data_3CL5 # _entry.id 3CL5 # _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 3CL5 RCSB RCSB046909 WWPDB D_1000046909 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3CL4 . unspecified PDB 1FLC . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3CL5 _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.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y # 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 3CL5 _cell.length_a 89.240 _cell.length_b 89.240 _cell.length_c 280.380 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 12 _cell.pdbx_unique_axis ? # _symmetry.entry_id 3CL5 _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 # 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 42630.230 1 3.1.1.53 S40A 'residues 19-388' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 7 ? ? ? ? 3 non-polymer man 'methyl 4,9-di-O-acetyl-5-(acetylamino)-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosidonic acid' 407.370 1 ? ? ? ? 4 non-polymer syn 'POTASSIUM ION' 39.098 1 ? ? ? ? 5 non-polymer syn 'ACETIC ACID' 60.052 1 ? ? ? ? 6 water nat water 18.015 281 ? ? ? ? # _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 ;FDNPPTNVVSHLNGDWFLFGDARSDCNHVVNTNPRNYSYMDLNPALCDSGKISSKAGNSIFRSFHFTDFYNYTGEGQQII FYEGVNFTPYHAFKCTTSGSNDIWMQNKGLFYTQVYKNMAVYRSLTFVNVPYVYNGSAQSTALCKSGSLVLNNPAYIARE ANFGDYYYKVEADFYLSGCDEYIVPLCIFNGKFLSNTKYYDDSQYYFNKDTGVIYGLNSTETITTGFDFNCHYLVLPSGN YLAISNELLLTVPTKAICLNKRKDFTPVQVVDSRWNNARQSDNMTAVACQPPYCYFRNSTTNYVGVYDINHGDAGFTSIL SGLLYDSPCFSQQGVFRYDNVSSVWPLYSYGRCPTAADINTPDVPICVYDSDPLVPR ; _entity_poly.pdbx_seq_one_letter_code_can ;FDNPPTNVVSHLNGDWFLFGDARSDCNHVVNTNPRNYSYMDLNPALCDSGKISSKAGNSIFRSFHFTDFYNYTGEGQQII 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 ALA 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 11128 _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 9606 _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 3CL5 _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 3CL5 ALA A 22 ? UNP P15776 SER 40 engineered 40 1 1 3CL5 SER A 371 ? UNP P15776 ? ? 'expression tag' 389 2 1 3CL5 ASP A 372 ? UNP P15776 ? ? 'expression tag' 390 3 1 3CL5 PRO A 373 ? UNP P15776 ? ? 'expression tag' 391 4 1 3CL5 LEU A 374 ? UNP P15776 ? ? 'expression tag' 392 5 1 3CL5 VAL A 375 ? UNP P15776 ? ? 'expression tag' 393 6 1 3CL5 PRO A 376 ? UNP P15776 ? ? 'expression tag' 394 7 1 3CL5 ARG A 377 ? UNP P15776 ? ? 'expression tag' 395 8 # 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 ACY non-polymer . 'ACETIC ACID' ? 'C2 H4 O2' 60.052 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 SIO saccharide . 'methyl 4,9-di-O-acetyl-5-(acetylamino)-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosidonic acid' ? 'C16 H25 N O11' 407.370 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 3CL5 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.78 _exptl_crystal.density_percent_sol 67.46 _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 '0.04 M KH2PO4, 16% (w/v) PEG 8000, 20% (w/v) glycerol., 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 315' _diffrn_detector.pdbx_collection_date 2006-07-22 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.0723 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID23-1' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID23-1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.0723 # _reflns.entry_id 3CL5 _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I -3.7 _reflns.d_resolution_high 1.8 _reflns.d_resolution_low 77.4 _reflns.number_all 60345 _reflns.number_obs 60283 _reflns.percent_possible_obs 97.2 _reflns.pdbx_Rmerge_I_obs 0.092 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 25.5 _reflns.B_iso_Wilson_estimate 27.1 _reflns.pdbx_redundancy 20.7 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.8 _reflns_shell.d_res_low 1.9 _reflns_shell.percent_possible_all 86.6 _reflns_shell.Rmerge_I_obs 0.866 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 3.5 _reflns_shell.pdbx_redundancy 19.0 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 7667 _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 3CL5 _refine.ls_number_reflns_obs 57018 _refine.ls_number_reflns_all 57018 _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 50.00 _refine.ls_d_res_high 1.80 _refine.ls_percent_reflns_obs 96.05 _refine.ls_R_factor_obs 0.1712 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.17031 _refine.ls_R_factor_R_free 0.1883 _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 3043 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.961 _refine.correlation_coeff_Fo_to_Fc_free 0.958 _refine.B_iso_mean 25.046 _refine.aniso_B[1][1] 0.28 _refine.aniso_B[2][2] 0.28 _refine.aniso_B[3][3] -0.42 _refine.aniso_B[1][2] 0.14 _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 'wild-type structure of Hemagglutinin-esterase' _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 0.086 _refine.pdbx_overall_ESU_R_Free 0.084 _refine.overall_SU_ML 0.056 _refine.overall_SU_B 3.463 _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_TLS_residual_ADP_flag 'LIKELY RESIDUAL' _refine.pdbx_diffrn_id 1 _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 2860 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 131 _refine_hist.number_atoms_solvent 281 _refine_hist.number_atoms_total 3272 _refine_hist.d_res_high 1.80 _refine_hist.d_res_low 50.00 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.012 0.022 ? 3086 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 1988 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.334 1.974 ? 4217 'X-RAY DIFFRACTION' ? r_angle_other_deg 1.282 3.005 ? 4776 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.754 5.000 ? 357 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 34.994 24.211 ? 152 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 12.665 15.000 ? 424 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 15.925 15.000 ? 11 'X-RAY DIFFRACTION' ? r_chiral_restr 0.083 0.200 ? 456 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.006 0.021 ? 3451 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 672 'X-RAY DIFFRACTION' ? r_mcbond_it 0.625 1.500 ? 1784 'X-RAY DIFFRACTION' ? r_mcbond_other 0.164 1.500 ? 723 'X-RAY DIFFRACTION' ? r_mcangle_it 1.134 2.000 ? 2883 'X-RAY DIFFRACTION' ? r_scbond_it 1.858 3.000 ? 1302 'X-RAY DIFFRACTION' ? r_scangle_it 2.974 4.500 ? 1334 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.797 _refine_ls_shell.d_res_low 1.844 _refine_ls_shell.number_reflns_R_work 3250 _refine_ls_shell.R_factor_R_work 0.237 _refine_ls_shell.percent_reflns_obs 76.70 _refine_ls_shell.R_factor_R_free 0.282 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 197 _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 3CL5 _struct.title 'Structure of coronavirus hemagglutinin-esterase in complex with 4,9-O-diacetyl sialic acid' _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 3CL5 _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 ? K N N 5 ? L N N 6 ? # _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 43 ? CYS A 47 ? ASN A 61 CYS A 65 5 ? 5 HELX_P HELX_P3 3 SER A 59 ? PHE A 66 ? SER A 77 PHE A 84 1 ? 8 HELX_P HELX_P4 4 THR A 88 ? ALA A 92 ? THR A 106 ALA A 110 5 ? 5 HELX_P HELX_P5 5 SER A 100 ? ALA A 120 ? SER A 118 ALA A 138 1 ? 21 HELX_P HELX_P6 6 ASN A 283 ? CYS A 289 ? ASN A 301 CYS A 307 1 ? 7 HELX_P HELX_P7 7 ALA A 314 ? SER A 321 ? ALA A 332 SER A 339 1 ? 8 HELX_P HELX_P8 8 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 ? ? ? ? ? ? ? 2.076 ? disulf2 disulf ? ? A CYS 144 SG ? ? ? 1_555 A CYS 95 SG ? ? A CYS 162 A CYS 113 1_555 ? ? ? ? ? ? ? 2.044 ? disulf3 disulf ? ? A CYS 231 SG ? ? ? 1_555 A CYS 187 SG ? ? A CYS 249 A CYS 205 1_555 ? ? ? ? ? ? ? 2.081 ? disulf4 disulf ? ? A CYS 258 SG ? ? ? 1_555 A CYS 179 SG ? ? A CYS 276 A CYS 197 1_555 ? ? ? ? ? ? ? 2.101 ? disulf5 disulf ? ? A CYS 294 SG ? ? ? 1_555 A CYS 289 SG ? ? A CYS 312 A CYS 307 1_555 ? ? ? ? ? ? ? 2.075 ? disulf6 disulf ? ? A CYS 353 SG ? ? ? 1_555 A CYS 329 SG ? ? A CYS 371 A CYS 347 1_555 ? ? ? ? ? ? ? 2.058 ? covale1 covale ? ? A ASN 36 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 54 A NAG 2520 1_555 ? ? ? ? ? ? ? 1.450 ? covale2 covale ? ? A ASN 71 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 89 A NAG 2523 1_555 ? ? ? ? ? ? ? 1.444 ? metalc1 metalc ? ? A ASP 202 OD1 ? ? ? 1_555 J K . K ? ? A ASP 220 A K 2 1_555 ? ? ? ? ? ? ? 2.566 ? metalc2 metalc ? ? A SER 203 O ? ? ? 1_555 J K . K ? ? A SER 221 A K 2 1_555 ? ? ? ? ? ? ? 2.768 ? metalc3 metalc ? ? A GLN 204 OE1 ? ? ? 1_555 J K . K ? ? A GLN 222 A K 2 1_555 ? ? ? ? ? ? ? 2.968 ? covale3 covale ? ? A ASN 218 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 236 A NAG 2525 1_555 ? ? ? ? ? ? ? 1.444 ? metalc4 metalc ? ? A SER 245 OG ? ? ? 1_555 J K . K ? ? A SER 263 A K 2 1_555 ? ? ? ? ? ? ? 2.712 ? metalc5 metalc ? ? A GLU 247 O ? ? ? 1_555 J K . K ? ? A GLU 265 A K 2 1_555 ? ? ? ? ? ? ? 2.967 ? metalc6 metalc ? ? A LEU 249 O ? ? ? 1_555 J K . K ? ? A LEU 267 A K 2 1_555 ? ? ? ? ? ? ? 2.634 ? covale4 covale ? ? A ASN 283 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 301 A NAG 1961 1_555 ? ? ? ? ? ? ? 1.445 ? covale5 covale ? ? A ASN 298 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 316 A NAG 2521 1_555 ? ? ? ? ? ? ? 1.427 ? covale6 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 2525 A NAG 2526 1_555 ? ? ? ? ? ? ? 1.453 ? covale7 covale ? ? A ASN 340 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 358 A NAG 2527 1_555 ? ? ? ? ? ? ? 1.849 ? metalc7 metalc ? ? J K . K ? ? ? 1_555 L HOH . O ? ? A K 2 A HOH 2549 1_555 ? ? ? ? ? ? ? 3.025 ? # 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 -1.70 2 ASN 153 A . ? ASN 171 A PRO 154 A ? PRO 172 A 1 -6.20 3 PRO 291 A . ? PRO 309 A PRO 292 A ? PRO 310 A 1 4.49 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 5 ? B ? 5 ? C ? 7 ? D ? 3 ? E ? 2 ? F ? 2 ? G ? 2 ? H ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? parallel A 2 3 ? parallel A 3 4 ? parallel A 4 5 ? parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel B 4 5 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel C 4 5 ? anti-parallel C 5 6 ? anti-parallel C 6 7 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel E 1 2 ? anti-parallel F 1 2 ? anti-parallel G 1 2 ? anti-parallel H 1 2 ? anti-parallel H 2 3 ? 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 ILE A 52 ? LYS A 55 ? ILE A 70 LYS A 73 A 2 TRP A 16 ? ASP A 21 ? TRP A 34 ASP A 39 A 3 GLN A 78 ? TYR A 82 ? GLN A 96 TYR A 100 A 4 VAL A 268 ? VAL A 271 ? VAL A 286 VAL A 289 A 5 CYS A 294 ? ARG A 297 ? CYS A 312 ARG A 315 B 1 GLY A 74 ? GLU A 75 ? GLY A 92 GLU A 93 B 2 TYR A 122 ? ASN A 129 ? TYR A 140 ASN A 147 B 3 LYS A 255 ? ARG A 262 ? LYS A 273 ARG A 280 B 4 VAL A 170 ? PHE A 189 ? VAL A 188 PHE A 207 B 5 TYR A 132 ? VAL A 133 ? TYR A 150 VAL A 151 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 PHE A 229 ? GLU A 247 ? PHE A 247 GLU A 265 C 6 SER A 203 ? ASN A 208 ? SER A 221 ASN A 226 C 7 ILE A 214 ? ASN A 218 ? ILE A 232 ASN A 236 D 1 SER A 140 ? THR A 141 ? SER A 158 THR A 159 D 2 ALA A 155 ? ILE A 157 ? ALA A 173 ILE A 175 D 3 LEU A 250 ? VAL A 252 ? LEU A 268 VAL A 270 E 1 LYS A 145 ? SER A 146 ? LYS A 163 SER A 164 E 2 LEU A 149 ? VAL A 150 ? LEU A 167 VAL A 168 F 1 PHE A 193 ? SER A 195 ? PHE A 211 SER A 213 F 2 LYS A 198 ? TYR A 200 ? LYS A 216 TYR A 218 G 1 GLY A 305 ? ASP A 308 ? GLY A 323 ASP A 326 G 2 HIS A 311 ? ASP A 313 ? HIS A 329 ASP A 331 H 1 GLY A 334 ? PHE A 336 ? GLY A 352 PHE A 354 H 2 CYS A 329 ? SER A 331 ? CYS A 347 SER A 349 H 3 TYR A 350 ? GLY A 351 ? TYR A 368 GLY A 369 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O SER A 53 ? O SER A 71 N LEU A 18 ? N LEU A 36 A 2 3 N PHE A 19 ? N PHE A 37 O TYR A 82 ? O TYR A 100 A 3 4 N PHE A 81 ? N PHE A 99 O VAL A 271 ? O VAL A 289 A 4 5 N VAL A 270 ? N VAL A 288 O TYR A 295 ? O TYR A 313 B 1 2 N GLY A 74 ? N GLY A 92 O LEU A 125 ? O LEU A 143 B 2 3 N THR A 126 ? N THR A 144 O CYS A 258 ? O CYS A 276 B 3 4 O LEU A 259 ? O LEU A 277 N GLU A 181 ? N GLU A 199 B 4 5 O ASP A 173 ? O ASP A 191 N VAL A 133 ? N VAL A 151 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 N ALA A 172 ? N ALA A 190 O ALA A 243 ? O ALA A 261 C 5 6 O ILE A 244 ? O ILE A 262 N TYR A 205 ? N TYR A 223 C 6 7 N TYR A 206 ? N TYR A 224 O TYR A 215 ? O TYR A 233 D 1 2 N THR A 141 ? N THR A 159 O TYR A 156 ? O TYR A 174 D 2 3 N ALA A 155 ? N ALA A 173 O VAL A 252 ? O VAL A 270 E 1 2 N SER A 146 ? N SER A 164 O LEU A 149 ? O LEU A 167 F 1 2 N PHE A 193 ? N PHE A 211 O TYR A 200 ? O TYR A 218 G 1 2 N TYR A 307 ? N TYR A 325 O HIS A 311 ? O HIS A 329 H 1 2 O PHE A 336 ? O PHE A 354 N CYS A 329 ? N CYS A 347 H 2 3 N PHE A 330 ? N PHE A 348 O TYR A 350 ? O TYR A 368 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE K A 2' AC2 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE SIO A 1' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ACY A 2001' # 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 L . ? HOH A 2549 . ? 1_555 ? 8 AC2 10 TYR A 166 ? TYR A 184 . ? 1_555 ? 9 AC2 10 PHE A 193 ? PHE A 211 . ? 1_555 ? 10 AC2 10 LEU A 194 ? LEU A 212 . ? 1_555 ? 11 AC2 10 SER A 195 ? SER A 213 . ? 1_555 ? 12 AC2 10 ASN A 196 ? ASN A 214 . ? 1_555 ? 13 AC2 10 LEU A 248 ? LEU A 266 . ? 1_555 ? 14 AC2 10 LEU A 249 ? LEU A 267 . ? 1_555 ? 15 AC2 10 HOH L . ? HOH A 2683 . ? 1_555 ? 16 AC2 10 HOH L . ? HOH A 2724 . ? 1_555 ? 17 AC2 10 HOH L . ? HOH A 2796 . ? 1_555 ? 18 AC3 5 ASP A 21 ? ASP A 39 . ? 1_555 ? 19 AC3 5 ALA A 22 ? ALA A 40 . ? 1_555 ? 20 AC3 5 GLY A 57 ? GLY A 75 . ? 1_555 ? 21 AC3 5 ASN A 86 ? ASN A 104 . ? 1_555 ? 22 AC3 5 HIS A 311 ? HIS A 329 . ? 1_555 ? # _database_PDB_matrix.entry_id 3CL5 _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 3CL5 _atom_sites.fract_transf_matrix[1][1] 0.011206 _atom_sites.fract_transf_matrix[1][2] 0.006470 _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] 0.012939 _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] 0.003567 _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 ? -29.760 54.160 19.877 1.00 44.05 ? 19 PHE A N 1 ATOM 2 C CA . PHE A 1 1 ? -28.365 54.036 19.319 1.00 43.39 ? 19 PHE A CA 1 ATOM 3 C C . PHE A 1 1 ? -27.523 53.111 20.149 1.00 43.35 ? 19 PHE A C 1 ATOM 4 O O . PHE A 1 1 ? -27.571 53.119 21.381 1.00 43.38 ? 19 PHE A O 1 ATOM 5 C CB . PHE A 1 1 ? -27.678 55.398 19.266 1.00 43.61 ? 19 PHE A CB 1 ATOM 6 C CG . PHE A 1 1 ? -26.266 55.340 18.761 1.00 42.51 ? 19 PHE A CG 1 ATOM 7 C CD1 . PHE A 1 1 ? -26.004 54.979 17.454 1.00 42.10 ? 19 PHE A CD1 1 ATOM 8 C CD2 . PHE A 1 1 ? -25.207 55.648 19.596 1.00 43.80 ? 19 PHE A CD2 1 ATOM 9 C CE1 . PHE A 1 1 ? -24.699 54.924 16.978 1.00 42.57 ? 19 PHE A CE1 1 ATOM 10 C CE2 . PHE A 1 1 ? -23.892 55.598 19.132 1.00 42.35 ? 19 PHE A CE2 1 ATOM 11 C CZ . PHE A 1 1 ? -23.642 55.236 17.824 1.00 42.20 ? 19 PHE A CZ 1 ATOM 12 N N . ASP A 1 2 ? -26.701 52.362 19.434 1.00 42.75 ? 20 ASP A N 1 ATOM 13 C CA . ASP A 1 2 ? -25.908 51.280 20.005 1.00 42.16 ? 20 ASP A CA 1 ATOM 14 C C . ASP A 1 2 ? -24.500 51.282 19.382 1.00 40.09 ? 20 ASP A C 1 ATOM 15 O O . ASP A 1 2 ? -24.350 51.251 18.161 1.00 39.95 ? 20 ASP A O 1 ATOM 16 C CB . ASP A 1 2 ? -26.643 49.962 19.708 1.00 43.09 ? 20 ASP A CB 1 ATOM 17 C CG . ASP A 1 2 ? -26.091 48.775 20.482 1.00 46.32 ? 20 ASP A CG 1 ATOM 18 O OD1 . ASP A 1 2 ? -25.767 48.930 21.696 1.00 48.82 ? 20 ASP A OD1 1 ATOM 19 O OD2 . ASP A 1 2 ? -25.998 47.678 19.861 1.00 50.04 ? 20 ASP A OD2 1 ATOM 20 N N . ASN A 1 3 ? -23.479 51.340 20.225 1.00 38.18 ? 21 ASN A N 1 ATOM 21 C CA . ASN A 1 3 ? -22.082 51.332 19.741 1.00 36.67 ? 21 ASN A CA 1 ATOM 22 C C . ASN A 1 3 ? -21.220 50.356 20.551 1.00 35.81 ? 21 ASN A C 1 ATOM 23 O O . ASN A 1 3 ? -20.317 50.767 21.269 1.00 35.12 ? 21 ASN A O 1 ATOM 24 C CB . ASN A 1 3 ? -21.512 52.757 19.806 1.00 36.76 ? 21 ASN A CB 1 ATOM 25 C CG . ASN A 1 3 ? -20.144 52.899 19.117 1.00 35.79 ? 21 ASN A CG 1 ATOM 26 O OD1 . ASN A 1 3 ? -19.793 52.109 18.230 1.00 34.34 ? 21 ASN A OD1 1 ATOM 27 N ND2 . ASN A 1 3 ? -19.394 53.947 19.492 1.00 32.47 ? 21 ASN A ND2 1 ATOM 28 N N . PRO A 1 4 ? -21.520 49.058 20.460 1.00 34.73 ? 22 PRO A N 1 ATOM 29 C CA . PRO A 1 4 ? -20.790 48.091 21.270 1.00 34.76 ? 22 PRO A CA 1 ATOM 30 C C . PRO A 1 4 ? -19.441 47.750 20.649 1.00 34.44 ? 22 PRO A C 1 ATOM 31 O O . PRO A 1 4 ? -19.237 47.994 19.474 1.00 34.21 ? 22 PRO A O 1 ATOM 32 C CB . PRO A 1 4 ? -21.682 46.858 21.214 1.00 34.92 ? 22 PRO A CB 1 ATOM 33 C CG . PRO A 1 4 ? -22.336 46.943 19.871 1.00 34.85 ? 22 PRO A CG 1 ATOM 34 C CD . PRO A 1 4 ? -22.445 48.405 19.517 1.00 34.80 ? 22 PRO A CD 1 ATOM 35 N N . PRO A 1 5 ? -18.522 47.191 21.433 1.00 34.33 ? 23 PRO A N 1 ATOM 36 C CA . PRO A 1 5 ? -17.311 46.673 20.769 1.00 34.26 ? 23 PRO A CA 1 ATOM 37 C C . PRO A 1 5 ? -17.676 45.444 19.980 1.00 34.16 ? 23 PRO A C 1 ATOM 38 O O . PRO A 1 5 ? -18.405 44.574 20.480 1.00 35.89 ? 23 PRO A O 1 ATOM 39 C CB . PRO A 1 5 ? -16.394 46.293 21.937 1.00 34.42 ? 23 PRO A CB 1 ATOM 40 C CG . PRO A 1 5 ? -17.352 46.043 23.104 1.00 35.00 ? 23 PRO A CG 1 ATOM 41 C CD . PRO A 1 5 ? -18.529 46.961 22.888 1.00 34.79 ? 23 PRO A CD 1 ATOM 42 N N . THR A 1 6 ? -17.235 45.392 18.735 1.00 32.91 ? 24 THR A N 1 ATOM 43 C CA . THR A 1 6 ? -17.591 44.277 17.875 1.00 32.14 ? 24 THR A CA 1 ATOM 44 C C . THR A 1 6 ? -16.412 43.373 17.610 1.00 32.02 ? 24 THR A C 1 ATOM 45 O O . THR A 1 6 ? -15.270 43.819 17.561 1.00 30.74 ? 24 THR A O 1 ATOM 46 C CB . THR A 1 6 ? -18.223 44.758 16.551 1.00 32.65 ? 24 THR A CB 1 ATOM 47 O OG1 . THR A 1 6 ? -17.227 45.380 15.731 1.00 32.26 ? 24 THR A OG1 1 ATOM 48 C CG2 . THR A 1 6 ? -19.382 45.734 16.835 1.00 31.77 ? 24 THR A CG2 1 ATOM 49 N N . ASN A 1 7 ? -16.742 42.089 17.494 1.00 31.13 ? 25 ASN A N 1 ATOM 50 C CA . ASN A 1 7 ? -15.764 41.001 17.348 1.00 30.55 ? 25 ASN A CA 1 ATOM 51 C C . ASN A 1 7 ? -15.405 40.779 15.890 1.00 29.90 ? 25 ASN A C 1 ATOM 52 O O . ASN A 1 7 ? -15.720 39.746 15.270 1.00 29.13 ? 25 ASN A O 1 ATOM 53 C CB . ASN A 1 7 ? -16.270 39.712 17.981 1.00 31.00 ? 25 ASN A CB 1 ATOM 54 C CG . ASN A 1 7 ? -15.199 38.673 18.104 1.00 32.47 ? 25 ASN A CG 1 ATOM 55 O OD1 . ASN A 1 7 ? -14.004 38.968 17.938 1.00 33.39 ? 25 ASN A OD1 1 ATOM 56 N ND2 . ASN A 1 7 ? -15.603 37.436 18.399 1.00 32.00 ? 25 ASN A ND2 1 ATOM 57 N N . VAL A 1 8 ? -14.725 41.792 15.362 1.00 29.51 ? 26 VAL A N 1 ATOM 58 C CA . VAL A 1 8 ? -14.217 41.762 13.984 1.00 29.03 ? 26 VAL A CA 1 ATOM 59 C C . VAL A 1 8 ? -12.784 42.267 13.882 1.00 28.39 ? 26 VAL A C 1 ATOM 60 O O . VAL A 1 8 ? -12.254 42.952 14.774 1.00 27.74 ? 26 VAL A O 1 ATOM 61 C CB . VAL A 1 8 ? -15.088 42.615 13.013 1.00 29.22 ? 26 VAL A CB 1 ATOM 62 C CG1 . VAL A 1 8 ? -16.554 42.109 12.973 1.00 29.49 ? 26 VAL A CG1 1 ATOM 63 C CG2 . VAL A 1 8 ? -15.024 44.109 13.369 1.00 29.93 ? 26 VAL A CG2 1 ATOM 64 N N . VAL A 1 9 ? -12.166 41.918 12.768 1.00 28.15 ? 27 VAL A N 1 ATOM 65 C CA . VAL A 1 9 ? -10.988 42.661 12.325 1.00 28.30 ? 27 VAL A CA 1 ATOM 66 C C . VAL A 1 9 ? -11.436 43.609 11.224 1.00 28.28 ? 27 VAL A C 1 ATOM 67 O O . VAL A 1 9 ? -12.340 43.309 10.439 1.00 29.05 ? 27 VAL A O 1 ATOM 68 C CB . VAL A 1 9 ? -9.797 41.762 11.881 1.00 28.15 ? 27 VAL A CB 1 ATOM 69 C CG1 . VAL A 1 9 ? -9.244 40.935 13.101 1.00 25.99 ? 27 VAL A CG1 1 ATOM 70 C CG2 . VAL A 1 9 ? -10.185 40.845 10.689 1.00 28.22 ? 27 VAL A CG2 1 ATOM 71 N N . SER A 1 10 ? -10.828 44.775 11.216 1.00 28.12 ? 28 SER A N 1 ATOM 72 C CA . SER A 1 10 ? -11.219 45.839 10.297 1.00 28.34 ? 28 SER A CA 1 ATOM 73 C C . SER A 1 10 ? -10.033 46.757 10.052 1.00 28.59 ? 28 SER A C 1 ATOM 74 O O . SER A 1 10 ? -8.865 46.394 10.291 1.00 29.07 ? 28 SER A O 1 ATOM 75 C CB . SER A 1 10 ? -12.444 46.613 10.848 1.00 28.07 ? 28 SER A CB 1 ATOM 76 O OG . SER A 1 10 ? -13.039 47.471 9.878 1.00 27.80 ? 28 SER A OG 1 ATOM 77 N N . HIS A 1 11 ? -10.323 47.941 9.545 1.00 28.27 ? 29 HIS A N 1 ATOM 78 C CA . HIS A 1 11 ? -9.281 48.891 9.217 1.00 28.77 ? 29 HIS A CA 1 ATOM 79 C C . HIS A 1 11 ? -9.789 50.302 9.253 1.00 29.41 ? 29 HIS A C 1 ATOM 80 O O . HIS A 1 11 ? -10.927 50.574 8.882 1.00 28.96 ? 29 HIS A O 1 ATOM 81 C CB . HIS A 1 11 ? -8.712 48.620 7.824 1.00 28.58 ? 29 HIS A CB 1 ATOM 82 C CG . HIS A 1 11 ? -9.739 48.201 6.816 1.00 28.38 ? 29 HIS A CG 1 ATOM 83 N ND1 . HIS A 1 11 ? -10.552 49.097 6.155 1.00 27.92 ? 29 HIS A ND1 1 ATOM 84 C CD2 . HIS A 1 11 ? -10.067 46.976 6.344 1.00 30.78 ? 29 HIS A CD2 1 ATOM 85 C CE1 . HIS A 1 11 ? -11.332 48.439 5.313 1.00 29.50 ? 29 HIS A CE1 1 ATOM 86 N NE2 . HIS A 1 11 ? -11.064 47.149 5.412 1.00 29.55 ? 29 HIS A NE2 1 ATOM 87 N N . LEU A 1 12 ? -8.911 51.195 9.682 1.00 29.70 ? 30 LEU A N 1 ATOM 88 C CA . LEU A 1 12 ? -9.255 52.616 9.860 1.00 30.61 ? 30 LEU A CA 1 ATOM 89 C C . LEU A 1 12 ? -9.498 53.274 8.513 1.00 30.91 ? 30 LEU A C 1 ATOM 90 O O . LEU A 1 12 ? -10.418 54.074 8.328 1.00 32.03 ? 30 LEU A O 1 ATOM 91 C CB . LEU A 1 12 ? -8.124 53.342 10.591 1.00 30.57 ? 30 LEU A CB 1 ATOM 92 C CG . LEU A 1 12 ? -8.288 54.812 10.928 1.00 32.79 ? 30 LEU A CG 1 ATOM 93 C CD1 . LEU A 1 12 ? -9.427 54.978 11.950 1.00 34.49 ? 30 LEU A CD1 1 ATOM 94 C CD2 . LEU A 1 12 ? -6.959 55.389 11.443 1.00 34.24 ? 30 LEU A CD2 1 ATOM 95 N N . ASN A 1 13 ? -8.662 52.902 7.564 1.00 30.60 ? 31 ASN A N 1 ATOM 96 C CA . ASN A 1 13 ? -8.785 53.385 6.194 1.00 30.51 ? 31 ASN A CA 1 ATOM 97 C C . ASN A 1 13 ? -8.315 52.266 5.281 1.00 30.11 ? 31 ASN A C 1 ATOM 98 O O . ASN A 1 13 ? -8.261 51.113 5.717 1.00 29.80 ? 31 ASN A O 1 ATOM 99 C CB . ASN A 1 13 ? -7.987 54.675 6.002 1.00 30.70 ? 31 ASN A CB 1 ATOM 100 C CG . ASN A 1 13 ? -6.566 54.542 6.456 1.00 31.85 ? 31 ASN A CG 1 ATOM 101 O OD1 . ASN A 1 13 ? -5.894 53.576 6.101 1.00 29.28 ? 31 ASN A OD1 1 ATOM 102 N ND2 . ASN A 1 13 ? -6.104 55.488 7.286 1.00 33.33 ? 31 ASN A ND2 1 ATOM 103 N N . GLY A 1 14 ? -7.947 52.595 4.052 1.00 29.54 ? 32 GLY A N 1 ATOM 104 C CA . GLY A 1 14 ? -7.564 51.569 3.064 1.00 29.61 ? 32 GLY A CA 1 ATOM 105 C C . GLY A 1 14 ? -6.161 50.985 3.214 1.00 29.44 ? 32 GLY A C 1 ATOM 106 O O . GLY A 1 14 ? -5.765 50.058 2.495 1.00 30.11 ? 32 GLY A O 1 ATOM 107 N N . ASP A 1 15 ? -5.412 51.519 4.177 1.00 29.07 ? 33 ASP A N 1 ATOM 108 C CA . ASP A 1 15 ? -3.984 51.183 4.336 1.00 27.87 ? 33 ASP A CA 1 ATOM 109 C C . ASP A 1 15 ? -3.832 50.036 5.333 1.00 27.81 ? 33 ASP A C 1 ATOM 110 O O . ASP A 1 15 ? -3.502 50.219 6.516 1.00 28.70 ? 33 ASP A O 1 ATOM 111 C CB . ASP A 1 15 ? -3.203 52.430 4.785 1.00 28.70 ? 33 ASP A CB 1 ATOM 112 C CG . ASP A 1 15 ? -1.684 52.294 4.631 1.00 28.97 ? 33 ASP A CG 1 ATOM 113 O OD1 . ASP A 1 15 ? -1.200 51.194 4.297 1.00 29.35 ? 33 ASP A OD1 1 ATOM 114 O OD2 . ASP A 1 15 ? -0.963 53.300 4.873 1.00 29.14 ? 33 ASP A OD2 1 ATOM 115 N N . TRP A 1 16 ? -4.092 48.844 4.831 1.00 26.20 ? 34 TRP A N 1 ATOM 116 C CA . TRP A 1 16 ? -4.028 47.619 5.623 1.00 25.74 ? 34 TRP A CA 1 ATOM 117 C C . TRP A 1 16 ? -3.570 46.442 4.785 1.00 26.05 ? 34 TRP A C 1 ATOM 118 O O . TRP A 1 16 ? -3.539 46.473 3.527 1.00 27.09 ? 34 TRP A O 1 ATOM 119 C CB . TRP A 1 16 ? -5.384 47.293 6.267 1.00 25.69 ? 34 TRP A CB 1 ATOM 120 C CG . TRP A 1 16 ? -6.507 47.036 5.261 1.00 25.57 ? 34 TRP A CG 1 ATOM 121 C CD1 . TRP A 1 16 ? -7.259 47.971 4.650 1.00 28.38 ? 34 TRP A CD1 1 ATOM 122 C CD2 . TRP A 1 16 ? -6.915 45.767 4.719 1.00 25.96 ? 34 TRP A CD2 1 ATOM 123 N NE1 . TRP A 1 16 ? -8.146 47.375 3.772 1.00 27.74 ? 34 TRP A NE1 1 ATOM 124 C CE2 . TRP A 1 16 ? -7.965 46.017 3.817 1.00 27.81 ? 34 TRP A CE2 1 ATOM 125 C CE3 . TRP A 1 16 ? -6.525 44.443 4.944 1.00 27.37 ? 34 TRP A CE3 1 ATOM 126 C CZ2 . TRP A 1 16 ? -8.616 44.994 3.115 1.00 28.45 ? 34 TRP A CZ2 1 ATOM 127 C CZ3 . TRP A 1 16 ? -7.170 43.425 4.251 1.00 28.04 ? 34 TRP A CZ3 1 ATOM 128 C CH2 . TRP A 1 16 ? -8.219 43.712 3.348 1.00 28.26 ? 34 TRP A CH2 1 ATOM 129 N N . PHE A 1 17 ? -3.228 45.389 5.493 1.00 25.84 ? 35 PHE A N 1 ATOM 130 C CA . PHE A 1 17 ? -2.758 44.155 4.861 1.00 25.62 ? 35 PHE A CA 1 ATOM 131 C C . PHE A 1 17 ? -3.007 42.932 5.738 1.00 25.98 ? 35 PHE A C 1 ATOM 132 O O . PHE A 1 17 ? -2.823 42.973 6.956 1.00 26.64 ? 35 PHE A O 1 ATOM 133 C CB . PHE A 1 17 ? -1.272 44.235 4.468 1.00 25.38 ? 35 PHE A CB 1 ATOM 134 C CG . PHE A 1 17 ? -0.907 43.312 3.346 1.00 25.24 ? 35 PHE A CG 1 ATOM 135 C CD1 . PHE A 1 17 ? -0.907 43.775 2.041 1.00 25.89 ? 35 PHE A CD1 1 ATOM 136 C CD2 . PHE A 1 17 ? -0.618 41.977 3.595 1.00 24.48 ? 35 PHE A CD2 1 ATOM 137 C CE1 . PHE A 1 17 ? -0.642 42.930 0.984 1.00 24.11 ? 35 PHE A CE1 1 ATOM 138 C CE2 . PHE A 1 17 ? -0.349 41.098 2.545 1.00 26.21 ? 35 PHE A CE2 1 ATOM 139 C CZ . PHE A 1 17 ? -0.365 41.590 1.226 1.00 24.52 ? 35 PHE A CZ 1 ATOM 140 N N . LEU A 1 18 ? -3.444 41.854 5.077 1.00 25.68 ? 36 LEU A N 1 ATOM 141 C CA . LEU A 1 18 ? -3.697 40.569 5.720 1.00 25.49 ? 36 LEU A CA 1 ATOM 142 C C . LEU A 1 18 ? -2.795 39.459 5.230 1.00 25.60 ? 36 LEU A C 1 ATOM 143 O O . LEU A 1 18 ? -2.619 39.232 4.015 1.00 25.26 ? 36 LEU A O 1 ATOM 144 C CB . LEU A 1 18 ? -5.158 40.148 5.491 1.00 25.88 ? 36 LEU A CB 1 ATOM 145 C CG . LEU A 1 18 ? -5.567 38.742 5.909 1.00 26.44 ? 36 LEU A CG 1 ATOM 146 C CD1 . LEU A 1 18 ? -5.660 38.632 7.437 1.00 27.08 ? 36 LEU A CD1 1 ATOM 147 C CD2 . LEU A 1 18 ? -6.903 38.323 5.233 1.00 26.01 ? 36 LEU A CD2 1 ATOM 148 N N . PHE A 1 19 ? -2.219 38.768 6.209 1.00 25.99 ? 37 PHE A N 1 ATOM 149 C CA . PHE A 1 19 ? -1.472 37.529 5.982 1.00 25.61 ? 37 PHE A CA 1 ATOM 150 C C . PHE A 1 19 ? -2.290 36.329 6.450 1.00 26.27 ? 37 PHE A C 1 ATOM 151 O O . PHE A 1 19 ? -2.836 36.320 7.561 1.00 25.67 ? 37 PHE A O 1 ATOM 152 C CB . PHE A 1 19 ? -0.133 37.565 6.724 1.00 24.66 ? 37 PHE A CB 1 ATOM 153 C CG . PHE A 1 19 ? 0.792 38.645 6.254 1.00 25.50 ? 37 PHE A CG 1 ATOM 154 C CD1 . PHE A 1 19 ? 1.539 38.488 5.106 1.00 26.59 ? 37 PHE A CD1 1 ATOM 155 C CD2 . PHE A 1 19 ? 0.907 39.841 6.955 1.00 26.32 ? 37 PHE A CD2 1 ATOM 156 C CE1 . PHE A 1 19 ? 2.361 39.505 4.635 1.00 27.70 ? 37 PHE A CE1 1 ATOM 157 C CE2 . PHE A 1 19 ? 1.740 40.868 6.488 1.00 26.68 ? 37 PHE A CE2 1 ATOM 158 C CZ . PHE A 1 19 ? 2.468 40.687 5.339 1.00 27.62 ? 37 PHE A CZ 1 ATOM 159 N N . GLY A 1 20 ? -2.368 35.308 5.597 1.00 26.46 ? 38 GLY A N 1 ATOM 160 C CA . GLY A 1 20 ? -3.173 34.144 5.912 1.00 26.35 ? 38 GLY A CA 1 ATOM 161 C C . GLY A 1 20 ? -2.816 32.833 5.263 1.00 26.23 ? 38 GLY A C 1 ATOM 162 O O . GLY A 1 20 ? -1.713 32.627 4.754 1.00 26.11 ? 38 GLY A O 1 ATOM 163 N N . ASP A 1 21 ? -3.815 31.963 5.290 1.00 26.47 ? 39 ASP A N 1 ATOM 164 C CA . ASP A 1 21 ? -3.724 30.609 4.760 1.00 26.35 ? 39 ASP A CA 1 ATOM 165 C C . ASP A 1 21 ? -4.903 30.298 3.824 1.00 26.58 ? 39 ASP A C 1 ATOM 166 O O . ASP A 1 21 ? -5.466 31.193 3.193 1.00 25.16 ? 39 ASP A O 1 ATOM 167 C CB . ASP A 1 21 ? -3.589 29.578 5.891 1.00 26.52 ? 39 ASP A CB 1 ATOM 168 C CG . ASP A 1 21 ? -4.724 29.646 6.907 1.00 28.50 ? 39 ASP A CG 1 ATOM 169 O OD1 . ASP A 1 21 ? -5.881 29.940 6.510 1.00 28.33 ? 39 ASP A OD1 1 ATOM 170 O OD2 . ASP A 1 21 ? -4.448 29.432 8.113 1.00 28.41 ? 39 ASP A OD2 1 ATOM 171 N N . ALA A 1 22 ? -5.259 29.029 3.729 1.00 27.37 ? 40 ALA A N 1 ATOM 172 C CA . ALA A 1 22 ? -6.280 28.631 2.736 1.00 27.35 ? 40 ALA A CA 1 ATOM 173 C C . ALA A 1 22 ? -7.563 29.419 2.977 1.00 27.49 ? 40 ALA A C 1 ATOM 174 O O . ALA A 1 22 ? -8.280 29.790 2.051 1.00 28.75 ? 40 ALA A O 1 ATOM 175 C CB . ALA A 1 22 ? -6.556 27.127 2.767 1.00 27.60 ? 40 ALA A CB 1 ATOM 176 N N . ARG A 1 23 ? -7.821 29.728 4.234 1.00 27.65 ? 41 ARG A N 1 ATOM 177 C CA . ARG A 1 23 ? -9.090 30.348 4.593 1.00 27.58 ? 41 ARG A CA 1 ATOM 178 C C . ARG A 1 23 ? -9.174 31.779 4.090 1.00 27.43 ? 41 ARG A C 1 ATOM 179 O O . ARG A 1 23 ? -10.226 32.432 4.200 1.00 26.91 ? 41 ARG A O 1 ATOM 180 C CB . ARG A 1 23 ? -9.321 30.262 6.098 1.00 27.86 ? 41 ARG A CB 1 ATOM 181 C CG . ARG A 1 23 ? -9.514 28.853 6.566 1.00 28.56 ? 41 ARG A CG 1 ATOM 182 C CD . ARG A 1 23 ? -9.142 28.708 8.019 1.00 28.90 ? 41 ARG A CD 1 ATOM 183 N NE . ARG A 1 23 ? -9.432 27.375 8.535 1.00 28.79 ? 41 ARG A NE 1 ATOM 184 C CZ . ARG A 1 23 ? -9.119 26.999 9.769 1.00 31.66 ? 41 ARG A CZ 1 ATOM 185 N NH1 . ARG A 1 23 ? -8.510 27.867 10.573 1.00 29.68 ? 41 ARG A NH1 1 ATOM 186 N NH2 . ARG A 1 23 ? -9.405 25.787 10.208 1.00 31.56 ? 41 ARG A NH2 1 ATOM 187 N N . SER A 1 24 ? -8.066 32.272 3.523 1.00 25.95 ? 42 SER A N 1 ATOM 188 C CA . SER A 1 24 ? -8.084 33.605 2.893 1.00 26.24 ? 42 SER A CA 1 ATOM 189 C C . SER A 1 24 ? -7.260 33.673 1.609 1.00 26.56 ? 42 SER A C 1 ATOM 190 O O . SER A 1 24 ? -6.821 34.746 1.171 1.00 26.70 ? 42 SER A O 1 ATOM 191 C CB . SER A 1 24 ? -7.653 34.689 3.874 1.00 26.04 ? 42 SER A CB 1 ATOM 192 O OG . SER A 1 24 ? -6.383 34.412 4.409 1.00 27.94 ? 42 SER A OG 1 ATOM 193 N N . ASP A 1 25 ? -7.086 32.507 1.000 1.00 27.34 ? 43 ASP A N 1 ATOM 194 C CA . ASP A 1 25 ? -6.274 32.332 -0.223 1.00 27.03 ? 43 ASP A CA 1 ATOM 195 C C . ASP A 1 25 ? -7.162 32.261 -1.445 1.00 27.63 ? 43 ASP A C 1 ATOM 196 O O . ASP A 1 25 ? -7.657 31.204 -1.808 1.00 27.27 ? 43 ASP A O 1 ATOM 197 C CB . ASP A 1 25 ? -5.461 31.050 -0.145 1.00 27.23 ? 43 ASP A CB 1 ATOM 198 C CG . ASP A 1 25 ? -4.572 30.820 -1.375 1.00 27.30 ? 43 ASP A CG 1 ATOM 199 O OD1 . ASP A 1 25 ? -4.507 31.691 -2.284 1.00 27.31 ? 43 ASP A OD1 1 ATOM 200 O OD2 . ASP A 1 25 ? -3.942 29.735 -1.426 1.00 28.67 ? 43 ASP A OD2 1 ATOM 201 N N . CYS A 1 26 ? -7.311 33.398 -2.087 1.00 28.49 ? 44 CYS A N 1 ATOM 202 C CA . CYS A 1 26 ? -8.171 33.509 -3.277 1.00 30.16 ? 44 CYS A CA 1 ATOM 203 C C . CYS A 1 26 ? -7.719 32.598 -4.414 1.00 30.06 ? 44 CYS A C 1 ATOM 204 O O . CYS A 1 26 ? -8.520 32.144 -5.235 1.00 30.57 ? 44 CYS A O 1 ATOM 205 C CB . CYS A 1 26 ? -8.194 34.968 -3.752 1.00 30.68 ? 44 CYS A CB 1 ATOM 206 S SG . CYS A 1 26 ? -9.022 36.065 -2.549 1.00 37.04 ? 44 CYS A SG 1 ATOM 207 N N . ASN A 1 27 ? -6.425 32.328 -4.456 1.00 30.10 ? 45 ASN A N 1 ATOM 208 C CA . ASN A 1 27 ? -5.847 31.586 -5.594 1.00 30.57 ? 45 ASN A CA 1 ATOM 209 C C . ASN A 1 27 ? -6.164 30.115 -5.523 1.00 29.58 ? 45 ASN A C 1 ATOM 210 O O . ASN A 1 27 ? -6.130 29.400 -6.529 1.00 30.17 ? 45 ASN A O 1 ATOM 211 C CB . ASN A 1 27 ? -4.344 31.759 -5.668 1.00 31.09 ? 45 ASN A CB 1 ATOM 212 C CG . ASN A 1 27 ? -3.948 33.181 -5.881 1.00 36.06 ? 45 ASN A CG 1 ATOM 213 O OD1 . ASN A 1 27 ? -2.994 33.675 -5.266 1.00 43.77 ? 45 ASN A OD1 1 ATOM 214 N ND2 . ASN A 1 27 ? -4.703 33.883 -6.721 1.00 40.75 ? 45 ASN A ND2 1 ATOM 215 N N . HIS A 1 28 ? -6.501 29.678 -4.328 1.00 29.17 ? 46 HIS A N 1 ATOM 216 C CA . HIS A 1 28 ? -6.690 28.257 -4.072 1.00 29.06 ? 46 HIS A CA 1 ATOM 217 C C . HIS A 1 28 ? -7.837 27.724 -4.918 1.00 29.61 ? 46 HIS A C 1 ATOM 218 O O . HIS A 1 28 ? -7.940 26.520 -5.200 1.00 28.80 ? 46 HIS A O 1 ATOM 219 C CB . HIS A 1 28 ? -6.978 27.999 -2.595 1.00 29.32 ? 46 HIS A CB 1 ATOM 220 C CG . HIS A 1 28 ? -7.169 26.555 -2.278 1.00 28.99 ? 46 HIS A CG 1 ATOM 221 N ND1 . HIS A 1 28 ? -6.214 25.608 -2.576 1.00 31.00 ? 46 HIS A ND1 1 ATOM 222 C CD2 . HIS A 1 28 ? -8.227 25.882 -1.768 1.00 30.99 ? 46 HIS A CD2 1 ATOM 223 C CE1 . HIS A 1 28 ? -6.663 24.414 -2.231 1.00 31.72 ? 46 HIS A CE1 1 ATOM 224 N NE2 . HIS A 1 28 ? -7.885 24.553 -1.741 1.00 32.50 ? 46 HIS A NE2 1 ATOM 225 N N . VAL A 1 29 ? -8.704 28.640 -5.311 1.00 29.38 ? 47 VAL A N 1 ATOM 226 C CA . VAL A 1 29 ? -9.974 28.245 -5.933 1.00 29.81 ? 47 VAL A CA 1 ATOM 227 C C . VAL A 1 29 ? -9.681 27.484 -7.222 1.00 30.00 ? 47 VAL A C 1 ATOM 228 O O . VAL A 1 29 ? -10.471 26.654 -7.669 1.00 29.86 ? 47 VAL A O 1 ATOM 229 C CB . VAL A 1 29 ? -10.898 29.465 -6.204 1.00 29.18 ? 47 VAL A CB 1 ATOM 230 C CG1 . VAL A 1 29 ? -10.311 30.364 -7.287 1.00 28.40 ? 47 VAL A CG1 1 ATOM 231 C CG2 . VAL A 1 29 ? -12.311 29.012 -6.576 1.00 29.83 ? 47 VAL A CG2 1 ATOM 232 N N . VAL A 1 30 ? -8.527 27.763 -7.816 1.00 30.83 ? 48 VAL A N 1 ATOM 233 C CA . VAL A 1 30 ? -8.190 27.126 -9.101 1.00 31.46 ? 48 VAL A CA 1 ATOM 234 C C . VAL A 1 30 ? -7.940 25.657 -8.875 1.00 32.50 ? 48 VAL A C 1 ATOM 235 O O . VAL A 1 30 ? -7.934 24.856 -9.827 1.00 32.21 ? 48 VAL A O 1 ATOM 236 C CB . VAL A 1 30 ? -6.960 27.740 -9.808 1.00 31.79 ? 48 VAL A CB 1 ATOM 237 C CG1 . VAL A 1 30 ? -7.155 29.255 -10.027 1.00 32.64 ? 48 VAL A CG1 1 ATOM 238 C CG2 . VAL A 1 30 ? -5.673 27.443 -9.027 1.00 30.86 ? 48 VAL A CG2 1 ATOM 239 N N . ASN A 1 31 ? -7.771 25.299 -7.610 1.00 33.71 ? 49 ASN A N 1 ATOM 240 C CA . ASN A 1 31 ? -7.454 23.912 -7.240 1.00 35.23 ? 49 ASN A CA 1 ATOM 241 C C . ASN A 1 31 ? -8.628 23.244 -6.563 1.00 36.02 ? 49 ASN A C 1 ATOM 242 O O . ASN A 1 31 ? -8.482 22.241 -5.869 1.00 37.09 ? 49 ASN A O 1 ATOM 243 C CB . ASN A 1 31 ? -6.184 23.826 -6.390 1.00 35.10 ? 49 ASN A CB 1 ATOM 244 C CG . ASN A 1 31 ? -4.974 24.323 -7.135 1.00 35.60 ? 49 ASN A CG 1 ATOM 245 O OD1 . ASN A 1 31 ? -4.758 23.961 -8.296 1.00 35.03 ? 49 ASN A OD1 1 ATOM 246 N ND2 . ASN A 1 31 ? -4.209 25.209 -6.505 1.00 35.67 ? 49 ASN A ND2 1 ATOM 247 N N . THR A 1 32 ? -9.796 23.833 -6.779 1.00 36.54 ? 50 THR A N 1 ATOM 248 C CA . THR A 1 32 ? -11.059 23.217 -6.388 1.00 36.54 ? 50 THR A CA 1 ATOM 249 C C . THR A 1 32 ? -11.806 22.828 -7.654 1.00 37.46 ? 50 THR A C 1 ATOM 250 O O . THR A 1 32 ? -11.730 23.505 -8.679 1.00 36.96 ? 50 THR A O 1 ATOM 251 C CB . THR A 1 32 ? -11.963 24.141 -5.519 1.00 36.45 ? 50 THR A CB 1 ATOM 252 O OG1 . THR A 1 32 ? -12.334 25.318 -6.253 1.00 35.21 ? 50 THR A OG1 1 ATOM 253 C CG2 . THR A 1 32 ? -11.247 24.537 -4.235 1.00 35.53 ? 50 THR A CG2 1 ATOM 254 N N . ASN A 1 33 ? -12.522 21.721 -7.568 1.00 38.38 ? 51 ASN A N 1 ATOM 255 C CA . ASN A 1 33 ? -13.314 21.256 -8.706 1.00 38.99 ? 51 ASN A CA 1 ATOM 256 C C . ASN A 1 33 ? -14.606 20.587 -8.274 1.00 38.71 ? 51 ASN A C 1 ATOM 257 O O . ASN A 1 33 ? -14.577 19.590 -7.569 1.00 39.45 ? 51 ASN A O 1 ATOM 258 C CB . ASN A 1 33 ? -12.494 20.299 -9.560 1.00 39.55 ? 51 ASN A CB 1 ATOM 259 C CG . ASN A 1 33 ? -13.237 19.849 -10.795 1.00 41.01 ? 51 ASN A CG 1 ATOM 260 O OD1 . ASN A 1 33 ? -13.882 20.648 -11.485 1.00 42.92 ? 51 ASN A OD1 1 ATOM 261 N ND2 . ASN A 1 33 ? -13.154 18.563 -11.087 1.00 44.06 ? 51 ASN A ND2 1 ATOM 262 N N . PRO A 1 34 ? -15.742 21.168 -8.672 1.00 38.18 ? 52 PRO A N 1 ATOM 263 C CA . PRO A 1 34 ? -15.708 22.404 -9.449 1.00 37.80 ? 52 PRO A CA 1 ATOM 264 C C . PRO A 1 34 ? -15.279 23.586 -8.600 1.00 37.33 ? 52 PRO A C 1 ATOM 265 O O . PRO A 1 34 ? -15.230 23.485 -7.375 1.00 37.45 ? 52 PRO A O 1 ATOM 266 C CB . PRO A 1 34 ? -17.156 22.593 -9.868 1.00 38.19 ? 52 PRO A CB 1 ATOM 267 C CG . PRO A 1 34 ? -17.938 21.944 -8.776 1.00 38.36 ? 52 PRO A CG 1 ATOM 268 C CD . PRO A 1 34 ? -17.115 20.769 -8.327 1.00 38.46 ? 52 PRO A CD 1 ATOM 269 N N . ARG A 1 35 ? -14.995 24.698 -9.263 1.00 36.34 ? 53 ARG A N 1 ATOM 270 C CA . ARG A 1 35 ? -14.522 25.894 -8.559 1.00 35.63 ? 53 ARG A CA 1 ATOM 271 C C . ARG A 1 35 ? -15.546 26.387 -7.560 1.00 35.15 ? 53 ARG A C 1 ATOM 272 O O . ARG A 1 35 ? -16.719 26.589 -7.861 1.00 33.60 ? 53 ARG A O 1 ATOM 273 C CB . ARG A 1 35 ? -14.119 26.998 -9.529 1.00 35.52 ? 53 ARG A CB 1 ATOM 274 C CG . ARG A 1 35 ? -12.810 26.633 -10.195 1.00 35.98 ? 53 ARG A CG 1 ATOM 275 C CD . ARG A 1 35 ? -12.172 27.787 -10.881 1.00 35.15 ? 53 ARG A CD 1 ATOM 276 N NE . ARG A 1 35 ? -11.040 27.360 -11.692 1.00 34.16 ? 53 ARG A NE 1 ATOM 277 C CZ . ARG A 1 35 ? -10.272 28.206 -12.370 1.00 34.64 ? 53 ARG A CZ 1 ATOM 278 N NH1 . ARG A 1 35 ? -10.529 29.505 -12.317 1.00 33.40 ? 53 ARG A NH1 1 ATOM 279 N NH2 . ARG A 1 35 ? -9.248 27.769 -13.093 1.00 32.86 ? 53 ARG A NH2 1 ATOM 280 N N . ASN A 1 36 ? -15.060 26.583 -6.347 1.00 33.93 ? 54 ASN A N 1 ATOM 281 C CA . ASN A 1 36 ? -15.934 26.878 -5.212 1.00 33.86 ? 54 ASN A CA 1 ATOM 282 C C . ASN A 1 36 ? -15.169 27.681 -4.169 1.00 32.98 ? 54 ASN A C 1 ATOM 283 O O . ASN A 1 36 ? -14.117 27.242 -3.719 1.00 33.31 ? 54 ASN A O 1 ATOM 284 C CB . ASN A 1 36 ? -16.406 25.558 -4.605 1.00 33.95 ? 54 ASN A CB 1 ATOM 285 C CG . ASN A 1 36 ? -17.568 25.728 -3.638 1.00 37.19 ? 54 ASN A CG 1 ATOM 286 O OD1 . ASN A 1 36 ? -17.573 26.627 -2.807 1.00 35.79 ? 54 ASN A OD1 1 ATOM 287 N ND2 . ASN A 1 36 ? -18.566 24.835 -3.744 1.00 41.28 ? 54 ASN A ND2 1 ATOM 288 N N . TYR A 1 37 ? -15.698 28.842 -3.795 1.00 32.09 ? 55 TYR A N 1 ATOM 289 C CA . TYR A 1 37 ? -15.013 29.737 -2.835 1.00 31.40 ? 55 TYR A CA 1 ATOM 290 C C . TYR A 1 37 ? -15.381 29.464 -1.369 1.00 31.73 ? 55 TYR A C 1 ATOM 291 O O . TYR A 1 37 ? -14.921 30.157 -0.460 1.00 31.37 ? 55 TYR A O 1 ATOM 292 C CB . TYR A 1 37 ? -15.306 31.212 -3.157 1.00 31.14 ? 55 TYR A CB 1 ATOM 293 C CG . TYR A 1 37 ? -14.668 31.724 -4.425 1.00 29.73 ? 55 TYR A CG 1 ATOM 294 C CD1 . TYR A 1 37 ? -13.372 32.223 -4.428 1.00 28.40 ? 55 TYR A CD1 1 ATOM 295 C CD2 . TYR A 1 37 ? -15.368 31.708 -5.620 1.00 29.11 ? 55 TYR A CD2 1 ATOM 296 C CE1 . TYR A 1 37 ? -12.794 32.705 -5.580 1.00 28.16 ? 55 TYR A CE1 1 ATOM 297 C CE2 . TYR A 1 37 ? -14.795 32.185 -6.795 1.00 30.60 ? 55 TYR A CE2 1 ATOM 298 C CZ . TYR A 1 37 ? -13.512 32.683 -6.766 1.00 29.62 ? 55 TYR A CZ 1 ATOM 299 O OH . TYR A 1 37 ? -12.937 33.134 -7.935 1.00 31.40 ? 55 TYR A OH 1 ATOM 300 N N . SER A 1 38 ? -16.188 28.439 -1.132 1.00 31.95 ? 56 SER A N 1 ATOM 301 C CA . SER A 1 38 ? -16.762 28.241 0.206 1.00 32.44 ? 56 SER A CA 1 ATOM 302 C C . SER A 1 38 ? -15.724 27.759 1.246 1.00 31.58 ? 56 SER A C 1 ATOM 303 O O . SER A 1 38 ? -16.014 27.677 2.441 1.00 31.78 ? 56 SER A O 1 ATOM 304 C CB . SER A 1 38 ? -18.012 27.348 0.155 1.00 33.24 ? 56 SER A CB 1 ATOM 305 O OG . SER A 1 38 ? -17.699 26.015 -0.210 1.00 37.44 ? 56 SER A OG 1 ATOM 306 N N . TYR A 1 39 ? -14.513 27.473 0.778 1.00 30.36 ? 57 TYR A N 1 ATOM 307 C CA . TYR A 1 39 ? -13.397 27.047 1.678 1.00 29.71 ? 57 TYR A CA 1 ATOM 308 C C . TYR A 1 39 ? -12.842 28.238 2.448 1.00 29.91 ? 57 TYR A C 1 ATOM 309 O O . TYR A 1 39 ? -12.070 28.091 3.411 1.00 29.45 ? 57 TYR A O 1 ATOM 310 C CB . TYR A 1 39 ? -12.253 26.392 0.897 1.00 29.49 ? 57 TYR A CB 1 ATOM 311 C CG . TYR A 1 39 ? -11.586 27.339 -0.062 1.00 28.63 ? 57 TYR A CG 1 ATOM 312 C CD1 . TYR A 1 39 ? -10.527 28.166 0.348 1.00 26.82 ? 57 TYR A CD1 1 ATOM 313 C CD2 . TYR A 1 39 ? -12.020 27.429 -1.381 1.00 28.02 ? 57 TYR A CD2 1 ATOM 314 C CE1 . TYR A 1 39 ? -9.928 29.051 -0.548 1.00 28.32 ? 57 TYR A CE1 1 ATOM 315 C CE2 . TYR A 1 39 ? -11.425 28.302 -2.286 1.00 28.84 ? 57 TYR A CE2 1 ATOM 316 C CZ . TYR A 1 39 ? -10.395 29.120 -1.867 1.00 27.97 ? 57 TYR A CZ 1 ATOM 317 O OH . TYR A 1 39 ? -9.856 29.977 -2.782 1.00 27.03 ? 57 TYR A OH 1 ATOM 318 N N . MET A 1 40 ? -13.243 29.420 2.004 1.00 29.49 ? 58 MET A N 1 ATOM 319 C CA . MET A 1 40 ? -12.773 30.673 2.603 1.00 30.46 ? 58 MET A CA 1 ATOM 320 C C . MET A 1 40 ? -13.652 31.234 3.684 1.00 29.93 ? 58 MET A C 1 ATOM 321 O O . MET A 1 40 ? -14.867 31.150 3.616 1.00 30.11 ? 58 MET A O 1 ATOM 322 C CB . MET A 1 40 ? -12.602 31.745 1.545 1.00 30.75 ? 58 MET A CB 1 ATOM 323 C CG . MET A 1 40 ? -11.403 31.421 0.674 1.00 33.55 ? 58 MET A CG 1 ATOM 324 S SD . MET A 1 40 ? -10.637 32.864 -0.019 1.00 35.41 ? 58 MET A SD 1 ATOM 325 C CE . MET A 1 40 ? -11.980 33.460 -1.005 1.00 30.88 ? 58 MET A CE 1 ATOM 326 N N . ASP A 1 41 ? -12.984 31.835 4.655 1.00 28.59 ? 59 ASP A N 1 ATOM 327 C CA . ASP A 1 41 ? -13.628 32.675 5.672 1.00 28.44 ? 59 ASP A CA 1 ATOM 328 C C . ASP A 1 41 ? -13.623 34.145 5.237 1.00 27.90 ? 59 ASP A C 1 ATOM 329 O O . ASP A 1 41 ? -14.472 34.942 5.616 1.00 28.15 ? 59 ASP A O 1 ATOM 330 C CB . ASP A 1 41 ? -12.921 32.523 7.020 1.00 28.09 ? 59 ASP A CB 1 ATOM 331 C CG . ASP A 1 41 ? -13.124 31.168 7.606 1.00 30.00 ? 59 ASP A CG 1 ATOM 332 O OD1 . ASP A 1 41 ? -14.228 30.573 7.373 1.00 30.29 ? 59 ASP A OD1 1 ATOM 333 O OD2 . ASP A 1 41 ? -12.181 30.681 8.251 1.00 29.91 ? 59 ASP A OD2 1 ATOM 334 N N . LEU A 1 42 ? -12.643 34.487 4.425 1.00 26.86 ? 60 LEU A N 1 ATOM 335 C CA . LEU A 1 42 ? -12.565 35.815 3.825 1.00 26.43 ? 60 LEU A CA 1 ATOM 336 C C . LEU A 1 42 ? -13.667 35.940 2.791 1.00 26.63 ? 60 LEU A C 1 ATOM 337 O O . LEU A 1 42 ? -13.988 34.970 2.132 1.00 26.22 ? 60 LEU A O 1 ATOM 338 C CB . LEU A 1 42 ? -11.217 35.972 3.116 1.00 27.14 ? 60 LEU A CB 1 ATOM 339 C CG . LEU A 1 42 ? -10.915 37.308 2.469 1.00 27.91 ? 60 LEU A CG 1 ATOM 340 C CD1 . LEU A 1 42 ? -10.530 38.325 3.525 1.00 27.75 ? 60 LEU A CD1 1 ATOM 341 C CD2 . LEU A 1 42 ? -9.810 37.175 1.426 1.00 29.99 ? 60 LEU A CD2 1 ATOM 342 N N . ASN A 1 43 ? -14.226 37.134 2.659 1.00 26.08 ? 61 ASN A N 1 ATOM 343 C CA . ASN A 1 43 ? -15.193 37.388 1.591 1.00 27.15 ? 61 ASN A CA 1 ATOM 344 C C . ASN A 1 43 ? -14.501 37.497 0.235 1.00 26.69 ? 61 ASN A C 1 ATOM 345 O O . ASN A 1 43 ? -13.603 38.314 0.065 1.00 27.22 ? 61 ASN A O 1 ATOM 346 C CB . ASN A 1 43 ? -16.032 38.636 1.853 1.00 26.90 ? 61 ASN A CB 1 ATOM 347 C CG . ASN A 1 43 ? -17.258 38.687 0.973 1.00 27.84 ? 61 ASN A CG 1 ATOM 348 O OD1 . ASN A 1 43 ? -17.154 38.924 -0.231 1.00 26.91 ? 61 ASN A OD1 1 ATOM 349 N ND2 . ASN A 1 43 ? -18.423 38.438 1.561 1.00 27.96 ? 61 ASN A ND2 1 ATOM 350 N N . PRO A 1 44 ? -14.946 36.704 -0.762 1.00 26.64 ? 62 PRO A N 1 ATOM 351 C CA . PRO A 1 44 ? -14.246 36.776 -2.038 1.00 26.76 ? 62 PRO A CA 1 ATOM 352 C C . PRO A 1 44 ? -14.287 38.130 -2.702 1.00 26.52 ? 62 PRO A C 1 ATOM 353 O O . PRO A 1 44 ? -13.512 38.398 -3.598 1.00 26.10 ? 62 PRO A O 1 ATOM 354 C CB . PRO A 1 44 ? -14.959 35.713 -2.888 1.00 27.12 ? 62 PRO A CB 1 ATOM 355 C CG . PRO A 1 44 ? -15.354 34.707 -1.904 1.00 26.26 ? 62 PRO A CG 1 ATOM 356 C CD . PRO A 1 44 ? -15.787 35.502 -0.687 1.00 27.38 ? 62 PRO A CD 1 ATOM 357 N N . ALA A 1 45 ? -15.171 38.997 -2.247 1.00 26.75 ? 63 ALA A N 1 ATOM 358 C CA . ALA A 1 45 ? -15.223 40.339 -2.834 1.00 26.48 ? 63 ALA A CA 1 ATOM 359 C C . ALA A 1 45 ? -13.886 41.067 -2.611 1.00 27.18 ? 63 ALA A C 1 ATOM 360 O O . ALA A 1 45 ? -13.578 42.062 -3.260 1.00 26.92 ? 63 ALA A O 1 ATOM 361 C CB . ALA A 1 45 ? -16.372 41.145 -2.264 1.00 26.32 ? 63 ALA A CB 1 ATOM 362 N N . LEU A 1 46 ? -13.101 40.564 -1.673 1.00 28.07 ? 64 LEU A N 1 ATOM 363 C CA . LEU A 1 46 ? -11.782 41.181 -1.341 1.00 29.35 ? 64 LEU A CA 1 ATOM 364 C C . LEU A 1 46 ? -10.644 40.603 -2.180 1.00 30.55 ? 64 LEU A C 1 ATOM 365 O O . LEU A 1 46 ? -9.464 40.946 -1.984 1.00 30.98 ? 64 LEU A O 1 ATOM 366 C CB . LEU A 1 46 ? -11.453 41.014 0.148 1.00 28.93 ? 64 LEU A CB 1 ATOM 367 C CG . LEU A 1 46 ? -12.294 41.892 1.088 1.00 29.63 ? 64 LEU A CG 1 ATOM 368 C CD1 . LEU A 1 46 ? -12.409 41.327 2.522 1.00 29.34 ? 64 LEU A CD1 1 ATOM 369 C CD2 . LEU A 1 46 ? -11.758 43.304 1.101 1.00 30.41 ? 64 LEU A CD2 1 ATOM 370 N N . CYS A 1 47 ? -10.995 39.711 -3.096 1.00 30.66 ? 65 CYS A N 1 ATOM 371 C CA . CYS A 1 47 ? -9.953 38.972 -3.865 1.00 32.39 ? 65 CYS A CA 1 ATOM 372 C C . CYS A 1 47 ? -9.114 39.840 -4.811 1.00 32.46 ? 65 CYS A C 1 ATOM 373 O O . CYS A 1 47 ? -7.970 39.479 -5.134 1.00 34.29 ? 65 CYS A O 1 ATOM 374 C CB . CYS A 1 47 ? -10.545 37.764 -4.594 1.00 33.05 ? 65 CYS A CB 1 ATOM 375 S SG . CYS A 1 47 ? -10.864 36.433 -3.432 1.00 37.98 ? 65 CYS A SG 1 ATOM 376 N N . ASP A 1 48 ? -9.632 41.000 -5.187 1.00 31.22 ? 66 ASP A N 1 ATOM 377 C CA . ASP A 1 48 ? -8.942 41.876 -6.142 1.00 31.86 ? 66 ASP A CA 1 ATOM 378 C C . ASP A 1 48 ? -8.241 43.035 -5.458 1.00 31.55 ? 66 ASP A C 1 ATOM 379 O O . ASP A 1 48 ? -7.752 43.954 -6.117 1.00 32.50 ? 66 ASP A O 1 ATOM 380 C CB . ASP A 1 48 ? -9.932 42.472 -7.159 1.00 31.82 ? 66 ASP A CB 1 ATOM 381 C CG . ASP A 1 48 ? -9.249 43.006 -8.426 1.00 33.82 ? 66 ASP A CG 1 ATOM 382 O OD1 . ASP A 1 48 ? -8.385 42.304 -8.992 1.00 35.37 ? 66 ASP A OD1 1 ATOM 383 O OD2 . ASP A 1 48 ? -9.626 44.109 -8.896 1.00 34.84 ? 66 ASP A OD2 1 ATOM 384 N N . SER A 1 49 ? -8.203 42.993 -4.140 1.00 31.55 ? 67 SER A N 1 ATOM 385 C CA . SER A 1 49 ? -7.847 44.187 -3.367 1.00 31.31 ? 67 SER A CA 1 ATOM 386 C C . SER A 1 49 ? -6.347 44.483 -3.399 1.00 30.80 ? 67 SER A C 1 ATOM 387 O O . SER A 1 49 ? -5.927 45.633 -3.263 1.00 31.96 ? 67 SER A O 1 ATOM 388 C CB . SER A 1 49 ? -8.315 44.040 -1.924 1.00 31.51 ? 67 SER A CB 1 ATOM 389 O OG . SER A 1 49 ? -7.626 42.961 -1.325 1.00 31.22 ? 67 SER A OG 1 ATOM 390 N N . GLY A 1 50 ? -5.555 43.442 -3.599 1.00 29.60 ? 68 GLY A N 1 ATOM 391 C CA . GLY A 1 50 ? -4.103 43.532 -3.504 1.00 29.23 ? 68 GLY A CA 1 ATOM 392 C C . GLY A 1 50 ? -3.612 43.638 -2.061 1.00 28.83 ? 68 GLY A C 1 ATOM 393 O O . GLY A 1 50 ? -2.451 43.978 -1.801 1.00 29.68 ? 68 GLY A O 1 ATOM 394 N N . LYS A 1 51 ? -4.481 43.345 -1.114 1.00 27.50 ? 69 LYS A N 1 ATOM 395 C CA . LYS A 1 51 ? -4.108 43.532 0.298 1.00 27.15 ? 69 LYS A CA 1 ATOM 396 C C . LYS A 1 51 ? -4.004 42.258 1.098 1.00 26.57 ? 69 LYS A C 1 ATOM 397 O O . LYS A 1 51 ? -4.024 42.276 2.319 1.00 25.16 ? 69 LYS A O 1 ATOM 398 C CB . LYS A 1 51 ? -5.089 44.492 0.949 1.00 27.58 ? 69 LYS A CB 1 ATOM 399 C CG . LYS A 1 51 ? -5.023 45.860 0.285 1.00 29.40 ? 69 LYS A CG 1 ATOM 400 C CD . LYS A 1 51 ? -6.100 46.798 0.759 1.00 29.17 ? 69 LYS A CD 1 ATOM 401 C CE . LYS A 1 51 ? -5.989 48.138 0.019 1.00 31.84 ? 69 LYS A CE 1 ATOM 402 N NZ . LYS A 1 51 ? -7.094 49.024 0.437 1.00 35.63 ? 69 LYS A NZ 1 ATOM 403 N N . ILE A 1 52 ? -3.854 41.153 0.376 1.00 26.22 ? 70 ILE A N 1 ATOM 404 C CA . ILE A 1 52 ? -3.792 39.807 0.977 1.00 27.33 ? 70 ILE A CA 1 ATOM 405 C C . ILE A 1 52 ? -2.611 38.996 0.458 1.00 26.99 ? 70 ILE A C 1 ATOM 406 O O . ILE A 1 52 ? -2.360 38.905 -0.746 1.00 26.42 ? 70 ILE A O 1 ATOM 407 C CB . ILE A 1 52 ? -5.052 38.935 0.683 1.00 28.23 ? 70 ILE A CB 1 ATOM 408 C CG1 . ILE A 1 52 ? -6.351 39.755 0.630 1.00 32.18 ? 70 ILE A CG1 1 ATOM 409 C CG2 . ILE A 1 52 ? -5.140 37.784 1.673 1.00 28.70 ? 70 ILE A CG2 1 ATOM 410 C CD1 . ILE A 1 52 ? -6.898 40.091 1.934 1.00 33.36 ? 70 ILE A CD1 1 ATOM 411 N N . SER A 1 53 ? -1.890 38.397 1.389 1.00 26.56 ? 71 SER A N 1 ATOM 412 C CA . SER A 1 53 ? -0.875 37.398 1.065 1.00 26.22 ? 71 SER A CA 1 ATOM 413 C C . SER A 1 53 ? -1.124 36.136 1.875 1.00 26.86 ? 71 SER A C 1 ATOM 414 O O . SER A 1 53 ? -0.878 36.096 3.067 1.00 25.31 ? 71 SER A O 1 ATOM 415 C CB . SER A 1 53 ? 0.539 37.919 1.358 1.00 26.86 ? 71 SER A CB 1 ATOM 416 O OG . SER A 1 53 ? 1.535 36.981 0.963 1.00 24.97 ? 71 SER A OG 1 ATOM 417 N N . SER A 1 54 ? -1.637 35.114 1.197 1.00 25.80 ? 72 SER A N 1 ATOM 418 C CA . SER A 1 54 ? -2.079 33.901 1.837 1.00 25.89 ? 72 SER A CA 1 ATOM 419 C C . SER A 1 54 ? -1.824 32.701 0.953 1.00 26.98 ? 72 SER A C 1 ATOM 420 O O . SER A 1 54 ? -1.887 32.783 -0.281 1.00 28.14 ? 72 SER A O 1 ATOM 421 C CB . SER A 1 54 ? -3.587 33.951 2.126 1.00 26.50 ? 72 SER A CB 1 ATOM 422 O OG . SER A 1 54 ? -3.915 35.015 3.008 1.00 25.94 ? 72 SER A OG 1 ATOM 423 N N . LYS A 1 55 ? -1.550 31.583 1.600 1.00 26.89 ? 73 LYS A N 1 ATOM 424 C CA . LYS A 1 55 ? -1.312 30.327 0.884 1.00 27.25 ? 73 LYS A CA 1 ATOM 425 C C . LYS A 1 55 ? -1.914 29.127 1.598 1.00 27.21 ? 73 LYS A C 1 ATOM 426 O O . LYS A 1 55 ? -1.589 28.829 2.742 1.00 26.71 ? 73 LYS A O 1 ATOM 427 C CB . LYS A 1 55 ? 0.190 30.138 0.663 1.00 26.98 ? 73 LYS A CB 1 ATOM 428 C CG . LYS A 1 55 ? 0.578 28.833 -0.038 1.00 28.15 ? 73 LYS A CG 1 ATOM 429 C CD . LYS A 1 55 ? 0.117 28.869 -1.473 1.00 31.38 ? 73 LYS A CD 1 ATOM 430 C CE . LYS A 1 55 ? 0.429 27.606 -2.237 1.00 33.74 ? 73 LYS A CE 1 ATOM 431 N NZ . LYS A 1 55 ? 0.035 27.804 -3.670 1.00 35.58 ? 73 LYS A NZ 1 ATOM 432 N N . ALA A 1 56 ? -2.810 28.436 0.899 1.00 27.27 ? 74 ALA A N 1 ATOM 433 C CA . ALA A 1 56 ? -3.380 27.216 1.433 1.00 27.89 ? 74 ALA A CA 1 ATOM 434 C C . ALA A 1 56 ? -2.257 26.281 1.908 1.00 28.36 ? 74 ALA A C 1 ATOM 435 O O . ALA A 1 56 ? -1.282 25.991 1.186 1.00 28.94 ? 74 ALA A O 1 ATOM 436 C CB . ALA A 1 56 ? -4.304 26.491 0.330 1.00 27.60 ? 74 ALA A CB 1 ATOM 437 N N . GLY A 1 57 ? -2.415 25.802 3.133 1.00 28.06 ? 75 GLY A N 1 ATOM 438 C CA . GLY A 1 57 ? -1.522 24.806 3.700 1.00 27.73 ? 75 GLY A CA 1 ATOM 439 C C . GLY A 1 57 ? -0.277 25.361 4.365 1.00 27.49 ? 75 GLY A C 1 ATOM 440 O O . GLY A 1 57 ? 0.526 24.610 4.930 1.00 27.46 ? 75 GLY A O 1 ATOM 441 N N . ASN A 1 58 ? -0.131 26.676 4.321 1.00 27.54 ? 76 ASN A N 1 ATOM 442 C CA . ASN A 1 58 ? 1.067 27.323 4.890 1.00 26.82 ? 76 ASN A CA 1 ATOM 443 C C . ASN A 1 58 ? 0.792 28.247 6.054 1.00 26.47 ? 76 ASN A C 1 ATOM 444 O O . ASN A 1 58 ? -0.351 28.502 6.445 1.00 26.35 ? 76 ASN A O 1 ATOM 445 C CB . ASN A 1 58 ? 1.855 28.054 3.788 1.00 27.48 ? 76 ASN A CB 1 ATOM 446 C CG . ASN A 1 58 ? 3.325 27.712 3.813 1.00 28.08 ? 76 ASN A CG 1 ATOM 447 O OD1 . ASN A 1 58 ? 3.892 27.108 2.861 1.00 30.58 ? 76 ASN A OD1 1 ATOM 448 N ND2 . ASN A 1 58 ? 3.950 28.050 4.889 1.00 25.22 ? 76 ASN A ND2 1 ATOM 449 N N . SER A 1 59 ? 1.889 28.712 6.621 1.00 26.56 ? 77 SER A N 1 ATOM 450 C CA . SER A 1 59 ? 1.867 29.728 7.692 1.00 26.38 ? 77 SER A CA 1 ATOM 451 C C . SER A 1 59 ? 3.211 30.445 7.728 1.00 26.50 ? 77 SER A C 1 ATOM 452 O O . SER A 1 59 ? 4.193 29.964 7.158 1.00 26.32 ? 77 SER A O 1 ATOM 453 C CB . SER A 1 59 ? 1.609 29.097 9.060 1.00 26.22 ? 77 SER A CB 1 ATOM 454 O OG . SER A 1 59 ? 2.786 28.490 9.541 1.00 27.11 ? 77 SER A OG 1 ATOM 455 N N . ILE A 1 60 ? 3.268 31.595 8.390 1.00 25.75 ? 78 ILE A N 1 ATOM 456 C CA . ILE A 1 60 ? 4.509 32.387 8.340 1.00 25.56 ? 78 ILE A CA 1 ATOM 457 C C . ILE A 1 60 ? 5.628 31.574 9.028 1.00 25.36 ? 78 ILE A C 1 ATOM 458 O O . ILE A 1 60 ? 6.745 31.501 8.542 1.00 26.32 ? 78 ILE A O 1 ATOM 459 C CB . ILE A 1 60 ? 4.356 33.809 8.943 1.00 25.71 ? 78 ILE A CB 1 ATOM 460 C CG1 . ILE A 1 60 ? 3.350 34.617 8.139 1.00 26.31 ? 78 ILE A CG1 1 ATOM 461 C CG2 . ILE A 1 60 ? 5.728 34.541 8.901 1.00 25.09 ? 78 ILE A CG2 1 ATOM 462 C CD1 . ILE A 1 60 ? 3.038 36.009 8.700 1.00 26.96 ? 78 ILE A CD1 1 ATOM 463 N N . PHE A 1 61 ? 5.291 30.919 10.128 1.00 25.25 ? 79 PHE A N 1 ATOM 464 C CA . PHE A 1 61 ? 6.271 30.108 10.894 1.00 25.16 ? 79 PHE A CA 1 ATOM 465 C C . PHE A 1 61 ? 6.729 28.919 10.058 1.00 25.44 ? 79 PHE A C 1 ATOM 466 O O . PHE A 1 61 ? 7.905 28.578 9.985 1.00 26.29 ? 79 PHE A O 1 ATOM 467 C CB . PHE A 1 61 ? 5.631 29.624 12.178 1.00 25.07 ? 79 PHE A CB 1 ATOM 468 C CG . PHE A 1 61 ? 6.547 28.854 13.063 1.00 25.93 ? 79 PHE A CG 1 ATOM 469 C CD1 . PHE A 1 61 ? 7.413 29.515 13.913 1.00 27.54 ? 79 PHE A CD1 1 ATOM 470 C CD2 . PHE A 1 61 ? 6.493 27.473 13.109 1.00 28.73 ? 79 PHE A CD2 1 ATOM 471 C CE1 . PHE A 1 61 ? 8.251 28.809 14.757 1.00 26.47 ? 79 PHE A CE1 1 ATOM 472 C CE2 . PHE A 1 61 ? 7.352 26.759 13.953 1.00 29.14 ? 79 PHE A CE2 1 ATOM 473 C CZ . PHE A 1 61 ? 8.205 27.440 14.786 1.00 26.73 ? 79 PHE A CZ 1 ATOM 474 N N . ARG A 1 62 ? 5.778 28.304 9.389 1.00 26.02 ? 80 ARG A N 1 ATOM 475 C CA . ARG A 1 62 ? 6.077 27.127 8.567 1.00 25.71 ? 80 ARG A CA 1 ATOM 476 C C . ARG A 1 62 ? 7.049 27.506 7.463 1.00 25.61 ? 80 ARG A C 1 ATOM 477 O O . ARG A 1 62 ? 8.035 26.818 7.236 1.00 26.27 ? 80 ARG A O 1 ATOM 478 C CB . ARG A 1 62 ? 4.797 26.522 7.974 1.00 26.08 ? 80 ARG A CB 1 ATOM 479 C CG . ARG A 1 62 ? 5.005 25.222 7.216 1.00 26.99 ? 80 ARG A CG 1 ATOM 480 C CD . ARG A 1 62 ? 3.607 24.576 7.008 1.00 30.76 ? 80 ARG A CD 1 ATOM 481 N NE . ARG A 1 62 ? 3.664 23.427 6.145 1.00 35.12 ? 80 ARG A NE 1 ATOM 482 C CZ . ARG A 1 62 ? 3.179 22.240 6.462 1.00 35.12 ? 80 ARG A CZ 1 ATOM 483 N NH1 . ARG A 1 62 ? 2.568 22.065 7.633 1.00 35.23 ? 80 ARG A NH1 1 ATOM 484 N NH2 . ARG A 1 62 ? 3.288 21.252 5.588 1.00 35.81 ? 80 ARG A NH2 1 ATOM 485 N N . SER A 1 63 ? 6.786 28.621 6.805 1.00 25.73 ? 81 SER A N 1 ATOM 486 C CA . SER A 1 63 ? 7.654 29.095 5.702 1.00 25.78 ? 81 SER A CA 1 ATOM 487 C C . SER A 1 63 ? 9.019 29.551 6.212 1.00 26.13 ? 81 SER A C 1 ATOM 488 O O . SER A 1 63 ? 10.033 29.471 5.517 1.00 26.69 ? 81 SER A O 1 ATOM 489 C CB . SER A 1 63 ? 6.979 30.217 4.900 1.00 26.03 ? 81 SER A CB 1 ATOM 490 O OG . SER A 1 63 ? 5.905 29.719 4.104 1.00 27.41 ? 81 SER A OG 1 ATOM 491 N N . PHE A 1 64 ? 9.025 30.033 7.443 1.00 26.05 ? 82 PHE A N 1 ATOM 492 C CA . PHE A 1 64 ? 10.268 30.516 8.062 1.00 26.12 ? 82 PHE A CA 1 ATOM 493 C C . PHE A 1 64 ? 11.267 29.397 8.240 1.00 26.39 ? 82 PHE A C 1 ATOM 494 O O . PHE A 1 64 ? 12.466 29.590 8.042 1.00 25.99 ? 82 PHE A O 1 ATOM 495 C CB . PHE A 1 64 ? 9.981 31.162 9.412 1.00 25.63 ? 82 PHE A CB 1 ATOM 496 C CG . PHE A 1 64 ? 11.176 31.855 10.042 1.00 25.13 ? 82 PHE A CG 1 ATOM 497 C CD1 . PHE A 1 64 ? 11.647 33.082 9.545 1.00 25.22 ? 82 PHE A CD1 1 ATOM 498 C CD2 . PHE A 1 64 ? 11.795 31.302 11.146 1.00 25.88 ? 82 PHE A CD2 1 ATOM 499 C CE1 . PHE A 1 64 ? 12.699 33.754 10.164 1.00 25.44 ? 82 PHE A CE1 1 ATOM 500 C CE2 . PHE A 1 64 ? 12.864 31.974 11.765 1.00 27.22 ? 82 PHE A CE2 1 ATOM 501 C CZ . PHE A 1 64 ? 13.321 33.186 11.260 1.00 25.73 ? 82 PHE A CZ 1 ATOM 502 N N . HIS A 1 65 ? 10.766 28.224 8.609 1.00 26.05 ? 83 HIS A N 1 ATOM 503 C CA . HIS A 1 65 ? 11.650 27.164 9.115 1.00 25.25 ? 83 HIS A CA 1 ATOM 504 C C . HIS A 1 65 ? 11.862 26.028 8.128 1.00 26.00 ? 83 HIS A C 1 ATOM 505 O O . HIS A 1 65 ? 12.861 25.336 8.201 1.00 25.86 ? 83 HIS A O 1 ATOM 506 C CB . HIS A 1 65 ? 11.134 26.558 10.426 1.00 26.16 ? 83 HIS A CB 1 ATOM 507 C CG . HIS A 1 65 ? 11.575 27.287 11.673 1.00 25.62 ? 83 HIS A CG 1 ATOM 508 N ND1 . HIS A 1 65 ? 12.901 27.388 12.057 1.00 25.29 ? 83 HIS A ND1 1 ATOM 509 C CD2 . HIS A 1 65 ? 10.857 27.892 12.648 1.00 27.12 ? 83 HIS A CD2 1 ATOM 510 C CE1 . HIS A 1 65 ? 12.975 28.058 13.197 1.00 27.45 ? 83 HIS A CE1 1 ATOM 511 N NE2 . HIS A 1 65 ? 11.748 28.371 13.581 1.00 25.29 ? 83 HIS A NE2 1 ATOM 512 N N . PHE A 1 66 ? 10.895 25.821 7.246 1.00 25.74 ? 84 PHE A N 1 ATOM 513 C CA . PHE A 1 66 ? 10.799 24.558 6.477 1.00 26.72 ? 84 PHE A CA 1 ATOM 514 C C . PHE A 1 66 ? 10.892 24.723 4.974 1.00 26.89 ? 84 PHE A C 1 ATOM 515 O O . PHE A 1 66 ? 10.739 25.811 4.447 1.00 27.24 ? 84 PHE A O 1 ATOM 516 C CB . PHE A 1 66 ? 9.486 23.849 6.857 1.00 27.64 ? 84 PHE A CB 1 ATOM 517 C CG . PHE A 1 66 ? 9.420 23.483 8.315 1.00 27.16 ? 84 PHE A CG 1 ATOM 518 C CD1 . PHE A 1 66 ? 10.085 22.367 8.784 1.00 29.41 ? 84 PHE A CD1 1 ATOM 519 C CD2 . PHE A 1 66 ? 8.754 24.307 9.229 1.00 28.04 ? 84 PHE A CD2 1 ATOM 520 C CE1 . PHE A 1 66 ? 10.049 22.047 10.138 1.00 30.99 ? 84 PHE A CE1 1 ATOM 521 C CE2 . PHE A 1 66 ? 8.708 23.990 10.561 1.00 27.87 ? 84 PHE A CE2 1 ATOM 522 C CZ . PHE A 1 66 ? 9.387 22.871 11.023 1.00 29.48 ? 84 PHE A CZ 1 ATOM 523 N N . THR A 1 67 ? 11.134 23.617 4.284 1.00 27.66 ? 85 THR A N 1 ATOM 524 C CA . THR A 1 67 ? 11.286 23.638 2.824 1.00 27.71 ? 85 THR A CA 1 ATOM 525 C C . THR A 1 67 ? 9.958 23.931 2.122 1.00 28.55 ? 85 THR A C 1 ATOM 526 O O . THR A 1 67 ? 9.925 24.338 0.962 1.00 28.75 ? 85 THR A O 1 ATOM 527 C CB . THR A 1 67 ? 11.869 22.310 2.287 1.00 27.65 ? 85 THR A CB 1 ATOM 528 O OG1 . THR A 1 67 ? 11.009 21.223 2.655 1.00 28.03 ? 85 THR A OG1 1 ATOM 529 C CG2 . THR A 1 67 ? 13.291 22.087 2.820 1.00 26.78 ? 85 THR A CG2 1 ATOM 530 N N . ASP A 1 68 ? 8.867 23.718 2.847 1.00 28.63 ? 86 ASP A N 1 ATOM 531 C CA . ASP A 1 68 ? 7.499 24.045 2.364 1.00 29.24 ? 86 ASP A CA 1 ATOM 532 C C . ASP A 1 68 ? 7.242 25.538 2.487 1.00 28.95 ? 86 ASP A C 1 ATOM 533 O O . ASP A 1 68 ? 6.615 26.014 3.419 1.00 29.46 ? 86 ASP A O 1 ATOM 534 C CB . ASP A 1 68 ? 6.439 23.266 3.148 1.00 29.24 ? 86 ASP A CB 1 ATOM 535 C CG . ASP A 1 68 ? 5.032 23.431 2.572 1.00 31.01 ? 86 ASP A CG 1 ATOM 536 O OD1 . ASP A 1 68 ? 4.911 23.914 1.424 1.00 31.53 ? 86 ASP A OD1 1 ATOM 537 O OD2 . ASP A 1 68 ? 4.052 23.061 3.272 1.00 33.07 ? 86 ASP A OD2 1 ATOM 538 N N . PHE A 1 69 ? 7.725 26.262 1.501 1.00 28.83 ? 87 PHE A N 1 ATOM 539 C CA . PHE A 1 69 ? 7.917 27.695 1.594 1.00 28.87 ? 87 PHE A CA 1 ATOM 540 C C . PHE A 1 69 ? 6.959 28.473 0.714 1.00 29.47 ? 87 PHE A C 1 ATOM 541 O O . PHE A 1 69 ? 6.805 28.163 -0.472 1.00 29.16 ? 87 PHE A O 1 ATOM 542 C CB . PHE A 1 69 ? 9.367 28.028 1.196 1.00 29.12 ? 87 PHE A CB 1 ATOM 543 C CG . PHE A 1 69 ? 9.631 29.467 1.097 1.00 27.00 ? 87 PHE A CG 1 ATOM 544 C CD1 . PHE A 1 69 ? 9.768 30.244 2.252 1.00 28.00 ? 87 PHE A CD1 1 ATOM 545 C CD2 . PHE A 1 69 ? 9.701 30.087 -0.137 1.00 28.85 ? 87 PHE A CD2 1 ATOM 546 C CE1 . PHE A 1 69 ? 9.989 31.593 2.154 1.00 26.55 ? 87 PHE A CE1 1 ATOM 547 C CE2 . PHE A 1 69 ? 9.920 31.447 -0.234 1.00 29.25 ? 87 PHE A CE2 1 ATOM 548 C CZ . PHE A 1 69 ? 10.054 32.204 0.920 1.00 25.85 ? 87 PHE A CZ 1 ATOM 549 N N . TYR A 1 70 ? 6.322 29.481 1.316 1.00 28.28 ? 88 TYR A N 1 ATOM 550 C CA . TYR A 1 70 ? 5.587 30.512 0.593 1.00 27.51 ? 88 TYR A CA 1 ATOM 551 C C . TYR A 1 70 ? 6.148 31.869 0.925 1.00 27.75 ? 88 TYR A C 1 ATOM 552 O O . TYR A 1 70 ? 6.339 32.203 2.091 1.00 26.56 ? 88 TYR A O 1 ATOM 553 C CB . TYR A 1 70 ? 4.112 30.500 0.968 1.00 27.97 ? 88 TYR A CB 1 ATOM 554 C CG . TYR A 1 70 ? 3.285 31.499 0.186 1.00 27.21 ? 88 TYR A CG 1 ATOM 555 C CD1 . TYR A 1 70 ? 3.015 31.281 -1.169 1.00 28.89 ? 88 TYR A CD1 1 ATOM 556 C CD2 . TYR A 1 70 ? 2.761 32.642 0.792 1.00 28.14 ? 88 TYR A CD2 1 ATOM 557 C CE1 . TYR A 1 70 ? 2.282 32.172 -1.903 1.00 29.97 ? 88 TYR A CE1 1 ATOM 558 C CE2 . TYR A 1 70 ? 1.996 33.556 0.046 1.00 28.11 ? 88 TYR A CE2 1 ATOM 559 C CZ . TYR A 1 70 ? 1.769 33.306 -1.289 1.00 29.83 ? 88 TYR A CZ 1 ATOM 560 O OH . TYR A 1 70 ? 1.019 34.169 -2.064 1.00 31.64 ? 88 TYR A OH 1 ATOM 561 N N . ASN A 1 71 ? 6.388 32.666 -0.101 1.00 26.72 ? 89 ASN A N 1 ATOM 562 C CA . ASN A 1 71 ? 6.996 33.969 0.135 1.00 27.26 ? 89 ASN A CA 1 ATOM 563 C C . ASN A 1 71 ? 5.982 35.017 0.545 1.00 26.50 ? 89 ASN A C 1 ATOM 564 O O . ASN A 1 71 ? 5.627 35.926 -0.217 1.00 27.01 ? 89 ASN A O 1 ATOM 565 C CB . ASN A 1 71 ? 7.813 34.422 -1.069 1.00 28.15 ? 89 ASN A CB 1 ATOM 566 C CG . ASN A 1 71 ? 8.588 35.677 -0.794 1.00 28.62 ? 89 ASN A CG 1 ATOM 567 O OD1 . ASN A 1 71 ? 8.764 36.089 0.361 1.00 27.58 ? 89 ASN A OD1 1 ATOM 568 N ND2 . ASN A 1 71 ? 9.049 36.308 -1.861 1.00 33.03 ? 89 ASN A ND2 1 ATOM 569 N N . TYR A 1 72 ? 5.530 34.899 1.786 1.00 26.40 ? 90 TYR A N 1 ATOM 570 C CA . TYR A 1 72 ? 4.597 35.899 2.324 1.00 26.37 ? 90 TYR A CA 1 ATOM 571 C C . TYR A 1 72 ? 5.186 37.299 2.165 1.00 27.02 ? 90 TYR A C 1 ATOM 572 O O . TYR A 1 72 ? 6.336 37.578 2.554 1.00 27.56 ? 90 TYR A O 1 ATOM 573 C CB . TYR A 1 72 ? 4.320 35.642 3.773 1.00 26.28 ? 90 TYR A CB 1 ATOM 574 C CG . TYR A 1 72 ? 3.418 34.478 4.051 1.00 25.74 ? 90 TYR A CG 1 ATOM 575 C CD1 . TYR A 1 72 ? 2.047 34.635 4.003 1.00 26.69 ? 90 TYR A CD1 1 ATOM 576 C CD2 . TYR A 1 72 ? 3.923 33.220 4.360 1.00 25.07 ? 90 TYR A CD2 1 ATOM 577 C CE1 . TYR A 1 72 ? 1.201 33.605 4.308 1.00 26.51 ? 90 TYR A CE1 1 ATOM 578 C CE2 . TYR A 1 72 ? 3.083 32.161 4.642 1.00 27.67 ? 90 TYR A CE2 1 ATOM 579 C CZ . TYR A 1 72 ? 1.707 32.369 4.612 1.00 27.22 ? 90 TYR A CZ 1 ATOM 580 O OH . TYR A 1 72 ? 0.831 31.350 4.902 1.00 27.07 ? 90 TYR A OH 1 ATOM 581 N N . THR A 1 73 ? 4.386 38.171 1.587 1.00 26.96 ? 91 THR A N 1 ATOM 582 C CA . THR A 1 73 ? 4.828 39.525 1.273 1.00 27.20 ? 91 THR A CA 1 ATOM 583 C C . THR A 1 73 ? 3.698 40.514 1.318 1.00 27.00 ? 91 THR A C 1 ATOM 584 O O . THR A 1 73 ? 2.676 40.325 0.678 1.00 25.50 ? 91 THR A O 1 ATOM 585 C CB . THR A 1 73 ? 5.455 39.580 -0.153 1.00 28.05 ? 91 THR A CB 1 ATOM 586 O OG1 . THR A 1 73 ? 6.530 38.643 -0.242 1.00 27.98 ? 91 THR A OG1 1 ATOM 587 C CG2 . THR A 1 73 ? 5.971 40.969 -0.476 1.00 28.33 ? 91 THR A CG2 1 ATOM 588 N N . GLY A 1 74 ? 3.877 41.572 2.096 1.00 26.34 ? 92 GLY A N 1 ATOM 589 C CA . GLY A 1 74 ? 2.840 42.588 2.197 1.00 26.87 ? 92 GLY A CA 1 ATOM 590 C C . GLY A 1 74 ? 3.283 43.830 2.935 1.00 27.43 ? 92 GLY A C 1 ATOM 591 O O . GLY A 1 74 ? 4.259 43.809 3.680 1.00 27.39 ? 92 GLY A O 1 ATOM 592 N N . GLU A 1 75 ? 2.577 44.911 2.658 1.00 27.26 ? 93 GLU A N 1 ATOM 593 C CA . GLU A 1 75 ? 2.817 46.202 3.294 1.00 28.18 ? 93 GLU A CA 1 ATOM 594 C C . GLU A 1 75 ? 1.503 46.922 3.639 1.00 27.70 ? 93 GLU A C 1 ATOM 595 O O . GLU A 1 75 ? 0.566 46.989 2.844 1.00 27.21 ? 93 GLU A O 1 ATOM 596 C CB . GLU A 1 75 ? 3.690 47.073 2.367 1.00 28.76 ? 93 GLU A CB 1 ATOM 597 C CG . GLU A 1 75 ? 3.968 48.462 2.906 1.00 32.30 ? 93 GLU A CG 1 ATOM 598 C CD . GLU A 1 75 ? 4.637 49.400 1.901 1.00 36.00 ? 93 GLU A CD 1 ATOM 599 O OE1 . GLU A 1 75 ? 5.172 48.899 0.889 1.00 35.79 ? 93 GLU A OE1 1 ATOM 600 O OE2 . GLU A 1 75 ? 4.638 50.640 2.145 1.00 34.66 ? 93 GLU A OE2 1 ATOM 601 N N . GLY A 1 76 ? 1.445 47.468 4.841 1.00 27.20 ? 94 GLY A N 1 ATOM 602 C CA . GLY A 1 76 ? 0.304 48.281 5.259 1.00 26.79 ? 94 GLY A CA 1 ATOM 603 C C . GLY A 1 76 ? 0.523 48.944 6.597 1.00 26.66 ? 94 GLY A C 1 ATOM 604 O O . GLY A 1 76 ? 1.418 48.547 7.351 1.00 27.33 ? 94 GLY A O 1 ATOM 605 N N . GLN A 1 77 ? -0.310 49.926 6.882 1.00 26.38 ? 95 GLN A N 1 ATOM 606 C CA . GLN A 1 77 ? -0.232 50.644 8.162 1.00 26.67 ? 95 GLN A CA 1 ATOM 607 C C . GLN A 1 77 ? -0.764 49.736 9.254 1.00 26.52 ? 95 GLN A C 1 ATOM 608 O O . GLN A 1 77 ? -0.114 49.527 10.260 1.00 27.03 ? 95 GLN A O 1 ATOM 609 C CB . GLN A 1 77 ? -0.985 51.969 8.158 1.00 27.21 ? 95 GLN A CB 1 ATOM 610 C CG . GLN A 1 77 ? -0.674 52.804 9.401 1.00 27.83 ? 95 GLN A CG 1 ATOM 611 C CD . GLN A 1 77 ? 0.657 53.487 9.347 1.00 29.12 ? 95 GLN A CD 1 ATOM 612 O OE1 . GLN A 1 77 ? 1.421 53.309 8.414 1.00 31.68 ? 95 GLN A OE1 1 ATOM 613 N NE2 . GLN A 1 77 ? 0.952 54.292 10.367 1.00 30.18 ? 95 GLN A NE2 1 ATOM 614 N N . GLN A 1 78 ? -1.955 49.218 9.036 1.00 26.15 ? 96 GLN A N 1 ATOM 615 C CA . GLN A 1 78 ? -2.537 48.192 9.920 1.00 25.74 ? 96 GLN A CA 1 ATOM 616 C C . GLN A 1 78 ? -2.357 46.818 9.323 1.00 26.67 ? 96 GLN A C 1 ATOM 617 O O . GLN A 1 78 ? -2.861 46.520 8.234 1.00 26.47 ? 96 GLN A O 1 ATOM 618 C CB . GLN A 1 78 ? -4.029 48.429 10.170 1.00 26.01 ? 96 GLN A CB 1 ATOM 619 C CG . GLN A 1 78 ? -4.330 49.456 11.253 1.00 26.07 ? 96 GLN A CG 1 ATOM 620 C CD . GLN A 1 78 ? -5.802 49.677 11.408 1.00 27.76 ? 96 GLN A CD 1 ATOM 621 O OE1 . GLN A 1 78 ? -6.479 50.125 10.467 1.00 28.64 ? 96 GLN A OE1 1 ATOM 622 N NE2 . GLN A 1 78 ? -6.316 49.368 12.584 1.00 26.93 ? 96 GLN A NE2 1 ATOM 623 N N . ILE A 1 79 ? -1.698 45.964 10.092 1.00 26.40 ? 97 ILE A N 1 ATOM 624 C CA . ILE A 1 79 ? -1.445 44.586 9.699 1.00 26.11 ? 97 ILE A CA 1 ATOM 625 C C . ILE A 1 79 ? -2.369 43.642 10.462 1.00 25.59 ? 97 ILE A C 1 ATOM 626 O O . ILE A 1 79 ? -2.593 43.793 11.660 1.00 24.84 ? 97 ILE A O 1 ATOM 627 C CB . ILE A 1 79 ? 0.055 44.185 9.935 1.00 27.34 ? 97 ILE A CB 1 ATOM 628 C CG1 . ILE A 1 79 ? 0.986 45.151 9.213 1.00 26.33 ? 97 ILE A CG1 1 ATOM 629 C CG2 . ILE A 1 79 ? 0.327 42.714 9.476 1.00 27.65 ? 97 ILE A CG2 1 ATOM 630 C CD1 . ILE A 1 79 ? 0.878 45.109 7.676 1.00 27.29 ? 97 ILE A CD1 1 ATOM 631 N N . ILE A 1 80 ? -2.908 42.687 9.720 1.00 24.51 ? 98 ILE A N 1 ATOM 632 C CA . ILE A 1 80 ? -3.814 41.660 10.238 1.00 25.01 ? 98 ILE A CA 1 ATOM 633 C C . ILE A 1 80 ? -3.270 40.296 9.869 1.00 25.40 ? 98 ILE A C 1 ATOM 634 O O . ILE A 1 80 ? -2.723 40.117 8.764 1.00 25.15 ? 98 ILE A O 1 ATOM 635 C CB . ILE A 1 80 ? -5.250 41.815 9.642 1.00 25.74 ? 98 ILE A CB 1 ATOM 636 C CG1 . ILE A 1 80 ? -5.786 43.230 9.861 1.00 29.18 ? 98 ILE A CG1 1 ATOM 637 C CG2 . ILE A 1 80 ? -6.217 40.774 10.257 1.00 25.10 ? 98 ILE A CG2 1 ATOM 638 C CD1 . ILE A 1 80 ? -5.814 44.128 8.650 1.00 32.76 ? 98 ILE A CD1 1 ATOM 639 N N . PHE A 1 81 ? -3.385 39.365 10.810 1.00 25.43 ? 99 PHE A N 1 ATOM 640 C CA . PHE A 1 81 ? -2.961 37.975 10.638 1.00 26.13 ? 99 PHE A CA 1 ATOM 641 C C . PHE A 1 81 ? -4.092 36.986 10.908 1.00 26.02 ? 99 PHE A C 1 ATOM 642 O O . PHE A 1 81 ? -4.776 37.071 11.921 1.00 26.75 ? 99 PHE A O 1 ATOM 643 C CB . PHE A 1 81 ? -1.843 37.618 11.610 1.00 26.71 ? 99 PHE A CB 1 ATOM 644 C CG . PHE A 1 81 ? -0.583 38.435 11.466 1.00 25.74 ? 99 PHE A CG 1 ATOM 645 C CD1 . PHE A 1 81 ? 0.469 37.956 10.730 1.00 27.37 ? 99 PHE A CD1 1 ATOM 646 C CD2 . PHE A 1 81 ? -0.445 39.664 12.100 1.00 29.45 ? 99 PHE A CD2 1 ATOM 647 C CE1 . PHE A 1 81 ? 1.673 38.714 10.615 1.00 28.44 ? 99 PHE A CE1 1 ATOM 648 C CE2 . PHE A 1 81 ? 0.734 40.401 12.005 1.00 27.80 ? 99 PHE A CE2 1 ATOM 649 C CZ . PHE A 1 81 ? 1.783 39.927 11.277 1.00 26.40 ? 99 PHE A CZ 1 ATOM 650 N N . TYR A 1 82 ? -4.254 36.038 9.997 1.00 26.40 ? 100 TYR A N 1 ATOM 651 C CA . TYR A 1 82 ? -5.162 34.899 10.183 1.00 26.24 ? 100 TYR A CA 1 ATOM 652 C C . TYR A 1 82 ? -4.476 33.649 9.641 1.00 26.46 ? 100 TYR A C 1 ATOM 653 O O . TYR A 1 82 ? -4.810 33.091 8.590 1.00 26.62 ? 100 TYR A O 1 ATOM 654 C CB . TYR A 1 82 ? -6.490 35.147 9.480 1.00 27.17 ? 100 TYR A CB 1 ATOM 655 C CG . TYR A 1 82 ? -7.527 34.071 9.678 1.00 27.58 ? 100 TYR A CG 1 ATOM 656 C CD1 . TYR A 1 82 ? -7.645 33.409 10.894 1.00 27.77 ? 100 TYR A CD1 1 ATOM 657 C CD2 . TYR A 1 82 ? -8.428 33.744 8.662 1.00 27.47 ? 100 TYR A CD2 1 ATOM 658 C CE1 . TYR A 1 82 ? -8.609 32.424 11.094 1.00 28.00 ? 100 TYR A CE1 1 ATOM 659 C CE2 . TYR A 1 82 ? -9.375 32.786 8.858 1.00 28.60 ? 100 TYR A CE2 1 ATOM 660 C CZ . TYR A 1 82 ? -9.480 32.128 10.072 1.00 28.53 ? 100 TYR A CZ 1 ATOM 661 O OH . TYR A 1 82 ? -10.464 31.167 10.250 1.00 28.77 ? 100 TYR A OH 1 ATOM 662 N N . GLU A 1 83 ? -3.469 33.236 10.389 1.00 27.06 ? 101 GLU A N 1 ATOM 663 C CA . GLU A 1 83 ? -2.668 32.065 10.049 1.00 27.00 ? 101 GLU A CA 1 ATOM 664 C C . GLU A 1 83 ? -1.985 31.522 11.294 1.00 27.18 ? 101 GLU A C 1 ATOM 665 O O . GLU A 1 83 ? -1.944 32.195 12.327 1.00 26.94 ? 101 GLU A O 1 ATOM 666 C CB . GLU A 1 83 ? -1.688 32.348 8.910 1.00 26.98 ? 101 GLU A CB 1 ATOM 667 C CG . GLU A 1 83 ? -0.816 33.607 9.048 1.00 27.25 ? 101 GLU A CG 1 ATOM 668 C CD . GLU A 1 83 ? 0.344 33.444 10.018 1.00 30.63 ? 101 GLU A CD 1 ATOM 669 O OE1 . GLU A 1 83 ? 0.574 34.418 10.785 1.00 31.82 ? 101 GLU A OE1 1 ATOM 670 O OE2 . GLU A 1 83 ? 1.028 32.374 10.007 1.00 30.17 ? 101 GLU A OE2 1 ATOM 671 N N . GLY A 1 84 ? -1.535 30.286 11.188 1.00 27.19 ? 102 GLY A N 1 ATOM 672 C CA . GLY A 1 84 ? -0.806 29.623 12.258 1.00 27.45 ? 102 GLY A CA 1 ATOM 673 C C . GLY A 1 84 ? -1.117 28.155 12.395 1.00 28.33 ? 102 GLY A C 1 ATOM 674 O O . GLY A 1 84 ? -0.292 27.363 12.855 1.00 27.90 ? 102 GLY A O 1 ATOM 675 N N . VAL A 1 85 ? -2.327 27.815 11.978 1.00 28.25 ? 103 VAL A N 1 ATOM 676 C CA . VAL A 1 85 ? -2.861 26.468 12.135 1.00 28.34 ? 103 VAL A CA 1 ATOM 677 C C . VAL A 1 85 ? -2.034 25.431 11.389 1.00 28.41 ? 103 VAL A C 1 ATOM 678 O O . VAL A 1 85 ? -1.987 24.271 11.769 1.00 29.27 ? 103 VAL A O 1 ATOM 679 C CB . VAL A 1 85 ? -4.351 26.396 11.726 1.00 28.27 ? 103 VAL A CB 1 ATOM 680 C CG1 . VAL A 1 85 ? -4.537 26.518 10.223 1.00 28.14 ? 103 VAL A CG1 1 ATOM 681 C CG2 . VAL A 1 85 ? -4.960 25.119 12.248 1.00 29.52 ? 103 VAL A CG2 1 ATOM 682 N N . ASN A 1 86 ? -1.349 25.863 10.342 1.00 28.08 ? 104 ASN A N 1 ATOM 683 C CA . ASN A 1 86 ? -0.557 24.953 9.535 1.00 28.74 ? 104 ASN A CA 1 ATOM 684 C C . ASN A 1 86 ? 0.781 24.600 10.180 1.00 30.25 ? 104 ASN A C 1 ATOM 685 O O . ASN A 1 86 ? 1.655 23.984 9.569 1.00 31.40 ? 104 ASN A O 1 ATOM 686 C CB . ASN A 1 86 ? -0.465 25.444 8.092 1.00 28.88 ? 104 ASN A CB 1 ATOM 687 C CG . ASN A 1 86 ? -1.807 25.303 7.390 1.00 29.15 ? 104 ASN A CG 1 ATOM 688 O OD1 . ASN A 1 86 ? -2.447 24.249 7.525 1.00 29.33 ? 104 ASN A OD1 1 ATOM 689 N ND2 . ASN A 1 86 ? -2.278 26.357 6.695 1.00 28.17 ? 104 ASN A ND2 1 ATOM 690 N N . PHE A 1 87 ? 0.904 24.968 11.453 1.00 30.13 ? 105 PHE A N 1 ATOM 691 C CA . PHE A 1 87 ? 1.899 24.326 12.345 1.00 29.93 ? 105 PHE A CA 1 ATOM 692 C C . PHE A 1 87 ? 1.377 24.240 13.788 1.00 29.81 ? 105 PHE A C 1 ATOM 693 O O . PHE A 1 87 ? 1.465 25.189 14.559 1.00 30.33 ? 105 PHE A O 1 ATOM 694 C CB . PHE A 1 87 ? 3.257 25.035 12.277 1.00 29.85 ? 105 PHE A CB 1 ATOM 695 C CG . PHE A 1 87 ? 4.382 24.276 12.961 1.00 28.29 ? 105 PHE A CG 1 ATOM 696 C CD1 . PHE A 1 87 ? 5.161 23.368 12.260 1.00 30.00 ? 105 PHE A CD1 1 ATOM 697 C CD2 . PHE A 1 87 ? 4.631 24.453 14.298 1.00 28.81 ? 105 PHE A CD2 1 ATOM 698 C CE1 . PHE A 1 87 ? 6.193 22.668 12.886 1.00 28.94 ? 105 PHE A CE1 1 ATOM 699 C CE2 . PHE A 1 87 ? 5.664 23.760 14.943 1.00 29.14 ? 105 PHE A CE2 1 ATOM 700 C CZ . PHE A 1 87 ? 6.439 22.862 14.239 1.00 28.17 ? 105 PHE A CZ 1 ATOM 701 N N . THR A 1 88 ? 0.817 23.077 14.122 1.00 29.71 ? 106 THR A N 1 ATOM 702 C CA . THR A 1 88 ? 0.111 22.848 15.377 1.00 29.74 ? 106 THR A CA 1 ATOM 703 C C . THR A 1 88 ? 0.459 21.472 15.970 1.00 29.97 ? 106 THR A C 1 ATOM 704 O O . THR A 1 88 ? 1.136 20.673 15.326 1.00 30.17 ? 106 THR A O 1 ATOM 705 C CB . THR A 1 88 ? -1.434 22.922 15.176 1.00 30.06 ? 106 THR A CB 1 ATOM 706 O OG1 . THR A 1 88 ? -1.798 22.274 13.951 1.00 31.42 ? 106 THR A OG1 1 ATOM 707 C CG2 . THR A 1 88 ? -1.927 24.363 15.109 1.00 28.44 ? 106 THR A CG2 1 ATOM 708 N N . PRO A 1 89 ? -0.010 21.193 17.194 1.00 29.46 ? 107 PRO A N 1 ATOM 709 C CA . PRO A 1 89 ? 0.351 19.915 17.771 1.00 29.80 ? 107 PRO A CA 1 ATOM 710 C C . PRO A 1 89 ? -0.160 18.765 16.908 1.00 29.45 ? 107 PRO A C 1 ATOM 711 O O . PRO A 1 89 ? 0.399 17.687 16.919 1.00 29.78 ? 107 PRO A O 1 ATOM 712 C CB . PRO A 1 89 ? -0.321 19.943 19.151 1.00 29.74 ? 107 PRO A CB 1 ATOM 713 C CG . PRO A 1 89 ? -0.427 21.385 19.498 1.00 29.79 ? 107 PRO A CG 1 ATOM 714 C CD . PRO A 1 89 ? -0.624 22.104 18.180 1.00 29.89 ? 107 PRO A CD 1 ATOM 715 N N . TYR A 1 90 ? -1.189 19.050 16.129 1.00 29.22 ? 108 TYR A N 1 ATOM 716 C CA . TYR A 1 90 ? -1.722 18.107 15.139 1.00 29.68 ? 108 TYR A CA 1 ATOM 717 C C . TYR A 1 90 ? -0.613 17.541 14.252 1.00 29.80 ? 108 TYR A C 1 ATOM 718 O O . TYR A 1 90 ? -0.579 16.346 13.956 1.00 30.49 ? 108 TYR A O 1 ATOM 719 C CB . TYR A 1 90 ? -2.803 18.793 14.292 1.00 29.96 ? 108 TYR A CB 1 ATOM 720 C CG . TYR A 1 90 ? -3.203 18.063 13.040 1.00 31.48 ? 108 TYR A CG 1 ATOM 721 C CD1 . TYR A 1 90 ? -3.946 16.884 13.094 1.00 33.44 ? 108 TYR A CD1 1 ATOM 722 C CD2 . TYR A 1 90 ? -2.861 18.565 11.795 1.00 31.89 ? 108 TYR A CD2 1 ATOM 723 C CE1 . TYR A 1 90 ? -4.310 16.224 11.935 1.00 33.98 ? 108 TYR A CE1 1 ATOM 724 C CE2 . TYR A 1 90 ? -3.225 17.909 10.636 1.00 35.71 ? 108 TYR A CE2 1 ATOM 725 C CZ . TYR A 1 90 ? -3.947 16.750 10.710 1.00 34.79 ? 108 TYR A CZ 1 ATOM 726 O OH . TYR A 1 90 ? -4.301 16.118 9.538 1.00 38.78 ? 108 TYR A OH 1 ATOM 727 N N . HIS A 1 91 ? 0.318 18.381 13.848 1.00 29.24 ? 109 HIS A N 1 ATOM 728 C CA . HIS A 1 91 ? 1.341 17.943 12.905 1.00 29.34 ? 109 HIS A CA 1 ATOM 729 C C . HIS A 1 91 ? 2.356 17.049 13.579 1.00 29.84 ? 109 HIS A C 1 ATOM 730 O O . HIS A 1 91 ? 3.138 16.355 12.926 1.00 29.72 ? 109 HIS A O 1 ATOM 731 C CB . HIS A 1 91 ? 2.030 19.132 12.238 1.00 29.29 ? 109 HIS A CB 1 ATOM 732 C CG . HIS A 1 91 ? 1.102 19.972 11.422 1.00 28.62 ? 109 HIS A CG 1 ATOM 733 N ND1 . HIS A 1 91 ? 0.460 21.082 11.933 1.00 30.07 ? 109 HIS A ND1 1 ATOM 734 C CD2 . HIS A 1 91 ? 0.688 19.851 10.138 1.00 30.31 ? 109 HIS A CD2 1 ATOM 735 C CE1 . HIS A 1 91 ? -0.300 21.612 10.989 1.00 29.65 ? 109 HIS A CE1 1 ATOM 736 N NE2 . HIS A 1 91 ? -0.189 20.876 9.898 1.00 29.91 ? 109 HIS A NE2 1 ATOM 737 N N . ALA A 1 92 ? 2.322 17.090 14.900 1.00 30.23 ? 110 ALA A N 1 ATOM 738 C CA . ALA A 1 92 ? 3.196 16.275 15.733 1.00 30.73 ? 110 ALA A CA 1 ATOM 739 C C . ALA A 1 92 ? 4.660 16.425 15.339 1.00 30.81 ? 110 ALA A C 1 ATOM 740 O O . ALA A 1 92 ? 5.427 15.457 15.377 1.00 30.87 ? 110 ALA A O 1 ATOM 741 C CB . ALA A 1 92 ? 2.770 14.796 15.656 1.00 30.87 ? 110 ALA A CB 1 ATOM 742 N N . PHE A 1 93 ? 5.063 17.631 14.949 1.00 30.11 ? 111 PHE A N 1 ATOM 743 C CA . PHE A 1 93 ? 6.451 17.819 14.534 1.00 30.30 ? 111 PHE A CA 1 ATOM 744 C C . PHE A 1 93 ? 7.437 17.678 15.683 1.00 30.57 ? 111 PHE A C 1 ATOM 745 O O . PHE A 1 93 ? 7.234 18.208 16.783 1.00 30.14 ? 111 PHE A O 1 ATOM 746 C CB . PHE A 1 93 ? 6.711 19.179 13.848 1.00 30.38 ? 111 PHE A CB 1 ATOM 747 C CG . PHE A 1 93 ? 8.074 19.268 13.250 1.00 29.71 ? 111 PHE A CG 1 ATOM 748 C CD1 . PHE A 1 93 ? 8.333 18.692 12.016 1.00 29.60 ? 111 PHE A CD1 1 ATOM 749 C CD2 . PHE A 1 93 ? 9.124 19.838 13.955 1.00 29.07 ? 111 PHE A CD2 1 ATOM 750 C CE1 . PHE A 1 93 ? 9.608 18.729 11.473 1.00 29.03 ? 111 PHE A CE1 1 ATOM 751 C CE2 . PHE A 1 93 ? 10.402 19.874 13.422 1.00 29.49 ? 111 PHE A CE2 1 ATOM 752 C CZ . PHE A 1 93 ? 10.643 19.317 12.179 1.00 31.10 ? 111 PHE A CZ 1 ATOM 753 N N . LYS A 1 94 ? 8.515 16.971 15.372 1.00 30.75 ? 112 LYS A N 1 ATOM 754 C CA . LYS A 1 94 ? 9.713 16.881 16.222 1.00 31.60 ? 112 LYS A CA 1 ATOM 755 C C . LYS A 1 94 ? 10.934 16.595 15.358 1.00 31.61 ? 112 LYS A C 1 ATOM 756 O O . LYS A 1 94 ? 10.815 15.999 14.286 1.00 31.07 ? 112 LYS A O 1 ATOM 757 C CB . LYS A 1 94 ? 9.548 15.822 17.332 1.00 32.55 ? 112 LYS A CB 1 ATOM 758 C CG . LYS A 1 94 ? 8.592 14.722 16.963 1.00 34.80 ? 112 LYS A CG 1 ATOM 759 C CD . LYS A 1 94 ? 8.574 13.571 17.985 1.00 38.15 ? 112 LYS A CD 1 ATOM 760 C CE . LYS A 1 94 ? 7.776 13.953 19.211 1.00 39.25 ? 112 LYS A CE 1 ATOM 761 N NZ . LYS A 1 94 ? 7.458 12.782 20.080 1.00 41.13 ? 112 LYS A NZ 1 ATOM 762 N N . CYS A 1 95 ? 12.095 17.067 15.793 1.00 31.56 ? 113 CYS A N 1 ATOM 763 C CA . CYS A 1 95 ? 13.300 16.941 14.960 1.00 32.74 ? 113 CYS A CA 1 ATOM 764 C C . CYS A 1 95 ? 13.712 15.489 14.766 1.00 32.69 ? 113 CYS A C 1 ATOM 765 O O . CYS A 1 95 ? 14.252 15.114 13.732 1.00 32.50 ? 113 CYS A O 1 ATOM 766 C CB . CYS A 1 95 ? 14.471 17.743 15.519 1.00 33.20 ? 113 CYS A CB 1 ATOM 767 S SG . CYS A 1 95 ? 14.352 19.512 15.136 1.00 35.82 ? 113 CYS A SG 1 ATOM 768 N N . THR A 1 96 ? 13.448 14.703 15.793 1.00 32.98 ? 114 THR A N 1 ATOM 769 C CA . THR A 1 96 ? 13.671 13.244 15.778 1.00 33.05 ? 114 THR A CA 1 ATOM 770 C C . THR A 1 96 ? 12.513 12.555 16.473 1.00 33.44 ? 114 THR A C 1 ATOM 771 O O . THR A 1 96 ? 11.689 13.199 17.136 1.00 32.58 ? 114 THR A O 1 ATOM 772 C CB . THR A 1 96 ? 14.937 12.831 16.519 1.00 33.33 ? 114 THR A CB 1 ATOM 773 O OG1 . THR A 1 96 ? 14.783 13.114 17.918 1.00 33.74 ? 114 THR A OG1 1 ATOM 774 C CG2 . THR A 1 96 ? 16.146 13.594 15.984 1.00 33.92 ? 114 THR A CG2 1 ATOM 775 N N . THR A 1 97 ? 12.456 11.237 16.346 1.00 34.02 ? 115 THR A N 1 ATOM 776 C CA . THR A 1 97 ? 11.275 10.519 16.818 1.00 34.79 ? 115 THR A CA 1 ATOM 777 C C . THR A 1 97 ? 11.196 10.577 18.332 1.00 35.04 ? 115 THR A C 1 ATOM 778 O O . THR A 1 97 ? 10.134 10.385 18.912 1.00 36.56 ? 115 THR A O 1 ATOM 779 C CB . THR A 1 97 ? 11.205 9.058 16.313 1.00 34.86 ? 115 THR A CB 1 ATOM 780 O OG1 . THR A 1 97 ? 12.490 8.443 16.423 1.00 35.54 ? 115 THR A OG1 1 ATOM 781 C CG2 . THR A 1 97 ? 10.777 9.046 14.860 1.00 34.66 ? 115 THR A CG2 1 ATOM 782 N N . SER A 1 98 ? 12.312 10.872 18.973 1.00 35.14 ? 116 SER A N 1 ATOM 783 C CA . SER A 1 98 ? 12.311 10.963 20.440 1.00 35.40 ? 116 SER A CA 1 ATOM 784 C C . SER A 1 98 ? 12.369 12.408 20.904 1.00 34.36 ? 116 SER A C 1 ATOM 785 O O . SER A 1 98 ? 12.758 12.708 22.034 1.00 34.23 ? 116 SER A O 1 ATOM 786 C CB . SER A 1 98 ? 13.463 10.166 21.047 1.00 35.71 ? 116 SER A CB 1 ATOM 787 O OG . SER A 1 98 ? 14.702 10.807 20.811 1.00 39.41 ? 116 SER A OG 1 ATOM 788 N N . GLY A 1 99 ? 11.956 13.295 20.020 1.00 33.38 ? 117 GLY A N 1 ATOM 789 C CA . GLY A 1 99 ? 11.945 14.729 20.316 1.00 32.66 ? 117 GLY A CA 1 ATOM 790 C C . GLY A 1 99 ? 10.746 15.188 21.113 1.00 32.48 ? 117 GLY A C 1 ATOM 791 O O . GLY A 1 99 ? 10.131 14.419 21.852 1.00 31.68 ? 117 GLY A O 1 ATOM 792 N N . SER A 1 100 ? 10.394 16.455 20.916 1.00 31.54 ? 118 SER A N 1 ATOM 793 C CA . SER A 1 100 ? 9.347 17.123 21.713 1.00 30.93 ? 118 SER A CA 1 ATOM 794 C C . SER A 1 100 ? 8.597 18.171 20.912 1.00 31.09 ? 118 SER A C 1 ATOM 795 O O . SER A 1 100 ? 9.173 19.184 20.524 1.00 30.33 ? 118 SER A O 1 ATOM 796 C CB . SER A 1 100 ? 9.971 17.831 22.913 1.00 31.53 ? 118 SER A CB 1 ATOM 797 O OG . SER A 1 100 ? 9.054 18.724 23.538 1.00 30.41 ? 118 SER A OG 1 ATOM 798 N N . ASN A 1 101 ? 7.310 17.936 20.693 1.00 30.50 ? 119 ASN A N 1 ATOM 799 C CA . ASN A 1 101 ? 6.478 18.945 20.040 1.00 30.10 ? 119 ASN A CA 1 ATOM 800 C C . ASN A 1 101 ? 6.283 20.177 20.930 1.00 30.25 ? 119 ASN A C 1 ATOM 801 O O . ASN A 1 101 ? 6.107 21.282 20.431 1.00 28.87 ? 119 ASN A O 1 ATOM 802 C CB . ASN A 1 101 ? 5.115 18.388 19.657 1.00 30.94 ? 119 ASN A CB 1 ATOM 803 C CG . ASN A 1 101 ? 4.362 19.321 18.743 1.00 30.38 ? 119 ASN A CG 1 ATOM 804 O OD1 . ASN A 1 101 ? 3.379 19.932 19.157 1.00 31.05 ? 119 ASN A OD1 1 ATOM 805 N ND2 . ASN A 1 101 ? 4.855 19.474 17.499 1.00 31.21 ? 119 ASN A ND2 1 ATOM 806 N N . ASP A 1 102 ? 6.322 19.974 22.242 1.00 30.17 ? 120 ASP A N 1 ATOM 807 C CA . ASP A 1 102 ? 6.194 21.090 23.209 1.00 30.47 ? 120 ASP A CA 1 ATOM 808 C C . ASP A 1 102 ? 7.294 22.143 23.004 1.00 29.88 ? 120 ASP A C 1 ATOM 809 O O . ASP A 1 102 ? 7.058 23.356 23.081 1.00 30.11 ? 120 ASP A O 1 ATOM 810 C CB . ASP A 1 102 ? 6.197 20.599 24.655 1.00 30.70 ? 120 ASP A CB 1 ATOM 811 C CG . ASP A 1 102 ? 4.891 19.930 25.041 1.00 33.82 ? 120 ASP A CG 1 ATOM 812 O OD1 . ASP A 1 102 ? 3.945 19.947 24.225 1.00 35.81 ? 120 ASP A OD1 1 ATOM 813 O OD2 . ASP A 1 102 ? 4.811 19.391 26.162 1.00 35.41 ? 120 ASP A OD2 1 ATOM 814 N N . ILE A 1 103 ? 8.493 21.670 22.720 1.00 28.76 ? 121 ILE A N 1 ATOM 815 C CA . ILE A 1 103 ? 9.602 22.570 22.367 1.00 28.08 ? 121 ILE A CA 1 ATOM 816 C C . ILE A 1 103 ? 9.237 23.405 21.129 1.00 28.40 ? 121 ILE A C 1 ATOM 817 O O . ILE A 1 103 ? 9.497 24.614 21.065 1.00 26.63 ? 121 ILE A O 1 ATOM 818 C CB . ILE A 1 103 ? 10.924 21.804 22.145 1.00 28.56 ? 121 ILE A CB 1 ATOM 819 C CG1 . ILE A 1 103 ? 11.495 21.330 23.494 1.00 27.93 ? 121 ILE A CG1 1 ATOM 820 C CG2 . ILE A 1 103 ? 11.981 22.642 21.411 1.00 27.13 ? 121 ILE A CG2 1 ATOM 821 C CD1 . ILE A 1 103 ? 11.828 22.477 24.482 1.00 27.74 ? 121 ILE A CD1 1 ATOM 822 N N . TRP A 1 104 ? 8.648 22.740 20.137 1.00 27.68 ? 122 TRP A N 1 ATOM 823 C CA . TRP A 1 104 ? 8.318 23.410 18.861 1.00 27.88 ? 122 TRP A CA 1 ATOM 824 C C . TRP A 1 104 ? 7.164 24.376 19.054 1.00 27.89 ? 122 TRP A C 1 ATOM 825 O O . TRP A 1 104 ? 7.096 25.454 18.441 1.00 26.83 ? 122 TRP A O 1 ATOM 826 C CB . TRP A 1 104 ? 8.097 22.395 17.726 1.00 27.80 ? 122 TRP A CB 1 ATOM 827 C CG . TRP A 1 104 ? 9.396 22.021 17.186 1.00 28.28 ? 122 TRP A CG 1 ATOM 828 C CD1 . TRP A 1 104 ? 10.149 20.936 17.518 1.00 28.28 ? 122 TRP A CD1 1 ATOM 829 C CD2 . TRP A 1 104 ? 10.190 22.808 16.304 1.00 27.31 ? 122 TRP A CD2 1 ATOM 830 N NE1 . TRP A 1 104 ? 11.361 20.975 16.856 1.00 27.28 ? 122 TRP A NE1 1 ATOM 831 C CE2 . TRP A 1 104 ? 11.405 22.118 16.104 1.00 27.25 ? 122 TRP A CE2 1 ATOM 832 C CE3 . TRP A 1 104 ? 9.984 24.024 15.637 1.00 27.28 ? 122 TRP A CE3 1 ATOM 833 C CZ2 . TRP A 1 104 ? 12.396 22.600 15.284 1.00 26.34 ? 122 TRP A CZ2 1 ATOM 834 C CZ3 . TRP A 1 104 ? 11.003 24.507 14.823 1.00 26.31 ? 122 TRP A CZ3 1 ATOM 835 C CH2 . TRP A 1 104 ? 12.178 23.799 14.658 1.00 27.15 ? 122 TRP A CH2 1 ATOM 836 N N . MET A 1 105 ? 6.283 24.037 19.979 1.00 27.70 ? 123 MET A N 1 ATOM 837 C CA . MET A 1 105 ? 5.225 24.985 20.358 1.00 27.91 ? 123 MET A CA 1 ATOM 838 C C . MET A 1 105 ? 5.804 26.222 21.032 1.00 27.80 ? 123 MET A C 1 ATOM 839 O O . MET A 1 105 ? 5.319 27.354 20.847 1.00 27.44 ? 123 MET A O 1 ATOM 840 C CB . MET A 1 105 ? 4.162 24.318 21.239 1.00 28.03 ? 123 MET A CB 1 ATOM 841 C CG . MET A 1 105 ? 3.268 23.342 20.464 1.00 29.45 ? 123 MET A CG 1 ATOM 842 S SD . MET A 1 105 ? 2.334 24.103 19.117 1.00 32.58 ? 123 MET A SD 1 ATOM 843 C CE . MET A 1 105 ? 3.284 23.590 17.702 1.00 30.45 ? 123 MET A CE 1 ATOM 844 N N . GLN A 1 106 ? 6.854 26.019 21.816 1.00 28.03 ? 124 GLN A N 1 ATOM 845 C CA . GLN A 1 106 ? 7.507 27.135 22.487 1.00 28.37 ? 124 GLN A CA 1 ATOM 846 C C . GLN A 1 106 ? 8.151 28.025 21.432 1.00 27.57 ? 124 GLN A C 1 ATOM 847 O O . GLN A 1 106 ? 8.040 29.246 21.468 1.00 26.72 ? 124 GLN A O 1 ATOM 848 C CB . GLN A 1 106 ? 8.540 26.635 23.498 1.00 29.47 ? 124 GLN A CB 1 ATOM 849 C CG . GLN A 1 106 ? 9.337 27.687 24.195 1.00 32.02 ? 124 GLN A CG 1 ATOM 850 C CD . GLN A 1 106 ? 10.224 27.086 25.280 1.00 35.05 ? 124 GLN A CD 1 ATOM 851 O OE1 . GLN A 1 106 ? 10.830 26.014 25.096 1.00 34.54 ? 124 GLN A OE1 1 ATOM 852 N NE2 . GLN A 1 106 ? 10.280 27.758 26.427 1.00 37.87 ? 124 GLN A NE2 1 ATOM 853 N N . ASN A 1 107 ? 8.757 27.374 20.454 1.00 26.56 ? 125 ASN A N 1 ATOM 854 C CA . ASN A 1 107 ? 9.410 28.076 19.340 1.00 25.64 ? 125 ASN A CA 1 ATOM 855 C C . ASN A 1 107 ? 8.383 28.923 18.600 1.00 25.18 ? 125 ASN A C 1 ATOM 856 O O . ASN A 1 107 ? 8.618 30.097 18.272 1.00 26.49 ? 125 ASN A O 1 ATOM 857 C CB . ASN A 1 107 ? 10.078 27.089 18.373 1.00 25.95 ? 125 ASN A CB 1 ATOM 858 C CG . ASN A 1 107 ? 11.337 26.389 18.948 1.00 25.67 ? 125 ASN A CG 1 ATOM 859 O OD1 . ASN A 1 107 ? 11.899 26.775 19.990 1.00 24.98 ? 125 ASN A OD1 1 ATOM 860 N ND2 . ASN A 1 107 ? 11.785 25.350 18.238 1.00 25.79 ? 125 ASN A ND2 1 ATOM 861 N N . LYS A 1 108 ? 7.236 28.324 18.345 1.00 25.76 ? 126 LYS A N 1 ATOM 862 C CA . LYS A 1 108 ? 6.136 28.995 17.630 1.00 25.69 ? 126 LYS A CA 1 ATOM 863 C C . LYS A 1 108 ? 5.727 30.302 18.329 1.00 25.61 ? 126 LYS A C 1 ATOM 864 O O . LYS A 1 108 ? 5.615 31.359 17.699 1.00 26.14 ? 126 LYS A O 1 ATOM 865 C CB . LYS A 1 108 ? 4.943 28.050 17.448 1.00 26.30 ? 126 LYS A CB 1 ATOM 866 C CG . LYS A 1 108 ? 3.713 28.709 16.814 1.00 26.47 ? 126 LYS A CG 1 ATOM 867 C CD . LYS A 1 108 ? 2.609 27.707 16.597 1.00 25.37 ? 126 LYS A CD 1 ATOM 868 C CE . LYS A 1 108 ? 1.296 28.360 16.197 1.00 27.13 ? 126 LYS A CE 1 ATOM 869 N NZ . LYS A 1 108 ? 0.245 27.328 15.816 1.00 27.60 ? 126 LYS A NZ 1 ATOM 870 N N . GLY A 1 109 ? 5.528 30.222 19.638 1.00 25.99 ? 127 GLY A N 1 ATOM 871 C CA . GLY A 1 109 ? 5.166 31.380 20.445 1.00 26.11 ? 127 GLY A CA 1 ATOM 872 C C . GLY A 1 109 ? 6.218 32.487 20.386 1.00 26.27 ? 127 GLY A C 1 ATOM 873 O O . GLY A 1 109 ? 5.897 33.681 20.226 1.00 26.05 ? 127 GLY A O 1 ATOM 874 N N . LEU A 1 110 ? 7.483 32.084 20.524 1.00 25.41 ? 128 LEU A N 1 ATOM 875 C CA . LEU A 1 110 ? 8.591 33.054 20.538 1.00 24.87 ? 128 LEU A CA 1 ATOM 876 C C . LEU A 1 110 ? 8.690 33.751 19.190 1.00 24.84 ? 128 LEU A C 1 ATOM 877 O O . LEU A 1 110 ? 8.924 34.968 19.124 1.00 24.70 ? 128 LEU A O 1 ATOM 878 C CB . LEU A 1 110 ? 9.908 32.407 20.900 1.00 24.51 ? 128 LEU A CB 1 ATOM 879 C CG . LEU A 1 110 ? 10.013 31.901 22.344 1.00 26.98 ? 128 LEU A CG 1 ATOM 880 C CD1 . LEU A 1 110 ? 11.284 31.080 22.559 1.00 27.45 ? 128 LEU A CD1 1 ATOM 881 C CD2 . LEU A 1 110 ? 9.916 33.142 23.306 1.00 29.11 ? 128 LEU A CD2 1 ATOM 882 N N . PHE A 1 111 ? 8.500 32.977 18.125 1.00 24.23 ? 129 PHE A N 1 ATOM 883 C CA . PHE A 1 111 ? 8.554 33.542 16.761 1.00 24.72 ? 129 PHE A CA 1 ATOM 884 C C . PHE A 1 111 ? 7.467 34.580 16.539 1.00 24.55 ? 129 PHE A C 1 ATOM 885 O O . PHE A 1 111 ? 7.756 35.688 16.095 1.00 25.06 ? 129 PHE A O 1 ATOM 886 C CB . PHE A 1 111 ? 8.454 32.444 15.694 1.00 25.17 ? 129 PHE A CB 1 ATOM 887 C CG . PHE A 1 111 ? 8.360 32.973 14.281 1.00 25.31 ? 129 PHE A CG 1 ATOM 888 C CD1 . PHE A 1 111 ? 9.482 33.420 13.632 1.00 26.52 ? 129 PHE A CD1 1 ATOM 889 C CD2 . PHE A 1 111 ? 7.147 32.985 13.611 1.00 26.37 ? 129 PHE A CD2 1 ATOM 890 C CE1 . PHE A 1 111 ? 9.413 33.900 12.323 1.00 28.46 ? 129 PHE A CE1 1 ATOM 891 C CE2 . PHE A 1 111 ? 7.052 33.459 12.328 1.00 24.75 ? 129 PHE A CE2 1 ATOM 892 C CZ . PHE A 1 111 ? 8.193 33.914 11.667 1.00 25.72 ? 129 PHE A CZ 1 ATOM 893 N N . TYR A 1 112 ? 6.211 34.214 16.822 1.00 25.19 ? 130 TYR A N 1 ATOM 894 C CA . TYR A 1 112 ? 5.073 35.110 16.526 1.00 24.96 ? 130 TYR A CA 1 ATOM 895 C C . TYR A 1 112 ? 5.142 36.323 17.425 1.00 25.05 ? 130 TYR A C 1 ATOM 896 O O . TYR A 1 112 ? 4.726 37.395 17.053 1.00 24.89 ? 130 TYR A O 1 ATOM 897 C CB . TYR A 1 112 ? 3.714 34.410 16.630 1.00 25.12 ? 130 TYR A CB 1 ATOM 898 C CG . TYR A 1 112 ? 3.404 33.614 15.378 1.00 25.05 ? 130 TYR A CG 1 ATOM 899 C CD1 . TYR A 1 112 ? 3.133 34.261 14.179 1.00 26.31 ? 130 TYR A CD1 1 ATOM 900 C CD2 . TYR A 1 112 ? 3.436 32.226 15.372 1.00 25.76 ? 130 TYR A CD2 1 ATOM 901 C CE1 . TYR A 1 112 ? 2.860 33.545 13.027 1.00 27.84 ? 130 TYR A CE1 1 ATOM 902 C CE2 . TYR A 1 112 ? 3.173 31.488 14.204 1.00 25.71 ? 130 TYR A CE2 1 ATOM 903 C CZ . TYR A 1 112 ? 2.888 32.153 13.043 1.00 27.88 ? 130 TYR A CZ 1 ATOM 904 O OH . TYR A 1 112 ? 2.622 31.436 11.889 1.00 26.50 ? 130 TYR A OH 1 ATOM 905 N N . THR A 1 113 ? 5.769 36.172 18.576 1.00 25.13 ? 131 THR A N 1 ATOM 906 C CA . THR A 1 113 ? 5.961 37.343 19.459 1.00 25.98 ? 131 THR A CA 1 ATOM 907 C C . THR A 1 113 ? 6.752 38.428 18.732 1.00 24.78 ? 131 THR A C 1 ATOM 908 O O . THR A 1 113 ? 6.397 39.604 18.745 1.00 26.17 ? 131 THR A O 1 ATOM 909 C CB . THR A 1 113 ? 6.608 36.969 20.831 1.00 25.97 ? 131 THR A CB 1 ATOM 910 O OG1 . THR A 1 113 ? 5.759 36.044 21.535 1.00 27.13 ? 131 THR A OG1 1 ATOM 911 C CG2 . THR A 1 113 ? 6.775 38.238 21.715 1.00 27.94 ? 131 THR A CG2 1 ATOM 912 N N . GLN A 1 114 ? 7.831 38.037 18.089 1.00 26.13 ? 132 GLN A N 1 ATOM 913 C CA . GLN A 1 114 ? 8.693 39.005 17.415 1.00 25.56 ? 132 GLN A CA 1 ATOM 914 C C . GLN A 1 114 ? 7.999 39.557 16.163 1.00 25.53 ? 132 GLN A C 1 ATOM 915 O O . GLN A 1 114 ? 8.138 40.733 15.806 1.00 25.37 ? 132 GLN A O 1 ATOM 916 C CB . GLN A 1 114 ? 10.032 38.410 17.034 1.00 26.94 ? 132 GLN A CB 1 ATOM 917 C CG . GLN A 1 114 ? 10.851 37.849 18.191 1.00 26.40 ? 132 GLN A CG 1 ATOM 918 C CD . GLN A 1 114 ? 11.377 38.908 19.138 1.00 33.04 ? 132 GLN A CD 1 ATOM 919 O OE1 . GLN A 1 114 ? 10.681 39.818 19.490 1.00 34.68 ? 132 GLN A OE1 1 ATOM 920 N NE2 . GLN A 1 114 ? 12.653 38.777 19.542 1.00 35.31 ? 132 GLN A NE2 1 ATOM 921 N N . VAL A 1 115 ? 7.296 38.678 15.458 1.00 25.41 ? 133 VAL A N 1 ATOM 922 C CA . VAL A 1 115 ? 6.562 39.134 14.272 1.00 24.71 ? 133 VAL A CA 1 ATOM 923 C C . VAL A 1 115 ? 5.524 40.209 14.630 1.00 25.31 ? 133 VAL A C 1 ATOM 924 O O . VAL A 1 115 ? 5.451 41.285 14.015 1.00 24.09 ? 133 VAL A O 1 ATOM 925 C CB . VAL A 1 115 ? 5.915 37.963 13.522 1.00 24.62 ? 133 VAL A CB 1 ATOM 926 C CG1 . VAL A 1 115 ? 5.023 38.502 12.413 1.00 23.84 ? 133 VAL A CG1 1 ATOM 927 C CG2 . VAL A 1 115 ? 7.000 37.005 12.949 1.00 24.77 ? 133 VAL A CG2 1 ATOM 928 N N . TYR A 1 116 ? 4.711 39.922 15.644 1.00 24.94 ? 134 TYR A N 1 ATOM 929 C CA . TYR A 1 116 ? 3.638 40.839 15.999 1.00 24.73 ? 134 TYR A CA 1 ATOM 930 C C . TYR A 1 116 ? 4.222 42.145 16.545 1.00 24.69 ? 134 TYR A C 1 ATOM 931 O O . TYR A 1 116 ? 3.778 43.217 16.194 1.00 25.57 ? 134 TYR A O 1 ATOM 932 C CB . TYR A 1 116 ? 2.647 40.244 17.018 1.00 24.40 ? 134 TYR A CB 1 ATOM 933 C CG . TYR A 1 116 ? 1.947 38.992 16.596 1.00 24.79 ? 134 TYR A CG 1 ATOM 934 C CD1 . TYR A 1 116 ? 1.787 38.668 15.250 1.00 26.26 ? 134 TYR A CD1 1 ATOM 935 C CD2 . TYR A 1 116 ? 1.482 38.099 17.547 1.00 25.36 ? 134 TYR A CD2 1 ATOM 936 C CE1 . TYR A 1 116 ? 1.168 37.493 14.860 1.00 26.72 ? 134 TYR A CE1 1 ATOM 937 C CE2 . TYR A 1 116 ? 0.866 36.934 17.180 1.00 26.41 ? 134 TYR A CE2 1 ATOM 938 C CZ . TYR A 1 116 ? 0.696 36.634 15.837 1.00 26.47 ? 134 TYR A CZ 1 ATOM 939 O OH . TYR A 1 116 ? 0.084 35.461 15.490 1.00 25.27 ? 134 TYR A OH 1 ATOM 940 N N . LYS A 1 117 ? 5.240 42.053 17.391 1.00 24.80 ? 135 LYS A N 1 ATOM 941 C CA . LYS A 1 117 ? 5.803 43.268 17.974 1.00 25.34 ? 135 LYS A CA 1 ATOM 942 C C . LYS A 1 117 ? 6.380 44.186 16.880 1.00 25.52 ? 135 LYS A C 1 ATOM 943 O O . LYS A 1 117 ? 6.219 45.407 16.903 1.00 25.37 ? 135 LYS A O 1 ATOM 944 C CB . LYS A 1 117 ? 6.865 42.943 19.023 1.00 25.17 ? 135 LYS A CB 1 ATOM 945 C CG . LYS A 1 117 ? 6.317 42.430 20.334 1.00 26.02 ? 135 LYS A CG 1 ATOM 946 C CD . LYS A 1 117 ? 7.492 42.188 21.299 1.00 28.28 ? 135 LYS A CD 1 ATOM 947 C CE . LYS A 1 117 ? 7.025 41.781 22.679 1.00 32.34 ? 135 LYS A CE 1 ATOM 948 N NZ . LYS A 1 117 ? 8.239 41.484 23.582 1.00 33.76 ? 135 LYS A NZ 1 ATOM 949 N N . ASN A 1 118 ? 7.027 43.571 15.903 1.00 25.51 ? 136 ASN A N 1 ATOM 950 C CA . ASN A 1 118 ? 7.717 44.333 14.880 1.00 25.49 ? 136 ASN A CA 1 ATOM 951 C C . ASN A 1 118 ? 6.784 44.872 13.807 1.00 25.49 ? 136 ASN A C 1 ATOM 952 O O . ASN A 1 118 ? 6.968 45.966 13.279 1.00 25.39 ? 136 ASN A O 1 ATOM 953 C CB . ASN A 1 118 ? 8.925 43.570 14.343 1.00 26.09 ? 136 ASN A CB 1 ATOM 954 C CG . ASN A 1 118 ? 10.068 43.627 15.319 1.00 28.03 ? 136 ASN A CG 1 ATOM 955 O OD1 . ASN A 1 118 ? 10.754 44.642 15.378 1.00 31.93 ? 136 ASN A OD1 1 ATOM 956 N ND2 . ASN A 1 118 ? 10.226 42.591 16.155 1.00 28.92 ? 136 ASN A ND2 1 ATOM 957 N N . MET A 1 119 ? 5.719 44.137 13.541 1.00 25.92 ? 137 MET A N 1 ATOM 958 C CA . MET A 1 119 ? 4.781 44.589 12.520 1.00 25.77 ? 137 MET A CA 1 ATOM 959 C C . MET A 1 119 ? 3.872 45.686 13.069 1.00 25.95 ? 137 MET A C 1 ATOM 960 O O . MET A 1 119 ? 3.044 46.228 12.361 1.00 26.56 ? 137 MET A O 1 ATOM 961 C CB . MET A 1 119 ? 3.997 43.448 11.907 1.00 26.23 ? 137 MET A CB 1 ATOM 962 C CG . MET A 1 119 ? 4.831 42.562 10.983 1.00 24.56 ? 137 MET A CG 1 ATOM 963 S SD . MET A 1 119 ? 5.972 43.459 9.892 1.00 28.16 ? 137 MET A SD 1 ATOM 964 C CE . MET A 1 119 ? 4.752 44.243 8.823 1.00 23.55 ? 137 MET A CE 1 ATOM 965 N N . ALA A 1 120 ? 4.048 46.022 14.341 1.00 26.21 ? 138 ALA A N 1 ATOM 966 C CA . ALA A 1 120 ? 3.402 47.227 14.903 1.00 25.44 ? 138 ALA A CA 1 ATOM 967 C C . ALA A 1 120 ? 4.214 48.501 14.595 1.00 25.16 ? 138 ALA A C 1 ATOM 968 O O . ALA A 1 120 ? 3.685 49.609 14.705 1.00 25.29 ? 138 ALA A O 1 ATOM 969 C CB . ALA A 1 120 ? 3.162 47.108 16.424 1.00 24.81 ? 138 ALA A CB 1 ATOM 970 N N . VAL A 1 121 ? 5.463 48.332 14.149 1.00 25.89 ? 139 VAL A N 1 ATOM 971 C CA . VAL A 1 121 ? 6.352 49.470 13.859 1.00 25.89 ? 139 VAL A CA 1 ATOM 972 C C . VAL A 1 121 ? 7.013 49.470 12.483 1.00 25.52 ? 139 VAL A C 1 ATOM 973 O O . VAL A 1 121 ? 7.787 50.381 12.172 1.00 27.19 ? 139 VAL A O 1 ATOM 974 C CB . VAL A 1 121 ? 7.443 49.687 14.971 1.00 25.49 ? 139 VAL A CB 1 ATOM 975 C CG1 . VAL A 1 121 ? 6.748 50.066 16.302 1.00 24.74 ? 139 VAL A CG1 1 ATOM 976 C CG2 . VAL A 1 121 ? 8.344 48.437 15.175 1.00 26.17 ? 139 VAL A CG2 1 ATOM 977 N N . TYR A 1 122 ? 6.710 48.453 11.670 1.00 26.35 ? 140 TYR A N 1 ATOM 978 C CA . TYR A 1 122 ? 7.152 48.390 10.262 1.00 25.62 ? 140 TYR A CA 1 ATOM 979 C C . TYR A 1 122 ? 5.947 48.179 9.353 1.00 26.12 ? 140 TYR A C 1 ATOM 980 O O . TYR A 1 122 ? 5.015 47.474 9.705 1.00 25.01 ? 140 TYR A O 1 ATOM 981 C CB . TYR A 1 122 ? 8.191 47.290 10.020 1.00 26.56 ? 140 TYR A CB 1 ATOM 982 C CG . TYR A 1 122 ? 9.514 47.619 10.664 1.00 24.87 ? 140 TYR A CG 1 ATOM 983 C CD1 . TYR A 1 122 ? 10.413 48.490 10.054 1.00 27.68 ? 140 TYR A CD1 1 ATOM 984 C CD2 . TYR A 1 122 ? 9.848 47.095 11.885 1.00 25.43 ? 140 TYR A CD2 1 ATOM 985 C CE1 . TYR A 1 122 ? 11.612 48.820 10.669 1.00 29.27 ? 140 TYR A CE1 1 ATOM 986 C CE2 . TYR A 1 122 ? 11.037 47.415 12.507 1.00 27.97 ? 140 TYR A CE2 1 ATOM 987 C CZ . TYR A 1 122 ? 11.926 48.273 11.887 1.00 29.52 ? 140 TYR A CZ 1 ATOM 988 O OH . TYR A 1 122 ? 13.096 48.610 12.528 1.00 31.83 ? 140 TYR A OH 1 ATOM 989 N N . ARG A 1 123 ? 5.983 48.790 8.179 1.00 25.85 ? 141 ARG A N 1 ATOM 990 C CA . ARG A 1 123 ? 4.879 48.651 7.219 1.00 26.04 ? 141 ARG A CA 1 ATOM 991 C C . ARG A 1 123 ? 4.978 47.335 6.492 1.00 26.25 ? 141 ARG A C 1 ATOM 992 O O . ARG A 1 123 ? 3.992 46.734 6.106 1.00 26.32 ? 141 ARG A O 1 ATOM 993 C CB . ARG A 1 123 ? 4.914 49.770 6.156 1.00 26.07 ? 141 ARG A CB 1 ATOM 994 C CG . ARG A 1 123 ? 4.621 51.171 6.655 1.00 27.84 ? 141 ARG A CG 1 ATOM 995 C CD . ARG A 1 123 ? 4.557 52.155 5.482 1.00 27.47 ? 141 ARG A CD 1 ATOM 996 N NE . ARG A 1 123 ? 3.627 51.709 4.434 1.00 26.99 ? 141 ARG A NE 1 ATOM 997 C CZ . ARG A 1 123 ? 2.313 51.904 4.461 1.00 28.42 ? 141 ARG A CZ 1 ATOM 998 N NH1 . ARG A 1 123 ? 1.753 52.520 5.485 1.00 28.14 ? 141 ARG A NH1 1 ATOM 999 N NH2 . ARG A 1 123 ? 1.559 51.454 3.457 1.00 28.18 ? 141 ARG A NH2 1 ATOM 1000 N N . SER A 1 124 ? 6.211 46.938 6.239 1.00 27.01 ? 142 SER A N 1 ATOM 1001 C CA . SER A 1 124 ? 6.487 45.898 5.243 1.00 27.35 ? 142 SER A CA 1 ATOM 1002 C C . SER A 1 124 ? 7.126 44.647 5.804 1.00 27.41 ? 142 SER A C 1 ATOM 1003 O O . SER A 1 124 ? 8.086 44.702 6.566 1.00 26.92 ? 142 SER A O 1 ATOM 1004 C CB . SER A 1 124 ? 7.370 46.503 4.133 1.00 28.24 ? 142 SER A CB 1 ATOM 1005 O OG . SER A 1 124 ? 7.674 45.540 3.157 1.00 32.22 ? 142 SER A OG 1 ATOM 1006 N N . LEU A 1 125 ? 6.576 43.510 5.379 1.00 26.74 ? 143 LEU A N 1 ATOM 1007 C CA . LEU A 1 125 ? 7.112 42.191 5.705 1.00 25.62 ? 143 LEU A CA 1 ATOM 1008 C C . LEU A 1 125 ? 7.272 41.397 4.410 1.00 26.65 ? 143 LEU A C 1 ATOM 1009 O O . LEU A 1 125 ? 6.376 41.401 3.529 1.00 26.49 ? 143 LEU A O 1 ATOM 1010 C CB . LEU A 1 125 ? 6.146 41.439 6.629 1.00 26.41 ? 143 LEU A CB 1 ATOM 1011 C CG . LEU A 1 125 ? 6.480 40.017 7.048 1.00 25.77 ? 143 LEU A CG 1 ATOM 1012 C CD1 . LEU A 1 125 ? 5.919 39.651 8.475 1.00 26.12 ? 143 LEU A CD1 1 ATOM 1013 C CD2 . LEU A 1 125 ? 6.004 38.998 5.983 1.00 26.27 ? 143 LEU A CD2 1 ATOM 1014 N N . THR A 1 126 ? 8.418 40.765 4.290 1.00 26.11 ? 144 THR A N 1 ATOM 1015 C CA . THR A 1 126 ? 8.633 39.735 3.271 1.00 26.35 ? 144 THR A CA 1 ATOM 1016 C C . THR A 1 126 ? 9.721 38.790 3.765 1.00 26.82 ? 144 THR A C 1 ATOM 1017 O O . THR A 1 126 ? 10.265 38.937 4.863 1.00 27.67 ? 144 THR A O 1 ATOM 1018 C CB . THR A 1 126 ? 8.998 40.339 1.874 1.00 26.89 ? 144 THR A CB 1 ATOM 1019 O OG1 . THR A 1 126 ? 8.928 39.332 0.835 1.00 28.30 ? 144 THR A OG1 1 ATOM 1020 C CG2 . THR A 1 126 ? 10.378 40.928 1.887 1.00 26.70 ? 144 THR A CG2 1 ATOM 1021 N N . PHE A 1 127 ? 10.051 37.829 2.925 1.00 27.52 ? 145 PHE A N 1 ATOM 1022 C CA . PHE A 1 127 ? 11.133 36.906 3.235 1.00 27.86 ? 145 PHE A CA 1 ATOM 1023 C C . PHE A 1 127 ? 12.313 37.259 2.366 1.00 28.19 ? 145 PHE A C 1 ATOM 1024 O O . PHE A 1 127 ? 12.149 37.601 1.193 1.00 27.87 ? 145 PHE A O 1 ATOM 1025 C CB . PHE A 1 127 ? 10.748 35.461 2.927 1.00 27.86 ? 145 PHE A CB 1 ATOM 1026 C CG . PHE A 1 127 ? 9.980 34.795 4.012 1.00 28.10 ? 145 PHE A CG 1 ATOM 1027 C CD1 . PHE A 1 127 ? 10.627 34.129 5.022 1.00 28.18 ? 145 PHE A CD1 1 ATOM 1028 C CD2 . PHE A 1 127 ? 8.610 34.813 4.006 1.00 29.72 ? 145 PHE A CD2 1 ATOM 1029 C CE1 . PHE A 1 127 ? 9.911 33.489 6.007 1.00 28.44 ? 145 PHE A CE1 1 ATOM 1030 C CE2 . PHE A 1 127 ? 7.890 34.189 5.005 1.00 30.35 ? 145 PHE A CE2 1 ATOM 1031 C CZ . PHE A 1 127 ? 8.538 33.532 5.994 1.00 27.94 ? 145 PHE A CZ 1 ATOM 1032 N N . VAL A 1 128 ? 13.505 37.122 2.936 1.00 28.31 ? 146 VAL A N 1 ATOM 1033 C CA . VAL A 1 128 ? 14.750 37.198 2.143 1.00 29.22 ? 146 VAL A CA 1 ATOM 1034 C C . VAL A 1 128 ? 15.608 35.993 2.424 1.00 29.27 ? 146 VAL A C 1 ATOM 1035 O O . VAL A 1 128 ? 15.654 35.473 3.534 1.00 28.71 ? 146 VAL A O 1 ATOM 1036 C CB . VAL A 1 128 ? 15.601 38.486 2.407 1.00 29.71 ? 146 VAL A CB 1 ATOM 1037 C CG1 . VAL A 1 128 ? 14.905 39.725 1.862 1.00 31.90 ? 146 VAL A CG1 1 ATOM 1038 C CG2 . VAL A 1 128 ? 15.936 38.648 3.872 1.00 30.27 ? 146 VAL A CG2 1 ATOM 1039 N N . ASN A 1 129 ? 16.253 35.518 1.383 1.00 30.32 ? 147 ASN A N 1 ATOM 1040 C CA . ASN A 1 129 ? 17.287 34.494 1.531 1.00 30.98 ? 147 ASN A CA 1 ATOM 1041 C C . ASN A 1 129 ? 18.487 35.136 2.219 1.00 30.51 ? 147 ASN A C 1 ATOM 1042 O O . ASN A 1 129 ? 18.797 36.312 2.000 1.00 32.13 ? 147 ASN A O 1 ATOM 1043 C CB . ASN A 1 129 ? 17.681 33.905 0.166 1.00 32.50 ? 147 ASN A CB 1 ATOM 1044 C CG . ASN A 1 129 ? 16.562 33.019 -0.437 1.00 34.87 ? 147 ASN A CG 1 ATOM 1045 O OD1 . ASN A 1 129 ? 16.321 33.034 -1.663 1.00 42.94 ? 147 ASN A OD1 1 ATOM 1046 N ND2 . ASN A 1 129 ? 15.890 32.228 0.418 1.00 36.74 ? 147 ASN A ND2 1 ATOM 1047 N N . VAL A 1 130 ? 19.120 34.380 3.094 1.00 28.46 ? 148 VAL A N 1 ATOM 1048 C CA . VAL A 1 130 ? 20.305 34.848 3.794 1.00 27.82 ? 148 VAL A CA 1 ATOM 1049 C C . VAL A 1 130 ? 21.526 34.145 3.162 1.00 28.43 ? 148 VAL A C 1 ATOM 1050 O O . VAL A 1 130 ? 21.724 32.947 3.312 1.00 27.47 ? 148 VAL A O 1 ATOM 1051 C CB . VAL A 1 130 ? 20.229 34.533 5.291 1.00 27.78 ? 148 VAL A CB 1 ATOM 1052 C CG1 . VAL A 1 130 ? 21.605 34.840 5.999 1.00 26.48 ? 148 VAL A CG1 1 ATOM 1053 C CG2 . VAL A 1 130 ? 19.093 35.305 5.943 1.00 27.18 ? 148 VAL A CG2 1 ATOM 1054 N N . PRO A 1 131 ? 22.334 34.887 2.421 1.00 28.41 ? 149 PRO A N 1 ATOM 1055 C CA . PRO A 1 131 ? 23.498 34.185 1.922 1.00 29.29 ? 149 PRO A CA 1 ATOM 1056 C C . PRO A 1 131 ? 24.514 33.913 3.016 1.00 28.34 ? 149 PRO A C 1 ATOM 1057 O O . PRO A 1 131 ? 24.722 34.732 3.927 1.00 27.90 ? 149 PRO A O 1 ATOM 1058 C CB . PRO A 1 131 ? 24.083 35.153 0.907 1.00 29.35 ? 149 PRO A CB 1 ATOM 1059 C CG . PRO A 1 131 ? 23.691 36.498 1.395 1.00 29.83 ? 149 PRO A CG 1 ATOM 1060 C CD . PRO A 1 131 ? 22.347 36.322 2.101 1.00 28.93 ? 149 PRO A CD 1 ATOM 1061 N N . TYR A 1 132 ? 25.125 32.748 2.908 1.00 27.88 ? 150 TYR A N 1 ATOM 1062 C CA . TYR A 1 132 ? 26.254 32.398 3.779 1.00 27.26 ? 150 TYR A CA 1 ATOM 1063 C C . TYR A 1 132 ? 27.359 31.673 3.024 1.00 27.90 ? 150 TYR A C 1 ATOM 1064 O O . TYR A 1 132 ? 27.130 31.031 1.992 1.00 27.26 ? 150 TYR A O 1 ATOM 1065 C CB . TYR A 1 132 ? 25.795 31.565 4.972 1.00 27.00 ? 150 TYR A CB 1 ATOM 1066 C CG . TYR A 1 132 ? 25.354 30.159 4.664 1.00 28.22 ? 150 TYR A CG 1 ATOM 1067 C CD1 . TYR A 1 132 ? 26.269 29.114 4.670 1.00 29.30 ? 150 TYR A CD1 1 ATOM 1068 C CD2 . TYR A 1 132 ? 24.035 29.874 4.365 1.00 30.52 ? 150 TYR A CD2 1 ATOM 1069 C CE1 . TYR A 1 132 ? 25.894 27.828 4.389 1.00 30.71 ? 150 TYR A CE1 1 ATOM 1070 C CE2 . TYR A 1 132 ? 23.635 28.573 4.096 1.00 31.94 ? 150 TYR A CE2 1 ATOM 1071 C CZ . TYR A 1 132 ? 24.572 27.556 4.113 1.00 31.53 ? 150 TYR A CZ 1 ATOM 1072 O OH . TYR A 1 132 ? 24.199 26.267 3.844 1.00 32.55 ? 150 TYR A OH 1 ATOM 1073 N N . VAL A 1 133 ? 28.559 31.815 3.558 1.00 27.57 ? 151 VAL A N 1 ATOM 1074 C CA . VAL A 1 133 ? 29.726 31.090 3.057 1.00 28.03 ? 151 VAL A CA 1 ATOM 1075 C C . VAL A 1 133 ? 30.361 30.269 4.164 1.00 28.30 ? 151 VAL A C 1 ATOM 1076 O O . VAL A 1 133 ? 30.713 30.772 5.224 1.00 27.91 ? 151 VAL A O 1 ATOM 1077 C CB . VAL A 1 133 ? 30.755 32.034 2.446 1.00 27.67 ? 151 VAL A CB 1 ATOM 1078 C CG1 . VAL A 1 133 ? 32.060 31.256 2.116 1.00 28.37 ? 151 VAL A CG1 1 ATOM 1079 C CG2 . VAL A 1 133 ? 30.166 32.704 1.220 1.00 28.10 ? 151 VAL A CG2 1 ATOM 1080 N N . TYR A 1 134 ? 30.454 28.976 3.901 1.00 29.50 ? 152 TYR A N 1 ATOM 1081 C CA . TYR A 1 134 ? 31.175 28.044 4.740 1.00 31.67 ? 152 TYR A CA 1 ATOM 1082 C C . TYR A 1 134 ? 32.384 27.543 3.930 1.00 33.67 ? 152 TYR A C 1 ATOM 1083 O O . TYR A 1 134 ? 32.258 27.205 2.754 1.00 35.15 ? 152 TYR A O 1 ATOM 1084 C CB . TYR A 1 134 ? 30.257 26.885 5.120 1.00 31.07 ? 152 TYR A CB 1 ATOM 1085 C CG . TYR A 1 134 ? 30.942 25.770 5.861 1.00 31.17 ? 152 TYR A CG 1 ATOM 1086 C CD1 . TYR A 1 134 ? 31.263 24.567 5.218 1.00 31.17 ? 152 TYR A CD1 1 ATOM 1087 C CD2 . TYR A 1 134 ? 31.274 25.909 7.203 1.00 29.93 ? 152 TYR A CD2 1 ATOM 1088 C CE1 . TYR A 1 134 ? 31.886 23.542 5.906 1.00 31.53 ? 152 TYR A CE1 1 ATOM 1089 C CE2 . TYR A 1 134 ? 31.908 24.897 7.890 1.00 30.67 ? 152 TYR A CE2 1 ATOM 1090 C CZ . TYR A 1 134 ? 32.211 23.711 7.233 1.00 31.52 ? 152 TYR A CZ 1 ATOM 1091 O OH . TYR A 1 134 ? 32.824 22.701 7.920 1.00 34.37 ? 152 TYR A OH 1 ATOM 1092 N N . ASN A 1 135 ? 33.520 27.482 4.589 1.00 36.97 ? 153 ASN A N 1 ATOM 1093 C CA . ASN A 1 135 ? 34.834 27.285 3.931 1.00 39.34 ? 153 ASN A CA 1 ATOM 1094 C C . ASN A 1 135 ? 35.271 25.843 3.795 1.00 39.59 ? 153 ASN A C 1 ATOM 1095 O O . ASN A 1 135 ? 36.191 25.519 3.034 1.00 40.85 ? 153 ASN A O 1 ATOM 1096 C CB . ASN A 1 135 ? 35.934 27.990 4.740 1.00 40.46 ? 153 ASN A CB 1 ATOM 1097 C CG . ASN A 1 135 ? 36.547 29.141 3.991 1.00 43.96 ? 153 ASN A CG 1 ATOM 1098 O OD1 . ASN A 1 135 ? 37.674 29.550 4.284 1.00 46.17 ? 153 ASN A OD1 1 ATOM 1099 N ND2 . ASN A 1 135 ? 35.816 29.670 3.008 1.00 46.57 ? 153 ASN A ND2 1 ATOM 1100 N N . GLY A 1 136 ? 34.665 24.996 4.601 1.00 39.27 ? 154 GLY A N 1 ATOM 1101 C CA . GLY A 1 136 ? 35.010 23.589 4.623 1.00 39.22 ? 154 GLY A CA 1 ATOM 1102 C C . GLY A 1 136 ? 34.520 22.917 3.374 1.00 39.39 ? 154 GLY A C 1 ATOM 1103 O O . GLY A 1 136 ? 34.003 23.572 2.475 1.00 39.46 ? 154 GLY A O 1 ATOM 1104 N N . SER A 1 137 ? 34.665 21.598 3.324 1.00 39.34 ? 155 SER A N 1 ATOM 1105 C CA . SER A 1 137 ? 34.166 20.829 2.194 1.00 39.44 ? 155 SER A CA 1 ATOM 1106 C C . SER A 1 137 ? 32.833 20.179 2.532 1.00 38.91 ? 155 SER A C 1 ATOM 1107 O O . SER A 1 137 ? 32.104 19.713 1.661 1.00 38.02 ? 155 SER A O 1 ATOM 1108 C CB . SER A 1 137 ? 35.183 19.771 1.782 1.00 39.93 ? 155 SER A CB 1 ATOM 1109 O OG . SER A 1 137 ? 36.406 20.386 1.409 1.00 41.60 ? 155 SER A OG 1 ATOM 1110 N N . ALA A 1 138 ? 32.516 20.163 3.819 1.00 38.39 ? 156 ALA A N 1 ATOM 1111 C CA . ALA A 1 138 ? 31.204 19.675 4.265 1.00 38.01 ? 156 ALA A CA 1 ATOM 1112 C C . ALA A 1 138 ? 30.059 20.460 3.643 1.00 37.82 ? 156 ALA A C 1 ATOM 1113 O O . ALA A 1 138 ? 30.159 21.659 3.366 1.00 37.65 ? 156 ALA A O 1 ATOM 1114 C CB . ALA A 1 138 ? 31.097 19.701 5.774 1.00 37.72 ? 156 ALA A CB 1 ATOM 1115 N N . GLN A 1 139 ? 28.971 19.738 3.424 1.00 37.65 ? 157 GLN A N 1 ATOM 1116 C CA . GLN A 1 139 ? 27.716 20.306 2.943 1.00 37.89 ? 157 GLN A CA 1 ATOM 1117 C C . GLN A 1 139 ? 26.657 20.316 4.034 1.00 36.90 ? 157 GLN A C 1 ATOM 1118 O O . GLN A 1 139 ? 26.796 19.699 5.085 1.00 36.08 ? 157 GLN A O 1 ATOM 1119 C CB . GLN A 1 139 ? 27.167 19.465 1.794 1.00 38.64 ? 157 GLN A CB 1 ATOM 1120 C CG . GLN A 1 139 ? 28.149 19.231 0.642 1.00 41.68 ? 157 GLN A CG 1 ATOM 1121 C CD . GLN A 1 139 ? 28.587 20.529 0.006 1.00 47.24 ? 157 GLN A CD 1 ATOM 1122 O OE1 . GLN A 1 139 ? 29.785 20.845 -0.029 1.00 52.13 ? 157 GLN A OE1 1 ATOM 1123 N NE2 . GLN A 1 139 ? 27.617 21.319 -0.464 1.00 49.19 ? 157 GLN A NE2 1 ATOM 1124 N N . SER A 1 140 ? 25.563 20.979 3.715 1.00 36.49 ? 158 SER A N 1 ATOM 1125 C CA . SER A 1 140 ? 24.386 21.013 4.598 1.00 36.29 ? 158 SER A CA 1 ATOM 1126 C C . SER A 1 140 ? 23.719 19.640 4.674 1.00 36.48 ? 158 SER A C 1 ATOM 1127 O O . SER A 1 140 ? 23.801 18.818 3.748 1.00 35.85 ? 158 SER A O 1 ATOM 1128 C CB . SER A 1 140 ? 23.388 22.059 4.133 1.00 36.04 ? 158 SER A CB 1 ATOM 1129 O OG . SER A 1 140 ? 22.897 21.741 2.842 1.00 37.77 ? 158 SER A OG 1 ATOM 1130 N N . THR A 1 141 ? 23.079 19.405 5.803 1.00 35.88 ? 159 THR A N 1 ATOM 1131 C CA . THR A 1 141 ? 22.437 18.143 6.078 1.00 36.23 ? 159 THR A CA 1 ATOM 1132 C C . THR A 1 141 ? 21.116 18.343 6.813 1.00 37.14 ? 159 THR A C 1 ATOM 1133 O O . THR A 1 141 ? 20.986 19.205 7.692 1.00 35.88 ? 159 THR A O 1 ATOM 1134 C CB . THR A 1 141 ? 23.403 17.210 6.860 1.00 36.88 ? 159 THR A CB 1 ATOM 1135 O OG1 . THR A 1 141 ? 22.845 15.897 6.963 1.00 36.29 ? 159 THR A OG1 1 ATOM 1136 C CG2 . THR A 1 141 ? 23.699 17.757 8.258 1.00 36.41 ? 159 THR A CG2 1 ATOM 1137 N N . ALA A 1 142 ? 20.123 17.565 6.408 1.00 37.45 ? 160 ALA A N 1 ATOM 1138 C CA . ALA A 1 142 ? 18.770 17.716 6.945 1.00 38.20 ? 160 ALA A CA 1 ATOM 1139 C C . ALA A 1 142 ? 18.590 16.848 8.173 1.00 38.52 ? 160 ALA A C 1 ATOM 1140 O O . ALA A 1 142 ? 18.015 15.763 8.120 1.00 39.92 ? 160 ALA A O 1 ATOM 1141 C CB . ALA A 1 142 ? 17.721 17.384 5.879 1.00 38.13 ? 160 ALA A CB 1 ATOM 1142 N N . LEU A 1 143 ? 19.080 17.350 9.290 1.00 38.62 ? 161 LEU A N 1 ATOM 1143 C CA . LEU A 1 143 ? 19.089 16.593 10.541 1.00 38.63 ? 161 LEU A CA 1 ATOM 1144 C C . LEU A 1 143 ? 17.714 16.631 11.206 1.00 38.48 ? 161 LEU A C 1 ATOM 1145 O O . LEU A 1 143 ? 17.310 15.690 11.875 1.00 39.97 ? 161 LEU A O 1 ATOM 1146 C CB . LEU A 1 143 ? 20.152 17.137 11.490 1.00 38.82 ? 161 LEU A CB 1 ATOM 1147 C CG . LEU A 1 143 ? 20.403 16.356 12.770 1.00 39.24 ? 161 LEU A CG 1 ATOM 1148 C CD1 . LEU A 1 143 ? 21.003 14.972 12.438 1.00 39.70 ? 161 LEU A CD1 1 ATOM 1149 C CD2 . LEU A 1 143 ? 21.335 17.149 13.679 1.00 40.55 ? 161 LEU A CD2 1 ATOM 1150 N N . CYS A 1 144 ? 16.983 17.716 10.992 1.00 36.87 ? 162 CYS A N 1 ATOM 1151 C CA . CYS A 1 144 ? 15.690 17.887 11.643 1.00 35.94 ? 162 CYS A CA 1 ATOM 1152 C C . CYS A 1 144 ? 14.569 17.714 10.624 1.00 35.52 ? 162 CYS A C 1 ATOM 1153 O O . CYS A 1 144 ? 14.434 18.508 9.693 1.00 34.73 ? 162 CYS A O 1 ATOM 1154 C CB . CYS A 1 144 ? 15.648 19.261 12.344 1.00 35.69 ? 162 CYS A CB 1 ATOM 1155 S SG . CYS A 1 144 ? 14.084 19.699 13.118 1.00 34.67 ? 162 CYS A SG 1 ATOM 1156 N N . LYS A 1 145 ? 13.788 16.654 10.799 1.00 35.69 ? 163 LYS A N 1 ATOM 1157 C CA . LYS A 1 145 ? 12.691 16.318 9.856 1.00 36.13 ? 163 LYS A CA 1 ATOM 1158 C C . LYS A 1 145 ? 11.683 15.331 10.402 1.00 35.85 ? 163 LYS A C 1 ATOM 1159 O O . LYS A 1 145 ? 12.012 14.461 11.183 1.00 35.58 ? 163 LYS A O 1 ATOM 1160 C CB . LYS A 1 145 ? 13.235 15.776 8.529 1.00 36.55 ? 163 LYS A CB 1 ATOM 1161 C CG . LYS A 1 145 ? 14.075 14.520 8.643 1.00 38.58 ? 163 LYS A CG 1 ATOM 1162 C CD . LYS A 1 145 ? 14.800 14.232 7.310 1.00 41.66 ? 163 LYS A CD 1 ATOM 1163 C CE . LYS A 1 145 ? 15.753 13.042 7.402 1.00 44.24 ? 163 LYS A CE 1 ATOM 1164 N NZ . LYS A 1 145 ? 16.796 13.239 8.464 1.00 46.71 ? 163 LYS A NZ 1 ATOM 1165 N N . SER A 1 146 ? 10.450 15.511 9.969 1.00 36.12 ? 164 SER A N 1 ATOM 1166 C CA . SER A 1 146 ? 9.322 14.658 10.359 1.00 37.21 ? 164 SER A CA 1 ATOM 1167 C C . SER A 1 146 ? 8.273 14.649 9.262 1.00 37.61 ? 164 SER A C 1 ATOM 1168 O O . SER A 1 146 ? 7.653 15.665 8.955 1.00 36.93 ? 164 SER A O 1 ATOM 1169 C CB . SER A 1 146 ? 8.691 15.155 11.662 1.00 37.76 ? 164 SER A CB 1 ATOM 1170 O OG . SER A 1 146 ? 7.776 14.206 12.187 1.00 38.69 ? 164 SER A OG 1 ATOM 1171 N N . GLY A 1 147 ? 8.095 13.484 8.656 1.00 38.46 ? 165 GLY A N 1 ATOM 1172 C CA . GLY A 1 147 ? 7.167 13.354 7.537 1.00 38.59 ? 165 GLY A CA 1 ATOM 1173 C C . GLY A 1 147 ? 7.504 14.315 6.427 1.00 38.64 ? 165 GLY A C 1 ATOM 1174 O O . GLY A 1 147 ? 8.626 14.338 5.922 1.00 39.30 ? 165 GLY A O 1 ATOM 1175 N N . SER A 1 148 ? 6.529 15.141 6.078 1.00 38.70 ? 166 SER A N 1 ATOM 1176 C CA . SER A 1 148 ? 6.661 16.052 4.944 1.00 38.64 ? 166 SER A CA 1 ATOM 1177 C C . SER A 1 148 ? 7.333 17.335 5.374 1.00 37.74 ? 166 SER A C 1 ATOM 1178 O O . SER A 1 148 ? 7.652 18.196 4.560 1.00 39.16 ? 166 SER A O 1 ATOM 1179 C CB . SER A 1 148 ? 5.295 16.359 4.320 1.00 38.97 ? 166 SER A CB 1 ATOM 1180 O OG . SER A 1 148 ? 4.452 16.978 5.269 1.00 40.06 ? 166 SER A OG 1 ATOM 1181 N N . LEU A 1 149 ? 7.552 17.463 6.668 1.00 36.05 ? 167 LEU A N 1 ATOM 1182 C CA . LEU A 1 149 ? 8.219 18.654 7.172 1.00 34.57 ? 167 LEU A CA 1 ATOM 1183 C C . LEU A 1 149 ? 9.706 18.441 7.329 1.00 33.67 ? 167 LEU A C 1 ATOM 1184 O O . LEU A 1 149 ? 10.153 17.588 8.101 1.00 33.99 ? 167 LEU A O 1 ATOM 1185 C CB . LEU A 1 149 ? 7.602 19.125 8.486 1.00 34.36 ? 167 LEU A CB 1 ATOM 1186 C CG . LEU A 1 149 ? 6.272 19.864 8.352 1.00 34.53 ? 167 LEU A CG 1 ATOM 1187 C CD1 . LEU A 1 149 ? 5.619 20.002 9.724 1.00 35.28 ? 167 LEU A CD1 1 ATOM 1188 C CD2 . LEU A 1 149 ? 6.448 21.201 7.680 1.00 36.29 ? 167 LEU A CD2 1 ATOM 1189 N N . VAL A 1 150 ? 10.456 19.230 6.577 1.00 32.03 ? 168 VAL A N 1 ATOM 1190 C CA . VAL A 1 150 ? 11.908 19.211 6.613 1.00 31.37 ? 168 VAL A CA 1 ATOM 1191 C C . VAL A 1 150 ? 12.461 20.614 6.907 1.00 30.90 ? 168 VAL A C 1 ATOM 1192 O O . VAL A 1 150 ? 12.264 21.546 6.138 1.00 30.68 ? 168 VAL A O 1 ATOM 1193 C CB . VAL A 1 150 ? 12.499 18.713 5.276 1.00 31.31 ? 168 VAL A CB 1 ATOM 1194 C CG1 . VAL A 1 150 ? 14.000 18.634 5.367 1.00 30.27 ? 168 VAL A CG1 1 ATOM 1195 C CG2 . VAL A 1 150 ? 11.894 17.349 4.871 1.00 32.18 ? 168 VAL A CG2 1 ATOM 1196 N N . LEU A 1 151 ? 13.135 20.734 8.042 1.00 30.26 ? 169 LEU A N 1 ATOM 1197 C CA . LEU A 1 151 ? 13.739 21.997 8.465 1.00 29.49 ? 169 LEU A CA 1 ATOM 1198 C C . LEU A 1 151 ? 14.827 22.416 7.499 1.00 28.94 ? 169 LEU A C 1 ATOM 1199 O O . LEU A 1 151 ? 15.692 21.602 7.133 1.00 29.80 ? 169 LEU A O 1 ATOM 1200 C CB . LEU A 1 151 ? 14.371 21.875 9.850 1.00 29.43 ? 169 LEU A CB 1 ATOM 1201 C CG . LEU A 1 151 ? 14.542 23.223 10.540 1.00 29.25 ? 169 LEU A CG 1 ATOM 1202 C CD1 . LEU A 1 151 ? 13.225 23.686 11.184 1.00 29.68 ? 169 LEU A CD1 1 ATOM 1203 C CD2 . LEU A 1 151 ? 15.647 23.106 11.567 1.00 29.52 ? 169 LEU A CD2 1 ATOM 1204 N N . ASN A 1 152 ? 14.789 23.670 7.063 1.00 28.15 ? 170 ASN A N 1 ATOM 1205 C CA . ASN A 1 152 ? 15.902 24.201 6.264 1.00 27.55 ? 170 ASN A CA 1 ATOM 1206 C C . ASN A 1 152 ? 16.480 25.540 6.740 1.00 27.42 ? 170 ASN A C 1 ATOM 1207 O O . ASN A 1 152 ? 17.413 26.061 6.157 1.00 27.38 ? 170 ASN A O 1 ATOM 1208 C CB . ASN A 1 152 ? 15.570 24.227 4.766 1.00 27.96 ? 170 ASN A CB 1 ATOM 1209 C CG . ASN A 1 152 ? 14.591 25.285 4.402 1.00 27.85 ? 170 ASN A CG 1 ATOM 1210 O OD1 . ASN A 1 152 ? 13.925 25.853 5.271 1.00 27.69 ? 170 ASN A OD1 1 ATOM 1211 N ND2 . ASN A 1 152 ? 14.486 25.572 3.102 1.00 27.45 ? 170 ASN A ND2 1 ATOM 1212 N N . ASN A 1 153 ? 15.905 26.056 7.813 1.00 27.46 ? 171 ASN A N 1 ATOM 1213 C CA . ASN A 1 153 ? 16.366 27.281 8.464 1.00 26.99 ? 171 ASN A CA 1 ATOM 1214 C C . ASN A 1 153 ? 16.247 27.149 9.982 1.00 26.77 ? 171 ASN A C 1 ATOM 1215 O O . ASN A 1 153 ? 15.143 26.898 10.484 1.00 25.99 ? 171 ASN A O 1 ATOM 1216 C CB . ASN A 1 153 ? 15.505 28.458 7.971 1.00 26.45 ? 171 ASN A CB 1 ATOM 1217 C CG . ASN A 1 153 ? 15.962 29.804 8.526 1.00 27.00 ? 171 ASN A CG 1 ATOM 1218 O OD1 . ASN A 1 153 ? 17.167 30.019 8.769 1.00 24.97 ? 171 ASN A OD1 1 ATOM 1219 N ND2 . ASN A 1 153 ? 14.996 30.704 8.757 1.00 24.49 ? 171 ASN A ND2 1 ATOM 1220 N N . PRO A 1 154 ? 17.375 27.249 10.718 1.00 26.51 ? 172 PRO A N 1 ATOM 1221 C CA . PRO A 1 154 ? 18.741 27.348 10.183 1.00 26.85 ? 172 PRO A CA 1 ATOM 1222 C C . PRO A 1 154 ? 19.173 26.072 9.474 1.00 26.53 ? 172 PRO A C 1 ATOM 1223 O O . PRO A 1 154 ? 18.600 25.014 9.668 1.00 26.80 ? 172 PRO A O 1 ATOM 1224 C CB . PRO A 1 154 ? 19.594 27.529 11.446 1.00 26.72 ? 172 PRO A CB 1 ATOM 1225 C CG . PRO A 1 154 ? 18.839 26.809 12.505 1.00 27.20 ? 172 PRO A CG 1 ATOM 1226 C CD . PRO A 1 154 ? 17.377 27.117 12.182 1.00 26.90 ? 172 PRO A CD 1 ATOM 1227 N N . ALA A 1 155 ? 20.179 26.205 8.627 1.00 27.16 ? 173 ALA A N 1 ATOM 1228 C CA . ALA A 1 155 ? 20.863 25.043 8.038 1.00 27.81 ? 173 ALA A CA 1 ATOM 1229 C C . ALA A 1 155 ? 21.774 24.396 9.058 1.00 28.38 ? 173 ALA A C 1 ATOM 1230 O O . ALA A 1 155 ? 22.297 25.064 9.933 1.00 27.14 ? 173 ALA A O 1 ATOM 1231 C CB . ALA A 1 155 ? 21.679 25.483 6.794 1.00 28.13 ? 173 ALA A CB 1 ATOM 1232 N N . TYR A 1 156 ? 21.934 23.080 8.942 1.00 28.35 ? 174 TYR A N 1 ATOM 1233 C CA . TYR A 1 156 ? 22.976 22.355 9.637 1.00 28.86 ? 174 TYR A CA 1 ATOM 1234 C C . TYR A 1 156 ? 24.058 22.025 8.626 1.00 29.41 ? 174 TYR A C 1 ATOM 1235 O O . TYR A 1 156 ? 23.768 21.527 7.532 1.00 29.33 ? 174 TYR A O 1 ATOM 1236 C CB . TYR A 1 156 ? 22.499 20.998 10.184 1.00 29.06 ? 174 TYR A CB 1 ATOM 1237 C CG . TYR A 1 156 ? 21.369 21.008 11.168 1.00 29.13 ? 174 TYR A CG 1 ATOM 1238 C CD1 . TYR A 1 156 ? 21.618 21.100 12.530 1.00 30.37 ? 174 TYR A CD1 1 ATOM 1239 C CD2 . TYR A 1 156 ? 20.067 20.852 10.743 1.00 28.35 ? 174 TYR A CD2 1 ATOM 1240 C CE1 . TYR A 1 156 ? 20.578 21.080 13.454 1.00 30.17 ? 174 TYR A CE1 1 ATOM 1241 C CE2 . TYR A 1 156 ? 19.022 20.826 11.640 1.00 29.42 ? 174 TYR A CE2 1 ATOM 1242 C CZ . TYR A 1 156 ? 19.284 20.937 13.002 1.00 29.54 ? 174 TYR A CZ 1 ATOM 1243 O OH . TYR A 1 156 ? 18.243 20.924 13.900 1.00 28.74 ? 174 TYR A OH 1 ATOM 1244 N N . ILE A 1 157 ? 25.297 22.261 9.026 1.00 29.61 ? 175 ILE A N 1 ATOM 1245 C CA . ILE A 1 157 ? 26.473 21.865 8.217 1.00 30.07 ? 175 ILE A CA 1 ATOM 1246 C C . ILE A 1 157 ? 27.104 20.601 8.808 1.00 30.37 ? 175 ILE A C 1 ATOM 1247 O O . ILE A 1 157 ? 27.365 20.511 10.003 1.00 30.23 ? 175 ILE A O 1 ATOM 1248 C CB . ILE A 1 157 ? 27.515 23.011 8.118 1.00 30.30 ? 175 ILE A CB 1 ATOM 1249 C CG1 . ILE A 1 157 ? 26.815 24.348 7.777 1.00 30.72 ? 175 ILE A CG1 1 ATOM 1250 C CG2 . ILE A 1 157 ? 28.642 22.654 7.133 1.00 29.23 ? 175 ILE A CG2 1 ATOM 1251 C CD1 . ILE A 1 157 ? 26.004 24.335 6.462 1.00 29.66 ? 175 ILE A CD1 1 ATOM 1252 N N . ALA A 1 158 ? 27.327 19.616 7.946 1.00 31.13 ? 176 ALA A N 1 ATOM 1253 C CA . ALA A 1 158 ? 27.920 18.341 8.362 1.00 31.99 ? 176 ALA A CA 1 ATOM 1254 C C . ALA A 1 158 ? 29.345 18.543 8.812 1.00 32.99 ? 176 ALA A C 1 ATOM 1255 O O . ALA A 1 158 ? 29.983 19.521 8.480 1.00 33.36 ? 176 ALA A O 1 ATOM 1256 C CB . ALA A 1 158 ? 27.871 17.300 7.200 1.00 31.91 ? 176 ALA A CB 1 ATOM 1257 N N . ARG A 1 159 ? 29.822 17.578 9.581 1.00 34.61 ? 177 ARG A N 1 ATOM 1258 C CA . ARG A 1 159 ? 31.205 17.530 10.053 1.00 35.76 ? 177 ARG A CA 1 ATOM 1259 C C . ARG A 1 159 ? 32.179 17.323 8.910 1.00 36.45 ? 177 ARG A C 1 ATOM 1260 O O . ARG A 1 159 ? 31.877 16.623 7.958 1.00 35.88 ? 177 ARG A O 1 ATOM 1261 C CB . ARG A 1 159 ? 31.353 16.380 11.061 1.00 36.39 ? 177 ARG A CB 1 ATOM 1262 C CG . ARG A 1 159 ? 32.742 16.164 11.595 1.00 37.99 ? 177 ARG A CG 1 ATOM 1263 C CD . ARG A 1 159 ? 32.714 15.083 12.680 1.00 39.98 ? 177 ARG A CD 1 ATOM 1264 N NE . ARG A 1 159 ? 32.424 13.750 12.147 1.00 42.19 ? 177 ARG A NE 1 ATOM 1265 C CZ . ARG A 1 159 ? 32.170 12.689 12.908 1.00 42.78 ? 177 ARG A CZ 1 ATOM 1266 N NH1 . ARG A 1 159 ? 32.138 12.814 14.228 1.00 44.41 ? 177 ARG A NH1 1 ATOM 1267 N NH2 . ARG A 1 159 ? 31.940 11.509 12.359 1.00 42.98 ? 177 ARG A NH2 1 ATOM 1268 N N . GLU A 1 160 ? 33.341 17.949 8.992 1.00 37.63 ? 178 GLU A N 1 ATOM 1269 C CA . GLU A 1 160 ? 34.419 17.708 8.050 1.00 38.76 ? 178 GLU A CA 1 ATOM 1270 C C . GLU A 1 160 ? 35.015 16.296 8.178 1.00 40.38 ? 178 GLU A C 1 ATOM 1271 O O . GLU A 1 160 ? 34.925 15.674 9.207 1.00 39.65 ? 178 GLU A O 1 ATOM 1272 C CB . GLU A 1 160 ? 35.531 18.727 8.225 1.00 38.86 ? 178 GLU A CB 1 ATOM 1273 C CG . GLU A 1 160 ? 35.161 20.148 7.943 1.00 38.67 ? 178 GLU A CG 1 ATOM 1274 C CD . GLU A 1 160 ? 34.761 20.383 6.513 1.00 40.08 ? 178 GLU A CD 1 ATOM 1275 O OE1 . GLU A 1 160 ? 33.722 20.992 6.289 1.00 37.54 ? 178 GLU A OE1 1 ATOM 1276 O OE2 . GLU A 1 160 ? 35.496 19.970 5.605 1.00 37.26 ? 178 GLU A OE2 1 ATOM 1277 N N . ALA A 1 161 ? 35.637 15.820 7.112 1.00 42.51 ? 179 ALA A N 1 ATOM 1278 C CA . ALA A 1 161 ? 36.206 14.472 7.070 1.00 44.32 ? 179 ALA A CA 1 ATOM 1279 C C . ALA A 1 161 ? 37.120 14.182 8.234 1.00 45.57 ? 179 ALA A C 1 ATOM 1280 O O . ALA A 1 161 ? 37.053 13.143 8.829 1.00 47.91 ? 179 ALA A O 1 ATOM 1281 C CB . ALA A 1 161 ? 36.958 14.269 5.794 1.00 44.28 ? 179 ALA A CB 1 ATOM 1282 N N . ASN A 1 162 ? 37.987 15.130 8.533 1.00 45.87 ? 180 ASN A N 1 ATOM 1283 C CA . ASN A 1 162 ? 39.092 14.948 9.438 1.00 45.95 ? 180 ASN A CA 1 ATOM 1284 C C . ASN A 1 162 ? 38.705 14.807 10.888 1.00 45.53 ? 180 ASN A C 1 ATOM 1285 O O . ASN A 1 162 ? 39.533 14.439 11.703 1.00 45.96 ? 180 ASN A O 1 ATOM 1286 C CB . ASN A 1 162 ? 40.001 16.144 9.330 1.00 46.23 ? 180 ASN A CB 1 ATOM 1287 C CG . ASN A 1 162 ? 39.273 17.360 8.828 1.00 48.25 ? 180 ASN A CG 1 ATOM 1288 O OD1 . ASN A 1 162 ? 39.339 18.425 9.408 1.00 50.42 ? 180 ASN A OD1 1 ATOM 1289 N ND2 . ASN A 1 162 ? 38.577 17.199 7.728 1.00 48.26 ? 180 ASN A ND2 1 ATOM 1290 N N . PHE A 1 163 ? 37.465 15.140 11.223 1.00 44.20 ? 181 PHE A N 1 ATOM 1291 C CA . PHE A 1 163 ? 37.068 15.164 12.612 1.00 43.29 ? 181 PHE A CA 1 ATOM 1292 C C . PHE A 1 163 ? 36.406 13.860 12.965 1.00 42.22 ? 181 PHE A C 1 ATOM 1293 O O . PHE A 1 163 ? 35.625 13.357 12.221 1.00 42.07 ? 181 PHE A O 1 ATOM 1294 C CB . PHE A 1 163 ? 36.117 16.339 12.906 1.00 43.26 ? 181 PHE A CB 1 ATOM 1295 C CG . PHE A 1 163 ? 36.747 17.687 12.793 1.00 43.84 ? 181 PHE A CG 1 ATOM 1296 C CD1 . PHE A 1 163 ? 37.836 18.016 13.538 1.00 44.96 ? 181 PHE A CD1 1 ATOM 1297 C CD2 . PHE A 1 163 ? 36.218 18.643 11.952 1.00 44.68 ? 181 PHE A CD2 1 ATOM 1298 C CE1 . PHE A 1 163 ? 38.396 19.236 13.428 1.00 45.36 ? 181 PHE A CE1 1 ATOM 1299 C CE2 . PHE A 1 163 ? 36.777 19.874 11.852 1.00 43.88 ? 181 PHE A CE2 1 ATOM 1300 C CZ . PHE A 1 163 ? 37.860 20.176 12.585 1.00 45.11 ? 181 PHE A CZ 1 ATOM 1301 N N . GLY A 1 164 ? 36.725 13.334 14.129 1.00 41.19 ? 182 GLY A N 1 ATOM 1302 C CA . GLY A 1 164 ? 36.203 12.046 14.579 1.00 40.39 ? 182 GLY A CA 1 ATOM 1303 C C . GLY A 1 164 ? 35.196 12.166 15.695 1.00 39.93 ? 182 GLY A C 1 ATOM 1304 O O . GLY A 1 164 ? 34.620 11.179 16.158 1.00 39.33 ? 182 GLY A O 1 ATOM 1305 N N . ASP A 1 165 ? 34.980 13.400 16.123 1.00 38.85 ? 183 ASP A N 1 ATOM 1306 C CA . ASP A 1 165 ? 33.955 13.679 17.117 1.00 38.45 ? 183 ASP A CA 1 ATOM 1307 C C . ASP A 1 165 ? 33.279 15.020 16.820 1.00 37.27 ? 183 ASP A C 1 ATOM 1308 O O . ASP A 1 165 ? 33.482 15.595 15.753 1.00 36.18 ? 183 ASP A O 1 ATOM 1309 C CB . ASP A 1 165 ? 34.534 13.647 18.534 1.00 38.24 ? 183 ASP A CB 1 ATOM 1310 C CG . ASP A 1 165 ? 35.588 14.710 18.762 1.00 39.89 ? 183 ASP A CG 1 ATOM 1311 O OD1 . ASP A 1 165 ? 35.396 15.863 18.300 1.00 39.03 ? 183 ASP A OD1 1 ATOM 1312 O OD2 . ASP A 1 165 ? 36.606 14.401 19.425 1.00 41.01 ? 183 ASP A OD2 1 ATOM 1313 N N . TYR A 1 166 ? 32.475 15.494 17.766 1.00 37.12 ? 184 TYR A N 1 ATOM 1314 C CA . TYR A 1 166 ? 31.701 16.749 17.573 1.00 36.58 ? 184 TYR A CA 1 ATOM 1315 C C . TYR A 1 166 ? 32.128 17.853 18.531 1.00 36.83 ? 184 TYR A C 1 ATOM 1316 O O . TYR A 1 166 ? 31.369 18.779 18.827 1.00 36.27 ? 184 TYR A O 1 ATOM 1317 C CB . TYR A 1 166 ? 30.196 16.482 17.664 1.00 36.54 ? 184 TYR A CB 1 ATOM 1318 C CG . TYR A 1 166 ? 29.678 15.828 16.402 1.00 36.33 ? 184 TYR A CG 1 ATOM 1319 C CD1 . TYR A 1 166 ? 29.566 16.555 15.224 1.00 35.43 ? 184 TYR A CD1 1 ATOM 1320 C CD2 . TYR A 1 166 ? 29.365 14.473 16.367 1.00 37.27 ? 184 TYR A CD2 1 ATOM 1321 C CE1 . TYR A 1 166 ? 29.130 15.973 14.064 1.00 35.38 ? 184 TYR A CE1 1 ATOM 1322 C CE2 . TYR A 1 166 ? 28.922 13.876 15.204 1.00 36.36 ? 184 TYR A CE2 1 ATOM 1323 C CZ . TYR A 1 166 ? 28.802 14.639 14.053 1.00 36.95 ? 184 TYR A CZ 1 ATOM 1324 O OH . TYR A 1 166 ? 28.365 14.062 12.878 1.00 38.11 ? 184 TYR A OH 1 ATOM 1325 N N . TYR A 1 167 ? 33.374 17.767 18.975 1.00 37.12 ? 185 TYR A N 1 ATOM 1326 C CA . TYR A 1 167 ? 33.915 18.750 19.919 1.00 37.76 ? 185 TYR A CA 1 ATOM 1327 C C . TYR A 1 167 ? 34.628 19.912 19.225 1.00 37.82 ? 185 TYR A C 1 ATOM 1328 O O . TYR A 1 167 ? 35.326 20.723 19.852 1.00 39.87 ? 185 TYR A O 1 ATOM 1329 C CB . TYR A 1 167 ? 34.853 18.072 20.917 1.00 38.30 ? 185 TYR A CB 1 ATOM 1330 C CG . TYR A 1 167 ? 34.131 17.160 21.876 1.00 39.02 ? 185 TYR A CG 1 ATOM 1331 C CD1 . TYR A 1 167 ? 33.203 17.666 22.772 1.00 40.62 ? 185 TYR A CD1 1 ATOM 1332 C CD2 . TYR A 1 167 ? 34.377 15.795 21.883 1.00 41.64 ? 185 TYR A CD2 1 ATOM 1333 C CE1 . TYR A 1 167 ? 32.535 16.832 23.655 1.00 42.58 ? 185 TYR A CE1 1 ATOM 1334 C CE2 . TYR A 1 167 ? 33.717 14.953 22.753 1.00 42.57 ? 185 TYR A CE2 1 ATOM 1335 C CZ . TYR A 1 167 ? 32.802 15.474 23.642 1.00 43.93 ? 185 TYR A CZ 1 ATOM 1336 O OH . TYR A 1 167 ? 32.149 14.634 24.508 1.00 44.47 ? 185 TYR A OH 1 ATOM 1337 N N . TYR A 1 168 ? 34.420 20.005 17.931 1.00 36.13 ? 186 TYR A N 1 ATOM 1338 C CA . TYR A 1 168 ? 35.156 20.948 17.095 1.00 34.97 ? 186 TYR A CA 1 ATOM 1339 C C . TYR A 1 168 ? 34.497 22.335 17.067 1.00 34.27 ? 186 TYR A C 1 ATOM 1340 O O . TYR A 1 168 ? 33.324 22.505 17.422 1.00 33.12 ? 186 TYR A O 1 ATOM 1341 C CB . TYR A 1 168 ? 35.312 20.404 15.668 1.00 34.61 ? 186 TYR A CB 1 ATOM 1342 C CG . TYR A 1 168 ? 34.002 20.052 14.983 1.00 34.21 ? 186 TYR A CG 1 ATOM 1343 C CD1 . TYR A 1 168 ? 33.204 21.039 14.421 1.00 33.34 ? 186 TYR A CD1 1 ATOM 1344 C CD2 . TYR A 1 168 ? 33.565 18.727 14.902 1.00 34.07 ? 186 TYR A CD2 1 ATOM 1345 C CE1 . TYR A 1 168 ? 32.007 20.722 13.798 1.00 32.49 ? 186 TYR A CE1 1 ATOM 1346 C CE2 . TYR A 1 168 ? 32.365 18.396 14.280 1.00 32.46 ? 186 TYR A CE2 1 ATOM 1347 C CZ . TYR A 1 168 ? 31.596 19.396 13.729 1.00 32.24 ? 186 TYR A CZ 1 ATOM 1348 O OH . TYR A 1 168 ? 30.425 19.068 13.105 1.00 31.55 ? 186 TYR A OH 1 ATOM 1349 N N . LYS A 1 169 ? 35.302 23.300 16.646 1.00 33.25 ? 187 LYS A N 1 ATOM 1350 C CA . LYS A 1 169 ? 34.873 24.670 16.411 1.00 32.96 ? 187 LYS A CA 1 ATOM 1351 C C . LYS A 1 169 ? 35.004 24.995 14.931 1.00 32.21 ? 187 LYS A C 1 ATOM 1352 O O . LYS A 1 169 ? 36.080 24.882 14.338 1.00 32.01 ? 187 LYS A O 1 ATOM 1353 C CB . LYS A 1 169 ? 35.722 25.645 17.235 1.00 33.54 ? 187 LYS A CB 1 ATOM 1354 C CG . LYS A 1 169 ? 35.334 27.119 17.057 1.00 34.57 ? 187 LYS A CG 1 ATOM 1355 C CD . LYS A 1 169 ? 36.214 28.041 17.900 1.00 37.36 ? 187 LYS A CD 1 ATOM 1356 C CE . LYS A 1 169 ? 35.939 29.500 17.551 1.00 39.85 ? 187 LYS A CE 1 ATOM 1357 N NZ . LYS A 1 169 ? 36.564 30.493 18.480 1.00 43.41 ? 187 LYS A NZ 1 ATOM 1358 N N . VAL A 1 170 ? 33.889 25.376 14.328 1.00 30.76 ? 188 VAL A N 1 ATOM 1359 C CA . VAL A 1 170 ? 33.885 25.829 12.944 1.00 30.00 ? 188 VAL A CA 1 ATOM 1360 C C . VAL A 1 170 ? 32.962 27.037 12.779 1.00 30.23 ? 188 VAL A C 1 ATOM 1361 O O . VAL A 1 170 ? 32.110 27.314 13.652 1.00 29.77 ? 188 VAL A O 1 ATOM 1362 C CB . VAL A 1 170 ? 33.419 24.716 11.986 1.00 30.28 ? 188 VAL A CB 1 ATOM 1363 C CG1 . VAL A 1 170 ? 34.463 23.598 11.939 1.00 30.04 ? 188 VAL A CG1 1 ATOM 1364 C CG2 . VAL A 1 170 ? 32.022 24.169 12.388 1.00 29.41 ? 188 VAL A CG2 1 ATOM 1365 N N . GLU A 1 171 ? 33.124 27.745 11.675 1.00 29.56 ? 189 GLU A N 1 ATOM 1366 C CA . GLU A 1 171 ? 32.309 28.955 11.438 1.00 30.13 ? 189 GLU A CA 1 ATOM 1367 C C . GLU A 1 171 ? 31.899 29.153 9.991 1.00 30.04 ? 189 GLU A C 1 ATOM 1368 O O . GLU A 1 171 ? 32.484 28.581 9.068 1.00 28.51 ? 189 GLU A O 1 ATOM 1369 C CB . GLU A 1 171 ? 33.051 30.192 11.942 1.00 30.71 ? 189 GLU A CB 1 ATOM 1370 C CG . GLU A 1 171 ? 34.209 30.609 11.088 1.00 34.60 ? 189 GLU A CG 1 ATOM 1371 C CD . GLU A 1 171 ? 35.114 31.598 11.813 1.00 40.01 ? 189 GLU A CD 1 ATOM 1372 O OE1 . GLU A 1 171 ? 35.135 31.563 13.063 1.00 41.92 ? 189 GLU A OE1 1 ATOM 1373 O OE2 . GLU A 1 171 ? 35.796 32.405 11.130 1.00 42.45 ? 189 GLU A OE2 1 ATOM 1374 N N . ALA A 1 172 ? 30.835 29.932 9.829 1.00 29.61 ? 190 ALA A N 1 ATOM 1375 C CA . ALA A 1 172 ? 30.379 30.448 8.523 1.00 28.83 ? 190 ALA A CA 1 ATOM 1376 C C . ALA A 1 172 ? 30.117 31.935 8.624 1.00 28.51 ? 190 ALA A C 1 ATOM 1377 O O . ALA A 1 172 ? 29.880 32.460 9.711 1.00 28.58 ? 190 ALA A O 1 ATOM 1378 C CB . ALA A 1 172 ? 29.144 29.742 8.067 1.00 28.82 ? 190 ALA A CB 1 ATOM 1379 N N . ASP A 1 173 ? 30.152 32.597 7.476 1.00 27.75 ? 191 ASP A N 1 ATOM 1380 C CA . ASP A 1 173 ? 29.821 34.004 7.372 1.00 27.14 ? 191 ASP A CA 1 ATOM 1381 C C . ASP A 1 173 ? 28.446 34.123 6.730 1.00 26.87 ? 191 ASP A C 1 ATOM 1382 O O . ASP A 1 173 ? 28.197 33.516 5.694 1.00 26.68 ? 191 ASP A O 1 ATOM 1383 C CB . ASP A 1 173 ? 30.868 34.734 6.528 1.00 27.55 ? 191 ASP A CB 1 ATOM 1384 C CG . ASP A 1 173 ? 30.686 36.238 6.537 1.00 28.51 ? 191 ASP A CG 1 ATOM 1385 O OD1 . ASP A 1 173 ? 29.544 36.738 6.299 1.00 27.34 ? 191 ASP A OD1 1 ATOM 1386 O OD2 . ASP A 1 173 ? 31.698 36.945 6.780 1.00 29.44 ? 191 ASP A OD2 1 ATOM 1387 N N . PHE A 1 174 ? 27.558 34.859 7.391 1.00 26.02 ? 192 PHE A N 1 ATOM 1388 C CA . PHE A 1 174 ? 26.239 35.214 6.833 1.00 25.69 ? 192 PHE A CA 1 ATOM 1389 C C . PHE A 1 174 ? 26.026 36.714 6.824 1.00 25.83 ? 192 PHE A C 1 ATOM 1390 O O . PHE A 1 174 ? 26.490 37.430 7.710 1.00 26.26 ? 192 PHE A O 1 ATOM 1391 C CB . PHE A 1 174 ? 25.093 34.437 7.509 1.00 25.82 ? 192 PHE A CB 1 ATOM 1392 C CG . PHE A 1 174 ? 24.757 34.868 8.930 1.00 24.60 ? 192 PHE A CG 1 ATOM 1393 C CD1 . PHE A 1 174 ? 23.785 35.795 9.158 1.00 27.07 ? 192 PHE A CD1 1 ATOM 1394 C CD2 . PHE A 1 174 ? 25.357 34.259 10.034 1.00 23.91 ? 192 PHE A CD2 1 ATOM 1395 C CE1 . PHE A 1 174 ? 23.422 36.160 10.477 1.00 26.00 ? 192 PHE A CE1 1 ATOM 1396 C CE2 . PHE A 1 174 ? 25.009 34.601 11.331 1.00 25.79 ? 192 PHE A CE2 1 ATOM 1397 C CZ . PHE A 1 174 ? 24.040 35.547 11.556 1.00 25.53 ? 192 PHE A CZ 1 ATOM 1398 N N . TYR A 1 175 ? 25.395 37.192 5.758 1.00 25.95 ? 193 TYR A N 1 ATOM 1399 C CA . TYR A 1 175 ? 25.289 38.624 5.493 1.00 25.80 ? 193 TYR A CA 1 ATOM 1400 C C . TYR A 1 175 ? 23.847 39.059 5.351 1.00 26.35 ? 193 TYR A C 1 ATOM 1401 O O . TYR A 1 175 ? 23.091 38.509 4.568 1.00 25.98 ? 193 TYR A O 1 ATOM 1402 C CB . TYR A 1 175 ? 26.059 38.997 4.225 1.00 25.57 ? 193 TYR A CB 1 ATOM 1403 C CG . TYR A 1 175 ? 26.002 40.428 3.862 1.00 26.14 ? 193 TYR A CG 1 ATOM 1404 C CD1 . TYR A 1 175 ? 26.490 41.399 4.727 1.00 27.83 ? 193 TYR A CD1 1 ATOM 1405 C CD2 . TYR A 1 175 ? 25.474 40.845 2.647 1.00 25.67 ? 193 TYR A CD2 1 ATOM 1406 C CE1 . TYR A 1 175 ? 26.437 42.731 4.409 1.00 29.35 ? 193 TYR A CE1 1 ATOM 1407 C CE2 . TYR A 1 175 ? 25.422 42.191 2.317 1.00 27.99 ? 193 TYR A CE2 1 ATOM 1408 C CZ . TYR A 1 175 ? 25.901 43.133 3.209 1.00 29.03 ? 193 TYR A CZ 1 ATOM 1409 O OH . TYR A 1 175 ? 25.864 44.486 2.921 1.00 31.13 ? 193 TYR A OH 1 ATOM 1410 N N . LEU A 1 176 ? 23.471 40.024 6.164 1.00 26.67 ? 194 LEU A N 1 ATOM 1411 C CA . LEU A 1 176 ? 22.113 40.575 6.142 1.00 26.76 ? 194 LEU A CA 1 ATOM 1412 C C . LEU A 1 176 ? 22.095 41.945 5.473 1.00 26.92 ? 194 LEU A C 1 ATOM 1413 O O . LEU A 1 176 ? 22.709 42.912 5.931 1.00 27.32 ? 194 LEU A O 1 ATOM 1414 C CB . LEU A 1 176 ? 21.548 40.674 7.572 1.00 26.88 ? 194 LEU A CB 1 ATOM 1415 C CG . LEU A 1 176 ? 21.536 39.401 8.440 1.00 27.16 ? 194 LEU A CG 1 ATOM 1416 C CD1 . LEU A 1 176 ? 20.899 39.714 9.824 1.00 25.76 ? 194 LEU A CD1 1 ATOM 1417 C CD2 . LEU A 1 176 ? 20.801 38.273 7.731 1.00 27.00 ? 194 LEU A CD2 1 ATOM 1418 N N . SER A 1 177 ? 21.330 42.031 4.404 1.00 27.80 ? 195 SER A N 1 ATOM 1419 C CA . SER A 1 177 ? 21.179 43.284 3.657 1.00 28.50 ? 195 SER A CA 1 ATOM 1420 C C . SER A 1 177 ? 19.791 43.384 3.035 1.00 28.96 ? 195 SER A C 1 ATOM 1421 O O . SER A 1 177 ? 19.106 42.375 2.826 1.00 30.24 ? 195 SER A O 1 ATOM 1422 C CB . SER A 1 177 ? 22.230 43.367 2.542 1.00 29.39 ? 195 SER A CB 1 ATOM 1423 O OG . SER A 1 177 ? 21.980 42.363 1.566 1.00 29.14 ? 195 SER A OG 1 ATOM 1424 N N . GLY A 1 178 ? 19.381 44.608 2.769 1.00 29.67 ? 196 GLY A N 1 ATOM 1425 C CA . GLY A 1 178 ? 18.136 44.868 2.044 1.00 30.19 ? 196 GLY A CA 1 ATOM 1426 C C . GLY A 1 178 ? 16.940 45.251 2.901 1.00 30.71 ? 196 GLY A C 1 ATOM 1427 O O . GLY A 1 178 ? 15.873 45.599 2.356 1.00 31.32 ? 196 GLY A O 1 ATOM 1428 N N . CYS A 1 179 ? 17.119 45.210 4.222 1.00 30.31 ? 197 CYS A N 1 ATOM 1429 C CA . CYS A 1 179 ? 16.013 45.436 5.193 1.00 29.35 ? 197 CYS A CA 1 ATOM 1430 C C . CYS A 1 179 ? 16.446 46.337 6.339 1.00 29.65 ? 197 CYS A C 1 ATOM 1431 O O . CYS A 1 179 ? 17.622 46.436 6.660 1.00 27.81 ? 197 CYS A O 1 ATOM 1432 C CB . CYS A 1 179 ? 15.544 44.081 5.792 1.00 29.76 ? 197 CYS A CB 1 ATOM 1433 S SG . CYS A 1 179 ? 15.377 42.723 4.557 1.00 34.06 ? 197 CYS A SG 1 ATOM 1434 N N . ASP A 1 180 ? 15.483 46.963 7.002 1.00 28.79 ? 198 ASP A N 1 ATOM 1435 C CA . ASP A 1 180 ? 15.811 47.746 8.194 1.00 29.52 ? 198 ASP A CA 1 ATOM 1436 C C . ASP A 1 180 ? 16.213 46.825 9.348 1.00 28.48 ? 198 ASP A C 1 ATOM 1437 O O . ASP A 1 180 ? 17.161 47.099 10.109 1.00 28.21 ? 198 ASP A O 1 ATOM 1438 C CB . ASP A 1 180 ? 14.643 48.622 8.629 1.00 30.17 ? 198 ASP A CB 1 ATOM 1439 C CG . ASP A 1 180 ? 14.378 49.769 7.673 1.00 33.00 ? 198 ASP A CG 1 ATOM 1440 O OD1 . ASP A 1 180 ? 15.342 50.309 7.089 1.00 34.78 ? 198 ASP A OD1 1 ATOM 1441 O OD2 . ASP A 1 180 ? 13.200 50.112 7.459 1.00 35.66 ? 198 ASP A OD2 1 ATOM 1442 N N . GLU A 1 181 ? 15.459 45.742 9.481 1.00 27.47 ? 199 GLU A N 1 ATOM 1443 C CA . GLU A 1 181 ? 15.713 44.720 10.489 1.00 28.02 ? 199 GLU A CA 1 ATOM 1444 C C . GLU A 1 181 ? 15.337 43.372 9.946 1.00 26.71 ? 199 GLU A C 1 ATOM 1445 O O . GLU A 1 181 ? 14.564 43.252 9.001 1.00 26.50 ? 199 GLU A O 1 ATOM 1446 C CB . GLU A 1 181 ? 14.924 44.954 11.783 1.00 29.27 ? 199 GLU A CB 1 ATOM 1447 C CG . GLU A 1 181 ? 15.103 46.293 12.373 1.00 36.11 ? 199 GLU A CG 1 ATOM 1448 C CD . GLU A 1 181 ? 15.971 46.268 13.555 1.00 44.02 ? 199 GLU A CD 1 ATOM 1449 O OE1 . GLU A 1 181 ? 17.130 45.890 13.386 1.00 50.03 ? 199 GLU A OE1 1 ATOM 1450 O OE2 . GLU A 1 181 ? 15.489 46.612 14.669 1.00 49.75 ? 199 GLU A OE2 1 ATOM 1451 N N . TYR A 1 182 ? 15.866 42.369 10.619 1.00 25.28 ? 200 TYR A N 1 ATOM 1452 C CA . TYR A 1 182 ? 15.741 40.975 10.213 1.00 25.13 ? 200 TYR A CA 1 ATOM 1453 C C . TYR A 1 182 ? 15.392 40.102 11.399 1.00 25.08 ? 200 TYR A C 1 ATOM 1454 O O . TYR A 1 182 ? 15.984 40.252 12.471 1.00 24.82 ? 200 TYR A O 1 ATOM 1455 C CB . TYR A 1 182 ? 17.066 40.471 9.627 1.00 25.14 ? 200 TYR A CB 1 ATOM 1456 C CG . TYR A 1 182 ? 17.699 41.391 8.588 1.00 26.27 ? 200 TYR A CG 1 ATOM 1457 C CD1 . TYR A 1 182 ? 17.646 41.083 7.213 1.00 28.63 ? 200 TYR A CD1 1 ATOM 1458 C CD2 . TYR A 1 182 ? 18.295 42.574 8.958 1.00 25.66 ? 200 TYR A CD2 1 ATOM 1459 C CE1 . TYR A 1 182 ? 18.186 41.955 6.242 1.00 27.36 ? 200 TYR A CE1 1 ATOM 1460 C CE2 . TYR A 1 182 ? 18.836 43.445 7.995 1.00 26.53 ? 200 TYR A CE2 1 ATOM 1461 C CZ . TYR A 1 182 ? 18.790 43.121 6.650 1.00 27.51 ? 200 TYR A CZ 1 ATOM 1462 O OH . TYR A 1 182 ? 19.347 44.010 5.740 1.00 26.32 ? 200 TYR A OH 1 ATOM 1463 N N . ILE A 1 183 ? 14.428 39.201 11.217 1.00 24.80 ? 201 ILE A N 1 ATOM 1464 C CA . ILE A 1 183 ? 14.186 38.144 12.227 1.00 24.94 ? 201 ILE A CA 1 ATOM 1465 C C . ILE A 1 183 ? 14.875 36.886 11.743 1.00 25.43 ? 201 ILE A C 1 ATOM 1466 O O . ILE A 1 183 ? 14.560 36.353 10.667 1.00 23.79 ? 201 ILE A O 1 ATOM 1467 C CB . ILE A 1 183 ? 12.680 37.891 12.507 1.00 25.03 ? 201 ILE A CB 1 ATOM 1468 C CG1 . ILE A 1 183 ? 11.960 39.196 12.849 1.00 26.92 ? 201 ILE A CG1 1 ATOM 1469 C CG2 . ILE A 1 183 ? 12.510 36.854 13.608 1.00 25.15 ? 201 ILE A CG2 1 ATOM 1470 C CD1 . ILE A 1 183 ? 10.429 39.042 13.012 1.00 27.80 ? 201 ILE A CD1 1 ATOM 1471 N N . VAL A 1 184 ? 15.833 36.403 12.538 1.00 25.82 ? 202 VAL A N 1 ATOM 1472 C CA . VAL A 1 184 ? 16.548 35.163 12.190 1.00 25.95 ? 202 VAL A CA 1 ATOM 1473 C C . VAL A 1 184 ? 16.533 34.209 13.383 1.00 25.58 ? 202 VAL A C 1 ATOM 1474 O O . VAL A 1 184 ? 16.488 34.678 14.532 1.00 25.69 ? 202 VAL A O 1 ATOM 1475 C CB . VAL A 1 184 ? 18.027 35.363 11.742 1.00 27.41 ? 202 VAL A CB 1 ATOM 1476 C CG1 . VAL A 1 184 ? 18.119 36.164 10.392 1.00 28.97 ? 202 VAL A CG1 1 ATOM 1477 C CG2 . VAL A 1 184 ? 18.859 36.027 12.833 1.00 27.31 ? 202 VAL A CG2 1 ATOM 1478 N N . PRO A 1 185 ? 16.627 32.892 13.119 1.00 25.29 ? 203 PRO A N 1 ATOM 1479 C CA . PRO A 1 185 ? 16.646 31.963 14.245 1.00 25.52 ? 203 PRO A CA 1 ATOM 1480 C C . PRO A 1 185 ? 18.057 31.659 14.686 1.00 25.64 ? 203 PRO A C 1 ATOM 1481 O O . PRO A 1 185 ? 18.933 31.467 13.841 1.00 25.21 ? 203 PRO A O 1 ATOM 1482 C CB . PRO A 1 185 ? 16.063 30.691 13.644 1.00 25.79 ? 203 PRO A CB 1 ATOM 1483 C CG . PRO A 1 185 ? 16.521 30.708 12.221 1.00 25.75 ? 203 PRO A CG 1 ATOM 1484 C CD . PRO A 1 185 ? 16.707 32.164 11.832 1.00 25.51 ? 203 PRO A CD 1 ATOM 1485 N N . LEU A 1 186 ? 18.218 31.578 15.996 1.00 25.44 ? 204 LEU A N 1 ATOM 1486 C CA . LEU A 1 186 ? 19.414 31.051 16.657 1.00 25.52 ? 204 LEU A CA 1 ATOM 1487 C C . LEU A 1 186 ? 18.933 29.879 17.518 1.00 26.46 ? 204 LEU A C 1 ATOM 1488 O O . LEU A 1 186 ? 18.105 30.058 18.415 1.00 25.90 ? 204 LEU A O 1 ATOM 1489 C CB . LEU A 1 186 ? 20.093 32.106 17.528 1.00 26.22 ? 204 LEU A CB 1 ATOM 1490 C CG . LEU A 1 186 ? 21.250 31.608 18.414 1.00 26.01 ? 204 LEU A CG 1 ATOM 1491 C CD1 . LEU A 1 186 ? 22.436 31.034 17.601 1.00 25.49 ? 204 LEU A CD1 1 ATOM 1492 C CD2 . LEU A 1 186 ? 21.703 32.771 19.354 1.00 26.31 ? 204 LEU A CD2 1 ATOM 1493 N N . CYS A 1 187 ? 19.388 28.677 17.172 1.00 26.61 ? 205 CYS A N 1 ATOM 1494 C CA . CYS A 1 187 ? 18.853 27.446 17.760 1.00 26.33 ? 205 CYS A CA 1 ATOM 1495 C C . CYS A 1 187 ? 19.957 26.473 18.159 1.00 26.77 ? 205 CYS A C 1 ATOM 1496 O O . CYS A 1 187 ? 21.045 26.445 17.583 1.00 26.83 ? 205 CYS A O 1 ATOM 1497 C CB . CYS A 1 187 ? 17.932 26.695 16.782 1.00 27.14 ? 205 CYS A CB 1 ATOM 1498 S SG . CYS A 1 187 ? 16.749 27.703 15.854 1.00 29.02 ? 205 CYS A SG 1 ATOM 1499 N N . ILE A 1 188 ? 19.615 25.650 19.131 1.00 25.85 ? 206 ILE A N 1 ATOM 1500 C CA . ILE A 1 188 ? 20.448 24.499 19.540 1.00 26.37 ? 206 ILE A CA 1 ATOM 1501 C C . ILE A 1 188 ? 19.589 23.326 19.986 1.00 26.60 ? 206 ILE A C 1 ATOM 1502 O O . ILE A 1 188 ? 18.453 23.495 20.434 1.00 27.25 ? 206 ILE A O 1 ATOM 1503 C CB . ILE A 1 188 ? 21.399 24.870 20.714 1.00 26.22 ? 206 ILE A CB 1 ATOM 1504 C CG1 . ILE A 1 188 ? 20.606 25.480 21.891 1.00 27.07 ? 206 ILE A CG1 1 ATOM 1505 C CG2 . ILE A 1 188 ? 22.494 25.840 20.252 1.00 27.63 ? 206 ILE A CG2 1 ATOM 1506 C CD1 . ILE A 1 188 ? 21.352 25.351 23.252 1.00 29.28 ? 206 ILE A CD1 1 ATOM 1507 N N . PHE A 1 189 ? 20.169 22.134 19.919 1.00 27.40 ? 207 PHE A N 1 ATOM 1508 C CA . PHE A 1 189 ? 19.608 21.007 20.647 1.00 27.28 ? 207 PHE A CA 1 ATOM 1509 C C . PHE A 1 189 ? 19.917 21.237 22.120 1.00 28.00 ? 207 PHE A C 1 ATOM 1510 O O . PHE A 1 189 ? 21.065 21.300 22.509 1.00 28.64 ? 207 PHE A O 1 ATOM 1511 C CB . PHE A 1 189 ? 20.179 19.689 20.137 1.00 27.73 ? 207 PHE A CB 1 ATOM 1512 C CG . PHE A 1 189 ? 19.586 19.270 18.838 1.00 27.58 ? 207 PHE A CG 1 ATOM 1513 C CD1 . PHE A 1 189 ? 18.300 18.763 18.797 1.00 30.20 ? 207 PHE A CD1 1 ATOM 1514 C CD2 . PHE A 1 189 ? 20.293 19.399 17.664 1.00 27.76 ? 207 PHE A CD2 1 ATOM 1515 C CE1 . PHE A 1 189 ? 17.721 18.370 17.572 1.00 30.38 ? 207 PHE A CE1 1 ATOM 1516 C CE2 . PHE A 1 189 ? 19.739 19.015 16.462 1.00 29.36 ? 207 PHE A CE2 1 ATOM 1517 C CZ . PHE A 1 189 ? 18.447 18.508 16.414 1.00 30.67 ? 207 PHE A CZ 1 ATOM 1518 N N . ASN A 1 190 ? 18.871 21.388 22.918 1.00 28.40 ? 208 ASN A N 1 ATOM 1519 C CA . ASN A 1 190 ? 19.018 21.630 24.343 1.00 29.15 ? 208 ASN A CA 1 ATOM 1520 C C . ASN A 1 190 ? 18.753 20.314 25.067 1.00 29.19 ? 208 ASN A C 1 ATOM 1521 O O . ASN A 1 190 ? 17.618 19.958 25.354 1.00 28.86 ? 208 ASN A O 1 ATOM 1522 C CB . ASN A 1 190 ? 18.064 22.726 24.815 1.00 29.68 ? 208 ASN A CB 1 ATOM 1523 C CG . ASN A 1 190 ? 18.284 23.106 26.265 1.00 30.48 ? 208 ASN A CG 1 ATOM 1524 O OD1 . ASN A 1 190 ? 19.295 22.729 26.866 1.00 31.07 ? 208 ASN A OD1 1 ATOM 1525 N ND2 . ASN A 1 190 ? 17.328 23.860 26.843 1.00 33.26 ? 208 ASN A ND2 1 ATOM 1526 N N . GLY A 1 191 ? 19.839 19.620 25.338 1.00 29.68 ? 209 GLY A N 1 ATOM 1527 C CA . GLY A 1 191 ? 19.803 18.233 25.839 1.00 30.30 ? 209 GLY A CA 1 ATOM 1528 C C . GLY A 1 191 ? 21.109 17.491 25.640 1.00 30.45 ? 209 GLY A C 1 ATOM 1529 O O . GLY A 1 191 ? 22.033 17.963 24.978 1.00 30.62 ? 209 GLY A O 1 ATOM 1530 N N . LYS A 1 192 ? 21.193 16.323 26.259 1.00 30.95 ? 210 LYS A N 1 ATOM 1531 C CA . LYS A 1 192 ? 22.357 15.447 26.110 1.00 31.26 ? 210 LYS A CA 1 ATOM 1532 C C . LYS A 1 192 ? 22.242 14.635 24.827 1.00 30.95 ? 210 LYS A C 1 ATOM 1533 O O . LYS A 1 192 ? 21.499 13.663 24.763 1.00 30.98 ? 210 LYS A O 1 ATOM 1534 C CB . LYS A 1 192 ? 22.499 14.546 27.345 1.00 31.16 ? 210 LYS A CB 1 ATOM 1535 C CG . LYS A 1 192 ? 22.839 15.315 28.629 1.00 32.30 ? 210 LYS A CG 1 ATOM 1536 C CD . LYS A 1 192 ? 24.206 15.967 28.506 1.00 33.77 ? 210 LYS A CD 1 ATOM 1537 C CE . LYS A 1 192 ? 24.628 16.663 29.778 1.00 35.77 ? 210 LYS A CE 1 ATOM 1538 N NZ . LYS A 1 192 ? 26.023 17.173 29.646 1.00 37.18 ? 210 LYS A NZ 1 ATOM 1539 N N . PHE A 1 193 ? 22.961 15.085 23.798 1.00 31.69 ? 211 PHE A N 1 ATOM 1540 C CA . PHE A 1 193 ? 22.821 14.576 22.415 1.00 32.23 ? 211 PHE A CA 1 ATOM 1541 C C . PHE A 1 193 ? 23.814 13.460 22.148 1.00 33.04 ? 211 PHE A C 1 ATOM 1542 O O . PHE A 1 193 ? 25.027 13.684 22.103 1.00 33.91 ? 211 PHE A O 1 ATOM 1543 C CB . PHE A 1 193 ? 23.048 15.703 21.395 1.00 32.45 ? 211 PHE A CB 1 ATOM 1544 C CG . PHE A 1 193 ? 22.637 15.360 19.980 1.00 32.84 ? 211 PHE A CG 1 ATOM 1545 C CD1 . PHE A 1 193 ? 21.514 15.946 19.417 1.00 33.84 ? 211 PHE A CD1 1 ATOM 1546 C CD2 . PHE A 1 193 ? 23.387 14.486 19.208 1.00 32.61 ? 211 PHE A CD2 1 ATOM 1547 C CE1 . PHE A 1 193 ? 21.136 15.665 18.114 1.00 33.40 ? 211 PHE A CE1 1 ATOM 1548 C CE2 . PHE A 1 193 ? 23.012 14.186 17.906 1.00 32.72 ? 211 PHE A CE2 1 ATOM 1549 C CZ . PHE A 1 193 ? 21.876 14.777 17.362 1.00 33.77 ? 211 PHE A CZ 1 ATOM 1550 N N . LEU A 1 194 ? 23.278 12.260 21.973 1.00 33.92 ? 212 LEU A N 1 ATOM 1551 C CA . LEU A 1 194 ? 24.108 11.055 21.767 1.00 34.43 ? 212 LEU A CA 1 ATOM 1552 C C . LEU A 1 194 ? 24.578 10.950 20.322 1.00 35.28 ? 212 LEU A C 1 ATOM 1553 O O . LEU A 1 194 ? 23.771 10.973 19.373 1.00 35.97 ? 212 LEU A O 1 ATOM 1554 C CB . LEU A 1 194 ? 23.345 9.786 22.148 1.00 34.54 ? 212 LEU A CB 1 ATOM 1555 C CG . LEU A 1 194 ? 24.164 8.478 21.973 1.00 33.55 ? 212 LEU A CG 1 ATOM 1556 C CD1 . LEU A 1 194 ? 25.415 8.500 22.812 1.00 32.00 ? 212 LEU A CD1 1 ATOM 1557 C CD2 . LEU A 1 194 ? 23.324 7.243 22.305 1.00 35.43 ? 212 LEU A CD2 1 ATOM 1558 N N . SER A 1 195 ? 25.893 10.890 20.172 1.00 36.05 ? 213 SER A N 1 ATOM 1559 C CA . SER A 1 195 ? 26.506 10.517 18.904 1.00 37.14 ? 213 SER A CA 1 ATOM 1560 C C . SER A 1 195 ? 27.749 9.651 19.077 1.00 37.80 ? 213 SER A C 1 ATOM 1561 O O . SER A 1 195 ? 28.733 10.027 19.743 1.00 37.77 ? 213 SER A O 1 ATOM 1562 C CB . SER A 1 195 ? 26.854 11.730 18.059 1.00 37.22 ? 213 SER A CB 1 ATOM 1563 O OG . SER A 1 195 ? 27.055 11.326 16.723 1.00 37.01 ? 213 SER A OG 1 ATOM 1564 N N . ASN A 1 196 ? 27.684 8.498 18.426 1.00 38.96 ? 214 ASN A N 1 ATOM 1565 C CA . ASN A 1 196 ? 28.745 7.494 18.492 1.00 39.37 ? 214 ASN A CA 1 ATOM 1566 C C . ASN A 1 196 ? 29.331 7.377 19.882 1.00 39.14 ? 214 ASN A C 1 ATOM 1567 O O . ASN A 1 196 ? 30.515 7.609 20.086 1.00 39.18 ? 214 ASN A O 1 ATOM 1568 C CB . ASN A 1 196 ? 29.869 7.787 17.505 1.00 39.85 ? 214 ASN A CB 1 ATOM 1569 C CG . ASN A 1 196 ? 30.884 6.635 17.432 1.00 42.45 ? 214 ASN A CG 1 ATOM 1570 O OD1 . ASN A 1 196 ? 32.083 6.841 17.206 1.00 45.95 ? 214 ASN A OD1 1 ATOM 1571 N ND2 . ASN A 1 196 ? 30.395 5.412 17.637 1.00 44.68 ? 214 ASN A ND2 1 ATOM 1572 N N . THR A 1 197 ? 28.462 7.033 20.821 1.00 39.23 ? 215 THR A N 1 ATOM 1573 C CA . THR A 1 197 ? 28.828 6.683 22.200 1.00 39.49 ? 215 THR A CA 1 ATOM 1574 C C . THR A 1 197 ? 29.112 7.872 23.103 1.00 39.43 ? 215 THR A C 1 ATOM 1575 O O . THR A 1 197 ? 29.263 7.723 24.310 1.00 39.28 ? 215 THR A O 1 ATOM 1576 C CB . THR A 1 197 ? 30.019 5.659 22.267 1.00 39.57 ? 215 THR A CB 1 ATOM 1577 O OG1 . THR A 1 197 ? 31.281 6.346 22.247 1.00 40.82 ? 215 THR A OG1 1 ATOM 1578 C CG2 . THR A 1 197 ? 29.953 4.679 21.107 1.00 39.78 ? 215 THR A CG2 1 ATOM 1579 N N . LYS A 1 198 ? 29.140 9.069 22.534 1.00 39.57 ? 216 LYS A N 1 ATOM 1580 C CA . LYS A 1 198 ? 29.373 10.276 23.348 1.00 39.62 ? 216 LYS A CA 1 ATOM 1581 C C . LYS A 1 198 ? 28.187 11.239 23.361 1.00 38.77 ? 216 LYS A C 1 ATOM 1582 O O . LYS A 1 198 ? 27.468 11.395 22.367 1.00 38.26 ? 216 LYS A O 1 ATOM 1583 C CB . LYS A 1 198 ? 30.647 10.984 22.891 1.00 40.11 ? 216 LYS A CB 1 ATOM 1584 C CG . LYS A 1 198 ? 31.840 10.039 22.823 1.00 42.40 ? 216 LYS A CG 1 ATOM 1585 C CD . LYS A 1 198 ? 33.155 10.775 22.691 1.00 45.19 ? 216 LYS A CD 1 ATOM 1586 C CE . LYS A 1 198 ? 34.225 10.093 23.536 1.00 47.06 ? 216 LYS A CE 1 ATOM 1587 N NZ . LYS A 1 198 ? 34.067 8.586 23.536 1.00 48.22 ? 216 LYS A NZ 1 ATOM 1588 N N . TYR A 1 199 ? 27.990 11.848 24.527 1.00 37.94 ? 217 TYR A N 1 ATOM 1589 C CA . TYR A 1 199 ? 26.898 12.819 24.755 1.00 37.72 ? 217 TYR A CA 1 ATOM 1590 C C . TYR A 1 199 ? 27.393 14.249 24.660 1.00 36.73 ? 217 TYR A C 1 ATOM 1591 O O . TYR A 1 199 ? 28.259 14.679 25.423 1.00 37.41 ? 217 TYR A O 1 ATOM 1592 C CB . TYR A 1 199 ? 26.248 12.597 26.122 1.00 37.90 ? 217 TYR A CB 1 ATOM 1593 C CG . TYR A 1 199 ? 25.438 11.326 26.193 1.00 39.05 ? 217 TYR A CG 1 ATOM 1594 C CD1 . TYR A 1 199 ? 24.117 11.302 25.764 1.00 40.44 ? 217 TYR A CD1 1 ATOM 1595 C CD2 . TYR A 1 199 ? 26.000 10.139 26.673 1.00 41.25 ? 217 TYR A CD2 1 ATOM 1596 C CE1 . TYR A 1 199 ? 23.362 10.140 25.822 1.00 42.27 ? 217 TYR A CE1 1 ATOM 1597 C CE2 . TYR A 1 199 ? 25.257 8.966 26.723 1.00 42.32 ? 217 TYR A CE2 1 ATOM 1598 C CZ . TYR A 1 199 ? 23.940 8.974 26.299 1.00 43.34 ? 217 TYR A CZ 1 ATOM 1599 O OH . TYR A 1 199 ? 23.189 7.820 26.353 1.00 46.71 ? 217 TYR A OH 1 ATOM 1600 N N . TYR A 1 200 ? 26.795 14.976 23.729 1.00 35.00 ? 218 TYR A N 1 ATOM 1601 C CA . TYR A 1 200 ? 27.169 16.357 23.393 1.00 33.64 ? 218 TYR A CA 1 ATOM 1602 C C . TYR A 1 200 ? 26.209 17.406 23.922 1.00 32.37 ? 218 TYR A C 1 ATOM 1603 O O . TYR A 1 200 ? 25.047 17.134 24.205 1.00 30.75 ? 218 TYR A O 1 ATOM 1604 C CB . TYR A 1 200 ? 27.305 16.515 21.877 1.00 33.64 ? 218 TYR A CB 1 ATOM 1605 C CG . TYR A 1 200 ? 28.432 15.679 21.339 1.00 32.87 ? 218 TYR A CG 1 ATOM 1606 C CD1 . TYR A 1 200 ? 29.743 16.138 21.399 1.00 33.38 ? 218 TYR A CD1 1 ATOM 1607 C CD2 . TYR A 1 200 ? 28.193 14.426 20.804 1.00 34.12 ? 218 TYR A CD2 1 ATOM 1608 C CE1 . TYR A 1 200 ? 30.793 15.371 20.930 1.00 33.62 ? 218 TYR A CE1 1 ATOM 1609 C CE2 . TYR A 1 200 ? 29.237 13.635 20.344 1.00 34.54 ? 218 TYR A CE2 1 ATOM 1610 C CZ . TYR A 1 200 ? 30.536 14.122 20.407 1.00 34.25 ? 218 TYR A CZ 1 ATOM 1611 O OH . TYR A 1 200 ? 31.578 13.371 19.919 1.00 34.38 ? 218 TYR A OH 1 ATOM 1612 N N . ASP A 1 201 ? 26.775 18.598 24.076 1.00 31.45 ? 219 ASP A N 1 ATOM 1613 C CA . ASP A 1 201 ? 26.051 19.803 24.517 1.00 30.64 ? 219 ASP A CA 1 ATOM 1614 C C . ASP A 1 201 ? 26.247 20.903 23.473 1.00 29.34 ? 219 ASP A C 1 ATOM 1615 O O . ASP A 1 201 ? 27.264 21.598 23.431 1.00 28.85 ? 219 ASP A O 1 ATOM 1616 C CB . ASP A 1 201 ? 26.561 20.285 25.876 1.00 31.16 ? 219 ASP A CB 1 ATOM 1617 C CG . ASP A 1 201 ? 26.478 19.216 26.945 1.00 33.44 ? 219 ASP A CG 1 ATOM 1618 O OD1 . ASP A 1 201 ? 25.376 18.964 27.468 1.00 35.95 ? 219 ASP A OD1 1 ATOM 1619 O OD2 . ASP A 1 201 ? 27.539 18.630 27.264 1.00 37.71 ? 219 ASP A OD2 1 ATOM 1620 N N . ASP A 1 202 ? 25.247 21.024 22.623 1.00 28.88 ? 220 ASP A N 1 ATOM 1621 C CA . ASP A 1 202 ? 25.287 21.922 21.455 1.00 28.46 ? 220 ASP A CA 1 ATOM 1622 C C . ASP A 1 202 ? 25.563 23.330 21.904 1.00 28.53 ? 220 ASP A C 1 ATOM 1623 O O . ASP A 1 202 ? 25.106 23.765 22.957 1.00 29.21 ? 220 ASP A O 1 ATOM 1624 C CB . ASP A 1 202 ? 23.941 21.858 20.711 1.00 28.13 ? 220 ASP A CB 1 ATOM 1625 C CG . ASP A 1 202 ? 23.974 22.460 19.310 1.00 28.90 ? 220 ASP A CG 1 ATOM 1626 O OD1 . ASP A 1 202 ? 25.012 22.984 18.837 1.00 31.85 ? 220 ASP A OD1 1 ATOM 1627 O OD2 . ASP A 1 202 ? 22.893 22.381 18.669 1.00 28.09 ? 220 ASP A OD2 1 ATOM 1628 N N . SER A 1 203 ? 26.324 24.037 21.089 1.00 28.20 ? 221 SER A N 1 ATOM 1629 C CA . SER A 1 203 ? 26.679 25.417 21.358 1.00 27.73 ? 221 SER A CA 1 ATOM 1630 C C . SER A 1 203 ? 26.730 26.186 20.059 1.00 27.77 ? 221 SER A C 1 ATOM 1631 O O . SER A 1 203 ? 27.366 25.753 19.092 1.00 26.98 ? 221 SER A O 1 ATOM 1632 C CB . SER A 1 203 ? 28.034 25.472 22.051 1.00 28.63 ? 221 SER A CB 1 ATOM 1633 O OG . SER A 1 203 ? 28.581 26.789 22.078 1.00 28.61 ? 221 SER A OG 1 ATOM 1634 N N . GLN A 1 204 ? 26.052 27.333 20.032 1.00 27.07 ? 222 GLN A N 1 ATOM 1635 C CA . GLN A 1 204 ? 26.047 28.180 18.824 1.00 26.47 ? 222 GLN A CA 1 ATOM 1636 C C . GLN A 1 204 ? 26.026 29.643 19.160 1.00 26.96 ? 222 GLN A C 1 ATOM 1637 O O . GLN A 1 204 ? 25.197 30.094 19.960 1.00 26.46 ? 222 GLN A O 1 ATOM 1638 C CB . GLN A 1 204 ? 24.823 27.876 17.954 1.00 27.90 ? 222 GLN A CB 1 ATOM 1639 C CG . GLN A 1 204 ? 24.858 28.535 16.585 1.00 25.96 ? 222 GLN A CG 1 ATOM 1640 C CD . GLN A 1 204 ? 26.002 28.061 15.735 1.00 27.08 ? 222 GLN A CD 1 ATOM 1641 O OE1 . GLN A 1 204 ? 26.220 26.848 15.572 1.00 25.34 ? 222 GLN A OE1 1 ATOM 1642 N NE2 . GLN A 1 204 ? 26.773 29.009 15.202 1.00 27.57 ? 222 GLN A NE2 1 ATOM 1643 N N . TYR A 1 205 ? 26.956 30.358 18.542 1.00 26.85 ? 223 TYR A N 1 ATOM 1644 C CA . TYR A 1 205 ? 27.037 31.801 18.642 1.00 26.15 ? 223 TYR A CA 1 ATOM 1645 C C . TYR A 1 205 ? 26.880 32.448 17.262 1.00 25.73 ? 223 TYR A C 1 ATOM 1646 O O . TYR A 1 205 ? 27.313 31.916 16.218 1.00 25.26 ? 223 TYR A O 1 ATOM 1647 C CB . TYR A 1 205 ? 28.396 32.280 19.133 1.00 26.64 ? 223 TYR A CB 1 ATOM 1648 C CG . TYR A 1 205 ? 28.929 31.791 20.469 1.00 27.50 ? 223 TYR A CG 1 ATOM 1649 C CD1 . TYR A 1 205 ? 28.178 30.999 21.321 1.00 28.44 ? 223 TYR A CD1 1 ATOM 1650 C CD2 . TYR A 1 205 ? 30.208 32.168 20.882 1.00 31.06 ? 223 TYR A CD2 1 ATOM 1651 C CE1 . TYR A 1 205 ? 28.702 30.577 22.551 1.00 30.19 ? 223 TYR A CE1 1 ATOM 1652 C CE2 . TYR A 1 205 ? 30.730 31.738 22.098 1.00 32.44 ? 223 TYR A CE2 1 ATOM 1653 C CZ . TYR A 1 205 ? 29.970 30.951 22.916 1.00 32.23 ? 223 TYR A CZ 1 ATOM 1654 O OH . TYR A 1 205 ? 30.485 30.553 24.120 1.00 35.38 ? 223 TYR A OH 1 ATOM 1655 N N . TYR A 1 206 ? 26.261 33.598 17.293 1.00 25.46 ? 224 TYR A N 1 ATOM 1656 C CA . TYR A 1 206 ? 26.276 34.545 16.160 1.00 25.88 ? 224 TYR A CA 1 ATOM 1657 C C . TYR A 1 206 ? 27.001 35.796 16.651 1.00 26.22 ? 224 TYR A C 1 ATOM 1658 O O . TYR A 1 206 ? 26.813 36.238 17.784 1.00 27.51 ? 224 TYR A O 1 ATOM 1659 C CB . TYR A 1 206 ? 24.877 34.941 15.641 1.00 25.57 ? 224 TYR A CB 1 ATOM 1660 C CG . TYR A 1 206 ? 23.981 33.838 15.069 1.00 25.34 ? 224 TYR A CG 1 ATOM 1661 C CD1 . TYR A 1 206 ? 24.490 32.598 14.713 1.00 25.11 ? 224 TYR A CD1 1 ATOM 1662 C CD2 . TYR A 1 206 ? 22.615 34.061 14.883 1.00 24.28 ? 224 TYR A CD2 1 ATOM 1663 C CE1 . TYR A 1 206 ? 23.669 31.616 14.173 1.00 25.29 ? 224 TYR A CE1 1 ATOM 1664 C CE2 . TYR A 1 206 ? 21.786 33.096 14.365 1.00 24.48 ? 224 TYR A CE2 1 ATOM 1665 C CZ . TYR A 1 206 ? 22.326 31.853 14.011 1.00 25.77 ? 224 TYR A CZ 1 ATOM 1666 O OH . TYR A 1 206 ? 21.504 30.893 13.489 1.00 26.34 ? 224 TYR A OH 1 ATOM 1667 N N . PHE A 1 207 ? 27.776 36.381 15.758 1.00 26.35 ? 225 PHE A N 1 ATOM 1668 C CA . PHE A 1 207 ? 28.619 37.532 16.051 1.00 27.23 ? 225 PHE A CA 1 ATOM 1669 C C . PHE A 1 207 ? 28.482 38.586 14.954 1.00 27.43 ? 225 PHE A C 1 ATOM 1670 O O . PHE A 1 207 ? 28.725 38.291 13.780 1.00 26.93 ? 225 PHE A O 1 ATOM 1671 C CB . PHE A 1 207 ? 30.079 37.058 16.168 1.00 27.09 ? 225 PHE A CB 1 ATOM 1672 C CG . PHE A 1 207 ? 31.076 38.158 16.362 1.00 28.31 ? 225 PHE A CG 1 ATOM 1673 C CD1 . PHE A 1 207 ? 30.950 39.055 17.411 1.00 27.54 ? 225 PHE A CD1 1 ATOM 1674 C CD2 . PHE A 1 207 ? 32.184 38.266 15.533 1.00 29.46 ? 225 PHE A CD2 1 ATOM 1675 C CE1 . PHE A 1 207 ? 31.885 40.051 17.606 1.00 28.65 ? 225 PHE A CE1 1 ATOM 1676 C CE2 . PHE A 1 207 ? 33.123 39.274 15.733 1.00 31.09 ? 225 PHE A CE2 1 ATOM 1677 C CZ . PHE A 1 207 ? 32.965 40.164 16.774 1.00 29.25 ? 225 PHE A CZ 1 ATOM 1678 N N . ASN A 1 208 ? 28.058 39.782 15.345 1.00 26.78 ? 226 ASN A N 1 ATOM 1679 C CA . ASN A 1 208 ? 28.011 40.936 14.423 1.00 27.35 ? 226 ASN A CA 1 ATOM 1680 C C . ASN A 1 208 ? 29.405 41.544 14.375 1.00 28.40 ? 226 ASN A C 1 ATOM 1681 O O . ASN A 1 208 ? 29.898 42.074 15.372 1.00 28.31 ? 226 ASN A O 1 ATOM 1682 C CB . ASN A 1 208 ? 26.972 41.992 14.864 1.00 27.01 ? 226 ASN A CB 1 ATOM 1683 C CG . ASN A 1 208 ? 26.831 43.147 13.854 1.00 26.26 ? 226 ASN A CG 1 ATOM 1684 O OD1 . ASN A 1 208 ? 27.829 43.619 13.296 1.00 26.35 ? 226 ASN A OD1 1 ATOM 1685 N ND2 . ASN A 1 208 ? 25.579 43.617 13.626 1.00 25.88 ? 226 ASN A ND2 1 ATOM 1686 N N . LYS A 1 209 ? 30.060 41.428 13.219 1.00 28.96 ? 227 LYS A N 1 ATOM 1687 C CA . LYS A 1 209 ? 31.464 41.803 13.095 1.00 30.63 ? 227 LYS A CA 1 ATOM 1688 C C . LYS A 1 209 ? 31.725 43.299 13.288 1.00 30.66 ? 227 LYS A C 1 ATOM 1689 O O . LYS A 1 209 ? 32.851 43.724 13.558 1.00 30.96 ? 227 LYS A O 1 ATOM 1690 C CB . LYS A 1 209 ? 32.005 41.361 11.725 1.00 30.77 ? 227 LYS A CB 1 ATOM 1691 C CG . LYS A 1 209 ? 32.045 39.845 11.599 1.00 34.70 ? 227 LYS A CG 1 ATOM 1692 C CD . LYS A 1 209 ? 32.629 39.357 10.280 1.00 40.71 ? 227 LYS A CD 1 ATOM 1693 C CE . LYS A 1 209 ? 34.124 39.713 10.197 1.00 44.20 ? 227 LYS A CE 1 ATOM 1694 N NZ . LYS A 1 209 ? 34.818 39.769 11.551 1.00 48.35 ? 227 LYS A NZ 1 ATOM 1695 N N . ASP A 1 210 ? 30.690 44.103 13.141 1.00 31.45 ? 228 ASP A N 1 ATOM 1696 C CA . ASP A 1 210 ? 30.875 45.537 13.252 1.00 31.49 ? 228 ASP A CA 1 ATOM 1697 C C . ASP A 1 210 ? 30.295 46.148 14.521 1.00 31.20 ? 228 ASP A C 1 ATOM 1698 O O . ASP A 1 210 ? 30.883 47.088 15.056 1.00 32.88 ? 228 ASP A O 1 ATOM 1699 C CB . ASP A 1 210 ? 30.334 46.227 12.025 1.00 32.11 ? 228 ASP A CB 1 ATOM 1700 C CG . ASP A 1 210 ? 31.118 45.858 10.790 1.00 33.83 ? 228 ASP A CG 1 ATOM 1701 O OD1 . ASP A 1 210 ? 30.557 45.153 9.936 1.00 34.21 ? 228 ASP A OD1 1 ATOM 1702 O OD2 . ASP A 1 210 ? 32.305 46.247 10.710 1.00 34.58 ? 228 ASP A OD2 1 ATOM 1703 N N . THR A 1 211 ? 29.187 45.622 15.022 1.00 29.55 ? 229 THR A N 1 ATOM 1704 C CA . THR A 1 211 ? 28.669 46.123 16.313 1.00 28.80 ? 229 THR A CA 1 ATOM 1705 C C . THR A 1 211 ? 29.427 45.437 17.455 1.00 28.65 ? 229 THR A C 1 ATOM 1706 O O . THR A 1 211 ? 29.514 45.953 18.575 1.00 28.05 ? 229 THR A O 1 ATOM 1707 C CB . THR A 1 211 ? 27.186 45.861 16.507 1.00 28.42 ? 229 THR A CB 1 ATOM 1708 O OG1 . THR A 1 211 ? 26.950 44.460 16.529 1.00 27.77 ? 229 THR A OG1 1 ATOM 1709 C CG2 . THR A 1 211 ? 26.348 46.539 15.398 1.00 28.06 ? 229 THR A CG2 1 ATOM 1710 N N . GLY A 1 212 ? 29.969 44.270 17.148 1.00 27.08 ? 230 GLY A N 1 ATOM 1711 C CA . GLY A 1 212 ? 30.704 43.464 18.122 1.00 27.12 ? 230 GLY A CA 1 ATOM 1712 C C . GLY A 1 212 ? 29.850 42.702 19.111 1.00 26.59 ? 230 GLY A C 1 ATOM 1713 O O . GLY A 1 212 ? 30.353 42.133 20.078 1.00 26.70 ? 230 GLY A O 1 ATOM 1714 N N . VAL A 1 213 ? 28.565 42.638 18.839 1.00 26.70 ? 231 VAL A N 1 ATOM 1715 C CA . VAL A 1 213 ? 27.634 41.895 19.711 1.00 27.34 ? 231 VAL A CA 1 ATOM 1716 C C . VAL A 1 213 ? 27.680 40.409 19.432 1.00 27.54 ? 231 VAL A C 1 ATOM 1717 O O . VAL A 1 213 ? 27.629 39.976 18.264 1.00 27.33 ? 231 VAL A O 1 ATOM 1718 C CB . VAL A 1 213 ? 26.185 42.413 19.565 1.00 27.15 ? 231 VAL A CB 1 ATOM 1719 C CG1 . VAL A 1 213 ? 25.247 41.658 20.532 1.00 27.74 ? 231 VAL A CG1 1 ATOM 1720 C CG2 . VAL A 1 213 ? 26.132 43.950 19.772 1.00 27.58 ? 231 VAL A CG2 1 ATOM 1721 N N . ILE A 1 214 ? 27.799 39.638 20.512 1.00 27.12 ? 232 ILE A N 1 ATOM 1722 C CA . ILE A 1 214 ? 27.714 38.187 20.475 1.00 27.17 ? 232 ILE A CA 1 ATOM 1723 C C . ILE A 1 214 ? 26.374 37.757 21.062 1.00 27.00 ? 232 ILE A C 1 ATOM 1724 O O . ILE A 1 214 ? 25.962 38.200 22.129 1.00 27.11 ? 232 ILE A O 1 ATOM 1725 C CB . ILE A 1 214 ? 28.836 37.465 21.304 1.00 27.38 ? 232 ILE A CB 1 ATOM 1726 C CG1 . ILE A 1 214 ? 30.232 37.651 20.691 1.00 29.61 ? 232 ILE A CG1 1 ATOM 1727 C CG2 . ILE A 1 214 ? 28.557 35.978 21.375 1.00 28.11 ? 232 ILE A CG2 1 ATOM 1728 C CD1 . ILE A 1 214 ? 31.002 38.820 21.126 1.00 30.87 ? 232 ILE A CD1 1 ATOM 1729 N N . TYR A 1 215 ? 25.697 36.917 20.312 1.00 26.13 ? 233 TYR A N 1 ATOM 1730 C CA . TYR A 1 215 ? 24.476 36.247 20.739 1.00 26.13 ? 233 TYR A CA 1 ATOM 1731 C C . TYR A 1 215 ? 24.754 34.788 20.753 1.00 26.01 ? 233 TYR A C 1 ATOM 1732 O O . TYR A 1 215 ? 25.082 34.214 19.720 1.00 26.65 ? 233 TYR A O 1 ATOM 1733 C CB . TYR A 1 215 ? 23.331 36.470 19.724 1.00 25.61 ? 233 TYR A CB 1 ATOM 1734 C CG . TYR A 1 215 ? 23.147 37.893 19.257 1.00 26.08 ? 233 TYR A CG 1 ATOM 1735 C CD1 . TYR A 1 215 ? 22.192 38.701 19.828 1.00 28.64 ? 233 TYR A CD1 1 ATOM 1736 C CD2 . TYR A 1 215 ? 23.933 38.424 18.238 1.00 27.63 ? 233 TYR A CD2 1 ATOM 1737 C CE1 . TYR A 1 215 ? 22.028 40.004 19.412 1.00 29.51 ? 233 TYR A CE1 1 ATOM 1738 C CE2 . TYR A 1 215 ? 23.767 39.721 17.817 1.00 28.71 ? 233 TYR A CE2 1 ATOM 1739 C CZ . TYR A 1 215 ? 22.802 40.502 18.408 1.00 29.59 ? 233 TYR A CZ 1 ATOM 1740 O OH . TYR A 1 215 ? 22.633 41.812 18.006 1.00 32.66 ? 233 TYR A OH 1 ATOM 1741 N N . GLY A 1 216 ? 24.622 34.153 21.900 1.00 26.37 ? 234 GLY A N 1 ATOM 1742 C CA . GLY A 1 216 ? 24.954 32.729 21.966 1.00 26.11 ? 234 GLY A CA 1 ATOM 1743 C C . GLY A 1 216 ? 23.961 31.926 22.758 1.00 25.61 ? 234 GLY A C 1 ATOM 1744 O O . GLY A 1 216 ? 23.217 32.465 23.584 1.00 25.02 ? 234 GLY A O 1 ATOM 1745 N N . LEU A 1 217 ? 23.939 30.634 22.458 1.00 25.62 ? 235 LEU A N 1 ATOM 1746 C CA . LEU A 1 217 ? 23.140 29.671 23.214 1.00 26.06 ? 235 LEU A CA 1 ATOM 1747 C C . LEU A 1 217 ? 23.935 28.393 23.402 1.00 26.63 ? 235 LEU A C 1 ATOM 1748 O O . LEU A 1 217 ? 24.424 27.786 22.427 1.00 27.13 ? 235 LEU A O 1 ATOM 1749 C CB . LEU A 1 217 ? 21.835 29.297 22.494 1.00 27.14 ? 235 LEU A CB 1 ATOM 1750 C CG . LEU A 1 217 ? 20.679 30.272 22.339 1.00 28.65 ? 235 LEU A CG 1 ATOM 1751 C CD1 . LEU A 1 217 ? 19.512 29.560 21.607 1.00 28.20 ? 235 LEU A CD1 1 ATOM 1752 C CD2 . LEU A 1 217 ? 20.214 30.784 23.693 1.00 28.51 ? 235 LEU A CD2 1 ATOM 1753 N N . ASN A 1 218 ? 24.051 28.012 24.661 1.00 26.72 ? 236 ASN A N 1 ATOM 1754 C CA . ASN A 1 218 ? 24.617 26.727 25.056 1.00 27.06 ? 236 ASN A CA 1 ATOM 1755 C C . ASN A 1 218 ? 23.575 25.839 25.719 1.00 27.81 ? 236 ASN A C 1 ATOM 1756 O O . ASN A 1 218 ? 22.713 26.299 26.492 1.00 27.55 ? 236 ASN A O 1 ATOM 1757 C CB . ASN A 1 218 ? 25.777 26.929 26.031 1.00 27.40 ? 236 ASN A CB 1 ATOM 1758 C CG . ASN A 1 218 ? 27.084 27.186 25.353 1.00 27.63 ? 236 ASN A CG 1 ATOM 1759 O OD1 . ASN A 1 218 ? 27.145 27.626 24.219 1.00 28.60 ? 236 ASN A OD1 1 ATOM 1760 N ND2 . ASN A 1 218 ? 28.169 26.918 26.073 1.00 29.23 ? 236 ASN A ND2 1 ATOM 1761 N N . SER A 1 219 ? 23.650 24.557 25.376 1.00 27.73 ? 237 SER A N 1 ATOM 1762 C CA . SER A 1 219 ? 22.783 23.529 25.948 1.00 28.33 ? 237 SER A CA 1 ATOM 1763 C C . SER A 1 219 ? 22.994 23.418 27.446 1.00 28.91 ? 237 SER A C 1 ATOM 1764 O O . SER A 1 219 ? 24.123 23.418 27.931 1.00 29.20 ? 237 SER A O 1 ATOM 1765 C CB . SER A 1 219 ? 23.048 22.165 25.273 1.00 28.51 ? 237 SER A CB 1 ATOM 1766 O OG . SER A 1 219 ? 22.187 21.164 25.793 1.00 27.40 ? 237 SER A OG 1 ATOM 1767 N N . THR A 1 220 ? 21.893 23.354 28.185 1.00 30.27 ? 238 THR A N 1 ATOM 1768 C CA . THR A 1 220 ? 21.943 23.198 29.640 1.00 31.42 ? 238 THR A CA 1 ATOM 1769 C C . THR A 1 220 ? 21.123 22.016 30.173 1.00 32.09 ? 238 THR A C 1 ATOM 1770 O O . THR A 1 220 ? 21.339 21.583 31.291 1.00 32.11 ? 238 THR A O 1 ATOM 1771 C CB . THR A 1 220 ? 21.475 24.489 30.375 1.00 31.57 ? 238 THR A CB 1 ATOM 1772 O OG1 . THR A 1 220 ? 20.109 24.747 30.051 1.00 32.53 ? 238 THR A OG1 1 ATOM 1773 C CG2 . THR A 1 220 ? 22.333 25.699 30.002 1.00 32.40 ? 238 THR A CG2 1 ATOM 1774 N N . GLU A 1 221 ? 20.217 21.474 29.370 1.00 32.54 ? 239 GLU A N 1 ATOM 1775 C CA . GLU A 1 221 ? 19.410 20.287 29.757 1.00 33.43 ? 239 GLU A CA 1 ATOM 1776 C C . GLU A 1 221 ? 20.271 19.044 30.036 1.00 33.51 ? 239 GLU A C 1 ATOM 1777 O O . GLU A 1 221 ? 21.277 18.802 29.375 1.00 33.08 ? 239 GLU A O 1 ATOM 1778 C CB . GLU A 1 221 ? 18.385 19.901 28.677 1.00 34.35 ? 239 GLU A CB 1 ATOM 1779 C CG . GLU A 1 221 ? 17.068 20.618 28.789 1.00 38.32 ? 239 GLU A CG 1 ATOM 1780 C CD . GLU A 1 221 ? 16.246 20.125 29.965 1.00 45.20 ? 239 GLU A CD 1 ATOM 1781 O OE1 . GLU A 1 221 ? 16.764 19.297 30.772 1.00 49.62 ? 239 GLU A OE1 1 ATOM 1782 O OE2 . GLU A 1 221 ? 15.082 20.569 30.081 1.00 48.30 ? 239 GLU A OE2 1 ATOM 1783 N N . THR A 1 222 ? 19.834 18.260 31.013 1.00 33.72 ? 240 THR A N 1 ATOM 1784 C CA . THR A 1 222 ? 20.536 17.025 31.406 1.00 34.37 ? 240 THR A CA 1 ATOM 1785 C C . THR A 1 222 ? 19.818 15.772 30.917 1.00 34.60 ? 240 THR A C 1 ATOM 1786 O O . THR A 1 222 ? 20.356 14.667 31.001 1.00 34.89 ? 240 THR A O 1 ATOM 1787 C CB . THR A 1 222 ? 20.711 16.941 32.947 1.00 34.65 ? 240 THR A CB 1 ATOM 1788 O OG1 . THR A 1 222 ? 19.435 17.060 33.590 1.00 34.94 ? 240 THR A OG1 1 ATOM 1789 C CG2 . THR A 1 222 ? 21.613 18.049 33.427 1.00 35.48 ? 240 THR A CG2 1 ATOM 1790 N N . ILE A 1 223 ? 18.605 15.945 30.408 1.00 34.42 ? 241 ILE A N 1 ATOM 1791 C CA . ILE A 1 223 ? 17.866 14.813 29.799 1.00 34.31 ? 241 ILE A CA 1 ATOM 1792 C C . ILE A 1 223 ? 18.522 14.283 28.527 1.00 34.05 ? 241 ILE A C 1 ATOM 1793 O O . ILE A 1 223 ? 19.110 15.029 27.738 1.00 33.90 ? 241 ILE A O 1 ATOM 1794 C CB . ILE A 1 223 ? 16.381 15.130 29.525 1.00 34.26 ? 241 ILE A CB 1 ATOM 1795 C CG1 . ILE A 1 223 ? 16.208 16.339 28.574 1.00 34.19 ? 241 ILE A CG1 1 ATOM 1796 C CG2 . ILE A 1 223 ? 15.659 15.358 30.841 1.00 34.50 ? 241 ILE A CG2 1 ATOM 1797 C CD1 . ILE A 1 223 ? 14.746 16.652 28.266 1.00 33.33 ? 241 ILE A CD1 1 ATOM 1798 N N . THR A 1 224 ? 18.406 12.973 28.342 1.00 33.56 ? 242 THR A N 1 ATOM 1799 C CA . THR A 1 224 ? 19.030 12.285 27.207 1.00 32.96 ? 242 THR A CA 1 ATOM 1800 C C . THR A 1 224 ? 18.007 11.888 26.164 1.00 33.15 ? 242 THR A C 1 ATOM 1801 O O . THR A 1 224 ? 18.334 11.317 25.112 1.00 33.33 ? 242 THR A O 1 ATOM 1802 C CB . THR A 1 224 ? 19.757 11.019 27.661 1.00 33.57 ? 242 THR A CB 1 ATOM 1803 O OG1 . THR A 1 224 ? 18.824 10.153 28.320 1.00 32.08 ? 242 THR A OG1 1 ATOM 1804 C CG2 . THR A 1 224 ? 20.877 11.373 28.593 1.00 31.73 ? 242 THR A CG2 1 ATOM 1805 N N . THR A 1 225 ? 16.764 12.214 26.471 1.00 32.94 ? 243 THR A N 1 ATOM 1806 C CA . THR A 1 225 ? 15.646 11.927 25.577 1.00 32.78 ? 243 THR A CA 1 ATOM 1807 C C . THR A 1 225 ? 14.527 12.915 25.808 1.00 32.40 ? 243 THR A C 1 ATOM 1808 O O . THR A 1 225 ? 14.466 13.564 26.857 1.00 32.34 ? 243 THR A O 1 ATOM 1809 C CB . THR A 1 225 ? 15.115 10.459 25.778 1.00 33.30 ? 243 THR A CB 1 ATOM 1810 O OG1 . THR A 1 225 ? 14.313 10.071 24.655 1.00 33.65 ? 243 THR A OG1 1 ATOM 1811 C CG2 . THR A 1 225 ? 14.288 10.357 27.053 1.00 33.09 ? 243 THR A CG2 1 ATOM 1812 N N . GLY A 1 226 ? 13.653 13.047 24.820 1.00 31.81 ? 244 GLY A N 1 ATOM 1813 C CA . GLY A 1 226 ? 12.510 13.944 24.947 1.00 31.97 ? 244 GLY A CA 1 ATOM 1814 C C . GLY A 1 226 ? 12.904 15.412 24.832 1.00 31.52 ? 244 GLY A C 1 ATOM 1815 O O . GLY A 1 226 ? 12.147 16.302 25.193 1.00 31.34 ? 244 GLY A O 1 ATOM 1816 N N . PHE A 1 227 ? 14.113 15.647 24.341 1.00 31.24 ? 245 PHE A N 1 ATOM 1817 C CA . PHE A 1 227 ? 14.569 17.017 24.037 1.00 31.16 ? 245 PHE A CA 1 ATOM 1818 C C . PHE A 1 227 ? 14.508 17.312 22.546 1.00 30.31 ? 245 PHE A C 1 ATOM 1819 O O . PHE A 1 227 ? 14.356 16.428 21.708 1.00 30.18 ? 245 PHE A O 1 ATOM 1820 C CB . PHE A 1 227 ? 15.994 17.280 24.552 1.00 30.69 ? 245 PHE A CB 1 ATOM 1821 C CG . PHE A 1 227 ? 17.052 16.492 23.849 1.00 32.02 ? 245 PHE A CG 1 ATOM 1822 C CD1 . PHE A 1 227 ? 17.559 16.914 22.633 1.00 33.73 ? 245 PHE A CD1 1 ATOM 1823 C CD2 . PHE A 1 227 ? 17.557 15.338 24.413 1.00 32.13 ? 245 PHE A CD2 1 ATOM 1824 C CE1 . PHE A 1 227 ? 18.539 16.187 21.980 1.00 34.69 ? 245 PHE A CE1 1 ATOM 1825 C CE2 . PHE A 1 227 ? 18.541 14.598 23.769 1.00 33.91 ? 245 PHE A CE2 1 ATOM 1826 C CZ . PHE A 1 227 ? 19.035 15.011 22.555 1.00 34.09 ? 245 PHE A CZ 1 ATOM 1827 N N . ASP A 1 228 ? 14.678 18.580 22.223 1.00 29.52 ? 246 ASP A N 1 ATOM 1828 C CA . ASP A 1 228 ? 14.569 19.011 20.826 1.00 29.26 ? 246 ASP A CA 1 ATOM 1829 C C . ASP A 1 228 ? 15.347 20.305 20.558 1.00 28.33 ? 246 ASP A C 1 ATOM 1830 O O . ASP A 1 228 ? 16.157 20.771 21.367 1.00 28.27 ? 246 ASP A O 1 ATOM 1831 C CB . ASP A 1 228 ? 13.095 19.163 20.430 1.00 28.89 ? 246 ASP A CB 1 ATOM 1832 C CG . ASP A 1 228 ? 12.796 18.681 18.992 1.00 30.75 ? 246 ASP A CG 1 ATOM 1833 O OD1 . ASP A 1 228 ? 13.432 19.158 18.006 1.00 30.31 ? 246 ASP A OD1 1 ATOM 1834 O OD2 . ASP A 1 228 ? 11.876 17.837 18.851 1.00 31.54 ? 246 ASP A OD2 1 ATOM 1835 N N . PHE A 1 229 ? 15.040 20.881 19.409 1.00 27.64 ? 247 PHE A N 1 ATOM 1836 C CA . PHE A 1 229 ? 15.785 21.992 18.852 1.00 27.23 ? 247 PHE A CA 1 ATOM 1837 C C . PHE A 1 229 ? 15.116 23.271 19.355 1.00 27.67 ? 247 PHE A C 1 ATOM 1838 O O . PHE A 1 229 ? 14.051 23.681 18.884 1.00 27.25 ? 247 PHE A O 1 ATOM 1839 C CB . PHE A 1 229 ? 15.765 21.887 17.319 1.00 27.99 ? 247 PHE A CB 1 ATOM 1840 C CG . PHE A 1 229 ? 16.868 22.641 16.600 1.00 27.61 ? 247 PHE A CG 1 ATOM 1841 C CD1 . PHE A 1 229 ? 18.201 22.484 16.945 1.00 26.83 ? 247 PHE A CD1 1 ATOM 1842 C CD2 . PHE A 1 229 ? 16.553 23.453 15.506 1.00 27.27 ? 247 PHE A CD2 1 ATOM 1843 C CE1 . PHE A 1 229 ? 19.216 23.154 16.228 1.00 27.24 ? 247 PHE A CE1 1 ATOM 1844 C CE2 . PHE A 1 229 ? 17.556 24.129 14.802 1.00 26.09 ? 247 PHE A CE2 1 ATOM 1845 C CZ . PHE A 1 229 ? 18.871 23.971 15.140 1.00 26.67 ? 247 PHE A CZ 1 ATOM 1846 N N . ASN A 1 230 ? 15.766 23.874 20.338 1.00 26.94 ? 248 ASN A N 1 ATOM 1847 C CA . ASN A 1 230 ? 15.274 25.089 20.964 1.00 27.35 ? 248 ASN A CA 1 ATOM 1848 C C . ASN A 1 230 ? 15.726 26.293 20.155 1.00 27.36 ? 248 ASN A C 1 ATOM 1849 O O . ASN A 1 230 ? 16.914 26.492 19.963 1.00 27.42 ? 248 ASN A O 1 ATOM 1850 C CB . ASN A 1 230 ? 15.839 25.280 22.371 1.00 27.77 ? 248 ASN A CB 1 ATOM 1851 C CG . ASN A 1 230 ? 15.326 24.285 23.392 1.00 29.26 ? 248 ASN A CG 1 ATOM 1852 O OD1 . ASN A 1 230 ? 15.167 24.657 24.551 1.00 30.21 ? 248 ASN A OD1 1 ATOM 1853 N ND2 . ASN A 1 230 ? 15.098 23.036 23.004 1.00 28.42 ? 248 ASN A ND2 1 ATOM 1854 N N . CYS A 1 231 ? 14.774 27.124 19.740 1.00 27.38 ? 249 CYS A N 1 ATOM 1855 C CA . CYS A 1 231 ? 15.097 28.350 19.015 1.00 27.19 ? 249 CYS A CA 1 ATOM 1856 C C . CYS A 1 231 ? 14.710 29.634 19.733 1.00 27.34 ? 249 CYS A C 1 ATOM 1857 O O . CYS A 1 231 ? 13.641 29.731 20.378 1.00 27.12 ? 249 CYS A O 1 ATOM 1858 C CB . CYS A 1 231 ? 14.400 28.367 17.661 1.00 28.30 ? 249 CYS A CB 1 ATOM 1859 S SG . CYS A 1 231 ? 14.879 27.089 16.531 1.00 29.55 ? 249 CYS A SG 1 ATOM 1860 N N . HIS A 1 232 ? 15.602 30.604 19.546 1.00 26.77 ? 250 HIS A N 1 ATOM 1861 C CA . HIS A 1 232 ? 15.384 32.005 19.826 1.00 27.41 ? 250 HIS A CA 1 ATOM 1862 C C . HIS A 1 232 ? 15.346 32.783 18.516 1.00 27.15 ? 250 HIS A C 1 ATOM 1863 O O . HIS A 1 232 ? 16.014 32.432 17.518 1.00 28.02 ? 250 HIS A O 1 ATOM 1864 C CB . HIS A 1 232 ? 16.464 32.578 20.716 1.00 27.65 ? 250 HIS A CB 1 ATOM 1865 C CG . HIS A 1 232 ? 16.401 32.081 22.126 1.00 31.05 ? 250 HIS A CG 1 ATOM 1866 N ND1 . HIS A 1 232 ? 17.065 32.703 23.157 1.00 33.77 ? 250 HIS A ND1 1 ATOM 1867 C CD2 . HIS A 1 232 ? 15.712 31.055 22.685 1.00 35.07 ? 250 HIS A CD2 1 ATOM 1868 C CE1 . HIS A 1 232 ? 16.819 32.062 24.289 1.00 35.98 ? 250 HIS A CE1 1 ATOM 1869 N NE2 . HIS A 1 232 ? 16.008 31.053 24.033 1.00 36.50 ? 250 HIS A NE2 1 ATOM 1870 N N . TYR A 1 233 ? 14.535 33.825 18.542 1.00 26.33 ? 251 TYR A N 1 ATOM 1871 C CA . TYR A 1 233 ? 14.301 34.640 17.360 1.00 25.57 ? 251 TYR A CA 1 ATOM 1872 C C . TYR A 1 233 ? 14.857 36.030 17.540 1.00 25.57 ? 251 TYR A C 1 ATOM 1873 O O . TYR A 1 233 ? 14.298 36.883 18.249 1.00 27.03 ? 251 TYR A O 1 ATOM 1874 C CB . TYR A 1 233 ? 12.814 34.591 16.982 1.00 26.38 ? 251 TYR A CB 1 ATOM 1875 C CG . TYR A 1 233 ? 12.403 33.161 16.736 1.00 25.53 ? 251 TYR A CG 1 ATOM 1876 C CD1 . TYR A 1 233 ? 12.512 32.590 15.475 1.00 25.00 ? 251 TYR A CD1 1 ATOM 1877 C CD2 . TYR A 1 233 ? 12.012 32.332 17.795 1.00 25.72 ? 251 TYR A CD2 1 ATOM 1878 C CE1 . TYR A 1 233 ? 12.194 31.260 15.253 1.00 25.06 ? 251 TYR A CE1 1 ATOM 1879 C CE2 . TYR A 1 233 ? 11.676 31.014 17.580 1.00 25.88 ? 251 TYR A CE2 1 ATOM 1880 C CZ . TYR A 1 233 ? 11.782 30.470 16.308 1.00 25.42 ? 251 TYR A CZ 1 ATOM 1881 O OH . TYR A 1 233 ? 11.446 29.156 16.116 1.00 25.82 ? 251 TYR A OH 1 ATOM 1882 N N . LEU A 1 234 ? 16.013 36.236 16.911 1.00 25.16 ? 252 LEU A N 1 ATOM 1883 C CA . LEU A 1 234 ? 16.753 37.476 17.044 1.00 24.72 ? 252 LEU A CA 1 ATOM 1884 C C . LEU A 1 234 ? 16.239 38.488 16.043 1.00 25.04 ? 252 LEU A C 1 ATOM 1885 O O . LEU A 1 234 ? 15.986 38.163 14.891 1.00 25.48 ? 252 LEU A O 1 ATOM 1886 C CB . LEU A 1 234 ? 18.257 37.279 16.812 1.00 24.94 ? 252 LEU A CB 1 ATOM 1887 C CG . LEU A 1 234 ? 18.933 36.165 17.639 1.00 24.97 ? 252 LEU A CG 1 ATOM 1888 C CD1 . LEU A 1 234 ? 20.417 36.045 17.238 1.00 27.36 ? 252 LEU A CD1 1 ATOM 1889 C CD2 . LEU A 1 234 ? 18.749 36.403 19.129 1.00 28.26 ? 252 LEU A CD2 1 ATOM 1890 N N . VAL A 1 235 ? 16.126 39.713 16.507 1.00 24.76 ? 253 VAL A N 1 ATOM 1891 C CA . VAL A 1 235 ? 15.799 40.854 15.636 1.00 25.44 ? 253 VAL A CA 1 ATOM 1892 C C . VAL A 1 235 ? 17.076 41.668 15.477 1.00 26.31 ? 253 VAL A C 1 ATOM 1893 O O . VAL A 1 235 ? 17.570 42.308 16.426 1.00 26.13 ? 253 VAL A O 1 ATOM 1894 C CB . VAL A 1 235 ? 14.618 41.687 16.160 1.00 26.62 ? 253 VAL A CB 1 ATOM 1895 C CG1 . VAL A 1 235 ? 14.245 42.751 15.145 1.00 26.17 ? 253 VAL A CG1 1 ATOM 1896 C CG2 . VAL A 1 235 ? 13.417 40.762 16.421 1.00 26.65 ? 253 VAL A CG2 1 ATOM 1897 N N . LEU A 1 236 ? 17.640 41.561 14.281 1.00 25.78 ? 254 LEU A N 1 ATOM 1898 C CA . LEU A 1 236 ? 18.998 42.012 14.016 1.00 25.65 ? 254 LEU A CA 1 ATOM 1899 C C . LEU A 1 236 ? 19.035 43.140 12.985 1.00 25.91 ? 254 LEU A C 1 ATOM 1900 O O . LEU A 1 236 ? 18.140 43.245 12.127 1.00 25.91 ? 254 LEU A O 1 ATOM 1901 C CB . LEU A 1 236 ? 19.846 40.838 13.508 1.00 25.76 ? 254 LEU A CB 1 ATOM 1902 C CG . LEU A 1 236 ? 20.028 39.649 14.443 1.00 25.04 ? 254 LEU A CG 1 ATOM 1903 C CD1 . LEU A 1 236 ? 20.853 38.586 13.745 1.00 26.11 ? 254 LEU A CD1 1 ATOM 1904 C CD2 . LEU A 1 236 ? 20.681 40.156 15.770 1.00 27.36 ? 254 LEU A CD2 1 ATOM 1905 N N . PRO A 1 237 ? 20.085 43.986 13.052 1.00 26.13 ? 255 PRO A N 1 ATOM 1906 C CA . PRO A 1 237 ? 20.307 45.020 12.062 1.00 26.40 ? 255 PRO A CA 1 ATOM 1907 C C . PRO A 1 237 ? 21.049 44.485 10.854 1.00 26.52 ? 255 PRO A C 1 ATOM 1908 O O . PRO A 1 237 ? 21.613 43.386 10.905 1.00 25.72 ? 255 PRO A O 1 ATOM 1909 C CB . PRO A 1 237 ? 21.206 45.985 12.789 1.00 26.61 ? 255 PRO A CB 1 ATOM 1910 C CG . PRO A 1 237 ? 22.022 45.139 13.647 1.00 27.16 ? 255 PRO A CG 1 ATOM 1911 C CD . PRO A 1 237 ? 21.106 44.046 14.115 1.00 26.52 ? 255 PRO A CD 1 ATOM 1912 N N . SER A 1 238 ? 21.046 45.255 9.774 1.00 26.53 ? 256 SER A N 1 ATOM 1913 C CA . SER A 1 238 ? 21.873 44.865 8.630 1.00 27.16 ? 256 SER A CA 1 ATOM 1914 C C . SER A 1 238 ? 23.309 44.758 9.109 1.00 27.21 ? 256 SER A C 1 ATOM 1915 O O . SER A 1 238 ? 23.786 45.545 9.957 1.00 27.43 ? 256 SER A O 1 ATOM 1916 C CB . SER A 1 238 ? 21.812 45.913 7.505 1.00 27.73 ? 256 SER A CB 1 ATOM 1917 O OG . SER A 1 238 ? 20.513 46.025 6.968 1.00 26.27 ? 256 SER A OG 1 ATOM 1918 N N . GLY A 1 239 ? 24.022 43.816 8.509 1.00 26.85 ? 257 GLY A N 1 ATOM 1919 C CA . GLY A 1 239 ? 25.434 43.665 8.791 1.00 26.25 ? 257 GLY A CA 1 ATOM 1920 C C . GLY A 1 239 ? 26.022 42.356 8.340 1.00 25.91 ? 257 GLY A C 1 ATOM 1921 O O . GLY A 1 239 ? 25.348 41.498 7.760 1.00 25.90 ? 257 GLY A O 1 ATOM 1922 N N . ASN A 1 240 ? 27.304 42.213 8.643 1.00 25.93 ? 258 ASN A N 1 ATOM 1923 C CA . ASN A 1 240 ? 28.020 40.994 8.336 1.00 25.80 ? 258 ASN A CA 1 ATOM 1924 C C . ASN A 1 240 ? 28.329 40.261 9.622 1.00 25.97 ? 258 ASN A C 1 ATOM 1925 O O . ASN A 1 240 ? 28.874 40.840 10.564 1.00 25.79 ? 258 ASN A O 1 ATOM 1926 C CB . ASN A 1 240 ? 29.302 41.311 7.588 1.00 26.20 ? 258 ASN A CB 1 ATOM 1927 C CG . ASN A 1 240 ? 29.789 40.139 6.777 1.00 27.95 ? 258 ASN A CG 1 ATOM 1928 O OD1 . ASN A 1 240 ? 29.015 39.235 6.444 1.00 29.68 ? 258 ASN A OD1 1 ATOM 1929 N ND2 . ASN A 1 240 ? 31.097 40.130 6.468 1.00 30.42 ? 258 ASN A ND2 1 ATOM 1930 N N . TYR A 1 241 ? 27.966 38.986 9.626 1.00 25.28 ? 259 TYR A N 1 ATOM 1931 C CA . TYR A 1 241 ? 27.981 38.136 10.805 1.00 25.06 ? 259 TYR A CA 1 ATOM 1932 C C . TYR A 1 241 ? 28.795 36.877 10.607 1.00 25.75 ? 259 TYR A C 1 ATOM 1933 O O . TYR A 1 241 ? 28.926 36.354 9.493 1.00 26.50 ? 259 TYR A O 1 ATOM 1934 C CB . TYR A 1 241 ? 26.533 37.714 11.165 1.00 24.92 ? 259 TYR A CB 1 ATOM 1935 C CG . TYR A 1 241 ? 25.603 38.864 11.564 1.00 26.47 ? 259 TYR A CG 1 ATOM 1936 C CD1 . TYR A 1 241 ? 25.248 39.069 12.900 1.00 27.70 ? 259 TYR A CD1 1 ATOM 1937 C CD2 . TYR A 1 241 ? 25.060 39.716 10.609 1.00 25.29 ? 259 TYR A CD2 1 ATOM 1938 C CE1 . TYR A 1 241 ? 24.391 40.102 13.269 1.00 25.31 ? 259 TYR A CE1 1 ATOM 1939 C CE2 . TYR A 1 241 ? 24.213 40.755 10.964 1.00 25.20 ? 259 TYR A CE2 1 ATOM 1940 C CZ . TYR A 1 241 ? 23.888 40.943 12.301 1.00 25.41 ? 259 TYR A CZ 1 ATOM 1941 O OH . TYR A 1 241 ? 23.067 41.964 12.695 1.00 25.51 ? 259 TYR A OH 1 ATOM 1942 N N . LEU A 1 242 ? 29.324 36.382 11.711 1.00 25.76 ? 260 LEU A N 1 ATOM 1943 C CA . LEU A 1 242 ? 29.807 35.004 11.796 1.00 26.15 ? 260 LEU A CA 1 ATOM 1944 C C . LEU A 1 242 ? 28.879 34.158 12.630 1.00 26.61 ? 260 LEU A C 1 ATOM 1945 O O . LEU A 1 242 ? 28.380 34.598 13.667 1.00 27.18 ? 260 LEU A O 1 ATOM 1946 C CB . LEU A 1 242 ? 31.207 34.941 12.408 1.00 25.89 ? 260 LEU A CB 1 ATOM 1947 C CG . LEU A 1 242 ? 32.262 35.766 11.690 1.00 28.53 ? 260 LEU A CG 1 ATOM 1948 C CD1 . LEU A 1 242 ? 33.616 35.618 12.409 1.00 30.78 ? 260 LEU A CD1 1 ATOM 1949 C CD2 . LEU A 1 242 ? 32.338 35.338 10.221 1.00 29.83 ? 260 LEU A CD2 1 ATOM 1950 N N . ALA A 1 243 ? 28.639 32.949 12.139 1.00 26.65 ? 261 ALA A N 1 ATOM 1951 C CA . ALA A 1 243 ? 27.997 31.889 12.902 1.00 26.59 ? 261 ALA A CA 1 ATOM 1952 C C . ALA A 1 243 ? 29.150 31.000 13.352 1.00 27.43 ? 261 ALA A C 1 ATOM 1953 O O . ALA A 1 243 ? 29.902 30.420 12.517 1.00 26.95 ? 261 ALA A O 1 ATOM 1954 C CB . ALA A 1 243 ? 26.978 31.101 12.055 1.00 26.66 ? 261 ALA A CB 1 ATOM 1955 N N . ILE A 1 244 ? 29.324 30.953 14.662 1.00 27.24 ? 262 ILE A N 1 ATOM 1956 C CA . ILE A 1 244 ? 30.443 30.238 15.289 1.00 27.85 ? 262 ILE A CA 1 ATOM 1957 C C . ILE A 1 244 ? 29.900 29.114 16.139 1.00 27.36 ? 262 ILE A C 1 ATOM 1958 O O . ILE A 1 244 ? 29.263 29.342 17.163 1.00 27.40 ? 262 ILE A O 1 ATOM 1959 C CB . ILE A 1 244 ? 31.316 31.163 16.137 1.00 28.28 ? 262 ILE A CB 1 ATOM 1960 C CG1 . ILE A 1 244 ? 31.884 32.303 15.293 1.00 30.84 ? 262 ILE A CG1 1 ATOM 1961 C CG2 . ILE A 1 244 ? 32.507 30.433 16.771 1.00 28.79 ? 262 ILE A CG2 1 ATOM 1962 C CD1 . ILE A 1 244 ? 32.330 33.462 16.128 1.00 32.77 ? 262 ILE A CD1 1 ATOM 1963 N N . SER A 1 245 ? 30.135 27.894 15.678 1.00 26.76 ? 263 SER A N 1 ATOM 1964 C CA . SER A 1 245 ? 29.696 26.674 16.381 1.00 27.20 ? 263 SER A CA 1 ATOM 1965 C C . SER A 1 245 ? 30.851 26.163 17.248 1.00 27.59 ? 263 SER A C 1 ATOM 1966 O O . SER A 1 245 ? 31.966 26.035 16.765 1.00 27.28 ? 263 SER A O 1 ATOM 1967 C CB . SER A 1 245 ? 29.265 25.581 15.384 1.00 27.56 ? 263 SER A CB 1 ATOM 1968 O OG . SER A 1 245 ? 28.820 24.387 16.027 1.00 28.08 ? 263 SER A OG 1 ATOM 1969 N N . ASN A 1 246 ? 30.558 25.857 18.510 1.00 27.54 ? 264 ASN A N 1 ATOM 1970 C CA . ASN A 1 246 ? 31.579 25.396 19.474 1.00 28.63 ? 264 ASN A CA 1 ATOM 1971 C C . ASN A 1 246 ? 31.434 23.930 19.861 1.00 28.69 ? 264 ASN A C 1 ATOM 1972 O O . ASN A 1 246 ? 32.283 23.375 20.562 1.00 28.84 ? 264 ASN A O 1 ATOM 1973 C CB . ASN A 1 246 ? 31.526 26.257 20.732 1.00 28.61 ? 264 ASN A CB 1 ATOM 1974 C CG . ASN A 1 246 ? 31.714 27.720 20.425 1.00 30.45 ? 264 ASN A CG 1 ATOM 1975 O OD1 . ASN A 1 246 ? 32.752 28.109 19.908 1.00 31.34 ? 264 ASN A OD1 1 ATOM 1976 N ND2 . ASN A 1 246 ? 30.683 28.539 20.691 1.00 31.50 ? 264 ASN A ND2 1 ATOM 1977 N N . GLU A 1 247 ? 30.329 23.343 19.428 1.00 28.49 ? 265 GLU A N 1 ATOM 1978 C CA . GLU A 1 247 ? 29.993 21.937 19.681 1.00 28.87 ? 265 GLU A CA 1 ATOM 1979 C C . GLU A 1 247 ? 28.840 21.486 18.815 1.00 28.73 ? 265 GLU A C 1 ATOM 1980 O O . GLU A 1 247 ? 27.977 22.268 18.444 1.00 28.55 ? 265 GLU A O 1 ATOM 1981 C CB . GLU A 1 247 ? 29.644 21.713 21.154 1.00 29.34 ? 265 GLU A CB 1 ATOM 1982 C CG . GLU A 1 247 ? 29.631 20.238 21.566 1.00 29.55 ? 265 GLU A CG 1 ATOM 1983 C CD . GLU A 1 247 ? 30.045 20.030 23.016 1.00 31.70 ? 265 GLU A CD 1 ATOM 1984 O OE1 . GLU A 1 247 ? 30.885 20.811 23.527 1.00 32.92 ? 265 GLU A OE1 1 ATOM 1985 O OE2 . GLU A 1 247 ? 29.534 19.083 23.650 1.00 32.50 ? 265 GLU A OE2 1 ATOM 1986 N N . LEU A 1 248 ? 28.846 20.205 18.500 1.00 28.39 ? 266 LEU A N 1 ATOM 1987 C CA . LEU A 1 248 ? 27.849 19.605 17.622 1.00 28.66 ? 266 LEU A CA 1 ATOM 1988 C C . LEU A 1 248 ? 27.912 20.195 16.211 1.00 29.04 ? 266 LEU A C 1 ATOM 1989 O O . LEU A 1 248 ? 28.965 20.556 15.710 1.00 30.09 ? 266 LEU A O 1 ATOM 1990 C CB . LEU A 1 248 ? 26.446 19.712 18.232 1.00 29.44 ? 266 LEU A CB 1 ATOM 1991 C CG . LEU A 1 248 ? 25.507 18.535 17.961 1.00 29.87 ? 266 LEU A CG 1 ATOM 1992 C CD1 . LEU A 1 248 ? 26.240 17.212 18.259 1.00 30.44 ? 266 LEU A CD1 1 ATOM 1993 C CD2 . LEU A 1 248 ? 24.177 18.628 18.752 1.00 30.94 ? 266 LEU A CD2 1 ATOM 1994 N N . LEU A 1 249 ? 26.778 20.260 15.545 1.00 29.51 ? 267 LEU A N 1 ATOM 1995 C CA . LEU A 1 249 ? 26.749 20.756 14.156 1.00 29.81 ? 267 LEU A CA 1 ATOM 1996 C C . LEU A 1 249 ? 26.622 22.283 14.092 1.00 29.39 ? 267 LEU A C 1 ATOM 1997 O O . LEU A 1 249 ? 25.854 22.884 14.817 1.00 28.98 ? 267 LEU A O 1 ATOM 1998 C CB . LEU A 1 249 ? 25.587 20.134 13.363 1.00 29.95 ? 267 LEU A CB 1 ATOM 1999 C CG . LEU A 1 249 ? 25.860 18.823 12.613 1.00 33.11 ? 267 LEU A CG 1 ATOM 2000 C CD1 . LEU A 1 249 ? 26.659 17.875 13.427 1.00 36.41 ? 267 LEU A CD1 1 ATOM 2001 C CD2 . LEU A 1 249 ? 24.550 18.178 12.093 1.00 36.41 ? 267 LEU A CD2 1 ATOM 2002 N N . LEU A 1 250 ? 27.391 22.883 13.200 1.00 28.76 ? 268 LEU A N 1 ATOM 2003 C CA . LEU A 1 250 ? 27.223 24.313 12.875 1.00 27.94 ? 268 LEU A CA 1 ATOM 2004 C C . LEU A 1 250 ? 25.837 24.585 12.291 1.00 27.52 ? 268 LEU A C 1 ATOM 2005 O O . LEU A 1 250 ? 25.378 23.883 11.393 1.00 26.87 ? 268 LEU A O 1 ATOM 2006 C CB . LEU A 1 250 ? 28.292 24.740 11.871 1.00 28.33 ? 268 LEU A CB 1 ATOM 2007 C CG . LEU A 1 250 ? 28.168 26.128 11.235 1.00 27.95 ? 268 LEU A CG 1 ATOM 2008 C CD1 . LEU A 1 250 ? 28.258 27.250 12.264 1.00 26.12 ? 268 LEU A CD1 1 ATOM 2009 C CD2 . LEU A 1 250 ? 29.252 26.271 10.147 1.00 29.26 ? 268 LEU A CD2 1 ATOM 2010 N N . THR A 1 251 ? 25.173 25.604 12.832 1.00 26.89 ? 269 THR A N 1 ATOM 2011 C CA . THR A 1 251 ? 23.901 26.068 12.305 1.00 27.32 ? 269 THR A CA 1 ATOM 2012 C C . THR A 1 251 ? 23.970 27.545 11.929 1.00 27.25 ? 269 THR A C 1 ATOM 2013 O O . THR A 1 251 ? 24.622 28.367 12.587 1.00 27.71 ? 269 THR A O 1 ATOM 2014 C CB . THR A 1 251 ? 22.739 25.787 13.288 1.00 27.51 ? 269 THR A CB 1 ATOM 2015 O OG1 . THR A 1 251 ? 22.975 26.456 14.532 1.00 27.22 ? 269 THR A OG1 1 ATOM 2016 C CG2 . THR A 1 251 ? 22.621 24.309 13.540 1.00 28.10 ? 269 THR A CG2 1 ATOM 2017 N N . VAL A 1 252 ? 23.311 27.857 10.831 1.00 27.07 ? 270 VAL A N 1 ATOM 2018 C CA . VAL A 1 252 ? 23.388 29.178 10.231 1.00 27.15 ? 270 VAL A CA 1 ATOM 2019 C C . VAL A 1 252 ? 22.057 29.527 9.570 1.00 26.41 ? 270 VAL A C 1 ATOM 2020 O O . VAL A 1 252 ? 21.443 28.672 8.938 1.00 25.43 ? 270 VAL A O 1 ATOM 2021 C CB . VAL A 1 252 ? 24.533 29.199 9.179 1.00 27.75 ? 270 VAL A CB 1 ATOM 2022 C CG1 . VAL A 1 252 ? 24.252 28.186 8.084 1.00 29.45 ? 270 VAL A CG1 1 ATOM 2023 C CG2 . VAL A 1 252 ? 24.748 30.608 8.578 1.00 28.73 ? 270 VAL A CG2 1 ATOM 2024 N N . PRO A 1 253 ? 21.610 30.784 9.706 1.00 26.16 ? 271 PRO A N 1 ATOM 2025 C CA . PRO A 1 253 ? 20.362 31.172 9.029 1.00 26.61 ? 271 PRO A CA 1 ATOM 2026 C C . PRO A 1 253 ? 20.448 31.128 7.512 1.00 26.76 ? 271 PRO A C 1 ATOM 2027 O O . PRO A 1 253 ? 21.489 31.452 6.936 1.00 25.98 ? 271 PRO A O 1 ATOM 2028 C CB . PRO A 1 253 ? 20.155 32.628 9.490 1.00 26.91 ? 271 PRO A CB 1 ATOM 2029 C CG . PRO A 1 253 ? 21.044 32.822 10.668 1.00 27.47 ? 271 PRO A CG 1 ATOM 2030 C CD . PRO A 1 253 ? 22.210 31.908 10.452 1.00 25.73 ? 271 PRO A CD 1 ATOM 2031 N N . THR A 1 254 ? 19.338 30.721 6.897 1.00 26.98 ? 272 THR A N 1 ATOM 2032 C CA . THR A 1 254 ? 19.170 30.664 5.453 1.00 27.12 ? 272 THR A CA 1 ATOM 2033 C C . THR A 1 254 ? 18.028 31.543 4.941 1.00 26.83 ? 272 THR A C 1 ATOM 2034 O O . THR A 1 254 ? 17.940 31.839 3.752 1.00 26.72 ? 272 THR A O 1 ATOM 2035 C CB . THR A 1 254 ? 18.919 29.215 4.976 1.00 27.74 ? 272 THR A CB 1 ATOM 2036 O OG1 . THR A 1 254 ? 17.643 28.777 5.452 1.00 27.81 ? 272 THR A OG1 1 ATOM 2037 C CG2 . THR A 1 254 ? 20.030 28.288 5.498 1.00 28.95 ? 272 THR A CG2 1 ATOM 2038 N N . LYS A 1 255 ? 17.159 31.938 5.863 1.00 26.91 ? 273 LYS A N 1 ATOM 2039 C CA . LYS A 1 255 ? 16.020 32.814 5.583 1.00 27.05 ? 273 LYS A CA 1 ATOM 2040 C C . LYS A 1 255 ? 15.828 33.764 6.747 1.00 26.86 ? 273 LYS A C 1 ATOM 2041 O O . LYS A 1 255 ? 16.088 33.405 7.904 1.00 26.55 ? 273 LYS A O 1 ATOM 2042 C CB . LYS A 1 255 ? 14.720 32.009 5.409 1.00 27.79 ? 273 LYS A CB 1 ATOM 2043 C CG . LYS A 1 255 ? 14.641 31.220 4.133 1.00 28.55 ? 273 LYS A CG 1 ATOM 2044 C CD . LYS A 1 255 ? 13.323 30.395 4.070 1.00 28.10 ? 273 LYS A CD 1 ATOM 2045 C CE . LYS A 1 255 ? 13.434 29.091 4.843 1.00 27.29 ? 273 LYS A CE 1 ATOM 2046 N NZ . LYS A 1 255 ? 12.353 28.132 4.515 1.00 24.48 ? 273 LYS A NZ 1 ATOM 2047 N N . ALA A 1 256 ? 15.394 34.965 6.421 1.00 25.96 ? 274 ALA A N 1 ATOM 2048 C CA . ALA A 1 256 ? 14.985 35.964 7.433 1.00 26.12 ? 274 ALA A CA 1 ATOM 2049 C C . ALA A 1 256 ? 13.643 36.564 7.111 1.00 25.62 ? 274 ALA A C 1 ATOM 2050 O O . ALA A 1 256 ? 13.244 36.656 5.952 1.00 26.03 ? 274 ALA A O 1 ATOM 2051 C CB . ALA A 1 256 ? 16.029 37.094 7.522 1.00 26.45 ? 274 ALA A CB 1 ATOM 2052 N N . ILE A 1 257 ? 12.924 36.975 8.153 1.00 26.35 ? 275 ILE A N 1 ATOM 2053 C CA . ILE A 1 257 ? 11.828 37.921 7.962 1.00 26.64 ? 275 ILE A CA 1 ATOM 2054 C C . ILE A 1 257 ? 12.455 39.298 7.771 1.00 27.19 ? 275 ILE A C 1 ATOM 2055 O O . ILE A 1 257 ? 13.212 39.779 8.611 1.00 27.20 ? 275 ILE A O 1 ATOM 2056 C CB . ILE A 1 257 ? 10.842 37.999 9.163 1.00 27.35 ? 275 ILE A CB 1 ATOM 2057 C CG1 . ILE A 1 257 ? 10.165 36.650 9.419 1.00 27.74 ? 275 ILE A CG1 1 ATOM 2058 C CG2 . ILE A 1 257 ? 9.816 39.081 8.892 1.00 27.35 ? 275 ILE A CG2 1 ATOM 2059 C CD1 . ILE A 1 257 ? 9.403 36.161 8.268 1.00 29.06 ? 275 ILE A CD1 1 ATOM 2060 N N . CYS A 1 258 ? 12.117 39.905 6.644 1.00 27.30 ? 276 CYS A N 1 ATOM 2061 C CA . CYS A 1 258 ? 12.605 41.205 6.228 1.00 28.27 ? 276 CYS A CA 1 ATOM 2062 C C . CYS A 1 258 ? 11.606 42.260 6.654 1.00 27.61 ? 276 CYS A C 1 ATOM 2063 O O . CYS A 1 258 ? 10.491 42.301 6.146 1.00 30.47 ? 276 CYS A O 1 ATOM 2064 C CB . CYS A 1 258 ? 12.764 41.214 4.701 1.00 29.41 ? 276 CYS A CB 1 ATOM 2065 S SG . CYS A 1 258 ? 13.347 42.762 4.017 1.00 34.81 ? 276 CYS A SG 1 ATOM 2066 N N . LEU A 1 259 ? 12.033 43.104 7.582 1.00 26.09 ? 277 LEU A N 1 ATOM 2067 C CA . LEU A 1 259 ? 11.237 44.231 8.106 1.00 26.29 ? 277 LEU A CA 1 ATOM 2068 C C . LEU A 1 259 ? 11.703 45.570 7.494 1.00 26.21 ? 277 LEU A C 1 ATOM 2069 O O . LEU A 1 259 ? 12.856 45.958 7.595 1.00 25.96 ? 277 LEU A O 1 ATOM 2070 C CB . LEU A 1 259 ? 11.321 44.280 9.635 1.00 26.83 ? 277 LEU A CB 1 ATOM 2071 C CG . LEU A 1 259 ? 10.958 43.028 10.458 1.00 26.13 ? 277 LEU A CG 1 ATOM 2072 C CD1 . LEU A 1 259 ? 11.551 43.127 11.896 1.00 23.81 ? 277 LEU A CD1 1 ATOM 2073 C CD2 . LEU A 1 259 ? 9.409 42.790 10.441 1.00 26.61 ? 277 LEU A CD2 1 ATOM 2074 N N . ASN A 1 260 ? 10.791 46.257 6.838 1.00 26.84 ? 278 ASN A N 1 ATOM 2075 C CA . ASN A 1 260 ? 11.092 47.524 6.190 1.00 27.15 ? 278 ASN A CA 1 ATOM 2076 C C . ASN A 1 260 ? 10.016 48.581 6.407 1.00 27.59 ? 278 ASN A C 1 ATOM 2077 O O . ASN A 1 260 ? 8.837 48.280 6.630 1.00 27.32 ? 278 ASN A O 1 ATOM 2078 C CB . ASN A 1 260 ? 11.260 47.329 4.694 1.00 27.94 ? 278 ASN A CB 1 ATOM 2079 C CG . ASN A 1 260 ? 12.702 47.129 4.289 1.00 30.08 ? 278 ASN A CG 1 ATOM 2080 O OD1 . ASN A 1 260 ? 13.616 47.775 4.823 1.00 29.71 ? 278 ASN A OD1 1 ATOM 2081 N ND2 . ASN A 1 260 ? 12.914 46.247 3.314 1.00 32.08 ? 278 ASN A ND2 1 ATOM 2082 N N . LYS A 1 261 ? 10.476 49.822 6.312 1.00 27.66 ? 279 LYS A N 1 ATOM 2083 C CA . LYS A 1 261 ? 9.640 51.032 6.355 1.00 28.11 ? 279 LYS A CA 1 ATOM 2084 C C . LYS A 1 261 ? 9.057 51.249 7.725 1.00 27.54 ? 279 LYS A C 1 ATOM 2085 O O . LYS A 1 261 ? 7.925 50.894 8.020 1.00 27.12 ? 279 LYS A O 1 ATOM 2086 C CB . LYS A 1 261 ? 8.537 51.022 5.291 1.00 27.98 ? 279 LYS A CB 1 ATOM 2087 C CG . LYS A 1 261 ? 9.052 50.914 3.847 1.00 32.53 ? 279 LYS A CG 1 ATOM 2088 C CD . LYS A 1 261 ? 7.902 50.931 2.820 1.00 34.39 ? 279 LYS A CD 1 ATOM 2089 C CE . LYS A 1 261 ? 8.432 50.883 1.377 1.00 37.12 ? 279 LYS A CE 1 ATOM 2090 N NZ . LYS A 1 261 ? 7.347 50.765 0.344 1.00 39.55 ? 279 LYS A NZ 1 ATOM 2091 N N . ARG A 1 262 ? 9.862 51.867 8.566 1.00 28.04 ? 280 ARG A N 1 ATOM 2092 C CA . ARG A 1 262 ? 9.419 52.201 9.915 1.00 28.54 ? 280 ARG A CA 1 ATOM 2093 C C . ARG A 1 262 ? 8.133 53.062 9.868 1.00 28.04 ? 280 ARG A C 1 ATOM 2094 O O . ARG A 1 262 ? 7.963 53.959 9.025 1.00 27.30 ? 280 ARG A O 1 ATOM 2095 C CB . ARG A 1 262 ? 10.572 52.902 10.662 1.00 29.88 ? 280 ARG A CB 1 ATOM 2096 C CG . ARG A 1 262 ? 10.354 52.999 12.134 1.00 32.02 ? 280 ARG A CG 1 ATOM 2097 C CD . ARG A 1 262 ? 10.867 51.746 12.871 1.00 35.07 ? 280 ARG A CD 1 ATOM 2098 N NE . ARG A 1 262 ? 10.488 51.856 14.277 1.00 35.93 ? 280 ARG A NE 1 ATOM 2099 C CZ . ARG A 1 262 ? 10.919 51.076 15.251 1.00 37.06 ? 280 ARG A CZ 1 ATOM 2100 N NH1 . ARG A 1 262 ? 11.783 50.108 15.014 1.00 36.56 ? 280 ARG A NH1 1 ATOM 2101 N NH2 . ARG A 1 262 ? 10.473 51.285 16.475 1.00 37.90 ? 280 ARG A NH2 1 ATOM 2102 N N . LYS A 1 263 ? 7.213 52.780 10.777 1.00 27.72 ? 281 LYS A N 1 ATOM 2103 C CA . LYS A 1 263 ? 5.963 53.528 10.863 1.00 27.87 ? 281 LYS A CA 1 ATOM 2104 C C . LYS A 1 263 ? 5.643 53.881 12.301 1.00 27.68 ? 281 LYS A C 1 ATOM 2105 O O . LYS A 1 263 ? 6.159 53.280 13.234 1.00 27.86 ? 281 LYS A O 1 ATOM 2106 C CB . LYS A 1 263 ? 4.796 52.740 10.278 1.00 28.41 ? 281 LYS A CB 1 ATOM 2107 C CG . LYS A 1 263 ? 4.376 51.546 11.122 1.00 28.23 ? 281 LYS A CG 1 ATOM 2108 C CD . LYS A 1 263 ? 3.426 50.591 10.374 1.00 26.93 ? 281 LYS A CD 1 ATOM 2109 C CE . LYS A 1 263 ? 3.054 49.402 11.268 1.00 26.95 ? 281 LYS A CE 1 ATOM 2110 N NZ . LYS A 1 263 ? 2.395 48.325 10.463 1.00 24.75 ? 281 LYS A NZ 1 ATOM 2111 N N . ASP A 1 264 ? 4.762 54.854 12.457 1.00 28.15 ? 282 ASP A N 1 ATOM 2112 C CA . ASP A 1 264 ? 4.254 55.170 13.793 1.00 28.94 ? 282 ASP A CA 1 ATOM 2113 C C . ASP A 1 264 ? 3.584 53.904 14.349 1.00 28.20 ? 282 ASP A C 1 ATOM 2114 O O . ASP A 1 264 ? 2.911 53.155 13.620 1.00 27.51 ? 282 ASP A O 1 ATOM 2115 C CB . ASP A 1 264 ? 3.267 56.336 13.756 1.00 29.51 ? 282 ASP A CB 1 ATOM 2116 C CG . ASP A 1 264 ? 3.930 57.653 13.401 1.00 32.69 ? 282 ASP A CG 1 ATOM 2117 O OD1 . ASP A 1 264 ? 5.161 57.766 13.524 1.00 35.66 ? 282 ASP A OD1 1 ATOM 2118 O OD2 . ASP A 1 264 ? 3.196 58.568 12.995 1.00 39.96 ? 282 ASP A OD2 1 ATOM 2119 N N . PHE A 1 265 ? 3.798 53.682 15.639 1.00 27.53 ? 283 PHE A N 1 ATOM 2120 C CA . PHE A 1 265 ? 3.221 52.533 16.346 1.00 26.96 ? 283 PHE A CA 1 ATOM 2121 C C . PHE A 1 265 ? 1.736 52.335 16.030 1.00 26.53 ? 283 PHE A C 1 ATOM 2122 O O . PHE A 1 265 ? 0.893 53.183 16.328 1.00 26.44 ? 283 PHE A O 1 ATOM 2123 C CB . PHE A 1 265 ? 3.378 52.694 17.873 1.00 27.06 ? 283 PHE A CB 1 ATOM 2124 C CG . PHE A 1 265 ? 3.026 51.461 18.649 1.00 26.53 ? 283 PHE A CG 1 ATOM 2125 C CD1 . PHE A 1 265 ? 3.936 50.439 18.791 1.00 28.69 ? 283 PHE A CD1 1 ATOM 2126 C CD2 . PHE A 1 265 ? 1.785 51.323 19.238 1.00 26.18 ? 283 PHE A CD2 1 ATOM 2127 C CE1 . PHE A 1 265 ? 3.627 49.295 19.530 1.00 26.99 ? 283 PHE A CE1 1 ATOM 2128 C CE2 . PHE A 1 265 ? 1.463 50.180 19.954 1.00 26.50 ? 283 PHE A CE2 1 ATOM 2129 C CZ . PHE A 1 265 ? 2.408 49.157 20.093 1.00 25.34 ? 283 PHE A CZ 1 ATOM 2130 N N . THR A 1 266 ? 1.438 51.186 15.464 1.00 25.87 ? 284 THR A N 1 ATOM 2131 C CA . THR A 1 266 ? 0.070 50.818 15.060 1.00 25.89 ? 284 THR A CA 1 ATOM 2132 C C . THR A 1 266 ? -0.191 49.346 15.414 1.00 25.24 ? 284 THR A C 1 ATOM 2133 O O . THR A 1 266 ? 0.389 48.443 14.795 1.00 25.72 ? 284 THR A O 1 ATOM 2134 C CB . THR A 1 266 ? -0.093 50.981 13.529 1.00 26.28 ? 284 THR A CB 1 ATOM 2135 O OG1 . THR A 1 266 ? 0.267 52.308 13.137 1.00 27.17 ? 284 THR A OG1 1 ATOM 2136 C CG2 . THR A 1 266 ? -1.499 50.625 13.066 1.00 24.59 ? 284 THR A CG2 1 ATOM 2137 N N . PRO A 1 267 ? -1.046 49.082 16.412 1.00 25.35 ? 285 PRO A N 1 ATOM 2138 C CA . PRO A 1 267 ? -1.254 47.697 16.829 1.00 25.38 ? 285 PRO A CA 1 ATOM 2139 C C . PRO A 1 267 ? -1.720 46.786 15.708 1.00 26.03 ? 285 PRO A C 1 ATOM 2140 O O . PRO A 1 267 ? -2.534 47.170 14.855 1.00 25.71 ? 285 PRO A O 1 ATOM 2141 C CB . PRO A 1 267 ? -2.318 47.789 17.927 1.00 25.28 ? 285 PRO A CB 1 ATOM 2142 C CG . PRO A 1 267 ? -2.205 49.221 18.451 1.00 25.86 ? 285 PRO A CG 1 ATOM 2143 C CD . PRO A 1 267 ? -1.707 50.053 17.296 1.00 25.75 ? 285 PRO A CD 1 ATOM 2144 N N . VAL A 1 268 ? -1.172 45.576 15.722 1.00 26.26 ? 286 VAL A N 1 ATOM 2145 C CA . VAL A 1 268 ? -1.589 44.541 14.772 1.00 26.78 ? 286 VAL A CA 1 ATOM 2146 C C . VAL A 1 268 ? -2.835 43.877 15.284 1.00 26.37 ? 286 VAL A C 1 ATOM 2147 O O . VAL A 1 268 ? -3.193 43.998 16.473 1.00 26.49 ? 286 VAL A O 1 ATOM 2148 C CB . VAL A 1 268 ? -0.478 43.468 14.524 1.00 27.79 ? 286 VAL A CB 1 ATOM 2149 C CG1 . VAL A 1 268 ? 0.829 44.106 14.125 1.00 26.66 ? 286 VAL A CG1 1 ATOM 2150 C CG2 . VAL A 1 268 ? -0.316 42.550 15.729 1.00 28.96 ? 286 VAL A CG2 1 ATOM 2151 N N . GLN A 1 269 ? -3.539 43.222 14.360 1.00 25.86 ? 287 GLN A N 1 ATOM 2152 C CA . GLN A 1 269 ? -4.733 42.447 14.682 1.00 25.87 ? 287 GLN A CA 1 ATOM 2153 C C . GLN A 1 269 ? -4.513 41.005 14.316 1.00 26.10 ? 287 GLN A C 1 ATOM 2154 O O . GLN A 1 269 ? -4.054 40.696 13.206 1.00 27.22 ? 287 GLN A O 1 ATOM 2155 C CB . GLN A 1 269 ? -5.934 42.961 13.884 1.00 25.04 ? 287 GLN A CB 1 ATOM 2156 C CG . GLN A 1 269 ? -6.330 44.364 14.230 1.00 24.60 ? 287 GLN A CG 1 ATOM 2157 C CD . GLN A 1 269 ? -7.298 44.944 13.222 1.00 26.74 ? 287 GLN A CD 1 ATOM 2158 O OE1 . GLN A 1 269 ? -8.499 44.644 13.250 1.00 27.54 ? 287 GLN A OE1 1 ATOM 2159 N NE2 . GLN A 1 269 ? -6.785 45.778 12.318 1.00 26.33 ? 287 GLN A NE2 1 ATOM 2160 N N . VAL A 1 270 ? -4.762 40.125 15.277 1.00 25.84 ? 288 VAL A N 1 ATOM 2161 C CA . VAL A 1 270 ? -4.525 38.685 15.103 1.00 26.47 ? 288 VAL A CA 1 ATOM 2162 C C . VAL A 1 270 ? -5.801 37.894 15.369 1.00 26.51 ? 288 VAL A C 1 ATOM 2163 O O . VAL A 1 270 ? -6.434 38.092 16.401 1.00 26.24 ? 288 VAL A O 1 ATOM 2164 C CB . VAL A 1 270 ? -3.402 38.188 16.030 1.00 26.93 ? 288 VAL A CB 1 ATOM 2165 C CG1 . VAL A 1 270 ? -3.277 36.675 16.004 1.00 27.22 ? 288 VAL A CG1 1 ATOM 2166 C CG2 . VAL A 1 270 ? -2.059 38.844 15.643 1.00 26.37 ? 288 VAL A CG2 1 ATOM 2167 N N . VAL A 1 271 ? -6.147 37.039 14.400 1.00 26.98 ? 289 VAL A N 1 ATOM 2168 C CA . VAL A 1 271 ? -7.284 36.112 14.492 1.00 27.46 ? 289 VAL A CA 1 ATOM 2169 C C . VAL A 1 271 ? -6.788 34.708 14.804 1.00 27.79 ? 289 VAL A C 1 ATOM 2170 O O . VAL A 1 271 ? -5.873 34.167 14.158 1.00 27.81 ? 289 VAL A O 1 ATOM 2171 C CB . VAL A 1 271 ? -8.084 36.102 13.176 1.00 27.60 ? 289 VAL A CB 1 ATOM 2172 C CG1 . VAL A 1 271 ? -9.353 35.242 13.318 1.00 26.45 ? 289 VAL A CG1 1 ATOM 2173 C CG2 . VAL A 1 271 ? -8.427 37.548 12.756 1.00 27.15 ? 289 VAL A CG2 1 ATOM 2174 N N . ASP A 1 272 ? -7.395 34.130 15.822 1.00 28.09 ? 290 ASP A N 1 ATOM 2175 C CA . ASP A 1 272 ? -7.074 32.766 16.245 1.00 28.58 ? 290 ASP A CA 1 ATOM 2176 C C . ASP A 1 272 ? -7.181 31.826 15.055 1.00 29.05 ? 290 ASP A C 1 ATOM 2177 O O . ASP A 1 272 ? -8.213 31.784 14.368 1.00 29.76 ? 290 ASP A O 1 ATOM 2178 C CB . ASP A 1 272 ? -8.006 32.314 17.365 1.00 28.59 ? 290 ASP A CB 1 ATOM 2179 C CG . ASP A 1 272 ? -7.560 31.010 18.018 1.00 30.14 ? 290 ASP A CG 1 ATOM 2180 O OD1 . ASP A 1 272 ? -6.350 30.750 18.066 1.00 30.99 ? 290 ASP A OD1 1 ATOM 2181 O OD2 . ASP A 1 272 ? -8.424 30.246 18.520 1.00 32.33 ? 290 ASP A OD2 1 ATOM 2182 N N . SER A 1 273 ? -6.087 31.107 14.821 1.00 28.57 ? 291 SER A N 1 ATOM 2183 C CA . SER A 1 273 ? -5.982 30.151 13.727 1.00 28.61 ? 291 SER A CA 1 ATOM 2184 C C . SER A 1 273 ? -5.915 28.741 14.278 1.00 29.17 ? 291 SER A C 1 ATOM 2185 O O . SER A 1 273 ? -4.875 28.295 14.799 1.00 29.71 ? 291 SER A O 1 ATOM 2186 C CB . SER A 1 273 ? -4.758 30.473 12.843 1.00 28.42 ? 291 SER A CB 1 ATOM 2187 O OG . SER A 1 273 ? -4.670 29.593 11.737 1.00 26.89 ? 291 SER A OG 1 ATOM 2188 N N . ARG A 1 274 ? -7.053 28.049 14.170 1.00 28.63 ? 292 ARG A N 1 ATOM 2189 C CA . ARG A 1 274 ? -7.202 26.713 14.737 1.00 28.14 ? 292 ARG A CA 1 ATOM 2190 C C . ARG A 1 274 ? -8.010 25.798 13.846 1.00 28.52 ? 292 ARG A C 1 ATOM 2191 O O . ARG A 1 274 ? -8.711 26.225 12.951 1.00 27.97 ? 292 ARG A O 1 ATOM 2192 C CB . ARG A 1 274 ? -7.871 26.762 16.119 1.00 28.15 ? 292 ARG A CB 1 ATOM 2193 C CG . ARG A 1 274 ? -9.150 27.618 16.197 1.00 28.62 ? 292 ARG A CG 1 ATOM 2194 C CD . ARG A 1 274 ? -9.853 27.503 17.579 1.00 28.51 ? 292 ARG A CD 1 ATOM 2195 N NE . ARG A 1 274 ? -10.750 28.617 17.906 1.00 28.35 ? 292 ARG A NE 1 ATOM 2196 C CZ . ARG A 1 274 ? -12.081 28.582 17.802 1.00 30.33 ? 292 ARG A CZ 1 ATOM 2197 N NH1 . ARG A 1 274 ? -12.684 27.489 17.369 1.00 29.03 ? 292 ARG A NH1 1 ATOM 2198 N NH2 . ARG A 1 274 ? -12.811 29.641 18.143 1.00 30.42 ? 292 ARG A NH2 1 ATOM 2199 N N . TRP A 1 275 ? -7.876 24.524 14.169 1.00 28.68 ? 293 TRP A N 1 ATOM 2200 C CA . TRP A 1 275 ? -8.617 23.453 13.531 1.00 28.78 ? 293 TRP A CA 1 ATOM 2201 C C . TRP A 1 275 ? -9.937 23.281 14.251 1.00 29.15 ? 293 TRP A C 1 ATOM 2202 O O . TRP A 1 275 ? -10.112 23.720 15.390 1.00 29.44 ? 293 TRP A O 1 ATOM 2203 C CB . TRP A 1 275 ? -7.890 22.121 13.679 1.00 28.55 ? 293 TRP A CB 1 ATOM 2204 C CG . TRP A 1 275 ? -6.531 22.011 13.073 1.00 27.87 ? 293 TRP A CG 1 ATOM 2205 C CD1 . TRP A 1 275 ? -5.377 21.803 13.736 1.00 29.05 ? 293 TRP A CD1 1 ATOM 2206 C CD2 . TRP A 1 275 ? -6.205 22.020 11.686 1.00 29.14 ? 293 TRP A CD2 1 ATOM 2207 N NE1 . TRP A 1 275 ? -4.332 21.696 12.856 1.00 29.38 ? 293 TRP A NE1 1 ATOM 2208 C CE2 . TRP A 1 275 ? -4.814 21.829 11.586 1.00 29.35 ? 293 TRP A CE2 1 ATOM 2209 C CE3 . TRP A 1 275 ? -6.951 22.179 10.517 1.00 31.40 ? 293 TRP A CE3 1 ATOM 2210 C CZ2 . TRP A 1 275 ? -4.151 21.796 10.365 1.00 30.27 ? 293 TRP A CZ2 1 ATOM 2211 C CZ3 . TRP A 1 275 ? -6.289 22.144 9.298 1.00 32.20 ? 293 TRP A CZ3 1 ATOM 2212 C CH2 . TRP A 1 275 ? -4.904 21.966 9.235 1.00 30.60 ? 293 TRP A CH2 1 ATOM 2213 N N . ASN A 1 276 ? -10.845 22.610 13.571 1.00 29.63 ? 294 ASN A N 1 ATOM 2214 C CA . ASN A 1 276 ? -11.994 21.988 14.226 1.00 29.81 ? 294 ASN A CA 1 ATOM 2215 C C . ASN A 1 276 ? -11.487 21.177 15.423 1.00 30.10 ? 294 ASN A C 1 ATOM 2216 O O . ASN A 1 276 ? -10.390 20.633 15.391 1.00 30.29 ? 294 ASN A O 1 ATOM 2217 C CB . ASN A 1 276 ? -12.745 21.100 13.225 1.00 30.11 ? 294 ASN A CB 1 ATOM 2218 C CG . ASN A 1 276 ? -13.870 20.297 13.863 1.00 31.04 ? 294 ASN A CG 1 ATOM 2219 O OD1 . ASN A 1 276 ? -13.660 19.165 14.290 1.00 32.89 ? 294 ASN A OD1 1 ATOM 2220 N ND2 . ASN A 1 276 ? -15.070 20.866 13.901 1.00 29.99 ? 294 ASN A ND2 1 ATOM 2221 N N . ASN A 1 277 ? -12.308 21.095 16.464 1.00 30.65 ? 295 ASN A N 1 ATOM 2222 C CA . ASN A 1 277 ? -11.893 20.541 17.762 1.00 31.04 ? 295 ASN A CA 1 ATOM 2223 C C . ASN A 1 277 ? -11.388 19.102 17.702 1.00 31.51 ? 295 ASN A C 1 ATOM 2224 O O . ASN A 1 277 ? -10.737 18.632 18.643 1.00 31.44 ? 295 ASN A O 1 ATOM 2225 C CB . ASN A 1 277 ? -13.021 20.618 18.804 1.00 31.65 ? 295 ASN A CB 1 ATOM 2226 C CG . ASN A 1 277 ? -13.201 22.018 19.396 1.00 32.75 ? 295 ASN A CG 1 ATOM 2227 O OD1 . ASN A 1 277 ? -14.146 22.244 20.152 1.00 33.82 ? 295 ASN A OD1 1 ATOM 2228 N ND2 . ASN A 1 277 ? -12.302 22.952 19.069 1.00 30.29 ? 295 ASN A ND2 1 ATOM 2229 N N . ALA A 1 278 ? -11.692 18.409 16.608 1.00 31.89 ? 296 ALA A N 1 ATOM 2230 C CA . ALA A 1 278 ? -11.304 16.999 16.449 1.00 32.21 ? 296 ALA A CA 1 ATOM 2231 C C . ALA A 1 278 ? -9.794 16.869 16.326 1.00 32.76 ? 296 ALA A C 1 ATOM 2232 O O . ALA A 1 278 ? -9.236 15.773 16.398 1.00 33.12 ? 296 ALA A O 1 ATOM 2233 C CB . ALA A 1 278 ? -11.974 16.375 15.230 1.00 32.32 ? 296 ALA A CB 1 ATOM 2234 N N . ARG A 1 279 ? -9.149 18.010 16.112 1.00 32.81 ? 297 ARG A N 1 ATOM 2235 C CA . ARG A 1 279 ? -7.693 18.087 15.931 1.00 32.44 ? 297 ARG A CA 1 ATOM 2236 C C . ARG A 1 279 ? -7.133 18.994 16.994 1.00 32.14 ? 297 ARG A C 1 ATOM 2237 O O . ARG A 1 279 ? -7.804 19.929 17.434 1.00 32.38 ? 297 ARG A O 1 ATOM 2238 C CB . ARG A 1 279 ? -7.310 18.659 14.560 1.00 32.58 ? 297 ARG A CB 1 ATOM 2239 C CG . ARG A 1 279 ? -7.547 17.754 13.389 1.00 33.21 ? 297 ARG A CG 1 ATOM 2240 C CD . ARG A 1 279 ? -7.153 18.445 12.091 1.00 34.03 ? 297 ARG A CD 1 ATOM 2241 N NE . ARG A 1 279 ? -7.473 17.594 10.954 1.00 35.36 ? 297 ARG A NE 1 ATOM 2242 C CZ . ARG A 1 279 ? -7.139 17.838 9.693 1.00 36.38 ? 297 ARG A CZ 1 ATOM 2243 N NH1 . ARG A 1 279 ? -6.471 18.929 9.371 1.00 36.58 ? 297 ARG A NH1 1 ATOM 2244 N NH2 . ARG A 1 279 ? -7.486 16.973 8.747 1.00 38.00 ? 297 ARG A NH2 1 ATOM 2245 N N . GLN A 1 280 ? -5.905 18.703 17.403 1.00 31.90 ? 298 GLN A N 1 ATOM 2246 C CA . GLN A 1 280 ? -5.245 19.478 18.460 1.00 32.07 ? 298 GLN A CA 1 ATOM 2247 C C . GLN A 1 280 ? -4.622 20.749 17.901 1.00 31.44 ? 298 GLN A C 1 ATOM 2248 O O . GLN A 1 280 ? -3.785 20.709 17.009 1.00 31.06 ? 298 GLN A O 1 ATOM 2249 C CB . GLN A 1 280 ? -4.164 18.659 19.163 1.00 32.26 ? 298 GLN A CB 1 ATOM 2250 C CG . GLN A 1 280 ? -3.908 19.145 20.582 1.00 35.71 ? 298 GLN A CG 1 ATOM 2251 C CD . GLN A 1 280 ? -2.744 18.436 21.269 1.00 37.99 ? 298 GLN A CD 1 ATOM 2252 O OE1 . GLN A 1 280 ? -2.275 17.379 20.825 1.00 40.75 ? 298 GLN A OE1 1 ATOM 2253 N NE2 . GLN A 1 280 ? -2.263 19.034 22.355 1.00 39.32 ? 298 GLN A NE2 1 ATOM 2254 N N . SER A 1 281 ? -5.052 21.865 18.463 1.00 31.58 ? 299 SER A N 1 ATOM 2255 C CA . SER A 1 281 ? -4.511 23.166 18.133 1.00 31.59 ? 299 SER A CA 1 ATOM 2256 C C . SER A 1 281 ? -3.685 23.645 19.302 1.00 31.71 ? 299 SER A C 1 ATOM 2257 O O . SER A 1 281 ? -3.415 22.884 20.206 1.00 32.90 ? 299 SER A O 1 ATOM 2258 C CB . SER A 1 281 ? -5.635 24.152 17.841 1.00 31.46 ? 299 SER A CB 1 ATOM 2259 O OG . SER A 1 281 ? -6.385 23.715 16.724 1.00 31.73 ? 299 SER A OG 1 ATOM 2260 N N . ASP A 1 282 ? -3.285 24.907 19.270 1.00 31.04 ? 300 ASP A N 1 ATOM 2261 C CA . ASP A 1 282 ? -2.486 25.501 20.365 1.00 30.69 ? 300 ASP A CA 1 ATOM 2262 C C . ASP A 1 282 ? -2.813 26.965 20.537 1.00 30.35 ? 300 ASP A C 1 ATOM 2263 O O . ASP A 1 282 ? -3.425 27.559 19.664 1.00 30.09 ? 300 ASP A O 1 ATOM 2264 C CB . ASP A 1 282 ? -0.991 25.360 20.094 1.00 30.46 ? 300 ASP A CB 1 ATOM 2265 C CG . ASP A 1 282 ? -0.542 26.168 18.881 1.00 30.83 ? 300 ASP A CG 1 ATOM 2266 O OD1 . ASP A 1 282 ? -0.393 25.582 17.772 1.00 28.69 ? 300 ASP A OD1 1 ATOM 2267 O OD2 . ASP A 1 282 ? -0.377 27.394 19.040 1.00 31.73 ? 300 ASP A OD2 1 ATOM 2268 N N . ASN A 1 283 ? -2.393 27.555 21.652 1.00 30.22 ? 301 ASN A N 1 ATOM 2269 C CA . ASN A 1 283 ? -2.733 28.956 21.911 1.00 30.65 ? 301 ASN A CA 1 ATOM 2270 C C . ASN A 1 283 ? -1.540 29.874 21.825 1.00 30.04 ? 301 ASN A C 1 ATOM 2271 O O . ASN A 1 283 ? -1.542 30.974 22.384 1.00 29.72 ? 301 ASN A O 1 ATOM 2272 C CB . ASN A 1 283 ? -3.451 29.132 23.259 1.00 31.62 ? 301 ASN A CB 1 ATOM 2273 C CG . ASN A 1 283 ? -2.556 28.896 24.438 1.00 33.83 ? 301 ASN A CG 1 ATOM 2274 O OD1 . ASN A 1 283 ? -1.419 28.425 24.305 1.00 32.34 ? 301 ASN A OD1 1 ATOM 2275 N ND2 . ASN A 1 283 ? -3.067 29.225 25.620 1.00 41.40 ? 301 ASN A ND2 1 ATOM 2276 N N . MET A 1 284 ? -0.531 29.430 21.093 1.00 29.60 ? 302 MET A N 1 ATOM 2277 C CA . MET A 1 284 ? 0.743 30.171 21.074 1.00 29.82 ? 302 MET A CA 1 ATOM 2278 C C . MET A 1 284 ? 0.609 31.570 20.435 1.00 29.00 ? 302 MET A C 1 ATOM 2279 O O . MET A 1 284 ? 1.257 32.504 20.893 1.00 28.55 ? 302 MET A O 1 ATOM 2280 C CB . MET A 1 284 ? 1.868 29.339 20.458 1.00 29.69 ? 302 MET A CB 1 ATOM 2281 C CG . MET A 1 284 ? 2.270 28.163 21.384 1.00 34.06 ? 302 MET A CG 1 ATOM 2282 S SD . MET A 1 284 ? 3.124 28.750 22.879 1.00 43.60 ? 302 MET A SD 1 ATOM 2283 C CE . MET A 1 284 ? 3.357 27.196 23.765 1.00 43.88 ? 302 MET A CE 1 ATOM 2284 N N . THR A 1 285 ? -0.253 31.740 19.424 1.00 28.23 ? 303 THR A N 1 ATOM 2285 C CA . THR A 1 285 ? -0.434 33.081 18.847 1.00 27.61 ? 303 THR A CA 1 ATOM 2286 C C . THR A 1 285 ? -1.171 33.992 19.833 1.00 27.51 ? 303 THR A C 1 ATOM 2287 O O . THR A 1 285 ? -0.960 35.203 19.861 1.00 27.55 ? 303 THR A O 1 ATOM 2288 C CB . THR A 1 285 ? -1.144 33.106 17.461 1.00 27.24 ? 303 THR A CB 1 ATOM 2289 O OG1 . THR A 1 285 ? -2.488 32.607 17.552 1.00 26.65 ? 303 THR A OG1 1 ATOM 2290 C CG2 . THR A 1 285 ? -0.312 32.330 16.382 1.00 26.01 ? 303 THR A CG2 1 ATOM 2291 N N . ALA A 1 286 ? -2.026 33.407 20.661 1.00 27.70 ? 304 ALA A N 1 ATOM 2292 C CA . ALA A 1 286 ? -2.711 34.185 21.686 1.00 28.17 ? 304 ALA A CA 1 ATOM 2293 C C . ALA A 1 286 ? -1.726 34.653 22.738 1.00 29.00 ? 304 ALA A C 1 ATOM 2294 O O . ALA A 1 286 ? -1.795 35.782 23.240 1.00 29.68 ? 304 ALA A O 1 ATOM 2295 C CB . ALA A 1 286 ? -3.872 33.370 22.352 1.00 28.72 ? 304 ALA A CB 1 ATOM 2296 N N . VAL A 1 287 ? -0.819 33.764 23.090 1.00 29.82 ? 305 VAL A N 1 ATOM 2297 C CA . VAL A 1 287 ? 0.238 34.086 24.056 1.00 30.09 ? 305 VAL A CA 1 ATOM 2298 C C . VAL A 1 287 ? 1.092 35.241 23.504 1.00 29.83 ? 305 VAL A C 1 ATOM 2299 O O . VAL A 1 287 ? 1.465 36.182 24.219 1.00 30.00 ? 305 VAL A O 1 ATOM 2300 C CB . VAL A 1 287 ? 1.131 32.858 24.329 1.00 31.05 ? 305 VAL A CB 1 ATOM 2301 C CG1 . VAL A 1 287 ? 2.418 33.269 25.099 1.00 32.48 ? 305 VAL A CG1 1 ATOM 2302 C CG2 . VAL A 1 287 ? 0.327 31.764 25.080 1.00 31.93 ? 305 VAL A CG2 1 ATOM 2303 N N . ALA A 1 288 ? 1.391 35.138 22.223 1.00 29.34 ? 306 ALA A N 1 ATOM 2304 C CA . ALA A 1 288 ? 2.264 36.099 21.524 1.00 29.40 ? 306 ALA A CA 1 ATOM 2305 C C . ALA A 1 288 ? 1.565 37.455 21.315 1.00 30.12 ? 306 ALA A C 1 ATOM 2306 O O . ALA A 1 288 ? 2.226 38.510 21.165 1.00 30.03 ? 306 ALA A O 1 ATOM 2307 C CB . ALA A 1 288 ? 2.738 35.536 20.181 1.00 28.54 ? 306 ALA A CB 1 ATOM 2308 N N . CYS A 1 289 ? 0.238 37.418 21.290 1.00 31.14 ? 307 CYS A N 1 ATOM 2309 C CA . CYS A 1 289 ? -0.537 38.624 20.986 1.00 31.55 ? 307 CYS A CA 1 ATOM 2310 C C . CYS A 1 289 ? -0.950 39.339 22.287 1.00 32.55 ? 307 CYS A C 1 ATOM 2311 O O . CYS A 1 289 ? -1.899 38.927 22.971 1.00 32.84 ? 307 CYS A O 1 ATOM 2312 C CB . CYS A 1 289 ? -1.736 38.281 20.065 1.00 32.58 ? 307 CYS A CB 1 ATOM 2313 S SG . CYS A 1 289 ? -2.814 39.713 19.663 1.00 36.01 ? 307 CYS A SG 1 ATOM 2314 N N . GLN A 1 290 ? -0.197 40.382 22.635 1.00 31.10 ? 308 GLN A N 1 ATOM 2315 C CA . GLN A 1 290 ? -0.443 41.161 23.866 1.00 31.29 ? 308 GLN A CA 1 ATOM 2316 C C . GLN A 1 290 ? -0.560 42.662 23.636 1.00 30.47 ? 308 GLN A C 1 ATOM 2317 O O . GLN A 1 290 ? -0.011 43.211 22.691 1.00 29.49 ? 308 GLN A O 1 ATOM 2318 C CB . GLN A 1 290 ? 0.671 40.923 24.901 1.00 31.49 ? 308 GLN A CB 1 ATOM 2319 C CG . GLN A 1 290 ? 0.816 39.481 25.368 1.00 33.32 ? 308 GLN A CG 1 ATOM 2320 C CD . GLN A 1 290 ? -0.406 38.999 26.118 1.00 37.74 ? 308 GLN A CD 1 ATOM 2321 O OE1 . GLN A 1 290 ? -0.957 39.729 26.926 1.00 38.69 ? 308 GLN A OE1 1 ATOM 2322 N NE2 . GLN A 1 290 ? -0.855 37.774 25.829 1.00 39.38 ? 308 GLN A NE2 1 ATOM 2323 N N . PRO A 1 291 ? -1.283 43.350 24.529 1.00 30.45 ? 309 PRO A N 1 ATOM 2324 C CA . PRO A 1 291 ? -1.282 44.804 24.499 1.00 30.47 ? 309 PRO A CA 1 ATOM 2325 C C . PRO A 1 291 ? 0.104 45.305 24.825 1.00 29.79 ? 309 PRO A C 1 ATOM 2326 O O . PRO A 1 291 ? 0.840 44.648 25.577 1.00 29.99 ? 309 PRO A O 1 ATOM 2327 C CB . PRO A 1 291 ? -2.287 45.211 25.602 1.00 31.47 ? 309 PRO A CB 1 ATOM 2328 C CG . PRO A 1 291 ? -2.638 43.988 26.327 1.00 31.29 ? 309 PRO A CG 1 ATOM 2329 C CD . PRO A 1 291 ? -2.077 42.786 25.634 1.00 31.06 ? 309 PRO A CD 1 ATOM 2330 N N . PRO A 1 292 ? 0.480 46.453 24.280 1.00 28.90 ? 310 PRO A N 1 ATOM 2331 C CA . PRO A 1 292 ? -0.349 47.327 23.467 1.00 28.60 ? 310 PRO A CA 1 ATOM 2332 C C . PRO A 1 292 ? -0.192 47.098 21.975 1.00 27.34 ? 310 PRO A C 1 ATOM 2333 O O . PRO A 1 292 ? -0.769 47.829 21.181 1.00 26.86 ? 310 PRO A O 1 ATOM 2334 C CB . PRO A 1 292 ? 0.206 48.699 23.799 1.00 29.35 ? 310 PRO A CB 1 ATOM 2335 C CG . PRO A 1 292 ? 1.653 48.436 23.991 1.00 28.84 ? 310 PRO A CG 1 ATOM 2336 C CD . PRO A 1 292 ? 1.733 47.104 24.668 1.00 29.12 ? 310 PRO A CD 1 ATOM 2337 N N . TYR A 1 293 ? 0.603 46.098 21.608 1.00 26.76 ? 311 TYR A N 1 ATOM 2338 C CA . TYR A 1 293 ? 1.043 45.954 20.209 1.00 25.67 ? 311 TYR A CA 1 ATOM 2339 C C . TYR A 1 293 ? 0.125 45.080 19.361 1.00 26.18 ? 311 TYR A C 1 ATOM 2340 O O . TYR A 1 293 ? 0.287 45.020 18.164 1.00 25.15 ? 311 TYR A O 1 ATOM 2341 C CB . TYR A 1 293 ? 2.503 45.436 20.095 1.00 25.90 ? 311 TYR A CB 1 ATOM 2342 C CG . TYR A 1 293 ? 2.747 44.101 20.741 1.00 25.15 ? 311 TYR A CG 1 ATOM 2343 C CD1 . TYR A 1 293 ? 2.569 42.908 20.028 1.00 24.08 ? 311 TYR A CD1 1 ATOM 2344 C CD2 . TYR A 1 293 ? 3.144 44.013 22.062 1.00 25.48 ? 311 TYR A CD2 1 ATOM 2345 C CE1 . TYR A 1 293 ? 2.806 41.679 20.623 1.00 26.70 ? 311 TYR A CE1 1 ATOM 2346 C CE2 . TYR A 1 293 ? 3.358 42.787 22.669 1.00 26.54 ? 311 TYR A CE2 1 ATOM 2347 C CZ . TYR A 1 293 ? 3.201 41.617 21.935 1.00 26.11 ? 311 TYR A CZ 1 ATOM 2348 O OH . TYR A 1 293 ? 3.415 40.376 22.545 1.00 28.94 ? 311 TYR A OH 1 ATOM 2349 N N . CYS A 1 294 ? -0.830 44.427 19.999 1.00 26.38 ? 312 CYS A N 1 ATOM 2350 C CA . CYS A 1 294 ? -1.675 43.434 19.315 1.00 27.15 ? 312 CYS A CA 1 ATOM 2351 C C . CYS A 1 294 ? -3.069 43.303 19.941 1.00 26.79 ? 312 CYS A C 1 ATOM 2352 O O . CYS A 1 294 ? -3.209 43.362 21.163 1.00 26.95 ? 312 CYS A O 1 ATOM 2353 C CB . CYS A 1 294 ? -0.970 42.077 19.362 1.00 27.95 ? 312 CYS A CB 1 ATOM 2354 S SG . CYS A 1 294 ? -1.689 40.791 18.292 1.00 32.18 ? 312 CYS A SG 1 ATOM 2355 N N . TYR A 1 295 ? -4.070 43.147 19.082 1.00 26.44 ? 313 TYR A N 1 ATOM 2356 C CA . TYR A 1 295 ? -5.438 42.808 19.494 1.00 26.99 ? 313 TYR A CA 1 ATOM 2357 C C . TYR A 1 295 ? -5.729 41.397 19.007 1.00 27.36 ? 313 TYR A C 1 ATOM 2358 O O . TYR A 1 295 ? -5.531 41.087 17.829 1.00 27.63 ? 313 TYR A O 1 ATOM 2359 C CB . TYR A 1 295 ? -6.455 43.757 18.868 1.00 27.73 ? 313 TYR A CB 1 ATOM 2360 C CG . TYR A 1 295 ? -6.208 45.244 19.088 1.00 26.83 ? 313 TYR A CG 1 ATOM 2361 C CD1 . TYR A 1 295 ? -6.242 45.797 20.348 1.00 27.47 ? 313 TYR A CD1 1 ATOM 2362 C CD2 . TYR A 1 295 ? -6.004 46.105 18.008 1.00 28.15 ? 313 TYR A CD2 1 ATOM 2363 C CE1 . TYR A 1 295 ? -6.018 47.145 20.547 1.00 28.14 ? 313 TYR A CE1 1 ATOM 2364 C CE2 . TYR A 1 295 ? -5.785 47.462 18.202 1.00 28.64 ? 313 TYR A CE2 1 ATOM 2365 C CZ . TYR A 1 295 ? -5.791 47.970 19.475 1.00 26.75 ? 313 TYR A CZ 1 ATOM 2366 O OH . TYR A 1 295 ? -5.590 49.308 19.682 1.00 26.92 ? 313 TYR A OH 1 ATOM 2367 N N . PHE A 1 296 ? -6.228 40.558 19.893 1.00 27.34 ? 314 PHE A N 1 ATOM 2368 C CA . PHE A 1 296 ? -6.543 39.173 19.532 1.00 28.47 ? 314 PHE A CA 1 ATOM 2369 C C . PHE A 1 296 ? -8.045 38.977 19.382 1.00 28.88 ? 314 PHE A C 1 ATOM 2370 O O . PHE A 1 296 ? -8.829 39.365 20.253 1.00 29.09 ? 314 PHE A O 1 ATOM 2371 C CB . PHE A 1 296 ? -5.985 38.249 20.609 1.00 29.56 ? 314 PHE A CB 1 ATOM 2372 C CG . PHE A 1 296 ? -6.032 36.809 20.258 1.00 30.70 ? 314 PHE A CG 1 ATOM 2373 C CD1 . PHE A 1 296 ? -5.127 36.283 19.352 1.00 31.44 ? 314 PHE A CD1 1 ATOM 2374 C CD2 . PHE A 1 296 ? -6.956 35.958 20.861 1.00 33.23 ? 314 PHE A CD2 1 ATOM 2375 C CE1 . PHE A 1 296 ? -5.163 34.942 19.015 1.00 32.01 ? 314 PHE A CE1 1 ATOM 2376 C CE2 . PHE A 1 296 ? -7.001 34.604 20.525 1.00 32.03 ? 314 PHE A CE2 1 ATOM 2377 C CZ . PHE A 1 296 ? -6.103 34.094 19.606 1.00 31.89 ? 314 PHE A CZ 1 ATOM 2378 N N . ARG A 1 297 ? -8.441 38.345 18.285 1.00 28.96 ? 315 ARG A N 1 ATOM 2379 C CA . ARG A 1 297 ? -9.843 38.002 18.035 1.00 28.60 ? 315 ARG A CA 1 ATOM 2380 C C . ARG A 1 297 ? -10.058 36.501 17.875 1.00 28.89 ? 315 ARG A C 1 ATOM 2381 O O . ARG A 1 297 ? -9.326 35.814 17.172 1.00 28.96 ? 315 ARG A O 1 ATOM 2382 C CB . ARG A 1 297 ? -10.346 38.696 16.778 1.00 28.11 ? 315 ARG A CB 1 ATOM 2383 C CG . ARG A 1 297 ? -10.179 40.182 16.758 1.00 28.46 ? 315 ARG A CG 1 ATOM 2384 C CD . ARG A 1 297 ? -10.795 40.940 17.912 1.00 29.82 ? 315 ARG A CD 1 ATOM 2385 N NE . ARG A 1 297 ? -10.443 42.353 17.766 1.00 31.46 ? 315 ARG A NE 1 ATOM 2386 C CZ . ARG A 1 297 ? -10.264 43.215 18.764 1.00 30.21 ? 315 ARG A CZ 1 ATOM 2387 N NH1 . ARG A 1 297 ? -10.435 42.838 20.025 1.00 30.88 ? 315 ARG A NH1 1 ATOM 2388 N NH2 . ARG A 1 297 ? -9.963 44.467 18.491 1.00 28.15 ? 315 ARG A NH2 1 ATOM 2389 N N . ASN A 1 298 ? -11.100 36.000 18.517 1.00 28.95 ? 316 ASN A N 1 ATOM 2390 C CA . ASN A 1 298 ? -11.437 34.577 18.448 1.00 29.09 ? 316 ASN A CA 1 ATOM 2391 C C . ASN A 1 298 ? -12.964 34.392 18.431 1.00 29.75 ? 316 ASN A C 1 ATOM 2392 O O . ASN A 1 298 ? -13.697 35.202 18.973 1.00 28.66 ? 316 ASN A O 1 ATOM 2393 C CB . ASN A 1 298 ? -10.790 33.887 19.646 1.00 29.82 ? 316 ASN A CB 1 ATOM 2394 C CG . ASN A 1 298 ? -10.950 32.382 19.647 1.00 29.74 ? 316 ASN A CG 1 ATOM 2395 O OD1 . ASN A 1 298 ? -11.162 31.739 18.609 1.00 29.52 ? 316 ASN A OD1 1 ATOM 2396 N ND2 . ASN A 1 298 ? -10.802 31.804 20.846 1.00 31.48 ? 316 ASN A ND2 1 ATOM 2397 N N . SER A 1 299 ? -13.440 33.369 17.740 1.00 30.72 ? 317 SER A N 1 ATOM 2398 C CA . SER A 1 299 ? -14.889 33.076 17.757 1.00 32.04 ? 317 SER A CA 1 ATOM 2399 C C . SER A 1 299 ? -15.241 32.373 19.073 1.00 32.15 ? 317 SER A C 1 ATOM 2400 O O . SER A 1 299 ? -14.363 31.903 19.789 1.00 32.55 ? 317 SER A O 1 ATOM 2401 C CB . SER A 1 299 ? -15.314 32.217 16.571 1.00 32.45 ? 317 SER A CB 1 ATOM 2402 O OG . SER A 1 299 ? -15.161 30.867 16.900 1.00 35.44 ? 317 SER A OG 1 ATOM 2403 N N . THR A 1 300 ? -16.528 32.296 19.387 1.00 32.96 ? 318 THR A N 1 ATOM 2404 C CA . THR A 1 300 ? -16.952 31.710 20.651 1.00 33.32 ? 318 THR A CA 1 ATOM 2405 C C . THR A 1 300 ? -17.315 30.260 20.458 1.00 34.01 ? 318 THR A C 1 ATOM 2406 O O . THR A 1 300 ? -17.741 29.563 21.387 1.00 34.85 ? 318 THR A O 1 ATOM 2407 C CB . THR A 1 300 ? -18.159 32.440 21.228 1.00 33.99 ? 318 THR A CB 1 ATOM 2408 O OG1 . THR A 1 300 ? -19.179 32.532 20.227 1.00 32.03 ? 318 THR A OG1 1 ATOM 2409 C CG2 . THR A 1 300 ? -17.740 33.830 21.701 1.00 34.63 ? 318 THR A CG2 1 ATOM 2410 N N . THR A 1 301 ? -17.135 29.808 19.239 1.00 33.63 ? 319 THR A N 1 ATOM 2411 C CA . THR A 1 301 ? -17.590 28.488 18.853 1.00 33.86 ? 319 THR A CA 1 ATOM 2412 C C . THR A 1 301 ? -16.495 27.628 18.234 1.00 33.74 ? 319 THR A C 1 ATOM 2413 O O . THR A 1 301 ? -15.458 28.116 17.763 1.00 32.77 ? 319 THR A O 1 ATOM 2414 C CB . THR A 1 301 ? -18.758 28.590 17.854 1.00 34.23 ? 319 THR A CB 1 ATOM 2415 O OG1 . THR A 1 301 ? -18.398 29.438 16.757 1.00 35.29 ? 319 THR A OG1 1 ATOM 2416 C CG2 . THR A 1 301 ? -20.013 29.160 18.518 1.00 34.46 ? 319 THR A CG2 1 ATOM 2417 N N . ASN A 1 302 ? -16.757 26.329 18.269 1.00 33.20 ? 320 ASN A N 1 ATOM 2418 C CA . ASN A 1 302 ? -15.973 25.340 17.513 1.00 33.01 ? 320 ASN A CA 1 ATOM 2419 C C . ASN A 1 302 ? -15.883 25.754 16.044 1.00 32.29 ? 320 ASN A C 1 ATOM 2420 O O . ASN A 1 302 ? -16.820 26.340 15.487 1.00 31.57 ? 320 ASN A O 1 ATOM 2421 C CB . ASN A 1 302 ? -16.645 23.962 17.643 1.00 33.40 ? 320 ASN A CB 1 ATOM 2422 C CG . ASN A 1 302 ? -15.820 22.826 17.063 1.00 33.58 ? 320 ASN A CG 1 ATOM 2423 O OD1 . ASN A 1 302 ? -14.630 22.965 16.772 1.00 31.42 ? 320 ASN A OD1 1 ATOM 2424 N ND2 . ASN A 1 302 ? -16.461 21.666 16.926 1.00 34.07 ? 320 ASN A ND2 1 ATOM 2425 N N . TYR A 1 303 ? -14.738 25.465 15.435 1.00 31.11 ? 321 TYR A N 1 ATOM 2426 C CA . TYR A 1 303 ? -14.555 25.664 13.999 1.00 31.14 ? 321 TYR A CA 1 ATOM 2427 C C . TYR A 1 303 ? -15.229 24.538 13.255 1.00 31.46 ? 321 TYR A C 1 ATOM 2428 O O . TYR A 1 303 ? -14.774 23.381 13.314 1.00 31.22 ? 321 TYR A O 1 ATOM 2429 C CB . TYR A 1 303 ? -13.072 25.738 13.588 1.00 30.67 ? 321 TYR A CB 1 ATOM 2430 C CG . TYR A 1 303 ? -12.905 26.314 12.199 1.00 29.77 ? 321 TYR A CG 1 ATOM 2431 C CD1 . TYR A 1 303 ? -12.414 27.603 12.004 1.00 29.76 ? 321 TYR A CD1 1 ATOM 2432 C CD2 . TYR A 1 303 ? -13.266 25.578 11.074 1.00 29.89 ? 321 TYR A CD2 1 ATOM 2433 C CE1 . TYR A 1 303 ? -12.272 28.145 10.727 1.00 30.17 ? 321 TYR A CE1 1 ATOM 2434 C CE2 . TYR A 1 303 ? -13.136 26.115 9.789 1.00 29.93 ? 321 TYR A CE2 1 ATOM 2435 C CZ . TYR A 1 303 ? -12.659 27.402 9.625 1.00 30.22 ? 321 TYR A CZ 1 ATOM 2436 O OH . TYR A 1 303 ? -12.514 27.940 8.356 1.00 29.38 ? 321 TYR A OH 1 ATOM 2437 N N . VAL A 1 304 ? -16.325 24.896 12.589 1.00 31.37 ? 322 VAL A N 1 ATOM 2438 C CA . VAL A 1 304 ? -17.118 23.952 11.781 1.00 32.36 ? 322 VAL A CA 1 ATOM 2439 C C . VAL A 1 304 ? -17.367 24.501 10.388 1.00 32.34 ? 322 VAL A C 1 ATOM 2440 O O . VAL A 1 304 ? -18.220 25.364 10.160 1.00 33.40 ? 322 VAL A O 1 ATOM 2441 C CB . VAL A 1 304 ? -18.451 23.597 12.465 1.00 32.02 ? 322 VAL A CB 1 ATOM 2442 C CG1 . VAL A 1 304 ? -19.245 22.566 11.605 1.00 32.48 ? 322 VAL A CG1 1 ATOM 2443 C CG2 . VAL A 1 304 ? -18.184 23.071 13.872 1.00 32.93 ? 322 VAL A CG2 1 ATOM 2444 N N . GLY A 1 305 ? -16.576 23.995 9.462 1.00 33.16 ? 323 GLY A N 1 ATOM 2445 C CA . GLY A 1 305 ? -16.543 24.494 8.110 1.00 33.48 ? 323 GLY A CA 1 ATOM 2446 C C . GLY A 1 305 ? -17.577 23.811 7.264 1.00 34.39 ? 323 GLY A C 1 ATOM 2447 O O . GLY A 1 305 ? -18.007 22.692 7.569 1.00 34.27 ? 323 GLY A O 1 ATOM 2448 N N . VAL A 1 306 ? -17.969 24.500 6.204 1.00 35.06 ? 324 VAL A N 1 ATOM 2449 C CA . VAL A 1 306 ? -19.045 24.020 5.329 1.00 35.73 ? 324 VAL A CA 1 ATOM 2450 C C . VAL A 1 306 ? -18.479 23.373 4.075 1.00 36.07 ? 324 VAL A C 1 ATOM 2451 O O . VAL A 1 306 ? -19.119 22.516 3.470 1.00 35.87 ? 324 VAL A O 1 ATOM 2452 C CB . VAL A 1 306 ? -20.076 25.140 4.946 1.00 36.07 ? 324 VAL A CB 1 ATOM 2453 C CG1 . VAL A 1 306 ? -20.773 25.688 6.186 1.00 36.63 ? 324 VAL A CG1 1 ATOM 2454 C CG2 . VAL A 1 306 ? -19.433 26.244 4.116 1.00 34.89 ? 324 VAL A CG2 1 ATOM 2455 N N . TYR A 1 307 ? -17.281 23.779 3.684 1.00 35.52 ? 325 TYR A N 1 ATOM 2456 C CA . TYR A 1 307 ? -16.645 23.176 2.511 1.00 35.77 ? 325 TYR A CA 1 ATOM 2457 C C . TYR A 1 307 ? -16.158 21.791 2.896 1.00 35.25 ? 325 TYR A C 1 ATOM 2458 O O . TYR A 1 307 ? -16.559 20.767 2.340 1.00 34.62 ? 325 TYR A O 1 ATOM 2459 C CB . TYR A 1 307 ? -15.479 24.006 2.014 1.00 36.01 ? 325 TYR A CB 1 ATOM 2460 C CG . TYR A 1 307 ? -14.933 23.522 0.703 1.00 37.83 ? 325 TYR A CG 1 ATOM 2461 C CD1 . TYR A 1 307 ? -15.663 23.687 -0.465 1.00 41.54 ? 325 TYR A CD1 1 ATOM 2462 C CD2 . TYR A 1 307 ? -13.702 22.882 0.629 1.00 40.14 ? 325 TYR A CD2 1 ATOM 2463 C CE1 . TYR A 1 307 ? -15.185 23.234 -1.677 1.00 42.70 ? 325 TYR A CE1 1 ATOM 2464 C CE2 . TYR A 1 307 ? -13.205 22.434 -0.581 1.00 41.67 ? 325 TYR A CE2 1 ATOM 2465 C CZ . TYR A 1 307 ? -13.953 22.615 -1.732 1.00 43.36 ? 325 TYR A CZ 1 ATOM 2466 O OH . TYR A 1 307 ? -13.487 22.170 -2.950 1.00 45.83 ? 325 TYR A OH 1 ATOM 2467 N N . ASP A 1 308 ? -15.228 21.792 3.827 1.00 34.15 ? 326 ASP A N 1 ATOM 2468 C CA . ASP A 1 308 ? -14.986 20.638 4.669 1.00 34.08 ? 326 ASP A CA 1 ATOM 2469 C C . ASP A 1 308 ? -14.962 21.124 6.105 1.00 33.67 ? 326 ASP A C 1 ATOM 2470 O O . ASP A 1 308 ? -15.168 22.311 6.364 1.00 33.91 ? 326 ASP A O 1 ATOM 2471 C CB . ASP A 1 308 ? -13.717 19.848 4.292 1.00 34.39 ? 326 ASP A CB 1 ATOM 2472 C CG . ASP A 1 308 ? -12.441 20.696 4.303 1.00 35.42 ? 326 ASP A CG 1 ATOM 2473 O OD1 . ASP A 1 308 ? -12.175 21.392 5.292 1.00 36.41 ? 326 ASP A OD1 1 ATOM 2474 O OD2 . ASP A 1 308 ? -11.682 20.635 3.311 1.00 37.08 ? 326 ASP A OD2 1 ATOM 2475 N N . ILE A 1 309 ? -14.717 20.209 7.028 1.00 32.95 ? 327 ILE A N 1 ATOM 2476 C CA . ILE A 1 309 ? -14.929 20.499 8.453 1.00 32.51 ? 327 ILE A CA 1 ATOM 2477 C C . ILE A 1 309 ? -13.939 21.572 8.938 1.00 31.62 ? 327 ILE A C 1 ATOM 2478 O O . ILE A 1 309 ? -14.184 22.270 9.918 1.00 30.61 ? 327 ILE A O 1 ATOM 2479 C CB . ILE A 1 309 ? -14.845 19.219 9.321 1.00 32.90 ? 327 ILE A CB 1 ATOM 2480 C CG1 . ILE A 1 309 ? -15.411 19.492 10.717 1.00 34.27 ? 327 ILE A CG1 1 ATOM 2481 C CG2 . ILE A 1 309 ? -13.420 18.682 9.396 1.00 32.49 ? 327 ILE A CG2 1 ATOM 2482 C CD1 . ILE A 1 309 ? -16.850 19.938 10.709 1.00 35.82 ? 327 ILE A CD1 1 ATOM 2483 N N . ASN A 1 310 ? -12.857 21.735 8.190 1.00 31.19 ? 328 ASN A N 1 ATOM 2484 C CA . ASN A 1 310 ? -11.787 22.671 8.587 1.00 31.17 ? 328 ASN A CA 1 ATOM 2485 C C . ASN A 1 310 ? -11.722 23.925 7.716 1.00 31.18 ? 328 ASN A C 1 ATOM 2486 O O . ASN A 1 310 ? -10.815 24.750 7.861 1.00 31.46 ? 328 ASN A O 1 ATOM 2487 C CB . ASN A 1 310 ? -10.437 21.963 8.669 1.00 30.53 ? 328 ASN A CB 1 ATOM 2488 C CG . ASN A 1 310 ? -10.287 21.180 9.958 1.00 31.01 ? 328 ASN A CG 1 ATOM 2489 O OD1 . ASN A 1 310 ? -10.324 21.756 11.044 1.00 31.44 ? 328 ASN A OD1 1 ATOM 2490 N ND2 . ASN A 1 310 ? -10.158 19.852 9.850 1.00 30.93 ? 328 ASN A ND2 1 ATOM 2491 N N . HIS A 1 311 ? -12.723 24.080 6.852 1.00 30.89 ? 329 HIS A N 1 ATOM 2492 C CA . HIS A 1 311 ? -12.807 25.264 5.973 1.00 31.00 ? 329 HIS A CA 1 ATOM 2493 C C . HIS A 1 311 ? -14.192 25.819 5.734 1.00 31.30 ? 329 HIS A C 1 ATOM 2494 O O . HIS A 1 311 ? -15.070 25.155 5.172 1.00 31.25 ? 329 HIS A O 1 ATOM 2495 C CB . HIS A 1 311 ? -12.144 24.983 4.616 1.00 31.45 ? 329 HIS A CB 1 ATOM 2496 C CG . HIS A 1 311 ? -10.722 24.550 4.730 1.00 30.97 ? 329 HIS A CG 1 ATOM 2497 N ND1 . HIS A 1 311 ? -10.368 23.254 5.026 1.00 32.79 ? 329 HIS A ND1 1 ATOM 2498 C CD2 . HIS A 1 311 ? -9.561 25.247 4.636 1.00 31.74 ? 329 HIS A CD2 1 ATOM 2499 C CE1 . HIS A 1 311 ? -9.049 23.165 5.099 1.00 32.86 ? 329 HIS A CE1 1 ATOM 2500 N NE2 . HIS A 1 311 ? -8.536 24.362 4.871 1.00 32.50 ? 329 HIS A NE2 1 ATOM 2501 N N . GLY A 1 312 ? -14.348 27.076 6.129 1.00 31.26 ? 330 GLY A N 1 ATOM 2502 C CA . GLY A 1 312 ? -15.568 27.856 5.848 1.00 31.17 ? 330 GLY A CA 1 ATOM 2503 C C . GLY A 1 312 ? -16.525 27.900 7.027 1.00 31.68 ? 330 GLY A C 1 ATOM 2504 O O . GLY A 1 312 ? -17.594 27.280 7.003 1.00 31.93 ? 330 GLY A O 1 ATOM 2505 N N . ASP A 1 313 ? -16.118 28.649 8.052 1.00 31.47 ? 331 ASP A N 1 ATOM 2506 C CA . ASP A 1 313 ? -16.783 28.678 9.359 1.00 31.80 ? 331 ASP A CA 1 ATOM 2507 C C . ASP A 1 313 ? -17.497 29.989 9.614 1.00 31.64 ? 331 ASP A C 1 ATOM 2508 O O . ASP A 1 313 ? -16.987 31.078 9.332 1.00 31.63 ? 331 ASP A O 1 ATOM 2509 C CB . ASP A 1 313 ? -15.764 28.447 10.461 1.00 31.60 ? 331 ASP A CB 1 ATOM 2510 C CG . ASP A 1 313 ? -16.346 28.604 11.841 1.00 32.02 ? 331 ASP A CG 1 ATOM 2511 O OD1 . ASP A 1 313 ? -17.023 27.657 12.297 1.00 32.05 ? 331 ASP A OD1 1 ATOM 2512 O OD2 . ASP A 1 313 ? -16.096 29.655 12.486 1.00 32.10 ? 331 ASP A OD2 1 ATOM 2513 N N . ALA A 1 314 ? -18.697 29.858 10.171 1.00 31.57 ? 332 ALA A N 1 ATOM 2514 C CA . ALA A 1 314 ? -19.587 31.002 10.366 1.00 31.23 ? 332 ALA A CA 1 ATOM 2515 C C . ALA A 1 314 ? -18.954 32.041 11.292 1.00 30.86 ? 332 ALA A C 1 ATOM 2516 O O . ALA A 1 314 ? -19.010 33.237 11.020 1.00 30.78 ? 332 ALA A O 1 ATOM 2517 C CB . ALA A 1 314 ? -20.949 30.532 10.916 1.00 31.98 ? 332 ALA A CB 1 ATOM 2518 N N . GLY A 1 315 ? -18.334 31.562 12.369 1.00 30.21 ? 333 GLY A N 1 ATOM 2519 C CA . GLY A 1 315 ? -17.744 32.440 13.391 1.00 30.09 ? 333 GLY A CA 1 ATOM 2520 C C . GLY A 1 315 ? -16.568 33.261 12.867 1.00 29.47 ? 333 GLY A C 1 ATOM 2521 O O . GLY A 1 315 ? -16.475 34.481 13.073 1.00 29.30 ? 333 GLY A O 1 ATOM 2522 N N . PHE A 1 316 ? -15.680 32.591 12.158 1.00 29.25 ? 334 PHE A N 1 ATOM 2523 C CA . PHE A 1 316 ? -14.488 33.263 11.636 1.00 29.38 ? 334 PHE A CA 1 ATOM 2524 C C . PHE A 1 316 ? -14.801 34.077 10.388 1.00 29.14 ? 334 PHE A C 1 ATOM 2525 O O . PHE A 1 316 ? -14.147 35.081 10.096 1.00 28.27 ? 334 PHE A O 1 ATOM 2526 C CB . PHE A 1 316 ? -13.331 32.281 11.456 1.00 29.61 ? 334 PHE A CB 1 ATOM 2527 C CG . PHE A 1 316 ? -12.707 31.884 12.760 1.00 28.66 ? 334 PHE A CG 1 ATOM 2528 C CD1 . PHE A 1 316 ? -11.788 32.703 13.380 1.00 28.30 ? 334 PHE A CD1 1 ATOM 2529 C CD2 . PHE A 1 316 ? -13.095 30.717 13.398 1.00 28.64 ? 334 PHE A CD2 1 ATOM 2530 C CE1 . PHE A 1 316 ? -11.237 32.355 14.602 1.00 28.39 ? 334 PHE A CE1 1 ATOM 2531 C CE2 . PHE A 1 316 ? -12.548 30.349 14.603 1.00 29.04 ? 334 PHE A CE2 1 ATOM 2532 C CZ . PHE A 1 316 ? -11.622 31.166 15.220 1.00 28.51 ? 334 PHE A CZ 1 ATOM 2533 N N . THR A 1 317 ? -15.820 33.644 9.647 1.00 29.50 ? 335 THR A N 1 ATOM 2534 C CA . THR A 1 317 ? -16.287 34.431 8.512 1.00 29.20 ? 335 THR A CA 1 ATOM 2535 C C . THR A 1 317 ? -16.790 35.772 9.058 1.00 29.22 ? 335 THR A C 1 ATOM 2536 O O . THR A 1 317 ? -16.570 36.851 8.480 1.00 28.37 ? 335 THR A O 1 ATOM 2537 C CB . THR A 1 317 ? -17.377 33.686 7.675 1.00 29.71 ? 335 THR A CB 1 ATOM 2538 O OG1 . THR A 1 317 ? -16.796 32.529 7.048 1.00 29.43 ? 335 THR A OG1 1 ATOM 2539 C CG2 . THR A 1 317 ? -17.963 34.594 6.598 1.00 29.67 ? 335 THR A CG2 1 ATOM 2540 N N . SER A 1 318 ? -17.450 35.702 10.207 1.00 29.44 ? 336 SER A N 1 ATOM 2541 C CA . SER A 1 318 ? -17.997 36.907 10.831 1.00 29.30 ? 336 SER A CA 1 ATOM 2542 C C . SER A 1 318 ? -16.892 37.874 11.241 1.00 28.81 ? 336 SER A C 1 ATOM 2543 O O . SER A 1 318 ? -16.974 39.097 11.048 1.00 29.01 ? 336 SER A O 1 ATOM 2544 C CB . SER A 1 318 ? -18.841 36.543 12.061 1.00 29.46 ? 336 SER A CB 1 ATOM 2545 O OG . SER A 1 318 ? -19.261 37.726 12.712 1.00 30.77 ? 336 SER A OG 1 ATOM 2546 N N . ILE A 1 319 ? -15.846 37.311 11.813 1.00 28.29 ? 337 ILE A N 1 ATOM 2547 C CA . ILE A 1 319 ? -14.712 38.126 12.284 1.00 27.89 ? 337 ILE A CA 1 ATOM 2548 C C . ILE A 1 319 ? -14.050 38.841 11.106 1.00 26.96 ? 337 ILE A C 1 ATOM 2549 O O . ILE A 1 319 ? -13.748 40.045 11.166 1.00 26.17 ? 337 ILE A O 1 ATOM 2550 C CB . ILE A 1 319 ? -13.679 37.293 13.083 1.00 27.87 ? 337 ILE A CB 1 ATOM 2551 C CG1 . ILE A 1 319 ? -14.240 36.946 14.461 1.00 28.74 ? 337 ILE A CG1 1 ATOM 2552 C CG2 . ILE A 1 319 ? -12.351 38.078 13.267 1.00 27.53 ? 337 ILE A CG2 1 ATOM 2553 C CD1 . ILE A 1 319 ? -13.528 35.768 15.135 1.00 28.13 ? 337 ILE A CD1 1 ATOM 2554 N N . LEU A 1 320 ? -13.867 38.113 10.012 1.00 27.52 ? 338 LEU A N 1 ATOM 2555 C CA . LEU A 1 320 ? -13.155 38.665 8.840 1.00 27.69 ? 338 LEU A CA 1 ATOM 2556 C C . LEU A 1 320 ? -14.040 39.651 8.075 1.00 27.60 ? 338 LEU A C 1 ATOM 2557 O O . LEU A 1 320 ? -13.562 40.450 7.269 1.00 26.47 ? 338 LEU A O 1 ATOM 2558 C CB . LEU A 1 320 ? -12.661 37.568 7.886 1.00 28.42 ? 338 LEU A CB 1 ATOM 2559 C CG . LEU A 1 320 ? -11.628 36.524 8.336 1.00 30.01 ? 338 LEU A CG 1 ATOM 2560 C CD1 . LEU A 1 320 ? -10.785 36.017 7.108 1.00 33.39 ? 338 LEU A CD1 1 ATOM 2561 C CD2 . LEU A 1 320 ? -10.750 36.972 9.440 1.00 32.46 ? 338 LEU A CD2 1 ATOM 2562 N N . SER A 1 321 ? -15.336 39.609 8.359 1.00 28.17 ? 339 SER A N 1 ATOM 2563 C CA . SER A 1 321 ? -16.295 40.420 7.613 1.00 28.31 ? 339 SER A CA 1 ATOM 2564 C C . SER A 1 321 ? -16.034 41.897 7.802 1.00 28.41 ? 339 SER A C 1 ATOM 2565 O O . SER A 1 321 ? -16.462 42.729 7.002 1.00 28.66 ? 339 SER A O 1 ATOM 2566 C CB . SER A 1 321 ? -17.761 40.076 7.969 1.00 28.59 ? 339 SER A CB 1 ATOM 2567 O OG . SER A 1 321 ? -18.152 40.640 9.213 1.00 29.76 ? 339 SER A OG 1 ATOM 2568 N N . GLY A 1 322 ? -15.310 42.228 8.860 1.00 28.19 ? 340 GLY A N 1 ATOM 2569 C CA . GLY A 1 322 ? -15.013 43.625 9.175 1.00 27.77 ? 340 GLY A CA 1 ATOM 2570 C C . GLY A 1 322 ? -14.027 44.233 8.192 1.00 27.66 ? 340 GLY A C 1 ATOM 2571 O O . GLY A 1 322 ? -13.832 45.449 8.150 1.00 28.76 ? 340 GLY A O 1 ATOM 2572 N N . LEU A 1 323 ? -13.417 43.392 7.381 1.00 27.04 ? 341 LEU A N 1 ATOM 2573 C CA . LEU A 1 323 ? -12.460 43.892 6.381 1.00 27.66 ? 341 LEU A CA 1 ATOM 2574 C C . LEU A 1 323 ? -13.209 44.541 5.227 1.00 27.93 ? 341 LEU A C 1 ATOM 2575 O O . LEU A 1 323 ? -12.613 45.202 4.374 1.00 27.03 ? 341 LEU A O 1 ATOM 2576 C CB . LEU A 1 323 ? -11.560 42.774 5.849 1.00 27.64 ? 341 LEU A CB 1 ATOM 2577 C CG . LEU A 1 323 ? -10.622 42.164 6.910 1.00 27.54 ? 341 LEU A CG 1 ATOM 2578 C CD1 . LEU A 1 323 ? -9.851 40.974 6.357 1.00 28.44 ? 341 LEU A CD1 1 ATOM 2579 C CD2 . LEU A 1 323 ? -9.674 43.228 7.471 1.00 30.03 ? 341 LEU A CD2 1 ATOM 2580 N N . LEU A 1 324 ? -14.522 44.350 5.216 1.00 28.45 ? 342 LEU A N 1 ATOM 2581 C CA . LEU A 1 324 ? -15.343 44.878 4.103 1.00 29.70 ? 342 LEU A CA 1 ATOM 2582 C C . LEU A 1 324 ? -15.687 46.354 4.262 1.00 30.32 ? 342 LEU A C 1 ATOM 2583 O O . LEU A 1 324 ? -16.249 46.977 3.363 1.00 31.41 ? 342 LEU A O 1 ATOM 2584 C CB . LEU A 1 324 ? -16.629 44.071 3.931 1.00 29.85 ? 342 LEU A CB 1 ATOM 2585 C CG . LEU A 1 324 ? -16.450 42.677 3.351 1.00 31.39 ? 342 LEU A CG 1 ATOM 2586 C CD1 . LEU A 1 324 ? -17.764 41.883 3.402 1.00 31.81 ? 342 LEU A CD1 1 ATOM 2587 C CD2 . LEU A 1 324 ? -15.904 42.764 1.922 1.00 31.56 ? 342 LEU A CD2 1 ATOM 2588 N N . TYR A 1 325 ? -15.351 46.916 5.412 1.00 29.67 ? 343 TYR A N 1 ATOM 2589 C CA . TYR A 1 325 ? -15.659 48.321 5.692 1.00 29.75 ? 343 TYR A CA 1 ATOM 2590 C C . TYR A 1 325 ? -14.599 48.951 6.579 1.00 30.11 ? 343 TYR A C 1 ATOM 2591 O O . TYR A 1 325 ? -13.830 48.237 7.228 1.00 29.57 ? 343 TYR A O 1 ATOM 2592 C CB . TYR A 1 325 ? -17.047 48.465 6.351 1.00 29.78 ? 343 TYR A CB 1 ATOM 2593 C CG . TYR A 1 325 ? -17.276 47.573 7.538 1.00 30.04 ? 343 TYR A CG 1 ATOM 2594 C CD1 . TYR A 1 325 ? -16.763 47.908 8.794 1.00 30.54 ? 343 TYR A CD1 1 ATOM 2595 C CD2 . TYR A 1 325 ? -18.010 46.406 7.421 1.00 29.75 ? 343 TYR A CD2 1 ATOM 2596 C CE1 . TYR A 1 325 ? -16.973 47.100 9.880 1.00 31.02 ? 343 TYR A CE1 1 ATOM 2597 C CE2 . TYR A 1 325 ? -18.234 45.592 8.504 1.00 31.71 ? 343 TYR A CE2 1 ATOM 2598 C CZ . TYR A 1 325 ? -17.698 45.937 9.732 1.00 31.25 ? 343 TYR A CZ 1 ATOM 2599 O OH . TYR A 1 325 ? -17.905 45.131 10.812 1.00 31.09 ? 343 TYR A OH 1 ATOM 2600 N N . ASP A 1 326 ? -14.546 50.278 6.569 1.00 30.12 ? 344 ASP A N 1 ATOM 2601 C CA . ASP A 1 326 ? -13.686 51.016 7.514 1.00 30.23 ? 344 ASP A CA 1 ATOM 2602 C C . ASP A 1 326 ? -14.372 51.167 8.848 1.00 29.98 ? 344 ASP A C 1 ATOM 2603 O O . ASP A 1 326 ? -15.601 51.336 8.933 1.00 30.39 ? 344 ASP A O 1 ATOM 2604 C CB . ASP A 1 326 ? -13.347 52.432 7.042 1.00 30.84 ? 344 ASP A CB 1 ATOM 2605 C CG . ASP A 1 326 ? -12.505 52.461 5.792 1.00 33.20 ? 344 ASP A CG 1 ATOM 2606 O OD1 . ASP A 1 326 ? -11.641 51.568 5.583 1.00 33.11 ? 344 ASP A OD1 1 ATOM 2607 O OD2 . ASP A 1 326 ? -12.680 53.431 5.025 1.00 36.27 ? 344 ASP A OD2 1 ATOM 2608 N N . SER A 1 327 ? -13.554 51.148 9.893 1.00 29.62 ? 345 SER A N 1 ATOM 2609 C CA . SER A 1 327 ? -14.019 51.325 11.253 1.00 29.28 ? 345 SER A CA 1 ATOM 2610 C C . SER A 1 327 ? -13.093 52.306 11.984 1.00 29.77 ? 345 SER A C 1 ATOM 2611 O O . SER A 1 327 ? -11.897 52.279 11.774 1.00 29.61 ? 345 SER A O 1 ATOM 2612 C CB . SER A 1 327 ? -14.023 49.981 11.983 1.00 29.34 ? 345 SER A CB 1 ATOM 2613 O OG . SER A 1 327 ? -14.820 49.010 11.337 1.00 29.43 ? 345 SER A OG 1 ATOM 2614 N N . PRO A 1 328 ? -13.637 53.163 12.855 1.00 29.99 ? 346 PRO A N 1 ATOM 2615 C CA . PRO A 1 328 ? -12.771 54.214 13.404 1.00 30.20 ? 346 PRO A CA 1 ATOM 2616 C C . PRO A 1 328 ? -11.930 53.823 14.630 1.00 30.12 ? 346 PRO A C 1 ATOM 2617 O O . PRO A 1 328 ? -10.881 54.413 14.861 1.00 30.91 ? 346 PRO A O 1 ATOM 2618 C CB . PRO A 1 328 ? -13.768 55.307 13.802 1.00 30.28 ? 346 PRO A CB 1 ATOM 2619 C CG . PRO A 1 328 ? -15.053 54.608 14.022 1.00 30.80 ? 346 PRO A CG 1 ATOM 2620 C CD . PRO A 1 328 ? -15.062 53.380 13.177 1.00 30.31 ? 346 PRO A CD 1 ATOM 2621 N N . CYS A 1 329 ? -12.398 52.860 15.409 1.00 29.81 ? 347 CYS A N 1 ATOM 2622 C CA . CYS A 1 329 ? -11.797 52.595 16.715 1.00 30.06 ? 347 CYS A CA 1 ATOM 2623 C C . CYS A 1 329 ? -11.524 51.118 16.975 1.00 29.89 ? 347 CYS A C 1 ATOM 2624 O O . CYS A 1 329 ? -12.389 50.255 16.825 1.00 30.45 ? 347 CYS A O 1 ATOM 2625 C CB . CYS A 1 329 ? -12.667 53.175 17.843 1.00 30.41 ? 347 CYS A CB 1 ATOM 2626 S SG . CYS A 1 329 ? -11.996 52.873 19.504 1.00 32.49 ? 347 CYS A SG 1 ATOM 2627 N N . PHE A 1 330 ? -10.279 50.861 17.363 1.00 28.93 ? 348 PHE A N 1 ATOM 2628 C CA . PHE A 1 330 ? -9.769 49.522 17.655 1.00 28.49 ? 348 PHE A CA 1 ATOM 2629 C C . PHE A 1 330 ? -9.319 49.463 19.108 1.00 28.73 ? 348 PHE A C 1 ATOM 2630 O O . PHE A 1 330 ? -8.710 50.386 19.615 1.00 28.86 ? 348 PHE A O 1 ATOM 2631 C CB . PHE A 1 330 ? -8.606 49.196 16.695 1.00 28.94 ? 348 PHE A CB 1 ATOM 2632 C CG . PHE A 1 330 ? -9.018 49.241 15.259 1.00 27.59 ? 348 PHE A CG 1 ATOM 2633 C CD1 . PHE A 1 330 ? -9.320 48.072 14.571 1.00 27.08 ? 348 PHE A CD1 1 ATOM 2634 C CD2 . PHE A 1 330 ? -9.165 50.461 14.606 1.00 28.73 ? 348 PHE A CD2 1 ATOM 2635 C CE1 . PHE A 1 330 ? -9.778 48.130 13.255 1.00 27.01 ? 348 PHE A CE1 1 ATOM 2636 C CE2 . PHE A 1 330 ? -9.641 50.518 13.281 1.00 28.32 ? 348 PHE A CE2 1 ATOM 2637 C CZ . PHE A 1 330 ? -9.939 49.351 12.624 1.00 26.81 ? 348 PHE A CZ 1 ATOM 2638 N N . SER A 1 331 ? -9.691 48.382 19.772 1.00 29.01 ? 349 SER A N 1 ATOM 2639 C CA . SER A 1 331 ? -9.491 48.222 21.190 1.00 29.50 ? 349 SER A CA 1 ATOM 2640 C C . SER A 1 331 ? -9.407 46.779 21.599 1.00 29.33 ? 349 SER A C 1 ATOM 2641 O O . SER A 1 331 ? -9.735 45.861 20.846 1.00 29.49 ? 349 SER A O 1 ATOM 2642 C CB . SER A 1 331 ? -10.631 48.896 21.979 1.00 29.31 ? 349 SER A CB 1 ATOM 2643 O OG . SER A 1 331 ? -11.808 48.109 21.945 1.00 29.33 ? 349 SER A OG 1 ATOM 2644 N N . GLN A 1 332 ? -8.958 46.584 22.821 1.00 30.37 ? 350 GLN A N 1 ATOM 2645 C CA . GLN A 1 332 ? -8.853 45.231 23.355 1.00 31.83 ? 350 GLN A CA 1 ATOM 2646 C C . GLN A 1 332 ? -10.200 44.529 23.274 1.00 32.17 ? 350 GLN A C 1 ATOM 2647 O O . GLN A 1 332 ? -10.271 43.332 22.971 1.00 32.42 ? 350 GLN A O 1 ATOM 2648 C CB . GLN A 1 332 ? -8.348 45.250 24.794 1.00 32.82 ? 350 GLN A CB 1 ATOM 2649 C CG . GLN A 1 332 ? -8.238 43.874 25.452 1.00 36.28 ? 350 GLN A CG 1 ATOM 2650 C CD . GLN A 1 332 ? -7.538 43.936 26.796 1.00 40.65 ? 350 GLN A CD 1 ATOM 2651 O OE1 . GLN A 1 332 ? -8.110 44.410 27.782 1.00 42.08 ? 350 GLN A OE1 1 ATOM 2652 N NE2 . GLN A 1 332 ? -6.284 43.479 26.838 1.00 42.34 ? 350 GLN A NE2 1 ATOM 2653 N N . GLN A 1 333 ? -11.275 45.284 23.530 1.00 31.56 ? 351 GLN A N 1 ATOM 2654 C CA . GLN A 1 333 ? -12.627 44.696 23.650 1.00 31.45 ? 351 GLN A CA 1 ATOM 2655 C C . GLN A 1 333 ? -13.258 44.388 22.303 1.00 31.21 ? 351 GLN A C 1 ATOM 2656 O O . GLN A 1 333 ? -14.200 43.590 22.215 1.00 30.73 ? 351 GLN A O 1 ATOM 2657 C CB . GLN A 1 333 ? -13.586 45.616 24.415 1.00 32.28 ? 351 GLN A CB 1 ATOM 2658 C CG . GLN A 1 333 ? -13.160 45.997 25.810 1.00 33.59 ? 351 GLN A CG 1 ATOM 2659 C CD . GLN A 1 333 ? -12.658 47.425 25.881 1.00 34.35 ? 351 GLN A CD 1 ATOM 2660 O OE1 . GLN A 1 333 ? -11.716 47.791 25.185 1.00 33.13 ? 351 GLN A OE1 1 ATOM 2661 N NE2 . GLN A 1 333 ? -13.277 48.237 26.747 1.00 33.69 ? 351 GLN A NE2 1 ATOM 2662 N N . GLY A 1 334 ? -12.719 45.017 21.261 1.00 29.84 ? 352 GLY A N 1 ATOM 2663 C CA . GLY A 1 334 ? -13.230 44.895 19.893 1.00 29.57 ? 352 GLY A CA 1 ATOM 2664 C C . GLY A 1 334 ? -13.163 46.177 19.102 1.00 29.51 ? 352 GLY A C 1 ATOM 2665 O O . GLY A 1 334 ? -12.496 47.134 19.471 1.00 29.21 ? 352 GLY A O 1 ATOM 2666 N N . VAL A 1 335 ? -13.912 46.198 18.011 1.00 29.58 ? 353 VAL A N 1 ATOM 2667 C CA . VAL A 1 335 ? -13.922 47.334 17.109 1.00 29.77 ? 353 VAL A CA 1 ATOM 2668 C C . VAL A 1 335 ? -15.232 48.089 17.287 1.00 30.88 ? 353 VAL A C 1 ATOM 2669 O O . VAL A 1 335 ? -16.320 47.491 17.251 1.00 30.95 ? 353 VAL A O 1 ATOM 2670 C CB . VAL A 1 335 ? -13.761 46.867 15.627 1.00 29.62 ? 353 VAL A CB 1 ATOM 2671 C CG1 . VAL A 1 335 ? -14.037 48.007 14.646 1.00 29.51 ? 353 VAL A CG1 1 ATOM 2672 C CG2 . VAL A 1 335 ? -12.369 46.285 15.408 1.00 28.75 ? 353 VAL A CG2 1 ATOM 2673 N N . PHE A 1 336 ? -15.122 49.396 17.503 1.00 31.76 ? 354 PHE A N 1 ATOM 2674 C CA . PHE A 1 336 ? -16.309 50.274 17.563 1.00 32.24 ? 354 PHE A CA 1 ATOM 2675 C C . PHE A 1 336 ? -16.541 50.916 16.196 1.00 32.56 ? 354 PHE A C 1 ATOM 2676 O O . PHE A 1 336 ? -15.618 51.485 15.593 1.00 32.17 ? 354 PHE A O 1 ATOM 2677 C CB . PHE A 1 336 ? -16.157 51.367 18.634 1.00 32.06 ? 354 PHE A CB 1 ATOM 2678 C CG . PHE A 1 336 ? -15.976 50.845 20.040 1.00 32.36 ? 354 PHE A CG 1 ATOM 2679 C CD1 . PHE A 1 336 ? -17.063 50.766 20.912 1.00 34.08 ? 354 PHE A CD1 1 ATOM 2680 C CD2 . PHE A 1 336 ? -14.726 50.474 20.513 1.00 32.82 ? 354 PHE A CD2 1 ATOM 2681 C CE1 . PHE A 1 336 ? -16.913 50.310 22.192 1.00 33.36 ? 354 PHE A CE1 1 ATOM 2682 C CE2 . PHE A 1 336 ? -14.573 50.012 21.799 1.00 31.60 ? 354 PHE A CE2 1 ATOM 2683 C CZ . PHE A 1 336 ? -15.669 49.937 22.650 1.00 33.36 ? 354 PHE A CZ 1 ATOM 2684 N N . ARG A 1 337 ? -17.784 50.816 15.723 1.00 33.15 ? 355 ARG A N 1 ATOM 2685 C CA . ARG A 1 337 ? -18.150 51.278 14.380 1.00 33.86 ? 355 ARG A CA 1 ATOM 2686 C C . ARG A 1 337 ? -18.345 52.794 14.338 1.00 33.54 ? 355 ARG A C 1 ATOM 2687 O O . ARG A 1 337 ? -18.272 53.420 13.277 1.00 32.99 ? 355 ARG A O 1 ATOM 2688 C CB . ARG A 1 337 ? -19.369 50.515 13.851 1.00 34.38 ? 355 ARG A CB 1 ATOM 2689 C CG . ARG A 1 337 ? -19.015 49.041 13.600 1.00 37.67 ? 355 ARG A CG 1 ATOM 2690 C CD . ARG A 1 337 ? -19.918 48.328 12.589 1.00 41.27 ? 355 ARG A CD 1 ATOM 2691 N NE . ARG A 1 337 ? -19.710 48.844 11.244 1.00 42.39 ? 355 ARG A NE 1 ATOM 2692 C CZ . ARG A 1 337 ? -20.314 48.376 10.167 1.00 43.25 ? 355 ARG A CZ 1 ATOM 2693 N NH1 . ARG A 1 337 ? -21.145 47.349 10.272 1.00 45.84 ? 355 ARG A NH1 1 ATOM 2694 N NH2 . ARG A 1 337 ? -20.085 48.937 8.991 1.00 42.83 ? 355 ARG A NH2 1 ATOM 2695 N N . TYR A 1 338 ? -18.536 53.373 15.512 1.00 33.43 ? 356 TYR A N 1 ATOM 2696 C CA . TYR A 1 338 ? -18.743 54.818 15.643 1.00 33.42 ? 356 TYR A CA 1 ATOM 2697 C C . TYR A 1 338 ? -17.750 55.442 16.605 1.00 32.98 ? 356 TYR A C 1 ATOM 2698 O O . TYR A 1 338 ? -17.361 54.825 17.579 1.00 32.96 ? 356 TYR A O 1 ATOM 2699 C CB . TYR A 1 338 ? -20.166 55.112 16.108 1.00 34.05 ? 356 TYR A CB 1 ATOM 2700 C CG . TYR A 1 338 ? -21.183 54.486 15.186 1.00 35.93 ? 356 TYR A CG 1 ATOM 2701 C CD1 . TYR A 1 338 ? -21.440 55.044 13.950 1.00 39.20 ? 356 TYR A CD1 1 ATOM 2702 C CD2 . TYR A 1 338 ? -21.825 53.306 15.527 1.00 38.46 ? 356 TYR A CD2 1 ATOM 2703 C CE1 . TYR A 1 338 ? -22.351 54.465 13.072 1.00 41.15 ? 356 TYR A CE1 1 ATOM 2704 C CE2 . TYR A 1 338 ? -22.741 52.713 14.654 1.00 41.41 ? 356 TYR A CE2 1 ATOM 2705 C CZ . TYR A 1 338 ? -22.992 53.305 13.431 1.00 42.38 ? 356 TYR A CZ 1 ATOM 2706 O OH . TYR A 1 338 ? -23.897 52.737 12.566 1.00 47.61 ? 356 TYR A OH 1 ATOM 2707 N N . ASP A 1 339 ? -17.365 56.676 16.305 1.00 32.69 ? 357 ASP A N 1 ATOM 2708 C CA . ASP A 1 339 ? -16.293 57.359 17.033 1.00 32.68 ? 357 ASP A CA 1 ATOM 2709 C C . ASP A 1 339 ? -16.803 58.333 18.070 1.00 32.47 ? 357 ASP A C 1 ATOM 2710 O O . ASP A 1 339 ? -16.018 59.054 18.680 1.00 32.86 ? 357 ASP A O 1 ATOM 2711 C CB . ASP A 1 339 ? -15.300 58.054 16.078 1.00 32.72 ? 357 ASP A CB 1 ATOM 2712 C CG . ASP A 1 339 ? -15.914 59.189 15.278 1.00 34.41 ? 357 ASP A CG 1 ATOM 2713 O OD1 . ASP A 1 339 ? -17.016 59.661 15.622 1.00 35.47 ? 357 ASP A OD1 1 ATOM 2714 O OD2 . ASP A 1 339 ? -15.265 59.629 14.306 1.00 37.50 ? 357 ASP A OD2 1 ATOM 2715 N N . ASN A 1 340 ? -18.113 58.346 18.290 1.00 32.49 ? 358 ASN A N 1 ATOM 2716 C CA . ASN A 1 340 ? -18.672 59.364 19.186 1.00 32.16 ? 358 ASN A CA 1 ATOM 2717 C C . ASN A 1 340 ? -18.920 58.963 20.635 1.00 31.67 ? 358 ASN A C 1 ATOM 2718 O O . ASN A 1 340 ? -18.195 59.392 21.539 1.00 32.16 ? 358 ASN A O 1 ATOM 2719 C CB . ASN A 1 340 ? -19.886 60.097 18.575 1.00 32.49 ? 358 ASN A CB 1 ATOM 2720 C CG . ASN A 1 340 ? -21.044 59.185 18.173 1.00 32.67 ? 358 ASN A CG 1 ATOM 2721 O OD1 . ASN A 1 340 ? -21.007 57.942 18.237 1.00 31.86 ? 358 ASN A OD1 1 ATOM 2722 N ND2 . ASN A 1 340 ? -22.122 59.843 17.733 1.00 36.54 ? 358 ASN A ND2 1 ATOM 2723 N N . VAL A 1 341 ? -19.943 58.148 20.838 1.00 32.08 ? 359 VAL A N 1 ATOM 2724 C CA . VAL A 1 341 ? -20.324 57.691 22.166 1.00 32.20 ? 359 VAL A CA 1 ATOM 2725 C C . VAL A 1 341 ? -20.461 56.187 22.240 1.00 32.58 ? 359 VAL A C 1 ATOM 2726 O O . VAL A 1 341 ? -20.808 55.523 21.276 1.00 33.07 ? 359 VAL A O 1 ATOM 2727 C CB . VAL A 1 341 ? -21.638 58.377 22.660 1.00 32.93 ? 359 VAL A CB 1 ATOM 2728 C CG1 . VAL A 1 341 ? -21.413 59.884 22.800 1.00 32.71 ? 359 VAL A CG1 1 ATOM 2729 C CG2 . VAL A 1 341 ? -22.823 58.060 21.728 1.00 31.33 ? 359 VAL A CG2 1 ATOM 2730 N N . SER A 1 342 ? -20.103 55.674 23.405 1.00 33.28 ? 360 SER A N 1 ATOM 2731 C CA . SER A 1 342 ? -20.243 54.252 23.745 1.00 33.78 ? 360 SER A CA 1 ATOM 2732 C C . SER A 1 342 ? -20.654 54.097 25.205 1.00 33.90 ? 360 SER A C 1 ATOM 2733 O O . SER A 1 342 ? -20.750 55.082 25.940 1.00 33.52 ? 360 SER A O 1 ATOM 2734 C CB . SER A 1 342 ? -18.908 53.507 23.507 1.00 33.74 ? 360 SER A CB 1 ATOM 2735 O OG . SER A 1 342 ? -17.821 54.077 24.244 1.00 34.92 ? 360 SER A OG 1 ATOM 2736 N N . SER A 1 343 ? -20.827 52.855 25.643 1.00 34.57 ? 361 SER A N 1 ATOM 2737 C CA . SER A 1 343 ? -21.146 52.592 27.053 1.00 35.14 ? 361 SER A CA 1 ATOM 2738 C C . SER A 1 343 ? -19.980 51.996 27.819 1.00 34.76 ? 361 SER A C 1 ATOM 2739 O O . SER A 1 343 ? -20.045 51.847 29.035 1.00 34.77 ? 361 SER A O 1 ATOM 2740 C CB . SER A 1 343 ? -22.392 51.711 27.195 1.00 35.75 ? 361 SER A CB 1 ATOM 2741 O OG . SER A 1 343 ? -22.289 50.526 26.427 1.00 38.42 ? 361 SER A OG 1 ATOM 2742 N N . VAL A 1 344 ? -18.918 51.653 27.103 1.00 34.05 ? 362 VAL A N 1 ATOM 2743 C CA . VAL A 1 344 ? -17.673 51.224 27.741 1.00 33.60 ? 362 VAL A CA 1 ATOM 2744 C C . VAL A 1 344 ? -16.500 52.026 27.226 1.00 32.78 ? 362 VAL A C 1 ATOM 2745 O O . VAL A 1 344 ? -16.501 52.510 26.091 1.00 32.54 ? 362 VAL A O 1 ATOM 2746 C CB . VAL A 1 344 ? -17.378 49.709 27.547 1.00 34.31 ? 362 VAL A CB 1 ATOM 2747 C CG1 . VAL A 1 344 ? -18.503 48.843 28.124 1.00 35.62 ? 362 VAL A CG1 1 ATOM 2748 C CG2 . VAL A 1 344 ? -17.153 49.382 26.091 1.00 32.86 ? 362 VAL A CG2 1 ATOM 2749 N N . TRP A 1 345 ? -15.507 52.174 28.097 1.00 32.63 ? 363 TRP A N 1 ATOM 2750 C CA . TRP A 1 345 ? -14.274 52.884 27.756 1.00 32.45 ? 363 TRP A CA 1 ATOM 2751 C C . TRP A 1 345 ? -13.345 51.947 26.981 1.00 32.26 ? 363 TRP A C 1 ATOM 2752 O O . TRP A 1 345 ? -12.930 50.909 27.502 1.00 31.60 ? 363 TRP A O 1 ATOM 2753 C CB . TRP A 1 345 ? -13.552 53.392 29.002 1.00 32.67 ? 363 TRP A CB 1 ATOM 2754 C CG . TRP A 1 345 ? -14.330 54.416 29.767 1.00 32.08 ? 363 TRP A CG 1 ATOM 2755 C CD1 . TRP A 1 345 ? -15.011 54.227 30.937 1.00 34.63 ? 363 TRP A CD1 1 ATOM 2756 C CD2 . TRP A 1 345 ? -14.481 55.804 29.435 1.00 33.28 ? 363 TRP A CD2 1 ATOM 2757 N NE1 . TRP A 1 345 ? -15.599 55.414 31.345 1.00 34.14 ? 363 TRP A NE1 1 ATOM 2758 C CE2 . TRP A 1 345 ? -15.288 56.392 30.435 1.00 34.28 ? 363 TRP A CE2 1 ATOM 2759 C CE3 . TRP A 1 345 ? -14.035 56.602 28.378 1.00 31.83 ? 363 TRP A CE3 1 ATOM 2760 C CZ2 . TRP A 1 345 ? -15.644 57.733 30.404 1.00 33.95 ? 363 TRP A CZ2 1 ATOM 2761 C CZ3 . TRP A 1 345 ? -14.390 57.929 28.355 1.00 31.85 ? 363 TRP A CZ3 1 ATOM 2762 C CH2 . TRP A 1 345 ? -15.191 58.482 29.361 1.00 32.61 ? 363 TRP A CH2 1 ATOM 2763 N N . PRO A 1 346 ? -13.018 52.312 25.735 1.00 32.11 ? 364 PRO A N 1 ATOM 2764 C CA . PRO A 1 346 ? -12.082 51.477 24.976 1.00 31.92 ? 364 PRO A CA 1 ATOM 2765 C C . PRO A 1 346 ? -10.715 51.409 25.634 1.00 31.93 ? 364 PRO A C 1 ATOM 2766 O O . PRO A 1 346 ? -10.196 52.418 26.106 1.00 32.14 ? 364 PRO A O 1 ATOM 2767 C CB . PRO A 1 346 ? -11.985 52.197 23.637 1.00 32.31 ? 364 PRO A CB 1 ATOM 2768 C CG . PRO A 1 346 ? -13.228 53.046 23.559 1.00 32.17 ? 364 PRO A CG 1 ATOM 2769 C CD . PRO A 1 346 ? -13.449 53.484 24.962 1.00 31.66 ? 364 PRO A CD 1 ATOM 2770 N N . LEU A 1 347 ? -10.166 50.201 25.655 1.00 31.27 ? 365 LEU A N 1 ATOM 2771 C CA . LEU A 1 347 ? -8.877 49.908 26.276 1.00 30.72 ? 365 LEU A CA 1 ATOM 2772 C C . LEU A 1 347 ? -7.813 49.689 25.220 1.00 30.08 ? 365 LEU A C 1 ATOM 2773 O O . LEU A 1 347 ? -8.057 49.034 24.199 1.00 28.90 ? 365 LEU A O 1 ATOM 2774 C CB . LEU A 1 347 ? -8.957 48.657 27.137 1.00 31.33 ? 365 LEU A CB 1 ATOM 2775 C CG . LEU A 1 347 ? -9.852 48.761 28.377 1.00 35.22 ? 365 LEU A CG 1 ATOM 2776 C CD1 . LEU A 1 347 ? -10.079 47.379 29.013 1.00 37.40 ? 365 LEU A CD1 1 ATOM 2777 C CD2 . LEU A 1 347 ? -9.296 49.759 29.416 1.00 37.53 ? 365 LEU A CD2 1 ATOM 2778 N N . TYR A 1 348 ? -6.628 50.227 25.501 1.00 29.24 ? 366 TYR A N 1 ATOM 2779 C CA . TYR A 1 348 ? -5.460 50.119 24.603 1.00 29.01 ? 366 TYR A CA 1 ATOM 2780 C C . TYR A 1 348 ? -5.821 50.488 23.167 1.00 29.08 ? 366 TYR A C 1 ATOM 2781 O O . TYR A 1 348 ? -5.411 49.831 22.187 1.00 28.51 ? 366 TYR A O 1 ATOM 2782 C CB . TYR A 1 348 ? -4.843 48.719 24.671 1.00 29.76 ? 366 TYR A CB 1 ATOM 2783 C CG . TYR A 1 348 ? -4.384 48.420 26.082 1.00 31.14 ? 366 TYR A CG 1 ATOM 2784 C CD1 . TYR A 1 348 ? -3.421 49.209 26.656 1.00 35.88 ? 366 TYR A CD1 1 ATOM 2785 C CD2 . TYR A 1 348 ? -4.936 47.399 26.837 1.00 33.58 ? 366 TYR A CD2 1 ATOM 2786 C CE1 . TYR A 1 348 ? -2.983 48.997 27.938 1.00 36.66 ? 366 TYR A CE1 1 ATOM 2787 C CE2 . TYR A 1 348 ? -4.493 47.173 28.146 1.00 36.25 ? 366 TYR A CE2 1 ATOM 2788 C CZ . TYR A 1 348 ? -3.526 47.985 28.677 1.00 36.83 ? 366 TYR A CZ 1 ATOM 2789 O OH . TYR A 1 348 ? -3.051 47.834 29.954 1.00 42.90 ? 366 TYR A OH 1 ATOM 2790 N N . SER A 1 349 ? -6.531 51.593 23.055 1.00 28.43 ? 367 SER A N 1 ATOM 2791 C CA . SER A 1 349 ? -7.203 51.913 21.809 1.00 28.75 ? 367 SER A CA 1 ATOM 2792 C C . SER A 1 349 ? -6.299 52.585 20.788 1.00 27.97 ? 367 SER A C 1 ATOM 2793 O O . SER A 1 349 ? -5.268 53.195 21.102 1.00 27.50 ? 367 SER A O 1 ATOM 2794 C CB . SER A 1 349 ? -8.448 52.766 22.070 1.00 29.32 ? 367 SER A CB 1 ATOM 2795 O OG . SER A 1 349 ? -8.059 54.082 22.389 1.00 30.77 ? 367 SER A OG 1 ATOM 2796 N N . TYR A 1 350 ? -6.721 52.410 19.548 1.00 27.13 ? 368 TYR A N 1 ATOM 2797 C CA . TYR A 1 350 ? -6.127 53.026 18.376 1.00 27.28 ? 368 TYR A CA 1 ATOM 2798 C C . TYR A 1 350 ? -7.236 53.538 17.448 1.00 27.91 ? 368 TYR A C 1 ATOM 2799 O O . TYR A 1 350 ? -8.196 52.829 17.190 1.00 27.30 ? 368 TYR A O 1 ATOM 2800 C CB . TYR A 1 350 ? -5.288 51.983 17.614 1.00 27.31 ? 368 TYR A CB 1 ATOM 2801 C CG . TYR A 1 350 ? -4.772 52.468 16.288 1.00 27.75 ? 368 TYR A CG 1 ATOM 2802 C CD1 . TYR A 1 350 ? -3.651 53.272 16.212 1.00 28.75 ? 368 TYR A CD1 1 ATOM 2803 C CD2 . TYR A 1 350 ? -5.440 52.158 15.108 1.00 27.80 ? 368 TYR A CD2 1 ATOM 2804 C CE1 . TYR A 1 350 ? -3.201 53.758 14.981 1.00 30.01 ? 368 TYR A CE1 1 ATOM 2805 C CE2 . TYR A 1 350 ? -4.981 52.603 13.886 1.00 28.44 ? 368 TYR A CE2 1 ATOM 2806 C CZ . TYR A 1 350 ? -3.873 53.413 13.828 1.00 31.47 ? 368 TYR A CZ 1 ATOM 2807 O OH . TYR A 1 350 ? -3.433 53.862 12.612 1.00 31.21 ? 368 TYR A OH 1 ATOM 2808 N N . GLY A 1 351 ? -7.077 54.763 16.963 1.00 28.28 ? 369 GLY A N 1 ATOM 2809 C CA . GLY A 1 351 ? -8.051 55.375 16.045 1.00 29.65 ? 369 GLY A CA 1 ATOM 2810 C C . GLY A 1 351 ? -8.803 56.510 16.693 1.00 30.79 ? 369 GLY A C 1 ATOM 2811 O O . GLY A 1 351 ? -8.329 57.131 17.653 1.00 32.42 ? 369 GLY A O 1 ATOM 2812 N N . ARG A 1 352 ? -9.980 56.788 16.147 1.00 31.36 ? 370 ARG A N 1 ATOM 2813 C CA . ARG A 1 352 ? -10.874 57.799 16.678 1.00 31.81 ? 370 ARG A CA 1 ATOM 2814 C C . ARG A 1 352 ? -11.897 57.108 17.558 1.00 31.60 ? 370 ARG A C 1 ATOM 2815 O O . ARG A 1 352 ? -12.818 56.435 17.071 1.00 31.74 ? 370 ARG A O 1 ATOM 2816 C CB . ARG A 1 352 ? -11.543 58.575 15.532 1.00 32.37 ? 370 ARG A CB 1 ATOM 2817 C CG . ARG A 1 352 ? -10.535 59.250 14.618 1.00 34.18 ? 370 ARG A CG 1 ATOM 2818 C CD . ARG A 1 352 ? -11.223 60.051 13.519 1.00 38.75 ? 370 ARG A CD 1 ATOM 2819 N NE . ARG A 1 352 ? -12.225 59.246 12.818 1.00 42.06 ? 370 ARG A NE 1 ATOM 2820 C CZ . ARG A 1 352 ? -11.969 58.484 11.752 1.00 43.96 ? 370 ARG A CZ 1 ATOM 2821 N NH1 . ARG A 1 352 ? -10.744 58.432 11.244 1.00 43.39 ? 370 ARG A NH1 1 ATOM 2822 N NH2 . ARG A 1 352 ? -12.946 57.785 11.180 1.00 43.44 ? 370 ARG A NH2 1 ATOM 2823 N N . CYS A 1 353 ? -11.727 57.264 18.864 1.00 31.49 ? 371 CYS A N 1 ATOM 2824 C CA . CYS A 1 353 ? -12.507 56.468 19.802 1.00 32.53 ? 371 CYS A CA 1 ATOM 2825 C C . CYS A 1 353 ? -13.583 57.244 20.570 1.00 32.07 ? 371 CYS A C 1 ATOM 2826 O O . CYS A 1 353 ? -13.430 58.420 20.905 1.00 32.09 ? 371 CYS A O 1 ATOM 2827 C CB . CYS A 1 353 ? -11.589 55.678 20.736 1.00 33.91 ? 371 CYS A CB 1 ATOM 2828 S SG . CYS A 1 353 ? -10.618 54.374 19.794 1.00 38.81 ? 371 CYS A SG 1 ATOM 2829 N N . PRO A 1 354 ? -14.706 56.577 20.814 1.00 32.00 ? 372 PRO A N 1 ATOM 2830 C CA . PRO A 1 354 ? -15.852 57.169 21.482 1.00 31.54 ? 372 PRO A CA 1 ATOM 2831 C C . PRO A 1 354 ? -15.602 57.351 22.946 1.00 31.67 ? 372 PRO A C 1 ATOM 2832 O O . PRO A 1 354 ? -14.731 56.695 23.522 1.00 31.22 ? 372 PRO A O 1 ATOM 2833 C CB . PRO A 1 354 ? -16.922 56.106 21.292 1.00 31.87 ? 372 PRO A CB 1 ATOM 2834 C CG . PRO A 1 354 ? -16.153 54.833 21.284 1.00 31.51 ? 372 PRO A CG 1 ATOM 2835 C CD . PRO A 1 354 ? -14.962 55.172 20.454 1.00 31.81 ? 372 PRO A CD 1 ATOM 2836 N N . THR A 1 355 ? -16.369 58.261 23.534 1.00 31.88 ? 373 THR A N 1 ATOM 2837 C CA . THR A 1 355 ? -16.395 58.475 24.978 1.00 32.09 ? 373 THR A CA 1 ATOM 2838 C C . THR A 1 355 ? -17.550 57.732 25.622 1.00 32.62 ? 373 THR A C 1 ATOM 2839 O O . THR A 1 355 ? -18.628 57.634 25.054 1.00 32.87 ? 373 THR A O 1 ATOM 2840 C CB . THR A 1 355 ? -16.535 59.958 25.349 1.00 32.00 ? 373 THR A CB 1 ATOM 2841 O OG1 . THR A 1 355 ? -16.403 60.092 26.765 1.00 31.89 ? 373 THR A OG1 1 ATOM 2842 C CG2 . THR A 1 355 ? -17.914 60.506 24.927 1.00 30.57 ? 373 THR A CG2 1 ATOM 2843 N N . ALA A 1 356 ? -17.296 57.181 26.797 1.00 33.66 ? 374 ALA A N 1 ATOM 2844 C CA . ALA A 1 356 ? -18.341 56.521 27.575 1.00 34.69 ? 374 ALA A CA 1 ATOM 2845 C C . ALA A 1 356 ? -18.859 57.480 28.644 1.00 35.55 ? 374 ALA A C 1 ATOM 2846 O O . ALA A 1 356 ? -19.516 57.058 29.600 1.00 35.90 ? 374 ALA A O 1 ATOM 2847 C CB . ALA A 1 356 ? -17.828 55.242 28.217 1.00 34.16 ? 374 ALA A CB 1 ATOM 2848 N N . ALA A 1 357 ? -18.550 58.762 28.481 1.00 36.25 ? 375 ALA A N 1 ATOM 2849 C CA . ALA A 1 357 ? -19.059 59.792 29.416 1.00 37.53 ? 375 ALA A CA 1 ATOM 2850 C C . ALA A 1 357 ? -20.537 60.118 29.182 1.00 38.65 ? 375 ALA A C 1 ATOM 2851 O O . ALA A 1 357 ? -21.115 59.847 28.135 1.00 39.13 ? 375 ALA A O 1 ATOM 2852 C CB . ALA A 1 357 ? -18.224 61.069 29.353 1.00 37.15 ? 375 ALA A CB 1 ATOM 2853 N N . ASP A 1 358 ? -21.132 60.728 30.194 1.00 40.47 ? 376 ASP A N 1 ATOM 2854 C CA . ASP A 1 358 ? -22.556 61.131 30.143 1.00 41.35 ? 376 ASP A CA 1 ATOM 2855 C C . ASP A 1 358 ? -22.997 61.828 28.842 1.00 41.30 ? 376 ASP A C 1 ATOM 2856 O O . ASP A 1 358 ? -22.718 63.006 28.612 1.00 41.28 ? 376 ASP A O 1 ATOM 2857 C CB . ASP A 1 358 ? -22.899 61.985 31.353 1.00 42.27 ? 376 ASP A CB 1 ATOM 2858 C CG . ASP A 1 358 ? -23.114 61.140 32.591 1.00 45.50 ? 376 ASP A CG 1 ATOM 2859 O OD1 . ASP A 1 358 ? -22.937 59.908 32.454 1.00 49.32 ? 376 ASP A OD1 1 ATOM 2860 O OD2 . ASP A 1 358 ? -23.484 61.685 33.674 1.00 50.60 ? 376 ASP A OD2 1 HETATM 2861 C C1 . NAG B 2 . ? -2.330 29.063 26.852 1.00 47.70 ? 1961 NAG A C1 1 HETATM 2862 C C2 . NAG B 2 . ? -2.908 30.109 27.808 1.00 50.54 ? 1961 NAG A C2 1 HETATM 2863 C C3 . NAG B 2 . ? -2.325 29.931 29.197 1.00 52.79 ? 1961 NAG A C3 1 HETATM 2864 C C4 . NAG B 2 . ? -2.553 28.502 29.678 1.00 53.76 ? 1961 NAG A C4 1 HETATM 2865 C C5 . NAG B 2 . ? -2.086 27.489 28.640 1.00 53.24 ? 1961 NAG A C5 1 HETATM 2866 C C6 . NAG B 2 . ? -2.607 26.118 29.040 1.00 54.01 ? 1961 NAG A C6 1 HETATM 2867 C C7 . NAG B 2 . ? -3.486 32.232 26.692 1.00 50.15 ? 1961 NAG A C7 1 HETATM 2868 C C8 . NAG B 2 . ? -2.983 33.614 26.378 1.00 49.49 ? 1961 NAG A C8 1 HETATM 2869 N N2 . NAG B 2 . ? -2.636 31.478 27.396 1.00 49.82 ? 1961 NAG A N2 1 HETATM 2870 O O3 . NAG B 2 . ? -2.942 30.879 30.048 1.00 53.71 ? 1961 NAG A O3 1 HETATM 2871 O O4 . NAG B 2 . ? -1.855 28.255 30.885 1.00 55.34 ? 1961 NAG A O4 1 HETATM 2872 O O5 . NAG B 2 . ? -2.574 27.765 27.336 1.00 50.10 ? 1961 NAG A O5 1 HETATM 2873 O O6 . NAG B 2 . ? -1.994 25.172 28.195 1.00 57.48 ? 1961 NAG A O6 1 HETATM 2874 O O7 . NAG B 2 . ? -4.598 31.860 26.297 1.00 49.46 ? 1961 NAG A O7 1 HETATM 2875 C C1 . NAG C 2 . ? 9.784 37.550 -1.801 1.00 34.19 ? 2523 NAG A C1 1 HETATM 2876 C C2 . NAG C 2 . ? 11.238 37.434 -2.226 1.00 34.63 ? 2523 NAG A C2 1 HETATM 2877 C C3 . NAG C 2 . ? 11.889 38.807 -2.233 1.00 38.44 ? 2523 NAG A C3 1 HETATM 2878 C C4 . NAG C 2 . ? 11.092 39.786 -3.058 1.00 39.29 ? 2523 NAG A C4 1 HETATM 2879 C C5 . NAG C 2 . ? 9.647 39.807 -2.558 1.00 39.46 ? 2523 NAG A C5 1 HETATM 2880 C C6 . NAG C 2 . ? 8.782 40.686 -3.442 1.00 41.04 ? 2523 NAG A C6 1 HETATM 2881 C C7 . NAG C 2 . ? 12.401 35.339 -1.594 1.00 34.37 ? 2523 NAG A C7 1 HETATM 2882 C C8 . NAG C 2 . ? 12.041 34.792 -2.915 1.00 27.80 ? 2523 NAG A C8 1 HETATM 2883 N N2 . NAG C 2 . ? 11.990 36.577 -1.331 1.00 32.93 ? 2523 NAG A N2 1 HETATM 2884 O O3 . NAG C 2 . ? 13.216 38.686 -2.680 1.00 38.55 ? 2523 NAG A O3 1 HETATM 2885 O O4 . NAG C 2 . ? 11.664 41.085 -2.974 1.00 43.59 ? 2523 NAG A O4 1 HETATM 2886 O O5 . NAG C 2 . ? 9.100 38.504 -2.591 1.00 37.04 ? 2523 NAG A O5 1 HETATM 2887 O O6 . NAG C 2 . ? 8.737 40.200 -4.781 1.00 41.16 ? 2523 NAG A O6 1 HETATM 2888 O O7 . NAG C 2 . ? 13.046 34.624 -0.805 1.00 37.50 ? 2523 NAG A O7 1 HETATM 2889 C C1 . NAG D 2 . ? 29.486 27.058 25.497 1.00 32.35 ? 2525 NAG A C1 1 HETATM 2890 C C2 . NAG D 2 . ? 30.525 27.556 26.494 1.00 32.92 ? 2525 NAG A C2 1 HETATM 2891 C C3 . NAG D 2 . ? 31.971 27.324 26.020 1.00 34.60 ? 2525 NAG A C3 1 HETATM 2892 C C4 . NAG D 2 . ? 32.183 25.914 25.483 1.00 34.15 ? 2525 NAG A C4 1 HETATM 2893 C C5 . NAG D 2 . ? 31.105 25.653 24.435 1.00 33.19 ? 2525 NAG A C5 1 HETATM 2894 C C6 . NAG D 2 . ? 31.246 24.269 23.767 1.00 33.40 ? 2525 NAG A C6 1 HETATM 2895 C C7 . NAG D 2 . ? 30.189 29.539 27.893 1.00 36.20 ? 2525 NAG A C7 1 HETATM 2896 C C8 . NAG D 2 . ? 30.210 28.588 29.027 1.00 32.24 ? 2525 NAG A C8 1 HETATM 2897 N N2 . NAG D 2 . ? 30.341 29.000 26.687 1.00 33.20 ? 2525 NAG A N2 1 HETATM 2898 O O3 . NAG D 2 . ? 32.907 27.623 27.046 1.00 33.95 ? 2525 NAG A O3 1 HETATM 2899 O O4 . NAG D 2 . ? 33.452 25.899 24.856 1.00 36.43 ? 2525 NAG A O4 1 HETATM 2900 O O5 . NAG D 2 . ? 29.827 25.748 25.058 1.00 31.80 ? 2525 NAG A O5 1 HETATM 2901 O O6 . NAG D 2 . ? 31.073 23.255 24.743 1.00 33.51 ? 2525 NAG A O6 1 HETATM 2902 O O7 . NAG D 2 . ? 30.043 30.764 28.072 1.00 38.46 ? 2525 NAG A O7 1 HETATM 2903 C C1 . NAG E 2 . ? 34.139 24.663 25.191 1.00 40.80 ? 2526 NAG A C1 1 HETATM 2904 C C2 . NAG E 2 . ? 35.501 24.668 24.522 1.00 42.13 ? 2526 NAG A C2 1 HETATM 2905 C C3 . NAG E 2 . ? 36.296 23.400 24.870 1.00 45.22 ? 2526 NAG A C3 1 HETATM 2906 C C4 . NAG E 2 . ? 36.375 23.190 26.369 1.00 47.29 ? 2526 NAG A C4 1 HETATM 2907 C C5 . NAG E 2 . ? 35.012 23.377 27.040 1.00 47.59 ? 2526 NAG A C5 1 HETATM 2908 C C6 . NAG E 2 . ? 35.245 23.587 28.533 1.00 47.53 ? 2526 NAG A C6 1 HETATM 2909 C C7 . NAG E 2 . ? 35.482 25.826 22.346 1.00 41.29 ? 2526 NAG A C7 1 HETATM 2910 C C8 . NAG E 2 . ? 35.885 27.093 23.020 1.00 39.14 ? 2526 NAG A C8 1 HETATM 2911 N N2 . NAG E 2 . ? 35.315 24.734 23.087 1.00 40.16 ? 2526 NAG A N2 1 HETATM 2912 O O3 . NAG E 2 . ? 37.598 23.536 24.352 1.00 45.07 ? 2526 NAG A O3 1 HETATM 2913 O O4 . NAG E 2 . ? 36.840 21.875 26.649 1.00 51.18 ? 2526 NAG A O4 1 HETATM 2914 O O5 . NAG E 2 . ? 34.307 24.519 26.584 1.00 42.98 ? 2526 NAG A O5 1 HETATM 2915 O O6 . NAG E 2 . ? 34.203 22.939 29.215 1.00 50.64 ? 2526 NAG A O6 1 HETATM 2916 O O7 . NAG E 2 . ? 35.300 25.811 21.115 1.00 46.29 ? 2526 NAG A O7 1 HETATM 2917 C C1 . NAG F 2 . ? -23.579 58.779 17.328 1.00 52.49 ? 2527 NAG A C1 1 HETATM 2918 C C2 . NAG F 2 . ? -24.626 59.856 17.532 1.00 52.86 ? 2527 NAG A C2 1 HETATM 2919 C C3 . NAG F 2 . ? -25.922 59.311 16.964 1.00 54.74 ? 2527 NAG A C3 1 HETATM 2920 C C4 . NAG F 2 . ? -25.739 58.882 15.508 1.00 55.72 ? 2527 NAG A C4 1 HETATM 2921 C C5 . NAG F 2 . ? -24.467 58.054 15.313 1.00 55.24 ? 2527 NAG A C5 1 HETATM 2922 C C6 . NAG F 2 . ? -24.161 57.864 13.833 1.00 55.70 ? 2527 NAG A C6 1 HETATM 2923 C C7 . NAG F 2 . ? -24.326 61.348 19.443 1.00 47.61 ? 2527 NAG A C7 1 HETATM 2924 C C8 . NAG F 2 . ? -23.623 62.315 18.545 1.00 45.81 ? 2527 NAG A C8 1 HETATM 2925 N N2 . NAG F 2 . ? -24.781 60.204 18.932 1.00 50.22 ? 2527 NAG A N2 1 HETATM 2926 O O3 . NAG F 2 . ? -26.867 60.341 17.066 1.00 55.37 ? 2527 NAG A O3 1 HETATM 2927 O O4 . NAG F 2 . ? -26.849 58.112 15.084 1.00 57.87 ? 2527 NAG A O4 1 HETATM 2928 O O5 . NAG F 2 . ? -23.377 58.697 15.936 1.00 53.97 ? 2527 NAG A O5 1 HETATM 2929 O O6 . NAG F 2 . ? -23.927 59.130 13.256 1.00 55.03 ? 2527 NAG A O6 1 HETATM 2930 O O7 . NAG F 2 . ? -24.470 61.614 20.627 1.00 48.05 ? 2527 NAG A O7 1 HETATM 2931 C C1 . NAG G 2 . ? -10.978 30.405 21.066 1.00 34.01 ? 2521 NAG A C1 1 HETATM 2932 C C2 . NAG G 2 . ? -10.044 29.818 22.111 1.00 35.25 ? 2521 NAG A C2 1 HETATM 2933 C C3 . NAG G 2 . ? -10.400 28.361 22.388 1.00 37.38 ? 2521 NAG A C3 1 HETATM 2934 C C4 . NAG G 2 . ? -11.897 28.204 22.637 1.00 36.81 ? 2521 NAG A C4 1 HETATM 2935 C C5 . NAG G 2 . ? -12.683 28.876 21.524 1.00 35.69 ? 2521 NAG A C5 1 HETATM 2936 C C6 . NAG G 2 . ? -14.182 28.738 21.752 1.00 37.32 ? 2521 NAG A C6 1 HETATM 2937 C C7 . NAG G 2 . ? -7.759 30.625 22.241 1.00 38.46 ? 2521 NAG A C7 1 HETATM 2938 C C8 . NAG G 2 . ? -6.375 30.658 21.634 1.00 35.11 ? 2521 NAG A C8 1 HETATM 2939 N N2 . NAG G 2 . ? -8.677 29.907 21.622 1.00 35.37 ? 2521 NAG A N2 1 HETATM 2940 O O3 . NAG G 2 . ? -9.630 27.884 23.482 1.00 37.58 ? 2521 NAG A O3 1 HETATM 2941 O O4 . NAG G 2 . ? -12.200 26.827 22.648 1.00 39.17 ? 2521 NAG A O4 1 HETATM 2942 O O5 . NAG G 2 . ? -12.327 30.239 21.501 1.00 34.63 ? 2521 NAG A O5 1 HETATM 2943 O O6 . NAG G 2 . ? -14.481 29.482 22.902 1.00 38.71 ? 2521 NAG A O6 1 HETATM 2944 O O7 . NAG G 2 . ? -8.022 31.244 23.267 1.00 41.50 ? 2521 NAG A O7 1 HETATM 2945 C C1 . NAG H 2 . ? -19.737 24.865 -2.890 1.00 51.86 ? 2520 NAG A C1 1 HETATM 2946 C C2 . NAG H 2 . ? -20.810 24.157 -3.729 1.00 56.73 ? 2520 NAG A C2 1 HETATM 2947 C C3 . NAG H 2 . ? -22.111 23.901 -2.966 1.00 57.89 ? 2520 NAG A C3 1 HETATM 2948 C C4 . NAG H 2 . ? -21.875 23.485 -1.514 1.00 57.41 ? 2520 NAG A C4 1 HETATM 2949 C C5 . NAG H 2 . ? -20.692 24.244 -0.896 1.00 55.75 ? 2520 NAG A C5 1 HETATM 2950 C C6 . NAG H 2 . ? -20.364 23.689 0.480 1.00 56.07 ? 2520 NAG A C6 1 HETATM 2951 C C7 . NAG H 2 . ? -20.720 24.497 -6.125 1.00 61.11 ? 2520 NAG A C7 1 HETATM 2952 C C8 . NAG H 2 . ? -21.048 25.391 -7.284 1.00 61.93 ? 2520 NAG A C8 1 HETATM 2953 N N2 . NAG H 2 . ? -21.089 24.939 -4.919 1.00 59.16 ? 2520 NAG A N2 1 HETATM 2954 O O3 . NAG H 2 . ? -22.833 22.885 -3.647 1.00 59.48 ? 2520 NAG A O3 1 HETATM 2955 O O4 . NAG H 2 . ? -23.052 23.688 -0.742 1.00 58.08 ? 2520 NAG A O4 1 HETATM 2956 O O5 . NAG H 2 . ? -19.559 24.102 -1.720 1.00 52.32 ? 2520 NAG A O5 1 HETATM 2957 O O6 . NAG H 2 . ? -19.869 22.379 0.305 1.00 56.88 ? 2520 NAG A O6 1 HETATM 2958 O O7 . NAG H 2 . ? -20.137 23.418 -6.297 1.00 62.18 ? 2520 NAG A O7 1 HETATM 2959 O OA4 . SIO I 3 . ? 18.330 8.296 19.934 1.00 47.83 ? 1 SIO A OA4 1 HETATM 2960 C CA4 . SIO I 3 . ? 19.494 8.417 19.588 1.00 45.87 ? 1 SIO A CA4 1 HETATM 2961 C CM4 . SIO I 3 . ? 20.592 8.711 20.553 1.00 45.08 ? 1 SIO A CM4 1 HETATM 2962 O O4 . SIO I 3 . ? 19.796 8.269 18.181 1.00 45.58 ? 1 SIO A O4 1 HETATM 2963 C C4 . SIO I 3 . ? 21.178 8.426 17.843 1.00 46.80 ? 1 SIO A C4 1 HETATM 2964 C C5 . SIO I 3 . ? 21.385 9.723 17.049 1.00 45.76 ? 1 SIO A C5 1 HETATM 2965 N N5 . SIO I 3 . ? 21.358 10.775 18.063 1.00 43.97 ? 1 SIO A N5 1 HETATM 2966 C C10 . SIO I 3 . ? 20.247 11.471 18.268 1.00 43.24 ? 1 SIO A C10 1 HETATM 2967 O O10 . SIO I 3 . ? 19.243 11.289 17.594 1.00 42.01 ? 1 SIO A O10 1 HETATM 2968 C C11 . SIO I 3 . ? 20.303 12.517 19.358 1.00 41.85 ? 1 SIO A C11 1 HETATM 2969 C C3 . SIO I 3 . ? 21.597 7.188 17.051 1.00 48.25 ? 1 SIO A C3 1 HETATM 2970 C C2 . SIO I 3 . ? 22.924 7.333 16.304 1.00 49.23 ? 1 SIO A C2 1 HETATM 2971 O O2 . SIO I 3 . ? 23.032 6.265 15.363 1.00 50.75 ? 1 SIO A O2 1 HETATM 2972 C CM2 . SIO I 3 . ? 24.076 6.516 14.445 1.00 51.11 ? 1 SIO A CM2 1 HETATM 2973 C C1 . SIO I 3 . ? 24.078 7.265 17.284 1.00 49.41 ? 1 SIO A C1 1 HETATM 2974 O O1 . SIO I 3 . ? 23.907 6.642 18.350 1.00 51.29 ? 1 SIO A O1 1 HETATM 2975 O O3 . SIO I 3 . ? 25.168 7.823 16.998 1.00 49.09 ? 1 SIO A O3 1 HETATM 2976 O O6 . SIO I 3 . ? 22.934 8.567 15.579 1.00 48.01 ? 1 SIO A O6 1 HETATM 2977 C C6 . SIO I 3 . ? 22.761 9.737 16.377 1.00 46.04 ? 1 SIO A C6 1 HETATM 2978 C C7 . SIO I 3 . ? 22.970 10.890 15.422 1.00 45.32 ? 1 SIO A C7 1 HETATM 2979 O O7 . SIO I 3 . ? 21.838 11.008 14.565 1.00 42.84 ? 1 SIO A O7 1 HETATM 2980 C C8 . SIO I 3 . ? 24.207 10.640 14.583 1.00 45.33 ? 1 SIO A C8 1 HETATM 2981 O O8 . SIO I 3 . ? 25.255 10.246 15.474 1.00 44.90 ? 1 SIO A O8 1 HETATM 2982 C C9 . SIO I 3 . ? 24.617 11.893 13.828 1.00 46.57 ? 1 SIO A C9 1 HETATM 2983 O O9 . SIO I 3 . ? 24.803 12.927 14.796 1.00 44.56 ? 1 SIO A O9 1 HETATM 2984 C CA9 . SIO I 3 . ? 25.181 14.257 14.371 1.00 44.61 ? 1 SIO A CA9 1 HETATM 2985 O OA9 . SIO I 3 . ? 25.142 14.501 13.165 1.00 42.46 ? 1 SIO A OA9 1 HETATM 2986 C CM9 . SIO I 3 . ? 25.587 15.252 15.436 1.00 41.03 ? 1 SIO A CM9 1 HETATM 2987 K K . K J 4 . ? 26.300 24.258 17.020 1.00 31.09 ? 2 K A K 1 HETATM 2988 C C . ACY K 5 . ? -5.417 25.684 5.482 1.00 34.96 ? 2001 ACY A C 1 HETATM 2989 O O . ACY K 5 . ? -4.431 26.329 5.055 1.00 34.19 ? 2001 ACY A O 1 HETATM 2990 O OXT . ACY K 5 . ? -5.717 24.530 5.077 1.00 36.39 ? 2001 ACY A OXT 1 HETATM 2991 C CH3 . ACY K 5 . ? -6.323 26.313 6.481 1.00 35.22 ? 2001 ACY A CH3 1 HETATM 2992 O O . HOH L 6 . ? -0.538 34.682 12.983 1.00 25.66 ? 2528 HOH A O 1 HETATM 2993 O O . HOH L 6 . ? -1.877 28.696 8.853 1.00 28.72 ? 2529 HOH A O 1 HETATM 2994 O O . HOH L 6 . ? 13.153 34.531 21.076 1.00 22.24 ? 2530 HOH A O 1 HETATM 2995 O O . HOH L 6 . ? 24.149 43.622 16.454 1.00 24.52 ? 2531 HOH A O 1 HETATM 2996 O O . HOH L 6 . ? 21.185 28.476 14.846 1.00 26.47 ? 2532 HOH A O 1 HETATM 2997 O O . HOH L 6 . ? -9.855 44.134 15.550 1.00 26.71 ? 2533 HOH A O 1 HETATM 2998 O O . HOH L 6 . ? -3.862 46.197 12.566 1.00 24.57 ? 2534 HOH A O 1 HETATM 2999 O O . HOH L 6 . ? 10.663 35.985 20.980 1.00 26.07 ? 2535 HOH A O 1 HETATM 3000 O O . HOH L 6 . ? -4.551 48.986 14.874 1.00 25.18 ? 2536 HOH A O 1 HETATM 3001 O O . HOH L 6 . ? 15.041 20.602 24.692 1.00 28.27 ? 2537 HOH A O 1 HETATM 3002 O O . HOH L 6 . ? 12.115 25.889 22.695 1.00 30.45 ? 2538 HOH A O 1 HETATM 3003 O O . HOH L 6 . ? -9.360 29.601 13.190 1.00 28.39 ? 2539 HOH A O 1 HETATM 3004 O O . HOH L 6 . ? -6.382 32.713 6.420 1.00 26.31 ? 2540 HOH A O 1 HETATM 3005 O O . HOH L 6 . ? 2.372 28.466 12.316 1.00 25.12 ? 2541 HOH A O 1 HETATM 3006 O O . HOH L 6 . ? -15.863 37.240 5.943 1.00 27.33 ? 2542 HOH A O 1 HETATM 3007 O O . HOH L 6 . ? -14.154 39.099 4.706 1.00 31.67 ? 2543 HOH A O 1 HETATM 3008 O O . HOH L 6 . ? -0.018 47.105 12.250 1.00 24.42 ? 2544 HOH A O 1 HETATM 3009 O O . HOH L 6 . ? 3.825 20.589 14.983 1.00 29.53 ? 2545 HOH A O 1 HETATM 3010 O O . HOH L 6 . ? -3.528 32.674 14.947 1.00 30.99 ? 2546 HOH A O 1 HETATM 3011 O O . HOH L 6 . ? 23.784 39.483 23.231 1.00 28.57 ? 2547 HOH A O 1 HETATM 3012 O O . HOH L 6 . ? -6.521 30.060 9.842 1.00 27.57 ? 2548 HOH A O 1 HETATM 3013 O O . HOH L 6 . ? 23.340 24.864 16.872 1.00 27.89 ? 2549 HOH A O 1 HETATM 3014 O O . HOH L 6 . ? 25.341 46.102 12.053 1.00 31.31 ? 2550 HOH A O 1 HETATM 3015 O O . HOH L 6 . ? 29.340 21.251 11.792 1.00 33.21 ? 2551 HOH A O 1 HETATM 3016 O O . HOH L 6 . ? 12.743 27.663 1.697 1.00 28.79 ? 2552 HOH A O 1 HETATM 3017 O O . HOH L 6 . ? 16.965 19.704 8.957 1.00 34.93 ? 2553 HOH A O 1 HETATM 3018 O O . HOH L 6 . ? 9.074 20.972 4.598 1.00 30.58 ? 2554 HOH A O 1 HETATM 3019 O O . HOH L 6 . ? 19.031 24.950 4.184 1.00 32.74 ? 2555 HOH A O 1 HETATM 3020 O O . HOH L 6 . ? 1.671 36.864 -1.741 1.00 29.57 ? 2556 HOH A O 1 HETATM 3021 O O . HOH L 6 . ? -17.907 38.183 14.985 1.00 34.95 ? 2557 HOH A O 1 HETATM 3022 O O . HOH L 6 . ? 3.467 56.083 10.271 1.00 27.88 ? 2558 HOH A O 1 HETATM 3023 O O . HOH L 6 . ? 18.160 22.592 8.540 1.00 29.74 ? 2559 HOH A O 1 HETATM 3024 O O . HOH L 6 . ? 9.981 43.978 3.945 1.00 30.58 ? 2560 HOH A O 1 HETATM 3025 O O . HOH L 6 . ? 6.113 31.928 -2.903 1.00 28.67 ? 2561 HOH A O 1 HETATM 3026 O O . HOH L 6 . ? -2.574 49.787 21.804 1.00 29.66 ? 2562 HOH A O 1 HETATM 3027 O O . HOH L 6 . ? 13.447 28.351 22.691 1.00 32.81 ? 2563 HOH A O 1 HETATM 3028 O O . HOH L 6 . ? 33.534 20.015 10.955 1.00 35.50 ? 2564 HOH A O 1 HETATM 3029 O O . HOH L 6 . ? 5.371 55.558 17.160 1.00 37.45 ? 2565 HOH A O 1 HETATM 3030 O O . HOH L 6 . ? -3.045 28.649 -3.670 1.00 32.93 ? 2566 HOH A O 1 HETATM 3031 O O . HOH L 6 . ? 19.563 47.660 9.279 1.00 28.17 ? 2567 HOH A O 1 HETATM 3032 O O . HOH L 6 . ? 31.525 21.338 9.841 1.00 36.24 ? 2568 HOH A O 1 HETATM 3033 O O . HOH L 6 . ? -12.199 24.529 16.816 1.00 31.42 ? 2569 HOH A O 1 HETATM 3034 O O . HOH L 6 . ? 30.719 22.595 16.248 1.00 33.73 ? 2570 HOH A O 1 HETATM 3035 O O . HOH L 6 . ? -15.676 28.994 15.074 1.00 36.11 ? 2571 HOH A O 1 HETATM 3036 O O . HOH L 6 . ? -2.343 51.284 24.117 1.00 33.59 ? 2572 HOH A O 1 HETATM 3037 O O . HOH L 6 . ? -2.200 29.154 15.313 1.00 28.31 ? 2573 HOH A O 1 HETATM 3038 O O . HOH L 6 . ? 23.896 48.212 13.379 1.00 33.54 ? 2574 HOH A O 1 HETATM 3039 O O . HOH L 6 . ? -21.073 37.486 0.446 1.00 32.98 ? 2575 HOH A O 1 HETATM 3040 O O . HOH L 6 . ? -17.555 35.455 15.468 1.00 39.61 ? 2576 HOH A O 1 HETATM 3041 O O . HOH L 6 . ? -19.986 49.533 17.351 1.00 35.67 ? 2577 HOH A O 1 HETATM 3042 O O . HOH L 6 . ? -3.797 30.854 19.252 1.00 30.80 ? 2578 HOH A O 1 HETATM 3043 O O . HOH L 6 . ? 21.342 34.346 22.571 1.00 31.46 ? 2579 HOH A O 1 HETATM 3044 O O . HOH L 6 . ? 21.987 39.709 2.144 1.00 36.37 ? 2580 HOH A O 1 HETATM 3045 O O . HOH L 6 . ? 15.985 36.952 -1.074 1.00 36.45 ? 2581 HOH A O 1 HETATM 3046 O O . HOH L 6 . ? -7.316 53.528 25.305 1.00 37.14 ? 2582 HOH A O 1 HETATM 3047 O O . HOH L 6 . ? 6.475 46.789 19.138 1.00 38.19 ? 2583 HOH A O 1 HETATM 3048 O O . HOH L 6 . ? 2.137 44.814 -0.459 1.00 34.28 ? 2584 HOH A O 1 HETATM 3049 O O . HOH L 6 . ? -19.951 27.311 10.608 1.00 37.02 ? 2585 HOH A O 1 HETATM 3050 O O . HOH L 6 . ? 12.006 25.910 -0.068 1.00 30.68 ? 2586 HOH A O 1 HETATM 3051 O O . HOH L 6 . ? -2.023 47.666 1.782 1.00 38.28 ? 2587 HOH A O 1 HETATM 3052 O O . HOH L 6 . ? -11.203 42.984 -4.118 1.00 32.77 ? 2588 HOH A O 1 HETATM 3053 O O . HOH L 6 . ? 33.057 41.722 7.614 1.00 37.28 ? 2589 HOH A O 1 HETATM 3054 O O . HOH L 6 . ? 12.415 52.738 7.656 1.00 32.99 ? 2590 HOH A O 1 HETATM 3055 O O . HOH L 6 . ? -1.366 51.991 20.649 1.00 38.47 ? 2591 HOH A O 1 HETATM 3056 O O . HOH L 6 . ? 6.031 35.641 24.210 1.00 34.10 ? 2592 HOH A O 1 HETATM 3057 O O . HOH L 6 . ? -19.368 42.586 10.259 1.00 38.63 ? 2593 HOH A O 1 HETATM 3058 O O . HOH L 6 . ? 4.611 39.652 24.946 1.00 36.34 ? 2594 HOH A O 1 HETATM 3059 O O . HOH L 6 . ? -1.730 29.372 18.043 1.00 31.13 ? 2595 HOH A O 1 HETATM 3060 O O . HOH L 6 . ? 8.407 35.281 -4.436 1.00 42.29 ? 2596 HOH A O 1 HETATM 3061 O O . HOH L 6 . ? 21.584 25.851 3.026 1.00 36.88 ? 2597 HOH A O 1 HETATM 3062 O O . HOH L 6 . ? 6.096 17.245 23.629 1.00 40.78 ? 2598 HOH A O 1 HETATM 3063 O O . HOH L 6 . ? 5.701 15.534 21.488 1.00 38.76 ? 2599 HOH A O 1 HETATM 3064 O O . HOH L 6 . ? 28.175 44.249 10.373 1.00 34.39 ? 2600 HOH A O 1 HETATM 3065 O O . HOH L 6 . ? -5.692 51.534 8.385 1.00 35.55 ? 2601 HOH A O 1 HETATM 3066 O O . HOH L 6 . ? -3.997 53.028 9.917 1.00 38.53 ? 2602 HOH A O 1 HETATM 3067 O O . HOH L 6 . ? 23.040 19.387 22.794 1.00 33.48 ? 2603 HOH A O 1 HETATM 3068 O O . HOH L 6 . ? -10.126 48.724 2.184 1.00 35.60 ? 2604 HOH A O 1 HETATM 3069 O O . HOH L 6 . ? 28.023 25.644 28.725 1.00 33.34 ? 2605 HOH A O 1 HETATM 3070 O O . HOH L 6 . ? -3.486 34.548 13.092 1.00 37.61 ? 2606 HOH A O 1 HETATM 3071 O O . HOH L 6 . ? -18.158 37.399 4.369 1.00 32.88 ? 2607 HOH A O 1 HETATM 3072 O O . HOH L 6 . ? -12.442 38.002 20.104 1.00 32.19 ? 2608 HOH A O 1 HETATM 3073 O O . HOH L 6 . ? -19.486 41.260 17.847 1.00 37.06 ? 2609 HOH A O 1 HETATM 3074 O O . HOH L 6 . ? 23.823 21.371 16.231 1.00 35.30 ? 2610 HOH A O 1 HETATM 3075 O O . HOH L 6 . ? 1.878 40.669 -1.868 1.00 36.81 ? 2611 HOH A O 1 HETATM 3076 O O . HOH L 6 . ? -3.837 26.153 -3.628 1.00 46.19 ? 2612 HOH A O 1 HETATM 3077 O O . HOH L 6 . ? 8.266 53.565 14.889 1.00 34.58 ? 2613 HOH A O 1 HETATM 3078 O O . HOH L 6 . ? 19.413 22.168 4.459 1.00 38.37 ? 2614 HOH A O 1 HETATM 3079 O O . HOH L 6 . ? 18.742 34.645 22.618 1.00 41.56 ? 2615 HOH A O 1 HETATM 3080 O O . HOH L 6 . ? -3.961 40.372 -2.626 1.00 33.48 ? 2616 HOH A O 1 HETATM 3081 O O . HOH L 6 . ? -5.741 51.389 28.045 1.00 36.84 ? 2617 HOH A O 1 HETATM 3082 O O . HOH L 6 . ? 11.408 42.697 19.039 1.00 32.78 ? 2618 HOH A O 1 HETATM 3083 O O . HOH L 6 . ? -19.248 25.410 19.536 1.00 37.81 ? 2619 HOH A O 1 HETATM 3084 O O . HOH L 6 . ? 24.026 45.149 4.937 1.00 33.48 ? 2620 HOH A O 1 HETATM 3085 O O . HOH L 6 . ? 24.043 30.756 0.748 1.00 42.54 ? 2621 HOH A O 1 HETATM 3086 O O . HOH L 6 . ? -1.610 50.165 1.594 1.00 39.11 ? 2622 HOH A O 1 HETATM 3087 O O . HOH L 6 . ? 11.276 13.321 13.652 1.00 40.27 ? 2623 HOH A O 1 HETATM 3088 O O . HOH L 6 . ? 23.168 20.294 28.057 1.00 34.11 ? 2624 HOH A O 1 HETATM 3089 O O . HOH L 6 . ? -11.111 51.150 2.876 1.00 33.50 ? 2625 HOH A O 1 HETATM 3090 O O . HOH L 6 . ? 20.146 21.823 6.928 1.00 31.93 ? 2626 HOH A O 1 HETATM 3091 O O . HOH L 6 . ? -5.004 56.622 17.382 1.00 34.01 ? 2627 HOH A O 1 HETATM 3092 O O . HOH L 6 . ? -2.942 53.925 19.740 1.00 35.99 ? 2628 HOH A O 1 HETATM 3093 O O . HOH L 6 . ? 2.465 19.898 21.754 1.00 41.73 ? 2629 HOH A O 1 HETATM 3094 O O . HOH L 6 . ? -1.794 31.965 -2.865 1.00 32.80 ? 2630 HOH A O 1 HETATM 3095 O O . HOH L 6 . ? -9.376 58.704 20.152 1.00 38.38 ? 2631 HOH A O 1 HETATM 3096 O O . HOH L 6 . ? 14.011 30.003 0.378 1.00 45.59 ? 2632 HOH A O 1 HETATM 3097 O O . HOH L 6 . ? -11.258 59.438 21.975 1.00 42.99 ? 2633 HOH A O 1 HETATM 3098 O O . HOH L 6 . ? -4.123 37.174 23.729 1.00 42.23 ? 2634 HOH A O 1 HETATM 3099 O O . HOH L 6 . ? 28.325 15.126 10.295 1.00 40.37 ? 2635 HOH A O 1 HETATM 3100 O O . HOH L 6 . ? 6.786 30.406 23.629 1.00 34.55 ? 2636 HOH A O 1 HETATM 3101 O O . HOH L 6 . ? -5.959 35.774 -1.144 1.00 33.02 ? 2637 HOH A O 1 HETATM 3102 O O . HOH L 6 . ? -15.803 50.656 30.678 1.00 44.01 ? 2638 HOH A O 1 HETATM 3103 O O . HOH L 6 . ? -18.457 45.552 13.361 1.00 42.57 ? 2639 HOH A O 1 HETATM 3104 O O . HOH L 6 . ? -7.274 54.960 2.605 1.00 41.93 ? 2640 HOH A O 1 HETATM 3105 O O . HOH L 6 . ? -12.369 46.866 1.994 1.00 46.84 ? 2641 HOH A O 1 HETATM 3106 O O . HOH L 6 . ? 4.875 44.587 -0.519 1.00 35.23 ? 2642 HOH A O 1 HETATM 3107 O O . HOH L 6 . ? -5.570 44.169 23.667 1.00 43.31 ? 2643 HOH A O 1 HETATM 3108 O O . HOH L 6 . ? 16.887 20.988 4.558 1.00 39.98 ? 2644 HOH A O 1 HETATM 3109 O O . HOH L 6 . ? 1.754 16.582 19.002 1.00 41.31 ? 2645 HOH A O 1 HETATM 3110 O O . HOH L 6 . ? -3.686 26.794 16.810 1.00 38.90 ? 2646 HOH A O 1 HETATM 3111 O O . HOH L 6 . ? -20.230 50.529 24.043 1.00 42.94 ? 2647 HOH A O 1 HETATM 3112 O O . HOH L 6 . ? -1.909 55.315 6.412 1.00 34.95 ? 2648 HOH A O 1 HETATM 3113 O O . HOH L 6 . ? 16.412 40.191 19.443 1.00 31.62 ? 2649 HOH A O 1 HETATM 3114 O O . HOH L 6 . ? 13.850 20.463 27.143 1.00 36.89 ? 2650 HOH A O 1 HETATM 3115 O O . HOH L 6 . ? 14.714 15.831 18.708 1.00 46.22 ? 2651 HOH A O 1 HETATM 3116 O O . HOH L 6 . ? -5.739 40.946 -4.804 1.00 45.84 ? 2652 HOH A O 1 HETATM 3117 O O . HOH L 6 . ? 35.409 26.980 10.116 1.00 40.13 ? 2653 HOH A O 1 HETATM 3118 O O . HOH L 6 . ? -8.531 22.415 17.452 1.00 34.17 ? 2654 HOH A O 1 HETATM 3119 O O . HOH L 6 . ? 21.208 46.809 3.665 1.00 48.45 ? 2655 HOH A O 1 HETATM 3120 O O . HOH L 6 . ? -9.822 53.331 28.634 1.00 38.52 ? 2656 HOH A O 1 HETATM 3121 O O . HOH L 6 . ? 4.269 27.599 -1.371 1.00 39.79 ? 2657 HOH A O 1 HETATM 3122 O O . HOH L 6 . ? 27.690 47.730 19.973 1.00 45.67 ? 2658 HOH A O 1 HETATM 3123 O O . HOH L 6 . ? -6.879 21.794 20.751 1.00 40.79 ? 2659 HOH A O 1 HETATM 3124 O O . HOH L 6 . ? 29.371 27.936 1.448 1.00 39.82 ? 2660 HOH A O 1 HETATM 3125 O O . HOH L 6 . ? 6.609 43.721 1.587 1.00 33.14 ? 2661 HOH A O 1 HETATM 3126 O O . HOH L 6 . ? -1.537 21.742 7.580 1.00 36.89 ? 2662 HOH A O 1 HETATM 3127 O O . HOH L 6 . ? 9.364 47.276 1.322 1.00 42.18 ? 2663 HOH A O 1 HETATM 3128 O O . HOH L 6 . ? 20.377 11.880 22.782 1.00 45.49 ? 2664 HOH A O 1 HETATM 3129 O O . HOH L 6 . ? -17.749 29.536 3.381 1.00 41.22 ? 2665 HOH A O 1 HETATM 3130 O O . HOH L 6 . ? 6.321 45.937 21.584 1.00 44.60 ? 2666 HOH A O 1 HETATM 3131 O O . HOH L 6 . ? -11.973 40.607 21.140 1.00 36.87 ? 2667 HOH A O 1 HETATM 3132 O O . HOH L 6 . ? 15.740 31.615 27.556 1.00 45.97 ? 2668 HOH A O 1 HETATM 3133 O O . HOH L 6 . ? -3.326 46.277 22.284 1.00 39.63 ? 2669 HOH A O 1 HETATM 3134 O O . HOH L 6 . ? -1.516 46.637 -0.790 1.00 38.92 ? 2670 HOH A O 1 HETATM 3135 O O . HOH L 6 . ? 3.387 54.858 7.474 1.00 34.21 ? 2671 HOH A O 1 HETATM 3136 O O . HOH L 6 . ? 23.074 46.053 17.370 1.00 39.57 ? 2672 HOH A O 1 HETATM 3137 O O . HOH L 6 . ? -10.768 33.647 23.104 1.00 41.55 ? 2673 HOH A O 1 HETATM 3138 O O . HOH L 6 . ? -1.616 35.531 -1.804 1.00 40.28 ? 2674 HOH A O 1 HETATM 3139 O O . HOH L 6 . ? 18.274 45.365 15.703 1.00 43.47 ? 2675 HOH A O 1 HETATM 3140 O O . HOH L 6 . ? 33.236 30.873 24.316 1.00 44.07 ? 2676 HOH A O 1 HETATM 3141 O O . HOH L 6 . ? 6.114 54.748 7.345 1.00 37.66 ? 2677 HOH A O 1 HETATM 3142 O O . HOH L 6 . ? 4.209 36.276 -2.501 1.00 36.11 ? 2678 HOH A O 1 HETATM 3143 O O . HOH L 6 . ? 25.349 45.174 0.577 1.00 43.71 ? 2679 HOH A O 1 HETATM 3144 O O . HOH L 6 . ? 6.081 28.999 25.763 1.00 42.95 ? 2680 HOH A O 1 HETATM 3145 O O . HOH L 6 . ? 22.583 48.170 15.867 1.00 43.13 ? 2681 HOH A O 1 HETATM 3146 O O . HOH L 6 . ? -1.485 25.486 23.537 1.00 38.55 ? 2682 HOH A O 1 HETATM 3147 O O . HOH L 6 . ? 19.897 12.633 15.247 1.00 46.71 ? 2683 HOH A O 1 HETATM 3148 O O . HOH L 6 . ? 2.325 18.953 7.368 1.00 45.41 ? 2684 HOH A O 1 HETATM 3149 O O . HOH L 6 . ? 33.543 31.846 5.137 1.00 38.76 ? 2685 HOH A O 1 HETATM 3150 O O . HOH L 6 . ? -4.639 16.157 16.635 1.00 38.82 ? 2686 HOH A O 1 HETATM 3151 O O . HOH L 6 . ? 8.616 53.516 17.530 1.00 42.02 ? 2687 HOH A O 1 HETATM 3152 O O . HOH L 6 . ? 12.652 46.130 16.424 1.00 40.15 ? 2688 HOH A O 1 HETATM 3153 O O . HOH L 6 . ? 10.173 39.854 22.377 1.00 36.04 ? 2689 HOH A O 1 HETATM 3154 O O . HOH L 6 . ? 34.522 44.452 10.099 1.00 36.58 ? 2690 HOH A O 1 HETATM 3155 O O . HOH L 6 . ? 34.037 30.341 20.523 1.00 36.40 ? 2691 HOH A O 1 HETATM 3156 O O . HOH L 6 . ? 10.090 37.005 23.435 1.00 35.70 ? 2692 HOH A O 1 HETATM 3157 O O . HOH L 6 . ? 13.903 34.115 23.746 1.00 44.75 ? 2693 HOH A O 1 HETATM 3158 O O . HOH L 6 . ? -0.924 54.713 12.514 1.00 37.21 ? 2694 HOH A O 1 HETATM 3159 O O . HOH L 6 . ? 5.029 34.071 -4.010 1.00 46.86 ? 2695 HOH A O 1 HETATM 3160 O O . HOH L 6 . ? -5.401 44.049 -7.373 1.00 51.67 ? 2696 HOH A O 1 HETATM 3161 O O . HOH L 6 . ? 13.658 29.395 25.140 1.00 42.89 ? 2697 HOH A O 1 HETATM 3162 O O . HOH L 6 . ? 10.251 44.963 19.892 1.00 49.55 ? 2698 HOH A O 1 HETATM 3163 O O . HOH L 6 . ? -12.641 55.011 9.806 1.00 43.45 ? 2699 HOH A O 1 HETATM 3164 O O . HOH L 6 . ? -3.338 55.348 8.499 1.00 37.60 ? 2700 HOH A O 1 HETATM 3165 O O . HOH L 6 . ? 14.616 50.811 11.471 1.00 42.33 ? 2701 HOH A O 1 HETATM 3166 O O . HOH L 6 . ? 15.559 13.795 22.205 1.00 39.04 ? 2702 HOH A O 1 HETATM 3167 O O . HOH L 6 . ? -14.055 36.069 21.766 1.00 43.56 ? 2703 HOH A O 1 HETATM 3168 O O . HOH L 6 . ? 18.138 40.856 0.690 1.00 45.87 ? 2704 HOH A O 1 HETATM 3169 O O . HOH L 6 . ? -18.459 57.437 13.642 1.00 49.10 ? 2705 HOH A O 1 HETATM 3170 O O . HOH L 6 . ? 13.993 24.628 -0.933 1.00 42.71 ? 2706 HOH A O 1 HETATM 3171 O O . HOH L 6 . ? 3.739 36.963 25.304 1.00 36.33 ? 2707 HOH A O 1 HETATM 3172 O O . HOH L 6 . ? 18.055 19.379 33.796 1.00 41.30 ? 2708 HOH A O 1 HETATM 3173 O O . HOH L 6 . ? 3.163 25.931 0.293 1.00 42.00 ? 2709 HOH A O 1 HETATM 3174 O O . HOH L 6 . ? -3.614 49.473 31.646 1.00 44.31 ? 2710 HOH A O 1 HETATM 3175 O O . HOH L 6 . ? 35.445 33.226 18.557 1.00 45.09 ? 2711 HOH A O 1 HETATM 3176 O O . HOH L 6 . ? -18.079 34.000 17.582 1.00 40.88 ? 2712 HOH A O 1 HETATM 3177 O O . HOH L 6 . ? -14.968 41.593 20.592 1.00 41.24 ? 2713 HOH A O 1 HETATM 3178 O O . HOH L 6 . ? 27.563 23.777 25.193 1.00 39.58 ? 2714 HOH A O 1 HETATM 3179 O O . HOH L 6 . ? 16.088 24.034 1.150 1.00 40.28 ? 2715 HOH A O 1 HETATM 3180 O O . HOH L 6 . ? -6.163 28.166 18.982 1.00 41.53 ? 2716 HOH A O 1 HETATM 3181 O O . HOH L 6 . ? 4.936 47.205 23.192 1.00 47.68 ? 2717 HOH A O 1 HETATM 3182 O O . HOH L 6 . ? -18.820 28.593 14.077 1.00 44.69 ? 2718 HOH A O 1 HETATM 3183 O O . HOH L 6 . ? 0.727 21.641 22.987 1.00 44.05 ? 2719 HOH A O 1 HETATM 3184 O O . HOH L 6 . ? 25.777 22.329 1.225 1.00 48.37 ? 2720 HOH A O 1 HETATM 3185 O O . HOH L 6 . ? 6.269 32.933 24.552 1.00 47.28 ? 2721 HOH A O 1 HETATM 3186 O O . HOH L 6 . ? 17.553 11.778 21.924 1.00 43.21 ? 2722 HOH A O 1 HETATM 3187 O O . HOH L 6 . ? -13.627 49.333 3.024 1.00 45.60 ? 2723 HOH A O 1 HETATM 3188 O O . HOH L 6 . ? 26.124 5.870 20.049 1.00 44.52 ? 2724 HOH A O 1 HETATM 3189 O O . HOH L 6 . ? 13.183 30.419 -2.107 1.00 56.14 ? 2725 HOH A O 1 HETATM 3190 O O . HOH L 6 . ? 27.180 48.120 11.598 1.00 43.05 ? 2726 HOH A O 1 HETATM 3191 O O . HOH L 6 . ? 20.944 28.027 1.667 1.00 40.01 ? 2727 HOH A O 1 HETATM 3192 O O . HOH L 6 . ? -15.413 21.946 -5.179 1.00 52.28 ? 2728 HOH A O 1 HETATM 3193 O O . HOH L 6 . ? 9.476 19.478 26.123 1.00 39.36 ? 2729 HOH A O 1 HETATM 3194 O O . HOH L 6 . ? -24.250 41.053 1.312 1.00 51.92 ? 2730 HOH A O 1 HETATM 3195 O O . HOH L 6 . ? 38.072 22.576 16.404 1.00 47.50 ? 2731 HOH A O 1 HETATM 3196 O O . HOH L 6 . ? -7.591 56.177 20.381 1.00 45.68 ? 2732 HOH A O 1 HETATM 3197 O O . HOH L 6 . ? 15.893 48.903 3.766 1.00 44.15 ? 2733 HOH A O 1 HETATM 3198 O O . HOH L 6 . ? 21.186 30.822 1.985 1.00 39.07 ? 2734 HOH A O 1 HETATM 3199 O O . HOH L 6 . ? -19.582 26.130 15.368 1.00 40.40 ? 2735 HOH A O 1 HETATM 3200 O O . HOH L 6 . ? -10.690 19.104 7.155 1.00 50.34 ? 2736 HOH A O 1 HETATM 3201 O O . HOH L 6 . ? -10.628 54.861 3.539 1.00 50.74 ? 2737 HOH A O 1 HETATM 3202 O O . HOH L 6 . ? -3.519 56.743 4.569 1.00 47.11 ? 2738 HOH A O 1 HETATM 3203 O O . HOH L 6 . ? 27.405 46.775 8.993 1.00 45.66 ? 2739 HOH A O 1 HETATM 3204 O O . HOH L 6 . ? -0.187 30.915 -4.935 1.00 53.17 ? 2740 HOH A O 1 HETATM 3205 O O . HOH L 6 . ? -13.671 33.389 22.114 1.00 48.68 ? 2741 HOH A O 1 HETATM 3206 O O . HOH L 6 . ? -14.918 17.282 6.471 1.00 48.84 ? 2742 HOH A O 1 HETATM 3207 O O . HOH L 6 . ? 8.437 36.335 24.945 1.00 47.34 ? 2743 HOH A O 1 HETATM 3208 O O . HOH L 6 . ? 17.276 30.453 1.479 1.00 42.71 ? 2744 HOH A O 1 HETATM 3209 O O . HOH L 6 . ? -20.364 37.818 5.934 1.00 42.41 ? 2745 HOH A O 1 HETATM 3210 O O . HOH L 6 . ? 35.176 42.698 14.226 1.00 46.59 ? 2746 HOH A O 1 HETATM 3211 O O . HOH L 6 . ? 1.506 17.401 21.609 1.00 47.44 ? 2747 HOH A O 1 HETATM 3212 O O . HOH L 6 . ? 19.680 38.496 1.350 1.00 41.26 ? 2748 HOH A O 1 HETATM 3213 O O . HOH L 6 . ? 24.256 42.392 -1.087 1.00 46.61 ? 2749 HOH A O 1 HETATM 3214 O O . HOH L 6 . ? -16.323 33.322 2.749 1.00 44.75 ? 2750 HOH A O 1 HETATM 3215 O O . HOH L 6 . ? -21.895 48.589 15.637 1.00 42.39 ? 2751 HOH A O 1 HETATM 3216 O O . HOH L 6 . ? -6.345 35.939 24.584 1.00 46.09 ? 2752 HOH A O 1 HETATM 3217 O O . HOH L 6 . ? 6.320 38.152 -3.278 1.00 44.88 ? 2753 HOH A O 1 HETATM 3218 O O . HOH L 6 . ? 16.161 19.591 2.627 1.00 50.99 ? 2754 HOH A O 1 HETATM 3219 O O . HOH L 6 . ? 11.112 44.878 1.745 1.00 41.78 ? 2755 HOH A O 1 HETATM 3220 O O . HOH L 6 . ? -4.054 53.492 23.641 0.50 23.80 ? 2756 HOH A O 1 HETATM 3221 O O . HOH L 6 . ? 14.181 42.625 19.711 1.00 49.95 ? 2757 HOH A O 1 HETATM 3222 O O . HOH L 6 . ? -15.347 54.402 9.524 1.00 51.01 ? 2758 HOH A O 1 HETATM 3223 O O . HOH L 6 . ? -20.411 37.094 8.465 1.00 39.08 ? 2759 HOH A O 1 HETATM 3224 O O . HOH L 6 . ? -20.867 40.591 5.819 1.00 44.01 ? 2760 HOH A O 1 HETATM 3225 O O . HOH L 6 . ? -5.730 49.954 30.366 1.00 42.93 ? 2761 HOH A O 1 HETATM 3226 O O . HOH L 6 . ? 15.210 37.156 21.122 1.00 42.99 ? 2762 HOH A O 1 HETATM 3227 O O . HOH L 6 . ? 13.419 32.068 25.823 1.00 48.13 ? 2763 HOH A O 1 HETATM 3228 O O . HOH L 6 . ? -15.210 46.988 28.526 1.00 45.43 ? 2764 HOH A O 1 HETATM 3229 O O . HOH L 6 . ? 28.188 11.208 12.820 1.00 46.92 ? 2765 HOH A O 1 HETATM 3230 O O . HOH L 6 . ? -21.151 58.634 26.175 1.00 43.13 ? 2766 HOH A O 1 HETATM 3231 O O . HOH L 6 . ? 3.068 44.536 26.940 1.00 48.97 ? 2767 HOH A O 1 HETATM 3232 O O . HOH L 6 . ? -18.190 35.013 3.112 1.00 51.08 ? 2768 HOH A O 1 HETATM 3233 O O . HOH L 6 . ? 16.369 11.777 30.094 1.00 48.14 ? 2769 HOH A O 1 HETATM 3234 O O . HOH L 6 . ? 22.316 13.219 31.880 1.00 44.22 ? 2770 HOH A O 1 HETATM 3235 O O . HOH L 6 . ? 28.596 49.260 13.408 1.00 45.64 ? 2771 HOH A O 1 HETATM 3236 O O . HOH L 6 . ? 19.848 25.995 26.852 1.00 46.62 ? 2772 HOH A O 1 HETATM 3237 O O . HOH L 6 . ? -21.187 40.872 2.952 1.00 49.54 ? 2773 HOH A O 1 HETATM 3238 O O . HOH L 6 . ? 7.229 49.462 20.151 1.00 45.93 ? 2774 HOH A O 1 HETATM 3239 O O . HOH L 6 . ? 0.031 21.960 5.307 1.00 45.19 ? 2775 HOH A O 1 HETATM 3240 O O . HOH L 6 . ? 31.085 10.909 19.068 1.00 47.85 ? 2776 HOH A O 1 HETATM 3241 O O . HOH L 6 . ? 4.033 15.111 19.338 1.00 45.61 ? 2777 HOH A O 1 HETATM 3242 O O . HOH L 6 . ? 29.924 18.627 26.100 1.00 40.47 ? 2778 HOH A O 1 HETATM 3243 O O . HOH L 6 . ? -17.868 52.807 10.728 1.00 52.11 ? 2779 HOH A O 1 HETATM 3244 O O . HOH L 6 . ? -16.721 32.103 0.515 1.00 53.95 ? 2780 HOH A O 1 HETATM 3245 O O . HOH L 6 . ? 17.950 26.623 24.887 1.00 42.02 ? 2781 HOH A O 1 HETATM 3246 O O . HOH L 6 . ? 28.419 24.457 2.841 1.00 54.78 ? 2782 HOH A O 1 HETATM 3247 O O . HOH L 6 . ? 14.216 44.952 18.338 1.00 50.34 ? 2783 HOH A O 1 HETATM 3248 O O . HOH L 6 . ? 1.794 22.755 2.192 1.00 42.15 ? 2784 HOH A O 1 HETATM 3249 O O . HOH L 6 . ? 1.505 50.129 0.724 1.00 47.47 ? 2786 HOH A O 1 HETATM 3250 O O . HOH L 6 . ? -6.181 38.234 -2.962 1.00 38.72 ? 2787 HOH A O 1 HETATM 3251 O O . HOH L 6 . ? -16.472 51.657 4.997 1.00 44.46 ? 2788 HOH A O 1 HETATM 3252 O O . HOH L 6 . ? 14.256 10.224 13.992 1.00 53.35 ? 2790 HOH A O 1 HETATM 3253 O O . HOH L 6 . ? 29.849 11.527 26.866 1.00 49.61 ? 2791 HOH A O 1 HETATM 3254 O O . HOH L 6 . ? -18.269 29.158 -4.797 1.00 46.82 ? 2792 HOH A O 1 HETATM 3255 O O . HOH L 6 . ? 1.295 34.017 -4.774 1.00 40.83 ? 2793 HOH A O 1 HETATM 3256 O O . HOH L 6 . ? 3.518 16.952 8.645 1.00 48.54 ? 2794 HOH A O 1 HETATM 3257 O O . HOH L 6 . ? 22.257 23.908 1.320 1.00 43.58 ? 2795 HOH A O 1 HETATM 3258 O O . HOH L 6 . ? 16.857 11.836 19.005 1.00 48.89 ? 2796 HOH A O 1 HETATM 3259 O O . HOH L 6 . ? 7.856 25.805 -1.534 1.00 43.06 ? 2797 HOH A O 1 HETATM 3260 O O . HOH L 6 . ? -18.283 36.847 19.192 1.00 43.48 ? 2798 HOH A O 1 HETATM 3261 O O . HOH L 6 . ? -15.096 18.455 16.578 1.00 52.47 ? 2799 HOH A O 1 HETATM 3262 O O . HOH L 6 . ? 9.173 11.887 21.792 1.00 51.17 ? 2800 HOH A O 1 HETATM 3263 O O . HOH L 6 . ? 25.515 46.942 6.919 1.00 46.79 ? 2801 HOH A O 1 HETATM 3264 O O . HOH L 6 . ? -20.775 34.483 9.325 1.00 40.64 ? 2802 HOH A O 1 HETATM 3265 O O . HOH L 6 . ? -10.582 56.815 8.575 1.00 46.38 ? 2803 HOH A O 1 HETATM 3266 O O . HOH L 6 . ? 10.900 26.737 -2.401 1.00 41.71 ? 2804 HOH A O 1 HETATM 3267 O O . HOH L 6 . ? 33.665 28.849 6.839 1.00 44.22 ? 2805 HOH A O 1 HETATM 3268 O O . HOH L 6 . ? 8.900 12.162 13.901 1.00 53.20 ? 2806 HOH A O 1 HETATM 3269 O O . HOH L 6 . ? -22.213 38.883 2.261 1.00 57.00 ? 2807 HOH A O 1 HETATM 3270 O O . HOH L 6 . ? 7.134 39.741 25.446 1.00 43.24 ? 2808 HOH A O 1 HETATM 3271 O O . HOH L 6 . ? -6.658 33.019 24.843 1.00 48.97 ? 2809 HOH A O 1 HETATM 3272 O O . HOH L 6 . ? -17.381 50.453 11.072 1.00 50.34 ? 2810 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 ALA 22 40 40 ALA ALA 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 SIO 1 1 1 SIO SIO A . J 4 K 1 2 2 K K A . K 5 ACY 1 2001 2001 ACY ACY A . L 6 HOH 1 2528 2528 HOH HOH A . L 6 HOH 2 2529 2529 HOH HOH A . L 6 HOH 3 2530 2530 HOH HOH A . L 6 HOH 4 2531 2531 HOH HOH A . L 6 HOH 5 2532 2532 HOH HOH A . L 6 HOH 6 2533 2533 HOH HOH A . L 6 HOH 7 2534 2534 HOH HOH A . L 6 HOH 8 2535 2535 HOH HOH A . L 6 HOH 9 2536 2536 HOH HOH A . L 6 HOH 10 2537 2537 HOH HOH A . L 6 HOH 11 2538 2538 HOH HOH A . L 6 HOH 12 2539 2539 HOH HOH A . L 6 HOH 13 2540 2540 HOH HOH A . L 6 HOH 14 2541 2541 HOH HOH A . L 6 HOH 15 2542 2542 HOH HOH A . L 6 HOH 16 2543 2543 HOH HOH A . L 6 HOH 17 2544 2544 HOH HOH A . L 6 HOH 18 2545 2545 HOH HOH A . L 6 HOH 19 2546 2546 HOH HOH A . L 6 HOH 20 2547 2547 HOH HOH A . L 6 HOH 21 2548 2548 HOH HOH A . L 6 HOH 22 2549 2549 HOH HOH A . L 6 HOH 23 2550 2550 HOH HOH A . L 6 HOH 24 2551 2551 HOH HOH A . L 6 HOH 25 2552 2552 HOH HOH A . L 6 HOH 26 2553 2553 HOH HOH A . L 6 HOH 27 2554 2554 HOH HOH A . L 6 HOH 28 2555 2555 HOH HOH A . L 6 HOH 29 2556 2556 HOH HOH A . L 6 HOH 30 2557 2557 HOH HOH A . L 6 HOH 31 2558 2558 HOH HOH A . L 6 HOH 32 2559 2559 HOH HOH A . L 6 HOH 33 2560 2560 HOH HOH A . L 6 HOH 34 2561 2561 HOH HOH A . L 6 HOH 35 2562 2562 HOH HOH A . L 6 HOH 36 2563 2563 HOH HOH A . L 6 HOH 37 2564 2564 HOH HOH A . L 6 HOH 38 2565 2565 HOH HOH A . L 6 HOH 39 2566 2566 HOH HOH A . L 6 HOH 40 2567 2567 HOH HOH A . L 6 HOH 41 2568 2568 HOH HOH A . L 6 HOH 42 2569 2569 HOH HOH A . L 6 HOH 43 2570 2570 HOH HOH A . L 6 HOH 44 2571 2571 HOH HOH A . L 6 HOH 45 2572 2572 HOH HOH A . L 6 HOH 46 2573 2573 HOH HOH A . L 6 HOH 47 2574 2574 HOH HOH A . L 6 HOH 48 2575 2575 HOH HOH A . L 6 HOH 49 2576 2576 HOH HOH A . L 6 HOH 50 2577 2577 HOH HOH A . L 6 HOH 51 2578 2578 HOH HOH A . L 6 HOH 52 2579 2579 HOH HOH A . L 6 HOH 53 2580 2580 HOH HOH A . L 6 HOH 54 2581 2581 HOH HOH A . L 6 HOH 55 2582 2582 HOH HOH A . L 6 HOH 56 2583 2583 HOH HOH A . L 6 HOH 57 2584 2584 HOH HOH A . L 6 HOH 58 2585 2585 HOH HOH A . L 6 HOH 59 2586 2586 HOH HOH A . L 6 HOH 60 2587 2587 HOH HOH A . L 6 HOH 61 2588 2588 HOH HOH A . L 6 HOH 62 2589 2589 HOH HOH A . L 6 HOH 63 2590 2590 HOH HOH A . L 6 HOH 64 2591 2591 HOH HOH A . L 6 HOH 65 2592 2592 HOH HOH A . L 6 HOH 66 2593 2593 HOH HOH A . L 6 HOH 67 2594 2594 HOH HOH A . L 6 HOH 68 2595 2595 HOH HOH A . L 6 HOH 69 2596 2596 HOH HOH A . L 6 HOH 70 2597 2597 HOH HOH A . L 6 HOH 71 2598 2598 HOH HOH A . L 6 HOH 72 2599 2599 HOH HOH A . L 6 HOH 73 2600 2600 HOH HOH A . L 6 HOH 74 2601 2601 HOH HOH A . L 6 HOH 75 2602 2602 HOH HOH A . L 6 HOH 76 2603 2603 HOH HOH A . L 6 HOH 77 2604 2604 HOH HOH A . L 6 HOH 78 2605 2605 HOH HOH A . L 6 HOH 79 2606 2606 HOH HOH A . L 6 HOH 80 2607 2607 HOH HOH A . L 6 HOH 81 2608 2608 HOH HOH A . L 6 HOH 82 2609 2609 HOH HOH A . L 6 HOH 83 2610 2610 HOH HOH A . L 6 HOH 84 2611 2611 HOH HOH A . L 6 HOH 85 2612 2612 HOH HOH A . L 6 HOH 86 2613 2613 HOH HOH A . L 6 HOH 87 2614 2614 HOH HOH A . L 6 HOH 88 2615 2615 HOH HOH A . L 6 HOH 89 2616 2616 HOH HOH A . L 6 HOH 90 2617 2617 HOH HOH A . L 6 HOH 91 2618 2618 HOH HOH A . L 6 HOH 92 2619 2619 HOH HOH A . L 6 HOH 93 2620 2620 HOH HOH A . L 6 HOH 94 2621 2621 HOH HOH A . L 6 HOH 95 2622 2622 HOH HOH A . L 6 HOH 96 2623 2623 HOH HOH A . L 6 HOH 97 2624 2624 HOH HOH A . L 6 HOH 98 2625 2625 HOH HOH A . L 6 HOH 99 2626 2626 HOH HOH A . L 6 HOH 100 2627 2627 HOH HOH A . L 6 HOH 101 2628 2628 HOH HOH A . L 6 HOH 102 2629 2629 HOH HOH A . L 6 HOH 103 2630 2630 HOH HOH A . L 6 HOH 104 2631 2631 HOH HOH A . L 6 HOH 105 2632 2632 HOH HOH A . L 6 HOH 106 2633 2633 HOH HOH A . L 6 HOH 107 2634 2634 HOH HOH A . L 6 HOH 108 2635 2635 HOH HOH A . L 6 HOH 109 2636 2636 HOH HOH A . L 6 HOH 110 2637 2637 HOH HOH A . L 6 HOH 111 2638 2638 HOH HOH A . L 6 HOH 112 2639 2639 HOH HOH A . L 6 HOH 113 2640 2640 HOH HOH A . L 6 HOH 114 2641 2641 HOH HOH A . L 6 HOH 115 2642 2642 HOH HOH A . L 6 HOH 116 2643 2643 HOH HOH A . L 6 HOH 117 2644 2644 HOH HOH A . L 6 HOH 118 2645 2645 HOH HOH A . L 6 HOH 119 2646 2646 HOH HOH A . L 6 HOH 120 2647 2647 HOH HOH A . L 6 HOH 121 2648 2648 HOH HOH A . L 6 HOH 122 2649 2649 HOH HOH A . L 6 HOH 123 2650 2650 HOH HOH A . L 6 HOH 124 2651 2651 HOH HOH A . L 6 HOH 125 2652 2652 HOH HOH A . L 6 HOH 126 2653 2653 HOH HOH A . L 6 HOH 127 2654 2654 HOH HOH A . L 6 HOH 128 2655 2655 HOH HOH A . L 6 HOH 129 2656 2656 HOH HOH A . L 6 HOH 130 2657 2657 HOH HOH A . L 6 HOH 131 2658 2658 HOH HOH A . L 6 HOH 132 2659 2659 HOH HOH A . L 6 HOH 133 2660 2660 HOH HOH A . L 6 HOH 134 2661 2661 HOH HOH A . L 6 HOH 135 2662 2662 HOH HOH A . L 6 HOH 136 2663 2663 HOH HOH A . L 6 HOH 137 2664 2664 HOH HOH A . L 6 HOH 138 2665 2665 HOH HOH A . L 6 HOH 139 2666 2666 HOH HOH A . L 6 HOH 140 2667 2667 HOH HOH A . L 6 HOH 141 2668 2668 HOH HOH A . L 6 HOH 142 2669 2669 HOH HOH A . L 6 HOH 143 2670 2670 HOH HOH A . L 6 HOH 144 2671 2671 HOH HOH A . L 6 HOH 145 2672 2672 HOH HOH A . L 6 HOH 146 2673 2673 HOH HOH A . L 6 HOH 147 2674 2674 HOH HOH A . L 6 HOH 148 2675 2675 HOH HOH A . L 6 HOH 149 2676 2676 HOH HOH A . L 6 HOH 150 2677 2677 HOH HOH A . L 6 HOH 151 2678 2678 HOH HOH A . L 6 HOH 152 2679 2679 HOH HOH A . L 6 HOH 153 2680 2680 HOH HOH A . L 6 HOH 154 2681 2681 HOH HOH A . L 6 HOH 155 2682 2682 HOH HOH A . L 6 HOH 156 2683 2683 HOH HOH A . L 6 HOH 157 2684 2684 HOH HOH A . L 6 HOH 158 2685 2685 HOH HOH A . L 6 HOH 159 2686 2686 HOH HOH A . L 6 HOH 160 2687 2687 HOH HOH A . L 6 HOH 161 2688 2688 HOH HOH A . L 6 HOH 162 2689 2689 HOH HOH A . L 6 HOH 163 2690 2690 HOH HOH A . L 6 HOH 164 2691 2691 HOH HOH A . L 6 HOH 165 2692 2692 HOH HOH A . L 6 HOH 166 2693 2693 HOH HOH A . L 6 HOH 167 2694 2694 HOH HOH A . L 6 HOH 168 2695 2695 HOH HOH A . L 6 HOH 169 2696 2696 HOH HOH A . L 6 HOH 170 2697 2697 HOH HOH A . L 6 HOH 171 2698 2698 HOH HOH A . L 6 HOH 172 2699 2699 HOH HOH A . L 6 HOH 173 2700 2700 HOH HOH A . L 6 HOH 174 2701 2701 HOH HOH A . L 6 HOH 175 2702 2702 HOH HOH A . L 6 HOH 176 2703 2703 HOH HOH A . L 6 HOH 177 2704 2704 HOH HOH A . L 6 HOH 178 2705 2705 HOH HOH A . L 6 HOH 179 2706 2706 HOH HOH A . L 6 HOH 180 2707 2707 HOH HOH A . L 6 HOH 181 2708 2708 HOH HOH A . L 6 HOH 182 2709 2709 HOH HOH A . L 6 HOH 183 2710 2710 HOH HOH A . L 6 HOH 184 2711 2711 HOH HOH A . L 6 HOH 185 2712 2712 HOH HOH A . L 6 HOH 186 2713 2713 HOH HOH A . L 6 HOH 187 2714 2714 HOH HOH A . L 6 HOH 188 2715 2715 HOH HOH A . L 6 HOH 189 2716 2716 HOH HOH A . L 6 HOH 190 2717 2717 HOH HOH A . L 6 HOH 191 2718 2718 HOH HOH A . L 6 HOH 192 2719 2719 HOH HOH A . L 6 HOH 193 2720 2720 HOH HOH A . L 6 HOH 194 2721 2721 HOH HOH A . L 6 HOH 195 2722 2722 HOH HOH A . L 6 HOH 196 2723 2723 HOH HOH A . L 6 HOH 197 2724 2724 HOH HOH A . L 6 HOH 198 2725 2725 HOH HOH A . L 6 HOH 199 2726 2726 HOH HOH A . L 6 HOH 200 2727 2727 HOH HOH A . L 6 HOH 201 2728 2728 HOH HOH A . L 6 HOH 202 2729 2729 HOH HOH A . L 6 HOH 203 2730 2730 HOH HOH A . L 6 HOH 204 2731 2731 HOH HOH A . L 6 HOH 205 2732 2732 HOH HOH A . L 6 HOH 206 2733 2733 HOH HOH A . L 6 HOH 207 2734 2734 HOH HOH A . L 6 HOH 208 2735 2735 HOH HOH A . L 6 HOH 209 2736 2736 HOH HOH A . L 6 HOH 210 2737 2737 HOH HOH A . L 6 HOH 211 2738 2738 HOH HOH A . L 6 HOH 212 2739 2739 HOH HOH A . L 6 HOH 213 2740 2740 HOH HOH A . L 6 HOH 214 2741 2741 HOH HOH A . L 6 HOH 215 2742 2742 HOH HOH A . L 6 HOH 216 2743 2743 HOH HOH A . L 6 HOH 217 2744 2744 HOH HOH A . L 6 HOH 218 2745 2745 HOH HOH A . L 6 HOH 219 2746 2746 HOH HOH A . L 6 HOH 220 2747 2747 HOH HOH A . L 6 HOH 221 2748 2748 HOH HOH A . L 6 HOH 222 2749 2749 HOH HOH A . L 6 HOH 223 2750 2750 HOH HOH A . L 6 HOH 224 2751 2751 HOH HOH A . L 6 HOH 225 2752 2752 HOH HOH A . L 6 HOH 226 2753 2753 HOH HOH A . L 6 HOH 227 2754 2754 HOH HOH A . L 6 HOH 228 2755 2755 HOH HOH A . L 6 HOH 229 2756 2756 HOH HOH A . L 6 HOH 230 2757 2757 HOH HOH A . L 6 HOH 231 2758 2758 HOH HOH A . L 6 HOH 232 2759 2759 HOH HOH A . L 6 HOH 233 2760 2760 HOH HOH A . L 6 HOH 234 2761 2761 HOH HOH A . L 6 HOH 235 2762 2762 HOH HOH A . L 6 HOH 236 2763 2763 HOH HOH A . L 6 HOH 237 2764 2764 HOH HOH A . L 6 HOH 238 2765 2765 HOH HOH A . L 6 HOH 239 2766 2766 HOH HOH A . L 6 HOH 240 2767 2767 HOH HOH A . L 6 HOH 241 2768 2768 HOH HOH A . L 6 HOH 242 2769 2769 HOH HOH A . L 6 HOH 243 2770 2770 HOH HOH A . L 6 HOH 244 2771 2771 HOH HOH A . L 6 HOH 245 2772 2772 HOH HOH A . L 6 HOH 246 2773 2773 HOH HOH A . L 6 HOH 247 2774 2774 HOH HOH A . L 6 HOH 248 2775 2775 HOH HOH A . L 6 HOH 249 2776 2776 HOH HOH A . L 6 HOH 250 2777 2777 HOH HOH A . L 6 HOH 251 2778 2778 HOH HOH A . L 6 HOH 252 2779 2779 HOH HOH A . L 6 HOH 253 2780 2780 HOH HOH A . L 6 HOH 254 2781 2781 HOH HOH A . L 6 HOH 255 2782 2782 HOH HOH A . L 6 HOH 256 2783 2783 HOH HOH A . L 6 HOH 257 2784 2784 HOH HOH A . L 6 HOH 258 2786 2786 HOH HOH A . L 6 HOH 259 2787 2787 HOH HOH A . L 6 HOH 260 2788 2788 HOH HOH A . L 6 HOH 261 2790 2790 HOH HOH A . L 6 HOH 262 2791 2791 HOH HOH A . L 6 HOH 263 2792 2792 HOH HOH A . L 6 HOH 264 2793 2793 HOH HOH A . L 6 HOH 265 2794 2794 HOH HOH A . L 6 HOH 266 2795 2795 HOH HOH A . L 6 HOH 267 2796 2796 HOH HOH A . L 6 HOH 268 2797 2797 HOH HOH A . L 6 HOH 269 2798 2798 HOH HOH A . L 6 HOH 270 2799 2799 HOH HOH A . L 6 HOH 271 2800 2800 HOH HOH A . L 6 HOH 272 2801 2801 HOH HOH A . L 6 HOH 273 2802 2802 HOH HOH A . L 6 HOH 274 2803 2803 HOH HOH A . L 6 HOH 275 2804 2804 HOH HOH A . L 6 HOH 276 2805 2805 HOH HOH A . L 6 HOH 277 2806 2806 HOH HOH A . L 6 HOH 278 2807 2807 HOH HOH A . L 6 HOH 279 2808 2808 HOH HOH A . L 6 HOH 280 2809 2809 HOH HOH A . L 6 HOH 281 2810 2810 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,K,L # 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)' 6730 ? 1 MORE 39.1 ? 1 'SSA (A^2)' 28680 ? # 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 44.6200000000 -0.8660254038 -0.5000000000 0.0000000000 77.2841070337 0.0000000000 0.0000000000 -1.0000000000 46.7300000000 # 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 ? J K . ? A K 2 ? 1_555 O ? A SER 203 ? A SER 221 ? 1_555 86.1 ? 2 OD1 ? A ASP 202 ? A ASP 220 ? 1_555 K ? J K . ? A K 2 ? 1_555 OE1 ? A GLN 204 ? A GLN 222 ? 1_555 139.9 ? 3 O ? A SER 203 ? A SER 221 ? 1_555 K ? J K . ? A K 2 ? 1_555 OE1 ? A GLN 204 ? A GLN 222 ? 1_555 84.5 ? 4 OD1 ? A ASP 202 ? A ASP 220 ? 1_555 K ? J K . ? A K 2 ? 1_555 OG ? A SER 245 ? A SER 263 ? 1_555 138.5 ? 5 O ? A SER 203 ? A SER 221 ? 1_555 K ? J K . ? A K 2 ? 1_555 OG ? A SER 245 ? A SER 263 ? 1_555 83.7 ? 6 OE1 ? A GLN 204 ? A GLN 222 ? 1_555 K ? J K . ? A K 2 ? 1_555 OG ? A SER 245 ? A SER 263 ? 1_555 78.7 ? 7 OD1 ? A ASP 202 ? A ASP 220 ? 1_555 K ? J K . ? A K 2 ? 1_555 O ? A GLU 247 ? A GLU 265 ? 1_555 67.1 ? 8 O ? A SER 203 ? A SER 221 ? 1_555 K ? J K . ? A K 2 ? 1_555 O ? A GLU 247 ? A GLU 265 ? 1_555 77.6 ? 9 OE1 ? A GLN 204 ? A GLN 222 ? 1_555 K ? J K . ? A K 2 ? 1_555 O ? A GLU 247 ? A GLU 265 ? 1_555 146.6 ? 10 OG ? A SER 245 ? A SER 263 ? 1_555 K ? J K . ? A K 2 ? 1_555 O ? A GLU 247 ? A GLU 265 ? 1_555 71.5 ? 11 OD1 ? A ASP 202 ? A ASP 220 ? 1_555 K ? J K . ? A K 2 ? 1_555 O ? A LEU 249 ? A LEU 267 ? 1_555 104.4 ? 12 O ? A SER 203 ? A SER 221 ? 1_555 K ? J K . ? A K 2 ? 1_555 O ? A LEU 249 ? A LEU 267 ? 1_555 166.6 ? 13 OE1 ? A GLN 204 ? A GLN 222 ? 1_555 K ? J K . ? A K 2 ? 1_555 O ? A LEU 249 ? A LEU 267 ? 1_555 92.4 ? 14 OG ? A SER 245 ? A SER 263 ? 1_555 K ? J K . ? A K 2 ? 1_555 O ? A LEU 249 ? A LEU 267 ? 1_555 82.9 ? 15 O ? A GLU 247 ? A GLU 265 ? 1_555 K ? J K . ? A K 2 ? 1_555 O ? A LEU 249 ? A LEU 267 ? 1_555 98.5 ? 16 OD1 ? A ASP 202 ? A ASP 220 ? 1_555 K ? J K . ? A K 2 ? 1_555 O ? L HOH . ? A HOH 2549 ? 1_555 69.1 ? 17 O ? A SER 203 ? A SER 221 ? 1_555 K ? J K . ? A K 2 ? 1_555 O ? L HOH . ? A HOH 2549 ? 1_555 107.8 ? 18 OE1 ? A GLN 204 ? A GLN 222 ? 1_555 K ? J K . ? A K 2 ? 1_555 O ? L HOH . ? A HOH 2549 ? 1_555 77.0 ? 19 OG ? A SER 245 ? A SER 263 ? 1_555 K ? J K . ? A K 2 ? 1_555 O ? L HOH . ? A HOH 2549 ? 1_555 151.9 ? 20 O ? A GLU 247 ? A GLU 265 ? 1_555 K ? J K . ? A K 2 ? 1_555 O ? L HOH . ? A HOH 2549 ? 1_555 135.3 ? 21 O ? A LEU 249 ? A LEU 267 ? 1_555 K ? J K . ? A K 2 ? 1_555 O ? L HOH . ? A HOH 2549 ? 1_555 84.1 ? # 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' Advisory 2 2 'Structure model' 'Version format compliance' # _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 5.4113 _pdbx_refine_tls.origin_y 33.4158 _pdbx_refine_tls.origin_z 12.5268 _pdbx_refine_tls.T[1][1] -0.0348 _pdbx_refine_tls.T[2][2] -0.0220 _pdbx_refine_tls.T[3][3] -0.0455 _pdbx_refine_tls.T[1][2] -0.0087 _pdbx_refine_tls.T[1][3] -0.0106 _pdbx_refine_tls.T[2][3] -0.0268 _pdbx_refine_tls.L[1][1] 0.7643 _pdbx_refine_tls.L[2][2] 0.3569 _pdbx_refine_tls.L[3][3] 0.5919 _pdbx_refine_tls.L[1][2] -0.1215 _pdbx_refine_tls.L[1][3] 0.1801 _pdbx_refine_tls.L[2][3] 0.0688 _pdbx_refine_tls.S[1][1] 0.0000 _pdbx_refine_tls.S[1][2] 0.0312 _pdbx_refine_tls.S[1][3] -0.0714 _pdbx_refine_tls.S[2][1] -0.0298 _pdbx_refine_tls.S[2][2] 0.0127 _pdbx_refine_tls.S[2][3] 0.0263 _pdbx_refine_tls.S[3][1] 0.1292 _pdbx_refine_tls.S[3][2] -0.0626 _pdbx_refine_tls.S[3][3] -0.0127 _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' # _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_auth_asym_id A _pdbx_refine_tls_group.beg_auth_seq_id 19 _pdbx_refine_tls_group.beg_label_asym_id A _pdbx_refine_tls_group.beg_label_seq_id 1 _pdbx_refine_tls_group.end_auth_asym_id A _pdbx_refine_tls_group.end_auth_seq_id 376 _pdbx_refine_tls_group.end_label_asym_id A _pdbx_refine_tls_group.end_label_seq_id 358 _pdbx_refine_tls_group.selection ? _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.selection_details ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.4.0067 ? 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 ? ? -147.13 -159.64 2 1 ASP A 39 ? ? -129.95 -152.55 3 1 SER A 42 ? ? -141.44 23.90 4 1 ASN A 214 ? ? 39.11 59.90 5 1 THR A 215 ? ? 79.23 -6.86 6 1 LEU A 266 ? ? 63.17 -148.46 7 1 LYS A 279 ? ? 69.09 83.69 8 1 SER A 299 ? ? -108.23 -169.57 9 1 ASN A 358 ? ? -96.86 -72.64 # 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 'methyl 4,9-di-O-acetyl-5-(acetylamino)-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosidonic acid' SIO 4 'POTASSIUM ION' K 5 'ACETIC ACID' ACY 6 water HOH #