 ? 456 ALA A CA 1 ATOM 3541 C C . ALA A 1 456 ? 5.786 30.567 16.615 1.00 24.31 ? 456 ALA A C 1 ATOM 3542 O O . ALA A 1 456 ? 5.986 29.362 16.432 1.00 26.05 ? 456 ALA A O 1 ATOM 3543 C CB . ALA A 1 456 ? 3.731 31.452 15.468 1.00 25.27 ? 456 ALA A CB 1 ATOM 3544 N N . GLY A 1 457 ? 5.974 31.180 17.788 1.00 22.85 ? 457 GLY A N 1 ATOM 3545 C CA . GLY A 1 457 ? 6.295 30.439 19.017 1.00 22.08 ? 457 GLY A CA 1 ATOM 3546 C C . GLY A 1 457 ? 7.586 29.621 18.897 1.00 21.76 ? 457 GLY A C 1 ATOM 3547 O O . GLY A 1 457 ? 7.786 28.622 19.606 1.00 23.46 ? 457 GLY A O 1 ATOM 3548 N N . GLY A 1 458 ? 8.453 30.047 17.979 1.00 21.91 ? 458 GLY A N 1 ATOM 3549 C CA . GLY A 1 458 ? 9.729 29.355 17.746 1.00 20.89 ? 458 GLY A CA 1 ATOM 3550 C C . GLY A 1 458 ? 9.560 27.926 17.267 1.00 21.79 ? 458 GLY A C 1 ATOM 3551 O O . GLY A 1 458 ? 10.495 27.110 17.348 1.00 21.44 ? 458 GLY A O 1 ATOM 3552 N N . LEU A 1 459 ? 8.372 27.605 16.766 1.00 21.78 ? 459 LEU A N 1 ATOM 3553 C CA . LEU A 1 459 ? 8.001 26.216 16.453 1.00 23.19 ? 459 LEU A CA 1 ATOM 3554 C C . LEU A 1 459 ? 8.589 25.700 15.118 1.00 21.33 ? 459 LEU A C 1 ATOM 3555 O O . LEU A 1 459 ? 8.695 26.460 14.160 1.00 22.36 ? 459 LEU A O 1 ATOM 3556 C CB . LEU A 1 459 ? 6.470 26.123 16.360 1.00 24.02 ? 459 LEU A CB 1 ATOM 3557 C CG . LEU A 1 459 ? 5.607 25.600 17.534 1.00 26.58 ? 459 LEU A CG 1 ATOM 3558 C CD1 . LEU A 1 459 ? 6.304 25.401 18.888 1.00 26.91 ? 459 LEU A CD1 1 ATOM 3559 C CD2 . LEU A 1 459 ? 4.209 26.137 17.635 1.00 26.03 ? 459 LEU A CD2 1 ATOM 3560 N N . PRO A 1 460 ? 8.978 24.412 15.062 1.00 21.47 ? 460 PRO A N 1 ATOM 3561 C CA . PRO A 1 460 ? 9.429 23.854 13.774 1.00 20.69 ? 460 PRO A CA 1 ATOM 3562 C C . PRO A 1 460 ? 8.243 23.665 12.824 1.00 23.05 ? 460 PRO A C 1 ATOM 3563 O O . PRO A 1 460 ? 7.096 23.523 13.263 1.00 24.11 ? 460 PRO A O 1 ATOM 3564 C CB . PRO A 1 460 ? 10.036 22.489 14.162 1.00 20.71 ? 460 PRO A CB 1 ATOM 3565 C CG . PRO A 1 460 ? 9.216 22.066 15.367 1.00 22.40 ? 460 PRO A CG 1 ATOM 3566 C CD . PRO A 1 460 ? 8.947 23.385 16.129 1.00 22.56 ? 460 PRO A CD 1 ATOM 3567 N N . ARG A 1 461 ? 8.507 23.743 11.525 1.00 21.12 ? 461 ARG A N 1 ATOM 3568 C CA . ARG A 1 461 ? 7.483 23.601 10.489 1.00 22.80 ? 461 ARG A CA 1 ATOM 3569 C C . ARG A 1 461 ? 7.977 22.491 9.559 1.00 23.55 ? 461 ARG A C 1 ATOM 3570 O O . ARG A 1 461 ? 9.160 22.458 9.214 1.00 22.50 ? 461 ARG A O 1 ATOM 3571 C CB . ARG A 1 461 ? 7.346 24.909 9.705 1.00 23.18 ? 461 ARG A CB 1 ATOM 3572 C CG . ARG A 1 461 ? 7.009 26.143 10.572 1.00 24.20 ? 461 ARG A CG 1 ATOM 3573 C CD . ARG A 1 461 ? 5.781 25.913 11.394 1.00 26.59 ? 461 ARG A CD 1 ATOM 3574 N NE . ARG A 1 461 ? 5.188 27.161 11.893 1.00 27.21 ? 461 ARG A NE 1 ATOM 3575 C CZ . ARG A 1 461 ? 4.303 27.221 12.883 1.00 29.92 ? 461 ARG A CZ 1 ATOM 3576 N NH1 . ARG A 1 461 ? 3.931 26.113 13.517 1.00 31.19 ? 461 ARG A NH1 1 ATOM 3577 N NH2 . ARG A 1 461 ? 3.796 28.386 13.266 1.00 30.60 ? 461 ARG A NH2 1 ATOM 3578 N N . VAL A 1 462 ? 7.096 21.561 9.196 1.00 21.48 ? 462 VAL A N 1 ATOM 3579 C CA . VAL A 1 462 ? 7.488 20.488 8.295 1.00 22.29 ? 462 VAL A CA 1 ATOM 3580 C C . VAL A 1 462 ? 6.451 20.372 7.192 1.00 21.72 ? 462 VAL A C 1 ATOM 3581 O O . VAL A 1 462 ? 5.271 20.033 7.460 1.00 21.64 ? 462 VAL A O 1 ATOM 3582 C CB . VAL A 1 462 ? 7.589 19.151 9.045 1.00 21.99 ? 462 VAL A CB 1 ATOM 3583 C CG1 . VAL A 1 462 ? 8.020 18.026 8.089 1.00 22.64 ? 462 VAL A CG1 1 ATOM 3584 C CG2 . VAL A 1 462 ? 8.629 19.268 10.181 1.00 22.33 ? 462 VAL A CG2 1 ATOM 3585 N N . LEU A 1 463 ? 6.878 20.698 5.961 1.00 20.71 ? 463 LEU A N 1 ATOM 3586 C CA . LEU A 1 463 ? 5.976 20.786 4.811 1.00 22.09 ? 463 LEU A CA 1 ATOM 3587 C C . LEU A 1 463 ? 6.030 19.577 3.895 1.00 21.09 ? 463 LEU A C 1 ATOM 3588 O O . LEU A 1 463 ? 7.092 18.979 3.680 1.00 20.51 ? 463 LEU A O 1 ATOM 3589 C CB . LEU A 1 463 ? 6.304 22.024 3.969 1.00 23.13 ? 463 LEU A CB 1 ATOM 3590 C CG . LEU A 1 463 ? 6.389 23.342 4.712 1.00 23.57 ? 463 LEU A CG 1 ATOM 3591 C CD1 . LEU A 1 463 ? 6.997 24.380 3.740 1.00 23.78 ? 463 LEU A CD1 1 ATOM 3592 C CD2 . LEU A 1 463 ? 5.011 23.778 5.205 1.00 24.20 ? 463 LEU A CD2 1 ATOM 3593 N N . TYR A 1 464 ? 4.878 19.244 3.333 1.00 21.03 ? 464 TYR A N 1 ATOM 3594 C CA . TYR A 1 464 ? 4.765 18.103 2.428 1.00 23.33 ? 464 TYR A CA 1 ATOM 3595 C C . TYR A 1 464 ? 3.548 18.376 1.563 1.00 22.80 ? 464 TYR A C 1 ATOM 3596 O O . TYR A 1 464 ? 2.582 18.978 2.029 1.00 22.57 ? 464 TYR A O 1 ATOM 3597 C CB . TYR A 1 464 ? 4.577 16.832 3.267 1.00 24.49 ? 464 TYR A CB 1 ATOM 3598 C CG . TYR A 1 464 ? 4.598 15.513 2.512 1.00 24.56 ? 464 TYR A CG 1 ATOM 3599 C CD1 . TYR A 1 464 ? 5.795 14.939 2.088 1.00 24.06 ? 464 TYR A CD1 1 ATOM 3600 C CD2 . TYR A 1 464 ? 3.412 14.818 2.255 1.00 25.35 ? 464 TYR A CD2 1 ATOM 3601 C CE1 . TYR A 1 464 ? 5.809 13.725 1.420 1.00 24.97 ? 464 TYR A CE1 1 ATOM 3602 C CE2 . TYR A 1 464 ? 3.423 13.597 1.579 1.00 25.69 ? 464 TYR A CE2 1 ATOM 3603 C CZ . TYR A 1 464 ? 4.633 13.051 1.179 1.00 24.92 ? 464 TYR A CZ 1 ATOM 3604 O OH . TYR A 1 464 ? 4.676 11.848 0.517 1.00 25.27 ? 464 TYR A OH 1 ATOM 3605 N N . PRO A 1 465 ? 3.600 18.018 0.272 1.00 21.91 ? 465 PRO A N 1 ATOM 3606 C CA . PRO A 1 465 ? 2.429 18.298 -0.576 1.00 22.20 ? 465 PRO A CA 1 ATOM 3607 C C . PRO A 1 465 ? 1.121 17.643 -0.114 1.00 21.28 ? 465 PRO A C 1 ATOM 3608 O O . PRO A 1 465 ? 1.056 16.435 0.089 1.00 21.53 ? 465 PRO A O 1 ATOM 3609 C CB . PRO A 1 465 ? 2.824 17.725 -1.933 1.00 22.93 ? 465 PRO A CB 1 ATOM 3610 C CG . PRO A 1 465 ? 4.335 17.715 -1.924 1.00 21.77 ? 465 PRO A CG 1 ATOM 3611 C CD . PRO A 1 465 ? 4.727 17.425 -0.476 1.00 21.92 ? 465 PRO A CD 1 ATOM 3612 N N . THR A 1 466 ? 0.084 18.449 0.026 1.00 24.88 ? 466 THR A N 1 ATOM 3613 C CA . THR A 1 466 ? -1.208 17.966 0.519 1.00 25.30 ? 466 THR A CA 1 ATOM 3614 C C . THR A 1 466 ? -1.796 16.805 -0.300 1.00 25.93 ? 466 THR A C 1 ATOM 3615 O O . THR A 1 466 ? -2.279 15.828 0.267 1.00 23.94 ? 466 THR A O 1 ATOM 3616 C CB . THR A 1 466 ? -2.190 19.133 0.591 1.00 26.33 ? 466 THR A CB 1 ATOM 3617 O OG1 . THR A 1 466 ? -1.565 20.200 1.313 1.00 25.17 ? 466 THR A OG1 1 ATOM 3618 C CG2 . THR A 1 466 ? -3.500 18.721 1.291 1.00 25.83 ? 466 THR A CG2 1 ATOM 3619 N N . GLU A 1 467 ? -1.732 16.881 -1.627 1.00 26.90 ? 467 GLU A N 1 ATOM 3620 C CA . GLU A 1 467 ? -2.336 15.837 -2.440 1.00 29.15 ? 467 GLU A CA 1 ATOM 3621 C C . GLU A 1 467 ? -1.708 14.469 -2.152 1.00 28.77 ? 467 GLU A C 1 ATOM 3622 O O . GLU A 1 467 ? -2.370 13.435 -2.257 1.00 29.25 ? 467 GLU A O 1 ATOM 3623 C CB . GLU A 1 467 ? -2.222 16.185 -3.929 1.00 31.80 ? 467 GLU A CB 1 ATOM 3624 C CG . GLU A 1 467 ? -0.799 16.150 -4.458 1.00 35.98 ? 467 GLU A CG 1 ATOM 3625 C CD . GLU A 1 467 ? -0.367 17.468 -5.078 1.00 37.61 ? 467 GLU A CD 1 ATOM 3626 O OE1 . GLU A 1 467 ? -1.256 18.237 -5.526 1.00 39.91 ? 467 GLU A OE1 1 ATOM 3627 O OE2 . GLU A 1 467 ? 0.861 17.735 -5.105 1.00 38.42 ? 467 GLU A OE2 1 ATOM 3628 N N . LYS A 1 468 ? -0.434 14.464 -1.782 1.00 27.43 ? 468 LYS A N 1 ATOM 3629 C CA . LYS A 1 468 ? 0.263 13.212 -1.539 1.00 26.97 ? 468 LYS A CA 1 ATOM 3630 C C . LYS A 1 468 ? -0.167 12.550 -0.228 1.00 27.57 ? 468 LYS A C 1 ATOM 3631 O O . LYS A 1 468 ? 0.136 11.382 0.009 1.00 26.55 ? 468 LYS A O 1 ATOM 3632 C CB . LYS A 1 468 ? 1.776 13.441 -1.512 1.00 28.64 ? 468 LYS A CB 1 ATOM 3633 C CG . LYS A 1 468 ? 2.372 13.901 -2.825 1.00 29.66 ? 468 LYS A CG 1 ATOM 3634 C CD . LYS A 1 468 ? 2.427 12.770 -3.806 1.00 31.79 ? 468 LYS A CD 1 ATOM 3635 C CE . LYS A 1 468 ? 3.465 13.042 -4.852 1.00 32.39 ? 468 LYS A CE 1 ATOM 3636 N NZ . LYS A 1 468 ? 3.223 12.170 -6.009 1.00 33.93 ? 468 LYS A NZ 1 ATOM 3637 N N . LEU A 1 469 ? -0.860 13.294 0.631 1.00 27.29 ? 469 LEU A N 1 ATOM 3638 C CA . LEU A 1 469 ? -1.299 12.739 1.917 1.00 28.40 ? 469 LEU A CA 1 ATOM 3639 C C . LEU A 1 469 ? -2.643 12.019 1.815 1.00 29.82 ? 469 LEU A C 1 ATOM 3640 O O . LEU A 1 469 ? -3.145 11.477 2.798 1.00 30.21 ? 469 LEU A O 1 ATOM 3641 C CB . LEU A 1 469 ? -1.402 13.834 2.980 1.00 27.48 ? 469 LEU A CB 1 ATOM 3642 C CG . LEU A 1 469 ? -0.092 14.412 3.513 1.00 27.93 ? 469 LEU A CG 1 ATOM 3643 C CD1 . LEU A 1 469 ? -0.373 15.640 4.376 1.00 28.14 ? 469 LEU A CD1 1 ATOM 3644 C CD2 . LEU A 1 469 ? 0.692 13.370 4.297 1.00 27.96 ? 469 LEU A CD2 1 ATOM 3645 N N . ALA A 1 470 ? -3.246 12.038 0.633 1.00 31.43 ? 470 ALA A N 1 ATOM 3646 C CA . ALA A 1 470 ? -4.560 11.428 0.472 1.00 33.72 ? 470 ALA A CA 1 ATOM 3647 C C . ALA A 1 470 ? -4.584 10.014 1.041 1.00 34.29 ? 470 ALA A C 1 ATOM 3648 O O . ALA A 1 470 ? -3.710 9.196 0.742 1.00 36.30 ? 470 ALA A O 1 ATOM 3649 C CB . ALA A 1 470 ? -4.972 11.421 -0.984 1.00 32.84 ? 470 ALA A CB 1 ATOM 3650 N N . GLY A 1 471 ? -5.582 9.737 1.871 1.00 35.71 ? 471 GLY A N 1 ATOM 3651 C CA . GLY A 1 471 ? -5.749 8.405 2.444 1.00 36.60 ? 471 GLY A CA 1 ATOM 3652 C C . GLY A 1 471 ? -4.906 8.090 3.666 1.00 37.46 ? 471 GLY A C 1 ATOM 3653 O O . GLY A 1 471 ? -5.006 7.001 4.221 1.00 38.56 ? 471 GLY A O 1 ATOM 3654 N N . SER A 1 472 ? -4.060 9.018 4.099 1.00 37.22 ? 472 SER A N 1 ATOM 3655 C CA . SER A 1 472 ? -3.240 8.751 5.284 1.00 35.96 ? 472 SER A CA 1 ATOM 3656 C C . SER A 1 472 ? -3.913 9.239 6.559 1.00 35.24 ? 472 SER A C 1 ATOM 3657 O O . SER A 1 472 ? -4.931 9.928 6.508 1.00 35.85 ? 472 SER A O 1 ATOM 3658 C CB . SER A 1 472 ? -1.876 9.416 5.165 1.00 36.63 ? 472 SER A CB 1 ATOM 3659 O OG . SER A 1 472 ? -1.964 10.789 5.497 1.00 37.41 ? 472 SER A OG 1 ATOM 3660 N N . LYS A 1 473 ? -3.320 8.905 7.702 1.00 34.62 ? 473 LYS A N 1 ATOM 3661 C CA . LYS A 1 473 ? -3.799 9.414 8.990 1.00 34.78 ? 473 LYS A CA 1 ATOM 3662 C C . LYS A 1 473 ? -3.198 10.763 9.372 1.00 34.25 ? 473 LYS A C 1 ATOM 3663 O O . LYS A 1 473 ? -3.565 11.332 10.399 1.00 36.76 ? 473 LYS A O 1 ATOM 3664 C CB . LYS A 1 473 ? -3.494 8.438 10.116 1.00 36.05 ? 473 LYS A CB 1 ATOM 3665 C CG . LYS A 1 473 ? -3.986 7.035 9.901 1.00 37.83 ? 473 LYS A CG 1 ATOM 3666 C CD . LYS A 1 473 ? -3.364 6.109 10.945 1.00 39.51 ? 473 LYS A CD 1 ATOM 3667 C CE . LYS A 1 473 ? -3.246 4.690 10.410 1.00 40.49 ? 473 LYS A CE 1 ATOM 3668 N NZ . LYS A 1 473 ? -2.669 3.789 11.433 1.00 42.35 ? 473 LYS A NZ 1 ATOM 3669 N N . ILE A 1 474 ? -2.287 11.282 8.564 1.00 31.62 ? 474 ILE A N 1 ATOM 3670 C CA . ILE A 1 474 ? -1.601 12.521 8.911 1.00 30.47 ? 474 ILE A CA 1 ATOM 3671 C C . ILE A 1 474 ? -2.510 13.745 8.687 1.00 30.12 ? 474 ILE A C 1 ATOM 3672 O O . ILE A 1 474 ? -2.992 13.981 7.583 1.00 28.43 ? 474 ILE A O 1 ATOM 3673 C CB . ILE A 1 474 ? -0.292 12.626 8.130 1.00 30.54 ? 474 ILE A CB 1 ATOM 3674 C CG1 . ILE A 1 474 ? 0.661 11.509 8.591 1.00 31.39 ? 474 ILE A CG1 1 ATOM 3675 C CG2 . ILE A 1 474 ? 0.334 14.029 8.255 1.00 29.84 ? 474 ILE A CG2 1 ATOM 3676 C CD1 . ILE A 1 474 ? 1.813 11.256 7.655 1.00 30.25 ? 474 ILE A CD1 1 ATOM 3677 N N . CYS A 1 475 ? -2.747 14.502 9.752 1.00 29.72 ? 475 CYS A N 1 ATOM 3678 C CA . CYS A 1 475 ? -3.588 15.698 9.673 1.00 29.38 ? 475 CYS A CA 1 ATOM 3679 C C . CYS A 1 475 ? -4.952 15.405 9.067 1.00 31.40 ? 475 CYS A C 1 ATOM 3680 O O . CYS A 1 475 ? -5.464 16.177 8.250 1.00 29.97 ? 475 CYS A O 1 ATOM 3681 C CB . CYS A 1 475 ? -2.910 16.785 8.844 1.00 29.10 ? 475 CYS A CB 1 ATOM 3682 S SG . CYS A 1 475 ? -1.357 17.349 9.582 1.00 28.62 ? 475 CYS A SG 1 ATOM 3683 N N . SER A 1 476 ? -5.557 14.296 9.468 1.00 32.97 ? 476 SER A N 1 ATOM 3684 C CA . SER A 1 476 ? -6.789 13.875 8.808 1.00 34.02 ? 476 SER A CA 1 ATOM 3685 C C . SER A 1 476 ? -8.027 14.495 9.448 1.00 35.67 ? 476 SER A C 1 ATOM 3686 O O . SER A 1 476 ? -9.102 14.512 8.834 1.00 36.46 ? 476 SER A O 1 ATOM 3687 C CB . SER A 1 476 ? -6.890 12.352 8.813 1.00 35.14 ? 476 SER A CB 1 ATOM 3688 O OG . SER A 1 476 ? -6.766 11.886 10.142 1.00 35.99 ? 476 SER A OG 1 HETATM 3689 C C1 . NAG B 2 . ? 24.395 -19.762 20.632 1.00 28.18 ? 1000 NAG A C1 1 HETATM 3690 C C2 . NAG B 2 . ? 25.644 -19.489 21.465 1.00 28.55 ? 1000 NAG A C2 1 HETATM 3691 C C3 . NAG B 2 . ? 26.749 -20.500 21.137 1.00 29.63 ? 1000 NAG A C3 1 HETATM 3692 C C4 . NAG B 2 . ? 26.245 -21.930 21.284 1.00 33.10 ? 1000 NAG A C4 1 HETATM 3693 C C5 . NAG B 2 . ? 24.979 -22.020 20.436 1.00 32.75 ? 1000 NAG A C5 1 HETATM 3694 C C6 . NAG B 2 . ? 24.378 -23.422 20.383 1.00 35.22 ? 1000 NAG A C6 1 HETATM 3695 C C7 . NAG B 2 . ? 26.073 -17.204 22.104 1.00 28.07 ? 1000 NAG A C7 1 HETATM 3696 C C8 . NAG B 2 . ? 26.828 -15.920 21.859 1.00 26.30 ? 1000 NAG A C8 1 HETATM 3697 N N2 . NAG B 2 . ? 26.168 -18.156 21.183 1.00 25.70 ? 1000 NAG A N2 1 HETATM 3698 O O3 . NAG B 2 . ? 27.863 -20.249 21.964 1.00 29.76 ? 1000 NAG A O3 1 HETATM 3699 O O4 . NAG B 2 . ? 27.190 -22.868 20.754 1.00 35.56 ? 1000 NAG A O4 1 HETATM 3700 O O5 . NAG B 2 . ? 23.972 -21.103 20.843 1.00 31.71 ? 1000 NAG A O5 1 HETATM 3701 O O6 . NAG B 2 . ? 24.163 -23.838 21.706 1.00 37.74 ? 1000 NAG A O6 1 HETATM 3702 O O7 . NAG B 2 . ? 25.415 -17.389 23.112 1.00 29.43 ? 1000 NAG A O7 1 HETATM 3703 C C1 . NAG C 2 . ? 28.237 -23.261 21.668 1.00 39.39 ? 1001 NAG A C1 1 HETATM 3704 C C2 . NAG C 2 . ? 28.624 -24.706 21.383 1.00 42.30 ? 1001 NAG A C2 1 HETATM 3705 C C3 . NAG C 2 . ? 29.896 -25.192 22.090 1.00 43.47 ? 1001 NAG A C3 1 HETATM 3706 C C4 . NAG C 2 . ? 31.031 -24.182 22.159 1.00 44.08 ? 1001 NAG A C4 1 HETATM 3707 C C5 . NAG C 2 . ? 30.358 -22.862 22.526 1.00 42.35 ? 1001 NAG A C5 1 HETATM 3708 C C6 . NAG C 2 . ? 31.359 -21.733 22.726 1.00 43.11 ? 1001 NAG A C6 1 HETATM 3709 C C7 . NAG C 2 . ? 26.783 -26.157 20.838 1.00 45.89 ? 1001 NAG A C7 1 HETATM 3710 C C8 . NAG C 2 . ? 25.635 -26.997 21.336 1.00 45.99 ? 1001 NAG A C8 1 HETATM 3711 N N2 . NAG C 2 . ? 27.536 -25.579 21.766 1.00 44.30 ? 1001 NAG A N2 1 HETATM 3712 O O3 . NAG C 2 . ? 30.350 -26.354 21.440 1.00 43.47 ? 1001 NAG A O3 1 HETATM 3713 O O4 . NAG C 2 . ? 31.871 -24.488 23.262 1.00 47.82 ? 1001 NAG A O4 1 HETATM 3714 O O5 . NAG C 2 . ? 29.409 -22.493 21.543 1.00 40.80 ? 1001 NAG A O5 1 HETATM 3715 O O6 . NAG C 2 . ? 32.163 -21.603 21.579 1.00 43.89 ? 1001 NAG A O6 1 HETATM 3716 O O7 . NAG C 2 . ? 26.995 -26.001 19.628 1.00 47.26 ? 1001 NAG A O7 1 HETATM 3717 C C1 . BMA D 3 . ? 32.956 -25.470 23.266 1.00 52.05 ? 1002 BMA A C1 1 HETATM 3718 C C2 . BMA D 3 . ? 32.837 -26.564 22.211 1.00 53.21 ? 1002 BMA A C2 1 HETATM 3719 C C3 . BMA D 3 . ? 34.035 -27.497 22.234 1.00 54.45 ? 1002 BMA A C3 1 HETATM 3720 C C4 . BMA D 3 . ? 35.275 -26.628 22.093 1.00 54.63 ? 1002 BMA A C4 1 HETATM 3721 C C5 . BMA D 3 . ? 35.355 -25.719 23.314 1.00 54.74 ? 1002 BMA A C5 1 HETATM 3722 C C6 . BMA D 3 . ? 36.653 -24.914 23.300 1.00 54.87 ? 1002 BMA A C6 1 HETATM 3723 O O2 . BMA D 3 . ? 32.778 -25.960 20.943 1.00 55.13 ? 1002 BMA A O2 1 HETATM 3724 O O3 . BMA D 3 . ? 33.929 -28.426 21.174 1.00 54.11 ? 1002 BMA A O3 1 HETATM 3725 O O4 . BMA D 3 . ? 36.458 -27.393 21.987 1.00 55.79 ? 1002 BMA A O4 1 HETATM 3726 O O5 . BMA D 3 . ? 34.237 -24.848 23.306 1.00 53.16 ? 1002 BMA A O5 1 HETATM 3727 O O6 . BMA D 3 . ? 37.375 -25.151 24.488 1.00 56.04 ? 1002 BMA A O6 1 HETATM 3728 CA CA . CA E 4 . ? 41.800 -1.589 22.326 1.00 20.48 ? 601 CA A CA 1 HETATM 3729 O O . HOH F 5 . ? 24.948 -6.640 30.474 1.00 19.74 ? 1003 HOH A O 1 HETATM 3730 O O . HOH F 5 . ? 29.153 -6.743 24.918 1.00 20.15 ? 1004 HOH A O 1 HETATM 3731 O O . HOH F 5 . ? 28.076 11.667 30.230 1.00 22.51 ? 1005 HOH A O 1 HETATM 3732 O O . HOH F 5 . ? 20.073 9.039 20.845 1.00 22.31 ? 1006 HOH A O 1 HETATM 3733 O O . HOH F 5 . ? 16.585 4.113 29.369 1.00 21.32 ? 1007 HOH A O 1 HETATM 3734 O O . HOH F 5 . ? 24.747 8.335 20.216 1.00 21.53 ? 1008 HOH A O 1 HETATM 3735 O O . HOH F 5 . ? 40.332 -0.835 27.291 1.00 20.87 ? 1009 HOH A O 1 HETATM 3736 O O . HOH F 5 . ? 23.977 13.644 15.215 1.00 20.62 ? 1010 HOH A O 1 HETATM 3737 O O . HOH F 5 . ? 18.762 12.144 20.090 1.00 22.94 ? 1011 HOH A O 1 HETATM 3738 O O . HOH F 5 . ? 28.221 2.133 37.203 1.00 22.53 ? 1012 HOH A O 1 HETATM 3739 O O . HOH F 5 . ? 22.602 -3.519 29.246 1.00 24.75 ? 1013 HOH A O 1 HETATM 3740 O O . HOH F 5 . ? 22.822 13.566 25.964 1.00 23.65 ? 1014 HOH A O 1 HETATM 3741 O O . HOH F 5 . ? 28.083 -5.081 38.767 1.00 23.67 ? 1015 HOH A O 1 HETATM 3742 O O . HOH F 5 . ? 27.629 18.063 24.742 1.00 23.50 ? 1016 HOH A O 1 HETATM 3743 O O . HOH F 5 . ? 18.438 11.073 10.821 1.00 24.71 ? 1017 HOH A O 1 HETATM 3744 O O . HOH F 5 . ? 18.121 -4.738 35.904 1.00 22.68 ? 1018 HOH A O 1 HETATM 3745 O O . HOH F 5 . ? 35.685 -7.842 38.831 1.00 21.75 ? 1019 HOH A O 1 HETATM 3746 O O . HOH F 5 . ? 21.005 3.516 41.118 1.00 26.68 ? 1020 HOH A O 1 HETATM 3747 O O . HOH F 5 . ? 31.547 18.395 14.926 1.00 26.17 ? 1021 HOH A O 1 HETATM 3748 O O . HOH F 5 . ? 26.591 6.589 21.648 1.00 22.61 ? 1022 HOH A O 1 HETATM 3749 O O . HOH F 5 . ? 21.114 -0.806 31.101 1.00 21.63 ? 1023 HOH A O 1 HETATM 3750 O O . HOH F 5 . ? 14.108 16.870 25.035 1.00 20.24 ? 1024 HOH A O 1 HETATM 3751 O O . HOH F 5 . ? 52.089 6.220 31.538 1.00 32.53 ? 1025 HOH A O 1 HETATM 3752 O O . HOH F 5 . ? 42.599 -2.883 20.365 1.00 20.26 ? 1026 HOH A O 1 HETATM 3753 O O . HOH F 5 . ? 0.746 12.551 12.316 1.00 29.97 ? 1027 HOH A O 1 HETATM 3754 O O . HOH F 5 . ? 30.144 17.697 28.681 1.00 29.49 ? 1028 HOH A O 1 HETATM 3755 O O . HOH F 5 . ? 28.638 4.347 24.910 1.00 22.35 ? 1029 HOH A O 1 HETATM 3756 O O . HOH F 5 . ? 6.999 -0.183 32.811 1.00 25.77 ? 1030 HOH A O 1 HETATM 3757 O O . HOH F 5 . ? 23.387 16.669 24.186 1.00 23.77 ? 1031 HOH A O 1 HETATM 3758 O O . HOH F 5 . ? 30.472 7.778 15.774 1.00 24.36 ? 1032 HOH A O 1 HETATM 3759 O O . HOH F 5 . ? 18.083 1.549 1.574 1.00 31.68 ? 1033 HOH A O 1 HETATM 3760 O O . HOH F 5 . ? 14.515 16.923 22.125 1.00 22.98 ? 1034 HOH A O 1 HETATM 3761 O O . HOH F 5 . ? 26.245 -7.262 24.233 1.00 19.92 ? 1035 HOH A O 1 HETATM 3762 O O . HOH F 5 . ? 24.444 20.779 30.301 1.00 28.92 ? 1036 HOH A O 1 HETATM 3763 O O . HOH F 5 . ? 12.901 27.743 18.517 1.00 25.78 ? 1037 HOH A O 1 HETATM 3764 O O . HOH F 5 . ? 6.798 0.969 13.845 1.00 27.75 ? 1038 HOH A O 1 HETATM 3765 O O . HOH F 5 . ? 2.147 4.864 28.422 1.00 27.98 ? 1039 HOH A O 1 HETATM 3766 O O . HOH F 5 . ? 25.852 -9.869 34.896 1.00 25.01 ? 1040 HOH A O 1 HETATM 3767 O O . HOH F 5 . ? 49.346 -2.118 25.762 1.00 28.55 ? 1041 HOH A O 1 HETATM 3768 O O . HOH F 5 . ? 24.318 14.216 8.301 1.00 28.50 ? 1042 HOH A O 1 HETATM 3769 O O . HOH F 5 . ? 13.090 -10.161 31.569 1.00 24.56 ? 1043 HOH A O 1 HETATM 3770 O O . HOH F 5 . ? 14.268 7.946 42.197 1.00 25.34 ? 1044 HOH A O 1 HETATM 3771 O O . HOH F 5 . ? 34.383 -11.503 38.954 1.00 28.05 ? 1045 HOH A O 1 HETATM 3772 O O . HOH F 5 . ? 3.661 18.842 20.757 1.00 28.25 ? 1046 HOH A O 1 HETATM 3773 O O . HOH F 5 . ? 7.406 -12.468 22.700 1.00 27.97 ? 1047 HOH A O 1 HETATM 3774 O O . HOH F 5 . ? 26.119 25.234 15.467 1.00 28.83 ? 1048 HOH A O 1 HETATM 3775 O O . HOH F 5 . ? 34.539 5.458 22.572 1.00 23.65 ? 1049 HOH A O 1 HETATM 3776 O O . HOH F 5 . ? 42.030 0.586 23.561 1.00 21.71 ? 1050 HOH A O 1 HETATM 3777 O O . HOH F 5 . ? 37.351 9.479 23.923 1.00 46.46 ? 1051 HOH A O 1 HETATM 3778 O O . HOH F 5 . ? 28.048 3.571 30.560 1.00 28.51 ? 1052 HOH A O 1 HETATM 3779 O O . HOH F 5 . ? 18.269 9.092 4.802 1.00 31.00 ? 1053 HOH A O 1 HETATM 3780 O O . HOH F 5 . ? 36.474 3.266 35.048 1.00 27.92 ? 1054 HOH A O 1 HETATM 3781 O O . HOH F 5 . ? 39.978 7.620 11.011 1.00 30.42 ? 1055 HOH A O 1 HETATM 3782 O O . HOH F 5 . ? 1.469 13.491 17.386 1.00 26.83 ? 1056 HOH A O 1 HETATM 3783 O O . HOH F 5 . ? 32.219 5.698 24.687 1.00 30.87 ? 1057 HOH A O 1 HETATM 3784 O O . HOH F 5 . ? 9.452 26.282 27.382 1.00 32.59 ? 1058 HOH A O 1 HETATM 3785 O O . HOH F 5 . ? 29.689 7.785 30.007 1.00 27.71 ? 1059 HOH A O 1 HETATM 3786 O O . HOH F 5 . ? 9.380 7.643 43.032 1.00 34.58 ? 1060 HOH A O 1 HETATM 3787 O O . HOH F 5 . ? 3.140 7.355 9.133 1.00 31.69 ? 1061 HOH A O 1 HETATM 3788 O O . HOH F 5 . ? 26.391 -7.546 37.174 1.00 27.92 ? 1062 HOH A O 1 HETATM 3789 O O . HOH F 5 . ? 10.769 27.966 -2.126 1.00 33.17 ? 1063 HOH A O 1 HETATM 3790 O O . HOH F 5 . ? 2.719 14.259 10.986 1.00 27.99 ? 1064 HOH A O 1 HETATM 3791 O O . HOH F 5 . ? 41.644 6.512 13.293 1.00 31.10 ? 1065 HOH A O 1 HETATM 3792 O O . HOH F 5 . ? 2.900 0.718 26.620 1.00 28.89 ? 1066 HOH A O 1 HETATM 3793 O O . HOH F 5 . ? 1.002 5.796 21.977 1.00 26.20 ? 1067 HOH A O 1 HETATM 3794 O O . HOH F 5 . ? 21.352 27.365 26.760 1.00 30.23 ? 1068 HOH A O 1 HETATM 3795 O O . HOH F 5 . ? 30.741 -2.261 5.709 1.00 32.82 ? 1069 HOH A O 1 HETATM 3796 O O . HOH F 5 . ? 10.267 -16.141 21.846 1.00 37.28 ? 1070 HOH A O 1 HETATM 3797 O O . HOH F 5 . ? 12.870 -0.863 43.598 1.00 31.41 ? 1071 HOH A O 1 HETATM 3798 O O . HOH F 5 . ? 46.690 -15.689 17.949 1.00 32.33 ? 1072 HOH A O 1 HETATM 3799 O O . HOH F 5 . ? 18.075 6.071 30.769 1.00 25.59 ? 1073 HOH A O 1 HETATM 3800 O O . HOH F 5 . ? 4.372 23.597 13.634 1.00 27.67 ? 1074 HOH A O 1 HETATM 3801 O O . HOH F 5 . ? 18.272 -5.852 38.482 1.00 27.35 ? 1075 HOH A O 1 HETATM 3802 O O . HOH F 5 . ? 4.239 8.269 14.542 1.00 31.41 ? 1076 HOH A O 1 HETATM 3803 O O . HOH F 5 . ? 47.615 -7.482 29.998 1.00 30.88 ? 1077 HOH A O 1 HETATM 3804 O O . HOH F 5 . ? 4.695 -7.718 20.060 1.00 33.62 ? 1078 HOH A O 1 HETATM 3805 O O . HOH F 5 . ? -0.064 10.622 21.653 1.00 35.61 ? 1079 HOH A O 1 HETATM 3806 O O . HOH F 5 . ? 24.273 -15.901 25.291 1.00 33.44 ? 1080 HOH A O 1 HETATM 3807 O O . HOH F 5 . ? 10.713 7.631 11.000 1.00 28.60 ? 1081 HOH A O 1 HETATM 3808 O O . HOH F 5 . ? 29.410 -18.504 14.903 1.00 36.03 ? 1082 HOH A O 1 HETATM 3809 O O . HOH F 5 . ? 13.470 -8.085 37.967 1.00 31.24 ? 1083 HOH A O 1 HETATM 3810 O O . HOH F 5 . ? 42.683 -3.092 43.312 1.00 38.11 ? 1084 HOH A O 1 HETATM 3811 O O . HOH F 5 . ? 8.833 32.460 16.365 1.00 30.99 ? 1085 HOH A O 1 HETATM 3812 O O . HOH F 5 . ? 21.543 -7.088 41.046 1.00 35.05 ? 1086 HOH A O 1 HETATM 3813 O O . HOH F 5 . ? 3.416 -2.782 24.838 1.00 36.96 ? 1087 HOH A O 1 HETATM 3814 O O . HOH F 5 . ? 30.241 14.255 27.948 1.00 35.44 ? 1088 HOH A O 1 HETATM 3815 O O . HOH F 5 . ? 17.645 15.444 36.133 1.00 34.98 ? 1089 HOH A O 1 HETATM 3816 O O . HOH F 5 . ? 22.529 -3.350 1.849 1.00 30.75 ? 1090 HOH A O 1 HETATM 3817 O O . HOH F 5 . ? 31.271 14.489 23.673 1.00 29.49 ? 1091 HOH A O 1 HETATM 3818 O O . HOH F 5 . ? 51.034 0.299 33.516 0.50 31.26 ? 1092 HOH A O 1 HETATM 3819 O O . HOH F 5 . ? 17.318 -1.038 42.847 1.00 39.58 ? 1093 HOH A O 1 HETATM 3820 O O . HOH F 5 . ? 45.607 -13.798 36.192 1.00 35.84 ? 1094 HOH A O 1 HETATM 3821 O O . HOH F 5 . ? 16.903 -9.295 10.268 1.00 33.18 ? 1095 HOH A O 1 HETATM 3822 O O . HOH F 5 . ? 7.616 -6.037 42.414 1.00 44.41 ? 1096 HOH A O 1 HETATM 3823 O O . HOH F 5 . ? 48.745 -4.301 19.403 1.00 37.49 ? 1097 HOH A O 1 HETATM 3824 O O . HOH F 5 . ? 26.093 -6.149 6.980 1.00 36.84 ? 1098 HOH A O 1 HETATM 3825 O O . HOH F 5 . ? 25.154 -14.696 34.333 1.00 41.32 ? 1099 HOH A O 1 HETATM 3826 O O . HOH F 5 . ? 37.715 -1.054 42.817 1.00 42.57 ? 1100 HOH A O 1 HETATM 3827 O O . HOH F 5 . ? 30.579 23.177 10.227 1.00 33.09 ? 1101 HOH A O 1 HETATM 3828 O O . HOH F 5 . ? 6.023 27.567 21.385 1.00 28.00 ? 1102 HOH A O 1 HETATM 3829 O O . HOH F 5 . ? 3.346 16.769 -5.944 1.00 48.85 ? 1103 HOH A O 1 HETATM 3830 O O . HOH F 5 . ? 2.469 17.526 16.397 1.00 31.67 ? 1104 HOH A O 1 HETATM 3831 O O . HOH F 5 . ? 18.201 10.195 40.440 1.00 34.18 ? 1105 HOH A O 1 HETATM 3832 O O . HOH F 5 . ? 52.844 6.621 34.203 1.00 34.51 ? 1106 HOH A O 1 HETATM 3833 O O . HOH F 5 . ? 0.930 -4.774 18.217 1.00 40.26 ? 1107 HOH A O 1 HETATM 3834 O O . HOH F 5 . ? 29.777 -6.971 5.721 1.00 38.09 ? 1108 HOH A O 1 HETATM 3835 O O . HOH F 5 . ? 14.152 34.742 20.419 1.00 41.12 ? 1109 HOH A O 1 HETATM 3836 O O . HOH F 5 . ? 10.948 -7.133 11.762 1.00 31.16 ? 1110 HOH A O 1 HETATM 3837 O O . HOH F 5 . ? 26.638 14.682 36.494 1.00 35.34 ? 1111 HOH A O 1 HETATM 3838 O O . HOH F 5 . ? 48.091 -13.807 15.575 1.00 39.62 ? 1112 HOH A O 1 HETATM 3839 O O . HOH F 5 . ? 30.906 -19.155 29.726 1.00 36.61 ? 1113 HOH A O 1 HETATM 3840 O O . HOH F 5 . ? 26.046 -19.507 25.690 1.00 37.37 ? 1114 HOH A O 1 HETATM 3841 O O . HOH F 5 . ? 12.966 37.009 -0.035 1.00 58.75 ? 1115 HOH A O 1 HETATM 3842 O O . HOH F 5 . ? 28.339 24.600 3.264 1.00 35.80 ? 1116 HOH A O 1 HETATM 3843 O O . HOH F 5 . ? 24.347 -6.117 46.863 1.00 42.86 ? 1117 HOH A O 1 HETATM 3844 O O . HOH F 5 . ? 22.088 16.605 36.227 1.00 36.89 ? 1118 HOH A O 1 HETATM 3845 O O . HOH F 5 . ? 9.055 26.074 -3.970 1.00 34.44 ? 1119 HOH A O 1 HETATM 3846 O O . HOH F 5 . ? 8.223 29.118 13.619 1.00 29.98 ? 1120 HOH A O 1 HETATM 3847 O O . HOH F 5 . ? 11.395 -17.063 24.262 1.00 38.71 ? 1121 HOH A O 1 HETATM 3848 O O . HOH F 5 . ? 46.456 -5.829 12.746 1.00 43.04 ? 1122 HOH A O 1 HETATM 3849 O O . HOH F 5 . ? 31.773 19.369 23.509 1.00 43.73 ? 1123 HOH A O 1 HETATM 3850 O O . HOH F 5 . ? 2.116 0.569 36.898 1.00 42.16 ? 1124 HOH A O 1 HETATM 3851 O O . HOH F 5 . ? 13.512 34.286 9.620 1.00 43.81 ? 1125 HOH A O 1 HETATM 3852 O O . HOH F 5 . ? -0.112 25.919 13.398 1.00 35.52 ? 1126 HOH A O 1 HETATM 3853 O O . HOH F 5 . ? 28.447 21.277 20.967 1.00 36.02 ? 1127 HOH A O 1 HETATM 3854 O O . HOH F 5 . ? -0.386 8.340 28.615 1.00 30.91 ? 1128 HOH A O 1 HETATM 3855 O O . HOH F 5 . ? 9.821 -5.780 38.592 1.00 27.65 ? 1129 HOH A O 1 HETATM 3856 O O . HOH F 5 . ? 7.679 3.367 5.994 1.00 39.09 ? 1130 HOH A O 1 HETATM 3857 O O . HOH F 5 . ? 5.961 38.950 8.348 1.00 40.86 ? 1131 HOH A O 1 HETATM 3858 O O . HOH F 5 . ? 13.252 -8.823 11.450 1.00 31.24 ? 1132 HOH A O 1 HETATM 3859 O O . HOH F 5 . ? 1.564 -6.728 14.388 1.00 43.19 ? 1133 HOH A O 1 HETATM 3860 O O . HOH F 5 . ? 17.456 11.570 38.078 1.00 43.73 ? 1134 HOH A O 1 HETATM 3861 O O . HOH F 5 . ? 16.333 9.220 6.899 1.00 29.83 ? 1135 HOH A O 1 HETATM 3862 O O . HOH F 5 . ? 23.589 -12.304 6.886 1.00 42.12 ? 1136 HOH A O 1 HETATM 3863 O O . HOH F 5 . ? 42.534 7.356 30.035 1.00 31.21 ? 1137 HOH A O 1 HETATM 3864 O O . HOH F 5 . ? 30.584 12.077 33.584 1.00 31.51 ? 1138 HOH A O 1 HETATM 3865 O O . HOH F 5 . ? 13.311 13.891 35.291 1.00 37.82 ? 1139 HOH A O 1 HETATM 3866 O O . HOH F 5 . ? 49.426 1.869 15.838 1.00 42.60 ? 1140 HOH A O 1 HETATM 3867 O O . HOH F 5 . ? 13.055 18.020 5.404 1.00 32.54 ? 1141 HOH A O 1 HETATM 3868 O O . HOH F 5 . ? 38.060 -3.977 44.564 1.00 40.81 ? 1142 HOH A O 1 HETATM 3869 O O . HOH F 5 . ? 3.863 15.765 30.103 1.00 39.86 ? 1143 HOH A O 1 HETATM 3870 O O . HOH F 5 . ? 1.856 13.676 32.720 1.00 55.50 ? 1144 HOH A O 1 HETATM 3871 O O . HOH F 5 . ? 29.280 2.036 45.405 1.00 40.82 ? 1145 HOH A O 1 HETATM 3872 O O . HOH F 5 . ? 26.493 3.183 0.670 1.00 42.26 ? 1146 HOH A O 1 HETATM 3873 O O . HOH F 5 . ? 5.915 12.987 33.425 1.00 40.03 ? 1147 HOH A O 1 HETATM 3874 O O . HOH F 5 . ? 32.691 -3.696 6.732 1.00 32.02 ? 1148 HOH A O 1 HETATM 3875 O O . HOH F 5 . ? 21.210 9.919 48.486 1.00 32.73 ? 1149 HOH A O 1 HETATM 3876 O O . HOH F 5 . ? 36.947 -19.529 30.262 1.00 49.45 ? 1150 HOH A O 1 HETATM 3877 O O . HOH F 5 . ? 12.436 11.308 37.982 1.00 36.92 ? 1151 HOH A O 1 HETATM 3878 O O . HOH F 5 . ? 30.475 22.794 4.066 1.00 38.98 ? 1152 HOH A O 1 HETATM 3879 O O . HOH F 5 . ? 34.098 18.894 19.623 1.00 56.60 ? 1153 HOH A O 1 HETATM 3880 O O . HOH F 5 . ? 12.725 -14.075 33.708 1.00 37.66 ? 1154 HOH A O 1 HETATM 3881 O O . HOH F 5 . ? 37.820 7.265 28.562 1.00 46.76 ? 1155 HOH A O 1 HETATM 3882 O O . HOH F 5 . ? 28.195 28.065 3.586 1.00 52.56 ? 1156 HOH A O 1 HETATM 3883 O O . HOH F 5 . ? 4.507 -6.176 23.282 1.00 38.55 ? 1157 HOH A O 1 HETATM 3884 O O . HOH F 5 . ? -0.704 15.302 17.501 1.00 39.87 ? 1158 HOH A O 1 HETATM 3885 O O . HOH F 5 . ? 12.685 -19.473 23.556 1.00 53.24 ? 1159 HOH A O 1 HETATM 3886 O O . HOH F 5 . ? 23.344 5.849 -0.749 1.00 34.81 ? 1160 HOH A O 1 HETATM 3887 O O . HOH F 5 . ? 16.191 -19.127 29.225 1.00 36.63 ? 1161 HOH A O 1 HETATM 3888 O O . HOH F 5 . ? 13.188 -14.689 18.824 1.00 40.33 ? 1162 HOH A O 1 HETATM 3889 O O . HOH F 5 . ? 0.221 32.141 -0.056 0.50 32.26 ? 1163 HOH A O 1 HETATM 3890 O O . HOH F 5 . ? 18.091 13.023 -7.210 1.00 47.83 ? 1164 HOH A O 1 HETATM 3891 O O . HOH F 5 . ? 21.452 32.839 23.991 1.00 42.85 ? 1165 HOH A O 1 HETATM 3892 O O . HOH F 5 . ? 24.945 -18.840 31.375 1.00 34.54 ? 1166 HOH A O 1 HETATM 3893 O O . HOH F 5 . ? 46.991 -15.085 33.018 1.00 36.21 ? 1167 HOH A O 1 HETATM 3894 O O . HOH F 5 . ? 29.962 -12.609 34.731 1.00 33.07 ? 1168 HOH A O 1 HETATM 3895 O O . HOH F 5 . ? 35.133 -1.342 46.230 1.00 31.26 ? 1169 HOH A O 1 HETATM 3896 O O . HOH F 5 . ? 3.118 5.522 7.010 1.00 39.22 ? 1170 HOH A O 1 HETATM 3897 O O . HOH F 5 . ? 23.911 26.778 26.517 1.00 34.45 ? 1171 HOH A O 1 HETATM 3898 O O . HOH F 5 . ? 31.670 6.817 37.662 1.00 40.35 ? 1172 HOH A O 1 HETATM 3899 O O . HOH F 5 . ? 43.678 5.226 9.795 1.00 43.57 ? 1173 HOH A O 1 HETATM 3900 O O . HOH F 5 . ? 28.889 19.383 32.127 1.00 47.38 ? 1174 HOH A O 1 HETATM 3901 O O . HOH F 5 . ? 4.795 21.740 18.014 1.00 33.79 ? 1175 HOH A O 1 HETATM 3902 O O . HOH F 5 . ? 47.863 -0.319 41.381 1.00 45.54 ? 1176 HOH A O 1 HETATM 3903 O O . HOH F 5 . ? 50.151 11.856 18.581 1.00 52.76 ? 1177 HOH A O 1 HETATM 3904 O O . HOH F 5 . ? 20.568 30.055 26.989 1.00 37.89 ? 1178 HOH A O 1 HETATM 3905 O O . HOH F 5 . ? 14.957 -4.007 41.555 1.00 37.78 ? 1179 HOH A O 1 HETATM 3906 O O . HOH F 5 . ? 10.080 4.082 8.089 1.00 33.59 ? 1180 HOH A O 1 HETATM 3907 O O . HOH F 5 . ? -3.335 26.899 1.885 1.00 34.71 ? 1181 HOH A O 1 HETATM 3908 O O . HOH F 5 . ? 8.263 -2.235 42.657 1.00 41.32 ? 1182 HOH A O 1 HETATM 3909 O O . HOH F 5 . ? 1.701 27.321 15.208 1.00 47.94 ? 1183 HOH A O 1 HETATM 3910 O O . HOH F 5 . ? 36.829 8.309 3.688 1.00 47.74 ? 1184 HOH A O 1 HETATM 3911 O O . HOH F 5 . ? 46.320 -18.822 26.818 1.00 55.83 ? 1185 HOH A O 1 HETATM 3912 O O . HOH F 5 . ? 14.080 14.570 -7.465 1.00 38.44 ? 1186 HOH A O 1 HETATM 3913 O O . HOH F 5 . ? 22.248 7.514 20.868 1.00 24.65 ? 1187 HOH A O 1 HETATM 3914 O O . HOH F 5 . ? 28.789 7.868 22.886 1.00 22.86 ? 1188 HOH A O 1 HETATM 3915 O O . HOH F 5 . ? 28.501 4.492 27.977 1.00 27.42 ? 1189 HOH A O 1 HETATM 3916 O O . HOH F 5 . ? 32.648 -4.772 28.261 1.00 21.75 ? 1190 HOH A O 1 HETATM 3917 O O . HOH F 5 . ? 29.844 -5.412 27.285 1.00 21.95 ? 1191 HOH A O 1 HETATM 3918 O O . HOH F 5 . ? 32.158 -8.082 20.769 1.00 22.15 ? 1192 HOH A O 1 HETATM 3919 O O . HOH F 5 . ? 34.229 -2.302 21.415 1.00 21.29 ? 1193 HOH A O 1 HETATM 3920 O O . HOH F 5 . ? 40.969 -3.863 22.460 1.00 19.26 ? 1194 HOH A O 1 HETATM 3921 O O . HOH F 5 . ? 40.807 2.459 15.055 1.00 29.09 ? 1195 HOH A O 1 HETATM 3922 O O . HOH F 5 . ? 44.764 -2.816 18.605 1.00 27.38 ? 1196 HOH A O 1 HETATM 3923 O O . HOH F 5 . ? 43.359 1.588 13.036 1.00 33.99 ? 1197 HOH A O 1 HETATM 3924 O O . HOH F 5 . ? 36.480 6.689 24.327 1.00 28.76 ? 1198 HOH A O 1 HETATM 3925 O O . HOH F 5 . ? 34.661 5.500 19.828 1.00 22.84 ? 1199 HOH A O 1 HETATM 3926 O O . HOH F 5 . ? 16.103 8.023 37.648 1.00 24.53 ? 1200 HOH A O 1 HETATM 3927 O O . HOH F 5 . ? 14.924 7.449 30.543 1.00 20.95 ? 1201 HOH A O 1 HETATM 3928 O O . HOH F 5 . ? 15.832 14.488 34.180 1.00 31.55 ? 1202 HOH A O 1 HETATM 3929 O O . HOH F 5 . ? 23.094 11.810 39.302 1.00 26.93 ? 1203 HOH A O 1 HETATM 3930 O O . HOH F 5 . ? 8.695 -0.037 35.098 1.00 25.69 ? 1204 HOH A O 1 HETATM 3931 O O . HOH F 5 . ? 4.355 0.419 33.360 1.00 30.99 ? 1205 HOH A O 1 HETATM 3932 O O . HOH F 5 . ? 2.777 2.302 32.119 1.00 32.25 ? 1206 HOH A O 1 HETATM 3933 O O . HOH F 5 . ? 6.905 -2.708 31.654 1.00 29.23 ? 1207 HOH A O 1 HETATM 3934 O O . HOH F 5 . ? 29.626 16.683 26.062 1.00 25.65 ? 1208 HOH A O 1 HETATM 3935 O O . HOH F 5 . ? 28.693 25.627 16.556 1.00 36.29 ? 1209 HOH A O 1 HETATM 3936 O O . HOH F 5 . ? 31.815 21.798 8.079 1.00 39.66 ? 1210 HOH A O 1 HETATM 3937 O O . HOH F 5 . ? 24.520 27.752 21.454 1.00 36.35 ? 1211 HOH A O 1 HETATM 3938 O O . HOH F 5 . ? 14.640 22.106 26.068 1.00 22.09 ? 1212 HOH A O 1 HETATM 3939 O O . HOH F 5 . ? 16.391 16.602 26.707 1.00 20.08 ? 1213 HOH A O 1 HETATM 3940 O O . HOH F 5 . ? 30.449 10.216 29.936 1.00 30.03 ? 1214 HOH A O 1 HETATM 3941 O O . HOH F 5 . ? 23.097 5.537 37.473 1.00 21.83 ? 1215 HOH A O 1 HETATM 3942 O O . HOH F 5 . ? 27.296 5.455 35.782 1.00 24.69 ? 1216 HOH A O 1 HETATM 3943 O O . HOH F 5 . ? 29.354 3.669 35.363 1.00 23.75 ? 1217 HOH A O 1 HETATM 3944 O O . HOH F 5 . ? 27.020 -8.115 43.868 1.00 26.46 ? 1218 HOH A O 1 HETATM 3945 O O . HOH F 5 . ? 42.285 4.824 30.837 1.00 26.86 ? 1219 HOH A O 1 HETATM 3946 O O . HOH F 5 . ? 0.627 16.172 13.287 1.00 33.78 ? 1220 HOH A O 1 HETATM 3947 O O . HOH F 5 . ? 29.104 19.958 23.314 1.00 29.42 ? 1221 HOH A O 1 HETATM 3948 O O . HOH F 5 . ? 32.007 16.939 24.799 1.00 34.33 ? 1222 HOH A O 1 HETATM 3949 O O . HOH F 5 . ? 28.651 20.185 28.154 1.00 31.82 ? 1223 HOH A O 1 HETATM 3950 O O . HOH F 5 . ? 27.436 21.118 30.249 1.00 35.93 ? 1224 HOH A O 1 HETATM 3951 O O . HOH F 5 . ? 6.338 14.309 30.750 1.00 30.06 ? 1225 HOH A O 1 HETATM 3952 O O . HOH F 5 . ? 0.717 11.247 19.083 1.00 31.25 ? 1226 HOH A O 1 HETATM 3953 O O . HOH F 5 . ? 0.122 3.627 20.443 1.00 34.40 ? 1227 HOH A O 1 HETATM 3954 O O . HOH F 5 . ? 0.931 11.968 15.042 1.00 27.47 ? 1228 HOH A O 1 HETATM 3955 O O . HOH F 5 . ? 4.012 19.075 18.179 1.00 31.43 ? 1229 HOH A O 1 HETATM 3956 O O . HOH F 5 . ? 0.408 27.426 8.088 1.00 38.09 ? 1230 HOH A O 1 HETATM 3957 O O . HOH F 5 . ? 6.159 24.869 22.246 1.00 39.66 ? 1231 HOH A O 1 HETATM 3958 O O . HOH F 5 . ? 5.591 29.531 23.167 1.00 38.81 ? 1232 HOH A O 1 HETATM 3959 O O . HOH F 5 . ? 13.581 31.813 13.007 1.00 31.82 ? 1233 HOH A O 1 HETATM 3960 O O . HOH F 5 . ? 15.077 11.291 7.686 1.00 32.85 ? 1234 HOH A O 1 HETATM 3961 O O . HOH F 5 . ? 18.724 6.517 5.830 1.00 34.61 ? 1235 HOH A O 1 HETATM 3962 O O . HOH F 5 . ? 15.199 0.654 4.249 1.00 34.15 ? 1236 HOH A O 1 HETATM 3963 O O . HOH F 5 . ? 12.791 5.674 0.746 1.00 38.25 ? 1237 HOH A O 1 HETATM 3964 O O . HOH F 5 . ? 23.507 11.743 8.232 1.00 28.23 ? 1238 HOH A O 1 HETATM 3965 O O . HOH F 5 . ? 27.695 10.844 1.935 1.00 31.20 ? 1239 HOH A O 1 HETATM 3966 O O . HOH F 5 . ? 26.946 8.468 -0.513 1.00 35.44 ? 1240 HOH A O 1 HETATM 3967 O O . HOH F 5 . ? 28.807 1.553 4.442 1.00 34.43 ? 1241 HOH A O 1 HETATM 3968 O O . HOH F 5 . ? 31.201 0.307 4.813 1.00 34.59 ? 1242 HOH A O 1 HETATM 3969 O O . HOH F 5 . ? 20.400 -5.392 27.549 1.00 20.89 ? 1243 HOH A O 1 HETATM 3970 O O . HOH F 5 . ? 13.903 -2.026 30.567 1.00 21.05 ? 1244 HOH A O 1 HETATM 3971 O O . HOH F 5 . ? 25.978 -13.912 25.956 1.00 29.29 ? 1245 HOH A O 1 HETATM 3972 O O . HOH F 5 . ? 27.824 -21.034 24.477 1.00 34.86 ? 1246 HOH A O 1 HETATM 3973 O O . HOH F 5 . ? 29.149 -20.935 28.397 1.00 37.47 ? 1247 HOH A O 1 HETATM 3974 O O . HOH F 5 . ? 39.802 -19.881 26.840 1.00 50.55 ? 1248 HOH A O 1 HETATM 3975 O O . HOH F 5 . ? 39.265 -20.877 30.001 1.00 36.50 ? 1249 HOH A O 1 HETATM 3976 O O . HOH F 5 . ? 36.046 -21.515 33.767 1.00 33.83 ? 1250 HOH A O 1 HETATM 3977 O O . HOH F 5 . ? 41.664 -19.488 16.701 1.00 43.97 ? 1251 HOH A O 1 HETATM 3978 O O . HOH F 5 . ? 51.401 0.004 21.158 0.50 35.29 ? 1252 HOH A O 1 HETATM 3979 O O . HOH F 5 . ? 46.501 -1.257 17.187 1.00 39.25 ? 1253 HOH A O 1 HETATM 3980 O O . HOH F 5 . ? 44.215 -1.859 11.175 1.00 35.01 ? 1254 HOH A O 1 HETATM 3981 O O . HOH F 5 . ? 37.355 5.814 35.028 1.00 37.36 ? 1255 HOH A O 1 HETATM 3982 O O . HOH F 5 . ? 31.792 4.852 36.041 1.00 39.27 ? 1256 HOH A O 1 HETATM 3983 O O . HOH F 5 . ? 23.091 -3.375 43.583 1.00 36.55 ? 1257 HOH A O 1 HETATM 3984 O O . HOH F 5 . ? 26.088 -5.916 41.076 1.00 33.40 ? 1258 HOH A O 1 HETATM 3985 O O . HOH F 5 . ? 26.680 -5.937 45.490 1.00 32.13 ? 1259 HOH A O 1 HETATM 3986 O O . HOH F 5 . ? 24.761 -8.532 39.076 1.00 34.22 ? 1260 HOH A O 1 HETATM 3987 O O . HOH F 5 . ? 24.437 -12.292 35.369 1.00 32.30 ? 1261 HOH A O 1 HETATM 3988 O O . HOH F 5 . ? 16.301 -7.991 37.711 1.00 40.20 ? 1262 HOH A O 1 HETATM 3989 O O . HOH F 5 . ? 17.363 -4.951 40.789 1.00 39.90 ? 1263 HOH A O 1 HETATM 3990 O O . HOH F 5 . ? 12.700 -5.594 42.534 1.00 44.85 ? 1264 HOH A O 1 HETATM 3991 O O . HOH F 5 . ? 12.172 -5.836 37.296 1.00 28.88 ? 1265 HOH A O 1 HETATM 3992 O O . HOH F 5 . ? 13.855 0.413 41.487 1.00 31.51 ? 1266 HOH A O 1 HETATM 3993 O O . HOH F 5 . ? 10.465 -1.964 43.998 1.00 37.24 ? 1267 HOH A O 1 HETATM 3994 O O . HOH F 5 . ? 5.995 -3.799 44.701 1.00 67.41 ? 1268 HOH A O 1 HETATM 3995 O O . HOH F 5 . ? 6.625 0.135 42.850 1.00 38.05 ? 1269 HOH A O 1 HETATM 3996 O O . HOH F 5 . ? 11.652 8.942 42.568 1.00 34.58 ? 1270 HOH A O 1 HETATM 3997 O O . HOH F 5 . ? 6.796 8.625 39.167 1.00 35.16 ? 1271 HOH A O 1 HETATM 3998 O O . HOH F 5 . ? 11.056 11.455 35.648 1.00 33.16 ? 1272 HOH A O 1 HETATM 3999 O O . HOH F 5 . ? 9.437 13.131 34.876 1.00 43.27 ? 1273 HOH A O 1 HETATM 4000 O O . HOH F 5 . ? 19.305 13.346 36.656 1.00 37.59 ? 1274 HOH A O 1 HETATM 4001 O O . HOH F 5 . ? 14.907 21.301 34.591 1.00 30.14 ? 1275 HOH A O 1 HETATM 4002 O O . HOH F 5 . ? 12.483 32.502 23.159 1.00 35.67 ? 1276 HOH A O 1 HETATM 4003 O O . HOH F 5 . ? 4.666 33.732 17.989 1.00 36.51 ? 1277 HOH A O 1 HETATM 4004 O O . HOH F 5 . ? 6.111 33.222 21.380 1.00 39.29 ? 1278 HOH A O 1 HETATM 4005 O O . HOH F 5 . ? 10.260 30.971 14.507 1.00 30.37 ? 1279 HOH A O 1 HETATM 4006 O O . HOH F 5 . ? 1.186 25.014 11.198 1.00 34.13 ? 1280 HOH A O 1 HETATM 4007 O O . HOH F 5 . ? 3.051 23.009 15.933 1.00 37.48 ? 1281 HOH A O 1 HETATM 4008 O O . HOH F 5 . ? 15.487 17.156 5.786 1.00 29.55 ? 1282 HOH A O 1 HETATM 4009 O O . HOH F 5 . ? 23.253 10.992 10.782 1.00 39.33 ? 1283 HOH A O 1 HETATM 4010 O O . HOH F 5 . ? 25.950 6.638 -1.994 1.00 49.44 ? 1284 HOH A O 1 HETATM 4011 O O . HOH F 5 . ? 30.467 5.863 -1.002 1.00 47.65 ? 1285 HOH A O 1 HETATM 4012 O O . HOH F 5 . ? 23.043 15.227 3.362 1.00 37.55 ? 1286 HOH A O 1 HETATM 4013 O O . HOH F 5 . ? 11.854 26.892 -5.103 1.00 34.70 ? 1287 HOH A O 1 HETATM 4014 O O . HOH F 5 . ? 38.657 -7.817 9.084 1.00 36.80 ? 1288 HOH A O 1 HETATM 4015 O O . HOH F 5 . ? 14.984 10.563 -5.916 1.00 42.84 ? 1289 HOH A O 1 HETATM 4016 O O . HOH F 5 . ? 17.097 9.343 -4.334 1.00 44.69 ? 1290 HOH A O 1 HETATM 4017 O O . HOH F 5 . ? 6.894 10.695 -0.296 1.00 33.57 ? 1291 HOH A O 1 HETATM 4018 O O . HOH F 5 . ? 16.637 30.285 0.497 1.00 53.13 ? 1292 HOH A O 1 HETATM 4019 O O . HOH F 5 . ? -0.317 10.150 11.692 1.00 33.11 ? 1293 HOH A O 1 HETATM 4020 O O . HOH F 5 . ? -1.358 14.210 12.285 1.00 32.33 ? 1294 HOH A O 1 HETATM 4021 O O . HOH F 5 . ? 0.337 4.193 24.076 1.00 29.29 ? 1295 HOH A O 1 HETATM 4022 O O . HOH F 5 . ? 16.664 1.580 43.215 1.00 42.10 ? 1296 HOH A O 1 HETATM 4023 O O . HOH F 5 . ? 18.739 3.576 43.089 1.00 38.45 ? 1297 HOH A O 1 HETATM 4024 O O . HOH F 5 . ? -2.256 10.436 26.218 1.00 43.32 ? 1298 HOH A O 1 HETATM 4025 O O . HOH F 5 . ? 1.749 3.393 37.209 1.00 37.71 ? 1299 HOH A O 1 HETATM 4026 O O . HOH F 5 . ? 3.731 2.418 40.206 1.00 35.21 ? 1300 HOH A O 1 HETATM 4027 O O . HOH F 5 . ? 5.847 -5.075 32.614 1.00 35.44 ? 1301 HOH A O 1 HETATM 4028 O O . HOH F 5 . ? -1.130 -3.256 22.168 1.00 500.00 ? 1302 HOH A O 1 HETATM 4029 O O . HOH F 5 . ? 2.182 -7.465 19.038 1.00 40.99 ? 1303 HOH A O 1 HETATM 4030 O O . HOH F 5 . ? 1.182 8.629 18.347 1.00 38.12 ? 1304 HOH A O 1 HETATM 4031 O O . HOH F 5 . ? 4.309 5.787 11.229 1.00 36.57 ? 1305 HOH A O 1 HETATM 4032 O O . HOH F 5 . ? 20.184 -14.914 32.481 1.00 42.46 ? 1306 HOH A O 1 HETATM 4033 O O . HOH F 5 . ? 17.289 -13.729 35.500 1.00 43.33 ? 1307 HOH A O 1 HETATM 4034 O O . HOH F 5 . ? 11.632 -10.412 34.119 1.00 34.48 ? 1308 HOH A O 1 HETATM 4035 O O . HOH F 5 . ? 11.263 -2.424 10.803 1.00 36.68 ? 1309 HOH A O 1 HETATM 4036 O O . HOH F 5 . ? 1.904 3.389 26.207 1.00 30.73 ? 1310 HOH A O 1 HETATM 4037 O O . HOH F 5 . ? 1.775 -3.560 14.331 1.00 42.83 ? 1311 HOH A O 1 HETATM 4038 O O . HOH F 5 . ? 23.737 -7.341 6.070 1.00 38.18 ? 1312 HOH A O 1 HETATM 4039 O O . HOH F 5 . ? 20.951 -9.227 7.684 1.00 34.38 ? 1313 HOH A O 1 HETATM 4040 O O . HOH F 5 . ? 32.575 -6.322 6.244 1.00 37.66 ? 1314 HOH A O 1 HETATM 4041 O O . HOH F 5 . ? 34.240 -12.796 9.357 1.00 32.08 ? 1315 HOH A O 1 HETATM 4042 O O . HOH F 5 . ? 24.422 -15.233 12.445 1.00 40.95 ? 1316 HOH A O 1 HETATM 4043 O O . HOH F 5 . ? 27.376 -8.432 7.062 1.00 44.24 ? 1317 HOH A O 1 HETATM 4044 O O . HOH F 5 . ? 43.217 4.531 12.352 1.00 38.58 ? 1318 HOH A O 1 HETATM 4045 O O . HOH F 5 . ? 20.586 -2.766 43.034 1.00 36.53 ? 1319 HOH A O 1 HETATM 4046 O O . HOH F 5 . ? 26.948 17.758 33.204 1.00 32.10 ? 1320 HOH A O 1 HETATM 4047 O O . HOH F 5 . ? 30.215 16.952 33.701 1.00 42.71 ? 1321 HOH A O 1 HETATM 4048 O O . HOH F 5 . ? 25.070 19.645 32.914 1.00 38.32 ? 1322 HOH A O 1 HETATM 4049 O O . HOH F 5 . ? 31.707 14.132 34.239 1.00 46.95 ? 1323 HOH A O 1 HETATM 4050 O O . HOH F 5 . ? 39.310 10.480 18.912 1.00 42.25 ? 1324 HOH A O 1 HETATM 4051 O O . HOH F 5 . ? 43.824 8.191 13.321 1.00 36.64 ? 1325 HOH A O 1 HETATM 4052 O O . HOH F 5 . ? 40.561 13.863 16.317 1.00 42.52 ? 1326 HOH A O 1 HETATM 4053 O O . HOH F 5 . ? 35.624 15.497 18.969 1.00 35.52 ? 1327 HOH A O 1 HETATM 4054 O O . HOH F 5 . ? 32.233 20.975 14.827 1.00 39.64 ? 1328 HOH A O 1 HETATM 4055 O O . HOH F 5 . ? 26.794 28.378 18.349 1.00 49.35 ? 1329 HOH A O 1 HETATM 4056 O O . HOH F 5 . ? 17.205 33.074 17.786 1.00 41.96 ? 1330 HOH A O 1 HETATM 4057 O O . HOH F 5 . ? 29.228 4.487 32.806 1.00 36.71 ? 1331 HOH A O 1 HETATM 4058 O O . HOH F 5 . ? 37.717 5.178 30.513 1.00 30.66 ? 1332 HOH A O 1 HETATM 4059 O O . HOH F 5 . ? 40.194 8.182 37.080 1.00 46.34 ? 1333 HOH A O 1 HETATM 4060 O O . HOH F 5 . ? 42.503 5.414 39.458 1.00 43.71 ? 1334 HOH A O 1 HETATM 4061 O O . HOH F 5 . ? 35.495 -0.249 43.884 1.00 41.04 ? 1335 HOH A O 1 HETATM 4062 O O . HOH F 5 . ? 23.671 -6.222 42.139 1.00 38.87 ? 1336 HOH A O 1 HETATM 4063 O O . HOH F 5 . ? 28.701 5.563 43.204 1.00 39.51 ? 1337 HOH A O 1 HETATM 4064 O O . HOH F 5 . ? 27.762 9.190 41.429 1.00 40.10 ? 1338 HOH A O 1 HETATM 4065 O O . HOH F 5 . ? 47.435 -0.823 38.598 1.00 34.12 ? 1339 HOH A O 1 HETATM 4066 O O . HOH F 5 . ? 50.284 0.113 38.555 1.00 56.09 ? 1340 HOH A O 1 HETATM 4067 O O . HOH F 5 . ? 47.452 10.093 16.336 1.00 41.52 ? 1341 HOH A O 1 HETATM 4068 O O . HOH F 5 . ? 50.104 7.550 17.032 1.00 53.55 ? 1342 HOH A O 1 HETATM 4069 O O . HOH F 5 . ? 52.709 7.520 19.394 1.00 50.40 ? 1343 HOH A O 1 HETATM 4070 O O . HOH F 5 . ? 44.966 -3.632 44.198 1.00 49.66 ? 1344 HOH A O 1 HETATM 4071 O O . HOH F 5 . ? 40.453 -4.681 44.470 1.00 38.64 ? 1345 HOH A O 1 HETATM 4072 O O . HOH F 5 . ? 47.339 -6.906 34.665 1.00 29.51 ? 1346 HOH A O 1 HETATM 4073 O O . HOH F 5 . ? 43.278 -19.749 29.572 1.00 44.04 ? 1347 HOH A O 1 HETATM 4074 O O . HOH F 5 . ? 31.118 -16.696 36.120 1.00 41.89 ? 1348 HOH A O 1 HETATM 4075 O O . HOH F 5 . ? 43.761 9.581 17.938 1.00 38.80 ? 1349 HOH A O 1 HETATM 4076 O O . HOH F 5 . ? 33.819 2.895 2.069 1.00 43.60 ? 1350 HOH A O 1 HETATM 4077 O O . HOH F 5 . ? 33.341 5.977 -0.727 1.00 52.91 ? 1351 HOH A O 1 HETATM 4078 O O . HOH F 5 . ? 22.730 8.289 -0.667 1.00 42.82 ? 1352 HOH A O 1 HETATM 4079 O O . HOH F 5 . ? 26.559 -5.196 3.184 1.00 46.75 ? 1353 HOH A O 1 HETATM 4080 O O . HOH F 5 . ? 28.099 -4.841 5.391 1.00 38.25 ? 1354 HOH A O 1 HETATM 4081 O O . HOH F 5 . ? 21.480 -4.735 -0.002 1.00 39.08 ? 1355 HOH A O 1 HETATM 4082 O O . HOH F 5 . ? 18.967 -5.527 1.346 1.00 39.20 ? 1356 HOH A O 1 HETATM 4083 O O . HOH F 5 . ? 19.691 -10.281 5.595 1.00 49.73 ? 1357 HOH A O 1 HETATM 4084 O O . HOH F 5 . ? 19.069 -11.831 12.398 1.00 33.92 ? 1358 HOH A O 1 HETATM 4085 O O . HOH F 5 . ? 18.083 -16.263 14.319 1.00 43.87 ? 1359 HOH A O 1 HETATM 4086 O O . HOH F 5 . ? 16.126 -11.258 12.849 1.00 39.50 ? 1360 HOH A O 1 HETATM 4087 O O . HOH F 5 . ? 13.662 -7.009 7.326 1.00 41.82 ? 1361 HOH A O 1 HETATM 4088 O O . HOH F 5 . ? 12.546 -11.617 11.726 1.00 53.38 ? 1362 HOH A O 1 HETATM 4089 O O . HOH F 5 . ? 20.131 -20.039 22.595 1.00 41.92 ? 1363 HOH A O 1 HETATM 4090 O O . HOH F 5 . ? 22.009 -18.490 23.271 1.00 37.95 ? 1364 HOH A O 1 HETATM 4091 O O . HOH F 5 . ? 23.613 -17.709 27.431 1.00 36.61 ? 1365 HOH A O 1 HETATM 4092 O O . HOH F 5 . ? 23.093 -16.910 30.269 1.00 40.46 ? 1366 HOH A O 1 HETATM 4093 O O . HOH F 5 . ? 34.547 -20.508 23.088 1.00 40.72 ? 1367 HOH A O 1 HETATM 4094 O O . HOH F 5 . ? 31.946 6.119 29.355 1.00 38.89 ? 1368 HOH A O 1 HETATM 4095 O O . HOH F 5 . ? 32.401 0.963 27.069 1.00 27.75 ? 1369 HOH A O 1 HETATM 4096 O O . HOH F 5 . ? 31.375 3.558 25.291 1.00 30.34 ? 1370 HOH A O 1 HETATM 4097 O O . HOH F 5 . ? 12.810 -17.535 31.444 1.00 44.83 ? 1371 HOH A O 1 HETATM 4098 O O . HOH F 5 . ? 0.647 -4.715 29.116 1.00 44.59 ? 1372 HOH A O 1 HETATM 4099 O O . HOH F 5 . ? 1.866 -5.612 25.007 1.00 39.60 ? 1373 HOH A O 1 HETATM 4100 O O . HOH F 5 . ? 0.658 -8.052 21.319 1.00 33.80 ? 1374 HOH A O 1 HETATM 4101 O O . HOH F 5 . ? 1.979 -2.880 16.327 1.00 41.38 ? 1375 HOH A O 1 HETATM 4102 O O . HOH F 5 . ? 5.724 -11.532 27.361 1.00 39.30 ? 1376 HOH A O 1 HETATM 4103 O O . HOH F 5 . ? -4.837 10.928 21.373 1.00 48.22 ? 1377 HOH A O 1 HETATM 4104 O O . HOH F 5 . ? -0.902 7.489 7.666 1.00 43.35 ? 1378 HOH A O 1 HETATM 4105 O O . HOH F 5 . ? -0.690 19.258 -3.224 1.00 40.31 ? 1379 HOH A O 1 HETATM 4106 O O . HOH F 5 . ? -1.868 21.747 -5.030 1.00 52.84 ? 1380 HOH A O 1 HETATM 4107 O O . HOH F 5 . ? 16.039 17.114 -6.321 1.00 44.43 ? 1381 HOH A O 1 HETATM 4108 O O . HOH F 5 . ? 7.408 12.618 -6.724 1.00 36.94 ? 1382 HOH A O 1 HETATM 4109 O O . HOH F 5 . ? 5.609 10.260 -3.410 1.00 41.63 ? 1383 HOH A O 1 HETATM 4110 O O . HOH F 5 . ? 9.342 11.787 -0.254 1.00 38.02 ? 1384 HOH A O 1 HETATM 4111 O O . HOH F 5 . ? 18.964 11.096 -5.134 1.00 48.85 ? 1385 HOH A O 1 HETATM 4112 O O . HOH F 5 . ? 12.783 2.885 0.755 1.00 41.88 ? 1386 HOH A O 1 HETATM 4113 O O . HOH F 5 . ? -3.690 19.084 5.191 1.00 40.09 ? 1387 HOH A O 1 HETATM 4114 O O . HOH F 5 . ? -5.831 19.925 3.526 1.00 48.11 ? 1388 HOH A O 1 HETATM 4115 O O . HOH F 5 . ? 2.912 34.487 8.292 1.00 55.68 ? 1389 HOH A O 1 HETATM 4116 O O . HOH F 5 . ? 2.868 33.471 11.935 1.00 38.20 ? 1390 HOH A O 1 HETATM 4117 O O . HOH F 5 . ? 10.572 26.934 12.189 1.00 35.23 ? 1391 HOH A O 1 HETATM 4118 O O . HOH F 5 . ? 0.471 33.806 15.863 1.00 42.69 ? 1392 HOH A O 1 HETATM 4119 O O . HOH F 5 . ? 23.372 23.745 0.749 1.00 36.75 ? 1393 HOH A O 1 HETATM 4120 O O . HOH F 5 . ? 20.453 30.969 2.406 1.00 46.36 ? 1394 HOH A O 1 HETATM 4121 O O . HOH F 5 . ? 16.941 29.153 25.938 1.00 38.04 ? 1395 HOH A O 1 HETATM 4122 O O . HOH F 5 . ? 27.764 22.750 32.961 1.00 98.52 ? 1396 HOH A O 1 HETATM 4123 O O . HOH F 5 . ? 32.533 7.386 26.665 1.00 42.04 ? 1397 HOH A O 1 HETATM 4124 O O . HOH F 5 . ? 17.343 28.088 29.182 1.00 27.49 ? 1398 HOH A O 1 HETATM 4125 O O . HOH F 5 . ? 6.944 12.170 37.149 1.00 53.29 ? 1399 HOH A O 1 HETATM 4126 O O . HOH F 5 . ? 37.883 18.040 9.275 1.00 47.17 ? 1400 HOH A O 1 HETATM 4127 O O . HOH F 5 . ? 35.630 15.771 6.111 1.00 47.41 ? 1401 HOH A O 1 HETATM 4128 O O . HOH F 5 . ? 39.964 11.899 6.485 1.00 40.89 ? 1402 HOH A O 1 HETATM 4129 O O . HOH F 5 . ? 38.068 16.121 17.348 1.00 40.44 ? 1403 HOH A O 1 HETATM 4130 O O . HOH F 5 . ? 38.155 -2.155 4.715 1.00 43.67 ? 1404 HOH A O 1 HETATM 4131 O O . HOH F 5 . ? 40.734 -6.055 7.284 1.00 35.46 ? 1405 HOH A O 1 HETATM 4132 O O . HOH F 5 . ? 39.078 -10.354 8.117 1.00 43.18 ? 1406 HOH A O 1 HETATM 4133 O O . HOH F 5 . ? 34.719 -3.190 4.593 1.00 47.89 ? 1407 HOH A O 1 HETATM 4134 O O . HOH F 5 . ? 50.659 -5.071 21.766 1.00 42.84 ? 1408 HOH A O 1 HETATM 4135 O O . HOH F 5 . ? 52.590 -3.376 32.005 1.00 38.94 ? 1409 HOH A O 1 HETATM 4136 O O . HOH F 5 . ? 48.967 1.875 37.557 1.00 46.99 ? 1410 HOH A O 1 HETATM 4137 O O . HOH F 5 . ? 30.040 22.624 16.497 1.00 47.94 ? 1411 HOH A O 1 HETATM 4138 O O . HOH F 5 . ? 18.658 17.948 35.607 1.00 33.19 ? 1412 HOH A O 1 HETATM 4139 O O . HOH F 5 . ? 18.990 18.695 38.270 1.00 30.31 ? 1413 HOH A O 1 HETATM 4140 O O . HOH F 5 . ? 11.449 10.994 40.571 1.00 33.16 ? 1414 HOH A O 1 HETATM 4141 O O . HOH F 5 . ? 18.689 30.683 25.090 1.00 35.79 ? 1415 HOH A O 1 HETATM 4142 O O . HOH F 5 . ? 0.650 7.951 10.057 1.00 40.11 ? 1416 HOH A O 1 HETATM 4143 O O . HOH F 5 . ? -4.740 12.350 12.437 1.00 49.82 ? 1417 HOH A O 1 HETATM 4144 O O . HOH F 5 . ? -2.125 24.302 14.568 1.00 41.88 ? 1418 HOH A O 1 HETATM 4145 O O . HOH F 5 . ? 7.750 -0.512 11.674 1.00 41.81 ? 1419 HOH A O 1 HETATM 4146 O O . HOH F 5 . ? 2.580 -10.031 13.436 1.00 33.19 ? 1420 HOH A O 1 HETATM 4147 O O . HOH F 5 . ? 1.844 -6.435 27.598 1.00 38.78 ? 1421 HOH A O 1 HETATM 4148 O O . HOH F 5 . ? 4.030 -9.555 28.105 1.00 40.35 ? 1422 HOH A O 1 HETATM 4149 O O . HOH F 5 . ? 4.191 -8.772 22.926 1.00 42.84 ? 1423 HOH A O 1 HETATM 4150 O O . HOH F 5 . ? 7.908 -14.165 27.247 1.00 51.37 ? 1424 HOH A O 1 HETATM 4151 O O . HOH F 5 . ? 1.805 3.998 40.837 1.00 46.86 ? 1425 HOH A O 1 HETATM 4152 O O . HOH F 5 . ? 9.523 -7.902 40.195 1.00 44.57 ? 1426 HOH A O 1 HETATM 4153 O O . HOH F 5 . ? 45.015 -16.930 33.512 1.00 46.66 ? 1427 HOH A O 1 HETATM 4154 O O . HOH F 5 . ? 13.194 10.701 41.894 1.00 80.45 ? 1428 HOH A O 1 HETATM 4155 O O . HOH F 5 . ? 0.624 7.476 31.192 1.00 42.47 ? 1429 HOH A O 1 HETATM 4156 O O . HOH F 5 . ? -2.493 12.145 22.171 1.00 45.16 ? 1430 HOH A O 1 HETATM 4157 O O . HOH F 5 . ? 1.423 9.259 15.226 1.00 46.32 ? 1431 HOH A O 1 HETATM 4158 O O . HOH F 5 . ? 4.663 38.204 17.606 1.00 44.69 ? 1432 HOH A O 1 HETATM 4159 O O . HOH F 5 . ? -0.877 19.625 16.119 1.00 52.87 ? 1433 HOH A O 1 HETATM 4160 O O . HOH F 5 . ? -4.130 20.250 7.626 1.00 40.33 ? 1434 HOH A O 1 HETATM 4161 O O . HOH F 5 . ? 7.796 2.032 3.651 1.00 43.67 ? 1435 HOH A O 1 HETATM 4162 O O . HOH F 5 . ? 1.697 14.833 29.765 1.00 41.38 ? 1436 HOH A O 1 HETATM 4163 O O . HOH F 5 . ? -2.969 12.808 14.057 1.00 67.45 ? 1437 HOH A O 1 HETATM 4164 O O . HOH F 5 . ? 3.252 3.592 15.163 1.00 47.52 ? 1438 HOH A O 1 HETATM 4165 O O . HOH F 5 . ? 13.336 -2.683 6.622 1.00 44.16 ? 1439 HOH A O 1 HETATM 4166 O O . HOH F 5 . ? 42.403 -19.204 33.530 1.00 43.74 ? 1440 HOH A O 1 HETATM 4167 O O . HOH F 5 . ? 37.665 -18.956 33.209 1.00 46.26 ? 1441 HOH A O 1 HETATM 4168 O O . HOH F 5 . ? 49.279 -9.697 16.735 1.00 47.82 ? 1442 HOH A O 1 HETATM 4169 O O . HOH F 5 . ? 49.866 10.872 16.728 1.00 49.33 ? 1443 HOH A O 1 HETATM 4170 O O . HOH F 5 . ? 46.271 7.432 12.788 1.00 47.24 ? 1444 HOH A O 1 HETATM 4171 O O . HOH F 5 . ? 51.817 10.551 22.837 1.00 42.05 ? 1445 HOH A O 1 HETATM 4172 O O . HOH F 5 . ? 49.567 -12.503 16.479 1.00 60.63 ? 1446 HOH A O 1 HETATM 4173 O O . HOH F 5 . ? 44.193 13.349 25.405 1.00 41.47 ? 1447 HOH A O 1 HETATM 4174 O O . HOH F 5 . ? 31.178 7.346 40.401 1.00 46.82 ? 1448 HOH A O 1 HETATM 4175 O O . HOH F 5 . ? 41.801 -0.108 43.162 1.00 41.21 ? 1449 HOH A O 1 HETATM 4176 O O . HOH F 5 . ? 6.079 -12.117 25.092 1.00 45.38 ? 1450 HOH A O 1 HETATM 4177 O O . HOH F 5 . ? 1.591 -11.689 15.471 1.00 34.21 ? 1451 HOH A O 1 HETATM 4178 O O . HOH F 5 . ? 1.883 -10.837 18.140 1.00 41.06 ? 1452 HOH A O 1 HETATM 4179 O O . HOH F 5 . ? 44.973 -7.425 13.078 1.00 41.98 ? 1453 HOH A O 1 HETATM 4180 O O . HOH F 5 . ? 47.000 -12.501 38.861 1.00 49.38 ? 1454 HOH A O 1 HETATM 4181 O O . HOH F 5 . ? 30.042 -19.276 19.578 1.00 46.70 ? 1455 HOH A O 1 HETATM 4182 O O . HOH F 5 . ? 23.710 -20.131 24.870 1.00 40.88 ? 1456 HOH A O 1 HETATM 4183 O O . HOH F 5 . ? 15.729 8.320 44.523 1.00 39.84 ? 1457 HOH A O 1 HETATM 4184 O O . HOH F 5 . ? 21.601 7.132 48.243 1.00 44.41 ? 1458 HOH A O 1 HETATM 4185 O O . HOH F 5 . ? 27.527 3.844 44.318 1.00 44.42 ? 1459 HOH A O 1 HETATM 4186 O O . HOH F 5 . ? 33.289 2.741 32.115 1.00 43.98 ? 1460 HOH A O 1 HETATM 4187 O O . HOH F 5 . ? 40.900 -6.095 42.456 1.00 45.01 ? 1461 HOH A O 1 HETATM 4188 O O . HOH F 5 . ? 10.470 -5.628 9.568 1.00 41.45 ? 1462 HOH A O 1 HETATM 4189 O O . HOH F 5 . ? 29.417 20.938 34.136 1.00 51.03 ? 1463 HOH A O 1 HETATM 4190 O O . HOH F 5 . ? 22.830 -14.361 38.676 1.00 50.48 ? 1464 HOH A O 1 HETATM 4191 O O . HOH F 5 . ? 27.807 -11.352 36.927 1.00 49.15 ? 1465 HOH A O 1 HETATM 4192 O O . HOH F 5 . ? 40.117 -18.506 18.743 1.00 42.57 ? 1466 HOH A O 1 HETATM 4193 O O . HOH F 5 . ? 26.755 -10.589 5.367 1.00 59.46 ? 1467 HOH A O 1 HETATM 4194 O O . HOH F 5 . ? 28.185 18.835 0.124 1.00 49.95 ? 1468 HOH A O 1 HETATM 4195 O O . HOH F 5 . ? 13.286 1.165 2.394 1.00 43.76 ? 1469 HOH A O 1 HETATM 4196 O O . HOH F 5 . ? 33.999 16.729 26.889 1.00 44.73 ? 1470 HOH A O 1 HETATM 4197 O O . HOH F 5 . ? 22.835 31.596 13.780 1.00 46.56 ? 1471 HOH A O 1 HETATM 4198 O O . HOH F 5 . ? 20.249 34.900 4.983 1.00 53.46 ? 1472 HOH A O 1 HETATM 4199 O O . HOH F 5 . ? 0.049 17.689 18.296 1.00 44.27 ? 1473 HOH A O 1 HETATM 4200 O O . HOH F 5 . ? -0.597 28.833 6.016 1.00 43.42 ? 1474 HOH A O 1 HETATM 4201 O O . HOH F 5 . ? 6.478 35.452 1.650 1.00 47.35 ? 1475 HOH A O 1 HETATM 4202 O O . HOH F 5 . ? 15.938 33.942 0.084 1.00 47.59 ? 1476 HOH A O 1 HETATM 4203 O O . HOH F 5 . ? 24.718 15.279 5.646 1.00 34.86 ? 1477 HOH A O 1 HETATM 4204 O O . HOH F 5 . ? 20.503 16.102 -2.551 1.00 40.74 ? 1478 HOH A O 1 HETATM 4205 O O . HOH F 5 . ? 21.944 0.034 -0.396 1.00 55.03 ? 1479 HOH A O 1 HETATM 4206 O O . HOH F 5 . ? 31.162 22.070 20.075 1.00 43.18 ? 1480 HOH A O 1 HETATM 4207 O O . HOH F 5 . ? 34.177 -15.198 10.464 1.00 53.63 ? 1481 HOH A O 1 HETATM 4208 O O . HOH F 5 . ? 37.178 -10.281 6.536 1.00 54.56 ? 1482 HOH A O 1 HETATM 4209 O O . HOH F 5 . ? 15.976 -16.009 18.478 1.00 43.43 ? 1483 HOH A O 1 HETATM 4210 O O . HOH F 5 . ? 25.518 12.806 39.204 1.00 39.88 ? 1484 HOH A O 1 HETATM 4211 O O . HOH F 5 . ? 5.867 -8.922 38.076 1.00 58.09 ? 1485 HOH A O 1 HETATM 4212 O O . HOH F 5 . ? 4.849 17.868 28.102 1.00 31.43 ? 1486 HOH A O 1 HETATM 4213 O O . HOH F 5 . ? 7.703 16.509 26.492 1.00 28.09 ? 1487 HOH A O 1 HETATM 4214 O O . HOH F 5 . ? -2.040 31.464 -1.947 1.00 38.59 ? 1488 HOH A O 1 HETATM 4215 O O . HOH F 5 . ? -4.023 29.721 -1.980 1.00 50.13 ? 1489 HOH A O 1 HETATM 4216 O O . HOH F 5 . ? 0.140 24.378 -8.519 1.00 55.40 ? 1490 HOH A O 1 HETATM 4217 O O . HOH F 5 . ? 3.456 27.608 20.785 1.00 43.39 ? 1491 HOH A O 1 HETATM 4218 O O . HOH F 5 . ? 35.200 4.171 30.202 1.00 46.47 ? 1492 HOH A O 1 HETATM 4219 O O . HOH F 5 . ? 34.001 4.021 34.465 1.00 42.18 ? 1493 HOH A O 1 HETATM 4220 O O . HOH F 5 . ? 38.698 11.976 26.740 1.00 55.39 ? 1494 HOH A O 1 HETATM 4221 O O . HOH F 5 . ? 50.002 -8.416 29.859 1.00 38.76 ? 1495 HOH A O 1 HETATM 4222 O O . HOH F 5 . ? 48.202 -13.498 34.824 1.00 42.08 ? 1496 HOH A O 1 HETATM 4223 O O . HOH F 5 . ? 47.383 -8.858 36.687 1.00 41.31 ? 1497 HOH A O 1 HETATM 4224 O O . HOH F 5 . ? 33.189 -19.613 28.178 1.00 36.16 ? 1498 HOH A O 1 HETATM 4225 O O . HOH F 5 . ? 33.045 -21.070 25.855 1.00 40.99 ? 1499 HOH A O 1 HETATM 4226 O O . HOH F 5 . ? 34.672 -20.969 29.895 1.00 47.06 ? 1500 HOH A O 1 HETATM 4227 O O . HOH F 5 . ? 30.387 -16.552 13.369 1.00 49.05 ? 1501 HOH A O 1 HETATM 4228 O O . HOH F 5 . ? 29.931 -20.928 16.574 1.00 59.36 ? 1502 HOH A O 1 HETATM 4229 O O . HOH F 5 . ? 50.100 -0.439 16.987 1.00 43.92 ? 1503 HOH A O 1 HETATM 4230 O O . HOH F 5 . ? 53.337 8.134 23.473 1.00 37.03 ? 1504 HOH A O 1 HETATM 4231 O O . HOH F 5 . ? 51.233 9.397 26.619 1.00 56.69 ? 1505 HOH A O 1 HETATM 4232 O O . HOH F 5 . ? 47.943 7.026 33.948 1.00 51.09 ? 1506 HOH A O 1 HETATM 4233 O O . HOH F 5 . ? 44.875 6.023 36.117 1.00 47.13 ? 1507 HOH A O 1 HETATM 4234 O O . HOH F 5 . ? 43.248 6.309 33.988 1.00 45.35 ? 1508 HOH A O 1 HETATM 4235 O O . HOH F 5 . ? 45.261 9.773 32.908 1.00 56.18 ? 1509 HOH A O 1 HETATM 4236 O O . HOH F 5 . ? 44.758 7.592 32.578 1.00 47.04 ? 1510 HOH A O 1 HETATM 4237 O O . HOH F 5 . ? 51.217 -4.632 35.865 1.00 44.30 ? 1511 HOH A O 1 HETATM 4238 O O . HOH F 5 . ? 38.643 -13.825 41.582 1.00 38.08 ? 1512 HOH A O 1 HETATM 4239 O O . HOH F 5 . ? 9.931 19.874 31.297 1.00 41.07 ? 1513 HOH A O 1 HETATM 4240 O O . HOH F 5 . ? 41.416 -16.783 41.683 1.00 37.29 ? 1514 HOH A O 1 HETATM 4241 O O . HOH F 5 . ? 19.486 -4.989 42.442 1.00 44.18 ? 1515 HOH A O 1 HETATM 4242 O O . HOH F 5 . ? 24.284 -8.010 44.073 1.00 48.11 ? 1516 HOH A O 1 HETATM 4243 O O . HOH F 5 . ? 19.584 -17.497 30.596 1.00 46.61 ? 1517 HOH A O 1 HETATM 4244 O O . HOH F 5 . ? 9.594 -12.233 33.884 1.00 45.41 ? 1518 HOH A O 1 HETATM 4245 O O . HOH F 5 . ? 6.422 -11.012 33.267 1.00 51.72 ? 1519 HOH A O 1 HETATM 4246 O O . HOH F 5 . ? 3.608 -10.746 30.384 1.00 50.57 ? 1520 HOH A O 1 HETATM 4247 O O . HOH F 5 . ? 7.867 13.268 32.738 1.00 84.76 ? 1521 HOH A O 1 HETATM 4248 O O . HOH F 5 . ? 10.160 22.333 31.080 1.00 56.84 ? 1522 HOH A O 1 HETATM 4249 O O . HOH F 5 . ? 2.611 27.097 9.820 1.00 45.53 ? 1523 HOH A O 1 HETATM 4250 O O . HOH F 5 . ? -0.911 28.538 13.520 1.00 42.09 ? 1524 HOH A O 1 HETATM 4251 O O . HOH F 5 . ? -0.232 34.221 11.407 1.00 53.13 ? 1525 HOH A O 1 HETATM 4252 O O . HOH F 5 . ? 6.147 19.838 -6.663 1.00 41.43 ? 1526 HOH A O 1 HETATM 4253 O O . HOH F 5 . ? 8.918 6.185 -5.365 1.00 42.30 ? 1527 HOH A O 1 HETATM 4254 O O . HOH F 5 . ? 14.165 2.530 -1.571 1.00 55.28 ? 1528 HOH A O 1 HETATM 4255 O O . HOH F 5 . ? 15.198 21.899 -2.745 1.00 39.50 ? 1529 HOH A O 1 HETATM 4256 O O . HOH F 5 . ? 2.559 24.470 20.459 1.00 54.06 ? 1530 HOH A O 1 HETATM 4257 O O . HOH F 5 . ? 5.570 28.587 25.714 1.00 46.10 ? 1531 HOH A O 1 HETATM 4258 O O . HOH F 5 . ? 14.320 30.428 24.922 1.00 52.60 ? 1532 HOH A O 1 HETATM 4259 O O . HOH F 5 . ? 5.564 -10.235 11.706 1.00 75.72 ? 1533 HOH A O 1 HETATM 4260 O O . HOH F 5 . ? 12.414 -13.645 16.457 1.00 51.02 ? 1534 HOH A O 1 HETATM 4261 O O . HOH F 5 . ? -7.111 11.991 13.379 1.00 40.99 ? 1535 HOH A O 1 HETATM 4262 O O . HOH F 5 . ? -5.954 19.142 9.133 1.00 45.78 ? 1536 HOH A O 1 HETATM 4263 O O . HOH F 5 . ? 0.542 3.694 10.977 1.00 54.80 ? 1537 HOH A O 1 HETATM 4264 O O . HOH F 5 . ? 27.245 -0.867 4.228 1.00 42.69 ? 1538 HOH A O 1 HETATM 4265 O O . HOH F 5 . ? 30.688 -3.366 2.982 1.00 49.35 ? 1539 HOH A O 1 HETATM 4266 O O . HOH F 5 . ? 19.759 -1.712 -1.900 1.00 53.33 ? 1540 HOH A O 1 HETATM 4267 O O . HOH F 5 . ? 27.790 -13.599 7.696 1.00 47.60 ? 1541 HOH A O 1 HETATM 4268 O O . HOH F 5 . ? 4.417 -2.328 40.066 1.00 45.63 ? 1542 HOH A O 1 HETATM 4269 O O . HOH F 5 . ? 10.972 2.138 45.433 1.00 45.39 ? 1543 HOH A O 1 HETATM 4270 O O . HOH F 5 . ? 22.225 2.780 47.462 1.00 47.91 ? 1544 HOH A O 1 HETATM 4271 O O . HOH F 5 . ? 19.619 -1.936 45.452 1.00 51.98 ? 1545 HOH A O 1 HETATM 4272 O O . HOH F 5 . ? 15.981 0.972 45.757 1.00 50.13 ? 1546 HOH A O 1 HETATM 4273 O O . HOH F 5 . ? 41.237 -2.756 46.904 1.00 50.49 ? 1547 HOH A O 1 HETATM 4274 O O . HOH F 5 . ? 41.743 -7.074 44.891 1.00 45.39 ? 1548 HOH A O 1 HETATM 4275 O O . HOH F 5 . ? 49.169 -10.795 35.986 1.00 50.85 ? 1549 HOH A O 1 HETATM 4276 O O . HOH F 5 . ? 35.635 10.366 5.188 1.00 39.34 ? 1550 HOH A O 1 HETATM 4277 O O . HOH F 5 . ? 41.663 13.943 6.343 1.00 49.93 ? 1551 HOH A O 1 HETATM 4278 O O . HOH F 5 . ? 41.483 9.651 9.768 1.00 43.05 ? 1552 HOH A O 1 HETATM 4279 O O . HOH F 5 . ? 28.994 3.398 2.640 1.00 43.89 ? 1553 HOH A O 1 HETATM 4280 O O . HOH F 5 . ? 24.990 1.046 0.410 1.00 48.73 ? 1554 HOH A O 1 HETATM 4281 O O . HOH F 5 . ? 25.442 -2.200 1.820 1.00 57.80 ? 1555 HOH A O 1 HETATM 4282 O O . HOH F 5 . ? 7.219 17.456 28.540 1.00 46.72 ? 1556 HOH A O 1 HETATM 4283 O O . HOH F 5 . ? 1.820 4.851 33.076 1.00 41.72 ? 1557 HOH A O 1 HETATM 4284 O O . HOH F 5 . ? -4.216 12.402 29.005 1.00 43.73 ? 1558 HOH A O 1 HETATM 4285 O O . HOH F 5 . ? 20.611 12.778 -3.563 1.00 41.19 ? 1559 HOH A O 1 HETATM 4286 O O . HOH F 5 . ? 15.165 16.957 -9.565 1.00 46.67 ? 1560 HOH A O 1 HETATM 4287 O O . HOH F 5 . ? 11.557 36.263 4.900 1.00 45.77 ? 1561 HOH A O 1 HETATM 4288 O O . HOH F 5 . ? 7.711 37.186 4.112 1.00 48.57 ? 1562 HOH A O 1 HETATM 4289 O O . HOH F 5 . ? 13.211 34.465 -0.240 1.00 51.24 ? 1563 HOH A O 1 HETATM 4290 O O . HOH F 5 . ? -4.381 14.769 27.666 1.00 71.53 ? 1564 HOH A O 1 HETATM 4291 O O . HOH F 5 . ? 20.398 11.415 42.056 1.00 20.00 ? 1565 HOH A O 1 HETATM 4292 O O . HOH F 5 . ? 15.556 10.516 37.961 1.00 20.00 ? 1566 HOH A O 1 # 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 ALA 1 1 1 ALA ALA A . n A 1 2 THR 2 2 2 THR THR A . n A 1 3 PRO 3 3 3 PRO PRO A . n A 1 4 ALA 4 4 4 ALA ALA A . n A 1 5 ASP 5 5 5 ASP ASP A . n A 1 6 TRP 6 6 6 TRP TRP A . n A 1 7 ARG 7 7 7 ARG ARG A . n A 1 8 SER 8 8 8 SER SER A . n A 1 9 GLN 9 9 9 GLN GLN A . n A 1 10 SER 10 10 10 SER SER A . n A 1 11 ILE 11 11 11 ILE ILE A . n A 1 12 TYR 12 12 12 TYR TYR A . n A 1 13 PHE 13 13 13 PHE PHE A . n A 1 14 LEU 14 14 14 LEU LEU A . n A 1 15 LEU 15 15 15 LEU LEU A . n A 1 16 THR 16 16 16 THR THR A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 ARG 18 18 18 ARG ARG A . n A 1 19 PHE 19 19 19 PHE PHE A . n A 1 20 ALA 20 20 20 ALA ALA A . n A 1 21 ARG 21 21 21 ARG ARG A . n A 1 22 THR 22 22 22 THR THR A . n A 1 23 ASP 23 23 23 ASP ASP A . n A 1 24 GLY 24 24 24 GLY GLY A . n A 1 25 SER 25 25 25 SER SER A . n A 1 26 THR 26 26 26 THR THR A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 ALA 28 28 28 ALA ALA A . n A 1 29 THR 29 29 29 THR THR A . n A 1 30 CYS 30 30 30 CYS CYS A . n A 1 31 ASN 31 31 31 ASN ASN A . n A 1 32 THR 32 32 32 THR THR A . n A 1 33 ALA 33 33 33 ALA ALA A . n A 1 34 ASP 34 34 34 ASP ASP A . n A 1 35 GLN 35 35 35 GLN GLN A . n A 1 36 LYS 36 36 36 LYS LYS A . n A 1 37 TYR 37 37 37 TYR TYR A . n A 1 38 CYS 38 38 38 CYS CYS A . n A 1 39 GLY 39 39 39 GLY GLY A . n A 1 40 GLY 40 40 40 GLY GLY A . n A 1 41 THR 41 41 41 THR THR A . n A 1 42 TRP 42 42 42 TRP TRP A . n A 1 43 GLN 43 43 43 GLN GLN A . n A 1 44 GLY 44 44 44 GLY GLY A . n A 1 45 ILE 45 45 45 ILE ILE A . n A 1 46 ILE 46 46 46 ILE ILE A . n A 1 47 ASP 47 47 47 ASP ASP A . n A 1 48 LYS 48 48 48 LYS LYS A . n A 1 49 LEU 49 49 49 LEU LEU A . n A 1 50 ASP 50 50 50 ASP ASP A . n A 1 51 TYR 51 51 51 TYR TYR A . n A 1 52 ILE 52 52 52 ILE ILE A . n A 1 53 GLN 53 53 53 GLN GLN A . n A 1 54 GLY 54 54 54 GLY GLY A . n A 1 55 MET 55 55 55 MET MET A . n A 1 56 GLY 56 56 56 GLY GLY A . n A 1 57 PHE 57 57 57 PHE PHE A . n A 1 58 THR 58 58 58 THR THR A . n A 1 59 ALA 59 59 59 ALA ALA A . n A 1 60 ILE 60 60 60 ILE ILE A . n A 1 61 TRP 61 61 61 TRP TRP A . n A 1 62 ILE 62 62 62 ILE ILE A . n A 1 63 THR 63 63 63 THR THR A . n A 1 64 PRO 64 64 64 PRO PRO A . n A 1 65 VAL 65 65 65 VAL VAL A . n A 1 66 THR 66 66 66 THR THR A . n A 1 67 ALA 67 67 67 ALA ALA A . n A 1 68 GLN 68 68 68 GLN GLN A . n A 1 69 LEU 69 69 69 LEU LEU A . n A 1 70 PRO 70 70 70 PRO PRO A . n A 1 71 GLN 71 71 71 GLN GLN A . n A 1 72 THR 72 72 72 THR THR A . n A 1 73 THR 73 73 73 THR THR A . n A 1 74 ALA 74 74 74 ALA ALA A . n A 1 75 TYR 75 75 75 TYR TYR A . n A 1 76 GLY 76 76 76 GLY GLY A . n A 1 77 ASP 77 77 77 ASP ASP A . n A 1 78 ALA 78 78 78 ALA ALA A . n A 1 79 TYR 79 79 79 TYR TYR A . n A 1 80 HIS 80 80 80 HIS HIS A . n A 1 81 GLY 81 81 81 GLY GLY A . n A 1 82 TYR 82 82 82 TYR TYR A . n A 1 83 TRP 83 83 83 TRP TRP A . n A 1 84 GLN 84 84 84 GLN GLN A . n A 1 85 GLN 85 85 85 GLN GLN A . n A 1 86 ASP 86 86 86 ASP ASP A . n A 1 87 ILE 87 87 87 ILE ILE A . n A 1 88 TYR 88 88 88 TYR TYR A . n A 1 89 SER 89 89 89 SER SER A . n A 1 90 LEU 90 90 90 LEU LEU A . n A 1 91 ASN 91 91 91 ASN ASN A . n A 1 92 GLU 92 92 92 GLU GLU A . n A 1 93 ASN 93 93 93 ASN ASN A . n A 1 94 TYR 94 94 94 TYR TYR A . n A 1 95 GLY 95 95 95 GLY GLY A . n A 1 96 THR 96 96 96 THR THR A . n A 1 97 ALA 97 97 97 ALA ALA A . n A 1 98 ASP 98 98 98 ASP ASP A . n A 1 99 ASP 99 99 99 ASP ASP A . n A 1 100 LEU 100 100 100 LEU LEU A . n A 1 101 LYS 101 101 101 LYS LYS A . n A 1 102 ALA 102 102 102 ALA ALA A . n A 1 103 LEU 103 103 103 LEU LEU A . n A 1 104 SER 104 104 104 SER SER A . n A 1 105 SER 105 105 105 SER SER A . n A 1 106 ALA 106 106 106 ALA ALA A . n A 1 107 LEU 107 107 107 LEU LEU A . n A 1 108 HIS 108 108 108 HIS HIS A . n A 1 109 GLU 109 109 109 GLU GLU A . n A 1 110 ARG 110 110 110 ARG ARG A . n A 1 111 GLY 111 111 111 GLY GLY A . n A 1 112 MET 112 112 112 MET MET A . n A 1 113 TYR 113 113 113 TYR TYR A . n A 1 114 LEU 114 114 114 LEU LEU A . n A 1 115 MET 115 115 115 MET MET A . n A 1 116 VAL 116 116 116 VAL VAL A . n A 1 117 ASP 117 117 117 ASP ASP A . n A 1 118 VAL 118 118 118 VAL VAL A . n A 1 119 VAL 119 119 119 VAL VAL A . n A 1 120 ALA 120 120 120 ALA ALA A . n A 1 121 ASN 121 121 121 ASN ASN A . n A 1 122 HIS 122 122 122 HIS HIS A . n A 1 123 MET 123 123 123 MET MET A . n A 1 124 GLY 124 124 124 GLY GLY A . n A 1 125 TYR 125 125 125 TYR TYR A . n A 1 126 ASP 126 126 126 ASP ASP A . n A 1 127 GLY 127 127 127 GLY GLY A . n A 1 128 ALA 128 128 128 ALA ALA A . n A 1 129 GLY 129 129 129 GLY GLY A . n A 1 130 SER 130 130 130 SER SER 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 ASP 133 133 133 ASP ASP A . n A 1 134 TYR 134 134 134 TYR TYR A . n A 1 135 SER 135 135 135 SER SER A . n A 1 136 VAL 136 136 136 VAL VAL A . n A 1 137 PHE 137 137 137 PHE PHE A . n A 1 138 LYS 138 138 138 LYS LYS A . n A 1 139 PRO 139 139 139 PRO PRO A . n A 1 140 PHE 140 140 140 PHE PHE A . n A 1 141 SER 141 141 141 SER SER A . n A 1 142 SER 142 142 142 SER SER A . n A 1 143 GLN 143 143 143 GLN GLN A . n A 1 144 ASP 144 144 144 ASP ASP A . n A 1 145 TYR 145 145 145 TYR TYR A . n A 1 146 PHE 146 146 146 PHE PHE A . n A 1 147 HIS 147 147 147 HIS HIS A . n A 1 148 PRO 148 148 148 PRO PRO A . n A 1 149 PHE 149 149 149 PHE PHE A . n A 1 150 CYS 150 150 150 CYS CYS A . n A 1 151 PHE 151 151 151 PHE PHE A . n A 1 152 ILE 152 152 152 ILE ILE A . n A 1 153 GLN 153 153 153 GLN GLN A . n A 1 154 ASN 154 154 154 ASN ASN A . n A 1 155 TYR 155 155 155 TYR TYR A . n A 1 156 GLU 156 156 156 GLU GLU A . n A 1 157 ASP 157 157 157 ASP ASP A . n A 1 158 GLN 158 158 158 GLN GLN A . n A 1 159 THR 159 159 159 THR THR A . n A 1 160 GLN 160 160 160 GLN GLN A . n A 1 161 VAL 161 161 161 VAL VAL A . n A 1 162 GLU 162 162 162 GLU GLU A . n A 1 163 ASP 163 163 163 ASP ASP A . n A 1 164 CYS 164 164 164 CYS CYS A . n A 1 165 TRP 165 165 165 TRP TRP A . n A 1 166 LEU 166 166 166 LEU LEU A . n A 1 167 GLY 167 167 167 GLY GLY A . n A 1 168 ASP 168 168 168 ASP ASP A . n A 1 169 ASN 169 169 169 ASN ASN A . n A 1 170 THR 170 170 170 THR THR A . n A 1 171 VAL 171 171 171 VAL VAL A . n A 1 172 SER 172 172 172 SER SER A . n A 1 173 LEU 173 173 173 LEU LEU A . n A 1 174 PRO 174 174 174 PRO PRO A . n A 1 175 ASP 175 175 175 ASP ASP A . n A 1 176 LEU 176 176 176 LEU LEU A . n A 1 177 ASP 177 177 177 ASP ASP A . n A 1 178 THR 178 178 178 THR THR A . n A 1 179 THR 179 179 179 THR THR A . n A 1 180 LYS 180 180 180 LYS LYS A . n A 1 181 ASP 181 181 181 ASP ASP A . n A 1 182 VAL 182 182 182 VAL VAL A . n A 1 183 VAL 183 183 183 VAL VAL A . n A 1 184 LYS 184 184 184 LYS LYS A . n A 1 185 ASN 185 185 185 ASN ASN A . n A 1 186 GLU 186 186 186 GLU GLU A . n A 1 187 TRP 187 187 187 TRP TRP A . n A 1 188 TYR 188 188 188 TYR TYR A . n A 1 189 ASP 189 189 189 ASP ASP A . n A 1 190 TRP 190 190 190 TRP TRP A . n A 1 191 VAL 191 191 191 VAL VAL A . n A 1 192 GLY 192 192 192 GLY GLY A . n A 1 193 SER 193 193 193 SER SER A . n A 1 194 LEU 194 194 194 LEU LEU A . n A 1 195 VAL 195 195 195 VAL VAL A . n A 1 196 SER 196 196 196 SER SER A . n A 1 197 ASN 197 197 197 ASN ASN A . n A 1 198 TYR 198 198 198 TYR TYR A . n A 1 199 SER 199 199 199 SER SER A . n A 1 200 ILE 200 200 200 ILE ILE A . n A 1 201 ASP 201 201 201 ASP ASP A . n A 1 202 GLY 202 202 202 GLY GLY A . n A 1 203 LEU 203 203 203 LEU LEU A . n A 1 204 ARG 204 204 204 ARG ARG A . n A 1 205 ILE 205 205 205 ILE ILE A . n A 1 206 ASP 206 206 206 ASP ASP A . n A 1 207 THR 207 207 207 THR THR A . n A 1 208 VAL 208 208 208 VAL VAL A . n A 1 209 LYS 209 209 209 LYS LYS A . n A 1 210 HIS 210 210 210 HIS HIS A . n A 1 211 VAL 211 211 211 VAL VAL A . n A 1 212 GLN 212 212 212 GLN GLN A . n A 1 213 LYS 213 213 213 LYS LYS A . n A 1 214 ASP 214 214 214 ASP ASP A . n A 1 215 PHE 215 215 215 PHE PHE A . n A 1 216 TRP 216 216 216 TRP TRP A . n A 1 217 PRO 217 217 217 PRO PRO A . n A 1 218 GLY 218 218 218 GLY GLY A . n A 1 219 TYR 219 219 219 TYR TYR A . n A 1 220 ASN 220 220 220 ASN ASN A . n A 1 221 LYS 221 221 221 LYS LYS A . n A 1 222 ALA 222 222 222 ALA ALA A . n A 1 223 ALA 223 223 223 ALA ALA A . n A 1 224 GLY 224 224 224 GLY GLY A . n A 1 225 VAL 225 225 225 VAL VAL A . n A 1 226 TYR 226 226 226 TYR TYR A . n A 1 227 CYS 227 227 227 CYS CYS A . n A 1 228 ILE 228 228 228 ILE ILE A . n A 1 229 GLY 229 229 229 GLY GLY A . n A 1 230 GLU 230 230 230 GLU GLU A . n A 1 231 VAL 231 231 231 VAL VAL A . n A 1 232 LEU 232 232 232 LEU LEU A . n A 1 233 ASP 233 233 233 ASP ASP A . n A 1 234 GLY 234 234 234 GLY GLY A . n A 1 235 ASP 235 235 235 ASP ASP A . n A 1 236 PRO 236 236 236 PRO PRO A . n A 1 237 ALA 237 237 237 ALA ALA A . n A 1 238 TYR 238 238 238 TYR TYR A . n A 1 239 THR 239 239 239 THR THR A . n A 1 240 CYS 240 240 240 CYS CYS A . n A 1 241 PRO 241 241 241 PRO PRO A . n A 1 242 TYR 242 242 242 TYR TYR A . n A 1 243 GLN 243 243 243 GLN GLN A . n A 1 244 ASN 244 244 244 ASN ASN A . n A 1 245 VAL 245 245 245 VAL VAL A . n A 1 246 MET 246 246 246 MET MET A . n A 1 247 ASP 247 247 247 ASP ASP A . n A 1 248 GLY 248 248 248 GLY GLY A . n A 1 249 VAL 249 249 249 VAL VAL A . n A 1 250 LEU 250 250 250 LEU LEU A . n A 1 251 ASN 251 251 251 ASN ASN A . n A 1 252 TYR 252 252 252 TYR TYR A . n A 1 253 PRO 253 253 253 PRO PRO A . n A 1 254 ILE 254 254 254 ILE ILE A . n A 1 255 TYR 255 255 255 TYR TYR A . n A 1 256 TYR 256 256 256 TYR TYR A . n A 1 257 PRO 257 257 257 PRO PRO A . n A 1 258 LEU 258 258 258 LEU LEU A . n A 1 259 LEU 259 259 259 LEU LEU A . n A 1 260 ASN 260 260 260 ASN ASN A . n A 1 261 ALA 261 261 261 ALA ALA A . n A 1 262 PHE 262 262 262 PHE PHE A . n A 1 263 LYS 263 263 263 LYS LYS A . n A 1 264 SER 264 264 264 SER SER A . n A 1 265 THR 265 265 265 THR THR A . n A 1 266 SER 266 266 266 SER SER A . n A 1 267 GLY 267 267 267 GLY GLY A . n A 1 268 SER 268 268 268 SER SER A . n A 1 269 MET 269 269 269 MET MET A . n A 1 270 ASP 270 270 270 ASP ASP A . n A 1 271 ASP 271 271 271 ASP ASP A . n A 1 272 LEU 272 272 272 LEU LEU A . n A 1 273 TYR 273 273 273 TYR TYR A . n A 1 274 ASN 274 274 274 ASN ASN A . n A 1 275 MET 275 275 275 MET MET A . n A 1 276 ILE 276 276 276 ILE ILE A . n A 1 277 ASN 277 277 277 ASN ASN A . n A 1 278 THR 278 278 278 THR THR A . n A 1 279 VAL 279 279 279 VAL VAL A . n A 1 280 LYS 280 280 280 LYS LYS A . n A 1 281 SER 281 281 281 SER SER A . n A 1 282 ASP 282 282 282 ASP ASP A . n A 1 283 CYS 283 283 283 CYS CYS A . n A 1 284 PRO 284 284 284 PRO PRO A . n A 1 285 ASP 285 285 285 ASP ASP A . n A 1 286 SER 286 286 286 SER SER A . n A 1 287 THR 287 287 287 THR THR A . n A 1 288 LEU 288 288 288 LEU LEU A . n A 1 289 LEU 289 289 289 LEU LEU A . n A 1 290 GLY 290 290 290 GLY GLY A . n A 1 291 THR 291 291 291 THR THR A . n A 1 292 PHE 292 292 292 PHE PHE A . n A 1 293 VAL 293 293 293 VAL VAL A . n A 1 294 GLU 294 294 294 GLU GLU A . n A 1 295 ASN 295 295 295 ASN ASN A . n A 1 296 HIS 296 296 296 HIS HIS A . n A 1 297 ASP 297 297 297 ASP ASP A . n A 1 298 ASN 298 298 298 ASN ASN A . n A 1 299 PRO 299 299 299 PRO PRO A . n A 1 300 ARG 300 300 300 ARG ARG A . n A 1 301 PHE 301 301 301 PHE PHE A . n A 1 302 ALA 302 302 302 ALA ALA A . n A 1 303 SER 303 303 303 SER SER A . n A 1 304 TYR 304 304 304 TYR TYR A . n A 1 305 THR 305 305 305 THR THR A . n A 1 306 ASN 306 306 306 ASN ASN A . n A 1 307 ASP 307 307 307 ASP ASP A . n A 1 308 ILE 308 308 308 ILE ILE A . n A 1 309 ALA 309 309 309 ALA ALA A . n A 1 310 LEU 310 310 310 LEU LEU A . n A 1 311 ALA 311 311 311 ALA ALA A . n A 1 312 LYS 312 312 312 LYS LYS A . n A 1 313 ASN 313 313 313 ASN ASN A . n A 1 314 VAL 314 314 314 VAL VAL A . n A 1 315 ALA 315 315 315 ALA ALA A . n A 1 316 ALA 316 316 316 ALA ALA A . n A 1 317 PHE 317 317 317 PHE PHE A . n A 1 318 ILE 318 318 318 ILE ILE A . n A 1 319 ILE 319 319 319 ILE ILE A . n A 1 320 LEU 320 320 320 LEU LEU A . n A 1 321 ASN 321 321 321 ASN ASN A . n A 1 322 ASP 322 322 322 ASP ASP A . n A 1 323 GLY 323 323 323 GLY GLY A . n A 1 324 ILE 324 324 324 ILE ILE A . n A 1 325 PRO 325 325 325 PRO PRO A . n A 1 326 ILE 326 326 326 ILE ILE A . n A 1 327 ILE 327 327 327 ILE ILE A . n A 1 328 TYR 328 328 328 TYR TYR A . n A 1 329 ALA 329 329 329 ALA ALA A . n A 1 330 GLY 330 330 330 GLY GLY A . n A 1 331 GLN 331 331 331 GLN GLN A . n A 1 332 GLU 332 332 332 GLU GLU A . n A 1 333 GLN 333 333 333 GLN GLN A . n A 1 334 HIS 334 334 334 HIS HIS A . n A 1 335 TYR 335 335 335 TYR TYR A . n A 1 336 ALA 336 336 336 ALA ALA A . n A 1 337 GLY 337 337 337 GLY GLY A . n A 1 338 GLY 338 338 338 GLY GLY A . n A 1 339 ASN 339 339 339 ASN ASN A . n A 1 340 ASP 340 340 340 ASP ASP A . n A 1 341 PRO 341 341 341 PRO PRO A . n A 1 342 ALA 342 342 342 ALA ALA A . n A 1 343 ASN 343 343 343 ASN ASN A . n A 1 344 ARG 344 344 344 ARG ARG A . n A 1 345 GLU 345 345 345 GLU GLU A . n A 1 346 ALA 346 346 346 ALA ALA A . n A 1 347 THR 347 347 347 THR THR A . n A 1 348 TRP 348 348 348 TRP TRP A . n A 1 349 LEU 349 349 349 LEU LEU A . n A 1 350 SER 350 350 350 SER SER A . n A 1 351 GLY 351 351 351 GLY GLY A . n A 1 352 TYR 352 352 352 TYR TYR A . n A 1 353 PRO 353 353 353 PRO PRO A . n A 1 354 THR 354 354 354 THR THR A . n A 1 355 ASP 355 355 355 ASP ASP A . n A 1 356 SER 356 356 356 SER SER A . n A 1 357 GLU 357 357 357 GLU GLU A . n A 1 358 LEU 358 358 358 LEU LEU A . n A 1 359 TYR 359 359 359 TYR TYR A . n A 1 360 LYS 360 360 360 LYS LYS A . n A 1 361 LEU 361 361 361 LEU LEU A . n A 1 362 ILE 362 362 362 ILE ILE A . n A 1 363 ALA 363 363 363 ALA ALA A . n A 1 364 SER 364 364 364 SER SER A . n A 1 365 ALA 365 365 365 ALA ALA A . n A 1 366 ASN 366 366 366 ASN ASN A . n A 1 367 ALA 367 367 367 ALA ALA A . n A 1 368 ILE 368 368 368 ILE ILE A . n A 1 369 ARG 369 369 369 ARG ARG A . n A 1 370 ASN 370 370 370 ASN ASN A . n A 1 371 TYR 371 371 371 TYR TYR A . n A 1 372 ALA 372 372 372 ALA ALA A . n A 1 373 ILE 373 373 373 ILE ILE A . n A 1 374 SER 374 374 374 SER SER A . n A 1 375 LYS 375 375 375 LYS LYS A . n A 1 376 ASP 376 376 376 ASP ASP A . n A 1 377 THR 377 377 377 THR THR A . n A 1 378 GLY 378 378 378 GLY GLY A . n A 1 379 PHE 379 379 379 PHE PHE A . n A 1 380 VAL 380 380 380 VAL VAL A . n A 1 381 THR 381 381 381 THR THR A . n A 1 382 TYR 382 382 382 TYR TYR A . n A 1 383 LYS 383 383 383 LYS LYS A . n A 1 384 ASN 384 384 384 ASN ASN A . n A 1 385 TRP 385 385 385 TRP TRP A . n A 1 386 PRO 386 386 386 PRO PRO A . n A 1 387 ILE 387 387 387 ILE ILE A . n A 1 388 TYR 388 388 388 TYR TYR A . n A 1 389 LYS 389 389 389 LYS LYS A . n A 1 390 ASP 390 390 390 ASP ASP A . n A 1 391 ASP 391 391 391 ASP ASP A . n A 1 392 THR 392 392 392 THR THR A . n A 1 393 THR 393 393 393 THR THR A . n A 1 394 ILE 394 394 394 ILE ILE A . n A 1 395 ALA 395 395 395 ALA ALA A . n A 1 396 MET 396 396 396 MET MET A . n A 1 397 ARG 397 397 397 ARG ARG A . n A 1 398 LYS 398 398 398 LYS LYS A . n A 1 399 GLY 399 399 399 GLY GLY A . n A 1 400 THR 400 400 400 THR THR A . n A 1 401 ASP 401 401 401 ASP ASP A . n A 1 402 GLY 402 402 402 GLY GLY A . n A 1 403 SER 403 403 403 SER SER A . n A 1 404 GLN 404 404 404 GLN GLN A . n A 1 405 ILE 405 405 405 ILE ILE A . n A 1 406 VAL 406 406 406 VAL VAL A . n A 1 407 THR 407 407 407 THR THR A . n A 1 408 ILE 408 408 408 ILE ILE A . n A 1 409 LEU 409 409 409 LEU LEU A . n A 1 410 SER 410 410 410 SER SER A . n A 1 411 ASN 411 411 411 ASN ASN A . n A 1 412 LYS 412 412 412 LYS LYS A . n A 1 413 GLY 413 413 413 GLY GLY A . n A 1 414 ALA 414 414 414 ALA ALA A . n A 1 415 SER 415 415 415 SER SER A . n A 1 416 GLY 416 416 416 GLY GLY A . n A 1 417 ASP 417 417 417 ASP ASP A . n A 1 418 SER 418 418 418 SER SER A . n A 1 419 TYR 419 419 419 TYR TYR A . n A 1 420 THR 420 420 420 THR THR A . n A 1 421 LEU 421 421 421 LEU LEU A . n A 1 422 SER 422 422 422 SER SER A . n A 1 423 LEU 423 423 423 LEU LEU A . n A 1 424 SER 424 424 424 SER SER A . n A 1 425 GLY 425 425 425 GLY GLY A . n A 1 426 ALA 426 426 426 ALA ALA A . n A 1 427 GLY 427 427 427 GLY GLY A . n A 1 428 TYR 428 428 428 TYR TYR A . n A 1 429 THR 429 429 429 THR THR A . n A 1 430 ALA 430 430 430 ALA ALA A . n A 1 431 GLY 431 431 431 GLY GLY A . n A 1 432 GLN 432 432 432 GLN GLN A . n A 1 433 GLN 433 433 433 GLN GLN A . n A 1 434 LEU 434 434 434 LEU LEU A . n A 1 435 THR 435 435 435 THR THR A . n A 1 436 GLU 436 436 436 GLU GLU A . n A 1 437 VAL 437 437 437 VAL VAL A . n A 1 438 ILE 438 438 438 ILE ILE A . n A 1 439 GLY 439 439 439 GLY GLY A . n A 1 440 CYS 440 440 440 CYS CYS A . n A 1 441 THR 441 441 441 THR THR A . n A 1 442 THR 442 442 442 THR THR A . n A 1 443 VAL 443 443 443 VAL VAL A . n A 1 444 THR 444 444 444 THR THR A . n A 1 445 VAL 445 445 445 VAL VAL A . n A 1 446 GLY 446 446 446 GLY GLY A . n A 1 447 SER 447 447 447 SER SER A . n A 1 448 ASP 448 448 448 ASP ASP A . n A 1 449 GLY 449 449 449 GLY GLY A . n A 1 450 ASN 450 450 450 ASN ASN A . n A 1 451 VAL 451 451 451 VAL VAL A . n A 1 452 PRO 452 452 452 PRO PRO A . n A 1 453 VAL 453 453 453 VAL VAL A . n A 1 454 PRO 454 454 454 PRO PRO A . n A 1 455 MET 455 455 455 MET MET A . n A 1 456 ALA 456 456 456 ALA ALA A . n A 1 457 GLY 457 457 457 GLY GLY A . n A 1 458 GLY 458 458 458 GLY GLY A . n A 1 459 LEU 459 459 459 LEU LEU A . n A 1 460 PRO 460 460 460 PRO PRO A . n A 1 461 ARG 461 461 461 ARG ARG A . n A 1 462 VAL 462 462 462 VAL VAL A . n A 1 463 LEU 463 463 463 LEU LEU A . n A 1 464 TYR 464 464 464 TYR TYR A . n A 1 465 PRO 465 465 465 PRO PRO A . n A 1 466 THR 466 466 466 THR THR A . n A 1 467 GLU 467 467 467 GLU GLU A . n A 1 468 LYS 468 468 468 LYS LYS A . n A 1 469 LEU 469 469 469 LEU LEU A . n A 1 470 ALA 470 470 470 ALA ALA A . n A 1 471 GLY 471 471 471 GLY GLY A . n A 1 472 SER 472 472 472 SER SER A . n A 1 473 LYS 473 473 473 LYS LYS A . n A 1 474 ILE 474 474 474 ILE ILE A . n A 1 475 CYS 475 475 475 CYS CYS A . n A 1 476 SER 476 476 476 SER SER A . n A 1 477 SER 477 477 ? ? ? A . n A 1 478 SER 478 478 ? ? ? A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 1000 1000 NAG NAG A . C 2 NAG 2 1001 1001 NAG NAG A . D 3 BMA 3 1002 1002 BMA MAN A . E 4 CA 1 601 1 CA CA A . F 5 HOH 1 1003 1 HOH HOH A . F 5 HOH 2 1004 2 HOH HOH A . F 5 HOH 3 1005 3 HOH HOH A . F 5 HOH 4 1006 4 HOH HOH A . F 5 HOH 5 1007 5 HOH HOH A . F 5 HOH 6 1008 6 HOH HOH A . F 5 HOH 7 1009 7 HOH HOH A . F 5 HOH 8 1010 8 HOH HOH A . F 5 HOH 9 1011 9 HOH HOH A . F 5 HOH 10 1012 10 HOH HOH A . F 5 HOH 11 1013 11 HOH HOH A . F 5 HOH 12 1014 12 HOH HOH A . F 5 HOH 13 1015 13 HOH HOH A . F 5 HOH 14 1016 14 HOH HOH A . F 5 HOH 15 1017 15 HOH HOH A . F 5 HOH 16 1018 16 HOH HOH A . F 5 HOH 17 1019 17 HOH HOH A . F 5 HOH 18 1020 18 HOH HOH A . F 5 HOH 19 1021 19 HOH HOH A . F 5 HOH 20 1022 20 HOH HOH A . F 5 HOH 21 1023 21 HOH HOH A . F 5 HOH 22 1024 22 HOH HOH A . F 5 HOH 23 1025 23 HOH HOH A . F 5 HOH 24 1026 24 HOH HOH A . F 5 HOH 25 1027 25 HOH HOH A . F 5 HOH 26 1028 26 HOH HOH A . F 5 HOH 27 1029 27 HOH HOH A . F 5 HOH 28 1030 28 HOH HOH A . F 5 HOH 29 1031 29 HOH HOH A . F 5 HOH 30 1032 30 HOH HOH A . F 5 HOH 31 1033 31 HOH HOH A . F 5 HOH 32 1034 32 HOH HOH A . F 5 HOH 33 1035 33 HOH HOH A . F 5 HOH 34 1036 34 HOH HOH A . F 5 HOH 35 1037 35 HOH HOH A . F 5 HOH 36 1038 36 HOH HOH A . F 5 HOH 37 1039 37 HOH HOH A . F 5 HOH 38 1040 38 HOH HOH A . F 5 HOH 39 1041 39 HOH HOH A . F 5 HOH 40 1042 40 HOH HOH A . F 5 HOH 41 1043 41 HOH HOH A . F 5 HOH 42 1044 42 HOH HOH A . F 5 HOH 43 1045 43 HOH HOH A . F 5 HOH 44 1046 44 HOH HOH A . F 5 HOH 45 1047 45 HOH HOH A . F 5 HOH 46 1048 46 HOH HOH A . F 5 HOH 47 1049 47 HOH HOH A . F 5 HOH 48 1050 48 HOH HOH A . F 5 HOH 49 1051 49 HOH HOH A . F 5 HOH 50 1052 50 HOH HOH A . F 5 HOH 51 1053 51 HOH HOH A . F 5 HOH 52 1054 52 HOH HOH A . F 5 HOH 53 1055 53 HOH HOH A . F 5 HOH 54 1056 54 HOH HOH A . F 5 HOH 55 1057 55 HOH HOH A . F 5 HOH 56 1058 56 HOH HOH A . F 5 HOH 57 1059 57 HOH HOH A . F 5 HOH 58 1060 58 HOH HOH A . F 5 HOH 59 1061 59 HOH HOH A . F 5 HOH 60 1062 60 HOH HOH A . F 5 HOH 61 1063 61 HOH HOH A . F 5 HOH 62 1064 62 HOH HOH A . F 5 HOH 63 1065 63 HOH HOH A . F 5 HOH 64 1066 64 HOH HOH A . F 5 HOH 65 1067 65 HOH HOH A . F 5 HOH 66 1068 66 HOH HOH A . F 5 HOH 67 1069 67 HOH HOH A . F 5 HOH 68 1070 68 HOH HOH A . F 5 HOH 69 1071 69 HOH HOH A . F 5 HOH 70 1072 70 HOH HOH A . F 5 HOH 71 1073 71 HOH HOH A . F 5 HOH 72 1074 72 HOH HOH A . F 5 HOH 73 1075 73 HOH HOH A . F 5 HOH 74 1076 74 HOH HOH A . F 5 HOH 75 1077 75 HOH HOH A . F 5 HOH 76 1078 76 HOH HOH A . F 5 HOH 77 1079 77 HOH HOH A . F 5 HOH 78 1080 78 HOH HOH A . F 5 HOH 79 1081 79 HOH HOH A . F 5 HOH 80 1082 80 HOH HOH A . F 5 HOH 81 1083 81 HOH HOH A . F 5 HOH 82 1084 82 HOH HOH A . F 5 HOH 83 1085 83 HOH HOH A . F 5 HOH 84 1086 84 HOH HOH A . F 5 HOH 85 1087 85 HOH HOH A . F 5 HOH 86 1088 86 HOH HOH A . F 5 HOH 87 1089 87 HOH HOH A . F 5 HOH 88 1090 88 HOH HOH A . F 5 HOH 89 1091 89 HOH HOH A . F 5 HOH 90 1092 90 HOH HOH A . F 5 HOH 91 1093 91 HOH HOH A . F 5 HOH 92 1094 92 HOH HOH A . F 5 HOH 93 1095 93 HOH HOH A . F 5 HOH 94 1096 94 HOH HOH A . F 5 HOH 95 1097 95 HOH HOH A . F 5 HOH 96 1098 96 HOH HOH A . F 5 HOH 97 1099 97 HOH HOH A . F 5 HOH 98 1100 98 HOH HOH A . F 5 HOH 99 1101 99 HOH HOH A . F 5 HOH 100 1102 100 HOH HOH A . F 5 HOH 101 1103 101 HOH HOH A . F 5 HOH 102 1104 102 HOH HOH A . F 5 HOH 103 1105 103 HOH HOH A . F 5 HOH 104 1106 104 HOH HOH A . F 5 HOH 105 1107 105 HOH HOH A . F 5 HOH 106 1108 106 HOH HOH A . F 5 HOH 107 1109 107 HOH HOH A . F 5 HOH 108 1110 108 HOH HOH A . F 5 HOH 109 1111 109 HOH HOH A . F 5 HOH 110 1112 110 HOH HOH A . F 5 HOH 111 1113 111 HOH HOH A . F 5 HOH 112 1114 112 HOH HOH A . F 5 HOH 113 1115 113 HOH HOH A . F 5 HOH 114 1116 114 HOH HOH A . F 5 HOH 115 1117 115 HOH HOH A . F 5 HOH 116 1118 116 HOH HOH A . F 5 HOH 117 1119 117 HOH HOH A . F 5 HOH 118 1120 118 HOH HOH A . F 5 HOH 119 1121 119 HOH HOH A . F 5 HOH 120 1122 120 HOH HOH A . F 5 HOH 121 1123 121 HOH HOH A . F 5 HOH 122 1124 122 HOH HOH A . F 5 HOH 123 1125 123 HOH HOH A . F 5 HOH 124 1126 124 HOH HOH A . F 5 HOH 125 1127 125 HOH HOH A . F 5 HOH 126 1128 126 HOH HOH A . F 5 HOH 127 1129 127 HOH HOH A . F 5 HOH 128 1130 128 HOH HOH A . F 5 HOH 129 1131 129 HOH HOH A . F 5 HOH 130 1132 130 HOH HOH A . F 5 HOH 131 1133 131 HOH HOH A . F 5 HOH 132 1134 132 HOH HOH A . F 5 HOH 133 1135 133 HOH HOH A . F 5 HOH 134 1136 134 HOH HOH A . F 5 HOH 135 1137 135 HOH HOH A . F 5 HOH 136 1138 136 HOH HOH A . F 5 HOH 137 1139 137 HOH HOH A . F 5 HOH 138 1140 138 HOH HOH A . F 5 HOH 139 1141 139 HOH HOH A . F 5 HOH 140 1142 140 HOH HOH A . F 5 HOH 141 1143 141 HOH HOH A . F 5 HOH 142 1144 142 HOH HOH A . F 5 HOH 143 1145 143 HOH HOH A . F 5 HOH 144 1146 144 HOH HOH A . F 5 HOH 145 1147 145 HOH HOH A . F 5 HOH 146 1148 146 HOH HOH A . F 5 HOH 147 1149 147 HOH HOH A . F 5 HOH 148 1150 148 HOH HOH A . F 5 HOH 149 1151 149 HOH HOH A . F 5 HOH 150 1152 150 HOH HOH A . F 5 HOH 151 1153 151 HOH HOH A . F 5 HOH 152 1154 152 HOH HOH A . F 5 HOH 153 1155 153 HOH HOH A . F 5 HOH 154 1156 154 HOH HOH A . F 5 HOH 155 1157 155 HOH HOH A . F 5 HOH 156 1158 156 HOH HOH A . F 5 HOH 157 1159 157 HOH HOH A . F 5 HOH 158 1160 158 HOH HOH A . F 5 HOH 159 1161 159 HOH HOH A . F 5 HOH 160 1162 160 HOH HOH A . F 5 HOH 161 1163 161 HOH HOH A . F 5 HOH 162 1164 162 HOH HOH A . F 5 HOH 163 1165 163 HOH HOH A . F 5 HOH 164 1166 164 HOH HOH A . F 5 HOH 165 1167 165 HOH HOH A . F 5 HOH 166 1168 166 HOH HOH A . F 5 HOH 167 1169 167 HOH HOH A . F 5 HOH 168 1170 168 HOH HOH A . F 5 HOH 169 1171 169 HOH HOH A . F 5 HOH 170 1172 170 HOH HOH A . F 5 HOH 171 1173 171 HOH HOH A . F 5 HOH 172 1174 172 HOH HOH A . F 5 HOH 173 1175 173 HOH HOH A . F 5 HOH 174 1176 174 HOH HOH A . F 5 HOH 175 1177 175 HOH HOH A . F 5 HOH 176 1178 176 HOH HOH A . F 5 HOH 177 1179 177 HOH HOH A . F 5 HOH 178 1180 178 HOH HOH A . F 5 HOH 179 1181 179 HOH HOH A . F 5 HOH 180 1182 180 HOH HOH A . F 5 HOH 181 1183 181 HOH HOH A . F 5 HOH 182 1184 182 HOH HOH A . F 5 HOH 183 1185 183 HOH HOH A . F 5 HOH 184 1186 184 HOH HOH A . F 5 HOH 185 1187 185 HOH HOH A . F 5 HOH 186 1188 186 HOH HOH A . F 5 HOH 187 1189 187 HOH HOH A . F 5 HOH 188 1190 188 HOH HOH A . F 5 HOH 189 1191 189 HOH HOH A . F 5 HOH 190 1192 190 HOH HOH A . F 5 HOH 191 1193 191 HOH HOH A . F 5 HOH 192 1194 192 HOH HOH A . F 5 HOH 193 1195 193 HOH HOH A . F 5 HOH 194 1196 194 HOH HOH A . F 5 HOH 195 1197 195 HOH HOH A . F 5 HOH 196 1198 196 HOH HOH A . F 5 HOH 197 1199 197 HOH HOH A . F 5 HOH 198 1200 198 HOH HOH A . F 5 HOH 199 1201 199 HOH HOH A . F 5 HOH 200 1202 200 HOH HOH A . F 5 HOH 201 1203 201 HOH HOH A . F 5 HOH 202 1204 202 HOH HOH A . F 5 HOH 203 1205 203 HOH HOH A . F 5 HOH 204 1206 204 HOH HOH A . F 5 HOH 205 1207 205 HOH HOH A . F 5 HOH 206 1208 206 HOH HOH A . F 5 HOH 207 1209 207 HOH HOH A . F 5 HOH 208 1210 208 HOH HOH A . F 5 HOH 209 1211 209 HOH HOH A . F 5 HOH 210 1212 210 HOH HOH A . F 5 HOH 211 1213 211 HOH HOH A . F 5 HOH 212 1214 212 HOH HOH A . F 5 HOH 213 1215 213 HOH HOH A . F 5 HOH 214 1216 214 HOH HOH A . F 5 HOH 215 1217 215 HOH HOH A . F 5 HOH 216 1218 216 HOH HOH A . F 5 HOH 217 1219 217 HOH HOH A . F 5 HOH 218 1220 218 HOH HOH A . F 5 HOH 219 1221 219 HOH HOH A . F 5 HOH 220 1222 220 HOH HOH A . F 5 HOH 221 1223 221 HOH HOH A . F 5 HOH 222 1224 222 HOH HOH A . F 5 HOH 223 1225 223 HOH HOH A . F 5 HOH 224 1226 224 HOH HOH A . F 5 HOH 225 1227 225 HOH HOH A . F 5 HOH 226 1228 226 HOH HOH A . F 5 HOH 227 1229 227 HOH HOH A . F 5 HOH 228 1230 228 HOH HOH A . F 5 HOH 229 1231 229 HOH HOH A . F 5 HOH 230 1232 230 HOH HOH A . F 5 HOH 231 1233 231 HOH HOH A . F 5 HOH 232 1234 232 HOH HOH A . F 5 HOH 233 1235 233 HOH HOH A . F 5 HOH 234 1236 234 HOH HOH A . F 5 HOH 235 1237 235 HOH HOH A . F 5 HOH 236 1238 236 HOH HOH A . F 5 HOH 237 1239 237 HOH HOH A . F 5 HOH 238 1240 238 HOH HOH A . F 5 HOH 239 1241 239 HOH HOH A . F 5 HOH 240 1242 240 HOH HOH A . F 5 HOH 241 1243 241 HOH HOH A . F 5 HOH 242 1244 242 HOH HOH A . F 5 HOH 243 1245 243 HOH HOH A . F 5 HOH 244 1246 244 HOH HOH A . F 5 HOH 245 1247 245 HOH HOH A . F 5 HOH 246 1248 246 HOH HOH A . F 5 HOH 247 1249 247 HOH HOH A . F 5 HOH 248 1250 248 HOH HOH A . F 5 HOH 249 1251 249 HOH HOH A . F 5 HOH 250 1252 250 HOH HOH A . F 5 HOH 251 1253 251 HOH HOH A . F 5 HOH 252 1254 252 HOH HOH A . F 5 HOH 253 1255 253 HOH HOH A . F 5 HOH 254 1256 254 HOH HOH A . F 5 HOH 255 1257 255 HOH HOH A . F 5 HOH 256 1258 256 HOH HOH A . F 5 HOH 257 1259 257 HOH HOH A . F 5 HOH 258 1260 258 HOH HOH A . F 5 HOH 259 1261 259 HOH HOH A . F 5 HOH 260 1262 260 HOH HOH A . F 5 HOH 261 1263 261 HOH HOH A . F 5 HOH 262 1264 262 HOH HOH A . F 5 HOH 263 1265 263 HOH HOH A . F 5 HOH 264 1266 264 HOH HOH A . F 5 HOH 265 1267 265 HOH HOH A . F 5 HOH 266 1268 266 HOH HOH A . F 5 HOH 267 1269 267 HOH HOH A . F 5 HOH 268 1270 268 HOH HOH A . F 5 HOH 269 1271 269 HOH HOH A . F 5 HOH 270 1272 270 HOH HOH A . F 5 HOH 271 1273 271 HOH HOH A . F 5 HOH 272 1274 272 HOH HOH A . F 5 HOH 273 1275 273 HOH HOH A . F 5 HOH 274 1276 274 HOH HOH A . F 5 HOH 275 1277 275 HOH HOH A . F 5 HOH 276 1278 276 HOH HOH A . F 5 HOH 277 1279 277 HOH HOH A . F 5 HOH 278 1280 278 HOH HOH A . F 5 HOH 279 1281 279 HOH HOH A . F 5 HOH 280 1282 280 HOH HOH A . F 5 HOH 281 1283 281 HOH HOH A . F 5 HOH 282 1284 282 HOH HOH A . F 5 HOH 283 1285 283 HOH HOH A . F 5 HOH 284 1286 284 HOH HOH A . F 5 HOH 285 1287 285 HOH HOH A . F 5 HOH 286 1288 286 HOH HOH A . F 5 HOH 287 1289 287 HOH HOH A . F 5 HOH 288 1290 288 HOH HOH A . F 5 HOH 289 1291 289 HOH HOH A . F 5 HOH 290 1292 290 HOH HOH A . F 5 HOH 291 1293 291 HOH HOH A . F 5 HOH 292 1294 292 HOH HOH A . F 5 HOH 293 1295 293 HOH HOH A . F 5 HOH 294 1296 294 HOH HOH A . F 5 HOH 295 1297 295 HOH HOH A . F 5 HOH 296 1298 296 HOH HOH A . F 5 HOH 297 1299 297 HOH HOH A . F 5 HOH 298 1300 298 HOH HOH A . F 5 HOH 299 1301 299 HOH HOH A . F 5 HOH 300 1302 300 HOH HOH A . F 5 HOH 301 1303 301 HOH HOH A . F 5 HOH 302 1304 302 HOH HOH A . F 5 HOH 303 1305 303 HOH HOH A . F 5 HOH 304 1306 304 HOH HOH A . F 5 HOH 305 1307 305 HOH HOH A . F 5 HOH 306 1308 306 HOH HOH A . F 5 HOH 307 1309 307 HOH HOH A . F 5 HOH 308 1310 308 HOH HOH A . F 5 HOH 309 1311 309 HOH HOH A . F 5 HOH 310 1312 310 HOH HOH A . F 5 HOH 311 1313 311 HOH HOH A . F 5 HOH 312 1314 312 HOH HOH A . F 5 HOH 313 1315 313 HOH HOH A . F 5 HOH 314 1316 314 HOH HOH A . F 5 HOH 315 1317 315 HOH HOH A . F 5 HOH 316 1318 316 HOH HOH A . F 5 HOH 317 1319 317 HOH HOH A . F 5 HOH 318 1320 318 HOH HOH A . F 5 HOH 319 1321 319 HOH HOH A . F 5 HOH 320 1322 320 HOH HOH A . F 5 HOH 321 1323 321 HOH HOH A . F 5 HOH 322 1324 322 HOH HOH A . F 5 HOH 323 1325 323 HOH HOH A . F 5 HOH 324 1326 324 HOH HOH A . F 5 HOH 325 1327 325 HOH HOH A . F 5 HOH 326 1328 326 HOH HOH A . F 5 HOH 327 1329 327 HOH HOH A . F 5 HOH 328 1330 328 HOH HOH A . F 5 HOH 329 1331 329 HOH HOH A . F 5 HOH 330 1332 330 HOH HOH A . F 5 HOH 331 1333 331 HOH HOH A . F 5 HOH 332 1334 332 HOH HOH A . F 5 HOH 333 1335 333 HOH HOH A . F 5 HOH 334 1336 334 HOH HOH A . F 5 HOH 335 1337 335 HOH HOH A . F 5 HOH 336 1338 336 HOH HOH A . F 5 HOH 337 1339 337 HOH HOH A . F 5 HOH 338 1340 338 HOH HOH A . F 5 HOH 339 1341 339 HOH HOH A . F 5 HOH 340 1342 340 HOH HOH A . F 5 HOH 341 1343 341 HOH HOH A . F 5 HOH 342 1344 342 HOH HOH A . F 5 HOH 343 1345 343 HOH HOH A . F 5 HOH 344 1346 344 HOH HOH A . F 5 HOH 345 1347 345 HOH HOH A . F 5 HOH 346 1348 346 HOH HOH A . F 5 HOH 347 1349 347 HOH HOH A . F 5 HOH 348 1350 348 HOH HOH A . F 5 HOH 349 1351 349 HOH HOH A . F 5 HOH 350 1352 350 HOH HOH A . F 5 HOH 351 1353 351 HOH HOH A . F 5 HOH 352 1354 352 HOH HOH A . F 5 HOH 353 1355 353 HOH HOH A . F 5 HOH 354 1356 354 HOH HOH A . F 5 HOH 355 1357 355 HOH HOH A . F 5 HOH 356 1358 356 HOH HOH A . F 5 HOH 357 1359 357 HOH HOH A . F 5 HOH 358 1360 358 HOH HOH A . F 5 HOH 359 1361 359 HOH HOH A . F 5 HOH 360 1362 360 HOH HOH A . F 5 HOH 361 1363 361 HOH HOH A . F 5 HOH 362 1364 362 HOH HOH A . F 5 HOH 363 1365 363 HOH HOH A . F 5 HOH 364 1366 364 HOH HOH A . F 5 HOH 365 1367 365 HOH HOH A . F 5 HOH 366 1368 366 HOH HOH A . F 5 HOH 367 1369 367 HOH HOH A . F 5 HOH 368 1370 368 HOH HOH A . F 5 HOH 369 1371 369 HOH HOH A . F 5 HOH 370 1372 370 HOH HOH A . F 5 HOH 371 1373 371 HOH HOH A . F 5 HOH 372 1374 372 HOH HOH A . F 5 HOH 373 1375 373 HOH HOH A . F 5 HOH 374 1376 374 HOH HOH A . F 5 HOH 375 1377 375 HOH HOH A . F 5 HOH 376 1378 376 HOH HOH A . F 5 HOH 377 1379 377 HOH HOH A . F 5 HOH 378 1380 378 HOH HOH A . F 5 HOH 379 1381 379 HOH HOH A . F 5 HOH 380 1382 380 HOH HOH A . F 5 HOH 381 1383 381 HOH HOH A . F 5 HOH 382 1384 382 HOH HOH A . F 5 HOH 383 1385 383 HOH HOH A . F 5 HOH 384 1386 384 HOH HOH A . F 5 HOH 385 1387 385 HOH HOH A . F 5 HOH 386 1388 386 HOH HOH A . F 5 HOH 387 1389 387 HOH HOH A . F 5 HOH 388 1390 388 HOH HOH A . F 5 HOH 389 1391 389 HOH HOH A . F 5 HOH 390 1392 390 HOH HOH A . F 5 HOH 391 1393 391 HOH HOH A . F 5 HOH 392 1394 392 HOH HOH A . F 5 HOH 393 1395 393 HOH HOH A . F 5 HOH 394 1396 394 HOH HOH A . F 5 HOH 395 1397 395 HOH HOH A . F 5 HOH 396 1398 396 HOH HOH A . F 5 HOH 397 1399 397 HOH HOH A . F 5 HOH 398 1400 398 HOH HOH A . F 5 HOH 399 1401 399 HOH HOH A . F 5 HOH 400 1402 400 HOH HOH A . F 5 HOH 401 1403 401 HOH HOH A . F 5 HOH 402 1404 402 HOH HOH A . F 5 HOH 403 1405 403 HOH HOH A . F 5 HOH 404 1406 404 HOH HOH A . F 5 HOH 405 1407 405 HOH HOH A . F 5 HOH 406 1408 406 HOH HOH A . F 5 HOH 407 1409 407 HOH HOH A . F 5 HOH 408 1410 408 HOH HOH A . F 5 HOH 409 1411 409 HOH HOH A . F 5 HOH 410 1412 410 HOH HOH A . F 5 HOH 411 1413 411 HOH HOH A . F 5 HOH 412 1414 412 HOH HOH A . F 5 HOH 413 1415 413 HOH HOH A . F 5 HOH 414 1416 414 HOH HOH A . F 5 HOH 415 1417 415 HOH HOH A . F 5 HOH 416 1418 416 HOH HOH A . F 5 HOH 417 1419 417 HOH HOH A . F 5 HOH 418 1420 418 HOH HOH A . F 5 HOH 419 1421 419 HOH HOH A . F 5 HOH 420 1422 420 HOH HOH A . F 5 HOH 421 1423 421 HOH HOH A . F 5 HOH 422 1424 422 HOH HOH A . F 5 HOH 423 1425 423 HOH HOH A . F 5 HOH 424 1426 424 HOH HOH A . F 5 HOH 425 1427 425 HOH HOH A . F 5 HOH 426 1428 426 HOH HOH A . F 5 HOH 427 1429 427 HOH HOH A . F 5 HOH 428 1430 428 HOH HOH A . F 5 HOH 429 1431 429 HOH HOH A . F 5 HOH 430 1432 430 HOH HOH A . F 5 HOH 431 1433 431 HOH HOH A . F 5 HOH 432 1434 432 HOH HOH A . F 5 HOH 433 1435 433 HOH HOH A . F 5 HOH 434 1436 434 HOH HOH A . F 5 HOH 435 1437 435 HOH HOH A . F 5 HOH 436 1438 436 HOH HOH A . F 5 HOH 437 1439 437 HOH HOH A . F 5 HOH 438 1440 438 HOH HOH A . F 5 HOH 439 1441 439 HOH HOH A . F 5 HOH 440 1442 440 HOH HOH A . F 5 HOH 441 1443 441 HOH HOH A . F 5 HOH 442 1444 442 HOH HOH A . F 5 HOH 443 1445 443 HOH HOH A . F 5 HOH 444 1446 444 HOH HOH A . F 5 HOH 445 1447 445 HOH HOH A . F 5 HOH 446 1448 446 HOH HOH A . F 5 HOH 447 1449 447 HOH HOH A . F 5 HOH 448 1450 448 HOH HOH A . F 5 HOH 449 1451 449 HOH HOH A . F 5 HOH 450 1452 450 HOH HOH A . F 5 HOH 451 1453 451 HOH HOH A . F 5 HOH 452 1454 452 HOH HOH A . F 5 HOH 453 1455 453 HOH HOH A . F 5 HOH 454 1456 454 HOH HOH A . F 5 HOH 455 1457 455 HOH HOH A . F 5 HOH 456 1458 456 HOH HOH A . F 5 HOH 457 1459 457 HOH HOH A . F 5 HOH 458 1460 458 HOH HOH A . F 5 HOH 459 1461 459 HOH HOH A . F 5 HOH 460 1462 460 HOH HOH A . F 5 HOH 461 1463 461 HOH HOH A . F 5 HOH 462 1464 462 HOH HOH A . F 5 HOH 463 1465 463 HOH HOH A . F 5 HOH 464 1466 464 HOH HOH A . F 5 HOH 465 1467 465 HOH HOH A . F 5 HOH 466 1468 466 HOH HOH A . F 5 HOH 467 1469 467 HOH HOH A . F 5 HOH 468 1470 468 HOH HOH A . F 5 HOH 469 1471 469 HOH HOH A . F 5 HOH 470 1472 470 HOH HOH A . F 5 HOH 471 1473 471 HOH HOH A . F 5 HOH 472 1474 472 HOH HOH A . F 5 HOH 473 1475 473 HOH HOH A . F 5 HOH 474 1476 474 HOH HOH A . F 5 HOH 475 1477 475 HOH HOH A . F 5 HOH 476 1478 476 HOH HOH A . F 5 HOH 477 1479 477 HOH HOH A . F 5 HOH 478 1480 478 HOH HOH A . F 5 HOH 479 1481 479 HOH HOH A . F 5 HOH 480 1482 480 HOH HOH A . F 5 HOH 481 1483 481 HOH HOH A . F 5 HOH 482 1484 482 HOH HOH A . F 5 HOH 483 1485 483 HOH HOH A . F 5 HOH 484 1486 484 HOH HOH A . F 5 HOH 485 1487 485 HOH HOH A . F 5 HOH 486 1488 486 HOH HOH A . F 5 HOH 487 1489 487 HOH HOH A . F 5 HOH 488 1490 488 HOH HOH A . F 5 HOH 489 1491 489 HOH HOH A . F 5 HOH 490 1492 490 HOH HOH A . F 5 HOH 491 1493 491 HOH HOH A . F 5 HOH 492 1494 492 HOH HOH A . F 5 HOH 493 1495 493 HOH HOH A . F 5 HOH 494 1496 494 HOH HOH A . F 5 HOH 495 1497 495 HOH HOH A . F 5 HOH 496 1498 496 HOH HOH A . F 5 HOH 497 1499 497 HOH HOH A . F 5 HOH 498 1500 498 HOH HOH A . F 5 HOH 499 1501 499 HOH HOH A . F 5 HOH 500 1502 500 HOH HOH A . F 5 HOH 501 1503 501 HOH HOH A . F 5 HOH 502 1504 502 HOH HOH A . F 5 HOH 503 1505 503 HOH HOH A . F 5 HOH 504 1506 504 HOH HOH A . F 5 HOH 505 1507 505 HOH HOH A . F 5 HOH 506 1508 506 HOH HOH A . F 5 HOH 507 1509 507 HOH HOH A . F 5 HOH 508 1510 508 HOH HOH A . F 5 HOH 509 1511 509 HOH HOH A . F 5 HOH 510 1512 510 HOH HOH A . F 5 HOH 511 1513 511 HOH HOH A . F 5 HOH 512 1514 512 HOH HOH A . F 5 HOH 513 1515 513 HOH HOH A . F 5 HOH 514 1516 514 HOH HOH A . F 5 HOH 515 1517 515 HOH HOH A . F 5 HOH 516 1518 516 HOH HOH A . F 5 HOH 517 1519 517 HOH HOH A . F 5 HOH 518 1520 518 HOH HOH A . F 5 HOH 519 1521 519 HOH HOH A . F 5 HOH 520 1522 520 HOH HOH A . F 5 HOH 521 1523 521 HOH HOH A . F 5 HOH 522 1524 522 HOH HOH A . F 5 HOH 523 1525 523 HOH HOH A . F 5 HOH 524 1526 524 HOH HOH A . F 5 HOH 525 1527 525 HOH HOH A . F 5 HOH 526 1528 526 HOH HOH A . F 5 HOH 527 1529 527 HOH HOH A . F 5 HOH 528 1530 528 HOH HOH A . F 5 HOH 529 1531 529 HOH HOH A . F 5 HOH 530 1532 530 HOH HOH A . F 5 HOH 531 1533 531 HOH HOH A . F 5 HOH 532 1534 532 HOH HOH A . F 5 HOH 533 1535 533 HOH HOH A . F 5 HOH 534 1536 534 HOH HOH A . F 5 HOH 535 1537 535 HOH HOH A . F 5 HOH 536 1538 536 HOH HOH A . F 5 HOH 537 1539 537 HOH HOH A . F 5 HOH 538 1540 538 HOH HOH A . F 5 HOH 539 1541 539 HOH HOH A . F 5 HOH 540 1542 540 HOH HOH A . F 5 HOH 541 1543 541 HOH HOH A . F 5 HOH 542 1544 542 HOH HOH A . F 5 HOH 543 1545 543 HOH HOH A . F 5 HOH 544 1546 544 HOH HOH A . F 5 HOH 545 1547 545 HOH HOH A . F 5 HOH 546 1548 546 HOH HOH A . F 5 HOH 547 1549 547 HOH HOH A . F 5 HOH 548 1550 548 HOH HOH A . F 5 HOH 549 1551 549 HOH HOH A . F 5 HOH 550 1552 550 HOH HOH A . F 5 HOH 551 1553 551 HOH HOH A . F 5 HOH 552 1554 552 HOH HOH A . F 5 HOH 553 1555 553 HOH HOH A . F 5 HOH 554 1556 554 HOH HOH A . F 5 HOH 555 1557 555 HOH HOH A . F 5 HOH 556 1558 556 HOH HOH A . F 5 HOH 557 1559 557 HOH HOH A . F 5 HOH 558 1560 558 HOH HOH A . F 5 HOH 559 1561 559 HOH HOH A . F 5 HOH 560 1562 560 HOH HOH A . F 5 HOH 561 1563 561 HOH HOH A . F 5 HOH 562 1564 562 HOH HOH A . F 5 HOH 563 1565 563 HOH HOH A . F 5 HOH 564 1566 564 HOH HOH A . # _pdbx_struct_mod_residue.id 1 _pdbx_struct_mod_residue.label_asym_id A _pdbx_struct_mod_residue.label_comp_id ASN _pdbx_struct_mod_residue.label_seq_id 197 _pdbx_struct_mod_residue.auth_asym_id A _pdbx_struct_mod_residue.auth_comp_id ASN _pdbx_struct_mod_residue.auth_seq_id 197 _pdbx_struct_mod_residue.PDB_ins_code ? _pdbx_struct_mod_residue.parent_comp_id ASN _pdbx_struct_mod_residue.details 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # _pdbx_struct_special_symmetry.id 1 _pdbx_struct_special_symmetry.PDB_model_num 1 _pdbx_struct_special_symmetry.auth_asym_id A _pdbx_struct_special_symmetry.auth_comp_id HOH _pdbx_struct_special_symmetry.auth_seq_id 1252 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id F _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 O ? F HOH . ? A HOH 1050 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 O ? A GLU 162 ? A GLU 162 ? 1_555 73.9 ? 2 O ? F HOH . ? A HOH 1050 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 OD2 ? A ASP 175 ? A ASP 175 ? 1_555 88.7 ? 3 O ? A GLU 162 ? A GLU 162 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 OD2 ? A ASP 175 ? A ASP 175 ? 1_555 78.1 ? 4 O ? F HOH . ? A HOH 1050 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 O ? F HOH . ? A HOH 1026 ? 1_555 144.2 ? 5 O ? A GLU 162 ? A GLU 162 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 O ? F HOH . ? A HOH 1026 ? 1_555 72.5 ? 6 OD2 ? A ASP 175 ? A ASP 175 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 O ? F HOH . ? A HOH 1026 ? 1_555 96.4 ? 7 O ? F HOH . ? A HOH 1050 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 O ? F HOH . ? A HOH 1194 ? 1_555 144.7 ? 8 O ? A GLU 162 ? A GLU 162 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 O ? F HOH . ? A HOH 1194 ? 1_555 132.4 ? 9 OD2 ? A ASP 175 ? A ASP 175 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 O ? F HOH . ? A HOH 1194 ? 1_555 77.4 ? 10 O ? F HOH . ? A HOH 1026 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 O ? F HOH . ? A HOH 1194 ? 1_555 70.4 ? 11 O ? F HOH . ? A HOH 1050 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 OD1 ? A ASP 175 ? A ASP 175 ? 1_555 68.3 ? 12 O ? A GLU 162 ? A GLU 162 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 OD1 ? A ASP 175 ? A ASP 175 ? 1_555 115.7 ? 13 OD2 ? A ASP 175 ? A ASP 175 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 OD1 ? A ASP 175 ? A ASP 175 ? 1_555 51.7 ? 14 O ? F HOH . ? A HOH 1026 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 OD1 ? A ASP 175 ? A ASP 175 ? 1_555 139.5 ? 15 O ? F HOH . ? A HOH 1194 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 OD1 ? A ASP 175 ? A ASP 175 ? 1_555 77.8 ? 16 O ? F HOH . ? A HOH 1050 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 OD1 ? A ASN 121 ? A ASN 121 ? 1_555 88.7 ? 17 O ? A GLU 162 ? A GLU 162 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 OD1 ? A ASN 121 ? A ASN 121 ? 1_555 152.1 ? 18 OD2 ? A ASP 175 ? A ASP 175 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 OD1 ? A ASN 121 ? A ASN 121 ? 1_555 124.0 ? 19 O ? F HOH . ? A HOH 1026 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 OD1 ? A ASN 121 ? A ASN 121 ? 1_555 116.4 ? 20 O ? F HOH . ? A HOH 1194 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 OD1 ? A ASN 121 ? A ASN 121 ? 1_555 73.4 ? 21 OD1 ? A ASP 175 ? A ASP 175 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 OD1 ? A ASN 121 ? A ASN 121 ? 1_555 75.8 ? 22 O ? F HOH . ? A HOH 1050 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 O ? A HIS 210 ? A HIS 210 ? 1_555 80.1 ? 23 O ? A GLU 162 ? A GLU 162 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 O ? A HIS 210 ? A HIS 210 ? 1_555 81.7 ? 24 OD2 ? A ASP 175 ? A ASP 175 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 O ? A HIS 210 ? A HIS 210 ? 1_555 159.0 ? 25 O ? F HOH . ? A HOH 1026 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 O ? A HIS 210 ? A HIS 210 ? 1_555 83.0 ? 26 O ? F HOH . ? A HOH 1194 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 O ? A HIS 210 ? A HIS 210 ? 1_555 121.4 ? 27 OD1 ? A ASP 175 ? A ASP 175 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 O ? A HIS 210 ? A HIS 210 ? 1_555 136.1 ? 28 OD1 ? A ASN 121 ? A ASN 121 ? 1_555 CA ? E CA . ? A CA 601 ? 1_555 O ? A HIS 210 ? A HIS 210 ? 1_555 73.8 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2006-08-15 2 'Structure model' 1 1 2008-05-01 3 'Structure model' 1 2 2011-07-13 4 'Structure model' 1 3 2017-10-18 # _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' Advisory 3 3 'Structure model' 'Version format compliance' 4 4 'Structure model' 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 4 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # loop_ _pdbx_audit_revision_item.ordinal _pdbx_audit_revision_item.revision_ordinal _pdbx_audit_revision_item.data_content_type _pdbx_audit_revision_item.item 1 4 'Structure model' '_software.classification' 2 4 'Structure model' '_software.name' # _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 21.5739 _pdbx_refine_tls.origin_y 6.5953 _pdbx_refine_tls.origin_z 18.7641 _pdbx_refine_tls.T[1][1] -0.0168 _pdbx_refine_tls.T[2][2] -0.0169 _pdbx_refine_tls.T[3][3] -0.0373 _pdbx_refine_tls.T[1][2] 0.0354 _pdbx_refine_tls.T[1][3] 0.0160 _pdbx_refine_tls.T[2][3] -0.0221 _pdbx_refine_tls.L[1][1] 1.0247 _pdbx_refine_tls.L[2][2] 0.8174 _pdbx_refine_tls.L[3][3] 0.6026 _pdbx_refine_tls.L[1][2] -0.3997 _pdbx_refine_tls.L[1][3] 0.0484 _pdbx_refine_tls.L[2][3] -0.2453 _pdbx_refine_tls.S[1][1] 0.1099 _pdbx_refine_tls.S[1][2] 0.1992 _pdbx_refine_tls.S[1][3] 0.0083 _pdbx_refine_tls.S[2][1] -0.0613 _pdbx_refine_tls.S[2][2] -0.1166 _pdbx_refine_tls.S[2][3] -0.0204 _pdbx_refine_tls.S[3][1] -0.0035 _pdbx_refine_tls.S[3][2] -0.0366 _pdbx_refine_tls.S[3][3] 0.0068 _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' # _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_auth_asym_id A _pdbx_refine_tls_group.beg_auth_seq_id 1 _pdbx_refine_tls_group.beg_label_asym_id A _pdbx_refine_tls_group.beg_label_seq_id 1 _pdbx_refine_tls_group.end_auth_asym_id A _pdbx_refine_tls_group.end_auth_seq_id 476 _pdbx_refine_tls_group.end_label_asym_id A _pdbx_refine_tls_group.end_label_seq_id 476 _pdbx_refine_tls_group.selection ? _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.selection_details ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.2.0019 ? 1 ProDC 'data collection' . ? 2 SCALEPACK 'data scaling' . ? 3 PHASER phasing . ? 4 # _pdbx_database_remark.id 999 _pdbx_database_remark.text ;SEQUENCE Currently there is no aminoacid sequence database reference available for the protein ; # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 NZ A LYS 412 ? ? CE1 A TYR 419 ? ? 2.02 2 1 O A HOH 1147 ? ? O A HOH 1521 ? ? 2.09 3 1 O A HOH 1177 ? ? O A HOH 1443 ? ? 2.12 4 1 O A HOH 1311 ? ? O A HOH 1375 ? ? 2.12 5 1 OE1 A GLU 109 ? ? O A HOH 1452 ? ? 2.13 6 1 O A HOH 1112 ? ? O A HOH 1446 ? ? 2.17 7 1 OG A SER 422 ? ? ND2 A ASN 450 ? ? 2.17 8 1 O A HOH 1134 ? ? O A HOH 1566 ? ? 2.18 # loop_ _pdbx_validate_symm_contact.id _pdbx_validate_symm_contact.PDB_model_num _pdbx_validate_symm_contact.auth_atom_id_1 _pdbx_validate_symm_contact.auth_asym_id_1 _pdbx_validate_symm_contact.auth_comp_id_1 _pdbx_validate_symm_contact.auth_seq_id_1 _pdbx_validate_symm_contact.PDB_ins_code_1 _pdbx_validate_symm_contact.label_alt_id_1 _pdbx_validate_symm_contact.site_symmetry_1 _pdbx_validate_symm_contact.auth_atom_id_2 _pdbx_validate_symm_contact.auth_asym_id_2 _pdbx_validate_symm_contact.auth_comp_id_2 _pdbx_validate_symm_contact.auth_seq_id_2 _pdbx_validate_symm_contact.PDB_ins_code_2 _pdbx_validate_symm_contact.label_alt_id_2 _pdbx_validate_symm_contact.site_symmetry_2 _pdbx_validate_symm_contact.dist 1 1 O A HOH 1227 ? ? 1_555 O A HOH 1302 ? ? 2_555 2.03 2 1 O A HOH 1428 ? ? 1_555 O A HOH 1441 ? ? 3_556 2.13 # 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 ALA A 78 ? ? -79.57 45.81 2 1 TRP A 83 ? ? -119.95 61.50 3 1 GLN A 85 ? ? -130.64 -34.80 4 1 ALA A 329 ? ? -36.03 121.60 5 1 ASP A 340 ? ? -33.64 126.94 # 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 SER 477 ? A SER 477 2 1 Y 1 A SER 478 ? A SER 478 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-MANNOSE BMA 4 'CALCIUM ION' CA 5 water HOH #