data_3CL4 # _entry.id 3CL4 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3CL4 RCSB RCSB046908 WWPDB D_1000046908 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1FLC . unspecified PDB 3CL5 . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3CL4 _pdbx_database_status.recvd_initial_deposition_date 2008-03-18 _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 ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Zeng, Q.H.' 1 'Langereis, M.A.' 2 'van Vliet, A.L.W.' 3 'Huizinga, E.G.' 4 'de Groot, R.J.' 5 # _citation.id primary _citation.title 'Structure of coronavirus hemagglutinin-esterase offers insight into corona and influenza virus evolution.' _citation.journal_abbrev Proc.Natl.Acad.Sci.Usa _citation.journal_volume 105 _citation.page_first 9065 _citation.page_last 9069 _citation.year 2008 _citation.journal_id_ASTM PNASA6 _citation.country US _citation.journal_id_ISSN 0027-8424 _citation.journal_id_CSD 0040 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 18550812 _citation.pdbx_database_id_DOI 10.1073/pnas.0800502105 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Zeng, Q.' 1 primary 'Langereis, M.A.' 2 primary 'van Vliet, A.L.' 3 primary 'Huizinga, E.G.' 4 primary 'de Groot, R.J.' 5 # _cell.entry_id 3CL4 _cell.length_a 88.830 _cell.length_b 88.830 _cell.length_c 282.360 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 12 _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 3CL4 _symmetry.space_group_name_H-M 'P 65 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 179 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man Hemagglutinin-esterase 42646.230 1 3.1.1.53 ? 'residues 19-388' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 7 ? ? ? ? 3 non-polymer syn 'POTASSIUM ION' 39.098 1 ? ? ? ? 4 water nat water 18.015 257 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'HE protein, E3 glycoprotein' # _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 ;FDNPPTNVVSHLNGDWFLFGDSRSDCNHVVNTNPRNYSYMDLNPALCDSGKISSKAGNSIFRSFHFTDFYNYTGEGQQII FYEGVNFTPYHAFKCTTSGSNDIWMQNKGLFYTQVYKNMAVYRSLTFVNVPYVYNGSAQSTALCKSGSLVLNNPAYIARE ANFGDYYYKVEADFYLSGCDEYIVPLCIFNGKFLSNTKYYDDSQYYFNKDTGVIYGLNSTETITTGFDFNCHYLVLPSGN YLAISNELLLTVPTKAICLNKRKDFTPVQVVDSRWNNARQSDNMTAVACQPPYCYFRNSTTNYVGVYDINHGDAGFTSIL SGLLYDSPCFSQQGVFRYDNVSSVWPLYSYGRCPTAADINTPDVPICVYDSDPLVPR ; _entity_poly.pdbx_seq_one_letter_code_can ;FDNPPTNVVSHLNGDWFLFGDSRSDCNHVVNTNPRNYSYMDLNPALCDSGKISSKAGNSIFRSFHFTDFYNYTGEGQQII FYEGVNFTPYHAFKCTTSGSNDIWMQNKGLFYTQVYKNMAVYRSLTFVNVPYVYNGSAQSTALCKSGSLVLNNPAYIARE ANFGDYYYKVEADFYLSGCDEYIVPLCIFNGKFLSNTKYYDDSQYYFNKDTGVIYGLNSTETITTGFDFNCHYLVLPSGN YLAISNELLLTVPTKAICLNKRKDFTPVQVVDSRWNNARQSDNMTAVACQPPYCYFRNSTTNYVGVYDINHGDAGFTSIL SGLLYDSPCFSQQGVFRYDNVSSVWPLYSYGRCPTAADINTPDVPICVYDSDPLVPR ; _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 PHE n 1 2 ASP n 1 3 ASN n 1 4 PRO n 1 5 PRO n 1 6 THR n 1 7 ASN n 1 8 VAL n 1 9 VAL n 1 10 SER n 1 11 HIS n 1 12 LEU n 1 13 ASN n 1 14 GLY n 1 15 ASP n 1 16 TRP n 1 17 PHE n 1 18 LEU n 1 19 PHE n 1 20 GLY n 1 21 ASP n 1 22 SER n 1 23 ARG n 1 24 SER n 1 25 ASP n 1 26 CYS n 1 27 ASN n 1 28 HIS n 1 29 VAL n 1 30 VAL n 1 31 ASN n 1 32 THR n 1 33 ASN n 1 34 PRO n 1 35 ARG n 1 36 ASN n 1 37 TYR n 1 38 SER n 1 39 TYR n 1 40 MET n 1 41 ASP n 1 42 LEU n 1 43 ASN n 1 44 PRO n 1 45 ALA n 1 46 LEU n 1 47 CYS n 1 48 ASP n 1 49 SER n 1 50 GLY n 1 51 LYS n 1 52 ILE n 1 53 SER n 1 54 SER n 1 55 LYS n 1 56 ALA n 1 57 GLY n 1 58 ASN n 1 59 SER n 1 60 ILE n 1 61 PHE n 1 62 ARG n 1 63 SER n 1 64 PHE n 1 65 HIS n 1 66 PHE n 1 67 THR n 1 68 ASP n 1 69 PHE n 1 70 TYR n 1 71 ASN n 1 72 TYR n 1 73 THR n 1 74 GLY n 1 75 GLU n 1 76 GLY n 1 77 GLN n 1 78 GLN n 1 79 ILE n 1 80 ILE n 1 81 PHE n 1 82 TYR n 1 83 GLU n 1 84 GLY n 1 85 VAL n 1 86 ASN n 1 87 PHE n 1 88 THR n 1 89 PRO n 1 90 TYR n 1 91 HIS n 1 92 ALA n 1 93 PHE n 1 94 LYS n 1 95 CYS n 1 96 THR n 1 97 THR n 1 98 SER n 1 99 GLY n 1 100 SER n 1 101 ASN n 1 102 ASP n 1 103 ILE n 1 104 TRP n 1 105 MET n 1 106 GLN n 1 107 ASN n 1 108 LYS n 1 109 GLY n 1 110 LEU n 1 111 PHE n 1 112 TYR n 1 113 THR n 1 114 GLN n 1 115 VAL n 1 116 TYR n 1 117 LYS n 1 118 ASN n 1 119 MET n 1 120 ALA n 1 121 VAL n 1 122 TYR n 1 123 ARG n 1 124 SER n 1 125 LEU n 1 126 THR n 1 127 PHE n 1 128 VAL n 1 129 ASN n 1 130 VAL n 1 131 PRO n 1 132 TYR n 1 133 VAL n 1 134 TYR n 1 135 ASN n 1 136 GLY n 1 137 SER n 1 138 ALA n 1 139 GLN n 1 140 SER n 1 141 THR n 1 142 ALA n 1 143 LEU n 1 144 CYS n 1 145 LYS n 1 146 SER n 1 147 GLY n 1 148 SER n 1 149 LEU n 1 150 VAL n 1 151 LEU n 1 152 ASN n 1 153 ASN n 1 154 PRO n 1 155 ALA n 1 156 TYR n 1 157 ILE n 1 158 ALA n 1 159 ARG n 1 160 GLU n 1 161 ALA n 1 162 ASN n 1 163 PHE n 1 164 GLY n 1 165 ASP n 1 166 TYR n 1 167 TYR n 1 168 TYR n 1 169 LYS n 1 170 VAL n 1 171 GLU n 1 172 ALA n 1 173 ASP n 1 174 PHE n 1 175 TYR n 1 176 LEU n 1 177 SER n 1 178 GLY n 1 179 CYS n 1 180 ASP n 1 181 GLU n 1 182 TYR n 1 183 ILE n 1 184 VAL n 1 185 PRO n 1 186 LEU n 1 187 CYS n 1 188 ILE n 1 189 PHE n 1 190 ASN n 1 191 GLY n 1 192 LYS n 1 193 PHE n 1 194 LEU n 1 195 SER n 1 196 ASN n 1 197 THR n 1 198 LYS n 1 199 TYR n 1 200 TYR n 1 201 ASP n 1 202 ASP n 1 203 SER n 1 204 GLN n 1 205 TYR n 1 206 TYR n 1 207 PHE n 1 208 ASN n 1 209 LYS n 1 210 ASP n 1 211 THR n 1 212 GLY n 1 213 VAL n 1 214 ILE n 1 215 TYR n 1 216 GLY n 1 217 LEU n 1 218 ASN n 1 219 SER n 1 220 THR n 1 221 GLU n 1 222 THR n 1 223 ILE n 1 224 THR n 1 225 THR n 1 226 GLY n 1 227 PHE n 1 228 ASP n 1 229 PHE n 1 230 ASN n 1 231 CYS n 1 232 HIS n 1 233 TYR n 1 234 LEU n 1 235 VAL n 1 236 LEU n 1 237 PRO n 1 238 SER n 1 239 GLY n 1 240 ASN n 1 241 TYR n 1 242 LEU n 1 243 ALA n 1 244 ILE n 1 245 SER n 1 246 ASN n 1 247 GLU n 1 248 LEU n 1 249 LEU n 1 250 LEU n 1 251 THR n 1 252 VAL n 1 253 PRO n 1 254 THR n 1 255 LYS n 1 256 ALA n 1 257 ILE n 1 258 CYS n 1 259 LEU n 1 260 ASN n 1 261 LYS n 1 262 ARG n 1 263 LYS n 1 264 ASP n 1 265 PHE n 1 266 THR n 1 267 PRO n 1 268 VAL n 1 269 GLN n 1 270 VAL n 1 271 VAL n 1 272 ASP n 1 273 SER n 1 274 ARG n 1 275 TRP n 1 276 ASN n 1 277 ASN n 1 278 ALA n 1 279 ARG n 1 280 GLN n 1 281 SER n 1 282 ASP n 1 283 ASN n 1 284 MET n 1 285 THR n 1 286 ALA n 1 287 VAL n 1 288 ALA n 1 289 CYS n 1 290 GLN n 1 291 PRO n 1 292 PRO n 1 293 TYR n 1 294 CYS n 1 295 TYR n 1 296 PHE n 1 297 ARG n 1 298 ASN n 1 299 SER n 1 300 THR n 1 301 THR n 1 302 ASN n 1 303 TYR n 1 304 VAL n 1 305 GLY n 1 306 VAL n 1 307 TYR n 1 308 ASP n 1 309 ILE n 1 310 ASN n 1 311 HIS n 1 312 GLY n 1 313 ASP n 1 314 ALA n 1 315 GLY n 1 316 PHE n 1 317 THR n 1 318 SER n 1 319 ILE n 1 320 LEU n 1 321 SER n 1 322 GLY n 1 323 LEU n 1 324 LEU n 1 325 TYR n 1 326 ASP n 1 327 SER n 1 328 PRO n 1 329 CYS n 1 330 PHE n 1 331 SER n 1 332 GLN n 1 333 GLN n 1 334 GLY n 1 335 VAL n 1 336 PHE n 1 337 ARG n 1 338 TYR n 1 339 ASP n 1 340 ASN n 1 341 VAL n 1 342 SER n 1 343 SER n 1 344 VAL n 1 345 TRP n 1 346 PRO n 1 347 LEU n 1 348 TYR n 1 349 SER n 1 350 TYR n 1 351 GLY n 1 352 ARG n 1 353 CYS n 1 354 PRO n 1 355 THR n 1 356 ALA n 1 357 ALA n 1 358 ASP n 1 359 ILE n 1 360 ASN n 1 361 THR n 1 362 PRO n 1 363 ASP n 1 364 VAL n 1 365 PRO n 1 366 ILE n 1 367 CYS n 1 368 VAL n 1 369 TYR n 1 370 ASP n 1 371 SER n 1 372 ASP n 1 373 PRO n 1 374 LEU n 1 375 VAL n 1 376 PRO n 1 377 ARG n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name 'strain Mebus' _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene HE _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain Mebus _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details 'HEK293S cell line' _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Bovine coronavirus' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id ? _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name human _entity_src_gen.pdbx_host_org_scientific_name 'Homo Sapiens' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id ? _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type plasmid _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name S1-Ig _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code HEMA_CVBM _struct_ref.pdbx_db_accession P15776 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;FDNPPTNVVSHLNGDWFLFGDSRSDCNHVVNTNPRNYSYMDLNPALCDSGKISSKAGNSIFRSFHFTDFYNYTGEGQQII FYEGVNFTPYHAFKCTTSGSNDIWMQNKGLFYTQVYKNMAVYRSLTFVNVPYVYNGSAQSTALCKSGSLVLNNPAYIARE ANFGDYYYKVEADFYLSGCDEYIVPLCIFNGKFLSNTKYYDDSQYYFNKDTGVIYGLNSTETITTGFDFNCHYLVLPSGN YLAISNELLLTVPTKAICLNKRKDFTPVQVVDSRWNNARQSDNMTAVACQPPYCYFRNSTTNYVGVYDINHGDAGFTSIL SGLLYDSPCFSQQGVFRYDNVSSVWPLYSYGRCPTAADINTPDVPICVYD ; _struct_ref.pdbx_align_begin 19 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 3CL4 _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 370 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P15776 _struct_ref_seq.db_align_beg 19 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 388 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 19 _struct_ref_seq.pdbx_auth_seq_align_end 388 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 3CL4 SER A 371 ? UNP P15776 ? ? 'expression tag' 389 1 1 3CL4 ASP A 372 ? UNP P15776 ? ? 'expression tag' 390 2 1 3CL4 PRO A 373 ? UNP P15776 ? ? 'expression tag' 391 3 1 3CL4 LEU A 374 ? UNP P15776 ? ? 'expression tag' 392 4 1 3CL4 VAL A 375 ? UNP P15776 ? ? 'expression tag' 393 5 1 3CL4 PRO A 376 ? UNP P15776 ? ? 'expression tag' 394 6 1 3CL4 ARG A 377 ? UNP P15776 ? ? 'expression tag' 395 7 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 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 K non-polymer . 'POTASSIUM ION' ? 'K 1' 39.098 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 3CL4 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.77 _exptl_crystal.density_percent_sol 67.38 _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 291 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pdbx_details '0.1 M KH2PO4, 10% (w/v) PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 291K' _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 4' _diffrn_detector.pdbx_collection_date 2006-03-11 _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 'three diamond monochromators' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.931 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID14-3' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID14-3 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.931 # _reflns.entry_id 3CL4 _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I -3.7 _reflns.d_resolution_high 2.1 _reflns.d_resolution_low 52 _reflns.number_all 39252 _reflns.number_obs 39252 _reflns.percent_possible_obs 99.6 _reflns.pdbx_Rmerge_I_obs 0.135 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 12.8 _reflns.B_iso_Wilson_estimate 29.0 _reflns.pdbx_redundancy 8.4 _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 2.10 _reflns_shell.d_res_low 2.21 _reflns_shell.percent_possible_all 99.9 _reflns_shell.Rmerge_I_obs 0.804 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.5 _reflns_shell.pdbx_redundancy 8.5 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 5637 _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 3CL4 _refine.ls_number_reflns_obs 37791 _refine.ls_number_reflns_all 37791 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 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 29.05 _refine.ls_d_res_high 2.1 _refine.ls_percent_reflns_obs 99.85 _refine.ls_R_factor_obs 0.18107 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.17946 _refine.ls_R_factor_R_free 0.21154 _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 2035 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.950 _refine.correlation_coeff_Fo_to_Fc_free 0.934 _refine.B_iso_mean 27.990 _refine.aniso_B[1][1] 0.41 _refine.aniso_B[2][2] 0.41 _refine.aniso_B[3][3] -0.61 _refine.aniso_B[1][2] 0.20 _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 1.40 _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 1FLC chain A resi 40-400' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model isotropic _refine.pdbx_stereochemistry_target_values 'Engh & Huber' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.137 _refine.pdbx_overall_ESU_R_Free 0.132 _refine.overall_SU_ML 0.090 _refine.overall_SU_B 3.338 _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_overall_phase_error ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2861 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 99 _refine_hist.number_atoms_solvent 257 _refine_hist.number_atoms_total 3217 _refine_hist.d_res_high 2.1 _refine_hist.d_res_low 29.05 # 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 0.017 0.022 ? 3057 'X-RAY DIFFRACTION' ? r_bond_other_d 0.002 0.020 ? 1981 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.555 1.964 ? 4177 'X-RAY DIFFRACTION' ? r_angle_other_deg 1.408 3.005 ? 4756 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 9.349 5.000 ? 357 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 35.595 24.211 ? 152 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 13.249 15.000 ? 425 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 16.995 15.000 ? 11 'X-RAY DIFFRACTION' ? r_chiral_restr 0.091 0.200 ? 450 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.008 0.021 ? 3435 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.002 0.020 ? 672 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 0.865 1.500 ? 1781 'X-RAY DIFFRACTION' ? r_mcbond_other 0.214 1.500 ? 723 'X-RAY DIFFRACTION' ? r_mcangle_it 1.524 2.000 ? 2882 'X-RAY DIFFRACTION' ? r_scbond_it 2.160 3.000 ? 1276 'X-RAY DIFFRACTION' ? r_scangle_it 3.384 4.500 ? 1295 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 2.094 _refine_ls_shell.d_res_low 2.148 _refine_ls_shell.number_reflns_R_work 2633 _refine_ls_shell.R_factor_R_work 0.23 _refine_ls_shell.percent_reflns_obs 97.87 _refine_ls_shell.R_factor_R_free 0.255 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 171 _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 3CL4 _struct.title 'Crystal structure of bovine coronavirus hemagglutinin-esterase' _struct.pdbx_descriptor 'Hemagglutinin-esterase (E.C.3.1.1.53)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3CL4 _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'SGNH-hydrolase fold, Swiss roll, Envelope protein, Glycoprotein, Hemagglutinin, Membrane, Transmembrane, Virion, 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 2 ? E N N 2 ? F N N 2 ? G N N 2 ? H N N 2 ? I N N 3 ? J N N 4 ? # _struct_biol.id 1 _struct_biol.details ? # 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 ARG A 23 ? THR A 32 ? ARG A 41 THR A 50 5 ? 10 HELX_P HELX_P2 2 ASN A 36 ? MET A 40 ? ASN A 54 MET A 58 5 ? 5 HELX_P HELX_P3 3 ASN A 43 ? CYS A 47 ? ASN A 61 CYS A 65 5 ? 5 HELX_P HELX_P4 4 SER A 59 ? PHE A 66 ? SER A 77 PHE A 84 1 ? 8 HELX_P HELX_P5 5 THR A 88 ? ALA A 92 ? THR A 106 ALA A 110 5 ? 5 HELX_P HELX_P6 6 SER A 100 ? ALA A 120 ? SER A 118 ALA A 138 1 ? 21 HELX_P HELX_P7 7 ASN A 283 ? CYS A 289 ? ASN A 301 CYS A 307 1 ? 7 HELX_P HELX_P8 8 ALA A 314 ? SER A 321 ? ALA A 332 SER A 339 1 ? 8 HELX_P HELX_P9 9 GLY A 322 ? TYR A 325 ? GLY A 340 TYR A 343 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 47 SG ? ? ? 1_555 A CYS 26 SG ? ? A CYS 65 A CYS 44 1_555 ? ? ? ? ? ? ? 2.066 ? disulf2 disulf ? ? A CYS 144 SG ? ? ? 1_555 A CYS 95 SG ? ? A CYS 162 A CYS 113 1_555 ? ? ? ? ? ? ? 2.023 ? disulf3 disulf ? ? A CYS 231 SG ? ? ? 1_555 A CYS 187 SG ? ? A CYS 249 A CYS 205 1_555 ? ? ? ? ? ? ? 2.014 ? disulf4 disulf ? ? A CYS 258 SG ? ? ? 1_555 A CYS 179 SG ? ? A CYS 276 A CYS 197 1_555 ? ? ? ? ? ? ? 2.054 ? disulf5 disulf ? ? A CYS 294 SG ? ? ? 1_555 A CYS 289 SG ? ? A CYS 312 A CYS 307 1_555 ? ? ? ? ? ? ? 2.035 ? disulf6 disulf ? ? A CYS 353 SG ? ? ? 1_555 A CYS 329 SG ? ? A CYS 371 A CYS 347 1_555 ? ? ? ? ? ? ? 2.027 ? covale1 covale ? ? A ASN 36 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 54 A NAG 2520 1_555 ? ? ? ? ? ? ? 1.433 ? covale2 covale ? ? A ASN 71 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 89 A NAG 2523 1_555 ? ? ? ? ? ? ? 1.443 ? metalc1 metalc ? ? A ASP 202 OD1 ? ? ? 1_555 I K . K ? ? A ASP 220 A K 2 1_555 ? ? ? ? ? ? ? 2.574 ? metalc2 metalc ? ? A SER 203 O ? ? ? 1_555 I K . K ? ? A SER 221 A K 2 1_555 ? ? ? ? ? ? ? 2.806 ? metalc3 metalc ? ? A GLN 204 OE1 ? ? ? 1_555 I K . K ? ? A GLN 222 A K 2 1_555 ? ? ? ? ? ? ? 2.865 ? covale3 covale ? ? A ASN 218 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 236 A NAG 2525 1_555 ? ? ? ? ? ? ? 1.442 ? metalc4 metalc ? ? A SER 245 OG ? ? ? 1_555 I K . K ? ? A SER 263 A K 2 1_555 ? ? ? ? ? ? ? 2.655 ? metalc5 metalc ? ? A LEU 249 O ? ? ? 1_555 I K . K ? ? A LEU 267 A K 2 1_555 ? ? ? ? ? ? ? 2.708 ? covale4 covale ? ? A ASN 283 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 301 A NAG 1961 1_555 ? ? ? ? ? ? ? 1.450 ? covale5 covale ? ? A ASN 298 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 316 A NAG 2521 1_555 ? ? ? ? ? ? ? 1.433 ? covale6 covale ? ? A ASN 340 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 358 A NAG 2527 1_555 ? ? ? ? ? ? ? 1.455 ? covale7 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 2525 A NAG 2526 1_555 ? ? ? ? ? ? ? 1.436 ? # 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 ASN 33 A . ? ASN 51 A PRO 34 A ? PRO 52 A 1 -2.16 2 ASN 153 A . ? ASN 171 A PRO 154 A ? PRO 172 A 1 -4.84 3 PRO 291 A . ? PRO 309 A PRO 292 A ? PRO 310 A 1 0.05 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 4 ? B ? 5 ? C ? 5 ? D ? 7 ? E ? 3 ? F ? 2 ? G ? 2 ? H ? 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 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel B 1 2 ? parallel B 2 3 ? parallel B 3 4 ? parallel B 4 5 ? parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel C 4 5 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel D 4 5 ? anti-parallel D 5 6 ? anti-parallel D 6 7 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel F 1 2 ? anti-parallel G 1 2 ? anti-parallel H 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 PRO A 5 ? THR A 6 ? PRO A 23 THR A 24 A 2 VAL A 335 ? PHE A 336 ? VAL A 353 PHE A 354 A 3 CYS A 329 ? PHE A 330 ? CYS A 347 PHE A 348 A 4 TYR A 350 ? GLY A 351 ? TYR A 368 GLY A 369 B 1 ILE A 52 ? LYS A 55 ? ILE A 70 LYS A 73 B 2 TRP A 16 ? ASP A 21 ? TRP A 34 ASP A 39 B 3 GLN A 78 ? TYR A 82 ? GLN A 96 TYR A 100 B 4 VAL A 268 ? VAL A 271 ? VAL A 286 VAL A 289 B 5 CYS A 294 ? ARG A 297 ? CYS A 312 ARG A 315 C 1 GLY A 74 ? GLU A 75 ? GLY A 92 GLU A 93 C 2 TYR A 122 ? ASN A 129 ? TYR A 140 ASN A 147 C 3 LYS A 255 ? ARG A 262 ? LYS A 273 ARG A 280 C 4 VAL A 170 ? PHE A 189 ? VAL A 188 PHE A 207 C 5 TYR A 132 ? TYR A 134 ? TYR A 150 TYR A 152 D 1 GLY A 74 ? GLU A 75 ? GLY A 92 GLU A 93 D 2 TYR A 122 ? ASN A 129 ? TYR A 140 ASN A 147 D 3 LYS A 255 ? ARG A 262 ? LYS A 273 ARG A 280 D 4 VAL A 170 ? PHE A 189 ? VAL A 188 PHE A 207 D 5 PHE A 229 ? GLU A 247 ? PHE A 247 GLU A 265 D 6 SER A 203 ? ASN A 208 ? SER A 221 ASN A 226 D 7 ILE A 214 ? ASN A 218 ? ILE A 232 ASN A 236 E 1 SER A 140 ? THR A 141 ? SER A 158 THR A 159 E 2 ALA A 155 ? ILE A 157 ? ALA A 173 ILE A 175 E 3 LEU A 250 ? VAL A 252 ? LEU A 268 VAL A 270 F 1 LYS A 145 ? SER A 146 ? LYS A 163 SER A 164 F 2 LEU A 149 ? VAL A 150 ? LEU A 167 VAL A 168 G 1 PHE A 193 ? SER A 195 ? PHE A 211 SER A 213 G 2 LYS A 198 ? TYR A 200 ? LYS A 216 TYR A 218 H 1 GLY A 305 ? ASP A 308 ? GLY A 323 ASP A 326 H 2 HIS A 311 ? ASP A 313 ? HIS A 329 ASP A 331 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N THR A 6 ? N THR A 24 O VAL A 335 ? O VAL A 353 A 2 3 O PHE A 336 ? O PHE A 354 N CYS A 329 ? N CYS A 347 A 3 4 N PHE A 330 ? N PHE A 348 O TYR A 350 ? O TYR A 368 B 1 2 O SER A 53 ? O SER A 71 N LEU A 18 ? N LEU A 36 B 2 3 N PHE A 17 ? N PHE A 35 O ILE A 80 ? O ILE A 98 B 3 4 N PHE A 81 ? N PHE A 99 O VAL A 271 ? O VAL A 289 B 4 5 N VAL A 270 ? N VAL A 288 O ARG A 297 ? O ARG A 315 C 1 2 N GLY A 74 ? N GLY A 92 O LEU A 125 ? O LEU A 143 C 2 3 N THR A 126 ? N THR A 144 O CYS A 258 ? O CYS A 276 C 3 4 O LEU A 259 ? O LEU A 277 N GLU A 181 ? N GLU A 199 C 4 5 O ASP A 173 ? O ASP A 191 N VAL A 133 ? N VAL A 151 D 1 2 N GLY A 74 ? N GLY A 92 O LEU A 125 ? O LEU A 143 D 2 3 N THR A 126 ? N THR A 144 O CYS A 258 ? O CYS A 276 D 3 4 O LEU A 259 ? O LEU A 277 N GLU A 181 ? N GLU A 199 D 4 5 N ALA A 172 ? N ALA A 190 O ALA A 243 ? O ALA A 261 D 5 6 O ILE A 244 ? O ILE A 262 N TYR A 205 ? N TYR A 223 D 6 7 N GLN A 204 ? N GLN A 222 O LEU A 217 ? O LEU A 235 E 1 2 N THR A 141 ? N THR A 159 O TYR A 156 ? O TYR A 174 E 2 3 N ALA A 155 ? N ALA A 173 O VAL A 252 ? O VAL A 270 F 1 2 N SER A 146 ? N SER A 164 O LEU A 149 ? O LEU A 167 G 1 2 N PHE A 193 ? N PHE A 211 O TYR A 200 ? O TYR A 218 H 1 2 N ASP A 308 ? N ASP A 326 O HIS A 311 ? O HIS A 329 # _struct_site.id AC1 _struct_site.pdbx_evidence_code Software _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 7 _struct_site.details 'BINDING SITE FOR RESIDUE K A 2' # 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 ASP A 202 ? ASP A 220 . ? 1_555 ? 2 AC1 7 SER A 203 ? SER A 221 . ? 1_555 ? 3 AC1 7 GLN A 204 ? GLN A 222 . ? 1_555 ? 4 AC1 7 SER A 245 ? SER A 263 . ? 1_555 ? 5 AC1 7 GLU A 247 ? GLU A 265 . ? 1_555 ? 6 AC1 7 LEU A 249 ? LEU A 267 . ? 1_555 ? 7 AC1 7 HOH J . ? HOH A 2549 . ? 1_555 ? # _database_PDB_matrix.entry_id 3CL4 _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 3CL4 _atom_sites.fract_transf_matrix[1][1] 0.011257 _atom_sites.fract_transf_matrix[1][2] 0.006499 _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] 0.012999 _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] 0.003542 _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 K 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 . PHE A 1 1 ? -28.451 53.119 19.970 1.00 60.72 ? 19 PHE A N 1 ATOM 2 C CA . PHE A 1 1 ? -27.071 53.097 19.374 1.00 60.45 ? 19 PHE A CA 1 ATOM 3 C C . PHE A 1 1 ? -26.191 52.162 20.156 1.00 59.70 ? 19 PHE A C 1 ATOM 4 O O . PHE A 1 1 ? -26.190 52.143 21.405 1.00 60.29 ? 19 PHE A O 1 ATOM 5 C CB . PHE A 1 1 ? -26.425 54.484 19.376 1.00 60.50 ? 19 PHE A CB 1 ATOM 6 C CG . PHE A 1 1 ? -25.034 54.511 18.774 1.00 61.59 ? 19 PHE A CG 1 ATOM 7 C CD1 . PHE A 1 1 ? -24.827 54.169 17.444 1.00 62.12 ? 19 PHE A CD1 1 ATOM 8 C CD2 . PHE A 1 1 ? -23.937 54.942 19.526 1.00 61.93 ? 19 PHE A CD2 1 ATOM 9 C CE1 . PHE A 1 1 ? -23.543 54.220 16.882 1.00 62.38 ? 19 PHE A CE1 1 ATOM 10 C CE2 . PHE A 1 1 ? -22.652 54.986 18.972 1.00 61.31 ? 19 PHE A CE2 1 ATOM 11 C CZ . PHE A 1 1 ? -22.454 54.626 17.654 1.00 61.50 ? 19 PHE A CZ 1 ATOM 12 N N . ASP A 1 2 ? -25.420 51.402 19.392 1.00 57.60 ? 20 ASP A N 1 ATOM 13 C CA . ASP A 1 2 ? -24.509 50.423 19.978 1.00 55.85 ? 20 ASP A CA 1 ATOM 14 C C . ASP A 1 2 ? -23.164 50.441 19.245 1.00 52.37 ? 20 ASP A C 1 ATOM 15 O O . ASP A 1 2 ? -23.089 50.427 18.009 1.00 51.92 ? 20 ASP A O 1 ATOM 16 C CB . ASP A 1 2 ? -25.146 49.026 19.987 1.00 56.94 ? 20 ASP A CB 1 ATOM 17 C CG . ASP A 1 2 ? -24.503 48.065 21.015 1.00 60.93 ? 20 ASP A CG 1 ATOM 18 O OD1 . ASP A 1 2 ? -23.920 48.504 22.060 1.00 63.40 ? 20 ASP A OD1 1 ATOM 19 O OD2 . ASP A 1 2 ? -24.607 46.831 20.763 1.00 65.64 ? 20 ASP A OD2 1 ATOM 20 N N . ASN A 1 3 ? -22.107 50.561 20.041 1.00 48.19 ? 21 ASN A N 1 ATOM 21 C CA . ASN A 1 3 ? -20.735 50.578 19.516 1.00 44.68 ? 21 ASN A CA 1 ATOM 22 C C . ASN A 1 3 ? -19.913 49.596 20.320 1.00 42.13 ? 21 ASN A C 1 ATOM 23 O O . ASN A 1 3 ? -19.062 49.976 21.123 1.00 41.05 ? 21 ASN A O 1 ATOM 24 C CB . ASN A 1 3 ? -20.183 51.995 19.611 1.00 44.14 ? 21 ASN A CB 1 ATOM 25 C CG . ASN A 1 3 ? -18.867 52.179 18.887 1.00 43.69 ? 21 ASN A CG 1 ATOM 26 O OD1 . ASN A 1 3 ? -18.511 51.426 17.971 1.00 43.21 ? 21 ASN A OD1 1 ATOM 27 N ND2 . ASN A 1 3 ? -18.153 53.240 19.263 1.00 40.65 ? 21 ASN A ND2 1 ATOM 28 N N . PRO A 1 4 ? -20.216 48.310 20.163 1.00 39.75 ? 22 PRO A N 1 ATOM 29 C CA . PRO A 1 4 ? -19.489 47.330 20.925 1.00 38.73 ? 22 PRO A CA 1 ATOM 30 C C . PRO A 1 4 ? -18.126 47.012 20.282 1.00 38.31 ? 22 PRO A C 1 ATOM 31 O O . PRO A 1 4 ? -17.940 47.296 19.100 1.00 37.12 ? 22 PRO A O 1 ATOM 32 C CB . PRO A 1 4 ? -20.376 46.104 20.820 1.00 38.74 ? 22 PRO A CB 1 ATOM 33 C CG . PRO A 1 4 ? -20.980 46.225 19.486 1.00 38.41 ? 22 PRO A CG 1 ATOM 34 C CD . PRO A 1 4 ? -21.165 47.684 19.237 1.00 40.15 ? 22 PRO A CD 1 ATOM 35 N N . PRO A 1 5 ? -17.191 46.420 21.064 1.00 37.49 ? 23 PRO A N 1 ATOM 36 C CA . PRO A 1 5 ? -15.998 45.862 20.446 1.00 37.11 ? 23 PRO A CA 1 ATOM 37 C C . PRO A 1 5 ? -16.381 44.634 19.651 1.00 36.69 ? 23 PRO A C 1 ATOM 38 O O . PRO A 1 5 ? -17.050 43.739 20.152 1.00 37.56 ? 23 PRO A O 1 ATOM 39 C CB . PRO A 1 5 ? -15.127 45.460 21.635 1.00 36.63 ? 23 PRO A CB 1 ATOM 40 C CG . PRO A 1 5 ? -16.057 45.185 22.722 1.00 38.12 ? 23 PRO A CG 1 ATOM 41 C CD . PRO A 1 5 ? -17.300 46.054 22.484 1.00 37.37 ? 23 PRO A CD 1 ATOM 42 N N . THR A 1 6 ? -15.967 44.608 18.395 1.00 35.64 ? 24 THR A N 1 ATOM 43 C CA . THR A 1 6 ? -16.333 43.510 17.505 1.00 33.95 ? 24 THR A CA 1 ATOM 44 C C . THR A 1 6 ? -15.106 42.633 17.261 1.00 33.38 ? 24 THR A C 1 ATOM 45 O O . THR A 1 6 ? -13.955 43.109 17.198 1.00 32.49 ? 24 THR A O 1 ATOM 46 C CB . THR A 1 6 ? -16.912 44.053 16.208 1.00 33.79 ? 24 THR A CB 1 ATOM 47 O OG1 . THR A 1 6 ? -15.895 44.789 15.497 1.00 34.97 ? 24 THR A OG1 1 ATOM 48 C CG2 . THR A 1 6 ? -18.080 44.997 16.518 1.00 31.63 ? 24 THR A CG2 1 ATOM 49 N N . ASN A 1 7 ? -15.405 41.354 17.171 1.00 32.20 ? 25 ASN A N 1 ATOM 50 C CA . ASN A 1 7 ? -14.439 40.295 16.943 1.00 32.36 ? 25 ASN A CA 1 ATOM 51 C C . ASN A 1 7 ? -14.058 40.141 15.451 1.00 31.71 ? 25 ASN A C 1 ATOM 52 O O . ASN A 1 7 ? -14.382 39.145 14.776 1.00 31.70 ? 25 ASN A O 1 ATOM 53 C CB . ASN A 1 7 ? -14.973 38.984 17.501 1.00 31.68 ? 25 ASN A CB 1 ATOM 54 C CG . ASN A 1 7 ? -13.917 37.934 17.579 1.00 33.37 ? 25 ASN A CG 1 ATOM 55 O OD1 . ASN A 1 7 ? -12.733 38.253 17.472 1.00 34.36 ? 25 ASN A OD1 1 ATOM 56 N ND2 . ASN A 1 7 ? -14.320 36.658 17.750 1.00 29.09 ? 25 ASN A ND2 1 ATOM 57 N N . VAL A 1 8 ? -13.330 41.142 14.982 1.00 31.18 ? 26 VAL A N 1 ATOM 58 C CA . VAL A 1 8 ? -12.793 41.148 13.624 1.00 30.95 ? 26 VAL A CA 1 ATOM 59 C C . VAL A 1 8 ? -11.360 41.656 13.573 1.00 30.67 ? 26 VAL A C 1 ATOM 60 O O . VAL A 1 8 ? -10.884 42.359 14.488 1.00 30.48 ? 26 VAL A O 1 ATOM 61 C CB . VAL A 1 8 ? -13.647 42.033 12.638 1.00 29.65 ? 26 VAL A CB 1 ATOM 62 C CG1 . VAL A 1 8 ? -15.100 41.517 12.569 1.00 32.72 ? 26 VAL A CG1 1 ATOM 63 C CG2 . VAL A 1 8 ? -13.592 43.481 13.001 1.00 29.38 ? 26 VAL A CG2 1 ATOM 64 N N . VAL A 1 9 ? -10.707 41.285 12.479 1.00 29.55 ? 27 VAL A N 1 ATOM 65 C CA . VAL A 1 9 ? -9.538 42.036 12.001 1.00 28.97 ? 27 VAL A CA 1 ATOM 66 C C . VAL A 1 9 ? -9.978 43.043 10.950 1.00 29.64 ? 27 VAL A C 1 ATOM 67 O O . VAL A 1 9 ? -10.861 42.763 10.126 1.00 28.83 ? 27 VAL A O 1 ATOM 68 C CB . VAL A 1 9 ? -8.380 41.152 11.552 1.00 28.93 ? 27 VAL A CB 1 ATOM 69 C CG1 . VAL A 1 9 ? -7.883 40.318 12.748 1.00 25.27 ? 27 VAL A CG1 1 ATOM 70 C CG2 . VAL A 1 9 ? -8.748 40.287 10.323 1.00 27.79 ? 27 VAL A CG2 1 ATOM 71 N N . SER A 1 10 ? -9.419 44.242 11.054 1.00 28.93 ? 28 SER A N 1 ATOM 72 C CA . SER A 1 10 ? -9.784 45.348 10.167 1.00 29.43 ? 28 SER A CA 1 ATOM 73 C C . SER A 1 10 ? -8.584 46.276 9.954 1.00 28.74 ? 28 SER A C 1 ATOM 74 O O . SER A 1 10 ? -7.454 45.908 10.221 1.00 29.04 ? 28 SER A O 1 ATOM 75 C CB . SER A 1 10 ? -11.013 46.121 10.714 1.00 29.90 ? 28 SER A CB 1 ATOM 76 O OG . SER A 1 10 ? -11.572 47.040 9.758 1.00 27.09 ? 28 SER A OG 1 ATOM 77 N N . HIS A 1 11 ? -8.860 47.472 9.488 1.00 28.83 ? 29 HIS A N 1 ATOM 78 C CA . HIS A 1 11 ? -7.840 48.466 9.172 1.00 28.68 ? 29 HIS A CA 1 ATOM 79 C C . HIS A 1 11 ? -8.367 49.886 9.293 1.00 30.47 ? 29 HIS A C 1 ATOM 80 O O . HIS A 1 11 ? -9.501 50.186 8.925 1.00 31.19 ? 29 HIS A O 1 ATOM 81 C CB . HIS A 1 11 ? -7.231 48.228 7.772 1.00 29.46 ? 29 HIS A CB 1 ATOM 82 C CG . HIS A 1 11 ? -8.236 47.856 6.714 1.00 28.79 ? 29 HIS A CG 1 ATOM 83 N ND1 . HIS A 1 11 ? -9.024 48.790 6.076 1.00 29.44 ? 29 HIS A ND1 1 ATOM 84 C CD2 . HIS A 1 11 ? -8.596 46.651 6.215 1.00 27.19 ? 29 HIS A CD2 1 ATOM 85 C CE1 . HIS A 1 11 ? -9.815 48.175 5.216 1.00 30.64 ? 29 HIS A CE1 1 ATOM 86 N NE2 . HIS A 1 11 ? -9.575 46.875 5.278 1.00 31.02 ? 29 HIS A NE2 1 ATOM 87 N N . LEU A 1 12 ? -7.518 50.762 9.815 1.00 30.74 ? 30 LEU A N 1 ATOM 88 C CA . LEU A 1 12 ? -7.869 52.158 10.000 1.00 32.03 ? 30 LEU A CA 1 ATOM 89 C C . LEU A 1 12 ? -8.099 52.809 8.651 1.00 32.90 ? 30 LEU A C 1 ATOM 90 O O . LEU A 1 12 ? -9.018 53.635 8.465 1.00 33.63 ? 30 LEU A O 1 ATOM 91 C CB . LEU A 1 12 ? -6.764 52.900 10.731 1.00 32.58 ? 30 LEU A CB 1 ATOM 92 C CG . LEU A 1 12 ? -6.924 54.370 11.044 1.00 33.31 ? 30 LEU A CG 1 ATOM 93 C CD1 . LEU A 1 12 ? -7.967 54.581 12.149 1.00 35.90 ? 30 LEU A CD1 1 ATOM 94 C CD2 . LEU A 1 12 ? -5.547 54.944 11.453 1.00 35.24 ? 30 LEU A CD2 1 ATOM 95 N N . ASN A 1 13 ? -7.230 52.471 7.716 1.00 31.96 ? 31 ASN A N 1 ATOM 96 C CA . ASN A 1 13 ? -7.344 52.984 6.360 1.00 31.53 ? 31 ASN A CA 1 ATOM 97 C C . ASN A 1 13 ? -6.869 51.890 5.416 1.00 31.09 ? 31 ASN A C 1 ATOM 98 O O . ASN A 1 13 ? -6.912 50.700 5.763 1.00 30.59 ? 31 ASN A O 1 ATOM 99 C CB . ASN A 1 13 ? -6.562 54.286 6.219 1.00 31.99 ? 31 ASN A CB 1 ATOM 100 C CG . ASN A 1 13 ? -5.111 54.139 6.688 1.00 33.63 ? 31 ASN A CG 1 ATOM 101 O OD1 . ASN A 1 13 ? -4.446 53.161 6.337 1.00 32.64 ? 31 ASN A OD1 1 ATOM 102 N ND2 . ASN A 1 13 ? -4.619 55.108 7.460 1.00 33.50 ? 31 ASN A ND2 1 ATOM 103 N N . GLY A 1 14 ? -6.474 52.268 4.219 1.00 30.66 ? 32 GLY A N 1 ATOM 104 C CA . GLY A 1 14 ? -6.100 51.277 3.191 1.00 31.40 ? 32 GLY A CA 1 ATOM 105 C C . GLY A 1 14 ? -4.703 50.712 3.365 1.00 30.93 ? 32 GLY A C 1 ATOM 106 O O . GLY A 1 14 ? -4.272 49.816 2.655 1.00 31.34 ? 32 GLY A O 1 ATOM 107 N N . ASP A 1 15 ? -3.998 51.261 4.322 1.00 30.65 ? 33 ASP A N 1 ATOM 108 C CA . ASP A 1 15 ? -2.571 50.922 4.497 1.00 30.82 ? 33 ASP A CA 1 ATOM 109 C C . ASP A 1 15 ? -2.407 49.754 5.415 1.00 30.30 ? 33 ASP A C 1 ATOM 110 O O . ASP A 1 15 ? -2.074 49.912 6.580 1.00 31.41 ? 33 ASP A O 1 ATOM 111 C CB . ASP A 1 15 ? -1.792 52.133 5.043 1.00 30.49 ? 33 ASP A CB 1 ATOM 112 C CG . ASP A 1 15 ? -0.299 51.987 4.864 1.00 30.40 ? 33 ASP A CG 1 ATOM 113 O OD1 . ASP A 1 15 ? 0.183 50.974 4.349 1.00 31.90 ? 33 ASP A OD1 1 ATOM 114 O OD2 . ASP A 1 15 ? 0.390 52.923 5.215 1.00 29.25 ? 33 ASP A OD2 1 ATOM 115 N N . TRP A 1 16 ? -2.694 48.578 4.890 1.00 29.60 ? 34 TRP A N 1 ATOM 116 C CA . TRP A 1 16 ? -2.606 47.315 5.649 1.00 28.98 ? 34 TRP A CA 1 ATOM 117 C C . TRP A 1 16 ? -2.162 46.166 4.785 1.00 27.79 ? 34 TRP A C 1 ATOM 118 O O . TRP A 1 16 ? -2.191 46.230 3.567 1.00 28.31 ? 34 TRP A O 1 ATOM 119 C CB . TRP A 1 16 ? -3.956 46.937 6.290 1.00 29.63 ? 34 TRP A CB 1 ATOM 120 C CG . TRP A 1 16 ? -5.056 46.655 5.264 1.00 29.26 ? 34 TRP A CG 1 ATOM 121 C CD1 . TRP A 1 16 ? -5.859 47.583 4.641 1.00 31.06 ? 34 TRP A CD1 1 ATOM 122 C CD2 . TRP A 1 16 ? -5.407 45.388 4.700 1.00 29.42 ? 34 TRP A CD2 1 ATOM 123 N NE1 . TRP A 1 16 ? -6.700 46.961 3.750 1.00 28.98 ? 34 TRP A NE1 1 ATOM 124 C CE2 . TRP A 1 16 ? -6.443 45.617 3.764 1.00 30.20 ? 34 TRP A CE2 1 ATOM 125 C CE3 . TRP A 1 16 ? -4.942 44.086 4.880 1.00 28.92 ? 34 TRP A CE3 1 ATOM 126 C CZ2 . TRP A 1 16 ? -7.038 44.591 3.052 1.00 28.00 ? 34 TRP A CZ2 1 ATOM 127 C CZ3 . TRP A 1 16 ? -5.526 43.068 4.166 1.00 30.47 ? 34 TRP A CZ3 1 ATOM 128 C CH2 . TRP A 1 16 ? -6.578 43.334 3.254 1.00 30.56 ? 34 TRP A CH2 1 ATOM 129 N N . PHE A 1 17 ? -1.761 45.104 5.440 1.00 27.08 ? 35 PHE A N 1 ATOM 130 C CA . PHE A 1 17 ? -1.286 43.905 4.750 1.00 26.90 ? 35 PHE A CA 1 ATOM 131 C C . PHE A 1 17 ? -1.520 42.648 5.548 1.00 26.92 ? 35 PHE A C 1 ATOM 132 O O . PHE A 1 17 ? -1.328 42.645 6.766 1.00 27.77 ? 35 PHE A O 1 ATOM 133 C CB . PHE A 1 17 ? 0.190 44.015 4.383 1.00 26.93 ? 35 PHE A CB 1 ATOM 134 C CG . PHE A 1 17 ? 0.562 43.134 3.227 1.00 26.17 ? 35 PHE A CG 1 ATOM 135 C CD1 . PHE A 1 17 ? 0.557 43.623 1.952 1.00 25.88 ? 35 PHE A CD1 1 ATOM 136 C CD2 . PHE A 1 17 ? 0.841 41.786 3.417 1.00 28.83 ? 35 PHE A CD2 1 ATOM 137 C CE1 . PHE A 1 17 ? 0.864 42.784 0.880 1.00 27.76 ? 35 PHE A CE1 1 ATOM 138 C CE2 . PHE A 1 17 ? 1.112 40.950 2.345 1.00 26.85 ? 35 PHE A CE2 1 ATOM 139 C CZ . PHE A 1 17 ? 1.124 41.452 1.099 1.00 28.69 ? 35 PHE A CZ 1 ATOM 140 N N . LEU A 1 18 ? -1.948 41.591 4.860 1.00 26.38 ? 36 LEU A N 1 ATOM 141 C CA . LEU A 1 18 ? -2.206 40.322 5.477 1.00 26.00 ? 36 LEU A CA 1 ATOM 142 C C . LEU A 1 18 ? -1.321 39.224 5.001 1.00 25.38 ? 36 LEU A C 1 ATOM 143 O O . LEU A 1 18 ? -1.145 39.033 3.810 1.00 26.37 ? 36 LEU A O 1 ATOM 144 C CB . LEU A 1 18 ? -3.660 39.923 5.245 1.00 27.25 ? 36 LEU A CB 1 ATOM 145 C CG . LEU A 1 18 ? -4.020 38.466 5.551 1.00 25.88 ? 36 LEU A CG 1 ATOM 146 C CD1 . LEU A 1 18 ? -4.022 38.270 7.067 1.00 25.86 ? 36 LEU A CD1 1 ATOM 147 C CD2 . LEU A 1 18 ? -5.380 38.094 4.919 1.00 27.91 ? 36 LEU A CD2 1 ATOM 148 N N . PHE A 1 19 ? -0.813 38.470 5.965 1.00 25.64 ? 37 PHE A N 1 ATOM 149 C CA . PHE A 1 19 ? 0.037 37.276 5.727 1.00 25.91 ? 37 PHE A CA 1 ATOM 150 C C . PHE A 1 19 ? -0.741 36.027 6.126 1.00 26.13 ? 37 PHE A C 1 ATOM 151 O O . PHE A 1 19 ? -1.312 35.960 7.205 1.00 25.98 ? 37 PHE A O 1 ATOM 152 C CB . PHE A 1 19 ? 1.330 37.335 6.527 1.00 26.20 ? 37 PHE A CB 1 ATOM 153 C CG . PHE A 1 19 ? 2.254 38.405 6.095 1.00 24.54 ? 37 PHE A CG 1 ATOM 154 C CD1 . PHE A 1 19 ? 2.977 38.271 4.949 1.00 24.95 ? 37 PHE A CD1 1 ATOM 155 C CD2 . PHE A 1 19 ? 2.394 39.546 6.827 1.00 25.92 ? 37 PHE A CD2 1 ATOM 156 C CE1 . PHE A 1 19 ? 3.789 39.275 4.527 1.00 25.53 ? 37 PHE A CE1 1 ATOM 157 C CE2 . PHE A 1 19 ? 3.246 40.539 6.430 1.00 25.28 ? 37 PHE A CE2 1 ATOM 158 C CZ . PHE A 1 19 ? 3.921 40.410 5.275 1.00 24.43 ? 37 PHE A CZ 1 ATOM 159 N N . GLY A 1 20 ? -0.776 35.038 5.240 1.00 26.59 ? 38 GLY A N 1 ATOM 160 C CA . GLY A 1 20 ? -1.699 33.911 5.430 1.00 27.18 ? 38 GLY A CA 1 ATOM 161 C C . GLY A 1 20 ? -1.305 32.587 4.833 1.00 27.98 ? 38 GLY A C 1 ATOM 162 O O . GLY A 1 20 ? -0.153 32.345 4.461 1.00 27.19 ? 38 GLY A O 1 ATOM 163 N N . ASP A 1 21 ? -2.310 31.721 4.776 1.00 27.85 ? 39 ASP A N 1 ATOM 164 C CA . ASP A 1 21 ? -2.173 30.377 4.292 1.00 28.51 ? 39 ASP A CA 1 ATOM 165 C C . ASP A 1 21 ? -3.319 30.084 3.289 1.00 28.91 ? 39 ASP A C 1 ATOM 166 O O . ASP A 1 21 ? -3.874 30.989 2.660 1.00 25.51 ? 39 ASP A O 1 ATOM 167 C CB . ASP A 1 21 ? -2.122 29.357 5.454 1.00 28.51 ? 39 ASP A CB 1 ATOM 168 C CG . ASP A 1 21 ? -3.341 29.408 6.379 1.00 30.15 ? 39 ASP A CG 1 ATOM 169 O OD1 . ASP A 1 21 ? -4.452 29.865 5.965 1.00 28.00 ? 39 ASP A OD1 1 ATOM 170 O OD2 . ASP A 1 21 ? -3.159 28.955 7.540 1.00 29.44 ? 39 ASP A OD2 1 ATOM 171 N N . SER A 1 22 ? -3.687 28.827 3.157 1.00 29.74 ? 40 SER A N 1 ATOM 172 C CA . SER A 1 22 ? -4.634 28.530 2.097 1.00 31.02 ? 40 SER A CA 1 ATOM 173 C C . SER A 1 22 ? -5.963 29.250 2.339 1.00 30.30 ? 40 SER A C 1 ATOM 174 O O . SER A 1 22 ? -6.602 29.688 1.409 1.00 30.47 ? 40 SER A O 1 ATOM 175 C CB . SER A 1 22 ? -4.842 27.046 1.916 1.00 32.35 ? 40 SER A CB 1 ATOM 176 O OG . SER A 1 22 ? -5.969 26.678 2.608 1.00 37.96 ? 40 SER A OG 1 ATOM 177 N N . ARG A 1 23 ? -6.294 29.495 3.602 1.00 29.89 ? 41 ARG A N 1 ATOM 178 C CA . ARG A 1 23 ? -7.574 30.091 3.969 1.00 28.77 ? 41 ARG A CA 1 ATOM 179 C C . ARG A 1 23 ? -7.679 31.534 3.536 1.00 28.79 ? 41 ARG A C 1 ATOM 180 O O . ARG A 1 23 ? -8.732 32.156 3.673 1.00 28.03 ? 41 ARG A O 1 ATOM 181 C CB . ARG A 1 23 ? -7.822 29.913 5.456 1.00 28.42 ? 41 ARG A CB 1 ATOM 182 C CG . ARG A 1 23 ? -7.969 28.492 5.845 1.00 27.73 ? 41 ARG A CG 1 ATOM 183 C CD . ARG A 1 23 ? -7.574 28.277 7.265 1.00 30.18 ? 41 ARG A CD 1 ATOM 184 N NE . ARG A 1 23 ? -7.902 26.954 7.768 1.00 31.83 ? 41 ARG A NE 1 ATOM 185 C CZ . ARG A 1 23 ? -7.703 26.576 9.036 1.00 34.48 ? 41 ARG A CZ 1 ATOM 186 N NH1 . ARG A 1 23 ? -7.136 27.417 9.911 1.00 33.48 ? 41 ARG A NH1 1 ATOM 187 N NH2 . ARG A 1 23 ? -8.061 25.357 9.441 1.00 34.96 ? 41 ARG A NH2 1 ATOM 188 N N . SER A 1 24 ? -6.569 32.071 3.020 1.00 27.79 ? 42 SER A N 1 ATOM 189 C CA . SER A 1 24 ? -6.557 33.407 2.410 1.00 28.29 ? 42 SER A CA 1 ATOM 190 C C . SER A 1 24 ? -5.727 33.467 1.122 1.00 28.72 ? 42 SER A C 1 ATOM 191 O O . SER A 1 24 ? -5.330 34.567 0.673 1.00 30.16 ? 42 SER A O 1 ATOM 192 C CB . SER A 1 24 ? -6.056 34.521 3.397 1.00 28.42 ? 42 SER A CB 1 ATOM 193 O OG . SER A 1 24 ? -4.757 34.211 3.959 1.00 27.97 ? 42 SER A OG 1 ATOM 194 N N . ASP A 1 25 ? -5.459 32.301 0.555 1.00 28.68 ? 43 ASP A N 1 ATOM 195 C CA . ASP A 1 25 ? -4.667 32.193 -0.682 1.00 29.35 ? 43 ASP A CA 1 ATOM 196 C C . ASP A 1 25 ? -5.529 32.146 -1.927 1.00 30.55 ? 43 ASP A C 1 ATOM 197 O O . ASP A 1 25 ? -6.015 31.072 -2.330 1.00 29.70 ? 43 ASP A O 1 ATOM 198 C CB . ASP A 1 25 ? -3.850 30.935 -0.648 1.00 28.67 ? 43 ASP A CB 1 ATOM 199 C CG . ASP A 1 25 ? -3.004 30.758 -1.868 1.00 30.74 ? 43 ASP A CG 1 ATOM 200 O OD1 . ASP A 1 25 ? -2.936 31.686 -2.707 1.00 30.53 ? 43 ASP A OD1 1 ATOM 201 O OD2 . ASP A 1 25 ? -2.377 29.697 -1.944 1.00 32.32 ? 43 ASP A OD2 1 ATOM 202 N N . CYS A 1 26 ? -5.671 33.310 -2.537 1.00 32.18 ? 44 CYS A N 1 ATOM 203 C CA . CYS A 1 26 ? -6.521 33.462 -3.720 1.00 33.65 ? 44 CYS A CA 1 ATOM 204 C C . CYS A 1 26 ? -6.022 32.633 -4.895 1.00 35.25 ? 44 CYS A C 1 ATOM 205 O O . CYS A 1 26 ? -6.811 32.263 -5.764 1.00 35.57 ? 44 CYS A O 1 ATOM 206 C CB . CYS A 1 26 ? -6.601 34.908 -4.150 1.00 33.72 ? 44 CYS A CB 1 ATOM 207 S SG . CYS A 1 26 ? -7.406 35.897 -2.942 1.00 36.22 ? 44 CYS A SG 1 ATOM 208 N N . ASN A 1 27 ? -4.732 32.312 -4.896 1.00 34.50 ? 45 ASN A N 1 ATOM 209 C CA . ASN A 1 27 ? -4.158 31.599 -6.024 1.00 35.25 ? 45 ASN A CA 1 ATOM 210 C C . ASN A 1 27 ? -4.477 30.113 -5.972 1.00 34.15 ? 45 ASN A C 1 ATOM 211 O O . ASN A 1 27 ? -4.305 29.399 -6.933 1.00 35.14 ? 45 ASN A O 1 ATOM 212 C CB . ASN A 1 27 ? -2.656 31.798 -6.083 1.00 35.88 ? 45 ASN A CB 1 ATOM 213 C CG . ASN A 1 27 ? -2.283 33.267 -6.165 1.00 41.59 ? 45 ASN A CG 1 ATOM 214 O OD1 . ASN A 1 27 ? -1.384 33.722 -5.451 1.00 51.05 ? 45 ASN A OD1 1 ATOM 215 N ND2 . ASN A 1 27 ? -2.991 34.033 -7.020 1.00 43.17 ? 45 ASN A ND2 1 ATOM 216 N N . HIS A 1 28 ? -4.912 29.649 -4.833 1.00 33.31 ? 46 HIS A N 1 ATOM 217 C CA . HIS A 1 28 ? -5.111 28.219 -4.658 1.00 33.37 ? 46 HIS A CA 1 ATOM 218 C C . HIS A 1 28 ? -6.297 27.725 -5.502 1.00 33.43 ? 46 HIS A C 1 ATOM 219 O O . HIS A 1 28 ? -6.445 26.537 -5.810 1.00 34.15 ? 46 HIS A O 1 ATOM 220 C CB . HIS A 1 28 ? -5.368 27.876 -3.199 1.00 33.40 ? 46 HIS A CB 1 ATOM 221 C CG . HIS A 1 28 ? -5.553 26.415 -2.963 1.00 31.38 ? 46 HIS A CG 1 ATOM 222 N ND1 . HIS A 1 28 ? -4.603 25.488 -3.305 1.00 33.24 ? 46 HIS A ND1 1 ATOM 223 C CD2 . HIS A 1 28 ? -6.599 25.720 -2.464 1.00 32.23 ? 46 HIS A CD2 1 ATOM 224 C CE1 . HIS A 1 28 ? -5.040 24.282 -2.983 1.00 35.35 ? 46 HIS A CE1 1 ATOM 225 N NE2 . HIS A 1 28 ? -6.246 24.399 -2.461 1.00 30.15 ? 46 HIS A NE2 1 ATOM 226 N N . VAL A 1 29 ? -7.150 28.661 -5.855 1.00 34.46 ? 47 VAL A N 1 ATOM 227 C CA . VAL A 1 29 ? -8.434 28.327 -6.529 1.00 33.92 ? 47 VAL A CA 1 ATOM 228 C C . VAL A 1 29 ? -8.147 27.542 -7.834 1.00 34.92 ? 47 VAL A C 1 ATOM 229 O O . VAL A 1 29 ? -8.965 26.749 -8.303 1.00 34.25 ? 47 VAL A O 1 ATOM 230 C CB . VAL A 1 29 ? -9.291 29.594 -6.831 1.00 33.58 ? 47 VAL A CB 1 ATOM 231 C CG1 . VAL A 1 29 ? -8.694 30.392 -7.949 1.00 30.37 ? 47 VAL A CG1 1 ATOM 232 C CG2 . VAL A 1 29 ? -10.800 29.224 -7.136 1.00 33.96 ? 47 VAL A CG2 1 ATOM 233 N N . VAL A 1 30 ? -6.968 27.750 -8.408 1.00 35.90 ? 48 VAL A N 1 ATOM 234 C CA . VAL A 1 30 ? -6.680 27.161 -9.709 1.00 36.83 ? 48 VAL A CA 1 ATOM 235 C C . VAL A 1 30 ? -6.389 25.684 -9.506 1.00 38.35 ? 48 VAL A C 1 ATOM 236 O O . VAL A 1 30 ? -6.385 24.902 -10.455 1.00 39.85 ? 48 VAL A O 1 ATOM 237 C CB . VAL A 1 30 ? -5.536 27.883 -10.498 1.00 36.54 ? 48 VAL A CB 1 ATOM 238 C CG1 . VAL A 1 30 ? -5.847 29.349 -10.672 1.00 36.10 ? 48 VAL A CG1 1 ATOM 239 C CG2 . VAL A 1 30 ? -4.173 27.655 -9.850 1.00 36.13 ? 48 VAL A CG2 1 ATOM 240 N N . ASN A 1 31 ? -6.190 25.294 -8.255 1.00 39.50 ? 49 ASN A N 1 ATOM 241 C CA . ASN A 1 31 ? -5.930 23.886 -7.931 1.00 40.68 ? 49 ASN A CA 1 ATOM 242 C C . ASN A 1 31 ? -7.136 23.257 -7.289 1.00 41.61 ? 49 ASN A C 1 ATOM 243 O O . ASN A 1 31 ? -7.058 22.219 -6.639 1.00 42.16 ? 49 ASN A O 1 ATOM 244 C CB . ASN A 1 31 ? -4.714 23.736 -7.043 1.00 41.31 ? 49 ASN A CB 1 ATOM 245 C CG . ASN A 1 31 ? -3.479 24.232 -7.721 1.00 41.91 ? 49 ASN A CG 1 ATOM 246 O OD1 . ASN A 1 31 ? -3.261 23.931 -8.883 1.00 46.45 ? 49 ASN A OD1 1 ATOM 247 N ND2 . ASN A 1 31 ? -2.707 25.046 -7.042 1.00 38.88 ? 49 ASN A ND2 1 ATOM 248 N N . THR A 1 32 ? -8.268 23.910 -7.502 1.00 42.40 ? 50 THR A N 1 ATOM 249 C CA . THR A 1 32 ? -9.562 23.331 -7.158 1.00 42.37 ? 50 THR A CA 1 ATOM 250 C C . THR A 1 32 ? -10.362 23.070 -8.439 1.00 43.62 ? 50 THR A C 1 ATOM 251 O O . THR A 1 32 ? -10.429 23.902 -9.358 1.00 43.13 ? 50 THR A O 1 ATOM 252 C CB . THR A 1 32 ? -10.371 24.240 -6.242 1.00 41.81 ? 50 THR A CB 1 ATOM 253 O OG1 . THR A 1 32 ? -10.738 25.427 -6.943 1.00 39.31 ? 50 THR A OG1 1 ATOM 254 C CG2 . THR A 1 32 ? -9.586 24.564 -4.949 1.00 39.79 ? 50 THR A CG2 1 ATOM 255 N N . ASN A 1 33 ? -10.955 21.889 -8.476 1.00 45.41 ? 51 ASN A N 1 ATOM 256 C CA . ASN A 1 33 ? -11.733 21.456 -9.634 1.00 46.93 ? 51 ASN A CA 1 ATOM 257 C C . ASN A 1 33 ? -13.015 20.710 -9.230 1.00 46.92 ? 51 ASN A C 1 ATOM 258 O O . ASN A 1 33 ? -12.961 19.656 -8.588 1.00 46.51 ? 51 ASN A O 1 ATOM 259 C CB . ASN A 1 33 ? -10.842 20.589 -10.507 1.00 47.86 ? 51 ASN A CB 1 ATOM 260 C CG . ASN A 1 33 ? -11.559 20.089 -11.752 1.00 51.92 ? 51 ASN A CG 1 ATOM 261 O OD1 . ASN A 1 33 ? -12.470 20.746 -12.272 1.00 54.66 ? 51 ASN A OD1 1 ATOM 262 N ND2 . ASN A 1 33 ? -11.151 18.913 -12.232 1.00 56.93 ? 51 ASN A ND2 1 ATOM 263 N N . PRO A 1 34 ? -14.174 21.300 -9.545 1.00 46.76 ? 52 PRO A N 1 ATOM 264 C CA . PRO A 1 34 ? -14.165 22.597 -10.189 1.00 46.97 ? 52 PRO A CA 1 ATOM 265 C C . PRO A 1 34 ? -13.674 23.747 -9.296 1.00 46.94 ? 52 PRO A C 1 ATOM 266 O O . PRO A 1 34 ? -13.487 23.608 -8.046 1.00 46.98 ? 52 PRO A O 1 ATOM 267 C CB . PRO A 1 34 ? -15.635 22.836 -10.556 1.00 47.30 ? 52 PRO A CB 1 ATOM 268 C CG . PRO A 1 34 ? -16.413 22.001 -9.639 1.00 47.10 ? 52 PRO A CG 1 ATOM 269 C CD . PRO A 1 34 ? -15.528 20.859 -9.183 1.00 47.36 ? 52 PRO A CD 1 ATOM 270 N N . ARG A 1 35 ? -13.480 24.874 -9.967 1.00 45.13 ? 53 ARG A N 1 ATOM 271 C CA . ARG A 1 35 ? -12.976 26.048 -9.293 1.00 44.40 ? 53 ARG A CA 1 ATOM 272 C C . ARG A 1 35 ? -13.967 26.482 -8.244 1.00 44.24 ? 53 ARG A C 1 ATOM 273 O O . ARG A 1 35 ? -15.127 26.738 -8.530 1.00 44.06 ? 53 ARG A O 1 ATOM 274 C CB . ARG A 1 35 ? -12.607 27.171 -10.271 1.00 43.82 ? 53 ARG A CB 1 ATOM 275 C CG . ARG A 1 35 ? -11.270 26.814 -10.903 1.00 42.96 ? 53 ARG A CG 1 ATOM 276 C CD . ARG A 1 35 ? -10.546 27.986 -11.401 1.00 40.76 ? 53 ARG A CD 1 ATOM 277 N NE . ARG A 1 35 ? -9.442 27.598 -12.268 1.00 35.46 ? 53 ARG A NE 1 ATOM 278 C CZ . ARG A 1 35 ? -8.755 28.467 -12.986 1.00 35.10 ? 53 ARG A CZ 1 ATOM 279 N NH1 . ARG A 1 35 ? -9.038 29.767 -12.927 1.00 34.61 ? 53 ARG A NH1 1 ATOM 280 N NH2 . ARG A 1 35 ? -7.793 28.045 -13.776 1.00 37.09 ? 53 ARG A NH2 1 ATOM 281 N N . ASN A 1 36 ? -13.474 26.547 -7.010 1.00 43.33 ? 54 ASN A N 1 ATOM 282 C CA . ASN A 1 36 ? -14.293 26.904 -5.878 1.00 42.62 ? 54 ASN A CA 1 ATOM 283 C C . ASN A 1 36 ? -13.530 27.719 -4.801 1.00 41.18 ? 54 ASN A C 1 ATOM 284 O O . ASN A 1 36 ? -12.531 27.280 -4.259 1.00 40.41 ? 54 ASN A O 1 ATOM 285 C CB . ASN A 1 36 ? -14.867 25.613 -5.300 1.00 42.90 ? 54 ASN A CB 1 ATOM 286 C CG . ASN A 1 36 ? -16.036 25.861 -4.345 1.00 47.17 ? 54 ASN A CG 1 ATOM 287 O OD1 . ASN A 1 36 ? -16.108 26.888 -3.653 1.00 44.30 ? 54 ASN A OD1 1 ATOM 288 N ND2 . ASN A 1 36 ? -16.966 24.913 -4.314 1.00 53.25 ? 54 ASN A ND2 1 ATOM 289 N N . TYR A 1 37 ? -14.052 28.889 -4.487 1.00 40.19 ? 55 TYR A N 1 ATOM 290 C CA . TYR A 1 37 ? -13.393 29.786 -3.513 1.00 39.66 ? 55 TYR A CA 1 ATOM 291 C C . TYR A 1 37 ? -13.708 29.493 -2.056 1.00 39.07 ? 55 TYR A C 1 ATOM 292 O O . TYR A 1 37 ? -13.220 30.193 -1.162 1.00 37.89 ? 55 TYR A O 1 ATOM 293 C CB . TYR A 1 37 ? -13.713 31.238 -3.805 1.00 38.83 ? 55 TYR A CB 1 ATOM 294 C CG . TYR A 1 37 ? -13.083 31.772 -5.044 1.00 39.77 ? 55 TYR A CG 1 ATOM 295 C CD1 . TYR A 1 37 ? -11.784 32.275 -5.018 1.00 36.42 ? 55 TYR A CD1 1 ATOM 296 C CD2 . TYR A 1 37 ? -13.783 31.780 -6.264 1.00 37.64 ? 55 TYR A CD2 1 ATOM 297 C CE1 . TYR A 1 37 ? -11.199 32.815 -6.156 1.00 37.58 ? 55 TYR A CE1 1 ATOM 298 C CE2 . TYR A 1 37 ? -13.202 32.301 -7.412 1.00 38.01 ? 55 TYR A CE2 1 ATOM 299 C CZ . TYR A 1 37 ? -11.903 32.805 -7.365 1.00 38.10 ? 55 TYR A CZ 1 ATOM 300 O OH . TYR A 1 37 ? -11.297 33.325 -8.494 1.00 34.22 ? 55 TYR A OH 1 ATOM 301 N N . SER A 1 38 ? -14.522 28.467 -1.813 1.00 38.75 ? 56 SER A N 1 ATOM 302 C CA . SER A 1 38 ? -15.111 28.298 -0.484 1.00 39.01 ? 56 SER A CA 1 ATOM 303 C C . SER A 1 38 ? -14.086 27.802 0.521 1.00 38.28 ? 56 SER A C 1 ATOM 304 O O . SER A 1 38 ? -14.368 27.730 1.701 1.00 38.26 ? 56 SER A O 1 ATOM 305 C CB . SER A 1 38 ? -16.368 27.391 -0.501 1.00 39.84 ? 56 SER A CB 1 ATOM 306 O OG . SER A 1 38 ? -16.018 26.024 -0.770 1.00 43.76 ? 56 SER A OG 1 ATOM 307 N N . TYR A 1 39 ? -12.900 27.452 0.026 1.00 37.34 ? 57 TYR A N 1 ATOM 308 C CA . TYR A 1 39 ? -11.813 26.911 0.880 1.00 36.05 ? 57 TYR A CA 1 ATOM 309 C C . TYR A 1 39 ? -11.194 28.034 1.737 1.00 35.34 ? 57 TYR A C 1 ATOM 310 O O . TYR A 1 39 ? -10.470 27.775 2.676 1.00 35.82 ? 57 TYR A O 1 ATOM 311 C CB . TYR A 1 39 ? -10.702 26.238 0.070 1.00 36.05 ? 57 TYR A CB 1 ATOM 312 C CG . TYR A 1 39 ? -9.999 27.212 -0.818 1.00 35.61 ? 57 TYR A CG 1 ATOM 313 C CD1 . TYR A 1 39 ? -8.900 27.978 -0.352 1.00 34.67 ? 57 TYR A CD1 1 ATOM 314 C CD2 . TYR A 1 39 ? -10.478 27.462 -2.088 1.00 33.89 ? 57 TYR A CD2 1 ATOM 315 C CE1 . TYR A 1 39 ? -8.295 28.915 -1.171 1.00 33.48 ? 57 TYR A CE1 1 ATOM 316 C CE2 . TYR A 1 39 ? -9.883 28.402 -2.915 1.00 33.18 ? 57 TYR A CE2 1 ATOM 317 C CZ . TYR A 1 39 ? -8.788 29.122 -2.465 1.00 32.82 ? 57 TYR A CZ 1 ATOM 318 O OH . TYR A 1 39 ? -8.249 30.052 -3.339 1.00 32.07 ? 57 TYR A OH 1 ATOM 319 N N . MET A 1 40 ? -11.582 29.253 1.408 1.00 34.12 ? 58 MET A N 1 ATOM 320 C CA . MET A 1 40 ? -11.105 30.474 2.025 1.00 34.09 ? 58 MET A CA 1 ATOM 321 C C . MET A 1 40 ? -12.026 31.033 3.092 1.00 34.42 ? 58 MET A C 1 ATOM 322 O O . MET A 1 40 ? -13.270 30.986 2.968 1.00 35.46 ? 58 MET A O 1 ATOM 323 C CB . MET A 1 40 ? -10.954 31.557 0.974 1.00 33.35 ? 58 MET A CB 1 ATOM 324 C CG . MET A 1 40 ? -9.775 31.311 0.064 1.00 35.15 ? 58 MET A CG 1 ATOM 325 S SD . MET A 1 40 ? -9.068 32.809 -0.617 1.00 35.23 ? 58 MET A SD 1 ATOM 326 C CE . MET A 1 40 ? -10.462 33.556 -1.418 1.00 36.16 ? 58 MET A CE 1 ATOM 327 N N . ASP A 1 41 ? -11.393 31.587 4.122 1.00 33.25 ? 59 ASP A N 1 ATOM 328 C CA . ASP A 1 41 ? -12.089 32.362 5.163 1.00 32.72 ? 59 ASP A CA 1 ATOM 329 C C . ASP A 1 41 ? -12.112 33.804 4.745 1.00 32.04 ? 59 ASP A C 1 ATOM 330 O O . ASP A 1 41 ? -13.021 34.564 5.095 1.00 32.42 ? 59 ASP A O 1 ATOM 331 C CB . ASP A 1 41 ? -11.435 32.153 6.539 1.00 32.90 ? 59 ASP A CB 1 ATOM 332 C CG . ASP A 1 41 ? -11.615 30.760 7.013 1.00 33.04 ? 59 ASP A CG 1 ATOM 333 O OD1 . ASP A 1 41 ? -12.683 30.237 6.676 1.00 32.76 ? 59 ASP A OD1 1 ATOM 334 O OD2 . ASP A 1 41 ? -10.744 30.180 7.699 1.00 30.09 ? 59 ASP A OD2 1 ATOM 335 N N . LEU A 1 42 ? -11.120 34.155 3.936 1.00 31.12 ? 60 LEU A N 1 ATOM 336 C CA . LEU A 1 42 ? -11.042 35.490 3.315 1.00 30.84 ? 60 LEU A CA 1 ATOM 337 C C . LEU A 1 42 ? -12.139 35.658 2.296 1.00 30.65 ? 60 LEU A C 1 ATOM 338 O O . LEU A 1 42 ? -12.457 34.725 1.592 1.00 31.30 ? 60 LEU A O 1 ATOM 339 C CB . LEU A 1 42 ? -9.707 35.657 2.584 1.00 30.48 ? 60 LEU A CB 1 ATOM 340 C CG . LEU A 1 42 ? -9.357 37.018 1.983 1.00 30.98 ? 60 LEU A CG 1 ATOM 341 C CD1 . LEU A 1 42 ? -8.921 38.008 3.091 1.00 28.47 ? 60 LEU A CD1 1 ATOM 342 C CD2 . LEU A 1 42 ? -8.275 36.817 0.857 1.00 29.18 ? 60 LEU A CD2 1 ATOM 343 N N . ASN A 1 43 ? -12.691 36.850 2.220 1.00 30.31 ? 61 ASN A N 1 ATOM 344 C CA . ASN A 1 43 ? -13.631 37.146 1.156 1.00 31.20 ? 61 ASN A CA 1 ATOM 345 C C . ASN A 1 43 ? -12.908 37.349 -0.182 1.00 30.33 ? 61 ASN A C 1 ATOM 346 O O . ASN A 1 43 ? -12.035 38.214 -0.295 1.00 29.09 ? 61 ASN A O 1 ATOM 347 C CB . ASN A 1 43 ? -14.504 38.365 1.454 1.00 31.01 ? 61 ASN A CB 1 ATOM 348 C CG . ASN A 1 43 ? -15.717 38.452 0.501 1.00 32.14 ? 61 ASN A CG 1 ATOM 349 O OD1 . ASN A 1 43 ? -15.555 38.701 -0.680 1.00 34.00 ? 61 ASN A OD1 1 ATOM 350 N ND2 . ASN A 1 43 ? -16.915 38.277 1.032 1.00 30.68 ? 61 ASN A ND2 1 ATOM 351 N N . PRO A 1 44 ? -13.307 36.574 -1.208 1.00 30.01 ? 62 PRO A N 1 ATOM 352 C CA . PRO A 1 44 ? -12.605 36.685 -2.469 1.00 29.49 ? 62 PRO A CA 1 ATOM 353 C C . PRO A 1 44 ? -12.691 38.019 -3.107 1.00 29.35 ? 62 PRO A C 1 ATOM 354 O O . PRO A 1 44 ? -11.922 38.281 -4.051 1.00 29.60 ? 62 PRO A O 1 ATOM 355 C CB . PRO A 1 44 ? -13.254 35.598 -3.340 1.00 30.08 ? 62 PRO A CB 1 ATOM 356 C CG . PRO A 1 44 ? -13.770 34.611 -2.418 1.00 29.17 ? 62 PRO A CG 1 ATOM 357 C CD . PRO A 1 44 ? -14.161 35.371 -1.170 1.00 29.90 ? 62 PRO A CD 1 ATOM 358 N N . ALA A 1 45 ? -13.571 38.888 -2.615 1.00 28.08 ? 63 ALA A N 1 ATOM 359 C CA . ALA A 1 45 ? -13.623 40.231 -3.156 1.00 28.28 ? 63 ALA A CA 1 ATOM 360 C C . ALA A 1 45 ? -12.289 40.952 -2.938 1.00 29.83 ? 63 ALA A C 1 ATOM 361 O O . ALA A 1 45 ? -12.024 41.991 -3.565 1.00 29.38 ? 63 ALA A O 1 ATOM 362 C CB . ALA A 1 45 ? -14.745 41.079 -2.538 1.00 28.24 ? 63 ALA A CB 1 ATOM 363 N N . LEU A 1 46 ? -11.499 40.438 -2.000 1.00 30.99 ? 64 LEU A N 1 ATOM 364 C CA . LEU A 1 46 ? -10.176 41.061 -1.664 1.00 32.07 ? 64 LEU A CA 1 ATOM 365 C C . LEU A 1 46 ? -9.035 40.482 -2.508 1.00 32.98 ? 64 LEU A C 1 ATOM 366 O O . LEU A 1 46 ? -7.865 40.855 -2.354 1.00 33.33 ? 64 LEU A O 1 ATOM 367 C CB . LEU A 1 46 ? -9.837 40.870 -0.185 1.00 31.71 ? 64 LEU A CB 1 ATOM 368 C CG . LEU A 1 46 ? -10.656 41.759 0.759 1.00 30.49 ? 64 LEU A CG 1 ATOM 369 C CD1 . LEU A 1 46 ? -10.774 41.081 2.121 1.00 28.11 ? 64 LEU A CD1 1 ATOM 370 C CD2 . LEU A 1 46 ? -10.086 43.194 0.802 1.00 28.23 ? 64 LEU A CD2 1 ATOM 371 N N . CYS A 1 47 ? -9.388 39.591 -3.424 1.00 34.24 ? 65 CYS A N 1 ATOM 372 C CA . CYS A 1 47 ? -8.376 38.872 -4.198 1.00 34.73 ? 65 CYS A CA 1 ATOM 373 C C . CYS A 1 47 ? -7.562 39.751 -5.145 1.00 36.27 ? 65 CYS A C 1 ATOM 374 O O . CYS A 1 47 ? -6.448 39.396 -5.509 1.00 38.71 ? 65 CYS A O 1 ATOM 375 C CB . CYS A 1 47 ? -8.935 37.669 -4.904 1.00 33.90 ? 65 CYS A CB 1 ATOM 376 S SG . CYS A 1 47 ? -9.243 36.364 -3.763 1.00 34.33 ? 65 CYS A SG 1 ATOM 377 N N . ASP A 1 48 ? -8.049 40.925 -5.462 1.00 37.00 ? 66 ASP A N 1 ATOM 378 C CA . ASP A 1 48 ? -7.327 41.817 -6.382 1.00 38.56 ? 66 ASP A CA 1 ATOM 379 C C . ASP A 1 48 ? -6.614 42.992 -5.659 1.00 38.21 ? 66 ASP A C 1 ATOM 380 O O . ASP A 1 48 ? -6.256 44.010 -6.267 1.00 39.02 ? 66 ASP A O 1 ATOM 381 C CB . ASP A 1 48 ? -8.329 42.383 -7.421 1.00 39.53 ? 66 ASP A CB 1 ATOM 382 C CG . ASP A 1 48 ? -7.649 42.902 -8.683 1.00 40.09 ? 66 ASP A CG 1 ATOM 383 O OD1 . ASP A 1 48 ? -6.832 42.129 -9.224 1.00 43.42 ? 66 ASP A OD1 1 ATOM 384 O OD2 . ASP A 1 48 ? -7.975 44.046 -9.142 1.00 42.34 ? 66 ASP A OD2 1 ATOM 385 N N . SER A 1 49 ? -6.452 42.870 -4.345 1.00 36.95 ? 67 SER A N 1 ATOM 386 C CA . SER A 1 49 ? -6.090 44.072 -3.530 1.00 35.81 ? 67 SER A CA 1 ATOM 387 C C . SER A 1 49 ? -4.624 44.370 -3.574 1.00 34.32 ? 67 SER A C 1 ATOM 388 O O . SER A 1 49 ? -4.232 45.517 -3.407 1.00 34.63 ? 67 SER A O 1 ATOM 389 C CB . SER A 1 49 ? -6.505 43.917 -2.071 1.00 35.69 ? 67 SER A CB 1 ATOM 390 O OG . SER A 1 49 ? -5.895 42.774 -1.498 1.00 35.69 ? 67 SER A OG 1 ATOM 391 N N . GLY A 1 50 ? -3.822 43.340 -3.801 1.00 32.53 ? 68 GLY A N 1 ATOM 392 C CA . GLY A 1 50 ? -2.366 43.471 -3.686 1.00 31.78 ? 68 GLY A CA 1 ATOM 393 C C . GLY A 1 50 ? -1.941 43.570 -2.212 1.00 31.24 ? 68 GLY A C 1 ATOM 394 O O . GLY A 1 50 ? -0.859 44.000 -1.894 1.00 30.03 ? 68 GLY A O 1 ATOM 395 N N . LYS A 1 51 ? -2.825 43.167 -1.309 1.00 30.66 ? 69 LYS A N 1 ATOM 396 C CA . LYS A 1 51 ? -2.573 43.319 0.153 1.00 30.03 ? 69 LYS A CA 1 ATOM 397 C C . LYS A 1 51 ? -2.462 42.037 0.916 1.00 29.07 ? 69 LYS A C 1 ATOM 398 O O . LYS A 1 51 ? -2.559 42.046 2.106 1.00 27.40 ? 69 LYS A O 1 ATOM 399 C CB . LYS A 1 51 ? -3.683 44.162 0.777 1.00 30.18 ? 69 LYS A CB 1 ATOM 400 C CG . LYS A 1 51 ? -3.645 45.607 0.260 1.00 32.17 ? 69 LYS A CG 1 ATOM 401 C CD . LYS A 1 51 ? -4.720 46.510 0.745 1.00 31.69 ? 69 LYS A CD 1 ATOM 402 C CE . LYS A 1 51 ? -4.446 47.889 0.123 1.00 35.99 ? 69 LYS A CE 1 ATOM 403 N NZ . LYS A 1 51 ? -5.507 48.817 0.433 1.00 36.14 ? 69 LYS A NZ 1 ATOM 404 N N . ILE A 1 52 ? -2.308 40.933 0.199 1.00 29.56 ? 70 ILE A N 1 ATOM 405 C CA . ILE A 1 52 ? -2.204 39.616 0.774 1.00 29.17 ? 70 ILE A CA 1 ATOM 406 C C . ILE A 1 52 ? -1.027 38.852 0.200 1.00 29.70 ? 70 ILE A C 1 ATOM 407 O O . ILE A 1 52 ? -0.800 38.862 -0.998 1.00 28.61 ? 70 ILE A O 1 ATOM 408 C CB . ILE A 1 52 ? -3.447 38.707 0.456 1.00 30.15 ? 70 ILE A CB 1 ATOM 409 C CG1 . ILE A 1 52 ? -4.753 39.539 0.365 1.00 32.40 ? 70 ILE A CG1 1 ATOM 410 C CG2 . ILE A 1 52 ? -3.494 37.540 1.399 1.00 26.88 ? 70 ILE A CG2 1 ATOM 411 C CD1 . ILE A 1 52 ? -5.216 40.064 1.598 1.00 31.15 ? 70 ILE A CD1 1 ATOM 412 N N . SER A 1 53 ? -0.320 38.174 1.104 1.00 28.58 ? 71 SER A N 1 ATOM 413 C CA . SER A 1 53 ? 0.717 37.218 0.780 1.00 27.83 ? 71 SER A CA 1 ATOM 414 C C . SER A 1 53 ? 0.426 35.957 1.576 1.00 27.61 ? 71 SER A C 1 ATOM 415 O O . SER A 1 53 ? 0.657 35.901 2.775 1.00 26.63 ? 71 SER A O 1 ATOM 416 C CB . SER A 1 53 ? 2.108 37.740 1.153 1.00 27.94 ? 71 SER A CB 1 ATOM 417 O OG . SER A 1 53 ? 3.127 36.844 0.727 1.00 26.29 ? 71 SER A OG 1 ATOM 418 N N . SER A 1 54 ? -0.135 34.977 0.876 1.00 28.14 ? 72 SER A N 1 ATOM 419 C CA . SER A 1 54 ? -0.587 33.731 1.465 1.00 28.57 ? 72 SER A CA 1 ATOM 420 C C . SER A 1 54 ? -0.281 32.562 0.550 1.00 29.40 ? 72 SER A C 1 ATOM 421 O O . SER A 1 54 ? -0.304 32.696 -0.677 1.00 28.91 ? 72 SER A O 1 ATOM 422 C CB . SER A 1 54 ? -2.079 33.811 1.712 1.00 29.43 ? 72 SER A CB 1 ATOM 423 O OG . SER A 1 54 ? -2.433 34.753 2.736 1.00 27.26 ? 72 SER A OG 1 ATOM 424 N N . LYS A 1 55 ? -0.040 31.414 1.153 1.00 28.61 ? 73 LYS A N 1 ATOM 425 C CA . LYS A 1 55 ? 0.225 30.220 0.389 1.00 28.89 ? 73 LYS A CA 1 ATOM 426 C C . LYS A 1 55 ? -0.339 28.962 1.058 1.00 28.84 ? 73 LYS A C 1 ATOM 427 O O . LYS A 1 55 ? -0.012 28.614 2.206 1.00 29.29 ? 73 LYS A O 1 ATOM 428 C CB . LYS A 1 55 ? 1.716 30.044 0.199 1.00 28.97 ? 73 LYS A CB 1 ATOM 429 C CG . LYS A 1 55 ? 2.098 28.791 -0.559 1.00 31.89 ? 73 LYS A CG 1 ATOM 430 C CD . LYS A 1 55 ? 1.670 28.902 -1.968 1.00 33.07 ? 73 LYS A CD 1 ATOM 431 C CE . LYS A 1 55 ? 1.999 27.660 -2.749 1.00 37.51 ? 73 LYS A CE 1 ATOM 432 N NZ . LYS A 1 55 ? 1.339 27.817 -4.088 1.00 40.84 ? 73 LYS A NZ 1 ATOM 433 N N . ALA A 1 56 ? -1.162 28.270 0.295 1.00 28.13 ? 74 ALA A N 1 ATOM 434 C CA . ALA A 1 56 ? -1.785 27.047 0.777 1.00 28.50 ? 74 ALA A CA 1 ATOM 435 C C . ALA A 1 56 ? -0.697 26.135 1.243 1.00 28.07 ? 74 ALA A C 1 ATOM 436 O O . ALA A 1 56 ? 0.249 25.946 0.580 1.00 29.35 ? 74 ALA A O 1 ATOM 437 C CB . ALA A 1 56 ? -2.630 26.388 -0.384 1.00 27.26 ? 74 ALA A CB 1 ATOM 438 N N . GLY A 1 57 ? -0.861 25.542 2.397 1.00 29.11 ? 75 GLY A N 1 ATOM 439 C CA . GLY A 1 57 ? 0.069 24.545 2.918 1.00 29.81 ? 75 GLY A CA 1 ATOM 440 C C . GLY A 1 57 ? 1.250 25.125 3.707 1.00 29.47 ? 75 GLY A C 1 ATOM 441 O O . GLY A 1 57 ? 2.095 24.413 4.228 1.00 28.77 ? 75 GLY A O 1 ATOM 442 N N . ASN A 1 58 ? 1.345 26.438 3.704 1.00 30.07 ? 76 ASN A N 1 ATOM 443 C CA . ASN A 1 58 ? 2.506 27.082 4.326 1.00 29.61 ? 76 ASN A CA 1 ATOM 444 C C . ASN A 1 58 ? 2.202 28.022 5.485 1.00 29.85 ? 76 ASN A C 1 ATOM 445 O O . ASN A 1 58 ? 1.045 28.328 5.826 1.00 29.90 ? 76 ASN A O 1 ATOM 446 C CB . ASN A 1 58 ? 3.320 27.829 3.280 1.00 29.41 ? 76 ASN A CB 1 ATOM 447 C CG . ASN A 1 58 ? 4.805 27.474 3.345 1.00 30.40 ? 76 ASN A CG 1 ATOM 448 O OD1 . ASN A 1 58 ? 5.373 26.870 2.408 1.00 29.07 ? 76 ASN A OD1 1 ATOM 449 N ND2 . ASN A 1 58 ? 5.435 27.808 4.463 1.00 27.17 ? 76 ASN A ND2 1 ATOM 450 N N . SER A 1 59 ? 3.302 28.429 6.130 1.00 28.73 ? 77 SER A N 1 ATOM 451 C CA . SER A 1 59 ? 3.256 29.356 7.240 1.00 28.06 ? 77 SER A CA 1 ATOM 452 C C . SER A 1 59 ? 4.587 30.076 7.291 1.00 27.43 ? 77 SER A C 1 ATOM 453 O O . SER A 1 59 ? 5.599 29.566 6.790 1.00 26.65 ? 77 SER A O 1 ATOM 454 C CB . SER A 1 59 ? 2.979 28.637 8.563 1.00 28.11 ? 77 SER A CB 1 ATOM 455 O OG . SER A 1 59 ? 4.155 28.063 9.128 1.00 26.74 ? 77 SER A OG 1 ATOM 456 N N . ILE A 1 60 ? 4.594 31.244 7.893 1.00 26.68 ? 78 ILE A N 1 ATOM 457 C CA . ILE A 1 60 ? 5.875 32.011 7.987 1.00 26.52 ? 78 ILE A CA 1 ATOM 458 C C . ILE A 1 60 ? 6.979 31.166 8.647 1.00 26.56 ? 78 ILE A C 1 ATOM 459 O O . ILE A 1 60 ? 8.117 31.131 8.174 1.00 27.36 ? 78 ILE A O 1 ATOM 460 C CB . ILE A 1 60 ? 5.696 33.396 8.636 1.00 26.26 ? 78 ILE A CB 1 ATOM 461 C CG1 . ILE A 1 60 ? 4.712 34.225 7.806 1.00 26.14 ? 78 ILE A CG1 1 ATOM 462 C CG2 . ILE A 1 60 ? 7.025 34.191 8.682 1.00 26.33 ? 78 ILE A CG2 1 ATOM 463 C CD1 . ILE A 1 60 ? 4.443 35.662 8.381 1.00 25.79 ? 78 ILE A CD1 1 ATOM 464 N N . PHE A 1 61 ? 6.623 30.417 9.688 1.00 26.35 ? 79 PHE A N 1 ATOM 465 C CA . PHE A 1 61 ? 7.606 29.641 10.486 1.00 26.61 ? 79 PHE A CA 1 ATOM 466 C C . PHE A 1 61 ? 8.110 28.462 9.656 1.00 27.73 ? 79 PHE A C 1 ATOM 467 O O . PHE A 1 61 ? 9.298 28.115 9.635 1.00 27.23 ? 79 PHE A O 1 ATOM 468 C CB . PHE A 1 61 ? 6.936 29.122 11.772 1.00 26.48 ? 79 PHE A CB 1 ATOM 469 C CG . PHE A 1 61 ? 7.826 28.304 12.646 1.00 27.00 ? 79 PHE A CG 1 ATOM 470 C CD1 . PHE A 1 61 ? 8.688 28.928 13.558 1.00 27.86 ? 79 PHE A CD1 1 ATOM 471 C CD2 . PHE A 1 61 ? 7.823 26.917 12.582 1.00 28.66 ? 79 PHE A CD2 1 ATOM 472 C CE1 . PHE A 1 61 ? 9.548 28.183 14.346 1.00 27.72 ? 79 PHE A CE1 1 ATOM 473 C CE2 . PHE A 1 61 ? 8.672 26.148 13.383 1.00 28.86 ? 79 PHE A CE2 1 ATOM 474 C CZ . PHE A 1 61 ? 9.548 26.780 14.263 1.00 28.95 ? 79 PHE A CZ 1 ATOM 475 N N . ARG A 1 62 ? 7.157 27.830 8.974 1.00 27.87 ? 80 ARG A N 1 ATOM 476 C CA . ARG A 1 62 ? 7.451 26.721 8.068 1.00 28.51 ? 80 ARG A CA 1 ATOM 477 C C . ARG A 1 62 ? 8.424 27.153 6.997 1.00 27.19 ? 80 ARG A C 1 ATOM 478 O O . ARG A 1 62 ? 9.455 26.507 6.759 1.00 27.23 ? 80 ARG A O 1 ATOM 479 C CB . ARG A 1 62 ? 6.160 26.251 7.406 1.00 28.57 ? 80 ARG A CB 1 ATOM 480 C CG . ARG A 1 62 ? 6.290 25.114 6.431 1.00 32.36 ? 80 ARG A CG 1 ATOM 481 C CD . ARG A 1 62 ? 4.896 24.433 6.253 1.00 34.10 ? 80 ARG A CD 1 ATOM 482 N NE . ARG A 1 62 ? 5.040 23.309 5.362 1.00 36.67 ? 80 ARG A NE 1 ATOM 483 C CZ . ARG A 1 62 ? 4.746 22.058 5.677 1.00 37.33 ? 80 ARG A CZ 1 ATOM 484 N NH1 . ARG A 1 62 ? 4.227 21.754 6.847 1.00 37.44 ? 80 ARG A NH1 1 ATOM 485 N NH2 . ARG A 1 62 ? 4.979 21.110 4.793 1.00 39.56 ? 80 ARG A NH2 1 ATOM 486 N N . SER A 1 63 ? 8.110 28.275 6.375 1.00 26.83 ? 81 SER A N 1 ATOM 487 C CA . SER A 1 63 ? 8.989 28.798 5.338 1.00 27.55 ? 81 SER A CA 1 ATOM 488 C C . SER A 1 63 ? 10.379 29.210 5.872 1.00 28.05 ? 81 SER A C 1 ATOM 489 O O . SER A 1 63 ? 11.410 29.113 5.177 1.00 28.13 ? 81 SER A O 1 ATOM 490 C CB . SER A 1 63 ? 8.334 29.928 4.545 1.00 28.32 ? 81 SER A CB 1 ATOM 491 O OG . SER A 1 63 ? 7.308 29.428 3.671 1.00 28.99 ? 81 SER A OG 1 ATOM 492 N N . PHE A 1 64 ? 10.412 29.644 7.121 1.00 27.74 ? 82 PHE A N 1 ATOM 493 C CA . PHE A 1 64 ? 11.657 30.178 7.698 1.00 26.94 ? 82 PHE A CA 1 ATOM 494 C C . PHE A 1 64 ? 12.675 29.044 7.868 1.00 26.53 ? 82 PHE A C 1 ATOM 495 O O . PHE A 1 64 ? 13.874 29.216 7.639 1.00 24.44 ? 82 PHE A O 1 ATOM 496 C CB . PHE A 1 64 ? 11.351 30.823 9.048 1.00 27.57 ? 82 PHE A CB 1 ATOM 497 C CG . PHE A 1 64 ? 12.528 31.448 9.725 1.00 25.28 ? 82 PHE A CG 1 ATOM 498 C CD1 . PHE A 1 64 ? 12.982 32.703 9.343 1.00 28.25 ? 82 PHE A CD1 1 ATOM 499 C CD2 . PHE A 1 64 ? 13.144 30.815 10.795 1.00 25.03 ? 82 PHE A CD2 1 ATOM 500 C CE1 . PHE A 1 64 ? 14.034 33.299 9.988 1.00 26.24 ? 82 PHE A CE1 1 ATOM 501 C CE2 . PHE A 1 64 ? 14.171 31.401 11.435 1.00 25.85 ? 82 PHE A CE2 1 ATOM 502 C CZ . PHE A 1 64 ? 14.616 32.641 11.064 1.00 24.35 ? 82 PHE A CZ 1 ATOM 503 N N . HIS A 1 65 ? 12.158 27.880 8.243 1.00 26.41 ? 83 HIS A N 1 ATOM 504 C CA . HIS A 1 65 ? 12.999 26.787 8.700 1.00 27.81 ? 83 HIS A CA 1 ATOM 505 C C . HIS A 1 65 ? 13.223 25.669 7.696 1.00 28.03 ? 83 HIS A C 1 ATOM 506 O O . HIS A 1 65 ? 14.234 24.972 7.756 1.00 29.51 ? 83 HIS A O 1 ATOM 507 C CB . HIS A 1 65 ? 12.432 26.129 9.945 1.00 28.00 ? 83 HIS A CB 1 ATOM 508 C CG . HIS A 1 65 ? 12.855 26.765 11.228 1.00 29.42 ? 83 HIS A CG 1 ATOM 509 N ND1 . HIS A 1 65 ? 14.169 26.821 11.633 1.00 28.58 ? 83 HIS A ND1 1 ATOM 510 C CD2 . HIS A 1 65 ? 12.127 27.347 12.214 1.00 28.92 ? 83 HIS A CD2 1 ATOM 511 C CE1 . HIS A 1 65 ? 14.233 27.400 12.819 1.00 28.50 ? 83 HIS A CE1 1 ATOM 512 N NE2 . HIS A 1 65 ? 13.011 27.742 13.188 1.00 28.01 ? 83 HIS A NE2 1 ATOM 513 N N . PHE A 1 66 ? 12.281 25.497 6.795 1.00 28.77 ? 84 PHE A N 1 ATOM 514 C CA . PHE A 1 66 ? 12.225 24.284 5.943 1.00 29.16 ? 84 PHE A CA 1 ATOM 515 C C . PHE A 1 66 ? 12.327 24.529 4.440 1.00 28.81 ? 84 PHE A C 1 ATOM 516 O O . PHE A 1 66 ? 12.133 25.636 3.948 1.00 28.36 ? 84 PHE A O 1 ATOM 517 C CB . PHE A 1 66 ? 10.948 23.485 6.256 1.00 29.41 ? 84 PHE A CB 1 ATOM 518 C CG . PHE A 1 66 ? 10.813 23.121 7.707 1.00 30.86 ? 84 PHE A CG 1 ATOM 519 C CD1 . PHE A 1 66 ? 11.417 21.977 8.203 1.00 31.95 ? 84 PHE A CD1 1 ATOM 520 C CD2 . PHE A 1 66 ? 10.104 23.925 8.587 1.00 30.06 ? 84 PHE A CD2 1 ATOM 521 C CE1 . PHE A 1 66 ? 11.326 21.646 9.563 1.00 31.45 ? 84 PHE A CE1 1 ATOM 522 C CE2 . PHE A 1 66 ? 10.006 23.590 9.941 1.00 30.28 ? 84 PHE A CE2 1 ATOM 523 C CZ . PHE A 1 66 ? 10.610 22.460 10.426 1.00 31.61 ? 84 PHE A CZ 1 ATOM 524 N N . THR A 1 67 ? 12.614 23.439 3.720 1.00 29.04 ? 85 THR A N 1 ATOM 525 C CA . THR A 1 67 ? 12.770 23.479 2.226 1.00 28.99 ? 85 THR A CA 1 ATOM 526 C C . THR A 1 67 ? 11.455 23.771 1.561 1.00 28.94 ? 85 THR A C 1 ATOM 527 O O . THR A 1 67 ? 11.421 24.252 0.444 1.00 29.06 ? 85 THR A O 1 ATOM 528 C CB . THR A 1 67 ? 13.279 22.139 1.633 1.00 28.80 ? 85 THR A CB 1 ATOM 529 O OG1 . THR A 1 67 ? 12.399 21.112 2.062 1.00 28.86 ? 85 THR A OG1 1 ATOM 530 C CG2 . THR A 1 67 ? 14.737 21.780 2.127 1.00 29.07 ? 85 THR A CG2 1 ATOM 531 N N . ASP A 1 68 ? 10.374 23.485 2.273 1.00 29.82 ? 86 ASP A N 1 ATOM 532 C CA . ASP A 1 68 ? 9.025 23.803 1.789 1.00 30.28 ? 86 ASP A CA 1 ATOM 533 C C . ASP A 1 68 ? 8.767 25.269 2.027 1.00 30.54 ? 86 ASP A C 1 ATOM 534 O O . ASP A 1 68 ? 8.095 25.667 2.973 1.00 31.55 ? 86 ASP A O 1 ATOM 535 C CB . ASP A 1 68 ? 7.947 22.949 2.444 1.00 30.07 ? 86 ASP A CB 1 ATOM 536 C CG . ASP A 1 68 ? 6.530 23.228 1.856 1.00 30.25 ? 86 ASP A CG 1 ATOM 537 O OD1 . ASP A 1 68 ? 6.441 23.772 0.738 1.00 30.02 ? 86 ASP A OD1 1 ATOM 538 O OD2 . ASP A 1 68 ? 5.511 22.934 2.532 1.00 29.75 ? 86 ASP A OD2 1 ATOM 539 N N . PHE A 1 69 ? 9.294 26.054 1.095 1.00 31.09 ? 87 PHE A N 1 ATOM 540 C CA . PHE A 1 69 ? 9.405 27.521 1.180 1.00 30.13 ? 87 PHE A CA 1 ATOM 541 C C . PHE A 1 69 ? 8.503 28.348 0.305 1.00 31.01 ? 87 PHE A C 1 ATOM 542 O O . PHE A 1 69 ? 8.400 28.114 -0.889 1.00 31.03 ? 87 PHE A O 1 ATOM 543 C CB . PHE A 1 69 ? 10.860 27.914 0.838 1.00 29.91 ? 87 PHE A CB 1 ATOM 544 C CG . PHE A 1 69 ? 11.110 29.396 0.779 1.00 28.69 ? 87 PHE A CG 1 ATOM 545 C CD1 . PHE A 1 69 ? 11.228 30.141 1.939 1.00 28.74 ? 87 PHE A CD1 1 ATOM 546 C CD2 . PHE A 1 69 ? 11.288 30.034 -0.423 1.00 30.42 ? 87 PHE A CD2 1 ATOM 547 C CE1 . PHE A 1 69 ? 11.428 31.506 1.899 1.00 27.89 ? 87 PHE A CE1 1 ATOM 548 C CE2 . PHE A 1 69 ? 11.516 31.409 -0.488 1.00 30.21 ? 87 PHE A CE2 1 ATOM 549 C CZ . PHE A 1 69 ? 11.590 32.161 0.699 1.00 29.23 ? 87 PHE A CZ 1 ATOM 550 N N . TYR A 1 70 ? 7.929 29.390 0.916 1.00 30.55 ? 88 TYR A N 1 ATOM 551 C CA . TYR A 1 70 ? 7.176 30.434 0.203 1.00 30.41 ? 88 TYR A CA 1 ATOM 552 C C . TYR A 1 70 ? 7.684 31.785 0.639 1.00 29.95 ? 88 TYR A C 1 ATOM 553 O O . TYR A 1 70 ? 7.772 32.083 1.815 1.00 29.04 ? 88 TYR A O 1 ATOM 554 C CB . TYR A 1 70 ? 5.663 30.377 0.489 1.00 30.51 ? 88 TYR A CB 1 ATOM 555 C CG . TYR A 1 70 ? 4.836 31.409 -0.270 1.00 31.33 ? 88 TYR A CG 1 ATOM 556 C CD1 . TYR A 1 70 ? 4.578 31.250 -1.618 1.00 33.30 ? 88 TYR A CD1 1 ATOM 557 C CD2 . TYR A 1 70 ? 4.311 32.514 0.358 1.00 33.04 ? 88 TYR A CD2 1 ATOM 558 C CE1 . TYR A 1 70 ? 3.851 32.173 -2.332 1.00 33.42 ? 88 TYR A CE1 1 ATOM 559 C CE2 . TYR A 1 70 ? 3.583 33.461 -0.333 1.00 32.75 ? 88 TYR A CE2 1 ATOM 560 C CZ . TYR A 1 70 ? 3.334 33.264 -1.692 1.00 34.30 ? 88 TYR A CZ 1 ATOM 561 O OH . TYR A 1 70 ? 2.604 34.153 -2.428 1.00 33.35 ? 88 TYR A OH 1 ATOM 562 N N . ASN A 1 71 ? 7.996 32.608 -0.335 1.00 29.65 ? 89 ASN A N 1 ATOM 563 C CA . ASN A 1 71 ? 8.591 33.909 -0.056 1.00 29.25 ? 89 ASN A CA 1 ATOM 564 C C . ASN A 1 71 ? 7.570 34.969 0.337 1.00 28.45 ? 89 ASN A C 1 ATOM 565 O O . ASN A 1 71 ? 7.345 35.975 -0.370 1.00 27.40 ? 89 ASN A O 1 ATOM 566 C CB . ASN A 1 71 ? 9.405 34.400 -1.227 1.00 29.64 ? 89 ASN A CB 1 ATOM 567 C CG . ASN A 1 71 ? 10.230 35.582 -0.866 1.00 30.17 ? 89 ASN A CG 1 ATOM 568 O OD1 . ASN A 1 71 ? 10.330 35.946 0.308 1.00 29.68 ? 89 ASN A OD1 1 ATOM 569 N ND2 . ASN A 1 71 ? 10.827 36.201 -1.859 1.00 31.76 ? 89 ASN A ND2 1 ATOM 570 N N . TYR A 1 72 ? 7.002 34.752 1.516 1.00 27.83 ? 90 TYR A N 1 ATOM 571 C CA . TYR A 1 72 ? 6.081 35.723 2.097 1.00 27.12 ? 90 TYR A CA 1 ATOM 572 C C . TYR A 1 72 ? 6.674 37.117 1.984 1.00 26.88 ? 90 TYR A C 1 ATOM 573 O O . TYR A 1 72 ? 7.812 37.392 2.391 1.00 26.55 ? 90 TYR A O 1 ATOM 574 C CB . TYR A 1 72 ? 5.797 35.396 3.558 1.00 26.56 ? 90 TYR A CB 1 ATOM 575 C CG . TYR A 1 72 ? 4.882 34.237 3.778 1.00 27.09 ? 90 TYR A CG 1 ATOM 576 C CD1 . TYR A 1 72 ? 3.509 34.408 3.780 1.00 26.28 ? 90 TYR A CD1 1 ATOM 577 C CD2 . TYR A 1 72 ? 5.393 32.953 4.013 1.00 25.14 ? 90 TYR A CD2 1 ATOM 578 C CE1 . TYR A 1 72 ? 2.680 33.359 3.989 1.00 25.25 ? 90 TYR A CE1 1 ATOM 579 C CE2 . TYR A 1 72 ? 4.576 31.903 4.234 1.00 26.51 ? 90 TYR A CE2 1 ATOM 580 C CZ . TYR A 1 72 ? 3.198 32.109 4.228 1.00 27.47 ? 90 TYR A CZ 1 ATOM 581 O OH . TYR A 1 72 ? 2.350 31.040 4.445 1.00 27.11 ? 90 TYR A OH 1 ATOM 582 N N . THR A 1 73 ? 5.881 38.010 1.421 1.00 26.71 ? 91 THR A N 1 ATOM 583 C CA . THR A 1 73 ? 6.347 39.346 1.119 1.00 26.89 ? 91 THR A CA 1 ATOM 584 C C . THR A 1 73 ? 5.249 40.366 1.195 1.00 26.72 ? 91 THR A C 1 ATOM 585 O O . THR A 1 73 ? 4.252 40.289 0.495 1.00 28.25 ? 91 THR A O 1 ATOM 586 C CB . THR A 1 73 ? 7.042 39.401 -0.319 1.00 26.48 ? 91 THR A CB 1 ATOM 587 O OG1 . THR A 1 73 ? 8.126 38.495 -0.350 1.00 28.18 ? 91 THR A OG1 1 ATOM 588 C CG2 . THR A 1 73 ? 7.544 40.793 -0.676 1.00 26.08 ? 91 THR A CG2 1 ATOM 589 N N . GLY A 1 74 ? 5.440 41.368 2.029 1.00 26.42 ? 92 GLY A N 1 ATOM 590 C CA . GLY A 1 74 ? 4.445 42.402 2.121 1.00 26.99 ? 92 GLY A CA 1 ATOM 591 C C . GLY A 1 74 ? 4.834 43.587 2.943 1.00 27.54 ? 92 GLY A C 1 ATOM 592 O O . GLY A 1 74 ? 5.775 43.496 3.716 1.00 26.79 ? 92 GLY A O 1 ATOM 593 N N . GLU A 1 75 ? 4.080 44.663 2.725 1.00 27.55 ? 93 GLU A N 1 ATOM 594 C CA . GLU A 1 75 ? 4.301 45.966 3.332 1.00 29.44 ? 93 GLU A CA 1 ATOM 595 C C . GLU A 1 75 ? 2.995 46.674 3.711 1.00 29.24 ? 93 GLU A C 1 ATOM 596 O O . GLU A 1 75 ? 2.043 46.729 2.952 1.00 30.01 ? 93 GLU A O 1 ATOM 597 C CB . GLU A 1 75 ? 5.092 46.848 2.354 1.00 30.06 ? 93 GLU A CB 1 ATOM 598 C CG . GLU A 1 75 ? 5.440 48.162 2.974 1.00 32.38 ? 93 GLU A CG 1 ATOM 599 C CD . GLU A 1 75 ? 6.144 49.129 2.044 1.00 33.42 ? 93 GLU A CD 1 ATOM 600 O OE1 . GLU A 1 75 ? 6.813 48.701 1.076 1.00 32.49 ? 93 GLU A OE1 1 ATOM 601 O OE2 . GLU A 1 75 ? 6.024 50.331 2.322 1.00 33.66 ? 93 GLU A OE2 1 ATOM 602 N N . GLY A 1 76 ? 2.953 47.197 4.922 1.00 29.05 ? 94 GLY A N 1 ATOM 603 C CA . GLY A 1 76 ? 1.764 47.869 5.424 1.00 28.18 ? 94 GLY A CA 1 ATOM 604 C C . GLY A 1 76 ? 1.986 48.527 6.759 1.00 27.86 ? 94 GLY A C 1 ATOM 605 O O . GLY A 1 76 ? 2.805 48.108 7.547 1.00 26.50 ? 94 GLY A O 1 ATOM 606 N N . GLN A 1 77 ? 1.217 49.561 7.016 1.00 28.04 ? 95 GLN A N 1 ATOM 607 C CA . GLN A 1 77 ? 1.232 50.206 8.331 1.00 28.02 ? 95 GLN A CA 1 ATOM 608 C C . GLN A 1 77 ? 0.695 49.233 9.368 1.00 28.29 ? 95 GLN A C 1 ATOM 609 O O . GLN A 1 77 ? 1.383 48.856 10.349 1.00 26.37 ? 95 GLN A O 1 ATOM 610 C CB . GLN A 1 77 ? 0.418 51.494 8.346 1.00 28.08 ? 95 GLN A CB 1 ATOM 611 C CG . GLN A 1 77 ? 0.691 52.323 9.611 1.00 28.23 ? 95 GLN A CG 1 ATOM 612 C CD . GLN A 1 77 ? 2.047 53.016 9.595 1.00 29.62 ? 95 GLN A CD 1 ATOM 613 O OE1 . GLN A 1 77 ? 2.783 52.923 8.654 1.00 31.45 ? 95 GLN A OE1 1 ATOM 614 N NE2 . GLN A 1 77 ? 2.347 53.742 10.635 1.00 34.16 ? 95 GLN A NE2 1 ATOM 615 N N . GLN A 1 78 ? -0.546 48.794 9.133 1.00 28.09 ? 96 GLN A N 1 ATOM 616 C CA . GLN A 1 78 ? -1.133 47.744 9.933 1.00 27.34 ? 96 GLN A CA 1 ATOM 617 C C . GLN A 1 78 ? -0.925 46.423 9.268 1.00 27.61 ? 96 GLN A C 1 ATOM 618 O O . GLN A 1 78 ? -1.334 46.211 8.122 1.00 28.09 ? 96 GLN A O 1 ATOM 619 C CB . GLN A 1 78 ? -2.619 47.975 10.196 1.00 28.11 ? 96 GLN A CB 1 ATOM 620 C CG . GLN A 1 78 ? -2.965 49.024 11.248 1.00 27.37 ? 96 GLN A CG 1 ATOM 621 C CD . GLN A 1 78 ? -4.458 49.158 11.442 1.00 29.59 ? 96 GLN A CD 1 ATOM 622 O OE1 . GLN A 1 78 ? -5.161 49.596 10.518 1.00 28.41 ? 96 GLN A OE1 1 ATOM 623 N NE2 . GLN A 1 78 ? -4.961 48.805 12.650 1.00 24.97 ? 96 GLN A NE2 1 ATOM 624 N N . ILE A 1 79 ? -0.294 45.528 10.019 1.00 26.08 ? 97 ILE A N 1 ATOM 625 C CA . ILE A 1 79 ? -0.032 44.144 9.608 1.00 26.98 ? 97 ILE A CA 1 ATOM 626 C C . ILE A 1 79 ? -0.989 43.180 10.326 1.00 27.00 ? 97 ILE A C 1 ATOM 627 O O . ILE A 1 79 ? -1.277 43.289 11.526 1.00 26.86 ? 97 ILE A O 1 ATOM 628 C CB . ILE A 1 79 ? 1.433 43.684 9.866 1.00 26.30 ? 97 ILE A CB 1 ATOM 629 C CG1 . ILE A 1 79 ? 2.447 44.666 9.239 1.00 28.17 ? 97 ILE A CG1 1 ATOM 630 C CG2 . ILE A 1 79 ? 1.655 42.241 9.434 1.00 25.93 ? 97 ILE A CG2 1 ATOM 631 C CD1 . ILE A 1 79 ? 2.404 44.842 7.704 1.00 25.97 ? 97 ILE A CD1 1 ATOM 632 N N . ILE A 1 80 ? -1.517 42.280 9.519 1.00 26.71 ? 98 ILE A N 1 ATOM 633 C CA . ILE A 1 80 ? -2.393 41.227 9.975 1.00 26.16 ? 98 ILE A CA 1 ATOM 634 C C . ILE A 1 80 ? -1.857 39.883 9.597 1.00 25.89 ? 98 ILE A C 1 ATOM 635 O O . ILE A 1 80 ? -1.304 39.703 8.508 1.00 26.70 ? 98 ILE A O 1 ATOM 636 C CB . ILE A 1 80 ? -3.845 41.425 9.408 1.00 26.39 ? 98 ILE A CB 1 ATOM 637 C CG1 . ILE A 1 80 ? -4.334 42.852 9.694 1.00 26.46 ? 98 ILE A CG1 1 ATOM 638 C CG2 . ILE A 1 80 ? -4.777 40.408 10.037 1.00 23.74 ? 98 ILE A CG2 1 ATOM 639 C CD1 . ILE A 1 80 ? -4.395 43.787 8.507 1.00 26.23 ? 98 ILE A CD1 1 ATOM 640 N N . PHE A 1 81 ? -2.009 38.944 10.520 1.00 26.51 ? 99 PHE A N 1 ATOM 641 C CA . PHE A 1 81 ? -1.565 37.552 10.344 1.00 25.96 ? 99 PHE A CA 1 ATOM 642 C C . PHE A 1 81 ? -2.701 36.597 10.550 1.00 27.13 ? 99 PHE A C 1 ATOM 643 O O . PHE A 1 81 ? -3.434 36.708 11.513 1.00 26.68 ? 99 PHE A O 1 ATOM 644 C CB . PHE A 1 81 ? -0.483 37.182 11.379 1.00 25.90 ? 99 PHE A CB 1 ATOM 645 C CG . PHE A 1 81 ? 0.770 38.024 11.297 1.00 23.74 ? 99 PHE A CG 1 ATOM 646 C CD1 . PHE A 1 81 ? 1.893 37.558 10.621 1.00 25.32 ? 99 PHE A CD1 1 ATOM 647 C CD2 . PHE A 1 81 ? 0.853 39.219 11.969 1.00 23.61 ? 99 PHE A CD2 1 ATOM 648 C CE1 . PHE A 1 81 ? 3.043 38.325 10.564 1.00 26.11 ? 99 PHE A CE1 1 ATOM 649 C CE2 . PHE A 1 81 ? 2.009 39.998 11.931 1.00 23.65 ? 99 PHE A CE2 1 ATOM 650 C CZ . PHE A 1 81 ? 3.101 39.554 11.238 1.00 25.45 ? 99 PHE A CZ 1 ATOM 651 N N . TYR A 1 82 ? -2.797 35.634 9.647 1.00 27.23 ? 100 TYR A N 1 ATOM 652 C CA . TYR A 1 82 ? -3.727 34.502 9.746 1.00 28.01 ? 100 TYR A CA 1 ATOM 653 C C . TYR A 1 82 ? -3.046 33.265 9.176 1.00 28.10 ? 100 TYR A C 1 ATOM 654 O O . TYR A 1 82 ? -3.374 32.760 8.118 1.00 29.54 ? 100 TYR A O 1 ATOM 655 C CB . TYR A 1 82 ? -5.072 34.799 9.026 1.00 28.99 ? 100 TYR A CB 1 ATOM 656 C CG . TYR A 1 82 ? -6.100 33.681 9.153 1.00 29.14 ? 100 TYR A CG 1 ATOM 657 C CD1 . TYR A 1 82 ? -6.170 32.912 10.295 1.00 29.16 ? 100 TYR A CD1 1 ATOM 658 C CD2 . TYR A 1 82 ? -7.042 33.431 8.136 1.00 30.60 ? 100 TYR A CD2 1 ATOM 659 C CE1 . TYR A 1 82 ? -7.106 31.885 10.424 1.00 29.18 ? 100 TYR A CE1 1 ATOM 660 C CE2 . TYR A 1 82 ? -7.977 32.431 8.251 1.00 27.56 ? 100 TYR A CE2 1 ATOM 661 C CZ . TYR A 1 82 ? -8.012 31.655 9.391 1.00 30.81 ? 100 TYR A CZ 1 ATOM 662 O OH . TYR A 1 82 ? -8.947 30.650 9.554 1.00 30.23 ? 100 TYR A OH 1 ATOM 663 N N . GLU A 1 83 ? -2.058 32.811 9.913 1.00 27.58 ? 101 GLU A N 1 ATOM 664 C CA . GLU A 1 83 ? -1.290 31.629 9.562 1.00 27.27 ? 101 GLU A CA 1 ATOM 665 C C . GLU A 1 83 ? -0.614 31.056 10.783 1.00 27.04 ? 101 GLU A C 1 ATOM 666 O O . GLU A 1 83 ? -0.550 31.685 11.833 1.00 26.01 ? 101 GLU A O 1 ATOM 667 C CB . GLU A 1 83 ? -0.275 31.918 8.432 1.00 28.19 ? 101 GLU A CB 1 ATOM 668 C CG . GLU A 1 83 ? 0.585 33.189 8.585 1.00 28.09 ? 101 GLU A CG 1 ATOM 669 C CD . GLU A 1 83 ? 1.710 33.037 9.607 1.00 28.98 ? 101 GLU A CD 1 ATOM 670 O OE1 . GLU A 1 83 ? 1.979 34.021 10.363 1.00 27.96 ? 101 GLU A OE1 1 ATOM 671 O OE2 . GLU A 1 83 ? 2.295 31.931 9.679 1.00 28.07 ? 101 GLU A OE2 1 ATOM 672 N N . GLY A 1 84 ? -0.126 29.838 10.616 1.00 26.96 ? 102 GLY A N 1 ATOM 673 C CA . GLY A 1 84 ? 0.558 29.157 11.686 1.00 28.47 ? 102 GLY A CA 1 ATOM 674 C C . GLY A 1 84 ? 0.215 27.688 11.747 1.00 29.04 ? 102 GLY A C 1 ATOM 675 O O . GLY A 1 84 ? 1.030 26.864 12.127 1.00 29.55 ? 102 GLY A O 1 ATOM 676 N N . VAL A 1 85 ? -0.994 27.382 11.318 1.00 29.75 ? 103 VAL A N 1 ATOM 677 C CA . VAL A 1 85 ? -1.528 26.004 11.416 1.00 29.59 ? 103 VAL A CA 1 ATOM 678 C C . VAL A 1 85 ? -0.675 24.984 10.693 1.00 29.77 ? 103 VAL A C 1 ATOM 679 O O . VAL A 1 85 ? -0.604 23.805 11.065 1.00 31.31 ? 103 VAL A O 1 ATOM 680 C CB . VAL A 1 85 ? -3.017 25.943 10.957 1.00 30.24 ? 103 VAL A CB 1 ATOM 681 C CG1 . VAL A 1 85 ? -3.153 26.175 9.446 1.00 27.43 ? 103 VAL A CG1 1 ATOM 682 C CG2 . VAL A 1 85 ? -3.660 24.616 11.428 1.00 28.96 ? 103 VAL A CG2 1 ATOM 683 N N . ASN A 1 86 ? 0.009 25.425 9.658 1.00 30.79 ? 104 ASN A N 1 ATOM 684 C CA . ASN A 1 86 ? 0.840 24.485 8.859 1.00 30.75 ? 104 ASN A CA 1 ATOM 685 C C . ASN A 1 86 ? 2.195 24.157 9.490 1.00 31.22 ? 104 ASN A C 1 ATOM 686 O O . ASN A 1 86 ? 3.120 23.596 8.855 1.00 31.48 ? 104 ASN A O 1 ATOM 687 C CB . ASN A 1 86 ? 0.967 24.941 7.428 1.00 31.09 ? 104 ASN A CB 1 ATOM 688 C CG . ASN A 1 86 ? -0.341 24.830 6.705 1.00 31.21 ? 104 ASN A CG 1 ATOM 689 O OD1 . ASN A 1 86 ? -0.837 23.727 6.528 1.00 35.08 ? 104 ASN A OD1 1 ATOM 690 N ND2 . ASN A 1 86 ? -0.912 25.943 6.312 1.00 25.61 ? 104 ASN A ND2 1 ATOM 691 N N . PHE A 1 87 ? 2.279 24.483 10.770 1.00 30.91 ? 105 PHE A N 1 ATOM 692 C CA . PHE A 1 87 ? 3.263 23.822 11.638 1.00 31.41 ? 105 PHE A CA 1 ATOM 693 C C . PHE A 1 87 ? 2.702 23.756 13.038 1.00 31.88 ? 105 PHE A C 1 ATOM 694 O O . PHE A 1 87 ? 2.737 24.744 13.804 1.00 31.18 ? 105 PHE A O 1 ATOM 695 C CB . PHE A 1 87 ? 4.644 24.512 11.612 1.00 31.31 ? 105 PHE A CB 1 ATOM 696 C CG . PHE A 1 87 ? 5.742 23.713 12.285 1.00 30.32 ? 105 PHE A CG 1 ATOM 697 C CD1 . PHE A 1 87 ? 6.492 22.804 11.566 1.00 31.29 ? 105 PHE A CD1 1 ATOM 698 C CD2 . PHE A 1 87 ? 5.997 23.857 13.638 1.00 28.91 ? 105 PHE A CD2 1 ATOM 699 C CE1 . PHE A 1 87 ? 7.514 22.070 12.174 1.00 32.18 ? 105 PHE A CE1 1 ATOM 700 C CE2 . PHE A 1 87 ? 6.994 23.131 14.254 1.00 29.79 ? 105 PHE A CE2 1 ATOM 701 C CZ . PHE A 1 87 ? 7.770 22.248 13.530 1.00 30.97 ? 105 PHE A CZ 1 ATOM 702 N N . THR A 1 88 ? 2.130 22.587 13.317 1.00 32.21 ? 106 THR A N 1 ATOM 703 C CA . THR A 1 88 ? 1.377 22.307 14.546 1.00 32.22 ? 106 THR A CA 1 ATOM 704 C C . THR A 1 88 ? 1.750 20.940 15.107 1.00 32.47 ? 106 THR A C 1 ATOM 705 O O . THR A 1 88 ? 2.554 20.252 14.502 1.00 31.95 ? 106 THR A O 1 ATOM 706 C CB . THR A 1 88 ? -0.145 22.452 14.304 1.00 32.60 ? 106 THR A CB 1 ATOM 707 O OG1 . THR A 1 88 ? -0.513 21.929 13.007 1.00 35.02 ? 106 THR A OG1 1 ATOM 708 C CG2 . THR A 1 88 ? -0.546 23.960 14.410 1.00 27.12 ? 106 THR A CG2 1 ATOM 709 N N . PRO A 1 89 ? 1.259 20.586 16.313 1.00 33.52 ? 107 PRO A N 1 ATOM 710 C CA . PRO A 1 89 ? 1.622 19.284 16.871 1.00 34.85 ? 107 PRO A CA 1 ATOM 711 C C . PRO A 1 89 ? 1.211 18.137 15.943 1.00 36.21 ? 107 PRO A C 1 ATOM 712 O O . PRO A 1 89 ? 1.873 17.107 15.834 1.00 36.39 ? 107 PRO A O 1 ATOM 713 C CB . PRO A 1 89 ? 0.849 19.260 18.190 1.00 35.02 ? 107 PRO A CB 1 ATOM 714 C CG . PRO A 1 89 ? 0.862 20.736 18.618 1.00 34.06 ? 107 PRO A CG 1 ATOM 715 C CD . PRO A 1 89 ? 0.619 21.456 17.308 1.00 33.51 ? 107 PRO A CD 1 ATOM 716 N N . TYR A 1 90 ? 0.141 18.391 15.229 1.00 37.11 ? 108 TYR A N 1 ATOM 717 C CA . TYR A 1 90 ? -0.345 17.471 14.215 1.00 38.27 ? 108 TYR A CA 1 ATOM 718 C C . TYR A 1 90 ? 0.757 16.965 13.298 1.00 38.59 ? 108 TYR A C 1 ATOM 719 O O . TYR A 1 90 ? 0.745 15.799 12.885 1.00 39.63 ? 108 TYR A O 1 ATOM 720 C CB . TYR A 1 90 ? -1.381 18.175 13.359 1.00 38.73 ? 108 TYR A CB 1 ATOM 721 C CG . TYR A 1 90 ? -1.760 17.487 12.055 1.00 42.12 ? 108 TYR A CG 1 ATOM 722 C CD1 . TYR A 1 90 ? -2.596 16.367 12.033 1.00 44.82 ? 108 TYR A CD1 1 ATOM 723 C CD2 . TYR A 1 90 ? -1.331 18.000 10.843 1.00 44.55 ? 108 TYR A CD2 1 ATOM 724 C CE1 . TYR A 1 90 ? -2.963 15.758 10.814 1.00 43.94 ? 108 TYR A CE1 1 ATOM 725 C CE2 . TYR A 1 90 ? -1.689 17.426 9.652 1.00 45.21 ? 108 TYR A CE2 1 ATOM 726 C CZ . TYR A 1 90 ? -2.498 16.299 9.627 1.00 46.91 ? 108 TYR A CZ 1 ATOM 727 O OH . TYR A 1 90 ? -2.837 15.768 8.380 1.00 46.53 ? 108 TYR A OH 1 ATOM 728 N N . HIS A 1 91 ? 1.694 17.841 12.948 1.00 37.06 ? 109 HIS A N 1 ATOM 729 C CA . HIS A 1 91 ? 2.732 17.477 11.975 1.00 36.61 ? 109 HIS A CA 1 ATOM 730 C C . HIS A 1 91 ? 3.737 16.576 12.649 1.00 36.70 ? 109 HIS A C 1 ATOM 731 O O . HIS A 1 91 ? 4.509 15.905 11.999 1.00 37.32 ? 109 HIS A O 1 ATOM 732 C CB . HIS A 1 91 ? 3.449 18.715 11.399 1.00 35.89 ? 109 HIS A CB 1 ATOM 733 C CG . HIS A 1 91 ? 2.560 19.599 10.586 1.00 35.03 ? 109 HIS A CG 1 ATOM 734 N ND1 . HIS A 1 91 ? 1.817 20.618 11.142 1.00 32.78 ? 109 HIS A ND1 1 ATOM 735 C CD2 . HIS A 1 91 ? 2.259 19.592 9.264 1.00 34.68 ? 109 HIS A CD2 1 ATOM 736 C CE1 . HIS A 1 91 ? 1.114 21.219 10.200 1.00 32.71 ? 109 HIS A CE1 1 ATOM 737 N NE2 . HIS A 1 91 ? 1.353 20.610 9.051 1.00 35.19 ? 109 HIS A NE2 1 ATOM 738 N N . ALA A 1 92 ? 3.705 16.581 13.972 1.00 37.53 ? 110 ALA A N 1 ATOM 739 C CA . ALA A 1 92 ? 4.608 15.755 14.797 1.00 38.05 ? 110 ALA A CA 1 ATOM 740 C C . ALA A 1 92 ? 6.079 15.895 14.410 1.00 37.93 ? 110 ALA A C 1 ATOM 741 O O . ALA A 1 92 ? 6.883 14.961 14.519 1.00 37.28 ? 110 ALA A O 1 ATOM 742 C CB . ALA A 1 92 ? 4.166 14.236 14.786 1.00 37.92 ? 110 ALA A CB 1 ATOM 743 N N . PHE A 1 93 ? 6.471 17.096 14.021 1.00 37.86 ? 111 PHE A N 1 ATOM 744 C CA . PHE A 1 93 ? 7.885 17.301 13.696 1.00 38.16 ? 111 PHE A CA 1 ATOM 745 C C . PHE A 1 93 ? 8.846 17.158 14.874 1.00 38.99 ? 111 PHE A C 1 ATOM 746 O O . PHE A 1 93 ? 8.629 17.656 15.978 1.00 39.03 ? 111 PHE A O 1 ATOM 747 C CB . PHE A 1 93 ? 8.136 18.648 13.033 1.00 37.81 ? 111 PHE A CB 1 ATOM 748 C CG . PHE A 1 93 ? 9.502 18.765 12.445 1.00 37.71 ? 111 PHE A CG 1 ATOM 749 C CD1 . PHE A 1 93 ? 9.777 18.226 11.206 1.00 35.59 ? 111 PHE A CD1 1 ATOM 750 C CD2 . PHE A 1 93 ? 10.539 19.357 13.158 1.00 34.11 ? 111 PHE A CD2 1 ATOM 751 C CE1 . PHE A 1 93 ? 11.025 18.309 10.685 1.00 35.65 ? 111 PHE A CE1 1 ATOM 752 C CE2 . PHE A 1 93 ? 11.784 19.437 12.638 1.00 35.25 ? 111 PHE A CE2 1 ATOM 753 C CZ . PHE A 1 93 ? 12.043 18.933 11.394 1.00 36.25 ? 111 PHE A CZ 1 ATOM 754 N N . LYS A 1 94 ? 9.917 16.449 14.594 1.00 40.22 ? 112 LYS A N 1 ATOM 755 C CA . LYS A 1 94 ? 11.065 16.358 15.494 1.00 42.03 ? 112 LYS A CA 1 ATOM 756 C C . LYS A 1 94 ? 12.253 16.088 14.616 1.00 41.90 ? 112 LYS A C 1 ATOM 757 O O . LYS A 1 94 ? 12.113 15.523 13.532 1.00 41.30 ? 112 LYS A O 1 ATOM 758 C CB . LYS A 1 94 ? 10.885 15.250 16.541 1.00 43.23 ? 112 LYS A CB 1 ATOM 759 C CG . LYS A 1 94 ? 10.003 14.112 16.072 1.00 48.09 ? 112 LYS A CG 1 ATOM 760 C CD . LYS A 1 94 ? 9.931 12.938 17.055 1.00 53.00 ? 112 LYS A CD 1 ATOM 761 C CE . LYS A 1 94 ? 8.853 13.167 18.144 1.00 56.48 ? 112 LYS A CE 1 ATOM 762 N NZ . LYS A 1 94 ? 8.242 11.876 18.635 1.00 58.50 ? 112 LYS A NZ 1 ATOM 763 N N . CYS A 1 95 ? 13.425 16.512 15.050 1.00 42.52 ? 113 CYS A N 1 ATOM 764 C CA . CYS A 1 95 ? 14.602 16.416 14.161 1.00 42.97 ? 113 CYS A CA 1 ATOM 765 C C . CYS A 1 95 ? 14.951 14.978 13.875 1.00 45.09 ? 113 CYS A C 1 ATOM 766 O O . CYS A 1 95 ? 15.436 14.625 12.792 1.00 45.49 ? 113 CYS A O 1 ATOM 767 C CB . CYS A 1 95 ? 15.812 17.124 14.743 1.00 42.61 ? 113 CYS A CB 1 ATOM 768 S SG . CYS A 1 95 ? 15.722 18.885 14.424 1.00 38.08 ? 113 CYS A SG 1 ATOM 769 N N . THR A 1 96 ? 14.671 14.170 14.879 1.00 46.57 ? 114 THR A N 1 ATOM 770 C CA . THR A 1 96 ? 14.884 12.730 14.814 1.00 48.04 ? 114 THR A CA 1 ATOM 771 C C . THR A 1 96 ? 13.761 12.015 15.530 1.00 48.82 ? 114 THR A C 1 ATOM 772 O O . THR A 1 96 ? 12.964 12.635 16.247 1.00 48.83 ? 114 THR A O 1 ATOM 773 C CB . THR A 1 96 ? 16.160 12.307 15.547 1.00 48.09 ? 114 THR A CB 1 ATOM 774 O OG1 . THR A 1 96 ? 15.919 12.350 16.961 1.00 47.17 ? 114 THR A OG1 1 ATOM 775 C CG2 . THR A 1 96 ? 17.329 13.227 15.146 1.00 48.09 ? 114 THR A CG2 1 ATOM 776 N N . THR A 1 97 ? 13.760 10.688 15.383 1.00 49.40 ? 115 THR A N 1 ATOM 777 C CA . THR A 1 97 ? 12.636 9.877 15.844 1.00 49.30 ? 115 THR A CA 1 ATOM 778 C C . THR A 1 97 ? 12.578 9.847 17.356 1.00 47.92 ? 115 THR A C 1 ATOM 779 O O . THR A 1 97 ? 11.520 9.591 17.919 1.00 47.59 ? 115 THR A O 1 ATOM 780 C CB . THR A 1 97 ? 12.700 8.434 15.308 1.00 49.90 ? 115 THR A CB 1 ATOM 781 O OG1 . THR A 1 97 ? 14.047 7.947 15.438 1.00 51.97 ? 115 THR A OG1 1 ATOM 782 C CG2 . THR A 1 97 ? 12.244 8.399 13.816 1.00 50.14 ? 115 THR A CG2 1 ATOM 783 N N . SER A 1 98 ? 13.703 10.145 17.996 1.00 47.07 ? 116 SER A N 1 ATOM 784 C CA . SER A 1 98 ? 13.743 10.175 19.463 1.00 46.87 ? 116 SER A CA 1 ATOM 785 C C . SER A 1 98 ? 13.580 11.587 20.027 1.00 46.61 ? 116 SER A C 1 ATOM 786 O O . SER A 1 98 ? 13.758 11.818 21.209 1.00 47.05 ? 116 SER A O 1 ATOM 787 C CB . SER A 1 98 ? 15.033 9.546 19.995 1.00 47.43 ? 116 SER A CB 1 ATOM 788 O OG . SER A 1 98 ? 16.199 10.161 19.442 1.00 48.29 ? 116 SER A OG 1 ATOM 789 N N . GLY A 1 99 ? 13.216 12.533 19.165 1.00 46.45 ? 117 GLY A N 1 ATOM 790 C CA . GLY A 1 99 ? 13.145 13.962 19.561 1.00 45.26 ? 117 GLY A CA 1 ATOM 791 C C . GLY A 1 99 ? 11.877 14.365 20.282 1.00 44.29 ? 117 GLY A C 1 ATOM 792 O O . GLY A 1 99 ? 11.183 13.550 20.829 1.00 44.29 ? 117 GLY A O 1 ATOM 793 N N . SER A 1 100 ? 11.580 15.655 20.243 1.00 43.28 ? 118 SER A N 1 ATOM 794 C CA . SER A 1 100 ? 10.449 16.242 20.979 1.00 42.28 ? 118 SER A CA 1 ATOM 795 C C . SER A 1 100 ? 9.748 17.344 20.212 1.00 40.72 ? 118 SER A C 1 ATOM 796 O O . SER A 1 100 ? 10.359 18.345 19.839 1.00 40.68 ? 118 SER A O 1 ATOM 797 C CB . SER A 1 100 ? 10.910 16.855 22.297 1.00 43.06 ? 118 SER A CB 1 ATOM 798 O OG . SER A 1 100 ? 9.878 17.705 22.839 1.00 44.45 ? 118 SER A OG 1 ATOM 799 N N . ASN A 1 101 ? 8.451 17.172 19.998 1.00 39.04 ? 119 ASN A N 1 ATOM 800 C CA . ASN A 1 101 ? 7.687 18.187 19.278 1.00 37.12 ? 119 ASN A CA 1 ATOM 801 C C . ASN A 1 101 ? 7.496 19.397 20.168 1.00 35.73 ? 119 ASN A C 1 ATOM 802 O O . ASN A 1 101 ? 7.319 20.530 19.679 1.00 35.46 ? 119 ASN A O 1 ATOM 803 C CB . ASN A 1 101 ? 6.338 17.659 18.772 1.00 36.64 ? 119 ASN A CB 1 ATOM 804 C CG . ASN A 1 101 ? 5.583 18.703 17.990 1.00 34.45 ? 119 ASN A CG 1 ATOM 805 O OD1 . ASN A 1 101 ? 4.584 19.255 18.472 1.00 30.68 ? 119 ASN A OD1 1 ATOM 806 N ND2 . ASN A 1 101 ? 6.085 19.027 16.784 1.00 33.01 ? 119 ASN A ND2 1 ATOM 807 N N . ASP A 1 102 ? 7.584 19.163 21.473 1.00 34.43 ? 120 ASP A N 1 ATOM 808 C CA . ASP A 1 102 ? 7.392 20.235 22.448 1.00 33.96 ? 120 ASP A CA 1 ATOM 809 C C . ASP A 1 102 ? 8.485 21.278 22.270 1.00 32.99 ? 120 ASP A C 1 ATOM 810 O O . ASP A 1 102 ? 8.245 22.468 22.446 1.00 32.43 ? 120 ASP A O 1 ATOM 811 C CB . ASP A 1 102 ? 7.401 19.747 23.885 1.00 34.74 ? 120 ASP A CB 1 ATOM 812 C CG . ASP A 1 102 ? 6.137 18.964 24.260 1.00 37.94 ? 120 ASP A CG 1 ATOM 813 O OD1 . ASP A 1 102 ? 5.185 18.891 23.449 1.00 37.96 ? 120 ASP A OD1 1 ATOM 814 O OD2 . ASP A 1 102 ? 6.135 18.388 25.382 1.00 38.17 ? 120 ASP A OD2 1 ATOM 815 N N . ILE A 1 103 ? 9.688 20.817 21.945 1.00 32.06 ? 121 ILE A N 1 ATOM 816 C CA . ILE A 1 103 ? 10.810 21.713 21.648 1.00 31.26 ? 121 ILE A CA 1 ATOM 817 C C . ILE A 1 103 ? 10.465 22.596 20.430 1.00 31.37 ? 121 ILE A C 1 ATOM 818 O O . ILE A 1 103 ? 10.759 23.801 20.384 1.00 32.40 ? 121 ILE A O 1 ATOM 819 C CB . ILE A 1 103 ? 12.123 20.930 21.392 1.00 31.16 ? 121 ILE A CB 1 ATOM 820 C CG1 . ILE A 1 103 ? 12.674 20.357 22.718 1.00 32.80 ? 121 ILE A CG1 1 ATOM 821 C CG2 . ILE A 1 103 ? 13.161 21.777 20.729 1.00 29.71 ? 121 ILE A CG2 1 ATOM 822 C CD1 . ILE A 1 103 ? 12.781 21.354 23.920 1.00 30.46 ? 121 ILE A CD1 1 ATOM 823 N N . TRP A 1 104 ? 9.830 21.969 19.449 1.00 30.51 ? 122 TRP A N 1 ATOM 824 C CA . TRP A 1 104 ? 9.501 22.640 18.185 1.00 30.09 ? 122 TRP A CA 1 ATOM 825 C C . TRP A 1 104 ? 8.350 23.618 18.382 1.00 29.22 ? 122 TRP A C 1 ATOM 826 O O . TRP A 1 104 ? 8.275 24.642 17.712 1.00 27.88 ? 122 TRP A O 1 ATOM 827 C CB . TRP A 1 104 ? 9.293 21.634 17.024 1.00 30.10 ? 122 TRP A CB 1 ATOM 828 C CG . TRP A 1 104 ? 10.648 21.302 16.490 1.00 30.42 ? 122 TRP A CG 1 ATOM 829 C CD1 . TRP A 1 104 ? 11.444 20.222 16.816 1.00 30.32 ? 122 TRP A CD1 1 ATOM 830 C CD2 . TRP A 1 104 ? 11.437 22.143 15.667 1.00 28.92 ? 122 TRP A CD2 1 ATOM 831 N NE1 . TRP A 1 104 ? 12.650 20.332 16.183 1.00 30.84 ? 122 TRP A NE1 1 ATOM 832 C CE2 . TRP A 1 104 ? 12.677 21.516 15.489 1.00 28.80 ? 122 TRP A CE2 1 ATOM 833 C CE3 . TRP A 1 104 ? 11.221 23.379 15.083 1.00 28.10 ? 122 TRP A CE3 1 ATOM 834 C CZ2 . TRP A 1 104 ? 13.685 22.077 14.723 1.00 28.92 ? 122 TRP A CZ2 1 ATOM 835 C CZ3 . TRP A 1 104 ? 12.217 23.929 14.328 1.00 30.13 ? 122 TRP A CZ3 1 ATOM 836 C CH2 . TRP A 1 104 ? 13.434 23.287 14.155 1.00 27.88 ? 122 TRP A CH2 1 ATOM 837 N N . MET A 1 105 ? 7.477 23.297 19.328 1.00 28.77 ? 123 MET A N 1 ATOM 838 C CA . MET A 1 105 ? 6.398 24.223 19.712 1.00 29.41 ? 123 MET A CA 1 ATOM 839 C C . MET A 1 105 ? 6.967 25.458 20.442 1.00 30.01 ? 123 MET A C 1 ATOM 840 O O . MET A 1 105 ? 6.502 26.612 20.272 1.00 30.40 ? 123 MET A O 1 ATOM 841 C CB . MET A 1 105 ? 5.379 23.522 20.589 1.00 30.23 ? 123 MET A CB 1 ATOM 842 C CG . MET A 1 105 ? 4.492 22.551 19.753 1.00 30.43 ? 123 MET A CG 1 ATOM 843 S SD . MET A 1 105 ? 3.568 23.345 18.401 1.00 33.40 ? 123 MET A SD 1 ATOM 844 C CE . MET A 1 105 ? 4.568 22.977 16.986 1.00 32.27 ? 123 MET A CE 1 ATOM 845 N N . GLN A 1 106 ? 7.984 25.208 21.248 1.00 29.24 ? 124 GLN A N 1 ATOM 846 C CA . GLN A 1 106 ? 8.642 26.285 21.980 1.00 29.82 ? 124 GLN A CA 1 ATOM 847 C C . GLN A 1 106 ? 9.333 27.224 20.985 1.00 28.35 ? 124 GLN A C 1 ATOM 848 O O . GLN A 1 106 ? 9.214 28.438 21.049 1.00 28.66 ? 124 GLN A O 1 ATOM 849 C CB . GLN A 1 106 ? 9.609 25.684 23.016 1.00 30.30 ? 124 GLN A CB 1 ATOM 850 C CG . GLN A 1 106 ? 10.376 26.691 23.806 1.00 34.29 ? 124 GLN A CG 1 ATOM 851 C CD . GLN A 1 106 ? 11.269 26.033 24.855 1.00 40.45 ? 124 GLN A CD 1 ATOM 852 O OE1 . GLN A 1 106 ? 11.809 24.912 24.650 1.00 41.19 ? 124 GLN A OE1 1 ATOM 853 N NE2 . GLN A 1 106 ? 11.435 26.728 25.988 1.00 39.57 ? 124 GLN A NE2 1 ATOM 854 N N . ASN A 1 107 ? 9.981 26.630 20.006 1.00 27.81 ? 125 ASN A N 1 ATOM 855 C CA . ASN A 1 107 ? 10.619 27.376 18.911 1.00 27.53 ? 125 ASN A CA 1 ATOM 856 C C . ASN A 1 107 ? 9.628 28.250 18.177 1.00 27.30 ? 125 ASN A C 1 ATOM 857 O O . ASN A 1 107 ? 9.859 29.462 17.887 1.00 27.05 ? 125 ASN A O 1 ATOM 858 C CB . ASN A 1 107 ? 11.266 26.422 17.882 1.00 27.83 ? 125 ASN A CB 1 ATOM 859 C CG . ASN A 1 107 ? 12.524 25.685 18.430 1.00 27.28 ? 125 ASN A CG 1 ATOM 860 O OD1 . ASN A 1 107 ? 13.006 25.973 19.528 1.00 26.86 ? 125 ASN A OD1 1 ATOM 861 N ND2 . ASN A 1 107 ? 13.029 24.714 17.655 1.00 27.13 ? 125 ASN A ND2 1 ATOM 862 N N . LYS A 1 108 ? 8.521 27.636 17.853 1.00 26.82 ? 126 LYS A N 1 ATOM 863 C CA . LYS A 1 108 ? 7.437 28.340 17.152 1.00 26.53 ? 126 LYS A CA 1 ATOM 864 C C . LYS A 1 108 ? 6.985 29.557 17.925 1.00 26.76 ? 126 LYS A C 1 ATOM 865 O O . LYS A 1 108 ? 6.798 30.630 17.375 1.00 28.03 ? 126 LYS A O 1 ATOM 866 C CB . LYS A 1 108 ? 6.267 27.390 16.862 1.00 26.76 ? 126 LYS A CB 1 ATOM 867 C CG . LYS A 1 108 ? 5.018 28.057 16.281 1.00 27.02 ? 126 LYS A CG 1 ATOM 868 C CD . LYS A 1 108 ? 3.860 27.039 16.092 1.00 28.47 ? 126 LYS A CD 1 ATOM 869 C CE . LYS A 1 108 ? 2.580 27.686 15.486 1.00 27.25 ? 126 LYS A CE 1 ATOM 870 N NZ . LYS A 1 108 ? 1.480 26.663 15.218 1.00 26.86 ? 126 LYS A NZ 1 ATOM 871 N N . GLY A 1 109 ? 6.829 29.414 19.219 1.00 27.06 ? 127 GLY A N 1 ATOM 872 C CA . GLY A 1 109 ? 6.422 30.545 20.054 1.00 26.10 ? 127 GLY A CA 1 ATOM 873 C C . GLY A 1 109 ? 7.428 31.677 20.057 1.00 26.31 ? 127 GLY A C 1 ATOM 874 O O . GLY A 1 109 ? 7.069 32.848 19.922 1.00 25.77 ? 127 GLY A O 1 ATOM 875 N N . LEU A 1 110 ? 8.692 31.313 20.221 1.00 25.83 ? 128 LEU A N 1 ATOM 876 C CA . LEU A 1 110 ? 9.764 32.294 20.238 1.00 25.88 ? 128 LEU A CA 1 ATOM 877 C C . LEU A 1 110 ? 9.910 33.041 18.899 1.00 25.69 ? 128 LEU A C 1 ATOM 878 O O . LEU A 1 110 ? 10.168 34.237 18.861 1.00 26.25 ? 128 LEU A O 1 ATOM 879 C CB . LEU A 1 110 ? 11.076 31.646 20.651 1.00 26.28 ? 128 LEU A CB 1 ATOM 880 C CG . LEU A 1 110 ? 11.188 31.126 22.098 1.00 27.10 ? 128 LEU A CG 1 ATOM 881 C CD1 . LEU A 1 110 ? 12.529 30.388 22.224 1.00 27.26 ? 128 LEU A CD1 1 ATOM 882 C CD2 . LEU A 1 110 ? 11.066 32.197 23.193 1.00 23.89 ? 128 LEU A CD2 1 ATOM 883 N N . PHE A 1 111 ? 9.727 32.321 17.803 1.00 24.71 ? 129 PHE A N 1 ATOM 884 C CA . PHE A 1 111 ? 9.805 32.903 16.462 1.00 23.66 ? 129 PHE A CA 1 ATOM 885 C C . PHE A 1 111 ? 8.751 33.972 16.266 1.00 24.06 ? 129 PHE A C 1 ATOM 886 O O . PHE A 1 111 ? 9.033 35.095 15.936 1.00 22.75 ? 129 PHE A O 1 ATOM 887 C CB . PHE A 1 111 ? 9.614 31.831 15.388 1.00 24.51 ? 129 PHE A CB 1 ATOM 888 C CG . PHE A 1 111 ? 9.632 32.369 13.995 1.00 24.37 ? 129 PHE A CG 1 ATOM 889 C CD1 . PHE A 1 111 ? 10.797 32.812 13.420 1.00 21.98 ? 129 PHE A CD1 1 ATOM 890 C CD2 . PHE A 1 111 ? 8.459 32.486 13.273 1.00 23.99 ? 129 PHE A CD2 1 ATOM 891 C CE1 . PHE A 1 111 ? 10.790 33.343 12.147 1.00 24.32 ? 129 PHE A CE1 1 ATOM 892 C CE2 . PHE A 1 111 ? 8.471 32.953 11.979 1.00 22.84 ? 129 PHE A CE2 1 ATOM 893 C CZ . PHE A 1 111 ? 9.617 33.377 11.408 1.00 21.26 ? 129 PHE A CZ 1 ATOM 894 N N . TYR A 1 112 ? 7.497 33.581 16.484 1.00 24.90 ? 130 TYR A N 1 ATOM 895 C CA . TYR A 1 112 ? 6.377 34.488 16.183 1.00 25.18 ? 130 TYR A CA 1 ATOM 896 C C . TYR A 1 112 ? 6.403 35.708 17.123 1.00 24.65 ? 130 TYR A C 1 ATOM 897 O O . TYR A 1 112 ? 5.992 36.823 16.750 1.00 24.02 ? 130 TYR A O 1 ATOM 898 C CB . TYR A 1 112 ? 5.039 33.728 16.209 1.00 25.25 ? 130 TYR A CB 1 ATOM 899 C CG . TYR A 1 112 ? 4.756 32.947 14.919 1.00 24.96 ? 130 TYR A CG 1 ATOM 900 C CD1 . TYR A 1 112 ? 4.397 33.612 13.743 1.00 26.47 ? 130 TYR A CD1 1 ATOM 901 C CD2 . TYR A 1 112 ? 4.807 31.587 14.889 1.00 23.94 ? 130 TYR A CD2 1 ATOM 902 C CE1 . TYR A 1 112 ? 4.096 32.923 12.572 1.00 26.80 ? 130 TYR A CE1 1 ATOM 903 C CE2 . TYR A 1 112 ? 4.502 30.865 13.703 1.00 26.91 ? 130 TYR A CE2 1 ATOM 904 C CZ . TYR A 1 112 ? 4.141 31.546 12.562 1.00 25.34 ? 130 TYR A CZ 1 ATOM 905 O OH . TYR A 1 112 ? 3.866 30.859 11.395 1.00 28.99 ? 130 TYR A OH 1 ATOM 906 N N . THR A 1 113 ? 6.962 35.508 18.316 1.00 25.46 ? 131 THR A N 1 ATOM 907 C CA . THR A 1 113 ? 7.149 36.629 19.256 1.00 24.95 ? 131 THR A CA 1 ATOM 908 C C . THR A 1 113 ? 7.959 37.701 18.605 1.00 25.53 ? 131 THR A C 1 ATOM 909 O O . THR A 1 113 ? 7.592 38.872 18.661 1.00 27.62 ? 131 THR A O 1 ATOM 910 C CB . THR A 1 113 ? 7.817 36.213 20.576 1.00 25.99 ? 131 THR A CB 1 ATOM 911 O OG1 . THR A 1 113 ? 7.022 35.196 21.215 1.00 24.03 ? 131 THR A OG1 1 ATOM 912 C CG2 . THR A 1 113 ? 8.003 37.411 21.496 1.00 25.08 ? 131 THR A CG2 1 ATOM 913 N N . GLN A 1 114 ? 9.057 37.316 17.948 1.00 25.83 ? 132 GLN A N 1 ATOM 914 C CA . GLN A 1 114 ? 9.946 38.301 17.317 1.00 25.49 ? 132 GLN A CA 1 ATOM 915 C C . GLN A 1 114 ? 9.256 38.927 16.085 1.00 24.91 ? 132 GLN A C 1 ATOM 916 O O . GLN A 1 114 ? 9.343 40.144 15.799 1.00 23.86 ? 132 GLN A O 1 ATOM 917 C CB . GLN A 1 114 ? 11.276 37.666 16.932 1.00 26.92 ? 132 GLN A CB 1 ATOM 918 C CG . GLN A 1 114 ? 12.132 37.130 18.095 1.00 27.58 ? 132 GLN A CG 1 ATOM 919 C CD . GLN A 1 114 ? 12.586 38.186 19.061 1.00 29.73 ? 132 GLN A CD 1 ATOM 920 O OE1 . GLN A 1 114 ? 11.832 39.080 19.400 1.00 28.68 ? 132 GLN A OE1 1 ATOM 921 N NE2 . GLN A 1 114 ? 13.857 38.086 19.507 1.00 27.89 ? 132 GLN A NE2 1 ATOM 922 N N . VAL A 1 115 ? 8.508 38.085 15.387 1.00 24.17 ? 133 VAL A N 1 ATOM 923 C CA . VAL A 1 115 ? 7.845 38.556 14.164 1.00 23.23 ? 133 VAL A CA 1 ATOM 924 C C . VAL A 1 115 ? 6.794 39.575 14.520 1.00 22.25 ? 133 VAL A C 1 ATOM 925 O O . VAL A 1 115 ? 6.705 40.590 13.886 1.00 23.10 ? 133 VAL A O 1 ATOM 926 C CB . VAL A 1 115 ? 7.212 37.398 13.324 1.00 22.80 ? 133 VAL A CB 1 ATOM 927 C CG1 . VAL A 1 115 ? 6.264 37.987 12.213 1.00 22.21 ? 133 VAL A CG1 1 ATOM 928 C CG2 . VAL A 1 115 ? 8.303 36.526 12.711 1.00 21.28 ? 133 VAL A CG2 1 ATOM 929 N N . TYR A 1 116 ? 6.022 39.312 15.567 1.00 22.16 ? 134 TYR A N 1 ATOM 930 C CA . TYR A 1 116 ? 4.890 40.194 15.896 1.00 22.77 ? 134 TYR A CA 1 ATOM 931 C C . TYR A 1 116 ? 5.408 41.526 16.443 1.00 23.20 ? 134 TYR A C 1 ATOM 932 O O . TYR A 1 116 ? 4.925 42.609 16.089 1.00 23.91 ? 134 TYR A O 1 ATOM 933 C CB . TYR A 1 116 ? 3.937 39.547 16.898 1.00 22.88 ? 134 TYR A CB 1 ATOM 934 C CG . TYR A 1 116 ? 3.260 38.286 16.388 1.00 23.32 ? 134 TYR A CG 1 ATOM 935 C CD1 . TYR A 1 116 ? 3.124 38.031 15.024 1.00 26.17 ? 134 TYR A CD1 1 ATOM 936 C CD2 . TYR A 1 116 ? 2.738 37.363 17.274 1.00 25.46 ? 134 TYR A CD2 1 ATOM 937 C CE1 . TYR A 1 116 ? 2.523 36.849 14.570 1.00 24.84 ? 134 TYR A CE1 1 ATOM 938 C CE2 . TYR A 1 116 ? 2.128 36.187 16.836 1.00 26.59 ? 134 TYR A CE2 1 ATOM 939 C CZ . TYR A 1 116 ? 2.019 35.940 15.493 1.00 25.97 ? 134 TYR A CZ 1 ATOM 940 O OH . TYR A 1 116 ? 1.426 34.780 15.113 1.00 24.69 ? 134 TYR A OH 1 ATOM 941 N N . LYS A 1 117 ? 6.418 41.441 17.306 1.00 24.08 ? 135 LYS A N 1 ATOM 942 C CA . LYS A 1 117 ? 6.953 42.621 17.971 1.00 24.16 ? 135 LYS A CA 1 ATOM 943 C C . LYS A 1 117 ? 7.578 43.525 16.934 1.00 24.32 ? 135 LYS A C 1 ATOM 944 O O . LYS A 1 117 ? 7.472 44.751 16.981 1.00 24.72 ? 135 LYS A O 1 ATOM 945 C CB . LYS A 1 117 ? 8.021 42.251 19.006 1.00 24.48 ? 135 LYS A CB 1 ATOM 946 C CG . LYS A 1 117 ? 7.498 41.611 20.303 1.00 25.64 ? 135 LYS A CG 1 ATOM 947 C CD . LYS A 1 117 ? 8.698 41.411 21.245 1.00 28.11 ? 135 LYS A CD 1 ATOM 948 C CE . LYS A 1 117 ? 8.261 41.045 22.614 1.00 31.07 ? 135 LYS A CE 1 ATOM 949 N NZ . LYS A 1 117 ? 9.440 40.743 23.431 1.00 34.32 ? 135 LYS A NZ 1 ATOM 950 N N . ASN A 1 118 ? 8.252 42.903 15.982 1.00 23.57 ? 136 ASN A N 1 ATOM 951 C CA . ASN A 1 118 ? 8.972 43.702 15.000 1.00 23.16 ? 136 ASN A CA 1 ATOM 952 C C . ASN A 1 118 ? 8.070 44.269 13.895 1.00 23.69 ? 136 ASN A C 1 ATOM 953 O O . ASN A 1 118 ? 8.313 45.336 13.360 1.00 24.04 ? 136 ASN A O 1 ATOM 954 C CB . ASN A 1 118 ? 10.163 42.934 14.446 1.00 23.24 ? 136 ASN A CB 1 ATOM 955 C CG . ASN A 1 118 ? 11.342 42.992 15.407 1.00 24.90 ? 136 ASN A CG 1 ATOM 956 O OD1 . ASN A 1 118 ? 12.007 44.021 15.513 1.00 26.98 ? 136 ASN A OD1 1 ATOM 957 N ND2 . ASN A 1 118 ? 11.452 41.983 16.247 1.00 20.10 ? 136 ASN A ND2 1 ATOM 958 N N . MET A 1 119 ? 6.998 43.558 13.565 1.00 24.27 ? 137 MET A N 1 ATOM 959 C CA . MET A 1 119 ? 6.075 44.092 12.533 1.00 23.60 ? 137 MET A CA 1 ATOM 960 C C . MET A 1 119 ? 5.157 45.182 13.102 1.00 23.93 ? 137 MET A C 1 ATOM 961 O O . MET A 1 119 ? 4.432 45.830 12.356 1.00 23.98 ? 137 MET A O 1 ATOM 962 C CB . MET A 1 119 ? 5.308 42.986 11.830 1.00 23.52 ? 137 MET A CB 1 ATOM 963 C CG . MET A 1 119 ? 6.210 42.128 10.992 1.00 22.46 ? 137 MET A CG 1 ATOM 964 S SD . MET A 1 119 ? 7.335 43.000 9.859 1.00 24.69 ? 137 MET A SD 1 ATOM 965 C CE . MET A 1 119 ? 6.094 43.698 8.758 1.00 21.25 ? 137 MET A CE 1 ATOM 966 N N . ALA A 1 120 ? 5.297 45.454 14.398 1.00 23.15 ? 138 ALA A N 1 ATOM 967 C CA . ALA A 1 120 ? 4.648 46.633 15.039 1.00 23.84 ? 138 ALA A CA 1 ATOM 968 C C . ALA A 1 120 ? 5.457 47.870 14.763 1.00 23.76 ? 138 ALA A C 1 ATOM 969 O O . ALA A 1 120 ? 4.937 48.973 14.897 1.00 25.73 ? 138 ALA A O 1 ATOM 970 C CB . ALA A 1 120 ? 4.441 46.468 16.574 1.00 22.61 ? 138 ALA A CB 1 ATOM 971 N N . VAL A 1 121 ? 6.702 47.687 14.323 1.00 23.71 ? 139 VAL A N 1 ATOM 972 C CA . VAL A 1 121 ? 7.630 48.793 14.091 1.00 23.45 ? 139 VAL A CA 1 ATOM 973 C C . VAL A 1 121 ? 8.345 48.867 12.736 1.00 24.60 ? 139 VAL A C 1 ATOM 974 O O . VAL A 1 121 ? 9.085 49.827 12.476 1.00 25.56 ? 139 VAL A O 1 ATOM 975 C CB . VAL A 1 121 ? 8.707 48.918 15.247 1.00 24.70 ? 139 VAL A CB 1 ATOM 976 C CG1 . VAL A 1 121 ? 8.024 49.405 16.591 1.00 24.87 ? 139 VAL A CG1 1 ATOM 977 C CG2 . VAL A 1 121 ? 9.576 47.635 15.394 1.00 24.95 ? 139 VAL A CG2 1 ATOM 978 N N . TYR A 1 122 ? 8.104 47.895 11.873 1.00 24.46 ? 140 TYR A N 1 ATOM 979 C CA . TYR A 1 122 ? 8.515 47.938 10.445 1.00 25.30 ? 140 TYR A CA 1 ATOM 980 C C . TYR A 1 122 ? 7.313 47.724 9.536 1.00 24.97 ? 140 TYR A C 1 ATOM 981 O O . TYR A 1 122 ? 6.400 46.977 9.886 1.00 23.69 ? 140 TYR A O 1 ATOM 982 C CB . TYR A 1 122 ? 9.541 46.824 10.160 1.00 25.88 ? 140 TYR A CB 1 ATOM 983 C CG . TYR A 1 122 ? 10.843 47.121 10.850 1.00 27.69 ? 140 TYR A CG 1 ATOM 984 C CD1 . TYR A 1 122 ? 11.707 48.064 10.319 1.00 28.01 ? 140 TYR A CD1 1 ATOM 985 C CD2 . TYR A 1 122 ? 11.186 46.499 12.080 1.00 27.47 ? 140 TYR A CD2 1 ATOM 986 C CE1 . TYR A 1 122 ? 12.899 48.371 10.941 1.00 29.48 ? 140 TYR A CE1 1 ATOM 987 C CE2 . TYR A 1 122 ? 12.386 46.811 12.715 1.00 29.78 ? 140 TYR A CE2 1 ATOM 988 C CZ . TYR A 1 122 ? 13.236 47.765 12.139 1.00 30.01 ? 140 TYR A CZ 1 ATOM 989 O OH . TYR A 1 122 ? 14.428 48.138 12.737 1.00 30.95 ? 140 TYR A OH 1 ATOM 990 N N . ARG A 1 123 ? 7.325 48.388 8.382 1.00 24.24 ? 141 ARG A N 1 ATOM 991 C CA . ARG A 1 123 ? 6.245 48.275 7.392 1.00 25.25 ? 141 ARG A CA 1 ATOM 992 C C . ARG A 1 123 ? 6.353 46.985 6.601 1.00 25.03 ? 141 ARG A C 1 ATOM 993 O O . ARG A 1 123 ? 5.352 46.325 6.315 1.00 26.03 ? 141 ARG A O 1 ATOM 994 C CB . ARG A 1 123 ? 6.301 49.435 6.364 1.00 25.27 ? 141 ARG A CB 1 ATOM 995 C CG . ARG A 1 123 ? 5.945 50.764 6.926 1.00 25.03 ? 141 ARG A CG 1 ATOM 996 C CD . ARG A 1 123 ? 5.911 51.837 5.834 1.00 27.92 ? 141 ARG A CD 1 ATOM 997 N NE . ARG A 1 123 ? 5.025 51.447 4.736 1.00 28.80 ? 141 ARG A NE 1 ATOM 998 C CZ . ARG A 1 123 ? 3.717 51.654 4.704 1.00 31.18 ? 141 ARG A CZ 1 ATOM 999 N NH1 . ARG A 1 123 ? 3.110 52.271 5.693 1.00 31.07 ? 141 ARG A NH1 1 ATOM 1000 N NH2 . ARG A 1 123 ? 3.016 51.255 3.669 1.00 31.12 ? 141 ARG A NH2 1 ATOM 1001 N N . SER A 1 124 ? 7.593 46.598 6.315 1.00 24.56 ? 142 SER A N 1 ATOM 1002 C CA . SER A 1 124 ? 7.903 45.566 5.320 1.00 25.16 ? 142 SER A CA 1 ATOM 1003 C C . SER A 1 124 ? 8.494 44.300 5.860 1.00 25.21 ? 142 SER A C 1 ATOM 1004 O O . SER A 1 124 ? 9.451 44.293 6.632 1.00 26.99 ? 142 SER A O 1 ATOM 1005 C CB . SER A 1 124 ? 8.866 46.213 4.288 1.00 25.59 ? 142 SER A CB 1 ATOM 1006 O OG . SER A 1 124 ? 9.289 45.298 3.316 1.00 27.45 ? 142 SER A OG 1 ATOM 1007 N N . LEU A 1 125 ? 7.911 43.194 5.436 1.00 25.86 ? 143 LEU A N 1 ATOM 1008 C CA . LEU A 1 125 ? 8.435 41.866 5.665 1.00 24.98 ? 143 LEU A CA 1 ATOM 1009 C C . LEU A 1 125 ? 8.633 41.117 4.351 1.00 25.39 ? 143 LEU A C 1 ATOM 1010 O O . LEU A 1 125 ? 7.775 41.163 3.456 1.00 24.61 ? 143 LEU A O 1 ATOM 1011 C CB . LEU A 1 125 ? 7.503 41.050 6.574 1.00 26.48 ? 143 LEU A CB 1 ATOM 1012 C CG . LEU A 1 125 ? 7.943 39.639 7.001 1.00 24.70 ? 143 LEU A CG 1 ATOM 1013 C CD1 . LEU A 1 125 ? 7.415 39.311 8.406 1.00 25.70 ? 143 LEU A CD1 1 ATOM 1014 C CD2 . LEU A 1 125 ? 7.508 38.572 5.981 1.00 22.87 ? 143 LEU A CD2 1 ATOM 1015 N N . THR A 1 126 ? 9.813 40.497 4.236 1.00 24.90 ? 144 THR A N 1 ATOM 1016 C CA . THR A 1 126 ? 10.086 39.459 3.245 1.00 26.23 ? 144 THR A CA 1 ATOM 1017 C C . THR A 1 126 ? 11.155 38.531 3.793 1.00 26.72 ? 144 THR A C 1 ATOM 1018 O O . THR A 1 126 ? 11.641 38.729 4.915 1.00 25.33 ? 144 THR A O 1 ATOM 1019 C CB . THR A 1 126 ? 10.506 40.067 1.814 1.00 27.43 ? 144 THR A CB 1 ATOM 1020 O OG1 . THR A 1 126 ? 10.491 39.032 0.810 1.00 29.28 ? 144 THR A OG1 1 ATOM 1021 C CG2 . THR A 1 126 ? 11.910 40.845 1.808 1.00 25.89 ? 144 THR A CG2 1 ATOM 1022 N N . PHE A 1 127 ? 11.515 37.536 2.983 1.00 26.99 ? 145 PHE A N 1 ATOM 1023 C CA . PHE A 1 127 ? 12.609 36.614 3.255 1.00 26.92 ? 145 PHE A CA 1 ATOM 1024 C C . PHE A 1 127 ? 13.792 36.956 2.371 1.00 27.72 ? 145 PHE A C 1 ATOM 1025 O O . PHE A 1 127 ? 13.640 37.391 1.220 1.00 28.54 ? 145 PHE A O 1 ATOM 1026 C CB . PHE A 1 127 ? 12.254 35.170 2.931 1.00 27.00 ? 145 PHE A CB 1 ATOM 1027 C CG . PHE A 1 127 ? 11.394 34.506 3.938 1.00 29.27 ? 145 PHE A CG 1 ATOM 1028 C CD1 . PHE A 1 127 ? 11.948 33.795 4.973 1.00 30.58 ? 145 PHE A CD1 1 ATOM 1029 C CD2 . PHE A 1 127 ? 10.012 34.603 3.859 1.00 31.13 ? 145 PHE A CD2 1 ATOM 1030 C CE1 . PHE A 1 127 ? 11.138 33.182 5.890 1.00 31.63 ? 145 PHE A CE1 1 ATOM 1031 C CE2 . PHE A 1 127 ? 9.192 33.989 4.801 1.00 31.87 ? 145 PHE A CE2 1 ATOM 1032 C CZ . PHE A 1 127 ? 9.750 33.294 5.810 1.00 29.31 ? 145 PHE A CZ 1 ATOM 1033 N N . VAL A 1 128 ? 14.983 36.778 2.929 1.00 27.93 ? 146 VAL A N 1 ATOM 1034 C CA . VAL A 1 128 ? 16.216 36.909 2.170 1.00 27.87 ? 146 VAL A CA 1 ATOM 1035 C C . VAL A 1 128 ? 17.091 35.714 2.417 1.00 28.89 ? 146 VAL A C 1 ATOM 1036 O O . VAL A 1 128 ? 17.125 35.168 3.512 1.00 28.48 ? 146 VAL A O 1 ATOM 1037 C CB . VAL A 1 128 ? 17.041 38.172 2.514 1.00 28.08 ? 146 VAL A CB 1 ATOM 1038 C CG1 . VAL A 1 128 ? 16.422 39.442 1.914 1.00 28.51 ? 146 VAL A CG1 1 ATOM 1039 C CG2 . VAL A 1 128 ? 17.306 38.290 4.022 1.00 25.70 ? 146 VAL A CG2 1 ATOM 1040 N N . ASN A 1 129 ? 17.802 35.304 1.375 1.00 30.66 ? 147 ASN A N 1 ATOM 1041 C CA . ASN A 1 129 ? 18.784 34.243 1.521 1.00 32.11 ? 147 ASN A CA 1 ATOM 1042 C C . ASN A 1 129 ? 19.934 34.873 2.291 1.00 31.59 ? 147 ASN A C 1 ATOM 1043 O O . ASN A 1 129 ? 20.258 36.057 2.143 1.00 31.90 ? 147 ASN A O 1 ATOM 1044 C CB . ASN A 1 129 ? 19.206 33.622 0.169 1.00 33.33 ? 147 ASN A CB 1 ATOM 1045 C CG . ASN A 1 129 ? 18.151 32.570 -0.353 1.00 38.33 ? 147 ASN A CG 1 ATOM 1046 O OD1 . ASN A 1 129 ? 17.880 32.500 -1.558 1.00 44.71 ? 147 ASN A OD1 1 ATOM 1047 N ND2 . ASN A 1 129 ? 17.549 31.760 0.573 1.00 41.02 ? 147 ASN A ND2 1 ATOM 1048 N N . VAL A 1 130 ? 20.522 34.088 3.167 1.00 30.85 ? 148 VAL A N 1 ATOM 1049 C CA . VAL A 1 130 ? 21.704 34.567 3.846 1.00 30.11 ? 148 VAL A CA 1 ATOM 1050 C C . VAL A 1 130 ? 22.925 33.855 3.258 1.00 30.10 ? 148 VAL A C 1 ATOM 1051 O O . VAL A 1 130 ? 23.152 32.674 3.505 1.00 28.55 ? 148 VAL A O 1 ATOM 1052 C CB . VAL A 1 130 ? 21.660 34.324 5.380 1.00 30.57 ? 148 VAL A CB 1 ATOM 1053 C CG1 . VAL A 1 130 ? 23.042 34.731 6.001 1.00 28.96 ? 148 VAL A CG1 1 ATOM 1054 C CG2 . VAL A 1 130 ? 20.459 35.036 6.007 1.00 27.11 ? 148 VAL A CG2 1 ATOM 1055 N N . PRO A 1 131 ? 23.757 34.588 2.535 1.00 30.21 ? 149 PRO A N 1 ATOM 1056 C CA . PRO A 1 131 ? 24.961 33.901 2.058 1.00 31.69 ? 149 PRO A CA 1 ATOM 1057 C C . PRO A 1 131 ? 25.968 33.607 3.141 1.00 31.87 ? 149 PRO A C 1 ATOM 1058 O O . PRO A 1 131 ? 26.209 34.413 4.040 1.00 32.86 ? 149 PRO A O 1 ATOM 1059 C CB . PRO A 1 131 ? 25.546 34.890 1.060 1.00 32.07 ? 149 PRO A CB 1 ATOM 1060 C CG . PRO A 1 131 ? 25.093 36.185 1.502 1.00 32.13 ? 149 PRO A CG 1 ATOM 1061 C CD . PRO A 1 131 ? 23.800 36.015 2.280 1.00 30.58 ? 149 PRO A CD 1 ATOM 1062 N N . TYR A 1 132 ? 26.527 32.416 3.072 1.00 32.58 ? 150 TYR A N 1 ATOM 1063 C CA . TYR A 1 132 ? 27.651 32.067 3.920 1.00 32.89 ? 150 TYR A CA 1 ATOM 1064 C C . TYR A 1 132 ? 28.784 31.391 3.138 1.00 33.62 ? 150 TYR A C 1 ATOM 1065 O O . TYR A 1 132 ? 28.587 30.845 2.061 1.00 32.29 ? 150 TYR A O 1 ATOM 1066 C CB . TYR A 1 132 ? 27.193 31.181 5.059 1.00 32.33 ? 150 TYR A CB 1 ATOM 1067 C CG . TYR A 1 132 ? 26.793 29.776 4.673 1.00 33.20 ? 150 TYR A CG 1 ATOM 1068 C CD1 . TYR A 1 132 ? 27.708 28.728 4.680 1.00 32.58 ? 150 TYR A CD1 1 ATOM 1069 C CD2 . TYR A 1 132 ? 25.474 29.476 4.378 1.00 34.26 ? 150 TYR A CD2 1 ATOM 1070 C CE1 . TYR A 1 132 ? 27.330 27.434 4.338 1.00 33.00 ? 150 TYR A CE1 1 ATOM 1071 C CE2 . TYR A 1 132 ? 25.089 28.187 4.092 1.00 35.37 ? 150 TYR A CE2 1 ATOM 1072 C CZ . TYR A 1 132 ? 26.009 27.170 4.051 1.00 35.36 ? 150 TYR A CZ 1 ATOM 1073 O OH . TYR A 1 132 ? 25.578 25.878 3.758 1.00 34.54 ? 150 TYR A OH 1 ATOM 1074 N N . VAL A 1 133 ? 29.974 31.476 3.724 1.00 34.23 ? 151 VAL A N 1 ATOM 1075 C CA . VAL A 1 133 ? 31.160 30.773 3.230 1.00 33.70 ? 151 VAL A CA 1 ATOM 1076 C C . VAL A 1 133 ? 31.769 29.946 4.344 1.00 34.50 ? 151 VAL A C 1 ATOM 1077 O O . VAL A 1 133 ? 32.079 30.439 5.407 1.00 34.64 ? 151 VAL A O 1 ATOM 1078 C CB . VAL A 1 133 ? 32.195 31.752 2.619 1.00 33.46 ? 151 VAL A CB 1 ATOM 1079 C CG1 . VAL A 1 133 ? 33.523 31.019 2.207 1.00 31.21 ? 151 VAL A CG1 1 ATOM 1080 C CG2 . VAL A 1 133 ? 31.586 32.504 1.444 1.00 31.74 ? 151 VAL A CG2 1 ATOM 1081 N N . TYR A 1 134 ? 31.913 28.667 4.070 1.00 35.30 ? 152 TYR A N 1 ATOM 1082 C CA . TYR A 1 134 ? 32.609 27.771 4.938 1.00 37.70 ? 152 TYR A CA 1 ATOM 1083 C C . TYR A 1 134 ? 33.879 27.281 4.225 1.00 40.45 ? 152 TYR A C 1 ATOM 1084 O O . TYR A 1 134 ? 33.848 26.827 3.088 1.00 40.34 ? 152 TYR A O 1 ATOM 1085 C CB . TYR A 1 134 ? 31.727 26.605 5.265 1.00 36.82 ? 152 TYR A CB 1 ATOM 1086 C CG . TYR A 1 134 ? 32.411 25.480 5.998 1.00 38.05 ? 152 TYR A CG 1 ATOM 1087 C CD1 . TYR A 1 134 ? 32.733 24.286 5.343 1.00 36.44 ? 152 TYR A CD1 1 ATOM 1088 C CD2 . TYR A 1 134 ? 32.738 25.602 7.340 1.00 36.11 ? 152 TYR A CD2 1 ATOM 1089 C CE1 . TYR A 1 134 ? 33.349 23.256 6.026 1.00 33.56 ? 152 TYR A CE1 1 ATOM 1090 C CE2 . TYR A 1 134 ? 33.335 24.573 8.026 1.00 36.63 ? 152 TYR A CE2 1 ATOM 1091 C CZ . TYR A 1 134 ? 33.659 23.401 7.358 1.00 35.19 ? 152 TYR A CZ 1 ATOM 1092 O OH . TYR A 1 134 ? 34.236 22.363 8.062 1.00 33.37 ? 152 TYR A OH 1 ATOM 1093 N N . ASN A 1 135 ? 34.977 27.321 4.935 1.00 43.85 ? 153 ASN A N 1 ATOM 1094 C CA . ASN A 1 135 ? 36.261 27.048 4.313 1.00 47.32 ? 153 ASN A CA 1 ATOM 1095 C C . ASN A 1 135 ? 36.675 25.609 4.136 1.00 47.68 ? 153 ASN A C 1 ATOM 1096 O O . ASN A 1 135 ? 37.539 25.319 3.329 1.00 50.18 ? 153 ASN A O 1 ATOM 1097 C CB . ASN A 1 135 ? 37.398 27.769 5.025 1.00 48.14 ? 153 ASN A CB 1 ATOM 1098 C CG . ASN A 1 135 ? 38.290 28.420 4.038 1.00 53.10 ? 153 ASN A CG 1 ATOM 1099 O OD1 . ASN A 1 135 ? 39.513 28.216 4.042 1.00 61.25 ? 153 ASN A OD1 1 ATOM 1100 N ND2 . ASN A 1 135 ? 37.675 29.181 3.112 1.00 57.28 ? 153 ASN A ND2 1 ATOM 1101 N N . GLY A 1 136 ? 36.094 24.722 4.904 1.00 47.93 ? 154 GLY A N 1 ATOM 1102 C CA . GLY A 1 136 ? 36.469 23.315 4.824 1.00 47.73 ? 154 GLY A CA 1 ATOM 1103 C C . GLY A 1 136 ? 35.956 22.707 3.547 1.00 47.82 ? 154 GLY A C 1 ATOM 1104 O O . GLY A 1 136 ? 35.371 23.410 2.727 1.00 47.58 ? 154 GLY A O 1 ATOM 1105 N N . SER A 1 137 ? 36.148 21.394 3.408 1.00 47.79 ? 155 SER A N 1 ATOM 1106 C CA . SER A 1 137 ? 35.656 20.650 2.246 1.00 48.32 ? 155 SER A CA 1 ATOM 1107 C C . SER A 1 137 ? 34.330 19.980 2.543 1.00 47.76 ? 155 SER A C 1 ATOM 1108 O O . SER A 1 137 ? 33.642 19.492 1.654 1.00 47.39 ? 155 SER A O 1 ATOM 1109 C CB . SER A 1 137 ? 36.677 19.573 1.821 1.00 48.62 ? 155 SER A CB 1 ATOM 1110 O OG . SER A 1 137 ? 37.863 20.183 1.336 1.00 49.50 ? 155 SER A OG 1 ATOM 1111 N N . ALA A 1 138 ? 33.970 19.959 3.814 1.00 47.24 ? 156 ALA A N 1 ATOM 1112 C CA . ALA A 1 138 ? 32.700 19.350 4.195 1.00 47.04 ? 156 ALA A CA 1 ATOM 1113 C C . ALA A 1 138 ? 31.572 20.194 3.623 1.00 46.65 ? 156 ALA A C 1 ATOM 1114 O O . ALA A 1 138 ? 31.715 21.388 3.362 1.00 44.95 ? 156 ALA A O 1 ATOM 1115 C CB . ALA A 1 138 ? 32.579 19.223 5.691 1.00 47.36 ? 156 ALA A CB 1 ATOM 1116 N N . GLN A 1 139 ? 30.477 19.509 3.348 1.00 47.55 ? 157 GLN A N 1 ATOM 1117 C CA . GLN A 1 139 ? 29.262 20.127 2.810 1.00 48.49 ? 157 GLN A CA 1 ATOM 1118 C C . GLN A 1 139 ? 28.142 20.135 3.850 1.00 47.43 ? 157 GLN A C 1 ATOM 1119 O O . GLN A 1 139 ? 28.170 19.427 4.854 1.00 47.03 ? 157 GLN A O 1 ATOM 1120 C CB . GLN A 1 139 ? 28.729 19.342 1.594 1.00 49.26 ? 157 GLN A CB 1 ATOM 1121 C CG . GLN A 1 139 ? 29.747 19.089 0.464 1.00 54.00 ? 157 GLN A CG 1 ATOM 1122 C CD . GLN A 1 139 ? 30.133 20.371 -0.269 1.00 60.08 ? 157 GLN A CD 1 ATOM 1123 O OE1 . GLN A 1 139 ? 31.196 20.971 0.003 1.00 64.79 ? 157 GLN A OE1 1 ATOM 1124 N NE2 . GLN A 1 139 ? 29.277 20.804 -1.204 1.00 62.90 ? 157 GLN A NE2 1 ATOM 1125 N N . SER A 1 140 ? 27.104 20.878 3.518 1.00 47.06 ? 158 SER A N 1 ATOM 1126 C CA . SER A 1 140 ? 25.897 20.928 4.354 1.00 46.70 ? 158 SER A CA 1 ATOM 1127 C C . SER A 1 140 ? 25.232 19.571 4.318 1.00 46.67 ? 158 SER A C 1 ATOM 1128 O O . SER A 1 140 ? 25.414 18.813 3.381 1.00 47.09 ? 158 SER A O 1 ATOM 1129 C CB . SER A 1 140 ? 24.941 22.001 3.867 1.00 46.53 ? 158 SER A CB 1 ATOM 1130 O OG . SER A 1 140 ? 24.424 21.692 2.596 1.00 45.30 ? 158 SER A OG 1 ATOM 1131 N N . THR A 1 141 ? 24.500 19.265 5.367 1.00 46.00 ? 159 THR A N 1 ATOM 1132 C CA . THR A 1 141 ? 23.870 17.967 5.518 1.00 46.16 ? 159 THR A CA 1 ATOM 1133 C C . THR A 1 141 ? 22.503 18.132 6.185 1.00 45.94 ? 159 THR A C 1 ATOM 1134 O O . THR A 1 141 ? 22.340 18.898 7.136 1.00 45.25 ? 159 THR A O 1 ATOM 1135 C CB . THR A 1 141 ? 24.781 16.978 6.343 1.00 46.36 ? 159 THR A CB 1 ATOM 1136 O OG1 . THR A 1 141 ? 24.181 15.688 6.404 1.00 47.50 ? 159 THR A OG1 1 ATOM 1137 C CG2 . THR A 1 141 ? 25.006 17.445 7.785 1.00 45.40 ? 159 THR A CG2 1 ATOM 1138 N N . ALA A 1 142 ? 21.533 17.379 5.680 1.00 45.86 ? 160 ALA A N 1 ATOM 1139 C CA . ALA A 1 142 ? 20.153 17.439 6.167 1.00 45.25 ? 160 ALA A CA 1 ATOM 1140 C C . ALA A 1 142 ? 19.917 16.516 7.322 1.00 45.21 ? 160 ALA A C 1 ATOM 1141 O O . ALA A 1 142 ? 19.293 15.476 7.167 1.00 46.65 ? 160 ALA A O 1 ATOM 1142 C CB . ALA A 1 142 ? 19.168 17.146 5.035 1.00 45.13 ? 160 ALA A CB 1 ATOM 1143 N N . LEU A 1 143 ? 20.377 16.928 8.494 1.00 44.57 ? 161 LEU A N 1 ATOM 1144 C CA . LEU A 1 143 ? 20.376 16.074 9.682 1.00 44.87 ? 161 LEU A CA 1 ATOM 1145 C C . LEU A 1 143 ? 19.069 16.178 10.423 1.00 43.84 ? 161 LEU A C 1 ATOM 1146 O O . LEU A 1 143 ? 18.768 15.344 11.253 1.00 44.10 ? 161 LEU A O 1 ATOM 1147 C CB . LEU A 1 143 ? 21.567 16.425 10.626 1.00 45.86 ? 161 LEU A CB 1 ATOM 1148 C CG . LEU A 1 143 ? 21.734 15.885 12.071 1.00 48.07 ? 161 LEU A CG 1 ATOM 1149 C CD1 . LEU A 1 143 ? 22.021 14.354 12.147 1.00 50.16 ? 161 LEU A CD1 1 ATOM 1150 C CD2 . LEU A 1 143 ? 22.846 16.681 12.802 1.00 49.19 ? 161 LEU A CD2 1 ATOM 1151 N N . CYS A 1 144 ? 18.293 17.217 10.138 1.00 42.65 ? 162 CYS A N 1 ATOM 1152 C CA . CYS A 1 144 ? 17.019 17.390 10.836 1.00 41.65 ? 162 CYS A CA 1 ATOM 1153 C C . CYS A 1 144 ? 15.852 17.303 9.866 1.00 41.86 ? 162 CYS A C 1 ATOM 1154 O O . CYS A 1 144 ? 15.621 18.202 9.055 1.00 40.30 ? 162 CYS A O 1 ATOM 1155 C CB . CYS A 1 144 ? 16.990 18.713 11.629 1.00 41.61 ? 162 CYS A CB 1 ATOM 1156 S SG . CYS A 1 144 ? 15.416 18.986 12.427 1.00 39.79 ? 162 CYS A SG 1 ATOM 1157 N N . LYS A 1 145 ? 15.113 16.204 9.989 1.00 42.57 ? 163 LYS A N 1 ATOM 1158 C CA . LYS A 1 145 ? 14.009 15.903 9.092 1.00 43.21 ? 163 LYS A CA 1 ATOM 1159 C C . LYS A 1 145 ? 13.040 14.852 9.602 1.00 43.28 ? 163 LYS A C 1 ATOM 1160 O O . LYS A 1 145 ? 13.361 13.965 10.393 1.00 42.48 ? 163 LYS A O 1 ATOM 1161 C CB . LYS A 1 145 ? 14.558 15.513 7.724 1.00 43.93 ? 163 LYS A CB 1 ATOM 1162 C CG . LYS A 1 145 ? 15.589 14.419 7.779 1.00 47.07 ? 163 LYS A CG 1 ATOM 1163 C CD . LYS A 1 145 ? 16.143 14.066 6.406 1.00 51.18 ? 163 LYS A CD 1 ATOM 1164 C CE . LYS A 1 145 ? 17.099 12.823 6.491 1.00 54.70 ? 163 LYS A CE 1 ATOM 1165 N NZ . LYS A 1 145 ? 17.940 12.736 7.785 1.00 56.03 ? 163 LYS A NZ 1 ATOM 1166 N N . SER A 1 146 ? 11.815 15.013 9.161 1.00 43.65 ? 164 SER A N 1 ATOM 1167 C CA . SER A 1 146 ? 10.725 14.168 9.613 1.00 45.24 ? 164 SER A CA 1 ATOM 1168 C C . SER A 1 146 ? 9.579 14.239 8.640 1.00 46.02 ? 164 SER A C 1 ATOM 1169 O O . SER A 1 146 ? 9.018 15.301 8.403 1.00 46.61 ? 164 SER A O 1 ATOM 1170 C CB . SER A 1 146 ? 10.247 14.605 10.992 1.00 45.56 ? 164 SER A CB 1 ATOM 1171 O OG . SER A 1 146 ? 9.085 13.883 11.379 1.00 48.79 ? 164 SER A OG 1 ATOM 1172 N N . GLY A 1 147 ? 9.257 13.108 8.034 1.00 46.85 ? 165 GLY A N 1 ATOM 1173 C CA . GLY A 1 147 ? 8.251 13.100 6.976 1.00 46.35 ? 165 GLY A CA 1 ATOM 1174 C C . GLY A 1 147 ? 8.729 13.939 5.816 1.00 45.66 ? 165 GLY A C 1 ATOM 1175 O O . GLY A 1 147 ? 9.878 13.866 5.393 1.00 46.79 ? 165 GLY A O 1 ATOM 1176 N N . SER A 1 148 ? 7.849 14.795 5.345 1.00 44.62 ? 166 SER A N 1 ATOM 1177 C CA . SER A 1 148 ? 8.133 15.603 4.160 1.00 43.72 ? 166 SER A CA 1 ATOM 1178 C C . SER A 1 148 ? 8.777 16.922 4.560 1.00 42.23 ? 166 SER A C 1 ATOM 1179 O O . SER A 1 148 ? 9.044 17.793 3.713 1.00 42.58 ? 166 SER A O 1 ATOM 1180 C CB . SER A 1 148 ? 6.830 15.895 3.418 1.00 44.37 ? 166 SER A CB 1 ATOM 1181 O OG . SER A 1 148 ? 5.946 16.591 4.285 1.00 45.81 ? 166 SER A OG 1 ATOM 1182 N N . LEU A 1 149 ? 8.979 17.080 5.870 1.00 39.89 ? 167 LEU A N 1 ATOM 1183 C CA . LEU A 1 149 ? 9.606 18.299 6.410 1.00 37.38 ? 167 LEU A CA 1 ATOM 1184 C C . LEU A 1 149 ? 11.093 18.123 6.555 1.00 35.91 ? 167 LEU A C 1 ATOM 1185 O O . LEU A 1 149 ? 11.569 17.297 7.300 1.00 36.04 ? 167 LEU A O 1 ATOM 1186 C CB . LEU A 1 149 ? 8.964 18.727 7.737 1.00 36.29 ? 167 LEU A CB 1 ATOM 1187 C CG . LEU A 1 149 ? 7.663 19.528 7.603 1.00 36.22 ? 167 LEU A CG 1 ATOM 1188 C CD1 . LEU A 1 149 ? 6.999 19.703 8.939 1.00 36.63 ? 167 LEU A CD1 1 ATOM 1189 C CD2 . LEU A 1 149 ? 7.894 20.856 6.917 1.00 35.58 ? 167 LEU A CD2 1 ATOM 1190 N N . VAL A 1 150 ? 11.816 18.915 5.789 1.00 35.91 ? 168 VAL A N 1 ATOM 1191 C CA . VAL A 1 150 ? 13.278 18.947 5.820 1.00 35.24 ? 168 VAL A CA 1 ATOM 1192 C C . VAL A 1 150 ? 13.781 20.344 6.227 1.00 34.46 ? 168 VAL A C 1 ATOM 1193 O O . VAL A 1 150 ? 13.616 21.333 5.524 1.00 33.66 ? 168 VAL A O 1 ATOM 1194 C CB . VAL A 1 150 ? 13.893 18.541 4.459 1.00 35.37 ? 168 VAL A CB 1 ATOM 1195 C CG1 . VAL A 1 150 ? 15.380 18.418 4.581 1.00 35.33 ? 168 VAL A CG1 1 ATOM 1196 C CG2 . VAL A 1 150 ? 13.282 17.192 3.950 1.00 36.09 ? 168 VAL A CG2 1 ATOM 1197 N N . LEU A 1 151 ? 14.376 20.403 7.407 1.00 34.22 ? 169 LEU A N 1 ATOM 1198 C CA . LEU A 1 151 ? 14.988 21.656 7.893 1.00 32.87 ? 169 LEU A CA 1 ATOM 1199 C C . LEU A 1 151 ? 16.106 22.095 6.964 1.00 32.23 ? 169 LEU A C 1 ATOM 1200 O O . LEU A 1 151 ? 16.976 21.289 6.602 1.00 33.38 ? 169 LEU A O 1 ATOM 1201 C CB . LEU A 1 151 ? 15.557 21.486 9.304 1.00 32.43 ? 169 LEU A CB 1 ATOM 1202 C CG . LEU A 1 151 ? 15.876 22.772 10.085 1.00 31.99 ? 169 LEU A CG 1 ATOM 1203 C CD1 . LEU A 1 151 ? 14.583 23.245 10.712 1.00 27.11 ? 169 LEU A CD1 1 ATOM 1204 C CD2 . LEU A 1 151 ? 16.972 22.518 11.132 1.00 29.02 ? 169 LEU A CD2 1 ATOM 1205 N N . ASN A 1 152 ? 16.138 23.389 6.632 1.00 31.08 ? 170 ASN A N 1 ATOM 1206 C CA . ASN A 1 152 ? 17.270 23.911 5.879 1.00 30.02 ? 170 ASN A CA 1 ATOM 1207 C C . ASN A 1 152 ? 17.848 25.235 6.377 1.00 29.86 ? 170 ASN A C 1 ATOM 1208 O O . ASN A 1 152 ? 18.781 25.788 5.782 1.00 28.36 ? 170 ASN A O 1 ATOM 1209 C CB . ASN A 1 152 ? 16.936 23.975 4.384 1.00 30.51 ? 170 ASN A CB 1 ATOM 1210 C CG . ASN A 1 152 ? 16.020 25.096 4.024 1.00 31.32 ? 170 ASN A CG 1 ATOM 1211 O OD1 . ASN A 1 152 ? 15.341 25.709 4.893 1.00 31.37 ? 170 ASN A OD1 1 ATOM 1212 N ND2 . ASN A 1 152 ? 15.993 25.412 2.732 1.00 28.49 ? 170 ASN A ND2 1 ATOM 1213 N N . ASN A 1 153 ? 17.282 25.701 7.495 1.00 29.20 ? 171 ASN A N 1 ATOM 1214 C CA . ASN A 1 153 ? 17.725 26.883 8.200 1.00 28.71 ? 171 ASN A CA 1 ATOM 1215 C C . ASN A 1 153 ? 17.556 26.690 9.687 1.00 28.52 ? 171 ASN A C 1 ATOM 1216 O O . ASN A 1 153 ? 16.445 26.487 10.167 1.00 28.88 ? 171 ASN A O 1 ATOM 1217 C CB . ASN A 1 153 ? 16.865 28.058 7.764 1.00 29.02 ? 171 ASN A CB 1 ATOM 1218 C CG . ASN A 1 153 ? 17.269 29.374 8.396 1.00 29.14 ? 171 ASN A CG 1 ATOM 1219 O OD1 . ASN A 1 153 ? 18.467 29.667 8.564 1.00 28.15 ? 171 ASN A OD1 1 ATOM 1220 N ND2 . ASN A 1 153 ? 16.269 30.235 8.631 1.00 26.27 ? 171 ASN A ND2 1 ATOM 1221 N N . PRO A 1 154 ? 18.651 26.760 10.438 1.00 28.57 ? 172 PRO A N 1 ATOM 1222 C CA . PRO A 1 154 ? 20.017 26.908 9.955 1.00 28.96 ? 172 PRO A CA 1 ATOM 1223 C C . PRO A 1 154 ? 20.491 25.636 9.199 1.00 29.51 ? 172 PRO A C 1 ATOM 1224 O O . PRO A 1 154 ? 19.920 24.587 9.348 1.00 29.55 ? 172 PRO A O 1 ATOM 1225 C CB . PRO A 1 154 ? 20.819 27.017 11.263 1.00 28.48 ? 172 PRO A CB 1 ATOM 1226 C CG . PRO A 1 154 ? 20.053 26.176 12.220 1.00 27.74 ? 172 PRO A CG 1 ATOM 1227 C CD . PRO A 1 154 ? 18.619 26.563 11.898 1.00 28.61 ? 172 PRO A CD 1 ATOM 1228 N N . ALA A 1 155 ? 21.540 25.779 8.414 1.00 30.46 ? 173 ALA A N 1 ATOM 1229 C CA . ALA A 1 155 ? 22.209 24.628 7.781 1.00 32.02 ? 173 ALA A CA 1 ATOM 1230 C C . ALA A 1 155 ? 23.088 23.942 8.795 1.00 33.19 ? 173 ALA A C 1 ATOM 1231 O O . ALA A 1 155 ? 23.647 24.602 9.687 1.00 34.32 ? 173 ALA A O 1 ATOM 1232 C CB . ALA A 1 155 ? 23.064 25.111 6.647 1.00 31.48 ? 173 ALA A CB 1 ATOM 1233 N N . TYR A 1 156 ? 23.224 22.629 8.668 1.00 33.79 ? 174 TYR A N 1 ATOM 1234 C CA . TYR A 1 156 ? 24.286 21.900 9.380 1.00 33.93 ? 174 TYR A CA 1 ATOM 1235 C C . TYR A 1 156 ? 25.432 21.657 8.411 1.00 35.50 ? 174 TYR A C 1 ATOM 1236 O O . TYR A 1 156 ? 25.207 21.327 7.249 1.00 35.09 ? 174 TYR A O 1 ATOM 1237 C CB . TYR A 1 156 ? 23.811 20.560 9.849 1.00 34.31 ? 174 TYR A CB 1 ATOM 1238 C CG . TYR A 1 156 ? 22.628 20.514 10.777 1.00 33.29 ? 174 TYR A CG 1 ATOM 1239 C CD1 . TYR A 1 156 ? 22.812 20.466 12.151 1.00 33.06 ? 174 TYR A CD1 1 ATOM 1240 C CD2 . TYR A 1 156 ? 21.358 20.415 10.298 1.00 30.99 ? 174 TYR A CD2 1 ATOM 1241 C CE1 . TYR A 1 156 ? 21.750 20.371 13.000 1.00 31.13 ? 174 TYR A CE1 1 ATOM 1242 C CE2 . TYR A 1 156 ? 20.290 20.317 11.138 1.00 31.33 ? 174 TYR A CE2 1 ATOM 1243 C CZ . TYR A 1 156 ? 20.490 20.313 12.492 1.00 31.64 ? 174 TYR A CZ 1 ATOM 1244 O OH . TYR A 1 156 ? 19.443 20.178 13.362 1.00 32.15 ? 174 TYR A OH 1 ATOM 1245 N N . ILE A 1 157 ? 26.658 21.831 8.881 1.00 36.28 ? 175 ILE A N 1 ATOM 1246 C CA . ILE A 1 157 ? 27.832 21.471 8.090 1.00 36.91 ? 175 ILE A CA 1 ATOM 1247 C C . ILE A 1 157 ? 28.475 20.184 8.640 1.00 37.75 ? 175 ILE A C 1 ATOM 1248 O O . ILE A 1 157 ? 28.744 20.044 9.841 1.00 36.22 ? 175 ILE A O 1 ATOM 1249 C CB . ILE A 1 157 ? 28.891 22.631 8.021 1.00 37.18 ? 175 ILE A CB 1 ATOM 1250 C CG1 . ILE A 1 157 ? 28.249 23.943 7.577 1.00 37.50 ? 175 ILE A CG1 1 ATOM 1251 C CG2 . ILE A 1 157 ? 29.994 22.316 7.043 1.00 35.05 ? 175 ILE A CG2 1 ATOM 1252 C CD1 . ILE A 1 157 ? 27.548 23.873 6.202 1.00 35.16 ? 175 ILE A CD1 1 ATOM 1253 N N . ALA A 1 158 ? 28.668 19.232 7.720 1.00 38.70 ? 176 ALA A N 1 ATOM 1254 C CA . ALA A 1 158 ? 29.268 17.933 8.042 1.00 39.70 ? 176 ALA A CA 1 ATOM 1255 C C . ALA A 1 158 ? 30.674 18.105 8.618 1.00 40.37 ? 176 ALA A C 1 ATOM 1256 O O . ALA A 1 158 ? 31.334 19.126 8.438 1.00 39.09 ? 176 ALA A O 1 ATOM 1257 C CB . ALA A 1 158 ? 29.290 17.016 6.774 1.00 39.75 ? 176 ALA A CB 1 ATOM 1258 N N . ARG A 1 159 ? 31.080 17.099 9.368 1.00 42.65 ? 177 ARG A N 1 ATOM 1259 C CA . ARG A 1 159 ? 32.457 17.018 9.908 1.00 44.80 ? 177 ARG A CA 1 ATOM 1260 C C . ARG A 1 159 ? 33.477 16.868 8.791 1.00 45.84 ? 177 ARG A C 1 ATOM 1261 O O . ARG A 1 159 ? 33.200 16.244 7.784 1.00 45.63 ? 177 ARG A O 1 ATOM 1262 C CB . ARG A 1 159 ? 32.559 15.822 10.869 1.00 45.13 ? 177 ARG A CB 1 ATOM 1263 C CG . ARG A 1 159 ? 33.942 15.578 11.443 1.00 46.83 ? 177 ARG A CG 1 ATOM 1264 C CD . ARG A 1 159 ? 33.890 14.506 12.523 1.00 48.45 ? 177 ARG A CD 1 ATOM 1265 N NE . ARG A 1 159 ? 33.505 13.190 12.014 1.00 51.20 ? 177 ARG A NE 1 ATOM 1266 C CZ . ARG A 1 159 ? 33.073 12.192 12.777 1.00 53.20 ? 177 ARG A CZ 1 ATOM 1267 N NH1 . ARG A 1 159 ? 32.931 12.364 14.078 1.00 54.18 ? 177 ARG A NH1 1 ATOM 1268 N NH2 . ARG A 1 159 ? 32.757 11.031 12.232 1.00 54.95 ? 177 ARG A NH2 1 ATOM 1269 N N . GLU A 1 160 ? 34.653 17.449 8.966 1.00 47.83 ? 178 GLU A N 1 ATOM 1270 C CA . GLU A 1 160 ? 35.748 17.241 7.979 1.00 49.19 ? 178 GLU A CA 1 ATOM 1271 C C . GLU A 1 160 ? 36.311 15.806 8.060 1.00 50.74 ? 178 GLU A C 1 ATOM 1272 O O . GLU A 1 160 ? 36.268 15.179 9.127 1.00 50.06 ? 178 GLU A O 1 ATOM 1273 C CB . GLU A 1 160 ? 36.868 18.252 8.178 1.00 49.20 ? 178 GLU A CB 1 ATOM 1274 C CG . GLU A 1 160 ? 36.491 19.708 7.975 1.00 48.78 ? 178 GLU A CG 1 ATOM 1275 C CD . GLU A 1 160 ? 36.140 20.045 6.549 1.00 50.26 ? 178 GLU A CD 1 ATOM 1276 O OE1 . GLU A 1 160 ? 35.069 20.652 6.329 1.00 49.86 ? 178 GLU A OE1 1 ATOM 1277 O OE2 . GLU A 1 160 ? 36.928 19.735 5.636 1.00 52.43 ? 178 GLU A OE2 1 ATOM 1278 N N . ALA A 1 161 ? 36.809 15.317 6.909 1.00 53.50 ? 179 ALA A N 1 ATOM 1279 C CA . ALA A 1 161 ? 37.548 14.004 6.725 1.00 55.00 ? 179 ALA A CA 1 ATOM 1280 C C . ALA A 1 161 ? 38.103 13.614 8.086 1.00 56.28 ? 179 ALA A C 1 ATOM 1281 O O . ALA A 1 161 ? 37.915 12.492 8.555 1.00 56.50 ? 179 ALA A O 1 ATOM 1282 C CB . ALA A 1 161 ? 38.642 14.142 5.663 1.00 55.48 ? 179 ALA A CB 1 ATOM 1283 N N . ASN A 1 162 ? 38.895 14.491 8.672 1.00 57.60 ? 180 ASN A N 1 ATOM 1284 C CA . ASN A 1 162 ? 40.234 14.195 9.067 1.00 58.74 ? 180 ASN A CA 1 ATOM 1285 C C . ASN A 1 162 ? 40.007 14.148 10.585 1.00 59.31 ? 180 ASN A C 1 ATOM 1286 O O . ASN A 1 162 ? 40.926 13.875 11.366 1.00 60.51 ? 180 ASN A O 1 ATOM 1287 C CB . ASN A 1 162 ? 41.190 15.326 8.793 1.00 59.37 ? 180 ASN A CB 1 ATOM 1288 C CG . ASN A 1 162 ? 40.478 16.640 8.714 1.00 60.86 ? 180 ASN A CG 1 ATOM 1289 O OD1 . ASN A 1 162 ? 40.653 17.527 9.551 1.00 62.61 ? 180 ASN A OD1 1 ATOM 1290 N ND2 . ASN A 1 162 ? 39.621 16.752 7.715 1.00 61.98 ? 180 ASN A ND2 1 ATOM 1291 N N . PHE A 1 163 ? 38.767 14.473 10.988 1.00 58.77 ? 181 PHE A N 1 ATOM 1292 C CA . PHE A 1 163 ? 38.352 14.514 12.392 1.00 57.99 ? 181 PHE A CA 1 ATOM 1293 C C . PHE A 1 163 ? 37.638 13.232 12.706 1.00 57.36 ? 181 PHE A C 1 ATOM 1294 O O . PHE A 1 163 ? 36.824 12.760 11.918 1.00 57.05 ? 181 PHE A O 1 ATOM 1295 C CB . PHE A 1 163 ? 37.360 15.654 12.675 1.00 57.87 ? 181 PHE A CB 1 ATOM 1296 C CG . PHE A 1 163 ? 37.960 17.035 12.631 1.00 58.71 ? 181 PHE A CG 1 ATOM 1297 C CD1 . PHE A 1 163 ? 39.029 17.376 13.437 1.00 60.23 ? 181 PHE A CD1 1 ATOM 1298 C CD2 . PHE A 1 163 ? 37.405 18.012 11.825 1.00 58.25 ? 181 PHE A CD2 1 ATOM 1299 C CE1 . PHE A 1 163 ? 39.561 18.683 13.398 1.00 60.41 ? 181 PHE A CE1 1 ATOM 1300 C CE2 . PHE A 1 163 ? 37.920 19.301 11.786 1.00 57.83 ? 181 PHE A CE2 1 ATOM 1301 C CZ . PHE A 1 163 ? 38.997 19.632 12.564 1.00 58.68 ? 181 PHE A CZ 1 ATOM 1302 N N . GLY A 1 164 ? 37.911 12.710 13.893 1.00 57.04 ? 182 GLY A N 1 ATOM 1303 C CA . GLY A 1 164 ? 37.356 11.421 14.315 1.00 57.03 ? 182 GLY A CA 1 ATOM 1304 C C . GLY A 1 164 ? 36.242 11.542 15.323 1.00 56.51 ? 182 GLY A C 1 ATOM 1305 O O . GLY A 1 164 ? 35.534 10.577 15.608 1.00 57.04 ? 182 GLY A O 1 ATOM 1306 N N . ASP A 1 165 ? 36.107 12.748 15.856 1.00 55.78 ? 183 ASP A N 1 ATOM 1307 C CA . ASP A 1 165 ? 35.092 13.072 16.865 1.00 55.05 ? 183 ASP A CA 1 ATOM 1308 C C . ASP A 1 165 ? 34.398 14.413 16.561 1.00 53.73 ? 183 ASP A C 1 ATOM 1309 O O . ASP A 1 165 ? 34.511 14.952 15.457 1.00 53.42 ? 183 ASP A O 1 ATOM 1310 C CB . ASP A 1 165 ? 35.702 13.080 18.268 1.00 55.03 ? 183 ASP A CB 1 ATOM 1311 C CG . ASP A 1 165 ? 36.803 14.108 18.435 1.00 57.23 ? 183 ASP A CG 1 ATOM 1312 O OD1 . ASP A 1 165 ? 36.697 15.211 17.857 1.00 58.88 ? 183 ASP A OD1 1 ATOM 1313 O OD2 . ASP A 1 165 ? 37.788 13.810 19.167 1.00 60.71 ? 183 ASP A OD2 1 ATOM 1314 N N . TYR A 1 166 ? 33.695 14.942 17.556 1.00 52.44 ? 184 TYR A N 1 ATOM 1315 C CA . TYR A 1 166 ? 32.872 16.156 17.374 1.00 51.05 ? 184 TYR A CA 1 ATOM 1316 C C . TYR A 1 166 ? 33.260 17.216 18.379 1.00 50.81 ? 184 TYR A C 1 ATOM 1317 O O . TYR A 1 166 ? 32.440 18.071 18.747 1.00 50.10 ? 184 TYR A O 1 ATOM 1318 C CB . TYR A 1 166 ? 31.373 15.848 17.486 1.00 50.37 ? 184 TYR A CB 1 ATOM 1319 C CG . TYR A 1 166 ? 30.802 15.319 16.214 1.00 48.52 ? 184 TYR A CG 1 ATOM 1320 C CD1 . TYR A 1 166 ? 30.624 16.147 15.109 1.00 48.49 ? 184 TYR A CD1 1 ATOM 1321 C CD2 . TYR A 1 166 ? 30.435 13.991 16.096 1.00 48.89 ? 184 TYR A CD2 1 ATOM 1322 C CE1 . TYR A 1 166 ? 30.102 15.666 13.930 1.00 47.27 ? 184 TYR A CE1 1 ATOM 1323 C CE2 . TYR A 1 166 ? 29.910 13.506 14.920 1.00 48.55 ? 184 TYR A CE2 1 ATOM 1324 C CZ . TYR A 1 166 ? 29.755 14.336 13.852 1.00 47.49 ? 184 TYR A CZ 1 ATOM 1325 O OH . TYR A 1 166 ? 29.254 13.816 12.703 1.00 47.42 ? 184 TYR A OH 1 ATOM 1326 N N . TYR A 1 167 ? 34.512 17.138 18.820 1.00 49.73 ? 185 TYR A N 1 ATOM 1327 C CA . TYR A 1 167 ? 35.055 18.080 19.778 1.00 49.72 ? 185 TYR A CA 1 ATOM 1328 C C . TYR A 1 167 ? 35.777 19.210 19.088 1.00 48.44 ? 185 TYR A C 1 ATOM 1329 O O . TYR A 1 167 ? 36.473 20.017 19.706 1.00 49.80 ? 185 TYR A O 1 ATOM 1330 C CB . TYR A 1 167 ? 35.995 17.400 20.775 1.00 50.28 ? 185 TYR A CB 1 ATOM 1331 C CG . TYR A 1 167 ? 35.252 16.458 21.691 1.00 53.53 ? 185 TYR A CG 1 ATOM 1332 C CD1 . TYR A 1 167 ? 34.246 16.927 22.507 1.00 55.14 ? 185 TYR A CD1 1 ATOM 1333 C CD2 . TYR A 1 167 ? 35.549 15.096 21.724 1.00 55.93 ? 185 TYR A CD2 1 ATOM 1334 C CE1 . TYR A 1 167 ? 33.545 16.077 23.327 1.00 57.55 ? 185 TYR A CE1 1 ATOM 1335 C CE2 . TYR A 1 167 ? 34.858 14.234 22.548 1.00 57.60 ? 185 TYR A CE2 1 ATOM 1336 C CZ . TYR A 1 167 ? 33.862 14.732 23.354 1.00 59.09 ? 185 TYR A CZ 1 ATOM 1337 O OH . TYR A 1 167 ? 33.161 13.893 24.189 1.00 61.32 ? 185 TYR A OH 1 ATOM 1338 N N . TYR A 1 168 ? 35.556 19.310 17.808 1.00 45.79 ? 186 TYR A N 1 ATOM 1339 C CA . TYR A 1 168 ? 36.277 20.292 17.011 1.00 43.49 ? 186 TYR A CA 1 ATOM 1340 C C . TYR A 1 168 ? 35.591 21.665 17.008 1.00 42.95 ? 186 TYR A C 1 ATOM 1341 O O . TYR A 1 168 ? 34.372 21.803 17.235 1.00 41.10 ? 186 TYR A O 1 ATOM 1342 C CB . TYR A 1 168 ? 36.464 19.782 15.558 1.00 43.23 ? 186 TYR A CB 1 ATOM 1343 C CG . TYR A 1 168 ? 35.175 19.461 14.854 1.00 41.73 ? 186 TYR A CG 1 ATOM 1344 C CD1 . TYR A 1 168 ? 34.419 20.464 14.261 1.00 41.69 ? 186 TYR A CD1 1 ATOM 1345 C CD2 . TYR A 1 168 ? 34.701 18.167 14.805 1.00 42.71 ? 186 TYR A CD2 1 ATOM 1346 C CE1 . TYR A 1 168 ? 33.213 20.172 13.613 1.00 40.52 ? 186 TYR A CE1 1 ATOM 1347 C CE2 . TYR A 1 168 ? 33.515 17.856 14.169 1.00 42.00 ? 186 TYR A CE2 1 ATOM 1348 C CZ . TYR A 1 168 ? 32.764 18.868 13.577 1.00 41.69 ? 186 TYR A CZ 1 ATOM 1349 O OH . TYR A 1 168 ? 31.584 18.523 12.946 1.00 37.80 ? 186 TYR A OH 1 ATOM 1350 N N . LYS A 1 169 ? 36.422 22.656 16.701 1.00 41.82 ? 187 LYS A N 1 ATOM 1351 C CA . LYS A 1 169 ? 35.995 24.026 16.481 1.00 41.38 ? 187 LYS A CA 1 ATOM 1352 C C . LYS A 1 169 ? 36.177 24.384 15.027 1.00 40.66 ? 187 LYS A C 1 ATOM 1353 O O . LYS A 1 169 ? 37.256 24.271 14.484 1.00 39.96 ? 187 LYS A O 1 ATOM 1354 C CB . LYS A 1 169 ? 36.788 24.983 17.384 1.00 41.42 ? 187 LYS A CB 1 ATOM 1355 C CG . LYS A 1 169 ? 36.541 26.468 17.106 1.00 42.07 ? 187 LYS A CG 1 ATOM 1356 C CD . LYS A 1 169 ? 37.341 27.357 18.058 1.00 42.86 ? 187 LYS A CD 1 ATOM 1357 C CE . LYS A 1 169 ? 36.991 28.814 17.828 1.00 44.62 ? 187 LYS A CE 1 ATOM 1358 N NZ . LYS A 1 169 ? 37.822 29.721 18.686 1.00 47.09 ? 187 LYS A NZ 1 ATOM 1359 N N . VAL A 1 170 ? 35.078 24.781 14.397 1.00 38.96 ? 188 VAL A N 1 ATOM 1360 C CA . VAL A 1 170 ? 35.116 25.282 13.020 1.00 38.46 ? 188 VAL A CA 1 ATOM 1361 C C . VAL A 1 170 ? 34.152 26.446 12.885 1.00 37.77 ? 188 VAL A C 1 ATOM 1362 O O . VAL A 1 170 ? 33.263 26.616 13.711 1.00 36.39 ? 188 VAL A O 1 ATOM 1363 C CB . VAL A 1 170 ? 34.706 24.196 11.976 1.00 38.69 ? 188 VAL A CB 1 ATOM 1364 C CG1 . VAL A 1 170 ? 35.799 23.071 11.888 1.00 37.69 ? 188 VAL A CG1 1 ATOM 1365 C CG2 . VAL A 1 170 ? 33.341 23.624 12.327 1.00 37.19 ? 188 VAL A CG2 1 ATOM 1366 N N . GLU A 1 171 ? 34.348 27.209 11.829 1.00 37.05 ? 189 GLU A N 1 ATOM 1367 C CA . GLU A 1 171 ? 33.532 28.373 11.566 1.00 37.81 ? 189 GLU A CA 1 ATOM 1368 C C . GLU A 1 171 ? 33.163 28.639 10.116 1.00 37.41 ? 189 GLU A C 1 ATOM 1369 O O . GLU A 1 171 ? 33.681 28.032 9.167 1.00 37.87 ? 189 GLU A O 1 ATOM 1370 C CB . GLU A 1 171 ? 34.195 29.598 12.170 1.00 37.70 ? 189 GLU A CB 1 ATOM 1371 C CG . GLU A 1 171 ? 35.371 30.067 11.453 1.00 41.18 ? 189 GLU A CG 1 ATOM 1372 C CD . GLU A 1 171 ? 36.127 31.101 12.256 1.00 42.69 ? 189 GLU A CD 1 ATOM 1373 O OE1 . GLU A 1 171 ? 36.060 31.023 13.520 1.00 39.32 ? 189 GLU A OE1 1 ATOM 1374 O OE2 . GLU A 1 171 ? 36.771 31.970 11.606 1.00 43.43 ? 189 GLU A OE2 1 ATOM 1375 N N . ALA A 1 172 ? 32.187 29.531 9.986 1.00 35.86 ? 190 ALA A N 1 ATOM 1376 C CA . ALA A 1 172 ? 31.710 30.053 8.686 1.00 34.28 ? 190 ALA A CA 1 ATOM 1377 C C . ALA A 1 172 ? 31.456 31.538 8.805 1.00 33.82 ? 190 ALA A C 1 ATOM 1378 O O . ALA A 1 172 ? 31.142 32.040 9.890 1.00 34.53 ? 190 ALA A O 1 ATOM 1379 C CB . ALA A 1 172 ? 30.424 29.333 8.264 1.00 32.68 ? 190 ALA A CB 1 ATOM 1380 N N . ASP A 1 173 ? 31.565 32.246 7.696 1.00 32.33 ? 191 ASP A N 1 ATOM 1381 C CA . ASP A 1 173 ? 31.233 33.672 7.656 1.00 30.67 ? 191 ASP A CA 1 ATOM 1382 C C . ASP A 1 173 ? 29.863 33.806 6.999 1.00 30.45 ? 191 ASP A C 1 ATOM 1383 O O . ASP A 1 173 ? 29.620 33.198 5.952 1.00 29.91 ? 191 ASP A O 1 ATOM 1384 C CB . ASP A 1 173 ? 32.287 34.428 6.881 1.00 29.96 ? 191 ASP A CB 1 ATOM 1385 C CG . ASP A 1 173 ? 32.052 35.901 6.857 1.00 32.19 ? 191 ASP A CG 1 ATOM 1386 O OD1 . ASP A 1 173 ? 30.934 36.338 6.503 1.00 33.74 ? 191 ASP A OD1 1 ATOM 1387 O OD2 . ASP A 1 173 ? 32.997 36.658 7.188 1.00 33.31 ? 191 ASP A OD2 1 ATOM 1388 N N . PHE A 1 174 ? 28.949 34.542 7.644 1.00 29.47 ? 192 PHE A N 1 ATOM 1389 C CA . PHE A 1 174 ? 27.631 34.847 7.036 1.00 28.34 ? 192 PHE A CA 1 ATOM 1390 C C . PHE A 1 174 ? 27.394 36.329 7.072 1.00 28.07 ? 192 PHE A C 1 ATOM 1391 O O . PHE A 1 174 ? 27.838 37.020 7.975 1.00 28.63 ? 192 PHE A O 1 ATOM 1392 C CB . PHE A 1 174 ? 26.456 34.040 7.636 1.00 28.26 ? 192 PHE A CB 1 ATOM 1393 C CG . PHE A 1 174 ? 26.088 34.397 9.083 1.00 28.08 ? 192 PHE A CG 1 ATOM 1394 C CD1 . PHE A 1 174 ? 25.081 35.319 9.354 1.00 29.74 ? 192 PHE A CD1 1 ATOM 1395 C CD2 . PHE A 1 174 ? 26.696 33.779 10.141 1.00 28.88 ? 192 PHE A CD2 1 ATOM 1396 C CE1 . PHE A 1 174 ? 24.716 35.643 10.684 1.00 28.44 ? 192 PHE A CE1 1 ATOM 1397 C CE2 . PHE A 1 174 ? 26.343 34.098 11.456 1.00 30.43 ? 192 PHE A CE2 1 ATOM 1398 C CZ . PHE A 1 174 ? 25.331 35.031 11.710 1.00 29.61 ? 192 PHE A CZ 1 ATOM 1399 N N . TYR A 1 175 ? 26.756 36.819 6.017 1.00 28.66 ? 193 TYR A N 1 ATOM 1400 C CA . TYR A 1 175 ? 26.655 38.235 5.761 1.00 28.01 ? 193 TYR A CA 1 ATOM 1401 C C . TYR A 1 175 ? 25.217 38.665 5.609 1.00 28.56 ? 193 TYR A C 1 ATOM 1402 O O . TYR A 1 175 ? 24.474 38.127 4.812 1.00 27.49 ? 193 TYR A O 1 ATOM 1403 C CB . TYR A 1 175 ? 27.421 38.607 4.491 1.00 28.47 ? 193 TYR A CB 1 ATOM 1404 C CG . TYR A 1 175 ? 27.384 40.084 4.180 1.00 25.81 ? 193 TYR A CG 1 ATOM 1405 C CD1 . TYR A 1 175 ? 27.902 40.980 5.053 1.00 24.16 ? 193 TYR A CD1 1 ATOM 1406 C CD2 . TYR A 1 175 ? 26.853 40.568 2.992 1.00 27.87 ? 193 TYR A CD2 1 ATOM 1407 C CE1 . TYR A 1 175 ? 27.882 42.315 4.793 1.00 26.08 ? 193 TYR A CE1 1 ATOM 1408 C CE2 . TYR A 1 175 ? 26.838 41.947 2.709 1.00 25.73 ? 193 TYR A CE2 1 ATOM 1409 C CZ . TYR A 1 175 ? 27.332 42.790 3.638 1.00 26.76 ? 193 TYR A CZ 1 ATOM 1410 O OH . TYR A 1 175 ? 27.377 44.156 3.471 1.00 33.90 ? 193 TYR A OH 1 ATOM 1411 N N . LEU A 1 176 ? 24.862 39.698 6.356 1.00 28.60 ? 194 LEU A N 1 ATOM 1412 C CA . LEU A 1 176 ? 23.485 40.222 6.363 1.00 27.58 ? 194 LEU A CA 1 ATOM 1413 C C . LEU A 1 176 ? 23.456 41.606 5.766 1.00 27.99 ? 194 LEU A C 1 ATOM 1414 O O . LEU A 1 176 ? 24.035 42.536 6.289 1.00 27.65 ? 194 LEU A O 1 ATOM 1415 C CB . LEU A 1 176 ? 22.940 40.266 7.797 1.00 26.98 ? 194 LEU A CB 1 ATOM 1416 C CG . LEU A 1 176 ? 22.817 38.969 8.617 1.00 26.74 ? 194 LEU A CG 1 ATOM 1417 C CD1 . LEU A 1 176 ? 22.193 39.242 10.037 1.00 26.00 ? 194 LEU A CD1 1 ATOM 1418 C CD2 . LEU A 1 176 ? 22.037 37.912 7.861 1.00 25.72 ? 194 LEU A CD2 1 ATOM 1419 N N . SER A 1 177 ? 22.765 41.713 4.640 1.00 28.60 ? 195 SER A N 1 ATOM 1420 C CA . SER A 1 177 ? 22.580 42.972 3.932 1.00 29.43 ? 195 SER A CA 1 ATOM 1421 C C . SER A 1 177 ? 21.186 43.010 3.341 1.00 29.34 ? 195 SER A C 1 ATOM 1422 O O . SER A 1 177 ? 20.526 41.970 3.151 1.00 29.99 ? 195 SER A O 1 ATOM 1423 C CB . SER A 1 177 ? 23.601 43.115 2.780 1.00 30.30 ? 195 SER A CB 1 ATOM 1424 O OG . SER A 1 177 ? 23.377 42.080 1.827 1.00 31.46 ? 195 SER A OG 1 ATOM 1425 N N . GLY A 1 178 ? 20.746 44.228 3.069 1.00 29.67 ? 196 GLY A N 1 ATOM 1426 C CA . GLY A 1 178 ? 19.478 44.472 2.354 1.00 29.89 ? 196 GLY A CA 1 ATOM 1427 C C . GLY A 1 178 ? 18.306 44.768 3.266 1.00 29.77 ? 196 GLY A C 1 ATOM 1428 O O . GLY A 1 178 ? 17.196 44.985 2.801 1.00 30.45 ? 196 GLY A O 1 ATOM 1429 N N . CYS A 1 179 ? 18.529 44.758 4.576 1.00 28.50 ? 197 CYS A N 1 ATOM 1430 C CA . CYS A 1 179 ? 17.423 45.006 5.524 1.00 27.92 ? 197 CYS A CA 1 ATOM 1431 C C . CYS A 1 179 ? 17.840 45.894 6.664 1.00 28.03 ? 197 CYS A C 1 ATOM 1432 O O . CYS A 1 179 ? 19.017 45.966 6.990 1.00 28.84 ? 197 CYS A O 1 ATOM 1433 C CB . CYS A 1 179 ? 16.906 43.703 6.087 1.00 27.96 ? 197 CYS A CB 1 ATOM 1434 S SG . CYS A 1 179 ? 16.829 42.289 4.939 1.00 28.67 ? 197 CYS A SG 1 ATOM 1435 N N . ASP A 1 180 ? 16.872 46.518 7.307 1.00 27.80 ? 198 ASP A N 1 ATOM 1436 C CA . ASP A 1 180 ? 17.136 47.320 8.497 1.00 27.83 ? 198 ASP A CA 1 ATOM 1437 C C . ASP A 1 180 ? 17.530 46.366 9.636 1.00 27.86 ? 198 ASP A C 1 ATOM 1438 O O . ASP A 1 180 ? 18.488 46.587 10.400 1.00 26.64 ? 198 ASP A O 1 ATOM 1439 C CB . ASP A 1 180 ? 15.926 48.151 8.900 1.00 29.47 ? 198 ASP A CB 1 ATOM 1440 C CG . ASP A 1 180 ? 15.690 49.331 7.972 1.00 32.84 ? 198 ASP A CG 1 ATOM 1441 O OD1 . ASP A 1 180 ? 16.674 49.817 7.399 1.00 35.60 ? 198 ASP A OD1 1 ATOM 1442 O OD2 . ASP A 1 180 ? 14.519 49.799 7.809 1.00 37.44 ? 198 ASP A OD2 1 ATOM 1443 N N . GLU A 1 181 ? 16.768 45.294 9.745 1.00 27.29 ? 199 GLU A N 1 ATOM 1444 C CA . GLU A 1 181 ? 17.090 44.211 10.690 1.00 27.16 ? 199 GLU A CA 1 ATOM 1445 C C . GLU A 1 181 ? 16.700 42.873 10.151 1.00 25.45 ? 199 GLU A C 1 ATOM 1446 O O . GLU A 1 181 ? 15.937 42.764 9.198 1.00 25.20 ? 199 GLU A O 1 ATOM 1447 C CB . GLU A 1 181 ? 16.380 44.376 12.019 1.00 28.68 ? 199 GLU A CB 1 ATOM 1448 C CG . GLU A 1 181 ? 16.325 45.754 12.484 1.00 35.49 ? 199 GLU A CG 1 ATOM 1449 C CD . GLU A 1 181 ? 16.806 45.874 13.850 1.00 44.68 ? 199 GLU A CD 1 ATOM 1450 O OE1 . GLU A 1 181 ? 18.046 45.711 13.964 1.00 48.71 ? 199 GLU A OE1 1 ATOM 1451 O OE2 . GLU A 1 181 ? 15.947 46.098 14.769 1.00 45.20 ? 199 GLU A OE2 1 ATOM 1452 N N . TYR A 1 182 ? 17.189 41.863 10.838 1.00 23.30 ? 200 TYR A N 1 ATOM 1453 C CA . TYR A 1 182 ? 17.057 40.491 10.362 1.00 22.84 ? 200 TYR A CA 1 ATOM 1454 C C . TYR A 1 182 ? 16.714 39.607 11.494 1.00 23.13 ? 200 TYR A C 1 ATOM 1455 O O . TYR A 1 182 ? 17.328 39.725 12.557 1.00 22.66 ? 200 TYR A O 1 ATOM 1456 C CB . TYR A 1 182 ? 18.376 40.006 9.726 1.00 22.90 ? 200 TYR A CB 1 ATOM 1457 C CG . TYR A 1 182 ? 19.006 40.979 8.738 1.00 21.44 ? 200 TYR A CG 1 ATOM 1458 C CD1 . TYR A 1 182 ? 19.002 40.726 7.378 1.00 24.41 ? 200 TYR A CD1 1 ATOM 1459 C CD2 . TYR A 1 182 ? 19.575 42.168 9.173 1.00 20.30 ? 200 TYR A CD2 1 ATOM 1460 C CE1 . TYR A 1 182 ? 19.566 41.637 6.474 1.00 24.84 ? 200 TYR A CE1 1 ATOM 1461 C CE2 . TYR A 1 182 ? 20.147 43.040 8.310 1.00 20.28 ? 200 TYR A CE2 1 ATOM 1462 C CZ . TYR A 1 182 ? 20.138 42.771 6.945 1.00 24.48 ? 200 TYR A CZ 1 ATOM 1463 O OH . TYR A 1 182 ? 20.680 43.707 6.067 1.00 27.68 ? 200 TYR A OH 1 ATOM 1464 N N . ILE A 1 183 ? 15.736 38.722 11.304 1.00 23.58 ? 201 ILE A N 1 ATOM 1465 C CA . ILE A 1 183 ? 15.516 37.646 12.287 1.00 24.09 ? 201 ILE A CA 1 ATOM 1466 C C . ILE A 1 183 ? 16.188 36.376 11.758 1.00 24.78 ? 201 ILE A C 1 ATOM 1467 O O . ILE A 1 183 ? 15.882 35.936 10.665 1.00 25.08 ? 201 ILE A O 1 ATOM 1468 C CB . ILE A 1 183 ? 14.024 37.351 12.549 1.00 24.61 ? 201 ILE A CB 1 ATOM 1469 C CG1 . ILE A 1 183 ? 13.226 38.626 12.858 1.00 24.58 ? 201 ILE A CG1 1 ATOM 1470 C CG2 . ILE A 1 183 ? 13.870 36.297 13.680 1.00 22.99 ? 201 ILE A CG2 1 ATOM 1471 C CD1 . ILE A 1 183 ? 11.685 38.364 13.046 1.00 23.56 ? 201 ILE A CD1 1 ATOM 1472 N N . VAL A 1 184 ? 17.121 35.830 12.539 1.00 25.45 ? 202 VAL A N 1 ATOM 1473 C CA . VAL A 1 184 ? 17.832 34.594 12.194 1.00 25.46 ? 202 VAL A CA 1 ATOM 1474 C C . VAL A 1 184 ? 17.801 33.604 13.351 1.00 25.64 ? 202 VAL A C 1 ATOM 1475 O O . VAL A 1 184 ? 17.703 34.008 14.517 1.00 25.40 ? 202 VAL A O 1 ATOM 1476 C CB . VAL A 1 184 ? 19.369 34.852 11.724 1.00 26.95 ? 202 VAL A CB 1 ATOM 1477 C CG1 . VAL A 1 184 ? 19.441 35.843 10.543 1.00 26.77 ? 202 VAL A CG1 1 ATOM 1478 C CG2 . VAL A 1 184 ? 20.245 35.293 12.857 1.00 24.01 ? 202 VAL A CG2 1 ATOM 1479 N N . PRO A 1 185 ? 17.916 32.302 13.044 1.00 25.76 ? 203 PRO A N 1 ATOM 1480 C CA . PRO A 1 185 ? 17.911 31.319 14.100 1.00 25.77 ? 203 PRO A CA 1 ATOM 1481 C C . PRO A 1 185 ? 19.303 30.984 14.541 1.00 26.05 ? 203 PRO A C 1 ATOM 1482 O O . PRO A 1 185 ? 20.227 30.834 13.710 1.00 27.64 ? 203 PRO A O 1 ATOM 1483 C CB . PRO A 1 185 ? 17.277 30.089 13.436 1.00 25.52 ? 203 PRO A CB 1 ATOM 1484 C CG . PRO A 1 185 ? 17.772 30.204 12.004 1.00 26.52 ? 203 PRO A CG 1 ATOM 1485 C CD . PRO A 1 185 ? 18.042 31.659 11.723 1.00 25.67 ? 203 PRO A CD 1 ATOM 1486 N N . LEU A 1 186 ? 19.410 30.887 15.858 1.00 25.93 ? 204 LEU A N 1 ATOM 1487 C CA . LEU A 1 186 ? 20.566 30.343 16.568 1.00 26.40 ? 204 LEU A CA 1 ATOM 1488 C C . LEU A 1 186 ? 20.096 29.153 17.376 1.00 26.51 ? 204 LEU A C 1 ATOM 1489 O O . LEU A 1 186 ? 19.299 29.305 18.301 1.00 26.72 ? 204 LEU A O 1 ATOM 1490 C CB . LEU A 1 186 ? 21.187 31.394 17.487 1.00 26.28 ? 204 LEU A CB 1 ATOM 1491 C CG . LEU A 1 186 ? 22.320 30.872 18.395 1.00 26.81 ? 204 LEU A CG 1 ATOM 1492 C CD1 . LEU A 1 186 ? 23.473 30.237 17.624 1.00 26.49 ? 204 LEU A CD1 1 ATOM 1493 C CD2 . LEU A 1 186 ? 22.867 31.903 19.383 1.00 25.57 ? 204 LEU A CD2 1 ATOM 1494 N N . CYS A 1 187 ? 20.579 27.981 16.982 1.00 27.15 ? 205 CYS A N 1 ATOM 1495 C CA . CYS A 1 187 ? 20.083 26.704 17.462 1.00 28.09 ? 205 CYS A CA 1 ATOM 1496 C C . CYS A 1 187 ? 21.184 25.733 17.878 1.00 28.72 ? 205 CYS A C 1 ATOM 1497 O O . CYS A 1 187 ? 22.299 25.706 17.332 1.00 28.41 ? 205 CYS A O 1 ATOM 1498 C CB . CYS A 1 187 ? 19.223 26.003 16.382 1.00 28.30 ? 205 CYS A CB 1 ATOM 1499 S SG . CYS A 1 187 ? 17.966 27.031 15.547 1.00 27.36 ? 205 CYS A SG 1 ATOM 1500 N N . ILE A 1 188 ? 20.802 24.901 18.838 1.00 29.73 ? 206 ILE A N 1 ATOM 1501 C CA . ILE A 1 188 ? 21.613 23.762 19.266 1.00 29.58 ? 206 ILE A CA 1 ATOM 1502 C C . ILE A 1 188 ? 20.720 22.602 19.613 1.00 29.81 ? 206 ILE A C 1 ATOM 1503 O O . ILE A 1 188 ? 19.541 22.764 19.961 1.00 29.36 ? 206 ILE A O 1 ATOM 1504 C CB . ILE A 1 188 ? 22.492 24.055 20.523 1.00 28.79 ? 206 ILE A CB 1 ATOM 1505 C CG1 . ILE A 1 188 ? 21.641 24.603 21.663 1.00 30.04 ? 206 ILE A CG1 1 ATOM 1506 C CG2 . ILE A 1 188 ? 23.627 24.964 20.177 1.00 29.92 ? 206 ILE A CG2 1 ATOM 1507 C CD1 . ILE A 1 188 ? 22.323 24.621 23.031 1.00 30.79 ? 206 ILE A CD1 1 ATOM 1508 N N . PHE A 1 189 ? 21.306 21.422 19.516 1.00 30.73 ? 207 PHE A N 1 ATOM 1509 C CA . PHE A 1 189 ? 20.767 20.250 20.204 1.00 31.52 ? 207 PHE A CA 1 ATOM 1510 C C . PHE A 1 189 ? 21.058 20.411 21.668 1.00 32.30 ? 207 PHE A C 1 ATOM 1511 O O . PHE A 1 189 ? 22.230 20.474 22.085 1.00 33.55 ? 207 PHE A O 1 ATOM 1512 C CB . PHE A 1 189 ? 21.379 18.953 19.678 1.00 31.79 ? 207 PHE A CB 1 ATOM 1513 C CG . PHE A 1 189 ? 20.828 18.557 18.345 1.00 31.77 ? 207 PHE A CG 1 ATOM 1514 C CD1 . PHE A 1 189 ? 19.509 18.135 18.244 1.00 31.22 ? 207 PHE A CD1 1 ATOM 1515 C CD2 . PHE A 1 189 ? 21.595 18.667 17.191 1.00 32.59 ? 207 PHE A CD2 1 ATOM 1516 C CE1 . PHE A 1 189 ? 18.968 17.793 17.012 1.00 30.88 ? 207 PHE A CE1 1 ATOM 1517 C CE2 . PHE A 1 189 ? 21.054 18.325 15.938 1.00 31.64 ? 207 PHE A CE2 1 ATOM 1518 C CZ . PHE A 1 189 ? 19.741 17.883 15.870 1.00 31.72 ? 207 PHE A CZ 1 ATOM 1519 N N . ASN A 1 190 ? 19.988 20.537 22.437 1.00 33.05 ? 208 ASN A N 1 ATOM 1520 C CA . ASN A 1 190 ? 20.095 20.713 23.863 1.00 33.87 ? 208 ASN A CA 1 ATOM 1521 C C . ASN A 1 190 ? 19.770 19.395 24.548 1.00 34.25 ? 208 ASN A C 1 ATOM 1522 O O . ASN A 1 190 ? 18.620 19.008 24.759 1.00 33.41 ? 208 ASN A O 1 ATOM 1523 C CB . ASN A 1 190 ? 19.213 21.862 24.333 1.00 34.17 ? 208 ASN A CB 1 ATOM 1524 C CG . ASN A 1 190 ? 19.396 22.154 25.814 1.00 36.62 ? 208 ASN A CG 1 ATOM 1525 O OD1 . ASN A 1 190 ? 20.406 21.767 26.414 1.00 34.46 ? 208 ASN A OD1 1 ATOM 1526 N ND2 . ASN A 1 190 ? 18.400 22.783 26.412 1.00 36.04 ? 208 ASN A ND2 1 ATOM 1527 N N . GLY A 1 191 ? 20.847 18.686 24.851 1.00 35.27 ? 209 GLY A N 1 ATOM 1528 C CA . GLY A 1 191 ? 20.758 17.307 25.334 1.00 35.45 ? 209 GLY A CA 1 ATOM 1529 C C . GLY A 1 191 ? 22.086 16.589 25.191 1.00 35.35 ? 209 GLY A C 1 ATOM 1530 O O . GLY A 1 191 ? 23.022 17.117 24.615 1.00 35.81 ? 209 GLY A O 1 ATOM 1531 N N . LYS A 1 192 ? 22.161 15.389 25.740 1.00 36.54 ? 210 LYS A N 1 ATOM 1532 C CA . LYS A 1 192 ? 23.403 14.588 25.651 1.00 37.99 ? 210 LYS A CA 1 ATOM 1533 C C . LYS A 1 192 ? 23.292 13.770 24.371 1.00 39.14 ? 210 LYS A C 1 ATOM 1534 O O . LYS A 1 192 ? 22.471 12.850 24.270 1.00 39.21 ? 210 LYS A O 1 ATOM 1535 C CB . LYS A 1 192 ? 23.549 13.684 26.877 1.00 38.39 ? 210 LYS A CB 1 ATOM 1536 C CG . LYS A 1 192 ? 23.822 14.424 28.153 1.00 37.97 ? 210 LYS A CG 1 ATOM 1537 C CD . LYS A 1 192 ? 25.191 15.046 28.108 1.00 41.97 ? 210 LYS A CD 1 ATOM 1538 C CE . LYS A 1 192 ? 25.583 15.687 29.463 1.00 42.55 ? 210 LYS A CE 1 ATOM 1539 N NZ . LYS A 1 192 ? 26.835 16.519 29.273 1.00 41.48 ? 210 LYS A NZ 1 ATOM 1540 N N . PHE A 1 193 ? 24.081 14.167 23.388 1.00 40.86 ? 211 PHE A N 1 ATOM 1541 C CA . PHE A 1 193 ? 23.937 13.711 21.998 1.00 42.47 ? 211 PHE A CA 1 ATOM 1542 C C . PHE A 1 193 ? 24.969 12.651 21.708 1.00 43.78 ? 211 PHE A C 1 ATOM 1543 O O . PHE A 1 193 ? 26.169 12.921 21.682 1.00 41.99 ? 211 PHE A O 1 ATOM 1544 C CB . PHE A 1 193 ? 24.097 14.888 21.017 1.00 42.90 ? 211 PHE A CB 1 ATOM 1545 C CG . PHE A 1 193 ? 23.734 14.571 19.597 1.00 44.09 ? 211 PHE A CG 1 ATOM 1546 C CD1 . PHE A 1 193 ? 22.555 15.050 19.042 1.00 45.33 ? 211 PHE A CD1 1 ATOM 1547 C CD2 . PHE A 1 193 ? 24.585 13.811 18.802 1.00 46.33 ? 211 PHE A CD2 1 ATOM 1548 C CE1 . PHE A 1 193 ? 22.230 14.790 17.733 1.00 46.63 ? 211 PHE A CE1 1 ATOM 1549 C CE2 . PHE A 1 193 ? 24.284 13.556 17.483 1.00 45.71 ? 211 PHE A CE2 1 ATOM 1550 C CZ . PHE A 1 193 ? 23.091 14.029 16.946 1.00 47.20 ? 211 PHE A CZ 1 ATOM 1551 N N . LEU A 1 194 ? 24.456 11.447 21.482 1.00 46.08 ? 212 LEU A N 1 ATOM 1552 C CA . LEU A 1 194 ? 25.292 10.246 21.334 1.00 48.42 ? 212 LEU A CA 1 ATOM 1553 C C . LEU A 1 194 ? 25.789 10.064 19.920 1.00 50.18 ? 212 LEU A C 1 ATOM 1554 O O . LEU A 1 194 ? 25.020 10.036 18.953 1.00 50.34 ? 212 LEU A O 1 ATOM 1555 C CB . LEU A 1 194 ? 24.535 8.970 21.741 1.00 48.44 ? 212 LEU A CB 1 ATOM 1556 C CG . LEU A 1 194 ? 25.377 7.674 21.692 1.00 48.51 ? 212 LEU A CG 1 ATOM 1557 C CD1 . LEU A 1 194 ? 26.640 7.730 22.588 1.00 48.26 ? 212 LEU A CD1 1 ATOM 1558 C CD2 . LEU A 1 194 ? 24.500 6.489 22.099 1.00 47.13 ? 212 LEU A CD2 1 ATOM 1559 N N . SER A 1 195 ? 27.099 9.963 19.806 1.00 52.69 ? 213 SER A N 1 ATOM 1560 C CA . SER A 1 195 ? 27.705 9.603 18.526 1.00 54.49 ? 213 SER A CA 1 ATOM 1561 C C . SER A 1 195 ? 28.969 8.816 18.757 1.00 55.68 ? 213 SER A C 1 ATOM 1562 O O . SER A 1 195 ? 29.932 9.313 19.368 1.00 55.57 ? 213 SER A O 1 ATOM 1563 C CB . SER A 1 195 ? 28.009 10.861 17.724 1.00 54.71 ? 213 SER A CB 1 ATOM 1564 O OG . SER A 1 195 ? 28.610 10.566 16.480 1.00 55.35 ? 213 SER A OG 1 ATOM 1565 N N . ASN A 1 196 ? 28.926 7.582 18.252 1.00 58.06 ? 214 ASN A N 1 ATOM 1566 C CA . ASN A 1 196 ? 30.015 6.586 18.390 1.00 58.82 ? 214 ASN A CA 1 ATOM 1567 C C . ASN A 1 196 ? 30.551 6.525 19.785 1.00 58.83 ? 214 ASN A C 1 ATOM 1568 O O . ASN A 1 196 ? 31.743 6.772 20.021 1.00 59.47 ? 214 ASN A O 1 ATOM 1569 C CB . ASN A 1 196 ? 31.193 6.871 17.462 1.00 59.56 ? 214 ASN A CB 1 ATOM 1570 C CG . ASN A 1 196 ? 32.198 5.720 17.464 1.00 61.72 ? 214 ASN A CG 1 ATOM 1571 O OD1 . ASN A 1 196 ? 33.411 5.923 17.558 1.00 62.28 ? 214 ASN A OD1 1 ATOM 1572 N ND2 . ASN A 1 196 ? 31.673 4.487 17.409 1.00 63.75 ? 214 ASN A ND2 1 ATOM 1573 N N . THR A 1 197 ? 29.652 6.242 20.709 1.00 58.91 ? 215 THR A N 1 ATOM 1574 C CA . THR A 1 197 ? 30.008 5.967 22.114 1.00 59.08 ? 215 THR A CA 1 ATOM 1575 C C . THR A 1 197 ? 30.290 7.182 22.962 1.00 58.65 ? 215 THR A C 1 ATOM 1576 O O . THR A 1 197 ? 30.426 7.068 24.186 1.00 59.00 ? 215 THR A O 1 ATOM 1577 C CB . THR A 1 197 ? 31.248 5.023 22.269 1.00 59.80 ? 215 THR A CB 1 ATOM 1578 O OG1 . THR A 1 197 ? 32.484 5.773 22.190 1.00 59.75 ? 215 THR A OG1 1 ATOM 1579 C CG2 . THR A 1 197 ? 31.205 3.874 21.221 1.00 59.58 ? 215 THR A CG2 1 ATOM 1580 N N . LYS A 1 198 ? 30.390 8.339 22.321 1.00 58.01 ? 216 LYS A N 1 ATOM 1581 C CA . LYS A 1 198 ? 30.614 9.604 23.055 1.00 57.28 ? 216 LYS A CA 1 ATOM 1582 C C . LYS A 1 198 ? 29.413 10.552 23.028 1.00 55.34 ? 216 LYS A C 1 ATOM 1583 O O . LYS A 1 198 ? 28.685 10.658 22.039 1.00 54.83 ? 216 LYS A O 1 ATOM 1584 C CB . LYS A 1 198 ? 31.880 10.271 22.546 1.00 57.91 ? 216 LYS A CB 1 ATOM 1585 C CG . LYS A 1 198 ? 33.120 9.504 22.960 1.00 60.58 ? 216 LYS A CG 1 ATOM 1586 C CD . LYS A 1 198 ? 34.407 10.181 22.454 1.00 64.23 ? 216 LYS A CD 1 ATOM 1587 C CE . LYS A 1 198 ? 35.524 10.190 23.537 1.00 66.75 ? 216 LYS A CE 1 ATOM 1588 N NZ . LYS A 1 198 ? 35.441 9.038 24.526 1.00 67.86 ? 216 LYS A NZ 1 ATOM 1589 N N . TYR A 1 199 ? 29.198 11.183 24.177 1.00 53.61 ? 217 TYR A N 1 ATOM 1590 C CA . TYR A 1 199 ? 28.078 12.115 24.384 1.00 52.14 ? 217 TYR A CA 1 ATOM 1591 C C . TYR A 1 199 ? 28.528 13.544 24.231 1.00 50.15 ? 217 TYR A C 1 ATOM 1592 O O . TYR A 1 199 ? 29.434 14.021 24.936 1.00 50.53 ? 217 TYR A O 1 ATOM 1593 C CB . TYR A 1 199 ? 27.441 11.945 25.757 1.00 52.26 ? 217 TYR A CB 1 ATOM 1594 C CG . TYR A 1 199 ? 26.670 10.667 25.892 1.00 54.39 ? 217 TYR A CG 1 ATOM 1595 C CD1 . TYR A 1 199 ? 25.337 10.595 25.528 1.00 54.78 ? 217 TYR A CD1 1 ATOM 1596 C CD2 . TYR A 1 199 ? 27.285 9.511 26.378 1.00 57.78 ? 217 TYR A CD2 1 ATOM 1597 C CE1 . TYR A 1 199 ? 24.632 9.420 25.648 1.00 55.77 ? 217 TYR A CE1 1 ATOM 1598 C CE2 . TYR A 1 199 ? 26.580 8.327 26.505 1.00 57.92 ? 217 TYR A CE2 1 ATOM 1599 C CZ . TYR A 1 199 ? 25.259 8.291 26.138 1.00 57.18 ? 217 TYR A CZ 1 ATOM 1600 O OH . TYR A 1 199 ? 24.563 7.119 26.265 1.00 59.21 ? 217 TYR A OH 1 ATOM 1601 N N . TYR A 1 200 ? 27.853 14.233 23.324 1.00 47.23 ? 218 TYR A N 1 ATOM 1602 C CA . TYR A 1 200 ? 28.182 15.634 23.009 1.00 45.36 ? 218 TYR A CA 1 ATOM 1603 C C . TYR A 1 200 ? 27.202 16.643 23.572 1.00 42.28 ? 218 TYR A C 1 ATOM 1604 O O . TYR A 1 200 ? 26.029 16.353 23.790 1.00 41.55 ? 218 TYR A O 1 ATOM 1605 C CB . TYR A 1 200 ? 28.344 15.811 21.507 1.00 45.47 ? 218 TYR A CB 1 ATOM 1606 C CG . TYR A 1 200 ? 29.521 15.015 20.994 1.00 48.69 ? 218 TYR A CG 1 ATOM 1607 C CD1 . TYR A 1 200 ? 30.814 15.513 21.122 1.00 50.53 ? 218 TYR A CD1 1 ATOM 1608 C CD2 . TYR A 1 200 ? 29.344 13.756 20.418 1.00 49.22 ? 218 TYR A CD2 1 ATOM 1609 C CE1 . TYR A 1 200 ? 31.914 14.793 20.672 1.00 52.43 ? 218 TYR A CE1 1 ATOM 1610 C CE2 . TYR A 1 200 ? 30.436 13.016 19.954 1.00 51.06 ? 218 TYR A CE2 1 ATOM 1611 C CZ . TYR A 1 200 ? 31.719 13.536 20.088 1.00 52.68 ? 218 TYR A CZ 1 ATOM 1612 O OH . TYR A 1 200 ? 32.816 12.847 19.644 1.00 51.70 ? 218 TYR A OH 1 ATOM 1613 N N . ASP A 1 201 ? 27.764 17.813 23.823 1.00 39.83 ? 219 ASP A N 1 ATOM 1614 C CA . ASP A 1 201 ? 27.044 19.025 24.252 1.00 37.75 ? 219 ASP A CA 1 ATOM 1615 C C . ASP A 1 201 ? 27.291 20.098 23.209 1.00 35.19 ? 219 ASP A C 1 ATOM 1616 O O . ASP A 1 201 ? 28.333 20.711 23.140 1.00 35.64 ? 219 ASP A O 1 ATOM 1617 C CB . ASP A 1 201 ? 27.530 19.513 25.616 1.00 38.19 ? 219 ASP A CB 1 ATOM 1618 C CG . ASP A 1 201 ? 27.445 18.449 26.672 1.00 40.03 ? 219 ASP A CG 1 ATOM 1619 O OD1 . ASP A 1 201 ? 26.343 18.173 27.185 1.00 38.50 ? 219 ASP A OD1 1 ATOM 1620 O OD2 . ASP A 1 201 ? 28.513 17.861 26.956 1.00 44.89 ? 219 ASP A OD2 1 ATOM 1621 N N . ASP A 1 202 ? 26.303 20.259 22.348 1.00 33.82 ? 220 ASP A N 1 ATOM 1622 C CA . ASP A 1 202 ? 26.383 21.173 21.220 1.00 32.59 ? 220 ASP A CA 1 ATOM 1623 C C . ASP A 1 202 ? 26.632 22.579 21.741 1.00 32.43 ? 220 ASP A C 1 ATOM 1624 O O . ASP A 1 202 ? 26.096 23.000 22.793 1.00 32.81 ? 220 ASP A O 1 ATOM 1625 C CB . ASP A 1 202 ? 25.071 21.094 20.425 1.00 32.72 ? 220 ASP A CB 1 ATOM 1626 C CG . ASP A 1 202 ? 25.131 21.735 19.072 1.00 30.15 ? 220 ASP A CG 1 ATOM 1627 O OD1 . ASP A 1 202 ? 26.167 22.306 18.642 1.00 29.09 ? 220 ASP A OD1 1 ATOM 1628 O OD2 . ASP A 1 202 ? 24.070 21.618 18.402 1.00 29.23 ? 220 ASP A OD2 1 ATOM 1629 N N . SER A 1 203 ? 27.476 23.277 21.012 1.00 31.58 ? 221 SER A N 1 ATOM 1630 C CA . SER A 1 203 ? 27.808 24.676 21.290 1.00 31.07 ? 221 SER A CA 1 ATOM 1631 C C . SER A 1 203 ? 27.838 25.494 20.011 1.00 30.56 ? 221 SER A C 1 ATOM 1632 O O . SER A 1 203 ? 28.556 25.147 19.067 1.00 31.05 ? 221 SER A O 1 ATOM 1633 C CB . SER A 1 203 ? 29.188 24.743 21.970 1.00 30.65 ? 221 SER A CB 1 ATOM 1634 O OG . SER A 1 203 ? 29.647 26.069 22.086 1.00 31.41 ? 221 SER A OG 1 ATOM 1635 N N . GLN A 1 204 ? 27.088 26.602 19.987 1.00 29.72 ? 222 GLN A N 1 ATOM 1636 C CA . GLN A 1 204 ? 27.090 27.493 18.807 1.00 28.57 ? 222 GLN A CA 1 ATOM 1637 C C . GLN A 1 204 ? 27.105 28.962 19.166 1.00 28.06 ? 222 GLN A C 1 ATOM 1638 O O . GLN A 1 204 ? 26.315 29.440 19.944 1.00 26.76 ? 222 GLN A O 1 ATOM 1639 C CB . GLN A 1 204 ? 25.901 27.178 17.841 1.00 28.87 ? 222 GLN A CB 1 ATOM 1640 C CG . GLN A 1 204 ? 25.975 27.895 16.465 1.00 26.51 ? 222 GLN A CG 1 ATOM 1641 C CD . GLN A 1 204 ? 27.212 27.409 15.660 1.00 27.39 ? 222 GLN A CD 1 ATOM 1642 O OE1 . GLN A 1 204 ? 27.416 26.190 15.503 1.00 28.91 ? 222 GLN A OE1 1 ATOM 1643 N NE2 . GLN A 1 204 ? 28.042 28.348 15.203 1.00 26.08 ? 222 GLN A NE2 1 ATOM 1644 N N . TYR A 1 205 ? 28.049 29.668 18.584 1.00 27.33 ? 223 TYR A N 1 ATOM 1645 C CA . TYR A 1 205 ? 28.131 31.124 18.697 1.00 26.91 ? 223 TYR A CA 1 ATOM 1646 C C . TYR A 1 205 ? 27.952 31.752 17.358 1.00 26.56 ? 223 TYR A C 1 ATOM 1647 O O . TYR A 1 205 ? 28.381 31.235 16.341 1.00 25.21 ? 223 TYR A O 1 ATOM 1648 C CB . TYR A 1 205 ? 29.515 31.592 19.154 1.00 27.00 ? 223 TYR A CB 1 ATOM 1649 C CG . TYR A 1 205 ? 30.027 31.075 20.475 1.00 28.90 ? 223 TYR A CG 1 ATOM 1650 C CD1 . TYR A 1 205 ? 29.246 30.270 21.306 1.00 28.32 ? 223 TYR A CD1 1 ATOM 1651 C CD2 . TYR A 1 205 ? 31.300 31.420 20.904 1.00 32.14 ? 223 TYR A CD2 1 ATOM 1652 C CE1 . TYR A 1 205 ? 29.727 29.801 22.514 1.00 31.52 ? 223 TYR A CE1 1 ATOM 1653 C CE2 . TYR A 1 205 ? 31.797 30.954 22.140 1.00 30.99 ? 223 TYR A CE2 1 ATOM 1654 C CZ . TYR A 1 205 ? 31.018 30.176 22.920 1.00 31.66 ? 223 TYR A CZ 1 ATOM 1655 O OH . TYR A 1 205 ? 31.502 29.701 24.113 1.00 33.71 ? 223 TYR A OH 1 ATOM 1656 N N . TYR A 1 206 ? 27.332 32.908 17.382 1.00 26.44 ? 224 TYR A N 1 ATOM 1657 C CA . TYR A 1 206 ? 27.443 33.886 16.282 1.00 27.19 ? 224 TYR A CA 1 ATOM 1658 C C . TYR A 1 206 ? 28.163 35.122 16.823 1.00 26.96 ? 224 TYR A C 1 ATOM 1659 O O . TYR A 1 206 ? 28.019 35.493 18.004 1.00 27.21 ? 224 TYR A O 1 ATOM 1660 C CB . TYR A 1 206 ? 26.075 34.317 15.693 1.00 26.36 ? 224 TYR A CB 1 ATOM 1661 C CG . TYR A 1 206 ? 25.209 33.233 15.091 1.00 27.63 ? 224 TYR A CG 1 ATOM 1662 C CD1 . TYR A 1 206 ? 25.753 32.027 14.635 1.00 25.47 ? 224 TYR A CD1 1 ATOM 1663 C CD2 . TYR A 1 206 ? 23.840 33.425 14.941 1.00 26.86 ? 224 TYR A CD2 1 ATOM 1664 C CE1 . TYR A 1 206 ? 24.957 31.065 14.093 1.00 28.65 ? 224 TYR A CE1 1 ATOM 1665 C CE2 . TYR A 1 206 ? 23.045 32.467 14.389 1.00 24.47 ? 224 TYR A CE2 1 ATOM 1666 C CZ . TYR A 1 206 ? 23.583 31.285 13.963 1.00 26.90 ? 224 TYR A CZ 1 ATOM 1667 O OH . TYR A 1 206 ? 22.745 30.300 13.452 1.00 25.63 ? 224 TYR A OH 1 ATOM 1668 N N . PHE A 1 207 ? 28.902 35.766 15.936 1.00 27.26 ? 225 PHE A N 1 ATOM 1669 C CA . PHE A 1 207 ? 29.761 36.915 16.270 1.00 28.10 ? 225 PHE A CA 1 ATOM 1670 C C . PHE A 1 207 ? 29.683 37.990 15.216 1.00 28.19 ? 225 PHE A C 1 ATOM 1671 O O . PHE A 1 207 ? 29.955 37.734 14.058 1.00 28.15 ? 225 PHE A O 1 ATOM 1672 C CB . PHE A 1 207 ? 31.203 36.414 16.420 1.00 28.20 ? 225 PHE A CB 1 ATOM 1673 C CG . PHE A 1 207 ? 32.216 37.496 16.664 1.00 29.23 ? 225 PHE A CG 1 ATOM 1674 C CD1 . PHE A 1 207 ? 32.109 38.341 17.770 1.00 28.75 ? 225 PHE A CD1 1 ATOM 1675 C CD2 . PHE A 1 207 ? 33.321 37.618 15.835 1.00 32.01 ? 225 PHE A CD2 1 ATOM 1676 C CE1 . PHE A 1 207 ? 33.047 39.322 18.007 1.00 28.59 ? 225 PHE A CE1 1 ATOM 1677 C CE2 . PHE A 1 207 ? 34.305 38.589 16.076 1.00 29.56 ? 225 PHE A CE2 1 ATOM 1678 C CZ . PHE A 1 207 ? 34.151 39.457 17.149 1.00 32.10 ? 225 PHE A CZ 1 ATOM 1679 N N . ASN A 1 208 ? 29.230 39.174 15.616 1.00 28.48 ? 226 ASN A N 1 ATOM 1680 C CA . ASN A 1 208 ? 29.240 40.354 14.748 1.00 28.88 ? 226 ASN A CA 1 ATOM 1681 C C . ASN A 1 208 ? 30.648 40.944 14.763 1.00 29.27 ? 226 ASN A C 1 ATOM 1682 O O . ASN A 1 208 ? 31.116 41.472 15.763 1.00 28.31 ? 226 ASN A O 1 ATOM 1683 C CB . ASN A 1 208 ? 28.187 41.392 15.173 1.00 28.52 ? 226 ASN A CB 1 ATOM 1684 C CG . ASN A 1 208 ? 28.097 42.548 14.232 1.00 29.94 ? 226 ASN A CG 1 ATOM 1685 O OD1 . ASN A 1 208 ? 29.126 43.013 13.685 1.00 29.54 ? 226 ASN A OD1 1 ATOM 1686 N ND2 . ASN A 1 208 ? 26.849 43.039 14.000 1.00 29.27 ? 226 ASN A ND2 1 ATOM 1687 N N . LYS A 1 209 ? 31.309 40.834 13.623 1.00 30.44 ? 227 LYS A N 1 ATOM 1688 C CA . LYS A 1 209 ? 32.730 41.132 13.506 1.00 31.97 ? 227 LYS A CA 1 ATOM 1689 C C . LYS A 1 209 ? 33.018 42.591 13.771 1.00 31.70 ? 227 LYS A C 1 ATOM 1690 O O . LYS A 1 209 ? 34.140 42.961 14.091 1.00 32.29 ? 227 LYS A O 1 ATOM 1691 C CB . LYS A 1 209 ? 33.300 40.679 12.140 1.00 33.17 ? 227 LYS A CB 1 ATOM 1692 C CG . LYS A 1 209 ? 33.377 39.155 12.007 1.00 36.60 ? 227 LYS A CG 1 ATOM 1693 C CD . LYS A 1 209 ? 33.540 38.619 10.554 1.00 42.42 ? 227 LYS A CD 1 ATOM 1694 C CE . LYS A 1 209 ? 34.876 38.968 9.923 1.00 45.83 ? 227 LYS A CE 1 ATOM 1695 N NZ . LYS A 1 209 ? 35.851 39.158 11.044 1.00 51.28 ? 227 LYS A NZ 1 ATOM 1696 N N . ASP A 1 210 ? 32.009 43.427 13.658 1.00 31.16 ? 228 ASP A N 1 ATOM 1697 C CA . ASP A 1 210 ? 32.213 44.851 13.793 1.00 30.36 ? 228 ASP A CA 1 ATOM 1698 C C . ASP A 1 210 ? 31.590 45.440 15.061 1.00 30.41 ? 228 ASP A C 1 ATOM 1699 O O . ASP A 1 210 ? 32.165 46.364 15.629 1.00 29.64 ? 228 ASP A O 1 ATOM 1700 C CB . ASP A 1 210 ? 31.688 45.559 12.572 1.00 31.74 ? 228 ASP A CB 1 ATOM 1701 C CG . ASP A 1 210 ? 32.496 45.204 11.330 1.00 34.94 ? 228 ASP A CG 1 ATOM 1702 O OD1 . ASP A 1 210 ? 31.984 44.406 10.540 1.00 35.64 ? 228 ASP A OD1 1 ATOM 1703 O OD2 . ASP A 1 210 ? 33.668 45.677 11.207 1.00 36.65 ? 228 ASP A OD2 1 ATOM 1704 N N . THR A 1 211 ? 30.455 44.915 15.525 1.00 28.35 ? 229 THR A N 1 ATOM 1705 C CA . THR A 1 211 ? 29.929 45.410 16.793 1.00 27.73 ? 229 THR A CA 1 ATOM 1706 C C . THR A 1 211 ? 30.602 44.675 17.957 1.00 27.47 ? 229 THR A C 1 ATOM 1707 O O . THR A 1 211 ? 30.587 45.104 19.108 1.00 27.84 ? 229 THR A O 1 ATOM 1708 C CB . THR A 1 211 ? 28.419 45.210 16.943 1.00 26.90 ? 229 THR A CB 1 ATOM 1709 O OG1 . THR A 1 211 ? 28.127 43.836 16.904 1.00 26.52 ? 229 THR A OG1 1 ATOM 1710 C CG2 . THR A 1 211 ? 27.598 45.985 15.879 1.00 25.61 ? 229 THR A CG2 1 ATOM 1711 N N . GLY A 1 212 ? 31.185 43.535 17.647 1.00 27.25 ? 230 GLY A N 1 ATOM 1712 C CA . GLY A 1 212 ? 31.894 42.766 18.645 1.00 26.81 ? 230 GLY A CA 1 ATOM 1713 C C . GLY A 1 212 ? 30.986 41.944 19.557 1.00 26.67 ? 230 GLY A C 1 ATOM 1714 O O . GLY A 1 212 ? 31.437 41.303 20.500 1.00 26.65 ? 230 GLY A O 1 ATOM 1715 N N . VAL A 1 213 ? 29.699 41.907 19.244 1.00 27.25 ? 231 VAL A N 1 ATOM 1716 C CA . VAL A 1 213 ? 28.735 41.141 20.054 1.00 25.51 ? 231 VAL A CA 1 ATOM 1717 C C . VAL A 1 213 ? 28.790 39.660 19.725 1.00 26.99 ? 231 VAL A C 1 ATOM 1718 O O . VAL A 1 213 ? 28.811 39.255 18.563 1.00 27.75 ? 231 VAL A O 1 ATOM 1719 C CB . VAL A 1 213 ? 27.303 41.640 19.892 1.00 26.64 ? 231 VAL A CB 1 ATOM 1720 C CG1 . VAL A 1 213 ? 26.322 40.707 20.647 1.00 23.09 ? 231 VAL A CG1 1 ATOM 1721 C CG2 . VAL A 1 213 ? 27.160 43.175 20.287 1.00 24.53 ? 231 VAL A CG2 1 ATOM 1722 N N . ILE A 1 214 ? 28.896 38.862 20.785 1.00 27.58 ? 232 ILE A N 1 ATOM 1723 C CA . ILE A 1 214 ? 28.835 37.391 20.730 1.00 26.28 ? 232 ILE A CA 1 ATOM 1724 C C . ILE A 1 214 ? 27.487 36.970 21.271 1.00 26.13 ? 232 ILE A C 1 ATOM 1725 O O . ILE A 1 214 ? 27.059 37.388 22.331 1.00 26.35 ? 232 ILE A O 1 ATOM 1726 C CB . ILE A 1 214 ? 29.902 36.710 21.592 1.00 26.16 ? 232 ILE A CB 1 ATOM 1727 C CG1 . ILE A 1 214 ? 31.317 36.884 21.019 1.00 27.18 ? 232 ILE A CG1 1 ATOM 1728 C CG2 . ILE A 1 214 ? 29.661 35.203 21.708 1.00 23.51 ? 232 ILE A CG2 1 ATOM 1729 C CD1 . ILE A 1 214 ? 32.091 37.999 21.583 1.00 26.81 ? 232 ILE A CD1 1 ATOM 1730 N N . TYR A 1 215 ? 26.798 36.195 20.466 1.00 25.46 ? 233 TYR A N 1 ATOM 1731 C CA . TYR A 1 215 ? 25.548 35.561 20.835 1.00 25.50 ? 233 TYR A CA 1 ATOM 1732 C C . TYR A 1 215 ? 25.814 34.062 20.847 1.00 25.36 ? 233 TYR A C 1 ATOM 1733 O O . TYR A 1 215 ? 26.078 33.480 19.811 1.00 26.20 ? 233 TYR A O 1 ATOM 1734 C CB . TYR A 1 215 ? 24.428 35.849 19.802 1.00 24.91 ? 233 TYR A CB 1 ATOM 1735 C CG . TYR A 1 215 ? 24.264 37.289 19.354 1.00 25.45 ? 233 TYR A CG 1 ATOM 1736 C CD1 . TYR A 1 215 ? 23.298 38.129 19.928 1.00 24.32 ? 233 TYR A CD1 1 ATOM 1737 C CD2 . TYR A 1 215 ? 25.038 37.799 18.367 1.00 23.51 ? 233 TYR A CD2 1 ATOM 1738 C CE1 . TYR A 1 215 ? 23.170 39.465 19.497 1.00 25.54 ? 233 TYR A CE1 1 ATOM 1739 C CE2 . TYR A 1 215 ? 24.925 39.095 17.949 1.00 25.25 ? 233 TYR A CE2 1 ATOM 1740 C CZ . TYR A 1 215 ? 23.976 39.930 18.513 1.00 23.71 ? 233 TYR A CZ 1 ATOM 1741 O OH . TYR A 1 215 ? 23.893 41.227 18.032 1.00 26.93 ? 233 TYR A OH 1 ATOM 1742 N N . GLY A 1 216 ? 25.705 33.416 21.993 1.00 25.89 ? 234 GLY A N 1 ATOM 1743 C CA . GLY A 1 216 ? 25.953 31.967 22.010 1.00 26.42 ? 234 GLY A CA 1 ATOM 1744 C C . GLY A 1 216 ? 24.973 31.167 22.798 1.00 26.53 ? 234 GLY A C 1 ATOM 1745 O O . GLY A 1 216 ? 24.247 31.704 23.646 1.00 26.62 ? 234 GLY A O 1 ATOM 1746 N N . LEU A 1 217 ? 24.919 29.887 22.433 1.00 26.70 ? 235 LEU A N 1 ATOM 1747 C CA . LEU A 1 217 ? 24.163 28.861 23.106 1.00 27.54 ? 235 LEU A CA 1 ATOM 1748 C C . LEU A 1 217 ? 24.988 27.610 23.284 1.00 27.40 ? 235 LEU A C 1 ATOM 1749 O O . LEU A 1 217 ? 25.557 27.081 22.294 1.00 28.17 ? 235 LEU A O 1 ATOM 1750 C CB . LEU A 1 217 ? 22.928 28.434 22.300 1.00 28.36 ? 235 LEU A CB 1 ATOM 1751 C CG . LEU A 1 217 ? 21.677 29.263 22.271 1.00 31.01 ? 235 LEU A CG 1 ATOM 1752 C CD1 . LEU A 1 217 ? 20.587 28.468 21.472 1.00 29.92 ? 235 LEU A CD1 1 ATOM 1753 C CD2 . LEU A 1 217 ? 21.211 29.599 23.730 1.00 35.05 ? 235 LEU A CD2 1 ATOM 1754 N N . ASN A 1 218 ? 25.019 27.125 24.520 1.00 27.11 ? 236 ASN A N 1 ATOM 1755 C CA . ASN A 1 218 ? 25.624 25.840 24.853 1.00 27.11 ? 236 ASN A CA 1 ATOM 1756 C C . ASN A 1 218 ? 24.608 24.929 25.457 1.00 29.16 ? 236 ASN A C 1 ATOM 1757 O O . ASN A 1 218 ? 23.792 25.350 26.249 1.00 28.34 ? 236 ASN A O 1 ATOM 1758 C CB . ASN A 1 218 ? 26.736 25.989 25.870 1.00 28.07 ? 236 ASN A CB 1 ATOM 1759 C CG . ASN A 1 218 ? 28.063 26.281 25.244 1.00 28.04 ? 236 ASN A CG 1 ATOM 1760 O OD1 . ASN A 1 218 ? 28.140 26.723 24.105 1.00 26.31 ? 236 ASN A OD1 1 ATOM 1761 N ND2 . ASN A 1 218 ? 29.137 26.023 25.993 1.00 32.44 ? 236 ASN A ND2 1 ATOM 1762 N N . SER A 1 219 ? 24.684 23.656 25.096 1.00 29.07 ? 237 SER A N 1 ATOM 1763 C CA . SER A 1 219 ? 23.762 22.635 25.613 1.00 30.03 ? 237 SER A CA 1 ATOM 1764 C C . SER A 1 219 ? 23.951 22.445 27.101 1.00 31.07 ? 237 SER A C 1 ATOM 1765 O O . SER A 1 219 ? 25.062 22.412 27.575 1.00 31.69 ? 237 SER A O 1 ATOM 1766 C CB . SER A 1 219 ? 24.023 21.291 24.928 1.00 29.60 ? 237 SER A CB 1 ATOM 1767 O OG . SER A 1 219 ? 23.122 20.294 25.402 1.00 32.37 ? 237 SER A OG 1 ATOM 1768 N N . THR A 1 220 ? 22.869 22.314 27.845 1.00 32.61 ? 238 THR A N 1 ATOM 1769 C CA . THR A 1 220 ? 22.968 22.154 29.295 1.00 34.22 ? 238 THR A CA 1 ATOM 1770 C C . THR A 1 220 ? 22.130 20.958 29.818 1.00 35.79 ? 238 THR A C 1 ATOM 1771 O O . THR A 1 220 ? 22.298 20.475 30.941 1.00 36.41 ? 238 THR A O 1 ATOM 1772 C CB . THR A 1 220 ? 22.530 23.469 30.035 1.00 34.20 ? 238 THR A CB 1 ATOM 1773 O OG1 . THR A 1 220 ? 21.144 23.718 29.778 1.00 34.42 ? 238 THR A OG1 1 ATOM 1774 C CG2 . THR A 1 220 ? 23.356 24.661 29.620 1.00 32.79 ? 238 THR A CG2 1 ATOM 1775 N N . GLU A 1 221 ? 21.203 20.506 29.004 1.00 37.48 ? 239 GLU A N 1 ATOM 1776 C CA . GLU A 1 221 ? 20.382 19.327 29.325 1.00 38.87 ? 239 GLU A CA 1 ATOM 1777 C C . GLU A 1 221 ? 21.213 18.084 29.548 1.00 39.54 ? 239 GLU A C 1 ATOM 1778 O O . GLU A 1 221 ? 22.247 17.894 28.906 1.00 40.06 ? 239 GLU A O 1 ATOM 1779 C CB . GLU A 1 221 ? 19.393 19.027 28.220 1.00 38.77 ? 239 GLU A CB 1 ATOM 1780 C CG . GLU A 1 221 ? 18.110 19.711 28.405 1.00 42.91 ? 239 GLU A CG 1 ATOM 1781 C CD . GLU A 1 221 ? 17.250 19.003 29.397 1.00 49.66 ? 239 GLU A CD 1 ATOM 1782 O OE1 . GLU A 1 221 ? 17.776 18.188 30.214 1.00 54.04 ? 239 GLU A OE1 1 ATOM 1783 O OE2 . GLU A 1 221 ? 16.027 19.252 29.353 1.00 53.11 ? 239 GLU A OE2 1 ATOM 1784 N N . THR A 1 222 ? 20.722 17.256 30.471 1.00 40.58 ? 240 THR A N 1 ATOM 1785 C CA . THR A 1 222 ? 21.381 16.017 30.872 1.00 41.94 ? 240 THR A CA 1 ATOM 1786 C C . THR A 1 222 ? 20.680 14.798 30.269 1.00 42.53 ? 240 THR A C 1 ATOM 1787 O O . THR A 1 222 ? 21.267 13.747 30.130 1.00 43.52 ? 240 THR A O 1 ATOM 1788 C CB . THR A 1 222 ? 21.442 15.837 32.416 1.00 42.01 ? 240 THR A CB 1 ATOM 1789 O OG1 . THR A 1 222 ? 20.124 15.951 32.984 1.00 43.01 ? 240 THR A OG1 1 ATOM 1790 C CG2 . THR A 1 222 ? 22.407 16.863 33.051 1.00 41.37 ? 240 THR A CG2 1 ATOM 1791 N N . ILE A 1 223 ? 19.434 14.954 29.870 1.00 42.74 ? 241 ILE A N 1 ATOM 1792 C CA . ILE A 1 223 ? 18.716 13.821 29.257 1.00 42.61 ? 241 ILE A CA 1 ATOM 1793 C C . ILE A 1 223 ? 19.406 13.337 27.980 1.00 43.02 ? 241 ILE A C 1 ATOM 1794 O O . ILE A 1 223 ? 20.008 14.111 27.224 1.00 43.36 ? 241 ILE A O 1 ATOM 1795 C CB . ILE A 1 223 ? 17.216 14.134 28.974 1.00 42.82 ? 241 ILE A CB 1 ATOM 1796 C CG1 . ILE A 1 223 ? 17.082 15.232 27.879 1.00 42.47 ? 241 ILE A CG1 1 ATOM 1797 C CG2 . ILE A 1 223 ? 16.497 14.446 30.315 1.00 40.45 ? 241 ILE A CG2 1 ATOM 1798 C CD1 . ILE A 1 223 ? 15.624 15.585 27.492 1.00 42.88 ? 241 ILE A CD1 1 ATOM 1799 N N . THR A 1 224 ? 19.312 12.036 27.761 1.00 43.46 ? 242 THR A N 1 ATOM 1800 C CA . THR A 1 224 ? 20.017 11.360 26.661 1.00 43.50 ? 242 THR A CA 1 ATOM 1801 C C . THR A 1 224 ? 19.047 10.987 25.574 1.00 43.53 ? 242 THR A C 1 ATOM 1802 O O . THR A 1 224 ? 19.423 10.475 24.518 1.00 44.22 ? 242 THR A O 1 ATOM 1803 C CB . THR A 1 224 ? 20.675 10.040 27.167 1.00 44.36 ? 242 THR A CB 1 ATOM 1804 O OG1 . THR A 1 224 ? 19.655 9.213 27.746 1.00 44.16 ? 242 THR A OG1 1 ATOM 1805 C CG2 . THR A 1 224 ? 21.735 10.335 28.251 1.00 41.82 ? 242 THR A CG2 1 ATOM 1806 N N . THR A 1 225 ? 17.784 11.258 25.839 1.00 43.00 ? 243 THR A N 1 ATOM 1807 C CA . THR A 1 225 ? 16.759 11.049 24.837 1.00 43.07 ? 243 THR A CA 1 ATOM 1808 C C . THR A 1 225 ? 15.576 11.984 25.078 1.00 42.33 ? 243 THR A C 1 ATOM 1809 O O . THR A 1 225 ? 15.454 12.608 26.141 1.00 42.84 ? 243 THR A O 1 ATOM 1810 C CB . THR A 1 225 ? 16.286 9.533 24.798 1.00 44.15 ? 243 THR A CB 1 ATOM 1811 O OG1 . THR A 1 225 ? 15.513 9.305 23.606 1.00 47.24 ? 243 THR A OG1 1 ATOM 1812 C CG2 . THR A 1 225 ? 15.441 9.160 26.039 1.00 42.35 ? 243 THR A CG2 1 ATOM 1813 N N . GLY A 1 226 ? 14.724 12.108 24.065 1.00 41.75 ? 244 GLY A N 1 ATOM 1814 C CA . GLY A 1 226 ? 13.528 12.953 24.155 1.00 41.12 ? 244 GLY A CA 1 ATOM 1815 C C . GLY A 1 226 ? 13.885 14.443 24.088 1.00 40.81 ? 244 GLY A C 1 ATOM 1816 O O . GLY A 1 226 ? 13.104 15.335 24.477 1.00 41.08 ? 244 GLY A O 1 ATOM 1817 N N . PHE A 1 227 ? 15.097 14.706 23.620 1.00 39.72 ? 245 PHE A N 1 ATOM 1818 C CA . PHE A 1 227 ? 15.556 16.099 23.428 1.00 38.43 ? 245 PHE A CA 1 ATOM 1819 C C . PHE A 1 227 ? 15.606 16.458 21.959 1.00 37.64 ? 245 PHE A C 1 ATOM 1820 O O . PHE A 1 227 ? 15.438 15.598 21.097 1.00 37.81 ? 245 PHE A O 1 ATOM 1821 C CB . PHE A 1 227 ? 16.918 16.349 24.078 1.00 38.48 ? 245 PHE A CB 1 ATOM 1822 C CG . PHE A 1 227 ? 18.055 15.699 23.390 1.00 37.11 ? 245 PHE A CG 1 ATOM 1823 C CD1 . PHE A 1 227 ? 18.692 16.319 22.344 1.00 35.86 ? 245 PHE A CD1 1 ATOM 1824 C CD2 . PHE A 1 227 ? 18.514 14.476 23.821 1.00 39.96 ? 245 PHE A CD2 1 ATOM 1825 C CE1 . PHE A 1 227 ? 19.766 15.746 21.732 1.00 39.68 ? 245 PHE A CE1 1 ATOM 1826 C CE2 . PHE A 1 227 ? 19.604 13.873 23.214 1.00 38.67 ? 245 PHE A CE2 1 ATOM 1827 C CZ . PHE A 1 227 ? 20.228 14.496 22.169 1.00 41.28 ? 245 PHE A CZ 1 ATOM 1828 N N . ASP A 1 228 ? 15.826 17.735 21.664 1.00 36.33 ? 246 ASP A N 1 ATOM 1829 C CA . ASP A 1 228 ? 15.777 18.173 20.250 1.00 35.33 ? 246 ASP A CA 1 ATOM 1830 C C . ASP A 1 228 ? 16.532 19.479 20.032 1.00 33.08 ? 246 ASP A C 1 ATOM 1831 O O . ASP A 1 228 ? 17.305 19.920 20.862 1.00 32.40 ? 246 ASP A O 1 ATOM 1832 C CB . ASP A 1 228 ? 14.327 18.303 19.764 1.00 35.28 ? 246 ASP A CB 1 ATOM 1833 C CG . ASP A 1 228 ? 14.109 17.847 18.292 1.00 38.04 ? 246 ASP A CG 1 ATOM 1834 O OD1 . ASP A 1 228 ? 14.662 18.396 17.351 1.00 38.08 ? 246 ASP A OD1 1 ATOM 1835 O OD2 . ASP A 1 228 ? 13.274 16.952 18.057 1.00 44.50 ? 246 ASP A OD2 1 ATOM 1836 N N . PHE A 1 229 ? 16.259 20.056 18.884 1.00 31.98 ? 247 PHE A N 1 ATOM 1837 C CA . PHE A 1 229 ? 16.977 21.229 18.358 1.00 31.32 ? 247 PHE A CA 1 ATOM 1838 C C . PHE A 1 229 ? 16.294 22.488 18.861 1.00 30.59 ? 247 PHE A C 1 ATOM 1839 O O . PHE A 1 229 ? 15.256 22.893 18.333 1.00 29.23 ? 247 PHE A O 1 ATOM 1840 C CB . PHE A 1 229 ? 16.968 21.195 16.829 1.00 31.21 ? 247 PHE A CB 1 ATOM 1841 C CG . PHE A 1 229 ? 18.107 21.919 16.159 1.00 29.60 ? 247 PHE A CG 1 ATOM 1842 C CD1 . PHE A 1 229 ? 19.421 21.678 16.495 1.00 31.39 ? 247 PHE A CD1 1 ATOM 1843 C CD2 . PHE A 1 229 ? 17.849 22.768 15.109 1.00 26.64 ? 247 PHE A CD2 1 ATOM 1844 C CE1 . PHE A 1 229 ? 20.434 22.319 15.812 1.00 31.72 ? 247 PHE A CE1 1 ATOM 1845 C CE2 . PHE A 1 229 ? 18.841 23.386 14.427 1.00 29.35 ? 247 PHE A CE2 1 ATOM 1846 C CZ . PHE A 1 229 ? 20.133 23.187 14.772 1.00 30.07 ? 247 PHE A CZ 1 ATOM 1847 N N . ASN A 1 230 ? 16.882 23.094 19.891 1.00 29.57 ? 248 ASN A N 1 ATOM 1848 C CA . ASN A 1 230 ? 16.306 24.327 20.508 1.00 29.17 ? 248 ASN A CA 1 ATOM 1849 C C . ASN A 1 230 ? 16.813 25.509 19.739 1.00 27.88 ? 248 ASN A C 1 ATOM 1850 O O . ASN A 1 230 ? 18.018 25.645 19.578 1.00 27.79 ? 248 ASN A O 1 ATOM 1851 C CB . ASN A 1 230 ? 16.746 24.576 21.955 1.00 29.65 ? 248 ASN A CB 1 ATOM 1852 C CG . ASN A 1 230 ? 16.393 23.454 22.938 1.00 32.38 ? 248 ASN A CG 1 ATOM 1853 O OD1 . ASN A 1 230 ? 16.363 23.727 24.136 1.00 33.29 ? 248 ASN A OD1 1 ATOM 1854 N ND2 . ASN A 1 230 ? 16.178 22.216 22.468 1.00 31.68 ? 248 ASN A ND2 1 ATOM 1855 N N . CYS A 1 231 ? 15.894 26.393 19.330 1.00 27.26 ? 249 CYS A N 1 ATOM 1856 C CA . CYS A 1 231 ? 16.239 27.618 18.645 1.00 26.19 ? 249 CYS A CA 1 ATOM 1857 C C . CYS A 1 231 ? 15.829 28.866 19.406 1.00 26.46 ? 249 CYS A C 1 ATOM 1858 O O . CYS A 1 231 ? 14.787 28.924 20.077 1.00 26.57 ? 249 CYS A O 1 ATOM 1859 C CB . CYS A 1 231 ? 15.609 27.684 17.256 1.00 26.96 ? 249 CYS A CB 1 ATOM 1860 S SG . CYS A 1 231 ? 16.156 26.377 16.140 1.00 26.41 ? 249 CYS A SG 1 ATOM 1861 N N . HIS A 1 232 ? 16.703 29.845 19.261 1.00 25.39 ? 250 HIS A N 1 ATOM 1862 C CA . HIS A 1 232 ? 16.481 31.244 19.640 1.00 26.33 ? 250 HIS A CA 1 ATOM 1863 C C . HIS A 1 232 ? 16.496 32.057 18.386 1.00 24.94 ? 250 HIS A C 1 ATOM 1864 O O . HIS A 1 232 ? 17.164 31.688 17.401 1.00 24.39 ? 250 HIS A O 1 ATOM 1865 C CB . HIS A 1 232 ? 17.593 31.755 20.536 1.00 26.61 ? 250 HIS A CB 1 ATOM 1866 C CG . HIS A 1 232 ? 17.542 31.207 21.922 1.00 29.25 ? 250 HIS A CG 1 ATOM 1867 N ND1 . HIS A 1 232 ? 18.201 31.801 22.973 1.00 28.23 ? 250 HIS A ND1 1 ATOM 1868 C CD2 . HIS A 1 232 ? 16.881 30.143 22.438 1.00 34.20 ? 250 HIS A CD2 1 ATOM 1869 C CE1 . HIS A 1 232 ? 17.973 31.098 24.073 1.00 31.62 ? 250 HIS A CE1 1 ATOM 1870 N NE2 . HIS A 1 232 ? 17.192 30.078 23.773 1.00 33.20 ? 250 HIS A NE2 1 ATOM 1871 N N . TYR A 1 233 ? 15.734 33.148 18.416 1.00 24.73 ? 251 TYR A N 1 ATOM 1872 C CA . TYR A 1 233 ? 15.541 33.961 17.233 1.00 24.25 ? 251 TYR A CA 1 ATOM 1873 C C . TYR A 1 233 ? 16.081 35.325 17.506 1.00 25.00 ? 251 TYR A C 1 ATOM 1874 O O . TYR A 1 233 ? 15.501 36.113 18.254 1.00 24.97 ? 251 TYR A O 1 ATOM 1875 C CB . TYR A 1 233 ? 14.056 33.968 16.866 1.00 25.47 ? 251 TYR A CB 1 ATOM 1876 C CG . TYR A 1 233 ? 13.647 32.538 16.567 1.00 24.49 ? 251 TYR A CG 1 ATOM 1877 C CD1 . TYR A 1 233 ? 13.816 32.000 15.293 1.00 26.12 ? 251 TYR A CD1 1 ATOM 1878 C CD2 . TYR A 1 233 ? 13.188 31.707 17.572 1.00 25.88 ? 251 TYR A CD2 1 ATOM 1879 C CE1 . TYR A 1 233 ? 13.468 30.661 15.019 1.00 24.84 ? 251 TYR A CE1 1 ATOM 1880 C CE2 . TYR A 1 233 ? 12.864 30.347 17.318 1.00 23.88 ? 251 TYR A CE2 1 ATOM 1881 C CZ . TYR A 1 233 ? 13.008 29.847 16.031 1.00 22.92 ? 251 TYR A CZ 1 ATOM 1882 O OH . TYR A 1 233 ? 12.687 28.517 15.766 1.00 24.79 ? 251 TYR A OH 1 ATOM 1883 N N . LEU A 1 234 ? 17.223 35.584 16.893 1.00 24.97 ? 252 LEU A N 1 ATOM 1884 C CA . LEU A 1 234 ? 17.949 36.790 17.099 1.00 24.44 ? 252 LEU A CA 1 ATOM 1885 C C . LEU A 1 234 ? 17.467 37.832 16.116 1.00 24.77 ? 252 LEU A C 1 ATOM 1886 O O . LEU A 1 234 ? 17.227 37.572 14.938 1.00 25.43 ? 252 LEU A O 1 ATOM 1887 C CB . LEU A 1 234 ? 19.446 36.545 16.908 1.00 24.25 ? 252 LEU A CB 1 ATOM 1888 C CG . LEU A 1 234 ? 20.131 35.439 17.718 1.00 24.86 ? 252 LEU A CG 1 ATOM 1889 C CD1 . LEU A 1 234 ? 21.690 35.357 17.395 1.00 23.47 ? 252 LEU A CD1 1 ATOM 1890 C CD2 . LEU A 1 234 ? 19.832 35.659 19.227 1.00 24.84 ? 252 LEU A CD2 1 ATOM 1891 N N . VAL A 1 235 ? 17.375 39.036 16.614 1.00 24.99 ? 253 VAL A N 1 ATOM 1892 C CA . VAL A 1 235 ? 17.077 40.193 15.775 1.00 25.58 ? 253 VAL A CA 1 ATOM 1893 C C . VAL A 1 235 ? 18.348 41.030 15.646 1.00 26.09 ? 253 VAL A C 1 ATOM 1894 O O . VAL A 1 235 ? 18.763 41.680 16.576 1.00 24.84 ? 253 VAL A O 1 ATOM 1895 C CB . VAL A 1 235 ? 15.923 41.031 16.372 1.00 25.83 ? 253 VAL A CB 1 ATOM 1896 C CG1 . VAL A 1 235 ? 15.604 42.256 15.450 1.00 25.77 ? 253 VAL A CG1 1 ATOM 1897 C CG2 . VAL A 1 235 ? 14.675 40.147 16.568 1.00 25.68 ? 253 VAL A CG2 1 ATOM 1898 N N . LEU A 1 236 ? 18.965 40.974 14.464 1.00 26.65 ? 254 LEU A N 1 ATOM 1899 C CA . LEU A 1 236 ? 20.329 41.465 14.256 1.00 26.47 ? 254 LEU A CA 1 ATOM 1900 C C . LEU A 1 236 ? 20.349 42.601 13.278 1.00 26.69 ? 254 LEU A C 1 ATOM 1901 O O . LEU A 1 236 ? 19.453 42.730 12.450 1.00 26.64 ? 254 LEU A O 1 ATOM 1902 C CB . LEU A 1 236 ? 21.212 40.309 13.698 1.00 26.83 ? 254 LEU A CB 1 ATOM 1903 C CG . LEU A 1 236 ? 21.347 39.082 14.596 1.00 27.07 ? 254 LEU A CG 1 ATOM 1904 C CD1 . LEU A 1 236 ? 22.238 38.035 13.946 1.00 24.44 ? 254 LEU A CD1 1 ATOM 1905 C CD2 . LEU A 1 236 ? 21.817 39.430 16.023 1.00 27.29 ? 254 LEU A CD2 1 ATOM 1906 N N . PRO A 1 237 ? 21.389 43.450 13.355 1.00 27.10 ? 255 PRO A N 1 ATOM 1907 C CA . PRO A 1 237 ? 21.570 44.493 12.392 1.00 27.62 ? 255 PRO A CA 1 ATOM 1908 C C . PRO A 1 237 ? 22.373 43.986 11.204 1.00 27.38 ? 255 PRO A C 1 ATOM 1909 O O . PRO A 1 237 ? 22.905 42.871 11.217 1.00 28.56 ? 255 PRO A O 1 ATOM 1910 C CB . PRO A 1 237 ? 22.348 45.543 13.188 1.00 27.95 ? 255 PRO A CB 1 ATOM 1911 C CG . PRO A 1 237 ? 23.253 44.627 14.037 1.00 27.05 ? 255 PRO A CG 1 ATOM 1912 C CD . PRO A 1 237 ? 22.369 43.538 14.442 1.00 26.89 ? 255 PRO A CD 1 ATOM 1913 N N . SER A 1 238 ? 22.394 44.791 10.153 1.00 28.39 ? 256 SER A N 1 ATOM 1914 C CA . SER A 1 238 ? 23.223 44.461 8.981 1.00 28.55 ? 256 SER A CA 1 ATOM 1915 C C . SER A 1 238 ? 24.660 44.343 9.468 1.00 29.17 ? 256 SER A C 1 ATOM 1916 O O . SER A 1 238 ? 25.120 45.064 10.371 1.00 28.97 ? 256 SER A O 1 ATOM 1917 C CB . SER A 1 238 ? 23.103 45.522 7.880 1.00 28.40 ? 256 SER A CB 1 ATOM 1918 O OG . SER A 1 238 ? 21.786 45.585 7.339 1.00 28.53 ? 256 SER A OG 1 ATOM 1919 N N . GLY A 1 239 ? 25.373 43.408 8.861 1.00 29.93 ? 257 GLY A N 1 ATOM 1920 C CA . GLY A 1 239 ? 26.815 43.315 9.060 1.00 28.73 ? 257 GLY A CA 1 ATOM 1921 C C . GLY A 1 239 ? 27.357 41.956 8.665 1.00 29.05 ? 257 GLY A C 1 ATOM 1922 O O . GLY A 1 239 ? 26.658 41.112 8.061 1.00 27.95 ? 257 GLY A O 1 ATOM 1923 N N . ASN A 1 240 ? 28.612 41.766 9.049 1.00 27.69 ? 258 ASN A N 1 ATOM 1924 C CA . ASN A 1 240 ? 29.372 40.567 8.726 1.00 27.59 ? 258 ASN A CA 1 ATOM 1925 C C . ASN A 1 240 ? 29.691 39.781 9.982 1.00 26.73 ? 258 ASN A C 1 ATOM 1926 O O . ASN A 1 240 ? 30.210 40.317 10.976 1.00 25.27 ? 258 ASN A O 1 ATOM 1927 C CB . ASN A 1 240 ? 30.639 40.950 7.951 1.00 28.58 ? 258 ASN A CB 1 ATOM 1928 C CG . ASN A 1 240 ? 31.193 39.800 7.135 1.00 29.68 ? 258 ASN A CG 1 ATOM 1929 O OD1 . ASN A 1 240 ? 30.501 38.817 6.887 1.00 28.02 ? 258 ASN A OD1 1 ATOM 1930 N ND2 . ASN A 1 240 ? 32.453 39.918 6.714 1.00 31.95 ? 258 ASN A ND2 1 ATOM 1931 N N . TYR A 1 241 ? 29.271 38.520 9.942 1.00 26.31 ? 259 TYR A N 1 ATOM 1932 C CA . TYR A 1 241 ? 29.279 37.661 11.086 1.00 26.28 ? 259 TYR A CA 1 ATOM 1933 C C . TYR A 1 241 ? 30.091 36.412 10.871 1.00 26.74 ? 259 TYR A C 1 ATOM 1934 O O . TYR A 1 241 ? 30.267 35.951 9.749 1.00 26.57 ? 259 TYR A O 1 ATOM 1935 C CB . TYR A 1 241 ? 27.831 37.225 11.430 1.00 26.52 ? 259 TYR A CB 1 ATOM 1936 C CG . TYR A 1 241 ? 26.887 38.351 11.847 1.00 25.06 ? 259 TYR A CG 1 ATOM 1937 C CD1 . TYR A 1 241 ? 26.527 38.523 13.173 1.00 24.34 ? 259 TYR A CD1 1 ATOM 1938 C CD2 . TYR A 1 241 ? 26.331 39.200 10.894 1.00 27.01 ? 259 TYR A CD2 1 ATOM 1939 C CE1 . TYR A 1 241 ? 25.681 39.563 13.574 1.00 26.53 ? 259 TYR A CE1 1 ATOM 1940 C CE2 . TYR A 1 241 ? 25.469 40.223 11.261 1.00 27.06 ? 259 TYR A CE2 1 ATOM 1941 C CZ . TYR A 1 241 ? 25.131 40.400 12.623 1.00 27.13 ? 259 TYR A CZ 1 ATOM 1942 O OH . TYR A 1 241 ? 24.293 41.466 12.973 1.00 25.87 ? 259 TYR A OH 1 ATOM 1943 N N . LEU A 1 242 ? 30.547 35.856 11.981 1.00 26.85 ? 260 LEU A N 1 ATOM 1944 C CA . LEU A 1 242 ? 30.999 34.460 12.033 1.00 28.12 ? 260 LEU A CA 1 ATOM 1945 C C . LEU A 1 242 ? 30.071 33.590 12.827 1.00 28.00 ? 260 LEU A C 1 ATOM 1946 O O . LEU A 1 242 ? 29.518 33.996 13.877 1.00 27.61 ? 260 LEU A O 1 ATOM 1947 C CB . LEU A 1 242 ? 32.423 34.332 12.646 1.00 28.47 ? 260 LEU A CB 1 ATOM 1948 C CG . LEU A 1 242 ? 33.540 35.188 11.997 1.00 31.03 ? 260 LEU A CG 1 ATOM 1949 C CD1 . LEU A 1 242 ? 34.852 35.149 12.810 1.00 26.99 ? 260 LEU A CD1 1 ATOM 1950 C CD2 . LEU A 1 242 ? 33.729 34.711 10.523 1.00 30.73 ? 260 LEU A CD2 1 ATOM 1951 N N . ALA A 1 243 ? 29.860 32.402 12.290 1.00 27.72 ? 261 ALA A N 1 ATOM 1952 C CA . ALA A 1 243 ? 29.247 31.334 12.997 1.00 28.68 ? 261 ALA A CA 1 ATOM 1953 C C . ALA A 1 243 ? 30.400 30.421 13.439 1.00 29.82 ? 261 ALA A C 1 ATOM 1954 O O . ALA A 1 243 ? 31.141 29.864 12.603 1.00 30.36 ? 261 ALA A O 1 ATOM 1955 C CB . ALA A 1 243 ? 28.175 30.572 12.135 1.00 28.40 ? 261 ALA A CB 1 ATOM 1956 N N . ILE A 1 244 ? 30.561 30.338 14.758 1.00 29.96 ? 262 ILE A N 1 ATOM 1957 C CA . ILE A 1 244 ? 31.666 29.631 15.390 1.00 31.10 ? 262 ILE A CA 1 ATOM 1958 C C . ILE A 1 244 ? 31.096 28.494 16.198 1.00 31.61 ? 262 ILE A C 1 ATOM 1959 O O . ILE A 1 244 ? 30.419 28.715 17.211 1.00 30.74 ? 262 ILE A O 1 ATOM 1960 C CB . ILE A 1 244 ? 32.517 30.554 16.290 1.00 31.31 ? 262 ILE A CB 1 ATOM 1961 C CG1 . ILE A 1 244 ? 33.015 31.755 15.480 1.00 32.23 ? 262 ILE A CG1 1 ATOM 1962 C CG2 . ILE A 1 244 ? 33.699 29.770 16.916 1.00 31.59 ? 262 ILE A CG2 1 ATOM 1963 C CD1 . ILE A 1 244 ? 33.493 32.968 16.313 1.00 34.02 ? 262 ILE A CD1 1 ATOM 1964 N N . SER A 1 245 ? 31.361 27.276 15.710 1.00 30.58 ? 263 SER A N 1 ATOM 1965 C CA . SER A 1 245 ? 30.899 26.049 16.357 1.00 31.50 ? 263 SER A CA 1 ATOM 1966 C C . SER A 1 245 ? 32.021 25.542 17.247 1.00 32.30 ? 263 SER A C 1 ATOM 1967 O O . SER A 1 245 ? 33.184 25.493 16.837 1.00 31.95 ? 263 SER A O 1 ATOM 1968 C CB . SER A 1 245 ? 30.522 24.983 15.311 1.00 30.60 ? 263 SER A CB 1 ATOM 1969 O OG . SER A 1 245 ? 29.924 23.862 15.903 1.00 31.79 ? 263 SER A OG 1 ATOM 1970 N N . ASN A 1 246 ? 31.664 25.153 18.461 1.00 32.80 ? 264 ASN A N 1 ATOM 1971 C CA . ASN A 1 246 ? 32.671 24.714 19.444 1.00 34.06 ? 264 ASN A CA 1 ATOM 1972 C C . ASN A 1 246 ? 32.510 23.246 19.792 1.00 34.63 ? 264 ASN A C 1 ATOM 1973 O O . ASN A 1 246 ? 33.316 22.678 20.523 1.00 35.46 ? 264 ASN A O 1 ATOM 1974 C CB . ASN A 1 246 ? 32.586 25.524 20.748 1.00 33.35 ? 264 ASN A CB 1 ATOM 1975 C CG . ASN A 1 246 ? 32.714 26.996 20.529 1.00 33.85 ? 264 ASN A CG 1 ATOM 1976 O OD1 . ASN A 1 246 ? 33.738 27.472 20.065 1.00 33.13 ? 264 ASN A OD1 1 ATOM 1977 N ND2 . ASN A 1 246 ? 31.670 27.743 20.895 1.00 32.75 ? 264 ASN A ND2 1 ATOM 1978 N N . GLU A 1 247 ? 31.448 22.655 19.275 1.00 36.02 ? 265 GLU A N 1 ATOM 1979 C CA . GLU A 1 247 ? 31.129 21.233 19.499 1.00 36.15 ? 265 GLU A CA 1 ATOM 1980 C C . GLU A 1 247 ? 29.923 20.789 18.688 1.00 36.71 ? 265 GLU A C 1 ATOM 1981 O O . GLU A 1 247 ? 28.981 21.554 18.426 1.00 36.61 ? 265 GLU A O 1 ATOM 1982 C CB . GLU A 1 247 ? 30.878 20.959 20.981 1.00 37.08 ? 265 GLU A CB 1 ATOM 1983 C CG . GLU A 1 247 ? 30.820 19.477 21.345 1.00 38.65 ? 265 GLU A CG 1 ATOM 1984 C CD . GLU A 1 247 ? 31.112 19.206 22.808 1.00 39.00 ? 265 GLU A CD 1 ATOM 1985 O OE1 . GLU A 1 247 ? 31.941 19.957 23.380 1.00 39.64 ? 265 GLU A OE1 1 ATOM 1986 O OE2 . GLU A 1 247 ? 30.517 18.252 23.375 1.00 37.29 ? 265 GLU A OE2 1 ATOM 1987 N N . LEU A 1 248 ? 29.953 19.516 18.336 1.00 35.45 ? 266 LEU A N 1 ATOM 1988 C CA . LEU A 1 248 ? 28.981 18.899 17.430 1.00 35.13 ? 266 LEU A CA 1 ATOM 1989 C C . LEU A 1 248 ? 29.103 19.576 16.060 1.00 34.36 ? 266 LEU A C 1 ATOM 1990 O O . LEU A 1 248 ? 30.193 20.003 15.639 1.00 34.73 ? 266 LEU A O 1 ATOM 1991 C CB . LEU A 1 248 ? 27.570 18.958 18.013 1.00 34.27 ? 266 LEU A CB 1 ATOM 1992 C CG . LEU A 1 248 ? 26.611 17.821 17.643 1.00 34.93 ? 266 LEU A CG 1 ATOM 1993 C CD1 . LEU A 1 248 ? 27.279 16.455 17.806 1.00 38.23 ? 266 LEU A CD1 1 ATOM 1994 C CD2 . LEU A 1 248 ? 25.313 17.852 18.487 1.00 32.76 ? 266 LEU A CD2 1 ATOM 1995 N N . LEU A 1 249 ? 27.976 19.687 15.385 1.00 33.98 ? 267 LEU A N 1 ATOM 1996 C CA . LEU A 1 249 ? 27.947 20.247 14.038 1.00 33.69 ? 267 LEU A CA 1 ATOM 1997 C C . LEU A 1 249 ? 27.757 21.753 14.021 1.00 33.48 ? 267 LEU A C 1 ATOM 1998 O O . LEU A 1 249 ? 26.868 22.293 14.687 1.00 33.59 ? 267 LEU A O 1 ATOM 1999 C CB . LEU A 1 249 ? 26.828 19.605 13.193 1.00 34.01 ? 267 LEU A CB 1 ATOM 2000 C CG . LEU A 1 249 ? 27.140 18.202 12.617 1.00 37.47 ? 267 LEU A CG 1 ATOM 2001 C CD1 . LEU A 1 249 ? 27.242 17.174 13.737 1.00 37.25 ? 267 LEU A CD1 1 ATOM 2002 C CD2 . LEU A 1 249 ? 26.107 17.752 11.597 1.00 41.32 ? 267 LEU A CD2 1 ATOM 2003 N N . LEU A 1 250 ? 28.564 22.386 13.182 1.00 32.49 ? 268 LEU A N 1 ATOM 2004 C CA . LEU A 1 250 ? 28.435 23.775 12.862 1.00 32.20 ? 268 LEU A CA 1 ATOM 2005 C C . LEU A 1 250 ? 27.091 24.047 12.194 1.00 32.45 ? 268 LEU A C 1 ATOM 2006 O O . LEU A 1 250 ? 26.664 23.348 11.245 1.00 31.25 ? 268 LEU A O 1 ATOM 2007 C CB . LEU A 1 250 ? 29.601 24.251 11.964 1.00 31.59 ? 268 LEU A CB 1 ATOM 2008 C CG . LEU A 1 250 ? 29.509 25.624 11.268 1.00 31.46 ? 268 LEU A CG 1 ATOM 2009 C CD1 . LEU A 1 250 ? 29.489 26.791 12.219 1.00 30.63 ? 268 LEU A CD1 1 ATOM 2010 C CD2 . LEU A 1 250 ? 30.648 25.782 10.273 1.00 31.49 ? 268 LEU A CD2 1 ATOM 2011 N N . THR A 1 251 ? 26.444 25.099 12.697 1.00 31.41 ? 269 THR A N 1 ATOM 2012 C CA . THR A 1 251 ? 25.166 25.553 12.164 1.00 30.22 ? 269 THR A CA 1 ATOM 2013 C C . THR A 1 251 ? 25.229 27.041 11.835 1.00 29.72 ? 269 THR A C 1 ATOM 2014 O O . THR A 1 251 ? 25.893 27.814 12.496 1.00 30.01 ? 269 THR A O 1 ATOM 2015 C CB . THR A 1 251 ? 23.984 25.209 13.135 1.00 31.45 ? 269 THR A CB 1 ATOM 2016 O OG1 . THR A 1 251 ? 24.230 25.781 14.444 1.00 32.40 ? 269 THR A OG1 1 ATOM 2017 C CG2 . THR A 1 251 ? 23.789 23.682 13.282 1.00 28.76 ? 269 THR A CG2 1 ATOM 2018 N N . VAL A 1 252 ? 24.594 27.414 10.738 1.00 29.28 ? 270 VAL A N 1 ATOM 2019 C CA . VAL A 1 252 ? 24.707 28.754 10.202 1.00 27.78 ? 270 VAL A CA 1 ATOM 2020 C C . VAL A 1 252 ? 23.400 29.101 9.509 1.00 28.30 ? 270 VAL A C 1 ATOM 2021 O O . VAL A 1 252 ? 22.795 28.222 8.875 1.00 29.48 ? 270 VAL A O 1 ATOM 2022 C CB . VAL A 1 252 ? 25.913 28.844 9.228 1.00 28.69 ? 270 VAL A CB 1 ATOM 2023 C CG1 . VAL A 1 252 ? 25.817 27.763 8.147 1.00 28.46 ? 270 VAL A CG1 1 ATOM 2024 C CG2 . VAL A 1 252 ? 26.044 30.232 8.611 1.00 25.83 ? 270 VAL A CG2 1 ATOM 2025 N N . PRO A 1 253 ? 22.919 30.356 9.664 1.00 27.76 ? 271 PRO A N 1 ATOM 2026 C CA . PRO A 1 253 ? 21.676 30.753 8.996 1.00 28.03 ? 271 PRO A CA 1 ATOM 2027 C C . PRO A 1 253 ? 21.794 30.723 7.475 1.00 27.34 ? 271 PRO A C 1 ATOM 2028 O O . PRO A 1 253 ? 22.849 31.059 6.916 1.00 27.26 ? 271 PRO A O 1 ATOM 2029 C CB . PRO A 1 253 ? 21.466 32.204 9.459 1.00 26.88 ? 271 PRO A CB 1 ATOM 2030 C CG . PRO A 1 253 ? 22.305 32.376 10.684 1.00 28.68 ? 271 PRO A CG 1 ATOM 2031 C CD . PRO A 1 253 ? 23.481 31.465 10.461 1.00 27.80 ? 271 PRO A CD 1 ATOM 2032 N N . THR A 1 254 ? 20.675 30.365 6.843 1.00 26.71 ? 272 THR A N 1 ATOM 2033 C CA . THR A 1 254 ? 20.538 30.326 5.397 1.00 26.30 ? 272 THR A CA 1 ATOM 2034 C C . THR A 1 254 ? 19.397 31.237 4.905 1.00 26.13 ? 272 THR A C 1 ATOM 2035 O O . THR A 1 254 ? 19.370 31.628 3.759 1.00 23.96 ? 272 THR A O 1 ATOM 2036 C CB . THR A 1 254 ? 20.287 28.887 4.885 1.00 26.89 ? 272 THR A CB 1 ATOM 2037 O OG1 . THR A 1 254 ? 19.013 28.422 5.362 1.00 24.83 ? 272 THR A OG1 1 ATOM 2038 C CG2 . THR A 1 254 ? 21.420 27.900 5.356 1.00 27.59 ? 272 THR A CG2 1 ATOM 2039 N N . LYS A 1 255 ? 18.490 31.570 5.820 1.00 24.89 ? 273 LYS A N 1 ATOM 2040 C CA . LYS A 1 255 ? 17.393 32.516 5.554 1.00 25.18 ? 273 LYS A CA 1 ATOM 2041 C C . LYS A 1 255 ? 17.176 33.456 6.756 1.00 25.06 ? 273 LYS A C 1 ATOM 2042 O O . LYS A 1 255 ? 17.427 33.105 7.914 1.00 24.92 ? 273 LYS A O 1 ATOM 2043 C CB . LYS A 1 255 ? 16.065 31.787 5.245 1.00 25.19 ? 273 LYS A CB 1 ATOM 2044 C CG . LYS A 1 255 ? 16.000 31.053 3.899 1.00 25.39 ? 273 LYS A CG 1 ATOM 2045 C CD . LYS A 1 255 ? 14.742 30.117 3.810 1.00 26.25 ? 273 LYS A CD 1 ATOM 2046 C CE . LYS A 1 255 ? 14.909 28.804 4.505 1.00 25.47 ? 273 LYS A CE 1 ATOM 2047 N NZ . LYS A 1 255 ? 13.763 27.889 4.153 1.00 25.35 ? 273 LYS A NZ 1 ATOM 2048 N N . ALA A 1 256 ? 16.737 34.657 6.442 1.00 23.91 ? 274 ALA A N 1 ATOM 2049 C CA . ALA A 1 256 ? 16.337 35.588 7.471 1.00 24.34 ? 274 ALA A CA 1 ATOM 2050 C C . ALA A 1 256 ? 14.979 36.193 7.121 1.00 24.65 ? 274 ALA A C 1 ATOM 2051 O O . ALA A 1 256 ? 14.619 36.335 5.962 1.00 22.98 ? 274 ALA A O 1 ATOM 2052 C CB . ALA A 1 256 ? 17.396 36.675 7.624 1.00 22.89 ? 274 ALA A CB 1 ATOM 2053 N N . ILE A 1 257 ? 14.240 36.568 8.156 1.00 25.92 ? 275 ILE A N 1 ATOM 2054 C CA . ILE A 1 257 ? 13.144 37.513 7.958 1.00 26.01 ? 275 ILE A CA 1 ATOM 2055 C C . ILE A 1 257 ? 13.829 38.852 7.803 1.00 26.52 ? 275 ILE A C 1 ATOM 2056 O O . ILE A 1 257 ? 14.607 39.277 8.654 1.00 27.83 ? 275 ILE A O 1 ATOM 2057 C CB . ILE A 1 257 ? 12.185 37.577 9.146 1.00 25.95 ? 275 ILE A CB 1 ATOM 2058 C CG1 . ILE A 1 257 ? 11.509 36.217 9.353 1.00 26.66 ? 275 ILE A CG1 1 ATOM 2059 C CG2 . ILE A 1 257 ? 11.206 38.751 8.970 1.00 24.60 ? 275 ILE A CG2 1 ATOM 2060 C CD1 . ILE A 1 257 ? 10.516 35.825 8.194 1.00 28.18 ? 275 ILE A CD1 1 ATOM 2061 N N . CYS A 1 258 ? 13.516 39.497 6.686 1.00 26.76 ? 276 CYS A N 1 ATOM 2062 C CA . CYS A 1 258 ? 14.013 40.790 6.312 1.00 26.10 ? 276 CYS A CA 1 ATOM 2063 C C . CYS A 1 258 ? 12.984 41.864 6.700 1.00 26.04 ? 276 CYS A C 1 ATOM 2064 O O . CYS A 1 258 ? 11.851 41.929 6.149 1.00 25.73 ? 276 CYS A O 1 ATOM 2065 C CB . CYS A 1 258 ? 14.240 40.802 4.793 1.00 26.08 ? 276 CYS A CB 1 ATOM 2066 S SG . CYS A 1 258 ? 14.921 42.326 4.180 1.00 29.21 ? 276 CYS A SG 1 ATOM 2067 N N . LEU A 1 259 ? 13.393 42.693 7.653 1.00 25.11 ? 277 LEU A N 1 ATOM 2068 C CA . LEU A 1 259 ? 12.566 43.797 8.170 1.00 24.09 ? 277 LEU A CA 1 ATOM 2069 C C . LEU A 1 259 ? 13.049 45.142 7.605 1.00 25.56 ? 277 LEU A C 1 ATOM 2070 O O . LEU A 1 259 ? 14.235 45.492 7.721 1.00 25.20 ? 277 LEU A O 1 ATOM 2071 C CB . LEU A 1 259 ? 12.681 43.835 9.680 1.00 24.35 ? 277 LEU A CB 1 ATOM 2072 C CG . LEU A 1 259 ? 12.321 42.572 10.472 1.00 22.93 ? 277 LEU A CG 1 ATOM 2073 C CD1 . LEU A 1 259 ? 12.892 42.665 11.909 1.00 22.72 ? 277 LEU A CD1 1 ATOM 2074 C CD2 . LEU A 1 259 ? 10.768 42.281 10.449 1.00 25.11 ? 277 LEU A CD2 1 ATOM 2075 N N . ASN A 1 260 ? 12.135 45.891 7.008 1.00 24.94 ? 278 ASN A N 1 ATOM 2076 C CA . ASN A 1 260 ? 12.439 47.160 6.424 1.00 25.03 ? 278 ASN A CA 1 ATOM 2077 C C . ASN A 1 260 ? 11.370 48.210 6.676 1.00 26.23 ? 278 ASN A C 1 ATOM 2078 O O . ASN A 1 260 ? 10.195 47.920 6.888 1.00 24.70 ? 278 ASN A O 1 ATOM 2079 C CB . ASN A 1 260 ? 12.638 47.037 4.897 1.00 25.85 ? 278 ASN A CB 1 ATOM 2080 C CG . ASN A 1 260 ? 14.073 46.708 4.498 1.00 27.12 ? 278 ASN A CG 1 ATOM 2081 O OD1 . ASN A 1 260 ? 15.010 47.355 4.937 1.00 29.78 ? 278 ASN A OD1 1 ATOM 2082 N ND2 . ASN A 1 260 ? 14.244 45.664 3.713 1.00 26.97 ? 278 ASN A ND2 1 ATOM 2083 N N . LYS A 1 261 ? 11.833 49.443 6.624 1.00 26.18 ? 279 LYS A N 1 ATOM 2084 C CA . LYS A 1 261 ? 11.015 50.627 6.705 1.00 27.59 ? 279 LYS A CA 1 ATOM 2085 C C . LYS A 1 261 ? 10.402 50.795 8.083 1.00 27.88 ? 279 LYS A C 1 ATOM 2086 O O . LYS A 1 261 ? 9.233 50.434 8.365 1.00 26.08 ? 279 LYS A O 1 ATOM 2087 C CB . LYS A 1 261 ? 9.927 50.648 5.591 1.00 28.70 ? 279 LYS A CB 1 ATOM 2088 C CG . LYS A 1 261 ? 10.514 50.555 4.179 1.00 31.11 ? 279 LYS A CG 1 ATOM 2089 C CD . LYS A 1 261 ? 9.419 50.774 3.127 1.00 36.08 ? 279 LYS A CD 1 ATOM 2090 C CE . LYS A 1 261 ? 9.988 50.571 1.710 1.00 39.51 ? 279 LYS A CE 1 ATOM 2091 N NZ . LYS A 1 261 ? 8.976 50.874 0.682 1.00 41.77 ? 279 LYS A NZ 1 ATOM 2092 N N . ARG A 1 262 ? 11.215 51.405 8.933 1.00 27.94 ? 280 ARG A N 1 ATOM 2093 C CA . ARG A 1 262 ? 10.821 51.692 10.306 1.00 28.28 ? 280 ARG A CA 1 ATOM 2094 C C . ARG A 1 262 ? 9.536 52.569 10.276 1.00 27.50 ? 280 ARG A C 1 ATOM 2095 O O . ARG A 1 262 ? 9.384 53.427 9.448 1.00 27.47 ? 280 ARG A O 1 ATOM 2096 C CB . ARG A 1 262 ? 11.953 52.390 11.053 1.00 28.41 ? 280 ARG A CB 1 ATOM 2097 C CG . ARG A 1 262 ? 11.714 52.462 12.577 1.00 30.08 ? 280 ARG A CG 1 ATOM 2098 C CD . ARG A 1 262 ? 12.054 51.154 13.272 1.00 31.23 ? 280 ARG A CD 1 ATOM 2099 N NE . ARG A 1 262 ? 11.694 51.248 14.683 1.00 33.76 ? 280 ARG A NE 1 ATOM 2100 C CZ . ARG A 1 262 ? 12.087 50.415 15.635 1.00 36.27 ? 280 ARG A CZ 1 ATOM 2101 N NH1 . ARG A 1 262 ? 12.885 49.383 15.355 1.00 36.44 ? 280 ARG A NH1 1 ATOM 2102 N NH2 . ARG A 1 262 ? 11.688 50.626 16.879 1.00 33.17 ? 280 ARG A NH2 1 ATOM 2103 N N . LYS A 1 263 ? 8.599 52.257 11.163 1.00 27.60 ? 281 LYS A N 1 ATOM 2104 C CA . LYS A 1 263 ? 7.337 52.992 11.274 1.00 27.24 ? 281 LYS A CA 1 ATOM 2105 C C . LYS A 1 263 ? 6.983 53.311 12.714 1.00 27.45 ? 281 LYS A C 1 ATOM 2106 O O . LYS A 1 263 ? 7.442 52.669 13.659 1.00 27.78 ? 281 LYS A O 1 ATOM 2107 C CB . LYS A 1 263 ? 6.184 52.200 10.635 1.00 26.53 ? 281 LYS A CB 1 ATOM 2108 C CG . LYS A 1 263 ? 5.792 51.000 11.391 1.00 26.17 ? 281 LYS A CG 1 ATOM 2109 C CD . LYS A 1 263 ? 4.821 50.095 10.588 1.00 26.69 ? 281 LYS A CD 1 ATOM 2110 C CE . LYS A 1 263 ? 4.430 48.880 11.373 1.00 23.80 ? 281 LYS A CE 1 ATOM 2111 N NZ . LYS A 1 263 ? 3.768 47.765 10.595 1.00 22.55 ? 281 LYS A NZ 1 ATOM 2112 N N . ASP A 1 264 ? 6.106 54.278 12.867 1.00 27.44 ? 282 ASP A N 1 ATOM 2113 C CA . ASP A 1 264 ? 5.486 54.538 14.183 1.00 27.45 ? 282 ASP A CA 1 ATOM 2114 C C . ASP A 1 264 ? 4.824 53.274 14.671 1.00 27.13 ? 282 ASP A C 1 ATOM 2115 O O . ASP A 1 264 ? 4.165 52.531 13.923 1.00 26.11 ? 282 ASP A O 1 ATOM 2116 C CB . ASP A 1 264 ? 4.411 55.619 14.092 1.00 28.47 ? 282 ASP A CB 1 ATOM 2117 C CG . ASP A 1 264 ? 4.987 57.016 13.869 1.00 31.66 ? 282 ASP A CG 1 ATOM 2118 O OD1 . ASP A 1 264 ? 6.213 57.199 13.992 1.00 35.63 ? 282 ASP A OD1 1 ATOM 2119 O OD2 . ASP A 1 264 ? 4.208 57.924 13.534 1.00 38.60 ? 282 ASP A OD2 1 ATOM 2120 N N . PHE A 1 265 ? 4.983 53.055 15.959 1.00 25.98 ? 283 PHE A N 1 ATOM 2121 C CA . PHE A 1 265 ? 4.497 51.853 16.604 1.00 26.41 ? 283 PHE A CA 1 ATOM 2122 C C . PHE A 1 265 ? 3.052 51.620 16.279 1.00 26.88 ? 283 PHE A C 1 ATOM 2123 O O . PHE A 1 265 ? 2.207 52.483 16.513 1.00 26.79 ? 283 PHE A O 1 ATOM 2124 C CB . PHE A 1 265 ? 4.688 51.930 18.125 1.00 26.18 ? 283 PHE A CB 1 ATOM 2125 C CG . PHE A 1 265 ? 4.321 50.663 18.850 1.00 25.91 ? 283 PHE A CG 1 ATOM 2126 C CD1 . PHE A 1 265 ? 5.231 49.642 18.989 1.00 24.50 ? 283 PHE A CD1 1 ATOM 2127 C CD2 . PHE A 1 265 ? 3.080 50.522 19.423 1.00 23.56 ? 283 PHE A CD2 1 ATOM 2128 C CE1 . PHE A 1 265 ? 4.912 48.502 19.683 1.00 25.91 ? 283 PHE A CE1 1 ATOM 2129 C CE2 . PHE A 1 265 ? 2.747 49.371 20.122 1.00 25.71 ? 283 PHE A CE2 1 ATOM 2130 C CZ . PHE A 1 265 ? 3.653 48.366 20.259 1.00 25.37 ? 283 PHE A CZ 1 ATOM 2131 N N . THR A 1 266 ? 2.778 50.430 15.737 1.00 26.33 ? 284 THR A N 1 ATOM 2132 C CA . THR A 1 266 ? 1.439 50.099 15.223 1.00 26.09 ? 284 THR A CA 1 ATOM 2133 C C . THR A 1 266 ? 1.152 48.637 15.478 1.00 27.41 ? 284 THR A C 1 ATOM 2134 O O . THR A 1 266 ? 1.727 47.767 14.818 1.00 28.45 ? 284 THR A O 1 ATOM 2135 C CB . THR A 1 266 ? 1.280 50.400 13.675 1.00 26.19 ? 284 THR A CB 1 ATOM 2136 O OG1 . THR A 1 266 ? 1.634 51.764 13.360 1.00 24.50 ? 284 THR A OG1 1 ATOM 2137 C CG2 . THR A 1 266 ? -0.115 50.120 13.177 1.00 24.16 ? 284 THR A CG2 1 ATOM 2138 N N . PRO A 1 267 ? 0.280 48.345 16.473 1.00 27.28 ? 285 PRO A N 1 ATOM 2139 C CA . PRO A 1 267 ? 0.107 46.968 16.847 1.00 27.08 ? 285 PRO A CA 1 ATOM 2140 C C . PRO A 1 267 ? -0.366 46.108 15.702 1.00 27.90 ? 285 PRO A C 1 ATOM 2141 O O . PRO A 1 267 ? -1.217 46.524 14.890 1.00 28.49 ? 285 PRO A O 1 ATOM 2142 C CB . PRO A 1 267 ? -0.929 46.998 17.960 1.00 26.41 ? 285 PRO A CB 1 ATOM 2143 C CG . PRO A 1 267 ? -0.902 48.363 18.521 1.00 27.36 ? 285 PRO A CG 1 ATOM 2144 C CD . PRO A 1 267 ? -0.354 49.285 17.410 1.00 27.36 ? 285 PRO A CD 1 ATOM 2145 N N . VAL A 1 268 ? 0.152 44.879 15.696 1.00 28.06 ? 286 VAL A N 1 ATOM 2146 C CA . VAL A 1 268 ? -0.208 43.894 14.688 1.00 26.60 ? 286 VAL A CA 1 ATOM 2147 C C . VAL A 1 268 ? -1.508 43.230 15.127 1.00 26.97 ? 286 VAL A C 1 ATOM 2148 O O . VAL A 1 268 ? -1.904 43.303 16.306 1.00 27.59 ? 286 VAL A O 1 ATOM 2149 C CB . VAL A 1 268 ? 0.907 42.870 14.421 1.00 26.90 ? 286 VAL A CB 1 ATOM 2150 C CG1 . VAL A 1 268 ? 2.152 43.576 13.933 1.00 24.44 ? 286 VAL A CG1 1 ATOM 2151 C CG2 . VAL A 1 268 ? 1.164 41.956 15.631 1.00 25.00 ? 286 VAL A CG2 1 ATOM 2152 N N . GLN A 1 269 ? -2.188 42.618 14.163 1.00 26.64 ? 287 GLN A N 1 ATOM 2153 C CA . GLN A 1 269 ? -3.391 41.825 14.460 1.00 26.61 ? 287 GLN A CA 1 ATOM 2154 C C . GLN A 1 269 ? -3.191 40.412 14.027 1.00 27.14 ? 287 GLN A C 1 ATOM 2155 O O . GLN A 1 269 ? -2.793 40.145 12.891 1.00 28.11 ? 287 GLN A O 1 ATOM 2156 C CB . GLN A 1 269 ? -4.593 42.389 13.733 1.00 26.10 ? 287 GLN A CB 1 ATOM 2157 C CG . GLN A 1 269 ? -4.929 43.800 14.088 1.00 25.99 ? 287 GLN A CG 1 ATOM 2158 C CD . GLN A 1 269 ? -5.902 44.364 13.100 1.00 28.51 ? 287 GLN A CD 1 ATOM 2159 O OE1 . GLN A 1 269 ? -7.096 44.004 13.124 1.00 28.29 ? 287 GLN A OE1 1 ATOM 2160 N NE2 . GLN A 1 269 ? -5.406 45.222 12.192 1.00 24.92 ? 287 GLN A NE2 1 ATOM 2161 N N . VAL A 1 270 ? -3.480 39.497 14.936 1.00 27.76 ? 288 VAL A N 1 ATOM 2162 C CA . VAL A 1 270 ? -3.198 38.067 14.744 1.00 26.67 ? 288 VAL A CA 1 ATOM 2163 C C . VAL A 1 270 ? -4.425 37.224 15.004 1.00 27.66 ? 288 VAL A C 1 ATOM 2164 O O . VAL A 1 270 ? -5.044 37.314 16.073 1.00 26.55 ? 288 VAL A O 1 ATOM 2165 C CB . VAL A 1 270 ? -2.055 37.545 15.673 1.00 27.12 ? 288 VAL A CB 1 ATOM 2166 C CG1 . VAL A 1 270 ? -1.998 35.981 15.626 1.00 25.01 ? 288 VAL A CG1 1 ATOM 2167 C CG2 . VAL A 1 270 ? -0.675 38.227 15.298 1.00 25.46 ? 288 VAL A CG2 1 ATOM 2168 N N . VAL A 1 271 ? -4.749 36.385 14.006 1.00 27.65 ? 289 VAL A N 1 ATOM 2169 C CA . VAL A 1 271 ? -5.914 35.517 14.054 1.00 26.65 ? 289 VAL A CA 1 ATOM 2170 C C . VAL A 1 271 ? -5.445 34.119 14.323 1.00 27.47 ? 289 VAL A C 1 ATOM 2171 O O . VAL A 1 271 ? -4.577 33.582 13.633 1.00 27.57 ? 289 VAL A O 1 ATOM 2172 C CB . VAL A 1 271 ? -6.706 35.583 12.726 1.00 26.27 ? 289 VAL A CB 1 ATOM 2173 C CG1 . VAL A 1 271 ? -7.989 34.723 12.786 1.00 25.57 ? 289 VAL A CG1 1 ATOM 2174 C CG2 . VAL A 1 271 ? -7.025 37.056 12.351 1.00 25.48 ? 289 VAL A CG2 1 ATOM 2175 N N . ASP A 1 272 ? -6.048 33.505 15.325 1.00 27.74 ? 290 ASP A N 1 ATOM 2176 C CA . ASP A 1 272 ? -5.735 32.116 15.671 1.00 28.85 ? 290 ASP A CA 1 ATOM 2177 C C . ASP A 1 272 ? -5.793 31.193 14.433 1.00 29.32 ? 290 ASP A C 1 ATOM 2178 O O . ASP A 1 272 ? -6.775 31.186 13.673 1.00 28.86 ? 290 ASP A O 1 ATOM 2179 C CB . ASP A 1 272 ? -6.677 31.610 16.782 1.00 29.31 ? 290 ASP A CB 1 ATOM 2180 C CG . ASP A 1 272 ? -6.273 30.276 17.340 1.00 33.16 ? 290 ASP A CG 1 ATOM 2181 O OD1 . ASP A 1 272 ? -5.055 29.995 17.376 1.00 34.80 ? 290 ASP A OD1 1 ATOM 2182 O OD2 . ASP A 1 272 ? -7.175 29.502 17.790 1.00 34.24 ? 290 ASP A OD2 1 ATOM 2183 N N . SER A 1 273 ? -4.718 30.423 14.251 1.00 29.16 ? 291 SER A N 1 ATOM 2184 C CA . SER A 1 273 ? -4.589 29.527 13.096 1.00 29.16 ? 291 SER A CA 1 ATOM 2185 C C . SER A 1 273 ? -4.519 28.125 13.614 1.00 30.58 ? 291 SER A C 1 ATOM 2186 O O . SER A 1 273 ? -3.490 27.685 14.125 1.00 30.35 ? 291 SER A O 1 ATOM 2187 C CB . SER A 1 273 ? -3.372 29.881 12.233 1.00 29.45 ? 291 SER A CB 1 ATOM 2188 O OG . SER A 1 273 ? -3.303 29.128 11.023 1.00 26.22 ? 291 SER A OG 1 ATOM 2189 N N . ARG A 1 274 ? -5.669 27.454 13.525 1.00 30.93 ? 292 ARG A N 1 ATOM 2190 C CA . ARG A 1 274 ? -5.839 26.095 14.029 1.00 32.07 ? 292 ARG A CA 1 ATOM 2191 C C . ARG A 1 274 ? -6.659 25.212 13.094 1.00 33.16 ? 292 ARG A C 1 ATOM 2192 O O . ARG A 1 274 ? -7.414 25.681 12.234 1.00 32.74 ? 292 ARG A O 1 ATOM 2193 C CB . ARG A 1 274 ? -6.511 26.113 15.423 1.00 31.56 ? 292 ARG A CB 1 ATOM 2194 C CG . ARG A 1 274 ? -7.827 26.852 15.493 1.00 32.26 ? 292 ARG A CG 1 ATOM 2195 C CD . ARG A 1 274 ? -8.446 26.807 16.899 1.00 32.13 ? 292 ARG A CD 1 ATOM 2196 N NE . ARG A 1 274 ? -9.388 27.896 17.114 1.00 32.16 ? 292 ARG A NE 1 ATOM 2197 C CZ . ARG A 1 274 ? -10.725 27.797 17.013 1.00 35.63 ? 292 ARG A CZ 1 ATOM 2198 N NH1 . ARG A 1 274 ? -11.284 26.647 16.639 1.00 37.64 ? 292 ARG A NH1 1 ATOM 2199 N NH2 . ARG A 1 274 ? -11.504 28.863 17.222 1.00 33.62 ? 292 ARG A NH2 1 ATOM 2200 N N . TRP A 1 275 ? -6.451 23.927 13.292 1.00 34.35 ? 293 TRP A N 1 ATOM 2201 C CA . TRP A 1 275 ? -7.228 22.867 12.636 1.00 35.71 ? 293 TRP A CA 1 ATOM 2202 C C . TRP A 1 275 ? -8.553 22.665 13.366 1.00 36.49 ? 293 TRP A C 1 ATOM 2203 O O . TRP A 1 275 ? -8.732 23.051 14.523 1.00 36.95 ? 293 TRP A O 1 ATOM 2204 C CB . TRP A 1 275 ? -6.501 21.526 12.704 1.00 36.21 ? 293 TRP A CB 1 ATOM 2205 C CG . TRP A 1 275 ? -5.152 21.433 12.116 1.00 36.19 ? 293 TRP A CG 1 ATOM 2206 C CD1 . TRP A 1 275 ? -3.992 21.115 12.767 1.00 35.05 ? 293 TRP A CD1 1 ATOM 2207 C CD2 . TRP A 1 275 ? -4.813 21.579 10.743 1.00 38.06 ? 293 TRP A CD2 1 ATOM 2208 N NE1 . TRP A 1 275 ? -2.956 21.076 11.890 1.00 34.60 ? 293 TRP A NE1 1 ATOM 2209 C CE2 . TRP A 1 275 ? -3.426 21.360 10.636 1.00 36.29 ? 293 TRP A CE2 1 ATOM 2210 C CE3 . TRP A 1 275 ? -5.538 21.910 9.593 1.00 37.41 ? 293 TRP A CE3 1 ATOM 2211 C CZ2 . TRP A 1 275 ? -2.754 21.441 9.426 1.00 37.04 ? 293 TRP A CZ2 1 ATOM 2212 C CZ3 . TRP A 1 275 ? -4.859 21.995 8.384 1.00 38.71 ? 293 TRP A CZ3 1 ATOM 2213 C CH2 . TRP A 1 275 ? -3.486 21.754 8.311 1.00 37.64 ? 293 TRP A CH2 1 ATOM 2214 N N . ASN A 1 276 ? -9.494 22.094 12.646 1.00 38.28 ? 294 ASN A N 1 ATOM 2215 C CA . ASN A 1 276 ? -10.665 21.436 13.269 1.00 38.43 ? 294 ASN A CA 1 ATOM 2216 C C . ASN A 1 276 ? -10.169 20.547 14.406 1.00 39.13 ? 294 ASN A C 1 ATOM 2217 O O . ASN A 1 276 ? -9.079 20.010 14.346 1.00 38.96 ? 294 ASN A O 1 ATOM 2218 C CB . ASN A 1 276 ? -11.413 20.622 12.225 1.00 39.02 ? 294 ASN A CB 1 ATOM 2219 C CG . ASN A 1 276 ? -12.422 19.665 12.840 1.00 38.88 ? 294 ASN A CG 1 ATOM 2220 O OD1 . ASN A 1 276 ? -12.091 18.543 13.172 1.00 38.25 ? 294 ASN A OD1 1 ATOM 2221 N ND2 . ASN A 1 276 ? -13.644 20.120 12.982 1.00 36.40 ? 294 ASN A ND2 1 ATOM 2222 N N . ASN A 1 277 ? -10.983 20.415 15.448 1.00 40.71 ? 295 ASN A N 1 ATOM 2223 C CA . ASN A 1 277 ? -10.534 19.837 16.732 1.00 40.88 ? 295 ASN A CA 1 ATOM 2224 C C . ASN A 1 277 ? -10.024 18.410 16.627 1.00 41.38 ? 295 ASN A C 1 ATOM 2225 O O . ASN A 1 277 ? -9.415 17.897 17.558 1.00 40.84 ? 295 ASN A O 1 ATOM 2226 C CB . ASN A 1 277 ? -11.638 19.893 17.779 1.00 41.23 ? 295 ASN A CB 1 ATOM 2227 C CG . ASN A 1 277 ? -11.828 21.279 18.374 1.00 42.99 ? 295 ASN A CG 1 ATOM 2228 O OD1 . ASN A 1 277 ? -12.812 21.512 19.082 1.00 43.67 ? 295 ASN A OD1 1 ATOM 2229 N ND2 . ASN A 1 277 ? -10.897 22.208 18.093 1.00 41.54 ? 295 ASN A ND2 1 ATOM 2230 N N . ALA A 1 278 ? -10.270 17.793 15.482 1.00 41.73 ? 296 ALA A N 1 ATOM 2231 C CA . ALA A 1 278 ? -9.924 16.390 15.274 1.00 42.39 ? 296 ALA A CA 1 ATOM 2232 C C . ALA A 1 278 ? -8.424 16.299 15.113 1.00 43.26 ? 296 ALA A C 1 ATOM 2233 O O . ALA A 1 278 ? -7.852 15.203 15.172 1.00 43.77 ? 296 ALA A O 1 ATOM 2234 C CB . ALA A 1 278 ? -10.651 15.775 14.010 1.00 41.90 ? 296 ALA A CB 1 ATOM 2235 N N . ARG A 1 279 ? -7.788 17.451 14.896 1.00 42.68 ? 297 ARG A N 1 ATOM 2236 C CA . ARG A 1 279 ? -6.304 17.481 14.821 1.00 42.92 ? 297 ARG A CA 1 ATOM 2237 C C . ARG A 1 279 ? -5.743 18.350 15.924 1.00 41.82 ? 297 ARG A C 1 ATOM 2238 O O . ARG A 1 279 ? -6.392 19.283 16.393 1.00 41.92 ? 297 ARG A O 1 ATOM 2239 C CB . ARG A 1 279 ? -5.763 18.003 13.482 1.00 43.19 ? 297 ARG A CB 1 ATOM 2240 C CG . ARG A 1 279 ? -6.153 17.195 12.270 1.00 43.39 ? 297 ARG A CG 1 ATOM 2241 C CD . ARG A 1 279 ? -5.752 17.938 11.029 1.00 44.64 ? 297 ARG A CD 1 ATOM 2242 N NE . ARG A 1 279 ? -5.913 17.145 9.824 1.00 46.01 ? 297 ARG A NE 1 ATOM 2243 C CZ . ARG A 1 279 ? -5.710 17.597 8.592 1.00 47.78 ? 297 ARG A CZ 1 ATOM 2244 N NH1 . ARG A 1 279 ? -5.298 18.839 8.384 1.00 47.18 ? 297 ARG A NH1 1 ATOM 2245 N NH2 . ARG A 1 279 ? -5.908 16.797 7.554 1.00 48.75 ? 297 ARG A NH2 1 ATOM 2246 N N . GLN A 1 280 ? -4.531 18.019 16.317 1.00 40.59 ? 298 GLN A N 1 ATOM 2247 C CA . GLN A 1 280 ? -3.855 18.762 17.388 1.00 40.70 ? 298 GLN A CA 1 ATOM 2248 C C . GLN A 1 280 ? -3.224 20.044 16.864 1.00 38.76 ? 298 GLN A C 1 ATOM 2249 O O . GLN A 1 280 ? -2.355 20.026 15.993 1.00 38.89 ? 298 GLN A O 1 ATOM 2250 C CB . GLN A 1 280 ? -2.815 17.906 18.108 1.00 40.55 ? 298 GLN A CB 1 ATOM 2251 C CG . GLN A 1 280 ? -2.503 18.428 19.524 1.00 43.29 ? 298 GLN A CG 1 ATOM 2252 C CD . GLN A 1 280 ? -1.403 17.629 20.235 1.00 47.00 ? 298 GLN A CD 1 ATOM 2253 O OE1 . GLN A 1 280 ? -0.989 16.539 19.780 1.00 48.76 ? 298 GLN A OE1 1 ATOM 2254 N NE2 . GLN A 1 280 ? -0.908 18.181 21.352 1.00 48.63 ? 298 GLN A NE2 1 ATOM 2255 N N . SER A 1 281 ? -3.711 21.147 17.415 1.00 37.78 ? 299 SER A N 1 ATOM 2256 C CA . SER A 1 281 ? -3.116 22.455 17.203 1.00 37.03 ? 299 SER A CA 1 ATOM 2257 C C . SER A 1 281 ? -2.350 22.910 18.451 1.00 36.31 ? 299 SER A C 1 ATOM 2258 O O . SER A 1 281 ? -2.083 22.120 19.349 1.00 36.58 ? 299 SER A O 1 ATOM 2259 C CB . SER A 1 281 ? -4.201 23.457 16.858 1.00 37.23 ? 299 SER A CB 1 ATOM 2260 O OG . SER A 1 281 ? -4.938 22.994 15.752 1.00 37.66 ? 299 SER A OG 1 ATOM 2261 N N . ASP A 1 282 ? -1.987 24.189 18.482 1.00 34.56 ? 300 ASP A N 1 ATOM 2262 C CA . ASP A 1 282 ? -1.241 24.773 19.603 1.00 33.66 ? 300 ASP A CA 1 ATOM 2263 C C . ASP A 1 282 ? -1.607 26.228 19.833 1.00 32.40 ? 300 ASP A C 1 ATOM 2264 O O . ASP A 1 282 ? -2.270 26.868 19.002 1.00 32.55 ? 300 ASP A O 1 ATOM 2265 C CB . ASP A 1 282 ? 0.268 24.649 19.385 1.00 34.07 ? 300 ASP A CB 1 ATOM 2266 C CG . ASP A 1 282 ? 0.767 25.520 18.232 1.00 34.32 ? 300 ASP A CG 1 ATOM 2267 O OD1 . ASP A 1 282 ? 1.109 24.933 17.172 1.00 31.19 ? 300 ASP A OD1 1 ATOM 2268 O OD2 . ASP A 1 282 ? 0.775 26.772 18.374 1.00 30.99 ? 300 ASP A OD2 1 ATOM 2269 N N . ASN A 1 283 ? -1.182 26.756 20.968 1.00 31.19 ? 301 ASN A N 1 ATOM 2270 C CA . ASN A 1 283 ? -1.522 28.149 21.313 1.00 32.04 ? 301 ASN A CA 1 ATOM 2271 C C . ASN A 1 283 ? -0.292 29.079 21.288 1.00 31.42 ? 301 ASN A C 1 ATOM 2272 O O . ASN A 1 283 ? -0.286 30.169 21.847 1.00 31.56 ? 301 ASN A O 1 ATOM 2273 C CB . ASN A 1 283 ? -2.292 28.234 22.638 1.00 32.47 ? 301 ASN A CB 1 ATOM 2274 C CG . ASN A 1 283 ? -1.434 27.951 23.815 1.00 35.52 ? 301 ASN A CG 1 ATOM 2275 O OD1 . ASN A 1 283 ? -0.312 27.481 23.656 1.00 34.51 ? 301 ASN A OD1 1 ATOM 2276 N ND2 . ASN A 1 283 ? -1.947 28.225 25.012 1.00 44.47 ? 301 ASN A ND2 1 ATOM 2277 N N . MET A 1 284 ? 0.711 28.662 20.534 1.00 30.57 ? 302 MET A N 1 ATOM 2278 C CA . MET A 1 284 ? 1.977 29.403 20.524 1.00 30.49 ? 302 MET A CA 1 ATOM 2279 C C . MET A 1 284 ? 1.849 30.829 19.931 1.00 30.40 ? 302 MET A C 1 ATOM 2280 O O . MET A 1 284 ? 2.474 31.780 20.434 1.00 30.28 ? 302 MET A O 1 ATOM 2281 C CB . MET A 1 284 ? 3.089 28.563 19.891 1.00 30.60 ? 302 MET A CB 1 ATOM 2282 C CG . MET A 1 284 ? 3.526 27.433 20.859 1.00 33.61 ? 302 MET A CG 1 ATOM 2283 S SD . MET A 1 284 ? 4.378 28.059 22.374 1.00 42.20 ? 302 MET A SD 1 ATOM 2284 C CE . MET A 1 284 ? 4.494 26.394 23.078 1.00 41.58 ? 302 MET A CE 1 ATOM 2285 N N . THR A 1 285 ? 1.004 31.011 18.914 1.00 29.02 ? 303 THR A N 1 ATOM 2286 C CA . THR A 1 285 ? 0.808 32.368 18.384 1.00 28.46 ? 303 THR A CA 1 ATOM 2287 C C . THR A 1 285 ? 0.039 33.220 19.390 1.00 29.34 ? 303 THR A C 1 ATOM 2288 O O . THR A 1 285 ? 0.203 34.445 19.430 1.00 29.81 ? 303 THR A O 1 ATOM 2289 C CB . THR A 1 285 ? 0.134 32.386 16.969 1.00 29.00 ? 303 THR A CB 1 ATOM 2290 O OG1 . THR A 1 285 ? -1.201 31.848 17.040 1.00 27.39 ? 303 THR A OG1 1 ATOM 2291 C CG2 . THR A 1 285 ? 0.954 31.595 15.950 1.00 26.39 ? 303 THR A CG2 1 ATOM 2292 N N . ALA A 1 286 ? -0.814 32.571 20.200 1.00 29.54 ? 304 ALA A N 1 ATOM 2293 C CA . ALA A 1 286 ? -1.525 33.279 21.273 1.00 29.70 ? 304 ALA A CA 1 ATOM 2294 C C . ALA A 1 286 ? -0.505 33.748 22.290 1.00 30.19 ? 304 ALA A C 1 ATOM 2295 O O . ALA A 1 286 ? -0.520 34.886 22.696 1.00 31.31 ? 304 ALA A O 1 ATOM 2296 C CB . ALA A 1 286 ? -2.594 32.379 21.955 1.00 30.03 ? 304 ALA A CB 1 ATOM 2297 N N . VAL A 1 287 ? 0.406 32.867 22.677 1.00 31.04 ? 305 VAL A N 1 ATOM 2298 C CA . VAL A 1 287 ? 1.461 33.235 23.670 1.00 30.95 ? 305 VAL A CA 1 ATOM 2299 C C . VAL A 1 287 ? 2.317 34.384 23.138 1.00 30.93 ? 305 VAL A C 1 ATOM 2300 O O . VAL A 1 287 ? 2.644 35.322 23.866 1.00 31.72 ? 305 VAL A O 1 ATOM 2301 C CB . VAL A 1 287 ? 2.315 31.992 24.055 1.00 32.31 ? 305 VAL A CB 1 ATOM 2302 C CG1 . VAL A 1 287 ? 3.575 32.377 24.906 1.00 31.37 ? 305 VAL A CG1 1 ATOM 2303 C CG2 . VAL A 1 287 ? 1.428 30.963 24.778 1.00 30.72 ? 305 VAL A CG2 1 ATOM 2304 N N . ALA A 1 288 ? 2.580 34.347 21.831 1.00 30.56 ? 306 ALA A N 1 ATOM 2305 C CA . ALA A 1 288 ? 3.441 35.346 21.142 1.00 29.24 ? 306 ALA A CA 1 ATOM 2306 C C . ALA A 1 288 ? 2.769 36.709 20.987 1.00 29.29 ? 306 ALA A C 1 ATOM 2307 O O . ALA A 1 288 ? 3.434 37.774 20.912 1.00 27.73 ? 306 ALA A O 1 ATOM 2308 C CB . ALA A 1 288 ? 3.913 34.811 19.753 1.00 28.88 ? 306 ALA A CB 1 ATOM 2309 N N . CYS A 1 289 ? 1.447 36.684 21.027 1.00 28.36 ? 307 CYS A N 1 ATOM 2310 C CA . CYS A 1 289 ? 0.679 37.865 20.677 1.00 28.58 ? 307 CYS A CA 1 ATOM 2311 C C . CYS A 1 289 ? 0.211 38.526 21.954 1.00 28.51 ? 307 CYS A C 1 ATOM 2312 O O . CYS A 1 289 ? -0.712 38.082 22.569 1.00 27.13 ? 307 CYS A O 1 ATOM 2313 C CB . CYS A 1 289 ? -0.502 37.496 19.799 1.00 29.34 ? 307 CYS A CB 1 ATOM 2314 S SG . CYS A 1 289 ? -1.575 38.896 19.367 1.00 29.32 ? 307 CYS A SG 1 ATOM 2315 N N . GLN A 1 290 ? 0.931 39.543 22.371 1.00 28.94 ? 308 GLN A N 1 ATOM 2316 C CA . GLN A 1 290 ? 0.645 40.216 23.622 1.00 29.30 ? 308 GLN A CA 1 ATOM 2317 C C . GLN A 1 290 ? 0.581 41.719 23.447 1.00 29.08 ? 308 GLN A C 1 ATOM 2318 O O . GLN A 1 290 ? 1.262 42.288 22.596 1.00 28.41 ? 308 GLN A O 1 ATOM 2319 C CB . GLN A 1 290 ? 1.747 39.919 24.660 1.00 28.82 ? 308 GLN A CB 1 ATOM 2320 C CG . GLN A 1 290 ? 1.917 38.464 25.009 1.00 29.42 ? 308 GLN A CG 1 ATOM 2321 C CD . GLN A 1 290 ? 0.728 37.927 25.805 1.00 33.52 ? 308 GLN A CD 1 ATOM 2322 O OE1 . GLN A 1 290 ? 0.166 38.637 26.638 1.00 35.10 ? 308 GLN A OE1 1 ATOM 2323 N NE2 . GLN A 1 290 ? 0.334 36.683 25.536 1.00 31.04 ? 308 GLN A NE2 1 ATOM 2324 N N . PRO A 1 291 ? -0.173 42.387 24.339 1.00 30.18 ? 309 PRO A N 1 ATOM 2325 C CA . PRO A 1 291 ? -0.139 43.840 24.326 1.00 30.45 ? 309 PRO A CA 1 ATOM 2326 C C . PRO A 1 291 ? 1.226 44.308 24.782 1.00 29.24 ? 309 PRO A C 1 ATOM 2327 O O . PRO A 1 291 ? 1.876 43.599 25.511 1.00 30.09 ? 309 PRO A O 1 ATOM 2328 C CB . PRO A 1 291 ? -1.251 44.241 25.321 1.00 31.37 ? 309 PRO A CB 1 ATOM 2329 C CG . PRO A 1 291 ? -1.469 43.036 26.182 1.00 31.28 ? 309 PRO A CG 1 ATOM 2330 C CD . PRO A 1 291 ? -1.052 41.833 25.377 1.00 30.66 ? 309 PRO A CD 1 ATOM 2331 N N . PRO A 1 292 ? 1.638 45.503 24.380 1.00 28.11 ? 310 PRO A N 1 ATOM 2332 C CA . PRO A 1 292 ? 0.877 46.404 23.532 1.00 27.37 ? 310 PRO A CA 1 ATOM 2333 C C . PRO A 1 292 ? 1.034 46.178 22.024 1.00 26.68 ? 310 PRO A C 1 ATOM 2334 O O . PRO A 1 292 ? 0.460 46.901 21.225 1.00 26.93 ? 310 PRO A O 1 ATOM 2335 C CB . PRO A 1 292 ? 1.473 47.763 23.875 1.00 28.14 ? 310 PRO A CB 1 ATOM 2336 C CG . PRO A 1 292 ? 2.901 47.478 24.143 1.00 27.93 ? 310 PRO A CG 1 ATOM 2337 C CD . PRO A 1 292 ? 2.903 46.093 24.816 1.00 28.36 ? 310 PRO A CD 1 ATOM 2338 N N . TYR A 1 293 ? 1.796 45.176 21.635 1.00 25.72 ? 311 TYR A N 1 ATOM 2339 C CA . TYR A 1 293 ? 2.262 45.119 20.225 1.00 26.13 ? 311 TYR A CA 1 ATOM 2340 C C . TYR A 1 293 ? 1.384 44.265 19.336 1.00 26.68 ? 311 TYR A C 1 ATOM 2341 O O . TYR A 1 293 ? 1.557 44.234 18.136 1.00 27.31 ? 311 TYR A O 1 ATOM 2342 C CB . TYR A 1 293 ? 3.724 44.633 20.107 1.00 25.34 ? 311 TYR A CB 1 ATOM 2343 C CG . TYR A 1 293 ? 3.963 43.273 20.690 1.00 23.25 ? 311 TYR A CG 1 ATOM 2344 C CD1 . TYR A 1 293 ? 3.767 42.123 19.936 1.00 23.22 ? 311 TYR A CD1 1 ATOM 2345 C CD2 . TYR A 1 293 ? 4.336 43.133 22.015 1.00 26.09 ? 311 TYR A CD2 1 ATOM 2346 C CE1 . TYR A 1 293 ? 3.970 40.875 20.463 1.00 22.32 ? 311 TYR A CE1 1 ATOM 2347 C CE2 . TYR A 1 293 ? 4.553 41.881 22.570 1.00 24.63 ? 311 TYR A CE2 1 ATOM 2348 C CZ . TYR A 1 293 ? 4.375 40.746 21.788 1.00 24.71 ? 311 TYR A CZ 1 ATOM 2349 O OH . TYR A 1 293 ? 4.610 39.495 22.338 1.00 24.97 ? 311 TYR A OH 1 ATOM 2350 N N . CYS A 1 294 ? 0.431 43.590 19.940 1.00 27.40 ? 312 CYS A N 1 ATOM 2351 C CA . CYS A 1 294 ? -0.385 42.654 19.215 1.00 27.44 ? 312 CYS A CA 1 ATOM 2352 C C . CYS A 1 294 ? -1.749 42.524 19.814 1.00 28.06 ? 312 CYS A C 1 ATOM 2353 O O . CYS A 1 294 ? -1.908 42.453 21.012 1.00 28.85 ? 312 CYS A O 1 ATOM 2354 C CB . CYS A 1 294 ? 0.299 41.303 19.177 1.00 27.39 ? 312 CYS A CB 1 ATOM 2355 S SG . CYS A 1 294 ? -0.412 39.984 18.100 1.00 27.51 ? 312 CYS A SG 1 ATOM 2356 N N . TYR A 1 295 ? -2.727 42.489 18.924 1.00 28.55 ? 313 TYR A N 1 ATOM 2357 C CA . TYR A 1 295 ? -4.101 42.064 19.264 1.00 27.85 ? 313 TYR A CA 1 ATOM 2358 C C . TYR A 1 295 ? -4.405 40.674 18.756 1.00 27.74 ? 313 TYR A C 1 ATOM 2359 O O . TYR A 1 295 ? -4.303 40.430 17.580 1.00 29.16 ? 313 TYR A O 1 ATOM 2360 C CB . TYR A 1 295 ? -5.121 43.006 18.626 1.00 27.14 ? 313 TYR A CB 1 ATOM 2361 C CG . TYR A 1 295 ? -4.911 44.469 18.900 1.00 26.80 ? 313 TYR A CG 1 ATOM 2362 C CD1 . TYR A 1 295 ? -4.955 44.974 20.204 1.00 25.82 ? 313 TYR A CD1 1 ATOM 2363 C CD2 . TYR A 1 295 ? -4.716 45.357 17.876 1.00 24.48 ? 313 TYR A CD2 1 ATOM 2364 C CE1 . TYR A 1 295 ? -4.769 46.329 20.452 1.00 24.56 ? 313 TYR A CE1 1 ATOM 2365 C CE2 . TYR A 1 295 ? -4.528 46.701 18.132 1.00 27.34 ? 313 TYR A CE2 1 ATOM 2366 C CZ . TYR A 1 295 ? -4.575 47.182 19.417 1.00 24.13 ? 313 TYR A CZ 1 ATOM 2367 O OH . TYR A 1 295 ? -4.348 48.532 19.623 1.00 24.30 ? 313 TYR A OH 1 ATOM 2368 N N . PHE A 1 296 ? -4.864 39.792 19.627 1.00 26.66 ? 314 PHE A N 1 ATOM 2369 C CA . PHE A 1 296 ? -5.221 38.433 19.261 1.00 27.68 ? 314 PHE A CA 1 ATOM 2370 C C . PHE A 1 296 ? -6.745 38.231 19.059 1.00 28.52 ? 314 PHE A C 1 ATOM 2371 O O . PHE A 1 296 ? -7.561 38.616 19.903 1.00 26.72 ? 314 PHE A O 1 ATOM 2372 C CB . PHE A 1 296 ? -4.718 37.447 20.317 1.00 27.86 ? 314 PHE A CB 1 ATOM 2373 C CG . PHE A 1 296 ? -4.766 35.982 19.881 1.00 27.77 ? 314 PHE A CG 1 ATOM 2374 C CD1 . PHE A 1 296 ? -3.840 35.482 18.974 1.00 28.86 ? 314 PHE A CD1 1 ATOM 2375 C CD2 . PHE A 1 296 ? -5.721 35.121 20.396 1.00 27.44 ? 314 PHE A CD2 1 ATOM 2376 C CE1 . PHE A 1 296 ? -3.869 34.158 18.579 1.00 30.30 ? 314 PHE A CE1 1 ATOM 2377 C CE2 . PHE A 1 296 ? -5.744 33.770 20.026 1.00 28.29 ? 314 PHE A CE2 1 ATOM 2378 C CZ . PHE A 1 296 ? -4.820 33.299 19.118 1.00 30.78 ? 314 PHE A CZ 1 ATOM 2379 N N . ARG A 1 297 ? -7.099 37.646 17.916 1.00 28.91 ? 315 ARG A N 1 ATOM 2380 C CA . ARG A 1 297 ? -8.493 37.281 17.629 1.00 29.40 ? 315 ARG A CA 1 ATOM 2381 C C . ARG A 1 297 ? -8.683 35.801 17.372 1.00 30.72 ? 315 ARG A C 1 ATOM 2382 O O . ARG A 1 297 ? -7.912 35.135 16.660 1.00 30.54 ? 315 ARG A O 1 ATOM 2383 C CB . ARG A 1 297 ? -9.048 38.057 16.443 1.00 29.42 ? 315 ARG A CB 1 ATOM 2384 C CG . ARG A 1 297 ? -8.780 39.494 16.448 1.00 27.10 ? 315 ARG A CG 1 ATOM 2385 C CD . ARG A 1 297 ? -9.531 40.185 17.553 1.00 27.40 ? 315 ARG A CD 1 ATOM 2386 N NE . ARG A 1 297 ? -9.224 41.612 17.491 1.00 29.98 ? 315 ARG A NE 1 ATOM 2387 C CZ . ARG A 1 297 ? -9.045 42.410 18.546 1.00 30.64 ? 315 ARG A CZ 1 ATOM 2388 N NH1 . ARG A 1 297 ? -9.160 41.949 19.785 1.00 34.04 ? 315 ARG A NH1 1 ATOM 2389 N NH2 . ARG A 1 297 ? -8.766 43.673 18.349 1.00 29.22 ? 315 ARG A NH2 1 ATOM 2390 N N . ASN A 1 298 ? -9.752 35.307 17.972 1.00 31.40 ? 316 ASN A N 1 ATOM 2391 C CA . ASN A 1 298 ? -10.138 33.903 17.889 1.00 33.07 ? 316 ASN A CA 1 ATOM 2392 C C . ASN A 1 298 ? -11.659 33.728 17.838 1.00 33.94 ? 316 ASN A C 1 ATOM 2393 O O . ASN A 1 298 ? -12.380 34.518 18.420 1.00 33.51 ? 316 ASN A O 1 ATOM 2394 C CB . ASN A 1 298 ? -9.610 33.193 19.129 1.00 32.75 ? 316 ASN A CB 1 ATOM 2395 C CG . ASN A 1 298 ? -9.730 31.716 19.043 1.00 33.43 ? 316 ASN A CG 1 ATOM 2396 O OD1 . ASN A 1 298 ? -9.932 31.154 17.957 1.00 34.81 ? 316 ASN A OD1 1 ATOM 2397 N ND2 . ASN A 1 298 ? -9.576 31.038 20.210 1.00 35.44 ? 316 ASN A ND2 1 ATOM 2398 N N . SER A 1 299 ? -12.128 32.683 17.161 1.00 35.67 ? 317 SER A N 1 ATOM 2399 C CA . SER A 1 299 ? -13.581 32.390 17.178 1.00 36.95 ? 317 SER A CA 1 ATOM 2400 C C . SER A 1 299 ? -13.875 31.608 18.433 1.00 37.69 ? 317 SER A C 1 ATOM 2401 O O . SER A 1 299 ? -12.966 31.072 19.092 1.00 38.87 ? 317 SER A O 1 ATOM 2402 C CB . SER A 1 299 ? -14.073 31.608 15.960 1.00 35.85 ? 317 SER A CB 1 ATOM 2403 O OG . SER A 1 299 ? -13.906 30.226 16.166 1.00 36.55 ? 317 SER A OG 1 ATOM 2404 N N . THR A 1 300 ? -15.164 31.536 18.742 1.00 38.40 ? 318 THR A N 1 ATOM 2405 C CA . THR A 1 300 ? -15.620 30.908 19.967 1.00 38.27 ? 318 THR A CA 1 ATOM 2406 C C . THR A 1 300 ? -16.017 29.484 19.688 1.00 38.54 ? 318 THR A C 1 ATOM 2407 O O . THR A 1 300 ? -16.413 28.774 20.569 1.00 38.99 ? 318 THR A O 1 ATOM 2408 C CB . THR A 1 300 ? -16.810 31.644 20.589 1.00 38.42 ? 318 THR A CB 1 ATOM 2409 O OG1 . THR A 1 300 ? -17.855 31.759 19.613 1.00 38.55 ? 318 THR A OG1 1 ATOM 2410 C CG2 . THR A 1 300 ? -16.398 33.012 21.082 1.00 38.54 ? 318 THR A CG2 1 ATOM 2411 N N . THR A 1 301 ? -15.825 29.054 18.456 1.00 38.64 ? 319 THR A N 1 ATOM 2412 C CA . THR A 1 301 ? -16.228 27.722 18.044 1.00 37.88 ? 319 THR A CA 1 ATOM 2413 C C . THR A 1 301 ? -15.106 26.867 17.488 1.00 38.82 ? 319 THR A C 1 ATOM 2414 O O . THR A 1 301 ? -14.029 27.349 17.092 1.00 38.16 ? 319 THR A O 1 ATOM 2415 C CB . THR A 1 301 ? -17.392 27.786 16.998 1.00 37.72 ? 319 THR A CB 1 ATOM 2416 O OG1 . THR A 1 301 ? -17.065 28.703 15.941 1.00 37.46 ? 319 THR A OG1 1 ATOM 2417 C CG2 . THR A 1 301 ? -18.693 28.260 17.660 1.00 35.55 ? 319 THR A CG2 1 ATOM 2418 N N . ASN A 1 302 ? -15.372 25.570 17.490 1.00 37.70 ? 320 ASN A N 1 ATOM 2419 C CA . ASN A 1 302 ? -14.616 24.624 16.674 1.00 38.40 ? 320 ASN A CA 1 ATOM 2420 C C . ASN A 1 302 ? -14.518 25.109 15.218 1.00 38.17 ? 320 ASN A C 1 ATOM 2421 O O . ASN A 1 302 ? -15.405 25.773 14.692 1.00 38.20 ? 320 ASN A O 1 ATOM 2422 C CB . ASN A 1 302 ? -15.293 23.237 16.719 1.00 38.19 ? 320 ASN A CB 1 ATOM 2423 C CG . ASN A 1 302 ? -14.463 22.132 16.101 1.00 39.76 ? 320 ASN A CG 1 ATOM 2424 O OD1 . ASN A 1 302 ? -13.226 22.229 15.946 1.00 38.59 ? 320 ASN A OD1 1 ATOM 2425 N ND2 . ASN A 1 302 ? -15.152 21.020 15.771 1.00 40.67 ? 320 ASN A ND2 1 ATOM 2426 N N . TYR A 1 303 ? -13.400 24.793 14.585 1.00 38.06 ? 321 TYR A N 1 ATOM 2427 C CA . TYR A 1 303 ? -13.195 25.140 13.172 1.00 37.54 ? 321 TYR A CA 1 ATOM 2428 C C . TYR A 1 303 ? -13.846 24.041 12.338 1.00 36.97 ? 321 TYR A C 1 ATOM 2429 O O . TYR A 1 303 ? -13.339 22.944 12.235 1.00 36.47 ? 321 TYR A O 1 ATOM 2430 C CB . TYR A 1 303 ? -11.710 25.236 12.791 1.00 36.66 ? 321 TYR A CB 1 ATOM 2431 C CG . TYR A 1 303 ? -11.511 25.836 11.395 1.00 36.89 ? 321 TYR A CG 1 ATOM 2432 C CD1 . TYR A 1 303 ? -11.098 27.139 11.236 1.00 38.13 ? 321 TYR A CD1 1 ATOM 2433 C CD2 . TYR A 1 303 ? -11.791 25.105 10.237 1.00 36.89 ? 321 TYR A CD2 1 ATOM 2434 C CE1 . TYR A 1 303 ? -10.951 27.706 9.975 1.00 38.08 ? 321 TYR A CE1 1 ATOM 2435 C CE2 . TYR A 1 303 ? -11.647 25.673 8.974 1.00 36.88 ? 321 TYR A CE2 1 ATOM 2436 C CZ . TYR A 1 303 ? -11.223 26.968 8.842 1.00 38.21 ? 321 TYR A CZ 1 ATOM 2437 O OH . TYR A 1 303 ? -11.045 27.566 7.587 1.00 36.92 ? 321 TYR A OH 1 ATOM 2438 N N . VAL A 1 304 ? -14.967 24.380 11.752 1.00 38.20 ? 322 VAL A N 1 ATOM 2439 C CA . VAL A 1 304 ? -15.713 23.449 10.897 1.00 38.62 ? 322 VAL A CA 1 ATOM 2440 C C . VAL A 1 304 ? -15.901 24.114 9.561 1.00 39.10 ? 322 VAL A C 1 ATOM 2441 O O . VAL A 1 304 ? -16.699 25.037 9.398 1.00 38.71 ? 322 VAL A O 1 ATOM 2442 C CB . VAL A 1 304 ? -17.057 23.013 11.533 1.00 38.69 ? 322 VAL A CB 1 ATOM 2443 C CG1 . VAL A 1 304 ? -17.831 22.106 10.572 1.00 37.92 ? 322 VAL A CG1 1 ATOM 2444 C CG2 . VAL A 1 304 ? -16.788 22.271 12.854 1.00 37.89 ? 322 VAL A CG2 1 ATOM 2445 N N . GLY A 1 305 ? -15.070 23.667 8.629 1.00 40.21 ? 323 GLY A N 1 ATOM 2446 C CA . GLY A 1 305 ? -15.082 24.163 7.272 1.00 41.62 ? 323 GLY A CA 1 ATOM 2447 C C . GLY A 1 305 ? -16.157 23.500 6.438 1.00 42.89 ? 323 GLY A C 1 ATOM 2448 O O . GLY A 1 305 ? -16.578 22.390 6.713 1.00 42.45 ? 323 GLY A O 1 ATOM 2449 N N . VAL A 1 306 ? -16.547 24.207 5.393 1.00 44.48 ? 324 VAL A N 1 ATOM 2450 C CA . VAL A 1 306 ? -17.613 23.778 4.483 1.00 45.97 ? 324 VAL A CA 1 ATOM 2451 C C . VAL A 1 306 ? -17.038 23.160 3.211 1.00 46.32 ? 324 VAL A C 1 ATOM 2452 O O . VAL A 1 306 ? -17.626 22.264 2.634 1.00 46.99 ? 324 VAL A O 1 ATOM 2453 C CB . VAL A 1 306 ? -18.582 24.946 4.120 1.00 45.77 ? 324 VAL A CB 1 ATOM 2454 C CG1 . VAL A 1 306 ? -19.249 25.506 5.393 1.00 46.90 ? 324 VAL A CG1 1 ATOM 2455 C CG2 . VAL A 1 306 ? -17.864 26.049 3.350 1.00 46.03 ? 324 VAL A CG2 1 ATOM 2456 N N . TYR A 1 307 ? -15.866 23.615 2.790 1.00 46.22 ? 325 TYR A N 1 ATOM 2457 C CA . TYR A 1 307 ? -15.218 23.016 1.619 1.00 45.83 ? 325 TYR A CA 1 ATOM 2458 C C . TYR A 1 307 ? -14.710 21.622 1.953 1.00 45.59 ? 325 TYR A C 1 ATOM 2459 O O . TYR A 1 307 ? -15.030 20.636 1.286 1.00 45.21 ? 325 TYR A O 1 ATOM 2460 C CB . TYR A 1 307 ? -14.073 23.869 1.146 1.00 45.99 ? 325 TYR A CB 1 ATOM 2461 C CG . TYR A 1 307 ? -13.503 23.402 -0.150 1.00 47.29 ? 325 TYR A CG 1 ATOM 2462 C CD1 . TYR A 1 307 ? -14.198 23.585 -1.331 1.00 49.67 ? 325 TYR A CD1 1 ATOM 2463 C CD2 . TYR A 1 307 ? -12.276 22.765 -0.202 1.00 47.49 ? 325 TYR A CD2 1 ATOM 2464 C CE1 . TYR A 1 307 ? -13.672 23.168 -2.532 1.00 50.08 ? 325 TYR A CE1 1 ATOM 2465 C CE2 . TYR A 1 307 ? -11.740 22.354 -1.399 1.00 48.60 ? 325 TYR A CE2 1 ATOM 2466 C CZ . TYR A 1 307 ? -12.442 22.558 -2.558 1.00 50.26 ? 325 TYR A CZ 1 ATOM 2467 O OH . TYR A 1 307 ? -11.922 22.133 -3.758 1.00 53.35 ? 325 TYR A OH 1 ATOM 2468 N N . ASP A 1 308 ? -13.810 21.588 2.927 1.00 44.39 ? 326 ASP A N 1 ATOM 2469 C CA . ASP A 1 308 ? -13.546 20.396 3.710 1.00 43.31 ? 326 ASP A CA 1 ATOM 2470 C C . ASP A 1 308 ? -13.497 20.827 5.174 1.00 42.68 ? 326 ASP A C 1 ATOM 2471 O O . ASP A 1 308 ? -13.692 21.997 5.504 1.00 41.72 ? 326 ASP A O 1 ATOM 2472 C CB . ASP A 1 308 ? -12.262 19.661 3.302 1.00 44.46 ? 326 ASP A CB 1 ATOM 2473 C CG . ASP A 1 308 ? -10.998 20.541 3.401 1.00 44.39 ? 326 ASP A CG 1 ATOM 2474 O OD1 . ASP A 1 308 ? -10.702 21.083 4.479 1.00 43.77 ? 326 ASP A OD1 1 ATOM 2475 O OD2 . ASP A 1 308 ? -10.334 20.692 2.376 1.00 42.63 ? 326 ASP A OD2 1 ATOM 2476 N N . ILE A 1 309 ? -13.272 19.870 6.045 1.00 41.82 ? 327 ILE A N 1 ATOM 2477 C CA . ILE A 1 309 ? -13.483 20.110 7.462 1.00 42.35 ? 327 ILE A CA 1 ATOM 2478 C C . ILE A 1 309 ? -12.512 21.193 8.008 1.00 41.71 ? 327 ILE A C 1 ATOM 2479 O O . ILE A 1 309 ? -12.779 21.864 9.005 1.00 40.81 ? 327 ILE A O 1 ATOM 2480 C CB . ILE A 1 309 ? -13.449 18.766 8.277 1.00 43.03 ? 327 ILE A CB 1 ATOM 2481 C CG1 . ILE A 1 309 ? -14.154 18.968 9.612 1.00 44.29 ? 327 ILE A CG1 1 ATOM 2482 C CG2 . ILE A 1 309 ? -12.030 18.203 8.421 1.00 41.50 ? 327 ILE A CG2 1 ATOM 2483 C CD1 . ILE A 1 309 ? -15.585 19.537 9.471 1.00 45.19 ? 327 ILE A CD1 1 ATOM 2484 N N . ASN A 1 310 ? -11.440 21.410 7.264 1.00 40.77 ? 328 ASN A N 1 ATOM 2485 C CA . ASN A 1 310 ? -10.372 22.322 7.691 1.00 40.13 ? 328 ASN A CA 1 ATOM 2486 C C . ASN A 1 310 ? -10.283 23.595 6.883 1.00 40.06 ? 328 ASN A C 1 ATOM 2487 O O . ASN A 1 310 ? -9.352 24.408 7.074 1.00 38.94 ? 328 ASN A O 1 ATOM 2488 C CB . ASN A 1 310 ? -9.029 21.592 7.689 1.00 39.36 ? 328 ASN A CB 1 ATOM 2489 C CG . ASN A 1 310 ? -8.851 20.786 8.917 1.00 37.98 ? 328 ASN A CG 1 ATOM 2490 O OD1 . ASN A 1 310 ? -8.862 21.318 10.010 1.00 39.23 ? 328 ASN A OD1 1 ATOM 2491 N ND2 . ASN A 1 310 ? -8.744 19.493 8.766 1.00 37.21 ? 328 ASN A ND2 1 ATOM 2492 N N . HIS A 1 311 ? -11.288 23.793 6.034 1.00 39.05 ? 329 HIS A N 1 ATOM 2493 C CA . HIS A 1 311 ? -11.342 24.986 5.194 1.00 39.16 ? 329 HIS A CA 1 ATOM 2494 C C . HIS A 1 311 ? -12.726 25.524 4.916 1.00 39.36 ? 329 HIS A C 1 ATOM 2495 O O . HIS A 1 311 ? -13.594 24.805 4.383 1.00 38.87 ? 329 HIS A O 1 ATOM 2496 C CB . HIS A 1 311 ? -10.658 24.708 3.858 1.00 39.36 ? 329 HIS A CB 1 ATOM 2497 C CG . HIS A 1 311 ? -9.265 24.210 4.005 1.00 39.79 ? 329 HIS A CG 1 ATOM 2498 N ND1 . HIS A 1 311 ? -8.971 22.891 4.268 1.00 40.78 ? 329 HIS A ND1 1 ATOM 2499 C CD2 . HIS A 1 311 ? -8.077 24.854 3.915 1.00 38.77 ? 329 HIS A CD2 1 ATOM 2500 C CE1 . HIS A 1 311 ? -7.659 22.749 4.356 1.00 41.50 ? 329 HIS A CE1 1 ATOM 2501 N NE2 . HIS A 1 311 ? -7.098 23.923 4.139 1.00 39.98 ? 329 HIS A NE2 1 ATOM 2502 N N . GLY A 1 312 ? -12.883 26.800 5.275 1.00 38.59 ? 330 GLY A N 1 ATOM 2503 C CA . GLY A 1 312 ? -14.068 27.613 5.053 1.00 38.42 ? 330 GLY A CA 1 ATOM 2504 C C . GLY A 1 312 ? -15.053 27.599 6.213 1.00 39.12 ? 330 GLY A C 1 ATOM 2505 O O . GLY A 1 312 ? -16.131 26.979 6.126 1.00 39.09 ? 330 GLY A O 1 ATOM 2506 N N . ASP A 1 313 ? -14.690 28.321 7.276 1.00 38.53 ? 331 ASP A N 1 ATOM 2507 C CA . ASP A 1 313 ? -15.389 28.284 8.567 1.00 37.55 ? 331 ASP A CA 1 ATOM 2508 C C . ASP A 1 313 ? -16.123 29.571 8.822 1.00 37.15 ? 331 ASP A C 1 ATOM 2509 O O . ASP A 1 313 ? -15.668 30.655 8.445 1.00 37.65 ? 331 ASP A O 1 ATOM 2510 C CB . ASP A 1 313 ? -14.381 28.012 9.691 1.00 38.28 ? 331 ASP A CB 1 ATOM 2511 C CG . ASP A 1 313 ? -14.997 28.151 11.080 1.00 37.22 ? 331 ASP A CG 1 ATOM 2512 O OD1 . ASP A 1 313 ? -15.600 27.171 11.551 1.00 36.94 ? 331 ASP A OD1 1 ATOM 2513 O OD2 . ASP A 1 313 ? -14.840 29.228 11.694 1.00 37.00 ? 331 ASP A OD2 1 ATOM 2514 N N . ALA A 1 314 ? -17.313 29.448 9.408 1.00 36.77 ? 332 ALA A N 1 ATOM 2515 C CA . ALA A 1 314 ? -18.181 30.633 9.638 1.00 35.91 ? 332 ALA A CA 1 ATOM 2516 C C . ALA A 1 314 ? -17.543 31.625 10.591 1.00 34.35 ? 332 ALA A C 1 ATOM 2517 O O . ALA A 1 314 ? -17.603 32.853 10.409 1.00 34.70 ? 332 ALA A O 1 ATOM 2518 C CB . ALA A 1 314 ? -19.605 30.218 10.171 1.00 35.33 ? 332 ALA A CB 1 ATOM 2519 N N . GLY A 1 315 ? -16.965 31.077 11.641 1.00 33.73 ? 333 GLY A N 1 ATOM 2520 C CA . GLY A 1 315 ? -16.361 31.880 12.709 1.00 32.83 ? 333 GLY A CA 1 ATOM 2521 C C . GLY A 1 315 ? -15.150 32.674 12.236 1.00 32.08 ? 333 GLY A C 1 ATOM 2522 O O . GLY A 1 315 ? -15.061 33.887 12.438 1.00 32.07 ? 333 GLY A O 1 ATOM 2523 N N . PHE A 1 316 ? -14.256 32.004 11.530 1.00 31.43 ? 334 PHE A N 1 ATOM 2524 C CA . PHE A 1 316 ? -13.079 32.712 10.976 1.00 31.53 ? 334 PHE A CA 1 ATOM 2525 C C . PHE A 1 316 ? -13.397 33.592 9.790 1.00 32.17 ? 334 PHE A C 1 ATOM 2526 O O . PHE A 1 316 ? -12.799 34.660 9.598 1.00 33.51 ? 334 PHE A O 1 ATOM 2527 C CB . PHE A 1 316 ? -11.935 31.747 10.743 1.00 31.63 ? 334 PHE A CB 1 ATOM 2528 C CG . PHE A 1 316 ? -11.313 31.324 12.025 1.00 29.14 ? 334 PHE A CG 1 ATOM 2529 C CD1 . PHE A 1 316 ? -10.402 32.159 12.673 1.00 31.50 ? 334 PHE A CD1 1 ATOM 2530 C CD2 . PHE A 1 316 ? -11.686 30.158 12.637 1.00 31.14 ? 334 PHE A CD2 1 ATOM 2531 C CE1 . PHE A 1 316 ? -9.846 31.811 13.897 1.00 30.89 ? 334 PHE A CE1 1 ATOM 2532 C CE2 . PHE A 1 316 ? -11.137 29.784 13.869 1.00 33.44 ? 334 PHE A CE2 1 ATOM 2533 C CZ . PHE A 1 316 ? -10.211 30.596 14.502 1.00 31.77 ? 334 PHE A CZ 1 ATOM 2534 N N . THR A 1 317 ? -14.434 33.216 9.040 1.00 32.27 ? 335 THR A N 1 ATOM 2535 C CA . THR A 1 317 ? -14.861 34.061 7.922 1.00 31.30 ? 335 THR A CA 1 ATOM 2536 C C . THR A 1 317 ? -15.308 35.371 8.473 1.00 31.39 ? 335 THR A C 1 ATOM 2537 O O . THR A 1 317 ? -15.027 36.460 7.950 1.00 32.06 ? 335 THR A O 1 ATOM 2538 C CB . THR A 1 317 ? -15.952 33.358 7.105 1.00 31.68 ? 335 THR A CB 1 ATOM 2539 O OG1 . THR A 1 317 ? -15.342 32.241 6.510 1.00 30.01 ? 335 THR A OG1 1 ATOM 2540 C CG2 . THR A 1 317 ? -16.547 34.240 6.022 1.00 29.83 ? 335 THR A CG2 1 ATOM 2541 N N . SER A 1 318 ? -15.982 35.274 9.593 1.00 32.47 ? 336 SER A N 1 ATOM 2542 C CA . SER A 1 318 ? -16.543 36.455 10.221 1.00 32.25 ? 336 SER A CA 1 ATOM 2543 C C . SER A 1 318 ? -15.420 37.362 10.735 1.00 31.74 ? 336 SER A C 1 ATOM 2544 O O . SER A 1 318 ? -15.436 38.583 10.551 1.00 30.13 ? 336 SER A O 1 ATOM 2545 C CB . SER A 1 318 ? -17.495 36.068 11.373 1.00 33.23 ? 336 SER A CB 1 ATOM 2546 O OG . SER A 1 318 ? -17.795 37.214 12.147 1.00 33.05 ? 336 SER A OG 1 ATOM 2547 N N . ILE A 1 319 ? -14.451 36.757 11.388 1.00 32.05 ? 337 ILE A N 1 ATOM 2548 C CA . ILE A 1 319 ? -13.315 37.551 11.884 1.00 32.38 ? 337 ILE A CA 1 ATOM 2549 C C . ILE A 1 319 ? -12.633 38.303 10.718 1.00 32.57 ? 337 ILE A C 1 ATOM 2550 O O . ILE A 1 319 ? -12.364 39.500 10.803 1.00 32.44 ? 337 ILE A O 1 ATOM 2551 C CB . ILE A 1 319 ? -12.294 36.701 12.685 1.00 33.03 ? 337 ILE A CB 1 ATOM 2552 C CG1 . ILE A 1 319 ? -12.928 36.193 13.998 1.00 30.49 ? 337 ILE A CG1 1 ATOM 2553 C CG2 . ILE A 1 319 ? -10.987 37.530 12.933 1.00 31.93 ? 337 ILE A CG2 1 ATOM 2554 C CD1 . ILE A 1 319 ? -12.161 35.147 14.733 1.00 26.93 ? 337 ILE A CD1 1 ATOM 2555 N N . LEU A 1 320 ? -12.400 37.608 9.623 1.00 33.33 ? 338 LEU A N 1 ATOM 2556 C CA . LEU A 1 320 ? -11.701 38.226 8.467 1.00 33.82 ? 338 LEU A CA 1 ATOM 2557 C C . LEU A 1 320 ? -12.546 39.232 7.692 1.00 32.83 ? 338 LEU A C 1 ATOM 2558 O O . LEU A 1 320 ? -12.003 40.020 6.927 1.00 32.01 ? 338 LEU A O 1 ATOM 2559 C CB . LEU A 1 320 ? -11.208 37.186 7.464 1.00 34.25 ? 338 LEU A CB 1 ATOM 2560 C CG . LEU A 1 320 ? -10.065 36.229 7.854 1.00 37.79 ? 338 LEU A CG 1 ATOM 2561 C CD1 . LEU A 1 320 ? -9.180 36.019 6.652 1.00 41.18 ? 338 LEU A CD1 1 ATOM 2562 C CD2 . LEU A 1 320 ? -9.277 36.670 9.001 1.00 40.72 ? 338 LEU A CD2 1 ATOM 2563 N N . SER A 1 321 ? -13.862 39.200 7.908 1.00 31.92 ? 339 SER A N 1 ATOM 2564 C CA . SER A 1 321 ? -14.801 40.064 7.135 1.00 31.21 ? 339 SER A CA 1 ATOM 2565 C C . SER A 1 321 ? -14.543 41.520 7.401 1.00 30.46 ? 339 SER A C 1 ATOM 2566 O O . SER A 1 321 ? -14.914 42.411 6.622 1.00 30.03 ? 339 SER A O 1 ATOM 2567 C CB . SER A 1 321 ? -16.280 39.749 7.452 1.00 32.35 ? 339 SER A CB 1 ATOM 2568 O OG . SER A 1 321 ? -16.634 40.128 8.769 1.00 32.06 ? 339 SER A OG 1 ATOM 2569 N N . GLY A 1 322 ? -13.885 41.782 8.524 1.00 29.74 ? 340 GLY A N 1 ATOM 2570 C CA . GLY A 1 322 ? -13.579 43.162 8.888 1.00 28.48 ? 340 GLY A CA 1 ATOM 2571 C C . GLY A 1 322 ? -12.585 43.804 7.934 1.00 28.75 ? 340 GLY A C 1 ATOM 2572 O O . GLY A 1 322 ? -12.428 45.029 7.908 1.00 30.02 ? 340 GLY A O 1 ATOM 2573 N N . LEU A 1 323 ? -11.886 42.973 7.168 1.00 29.71 ? 341 LEU A N 1 ATOM 2574 C CA . LEU A 1 323 ? -10.933 43.492 6.153 1.00 30.70 ? 341 LEU A CA 1 ATOM 2575 C C . LEU A 1 323 ? -11.639 44.181 4.973 1.00 32.48 ? 341 LEU A C 1 ATOM 2576 O O . LEU A 1 323 ? -11.006 44.832 4.136 1.00 31.85 ? 341 LEU A O 1 ATOM 2577 C CB . LEU A 1 323 ? -10.025 42.391 5.618 1.00 30.23 ? 341 LEU A CB 1 ATOM 2578 C CG . LEU A 1 323 ? -9.021 41.784 6.628 1.00 30.83 ? 341 LEU A CG 1 ATOM 2579 C CD1 . LEU A 1 323 ? -8.160 40.669 5.997 1.00 30.13 ? 341 LEU A CD1 1 ATOM 2580 C CD2 . LEU A 1 323 ? -8.121 42.927 7.260 1.00 26.65 ? 341 LEU A CD2 1 ATOM 2581 N N . LEU A 1 324 ? -12.957 44.019 4.925 1.00 34.52 ? 342 LEU A N 1 ATOM 2582 C CA . LEU A 1 324 ? -13.782 44.565 3.804 1.00 34.92 ? 342 LEU A CA 1 ATOM 2583 C C . LEU A 1 324 ? -14.147 46.005 4.038 1.00 35.56 ? 342 LEU A C 1 ATOM 2584 O O . LEU A 1 324 ? -14.661 46.691 3.144 1.00 37.68 ? 342 LEU A O 1 ATOM 2585 C CB . LEU A 1 324 ? -15.085 43.768 3.613 1.00 34.99 ? 342 LEU A CB 1 ATOM 2586 C CG . LEU A 1 324 ? -14.988 42.379 2.973 1.00 35.16 ? 342 LEU A CG 1 ATOM 2587 C CD1 . LEU A 1 324 ? -16.336 41.579 3.041 1.00 35.27 ? 342 LEU A CD1 1 ATOM 2588 C CD2 . LEU A 1 324 ? -14.469 42.487 1.531 1.00 33.05 ? 342 LEU A CD2 1 ATOM 2589 N N . TYR A 1 325 ? -13.881 46.485 5.238 1.00 35.00 ? 343 TYR A N 1 ATOM 2590 C CA . TYR A 1 325 ? -14.138 47.891 5.565 1.00 34.88 ? 343 TYR A CA 1 ATOM 2591 C C . TYR A 1 325 ? -13.058 48.511 6.473 1.00 34.73 ? 343 TYR A C 1 ATOM 2592 O O . TYR A 1 325 ? -12.303 47.816 7.111 1.00 33.99 ? 343 TYR A O 1 ATOM 2593 C CB . TYR A 1 325 ? -15.539 48.066 6.199 1.00 35.42 ? 343 TYR A CB 1 ATOM 2594 C CG . TYR A 1 325 ? -15.850 47.109 7.318 1.00 34.86 ? 343 TYR A CG 1 ATOM 2595 C CD1 . TYR A 1 325 ? -15.400 47.359 8.612 1.00 34.70 ? 343 TYR A CD1 1 ATOM 2596 C CD2 . TYR A 1 325 ? -16.581 45.944 7.083 1.00 34.91 ? 343 TYR A CD2 1 ATOM 2597 C CE1 . TYR A 1 325 ? -15.652 46.478 9.639 1.00 32.62 ? 343 TYR A CE1 1 ATOM 2598 C CE2 . TYR A 1 325 ? -16.858 45.052 8.103 1.00 34.43 ? 343 TYR A CE2 1 ATOM 2599 C CZ . TYR A 1 325 ? -16.368 45.317 9.384 1.00 36.13 ? 343 TYR A CZ 1 ATOM 2600 O OH . TYR A 1 325 ? -16.655 44.426 10.391 1.00 32.25 ? 343 TYR A OH 1 ATOM 2601 N N . ASP A 1 326 ? -12.992 49.837 6.454 1.00 34.98 ? 344 ASP A N 1 ATOM 2602 C CA . ASP A 1 326 ? -12.200 50.614 7.409 1.00 34.66 ? 344 ASP A CA 1 ATOM 2603 C C . ASP A 1 326 ? -12.911 50.651 8.749 1.00 35.35 ? 344 ASP A C 1 ATOM 2604 O O . ASP A 1 326 ? -14.137 50.636 8.815 1.00 35.77 ? 344 ASP A O 1 ATOM 2605 C CB . ASP A 1 326 ? -11.964 52.046 6.959 1.00 34.04 ? 344 ASP A CB 1 ATOM 2606 C CG . ASP A 1 326 ? -11.001 52.158 5.819 1.00 35.13 ? 344 ASP A CG 1 ATOM 2607 O OD1 . ASP A 1 326 ? -10.119 51.283 5.610 1.00 37.97 ? 344 ASP A OD1 1 ATOM 2608 O OD2 . ASP A 1 326 ? -11.116 53.159 5.106 1.00 34.65 ? 344 ASP A OD2 1 ATOM 2609 N N . SER A 1 327 ? -12.121 50.627 9.826 1.00 34.97 ? 345 SER A N 1 ATOM 2610 C CA . SER A 1 327 ? -12.640 50.763 11.189 1.00 34.54 ? 345 SER A CA 1 ATOM 2611 C C . SER A 1 327 ? -11.707 51.699 11.994 1.00 34.81 ? 345 SER A C 1 ATOM 2612 O O . SER A 1 327 ? -10.488 51.669 11.809 1.00 35.79 ? 345 SER A O 1 ATOM 2613 C CB . SER A 1 327 ? -12.710 49.419 11.896 1.00 33.91 ? 345 SER A CB 1 ATOM 2614 O OG . SER A 1 327 ? -13.446 48.427 11.189 1.00 32.90 ? 345 SER A OG 1 ATOM 2615 N N . PRO A 1 328 ? -12.267 52.519 12.884 1.00 34.51 ? 346 PRO A N 1 ATOM 2616 C CA . PRO A 1 328 ? -11.440 53.604 13.448 1.00 33.90 ? 346 PRO A CA 1 ATOM 2617 C C . PRO A 1 328 ? -10.605 53.210 14.662 1.00 33.20 ? 346 PRO A C 1 ATOM 2618 O O . PRO A 1 328 ? -9.558 53.796 14.879 1.00 33.05 ? 346 PRO A O 1 ATOM 2619 C CB . PRO A 1 328 ? -12.470 54.643 13.884 1.00 33.93 ? 346 PRO A CB 1 ATOM 2620 C CG . PRO A 1 328 ? -13.726 53.818 14.150 1.00 34.10 ? 346 PRO A CG 1 ATOM 2621 C CD . PRO A 1 328 ? -13.711 52.750 13.112 1.00 34.25 ? 346 PRO A CD 1 ATOM 2622 N N . CYS A 1 329 ? -11.078 52.221 15.410 1.00 32.49 ? 347 CYS A N 1 ATOM 2623 C CA . CYS A 1 329 ? -10.501 51.894 16.709 1.00 32.54 ? 347 CYS A CA 1 ATOM 2624 C C . CYS A 1 329 ? -10.277 50.424 16.899 1.00 32.10 ? 347 CYS A C 1 ATOM 2625 O O . CYS A 1 329 ? -11.192 49.618 16.755 1.00 31.85 ? 347 CYS A O 1 ATOM 2626 C CB . CYS A 1 329 ? -11.379 52.416 17.855 1.00 32.94 ? 347 CYS A CB 1 ATOM 2627 S SG . CYS A 1 329 ? -10.749 52.080 19.531 1.00 33.47 ? 347 CYS A SG 1 ATOM 2628 N N . PHE A 1 330 ? -9.028 50.135 17.251 1.00 30.44 ? 348 PHE A N 1 ATOM 2629 C CA . PHE A 1 330 ? -8.530 48.788 17.567 1.00 30.69 ? 348 PHE A CA 1 ATOM 2630 C C . PHE A 1 330 ? -8.104 48.714 19.047 1.00 30.09 ? 348 PHE A C 1 ATOM 2631 O O . PHE A 1 330 ? -7.441 49.601 19.556 1.00 29.13 ? 348 PHE A O 1 ATOM 2632 C CB . PHE A 1 330 ? -7.319 48.468 16.662 1.00 30.50 ? 348 PHE A CB 1 ATOM 2633 C CG . PHE A 1 330 ? -7.651 48.560 15.213 1.00 28.81 ? 348 PHE A CG 1 ATOM 2634 C CD1 . PHE A 1 330 ? -7.999 47.431 14.511 1.00 27.99 ? 348 PHE A CD1 1 ATOM 2635 C CD2 . PHE A 1 330 ? -7.761 49.802 14.590 1.00 29.08 ? 348 PHE A CD2 1 ATOM 2636 C CE1 . PHE A 1 330 ? -8.410 47.518 13.201 1.00 26.58 ? 348 PHE A CE1 1 ATOM 2637 C CE2 . PHE A 1 330 ? -8.193 49.876 13.287 1.00 28.24 ? 348 PHE A CE2 1 ATOM 2638 C CZ . PHE A 1 330 ? -8.479 48.714 12.602 1.00 27.19 ? 348 PHE A CZ 1 ATOM 2639 N N . SER A 1 331 ? -8.526 47.649 19.696 1.00 30.07 ? 349 SER A N 1 ATOM 2640 C CA . SER A 1 331 ? -8.287 47.455 21.120 1.00 31.14 ? 349 SER A CA 1 ATOM 2641 C C . SER A 1 331 ? -8.221 45.992 21.498 1.00 31.60 ? 349 SER A C 1 ATOM 2642 O O . SER A 1 331 ? -8.557 45.099 20.731 1.00 31.72 ? 349 SER A O 1 ATOM 2643 C CB . SER A 1 331 ? -9.405 48.100 21.927 1.00 32.52 ? 349 SER A CB 1 ATOM 2644 O OG . SER A 1 331 ? -10.596 47.307 21.803 1.00 31.89 ? 349 SER A OG 1 ATOM 2645 N N . GLN A 1 332 ? -7.765 45.743 22.698 1.00 32.11 ? 350 GLN A N 1 ATOM 2646 C CA . GLN A 1 332 ? -7.658 44.372 23.142 1.00 33.47 ? 350 GLN A CA 1 ATOM 2647 C C . GLN A 1 332 ? -9.004 43.692 23.047 1.00 33.72 ? 350 GLN A C 1 ATOM 2648 O O . GLN A 1 332 ? -9.081 42.520 22.726 1.00 32.67 ? 350 GLN A O 1 ATOM 2649 C CB . GLN A 1 332 ? -7.163 44.290 24.591 1.00 35.20 ? 350 GLN A CB 1 ATOM 2650 C CG . GLN A 1 332 ? -6.902 42.905 25.102 1.00 37.82 ? 350 GLN A CG 1 ATOM 2651 C CD . GLN A 1 332 ? -6.410 42.935 26.556 1.00 46.61 ? 350 GLN A CD 1 ATOM 2652 O OE1 . GLN A 1 332 ? -7.108 43.442 27.441 1.00 48.17 ? 350 GLN A OE1 1 ATOM 2653 N NE2 . GLN A 1 332 ? -5.198 42.382 26.806 1.00 47.34 ? 350 GLN A NE2 1 ATOM 2654 N N . GLN A 1 333 ? -10.071 44.431 23.359 1.00 34.65 ? 351 GLN A N 1 ATOM 2655 C CA . GLN A 1 333 ? -11.429 43.819 23.456 1.00 35.01 ? 351 GLN A CA 1 ATOM 2656 C C . GLN A 1 333 ? -12.049 43.615 22.078 1.00 34.64 ? 351 GLN A C 1 ATOM 2657 O O . GLN A 1 333 ? -12.964 42.808 21.888 1.00 35.67 ? 351 GLN A O 1 ATOM 2658 C CB . GLN A 1 333 ? -12.406 44.693 24.245 1.00 35.65 ? 351 GLN A CB 1 ATOM 2659 C CG . GLN A 1 333 ? -11.961 44.992 25.643 1.00 35.42 ? 351 GLN A CG 1 ATOM 2660 C CD . GLN A 1 333 ? -11.448 46.384 25.761 1.00 35.52 ? 351 GLN A CD 1 ATOM 2661 O OE1 . GLN A 1 333 ? -10.543 46.786 25.039 1.00 34.48 ? 351 GLN A OE1 1 ATOM 2662 N NE2 . GLN A 1 333 ? -12.008 47.138 26.698 1.00 36.90 ? 351 GLN A NE2 1 ATOM 2663 N N . GLY A 1 334 ? -11.549 44.363 21.116 1.00 34.12 ? 352 GLY A N 1 ATOM 2664 C CA . GLY A 1 334 ? -11.988 44.193 19.745 1.00 33.33 ? 352 GLY A CA 1 ATOM 2665 C C . GLY A 1 334 ? -11.890 45.437 18.945 1.00 33.13 ? 352 GLY A C 1 ATOM 2666 O O . GLY A 1 334 ? -11.193 46.377 19.318 1.00 33.47 ? 352 GLY A O 1 ATOM 2667 N N . VAL A 1 335 ? -12.618 45.438 17.833 1.00 32.95 ? 353 VAL A N 1 ATOM 2668 C CA . VAL A 1 335 ? -12.617 46.587 16.936 1.00 33.24 ? 353 VAL A CA 1 ATOM 2669 C C . VAL A 1 335 ? -13.914 47.341 17.079 1.00 33.85 ? 353 VAL A C 1 ATOM 2670 O O . VAL A 1 335 ? -14.975 46.750 17.009 1.00 32.23 ? 353 VAL A O 1 ATOM 2671 C CB . VAL A 1 335 ? -12.449 46.171 15.445 1.00 32.93 ? 353 VAL A CB 1 ATOM 2672 C CG1 . VAL A 1 335 ? -12.575 47.404 14.568 1.00 31.58 ? 353 VAL A CG1 1 ATOM 2673 C CG2 . VAL A 1 335 ? -11.070 45.396 15.208 1.00 33.26 ? 353 VAL A CG2 1 ATOM 2674 N N . PHE A 1 336 ? -13.796 48.645 17.292 1.00 34.87 ? 354 PHE A N 1 ATOM 2675 C CA . PHE A 1 336 ? -14.960 49.520 17.394 1.00 37.05 ? 354 PHE A CA 1 ATOM 2676 C C . PHE A 1 336 ? -15.200 50.190 16.044 1.00 38.01 ? 354 PHE A C 1 ATOM 2677 O O . PHE A 1 336 ? -14.299 50.830 15.478 1.00 36.44 ? 354 PHE A O 1 ATOM 2678 C CB . PHE A 1 336 ? -14.785 50.614 18.466 1.00 37.19 ? 354 PHE A CB 1 ATOM 2679 C CG . PHE A 1 336 ? -14.642 50.076 19.879 1.00 37.50 ? 354 PHE A CG 1 ATOM 2680 C CD1 . PHE A 1 336 ? -15.751 50.004 20.723 1.00 36.72 ? 354 PHE A CD1 1 ATOM 2681 C CD2 . PHE A 1 336 ? -13.395 49.636 20.356 1.00 35.99 ? 354 PHE A CD2 1 ATOM 2682 C CE1 . PHE A 1 336 ? -15.641 49.509 22.005 1.00 37.64 ? 354 PHE A CE1 1 ATOM 2683 C CE2 . PHE A 1 336 ? -13.266 49.121 21.625 1.00 35.06 ? 354 PHE A CE2 1 ATOM 2684 C CZ . PHE A 1 336 ? -14.389 49.065 22.470 1.00 38.96 ? 354 PHE A CZ 1 ATOM 2685 N N . ARG A 1 337 ? -16.440 50.053 15.567 1.00 38.81 ? 355 ARG A N 1 ATOM 2686 C CA . ARG A 1 337 ? -16.804 50.584 14.256 1.00 39.70 ? 355 ARG A CA 1 ATOM 2687 C C . ARG A 1 337 ? -16.999 52.102 14.253 1.00 39.52 ? 355 ARG A C 1 ATOM 2688 O O . ARG A 1 337 ? -16.856 52.735 13.214 1.00 38.20 ? 355 ARG A O 1 ATOM 2689 C CB . ARG A 1 337 ? -18.002 49.840 13.689 1.00 40.74 ? 355 ARG A CB 1 ATOM 2690 C CG . ARG A 1 337 ? -17.649 48.358 13.461 1.00 43.69 ? 355 ARG A CG 1 ATOM 2691 C CD . ARG A 1 337 ? -18.517 47.695 12.389 1.00 47.99 ? 355 ARG A CD 1 ATOM 2692 N NE . ARG A 1 337 ? -18.323 48.314 11.076 1.00 49.33 ? 355 ARG A NE 1 ATOM 2693 C CZ . ARG A 1 337 ? -18.942 47.922 9.970 1.00 50.03 ? 355 ARG A CZ 1 ATOM 2694 N NH1 . ARG A 1 337 ? -19.803 46.910 10.010 1.00 51.50 ? 355 ARG A NH1 1 ATOM 2695 N NH2 . ARG A 1 337 ? -18.695 48.546 8.832 1.00 49.41 ? 355 ARG A NH2 1 ATOM 2696 N N . TYR A 1 338 ? -17.222 52.668 15.445 1.00 39.90 ? 356 TYR A N 1 ATOM 2697 C CA . TYR A 1 338 ? -17.403 54.137 15.628 1.00 40.78 ? 356 TYR A CA 1 ATOM 2698 C C . TYR A 1 338 ? -16.458 54.762 16.659 1.00 40.34 ? 356 TYR A C 1 ATOM 2699 O O . TYR A 1 338 ? -16.140 54.167 17.661 1.00 40.92 ? 356 TYR A O 1 ATOM 2700 C CB . TYR A 1 338 ? -18.864 54.451 16.020 1.00 41.92 ? 356 TYR A CB 1 ATOM 2701 C CG . TYR A 1 338 ? -19.850 53.795 15.076 1.00 43.91 ? 356 TYR A CG 1 ATOM 2702 C CD1 . TYR A 1 338 ? -20.100 54.352 13.819 1.00 48.16 ? 356 TYR A CD1 1 ATOM 2703 C CD2 . TYR A 1 338 ? -20.447 52.589 15.400 1.00 45.42 ? 356 TYR A CD2 1 ATOM 2704 C CE1 . TYR A 1 338 ? -20.974 53.744 12.923 1.00 50.58 ? 356 TYR A CE1 1 ATOM 2705 C CE2 . TYR A 1 338 ? -21.317 51.965 14.526 1.00 50.19 ? 356 TYR A CE2 1 ATOM 2706 C CZ . TYR A 1 338 ? -21.583 52.550 13.285 1.00 53.00 ? 356 TYR A CZ 1 ATOM 2707 O OH . TYR A 1 338 ? -22.457 51.925 12.406 1.00 57.92 ? 356 TYR A OH 1 ATOM 2708 N N . ASP A 1 339 ? -16.060 55.983 16.396 1.00 40.31 ? 357 ASP A N 1 ATOM 2709 C CA . ASP A 1 339 ? -14.976 56.631 17.129 1.00 40.78 ? 357 ASP A CA 1 ATOM 2710 C C . ASP A 1 339 ? -15.485 57.623 18.155 1.00 40.70 ? 357 ASP A C 1 ATOM 2711 O O . ASP A 1 339 ? -14.708 58.417 18.708 1.00 40.78 ? 357 ASP A O 1 ATOM 2712 C CB . ASP A 1 339 ? -13.980 57.327 16.174 1.00 40.78 ? 357 ASP A CB 1 ATOM 2713 C CG . ASP A 1 339 ? -14.557 58.545 15.449 1.00 42.51 ? 357 ASP A CG 1 ATOM 2714 O OD1 . ASP A 1 339 ? -15.668 59.003 15.801 1.00 42.88 ? 357 ASP A OD1 1 ATOM 2715 O OD2 . ASP A 1 339 ? -13.872 59.050 14.518 1.00 43.21 ? 357 ASP A OD2 1 ATOM 2716 N N . ASN A 1 340 ? -16.797 57.590 18.384 1.00 40.77 ? 358 ASN A N 1 ATOM 2717 C CA . ASN A 1 340 ? -17.423 58.590 19.265 1.00 40.54 ? 358 ASN A CA 1 ATOM 2718 C C . ASN A 1 340 ? -17.702 58.130 20.673 1.00 39.39 ? 358 ASN A C 1 ATOM 2719 O O . ASN A 1 340 ? -17.008 58.498 21.598 1.00 38.70 ? 358 ASN A O 1 ATOM 2720 C CB . ASN A 1 340 ? -18.642 59.307 18.629 1.00 41.33 ? 358 ASN A CB 1 ATOM 2721 C CG . ASN A 1 340 ? -19.757 58.370 18.133 1.00 44.21 ? 358 ASN A CG 1 ATOM 2722 O OD1 . ASN A 1 340 ? -19.694 57.126 18.217 1.00 43.12 ? 358 ASN A OD1 1 ATOM 2723 N ND2 . ASN A 1 340 ? -20.812 59.006 17.578 1.00 50.66 ? 358 ASN A ND2 1 ATOM 2724 N N . VAL A 1 341 ? -18.725 57.326 20.823 1.00 39.74 ? 359 VAL A N 1 ATOM 2725 C CA . VAL A 1 341 ? -19.139 56.838 22.134 1.00 40.12 ? 359 VAL A CA 1 ATOM 2726 C C . VAL A 1 341 ? -19.267 55.335 22.220 1.00 40.85 ? 359 VAL A C 1 ATOM 2727 O O . VAL A 1 341 ? -19.635 54.661 21.276 1.00 41.43 ? 359 VAL A O 1 ATOM 2728 C CB . VAL A 1 341 ? -20.488 57.538 22.650 1.00 40.51 ? 359 VAL A CB 1 ATOM 2729 C CG1 . VAL A 1 341 ? -20.238 59.009 22.914 1.00 39.25 ? 359 VAL A CG1 1 ATOM 2730 C CG2 . VAL A 1 341 ? -21.664 57.348 21.644 1.00 40.25 ? 359 VAL A CG2 1 ATOM 2731 N N . SER A 1 342 ? -18.932 54.825 23.404 1.00 41.67 ? 360 SER A N 1 ATOM 2732 C CA . SER A 1 342 ? -19.075 53.400 23.721 1.00 42.18 ? 360 SER A CA 1 ATOM 2733 C C . SER A 1 342 ? -19.446 53.175 25.174 1.00 42.37 ? 360 SER A C 1 ATOM 2734 O O . SER A 1 342 ? -19.512 54.102 25.954 1.00 42.67 ? 360 SER A O 1 ATOM 2735 C CB . SER A 1 342 ? -17.744 52.683 23.449 1.00 42.60 ? 360 SER A CB 1 ATOM 2736 O OG . SER A 1 342 ? -16.699 53.221 24.273 1.00 42.25 ? 360 SER A OG 1 ATOM 2737 N N . SER A 1 343 ? -19.592 51.920 25.544 1.00 43.34 ? 361 SER A N 1 ATOM 2738 C CA . SER A 1 343 ? -19.923 51.586 26.908 1.00 44.59 ? 361 SER A CA 1 ATOM 2739 C C . SER A 1 343 ? -18.796 50.849 27.633 1.00 45.26 ? 361 SER A C 1 ATOM 2740 O O . SER A 1 343 ? -18.909 50.476 28.815 1.00 45.82 ? 361 SER A O 1 ATOM 2741 C CB . SER A 1 343 ? -21.172 50.732 26.939 1.00 45.44 ? 361 SER A CB 1 ATOM 2742 O OG . SER A 1 343 ? -20.939 49.466 26.388 1.00 47.80 ? 361 SER A OG 1 ATOM 2743 N N . VAL A 1 344 ? -17.714 50.623 26.908 1.00 44.95 ? 362 VAL A N 1 ATOM 2744 C CA . VAL A 1 344 ? -16.495 50.119 27.518 1.00 44.09 ? 362 VAL A CA 1 ATOM 2745 C C . VAL A 1 344 ? -15.333 50.969 27.052 1.00 42.44 ? 362 VAL A C 1 ATOM 2746 O O . VAL A 1 344 ? -15.361 51.555 25.972 1.00 42.58 ? 362 VAL A O 1 ATOM 2747 C CB . VAL A 1 344 ? -16.270 48.638 27.201 1.00 45.17 ? 362 VAL A CB 1 ATOM 2748 C CG1 . VAL A 1 344 ? -17.545 47.841 27.486 1.00 45.76 ? 362 VAL A CG1 1 ATOM 2749 C CG2 . VAL A 1 344 ? -15.822 48.438 25.758 1.00 43.70 ? 362 VAL A CG2 1 ATOM 2750 N N . TRP A 1 345 ? -14.346 51.073 27.924 1.00 40.72 ? 363 TRP A N 1 ATOM 2751 C CA . TRP A 1 345 ? -13.108 51.811 27.618 1.00 39.40 ? 363 TRP A CA 1 ATOM 2752 C C . TRP A 1 345 ? -12.155 50.916 26.805 1.00 37.61 ? 363 TRP A C 1 ATOM 2753 O O . TRP A 1 345 ? -11.766 49.828 27.256 1.00 36.28 ? 363 TRP A O 1 ATOM 2754 C CB . TRP A 1 345 ? -12.418 52.283 28.878 1.00 39.10 ? 363 TRP A CB 1 ATOM 2755 C CG . TRP A 1 345 ? -13.210 53.315 29.684 1.00 41.83 ? 363 TRP A CG 1 ATOM 2756 C CD1 . TRP A 1 345 ? -13.903 53.095 30.847 1.00 43.40 ? 363 TRP A CD1 1 ATOM 2757 C CD2 . TRP A 1 345 ? -13.348 54.728 29.405 1.00 43.12 ? 363 TRP A CD2 1 ATOM 2758 N NE1 . TRP A 1 345 ? -14.456 54.279 31.307 1.00 43.93 ? 363 TRP A NE1 1 ATOM 2759 C CE2 . TRP A 1 345 ? -14.129 55.286 30.439 1.00 44.73 ? 363 TRP A CE2 1 ATOM 2760 C CE3 . TRP A 1 345 ? -12.882 55.564 28.393 1.00 41.51 ? 363 TRP A CE3 1 ATOM 2761 C CZ2 . TRP A 1 345 ? -14.463 56.624 30.466 1.00 45.69 ? 363 TRP A CZ2 1 ATOM 2762 C CZ3 . TRP A 1 345 ? -13.201 56.890 28.433 1.00 42.35 ? 363 TRP A CZ3 1 ATOM 2763 C CH2 . TRP A 1 345 ? -13.992 57.409 29.448 1.00 45.04 ? 363 TRP A CH2 1 ATOM 2764 N N . PRO A 1 346 ? -11.802 51.358 25.586 1.00 36.30 ? 364 PRO A N 1 ATOM 2765 C CA . PRO A 1 346 ? -10.863 50.562 24.777 1.00 35.82 ? 364 PRO A CA 1 ATOM 2766 C C . PRO A 1 346 ? -9.529 50.424 25.489 1.00 35.06 ? 364 PRO A C 1 ATOM 2767 O O . PRO A 1 346 ? -8.954 51.405 25.939 1.00 34.26 ? 364 PRO A O 1 ATOM 2768 C CB . PRO A 1 346 ? -10.711 51.374 23.485 1.00 35.90 ? 364 PRO A CB 1 ATOM 2769 C CG . PRO A 1 346 ? -11.915 52.311 23.450 1.00 37.23 ? 364 PRO A CG 1 ATOM 2770 C CD . PRO A 1 346 ? -12.240 52.589 24.904 1.00 36.13 ? 364 PRO A CD 1 ATOM 2771 N N . LEU A 1 347 ? -9.069 49.197 25.578 1.00 34.32 ? 365 LEU A N 1 ATOM 2772 C CA . LEU A 1 347 ? -7.787 48.889 26.195 1.00 34.62 ? 365 LEU A CA 1 ATOM 2773 C C . LEU A 1 347 ? -6.681 48.700 25.146 1.00 33.73 ? 365 LEU A C 1 ATOM 2774 O O . LEU A 1 347 ? -6.884 48.131 24.071 1.00 32.70 ? 365 LEU A O 1 ATOM 2775 C CB . LEU A 1 347 ? -7.904 47.649 27.100 1.00 34.80 ? 365 LEU A CB 1 ATOM 2776 C CG . LEU A 1 347 ? -8.748 47.805 28.385 1.00 37.28 ? 365 LEU A CG 1 ATOM 2777 C CD1 . LEU A 1 347 ? -8.861 46.479 29.173 1.00 37.96 ? 365 LEU A CD1 1 ATOM 2778 C CD2 . LEU A 1 347 ? -8.218 48.930 29.310 1.00 37.33 ? 365 LEU A CD2 1 ATOM 2779 N N . TYR A 1 348 ? -5.511 49.233 25.492 1.00 33.26 ? 366 TYR A N 1 ATOM 2780 C CA . TYR A 1 348 ? -4.327 49.187 24.640 1.00 32.52 ? 366 TYR A CA 1 ATOM 2781 C C . TYR A 1 348 ? -4.676 49.628 23.226 1.00 32.06 ? 366 TYR A C 1 ATOM 2782 O O . TYR A 1 348 ? -4.327 48.987 22.229 1.00 32.61 ? 366 TYR A O 1 ATOM 2783 C CB . TYR A 1 348 ? -3.743 47.764 24.649 1.00 32.27 ? 366 TYR A CB 1 ATOM 2784 C CG . TYR A 1 348 ? -3.342 47.340 26.035 1.00 34.29 ? 366 TYR A CG 1 ATOM 2785 C CD1 . TYR A 1 348 ? -2.367 48.062 26.725 1.00 36.68 ? 366 TYR A CD1 1 ATOM 2786 C CD2 . TYR A 1 348 ? -3.939 46.278 26.671 1.00 36.32 ? 366 TYR A CD2 1 ATOM 2787 C CE1 . TYR A 1 348 ? -1.988 47.724 27.972 1.00 38.67 ? 366 TYR A CE1 1 ATOM 2788 C CE2 . TYR A 1 348 ? -3.553 45.923 27.940 1.00 40.62 ? 366 TYR A CE2 1 ATOM 2789 C CZ . TYR A 1 348 ? -2.563 46.644 28.569 1.00 41.31 ? 366 TYR A CZ 1 ATOM 2790 O OH . TYR A 1 348 ? -2.177 46.325 29.837 1.00 48.35 ? 366 TYR A OH 1 ATOM 2791 N N . SER A 1 349 ? -5.342 50.759 23.131 1.00 31.58 ? 367 SER A N 1 ATOM 2792 C CA . SER A 1 349 ? -6.012 51.119 21.867 1.00 31.95 ? 367 SER A CA 1 ATOM 2793 C C . SER A 1 349 ? -5.076 51.762 20.849 1.00 31.39 ? 367 SER A C 1 ATOM 2794 O O . SER A 1 349 ? -4.029 52.309 21.168 1.00 31.08 ? 367 SER A O 1 ATOM 2795 C CB . SER A 1 349 ? -7.267 51.999 22.154 1.00 31.45 ? 367 SER A CB 1 ATOM 2796 O OG . SER A 1 349 ? -6.857 53.314 22.476 1.00 32.19 ? 367 SER A OG 1 ATOM 2797 N N . TYR A 1 350 ? -5.488 51.634 19.595 1.00 30.65 ? 368 TYR A N 1 ATOM 2798 C CA . TYR A 1 350 ? -4.855 52.309 18.462 1.00 30.77 ? 368 TYR A CA 1 ATOM 2799 C C . TYR A 1 350 ? -5.957 52.837 17.536 1.00 30.93 ? 368 TYR A C 1 ATOM 2800 O O . TYR A 1 350 ? -6.952 52.175 17.306 1.00 30.79 ? 368 TYR A O 1 ATOM 2801 C CB . TYR A 1 350 ? -3.952 51.324 17.708 1.00 30.49 ? 368 TYR A CB 1 ATOM 2802 C CG . TYR A 1 350 ? -3.450 51.844 16.385 1.00 31.18 ? 368 TYR A CG 1 ATOM 2803 C CD1 . TYR A 1 350 ? -2.295 52.561 16.293 1.00 28.54 ? 368 TYR A CD1 1 ATOM 2804 C CD2 . TYR A 1 350 ? -4.154 51.569 15.207 1.00 31.81 ? 368 TYR A CD2 1 ATOM 2805 C CE1 . TYR A 1 350 ? -1.854 53.021 15.053 1.00 31.93 ? 368 TYR A CE1 1 ATOM 2806 C CE2 . TYR A 1 350 ? -3.745 52.011 14.005 1.00 29.00 ? 368 TYR A CE2 1 ATOM 2807 C CZ . TYR A 1 350 ? -2.587 52.732 13.911 1.00 31.95 ? 368 TYR A CZ 1 ATOM 2808 O OH . TYR A 1 350 ? -2.202 53.162 12.669 1.00 30.24 ? 368 TYR A OH 1 ATOM 2809 N N . GLY A 1 351 ? -5.774 54.057 17.078 1.00 32.03 ? 369 GLY A N 1 ATOM 2810 C CA . GLY A 1 351 ? -6.706 54.724 16.180 1.00 33.52 ? 369 GLY A CA 1 ATOM 2811 C C . GLY A 1 351 ? -7.555 55.730 16.920 1.00 34.89 ? 369 GLY A C 1 ATOM 2812 O O . GLY A 1 351 ? -7.232 56.170 18.030 1.00 35.10 ? 369 GLY A O 1 ATOM 2813 N N . ARG A 1 352 ? -8.688 56.053 16.304 1.00 35.63 ? 370 ARG A N 1 ATOM 2814 C CA . ARG A 1 352 ? -9.617 57.069 16.801 1.00 35.40 ? 370 ARG A CA 1 ATOM 2815 C C . ARG A 1 352 ? -10.675 56.338 17.572 1.00 35.51 ? 370 ARG A C 1 ATOM 2816 O O . ARG A 1 352 ? -11.549 55.673 17.022 1.00 35.12 ? 370 ARG A O 1 ATOM 2817 C CB . ARG A 1 352 ? -10.253 57.847 15.649 1.00 36.08 ? 370 ARG A CB 1 ATOM 2818 C CG . ARG A 1 352 ? -9.248 58.626 14.825 1.00 37.20 ? 370 ARG A CG 1 ATOM 2819 C CD . ARG A 1 352 ? -9.934 59.453 13.735 1.00 42.47 ? 370 ARG A CD 1 ATOM 2820 N NE . ARG A 1 352 ? -10.873 58.629 12.976 1.00 47.90 ? 370 ARG A NE 1 ATOM 2821 C CZ . ARG A 1 352 ? -10.521 57.881 11.928 1.00 48.70 ? 370 ARG A CZ 1 ATOM 2822 N NH1 . ARG A 1 352 ? -9.273 57.909 11.477 1.00 48.68 ? 370 ARG A NH1 1 ATOM 2823 N NH2 . ARG A 1 352 ? -11.418 57.135 11.311 1.00 49.17 ? 370 ARG A NH2 1 ATOM 2824 N N . CYS A 1 353 ? -10.572 56.449 18.881 1.00 35.19 ? 371 CYS A N 1 ATOM 2825 C CA . CYS A 1 353 ? -11.325 55.595 19.752 1.00 34.67 ? 371 CYS A CA 1 ATOM 2826 C C . CYS A 1 353 ? -12.389 56.359 20.541 1.00 35.16 ? 371 CYS A C 1 ATOM 2827 O O . CYS A 1 353 ? -12.227 57.517 20.883 1.00 33.60 ? 371 CYS A O 1 ATOM 2828 C CB . CYS A 1 353 ? -10.372 54.856 20.698 1.00 34.74 ? 371 CYS A CB 1 ATOM 2829 S SG . CYS A 1 353 ? -9.409 53.566 19.855 1.00 32.64 ? 371 CYS A SG 1 ATOM 2830 N N . PRO A 1 354 ? -13.488 55.679 20.820 1.00 35.90 ? 372 PRO A N 1 ATOM 2831 C CA . PRO A 1 354 ? -14.599 56.249 21.537 1.00 37.70 ? 372 PRO A CA 1 ATOM 2832 C C . PRO A 1 354 ? -14.361 56.406 23.042 1.00 39.00 ? 372 PRO A C 1 ATOM 2833 O O . PRO A 1 354 ? -13.604 55.649 23.672 1.00 39.08 ? 372 PRO A O 1 ATOM 2834 C CB . PRO A 1 354 ? -15.691 55.199 21.319 1.00 37.73 ? 372 PRO A CB 1 ATOM 2835 C CG . PRO A 1 354 ? -14.879 53.879 21.319 1.00 36.95 ? 372 PRO A CG 1 ATOM 2836 C CD . PRO A 1 354 ? -13.719 54.271 20.458 1.00 36.22 ? 372 PRO A CD 1 ATOM 2837 N N . THR A 1 355 ? -15.071 57.372 23.602 1.00 39.36 ? 373 THR A N 1 ATOM 2838 C CA . THR A 1 355 ? -15.190 57.499 25.049 1.00 40.42 ? 373 THR A CA 1 ATOM 2839 C C . THR A 1 355 ? -16.330 56.664 25.613 1.00 41.49 ? 373 THR A C 1 ATOM 2840 O O . THR A 1 355 ? -17.402 56.527 25.017 1.00 41.64 ? 373 THR A O 1 ATOM 2841 C CB . THR A 1 355 ? -15.392 58.959 25.494 1.00 40.52 ? 373 THR A CB 1 ATOM 2842 O OG1 . THR A 1 355 ? -15.325 59.019 26.926 1.00 40.23 ? 373 THR A OG1 1 ATOM 2843 C CG2 . THR A 1 355 ? -16.735 59.508 24.998 1.00 40.25 ? 373 THR A CG2 1 ATOM 2844 N N . ALA A 1 356 ? -16.086 56.118 26.791 1.00 42.93 ? 374 ALA A N 1 ATOM 2845 C CA . ALA A 1 356 ? -17.116 55.408 27.548 1.00 43.71 ? 374 ALA A CA 1 ATOM 2846 C C . ALA A 1 356 ? -17.682 56.361 28.624 1.00 45.49 ? 374 ALA A C 1 ATOM 2847 O O . ALA A 1 356 ? -18.403 55.947 29.507 1.00 45.05 ? 374 ALA A O 1 ATOM 2848 C CB . ALA A 1 356 ? -16.557 54.149 28.174 1.00 42.70 ? 374 ALA A CB 1 ATOM 2849 N N . ALA A 1 357 ? -17.323 57.638 28.538 1.00 47.84 ? 375 ALA A N 1 ATOM 2850 C CA . ALA A 1 357 ? -17.875 58.653 29.455 1.00 49.97 ? 375 ALA A CA 1 ATOM 2851 C C . ALA A 1 357 ? -19.372 59.014 29.150 1.00 52.29 ? 375 ALA A C 1 ATOM 2852 O O . ALA A 1 357 ? -19.976 58.623 28.153 1.00 52.28 ? 375 ALA A O 1 ATOM 2853 C CB . ALA A 1 357 ? -17.008 59.913 29.457 1.00 48.86 ? 375 ALA A CB 1 ATOM 2854 N N . ASP A 1 358 ? -19.956 59.780 30.052 1.00 55.35 ? 376 ASP A N 1 ATOM 2855 C CA . ASP A 1 358 ? -21.373 60.237 29.897 1.00 57.19 ? 376 ASP A CA 1 ATOM 2856 C C . ASP A 1 358 ? -21.751 60.878 28.553 1.00 57.01 ? 376 ASP A C 1 ATOM 2857 O O . ASP A 1 358 ? -21.594 62.081 28.360 1.00 57.60 ? 376 ASP A O 1 ATOM 2858 C CB . ASP A 1 358 ? -21.717 61.175 31.023 1.00 58.20 ? 376 ASP A CB 1 ATOM 2859 C CG . ASP A 1 358 ? -21.963 60.417 32.300 1.00 63.16 ? 376 ASP A CG 1 ATOM 2860 O OD1 . ASP A 1 358 ? -22.032 59.154 32.192 1.00 69.16 ? 376 ASP A OD1 1 ATOM 2861 O OD2 . ASP A 1 358 ? -22.078 61.046 33.390 1.00 69.62 ? 376 ASP A OD2 1 HETATM 2862 C C1 . NAG B 2 . ? -1.238 28.022 26.261 1.00 51.70 ? 1961 NAG A C1 1 HETATM 2863 C C2 . NAG B 2 . ? -1.794 29.027 27.270 1.00 54.02 ? 1961 NAG A C2 1 HETATM 2864 C C3 . NAG B 2 . ? -1.080 28.836 28.614 1.00 57.30 ? 1961 NAG A C3 1 HETATM 2865 C C4 . NAG B 2 . ? -1.260 27.389 29.104 1.00 59.03 ? 1961 NAG A C4 1 HETATM 2866 C C5 . NAG B 2 . ? -0.724 26.463 28.020 1.00 58.86 ? 1961 NAG A C5 1 HETATM 2867 C C6 . NAG B 2 . ? -0.978 25.029 28.444 1.00 60.32 ? 1961 NAG A C6 1 HETATM 2868 C C7 . NAG B 2 . ? -2.416 31.102 26.083 1.00 50.20 ? 1961 NAG A C7 1 HETATM 2869 C C8 . NAG B 2 . ? -1.985 32.530 25.811 1.00 47.72 ? 1961 NAG A C8 1 HETATM 2870 N N2 . NAG B 2 . ? -1.593 30.410 26.862 1.00 51.83 ? 1961 NAG A N2 1 HETATM 2871 O O3 . NAG B 2 . ? -1.621 29.776 29.525 1.00 56.79 ? 1961 NAG A O3 1 HETATM 2872 O O4 . NAG B 2 . ? -0.664 27.111 30.377 1.00 59.99 ? 1961 NAG A O4 1 HETATM 2873 O O5 . NAG B 2 . ? -1.352 26.699 26.763 1.00 55.54 ? 1961 NAG A O5 1 HETATM 2874 O O6 . NAG B 2 . ? -0.169 24.224 27.622 1.00 62.26 ? 1961 NAG A O6 1 HETATM 2875 O O7 . NAG B 2 . ? -3.440 30.625 25.591 1.00 49.85 ? 1961 NAG A O7 1 HETATM 2876 C C1 . NAG C 2 . ? 11.626 37.380 -1.626 1.00 31.21 ? 2523 NAG A C1 1 HETATM 2877 C C2 . NAG C 2 . ? 13.064 37.120 -2.064 1.00 30.98 ? 2523 NAG A C2 1 HETATM 2878 C C3 . NAG C 2 . ? 13.894 38.394 -1.995 1.00 33.50 ? 2523 NAG A C3 1 HETATM 2879 C C4 . NAG C 2 . ? 13.261 39.493 -2.785 1.00 34.41 ? 2523 NAG A C4 1 HETATM 2880 C C5 . NAG C 2 . ? 11.821 39.608 -2.299 1.00 33.39 ? 2523 NAG A C5 1 HETATM 2881 C C6 . NAG C 2 . ? 11.083 40.723 -3.012 1.00 34.92 ? 2523 NAG A C6 1 HETATM 2882 C C7 . NAG C 2 . ? 14.062 34.953 -1.558 1.00 32.68 ? 2523 NAG A C7 1 HETATM 2883 C C8 . NAG C 2 . ? 13.772 34.504 -2.921 1.00 29.46 ? 2523 NAG A C8 1 HETATM 2884 N N2 . NAG C 2 . ? 13.705 36.176 -1.231 1.00 29.96 ? 2523 NAG A N2 1 HETATM 2885 O O3 . NAG C 2 . ? 15.162 38.109 -2.480 1.00 33.28 ? 2523 NAG A O3 1 HETATM 2886 O O4 . NAG C 2 . ? 13.990 40.662 -2.539 1.00 38.58 ? 2523 NAG A O4 1 HETATM 2887 O O5 . NAG C 2 . ? 11.141 38.376 -2.500 1.00 29.91 ? 2523 NAG A O5 1 HETATM 2888 O O6 . NAG C 2 . ? 11.151 40.470 -4.384 1.00 38.30 ? 2523 NAG A O6 1 HETATM 2889 O O7 . NAG C 2 . ? 14.647 34.214 -0.746 1.00 39.63 ? 2523 NAG A O7 1 HETATM 2890 C C1 . NAG D 2 . ? 30.469 26.166 25.460 1.00 34.84 ? 2525 NAG A C1 1 HETATM 2891 C C2 . NAG D 2 . ? 31.443 26.618 26.550 1.00 37.70 ? 2525 NAG A C2 1 HETATM 2892 C C3 . NAG D 2 . ? 32.892 26.433 26.085 1.00 38.85 ? 2525 NAG A C3 1 HETATM 2893 C C4 . NAG D 2 . ? 33.109 25.032 25.554 1.00 39.77 ? 2525 NAG A C4 1 HETATM 2894 C C5 . NAG D 2 . ? 32.104 24.746 24.444 1.00 39.44 ? 2525 NAG A C5 1 HETATM 2895 C C6 . NAG D 2 . ? 32.328 23.397 23.773 1.00 37.91 ? 2525 NAG A C6 1 HETATM 2896 C C7 . NAG D 2 . ? 31.056 28.629 27.911 1.00 38.61 ? 2525 NAG A C7 1 HETATM 2897 C C8 . NAG D 2 . ? 31.086 27.708 29.057 1.00 35.71 ? 2525 NAG A C8 1 HETATM 2898 N N2 . NAG D 2 . ? 31.221 28.041 26.740 1.00 37.57 ? 2525 NAG A N2 1 HETATM 2899 O O3 . NAG D 2 . ? 33.855 26.752 27.088 1.00 38.00 ? 2525 NAG A O3 1 HETATM 2900 O O4 . NAG D 2 . ? 34.418 25.065 25.029 1.00 41.77 ? 2525 NAG A O4 1 HETATM 2901 O O5 . NAG D 2 . ? 30.787 24.855 24.965 1.00 37.08 ? 2525 NAG A O5 1 HETATM 2902 O O6 . NAG D 2 . ? 31.988 22.319 24.621 1.00 33.94 ? 2525 NAG A O6 1 HETATM 2903 O O7 . NAG D 2 . ? 30.859 29.865 28.042 1.00 44.15 ? 2525 NAG A O7 1 HETATM 2904 C C1 . NAG E 2 . ? 35.127 23.867 25.383 1.00 46.46 ? 2526 NAG A C1 1 HETATM 2905 C C2 . NAG E 2 . ? 36.496 23.926 24.749 1.00 47.72 ? 2526 NAG A C2 1 HETATM 2906 C C3 . NAG E 2 . ? 37.269 22.632 25.072 1.00 49.26 ? 2526 NAG A C3 1 HETATM 2907 C C4 . NAG E 2 . ? 37.323 22.375 26.576 1.00 51.53 ? 2526 NAG A C4 1 HETATM 2908 C C5 . NAG E 2 . ? 35.969 22.606 27.246 1.00 50.68 ? 2526 NAG A C5 1 HETATM 2909 C C6 . NAG E 2 . ? 36.213 22.891 28.720 1.00 51.09 ? 2526 NAG A C6 1 HETATM 2910 C C7 . NAG E 2 . ? 36.575 25.111 22.577 1.00 46.15 ? 2526 NAG A C7 1 HETATM 2911 C C8 . NAG E 2 . ? 37.010 26.362 23.260 1.00 47.88 ? 2526 NAG A C8 1 HETATM 2912 N N2 . NAG E 2 . ? 36.345 24.039 23.309 1.00 45.69 ? 2526 NAG A N2 1 HETATM 2913 O O3 . NAG E 2 . ? 38.589 22.732 24.582 1.00 47.97 ? 2526 NAG A O3 1 HETATM 2914 O O4 . NAG E 2 . ? 37.734 21.050 26.873 1.00 55.26 ? 2526 NAG A O4 1 HETATM 2915 O O5 . NAG E 2 . ? 35.295 23.744 26.774 1.00 48.67 ? 2526 NAG A O5 1 HETATM 2916 O O6 . NAG E 2 . ? 35.117 22.301 29.361 1.00 53.42 ? 2526 NAG A O6 1 HETATM 2917 O O7 . NAG E 2 . ? 36.441 25.054 21.341 1.00 49.67 ? 2526 NAG A O7 1 HETATM 2918 C C1 . NAG F 2 . ? -21.957 58.271 17.062 1.00 55.70 ? 2527 NAG A C1 1 HETATM 2919 C C2 . NAG F 2 . ? -23.192 59.119 17.352 1.00 58.53 ? 2527 NAG A C2 1 HETATM 2920 C C3 . NAG F 2 . ? -24.400 58.349 16.852 1.00 60.62 ? 2527 NAG A C3 1 HETATM 2921 C C4 . NAG F 2 . ? -24.274 58.140 15.352 1.00 61.57 ? 2527 NAG A C4 1 HETATM 2922 C C5 . NAG F 2 . ? -22.989 57.343 15.114 1.00 60.61 ? 2527 NAG A C5 1 HETATM 2923 C C6 . NAG F 2 . ? -22.745 57.217 13.632 1.00 61.08 ? 2527 NAG A C6 1 HETATM 2924 C C7 . NAG F 2 . ? -22.966 60.465 19.368 1.00 54.54 ? 2527 NAG A C7 1 HETATM 2925 C C8 . NAG F 2 . ? -22.227 61.508 18.599 1.00 55.75 ? 2527 NAG A C8 1 HETATM 2926 N N2 . NAG F 2 . ? -23.391 59.377 18.765 1.00 56.34 ? 2527 NAG A N2 1 HETATM 2927 O O3 . NAG F 2 . ? -25.538 59.095 17.191 1.00 62.73 ? 2527 NAG A O3 1 HETATM 2928 O O4 . NAG F 2 . ? -25.426 57.483 14.861 1.00 63.07 ? 2527 NAG A O4 1 HETATM 2929 O O5 . NAG F 2 . ? -21.877 58.037 15.668 1.00 57.23 ? 2527 NAG A O5 1 HETATM 2930 O O6 . NAG F 2 . ? -22.389 58.505 13.172 1.00 61.21 ? 2527 NAG A O6 1 HETATM 2931 O O7 . NAG F 2 . ? -23.184 60.615 20.554 1.00 56.81 ? 2527 NAG A O7 1 HETATM 2932 C C1 . NAG G 2 . ? -9.691 29.617 20.353 1.00 36.42 ? 2521 NAG A C1 1 HETATM 2933 C C2 . NAG G 2 . ? -8.774 28.973 21.381 1.00 39.30 ? 2521 NAG A C2 1 HETATM 2934 C C3 . NAG G 2 . ? -9.167 27.516 21.579 1.00 40.41 ? 2521 NAG A C3 1 HETATM 2935 C C4 . NAG G 2 . ? -10.638 27.317 21.921 1.00 41.66 ? 2521 NAG A C4 1 HETATM 2936 C C5 . NAG G 2 . ? -11.408 28.009 20.824 1.00 39.29 ? 2521 NAG A C5 1 HETATM 2937 C C6 . NAG G 2 . ? -12.906 27.873 21.038 1.00 40.22 ? 2521 NAG A C6 1 HETATM 2938 C C7 . NAG G 2 . ? -6.445 29.715 21.656 1.00 39.92 ? 2521 NAG A C7 1 HETATM 2939 C C8 . NAG G 2 . ? -5.050 29.723 21.111 1.00 34.07 ? 2521 NAG A C8 1 HETATM 2940 N N2 . NAG G 2 . ? -7.378 29.032 20.979 1.00 37.67 ? 2521 NAG A N2 1 HETATM 2941 O O3 . NAG G 2 . ? -8.388 26.993 22.609 1.00 40.53 ? 2521 NAG A O3 1 HETATM 2942 O O4 . NAG G 2 . ? -10.907 25.912 22.015 1.00 41.46 ? 2521 NAG A O4 1 HETATM 2943 O O5 . NAG G 2 . ? -11.026 29.366 20.768 1.00 37.26 ? 2521 NAG A O5 1 HETATM 2944 O O6 . NAG G 2 . ? -13.254 28.579 22.195 1.00 41.56 ? 2521 NAG A O6 1 HETATM 2945 O O7 . NAG G 2 . ? -6.694 30.327 22.689 1.00 41.64 ? 2521 NAG A O7 1 HETATM 2946 C C1 . NAG H 2 . ? -18.107 25.076 -3.463 1.00 64.14 ? 2520 NAG A C1 1 HETATM 2947 C C2 . NAG H 2 . ? -19.365 24.905 -4.324 1.00 69.26 ? 2520 NAG A C2 1 HETATM 2948 C C3 . NAG H 2 . ? -20.646 24.609 -3.512 1.00 70.57 ? 2520 NAG A C3 1 HETATM 2949 C C4 . NAG H 2 . ? -20.428 24.244 -2.035 1.00 69.58 ? 2520 NAG A C4 1 HETATM 2950 C C5 . NAG H 2 . ? -19.019 24.509 -1.492 1.00 66.88 ? 2520 NAG A C5 1 HETATM 2951 C C6 . NAG H 2 . ? -18.790 23.704 -0.229 1.00 66.00 ? 2520 NAG A C6 1 HETATM 2952 C C7 . NAG H 2 . ? -19.578 25.947 -6.519 1.00 71.91 ? 2520 NAG A C7 1 HETATM 2953 C C8 . NAG H 2 . ? -19.897 27.201 -7.306 1.00 72.13 ? 2520 NAG A C8 1 HETATM 2954 N N2 . NAG H 2 . ? -19.632 26.053 -5.192 1.00 69.91 ? 2520 NAG A N2 1 HETATM 2955 O O3 . NAG H 2 . ? -21.349 23.537 -4.132 1.00 72.39 ? 2520 NAG A O3 1 HETATM 2956 O O4 . NAG H 2 . ? -21.389 24.925 -1.257 1.00 70.22 ? 2520 NAG A O4 1 HETATM 2957 O O5 . NAG H 2 . ? -18.071 24.107 -2.450 1.00 64.39 ? 2520 NAG A O5 1 HETATM 2958 O O6 . NAG H 2 . ? -18.564 22.377 -0.663 1.00 66.94 ? 2520 NAG A O6 1 HETATM 2959 O O7 . NAG H 2 . ? -19.265 24.888 -7.083 1.00 73.35 ? 2520 NAG A O7 1 HETATM 2960 K K . K I 3 . ? 27.476 23.700 16.919 1.00 32.53 ? 2 K A K 1 HETATM 2961 O O . HOH J 4 . ? 0.682 34.132 12.645 1.00 22.18 ? 2528 HOH A O 1 HETATM 2962 O O . HOH J 4 . ? -0.442 28.245 8.288 1.00 26.31 ? 2529 HOH A O 1 HETATM 2963 O O . HOH J 4 . ? 14.334 33.734 20.860 1.00 26.30 ? 2530 HOH A O 1 HETATM 2964 O O . HOH J 4 . ? 25.508 43.060 16.854 1.00 26.02 ? 2531 HOH A O 1 HETATM 2965 O O . HOH J 4 . ? 22.318 27.781 14.753 1.00 26.64 ? 2532 HOH A O 1 HETATM 2966 O O . HOH J 4 . ? -8.549 43.446 15.335 1.00 22.02 ? 2533 HOH A O 1 HETATM 2967 O O . HOH J 4 . ? -2.495 45.668 12.562 1.00 23.27 ? 2534 HOH A O 1 HETATM 2968 O O . HOH J 4 . ? 11.798 35.070 20.773 1.00 23.62 ? 2535 HOH A O 1 HETATM 2969 O O . HOH J 4 . ? -3.237 48.403 14.911 1.00 26.42 ? 2536 HOH A O 1 HETATM 2970 O O . HOH J 4 . ? 16.084 19.712 24.135 1.00 33.24 ? 2537 HOH A O 1 HETATM 2971 O O . HOH J 4 . ? 13.284 24.966 22.173 1.00 31.67 ? 2538 HOH A O 1 HETATM 2972 O O . HOH J 4 . ? -7.859 29.055 12.372 1.00 31.72 ? 2539 HOH A O 1 HETATM 2973 O O . HOH J 4 . ? -4.844 32.235 5.942 1.00 26.59 ? 2540 HOH A O 1 HETATM 2974 O O . HOH J 4 . ? 3.641 27.895 11.849 1.00 25.86 ? 2541 HOH A O 1 HETATM 2975 O O . HOH J 4 . ? -14.277 37.035 5.508 1.00 27.69 ? 2542 HOH A O 1 HETATM 2976 O O . HOH J 4 . ? -12.654 38.823 4.382 1.00 35.58 ? 2543 HOH A O 1 HETATM 2977 O O . HOH J 4 . ? 1.325 46.742 12.236 1.00 25.76 ? 2544 HOH A O 1 HETATM 2978 O O . HOH J 4 . ? 5.133 20.107 14.142 1.00 31.47 ? 2545 HOH A O 1 HETATM 2979 O O . HOH J 4 . ? -2.045 31.985 14.505 1.00 32.10 ? 2546 HOH A O 1 HETATM 2980 O O . HOH J 4 . ? 24.790 38.723 23.473 1.00 28.73 ? 2547 HOH A O 1 HETATM 2981 O O . HOH J 4 . ? -5.147 29.677 9.214 1.00 31.30 ? 2548 HOH A O 1 HETATM 2982 O O . HOH J 4 . ? 24.486 24.163 16.747 1.00 26.54 ? 2549 HOH A O 1 HETATM 2983 O O . HOH J 4 . ? 26.641 45.497 12.549 1.00 30.12 ? 2550 HOH A O 1 HETATM 2984 O O . HOH J 4 . ? 30.604 20.695 11.573 1.00 30.36 ? 2551 HOH A O 1 HETATM 2985 O O . HOH J 4 . ? 14.335 27.567 1.454 1.00 26.83 ? 2552 HOH A O 1 HETATM 2986 O O . HOH J 4 . ? 18.474 19.568 8.215 1.00 32.49 ? 2553 HOH A O 1 HETATM 2987 O O . HOH J 4 . ? 10.481 20.832 3.895 1.00 35.75 ? 2554 HOH A O 1 HETATM 2988 O O . HOH J 4 . ? 20.671 24.600 3.990 1.00 31.48 ? 2555 HOH A O 1 HETATM 2989 O O . HOH J 4 . ? 3.362 36.724 -1.991 1.00 31.88 ? 2556 HOH A O 1 HETATM 2990 O O . HOH J 4 . ? -16.558 37.468 14.513 1.00 34.38 ? 2557 HOH A O 1 HETATM 2991 O O . HOH J 4 . ? 4.829 55.652 10.620 1.00 28.80 ? 2558 HOH A O 1 HETATM 2992 O O . HOH J 4 . ? 19.403 22.192 7.950 1.00 30.63 ? 2559 HOH A O 1 HETATM 2993 O O . HOH J 4 . ? 11.484 43.595 4.056 1.00 23.54 ? 2560 HOH A O 1 HETATM 2994 O O . HOH J 4 . ? 7.798 31.996 -3.100 1.00 33.58 ? 2561 HOH A O 1 HETATM 2995 O O . HOH J 4 . ? -1.423 48.791 21.889 1.00 32.07 ? 2562 HOH A O 1 HETATM 2996 O O . HOH J 4 . ? 14.381 27.337 22.346 1.00 25.11 ? 2563 HOH A O 1 HETATM 2997 O O . HOH J 4 . ? 34.690 19.577 10.947 1.00 36.31 ? 2564 HOH A O 1 HETATM 2998 O O . HOH J 4 . ? 6.785 54.767 17.627 1.00 41.77 ? 2565 HOH A O 1 HETATM 2999 O O . HOH J 4 . ? -1.354 28.353 -4.098 1.00 28.96 ? 2566 HOH A O 1 HETATM 3000 O O . HOH J 4 . ? 20.922 47.179 9.575 1.00 28.87 ? 2567 HOH A O 1 HETATM 3001 O O . HOH J 4 . ? 32.719 20.902 9.701 1.00 34.72 ? 2568 HOH A O 1 HETATM 3002 O O . HOH J 4 . ? -10.713 23.902 15.833 1.00 34.56 ? 2569 HOH A O 1 HETATM 3003 O O . HOH J 4 . ? 31.831 22.026 16.208 1.00 31.81 ? 2570 HOH A O 1 HETATM 3004 O O . HOH J 4 . ? -14.263 28.511 14.321 1.00 37.30 ? 2571 HOH A O 1 HETATM 3005 O O . HOH J 4 . ? -1.105 50.425 24.294 1.00 34.99 ? 2572 HOH A O 1 HETATM 3006 O O . HOH J 4 . ? -0.796 28.435 14.636 1.00 29.63 ? 2573 HOH A O 1 HETATM 3007 O O . HOH J 4 . ? 25.170 47.595 13.872 1.00 35.05 ? 2574 HOH A O 1 HETATM 3008 O O . HOH J 4 . ? -19.440 37.411 0.010 1.00 31.65 ? 2575 HOH A O 1 HETATM 3009 O O . HOH J 4 . ? -16.272 34.933 14.948 1.00 41.62 ? 2576 HOH A O 1 HETATM 3010 O O . HOH J 4 . ? -18.615 48.786 17.180 1.00 37.32 ? 2577 HOH A O 1 HETATM 3011 O O . HOH J 4 . ? -2.344 30.186 18.686 1.00 27.05 ? 2578 HOH A O 1 HETATM 3012 O O . HOH J 4 . ? 22.480 33.731 22.551 1.00 25.18 ? 2579 HOH A O 1 HETATM 3013 O O . HOH J 4 . ? 23.615 39.644 2.407 1.00 33.63 ? 2580 HOH A O 1 HETATM 3014 O O . HOH J 4 . ? 17.460 36.720 -0.944 1.00 36.34 ? 2581 HOH A O 1 HETATM 3015 O O . HOH J 4 . ? -6.056 52.542 25.446 1.00 44.55 ? 2582 HOH A O 1 HETATM 3016 O O . HOH J 4 . ? 7.472 46.074 19.261 1.00 36.80 ? 2583 HOH A O 1 HETATM 3017 O O . HOH J 4 . ? 3.479 44.920 -0.278 1.00 32.81 ? 2584 HOH A O 1 HETATM 3018 O O . HOH J 4 . ? -18.334 26.677 9.609 1.00 37.79 ? 2585 HOH A O 1 HETATM 3019 O O . HOH J 4 . ? 13.467 25.704 -0.433 1.00 29.16 ? 2586 HOH A O 1 HETATM 3020 O O . HOH J 4 . ? -0.663 47.557 1.765 1.00 37.35 ? 2587 HOH A O 1 HETATM 3021 O O . HOH J 4 . ? -9.578 43.150 -4.460 1.00 35.17 ? 2588 HOH A O 1 HETATM 3022 O O . HOH J 4 . ? 34.545 41.244 7.993 1.00 33.10 ? 2589 HOH A O 1 HETATM 3023 O O . HOH J 4 . ? 13.865 52.204 7.956 1.00 33.93 ? 2590 HOH A O 1 HETATM 3024 O O . HOH J 4 . ? -0.411 51.237 20.710 1.00 42.35 ? 2591 HOH A O 1 HETATM 3025 O O . HOH J 4 . ? 7.033 34.717 23.908 1.00 31.23 ? 2592 HOH A O 1 HETATM 3026 O O . HOH J 4 . ? -17.723 42.296 9.753 1.00 34.75 ? 2593 HOH A O 1 HETATM 3027 O O . HOH J 4 . ? 5.804 38.637 24.816 1.00 36.73 ? 2594 HOH A O 1 HETATM 3028 O O . HOH J 4 . ? -0.452 28.732 17.389 1.00 27.58 ? 2595 HOH A O 1 HETATM 3029 O O . HOH J 4 . ? 10.586 35.441 -4.497 1.00 40.12 ? 2596 HOH A O 1 HETATM 3030 O O . HOH J 4 . ? 23.147 25.547 2.932 1.00 30.44 ? 2597 HOH A O 1 HETATM 3031 O O . HOH J 4 . ? 7.070 16.261 22.633 1.00 51.27 ? 2598 HOH A O 1 HETATM 3032 O O . HOH J 4 . ? 6.941 14.675 20.759 1.00 46.37 ? 2599 HOH A O 1 HETATM 3033 O O . HOH J 4 . ? 29.505 43.883 10.884 1.00 31.48 ? 2600 HOH A O 1 HETATM 3034 O O . HOH J 4 . ? -4.472 51.089 8.468 1.00 34.07 ? 2601 HOH A O 1 HETATM 3035 O O . HOH J 4 . ? -2.541 52.529 9.996 1.00 31.36 ? 2602 HOH A O 1 HETATM 3036 O O . HOH J 4 . ? 24.018 18.465 22.388 1.00 33.35 ? 2603 HOH A O 1 HETATM 3037 O O . HOH J 4 . ? -8.697 48.519 2.138 1.00 40.16 ? 2604 HOH A O 1 HETATM 3038 O O . HOH J 4 . ? 28.987 24.744 28.448 1.00 36.97 ? 2605 HOH A O 1 HETATM 3039 O O . HOH J 4 . ? -2.018 33.797 12.586 1.00 42.59 ? 2606 HOH A O 1 HETATM 3040 O O . HOH J 4 . ? -16.496 36.992 3.955 1.00 30.45 ? 2607 HOH A O 1 HETATM 3041 O O . HOH J 4 . ? -11.187 37.261 19.653 1.00 34.18 ? 2608 HOH A O 1 HETATM 3042 O O . HOH J 4 . ? -17.954 40.591 17.305 1.00 39.18 ? 2609 HOH A O 1 HETATM 3043 O O . HOH J 4 . ? 24.898 20.665 16.005 1.00 34.41 ? 2610 HOH A O 1 HETATM 3044 O O . HOH J 4 . ? 3.486 40.806 -1.821 1.00 36.70 ? 2611 HOH A O 1 HETATM 3045 O O . HOH J 4 . ? -2.226 25.968 -4.332 1.00 35.29 ? 2612 HOH A O 1 HETATM 3046 O O . HOH J 4 . ? 9.529 52.978 15.367 1.00 29.57 ? 2613 HOH A O 1 HETATM 3047 O O . HOH J 4 . ? 20.746 22.006 3.984 1.00 34.49 ? 2614 HOH A O 1 HETATM 3048 O O . HOH J 4 . ? 19.912 33.691 22.749 1.00 43.85 ? 2615 HOH A O 1 HETATM 3049 O O . HOH J 4 . ? -2.488 40.333 -2.920 1.00 37.71 ? 2616 HOH A O 1 HETATM 3050 O O . HOH J 4 . ? -4.637 50.517 27.976 1.00 38.06 ? 2617 HOH A O 1 HETATM 3051 O O . HOH J 4 . ? 12.429 41.889 19.124 1.00 32.45 ? 2618 HOH A O 1 HETATM 3052 O O . HOH J 4 . ? -17.882 24.698 18.554 1.00 42.89 ? 2619 HOH A O 1 HETATM 3053 O O . HOH J 4 . ? 25.441 44.986 5.486 1.00 41.04 ? 2620 HOH A O 1 HETATM 3054 O O . HOH J 4 . ? 25.518 30.640 0.595 1.00 41.54 ? 2621 HOH A O 1 HETATM 3055 O O . HOH J 4 . ? -0.113 49.961 1.848 1.00 41.16 ? 2622 HOH A O 1 HETATM 3056 O O . HOH J 4 . ? 12.593 12.735 12.710 1.00 43.92 ? 2623 HOH A O 1 HETATM 3057 O O . HOH J 4 . ? 24.029 19.351 27.600 1.00 38.18 ? 2624 HOH A O 1 HETATM 3058 O O . HOH J 4 . ? -9.681 50.861 2.939 1.00 28.82 ? 2625 HOH A O 1 HETATM 3059 O O . HOH J 4 . ? 21.556 21.451 6.595 1.00 32.01 ? 2626 HOH A O 1 HETATM 3060 O O . HOH J 4 . ? -3.771 55.932 17.716 1.00 32.83 ? 2627 HOH A O 1 HETATM 3061 O O . HOH J 4 . ? -1.648 53.196 19.837 1.00 39.91 ? 2628 HOH A O 1 HETATM 3062 O O . HOH J 4 . ? 3.587 19.135 20.923 1.00 37.88 ? 2629 HOH A O 1 HETATM 3063 O O . HOH J 4 . ? -0.196 32.184 -3.384 1.00 35.78 ? 2630 HOH A O 1 HETATM 3064 O O . HOH J 4 . ? -8.406 57.838 20.265 1.00 46.71 ? 2631 HOH A O 1 HETATM 3065 O O . HOH J 4 . ? 15.630 29.747 0.328 1.00 41.74 ? 2632 HOH A O 1 HETATM 3066 O O . HOH J 4 . ? -10.052 58.384 22.421 1.00 45.83 ? 2633 HOH A O 1 HETATM 3067 O O . HOH J 4 . ? -2.994 36.123 23.319 1.00 36.61 ? 2634 HOH A O 1 HETATM 3068 O O . HOH J 4 . ? 29.482 14.631 10.237 1.00 42.94 ? 2635 HOH A O 1 HETATM 3069 O O . HOH J 4 . ? 7.747 29.481 23.117 1.00 41.31 ? 2636 HOH A O 1 HETATM 3070 O O . HOH J 4 . ? -4.410 35.719 -1.679 1.00 32.09 ? 2637 HOH A O 1 HETATM 3071 O O . HOH J 4 . ? -14.647 49.638 30.298 1.00 44.68 ? 2638 HOH A O 1 HETATM 3072 O O . HOH J 4 . ? -17.055 45.034 12.993 1.00 39.89 ? 2639 HOH A O 1 HETATM 3073 O O . HOH J 4 . ? -6.190 54.413 2.656 1.00 50.30 ? 2640 HOH A O 1 HETATM 3074 O O . HOH J 4 . ? -10.663 46.693 2.054 1.00 47.59 ? 2641 HOH A O 1 HETATM 3075 O O . HOH J 4 . ? 6.190 44.503 -0.238 1.00 43.42 ? 2642 HOH A O 1 HETATM 3076 O O . HOH J 4 . ? -4.362 43.539 23.563 1.00 44.06 ? 2643 HOH A O 1 HETATM 3077 O O . HOH J 4 . ? 18.346 20.874 4.150 1.00 30.09 ? 2644 HOH A O 1 HETATM 3078 O O . HOH J 4 . ? 3.168 15.730 17.853 1.00 44.78 ? 2645 HOH A O 1 HETATM 3079 O O . HOH J 4 . ? -2.398 26.194 16.218 1.00 39.74 ? 2646 HOH A O 1 HETATM 3080 O O . HOH J 4 . ? -19.085 49.534 23.887 1.00 38.32 ? 2647 HOH A O 1 HETATM 3081 O O . HOH J 4 . ? -0.427 55.067 6.721 1.00 35.22 ? 2648 HOH A O 1 HETATM 3082 O O . HOH J 4 . ? 17.556 39.430 19.512 1.00 31.32 ? 2649 HOH A O 1 HETATM 3083 O O . HOH J 4 . ? 15.097 19.392 26.597 1.00 47.74 ? 2650 HOH A O 1 HETATM 3084 O O . HOH J 4 . ? 16.931 14.513 18.690 1.00 49.91 ? 2651 HOH A O 1 HETATM 3085 O O . HOH J 4 . ? -4.466 40.981 -5.102 1.00 53.80 ? 2652 HOH A O 1 HETATM 3086 O O . HOH J 4 . ? 36.722 26.572 10.181 1.00 38.60 ? 2653 HOH A O 1 HETATM 3087 O O . HOH J 4 . ? -7.258 21.753 16.428 1.00 33.05 ? 2654 HOH A O 1 HETATM 3088 O O . HOH J 4 . ? 22.225 46.652 3.888 1.00 47.32 ? 2655 HOH A O 1 HETATM 3089 O O . HOH J 4 . ? -8.843 52.538 28.469 1.00 53.27 ? 2656 HOH A O 1 HETATM 3090 O O . HOH J 4 . ? 5.798 27.538 -1.762 1.00 43.42 ? 2657 HOH A O 1 HETATM 3091 O O . HOH J 4 . ? 28.829 46.813 20.481 1.00 48.19 ? 2658 HOH A O 1 HETATM 3092 O O . HOH J 4 . ? -5.694 21.034 19.680 1.00 43.32 ? 2659 HOH A O 1 HETATM 3093 O O . HOH J 4 . ? 30.884 27.679 1.637 1.00 47.18 ? 2660 HOH A O 1 HETATM 3094 O O . HOH J 4 . ? 8.050 43.597 1.625 1.00 36.10 ? 2661 HOH A O 1 HETATM 3095 O O . HOH J 4 . ? 0.176 21.144 6.568 1.00 32.12 ? 2662 HOH A O 1 HETATM 3096 O O . HOH J 4 . ? 11.234 47.113 1.550 1.00 46.96 ? 2663 HOH A O 1 HETATM 3097 O O . HOH J 4 . ? -16.301 29.267 2.697 1.00 48.76 ? 2664 HOH A O 1 HETATM 3098 O O . HOH J 4 . ? 7.467 45.088 21.474 1.00 44.41 ? 2665 HOH A O 1 HETATM 3099 O O . HOH J 4 . ? -10.727 39.694 20.631 1.00 33.86 ? 2666 HOH A O 1 HETATM 3100 O O . HOH J 4 . ? 16.560 30.560 27.331 1.00 47.06 ? 2667 HOH A O 1 HETATM 3101 O O . HOH J 4 . ? -2.138 45.160 22.344 1.00 44.22 ? 2668 HOH A O 1 HETATM 3102 O O . HOH J 4 . ? -0.005 46.575 -0.809 1.00 36.81 ? 2669 HOH A O 1 HETATM 3103 O O . HOH J 4 . ? 4.789 54.401 7.889 1.00 37.32 ? 2670 HOH A O 1 HETATM 3104 O O . HOH J 4 . ? 24.260 45.390 17.737 1.00 39.74 ? 2671 HOH A O 1 HETATM 3105 O O . HOH J 4 . ? -0.312 35.357 -2.148 1.00 42.76 ? 2672 HOH A O 1 HETATM 3106 O O . HOH J 4 . ? 19.489 44.859 16.102 1.00 46.54 ? 2673 HOH A O 1 HETATM 3107 O O . HOH J 4 . ? 33.909 29.719 24.215 1.00 44.87 ? 2674 HOH A O 1 HETATM 3108 O O . HOH J 4 . ? 7.570 54.265 7.857 1.00 33.90 ? 2675 HOH A O 1 HETATM 3109 O O . HOH J 4 . ? 5.825 36.496 -2.688 1.00 38.21 ? 2676 HOH A O 1 HETATM 3110 O O . HOH J 4 . ? 23.777 47.556 16.166 1.00 43.77 ? 2677 HOH A O 1 HETATM 3111 O O . HOH J 4 . ? -0.175 24.606 22.768 1.00 41.03 ? 2678 HOH A O 1 HETATM 3112 O O . HOH J 4 . ? 3.819 18.567 6.325 1.00 41.68 ? 2679 HOH A O 1 HETATM 3113 O O . HOH J 4 . ? 35.062 31.672 5.328 1.00 39.80 ? 2680 HOH A O 1 HETATM 3114 O O . HOH J 4 . ? -3.159 15.631 15.595 1.00 39.96 ? 2681 HOH A O 1 HETATM 3115 O O . HOH J 4 . ? 9.244 53.140 17.724 1.00 51.46 ? 2682 HOH A O 1 HETATM 3116 O O . HOH J 4 . ? 13.946 45.369 16.586 1.00 42.14 ? 2683 HOH A O 1 HETATM 3117 O O . HOH J 4 . ? 11.334 39.099 22.206 1.00 34.78 ? 2684 HOH A O 1 HETATM 3118 O O . HOH J 4 . ? 35.891 44.097 10.739 1.00 39.31 ? 2685 HOH A O 1 HETATM 3119 O O . HOH J 4 . ? 35.032 29.791 20.695 1.00 48.86 ? 2686 HOH A O 1 HETATM 3120 O O . HOH J 4 . ? 11.186 36.280 23.071 1.00 37.15 ? 2687 HOH A O 1 HETATM 3121 O O . HOH J 4 . ? 15.218 33.254 23.546 1.00 46.89 ? 2688 HOH A O 1 HETATM 3122 O O . HOH J 4 . ? 0.466 54.075 12.853 1.00 35.17 ? 2689 HOH A O 1 HETATM 3123 O O . HOH J 4 . ? 6.709 34.001 -4.431 1.00 43.92 ? 2690 HOH A O 1 HETATM 3124 O O . HOH J 4 . ? -3.376 45.474 -7.339 1.00 52.93 ? 2691 HOH A O 1 HETATM 3125 O O . HOH J 4 . ? 14.371 28.438 24.770 1.00 46.71 ? 2692 HOH A O 1 HETATM 3126 O O . HOH J 4 . ? 11.245 44.111 19.853 1.00 42.16 ? 2693 HOH A O 1 HETATM 3127 O O . HOH J 4 . ? -11.377 54.589 9.981 1.00 34.32 ? 2694 HOH A O 1 HETATM 3128 O O . HOH J 4 . ? -1.988 54.687 8.719 1.00 41.38 ? 2695 HOH A O 1 HETATM 3129 O O . HOH J 4 . ? 15.970 50.056 11.912 1.00 43.22 ? 2696 HOH A O 1 HETATM 3130 O O . HOH J 4 . ? 16.805 12.704 21.360 1.00 51.49 ? 2697 HOH A O 1 HETATM 3131 O O . HOH J 4 . ? -12.811 35.126 21.197 1.00 43.91 ? 2698 HOH A O 1 HETATM 3132 O O . HOH J 4 . ? 19.634 40.453 1.108 1.00 47.59 ? 2699 HOH A O 1 HETATM 3133 O O . HOH J 4 . ? -16.904 57.102 13.778 1.00 44.26 ? 2700 HOH A O 1 HETATM 3134 O O . HOH J 4 . ? 15.581 24.263 -1.123 1.00 43.24 ? 2701 HOH A O 1 HETATM 3135 O O . HOH J 4 . ? 4.914 36.070 24.947 1.00 31.97 ? 2702 HOH A O 1 HETATM 3136 O O . HOH J 4 . ? 19.035 18.487 33.464 1.00 51.00 ? 2703 HOH A O 1 HETATM 3137 O O . HOH J 4 . ? 4.667 25.672 -0.102 1.00 46.27 ? 2704 HOH A O 1 HETATM 3138 O O . HOH J 4 . ? -2.769 48.380 31.743 1.00 43.33 ? 2705 HOH A O 1 HETATM 3139 O O . HOH J 4 . ? 36.431 32.363 18.817 1.00 45.68 ? 2706 HOH A O 1 HETATM 3140 O O . HOH J 4 . ? -16.799 33.102 17.098 1.00 36.73 ? 2707 HOH A O 1 HETATM 3141 O O . HOH J 4 . ? -13.409 40.804 20.355 1.00 47.21 ? 2708 HOH A O 1 HETATM 3142 O O . HOH J 4 . ? 28.311 23.017 25.222 1.00 47.01 ? 2709 HOH A O 1 HETATM 3143 O O . HOH J 4 . ? 17.565 24.118 0.755 1.00 40.21 ? 2710 HOH A O 1 HETATM 3144 O O . HOH J 4 . ? -4.830 27.544 18.316 1.00 35.24 ? 2711 HOH A O 1 HETATM 3145 O O . HOH J 4 . ? 6.052 46.216 23.245 1.00 48.69 ? 2712 HOH A O 1 HETATM 3146 O O . HOH J 4 . ? -17.402 28.178 13.114 1.00 38.24 ? 2713 HOH A O 1 HETATM 3147 O O . HOH J 4 . ? 1.649 21.210 22.015 1.00 46.29 ? 2714 HOH A O 1 HETATM 3148 O O . HOH J 4 . ? 27.449 22.223 1.240 1.00 50.13 ? 2715 HOH A O 1 HETATM 3149 O O . HOH J 4 . ? 7.084 32.019 24.104 1.00 47.16 ? 2716 HOH A O 1 HETATM 3150 O O . HOH J 4 . ? -12.063 49.361 2.712 1.00 51.43 ? 2717 HOH A O 1 HETATM 3151 O O . HOH J 4 . ? 14.738 29.859 -2.250 1.00 46.09 ? 2718 HOH A O 1 HETATM 3152 O O . HOH J 4 . ? 28.425 47.439 12.181 1.00 40.14 ? 2719 HOH A O 1 HETATM 3153 O O . HOH J 4 . ? -13.961 22.216 -6.093 1.00 50.83 ? 2720 HOH A O 1 HETATM 3154 O O . HOH J 4 . ? 22.054 35.788 -1.262 1.00 52.53 ? 2721 HOH A O 1 HETATM 3155 O O . HOH J 4 . ? 39.151 22.066 16.643 1.00 47.63 ? 2722 HOH A O 1 HETATM 3156 O O . HOH J 4 . ? -6.421 55.148 20.531 1.00 39.45 ? 2723 HOH A O 1 HETATM 3157 O O . HOH J 4 . ? 17.530 48.451 4.025 1.00 40.00 ? 2724 HOH A O 1 HETATM 3158 O O . HOH J 4 . ? 22.727 30.595 2.092 1.00 44.82 ? 2725 HOH A O 1 HETATM 3159 O O . HOH J 4 . ? -18.180 25.458 14.205 1.00 40.89 ? 2726 HOH A O 1 HETATM 3160 O O . HOH J 4 . ? -3.821 23.087 3.749 1.00 32.82 ? 2727 HOH A O 1 HETATM 3161 O O . HOH J 4 . ? -8.997 54.984 3.886 1.00 55.51 ? 2728 HOH A O 1 HETATM 3162 O O . HOH J 4 . ? -2.059 56.486 5.196 1.00 44.54 ? 2729 HOH A O 1 HETATM 3163 O O . HOH J 4 . ? 28.943 46.386 9.731 1.00 47.20 ? 2730 HOH A O 1 HETATM 3164 O O . HOH J 4 . ? 1.259 30.785 -5.288 1.00 56.20 ? 2731 HOH A O 1 HETATM 3165 O O . HOH J 4 . ? -12.584 32.343 21.729 1.00 49.30 ? 2732 HOH A O 1 HETATM 3166 O O . HOH J 4 . ? -2.908 26.110 4.384 1.00 29.51 ? 2733 HOH A O 1 HETATM 3167 O O . HOH J 4 . ? 9.605 35.884 24.951 1.00 39.37 ? 2734 HOH A O 1 HETATM 3168 O O . HOH J 4 . ? 18.888 29.993 1.499 1.00 47.83 ? 2735 HOH A O 1 HETATM 3169 O O . HOH J 4 . ? -18.707 37.440 5.362 1.00 38.96 ? 2736 HOH A O 1 HETATM 3170 O O . HOH J 4 . ? 36.338 41.881 14.717 1.00 47.72 ? 2737 HOH A O 1 HETATM 3171 O O . HOH J 4 . ? -18.667 34.769 0.773 1.00 44.93 ? 2738 HOH A O 1 HETATM 3172 O O . HOH J 4 . ? -20.537 47.824 15.504 1.00 40.59 ? 2739 HOH A O 1 HETATM 3173 O O . HOH J 4 . ? -5.176 34.639 23.990 1.00 40.54 ? 2740 HOH A O 1 HETATM 3174 O O . HOH J 4 . ? 8.364 38.264 -3.342 1.00 39.86 ? 2741 HOH A O 1 HETATM 3175 O O . HOH J 4 . ? -2.590 52.916 23.493 0.50 34.11 ? 2742 HOH A O 1 HETATM 3176 O O . HOH J 4 . ? 15.242 41.907 19.996 1.00 46.61 ? 2743 HOH A O 1 HETATM 3177 O O . HOH J 4 . ? -18.857 36.452 7.802 1.00 37.25 ? 2744 HOH A O 1 HETATM 3178 O O . HOH J 4 . ? -19.378 39.996 5.275 1.00 45.15 ? 2745 HOH A O 1 HETATM 3179 O O . HOH J 4 . ? -4.774 48.546 30.518 1.00 52.84 ? 2746 HOH A O 1 HETATM 3180 O O . HOH J 4 . ? 16.364 36.036 20.944 1.00 36.33 ? 2747 HOH A O 1 HETATM 3181 O O . HOH J 4 . ? 14.348 31.166 25.616 1.00 47.32 ? 2748 HOH A O 1 HETATM 3182 O O . HOH J 4 . ? -14.074 45.622 28.509 1.00 42.93 ? 2749 HOH A O 1 HETATM 3183 O O . HOH J 4 . ? 28.942 10.804 12.140 1.00 53.77 ? 2750 HOH A O 1 HETATM 3184 O O . HOH J 4 . ? -20.084 57.144 26.221 1.00 49.21 ? 2751 HOH A O 1 HETATM 3185 O O . HOH J 4 . ? 4.315 43.526 26.888 1.00 47.62 ? 2752 HOH A O 1 HETATM 3186 O O . HOH J 4 . ? -16.516 34.941 2.489 1.00 48.38 ? 2753 HOH A O 1 HETATM 3187 O O . HOH J 4 . ? 17.109 10.586 29.444 1.00 56.63 ? 2754 HOH A O 1 HETATM 3188 O O . HOH J 4 . ? 23.115 12.352 31.599 1.00 46.60 ? 2755 HOH A O 1 HETATM 3189 O O . HOH J 4 . ? 29.829 48.462 14.020 1.00 46.82 ? 2756 HOH A O 1 HETATM 3190 O O . HOH J 4 . ? 20.948 25.210 26.506 1.00 43.93 ? 2757 HOH A O 1 HETATM 3191 O O . HOH J 4 . ? 8.566 48.840 20.323 1.00 46.29 ? 2758 HOH A O 1 HETATM 3192 O O . HOH J 4 . ? 1.536 21.704 4.377 1.00 41.96 ? 2759 HOH A O 1 HETATM 3193 O O . HOH J 4 . ? 5.403 14.454 18.167 1.00 45.50 ? 2760 HOH A O 1 HETATM 3194 O O . HOH J 4 . ? 30.885 17.963 26.134 1.00 37.72 ? 2761 HOH A O 1 HETATM 3195 O O . HOH J 4 . ? -14.872 32.034 0.029 1.00 45.29 ? 2762 HOH A O 1 HETATM 3196 O O . HOH J 4 . ? 18.797 25.651 24.372 1.00 48.45 ? 2763 HOH A O 1 HETATM 3197 O O . HOH J 4 . ? 30.074 24.119 2.603 1.00 58.85 ? 2764 HOH A O 1 HETATM 3198 O O . HOH J 4 . ? 16.160 44.199 18.613 1.00 47.22 ? 2765 HOH A O 1 HETATM 3199 O O . HOH J 4 . ? 3.386 22.573 1.263 1.00 42.81 ? 2766 HOH A O 1 HETATM 3200 O O . HOH J 4 . ? 25.684 32.654 -1.581 1.00 50.28 ? 2767 HOH A O 1 HETATM 3201 O O . HOH J 4 . ? 2.773 49.995 0.837 1.00 38.32 ? 2768 HOH A O 1 HETATM 3202 O O . HOH J 4 . ? -4.400 37.779 -3.223 1.00 44.24 ? 2769 HOH A O 1 HETATM 3203 O O . HOH J 4 . ? -14.630 51.417 4.946 1.00 50.61 ? 2770 HOH A O 1 HETATM 3204 O O . HOH J 4 . ? 15.192 9.705 13.181 1.00 52.98 ? 2771 HOH A O 1 HETATM 3205 O O . HOH J 4 . ? -16.588 29.269 -5.388 1.00 43.54 ? 2772 HOH A O 1 HETATM 3206 O O . HOH J 4 . ? 2.758 33.868 -5.075 1.00 42.92 ? 2773 HOH A O 1 HETATM 3207 O O . HOH J 4 . ? 5.199 16.512 7.438 1.00 58.36 ? 2774 HOH A O 1 HETATM 3208 O O . HOH J 4 . ? 24.130 23.861 1.283 1.00 50.14 ? 2775 HOH A O 1 HETATM 3209 O O . HOH J 4 . ? 9.406 25.886 -1.907 1.00 34.98 ? 2776 HOH A O 1 HETATM 3210 O O . HOH J 4 . ? -17.009 36.206 18.556 1.00 40.15 ? 2777 HOH A O 1 HETATM 3211 O O . HOH J 4 . ? -13.850 18.254 15.630 1.00 59.28 ? 2778 HOH A O 1 HETATM 3212 O O . HOH J 4 . ? 26.916 46.496 7.221 1.00 43.25 ? 2779 HOH A O 1 HETATM 3213 O O . HOH J 4 . ? -19.434 34.138 8.788 1.00 34.31 ? 2780 HOH A O 1 HETATM 3214 O O . HOH J 4 . ? 35.245 28.406 7.136 1.00 42.60 ? 2781 HOH A O 1 HETATM 3215 O O . HOH J 4 . ? 10.443 11.354 12.640 1.00 56.31 ? 2782 HOH A O 1 HETATM 3216 O O . HOH J 4 . ? 8.376 38.464 25.244 1.00 42.65 ? 2783 HOH A O 1 HETATM 3217 O O . HOH J 4 . ? -5.451 32.315 24.255 1.00 41.28 ? 2784 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 PHE 1 19 19 PHE PHE A . n A 1 2 ASP 2 20 20 ASP ASP A . n A 1 3 ASN 3 21 21 ASN ASN A . n A 1 4 PRO 4 22 22 PRO PRO A . n A 1 5 PRO 5 23 23 PRO PRO A . n A 1 6 THR 6 24 24 THR THR A . n A 1 7 ASN 7 25 25 ASN ASN A . n A 1 8 VAL 8 26 26 VAL VAL A . n A 1 9 VAL 9 27 27 VAL VAL A . n A 1 10 SER 10 28 28 SER SER A . n A 1 11 HIS 11 29 29 HIS HIS A . n A 1 12 LEU 12 30 30 LEU LEU A . n A 1 13 ASN 13 31 31 ASN ASN A . n A 1 14 GLY 14 32 32 GLY GLY A . n A 1 15 ASP 15 33 33 ASP ASP A . n A 1 16 TRP 16 34 34 TRP TRP A . n A 1 17 PHE 17 35 35 PHE PHE A . n A 1 18 LEU 18 36 36 LEU LEU A . n A 1 19 PHE 19 37 37 PHE PHE A . n A 1 20 GLY 20 38 38 GLY GLY A . n A 1 21 ASP 21 39 39 ASP ASP A . n A 1 22 SER 22 40 40 SER SER A . n A 1 23 ARG 23 41 41 ARG ARG A . n A 1 24 SER 24 42 42 SER SER A . n A 1 25 ASP 25 43 43 ASP ASP A . n A 1 26 CYS 26 44 44 CYS CYS A . n A 1 27 ASN 27 45 45 ASN ASN A . n A 1 28 HIS 28 46 46 HIS HIS A . n A 1 29 VAL 29 47 47 VAL VAL A . n A 1 30 VAL 30 48 48 VAL VAL A . n A 1 31 ASN 31 49 49 ASN ASN A . n A 1 32 THR 32 50 50 THR THR A . n A 1 33 ASN 33 51 51 ASN ASN A . n A 1 34 PRO 34 52 52 PRO PRO A . n A 1 35 ARG 35 53 53 ARG ARG A . n A 1 36 ASN 36 54 54 ASN ASN A . n A 1 37 TYR 37 55 55 TYR TYR A . n A 1 38 SER 38 56 56 SER SER A . n A 1 39 TYR 39 57 57 TYR TYR A . n A 1 40 MET 40 58 58 MET MET A . n A 1 41 ASP 41 59 59 ASP ASP A . n A 1 42 LEU 42 60 60 LEU LEU A . n A 1 43 ASN 43 61 61 ASN ASN A . n A 1 44 PRO 44 62 62 PRO PRO A . n A 1 45 ALA 45 63 63 ALA ALA A . n A 1 46 LEU 46 64 64 LEU LEU A . n A 1 47 CYS 47 65 65 CYS CYS A . n A 1 48 ASP 48 66 66 ASP ASP A . n A 1 49 SER 49 67 67 SER SER A . n A 1 50 GLY 50 68 68 GLY GLY A . n A 1 51 LYS 51 69 69 LYS LYS A . n A 1 52 ILE 52 70 70 ILE ILE A . n A 1 53 SER 53 71 71 SER SER A . n A 1 54 SER 54 72 72 SER SER A . n A 1 55 LYS 55 73 73 LYS LYS A . n A 1 56 ALA 56 74 74 ALA ALA A . n A 1 57 GLY 57 75 75 GLY GLY A . n A 1 58 ASN 58 76 76 ASN ASN A . n A 1 59 SER 59 77 77 SER SER A . n A 1 60 ILE 60 78 78 ILE ILE A . n A 1 61 PHE 61 79 79 PHE PHE A . n A 1 62 ARG 62 80 80 ARG ARG A . n A 1 63 SER 63 81 81 SER SER A . n A 1 64 PHE 64 82 82 PHE PHE A . n A 1 65 HIS 65 83 83 HIS HIS A . n A 1 66 PHE 66 84 84 PHE PHE A . n A 1 67 THR 67 85 85 THR THR A . n A 1 68 ASP 68 86 86 ASP ASP A . n A 1 69 PHE 69 87 87 PHE PHE A . n A 1 70 TYR 70 88 88 TYR TYR A . n A 1 71 ASN 71 89 89 ASN ASN A . n A 1 72 TYR 72 90 90 TYR TYR A . n A 1 73 THR 73 91 91 THR THR A . n A 1 74 GLY 74 92 92 GLY GLY A . n A 1 75 GLU 75 93 93 GLU GLU A . n A 1 76 GLY 76 94 94 GLY GLY A . n A 1 77 GLN 77 95 95 GLN GLN A . n A 1 78 GLN 78 96 96 GLN GLN A . n A 1 79 ILE 79 97 97 ILE ILE A . n A 1 80 ILE 80 98 98 ILE ILE A . n A 1 81 PHE 81 99 99 PHE PHE A . n A 1 82 TYR 82 100 100 TYR TYR A . n A 1 83 GLU 83 101 101 GLU GLU A . n A 1 84 GLY 84 102 102 GLY GLY A . n A 1 85 VAL 85 103 103 VAL VAL A . n A 1 86 ASN 86 104 104 ASN ASN A . n A 1 87 PHE 87 105 105 PHE PHE A . n A 1 88 THR 88 106 106 THR THR A . n A 1 89 PRO 89 107 107 PRO PRO A . n A 1 90 TYR 90 108 108 TYR TYR A . n A 1 91 HIS 91 109 109 HIS HIS A . n A 1 92 ALA 92 110 110 ALA ALA A . n A 1 93 PHE 93 111 111 PHE PHE A . n A 1 94 LYS 94 112 112 LYS LYS A . n A 1 95 CYS 95 113 113 CYS CYS A . n A 1 96 THR 96 114 114 THR THR A . n A 1 97 THR 97 115 115 THR THR A . n A 1 98 SER 98 116 116 SER SER A . n A 1 99 GLY 99 117 117 GLY GLY A . n A 1 100 SER 100 118 118 SER SER A . n A 1 101 ASN 101 119 119 ASN ASN A . n A 1 102 ASP 102 120 120 ASP ASP A . n A 1 103 ILE 103 121 121 ILE ILE A . n A 1 104 TRP 104 122 122 TRP TRP A . n A 1 105 MET 105 123 123 MET MET A . n A 1 106 GLN 106 124 124 GLN GLN A . n A 1 107 ASN 107 125 125 ASN ASN A . n A 1 108 LYS 108 126 126 LYS LYS A . n A 1 109 GLY 109 127 127 GLY GLY A . n A 1 110 LEU 110 128 128 LEU LEU A . n A 1 111 PHE 111 129 129 PHE PHE A . n A 1 112 TYR 112 130 130 TYR TYR A . n A 1 113 THR 113 131 131 THR THR A . n A 1 114 GLN 114 132 132 GLN GLN A . n A 1 115 VAL 115 133 133 VAL VAL A . n A 1 116 TYR 116 134 134 TYR TYR A . n A 1 117 LYS 117 135 135 LYS LYS A . n A 1 118 ASN 118 136 136 ASN ASN A . n A 1 119 MET 119 137 137 MET MET A . n A 1 120 ALA 120 138 138 ALA ALA A . n A 1 121 VAL 121 139 139 VAL VAL A . n A 1 122 TYR 122 140 140 TYR TYR A . n A 1 123 ARG 123 141 141 ARG ARG A . n A 1 124 SER 124 142 142 SER SER A . n A 1 125 LEU 125 143 143 LEU LEU A . n A 1 126 THR 126 144 144 THR THR A . n A 1 127 PHE 127 145 145 PHE PHE A . n A 1 128 VAL 128 146 146 VAL VAL A . n A 1 129 ASN 129 147 147 ASN ASN A . n A 1 130 VAL 130 148 148 VAL VAL A . n A 1 131 PRO 131 149 149 PRO PRO A . n A 1 132 TYR 132 150 150 TYR TYR A . n A 1 133 VAL 133 151 151 VAL VAL A . n A 1 134 TYR 134 152 152 TYR TYR A . n A 1 135 ASN 135 153 153 ASN ASN A . n A 1 136 GLY 136 154 154 GLY GLY A . n A 1 137 SER 137 155 155 SER SER A . n A 1 138 ALA 138 156 156 ALA ALA A . n A 1 139 GLN 139 157 157 GLN GLN A . n A 1 140 SER 140 158 158 SER SER A . n A 1 141 THR 141 159 159 THR THR A . n A 1 142 ALA 142 160 160 ALA ALA A . n A 1 143 LEU 143 161 161 LEU LEU A . n A 1 144 CYS 144 162 162 CYS CYS A . n A 1 145 LYS 145 163 163 LYS LYS A . n A 1 146 SER 146 164 164 SER SER A . n A 1 147 GLY 147 165 165 GLY GLY A . n A 1 148 SER 148 166 166 SER SER A . n A 1 149 LEU 149 167 167 LEU LEU A . n A 1 150 VAL 150 168 168 VAL VAL A . n A 1 151 LEU 151 169 169 LEU LEU A . n A 1 152 ASN 152 170 170 ASN ASN A . n A 1 153 ASN 153 171 171 ASN ASN A . n A 1 154 PRO 154 172 172 PRO PRO A . n A 1 155 ALA 155 173 173 ALA ALA A . n A 1 156 TYR 156 174 174 TYR TYR A . n A 1 157 ILE 157 175 175 ILE ILE A . n A 1 158 ALA 158 176 176 ALA ALA A . n A 1 159 ARG 159 177 177 ARG ARG A . n A 1 160 GLU 160 178 178 GLU GLU A . n A 1 161 ALA 161 179 179 ALA ALA A . n A 1 162 ASN 162 180 180 ASN ASN A . n A 1 163 PHE 163 181 181 PHE PHE A . n A 1 164 GLY 164 182 182 GLY GLY A . n A 1 165 ASP 165 183 183 ASP ASP A . n A 1 166 TYR 166 184 184 TYR TYR A . n A 1 167 TYR 167 185 185 TYR TYR A . n A 1 168 TYR 168 186 186 TYR TYR A . n A 1 169 LYS 169 187 187 LYS LYS A . n A 1 170 VAL 170 188 188 VAL VAL A . n A 1 171 GLU 171 189 189 GLU GLU A . n A 1 172 ALA 172 190 190 ALA ALA A . n A 1 173 ASP 173 191 191 ASP ASP A . n A 1 174 PHE 174 192 192 PHE PHE A . n A 1 175 TYR 175 193 193 TYR TYR A . n A 1 176 LEU 176 194 194 LEU LEU A . n A 1 177 SER 177 195 195 SER SER A . n A 1 178 GLY 178 196 196 GLY GLY A . n A 1 179 CYS 179 197 197 CYS CYS A . n A 1 180 ASP 180 198 198 ASP ASP A . n A 1 181 GLU 181 199 199 GLU GLU A . n A 1 182 TYR 182 200 200 TYR TYR A . n A 1 183 ILE 183 201 201 ILE ILE A . n A 1 184 VAL 184 202 202 VAL VAL A . n A 1 185 PRO 185 203 203 PRO PRO A . n A 1 186 LEU 186 204 204 LEU LEU A . n A 1 187 CYS 187 205 205 CYS CYS A . n A 1 188 ILE 188 206 206 ILE ILE A . n A 1 189 PHE 189 207 207 PHE PHE A . n A 1 190 ASN 190 208 208 ASN ASN A . n A 1 191 GLY 191 209 209 GLY GLY A . n A 1 192 LYS 192 210 210 LYS LYS A . n A 1 193 PHE 193 211 211 PHE PHE A . n A 1 194 LEU 194 212 212 LEU LEU A . n A 1 195 SER 195 213 213 SER SER A . n A 1 196 ASN 196 214 214 ASN ASN A . n A 1 197 THR 197 215 215 THR THR A . n A 1 198 LYS 198 216 216 LYS LYS A . n A 1 199 TYR 199 217 217 TYR TYR A . n A 1 200 TYR 200 218 218 TYR TYR A . n A 1 201 ASP 201 219 219 ASP ASP A . n A 1 202 ASP 202 220 220 ASP ASP A . n A 1 203 SER 203 221 221 SER SER A . n A 1 204 GLN 204 222 222 GLN GLN A . n A 1 205 TYR 205 223 223 TYR TYR A . n A 1 206 TYR 206 224 224 TYR TYR A . n A 1 207 PHE 207 225 225 PHE PHE A . n A 1 208 ASN 208 226 226 ASN ASN A . n A 1 209 LYS 209 227 227 LYS LYS A . n A 1 210 ASP 210 228 228 ASP ASP A . n A 1 211 THR 211 229 229 THR THR A . n A 1 212 GLY 212 230 230 GLY GLY A . n A 1 213 VAL 213 231 231 VAL VAL A . n A 1 214 ILE 214 232 232 ILE ILE A . n A 1 215 TYR 215 233 233 TYR TYR A . n A 1 216 GLY 216 234 234 GLY GLY A . n A 1 217 LEU 217 235 235 LEU LEU A . n A 1 218 ASN 218 236 236 ASN ASN A . n A 1 219 SER 219 237 237 SER SER A . n A 1 220 THR 220 238 238 THR THR A . n A 1 221 GLU 221 239 239 GLU GLU A . n A 1 222 THR 222 240 240 THR THR A . n A 1 223 ILE 223 241 241 ILE ILE A . n A 1 224 THR 224 242 242 THR THR A . n A 1 225 THR 225 243 243 THR THR A . n A 1 226 GLY 226 244 244 GLY GLY A . n A 1 227 PHE 227 245 245 PHE PHE A . n A 1 228 ASP 228 246 246 ASP ASP A . n A 1 229 PHE 229 247 247 PHE PHE A . n A 1 230 ASN 230 248 248 ASN ASN A . n A 1 231 CYS 231 249 249 CYS CYS A . n A 1 232 HIS 232 250 250 HIS HIS A . n A 1 233 TYR 233 251 251 TYR TYR A . n A 1 234 LEU 234 252 252 LEU LEU A . n A 1 235 VAL 235 253 253 VAL VAL A . n A 1 236 LEU 236 254 254 LEU LEU A . n A 1 237 PRO 237 255 255 PRO PRO A . n A 1 238 SER 238 256 256 SER SER A . n A 1 239 GLY 239 257 257 GLY GLY A . n A 1 240 ASN 240 258 258 ASN ASN A . n A 1 241 TYR 241 259 259 TYR TYR A . n A 1 242 LEU 242 260 260 LEU LEU A . n A 1 243 ALA 243 261 261 ALA ALA A . n A 1 244 ILE 244 262 262 ILE ILE A . n A 1 245 SER 245 263 263 SER SER A . n A 1 246 ASN 246 264 264 ASN ASN A . n A 1 247 GLU 247 265 265 GLU GLU A . n A 1 248 LEU 248 266 266 LEU LEU A . n A 1 249 LEU 249 267 267 LEU LEU A . n A 1 250 LEU 250 268 268 LEU LEU A . n A 1 251 THR 251 269 269 THR THR A . n A 1 252 VAL 252 270 270 VAL VAL A . n A 1 253 PRO 253 271 271 PRO PRO A . n A 1 254 THR 254 272 272 THR THR A . n A 1 255 LYS 255 273 273 LYS LYS A . n A 1 256 ALA 256 274 274 ALA ALA A . n A 1 257 ILE 257 275 275 ILE ILE A . n A 1 258 CYS 258 276 276 CYS CYS A . n A 1 259 LEU 259 277 277 LEU LEU A . n A 1 260 ASN 260 278 278 ASN ASN A . n A 1 261 LYS 261 279 279 LYS LYS A . n A 1 262 ARG 262 280 280 ARG ARG A . n A 1 263 LYS 263 281 281 LYS LYS A . n A 1 264 ASP 264 282 282 ASP ASP A . n A 1 265 PHE 265 283 283 PHE PHE A . n A 1 266 THR 266 284 284 THR THR A . n A 1 267 PRO 267 285 285 PRO PRO A . n A 1 268 VAL 268 286 286 VAL VAL A . n A 1 269 GLN 269 287 287 GLN GLN A . n A 1 270 VAL 270 288 288 VAL VAL A . n A 1 271 VAL 271 289 289 VAL VAL A . n A 1 272 ASP 272 290 290 ASP ASP A . n A 1 273 SER 273 291 291 SER SER A . n A 1 274 ARG 274 292 292 ARG ARG A . n A 1 275 TRP 275 293 293 TRP TRP A . n A 1 276 ASN 276 294 294 ASN ASN A . n A 1 277 ASN 277 295 295 ASN ASN A . n A 1 278 ALA 278 296 296 ALA ALA A . n A 1 279 ARG 279 297 297 ARG ARG A . n A 1 280 GLN 280 298 298 GLN GLN A . n A 1 281 SER 281 299 299 SER SER A . n A 1 282 ASP 282 300 300 ASP ASP A . n A 1 283 ASN 283 301 301 ASN ASN A . n A 1 284 MET 284 302 302 MET MET A . n A 1 285 THR 285 303 303 THR THR A . n A 1 286 ALA 286 304 304 ALA ALA A . n A 1 287 VAL 287 305 305 VAL VAL A . n A 1 288 ALA 288 306 306 ALA ALA A . n A 1 289 CYS 289 307 307 CYS CYS A . n A 1 290 GLN 290 308 308 GLN GLN A . n A 1 291 PRO 291 309 309 PRO PRO A . n A 1 292 PRO 292 310 310 PRO PRO A . n A 1 293 TYR 293 311 311 TYR TYR A . n A 1 294 CYS 294 312 312 CYS CYS A . n A 1 295 TYR 295 313 313 TYR TYR A . n A 1 296 PHE 296 314 314 PHE PHE A . n A 1 297 ARG 297 315 315 ARG ARG A . n A 1 298 ASN 298 316 316 ASN ASN A . n A 1 299 SER 299 317 317 SER SER A . n A 1 300 THR 300 318 318 THR THR A . n A 1 301 THR 301 319 319 THR THR A . n A 1 302 ASN 302 320 320 ASN ASN A . n A 1 303 TYR 303 321 321 TYR TYR A . n A 1 304 VAL 304 322 322 VAL VAL A . n A 1 305 GLY 305 323 323 GLY GLY A . n A 1 306 VAL 306 324 324 VAL VAL A . n A 1 307 TYR 307 325 325 TYR TYR A . n A 1 308 ASP 308 326 326 ASP ASP A . n A 1 309 ILE 309 327 327 ILE ILE A . n A 1 310 ASN 310 328 328 ASN ASN A . n A 1 311 HIS 311 329 329 HIS HIS A . n A 1 312 GLY 312 330 330 GLY GLY A . n A 1 313 ASP 313 331 331 ASP ASP A . n A 1 314 ALA 314 332 332 ALA ALA A . n A 1 315 GLY 315 333 333 GLY GLY A . n A 1 316 PHE 316 334 334 PHE PHE A . n A 1 317 THR 317 335 335 THR THR A . n A 1 318 SER 318 336 336 SER SER A . n A 1 319 ILE 319 337 337 ILE ILE A . n A 1 320 LEU 320 338 338 LEU LEU A . n A 1 321 SER 321 339 339 SER SER A . n A 1 322 GLY 322 340 340 GLY GLY A . n A 1 323 LEU 323 341 341 LEU LEU A . n A 1 324 LEU 324 342 342 LEU LEU A . n A 1 325 TYR 325 343 343 TYR TYR A . n A 1 326 ASP 326 344 344 ASP ASP A . n A 1 327 SER 327 345 345 SER SER A . n A 1 328 PRO 328 346 346 PRO PRO A . n A 1 329 CYS 329 347 347 CYS CYS A . n A 1 330 PHE 330 348 348 PHE PHE A . n A 1 331 SER 331 349 349 SER SER A . n A 1 332 GLN 332 350 350 GLN GLN A . n A 1 333 GLN 333 351 351 GLN GLN A . n A 1 334 GLY 334 352 352 GLY GLY A . n A 1 335 VAL 335 353 353 VAL VAL A . n A 1 336 PHE 336 354 354 PHE PHE A . n A 1 337 ARG 337 355 355 ARG ARG A . n A 1 338 TYR 338 356 356 TYR TYR A . n A 1 339 ASP 339 357 357 ASP ASP A . n A 1 340 ASN 340 358 358 ASN ASN A . n A 1 341 VAL 341 359 359 VAL VAL A . n A 1 342 SER 342 360 360 SER SER A . n A 1 343 SER 343 361 361 SER SER A . n A 1 344 VAL 344 362 362 VAL VAL A . n A 1 345 TRP 345 363 363 TRP TRP A . n A 1 346 PRO 346 364 364 PRO PRO A . n A 1 347 LEU 347 365 365 LEU LEU A . n A 1 348 TYR 348 366 366 TYR TYR A . n A 1 349 SER 349 367 367 SER SER A . n A 1 350 TYR 350 368 368 TYR TYR A . n A 1 351 GLY 351 369 369 GLY GLY A . n A 1 352 ARG 352 370 370 ARG ARG A . n A 1 353 CYS 353 371 371 CYS CYS A . n A 1 354 PRO 354 372 372 PRO PRO A . n A 1 355 THR 355 373 373 THR THR A . n A 1 356 ALA 356 374 374 ALA ALA A . n A 1 357 ALA 357 375 375 ALA ALA A . n A 1 358 ASP 358 376 376 ASP ASP A . n A 1 359 ILE 359 377 ? ? ? A . n A 1 360 ASN 360 378 ? ? ? A . n A 1 361 THR 361 379 ? ? ? A . n A 1 362 PRO 362 380 ? ? ? A . n A 1 363 ASP 363 381 ? ? ? A . n A 1 364 VAL 364 382 ? ? ? A . n A 1 365 PRO 365 383 ? ? ? A . n A 1 366 ILE 366 384 ? ? ? A . n A 1 367 CYS 367 385 ? ? ? A . n A 1 368 VAL 368 386 ? ? ? A . n A 1 369 TYR 369 387 ? ? ? A . n A 1 370 ASP 370 388 ? ? ? A . n A 1 371 SER 371 389 ? ? ? A . n A 1 372 ASP 372 390 ? ? ? A . n A 1 373 PRO 373 391 ? ? ? A . n A 1 374 LEU 374 392 ? ? ? A . n A 1 375 VAL 375 393 ? ? ? A . n A 1 376 PRO 376 394 ? ? ? A . n A 1 377 ARG 377 395 ? ? ? 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 1961 1961 NAG NAG A . C 2 NAG 1 2523 2523 NAG NAG A . D 2 NAG 1 2525 2525 NAG NAG A . E 2 NAG 2 2526 2526 NAG NAG A . F 2 NAG 1 2527 2527 NAG NAG A . G 2 NAG 1 2521 2521 NAG NAG A . H 2 NAG 1 2520 2520 NAG NAG A . I 3 K 1 2 2 K K A . J 4 HOH 1 2528 2 HOH HOH A . J 4 HOH 2 2529 3 HOH HOH A . J 4 HOH 3 2530 4 HOH HOH A . J 4 HOH 4 2531 5 HOH HOH A . J 4 HOH 5 2532 6 HOH HOH A . J 4 HOH 6 2533 7 HOH HOH A . J 4 HOH 7 2534 8 HOH HOH A . J 4 HOH 8 2535 10 HOH HOH A . J 4 HOH 9 2536 11 HOH HOH A . J 4 HOH 10 2537 12 HOH HOH A . J 4 HOH 11 2538 13 HOH HOH A . J 4 HOH 12 2539 14 HOH HOH A . J 4 HOH 13 2540 15 HOH HOH A . J 4 HOH 14 2541 16 HOH HOH A . J 4 HOH 15 2542 17 HOH HOH A . J 4 HOH 16 2543 18 HOH HOH A . J 4 HOH 17 2544 19 HOH HOH A . J 4 HOH 18 2545 20 HOH HOH A . J 4 HOH 19 2546 21 HOH HOH A . J 4 HOH 20 2547 22 HOH HOH A . J 4 HOH 21 2548 23 HOH HOH A . J 4 HOH 22 2549 24 HOH HOH A . J 4 HOH 23 2550 25 HOH HOH A . J 4 HOH 24 2551 26 HOH HOH A . J 4 HOH 25 2552 27 HOH HOH A . J 4 HOH 26 2553 28 HOH HOH A . J 4 HOH 27 2554 29 HOH HOH A . J 4 HOH 28 2555 30 HOH HOH A . J 4 HOH 29 2556 31 HOH HOH A . J 4 HOH 30 2557 32 HOH HOH A . J 4 HOH 31 2558 33 HOH HOH A . J 4 HOH 32 2559 34 HOH HOH A . J 4 HOH 33 2560 35 HOH HOH A . J 4 HOH 34 2561 36 HOH HOH A . J 4 HOH 35 2562 37 HOH HOH A . J 4 HOH 36 2563 38 HOH HOH A . J 4 HOH 37 2564 39 HOH HOH A . J 4 HOH 38 2565 40 HOH HOH A . J 4 HOH 39 2566 41 HOH HOH A . J 4 HOH 40 2567 42 HOH HOH A . J 4 HOH 41 2568 43 HOH HOH A . J 4 HOH 42 2569 44 HOH HOH A . J 4 HOH 43 2570 45 HOH HOH A . J 4 HOH 44 2571 46 HOH HOH A . J 4 HOH 45 2572 47 HOH HOH A . J 4 HOH 46 2573 49 HOH HOH A . J 4 HOH 47 2574 50 HOH HOH A . J 4 HOH 48 2575 51 HOH HOH A . J 4 HOH 49 2576 52 HOH HOH A . J 4 HOH 50 2577 53 HOH HOH A . J 4 HOH 51 2578 54 HOH HOH A . J 4 HOH 52 2579 55 HOH HOH A . J 4 HOH 53 2580 56 HOH HOH A . J 4 HOH 54 2581 57 HOH HOH A . J 4 HOH 55 2582 58 HOH HOH A . J 4 HOH 56 2583 59 HOH HOH A . J 4 HOH 57 2584 60 HOH HOH A . J 4 HOH 58 2585 61 HOH HOH A . J 4 HOH 59 2586 62 HOH HOH A . J 4 HOH 60 2587 63 HOH HOH A . J 4 HOH 61 2588 64 HOH HOH A . J 4 HOH 62 2589 65 HOH HOH A . J 4 HOH 63 2590 66 HOH HOH A . J 4 HOH 64 2591 67 HOH HOH A . J 4 HOH 65 2592 68 HOH HOH A . J 4 HOH 66 2593 69 HOH HOH A . J 4 HOH 67 2594 70 HOH HOH A . J 4 HOH 68 2595 72 HOH HOH A . J 4 HOH 69 2596 73 HOH HOH A . J 4 HOH 70 2597 74 HOH HOH A . J 4 HOH 71 2598 75 HOH HOH A . J 4 HOH 72 2599 76 HOH HOH A . J 4 HOH 73 2600 77 HOH HOH A . J 4 HOH 74 2601 78 HOH HOH A . J 4 HOH 75 2602 79 HOH HOH A . J 4 HOH 76 2603 80 HOH HOH A . J 4 HOH 77 2604 81 HOH HOH A . J 4 HOH 78 2605 82 HOH HOH A . J 4 HOH 79 2606 83 HOH HOH A . J 4 HOH 80 2607 85 HOH HOH A . J 4 HOH 81 2608 86 HOH HOH A . J 4 HOH 82 2609 87 HOH HOH A . J 4 HOH 83 2610 88 HOH HOH A . J 4 HOH 84 2611 89 HOH HOH A . J 4 HOH 85 2612 90 HOH HOH A . J 4 HOH 86 2613 91 HOH HOH A . J 4 HOH 87 2614 92 HOH HOH A . J 4 HOH 88 2615 93 HOH HOH A . J 4 HOH 89 2616 94 HOH HOH A . J 4 HOH 90 2617 95 HOH HOH A . J 4 HOH 91 2618 96 HOH HOH A . J 4 HOH 92 2619 97 HOH HOH A . J 4 HOH 93 2620 98 HOH HOH A . J 4 HOH 94 2621 99 HOH HOH A . J 4 HOH 95 2622 100 HOH HOH A . J 4 HOH 96 2623 101 HOH HOH A . J 4 HOH 97 2624 102 HOH HOH A . J 4 HOH 98 2625 103 HOH HOH A . J 4 HOH 99 2626 104 HOH HOH A . J 4 HOH 100 2627 105 HOH HOH A . J 4 HOH 101 2628 106 HOH HOH A . J 4 HOH 102 2629 107 HOH HOH A . J 4 HOH 103 2630 108 HOH HOH A . J 4 HOH 104 2631 109 HOH HOH A . J 4 HOH 105 2632 110 HOH HOH A . J 4 HOH 106 2633 111 HOH HOH A . J 4 HOH 107 2634 112 HOH HOH A . J 4 HOH 108 2635 113 HOH HOH A . J 4 HOH 109 2636 114 HOH HOH A . J 4 HOH 110 2637 115 HOH HOH A . J 4 HOH 111 2638 116 HOH HOH A . J 4 HOH 112 2639 117 HOH HOH A . J 4 HOH 113 2640 118 HOH HOH A . J 4 HOH 114 2641 119 HOH HOH A . J 4 HOH 115 2642 120 HOH HOH A . J 4 HOH 116 2643 121 HOH HOH A . J 4 HOH 117 2644 122 HOH HOH A . J 4 HOH 118 2645 123 HOH HOH A . J 4 HOH 119 2646 124 HOH HOH A . J 4 HOH 120 2647 125 HOH HOH A . J 4 HOH 121 2648 126 HOH HOH A . J 4 HOH 122 2649 127 HOH HOH A . J 4 HOH 123 2650 128 HOH HOH A . J 4 HOH 124 2651 129 HOH HOH A . J 4 HOH 125 2652 130 HOH HOH A . J 4 HOH 126 2653 131 HOH HOH A . J 4 HOH 127 2654 132 HOH HOH A . J 4 HOH 128 2655 133 HOH HOH A . J 4 HOH 129 2656 135 HOH HOH A . J 4 HOH 130 2657 136 HOH HOH A . J 4 HOH 131 2658 137 HOH HOH A . J 4 HOH 132 2659 138 HOH HOH A . J 4 HOH 133 2660 139 HOH HOH A . J 4 HOH 134 2661 140 HOH HOH A . J 4 HOH 135 2662 142 HOH HOH A . J 4 HOH 136 2663 143 HOH HOH A . J 4 HOH 137 2664 145 HOH HOH A . J 4 HOH 138 2665 146 HOH HOH A . J 4 HOH 139 2666 147 HOH HOH A . J 4 HOH 140 2667 148 HOH HOH A . J 4 HOH 141 2668 149 HOH HOH A . J 4 HOH 142 2669 150 HOH HOH A . J 4 HOH 143 2670 151 HOH HOH A . J 4 HOH 144 2671 152 HOH HOH A . J 4 HOH 145 2672 154 HOH HOH A . J 4 HOH 146 2673 155 HOH HOH A . J 4 HOH 147 2674 156 HOH HOH A . J 4 HOH 148 2675 157 HOH HOH A . J 4 HOH 149 2676 158 HOH HOH A . J 4 HOH 150 2677 162 HOH HOH A . J 4 HOH 151 2678 163 HOH HOH A . J 4 HOH 152 2679 165 HOH HOH A . J 4 HOH 153 2680 166 HOH HOH A . J 4 HOH 154 2681 168 HOH HOH A . J 4 HOH 155 2682 170 HOH HOH A . J 4 HOH 156 2683 172 HOH HOH A . J 4 HOH 157 2684 173 HOH HOH A . J 4 HOH 158 2685 174 HOH HOH A . J 4 HOH 159 2686 175 HOH HOH A . J 4 HOH 160 2687 176 HOH HOH A . J 4 HOH 161 2688 177 HOH HOH A . J 4 HOH 162 2689 178 HOH HOH A . J 4 HOH 163 2690 179 HOH HOH A . J 4 HOH 164 2691 180 HOH HOH A . J 4 HOH 165 2692 181 HOH HOH A . J 4 HOH 166 2693 182 HOH HOH A . J 4 HOH 167 2694 183 HOH HOH A . J 4 HOH 168 2695 184 HOH HOH A . J 4 HOH 169 2696 185 HOH HOH A . J 4 HOH 170 2697 187 HOH HOH A . J 4 HOH 171 2698 188 HOH HOH A . J 4 HOH 172 2699 189 HOH HOH A . J 4 HOH 173 2700 190 HOH HOH A . J 4 HOH 174 2701 191 HOH HOH A . J 4 HOH 175 2702 192 HOH HOH A . J 4 HOH 176 2703 194 HOH HOH A . J 4 HOH 177 2704 195 HOH HOH A . J 4 HOH 178 2705 196 HOH HOH A . J 4 HOH 179 2706 197 HOH HOH A . J 4 HOH 180 2707 198 HOH HOH A . J 4 HOH 181 2708 199 HOH HOH A . J 4 HOH 182 2709 200 HOH HOH A . J 4 HOH 183 2710 201 HOH HOH A . J 4 HOH 184 2711 202 HOH HOH A . J 4 HOH 185 2712 204 HOH HOH A . J 4 HOH 186 2713 205 HOH HOH A . J 4 HOH 187 2714 206 HOH HOH A . J 4 HOH 188 2715 207 HOH HOH A . J 4 HOH 189 2716 209 HOH HOH A . J 4 HOH 190 2717 211 HOH HOH A . J 4 HOH 191 2718 214 HOH HOH A . J 4 HOH 192 2719 215 HOH HOH A . J 4 HOH 193 2720 223 HOH HOH A . J 4 HOH 194 2721 226 HOH HOH A . J 4 HOH 195 2722 227 HOH HOH A . J 4 HOH 196 2723 228 HOH HOH A . J 4 HOH 197 2724 229 HOH HOH A . J 4 HOH 198 2725 231 HOH HOH A . J 4 HOH 199 2726 232 HOH HOH A . J 4 HOH 200 2727 233 HOH HOH A . J 4 HOH 201 2728 234 HOH HOH A . J 4 HOH 202 2729 235 HOH HOH A . J 4 HOH 203 2730 236 HOH HOH A . J 4 HOH 204 2731 237 HOH HOH A . J 4 HOH 205 2732 238 HOH HOH A . J 4 HOH 206 2733 239 HOH HOH A . J 4 HOH 207 2734 240 HOH HOH A . J 4 HOH 208 2735 242 HOH HOH A . J 4 HOH 209 2736 245 HOH HOH A . J 4 HOH 210 2737 246 HOH HOH A . J 4 HOH 211 2738 250 HOH HOH A . J 4 HOH 212 2739 252 HOH HOH A . J 4 HOH 213 2740 253 HOH HOH A . J 4 HOH 214 2741 254 HOH HOH A . J 4 HOH 215 2742 258 HOH HOH A . J 4 HOH 216 2743 259 HOH HOH A . J 4 HOH 217 2744 261 HOH HOH A . J 4 HOH 218 2745 262 HOH HOH A . J 4 HOH 219 2746 263 HOH HOH A . J 4 HOH 220 2747 264 HOH HOH A . J 4 HOH 221 2748 265 HOH HOH A . J 4 HOH 222 2749 266 HOH HOH A . J 4 HOH 223 2750 268 HOH HOH A . J 4 HOH 224 2751 270 HOH HOH A . J 4 HOH 225 2752 271 HOH HOH A . J 4 HOH 226 2753 272 HOH HOH A . J 4 HOH 227 2754 273 HOH HOH A . J 4 HOH 228 2755 275 HOH HOH A . J 4 HOH 229 2756 276 HOH HOH A . J 4 HOH 230 2757 278 HOH HOH A . J 4 HOH 231 2758 282 HOH HOH A . J 4 HOH 232 2759 283 HOH HOH A . J 4 HOH 233 2760 286 HOH HOH A . J 4 HOH 234 2761 288 HOH HOH A . J 4 HOH 235 2762 291 HOH HOH A . J 4 HOH 236 2763 293 HOH HOH A . J 4 HOH 237 2764 296 HOH HOH A . J 4 HOH 238 2765 300 HOH HOH A . J 4 HOH 239 2766 304 HOH HOH A . J 4 HOH 240 2767 305 HOH HOH A . J 4 HOH 241 2768 307 HOH HOH A . J 4 HOH 242 2769 309 HOH HOH A . J 4 HOH 243 2770 310 HOH HOH A . J 4 HOH 244 2771 320 HOH HOH A . J 4 HOH 245 2772 326 HOH HOH A . J 4 HOH 246 2773 327 HOH HOH A . J 4 HOH 247 2774 330 HOH HOH A . J 4 HOH 248 2775 332 HOH HOH A . J 4 HOH 249 2776 338 HOH HOH A . J 4 HOH 250 2777 339 HOH HOH A . J 4 HOH 251 2778 342 HOH HOH A . J 4 HOH 252 2779 357 HOH HOH A . J 4 HOH 253 2780 368 HOH HOH A . J 4 HOH 254 2781 379 HOH HOH A . J 4 HOH 255 2782 386 HOH HOH A . J 4 HOH 256 2783 402 HOH HOH A . J 4 HOH 257 2784 404 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 36 A ASN 54 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 71 A ASN 89 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 218 A ASN 236 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 283 A ASN 301 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 298 A ASN 316 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 340 A ASN 358 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 6710 ? 1 MORE 40.2 ? 1 'SSA (A^2)' 28510 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 10_665 -y+1,-x+1,-z+1/6 0.5000000000 -0.8660254038 0.0000000000 44.4150000000 -0.8660254038 -0.5000000000 0.0000000000 76.9290366182 0.0000000000 0.0000000000 -1.0000000000 47.0600000000 # _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 2742 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id J _pdbx_struct_special_symmetry.label_comp_id HOH _pdbx_struct_special_symmetry.label_seq_id . # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 OD1 ? A ASP 202 ? A ASP 220 ? 1_555 K ? I K . ? A K 2 ? 1_555 O ? A SER 203 ? A SER 221 ? 1_555 87.9 ? 2 OD1 ? A ASP 202 ? A ASP 220 ? 1_555 K ? I K . ? A K 2 ? 1_555 OE1 ? A GLN 204 ? A GLN 222 ? 1_555 142.3 ? 3 O ? A SER 203 ? A SER 221 ? 1_555 K ? I K . ? A K 2 ? 1_555 OE1 ? A GLN 204 ? A GLN 222 ? 1_555 86.5 ? 4 OD1 ? A ASP 202 ? A ASP 220 ? 1_555 K ? I K . ? A K 2 ? 1_555 OG ? A SER 245 ? A SER 263 ? 1_555 139.3 ? 5 O ? A SER 203 ? A SER 221 ? 1_555 K ? I K . ? A K 2 ? 1_555 OG ? A SER 245 ? A SER 263 ? 1_555 84.6 ? 6 OE1 ? A GLN 204 ? A GLN 222 ? 1_555 K ? I K . ? A K 2 ? 1_555 OG ? A SER 245 ? A SER 263 ? 1_555 77.1 ? 7 OD1 ? A ASP 202 ? A ASP 220 ? 1_555 K ? I K . ? A K 2 ? 1_555 O ? A LEU 249 ? A LEU 267 ? 1_555 99.0 ? 8 O ? A SER 203 ? A SER 221 ? 1_555 K ? I K . ? A K 2 ? 1_555 O ? A LEU 249 ? A LEU 267 ? 1_555 170.2 ? 9 OE1 ? A GLN 204 ? A GLN 222 ? 1_555 K ? I K . ? A K 2 ? 1_555 O ? A LEU 249 ? A LEU 267 ? 1_555 92.3 ? 10 OG ? A SER 245 ? A SER 263 ? 1_555 K ? I K . ? A K 2 ? 1_555 O ? A LEU 249 ? A LEU 267 ? 1_555 85.6 ? # 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 2008-06-03 2 'Structure model' 1 1 2011-07-13 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Non-polymer description' 2 2 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.4.0067 ? 1 DNA 'data collection' . ? 2 XDS 'data reduction' . ? 3 SCALA 'data scaling' . ? 4 PHASER phasing . ? 5 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 31 ? ? -145.64 -158.22 2 1 ASP A 39 ? ? -132.34 -153.44 3 1 SER A 164 ? ? -160.60 117.29 4 1 ALA A 179 ? ? -21.96 -56.98 5 1 THR A 215 ? ? 79.37 -9.94 6 1 GLU A 265 ? ? -174.90 149.76 7 1 LEU A 266 ? ? 62.87 -146.30 8 1 LYS A 279 ? ? 68.16 84.83 9 1 SER A 299 ? ? -105.57 -167.17 10 1 ASN A 358 ? ? -99.84 -75.35 # _pdbx_validate_peptide_omega.id 1 _pdbx_validate_peptide_omega.PDB_model_num 1 _pdbx_validate_peptide_omega.auth_comp_id_1 ALA _pdbx_validate_peptide_omega.auth_asym_id_1 A _pdbx_validate_peptide_omega.auth_seq_id_1 179 _pdbx_validate_peptide_omega.PDB_ins_code_1 ? _pdbx_validate_peptide_omega.label_alt_id_1 ? _pdbx_validate_peptide_omega.auth_comp_id_2 ASN _pdbx_validate_peptide_omega.auth_asym_id_2 A _pdbx_validate_peptide_omega.auth_seq_id_2 180 _pdbx_validate_peptide_omega.PDB_ins_code_2 ? _pdbx_validate_peptide_omega.label_alt_id_2 ? _pdbx_validate_peptide_omega.omega -122.19 # 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 ILE 377 ? A ILE 359 2 1 Y 1 A ASN 378 ? A ASN 360 3 1 Y 1 A THR 379 ? A THR 361 4 1 Y 1 A PRO 380 ? A PRO 362 5 1 Y 1 A ASP 381 ? A ASP 363 6 1 Y 1 A VAL 382 ? A VAL 364 7 1 Y 1 A PRO 383 ? A PRO 365 8 1 Y 1 A ILE 384 ? A ILE 366 9 1 Y 1 A CYS 385 ? A CYS 367 10 1 Y 1 A VAL 386 ? A VAL 368 11 1 Y 1 A TYR 387 ? A TYR 369 12 1 Y 1 A ASP 388 ? A ASP 370 13 1 Y 1 A SER 389 ? A SER 371 14 1 Y 1 A ASP 390 ? A ASP 372 15 1 Y 1 A PRO 391 ? A PRO 373 16 1 Y 1 A LEU 392 ? A LEU 374 17 1 Y 1 A VAL 393 ? A VAL 375 18 1 Y 1 A PRO 394 ? A PRO 376 19 1 Y 1 A ARG 395 ? A ARG 377 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 'POTASSIUM ION' K 4 water HOH #