data_4C2L # _entry.id 4C2L # _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 4C2L PDBE EBI-58038 WWPDB D_1290058038 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4C2L _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2013-08-19 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Rozeboom, H.J.' 1 'Beldman, G.' 2 'Schols, H.A.' 3 'Dijkstra, B.W.' 4 # _citation.id primary _citation.title 'Crystal Structure of Endo-Xylogalacturonan Hydrolase from Aspergillus Tubingensis.' _citation.journal_abbrev 'FEBS J.' _citation.journal_volume 280 _citation.page_first 6061 _citation.page_last ? _citation.year 2013 _citation.journal_id_ASTM ? _citation.country UK _citation.journal_id_ISSN 1742-464X _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 24034788 _citation.pdbx_database_id_DOI 10.1111/FEBS.12524 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Rozeboom, H.J.' 1 primary 'Beldman, G.' 2 primary 'Schols, H.A.' 3 primary 'Dijkstra, B.W.' 4 # _cell.entry_id 4C2L _cell.length_a 76.440 _cell.length_b 121.180 _cell.length_c 129.670 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4C2L _symmetry.space_group_name_H-M 'I 2 2 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 23 # 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 'ENDO-XYLOGALACTURONAN HYDROLASE A' 40158.527 1 3.2.1.- ? 'RESIDUES 19-406' ? 2 non-polymer man ALPHA-D-MANNOSE 180.156 1 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 3 ? ? ? ? 4 non-polymer syn 'SULFATE ION' 96.063 7 ? ? ? ? 5 non-polymer syn GLYCEROL 92.094 1 ? ? ? ? 6 water nat water 18.015 458 ? ? ? ? # _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 ;APSKVQRAPDSSIHARAVCTPTAGGDSSTDDVPAITEALSSCGNGGTIVFPEGSTYYLNSVLDLGSCSDCDIQVEGLLKF ASDTDYWSGRTAMISVSNVDGLKLRSLTGSGVIDGNGQDAWDLFASDSSYSRPTLLYITGGSNLEISGLRQKNPPNVFNS VKGGATNVVFSNLKMDANSKSDNPPKNTDGFDIGESTYVTITEVTVVNDDDCVAFKPSSNYVTVDTISCTGSHGISVGSL GKSSDDSVKNIYVTGATMINSTKAAGIKTYPSGGDHGTSTVSNVTFNDFTVDNSDYAFQIQSCYGEDDDYCEENPGNAKL TDIVVSSFSGTTSDKYDPVVANLDCGADGTCGISISGFDVKAPSGKSEVLCANTPSDLGVTCTSGASG ; _entity_poly.pdbx_seq_one_letter_code_can ;APSKVQRAPDSSIHARAVCTPTAGGDSSTDDVPAITEALSSCGNGGTIVFPEGSTYYLNSVLDLGSCSDCDIQVEGLLKF ASDTDYWSGRTAMISVSNVDGLKLRSLTGSGVIDGNGQDAWDLFASDSSYSRPTLLYITGGSNLEISGLRQKNPPNVFNS VKGGATNVVFSNLKMDANSKSDNPPKNTDGFDIGESTYVTITEVTVVNDDDCVAFKPSSNYVTVDTISCTGSHGISVGSL GKSSDDSVKNIYVTGATMINSTKAAGIKTYPSGGDHGTSTVSNVTFNDFTVDNSDYAFQIQSCYGEDDDYCEENPGNAKL TDIVVSSFSGTTSDKYDPVVANLDCGADGTCGISISGFDVKAPSGKSEVLCANTPSDLGVTCTSGASG ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ALA n 1 2 PRO n 1 3 SER n 1 4 LYS n 1 5 VAL n 1 6 GLN n 1 7 ARG n 1 8 ALA n 1 9 PRO n 1 10 ASP n 1 11 SER n 1 12 SER n 1 13 ILE n 1 14 HIS n 1 15 ALA n 1 16 ARG n 1 17 ALA n 1 18 VAL n 1 19 CYS n 1 20 THR n 1 21 PRO n 1 22 THR n 1 23 ALA n 1 24 GLY n 1 25 GLY n 1 26 ASP n 1 27 SER n 1 28 SER n 1 29 THR n 1 30 ASP n 1 31 ASP n 1 32 VAL n 1 33 PRO n 1 34 ALA n 1 35 ILE n 1 36 THR n 1 37 GLU n 1 38 ALA n 1 39 LEU n 1 40 SER n 1 41 SER n 1 42 CYS n 1 43 GLY n 1 44 ASN n 1 45 GLY n 1 46 GLY n 1 47 THR n 1 48 ILE n 1 49 VAL n 1 50 PHE n 1 51 PRO n 1 52 GLU n 1 53 GLY n 1 54 SER n 1 55 THR n 1 56 TYR n 1 57 TYR n 1 58 LEU n 1 59 ASN n 1 60 SER n 1 61 VAL n 1 62 LEU n 1 63 ASP n 1 64 LEU n 1 65 GLY n 1 66 SER n 1 67 CYS n 1 68 SER n 1 69 ASP n 1 70 CYS n 1 71 ASP n 1 72 ILE n 1 73 GLN n 1 74 VAL n 1 75 GLU n 1 76 GLY n 1 77 LEU n 1 78 LEU n 1 79 LYS n 1 80 PHE n 1 81 ALA n 1 82 SER n 1 83 ASP n 1 84 THR n 1 85 ASP n 1 86 TYR n 1 87 TRP n 1 88 SER n 1 89 GLY n 1 90 ARG n 1 91 THR n 1 92 ALA n 1 93 MET n 1 94 ILE n 1 95 SER n 1 96 VAL n 1 97 SER n 1 98 ASN n 1 99 VAL n 1 100 ASP n 1 101 GLY n 1 102 LEU n 1 103 LYS n 1 104 LEU n 1 105 ARG n 1 106 SER n 1 107 LEU n 1 108 THR n 1 109 GLY n 1 110 SER n 1 111 GLY n 1 112 VAL n 1 113 ILE n 1 114 ASP n 1 115 GLY n 1 116 ASN n 1 117 GLY n 1 118 GLN n 1 119 ASP n 1 120 ALA n 1 121 TRP n 1 122 ASP n 1 123 LEU n 1 124 PHE n 1 125 ALA n 1 126 SER n 1 127 ASP n 1 128 SER n 1 129 SER n 1 130 TYR n 1 131 SER n 1 132 ARG n 1 133 PRO n 1 134 THR n 1 135 LEU n 1 136 LEU n 1 137 TYR n 1 138 ILE n 1 139 THR n 1 140 GLY n 1 141 GLY n 1 142 SER n 1 143 ASN n 1 144 LEU n 1 145 GLU n 1 146 ILE n 1 147 SER n 1 148 GLY n 1 149 LEU n 1 150 ARG n 1 151 GLN n 1 152 LYS n 1 153 ASN n 1 154 PRO n 1 155 PRO n 1 156 ASN n 1 157 VAL n 1 158 PHE n 1 159 ASN n 1 160 SER n 1 161 VAL n 1 162 LYS n 1 163 GLY n 1 164 GLY n 1 165 ALA n 1 166 THR n 1 167 ASN n 1 168 VAL n 1 169 VAL n 1 170 PHE n 1 171 SER n 1 172 ASN n 1 173 LEU n 1 174 LYS n 1 175 MET n 1 176 ASP n 1 177 ALA n 1 178 ASN n 1 179 SER n 1 180 LYS n 1 181 SER n 1 182 ASP n 1 183 ASN n 1 184 PRO n 1 185 PRO n 1 186 LYS n 1 187 ASN n 1 188 THR n 1 189 ASP n 1 190 GLY n 1 191 PHE n 1 192 ASP n 1 193 ILE n 1 194 GLY n 1 195 GLU n 1 196 SER n 1 197 THR n 1 198 TYR n 1 199 VAL n 1 200 THR n 1 201 ILE n 1 202 THR n 1 203 GLU n 1 204 VAL n 1 205 THR n 1 206 VAL n 1 207 VAL n 1 208 ASN n 1 209 ASP n 1 210 ASP n 1 211 ASP n 1 212 CYS n 1 213 VAL n 1 214 ALA n 1 215 PHE n 1 216 LYS n 1 217 PRO n 1 218 SER n 1 219 SER n 1 220 ASN n 1 221 TYR n 1 222 VAL n 1 223 THR n 1 224 VAL n 1 225 ASP n 1 226 THR n 1 227 ILE n 1 228 SER n 1 229 CYS n 1 230 THR n 1 231 GLY n 1 232 SER n 1 233 HIS n 1 234 GLY n 1 235 ILE n 1 236 SER n 1 237 VAL n 1 238 GLY n 1 239 SER n 1 240 LEU n 1 241 GLY n 1 242 LYS n 1 243 SER n 1 244 SER n 1 245 ASP n 1 246 ASP n 1 247 SER n 1 248 VAL n 1 249 LYS n 1 250 ASN n 1 251 ILE n 1 252 TYR n 1 253 VAL n 1 254 THR n 1 255 GLY n 1 256 ALA n 1 257 THR n 1 258 MET n 1 259 ILE n 1 260 ASN n 1 261 SER n 1 262 THR n 1 263 LYS n 1 264 ALA n 1 265 ALA n 1 266 GLY n 1 267 ILE n 1 268 LYS n 1 269 THR n 1 270 TYR n 1 271 PRO n 1 272 SER n 1 273 GLY n 1 274 GLY n 1 275 ASP n 1 276 HIS n 1 277 GLY n 1 278 THR n 1 279 SER n 1 280 THR n 1 281 VAL n 1 282 SER n 1 283 ASN n 1 284 VAL n 1 285 THR n 1 286 PHE n 1 287 ASN n 1 288 ASP n 1 289 PHE n 1 290 THR n 1 291 VAL n 1 292 ASP n 1 293 ASN n 1 294 SER n 1 295 ASP n 1 296 TYR n 1 297 ALA n 1 298 PHE n 1 299 GLN n 1 300 ILE n 1 301 GLN n 1 302 SER n 1 303 CYS n 1 304 TYR n 1 305 GLY n 1 306 GLU n 1 307 ASP n 1 308 ASP n 1 309 ASP n 1 310 TYR n 1 311 CYS n 1 312 GLU n 1 313 GLU n 1 314 ASN n 1 315 PRO n 1 316 GLY n 1 317 ASN n 1 318 ALA n 1 319 LYS n 1 320 LEU n 1 321 THR n 1 322 ASP n 1 323 ILE n 1 324 VAL n 1 325 VAL n 1 326 SER n 1 327 SER n 1 328 PHE n 1 329 SER n 1 330 GLY n 1 331 THR n 1 332 THR n 1 333 SER n 1 334 ASP n 1 335 LYS n 1 336 TYR n 1 337 ASP n 1 338 PRO n 1 339 VAL n 1 340 VAL n 1 341 ALA n 1 342 ASN n 1 343 LEU n 1 344 ASP n 1 345 CYS n 1 346 GLY n 1 347 ALA n 1 348 ASP n 1 349 GLY n 1 350 THR n 1 351 CYS n 1 352 GLY n 1 353 ILE n 1 354 SER n 1 355 ILE n 1 356 SER n 1 357 GLY n 1 358 PHE n 1 359 ASP n 1 360 VAL n 1 361 LYS n 1 362 ALA n 1 363 PRO n 1 364 SER n 1 365 GLY n 1 366 LYS n 1 367 SER n 1 368 GLU n 1 369 VAL n 1 370 LEU n 1 371 CYS n 1 372 ALA n 1 373 ASN n 1 374 THR n 1 375 PRO n 1 376 SER n 1 377 ASP n 1 378 LEU n 1 379 GLY n 1 380 VAL n 1 381 THR n 1 382 CYS n 1 383 THR n 1 384 SER n 1 385 GLY n 1 386 ALA n 1 387 SER n 1 388 GLY 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 ? _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'ASPERGILLUS TUBINGENSIS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 5068 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'ASPERGILLUS NIGER' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 5061 _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 ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code XGHA_ASPTU _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession Q9UUZ2 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4C2L _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 388 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q9UUZ2 _struct_ref_seq.db_align_beg 19 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 406 _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 406 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 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 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 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 4C2L _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.8 _exptl_crystal.density_percent_sol 67 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 4.4 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '2.9 M AMMONIUM SULFATE, 0.1 M NA-ACETATE BUFFER PH 4.4, VAPOR DIFFUSION, HANGING DROP, 298 K' # _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 315r' _diffrn_detector.pdbx_collection_date 2010-02-27 _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 0.9724 _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 0.9724 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4C2L _reflns.observed_criterion_sigma_I -3.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 40.70 _reflns.d_resolution_high 1.75 _reflns.number_obs 60896 _reflns.number_all ? _reflns.percent_possible_obs 99.8 _reflns.pdbx_Rmerge_I_obs 0.10 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 11.60 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 7.1 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.75 _reflns_shell.d_res_low 1.84 _reflns_shell.percent_possible_all 100.0 _reflns_shell.Rmerge_I_obs 0.58 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 3.70 _reflns_shell.pdbx_redundancy 7.2 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4C2L _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 57809 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F . _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 88.54 _refine.ls_d_res_high 1.75 _refine.ls_percent_reflns_obs 99.90 _refine.ls_R_factor_obs 0.16846 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.16734 _refine.ls_R_factor_R_free 0.18927 _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 3084 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.963 _refine.correlation_coeff_Fo_to_Fc_free 0.954 _refine.B_iso_mean 20.587 _refine.aniso_B[1][1] 0.41 _refine.aniso_B[2][2] -0.47 _refine.aniso_B[3][3] 0.06 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.' _refine.pdbx_starting_model 'PDB ENTRIES 1NHC, 1RMG, 1CZF AND 2IQ7' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.081 _refine.pdbx_overall_ESU_R_Free 0.080 _refine.overall_SU_ML 0.049 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 1.522 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2690 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 94 _refine_hist.number_atoms_solvent 458 _refine_hist.number_atoms_total 3242 _refine_hist.d_res_high 1.75 _refine_hist.d_res_low 88.54 # 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 0.008 0.020 ? 2869 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.327 1.989 ? 3934 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.734 5.000 ? 389 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 34.957 26.636 ? 110 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 10.835 15.000 ? 420 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 19.223 15.000 ? 4 'X-RAY DIFFRACTION' ? r_chiral_restr 0.087 0.200 ? 471 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.005 0.021 ? 2153 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.750 _refine_ls_shell.d_res_low 1.795 _refine_ls_shell.number_reflns_R_work 4044 _refine_ls_shell.R_factor_R_work 0.246 _refine_ls_shell.percent_reflns_obs 99.95 _refine_ls_shell.R_factor_R_free 0.248 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 202 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4C2L _struct.title 'Crystal structure of endo-xylogalacturonan hydrolase from Aspergillus tubingensis' _struct.pdbx_descriptor 'ENDO-XYLOGALACTURONAN HYDROLASE A (E.C.3.2.1.-)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4C2L _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, POLYGALACTURONAN, GH28' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 3 ? F N N 4 ? G N N 4 ? H N N 4 ? I N N 4 ? J N N 4 ? K N N 4 ? L N N 4 ? M N N 5 ? N N N 6 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASP A 31 ? GLY A 43 ? ASP A 49 GLY A 61 1 ? 13 HELX_P HELX_P2 2 ASP A 83 ? SER A 88 ? ASP A 101 SER A 106 1 ? 6 HELX_P HELX_P3 3 GLY A 117 ? ASP A 127 ? GLY A 135 ASP A 145 1 ? 11 HELX_P HELX_P4 4 ASP A 307 ? ASN A 314 ? ASP A 325 ASN A 332 1 ? 8 # _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 19 SG ? ? ? 1_555 A CYS 42 SG ? ? A CYS 37 A CYS 60 1_555 ? ? ? ? ? ? ? 2.048 ? disulf2 disulf ? ? A CYS 67 SG ? ? ? 1_555 A CYS 70 SG ? ? A CYS 85 A CYS 88 1_555 ? ? ? ? ? ? ? 2.018 ? disulf3 disulf ? ? A CYS 212 SG ? ? ? 1_555 A CYS 229 SG ? ? A CYS 230 A CYS 247 1_555 ? ? ? ? ? ? ? 2.033 ? disulf4 disulf ? ? A CYS 303 SG ? ? ? 1_555 A CYS 311 SG ? ? A CYS 321 A CYS 329 1_555 ? ? ? ? ? ? ? 2.036 ? disulf5 disulf ? ? A CYS 345 SG ? ? ? 1_555 A CYS 351 SG ? ? A CYS 363 A CYS 369 1_555 ? ? ? ? ? ? ? 2.030 ? disulf6 disulf ? ? A CYS 371 SG ? ? ? 1_555 A CYS 382 SG ? ? A CYS 389 A CYS 400 1_555 ? ? ? ? ? ? ? 2.076 ? covale1 covale ? ? A THR 20 OG1 ? ? ? 1_555 B MAN . C1 ? ? A THR 38 A MAN 410 1_555 ? ? ? ? ? ? ? 1.449 ? covale2 covale ? ? A ASN 260 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 278 A NAG 411 1_555 ? ? ? ? ? ? ? 1.438 ? covale3 covale ? ? A ASN 283 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 301 A NAG 412 1_555 ? ? ? ? ? ? ? 1.434 ? covale4 covale ? ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 412 A NAG 413 1_555 ? ? ? ? ? ? ? 1.444 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # 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 GLY 238 A . ? GLY 256 A SER 239 A ? SER 257 A 1 0.59 2 ASP 337 A . ? ASP 355 A PRO 338 A ? PRO 356 A 1 11.54 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 12 ? AB ? 10 ? AC ? 12 ? # 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 AA 1 2 ? parallel AA 2 3 ? parallel AA 3 4 ? parallel AA 4 5 ? parallel AA 5 6 ? parallel AA 6 7 ? parallel AA 7 8 ? parallel AA 8 9 ? parallel AA 9 10 ? parallel AA 10 11 ? parallel AA 11 12 ? parallel AB 1 2 ? parallel AB 2 3 ? parallel AB 3 4 ? parallel AB 4 5 ? parallel AB 5 6 ? parallel AB 6 7 ? anti-parallel AB 7 8 ? parallel AB 8 9 ? anti-parallel AB 9 10 ? anti-parallel AC 1 2 ? parallel AC 2 3 ? parallel AC 3 4 ? parallel AC 4 5 ? parallel AC 5 6 ? parallel AC 6 7 ? parallel AC 7 8 ? parallel AC 8 9 ? parallel AC 9 10 ? parallel AC 10 11 ? parallel AC 11 12 ? 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 AA 1 VAL A 18 ? CYS A 19 ? VAL A 36 CYS A 37 AA 2 THR A 47 ? PHE A 50 ? THR A 65 PHE A 68 AA 3 CYS A 70 ? VAL A 74 ? CYS A 88 VAL A 92 AA 4 ASP A 100 ? ARG A 105 ? ASP A 118 ARG A 123 AA 5 SER A 142 ? SER A 147 ? SER A 160 SER A 165 AA 6 ALA A 165 ? ASP A 176 ? ALA A 183 ASP A 194 AA 7 SER A 196 ? VAL A 207 ? SER A 214 VAL A 225 AA 8 SER A 219 ? THR A 230 ? SER A 237 THR A 248 AA 9 ASP A 246 ? ILE A 259 ? ASP A 264 ILE A 277 AA 10 SER A 279 ? SER A 294 ? SER A 297 SER A 312 AA 11 LYS A 319 ? THR A 332 ? LYS A 337 THR A 350 AA 12 THR A 350 ? PHE A 358 ? THR A 368 PHE A 376 AB 1 VAL A 18 ? CYS A 19 ? VAL A 36 CYS A 37 AB 2 THR A 47 ? PHE A 50 ? THR A 65 PHE A 68 AB 3 CYS A 70 ? VAL A 74 ? CYS A 88 VAL A 92 AB 4 ASP A 100 ? ARG A 105 ? ASP A 118 ARG A 123 AB 5 SER A 142 ? SER A 147 ? SER A 160 SER A 165 AB 6 ALA A 165 ? ASP A 176 ? ALA A 183 ASP A 194 AB 7 ARG A 150 ? LYS A 152 ? ARG A 168 LYS A 170 AB 8 VAL A 112 ? ASP A 114 ? VAL A 130 ASP A 132 AB 9 LEU A 77 ? PHE A 80 ? LEU A 95 PHE A 98 AB 10 THR A 55 ? LEU A 58 ? THR A 73 LEU A 76 AC 1 LEU A 62 ? ASP A 63 ? LEU A 80 ASP A 81 AC 2 ALA A 92 ? SER A 97 ? ALA A 110 SER A 115 AC 3 THR A 134 ? THR A 139 ? THR A 152 THR A 157 AC 4 ASN A 159 ? LYS A 162 ? ASN A 177 LYS A 180 AC 5 PHE A 191 ? ILE A 193 ? PHE A 209 ILE A 211 AC 6 VAL A 213 ? PHE A 215 ? VAL A 231 PHE A 233 AC 7 ILE A 235 ? LEU A 240 ? ILE A 253 LEU A 258 AC 8 LYS A 263 ? THR A 269 ? LYS A 281 THR A 287 AC 9 TYR A 296 ? GLN A 301 ? TYR A 314 GLN A 319 AC 10 VAL A 339 ? ASP A 344 ? VAL A 357 ASP A 362 AC 11 GLU A 368 ? ALA A 372 ? GLU A 386 ALA A 390 AC 12 THR A 383 ? SER A 384 ? THR A 401 SER A 402 # 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 AA 1 2 N CYS A 19 ? N CYS A 37 O THR A 47 ? O THR A 65 AA 2 3 N ILE A 48 ? N ILE A 66 O ASP A 71 ? O ASP A 89 AA 3 4 N CYS A 70 ? N CYS A 88 O GLY A 101 ? O GLY A 119 AA 4 5 N GLY A 101 ? N GLY A 119 O SER A 142 ? O SER A 160 AA 5 6 N ASN A 143 ? N ASN A 161 O THR A 166 ? O THR A 184 AA 6 7 N ASN A 167 ? N ASN A 185 O THR A 197 ? O THR A 215 AA 7 8 N TYR A 198 ? N TYR A 216 O ASN A 220 ? O ASN A 238 AA 8 9 N TYR A 221 ? N TYR A 239 O LYS A 249 ? O LYS A 267 AA 9 10 N VAL A 248 ? N VAL A 266 O THR A 280 ? O THR A 298 AA 10 11 N VAL A 281 ? N VAL A 299 O LYS A 319 ? O LYS A 337 AA 11 12 N LEU A 320 ? N LEU A 338 O THR A 350 ? O THR A 368 AB 1 2 N CYS A 19 ? N CYS A 37 O THR A 47 ? O THR A 65 AB 2 3 N ILE A 48 ? N ILE A 66 O ASP A 71 ? O ASP A 89 AB 3 4 N CYS A 70 ? N CYS A 88 O GLY A 101 ? O GLY A 119 AB 4 5 N GLY A 101 ? N GLY A 119 O SER A 142 ? O SER A 160 AB 5 6 N ASN A 143 ? N ASN A 161 O THR A 166 ? O THR A 184 AB 6 7 N ASP A 176 ? N ASP A 194 O GLN A 151 ? O GLN A 169 AB 7 8 N LYS A 152 ? N LYS A 170 O ILE A 113 ? O ILE A 131 AB 8 9 N ASP A 114 ? N ASP A 132 O LEU A 78 ? O LEU A 96 AB 9 10 N LYS A 79 ? N LYS A 97 O TYR A 56 ? O TYR A 74 AC 1 2 N LEU A 62 ? N LEU A 80 O MET A 93 ? O MET A 111 AC 2 3 N MET A 93 ? N MET A 111 O THR A 134 ? O THR A 152 AC 3 4 N ILE A 138 ? N ILE A 156 O SER A 160 ? O SER A 178 AC 4 5 N VAL A 161 ? N VAL A 179 O ASP A 192 ? O ASP A 210 AC 5 6 N ILE A 193 ? N ILE A 211 O ALA A 214 ? O ALA A 232 AC 6 7 N PHE A 215 ? N PHE A 233 O SER A 236 ? O SER A 254 AC 7 8 N ILE A 235 ? N ILE A 253 O ALA A 264 ? O ALA A 282 AC 8 9 N ALA A 264 ? N ALA A 282 O TYR A 296 ? O TYR A 314 AC 9 10 N ALA A 297 ? N ALA A 315 O VAL A 340 ? O VAL A 358 AC 10 11 N VAL A 340 ? N VAL A 358 O GLU A 368 ? O GLU A 386 AC 11 12 N CYS A 371 ? N CYS A 389 O THR A 383 ? O THR A 401 # 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 SO4 A 1407' AC2 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE SO4 A 1408' AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 1409' AC4 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE SO4 A 1410' AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE SO4 A 1411' AC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 1412' AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 A 1413' AC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 1414' AC9 Software ? ? ? ? 5 'Binding site for Mono-Saccharide MAN A 410 bound to THR A 38' BC1 Software ? ? ? ? 3 'Binding site for Mono-Saccharide NAG A 411 bound to ASN A 278' BC2 Software ? ? ? ? 9 'Binding site for Poly-Saccharide residues NAG A 412 through NAG A 413 bound to ASN A 301' # 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 LYS A 216 ? LYS A 234 . ? 1_555 ? 2 AC1 7 GLY A 238 ? GLY A 256 . ? 1_555 ? 3 AC1 7 SER A 239 ? SER A 257 . ? 1_555 ? 4 AC1 7 LYS A 268 ? LYS A 286 . ? 1_555 ? 5 AC1 7 TYR A 304 ? TYR A 322 . ? 1_555 ? 6 AC1 7 HOH N . ? HOH A 2270 . ? 1_555 ? 7 AC1 7 HOH N . ? HOH A 2292 . ? 1_555 ? 8 AC2 9 PRO A 33 ? PRO A 51 . ? 2_555 ? 9 AC2 9 ARG A 90 ? ARG A 108 . ? 1_555 ? 10 AC2 9 THR A 91 ? THR A 109 . ? 1_555 ? 11 AC2 9 HOH N . ? HOH A 2120 . ? 1_555 ? 12 AC2 9 HOH N . ? HOH A 2123 . ? 1_555 ? 13 AC2 9 HOH N . ? HOH A 2124 . ? 1_555 ? 14 AC2 9 HOH N . ? HOH A 2128 . ? 1_555 ? 15 AC2 9 HOH N . ? HOH A 2451 . ? 1_555 ? 16 AC2 9 HOH N . ? HOH A 2452 . ? 1_555 ? 17 AC3 5 ARG A 150 ? ARG A 168 . ? 1_555 ? 18 AC3 5 LYS A 152 ? LYS A 170 . ? 1_555 ? 19 AC3 5 GOL M . ? GOL A 1414 . ? 1_555 ? 20 AC3 5 HOH N . ? HOH A 2453 . ? 1_555 ? 21 AC3 5 HOH N . ? HOH A 2454 . ? 1_555 ? 22 AC4 9 HIS A 233 ? HIS A 251 . ? 1_555 ? 23 AC4 9 LYS A 268 ? LYS A 286 . ? 1_555 ? 24 AC4 9 TYR A 304 ? TYR A 322 . ? 1_555 ? 25 AC4 9 HOH N . ? HOH A 2247 . ? 1_555 ? 26 AC4 9 HOH N . ? HOH A 2270 . ? 1_555 ? 27 AC4 9 HOH N . ? HOH A 2271 . ? 1_555 ? 28 AC4 9 HOH N . ? HOH A 2320 . ? 1_555 ? 29 AC4 9 HOH N . ? HOH A 2321 . ? 1_555 ? 30 AC4 9 HOH N . ? HOH A 2363 . ? 1_555 ? 31 AC5 6 ASN A 287 ? ASN A 305 . ? 1_555 ? 32 AC5 6 ASP A 288 ? ASP A 306 . ? 1_555 ? 33 AC5 6 HOH N . ? HOH A 2342 . ? 1_555 ? 34 AC5 6 HOH N . ? HOH A 2343 . ? 1_555 ? 35 AC5 6 HOH N . ? HOH A 2344 . ? 1_555 ? 36 AC5 6 HOH N . ? HOH A 2455 . ? 1_555 ? 37 AC6 5 LYS A 249 ? LYS A 267 . ? 1_555 ? 38 AC6 5 ASN A 250 ? ASN A 268 . ? 1_555 ? 39 AC6 5 HOH N . ? HOH A 2278 . ? 1_555 ? 40 AC6 5 HOH N . ? HOH A 2308 . ? 1_555 ? 41 AC6 5 HOH N . ? HOH A 2456 . ? 1_555 ? 42 AC7 4 ASN A 44 ? ASN A 62 . ? 1_555 ? 43 AC7 4 ASN A 98 ? ASN A 116 . ? 2_555 ? 44 AC7 4 HOH N . ? HOH A 2032 . ? 1_555 ? 45 AC7 4 HOH N . ? HOH A 2457 . ? 1_555 ? 46 AC8 6 ASP A 114 ? ASP A 132 . ? 1_555 ? 47 AC8 6 LYS A 152 ? LYS A 170 . ? 1_555 ? 48 AC8 6 LYS A 180 ? LYS A 198 . ? 1_555 ? 49 AC8 6 SO4 H . ? SO4 A 1409 . ? 1_555 ? 50 AC8 6 HOH N . ? HOH A 2096 . ? 1_555 ? 51 AC8 6 HOH N . ? HOH A 2158 . ? 1_555 ? 52 AC9 5 VAL A 18 ? VAL A 36 . ? 1_555 ? 53 AC9 5 THR A 20 ? THR A 38 . ? 1_555 ? 54 AC9 5 HOH N . ? HOH A 2436 . ? 8_455 ? 55 AC9 5 HOH N . ? HOH A 2444 . ? 1_555 ? 56 AC9 5 HOH N . ? HOH A 2445 . ? 1_555 ? 57 BC1 3 ASN A 260 ? ASN A 278 . ? 1_555 ? 58 BC1 3 HOH N . ? HOH A 2446 . ? 1_555 ? 59 BC1 3 HOH N . ? HOH A 2447 . ? 1_555 ? 60 BC2 9 TYR A 221 ? TYR A 239 . ? 1_555 ? 61 BC2 9 THR A 223 ? THR A 241 . ? 1_555 ? 62 BC2 9 ASN A 250 ? ASN A 268 . ? 1_555 ? 63 BC2 9 TYR A 252 ? TYR A 270 . ? 1_555 ? 64 BC2 9 ASN A 283 ? ASN A 301 . ? 1_555 ? 65 BC2 9 HOH N . ? HOH A 2280 . ? 1_555 ? 66 BC2 9 HOH N . ? HOH A 2281 . ? 1_555 ? 67 BC2 9 HOH N . ? HOH A 2449 . ? 1_555 ? 68 BC2 9 HOH N . ? HOH A 2450 . ? 1_555 ? # _database_PDB_matrix.entry_id 4C2L _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 4C2L _atom_sites.fract_transf_matrix[1][1] 0.013082 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.008252 _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] 0.007712 _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 N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ALA A 1 17 ? -14.075 -0.816 27.604 1.00 23.90 ? 35 ALA A N 1 ATOM 2 C CA . ALA A 1 17 ? -14.928 -1.303 28.724 1.00 23.74 ? 35 ALA A CA 1 ATOM 3 C C . ALA A 1 17 ? -14.889 -0.332 29.907 1.00 23.74 ? 35 ALA A C 1 ATOM 4 O O . ALA A 1 17 ? -13.950 0.461 30.037 1.00 23.33 ? 35 ALA A O 1 ATOM 5 C CB . ALA A 1 17 ? -14.469 -2.688 29.159 1.00 25.46 ? 35 ALA A CB 1 ATOM 6 N N . VAL A 1 18 ? -15.911 -0.400 30.752 1.00 22.85 ? 36 VAL A N 1 ATOM 7 C CA . VAL A 1 18 ? -16.033 0.471 31.924 1.00 22.88 ? 36 VAL A CA 1 ATOM 8 C C . VAL A 1 18 ? -15.919 -0.353 33.212 1.00 22.91 ? 36 VAL A C 1 ATOM 9 O O . VAL A 1 18 ? -16.578 -1.376 33.359 1.00 23.04 ? 36 VAL A O 1 ATOM 10 C CB . VAL A 1 18 ? -17.364 1.255 31.918 1.00 23.70 ? 36 VAL A CB 1 ATOM 11 C CG1 . VAL A 1 18 ? -17.435 2.198 33.108 1.00 24.50 ? 36 VAL A CG1 1 ATOM 12 C CG2 . VAL A 1 18 ? -17.502 2.044 30.625 1.00 25.79 ? 36 VAL A CG2 1 ATOM 13 N N . CYS A 1 19 ? -15.077 0.092 34.138 1.00 21.56 ? 37 CYS A N 1 ATOM 14 C CA . CYS A 1 19 ? -14.836 -0.637 35.384 1.00 22.01 ? 37 CYS A CA 1 ATOM 15 C C . CYS A 1 19 ? -15.166 0.291 36.545 1.00 20.06 ? 37 CYS A C 1 ATOM 16 O O . CYS A 1 19 ? -14.773 1.462 36.529 1.00 20.06 ? 37 CYS A O 1 ATOM 17 C CB . CYS A 1 19 ? -13.349 -1.030 35.482 1.00 23.78 ? 37 CYS A CB 1 ATOM 18 S SG . CYS A 1 19 ? -12.813 -2.438 34.465 1.00 32.46 ? 37 CYS A SG 1 ATOM 19 N N . THR A 1 20 ? -15.866 -0.218 37.553 1.00 17.74 ? 38 THR A N 1 ATOM 20 C CA . THR A 1 20 ? -16.059 0.536 38.785 1.00 18.33 ? 38 THR A CA 1 ATOM 21 C C . THR A 1 20 ? -15.307 -0.148 39.915 1.00 17.56 ? 38 THR A C 1 ATOM 22 O O . THR A 1 20 ? -15.678 -1.252 40.304 1.00 17.57 ? 38 THR A O 1 ATOM 23 C CB . THR A 1 20 ? -17.548 0.647 39.152 1.00 18.96 ? 38 THR A CB 1 ATOM 24 O OG1 . THR A 1 20 ? -18.239 1.245 38.053 1.00 20.66 ? 38 THR A OG1 1 ATOM 25 C CG2 . THR A 1 20 ? -17.755 1.480 40.423 1.00 18.64 ? 38 THR A CG2 1 ATOM 26 N N . PRO A 1 21 ? -14.273 0.509 40.473 1.00 17.16 ? 39 PRO A N 1 ATOM 27 C CA . PRO A 1 21 ? -13.518 -0.159 41.546 1.00 16.99 ? 39 PRO A CA 1 ATOM 28 C C . PRO A 1 21 ? -14.387 -0.451 42.748 1.00 16.91 ? 39 PRO A C 1 ATOM 29 O O . PRO A 1 21 ? -15.233 0.365 43.124 1.00 15.70 ? 39 PRO A O 1 ATOM 30 C CB . PRO A 1 21 ? -12.450 0.865 41.951 1.00 16.63 ? 39 PRO A CB 1 ATOM 31 C CG . PRO A 1 21 ? -12.488 1.935 40.909 1.00 16.75 ? 39 PRO A CG 1 ATOM 32 C CD . PRO A 1 21 ? -13.810 1.887 40.219 1.00 16.44 ? 39 PRO A CD 1 ATOM 33 N N . THR A 1 22 ? -14.159 -1.608 43.360 1.00 17.88 ? 40 THR A N 1 ATOM 34 C CA . THR A 1 22 ? -14.872 -1.982 44.574 1.00 19.81 ? 40 THR A CA 1 ATOM 35 C C . THR A 1 22 ? -14.471 -1.088 45.734 1.00 19.49 ? 40 THR A C 1 ATOM 36 O O . THR A 1 22 ? -13.302 -0.998 46.070 1.00 19.60 ? 40 THR A O 1 ATOM 37 C CB . THR A 1 22 ? -14.568 -3.447 44.942 1.00 22.05 ? 40 THR A CB 1 ATOM 38 O OG1 . THR A 1 22 ? -14.870 -4.270 43.814 1.00 25.09 ? 40 THR A OG1 1 ATOM 39 C CG2 . THR A 1 22 ? -15.403 -3.881 46.133 1.00 24.08 ? 40 THR A CG2 1 ATOM 40 N N . ALA A 1 23 ? -15.447 -0.405 46.320 1.00 19.62 ? 41 ALA A N 1 ATOM 41 C CA . ALA A 1 23 ? -15.209 0.424 47.485 1.00 20.03 ? 41 ALA A CA 1 ATOM 42 C C . ALA A 1 23 ? -15.321 -0.451 48.735 1.00 21.25 ? 41 ALA A C 1 ATOM 43 O O . ALA A 1 23 ? -16.348 -1.101 48.949 1.00 22.49 ? 41 ALA A O 1 ATOM 44 C CB . ALA A 1 23 ? -16.218 1.571 47.524 1.00 20.37 ? 41 ALA A CB 1 ATOM 45 N N . GLY A 1 24 ? -14.268 -0.478 49.550 1.00 20.51 ? 42 GLY A N 1 ATOM 46 C CA . GLY A 1 24 ? -14.254 -1.268 50.788 1.00 20.93 ? 42 GLY A CA 1 ATOM 47 C C . GLY A 1 24 ? -15.155 -0.699 51.868 1.00 21.62 ? 42 GLY A C 1 ATOM 48 O O . GLY A 1 24 ? -15.591 -1.432 52.779 1.00 22.30 ? 42 GLY A O 1 ATOM 49 N N . GLY A 1 25 ? -15.436 0.604 51.775 1.00 19.89 ? 43 GLY A N 1 ATOM 50 C CA . GLY A 1 25 ? -16.347 1.290 52.695 1.00 21.00 ? 43 GLY A CA 1 ATOM 51 C C . GLY A 1 25 ? -15.788 1.562 54.082 1.00 22.17 ? 43 GLY A C 1 ATOM 52 O O . GLY A 1 25 ? -16.525 1.925 55.002 1.00 22.19 ? 43 GLY A O 1 ATOM 53 N N . ASP A 1 26 ? -14.486 1.393 54.258 1.00 21.35 ? 44 ASP A N 1 ATOM 54 C CA . ASP A 1 26 ? -13.899 1.638 55.572 1.00 22.32 ? 44 ASP A CA 1 ATOM 55 C C . ASP A 1 26 ? -12.485 2.175 55.495 1.00 20.28 ? 44 ASP A C 1 ATOM 56 O O . ASP A 1 26 ? -11.664 1.647 54.750 1.00 19.02 ? 44 ASP A O 1 ATOM 57 C CB . ASP A 1 26 ? -13.909 0.368 56.420 1.00 25.95 ? 44 ASP A CB 1 ATOM 58 C CG . ASP A 1 26 ? -13.500 0.647 57.846 1.00 29.17 ? 44 ASP A CG 1 ATOM 59 O OD1 . ASP A 1 26 ? -14.308 1.246 58.599 1.00 35.30 ? 44 ASP A OD1 1 ATOM 60 O OD2 . ASP A 1 26 ? -12.361 0.315 58.198 1.00 29.53 ? 44 ASP A OD2 1 ATOM 61 N N . SER A 1 27 ? -12.201 3.208 56.285 1.00 20.13 ? 45 SER A N 1 ATOM 62 C CA . SER A 1 27 ? -10.910 3.889 56.210 1.00 19.74 ? 45 SER A CA 1 ATOM 63 C C . SER A 1 27 ? -9.748 2.995 56.633 1.00 19.38 ? 45 SER A C 1 ATOM 64 O O . SER A 1 27 ? -8.620 3.279 56.298 1.00 19.89 ? 45 SER A O 1 ATOM 65 C CB . SER A 1 27 ? -10.902 5.180 57.036 1.00 20.92 ? 45 SER A CB 1 ATOM 66 O OG . SER A 1 27 ? -11.103 4.899 58.411 1.00 22.04 ? 45 SER A OG 1 ATOM 67 N N . SER A 1 28 ? -10.026 1.916 57.362 1.00 19.41 ? 46 SER A N 1 ATOM 68 C CA . SER A 1 28 ? -8.961 0.967 57.705 1.00 20.53 ? 46 SER A CA 1 ATOM 69 C C . SER A 1 28 ? -8.642 -0.007 56.579 1.00 19.69 ? 46 SER A C 1 ATOM 70 O O . SER A 1 28 ? -7.699 -0.794 56.691 1.00 21.06 ? 46 SER A O 1 ATOM 71 C CB . SER A 1 28 ? -9.308 0.190 58.976 1.00 22.19 ? 46 SER A CB 1 ATOM 72 O OG . SER A 1 28 ? -9.215 1.070 60.073 1.00 26.59 ? 46 SER A OG 1 ATOM 73 N N . THR A 1 29 ? -9.435 0.022 55.514 1.00 18.06 ? 47 THR A N 1 ATOM 74 C CA . THR A 1 29 ? -9.184 -0.840 54.361 1.00 17.55 ? 47 THR A CA 1 ATOM 75 C C . THR A 1 29 ? -8.716 -0.012 53.180 1.00 15.94 ? 47 THR A C 1 ATOM 76 O O . THR A 1 29 ? -9.431 0.878 52.723 1.00 15.05 ? 47 THR A O 1 ATOM 77 C CB . THR A 1 29 ? -10.428 -1.660 53.984 1.00 19.48 ? 47 THR A CB 1 ATOM 78 O OG1 . THR A 1 29 ? -10.766 -2.500 55.091 1.00 21.53 ? 47 THR A OG1 1 ATOM 79 C CG2 . THR A 1 29 ? -10.152 -2.535 52.767 1.00 20.66 ? 47 THR A CG2 1 ATOM 80 N N . ASP A 1 30 ? -7.517 -0.324 52.695 1.00 14.11 ? 48 ASP A N 1 ATOM 81 C CA . ASP A 1 30 ? -6.942 0.404 51.565 1.00 13.52 ? 48 ASP A CA 1 ATOM 82 C C . ASP A 1 30 ? -7.682 -0.001 50.281 1.00 13.45 ? 48 ASP A C 1 ATOM 83 O O . ASP A 1 30 ? -7.758 -1.193 49.957 1.00 13.26 ? 48 ASP A O 1 ATOM 84 C CB . ASP A 1 30 ? -5.457 0.047 51.467 1.00 13.31 ? 48 ASP A CB 1 ATOM 85 C CG . ASP A 1 30 ? -4.693 0.986 50.558 1.00 13.73 ? 48 ASP A CG 1 ATOM 86 O OD1 . ASP A 1 30 ? -5.320 1.856 49.911 1.00 13.46 ? 48 ASP A OD1 1 ATOM 87 O OD2 . ASP A 1 30 ? -3.456 0.850 50.526 1.00 14.41 ? 48 ASP A OD2 1 ATOM 88 N N . ASP A 1 31 ? -8.251 0.984 49.567 1.00 12.39 ? 49 ASP A N 1 ATOM 89 C CA . ASP A 1 31 ? -8.914 0.733 48.288 1.00 12.45 ? 49 ASP A CA 1 ATOM 90 C C . ASP A 1 31 ? -7.983 0.793 47.082 1.00 11.64 ? 49 ASP A C 1 ATOM 91 O O . ASP A 1 31 ? -8.399 0.504 45.957 1.00 11.61 ? 49 ASP A O 1 ATOM 92 C CB . ASP A 1 31 ? -10.069 1.734 48.068 1.00 13.20 ? 49 ASP A CB 1 ATOM 93 C CG . ASP A 1 31 ? -11.236 1.501 49.015 1.00 14.41 ? 49 ASP A CG 1 ATOM 94 O OD1 . ASP A 1 31 ? -11.532 0.326 49.349 1.00 15.20 ? 49 ASP A OD1 1 ATOM 95 O OD2 . ASP A 1 31 ? -11.877 2.498 49.422 1.00 15.00 ? 49 ASP A OD2 1 ATOM 96 N N . VAL A 1 32 ? -6.732 1.194 47.294 1.00 11.11 ? 50 VAL A N 1 ATOM 97 C CA . VAL A 1 32 ? -5.797 1.328 46.171 1.00 11.39 ? 50 VAL A CA 1 ATOM 98 C C . VAL A 1 32 ? -5.700 0.050 45.305 1.00 11.54 ? 50 VAL A C 1 ATOM 99 O O . VAL A 1 32 ? -5.766 0.140 44.092 1.00 11.41 ? 50 VAL A O 1 ATOM 100 C CB . VAL A 1 32 ? -4.418 1.851 46.631 1.00 11.31 ? 50 VAL A CB 1 ATOM 101 C CG1 . VAL A 1 32 ? -3.356 1.675 45.553 1.00 11.65 ? 50 VAL A CG1 1 ATOM 102 C CG2 . VAL A 1 32 ? -4.518 3.330 47.019 1.00 11.34 ? 50 VAL A CG2 1 ATOM 103 N N . PRO A 1 33 ? -5.596 -1.146 45.925 1.00 11.70 ? 51 PRO A N 1 ATOM 104 C CA . PRO A 1 33 ? -5.492 -2.315 45.023 1.00 11.90 ? 51 PRO A CA 1 ATOM 105 C C . PRO A 1 33 ? -6.708 -2.506 44.121 1.00 12.02 ? 51 PRO A C 1 ATOM 106 O O . PRO A 1 33 ? -6.548 -2.832 42.942 1.00 12.93 ? 51 PRO A O 1 ATOM 107 C CB . PRO A 1 33 ? -5.336 -3.490 45.998 1.00 11.43 ? 51 PRO A CB 1 ATOM 108 C CG . PRO A 1 33 ? -4.607 -2.870 47.148 1.00 11.28 ? 51 PRO A CG 1 ATOM 109 C CD . PRO A 1 33 ? -5.239 -1.497 47.312 1.00 11.54 ? 51 PRO A CD 1 ATOM 110 N N . ALA A 1 34 ? -7.908 -2.294 44.665 1.00 12.25 ? 52 ALA A N 1 ATOM 111 C CA . ALA A 1 34 ? -9.132 -2.361 43.868 1.00 12.47 ? 52 ALA A CA 1 ATOM 112 C C . ALA A 1 34 ? -9.115 -1.357 42.726 1.00 12.35 ? 52 ALA A C 1 ATOM 113 O O . ALA A 1 34 ? -9.563 -1.666 41.615 1.00 12.08 ? 52 ALA A O 1 ATOM 114 C CB . ALA A 1 34 ? -10.363 -2.135 44.739 1.00 12.25 ? 52 ALA A CB 1 ATOM 115 N N . ILE A 1 35 ? -8.601 -0.159 43.004 1.00 11.96 ? 53 ILE A N 1 ATOM 116 C CA . ILE A 1 35 ? -8.506 0.885 41.993 1.00 12.13 ? 53 ILE A CA 1 ATOM 117 C C . ILE A 1 35 ? -7.502 0.527 40.884 1.00 12.19 ? 53 ILE A C 1 ATOM 118 O O . ILE A 1 35 ? -7.810 0.649 39.696 1.00 11.87 ? 53 ILE A O 1 ATOM 119 C CB . ILE A 1 35 ? -8.169 2.251 42.635 1.00 11.79 ? 53 ILE A CB 1 ATOM 120 C CG1 . ILE A 1 35 ? -9.287 2.667 43.605 1.00 11.97 ? 53 ILE A CG1 1 ATOM 121 C CG2 . ILE A 1 35 ? -7.917 3.300 41.559 1.00 11.69 ? 53 ILE A CG2 1 ATOM 122 C CD1 . ILE A 1 35 ? -8.924 3.820 44.538 1.00 12.61 ? 53 ILE A CD1 1 ATOM 123 N N . THR A 1 36 ? -6.309 0.065 41.254 1.00 12.49 ? 54 THR A N 1 ATOM 124 C CA . THR A 1 36 ? -5.329 -0.269 40.218 1.00 13.12 ? 54 THR A CA 1 ATOM 125 C C . THR A 1 36 ? -5.725 -1.512 39.444 1.00 13.24 ? 54 THR A C 1 ATOM 126 O O . THR A 1 36 ? -5.379 -1.638 38.278 1.00 14.12 ? 54 THR A O 1 ATOM 127 C CB . THR A 1 36 ? -3.886 -0.376 40.750 1.00 13.18 ? 54 THR A CB 1 ATOM 128 O OG1 . THR A 1 36 ? -3.850 -1.351 41.800 1.00 13.82 ? 54 THR A OG1 1 ATOM 129 C CG2 . THR A 1 36 ? -3.429 0.991 41.288 1.00 13.51 ? 54 THR A CG2 1 ATOM 130 N N . GLU A 1 37 ? -6.462 -2.422 40.065 1.00 14.52 ? 55 GLU A N 1 ATOM 131 C CA . GLU A 1 37 ? -6.941 -3.584 39.313 1.00 14.99 ? 55 GLU A CA 1 ATOM 132 C C . GLU A 1 37 ? -7.976 -3.139 38.282 1.00 15.03 ? 55 GLU A C 1 ATOM 133 O O . GLU A 1 37 ? -7.951 -3.614 37.149 1.00 14.79 ? 55 GLU A O 1 ATOM 134 C CB . GLU A 1 37 ? -7.501 -4.673 40.222 1.00 17.51 ? 55 GLU A CB 1 ATOM 135 C CG . GLU A 1 37 ? -7.591 -6.039 39.536 1.00 20.14 ? 55 GLU A CG 1 ATOM 136 C CD . GLU A 1 37 ? -8.795 -6.143 38.623 1.00 23.56 ? 55 GLU A CD 1 ATOM 137 O OE1 . GLU A 1 37 ? -9.831 -5.504 38.948 1.00 25.10 ? 55 GLU A OE1 1 ATOM 138 O OE2 . GLU A 1 37 ? -8.707 -6.852 37.587 1.00 24.85 ? 55 GLU A OE2 1 ATOM 139 N N . ALA A 1 38 ? -8.862 -2.221 38.674 1.00 14.69 ? 56 ALA A N 1 ATOM 140 C CA . ALA A 1 38 ? -9.834 -1.657 37.733 1.00 15.09 ? 56 ALA A CA 1 ATOM 141 C C . ALA A 1 38 ? -9.120 -0.947 36.584 1.00 15.27 ? 56 ALA A C 1 ATOM 142 O O . ALA A 1 38 ? -9.482 -1.126 35.411 1.00 16.23 ? 56 ALA A O 1 ATOM 143 C CB . ALA A 1 38 ? -10.783 -0.697 38.448 1.00 15.84 ? 56 ALA A CB 1 ATOM 144 N N . LEU A 1 39 ? -8.094 -0.160 36.909 1.00 14.57 ? 57 LEU A N 1 ATOM 145 C CA . LEU A 1 39 ? -7.306 0.517 35.883 1.00 16.05 ? 57 LEU A CA 1 ATOM 146 C C . LEU A 1 39 ? -6.586 -0.482 34.980 1.00 16.00 ? 57 LEU A C 1 ATOM 147 O O . LEU A 1 39 ? -6.544 -0.317 33.764 1.00 16.58 ? 57 LEU A O 1 ATOM 148 C CB . LEU A 1 39 ? -6.312 1.516 36.498 1.00 17.64 ? 57 LEU A CB 1 ATOM 149 C CG . LEU A 1 39 ? -5.824 2.603 35.533 1.00 21.54 ? 57 LEU A CG 1 ATOM 150 C CD1 . LEU A 1 39 ? -6.967 3.540 35.139 1.00 22.76 ? 57 LEU A CD1 1 ATOM 151 C CD2 . LEU A 1 39 ? -4.689 3.411 36.148 1.00 22.49 ? 57 LEU A CD2 1 ATOM 152 N N . SER A 1 40 ? -6.018 -1.525 35.569 1.00 15.88 ? 58 SER A N 1 ATOM 153 C CA . SER A 1 40 ? -5.332 -2.529 34.771 1.00 16.64 ? 58 SER A CA 1 ATOM 154 C C . SER A 1 40 ? -6.308 -3.250 33.840 1.00 17.11 ? 58 SER A C 1 ATOM 155 O O . SER A 1 40 ? -5.994 -3.541 32.671 1.00 16.83 ? 58 SER A O 1 ATOM 156 C CB . SER A 1 40 ? -4.629 -3.542 35.674 1.00 17.48 ? 58 SER A CB 1 ATOM 157 O OG . SER A 1 40 ? -3.726 -4.282 34.875 1.00 19.93 ? 58 SER A OG 1 ATOM 158 N N . SER A 1 41 ? -7.502 -3.509 34.350 1.00 17.03 ? 59 SER A N 1 ATOM 159 C CA . SER A 1 41 ? -8.495 -4.245 33.585 1.00 19.71 ? 59 SER A CA 1 ATOM 160 C C . SER A 1 41 ? -9.089 -3.399 32.438 1.00 20.85 ? 59 SER A C 1 ATOM 161 O O . SER A 1 41 ? -9.234 -3.894 31.314 1.00 21.68 ? 59 SER A O 1 ATOM 162 C CB . SER A 1 41 ? -9.586 -4.758 34.515 1.00 20.77 ? 59 SER A CB 1 ATOM 163 O OG . SER A 1 41 ? -10.592 -5.429 33.774 1.00 24.81 ? 59 SER A OG 1 ATOM 164 N N . CYS A 1 42 ? -9.406 -2.136 32.724 1.00 21.01 ? 60 CYS A N 1 ATOM 165 C CA . CYS A 1 42 ? -10.116 -1.258 31.780 1.00 23.51 ? 60 CYS A CA 1 ATOM 166 C C . CYS A 1 42 ? -9.282 -0.128 31.172 1.00 24.61 ? 60 CYS A C 1 ATOM 167 O O . CYS A 1 42 ? -9.742 0.547 30.242 1.00 25.44 ? 60 CYS A O 1 ATOM 168 C CB . CYS A 1 42 ? -11.353 -0.656 32.447 1.00 25.51 ? 60 CYS A CB 1 ATOM 169 S SG . CYS A 1 42 ? -12.746 -1.801 32.520 1.00 31.20 ? 60 CYS A SG 1 ATOM 170 N N . GLY A 1 43 ? -8.070 0.078 31.681 1.00 23.66 ? 61 GLY A N 1 ATOM 171 C CA . GLY A 1 43 ? -7.276 1.265 31.347 1.00 23.84 ? 61 GLY A CA 1 ATOM 172 C C . GLY A 1 43 ? -6.639 1.324 29.974 1.00 24.16 ? 61 GLY A C 1 ATOM 173 O O . GLY A 1 43 ? -6.090 2.358 29.602 1.00 23.53 ? 61 GLY A O 1 ATOM 174 N N . ASN A 1 44 ? -6.694 0.224 29.223 1.00 24.73 ? 62 ASN A N 1 ATOM 175 C CA . ASN A 1 44 ? -6.247 0.231 27.840 1.00 25.66 ? 62 ASN A CA 1 ATOM 176 C C . ASN A 1 44 ? -7.387 0.718 26.946 1.00 24.78 ? 62 ASN A C 1 ATOM 177 O O . ASN A 1 44 ? -8.101 -0.072 26.320 1.00 24.44 ? 62 ASN A O 1 ATOM 178 C CB . ASN A 1 44 ? -5.712 -1.140 27.398 1.00 29.84 ? 62 ASN A CB 1 ATOM 179 C CG . ASN A 1 44 ? -4.973 -1.079 26.065 1.00 32.54 ? 62 ASN A CG 1 ATOM 180 O OD1 . ASN A 1 44 ? -4.581 -0.008 25.608 1.00 34.99 ? 62 ASN A OD1 1 ATOM 181 N ND2 . ASN A 1 44 ? -4.782 -2.235 25.435 1.00 36.73 ? 62 ASN A ND2 1 ATOM 182 N N . GLY A 1 45 ? -7.584 2.030 26.932 1.00 22.70 ? 63 GLY A N 1 ATOM 183 C CA . GLY A 1 45 ? -8.624 2.633 26.115 1.00 21.18 ? 63 GLY A CA 1 ATOM 184 C C . GLY A 1 45 ? -10.012 2.684 26.724 1.00 21.47 ? 63 GLY A C 1 ATOM 185 O O . GLY A 1 45 ? -10.960 3.119 26.070 1.00 22.86 ? 63 GLY A O 1 ATOM 186 N N . GLY A 1 46 ? -10.144 2.253 27.974 1.00 20.33 ? 64 GLY A N 1 ATOM 187 C CA . GLY A 1 46 ? -11.440 2.197 28.638 1.00 20.23 ? 64 GLY A CA 1 ATOM 188 C C . GLY A 1 46 ? -11.655 3.260 29.697 1.00 20.48 ? 64 GLY A C 1 ATOM 189 O O . GLY A 1 46 ? -10.962 4.293 29.731 1.00 20.85 ? 64 GLY A O 1 ATOM 190 N N . THR A 1 47 ? -12.619 2.995 30.571 1.00 19.49 ? 65 THR A N 1 ATOM 191 C CA . THR A 1 47 ? -13.070 3.965 31.550 1.00 19.13 ? 65 THR A CA 1 ATOM 192 C C . THR A 1 47 ? -13.156 3.349 32.937 1.00 18.75 ? 65 THR A C 1 ATOM 193 O O . THR A 1 47 ? -13.583 2.199 33.100 1.00 17.96 ? 65 THR A O 1 ATOM 194 C CB . THR A 1 47 ? -14.429 4.548 31.141 1.00 19.46 ? 65 THR A CB 1 ATOM 195 O OG1 . THR A 1 47 ? -14.301 5.090 29.825 1.00 21.43 ? 65 THR A OG1 1 ATOM 196 C CG2 . THR A 1 47 ? -14.888 5.649 32.107 1.00 19.01 ? 65 THR A CG2 1 ATOM 197 N N . ILE A 1 48 ? -12.714 4.123 33.920 1.00 17.65 ? 66 ILE A N 1 ATOM 198 C CA . ILE A 1 48 ? -12.845 3.766 35.317 1.00 18.18 ? 66 ILE A CA 1 ATOM 199 C C . ILE A 1 48 ? -13.712 4.833 35.980 1.00 17.20 ? 66 ILE A C 1 ATOM 200 O O . ILE A 1 48 ? -13.506 6.029 35.776 1.00 17.42 ? 66 ILE A O 1 ATOM 201 C CB . ILE A 1 48 ? -11.442 3.684 35.961 1.00 20.57 ? 66 ILE A CB 1 ATOM 202 C CG1 . ILE A 1 48 ? -10.725 2.413 35.470 1.00 21.20 ? 66 ILE A CG1 1 ATOM 203 C CG2 . ILE A 1 48 ? -11.519 3.734 37.469 1.00 21.10 ? 66 ILE A CG2 1 ATOM 204 C CD1 . ILE A 1 48 ? -10.048 2.577 34.119 1.00 22.92 ? 66 ILE A CD1 1 ATOM 205 N N . VAL A 1 49 ? -14.700 4.399 36.748 1.00 16.04 ? 67 VAL A N 1 ATOM 206 C CA . VAL A 1 49 ? -15.675 5.320 37.330 1.00 15.69 ? 67 VAL A CA 1 ATOM 207 C C . VAL A 1 49 ? -15.664 5.239 38.856 1.00 16.05 ? 67 VAL A C 1 ATOM 208 O O . VAL A 1 49 ? -15.802 4.164 39.432 1.00 15.35 ? 67 VAL A O 1 ATOM 209 C CB . VAL A 1 49 ? -17.112 5.031 36.807 1.00 15.55 ? 67 VAL A CB 1 ATOM 210 C CG1 . VAL A 1 49 ? -18.140 5.877 37.552 1.00 16.36 ? 67 VAL A CG1 1 ATOM 211 C CG2 . VAL A 1 49 ? -17.191 5.286 35.301 1.00 16.11 ? 67 VAL A CG2 1 ATOM 212 N N . PHE A 1 50 ? -15.483 6.382 39.510 1.00 15.45 ? 68 PHE A N 1 ATOM 213 C CA . PHE A 1 50 ? -15.746 6.484 40.930 1.00 16.03 ? 68 PHE A CA 1 ATOM 214 C C . PHE A 1 50 ? -17.096 7.180 41.045 1.00 16.84 ? 68 PHE A C 1 ATOM 215 O O . PHE A 1 50 ? -17.174 8.391 40.809 1.00 16.55 ? 68 PHE A O 1 ATOM 216 C CB . PHE A 1 50 ? -14.671 7.336 41.617 1.00 15.75 ? 68 PHE A CB 1 ATOM 217 C CG . PHE A 1 50 ? -13.286 6.780 41.489 1.00 15.75 ? 68 PHE A CG 1 ATOM 218 C CD1 . PHE A 1 50 ? -12.817 5.858 42.415 1.00 15.98 ? 68 PHE A CD1 1 ATOM 219 C CD2 . PHE A 1 50 ? -12.443 7.192 40.469 1.00 16.49 ? 68 PHE A CD2 1 ATOM 220 C CE1 . PHE A 1 50 ? -11.532 5.345 42.313 1.00 15.73 ? 68 PHE A CE1 1 ATOM 221 C CE2 . PHE A 1 50 ? -11.152 6.680 40.358 1.00 17.22 ? 68 PHE A CE2 1 ATOM 222 C CZ . PHE A 1 50 ? -10.697 5.758 41.291 1.00 16.02 ? 68 PHE A CZ 1 ATOM 223 N N . PRO A 1 51 ? -18.168 6.429 41.389 1.00 17.37 ? 69 PRO A N 1 ATOM 224 C CA . PRO A 1 51 ? -19.511 6.992 41.299 1.00 17.99 ? 69 PRO A CA 1 ATOM 225 C C . PRO A 1 51 ? -19.794 8.176 42.208 1.00 17.92 ? 69 PRO A C 1 ATOM 226 O O . PRO A 1 51 ? -19.230 8.304 43.287 1.00 17.22 ? 69 PRO A O 1 ATOM 227 C CB . PRO A 1 51 ? -20.414 5.824 41.742 1.00 18.22 ? 69 PRO A CB 1 ATOM 228 C CG . PRO A 1 51 ? -19.608 4.604 41.451 1.00 18.40 ? 69 PRO A CG 1 ATOM 229 C CD . PRO A 1 51 ? -18.206 5.020 41.820 1.00 17.49 ? 69 PRO A CD 1 ATOM 230 N N . GLU A 1 52 ? -20.732 9.012 41.771 1.00 19.91 ? 70 GLU A N 1 ATOM 231 C CA . GLU A 1 52 ? -21.223 10.094 42.607 1.00 22.71 ? 70 GLU A CA 1 ATOM 232 C C . GLU A 1 52 ? -21.709 9.556 43.964 1.00 22.53 ? 70 GLU A C 1 ATOM 233 O O . GLU A 1 52 ? -22.380 8.524 44.031 1.00 22.85 ? 70 GLU A O 1 ATOM 234 C CB . GLU A 1 52 ? -22.330 10.865 41.861 1.00 27.28 ? 70 GLU A CB 1 ATOM 235 C CG . GLU A 1 52 ? -22.913 12.044 42.623 1.00 34.48 ? 70 GLU A CG 1 ATOM 236 C CD . GLU A 1 52 ? -24.286 11.751 43.225 1.00 40.33 ? 70 GLU A CD 1 ATOM 237 O OE1 . GLU A 1 52 ? -24.699 10.565 43.263 1.00 43.33 ? 70 GLU A OE1 1 ATOM 238 O OE2 . GLU A 1 52 ? -24.967 12.717 43.653 1.00 44.31 ? 70 GLU A OE2 1 ATOM 239 N N . GLY A 1 53 ? -21.328 10.243 45.032 1.00 20.81 ? 71 GLY A N 1 ATOM 240 C CA . GLY A 1 53 ? -21.703 9.872 46.388 1.00 20.91 ? 71 GLY A CA 1 ATOM 241 C C . GLY A 1 53 ? -20.829 8.793 47.007 1.00 20.26 ? 71 GLY A C 1 ATOM 242 O O . GLY A 1 53 ? -21.044 8.420 48.157 1.00 22.03 ? 71 GLY A O 1 ATOM 243 N N . SER A 1 54 ? -19.860 8.275 46.254 1.00 17.92 ? 72 SER A N 1 ATOM 244 C CA . SER A 1 54 ? -18.950 7.248 46.798 1.00 17.41 ? 72 SER A CA 1 ATOM 245 C C . SER A 1 54 ? -17.804 7.871 47.604 1.00 17.26 ? 72 SER A C 1 ATOM 246 O O . SER A 1 54 ? -17.492 9.057 47.439 1.00 17.19 ? 72 SER A O 1 ATOM 247 C CB . SER A 1 54 ? -18.416 6.330 45.692 1.00 16.96 ? 72 SER A CB 1 ATOM 248 O OG . SER A 1 54 ? -17.560 7.027 44.795 1.00 16.59 ? 72 SER A OG 1 ATOM 249 N N . THR A 1 55 ? -17.203 7.083 48.495 1.00 16.72 ? 73 THR A N 1 ATOM 250 C CA . THR A 1 55 ? -15.967 7.479 49.180 1.00 16.38 ? 73 THR A CA 1 ATOM 251 C C . THR A 1 55 ? -14.987 6.309 49.106 1.00 15.91 ? 73 THR A C 1 ATOM 252 O O . THR A 1 55 ? -15.312 5.181 49.511 1.00 15.79 ? 73 THR A O 1 ATOM 253 C CB . THR A 1 55 ? -16.188 7.885 50.657 1.00 18.00 ? 73 THR A CB 1 ATOM 254 O OG1 . THR A 1 55 ? -17.070 9.022 50.728 1.00 18.45 ? 73 THR A OG1 1 ATOM 255 C CG2 . THR A 1 55 ? -14.864 8.277 51.314 1.00 17.43 ? 73 THR A CG2 1 ATOM 256 N N . TYR A 1 56 ? -13.808 6.584 48.571 1.00 13.90 ? 74 TYR A N 1 ATOM 257 C CA . TYR A 1 56 ? -12.736 5.593 48.510 1.00 13.61 ? 74 TYR A CA 1 ATOM 258 C C . TYR A 1 56 ? -11.612 6.051 49.421 1.00 13.85 ? 74 TYR A C 1 ATOM 259 O O . TYR A 1 56 ? -11.333 7.248 49.508 1.00 13.88 ? 74 TYR A O 1 ATOM 260 C CB . TYR A 1 56 ? -12.217 5.454 47.082 1.00 13.26 ? 74 TYR A CB 1 ATOM 261 C CG . TYR A 1 56 ? -13.196 4.763 46.153 1.00 13.42 ? 74 TYR A CG 1 ATOM 262 C CD1 . TYR A 1 56 ? -14.316 5.438 45.654 1.00 13.69 ? 74 TYR A CD1 1 ATOM 263 C CD2 . TYR A 1 56 ? -13.004 3.437 45.784 1.00 13.61 ? 74 TYR A CD2 1 ATOM 264 C CE1 . TYR A 1 56 ? -15.213 4.803 44.807 1.00 13.89 ? 74 TYR A CE1 1 ATOM 265 C CE2 . TYR A 1 56 ? -13.896 2.785 44.950 1.00 13.73 ? 74 TYR A CE2 1 ATOM 266 C CZ . TYR A 1 56 ? -14.995 3.474 44.461 1.00 13.87 ? 74 TYR A CZ 1 ATOM 267 O OH . TYR A 1 56 ? -15.867 2.827 43.622 1.00 14.64 ? 74 TYR A OH 1 ATOM 268 N N . TYR A 1 57 ? -10.980 5.094 50.102 1.00 13.00 ? 75 TYR A N 1 ATOM 269 C CA . TYR A 1 57 ? -9.940 5.372 51.076 1.00 13.27 ? 75 TYR A CA 1 ATOM 270 C C . TYR A 1 57 ? -8.645 4.906 50.474 1.00 13.70 ? 75 TYR A C 1 ATOM 271 O O . TYR A 1 57 ? -8.487 3.730 50.177 1.00 13.58 ? 75 TYR A O 1 ATOM 272 C CB . TYR A 1 57 ? -10.223 4.644 52.405 1.00 14.27 ? 75 TYR A CB 1 ATOM 273 C CG . TYR A 1 57 ? -11.493 5.164 53.002 1.00 15.22 ? 75 TYR A CG 1 ATOM 274 C CD1 . TYR A 1 57 ? -11.504 6.382 53.689 1.00 15.91 ? 75 TYR A CD1 1 ATOM 275 C CD2 . TYR A 1 57 ? -12.694 4.478 52.826 1.00 15.68 ? 75 TYR A CD2 1 ATOM 276 C CE1 . TYR A 1 57 ? -12.679 6.885 54.227 1.00 17.71 ? 75 TYR A CE1 1 ATOM 277 C CE2 . TYR A 1 57 ? -13.886 4.978 53.346 1.00 17.46 ? 75 TYR A CE2 1 ATOM 278 C CZ . TYR A 1 57 ? -13.864 6.175 54.046 1.00 17.92 ? 75 TYR A CZ 1 ATOM 279 O OH . TYR A 1 57 ? -15.034 6.691 54.557 1.00 19.10 ? 75 TYR A OH 1 ATOM 280 N N . LEU A 1 58 ? -7.735 5.846 50.249 1.00 12.54 ? 76 LEU A N 1 ATOM 281 C CA . LEU A 1 58 ? -6.499 5.524 49.570 1.00 12.68 ? 76 LEU A CA 1 ATOM 282 C C . LEU A 1 58 ? -5.401 5.598 50.610 1.00 12.53 ? 76 LEU A C 1 ATOM 283 O O . LEU A 1 58 ? -5.021 6.682 51.044 1.00 12.89 ? 76 LEU A O 1 ATOM 284 C CB . LEU A 1 58 ? -6.253 6.524 48.431 1.00 13.23 ? 76 LEU A CB 1 ATOM 285 C CG . LEU A 1 58 ? -7.096 6.346 47.148 1.00 14.77 ? 76 LEU A CG 1 ATOM 286 C CD1 . LEU A 1 58 ? -8.582 6.414 47.383 1.00 15.93 ? 76 LEU A CD1 1 ATOM 287 C CD2 . LEU A 1 58 ? -6.701 7.426 46.153 1.00 14.66 ? 76 LEU A CD2 1 ATOM 288 N N . ASN A 1 59 ? -4.894 4.449 51.029 1.00 11.92 ? 77 ASN A N 1 ATOM 289 C CA . ASN A 1 59 ? -3.967 4.428 52.162 1.00 11.87 ? 77 ASN A CA 1 ATOM 290 C C . ASN A 1 59 ? -2.516 4.169 51.744 1.00 11.84 ? 77 ASN A C 1 ATOM 291 O O . ASN A 1 59 ? -1.643 3.868 52.585 1.00 12.15 ? 77 ASN A O 1 ATOM 292 C CB . ASN A 1 59 ? -4.425 3.386 53.180 1.00 12.94 ? 77 ASN A CB 1 ATOM 293 C CG . ASN A 1 59 ? -5.782 3.704 53.765 1.00 13.65 ? 77 ASN A CG 1 ATOM 294 O OD1 . ASN A 1 59 ? -6.271 4.830 53.648 1.00 14.18 ? 77 ASN A OD1 1 ATOM 295 N ND2 . ASN A 1 59 ? -6.412 2.702 54.391 1.00 13.94 ? 77 ASN A ND2 1 ATOM 296 N N . SER A 1 60 ? -2.268 4.324 50.447 1.00 11.68 ? 78 SER A N 1 ATOM 297 C CA . SER A 1 60 ? -0.945 4.124 49.869 1.00 11.52 ? 78 SER A CA 1 ATOM 298 C C . SER A 1 60 ? -0.859 4.887 48.562 1.00 11.47 ? 78 SER A C 1 ATOM 299 O O . SER A 1 60 ? -1.868 5.453 48.106 1.00 10.96 ? 78 SER A O 1 ATOM 300 C CB . SER A 1 60 ? -0.717 2.632 49.629 1.00 12.30 ? 78 SER A CB 1 ATOM 301 O OG . SER A 1 60 ? -1.713 2.104 48.772 1.00 13.06 ? 78 SER A OG 1 ATOM 302 N N . VAL A 1 61 ? 0.327 4.906 47.950 1.00 11.17 ? 79 VAL A N 1 ATOM 303 C CA . VAL A 1 61 ? 0.500 5.586 46.657 1.00 11.02 ? 79 VAL A CA 1 ATOM 304 C C . VAL A 1 61 ? -0.434 4.978 45.613 1.00 11.35 ? 79 VAL A C 1 ATOM 305 O O . VAL A 1 61 ? -0.495 3.751 45.494 1.00 11.62 ? 79 VAL A O 1 ATOM 306 C CB . VAL A 1 61 ? 1.943 5.435 46.155 1.00 11.10 ? 79 VAL A CB 1 ATOM 307 C CG1 . VAL A 1 61 ? 2.076 5.982 44.731 1.00 10.92 ? 79 VAL A CG1 1 ATOM 308 C CG2 . VAL A 1 61 ? 2.906 6.130 47.117 1.00 11.11 ? 79 VAL A CG2 1 ATOM 309 N N . LEU A 1 62 ? -1.153 5.823 44.879 1.00 11.14 ? 80 LEU A N 1 ATOM 310 C CA . LEU A 1 62 ? -1.992 5.369 43.763 1.00 12.03 ? 80 LEU A CA 1 ATOM 311 C C . LEU A 1 62 ? -1.230 5.589 42.471 1.00 12.70 ? 80 LEU A C 1 ATOM 312 O O . LEU A 1 62 ? -0.983 6.726 42.070 1.00 12.50 ? 80 LEU A O 1 ATOM 313 C CB . LEU A 1 62 ? -3.306 6.161 43.708 1.00 12.48 ? 80 LEU A CB 1 ATOM 314 C CG . LEU A 1 62 ? -4.229 5.863 42.524 1.00 13.04 ? 80 LEU A CG 1 ATOM 315 C CD1 . LEU A 1 62 ? -4.591 4.388 42.467 1.00 13.45 ? 80 LEU A CD1 1 ATOM 316 C CD2 . LEU A 1 62 ? -5.491 6.716 42.626 1.00 13.48 ? 80 LEU A CD2 1 ATOM 317 N N . ASP A 1 63 ? -0.842 4.494 41.836 1.00 13.09 ? 81 ASP A N 1 ATOM 318 C CA . ASP A 1 63 ? -0.037 4.565 40.635 1.00 14.45 ? 81 ASP A CA 1 ATOM 319 C C . ASP A 1 63 ? -0.952 4.368 39.431 1.00 14.68 ? 81 ASP A C 1 ATOM 320 O O . ASP A 1 63 ? -1.650 3.356 39.342 1.00 15.22 ? 81 ASP A O 1 ATOM 321 C CB . ASP A 1 63 ? 1.047 3.482 40.693 1.00 16.49 ? 81 ASP A CB 1 ATOM 322 C CG . ASP A 1 63 ? 2.097 3.665 39.632 1.00 18.47 ? 81 ASP A CG 1 ATOM 323 O OD1 . ASP A 1 63 ? 1.724 3.615 38.442 1.00 19.17 ? 81 ASP A OD1 1 ATOM 324 O OD2 . ASP A 1 63 ? 3.290 3.857 39.981 1.00 20.72 ? 81 ASP A OD2 1 ATOM 325 N N . LEU A 1 64 ? -0.982 5.348 38.537 1.00 14.32 ? 82 LEU A N 1 ATOM 326 C CA . LEU A 1 64 ? -1.891 5.319 37.381 1.00 14.00 ? 82 LEU A CA 1 ATOM 327 C C . LEU A 1 64 ? -1.222 4.796 36.106 1.00 14.50 ? 82 LEU A C 1 ATOM 328 O O . LEU A 1 64 ? -1.748 4.969 34.998 1.00 14.57 ? 82 LEU A O 1 ATOM 329 C CB . LEU A 1 64 ? -2.498 6.710 37.138 1.00 14.09 ? 82 LEU A CB 1 ATOM 330 C CG . LEU A 1 64 ? -3.311 7.292 38.302 1.00 14.27 ? 82 LEU A CG 1 ATOM 331 C CD1 . LEU A 1 64 ? -3.966 8.610 37.870 1.00 14.23 ? 82 LEU A CD1 1 ATOM 332 C CD2 . LEU A 1 64 ? -4.365 6.305 38.797 1.00 14.25 ? 82 LEU A CD2 1 ATOM 333 N N . GLY A 1 65 ? -0.101 4.107 36.279 1.00 15.58 ? 83 GLY A N 1 ATOM 334 C CA . GLY A 1 65 ? 0.727 3.707 35.146 1.00 16.60 ? 83 GLY A CA 1 ATOM 335 C C . GLY A 1 65 ? 0.080 2.785 34.127 1.00 17.11 ? 83 GLY A C 1 ATOM 336 O O . GLY A 1 65 ? 0.537 2.724 32.995 1.00 19.00 ? 83 GLY A O 1 ATOM 337 N N . SER A 1 66 ? -0.975 2.069 34.490 1.00 17.69 ? 84 SER A N 1 ATOM 338 C CA . SER A 1 66 ? -1.586 1.151 33.518 1.00 19.33 ? 84 SER A CA 1 ATOM 339 C C . SER A 1 66 ? -2.557 1.866 32.571 1.00 19.76 ? 84 SER A C 1 ATOM 340 O O . SER A 1 66 ? -3.135 1.257 31.675 1.00 19.81 ? 84 SER A O 1 ATOM 341 C CB . SER A 1 66 ? -2.262 -0.018 34.224 1.00 21.05 ? 84 SER A CB 1 ATOM 342 O OG . SER A 1 66 ? -3.365 0.456 34.945 1.00 23.68 ? 84 SER A OG 1 ATOM 343 N N . CYS A 1 67 ? -2.725 3.164 32.774 1.00 19.12 ? 85 CYS A N 1 ATOM 344 C CA . CYS A 1 67 ? -3.577 3.966 31.917 1.00 19.37 ? 85 CYS A CA 1 ATOM 345 C C . CYS A 1 67 ? -2.924 4.110 30.550 1.00 19.04 ? 85 CYS A C 1 ATOM 346 O O . CYS A 1 67 ? -1.776 4.511 30.450 1.00 17.64 ? 85 CYS A O 1 ATOM 347 C CB . CYS A 1 67 ? -3.752 5.351 32.529 1.00 21.36 ? 85 CYS A CB 1 ATOM 348 S SG . CYS A 1 67 ? -4.700 6.458 31.473 1.00 26.30 ? 85 CYS A SG 1 ATOM 349 N N . SER A 1 68 ? -3.665 3.792 29.496 1.00 19.41 ? 86 SER A N 1 ATOM 350 C CA . SER A 1 68 ? -3.200 4.071 28.136 1.00 19.55 ? 86 SER A CA 1 ATOM 351 C C . SER A 1 68 ? -4.428 4.516 27.351 1.00 19.41 ? 86 SER A C 1 ATOM 352 O O . SER A 1 68 ? -5.266 3.697 26.974 1.00 19.10 ? 86 SER A O 1 ATOM 353 C CB . SER A 1 68 ? -2.566 2.811 27.535 1.00 21.09 ? 86 SER A CB 1 ATOM 354 O OG . SER A 1 68 ? -2.172 3.028 26.198 1.00 23.98 ? 86 SER A OG 1 ATOM 355 N N . ASP A 1 69 ? -4.547 5.823 27.147 1.00 19.50 ? 87 ASP A N 1 ATOM 356 C CA . ASP A 1 69 ? -5.765 6.429 26.576 1.00 21.88 ? 87 ASP A CA 1 ATOM 357 C C . ASP A 1 69 ? -6.980 6.079 27.414 1.00 21.76 ? 87 ASP A C 1 ATOM 358 O O . ASP A 1 69 ? -8.039 5.719 26.883 1.00 22.90 ? 87 ASP A O 1 ATOM 359 C CB . ASP A 1 69 ? -5.967 6.002 25.114 1.00 24.67 ? 87 ASP A CB 1 ATOM 360 C CG . ASP A 1 69 ? -4.789 6.362 24.242 1.00 29.62 ? 87 ASP A CG 1 ATOM 361 O OD1 . ASP A 1 69 ? -4.417 7.554 24.217 1.00 31.30 ? 87 ASP A OD1 1 ATOM 362 O OD2 . ASP A 1 69 ? -4.219 5.453 23.585 1.00 35.09 ? 87 ASP A OD2 1 ATOM 363 N N . CYS A 1 70 ? -6.817 6.164 28.731 1.00 20.46 ? 88 CYS A N 1 ATOM 364 C CA . CYS A 1 70 ? -7.881 5.801 29.651 1.00 19.95 ? 88 CYS A CA 1 ATOM 365 C C . CYS A 1 70 ? -8.613 7.049 30.105 1.00 18.79 ? 88 CYS A C 1 ATOM 366 O O . CYS A 1 70 ? -8.105 8.172 29.985 1.00 18.12 ? 88 CYS A O 1 ATOM 367 C CB . CYS A 1 70 ? -7.330 5.035 30.860 1.00 23.29 ? 88 CYS A CB 1 ATOM 368 S SG . CYS A 1 70 ? -6.581 6.094 32.107 1.00 28.29 ? 88 CYS A SG 1 ATOM 369 N N . ASP A 1 71 ? -9.811 6.840 30.626 1.00 17.43 ? 89 ASP A N 1 ATOM 370 C CA . ASP A 1 71 ? -10.634 7.918 31.154 1.00 17.25 ? 89 ASP A CA 1 ATOM 371 C C . ASP A 1 71 ? -11.005 7.557 32.594 1.00 16.62 ? 89 ASP A C 1 ATOM 372 O O . ASP A 1 71 ? -11.689 6.561 32.838 1.00 16.63 ? 89 ASP A O 1 ATOM 373 C CB . ASP A 1 71 ? -11.870 8.078 30.254 1.00 18.72 ? 89 ASP A CB 1 ATOM 374 C CG . ASP A 1 71 ? -12.826 9.178 30.712 1.00 20.54 ? 89 ASP A CG 1 ATOM 375 O OD1 . ASP A 1 71 ? -12.456 10.077 31.510 1.00 20.64 ? 89 ASP A OD1 1 ATOM 376 O OD2 . ASP A 1 71 ? -13.981 9.146 30.230 1.00 22.05 ? 89 ASP A OD2 1 ATOM 377 N N . ILE A 1 72 ? -10.512 8.345 33.547 1.00 14.82 ? 90 ILE A N 1 ATOM 378 C CA . ILE A 1 72 ? -10.781 8.122 34.965 1.00 14.73 ? 90 ILE A CA 1 ATOM 379 C C . ILE A 1 72 ? -11.767 9.185 35.453 1.00 14.70 ? 90 ILE A C 1 ATOM 380 O O . ILE A 1 72 ? -11.414 10.359 35.610 1.00 14.56 ? 90 ILE A O 1 ATOM 381 C CB . ILE A 1 72 ? -9.478 8.176 35.799 1.00 15.02 ? 90 ILE A CB 1 ATOM 382 C CG1 . ILE A 1 72 ? -8.440 7.210 35.216 1.00 15.48 ? 90 ILE A CG1 1 ATOM 383 C CG2 . ILE A 1 72 ? -9.753 7.873 37.261 1.00 15.17 ? 90 ILE A CG2 1 ATOM 384 C CD1 . ILE A 1 72 ? -7.056 7.305 35.851 1.00 16.28 ? 90 ILE A CD1 1 ATOM 385 N N . GLN A 1 73 ? -13.002 8.765 35.681 1.00 13.94 ? 91 GLN A N 1 ATOM 386 C CA . GLN A 1 73 ? -14.074 9.694 36.065 1.00 14.58 ? 91 GLN A CA 1 ATOM 387 C C . GLN A 1 73 ? -14.263 9.678 37.569 1.00 14.87 ? 91 GLN A C 1 ATOM 388 O O . GLN A 1 73 ? -14.777 8.717 38.156 1.00 14.49 ? 91 GLN A O 1 ATOM 389 C CB . GLN A 1 73 ? -15.372 9.368 35.314 1.00 15.16 ? 91 GLN A CB 1 ATOM 390 C CG . GLN A 1 73 ? -15.143 9.303 33.810 1.00 16.30 ? 91 GLN A CG 1 ATOM 391 C CD . GLN A 1 73 ? -16.385 8.935 33.015 1.00 16.55 ? 91 GLN A CD 1 ATOM 392 O OE1 . GLN A 1 73 ? -17.462 8.678 33.584 1.00 17.13 ? 91 GLN A OE1 1 ATOM 393 N NE2 . GLN A 1 73 ? -16.234 8.885 31.693 1.00 16.48 ? 91 GLN A NE2 1 ATOM 394 N N . VAL A 1 74 ? -13.819 10.752 38.205 1.00 14.62 ? 92 VAL A N 1 ATOM 395 C CA . VAL A 1 74 ? -13.899 10.860 39.654 1.00 14.63 ? 92 VAL A CA 1 ATOM 396 C C . VAL A 1 74 ? -15.127 11.694 39.979 1.00 14.92 ? 92 VAL A C 1 ATOM 397 O O . VAL A 1 74 ? -15.115 12.917 39.780 1.00 14.19 ? 92 VAL A O 1 ATOM 398 C CB . VAL A 1 74 ? -12.627 11.518 40.230 1.00 14.86 ? 92 VAL A CB 1 ATOM 399 C CG1 . VAL A 1 74 ? -12.665 11.532 41.758 1.00 14.78 ? 92 VAL A CG1 1 ATOM 400 C CG2 . VAL A 1 74 ? -11.368 10.815 39.701 1.00 15.09 ? 92 VAL A CG2 1 ATOM 401 N N . GLU A 1 75 ? -16.200 11.045 40.441 1.00 14.61 ? 93 GLU A N 1 ATOM 402 C CA . GLU A 1 75 ? -17.404 11.794 40.843 1.00 15.05 ? 93 GLU A CA 1 ATOM 403 C C . GLU A 1 75 ? -17.621 11.765 42.348 1.00 14.96 ? 93 GLU A C 1 ATOM 404 O O . GLU A 1 75 ? -18.420 12.532 42.884 1.00 16.54 ? 93 GLU A O 1 ATOM 405 C CB . GLU A 1 75 ? -18.654 11.283 40.104 1.00 15.03 ? 93 GLU A CB 1 ATOM 406 C CG . GLU A 1 75 ? -18.435 11.028 38.619 1.00 15.43 ? 93 GLU A CG 1 ATOM 407 C CD . GLU A 1 75 ? -18.002 12.272 37.848 1.00 15.15 ? 93 GLU A CD 1 ATOM 408 O OE1 . GLU A 1 75 ? -18.153 13.391 38.367 1.00 16.61 ? 93 GLU A OE1 1 ATOM 409 O OE2 . GLU A 1 75 ? -17.518 12.124 36.721 1.00 16.28 ? 93 GLU A OE2 1 ATOM 410 N N . GLY A 1 76 ? -16.882 10.894 43.033 1.00 15.15 ? 94 GLY A N 1 ATOM 411 C CA . GLY A 1 76 ? -16.970 10.787 44.478 1.00 13.97 ? 94 GLY A CA 1 ATOM 412 C C . GLY A 1 76 ? -15.751 11.373 45.159 1.00 14.17 ? 94 GLY A C 1 ATOM 413 O O . GLY A 1 76 ? -15.018 12.187 44.579 1.00 14.08 ? 94 GLY A O 1 ATOM 414 N N . LEU A 1 77 ? -15.531 10.928 46.390 1.00 13.52 ? 95 LEU A N 1 ATOM 415 C CA . LEU A 1 77 ? -14.437 11.407 47.222 1.00 13.43 ? 95 LEU A CA 1 ATOM 416 C C . LEU A 1 77 ? -13.326 10.362 47.249 1.00 13.81 ? 95 LEU A C 1 ATOM 417 O O . LEU A 1 77 ? -13.588 9.195 47.532 1.00 14.35 ? 95 LEU A O 1 ATOM 418 C CB . LEU A 1 77 ? -14.950 11.632 48.651 1.00 13.59 ? 95 LEU A CB 1 ATOM 419 C CG . LEU A 1 77 ? -13.897 11.994 49.730 1.00 13.48 ? 95 LEU A CG 1 ATOM 420 C CD1 . LEU A 1 77 ? -13.106 13.245 49.325 1.00 13.52 ? 95 LEU A CD1 1 ATOM 421 C CD2 . LEU A 1 77 ? -14.566 12.171 51.085 1.00 13.79 ? 95 LEU A CD2 1 ATOM 422 N N . LEU A 1 78 ? -12.106 10.771 46.901 1.00 13.40 ? 96 LEU A N 1 ATOM 423 C CA . LEU A 1 78 ? -10.929 9.917 47.092 1.00 13.30 ? 96 LEU A CA 1 ATOM 424 C C . LEU A 1 78 ? -10.196 10.518 48.260 1.00 13.50 ? 96 LEU A C 1 ATOM 425 O O . LEU A 1 78 ? -9.653 11.625 48.153 1.00 12.95 ? 96 LEU A O 1 ATOM 426 C CB . LEU A 1 78 ? -10.013 9.930 45.856 1.00 14.34 ? 96 LEU A CB 1 ATOM 427 C CG . LEU A 1 78 ? -10.633 9.606 44.490 1.00 15.28 ? 96 LEU A CG 1 ATOM 428 C CD1 . LEU A 1 78 ? -9.581 9.469 43.399 1.00 15.20 ? 96 LEU A CD1 1 ATOM 429 C CD2 . LEU A 1 78 ? -11.465 8.346 44.562 1.00 16.15 ? 96 LEU A CD2 1 ATOM 430 N N . LYS A 1 79 ? -10.207 9.816 49.390 1.00 12.74 ? 97 LYS A N 1 ATOM 431 C CA . LYS A 1 79 ? -9.641 10.369 50.593 1.00 13.23 ? 97 LYS A CA 1 ATOM 432 C C . LYS A 1 79 ? -8.357 9.640 50.947 1.00 12.52 ? 97 LYS A C 1 ATOM 433 O O . LYS A 1 79 ? -8.391 8.456 51.285 1.00 11.69 ? 97 LYS A O 1 ATOM 434 C CB . LYS A 1 79 ? -10.632 10.282 51.753 1.00 15.06 ? 97 LYS A CB 1 ATOM 435 C CG . LYS A 1 79 ? -10.040 10.905 53.015 1.00 17.76 ? 97 LYS A CG 1 ATOM 436 C CD . LYS A 1 79 ? -11.056 11.057 54.113 1.00 21.26 ? 97 LYS A CD 1 ATOM 437 C CE . LYS A 1 79 ? -10.493 11.917 55.231 1.00 23.73 ? 97 LYS A CE 1 ATOM 438 N NZ . LYS A 1 79 ? -11.427 11.845 56.390 1.00 28.30 ? 97 LYS A NZ 1 ATOM 439 N N . PHE A 1 80 ? -7.232 10.350 50.852 1.00 11.53 ? 98 PHE A N 1 ATOM 440 C CA . PHE A 1 80 ? -5.946 9.774 51.275 1.00 12.05 ? 98 PHE A CA 1 ATOM 441 C C . PHE A 1 80 ? -5.796 9.691 52.781 1.00 12.38 ? 98 PHE A C 1 ATOM 442 O O . PHE A 1 80 ? -6.278 10.553 53.514 1.00 12.94 ? 98 PHE A O 1 ATOM 443 C CB . PHE A 1 80 ? -4.786 10.585 50.709 1.00 11.93 ? 98 PHE A CB 1 ATOM 444 C CG . PHE A 1 80 ? -4.477 10.249 49.299 1.00 11.88 ? 98 PHE A CG 1 ATOM 445 C CD1 . PHE A 1 80 ? -3.700 9.126 48.996 1.00 12.05 ? 98 PHE A CD1 1 ATOM 446 C CD2 . PHE A 1 80 ? -4.961 11.042 48.250 1.00 12.14 ? 98 PHE A CD2 1 ATOM 447 C CE1 . PHE A 1 80 ? -3.413 8.808 47.674 1.00 12.03 ? 98 PHE A CE1 1 ATOM 448 C CE2 . PHE A 1 80 ? -4.670 10.715 46.930 1.00 12.55 ? 98 PHE A CE2 1 ATOM 449 C CZ . PHE A 1 80 ? -3.896 9.606 46.646 1.00 12.30 ? 98 PHE A CZ 1 ATOM 450 N N . ALA A 1 81 ? -5.115 8.639 53.241 1.00 12.18 ? 99 ALA A N 1 ATOM 451 C CA . ALA A 1 81 ? -4.720 8.541 54.643 1.00 12.44 ? 99 ALA A CA 1 ATOM 452 C C . ALA A 1 81 ? -3.702 9.617 54.981 1.00 13.05 ? 99 ALA A C 1 ATOM 453 O O . ALA A 1 81 ? -2.858 9.944 54.152 1.00 13.05 ? 99 ALA A O 1 ATOM 454 C CB . ALA A 1 81 ? -4.109 7.179 54.912 1.00 12.50 ? 99 ALA A CB 1 ATOM 455 N N . SER A 1 82 ? -3.776 10.156 56.196 1.00 13.05 ? 100 SER A N 1 ATOM 456 C CA . SER A 1 82 ? -2.748 11.098 56.667 1.00 14.16 ? 100 SER A CA 1 ATOM 457 C C . SER A 1 82 ? -1.417 10.387 56.928 1.00 14.72 ? 100 SER A C 1 ATOM 458 O O . SER A 1 82 ? -0.354 10.952 56.680 1.00 15.84 ? 100 SER A O 1 ATOM 459 C CB . SER A 1 82 ? -3.230 11.814 57.929 1.00 14.94 ? 100 SER A CB 1 ATOM 460 O OG . SER A 1 82 ? -3.477 10.850 58.951 1.00 16.62 ? 100 SER A OG 1 ATOM 461 N N . ASP A 1 83 ? -1.504 9.154 57.439 1.00 15.40 ? 101 ASP A N 1 ATOM 462 C CA . ASP A 1 83 ? -0.361 8.274 57.802 1.00 15.24 ? 101 ASP A CA 1 ATOM 463 C C . ASP A 1 83 ? 1.010 8.910 57.545 1.00 14.83 ? 101 ASP A C 1 ATOM 464 O O . ASP A 1 83 ? 1.672 8.615 56.546 1.00 14.58 ? 101 ASP A O 1 ATOM 465 C CB . ASP A 1 83 ? -0.515 6.954 57.038 1.00 16.49 ? 101 ASP A CB 1 ATOM 466 C CG . ASP A 1 83 ? 0.357 5.821 57.582 1.00 17.36 ? 101 ASP A CG 1 ATOM 467 O OD1 . ASP A 1 83 ? 1.331 6.060 58.338 1.00 18.17 ? 101 ASP A OD1 1 ATOM 468 O OD2 . ASP A 1 83 ? 0.066 4.658 57.205 1.00 18.58 ? 101 ASP A OD2 1 ATOM 469 N N . THR A 1 84 ? 1.447 9.790 58.446 1.00 14.08 ? 102 THR A N 1 ATOM 470 C CA . THR A 1 84 ? 2.690 10.523 58.182 1.00 14.00 ? 102 THR A CA 1 ATOM 471 C C . THR A 1 84 ? 3.941 9.631 58.085 1.00 14.01 ? 102 THR A C 1 ATOM 472 O O . THR A 1 84 ? 4.856 9.961 57.350 1.00 13.49 ? 102 THR A O 1 ATOM 473 C CB . THR A 1 84 ? 2.919 11.687 59.174 1.00 14.42 ? 102 THR A CB 1 ATOM 474 O OG1 . THR A 1 84 ? 2.882 11.192 60.517 1.00 14.46 ? 102 THR A OG1 1 ATOM 475 C CG2 . THR A 1 84 ? 1.839 12.738 58.984 1.00 14.46 ? 102 THR A CG2 1 ATOM 476 N N . ASP A 1 85 ? 3.971 8.515 58.821 1.00 14.81 ? 103 ASP A N 1 ATOM 477 C CA . ASP A 1 85 ? 5.093 7.584 58.728 1.00 15.58 ? 103 ASP A CA 1 ATOM 478 C C . ASP A 1 85 ? 5.149 6.980 57.328 1.00 14.68 ? 103 ASP A C 1 ATOM 479 O O . ASP A 1 85 ? 6.232 6.810 56.756 1.00 16.16 ? 103 ASP A O 1 ATOM 480 C CB . ASP A 1 85 ? 4.952 6.436 59.741 1.00 17.76 ? 103 ASP A CB 1 ATOM 481 C CG . ASP A 1 85 ? 5.322 6.834 61.169 1.00 21.23 ? 103 ASP A CG 1 ATOM 482 O OD1 . ASP A 1 85 ? 5.804 7.958 61.411 1.00 22.57 ? 103 ASP A OD1 1 ATOM 483 O OD2 . ASP A 1 85 ? 5.126 5.984 62.066 1.00 23.80 ? 103 ASP A OD2 1 ATOM 484 N N . TYR A 1 86 ? 3.986 6.629 56.781 1.00 14.07 ? 104 TYR A N 1 ATOM 485 C CA . TYR A 1 86 ? 3.961 6.039 55.441 1.00 12.82 ? 104 TYR A CA 1 ATOM 486 C C . TYR A 1 86 ? 4.438 7.039 54.373 1.00 12.61 ? 104 TYR A C 1 ATOM 487 O O . TYR A 1 86 ? 5.267 6.713 53.510 1.00 12.09 ? 104 TYR A O 1 ATOM 488 C CB . TYR A 1 86 ? 2.564 5.505 55.090 1.00 12.92 ? 104 TYR A CB 1 ATOM 489 C CG . TYR A 1 86 ? 2.500 5.017 53.667 1.00 12.59 ? 104 TYR A CG 1 ATOM 490 C CD1 . TYR A 1 86 ? 2.922 3.716 53.332 1.00 12.68 ? 104 TYR A CD1 1 ATOM 491 C CD2 . TYR A 1 86 ? 2.075 5.873 52.625 1.00 12.03 ? 104 TYR A CD2 1 ATOM 492 C CE1 . TYR A 1 86 ? 2.894 3.279 52.014 1.00 12.19 ? 104 TYR A CE1 1 ATOM 493 C CE2 . TYR A 1 86 ? 2.051 5.441 51.316 1.00 12.16 ? 104 TYR A CE2 1 ATOM 494 C CZ . TYR A 1 86 ? 2.450 4.152 51.010 1.00 12.40 ? 104 TYR A CZ 1 ATOM 495 O OH . TYR A 1 86 ? 2.411 3.734 49.704 1.00 11.93 ? 104 TYR A OH 1 ATOM 496 N N . TRP A 1 87 ? 3.905 8.253 54.427 1.00 11.69 ? 105 TRP A N 1 ATOM 497 C CA . TRP A 1 87 ? 4.184 9.249 53.390 1.00 11.69 ? 105 TRP A CA 1 ATOM 498 C C . TRP A 1 87 ? 5.545 9.864 53.485 1.00 11.82 ? 105 TRP A C 1 ATOM 499 O O . TRP A 1 87 ? 6.007 10.501 52.530 1.00 11.27 ? 105 TRP A O 1 ATOM 500 C CB . TRP A 1 87 ? 3.116 10.351 53.434 1.00 11.56 ? 105 TRP A CB 1 ATOM 501 C CG . TRP A 1 87 ? 1.788 9.821 52.991 1.00 11.66 ? 105 TRP A CG 1 ATOM 502 C CD1 . TRP A 1 87 ? 0.623 9.667 53.744 1.00 12.12 ? 105 TRP A CD1 1 ATOM 503 C CD2 . TRP A 1 87 ? 1.458 9.311 51.663 1.00 12.00 ? 105 TRP A CD2 1 ATOM 504 N NE1 . TRP A 1 87 ? -0.381 9.117 52.974 1.00 12.29 ? 105 TRP A NE1 1 ATOM 505 C CE2 . TRP A 1 87 ? 0.055 8.882 51.719 1.00 12.06 ? 105 TRP A CE2 1 ATOM 506 C CE3 . TRP A 1 87 ? 2.159 9.170 50.473 1.00 12.31 ? 105 TRP A CE3 1 ATOM 507 C CZ2 . TRP A 1 87 ? -0.595 8.345 50.613 1.00 12.09 ? 105 TRP A CZ2 1 ATOM 508 C CZ3 . TRP A 1 87 ? 1.488 8.638 49.360 1.00 12.02 ? 105 TRP A CZ3 1 ATOM 509 C CH2 . TRP A 1 87 ? 0.145 8.233 49.435 1.00 12.37 ? 105 TRP A CH2 1 ATOM 510 N N . SER A 1 88 ? 6.210 9.674 54.621 1.00 12.76 ? 106 SER A N 1 ATOM 511 C CA . SER A 1 88 ? 7.525 10.280 54.857 1.00 13.48 ? 106 SER A CA 1 ATOM 512 C C . SER A 1 88 ? 8.515 10.032 53.701 1.00 13.60 ? 106 SER A C 1 ATOM 513 O O . SER A 1 88 ? 8.833 8.884 53.386 1.00 14.28 ? 106 SER A O 1 ATOM 514 C CB . SER A 1 88 ? 8.120 9.738 56.169 1.00 14.19 ? 106 SER A CB 1 ATOM 515 O OG . SER A 1 88 ? 9.330 10.411 56.453 1.00 15.56 ? 106 SER A OG 1 ATOM 516 N N . GLY A 1 89 ? 8.993 11.112 53.089 1.00 13.52 ? 107 GLY A N 1 ATOM 517 C CA . GLY A 1 89 ? 9.971 11.039 52.007 1.00 13.44 ? 107 GLY A CA 1 ATOM 518 C C . GLY A 1 89 ? 9.468 10.500 50.673 1.00 13.46 ? 107 GLY A C 1 ATOM 519 O O . GLY A 1 89 ? 10.262 10.305 49.743 1.00 14.23 ? 107 GLY A O 1 ATOM 520 N N . ARG A 1 90 ? 8.170 10.235 50.567 1.00 12.31 ? 108 ARG A N 1 ATOM 521 C CA . ARG A 1 90 ? 7.621 9.718 49.324 1.00 11.91 ? 108 ARG A CA 1 ATOM 522 C C . ARG A 1 90 ? 7.436 10.824 48.293 1.00 11.78 ? 108 ARG A C 1 ATOM 523 O O . ARG A 1 90 ? 7.126 11.964 48.635 1.00 11.39 ? 108 ARG A O 1 ATOM 524 C CB . ARG A 1 90 ? 6.302 8.975 49.569 1.00 11.50 ? 108 ARG A CB 1 ATOM 525 C CG . ARG A 1 90 ? 6.510 7.688 50.360 1.00 11.67 ? 108 ARG A CG 1 ATOM 526 C CD . ARG A 1 90 ? 5.323 6.744 50.210 1.00 11.63 ? 108 ARG A CD 1 ATOM 527 N NE . ARG A 1 90 ? 5.587 5.488 50.919 1.00 11.61 ? 108 ARG A NE 1 ATOM 528 C CZ . ARG A 1 90 ? 6.307 4.475 50.424 1.00 11.55 ? 108 ARG A CZ 1 ATOM 529 N NH1 . ARG A 1 90 ? 6.851 4.541 49.205 1.00 11.19 ? 108 ARG A NH1 1 ATOM 530 N NH2 . ARG A 1 90 ? 6.491 3.394 51.173 1.00 11.74 ? 108 ARG A NH2 1 ATOM 531 N N . THR A 1 91 ? 7.610 10.472 47.023 1.00 11.68 ? 109 THR A N 1 ATOM 532 C CA . THR A 1 91 ? 7.514 11.439 45.943 1.00 11.84 ? 109 THR A CA 1 ATOM 533 C C . THR A 1 91 ? 6.084 11.897 45.652 1.00 11.40 ? 109 THR A C 1 ATOM 534 O O . THR A 1 91 ? 5.830 13.096 45.504 1.00 10.90 ? 109 THR A O 1 ATOM 535 C CB . THR A 1 91 ? 8.159 10.858 44.672 1.00 13.00 ? 109 THR A CB 1 ATOM 536 O OG1 . THR A 1 91 ? 9.561 10.707 44.923 1.00 14.58 ? 109 THR A OG1 1 ATOM 537 C CG2 . THR A 1 91 ? 7.950 11.788 43.460 1.00 12.80 ? 109 THR A CG2 1 ATOM 538 N N . ALA A 1 92 ? 5.164 10.937 45.543 1.00 11.57 ? 110 ALA A N 1 ATOM 539 C CA . ALA A 1 92 ? 3.849 11.189 44.947 1.00 10.91 ? 110 ALA A CA 1 ATOM 540 C C . ALA A 1 92 ? 2.755 10.449 45.706 1.00 10.98 ? 110 ALA A C 1 ATOM 541 O O . ALA A 1 92 ? 2.964 9.328 46.169 1.00 10.76 ? 110 ALA A O 1 ATOM 542 C CB . ALA A 1 92 ? 3.847 10.707 43.510 1.00 11.34 ? 110 ALA A CB 1 ATOM 543 N N . MET A 1 93 ? 1.591 11.083 45.823 1.00 10.24 ? 111 MET A N 1 ATOM 544 C CA . MET A 1 93 ? 0.414 10.382 46.332 1.00 10.33 ? 111 MET A CA 1 ATOM 545 C C . MET A 1 93 ? -0.317 9.733 45.166 1.00 10.63 ? 111 MET A C 1 ATOM 546 O O . MET A 1 93 ? -0.720 8.570 45.256 1.00 10.70 ? 111 MET A O 1 ATOM 547 C CB . MET A 1 93 ? -0.481 11.373 47.060 1.00 10.37 ? 111 MET A CB 1 ATOM 548 C CG . MET A 1 93 ? 0.304 12.092 48.148 1.00 10.54 ? 111 MET A CG 1 ATOM 549 S SD . MET A 1 93 ? -0.686 13.274 49.071 1.00 12.33 ? 111 MET A SD 1 ATOM 550 C CE . MET A 1 93 ? -1.618 12.168 50.112 1.00 11.81 ? 111 MET A CE 1 ATOM 551 N N . ILE A 1 94 ? -0.513 10.490 44.085 1.00 10.53 ? 112 ILE A N 1 ATOM 552 C CA . ILE A 1 94 ? -0.961 9.923 42.810 1.00 10.81 ? 112 ILE A CA 1 ATOM 553 C C . ILE A 1 94 ? 0.198 10.064 41.832 1.00 11.72 ? 112 ILE A C 1 ATOM 554 O O . ILE A 1 94 ? 0.643 11.186 41.536 1.00 11.38 ? 112 ILE A O 1 ATOM 555 C CB . ILE A 1 94 ? -2.206 10.651 42.237 1.00 10.84 ? 112 ILE A CB 1 ATOM 556 C CG1 . ILE A 1 94 ? -3.351 10.607 43.248 1.00 10.95 ? 112 ILE A CG1 1 ATOM 557 C CG2 . ILE A 1 94 ? -2.637 10.017 40.921 1.00 11.02 ? 112 ILE A CG2 1 ATOM 558 C CD1 . ILE A 1 94 ? -4.508 11.537 42.882 1.00 11.48 ? 112 ILE A CD1 1 ATOM 559 N N . SER A 1 95 ? 0.700 8.925 41.356 1.00 12.03 ? 113 SER A N 1 ATOM 560 C CA . SER A 1 95 ? 1.893 8.926 40.490 1.00 12.76 ? 113 SER A CA 1 ATOM 561 C C . SER A 1 95 ? 1.472 8.651 39.045 1.00 13.14 ? 113 SER A C 1 ATOM 562 O O . SER A 1 95 ? 0.804 7.649 38.766 1.00 12.78 ? 113 SER A O 1 ATOM 563 C CB . SER A 1 95 ? 2.907 7.886 40.974 1.00 13.57 ? 113 SER A CB 1 ATOM 564 O OG . SER A 1 95 ? 3.951 7.733 40.008 1.00 15.85 ? 113 SER A OG 1 ATOM 565 N N . VAL A 1 96 ? 1.841 9.557 38.135 1.00 12.86 ? 114 VAL A N 1 ATOM 566 C CA . VAL A 1 96 ? 1.458 9.443 36.727 1.00 13.30 ? 114 VAL A CA 1 ATOM 567 C C . VAL A 1 96 ? 2.764 9.494 35.947 1.00 13.12 ? 114 VAL A C 1 ATOM 568 O O . VAL A 1 96 ? 3.228 10.569 35.550 1.00 12.64 ? 114 VAL A O 1 ATOM 569 C CB . VAL A 1 96 ? 0.486 10.570 36.290 1.00 12.82 ? 114 VAL A CB 1 ATOM 570 C CG1 . VAL A 1 96 ? -0.022 10.336 34.868 1.00 13.46 ? 114 VAL A CG1 1 ATOM 571 C CG2 . VAL A 1 96 ? -0.712 10.652 37.241 1.00 13.83 ? 114 VAL A CG2 1 ATOM 572 N N . SER A 1 97 ? 3.375 8.325 35.775 1.00 14.10 ? 115 SER A N 1 ATOM 573 C CA . SER A 1 97 ? 4.713 8.248 35.201 1.00 14.24 ? 115 SER A CA 1 ATOM 574 C C . SER A 1 97 ? 4.658 7.636 33.813 1.00 15.13 ? 115 SER A C 1 ATOM 575 O O . SER A 1 97 ? 4.197 6.501 33.656 1.00 14.83 ? 115 SER A O 1 ATOM 576 C CB . SER A 1 97 ? 5.621 7.399 36.097 1.00 15.45 ? 115 SER A CB 1 ATOM 577 O OG . SER A 1 97 ? 6.959 7.424 35.613 1.00 17.91 ? 115 SER A OG 1 ATOM 578 N N . ASN A 1 98 ? 5.123 8.381 32.816 1.00 15.29 ? 116 ASN A N 1 ATOM 579 C CA . ASN A 1 98 ? 5.166 7.876 31.441 1.00 16.20 ? 116 ASN A CA 1 ATOM 580 C C . ASN A 1 98 ? 3.813 7.349 30.958 1.00 16.20 ? 116 ASN A C 1 ATOM 581 O O . ASN A 1 98 ? 3.715 6.269 30.366 1.00 16.06 ? 116 ASN A O 1 ATOM 582 C CB . ASN A 1 98 ? 6.256 6.798 31.303 1.00 18.15 ? 116 ASN A CB 1 ATOM 583 C CG . ASN A 1 98 ? 6.681 6.591 29.861 1.00 21.51 ? 116 ASN A CG 1 ATOM 584 O OD1 . ASN A 1 98 ? 6.415 7.429 28.999 1.00 23.67 ? 116 ASN A OD1 1 ATOM 585 N ND2 . ASN A 1 98 ? 7.336 5.472 29.589 1.00 24.11 ? 116 ASN A ND2 1 ATOM 586 N N . VAL A 1 99 ? 2.761 8.126 31.200 1.00 14.70 ? 117 VAL A N 1 ATOM 587 C CA . VAL A 1 99 ? 1.440 7.731 30.766 1.00 14.85 ? 117 VAL A CA 1 ATOM 588 C C . VAL A 1 99 ? 1.137 8.527 29.512 1.00 15.70 ? 117 VAL A C 1 ATOM 589 O O . VAL A 1 99 ? 1.357 9.736 29.485 1.00 14.52 ? 117 VAL A O 1 ATOM 590 C CB . VAL A 1 99 ? 0.396 8.005 31.869 1.00 14.89 ? 117 VAL A CB 1 ATOM 591 C CG1 . VAL A 1 99 ? -1.026 7.902 31.325 1.00 14.83 ? 117 VAL A CG1 1 ATOM 592 C CG2 . VAL A 1 99 ? 0.626 7.038 33.025 1.00 15.17 ? 117 VAL A CG2 1 ATOM 593 N N . ASP A 1 100 ? 0.688 7.827 28.469 1.00 16.61 ? 118 ASP A N 1 ATOM 594 C CA . ASP A 1 100 ? 0.273 8.470 27.228 1.00 18.61 ? 118 ASP A CA 1 ATOM 595 C C . ASP A 1 100 ? -1.234 8.360 27.086 1.00 18.50 ? 118 ASP A C 1 ATOM 596 O O . ASP A 1 100 ? -1.765 7.271 26.883 1.00 19.01 ? 118 ASP A O 1 ATOM 597 C CB . ASP A 1 100 ? 0.972 7.810 26.034 1.00 21.05 ? 118 ASP A CB 1 ATOM 598 C CG . ASP A 1 100 ? 2.478 7.924 26.116 1.00 24.17 ? 118 ASP A CG 1 ATOM 599 O OD1 . ASP A 1 100 ? 2.974 9.060 26.259 1.00 25.57 ? 118 ASP A OD1 1 ATOM 600 O OD2 . ASP A 1 100 ? 3.175 6.884 26.039 1.00 26.76 ? 118 ASP A OD2 1 ATOM 601 N N . GLY A 1 101 ? -1.923 9.489 27.213 1.00 17.52 ? 119 GLY A N 1 ATOM 602 C CA . GLY A 1 101 ? -3.366 9.522 27.039 1.00 17.81 ? 119 GLY A CA 1 ATOM 603 C C . GLY A 1 101 ? -4.065 9.237 28.344 1.00 17.70 ? 119 GLY A C 1 ATOM 604 O O . GLY A 1 101 ? -4.319 8.090 28.685 1.00 18.42 ? 119 GLY A O 1 ATOM 605 N N . LEU A 1 102 ? -4.342 10.282 29.102 1.00 17.16 ? 120 LEU A N 1 ATOM 606 C CA . LEU A 1 102 ? -5.073 10.125 30.333 1.00 17.44 ? 120 LEU A CA 1 ATOM 607 C C . LEU A 1 102 ? -6.065 11.261 30.444 1.00 17.11 ? 120 LEU A C 1 ATOM 608 O O . LEU A 1 102 ? -5.752 12.402 30.108 1.00 16.75 ? 120 LEU A O 1 ATOM 609 C CB . LEU A 1 102 ? -4.121 10.144 31.537 1.00 18.45 ? 120 LEU A CB 1 ATOM 610 C CG . LEU A 1 102 ? -4.789 10.518 32.867 1.00 20.40 ? 120 LEU A CG 1 ATOM 611 C CD1 . LEU A 1 102 ? -5.458 9.301 33.481 1.00 22.84 ? 120 LEU A CD1 1 ATOM 612 C CD2 . LEU A 1 102 ? -3.842 11.173 33.856 1.00 23.18 ? 120 LEU A CD2 1 ATOM 613 N N . LYS A 1 103 ? -7.260 10.934 30.908 1.00 16.52 ? 121 LYS A N 1 ATOM 614 C CA . LYS A 1 103 ? -8.192 11.952 31.378 1.00 17.43 ? 121 LYS A CA 1 ATOM 615 C C . LYS A 1 103 ? -8.493 11.623 32.831 1.00 16.63 ? 121 LYS A C 1 ATOM 616 O O . LYS A 1 103 ? -8.966 10.528 33.141 1.00 17.04 ? 121 LYS A O 1 ATOM 617 C CB . LYS A 1 103 ? -9.481 11.954 30.555 1.00 19.97 ? 121 LYS A CB 1 ATOM 618 C CG . LYS A 1 103 ? -9.253 12.032 29.051 1.00 23.35 ? 121 LYS A CG 1 ATOM 619 C CD . LYS A 1 103 ? -10.580 11.957 28.301 1.00 27.55 ? 121 LYS A CD 1 ATOM 620 C CE . LYS A 1 103 ? -10.375 11.667 26.818 1.00 31.42 ? 121 LYS A CE 1 ATOM 621 N NZ . LYS A 1 103 ? -10.134 10.212 26.597 1.00 36.11 ? 121 LYS A NZ 1 ATOM 622 N N . LEU A 1 104 ? -8.185 12.553 33.719 1.00 14.34 ? 122 LEU A N 1 ATOM 623 C CA . LEU A 1 104 ? -8.514 12.405 35.125 1.00 14.47 ? 122 LEU A CA 1 ATOM 624 C C . LEU A 1 104 ? -9.468 13.533 35.402 1.00 14.71 ? 122 LEU A C 1 ATOM 625 O O . LEU A 1 104 ? -9.065 14.704 35.468 1.00 14.44 ? 122 LEU A O 1 ATOM 626 C CB . LEU A 1 104 ? -7.260 12.515 36.007 1.00 14.51 ? 122 LEU A CB 1 ATOM 627 C CG . LEU A 1 104 ? -7.439 12.470 37.535 1.00 15.25 ? 122 LEU A CG 1 ATOM 628 C CD1 . LEU A 1 104 ? -7.962 11.120 38.001 1.00 14.94 ? 122 LEU A CD1 1 ATOM 629 C CD2 . LEU A 1 104 ? -6.124 12.763 38.249 1.00 15.24 ? 122 LEU A CD2 1 ATOM 630 N N . ARG A 1 105 ? -10.740 13.200 35.530 1.00 13.80 ? 123 ARG A N 1 ATOM 631 C CA . ARG A 1 105 ? -11.733 14.276 35.472 1.00 13.90 ? 123 ARG A CA 1 ATOM 632 C C . ARG A 1 105 ? -12.976 13.997 36.263 1.00 14.24 ? 123 ARG A C 1 ATOM 633 O O . ARG A 1 105 ? -13.329 12.847 36.478 1.00 14.09 ? 123 ARG A O 1 ATOM 634 C CB . ARG A 1 105 ? -12.082 14.550 34.017 1.00 14.19 ? 123 ARG A CB 1 ATOM 635 C CG . ARG A 1 105 ? -12.609 13.344 33.252 1.00 14.96 ? 123 ARG A CG 1 ATOM 636 C CD . ARG A 1 105 ? -12.862 13.764 31.808 1.00 16.33 ? 123 ARG A CD 1 ATOM 637 N NE . ARG A 1 105 ? -13.432 12.683 31.028 1.00 16.69 ? 123 ARG A NE 1 ATOM 638 C CZ . ARG A 1 105 ? -14.059 12.866 29.871 1.00 17.33 ? 123 ARG A CZ 1 ATOM 639 N NH1 . ARG A 1 105 ? -14.210 14.100 29.388 1.00 17.22 ? 123 ARG A NH1 1 ATOM 640 N NH2 . ARG A 1 105 ? -14.539 11.825 29.216 1.00 18.98 ? 123 ARG A NH2 1 ATOM 641 N N . SER A 1 106 ? -13.636 15.056 36.713 1.00 14.08 ? 124 SER A N 1 ATOM 642 C CA . SER A 1 106 ? -14.972 14.916 37.254 1.00 14.37 ? 124 SER A CA 1 ATOM 643 C C . SER A 1 106 ? -15.922 15.482 36.216 1.00 14.65 ? 124 SER A C 1 ATOM 644 O O . SER A 1 106 ? -15.803 16.649 35.843 1.00 15.77 ? 124 SER A O 1 ATOM 645 C CB . SER A 1 106 ? -15.138 15.658 38.582 1.00 13.96 ? 124 SER A CB 1 ATOM 646 O OG . SER A 1 106 ? -16.492 15.545 39.017 1.00 13.94 ? 124 SER A OG 1 ATOM 647 N N . LEU A 1 107 ? -16.812 14.641 35.704 1.00 14.91 ? 125 LEU A N 1 ATOM 648 C CA . LEU A 1 107 ? -17.773 15.095 34.693 1.00 15.49 ? 125 LEU A CA 1 ATOM 649 C C . LEU A 1 107 ? -19.012 15.717 35.335 1.00 15.75 ? 125 LEU A C 1 ATOM 650 O O . LEU A 1 107 ? -19.727 16.486 34.693 1.00 16.51 ? 125 LEU A O 1 ATOM 651 C CB . LEU A 1 107 ? -18.128 13.968 33.711 1.00 15.76 ? 125 LEU A CB 1 ATOM 652 C CG . LEU A 1 107 ? -17.031 13.558 32.716 1.00 17.20 ? 125 LEU A CG 1 ATOM 653 C CD1 . LEU A 1 107 ? -17.477 12.380 31.850 1.00 17.43 ? 125 LEU A CD1 1 ATOM 654 C CD2 . LEU A 1 107 ? -16.608 14.746 31.843 1.00 18.81 ? 125 LEU A CD2 1 ATOM 655 N N . THR A 1 108 ? -19.260 15.409 36.604 1.00 16.17 ? 126 THR A N 1 ATOM 656 C CA . THR A 1 108 ? -20.370 16.044 37.325 1.00 16.02 ? 126 THR A CA 1 ATOM 657 C C . THR A 1 108 ? -19.938 17.318 38.019 1.00 16.61 ? 126 THR A C 1 ATOM 658 O O . THR A 1 108 ? -20.770 18.186 38.326 1.00 17.01 ? 126 THR A O 1 ATOM 659 C CB . THR A 1 108 ? -20.994 15.120 38.392 1.00 16.43 ? 126 THR A CB 1 ATOM 660 O OG1 . THR A 1 108 ? -20.026 14.868 39.423 1.00 16.34 ? 126 THR A OG1 1 ATOM 661 C CG2 . THR A 1 108 ? -21.465 13.804 37.773 1.00 16.60 ? 126 THR A CG2 1 ATOM 662 N N . GLY A 1 109 ? -18.640 17.418 38.303 1.00 16.45 ? 127 GLY A N 1 ATOM 663 C CA . GLY A 1 109 ? -18.100 18.486 39.137 1.00 15.89 ? 127 GLY A CA 1 ATOM 664 C C . GLY A 1 109 ? -18.096 18.186 40.630 1.00 16.17 ? 127 GLY A C 1 ATOM 665 O O . GLY A 1 109 ? -17.699 19.037 41.427 1.00 17.81 ? 127 GLY A O 1 ATOM 666 N N . SER A 1 110 ? -18.549 16.994 41.023 1.00 15.67 ? 128 SER A N 1 ATOM 667 C CA A SER A 1 110 ? -18.655 16.642 42.436 0.50 15.30 ? 128 SER A CA 1 ATOM 668 C CA B SER A 1 110 ? -18.651 16.650 42.441 0.50 15.52 ? 128 SER A CA 1 ATOM 669 C C . SER A 1 110 ? -17.417 15.925 42.962 1.00 14.91 ? 128 SER A C 1 ATOM 670 O O . SER A 1 110 ? -17.292 15.724 44.171 1.00 15.16 ? 128 SER A O 1 ATOM 671 C CB A SER A 1 110 ? -19.904 15.791 42.694 0.50 15.93 ? 128 SER A CB 1 ATOM 672 C CB B SER A 1 110 ? -19.899 15.805 42.728 0.50 16.37 ? 128 SER A CB 1 ATOM 673 O OG A SER A 1 110 ? -21.059 16.466 42.226 0.50 15.58 ? 128 SER A OG 1 ATOM 674 O OG B SER A 1 110 ? -19.827 14.562 42.062 0.50 17.28 ? 128 SER A OG 1 ATOM 675 N N . GLY A 1 111 ? -16.522 15.537 42.053 1.00 13.48 ? 129 GLY A N 1 ATOM 676 C CA . GLY A 1 111 ? -15.327 14.763 42.451 1.00 12.93 ? 129 GLY A CA 1 ATOM 677 C C . GLY A 1 111 ? -14.357 15.551 43.318 1.00 12.56 ? 129 GLY A C 1 ATOM 678 O O . GLY A 1 111 ? -14.054 16.714 43.034 1.00 12.77 ? 129 GLY A O 1 ATOM 679 N N . VAL A 1 112 ? -13.842 14.907 44.363 1.00 11.82 ? 130 VAL A N 1 ATOM 680 C CA . VAL A 1 112 ? -12.907 15.555 45.274 1.00 11.59 ? 130 VAL A CA 1 ATOM 681 C C . VAL A 1 112 ? -11.750 14.601 45.558 1.00 11.80 ? 130 VAL A C 1 ATOM 682 O O . VAL A 1 112 ? -11.977 13.417 45.845 1.00 12.09 ? 130 VAL A O 1 ATOM 683 C CB . VAL A 1 112 ? -13.598 15.925 46.616 1.00 11.69 ? 130 VAL A CB 1 ATOM 684 C CG1 . VAL A 1 112 ? -12.589 16.523 47.590 1.00 11.80 ? 130 VAL A CG1 1 ATOM 685 C CG2 . VAL A 1 112 ? -14.739 16.914 46.385 1.00 11.69 ? 130 VAL A CG2 1 ATOM 686 N N . ILE A 1 113 ? -10.520 15.107 45.456 1.00 11.26 ? 131 ILE A N 1 ATOM 687 C CA . ILE A 1 113 ? -9.341 14.352 45.888 1.00 11.38 ? 131 ILE A CA 1 ATOM 688 C C . ILE A 1 113 ? -8.871 15.071 47.143 1.00 11.08 ? 131 ILE A C 1 ATOM 689 O O . ILE A 1 113 ? -8.455 16.231 47.084 1.00 11.12 ? 131 ILE A O 1 ATOM 690 C CB . ILE A 1 113 ? -8.227 14.328 44.809 1.00 11.51 ? 131 ILE A CB 1 ATOM 691 C CG1 . ILE A 1 113 ? -8.763 13.728 43.501 1.00 12.11 ? 131 ILE A CG1 1 ATOM 692 C CG2 . ILE A 1 113 ? -7.003 13.552 45.313 1.00 11.25 ? 131 ILE A CG2 1 ATOM 693 C CD1 . ILE A 1 113 ? -7.838 13.920 42.301 1.00 12.52 ? 131 ILE A CD1 1 ATOM 694 N N . ASP A 1 114 ? -8.942 14.379 48.272 1.00 11.29 ? 132 ASP A N 1 ATOM 695 C CA . ASP A 1 114 ? -8.621 14.955 49.570 1.00 11.83 ? 132 ASP A CA 1 ATOM 696 C C . ASP A 1 114 ? -7.263 14.415 50.017 1.00 12.20 ? 132 ASP A C 1 ATOM 697 O O . ASP A 1 114 ? -7.166 13.245 50.394 1.00 11.93 ? 132 ASP A O 1 ATOM 698 C CB . ASP A 1 114 ? -9.726 14.568 50.579 1.00 12.60 ? 132 ASP A CB 1 ATOM 699 C CG . ASP A 1 114 ? -9.535 15.196 51.970 1.00 13.94 ? 132 ASP A CG 1 ATOM 700 O OD1 . ASP A 1 114 ? -8.503 15.838 52.239 1.00 13.66 ? 132 ASP A OD1 1 ATOM 701 O OD2 . ASP A 1 114 ? -10.453 15.042 52.819 1.00 15.48 ? 132 ASP A OD2 1 ATOM 702 N N . GLY A 1 115 ? -6.235 15.270 50.008 1.00 11.34 ? 133 GLY A N 1 ATOM 703 C CA . GLY A 1 115 ? -4.896 14.885 50.461 1.00 11.65 ? 133 GLY A CA 1 ATOM 704 C C . GLY A 1 115 ? -4.719 14.720 51.953 1.00 11.47 ? 133 GLY A C 1 ATOM 705 O O . GLY A 1 115 ? -3.685 14.206 52.393 1.00 11.94 ? 133 GLY A O 1 ATOM 706 N N . ASN A 1 116 ? -5.715 15.154 52.733 1.00 11.68 ? 134 ASN A N 1 ATOM 707 C CA . ASN A 1 116 ? -5.750 14.941 54.178 1.00 12.20 ? 134 ASN A CA 1 ATOM 708 C C . ASN A 1 116 ? -4.470 15.452 54.836 1.00 11.83 ? 134 ASN A C 1 ATOM 709 O O . ASN A 1 116 ? -3.850 14.768 55.653 1.00 11.90 ? 134 ASN A O 1 ATOM 710 C CB . ASN A 1 116 ? -5.979 13.445 54.468 1.00 12.33 ? 134 ASN A CB 1 ATOM 711 C CG . ASN A 1 116 ? -6.549 13.173 55.851 1.00 13.25 ? 134 ASN A CG 1 ATOM 712 O OD1 . ASN A 1 116 ? -6.825 14.089 56.635 1.00 13.45 ? 134 ASN A OD1 1 ATOM 713 N ND2 . ASN A 1 116 ? -6.743 11.881 56.153 1.00 13.84 ? 134 ASN A ND2 1 ATOM 714 N N . GLY A 1 117 ? -4.096 16.679 54.484 1.00 11.08 ? 135 GLY A N 1 ATOM 715 C CA . GLY A 1 117 ? -2.769 17.196 54.774 1.00 11.04 ? 135 GLY A CA 1 ATOM 716 C C . GLY A 1 117 ? -2.527 17.745 56.165 1.00 10.67 ? 135 GLY A C 1 ATOM 717 O O . GLY A 1 117 ? -1.402 18.096 56.485 1.00 11.51 ? 135 GLY A O 1 ATOM 718 N N . GLN A 1 118 ? -3.565 17.840 56.997 1.00 10.69 ? 136 GLN A N 1 ATOM 719 C CA . GLN A 1 118 ? -3.410 18.542 58.289 1.00 11.36 ? 136 GLN A CA 1 ATOM 720 C C . GLN A 1 118 ? -2.257 17.985 59.119 1.00 11.82 ? 136 GLN A C 1 ATOM 721 O O . GLN A 1 118 ? -1.439 18.747 59.644 1.00 11.69 ? 136 GLN A O 1 ATOM 722 C CB . GLN A 1 118 ? -4.700 18.471 59.127 1.00 11.60 ? 136 GLN A CB 1 ATOM 723 C CG . GLN A 1 118 ? -4.622 19.328 60.389 1.00 11.70 ? 136 GLN A CG 1 ATOM 724 C CD . GLN A 1 118 ? -4.625 20.828 60.087 1.00 11.56 ? 136 GLN A CD 1 ATOM 725 O OE1 . GLN A 1 118 ? -5.492 21.326 59.358 1.00 12.86 ? 136 GLN A OE1 1 ATOM 726 N NE2 . GLN A 1 118 ? -3.654 21.553 60.639 1.00 11.56 ? 136 GLN A NE2 1 ATOM 727 N N . ASP A 1 119 ? -2.214 16.664 59.263 1.00 12.38 ? 137 ASP A N 1 ATOM 728 C CA . ASP A 1 119 ? -1.176 16.062 60.094 1.00 13.31 ? 137 ASP A CA 1 ATOM 729 C C . ASP A 1 119 ? 0.220 16.391 59.562 1.00 12.77 ? 137 ASP A C 1 ATOM 730 O O . ASP A 1 119 ? 1.135 16.665 60.343 1.00 12.70 ? 137 ASP A O 1 ATOM 731 C CB . ASP A 1 119 ? -1.360 14.549 60.199 1.00 14.58 ? 137 ASP A CB 1 ATOM 732 C CG . ASP A 1 119 ? -2.537 14.156 61.072 1.00 17.20 ? 137 ASP A CG 1 ATOM 733 O OD1 . ASP A 1 119 ? -3.199 15.036 61.668 1.00 19.19 ? 137 ASP A OD1 1 ATOM 734 O OD2 . ASP A 1 119 ? -2.809 12.942 61.144 1.00 19.55 ? 137 ASP A OD2 1 ATOM 735 N N . ALA A 1 120 ? 0.369 16.360 58.240 1.00 11.87 ? 138 ALA A N 1 ATOM 736 C CA . ALA A 1 120 ? 1.640 16.691 57.602 1.00 11.78 ? 138 ALA A CA 1 ATOM 737 C C . ALA A 1 120 ? 2.014 18.138 57.887 1.00 11.62 ? 138 ALA A C 1 ATOM 738 O O . ALA A 1 120 ? 3.179 18.435 58.165 1.00 11.83 ? 138 ALA A O 1 ATOM 739 C CB . ALA A 1 120 ? 1.577 16.429 56.102 1.00 11.51 ? 138 ALA A CB 1 ATOM 740 N N . TRP A 1 121 ? 1.042 19.053 57.825 1.00 10.93 ? 139 TRP A N 1 ATOM 741 C CA . TRP A 1 121 ? 1.385 20.459 58.087 1.00 11.02 ? 139 TRP A CA 1 ATOM 742 C C . TRP A 1 121 ? 1.821 20.665 59.506 1.00 11.44 ? 139 TRP A C 1 ATOM 743 O O . TRP A 1 121 ? 2.728 21.439 59.777 1.00 11.76 ? 139 TRP A O 1 ATOM 744 C CB . TRP A 1 121 ? 0.223 21.397 57.786 1.00 10.39 ? 139 TRP A CB 1 ATOM 745 C CG . TRP A 1 121 ? -0.335 21.247 56.406 1.00 10.20 ? 139 TRP A CG 1 ATOM 746 C CD1 . TRP A 1 121 ? 0.343 20.879 55.239 1.00 10.18 ? 139 TRP A CD1 1 ATOM 747 C CD2 . TRP A 1 121 ? -1.724 21.469 55.996 1.00 10.21 ? 139 TRP A CD2 1 ATOM 748 N NE1 . TRP A 1 121 ? -0.529 20.847 54.169 1.00 10.06 ? 139 TRP A NE1 1 ATOM 749 C CE2 . TRP A 1 121 ? -1.779 21.204 54.563 1.00 10.16 ? 139 TRP A CE2 1 ATOM 750 C CE3 . TRP A 1 121 ? -2.900 21.838 56.669 1.00 10.09 ? 139 TRP A CE3 1 ATOM 751 C CZ2 . TRP A 1 121 ? -2.971 21.303 53.837 1.00 10.23 ? 139 TRP A CZ2 1 ATOM 752 C CZ3 . TRP A 1 121 ? -4.085 21.951 55.929 1.00 10.41 ? 139 TRP A CZ3 1 ATOM 753 C CH2 . TRP A 1 121 ? -4.122 21.694 54.548 1.00 10.11 ? 139 TRP A CH2 1 ATOM 754 N N . ASP A 1 122 ? 1.170 19.974 60.434 1.00 12.25 ? 140 ASP A N 1 ATOM 755 C CA . ASP A 1 122 ? 1.510 20.122 61.848 1.00 13.60 ? 140 ASP A CA 1 ATOM 756 C C . ASP A 1 122 ? 2.858 19.493 62.167 1.00 13.92 ? 140 ASP A C 1 ATOM 757 O O . ASP A 1 122 ? 3.648 20.063 62.928 1.00 13.98 ? 140 ASP A O 1 ATOM 758 C CB . ASP A 1 122 ? 0.406 19.523 62.724 1.00 15.06 ? 140 ASP A CB 1 ATOM 759 C CG . ASP A 1 122 ? -0.893 20.325 62.658 1.00 17.23 ? 140 ASP A CG 1 ATOM 760 O OD1 . ASP A 1 122 ? -0.872 21.560 62.541 1.00 20.15 ? 140 ASP A OD1 1 ATOM 761 O OD2 . ASP A 1 122 ? -1.950 19.706 62.771 1.00 20.40 ? 140 ASP A OD2 1 ATOM 762 N N . LEU A 1 123 ? 3.138 18.337 61.566 1.00 13.64 ? 141 LEU A N 1 ATOM 763 C CA . LEU A 1 123 ? 4.442 17.692 61.730 1.00 13.54 ? 141 LEU A CA 1 ATOM 764 C C . LEU A 1 123 ? 5.557 18.549 61.132 1.00 13.37 ? 141 LEU A C 1 ATOM 765 O O . LEU A 1 123 ? 6.570 18.796 61.776 1.00 13.09 ? 141 LEU A O 1 ATOM 766 C CB . LEU A 1 123 ? 4.446 16.297 61.108 1.00 13.57 ? 141 LEU A CB 1 ATOM 767 C CG . LEU A 1 123 ? 5.729 15.473 61.239 1.00 14.33 ? 141 LEU A CG 1 ATOM 768 C CD1 . LEU A 1 123 ? 6.194 15.386 62.690 1.00 14.92 ? 141 LEU A CD1 1 ATOM 769 C CD2 . LEU A 1 123 ? 5.479 14.076 60.681 1.00 14.34 ? 141 LEU A CD2 1 ATOM 770 N N . PHE A 1 124 ? 5.351 19.022 59.907 1.00 13.48 ? 142 PHE A N 1 ATOM 771 C CA . PHE A 1 124 ? 6.351 19.877 59.271 1.00 13.37 ? 142 PHE A CA 1 ATOM 772 C C . PHE A 1 124 ? 6.620 21.148 60.097 1.00 13.99 ? 142 PHE A C 1 ATOM 773 O O . PHE A 1 124 ? 7.745 21.625 60.154 1.00 14.17 ? 142 PHE A O 1 ATOM 774 C CB . PHE A 1 124 ? 5.891 20.261 57.875 1.00 13.79 ? 142 PHE A CB 1 ATOM 775 C CG . PHE A 1 124 ? 6.877 21.110 57.143 1.00 13.72 ? 142 PHE A CG 1 ATOM 776 C CD1 . PHE A 1 124 ? 8.049 20.543 56.662 1.00 14.59 ? 142 PHE A CD1 1 ATOM 777 C CD2 . PHE A 1 124 ? 6.656 22.476 56.966 1.00 14.27 ? 142 PHE A CD2 1 ATOM 778 C CE1 . PHE A 1 124 ? 8.978 21.314 55.984 1.00 14.96 ? 142 PHE A CE1 1 ATOM 779 C CE2 . PHE A 1 124 ? 7.588 23.253 56.296 1.00 14.70 ? 142 PHE A CE2 1 ATOM 780 C CZ . PHE A 1 124 ? 8.754 22.665 55.812 1.00 15.20 ? 142 PHE A CZ 1 ATOM 781 N N . ALA A 1 125 ? 5.575 21.697 60.715 1.00 14.29 ? 143 ALA A N 1 ATOM 782 C CA . ALA A 1 125 ? 5.708 22.912 61.530 1.00 15.29 ? 143 ALA A CA 1 ATOM 783 C C . ALA A 1 125 ? 6.675 22.708 62.699 1.00 16.53 ? 143 ALA A C 1 ATOM 784 O O . ALA A 1 125 ? 7.432 23.617 63.033 1.00 16.88 ? 143 ALA A O 1 ATOM 785 C CB . ALA A 1 125 ? 4.342 23.369 62.036 1.00 15.05 ? 143 ALA A CB 1 ATOM 786 N N . SER A 1 126 ? 6.669 21.512 63.287 1.00 16.98 ? 144 SER A N 1 ATOM 787 C CA A SER A 1 126 ? 7.560 21.197 64.417 0.50 18.48 ? 144 SER A CA 1 ATOM 788 C CA B SER A 1 126 ? 7.555 21.201 64.418 0.50 18.47 ? 144 SER A CA 1 ATOM 789 C C . SER A 1 126 ? 8.892 20.608 63.972 1.00 19.47 ? 144 SER A C 1 ATOM 790 O O . SER A 1 126 ? 9.879 20.658 64.718 1.00 20.80 ? 144 SER A O 1 ATOM 791 C CB A SER A 1 126 ? 6.888 20.222 65.385 0.50 18.81 ? 144 SER A CB 1 ATOM 792 C CB B SER A 1 126 ? 6.867 20.232 65.382 0.50 18.79 ? 144 SER A CB 1 ATOM 793 O OG A SER A 1 126 ? 5.891 20.864 66.148 0.50 19.78 ? 144 SER A OG 1 ATOM 794 O OG B SER A 1 126 ? 6.616 18.991 64.744 0.50 19.70 ? 144 SER A OG 1 ATOM 795 N N . ASP A 1 127 ? 8.919 20.039 62.769 1.00 18.78 ? 145 ASP A N 1 ATOM 796 C CA . ASP A 1 127 ? 10.100 19.331 62.266 1.00 19.56 ? 145 ASP A CA 1 ATOM 797 C C . ASP A 1 127 ? 10.270 19.587 60.766 1.00 19.51 ? 145 ASP A C 1 ATOM 798 O O . ASP A 1 127 ? 9.670 18.914 59.936 1.00 17.47 ? 145 ASP A O 1 ATOM 799 C CB . ASP A 1 127 ? 9.943 17.835 62.548 1.00 20.88 ? 145 ASP A CB 1 ATOM 800 C CG . ASP A 1 127 ? 11.130 16.997 62.055 1.00 23.21 ? 145 ASP A CG 1 ATOM 801 O OD1 . ASP A 1 127 ? 12.108 17.543 61.500 1.00 23.00 ? 145 ASP A OD1 1 ATOM 802 O OD2 . ASP A 1 127 ? 11.056 15.765 62.217 1.00 25.78 ? 145 ASP A OD2 1 ATOM 803 N N . SER A 1 128 ? 11.096 20.565 60.429 1.00 19.95 ? 146 SER A N 1 ATOM 804 C CA . SER A 1 128 ? 11.250 20.983 59.047 1.00 21.12 ? 146 SER A CA 1 ATOM 805 C C . SER A 1 128 ? 11.954 19.916 58.189 1.00 19.90 ? 146 SER A C 1 ATOM 806 O O . SER A 1 128 ? 12.021 20.063 56.983 1.00 21.54 ? 146 SER A O 1 ATOM 807 C CB . SER A 1 128 ? 12.022 22.306 58.985 1.00 23.53 ? 146 SER A CB 1 ATOM 808 O OG . SER A 1 128 ? 13.334 22.096 59.474 1.00 26.43 ? 146 SER A OG 1 ATOM 809 N N . SER A 1 129 ? 12.462 18.850 58.806 1.00 19.03 ? 147 SER A N 1 ATOM 810 C CA . SER A 1 129 ? 13.096 17.777 58.043 1.00 18.97 ? 147 SER A CA 1 ATOM 811 C C . SER A 1 129 ? 12.056 16.792 57.488 1.00 18.30 ? 147 SER A C 1 ATOM 812 O O . SER A 1 129 ? 12.401 15.904 56.702 1.00 18.54 ? 147 SER A O 1 ATOM 813 C CB . SER A 1 129 ? 14.147 17.037 58.882 1.00 20.14 ? 147 SER A CB 1 ATOM 814 O OG . SER A 1 129 ? 13.537 16.164 59.814 1.00 22.75 ? 147 SER A OG 1 ATOM 815 N N . TYR A 1 130 ? 10.798 16.927 57.915 1.00 16.84 ? 148 TYR A N 1 ATOM 816 C CA . TYR A 1 130 ? 9.754 16.038 57.411 1.00 16.06 ? 148 TYR A CA 1 ATOM 817 C C . TYR A 1 130 ? 9.511 16.319 55.917 1.00 16.04 ? 148 TYR A C 1 ATOM 818 O O . TYR A 1 130 ? 9.245 17.458 55.525 1.00 16.91 ? 148 TYR A O 1 ATOM 819 C CB . TYR A 1 130 ? 8.461 16.159 58.235 1.00 14.84 ? 148 TYR A CB 1 ATOM 820 C CG . TYR A 1 130 ? 7.407 15.188 57.764 1.00 14.69 ? 148 TYR A CG 1 ATOM 821 C CD1 . TYR A 1 130 ? 7.644 13.813 57.802 1.00 14.36 ? 148 TYR A CD1 1 ATOM 822 C CD2 . TYR A 1 130 ? 6.182 15.638 57.261 1.00 14.59 ? 148 TYR A CD2 1 ATOM 823 C CE1 . TYR A 1 130 ? 6.694 12.902 57.363 1.00 14.05 ? 148 TYR A CE1 1 ATOM 824 C CE2 . TYR A 1 130 ? 5.217 14.728 56.827 1.00 14.12 ? 148 TYR A CE2 1 ATOM 825 C CZ . TYR A 1 130 ? 5.489 13.365 56.863 1.00 14.16 ? 148 TYR A CZ 1 ATOM 826 O OH . TYR A 1 130 ? 4.554 12.440 56.407 1.00 13.55 ? 148 TYR A OH 1 ATOM 827 N N . SER A 1 131 ? 9.619 15.276 55.095 1.00 15.33 ? 149 SER A N 1 ATOM 828 C CA . SER A 1 131 ? 9.536 15.382 53.648 1.00 15.14 ? 149 SER A CA 1 ATOM 829 C C . SER A 1 131 ? 8.184 14.821 53.200 1.00 14.68 ? 149 SER A C 1 ATOM 830 O O . SER A 1 131 ? 7.835 13.682 53.529 1.00 14.76 ? 149 SER A O 1 ATOM 831 C CB . SER A 1 131 ? 10.683 14.577 53.009 1.00 16.03 ? 149 SER A CB 1 ATOM 832 O OG . SER A 1 131 ? 10.625 14.616 51.601 1.00 18.41 ? 149 SER A OG 1 ATOM 833 N N . ARG A 1 132 ? 7.428 15.656 52.486 1.00 12.99 ? 150 ARG A N 1 ATOM 834 C CA . ARG A 1 132 ? 6.034 15.346 52.115 1.00 12.61 ? 150 ARG A CA 1 ATOM 835 C C . ARG A 1 132 ? 5.865 15.104 50.615 1.00 12.05 ? 150 ARG A C 1 ATOM 836 O O . ARG A 1 132 ? 6.545 15.734 49.795 1.00 12.39 ? 150 ARG A O 1 ATOM 837 C CB . ARG A 1 132 ? 5.115 16.506 52.518 1.00 12.14 ? 150 ARG A CB 1 ATOM 838 C CG . ARG A 1 132 ? 5.113 16.806 54.008 1.00 12.38 ? 150 ARG A CG 1 ATOM 839 C CD . ARG A 1 132 ? 4.552 18.192 54.255 1.00 12.52 ? 150 ARG A CD 1 ATOM 840 N NE . ARG A 1 132 ? 5.570 19.205 53.944 1.00 12.40 ? 150 ARG A NE 1 ATOM 841 C CZ . ARG A 1 132 ? 5.315 20.489 53.723 1.00 13.08 ? 150 ARG A CZ 1 ATOM 842 N NH1 . ARG A 1 132 ? 4.064 20.939 53.721 1.00 12.63 ? 150 ARG A NH1 1 ATOM 843 N NH2 . ARG A 1 132 ? 6.324 21.332 53.495 1.00 12.78 ? 150 ARG A NH2 1 ATOM 844 N N . PRO A 1 133 ? 4.915 14.228 50.242 1.00 11.33 ? 151 PRO A N 1 ATOM 845 C CA . PRO A 1 133 ? 4.678 13.935 48.831 1.00 11.07 ? 151 PRO A CA 1 ATOM 846 C C . PRO A 1 133 ? 3.853 15.012 48.117 1.00 10.86 ? 151 PRO A C 1 ATOM 847 O O . PRO A 1 133 ? 3.105 15.743 48.761 1.00 11.32 ? 151 PRO A O 1 ATOM 848 C CB . PRO A 1 133 ? 3.853 12.642 48.883 1.00 11.04 ? 151 PRO A CB 1 ATOM 849 C CG . PRO A 1 133 ? 3.100 12.757 50.183 1.00 10.94 ? 151 PRO A CG 1 ATOM 850 C CD . PRO A 1 133 ? 4.071 13.408 51.134 1.00 11.36 ? 151 PRO A CD 1 ATOM 851 N N . THR A 1 134 ? 3.975 15.050 46.794 1.00 10.72 ? 152 THR A N 1 ATOM 852 C CA . THR A 1 134 ? 3.101 15.841 45.909 1.00 10.29 ? 152 THR A CA 1 ATOM 853 C C . THR A 1 134 ? 1.819 15.079 45.663 1.00 10.65 ? 152 THR A C 1 ATOM 854 O O . THR A 1 134 ? 1.850 13.853 45.495 1.00 10.16 ? 152 THR A O 1 ATOM 855 C CB . THR A 1 134 ? 3.845 16.068 44.588 1.00 10.77 ? 152 THR A CB 1 ATOM 856 O OG1 . THR A 1 134 ? 4.977 16.883 44.897 1.00 11.42 ? 152 THR A OG1 1 ATOM 857 C CG2 . THR A 1 134 ? 2.948 16.727 43.494 1.00 11.07 ? 152 THR A CG2 1 ATOM 858 N N . LEU A 1 135 ? 0.692 15.794 45.640 1.00 9.69 ? 153 LEU A N 1 ATOM 859 C CA . LEU A 1 135 ? -0.609 15.129 45.515 1.00 9.96 ? 153 LEU A CA 1 ATOM 860 C C . LEU A 1 135 ? -0.802 14.478 44.134 1.00 10.15 ? 153 LEU A C 1 ATOM 861 O O . LEU A 1 135 ? -1.160 13.286 44.065 1.00 10.59 ? 153 LEU A O 1 ATOM 862 C CB . LEU A 1 135 ? -1.745 16.130 45.815 1.00 9.98 ? 153 LEU A CB 1 ATOM 863 C CG . LEU A 1 135 ? -3.150 15.584 45.598 1.00 10.21 ? 153 LEU A CG 1 ATOM 864 C CD1 . LEU A 1 135 ? -3.439 14.491 46.626 1.00 10.81 ? 153 LEU A CD1 1 ATOM 865 C CD2 . LEU A 1 135 ? -4.140 16.731 45.736 1.00 10.38 ? 153 LEU A CD2 1 ATOM 866 N N . LEU A 1 136 ? -0.594 15.244 43.049 1.00 9.55 ? 154 LEU A N 1 ATOM 867 C CA . LEU A 1 136 ? -0.700 14.718 41.680 1.00 10.33 ? 154 LEU A CA 1 ATOM 868 C C . LEU A 1 136 ? 0.631 14.988 40.985 1.00 10.49 ? 154 LEU A C 1 ATOM 869 O O . LEU A 1 136 ? 0.983 16.146 40.692 1.00 10.27 ? 154 LEU A O 1 ATOM 870 C CB . LEU A 1 136 ? -1.848 15.396 40.915 1.00 10.49 ? 154 LEU A CB 1 ATOM 871 C CG . LEU A 1 136 ? -2.056 14.914 39.471 1.00 10.82 ? 154 LEU A CG 1 ATOM 872 C CD1 . LEU A 1 136 ? -2.265 13.395 39.403 1.00 11.52 ? 154 LEU A CD1 1 ATOM 873 C CD2 . LEU A 1 136 ? -3.261 15.632 38.889 1.00 10.97 ? 154 LEU A CD2 1 ATOM 874 N N . TYR A 1 137 ? 1.374 13.920 40.749 1.00 10.76 ? 155 TYR A N 1 ATOM 875 C CA . TYR A 1 137 ? 2.750 14.030 40.303 1.00 11.36 ? 155 TYR A CA 1 ATOM 876 C C . TYR A 1 137 ? 2.851 13.407 38.920 1.00 11.33 ? 155 TYR A C 1 ATOM 877 O O . TYR A 1 137 ? 2.719 12.179 38.751 1.00 11.10 ? 155 TYR A O 1 ATOM 878 C CB . TYR A 1 137 ? 3.647 13.290 41.301 1.00 12.19 ? 155 TYR A CB 1 ATOM 879 C CG . TYR A 1 137 ? 5.120 13.383 41.022 1.00 12.69 ? 155 TYR A CG 1 ATOM 880 C CD1 . TYR A 1 137 ? 5.885 14.423 41.567 1.00 13.59 ? 155 TYR A CD1 1 ATOM 881 C CD2 . TYR A 1 137 ? 5.768 12.405 40.262 1.00 13.76 ? 155 TYR A CD2 1 ATOM 882 C CE1 . TYR A 1 137 ? 7.249 14.512 41.325 1.00 15.15 ? 155 TYR A CE1 1 ATOM 883 C CE2 . TYR A 1 137 ? 7.140 12.482 40.019 1.00 14.84 ? 155 TYR A CE2 1 ATOM 884 C CZ . TYR A 1 137 ? 7.865 13.536 40.559 1.00 15.04 ? 155 TYR A CZ 1 ATOM 885 O OH . TYR A 1 137 ? 9.218 13.634 40.349 1.00 16.83 ? 155 TYR A OH 1 ATOM 886 N N . ILE A 1 138 ? 3.049 14.262 37.922 1.00 11.24 ? 156 ILE A N 1 ATOM 887 C CA . ILE A 1 138 ? 3.096 13.827 36.527 1.00 11.85 ? 156 ILE A CA 1 ATOM 888 C C . ILE A 1 138 ? 4.550 13.913 36.068 1.00 12.33 ? 156 ILE A C 1 ATOM 889 O O . ILE A 1 138 ? 5.194 14.966 36.190 1.00 12.25 ? 156 ILE A O 1 ATOM 890 C CB . ILE A 1 138 ? 2.199 14.740 35.650 1.00 12.24 ? 156 ILE A CB 1 ATOM 891 C CG1 . ILE A 1 138 ? 0.733 14.495 35.952 1.00 12.45 ? 156 ILE A CG1 1 ATOM 892 C CG2 . ILE A 1 138 ? 2.464 14.523 34.153 1.00 13.27 ? 156 ILE A CG2 1 ATOM 893 C CD1 . ILE A 1 138 ? -0.150 15.681 35.582 1.00 13.00 ? 156 ILE A CD1 1 ATOM 894 N N . THR A 1 139 ? 5.086 12.803 35.560 1.00 12.14 ? 157 THR A N 1 ATOM 895 C CA . THR A 1 139 ? 6.443 12.828 35.054 1.00 12.70 ? 157 THR A CA 1 ATOM 896 C C . THR A 1 139 ? 6.499 12.073 33.743 1.00 12.72 ? 157 THR A C 1 ATOM 897 O O . THR A 1 139 ? 6.051 10.928 33.667 1.00 12.56 ? 157 THR A O 1 ATOM 898 C CB . THR A 1 139 ? 7.472 12.296 36.073 1.00 13.42 ? 157 THR A CB 1 ATOM 899 O OG1 . THR A 1 139 ? 8.775 12.366 35.488 1.00 14.79 ? 157 THR A OG1 1 ATOM 900 C CG2 . THR A 1 139 ? 7.153 10.860 36.520 1.00 13.39 ? 157 THR A CG2 1 ATOM 901 N N . GLY A 1 140 ? 7.016 12.727 32.704 1.00 12.94 ? 158 GLY A N 1 ATOM 902 C CA . GLY A 1 140 ? 7.017 12.104 31.375 1.00 13.89 ? 158 GLY A CA 1 ATOM 903 C C . GLY A 1 140 ? 5.615 11.918 30.821 1.00 14.22 ? 158 GLY A C 1 ATOM 904 O O . GLY A 1 140 ? 4.647 12.492 31.319 1.00 14.41 ? 158 GLY A O 1 ATOM 905 N N . GLY A 1 141 ? 5.521 11.136 29.750 1.00 14.87 ? 159 GLY A N 1 ATOM 906 C CA . GLY A 1 141 ? 4.263 10.861 29.094 1.00 14.49 ? 159 GLY A CA 1 ATOM 907 C C . GLY A 1 141 ? 3.742 12.034 28.282 1.00 14.82 ? 159 GLY A C 1 ATOM 908 O O . GLY A 1 141 ? 4.464 13.003 28.021 1.00 14.50 ? 159 GLY A O 1 ATOM 909 N N . SER A 1 142 ? 2.481 11.938 27.893 1.00 15.15 ? 160 SER A N 1 ATOM 910 C CA . SER A 1 142 ? 1.889 12.879 26.951 1.00 15.64 ? 160 SER A CA 1 ATOM 911 C C . SER A 1 142 ? 0.373 12.827 26.970 1.00 16.46 ? 160 SER A C 1 ATOM 912 O O . SER A 1 142 ? -0.216 11.811 27.365 1.00 16.10 ? 160 SER A O 1 ATOM 913 C CB . SER A 1 142 ? 2.399 12.587 25.535 1.00 17.00 ? 160 SER A CB 1 ATOM 914 O OG . SER A 1 142 ? 2.005 11.290 25.093 1.00 18.63 ? 160 SER A OG 1 ATOM 915 N N . ASN A 1 143 ? -0.251 13.917 26.512 1.00 15.84 ? 161 ASN A N 1 ATOM 916 C CA . ASN A 1 143 ? -1.690 13.980 26.306 1.00 16.59 ? 161 ASN A CA 1 ATOM 917 C C . ASN A 1 143 ? -2.452 13.641 27.585 1.00 16.46 ? 161 ASN A C 1 ATOM 918 O O . ASN A 1 143 ? -3.171 12.646 27.654 1.00 15.64 ? 161 ASN A O 1 ATOM 919 C CB . ASN A 1 143 ? -2.106 13.054 25.143 1.00 19.08 ? 161 ASN A CB 1 ATOM 920 C CG . ASN A 1 143 ? -1.356 13.360 23.849 1.00 21.84 ? 161 ASN A CG 1 ATOM 921 O OD1 . ASN A 1 143 ? -0.925 12.450 23.127 1.00 25.28 ? 161 ASN A OD1 1 ATOM 922 N ND2 . ASN A 1 143 ? -1.186 14.635 23.557 1.00 21.64 ? 161 ASN A ND2 1 ATOM 923 N N . LEU A 1 144 ? -2.244 14.460 28.609 1.00 15.44 ? 162 LEU A N 1 ATOM 924 C CA . LEU A 1 144 ? -2.866 14.264 29.904 1.00 15.57 ? 162 LEU A CA 1 ATOM 925 C C . LEU A 1 144 ? -3.814 15.415 30.153 1.00 15.76 ? 162 LEU A C 1 ATOM 926 O O . LEU A 1 144 ? -3.454 16.573 29.948 1.00 15.36 ? 162 LEU A O 1 ATOM 927 C CB . LEU A 1 144 ? -1.806 14.225 31.004 1.00 16.15 ? 162 LEU A CB 1 ATOM 928 C CG . LEU A 1 144 ? -0.618 13.289 30.705 1.00 16.95 ? 162 LEU A CG 1 ATOM 929 C CD1 . LEU A 1 144 ? 0.543 13.539 31.644 1.00 19.71 ? 162 LEU A CD1 1 ATOM 930 C CD2 . LEU A 1 144 ? -1.048 11.836 30.766 1.00 18.88 ? 162 LEU A CD2 1 ATOM 931 N N . GLU A 1 145 ? -5.017 15.089 30.608 1.00 15.25 ? 163 GLU A N 1 ATOM 932 C CA . GLU A 1 145 ? -6.041 16.096 30.839 1.00 17.01 ? 163 GLU A CA 1 ATOM 933 C C . GLU A 1 145 ? -6.581 15.889 32.255 1.00 16.23 ? 163 GLU A C 1 ATOM 934 O O . GLU A 1 145 ? -6.975 14.774 32.617 1.00 16.12 ? 163 GLU A O 1 ATOM 935 C CB . GLU A 1 145 ? -7.138 15.941 29.770 1.00 20.08 ? 163 GLU A CB 1 ATOM 936 C CG . GLU A 1 145 ? -8.215 17.010 29.787 1.00 25.38 ? 163 GLU A CG 1 ATOM 937 C CD . GLU A 1 145 ? -9.447 16.648 30.615 1.00 29.52 ? 163 GLU A CD 1 ATOM 938 O OE1 . GLU A 1 145 ? -9.576 15.499 31.117 1.00 32.44 ? 163 GLU A OE1 1 ATOM 939 O OE2 . GLU A 1 145 ? -10.315 17.534 30.748 1.00 33.32 ? 163 GLU A OE2 1 ATOM 940 N N . ILE A 1 146 ? -6.546 16.952 33.057 1.00 14.56 ? 164 ILE A N 1 ATOM 941 C CA . ILE A 1 146 ? -6.987 16.930 34.442 1.00 14.22 ? 164 ILE A CA 1 ATOM 942 C C . ILE A 1 146 ? -8.024 18.037 34.592 1.00 14.23 ? 164 ILE A C 1 ATOM 943 O O . ILE A 1 146 ? -7.709 19.212 34.423 1.00 12.95 ? 164 ILE A O 1 ATOM 944 C CB . ILE A 1 146 ? -5.820 17.173 35.431 1.00 14.87 ? 164 ILE A CB 1 ATOM 945 C CG1 . ILE A 1 146 ? -4.659 16.199 35.157 1.00 15.95 ? 164 ILE A CG1 1 ATOM 946 C CG2 . ILE A 1 146 ? -6.287 17.024 36.880 1.00 14.70 ? 164 ILE A CG2 1 ATOM 947 C CD1 . ILE A 1 146 ? -3.702 16.702 34.094 1.00 17.30 ? 164 ILE A CD1 1 ATOM 948 N N . SER A 1 147 ? -9.260 17.680 34.938 1.00 14.17 ? 165 SER A N 1 ATOM 949 C CA . SER A 1 147 ? -10.323 18.682 34.869 1.00 14.25 ? 165 SER A CA 1 ATOM 950 C C . SER A 1 147 ? -11.529 18.431 35.753 1.00 14.00 ? 165 SER A C 1 ATOM 951 O O . SER A 1 147 ? -11.857 17.293 36.080 1.00 13.39 ? 165 SER A O 1 ATOM 952 C CB . SER A 1 147 ? -10.800 18.819 33.423 1.00 15.55 ? 165 SER A CB 1 ATOM 953 O OG . SER A 1 147 ? -11.478 17.645 32.991 1.00 16.95 ? 165 SER A OG 1 ATOM 954 N N . GLY A 1 148 ? -12.178 19.523 36.138 1.00 13.50 ? 166 GLY A N 1 ATOM 955 C CA . GLY A 1 148 ? -13.481 19.485 36.757 1.00 14.29 ? 166 GLY A CA 1 ATOM 956 C C . GLY A 1 148 ? -13.525 19.151 38.222 1.00 15.68 ? 166 GLY A C 1 ATOM 957 O O . GLY A 1 148 ? -14.599 19.148 38.823 1.00 16.63 ? 166 GLY A O 1 ATOM 958 N N . LEU A 1 149 ? -12.377 18.898 38.831 1.00 15.47 ? 167 LEU A N 1 ATOM 959 C CA . LEU A 1 149 ? -12.423 18.365 40.183 1.00 15.88 ? 167 LEU A CA 1 ATOM 960 C C . LEU A 1 149 ? -11.855 19.321 41.204 1.00 14.71 ? 167 LEU A C 1 ATOM 961 O O . LEU A 1 149 ? -11.260 20.337 40.846 1.00 14.26 ? 167 LEU A O 1 ATOM 962 C CB . LEU A 1 149 ? -11.745 16.997 40.233 1.00 17.79 ? 167 LEU A CB 1 ATOM 963 C CG . LEU A 1 149 ? -10.361 16.890 39.638 1.00 17.87 ? 167 LEU A CG 1 ATOM 964 C CD1 . LEU A 1 149 ? -9.372 17.372 40.691 1.00 18.59 ? 167 LEU A CD1 1 ATOM 965 C CD2 . LEU A 1 149 ? -10.104 15.443 39.250 1.00 18.25 ? 167 LEU A CD2 1 ATOM 966 N N . ARG A 1 150 ? -12.073 18.997 42.469 1.00 13.41 ? 168 ARG A N 1 ATOM 967 C CA . ARG A 1 150 ? -11.518 19.739 43.580 1.00 12.81 ? 168 ARG A CA 1 ATOM 968 C C . ARG A 1 150 ? -10.357 18.940 44.168 1.00 12.82 ? 168 ARG A C 1 ATOM 969 O O . ARG A 1 150 ? -10.472 17.725 44.373 1.00 12.82 ? 168 ARG A O 1 ATOM 970 C CB . ARG A 1 150 ? -12.586 19.914 44.649 1.00 13.51 ? 168 ARG A CB 1 ATOM 971 C CG . ARG A 1 150 ? -12.098 20.582 45.921 1.00 14.27 ? 168 ARG A CG 1 ATOM 972 C CD . ARG A 1 150 ? -13.232 20.794 46.916 1.00 15.24 ? 168 ARG A CD 1 ATOM 973 N NE . ARG A 1 150 ? -12.698 21.353 48.150 1.00 16.35 ? 168 ARG A NE 1 ATOM 974 C CZ . ARG A 1 150 ? -13.239 21.189 49.356 1.00 17.10 ? 168 ARG A CZ 1 ATOM 975 N NH1 . ARG A 1 150 ? -14.358 20.479 49.503 1.00 18.04 ? 168 ARG A NH1 1 ATOM 976 N NH2 . ARG A 1 150 ? -12.657 21.745 50.414 1.00 18.45 ? 168 ARG A NH2 1 ATOM 977 N N . GLN A 1 151 ? -9.260 19.642 44.451 1.00 11.83 ? 169 GLN A N 1 ATOM 978 C CA . GLN A 1 151 ? -8.166 19.075 45.226 1.00 11.55 ? 169 GLN A CA 1 ATOM 979 C C . GLN A 1 151 ? -8.161 19.788 46.559 1.00 11.46 ? 169 GLN A C 1 ATOM 980 O O . GLN A 1 151 ? -8.086 21.022 46.608 1.00 11.36 ? 169 GLN A O 1 ATOM 981 C CB . GLN A 1 151 ? -6.830 19.276 44.504 1.00 11.93 ? 169 GLN A CB 1 ATOM 982 C CG . GLN A 1 151 ? -6.723 18.485 43.204 1.00 12.40 ? 169 GLN A CG 1 ATOM 983 C CD . GLN A 1 151 ? -5.475 18.865 42.422 1.00 13.07 ? 169 GLN A CD 1 ATOM 984 O OE1 . GLN A 1 151 ? -4.992 19.986 42.528 1.00 13.66 ? 169 GLN A OE1 1 ATOM 985 N NE2 . GLN A 1 151 ? -4.958 17.944 41.635 1.00 13.78 ? 169 GLN A NE2 1 ATOM 986 N N . LYS A 1 152 ? -8.233 19.010 47.639 1.00 11.17 ? 170 LYS A N 1 ATOM 987 C CA . LYS A 1 152 ? -8.424 19.529 48.991 1.00 11.83 ? 170 LYS A CA 1 ATOM 988 C C . LYS A 1 152 ? -7.260 19.124 49.899 1.00 11.43 ? 170 LYS A C 1 ATOM 989 O O . LYS A 1 152 ? -6.903 17.947 49.952 1.00 11.38 ? 170 LYS A O 1 ATOM 990 C CB . LYS A 1 152 ? -9.724 18.929 49.555 1.00 12.19 ? 170 LYS A CB 1 ATOM 991 C CG . LYS A 1 152 ? -10.013 19.285 51.001 1.00 13.43 ? 170 LYS A CG 1 ATOM 992 C CD . LYS A 1 152 ? -11.300 18.591 51.436 1.00 14.37 ? 170 LYS A CD 1 ATOM 993 C CE . LYS A 1 152 ? -11.514 18.744 52.933 1.00 16.03 ? 170 LYS A CE 1 ATOM 994 N NZ . LYS A 1 152 ? -12.826 18.121 53.290 1.00 16.19 ? 170 LYS A NZ 1 ATOM 995 N N . ASN A 1 153 ? -6.664 20.105 50.574 1.00 10.47 ? 171 ASN A N 1 ATOM 996 C CA . ASN A 1 153 ? -5.696 19.868 51.652 1.00 10.40 ? 171 ASN A CA 1 ATOM 997 C C . ASN A 1 153 ? -4.558 18.895 51.307 1.00 10.36 ? 171 ASN A C 1 ATOM 998 O O . ASN A 1 153 ? -4.357 17.887 51.988 1.00 10.55 ? 171 ASN A O 1 ATOM 999 C CB . ASN A 1 153 ? -6.423 19.443 52.937 1.00 10.69 ? 171 ASN A CB 1 ATOM 1000 C CG . ASN A 1 153 ? -7.422 20.481 53.412 1.00 11.54 ? 171 ASN A CG 1 ATOM 1001 O OD1 . ASN A 1 153 ? -7.286 21.673 53.099 1.00 11.82 ? 171 ASN A OD1 1 ATOM 1002 N ND2 . ASN A 1 153 ? -8.432 20.043 54.192 1.00 11.47 ? 171 ASN A ND2 1 ATOM 1003 N N . PRO A 1 154 ? -3.788 19.205 50.256 1.00 10.27 ? 172 PRO A N 1 ATOM 1004 C CA . PRO A 1 154 ? -2.593 18.393 49.974 1.00 10.42 ? 172 PRO A CA 1 ATOM 1005 C C . PRO A 1 154 ? -1.571 18.581 51.092 1.00 10.60 ? 172 PRO A C 1 ATOM 1006 O O . PRO A 1 154 ? -1.472 19.669 51.659 1.00 10.58 ? 172 PRO A O 1 ATOM 1007 C CB . PRO A 1 154 ? -2.049 19.027 48.694 1.00 10.44 ? 172 PRO A CB 1 ATOM 1008 C CG . PRO A 1 154 ? -2.476 20.466 48.790 1.00 10.05 ? 172 PRO A CG 1 ATOM 1009 C CD . PRO A 1 154 ? -3.880 20.370 49.364 1.00 10.55 ? 172 PRO A CD 1 ATOM 1010 N N . PRO A 1 155 ? -0.807 17.528 51.424 1.00 10.65 ? 173 PRO A N 1 ATOM 1011 C CA . PRO A 1 155 ? 0.254 17.686 52.426 1.00 10.60 ? 173 PRO A CA 1 ATOM 1012 C C . PRO A 1 155 ? 1.293 18.732 51.990 1.00 10.33 ? 173 PRO A C 1 ATOM 1013 O O . PRO A 1 155 ? 1.900 19.397 52.829 1.00 10.35 ? 173 PRO A O 1 ATOM 1014 C CB . PRO A 1 155 ? 0.933 16.311 52.451 1.00 10.85 ? 173 PRO A CB 1 ATOM 1015 C CG . PRO A 1 155 ? -0.029 15.364 51.851 1.00 11.13 ? 173 PRO A CG 1 ATOM 1016 C CD . PRO A 1 155 ? -1.008 16.127 50.991 1.00 10.80 ? 173 PRO A CD 1 ATOM 1017 N N . ASN A 1 156 ? 1.465 18.895 50.685 1.00 10.70 ? 174 ASN A N 1 ATOM 1018 C CA . ASN A 1 156 ? 2.570 19.710 50.142 1.00 10.73 ? 174 ASN A CA 1 ATOM 1019 C C . ASN A 1 156 ? 2.070 20.190 48.766 1.00 10.50 ? 174 ASN A C 1 ATOM 1020 O O . ASN A 1 156 ? 0.965 20.714 48.665 1.00 10.19 ? 174 ASN A O 1 ATOM 1021 C CB . ASN A 1 156 ? 3.813 18.791 50.052 1.00 11.81 ? 174 ASN A CB 1 ATOM 1022 C CG . ASN A 1 156 ? 5.176 19.528 50.021 1.00 13.21 ? 174 ASN A CG 1 ATOM 1023 O OD1 . ASN A 1 156 ? 6.202 18.896 50.315 1.00 15.31 ? 174 ASN A OD1 1 ATOM 1024 N ND2 . ASN A 1 156 ? 5.216 20.778 49.601 1.00 12.81 ? 174 ASN A ND2 1 ATOM 1025 N N . VAL A 1 157 ? 2.853 20.001 47.702 1.00 9.66 ? 175 VAL A N 1 ATOM 1026 C CA . VAL A 1 157 ? 2.487 20.547 46.380 1.00 9.44 ? 175 VAL A CA 1 ATOM 1027 C C . VAL A 1 157 ? 1.218 19.864 45.860 1.00 9.21 ? 175 VAL A C 1 ATOM 1028 O O . VAL A 1 157 ? 1.050 18.650 46.031 1.00 9.42 ? 175 VAL A O 1 ATOM 1029 C CB . VAL A 1 157 ? 3.660 20.364 45.380 1.00 9.31 ? 175 VAL A CB 1 ATOM 1030 C CG1 . VAL A 1 157 ? 3.257 20.779 43.956 1.00 9.62 ? 175 VAL A CG1 1 ATOM 1031 C CG2 . VAL A 1 157 ? 4.864 21.178 45.875 1.00 9.87 ? 175 VAL A CG2 1 ATOM 1032 N N . PHE A 1 158 ? 0.316 20.636 45.239 1.00 8.90 ? 176 PHE A N 1 ATOM 1033 C CA . PHE A 1 158 ? -0.887 20.047 44.639 1.00 9.55 ? 176 PHE A CA 1 ATOM 1034 C C . PHE A 1 158 ? -0.507 19.261 43.381 1.00 9.85 ? 176 PHE A C 1 ATOM 1035 O O . PHE A 1 158 ? -0.779 18.061 43.273 1.00 10.38 ? 176 PHE A O 1 ATOM 1036 C CB . PHE A 1 158 ? -1.877 21.133 44.197 1.00 9.46 ? 176 PHE A CB 1 ATOM 1037 C CG . PHE A 1 158 ? -2.680 21.770 45.303 1.00 9.44 ? 176 PHE A CG 1 ATOM 1038 C CD1 . PHE A 1 158 ? -2.202 22.894 45.990 1.00 9.70 ? 176 PHE A CD1 1 ATOM 1039 C CD2 . PHE A 1 158 ? -3.975 21.322 45.564 1.00 9.72 ? 176 PHE A CD2 1 ATOM 1040 C CE1 . PHE A 1 158 ? -2.983 23.528 46.964 1.00 9.72 ? 176 PHE A CE1 1 ATOM 1041 C CE2 . PHE A 1 158 ? -4.771 21.947 46.525 1.00 9.57 ? 176 PHE A CE2 1 ATOM 1042 C CZ . PHE A 1 158 ? -4.278 23.043 47.237 1.00 9.78 ? 176 PHE A CZ 1 ATOM 1043 N N . ASN A 1 159 ? 0.080 19.949 42.401 1.00 9.78 ? 177 ASN A N 1 ATOM 1044 C CA . ASN A 1 159 ? 0.331 19.356 41.088 1.00 10.18 ? 177 ASN A CA 1 ATOM 1045 C C . ASN A 1 159 ? 1.737 19.676 40.649 1.00 10.50 ? 177 ASN A C 1 ATOM 1046 O O . ASN A 1 159 ? 2.195 20.816 40.782 1.00 10.12 ? 177 ASN A O 1 ATOM 1047 C CB . ASN A 1 159 ? -0.600 19.981 40.030 1.00 10.34 ? 177 ASN A CB 1 ATOM 1048 C CG . ASN A 1 159 ? -2.050 19.785 40.354 1.00 10.96 ? 177 ASN A CG 1 ATOM 1049 O OD1 . ASN A 1 159 ? -2.563 18.682 40.238 1.00 11.27 ? 177 ASN A OD1 1 ATOM 1050 N ND2 . ASN A 1 159 ? -2.715 20.849 40.799 1.00 10.85 ? 177 ASN A ND2 1 ATOM 1051 N N . SER A 1 160 ? 2.425 18.677 40.108 1.00 11.11 ? 178 SER A N 1 ATOM 1052 C CA A SER A 1 160 ? 3.754 18.868 39.551 0.50 11.68 ? 178 SER A CA 1 ATOM 1053 C CA B SER A 1 160 ? 3.708 18.952 39.491 0.50 11.26 ? 178 SER A CA 1 ATOM 1054 C C . SER A 1 160 ? 3.814 18.211 38.169 1.00 11.63 ? 178 SER A C 1 ATOM 1055 O O . SER A 1 160 ? 3.223 17.144 37.980 1.00 11.51 ? 178 SER A O 1 ATOM 1056 C CB A SER A 1 160 ? 4.787 18.236 40.483 0.50 12.50 ? 178 SER A CB 1 ATOM 1057 C CB B SER A 1 160 ? 4.871 18.617 40.426 0.50 11.53 ? 178 SER A CB 1 ATOM 1058 O OG A SER A 1 160 ? 6.091 18.375 39.963 0.50 13.69 ? 178 SER A OG 1 ATOM 1059 O OG B SER A 1 160 ? 4.953 17.231 40.654 0.50 11.09 ? 178 SER A OG 1 ATOM 1060 N N . VAL A 1 161 ? 4.534 18.826 37.233 1.00 11.21 ? 179 VAL A N 1 ATOM 1061 C CA . VAL A 1 161 ? 4.722 18.242 35.910 1.00 11.59 ? 179 VAL A CA 1 ATOM 1062 C C . VAL A 1 161 ? 6.207 18.343 35.625 1.00 12.52 ? 179 VAL A C 1 ATOM 1063 O O . VAL A 1 161 ? 6.799 19.427 35.717 1.00 12.24 ? 179 VAL A O 1 ATOM 1064 C CB . VAL A 1 161 ? 3.930 19.005 34.819 1.00 11.64 ? 179 VAL A CB 1 ATOM 1065 C CG1 . VAL A 1 161 ? 4.171 18.380 33.445 1.00 12.70 ? 179 VAL A CG1 1 ATOM 1066 C CG2 . VAL A 1 161 ? 2.436 19.008 35.136 1.00 11.73 ? 179 VAL A CG2 1 ATOM 1067 N N . LYS A 1 162 ? 6.816 17.203 35.322 1.00 12.81 ? 180 LYS A N 1 ATOM 1068 C CA . LYS A 1 162 ? 8.224 17.186 34.964 1.00 14.18 ? 180 LYS A CA 1 ATOM 1069 C C . LYS A 1 162 ? 8.531 15.989 34.070 1.00 13.59 ? 180 LYS A C 1 ATOM 1070 O O . LYS A 1 162 ? 7.621 15.418 33.468 1.00 12.62 ? 180 LYS A O 1 ATOM 1071 C CB . LYS A 1 162 ? 9.103 17.200 36.206 1.00 17.42 ? 180 LYS A CB 1 ATOM 1072 C CG . LYS A 1 162 ? 9.031 15.940 37.029 1.00 20.07 ? 180 LYS A CG 1 ATOM 1073 C CD . LYS A 1 162 ? 10.020 16.051 38.187 1.00 24.22 ? 180 LYS A CD 1 ATOM 1074 C CE . LYS A 1 162 ? 9.494 17.017 39.229 1.00 25.90 ? 180 LYS A CE 1 ATOM 1075 N NZ . LYS A 1 162 ? 10.567 17.304 40.218 1.00 31.10 ? 180 LYS A NZ 1 ATOM 1076 N N . GLY A 1 163 ? 9.810 15.653 33.953 1.00 14.31 ? 181 GLY A N 1 ATOM 1077 C CA . GLY A 1 163 ? 10.240 14.490 33.171 1.00 14.72 ? 181 GLY A CA 1 ATOM 1078 C C . GLY A 1 163 ? 9.983 14.551 31.673 1.00 15.87 ? 181 GLY A C 1 ATOM 1079 O O . GLY A 1 163 ? 9.949 13.505 31.009 1.00 16.19 ? 181 GLY A O 1 ATOM 1080 N N . GLY A 1 164 ? 9.794 15.756 31.136 1.00 15.32 ? 182 GLY A N 1 ATOM 1081 C CA . GLY A 1 164 ? 9.537 15.932 29.700 1.00 15.59 ? 182 GLY A CA 1 ATOM 1082 C C . GLY A 1 164 ? 8.119 15.613 29.266 1.00 15.27 ? 182 GLY A C 1 ATOM 1083 O O . GLY A 1 164 ? 7.870 15.374 28.074 1.00 16.43 ? 182 GLY A O 1 ATOM 1084 N N . ALA A 1 165 ? 7.170 15.629 30.211 1.00 15.16 ? 183 ALA A N 1 ATOM 1085 C CA . ALA A 1 165 ? 5.747 15.484 29.880 1.00 15.21 ? 183 ALA A CA 1 ATOM 1086 C C . ALA A 1 165 ? 5.390 16.476 28.788 1.00 15.61 ? 183 ALA A C 1 ATOM 1087 O O . ALA A 1 165 ? 5.941 17.590 28.761 1.00 16.13 ? 183 ALA A O 1 ATOM 1088 C CB . ALA A 1 165 ? 4.878 15.734 31.113 1.00 14.82 ? 183 ALA A CB 1 ATOM 1089 N N . THR A 1 166 ? 4.508 16.092 27.873 1.00 15.03 ? 184 THR A N 1 ATOM 1090 C CA . THR A 1 166 ? 4.092 17.039 26.841 1.00 16.93 ? 184 THR A CA 1 ATOM 1091 C C . THR A 1 166 ? 2.583 17.021 26.651 1.00 16.72 ? 184 THR A C 1 ATOM 1092 O O . THR A 1 166 ? 1.952 15.981 26.812 1.00 16.51 ? 184 THR A O 1 ATOM 1093 C CB . THR A 1 166 ? 4.828 16.798 25.495 1.00 18.32 ? 184 THR A CB 1 ATOM 1094 O OG1 . THR A 1 166 ? 4.479 17.840 24.571 1.00 20.99 ? 184 THR A OG1 1 ATOM 1095 C CG2 . THR A 1 166 ? 4.438 15.469 24.896 1.00 18.61 ? 184 THR A CG2 1 ATOM 1096 N N . ASN A 1 167 ? 2.001 18.174 26.330 1.00 17.11 ? 185 ASN A N 1 ATOM 1097 C CA . ASN A 1 167 ? 0.553 18.288 26.106 1.00 18.08 ? 185 ASN A CA 1 ATOM 1098 C C . ASN A 1 167 ? -0.242 17.902 27.362 1.00 17.30 ? 185 ASN A C 1 ATOM 1099 O O . ASN A 1 167 ? -0.937 16.871 27.392 1.00 16.27 ? 185 ASN A O 1 ATOM 1100 C CB . ASN A 1 167 ? 0.071 17.431 24.918 1.00 21.34 ? 185 ASN A CB 1 ATOM 1101 C CG . ASN A 1 167 ? 0.857 17.683 23.636 1.00 26.33 ? 185 ASN A CG 1 ATOM 1102 O OD1 . ASN A 1 167 ? 1.187 18.824 23.304 1.00 30.98 ? 185 ASN A OD1 1 ATOM 1103 N ND2 . ASN A 1 167 ? 1.133 16.613 22.891 1.00 29.09 ? 185 ASN A ND2 1 ATOM 1104 N N . VAL A 1 168 ? -0.108 18.719 28.399 1.00 15.69 ? 186 VAL A N 1 ATOM 1105 C CA . VAL A 1 168 ? -0.780 18.488 29.664 1.00 14.98 ? 186 VAL A CA 1 ATOM 1106 C C . VAL A 1 168 ? -1.716 19.668 29.886 1.00 15.00 ? 186 VAL A C 1 ATOM 1107 O O . VAL A 1 168 ? -1.291 20.832 29.812 1.00 14.47 ? 186 VAL A O 1 ATOM 1108 C CB . VAL A 1 168 ? 0.234 18.413 30.815 1.00 14.94 ? 186 VAL A CB 1 ATOM 1109 C CG1 . VAL A 1 168 ? -0.465 18.151 32.145 1.00 14.83 ? 186 VAL A CG1 1 ATOM 1110 C CG2 . VAL A 1 168 ? 1.260 17.319 30.518 1.00 14.81 ? 186 VAL A CG2 1 ATOM 1111 N N . VAL A 1 169 ? -2.981 19.370 30.163 1.00 14.03 ? 187 VAL A N 1 ATOM 1112 C CA . VAL A 1 169 ? -3.964 20.433 30.362 1.00 14.58 ? 187 VAL A CA 1 ATOM 1113 C C . VAL A 1 169 ? -4.689 20.273 31.690 1.00 14.38 ? 187 VAL A C 1 ATOM 1114 O O . VAL A 1 169 ? -5.256 19.211 31.955 1.00 15.20 ? 187 VAL A O 1 ATOM 1115 C CB . VAL A 1 169 ? -5.001 20.482 29.211 1.00 15.67 ? 187 VAL A CB 1 ATOM 1116 C CG1 . VAL A 1 169 ? -6.024 21.577 29.480 1.00 17.51 ? 187 VAL A CG1 1 ATOM 1117 C CG2 . VAL A 1 169 ? -4.314 20.727 27.878 1.00 16.84 ? 187 VAL A CG2 1 ATOM 1118 N N . PHE A 1 170 ? -4.664 21.328 32.508 1.00 13.18 ? 188 PHE A N 1 ATOM 1119 C CA . PHE A 1 170 ? -5.411 21.391 33.766 1.00 13.35 ? 188 PHE A CA 1 ATOM 1120 C C . PHE A 1 170 ? -6.526 22.391 33.527 1.00 14.16 ? 188 PHE A C 1 ATOM 1121 O O . PHE A 1 170 ? -6.253 23.540 33.186 1.00 13.75 ? 188 PHE A O 1 ATOM 1122 C CB . PHE A 1 170 ? -4.535 21.921 34.907 1.00 12.81 ? 188 PHE A CB 1 ATOM 1123 C CG . PHE A 1 170 ? -3.346 21.053 35.236 1.00 13.01 ? 188 PHE A CG 1 ATOM 1124 C CD1 . PHE A 1 170 ? -2.127 21.252 34.590 1.00 12.82 ? 188 PHE A CD1 1 ATOM 1125 C CD2 . PHE A 1 170 ? -3.428 20.071 36.215 1.00 13.05 ? 188 PHE A CD2 1 ATOM 1126 C CE1 . PHE A 1 170 ? -1.008 20.477 34.908 1.00 13.16 ? 188 PHE A CE1 1 ATOM 1127 C CE2 . PHE A 1 170 ? -2.319 19.277 36.534 1.00 13.14 ? 188 PHE A CE2 1 ATOM 1128 C CZ . PHE A 1 170 ? -1.105 19.485 35.876 1.00 13.18 ? 188 PHE A CZ 1 ATOM 1129 N N . SER A 1 171 ? -7.776 21.965 33.695 1.00 14.03 ? 189 SER A N 1 ATOM 1130 C CA . SER A 1 171 ? -8.908 22.867 33.426 1.00 14.57 ? 189 SER A CA 1 ATOM 1131 C C . SER A 1 171 ? -9.991 22.788 34.490 1.00 14.45 ? 189 SER A C 1 ATOM 1132 O O . SER A 1 171 ? -10.309 21.702 34.959 1.00 13.38 ? 189 SER A O 1 ATOM 1133 C CB . SER A 1 171 ? -9.523 22.505 32.058 1.00 16.31 ? 189 SER A CB 1 ATOM 1134 O OG . SER A 1 171 ? -10.621 23.337 31.796 1.00 21.58 ? 189 SER A OG 1 ATOM 1135 N N . ASN A 1 172 ? -10.584 23.932 34.846 1.00 13.70 ? 190 ASN A N 1 ATOM 1136 C CA . ASN A 1 172 ? -11.746 23.937 35.733 1.00 14.44 ? 190 ASN A CA 1 ATOM 1137 C C . ASN A 1 172 ? -11.472 23.209 37.050 1.00 14.31 ? 190 ASN A C 1 ATOM 1138 O O . ASN A 1 172 ? -12.222 22.312 37.446 1.00 14.24 ? 190 ASN A O 1 ATOM 1139 C CB . ASN A 1 172 ? -12.949 23.296 35.021 1.00 15.43 ? 190 ASN A CB 1 ATOM 1140 C CG . ASN A 1 172 ? -13.462 24.153 33.887 1.00 17.43 ? 190 ASN A CG 1 ATOM 1141 O OD1 . ASN A 1 172 ? -13.541 25.372 34.023 1.00 20.77 ? 190 ASN A OD1 1 ATOM 1142 N ND2 . ASN A 1 172 ? -13.801 23.530 32.774 1.00 17.52 ? 190 ASN A ND2 1 ATOM 1143 N N . LEU A 1 173 ? -10.371 23.564 37.701 1.00 13.67 ? 191 LEU A N 1 ATOM 1144 C CA . LEU A 1 173 ? -10.006 22.948 38.967 1.00 14.75 ? 191 LEU A CA 1 ATOM 1145 C C . LEU A 1 173 ? -10.244 23.910 40.122 1.00 15.21 ? 191 LEU A C 1 ATOM 1146 O O . LEU A 1 173 ? -10.012 25.126 40.000 1.00 15.20 ? 191 LEU A O 1 ATOM 1147 C CB . LEU A 1 173 ? -8.530 22.513 38.965 1.00 14.11 ? 191 LEU A CB 1 ATOM 1148 C CG . LEU A 1 173 ? -8.051 21.500 37.930 1.00 14.74 ? 191 LEU A CG 1 ATOM 1149 C CD1 . LEU A 1 173 ? -6.587 21.168 38.189 1.00 15.14 ? 191 LEU A CD1 1 ATOM 1150 C CD2 . LEU A 1 173 ? -8.894 20.222 37.987 1.00 14.28 ? 191 LEU A CD2 1 ATOM 1151 N N . LYS A 1 174 ? -10.723 23.361 41.235 1.00 15.25 ? 192 LYS A N 1 ATOM 1152 C CA . LYS A 1 174 ? -10.844 24.112 42.476 1.00 15.90 ? 192 LYS A CA 1 ATOM 1153 C C . LYS A 1 174 ? -9.854 23.513 43.466 1.00 15.12 ? 192 LYS A C 1 ATOM 1154 O O . LYS A 1 174 ? -9.928 22.335 43.770 1.00 14.30 ? 192 LYS A O 1 ATOM 1155 C CB . LYS A 1 174 ? -12.265 24.032 43.025 1.00 19.37 ? 192 LYS A CB 1 ATOM 1156 C CG . LYS A 1 174 ? -12.467 24.846 44.294 1.00 24.15 ? 192 LYS A CG 1 ATOM 1157 C CD . LYS A 1 174 ? -13.899 25.352 44.406 1.00 29.25 ? 192 LYS A CD 1 ATOM 1158 C CE . LYS A 1 174 ? -14.743 24.421 45.266 1.00 32.58 ? 192 LYS A CE 1 ATOM 1159 N NZ . LYS A 1 174 ? -14.409 24.602 46.706 1.00 33.40 ? 192 LYS A NZ 1 ATOM 1160 N N . MET A 1 175 ? -8.913 24.325 43.937 1.00 13.64 ? 193 MET A N 1 ATOM 1161 C CA . MET A 1 175 ? -7.832 23.804 44.765 1.00 13.75 ? 193 MET A CA 1 ATOM 1162 C C . MET A 1 175 ? -7.762 24.607 46.039 1.00 13.57 ? 193 MET A C 1 ATOM 1163 O O . MET A 1 175 ? -7.681 25.832 46.010 1.00 13.81 ? 193 MET A O 1 ATOM 1164 C CB . MET A 1 175 ? -6.511 23.886 43.997 1.00 13.58 ? 193 MET A CB 1 ATOM 1165 C CG . MET A 1 175 ? -6.549 23.038 42.735 1.00 14.24 ? 193 MET A CG 1 ATOM 1166 S SD . MET A 1 175 ? -5.412 23.629 41.474 1.00 15.13 ? 193 MET A SD 1 ATOM 1167 C CE . MET A 1 175 ? -3.899 23.628 42.424 1.00 13.05 ? 193 MET A CE 1 ATOM 1168 N N . ASP A 1 176 ? -7.835 23.923 47.177 1.00 13.36 ? 194 ASP A N 1 ATOM 1169 C CA . ASP A 1 176 ? -7.834 24.650 48.435 1.00 13.79 ? 194 ASP A CA 1 ATOM 1170 C C . ASP A 1 176 ? -7.113 23.889 49.513 1.00 13.19 ? 194 ASP A C 1 ATOM 1171 O O . ASP A 1 176 ? -7.287 22.679 49.652 1.00 13.17 ? 194 ASP A O 1 ATOM 1172 C CB . ASP A 1 176 ? -9.277 24.983 48.878 1.00 15.50 ? 194 ASP A CB 1 ATOM 1173 C CG . ASP A 1 176 ? -10.190 23.759 48.867 1.00 17.94 ? 194 ASP A CG 1 ATOM 1174 O OD1 . ASP A 1 176 ? -10.243 23.042 49.875 1.00 21.32 ? 194 ASP A OD1 1 ATOM 1175 O OD2 . ASP A 1 176 ? -10.885 23.515 47.865 1.00 21.34 ? 194 ASP A OD2 1 ATOM 1176 N N . ALA A 1 177 ? -6.293 24.614 50.260 1.00 12.37 ? 195 ALA A N 1 ATOM 1177 C CA . ALA A 1 177 ? -5.607 24.089 51.434 1.00 12.85 ? 195 ALA A CA 1 ATOM 1178 C C . ALA A 1 177 ? -5.917 25.041 52.576 1.00 13.58 ? 195 ALA A C 1 ATOM 1179 O O . ALA A 1 177 ? -5.557 26.221 52.500 1.00 13.72 ? 195 ALA A O 1 ATOM 1180 C CB . ALA A 1 177 ? -4.104 24.029 51.177 1.00 12.94 ? 195 ALA A CB 1 ATOM 1181 N N . ASN A 1 178 ? -6.610 24.537 53.606 1.00 13.60 ? 196 ASN A N 1 ATOM 1182 C CA . ASN A 1 178 ? -6.970 25.322 54.787 1.00 14.78 ? 196 ASN A CA 1 ATOM 1183 C C . ASN A 1 178 ? -6.668 24.539 56.045 1.00 14.53 ? 196 ASN A C 1 ATOM 1184 O O . ASN A 1 178 ? -7.164 23.430 56.207 1.00 14.71 ? 196 ASN A O 1 ATOM 1185 C CB . ASN A 1 178 ? -8.459 25.671 54.761 1.00 16.45 ? 196 ASN A CB 1 ATOM 1186 C CG . ASN A 1 178 ? -8.795 26.652 53.654 1.00 17.63 ? 196 ASN A CG 1 ATOM 1187 O OD1 . ASN A 1 178 ? -9.258 26.245 52.586 1.00 20.61 ? 196 ASN A OD1 1 ATOM 1188 N ND2 . ASN A 1 178 ? -8.511 27.932 53.876 1.00 17.40 ? 196 ASN A ND2 1 ATOM 1189 N N . SER A 1 179 ? -5.837 25.114 56.904 1.00 14.65 ? 197 SER A N 1 ATOM 1190 C CA . SER A 1 179 ? -5.468 24.481 58.162 1.00 14.63 ? 197 SER A CA 1 ATOM 1191 C C . SER A 1 179 ? -6.531 24.716 59.225 1.00 15.85 ? 197 SER A C 1 ATOM 1192 O O . SER A 1 179 ? -7.076 25.802 59.333 1.00 16.37 ? 197 SER A O 1 ATOM 1193 C CB . SER A 1 179 ? -4.156 25.061 58.674 1.00 13.74 ? 197 SER A CB 1 ATOM 1194 O OG . SER A 1 179 ? -3.825 24.451 59.915 1.00 13.79 ? 197 SER A OG 1 ATOM 1195 N N . LYS A 1 180 ? -6.806 23.679 60.003 1.00 16.61 ? 198 LYS A N 1 ATOM 1196 C CA . LYS A 1 180 ? -7.706 23.764 61.150 1.00 17.81 ? 198 LYS A CA 1 ATOM 1197 C C . LYS A 1 180 ? -6.992 24.253 62.415 1.00 18.16 ? 198 LYS A C 1 ATOM 1198 O O . LYS A 1 180 ? -7.615 24.406 63.476 1.00 18.48 ? 198 LYS A O 1 ATOM 1199 C CB . LYS A 1 180 ? -8.328 22.389 61.380 1.00 20.46 ? 198 LYS A CB 1 ATOM 1200 C CG . LYS A 1 180 ? -9.359 22.035 60.322 1.00 23.87 ? 198 LYS A CG 1 ATOM 1201 C CD . LYS A 1 180 ? -10.054 20.714 60.623 1.00 28.70 ? 198 LYS A CD 1 ATOM 1202 C CE . LYS A 1 180 ? -9.550 19.584 59.740 1.00 31.50 ? 198 LYS A CE 1 ATOM 1203 N NZ . LYS A 1 180 ? -9.812 19.804 58.279 1.00 35.26 ? 198 LYS A NZ 1 ATOM 1204 N N . SER A 1 181 ? -5.689 24.498 62.309 1.00 17.40 ? 199 SER A N 1 ATOM 1205 C CA . SER A 1 181 ? -4.908 24.965 63.457 1.00 18.07 ? 199 SER A CA 1 ATOM 1206 C C . SER A 1 181 ? -4.198 26.263 63.106 1.00 18.17 ? 199 SER A C 1 ATOM 1207 O O . SER A 1 181 ? -4.513 26.887 62.095 1.00 19.01 ? 199 SER A O 1 ATOM 1208 C CB . SER A 1 181 ? -3.893 23.904 63.886 1.00 17.11 ? 199 SER A CB 1 ATOM 1209 O OG . SER A 1 181 ? -2.843 23.772 62.959 1.00 18.50 ? 199 SER A OG 1 ATOM 1210 N N . ASP A 1 182 ? -3.226 26.635 63.930 1.00 18.82 ? 200 ASP A N 1 ATOM 1211 C CA . ASP A 1 182 ? -2.437 27.839 63.709 1.00 20.86 ? 200 ASP A CA 1 ATOM 1212 C C . ASP A 1 182 ? -1.261 27.573 62.788 1.00 19.56 ? 200 ASP A C 1 ATOM 1213 O O . ASP A 1 182 ? -0.573 28.506 62.389 1.00 20.01 ? 200 ASP A O 1 ATOM 1214 C CB . ASP A 1 182 ? -1.911 28.373 65.037 1.00 25.09 ? 200 ASP A CB 1 ATOM 1215 C CG . ASP A 1 182 ? -3.026 28.771 65.983 1.00 30.63 ? 200 ASP A CG 1 ATOM 1216 O OD1 . ASP A 1 182 ? -3.726 29.756 65.658 1.00 33.66 ? 200 ASP A OD1 1 ATOM 1217 O OD2 . ASP A 1 182 ? -3.199 28.099 67.036 1.00 35.55 ? 200 ASP A OD2 1 ATOM 1218 N N . ASN A 1 183 ? -1.012 26.303 62.480 1.00 17.87 ? 201 ASN A N 1 ATOM 1219 C CA . ASN A 1 183 ? 0.064 25.959 61.549 1.00 18.12 ? 201 ASN A CA 1 ATOM 1220 C C . ASN A 1 183 ? -0.441 26.076 60.124 1.00 17.10 ? 201 ASN A C 1 ATOM 1221 O O . ASN A 1 183 ? -1.415 25.427 59.770 1.00 16.75 ? 201 ASN A O 1 ATOM 1222 C CB . ASN A 1 183 ? 0.568 24.544 61.804 1.00 18.57 ? 201 ASN A CB 1 ATOM 1223 C CG . ASN A 1 183 ? 1.269 24.417 63.140 1.00 19.63 ? 201 ASN A CG 1 ATOM 1224 O OD1 . ASN A 1 183 ? 2.029 25.299 63.532 1.00 21.55 ? 201 ASN A OD1 1 ATOM 1225 N ND2 . ASN A 1 183 ? 1.047 23.311 63.813 1.00 21.62 ? 201 ASN A ND2 1 ATOM 1226 N N . PRO A 1 184 ? 0.227 26.905 59.298 1.00 17.22 ? 202 PRO A N 1 ATOM 1227 C CA . PRO A 1 184 ? -0.252 27.087 57.926 1.00 16.75 ? 202 PRO A CA 1 ATOM 1228 C C . PRO A 1 184 ? 0.053 25.889 57.022 1.00 15.89 ? 202 PRO A C 1 ATOM 1229 O O . PRO A 1 184 ? 0.920 25.050 57.353 1.00 15.56 ? 202 PRO A O 1 ATOM 1230 C CB . PRO A 1 184 ? 0.501 28.335 57.435 1.00 17.22 ? 202 PRO A CB 1 ATOM 1231 C CG . PRO A 1 184 ? 1.656 28.497 58.353 1.00 18.84 ? 202 PRO A CG 1 ATOM 1232 C CD . PRO A 1 184 ? 1.448 27.680 59.594 1.00 17.84 ? 202 PRO A CD 1 ATOM 1233 N N . PRO A 1 185 ? -0.672 25.785 55.897 1.00 15.30 ? 203 PRO A N 1 ATOM 1234 C CA . PRO A 1 185 ? -0.409 24.717 54.924 1.00 14.75 ? 203 PRO A CA 1 ATOM 1235 C C . PRO A 1 185 ? 0.822 25.080 54.077 1.00 14.51 ? 203 PRO A C 1 ATOM 1236 O O . PRO A 1 185 ? 0.698 25.489 52.923 1.00 13.79 ? 203 PRO A O 1 ATOM 1237 C CB . PRO A 1 185 ? -1.681 24.688 54.082 1.00 14.42 ? 203 PRO A CB 1 ATOM 1238 C CG . PRO A 1 185 ? -2.284 26.054 54.214 1.00 14.86 ? 203 PRO A CG 1 ATOM 1239 C CD . PRO A 1 185 ? -1.854 26.595 55.547 1.00 15.07 ? 203 PRO A CD 1 ATOM 1240 N N . LYS A 1 186 ? 2.004 24.929 54.668 1.00 14.61 ? 204 LYS A N 1 ATOM 1241 C CA . LYS A 1 186 ? 3.256 25.358 54.030 1.00 14.76 ? 204 LYS A CA 1 ATOM 1242 C C . LYS A 1 186 ? 3.529 24.620 52.717 1.00 14.34 ? 204 LYS A C 1 ATOM 1243 O O . LYS A 1 186 ? 3.267 23.429 52.614 1.00 13.45 ? 204 LYS A O 1 ATOM 1244 C CB . LYS A 1 186 ? 4.437 25.091 54.962 1.00 16.65 ? 204 LYS A CB 1 ATOM 1245 C CG . LYS A 1 186 ? 4.496 25.973 56.190 1.00 19.67 ? 204 LYS A CG 1 ATOM 1246 C CD . LYS A 1 186 ? 4.868 27.396 55.847 1.00 20.73 ? 204 LYS A CD 1 ATOM 1247 C CE . LYS A 1 186 ? 5.224 28.166 57.114 1.00 24.26 ? 204 LYS A CE 1 ATOM 1248 N NZ . LYS A 1 186 ? 5.564 29.585 56.788 1.00 26.47 ? 204 LYS A NZ 1 ATOM 1249 N N . ASN A 1 187 ? 4.072 25.340 51.735 1.00 12.94 ? 205 ASN A N 1 ATOM 1250 C CA . ASN A 1 187 ? 4.570 24.732 50.495 1.00 12.84 ? 205 ASN A CA 1 ATOM 1251 C C . ASN A 1 187 ? 3.484 24.023 49.699 1.00 12.36 ? 205 ASN A C 1 ATOM 1252 O O . ASN A 1 187 ? 3.763 23.042 49.015 1.00 12.56 ? 205 ASN A O 1 ATOM 1253 C CB . ASN A 1 187 ? 5.721 23.764 50.808 1.00 13.63 ? 205 ASN A CB 1 ATOM 1254 C CG . ASN A 1 187 ? 6.805 24.413 51.653 1.00 14.28 ? 205 ASN A CG 1 ATOM 1255 O OD1 . ASN A 1 187 ? 6.963 24.088 52.831 1.00 15.17 ? 205 ASN A OD1 1 ATOM 1256 N ND2 . ASN A 1 187 ? 7.552 25.353 51.051 1.00 15.54 ? 205 ASN A ND2 1 ATOM 1257 N N . THR A 1 188 ? 2.252 24.522 49.802 1.00 11.73 ? 206 THR A N 1 ATOM 1258 C CA . THR A 1 188 ? 1.146 23.957 49.042 1.00 11.66 ? 206 THR A CA 1 ATOM 1259 C C . THR A 1 188 ? 1.053 24.597 47.655 1.00 11.72 ? 206 THR A C 1 ATOM 1260 O O . THR A 1 188 ? -0.001 25.110 47.269 1.00 11.51 ? 206 THR A O 1 ATOM 1261 C CB . THR A 1 188 ? -0.182 24.045 49.816 1.00 11.81 ? 206 THR A CB 1 ATOM 1262 O OG1 . THR A 1 188 ? -0.329 25.356 50.389 1.00 11.80 ? 206 THR A OG1 1 ATOM 1263 C CG2 . THR A 1 188 ? -0.183 22.977 50.937 1.00 11.58 ? 206 THR A CG2 1 ATOM 1264 N N . ASP A 1 189 ? 2.168 24.569 46.900 1.00 11.57 ? 207 ASP A N 1 ATOM 1265 C CA . ASP A 1 189 ? 2.192 25.168 45.550 1.00 12.71 ? 207 ASP A CA 1 ATOM 1266 C C . ASP A 1 189 ? 1.049 24.606 44.705 1.00 11.51 ? 207 ASP A C 1 ATOM 1267 O O . ASP A 1 189 ? 0.808 23.394 44.712 1.00 11.52 ? 207 ASP A O 1 ATOM 1268 C CB . ASP A 1 189 ? 3.477 24.796 44.799 1.00 14.05 ? 207 ASP A CB 1 ATOM 1269 C CG . ASP A 1 189 ? 4.746 25.233 45.493 1.00 16.18 ? 207 ASP A CG 1 ATOM 1270 O OD1 . ASP A 1 189 ? 4.735 25.536 46.701 1.00 16.88 ? 207 ASP A OD1 1 ATOM 1271 O OD2 . ASP A 1 189 ? 5.799 25.237 44.802 1.00 17.31 ? 207 ASP A OD2 1 ATOM 1272 N N . GLY A 1 190 ? 0.349 25.456 43.954 1.00 11.21 ? 208 GLY A N 1 ATOM 1273 C CA . GLY A 1 190 ? -0.703 24.950 43.082 1.00 10.79 ? 208 GLY A CA 1 ATOM 1274 C C . GLY A 1 190 ? -0.156 24.084 41.952 1.00 11.03 ? 208 GLY A C 1 ATOM 1275 O O . GLY A 1 190 ? -0.645 22.977 41.695 1.00 10.35 ? 208 GLY A O 1 ATOM 1276 N N . PHE A 1 191 ? 0.825 24.614 41.230 1.00 11.09 ? 209 PHE A N 1 ATOM 1277 C CA . PHE A 1 191 ? 1.377 23.921 40.064 1.00 11.24 ? 209 PHE A CA 1 ATOM 1278 C C . PHE A 1 191 ? 2.850 24.210 40.033 1.00 12.29 ? 209 PHE A C 1 ATOM 1279 O O . PHE A 1 191 ? 3.246 25.372 39.967 1.00 12.80 ? 209 PHE A O 1 ATOM 1280 C CB . PHE A 1 191 ? 0.756 24.457 38.755 1.00 11.60 ? 209 PHE A CB 1 ATOM 1281 C CG . PHE A 1 191 ? -0.729 24.363 38.720 1.00 11.35 ? 209 PHE A CG 1 ATOM 1282 C CD1 . PHE A 1 191 ? -1.513 25.358 39.296 1.00 11.05 ? 209 PHE A CD1 1 ATOM 1283 C CD2 . PHE A 1 191 ? -1.349 23.260 38.146 1.00 11.52 ? 209 PHE A CD2 1 ATOM 1284 C CE1 . PHE A 1 191 ? -2.895 25.265 39.280 1.00 11.62 ? 209 PHE A CE1 1 ATOM 1285 C CE2 . PHE A 1 191 ? -2.739 23.167 38.126 1.00 11.57 ? 209 PHE A CE2 1 ATOM 1286 C CZ . PHE A 1 191 ? -3.505 24.170 38.701 1.00 11.70 ? 209 PHE A CZ 1 ATOM 1287 N N . ASP A 1 192 ? 3.664 23.154 40.078 1.00 12.26 ? 210 ASP A N 1 ATOM 1288 C CA . ASP A 1 192 ? 5.097 23.297 39.899 1.00 12.71 ? 210 ASP A CA 1 ATOM 1289 C C . ASP A 1 192 ? 5.369 22.711 38.529 1.00 12.56 ? 210 ASP A C 1 ATOM 1290 O O . ASP A 1 192 ? 5.307 21.483 38.362 1.00 12.39 ? 210 ASP A O 1 ATOM 1291 C CB . ASP A 1 192 ? 5.859 22.488 40.952 1.00 13.71 ? 210 ASP A CB 1 ATOM 1292 C CG . ASP A 1 192 ? 6.006 23.218 42.282 1.00 14.88 ? 210 ASP A CG 1 ATOM 1293 O OD1 . ASP A 1 192 ? 5.553 24.365 42.431 1.00 14.60 ? 210 ASP A OD1 1 ATOM 1294 O OD2 . ASP A 1 192 ? 6.603 22.614 43.179 1.00 17.63 ? 210 ASP A OD2 1 ATOM 1295 N N . ILE A 1 193 ? 5.627 23.573 37.546 1.00 11.89 ? 211 ILE A N 1 ATOM 1296 C CA . ILE A 1 193 ? 5.780 23.113 36.164 1.00 12.12 ? 211 ILE A CA 1 ATOM 1297 C C . ILE A 1 193 ? 7.255 23.116 35.815 1.00 12.65 ? 211 ILE A C 1 ATOM 1298 O O . ILE A 1 193 ? 7.857 24.177 35.687 1.00 12.57 ? 211 ILE A O 1 ATOM 1299 C CB . ILE A 1 193 ? 4.960 23.991 35.176 1.00 12.01 ? 211 ILE A CB 1 ATOM 1300 C CG1 . ILE A 1 193 ? 3.483 24.077 35.631 1.00 12.15 ? 211 ILE A CG1 1 ATOM 1301 C CG2 . ILE A 1 193 ? 5.095 23.457 33.743 1.00 12.28 ? 211 ILE A CG2 1 ATOM 1302 C CD1 . ILE A 1 193 ? 2.755 22.740 35.720 1.00 11.87 ? 211 ILE A CD1 1 ATOM 1303 N N . GLY A 1 194 ? 7.835 21.919 35.720 1.00 12.29 ? 212 GLY A N 1 ATOM 1304 C CA . GLY A 1 194 ? 9.241 21.760 35.389 1.00 13.05 ? 212 GLY A CA 1 ATOM 1305 C C . GLY A 1 194 ? 9.407 21.294 33.955 1.00 13.17 ? 212 GLY A C 1 ATOM 1306 O O . GLY A 1 194 ? 8.723 21.787 33.046 1.00 13.21 ? 212 GLY A O 1 ATOM 1307 N N . GLU A 1 195 ? 10.313 20.332 33.758 1.00 13.87 ? 213 GLU A N 1 ATOM 1308 C CA . GLU A 1 195 ? 10.682 19.869 32.430 1.00 15.17 ? 213 GLU A CA 1 ATOM 1309 C C . GLU A 1 195 ? 9.466 19.340 31.692 1.00 14.92 ? 213 GLU A C 1 ATOM 1310 O O . GLU A 1 195 ? 8.945 18.255 32.010 1.00 14.91 ? 213 GLU A O 1 ATOM 1311 C CB . GLU A 1 195 ? 11.752 18.777 32.534 1.00 16.63 ? 213 GLU A CB 1 ATOM 1312 C CG . GLU A 1 195 ? 12.360 18.413 31.188 1.00 19.12 ? 213 GLU A CG 1 ATOM 1313 C CD . GLU A 1 195 ? 13.122 17.098 31.215 1.00 22.82 ? 213 GLU A CD 1 ATOM 1314 O OE1 . GLU A 1 195 ? 13.241 16.464 32.285 1.00 23.75 ? 213 GLU A OE1 1 ATOM 1315 O OE2 . GLU A 1 195 ? 13.601 16.689 30.139 1.00 26.16 ? 213 GLU A OE2 1 ATOM 1316 N N . SER A 1 196 ? 8.996 20.120 30.718 1.00 14.18 ? 214 SER A N 1 ATOM 1317 C CA . SER A 1 196 ? 7.775 19.805 30.007 1.00 14.64 ? 214 SER A CA 1 ATOM 1318 C C . SER A 1 196 ? 7.619 20.769 28.858 1.00 15.03 ? 214 SER A C 1 ATOM 1319 O O . SER A 1 196 ? 8.300 21.798 28.811 1.00 15.69 ? 214 SER A O 1 ATOM 1320 C CB . SER A 1 196 ? 6.547 19.932 30.936 1.00 14.35 ? 214 SER A CB 1 ATOM 1321 O OG . SER A 1 196 ? 6.458 21.244 31.472 1.00 15.07 ? 214 SER A OG 1 ATOM 1322 N N . THR A 1 197 ? 6.718 20.440 27.946 1.00 14.91 ? 215 THR A N 1 ATOM 1323 C CA . THR A 1 197 ? 6.316 21.356 26.880 1.00 16.15 ? 215 THR A CA 1 ATOM 1324 C C . THR A 1 197 ? 4.810 21.298 26.694 1.00 16.47 ? 215 THR A C 1 ATOM 1325 O O . THR A 1 197 ? 4.209 20.235 26.843 1.00 15.81 ? 215 THR A O 1 ATOM 1326 C CB . THR A 1 197 ? 7.000 21.010 25.538 1.00 17.57 ? 215 THR A CB 1 ATOM 1327 O OG1 . THR A 1 197 ? 6.691 19.656 25.191 1.00 18.13 ? 215 THR A OG1 1 ATOM 1328 C CG2 . THR A 1 197 ? 8.510 21.177 25.641 1.00 17.66 ? 215 THR A CG2 1 ATOM 1329 N N . TYR A 1 198 ? 4.219 22.440 26.354 1.00 15.63 ? 216 TYR A N 1 ATOM 1330 C CA . TYR A 1 198 ? 2.800 22.558 26.028 1.00 16.29 ? 216 TYR A CA 1 ATOM 1331 C C . TYR A 1 198 ? 1.927 22.148 27.209 1.00 15.83 ? 216 TYR A C 1 ATOM 1332 O O . TYR A 1 198 ? 1.070 21.256 27.115 1.00 16.26 ? 216 TYR A O 1 ATOM 1333 C CB . TYR A 1 198 ? 2.447 21.794 24.741 1.00 18.30 ? 216 TYR A CB 1 ATOM 1334 C CG . TYR A 1 198 ? 3.420 22.092 23.618 1.00 20.79 ? 216 TYR A CG 1 ATOM 1335 C CD1 . TYR A 1 198 ? 3.457 23.353 23.011 1.00 23.26 ? 216 TYR A CD1 1 ATOM 1336 C CD2 . TYR A 1 198 ? 4.306 21.118 23.174 1.00 23.27 ? 216 TYR A CD2 1 ATOM 1337 C CE1 . TYR A 1 198 ? 4.366 23.627 21.994 1.00 24.80 ? 216 TYR A CE1 1 ATOM 1338 C CE2 . TYR A 1 198 ? 5.208 21.376 22.149 1.00 26.43 ? 216 TYR A CE2 1 ATOM 1339 C CZ . TYR A 1 198 ? 5.236 22.629 21.571 1.00 26.23 ? 216 TYR A CZ 1 ATOM 1340 O OH . TYR A 1 198 ? 6.155 22.869 20.560 1.00 31.95 ? 216 TYR A OH 1 ATOM 1341 N N . VAL A 1 199 ? 2.174 22.807 28.331 1.00 14.81 ? 217 VAL A N 1 ATOM 1342 C CA . VAL A 1 199 ? 1.324 22.685 29.507 1.00 14.29 ? 217 VAL A CA 1 ATOM 1343 C C . VAL A 1 199 ? 0.375 23.880 29.510 1.00 14.19 ? 217 VAL A C 1 ATOM 1344 O O . VAL A 1 199 ? 0.800 25.024 29.301 1.00 13.85 ? 217 VAL A O 1 ATOM 1345 C CB . VAL A 1 199 ? 2.162 22.656 30.807 1.00 14.04 ? 217 VAL A CB 1 ATOM 1346 C CG1 . VAL A 1 199 ? 1.266 22.701 32.039 1.00 14.43 ? 217 VAL A CG1 1 ATOM 1347 C CG2 . VAL A 1 199 ? 3.041 21.404 30.846 1.00 14.58 ? 217 VAL A CG2 1 ATOM 1348 N N . THR A 1 200 ? -0.906 23.609 29.736 1.00 13.58 ? 218 THR A N 1 ATOM 1349 C CA . THR A 1 200 ? -1.906 24.667 29.852 1.00 14.16 ? 218 THR A CA 1 ATOM 1350 C C . THR A 1 200 ? -2.641 24.539 31.182 1.00 13.68 ? 218 THR A C 1 ATOM 1351 O O . THR A 1 200 ? -3.030 23.435 31.590 1.00 13.54 ? 218 THR A O 1 ATOM 1352 C CB . THR A 1 200 ? -2.915 24.623 28.689 1.00 15.12 ? 218 THR A CB 1 ATOM 1353 O OG1 . THR A 1 200 ? -2.223 24.838 27.451 1.00 17.58 ? 218 THR A OG1 1 ATOM 1354 C CG2 . THR A 1 200 ? -3.988 25.719 28.847 1.00 16.25 ? 218 THR A CG2 1 ATOM 1355 N N . ILE A 1 201 ? -2.818 25.672 31.846 1.00 12.60 ? 219 ILE A N 1 ATOM 1356 C CA . ILE A 1 201 ? -3.552 25.734 33.102 1.00 12.52 ? 219 ILE A CA 1 ATOM 1357 C C . ILE A 1 201 ? -4.613 26.793 32.877 1.00 13.52 ? 219 ILE A C 1 ATOM 1358 O O . ILE A 1 201 ? -4.280 27.940 32.590 1.00 12.78 ? 219 ILE A O 1 ATOM 1359 C CB . ILE A 1 201 ? -2.636 26.165 34.270 1.00 12.42 ? 219 ILE A CB 1 ATOM 1360 C CG1 . ILE A 1 201 ? -1.546 25.121 34.496 1.00 12.00 ? 219 ILE A CG1 1 ATOM 1361 C CG2 . ILE A 1 201 ? -3.452 26.359 35.555 1.00 12.25 ? 219 ILE A CG2 1 ATOM 1362 C CD1 . ILE A 1 201 ? -0.371 25.632 35.301 1.00 12.61 ? 219 ILE A CD1 1 ATOM 1363 N N . THR A 1 202 ? -5.884 26.414 32.992 1.00 13.87 ? 220 THR A N 1 ATOM 1364 C CA . THR A 1 202 ? -6.935 27.377 32.661 1.00 14.51 ? 220 THR A CA 1 ATOM 1365 C C . THR A 1 202 ? -8.168 27.199 33.513 1.00 14.62 ? 220 THR A C 1 ATOM 1366 O O . THR A 1 202 ? -8.586 26.060 33.790 1.00 13.74 ? 220 THR A O 1 ATOM 1367 C CB . THR A 1 202 ? -7.278 27.341 31.148 1.00 16.23 ? 220 THR A CB 1 ATOM 1368 O OG1 . THR A 1 202 ? -8.244 28.362 30.858 1.00 18.68 ? 220 THR A OG1 1 ATOM 1369 C CG2 . THR A 1 202 ? -7.839 25.968 30.733 1.00 17.96 ? 220 THR A CG2 1 ATOM 1370 N N . GLU A 1 203 ? -8.736 28.329 33.922 1.00 14.60 ? 221 GLU A N 1 ATOM 1371 C CA . GLU A 1 203 ? -9.964 28.374 34.731 1.00 15.95 ? 221 GLU A CA 1 ATOM 1372 C C . GLU A 1 203 ? -9.779 27.585 36.023 1.00 15.61 ? 221 GLU A C 1 ATOM 1373 O O . GLU A 1 203 ? -10.468 26.597 36.300 1.00 15.11 ? 221 GLU A O 1 ATOM 1374 C CB . GLU A 1 203 ? -11.175 27.901 33.925 1.00 17.81 ? 221 GLU A CB 1 ATOM 1375 C CG . GLU A 1 203 ? -11.432 28.785 32.705 1.00 20.41 ? 221 GLU A CG 1 ATOM 1376 C CD . GLU A 1 203 ? -11.956 30.179 33.038 1.00 23.66 ? 221 GLU A CD 1 ATOM 1377 O OE1 . GLU A 1 203 ? -12.510 30.389 34.139 1.00 26.22 ? 221 GLU A OE1 1 ATOM 1378 O OE2 . GLU A 1 203 ? -11.832 31.084 32.162 1.00 26.94 ? 221 GLU A OE2 1 ATOM 1379 N N . VAL A 1 204 ? -8.792 28.009 36.794 1.00 14.94 ? 222 VAL A N 1 ATOM 1380 C CA . VAL A 1 204 ? -8.510 27.355 38.072 1.00 14.59 ? 222 VAL A CA 1 ATOM 1381 C C . VAL A 1 204 ? -8.577 28.365 39.212 1.00 14.46 ? 222 VAL A C 1 ATOM 1382 O O . VAL A 1 204 ? -8.312 29.563 39.015 1.00 14.13 ? 222 VAL A O 1 ATOM 1383 C CB . VAL A 1 204 ? -7.147 26.594 38.073 1.00 15.28 ? 222 VAL A CB 1 ATOM 1384 C CG1 . VAL A 1 204 ? -7.078 25.608 36.922 1.00 15.45 ? 222 VAL A CG1 1 ATOM 1385 C CG2 . VAL A 1 204 ? -5.975 27.549 38.027 1.00 17.10 ? 222 VAL A CG2 1 ATOM 1386 N N . THR A 1 205 ? -8.985 27.893 40.385 1.00 13.93 ? 223 THR A N 1 ATOM 1387 C CA A THR A 1 205 ? -9.005 28.703 41.582 0.50 14.32 ? 223 THR A CA 1 ATOM 1388 C CA B THR A 1 205 ? -8.957 28.720 41.590 0.50 13.89 ? 223 THR A CA 1 ATOM 1389 C C . THR A 1 205 ? -8.112 28.018 42.622 1.00 14.16 ? 223 THR A C 1 ATOM 1390 O O . THR A 1 205 ? -8.231 26.806 42.831 1.00 15.08 ? 223 THR A O 1 ATOM 1391 C CB A THR A 1 205 ? -10.444 28.851 42.102 0.50 15.06 ? 223 THR A CB 1 ATOM 1392 C CB B THR A 1 205 ? -10.341 29.023 42.206 0.50 13.97 ? 223 THR A CB 1 ATOM 1393 O OG1 A THR A 1 205 ? -11.295 29.324 41.041 0.50 15.17 ? 223 THR A OG1 1 ATOM 1394 O OG1 B THR A 1 205 ? -11.051 27.800 42.454 0.50 13.56 ? 223 THR A OG1 1 ATOM 1395 C CG2 A THR A 1 205 ? -10.497 29.815 43.244 0.50 15.60 ? 223 THR A CG2 1 ATOM 1396 C CG2 B THR A 1 205 ? -11.165 29.946 41.294 0.50 13.92 ? 223 THR A CG2 1 ATOM 1397 N N . VAL A 1 206 ? -7.242 28.785 43.252 1.00 12.88 ? 224 VAL A N 1 ATOM 1398 C CA . VAL A 1 206 ? -6.291 28.246 44.228 1.00 13.61 ? 224 VAL A CA 1 ATOM 1399 C C . VAL A 1 206 ? -6.380 29.047 45.515 1.00 13.31 ? 224 VAL A C 1 ATOM 1400 O O . VAL A 1 206 ? -6.315 30.287 45.505 1.00 14.25 ? 224 VAL A O 1 ATOM 1401 C CB . VAL A 1 206 ? -4.830 28.302 43.713 1.00 13.58 ? 224 VAL A CB 1 ATOM 1402 C CG1 . VAL A 1 206 ? -3.869 27.699 44.750 1.00 14.14 ? 224 VAL A CG1 1 ATOM 1403 C CG2 . VAL A 1 206 ? -4.679 27.575 42.380 1.00 13.61 ? 224 VAL A CG2 1 ATOM 1404 N N . VAL A 1 207 ? -6.534 28.341 46.630 1.00 12.79 ? 225 VAL A N 1 ATOM 1405 C CA . VAL A 1 207 ? -6.405 28.938 47.950 1.00 13.00 ? 225 VAL A CA 1 ATOM 1406 C C . VAL A 1 207 ? -5.309 28.132 48.627 1.00 12.96 ? 225 VAL A C 1 ATOM 1407 O O . VAL A 1 207 ? -5.469 26.931 48.857 1.00 12.95 ? 225 VAL A O 1 ATOM 1408 C CB . VAL A 1 207 ? -7.721 28.841 48.767 1.00 13.26 ? 225 VAL A CB 1 ATOM 1409 C CG1 . VAL A 1 207 ? -7.512 29.305 50.216 1.00 13.73 ? 225 VAL A CG1 1 ATOM 1410 C CG2 . VAL A 1 207 ? -8.841 29.605 48.081 1.00 13.69 ? 225 VAL A CG2 1 ATOM 1411 N N . ASN A 1 208 ? -4.180 28.772 48.912 1.00 12.43 ? 226 ASN A N 1 ATOM 1412 C CA . ASN A 1 208 ? -3.035 28.022 49.449 1.00 12.84 ? 226 ASN A CA 1 ATOM 1413 C C . ASN A 1 208 ? -2.079 28.922 50.223 1.00 13.42 ? 226 ASN A C 1 ATOM 1414 O O . ASN A 1 208 ? -2.458 29.997 50.662 1.00 13.71 ? 226 ASN A O 1 ATOM 1415 C CB . ASN A 1 208 ? -2.301 27.309 48.297 1.00 12.35 ? 226 ASN A CB 1 ATOM 1416 C CG . ASN A 1 208 ? -1.538 28.279 47.400 1.00 13.20 ? 226 ASN A CG 1 ATOM 1417 O OD1 . ASN A 1 208 ? -1.759 29.485 47.455 1.00 13.60 ? 226 ASN A OD1 1 ATOM 1418 N ND2 . ASN A 1 208 ? -0.646 27.753 46.573 1.00 12.44 ? 226 ASN A ND2 1 ATOM 1419 N N . ASP A 1 209 ? -0.839 28.476 50.393 1.00 13.31 ? 227 ASP A N 1 ATOM 1420 C CA . ASP A 1 209 ? 0.130 29.245 51.160 1.00 14.48 ? 227 ASP A CA 1 ATOM 1421 C C . ASP A 1 209 ? 1.507 29.220 50.517 1.00 14.28 ? 227 ASP A C 1 ATOM 1422 O O . ASP A 1 209 ? 2.516 29.397 51.193 1.00 14.86 ? 227 ASP A O 1 ATOM 1423 C CB . ASP A 1 209 ? 0.189 28.739 52.615 1.00 15.02 ? 227 ASP A CB 1 ATOM 1424 C CG . ASP A 1 209 ? 1.042 29.612 53.510 1.00 16.67 ? 227 ASP A CG 1 ATOM 1425 O OD1 . ASP A 1 209 ? 0.973 30.859 53.382 1.00 17.93 ? 227 ASP A OD1 1 ATOM 1426 O OD2 . ASP A 1 209 ? 1.817 29.046 54.324 1.00 18.27 ? 227 ASP A OD2 1 ATOM 1427 N N . ASP A 1 210 ? 1.556 29.024 49.207 1.00 13.96 ? 228 ASP A N 1 ATOM 1428 C CA . ASP A 1 210 ? 2.845 29.099 48.506 1.00 14.57 ? 228 ASP A CA 1 ATOM 1429 C C . ASP A 1 210 ? 2.584 29.475 47.064 1.00 13.58 ? 228 ASP A C 1 ATOM 1430 O O . ASP A 1 210 ? 1.522 29.990 46.766 1.00 12.94 ? 228 ASP A O 1 ATOM 1431 C CB . ASP A 1 210 ? 3.661 27.801 48.640 1.00 15.67 ? 228 ASP A CB 1 ATOM 1432 C CG . ASP A 1 210 ? 5.172 28.074 48.649 1.00 17.64 ? 228 ASP A CG 1 ATOM 1433 O OD1 . ASP A 1 210 ? 5.694 28.622 47.642 1.00 17.70 ? 228 ASP A OD1 1 ATOM 1434 O OD2 . ASP A 1 210 ? 5.840 27.782 49.673 1.00 19.04 ? 228 ASP A OD2 1 ATOM 1435 N N . ASP A 1 211 ? 3.556 29.285 46.175 1.00 13.91 ? 229 ASP A N 1 ATOM 1436 C CA . ASP A 1 211 ? 3.354 29.685 44.784 1.00 13.57 ? 229 ASP A CA 1 ATOM 1437 C C . ASP A 1 211 ? 2.045 29.169 44.207 1.00 13.41 ? 229 ASP A C 1 ATOM 1438 O O . ASP A 1 211 ? 1.690 28.006 44.390 1.00 13.49 ? 229 ASP A O 1 ATOM 1439 C CB . ASP A 1 211 ? 4.527 29.193 43.917 1.00 14.42 ? 229 ASP A CB 1 ATOM 1440 C CG . ASP A 1 211 ? 5.831 29.870 44.286 1.00 15.65 ? 229 ASP A CG 1 ATOM 1441 O OD1 . ASP A 1 211 ? 5.773 31.026 44.736 1.00 17.72 ? 229 ASP A OD1 1 ATOM 1442 O OD2 . ASP A 1 211 ? 6.910 29.267 44.124 1.00 17.32 ? 229 ASP A OD2 1 ATOM 1443 N N . CYS A 1 212 ? 1.334 30.048 43.519 1.00 13.61 ? 230 CYS A N 1 ATOM 1444 C CA . CYS A 1 212 ? 0.155 29.681 42.769 1.00 15.25 ? 230 CYS A CA 1 ATOM 1445 C C . CYS A 1 212 ? 0.587 28.778 41.598 1.00 14.29 ? 230 CYS A C 1 ATOM 1446 O O . CYS A 1 212 ? 0.169 27.620 41.491 1.00 13.22 ? 230 CYS A O 1 ATOM 1447 C CB . CYS A 1 212 ? -0.559 30.954 42.279 1.00 18.94 ? 230 CYS A CB 1 ATOM 1448 S SG . CYS A 1 212 ? -2.225 30.523 41.753 1.00 27.94 ? 230 CYS A SG 1 ATOM 1449 N N . VAL A 1 213 ? 1.456 29.314 40.747 1.00 12.85 ? 231 VAL A N 1 ATOM 1450 C CA . VAL A 1 213 ? 2.093 28.554 39.668 1.00 12.66 ? 231 VAL A CA 1 ATOM 1451 C C . VAL A 1 213 ? 3.558 28.904 39.779 1.00 12.62 ? 231 VAL A C 1 ATOM 1452 O O . VAL A 1 213 ? 3.899 30.087 39.907 1.00 12.59 ? 231 VAL A O 1 ATOM 1453 C CB . VAL A 1 213 ? 1.566 28.965 38.265 1.00 13.00 ? 231 VAL A CB 1 ATOM 1454 C CG1 . VAL A 1 213 ? 2.308 28.188 37.169 1.00 13.46 ? 231 VAL A CG1 1 ATOM 1455 C CG2 . VAL A 1 213 ? 0.056 28.733 38.152 1.00 13.77 ? 231 VAL A CG2 1 ATOM 1456 N N . ALA A 1 214 ? 4.419 27.881 39.794 1.00 12.66 ? 232 ALA A N 1 ATOM 1457 C CA . ALA A 1 214 ? 5.847 28.097 39.778 1.00 12.09 ? 232 ALA A CA 1 ATOM 1458 C C . ALA A 1 214 ? 6.401 27.468 38.521 1.00 12.27 ? 232 ALA A C 1 ATOM 1459 O O . ALA A 1 214 ? 6.117 26.295 38.222 1.00 11.81 ? 232 ALA A O 1 ATOM 1460 C CB . ALA A 1 214 ? 6.508 27.500 41.016 1.00 12.00 ? 232 ALA A CB 1 ATOM 1461 N N . PHE A 1 215 ? 7.144 28.269 37.761 1.00 11.60 ? 233 PHE A N 1 ATOM 1462 C CA . PHE A 1 215 ? 7.822 27.758 36.598 1.00 12.66 ? 233 PHE A CA 1 ATOM 1463 C C . PHE A 1 215 ? 9.223 27.363 36.993 1.00 13.18 ? 233 PHE A C 1 ATOM 1464 O O . PHE A 1 215 ? 10.065 28.196 37.373 1.00 13.20 ? 233 PHE A O 1 ATOM 1465 C CB . PHE A 1 215 ? 7.795 28.771 35.459 1.00 12.52 ? 233 PHE A CB 1 ATOM 1466 C CG . PHE A 1 215 ? 6.418 29.297 35.170 1.00 12.47 ? 233 PHE A CG 1 ATOM 1467 C CD1 . PHE A 1 215 ? 5.508 28.533 34.445 1.00 12.96 ? 233 PHE A CD1 1 ATOM 1468 C CD2 . PHE A 1 215 ? 6.023 30.532 35.666 1.00 12.78 ? 233 PHE A CD2 1 ATOM 1469 C CE1 . PHE A 1 215 ? 4.224 29.011 34.180 1.00 13.08 ? 233 PHE A CE1 1 ATOM 1470 C CE2 . PHE A 1 215 ? 4.739 31.027 35.407 1.00 12.97 ? 233 PHE A CE2 1 ATOM 1471 C CZ . PHE A 1 215 ? 3.835 30.253 34.678 1.00 12.75 ? 233 PHE A CZ 1 ATOM 1472 N N . LYS A 1 216 ? 9.447 26.063 36.920 1.00 12.79 ? 234 LYS A N 1 ATOM 1473 C CA . LYS A 1 216 ? 10.680 25.467 37.397 1.00 13.41 ? 234 LYS A CA 1 ATOM 1474 C C . LYS A 1 216 ? 11.593 25.193 36.198 1.00 13.17 ? 234 LYS A C 1 ATOM 1475 O O . LYS A 1 216 ? 11.153 25.311 35.050 1.00 12.23 ? 234 LYS A O 1 ATOM 1476 C CB . LYS A 1 216 ? 10.345 24.179 38.149 1.00 13.98 ? 234 LYS A CB 1 ATOM 1477 C CG . LYS A 1 216 ? 9.422 24.416 39.343 1.00 15.21 ? 234 LYS A CG 1 ATOM 1478 C CD . LYS A 1 216 ? 10.096 25.328 40.372 1.00 15.93 ? 234 LYS A CD 1 ATOM 1479 C CE . LYS A 1 216 ? 9.423 25.255 41.747 1.00 16.98 ? 234 LYS A CE 1 ATOM 1480 N NZ . LYS A 1 216 ? 9.966 26.320 42.641 1.00 16.31 ? 234 LYS A NZ 1 ATOM 1481 N N . PRO A 1 217 ? 12.852 24.807 36.461 1.00 13.71 ? 235 PRO A N 1 ATOM 1482 C CA . PRO A 1 217 ? 13.816 24.595 35.377 1.00 14.21 ? 235 PRO A CA 1 ATOM 1483 C C . PRO A 1 217 ? 13.303 23.670 34.286 1.00 14.54 ? 235 PRO A C 1 ATOM 1484 O O . PRO A 1 217 ? 12.665 22.643 34.571 1.00 14.90 ? 235 PRO A O 1 ATOM 1485 C CB . PRO A 1 217 ? 15.009 23.977 36.109 1.00 14.59 ? 235 PRO A CB 1 ATOM 1486 C CG . PRO A 1 217 ? 14.977 24.665 37.426 1.00 14.77 ? 235 PRO A CG 1 ATOM 1487 C CD . PRO A 1 217 ? 13.505 24.706 37.782 1.00 14.14 ? 235 PRO A CD 1 ATOM 1488 N N . SER A 1 218 ? 13.582 24.053 33.043 1.00 14.08 ? 236 SER A N 1 ATOM 1489 C CA . SER A 1 218 ? 13.183 23.340 31.820 1.00 14.54 ? 236 SER A CA 1 ATOM 1490 C C . SER A 1 218 ? 11.701 23.415 31.444 1.00 14.09 ? 236 SER A C 1 ATOM 1491 O O . SER A 1 218 ? 11.261 22.708 30.530 1.00 14.10 ? 236 SER A O 1 ATOM 1492 C CB . SER A 1 218 ? 13.716 21.894 31.780 1.00 15.85 ? 236 SER A CB 1 ATOM 1493 O OG . SER A 1 218 ? 15.111 21.907 32.026 1.00 17.21 ? 236 SER A OG 1 ATOM 1494 N N . SER A 1 219 ? 10.924 24.272 32.112 1.00 14.16 ? 237 SER A N 1 ATOM 1495 C CA . SER A 1 219 ? 9.579 24.533 31.605 1.00 13.66 ? 237 SER A CA 1 ATOM 1496 C C . SER A 1 219 ? 9.658 25.336 30.307 1.00 14.33 ? 237 SER A C 1 ATOM 1497 O O . SER A 1 219 ? 10.499 26.234 30.161 1.00 14.61 ? 237 SER A O 1 ATOM 1498 C CB . SER A 1 219 ? 8.684 25.235 32.637 1.00 13.82 ? 237 SER A CB 1 ATOM 1499 O OG . SER A 1 219 ? 9.338 26.337 33.233 1.00 13.69 ? 237 SER A OG 1 ATOM 1500 N N . ASN A 1 220 ? 8.782 24.992 29.373 1.00 14.58 ? 238 ASN A N 1 ATOM 1501 C CA . ASN A 1 220 ? 8.797 25.592 28.033 1.00 14.91 ? 238 ASN A CA 1 ATOM 1502 C C . ASN A 1 220 ? 7.407 25.485 27.446 1.00 14.82 ? 238 ASN A C 1 ATOM 1503 O O . ASN A 1 220 ? 6.767 24.428 27.516 1.00 15.16 ? 238 ASN A O 1 ATOM 1504 C CB . ASN A 1 220 ? 9.801 24.821 27.152 1.00 15.61 ? 238 ASN A CB 1 ATOM 1505 C CG . ASN A 1 220 ? 10.084 25.494 25.818 1.00 17.03 ? 238 ASN A CG 1 ATOM 1506 O OD1 . ASN A 1 220 ? 9.747 26.661 25.592 1.00 17.20 ? 238 ASN A OD1 1 ATOM 1507 N ND2 . ASN A 1 220 ? 10.723 24.737 24.911 1.00 18.19 ? 238 ASN A ND2 1 ATOM 1508 N N . TYR A 1 221 ? 6.938 26.580 26.851 1.00 14.20 ? 239 TYR A N 1 ATOM 1509 C CA . TYR A 1 221 ? 5.598 26.636 26.251 1.00 14.35 ? 239 TYR A CA 1 ATOM 1510 C C . TYR A 1 221 ? 4.518 26.294 27.280 1.00 14.12 ? 239 TYR A C 1 ATOM 1511 O O . TYR A 1 221 ? 3.823 25.270 27.169 1.00 14.55 ? 239 TYR A O 1 ATOM 1512 C CB . TYR A 1 221 ? 5.494 25.749 25.010 1.00 15.92 ? 239 TYR A CB 1 ATOM 1513 C CG . TYR A 1 221 ? 6.397 26.205 23.888 1.00 17.37 ? 239 TYR A CG 1 ATOM 1514 C CD1 . TYR A 1 221 ? 6.181 27.426 23.252 1.00 18.66 ? 239 TYR A CD1 1 ATOM 1515 C CD2 . TYR A 1 221 ? 7.461 25.413 23.461 1.00 18.91 ? 239 TYR A CD2 1 ATOM 1516 C CE1 . TYR A 1 221 ? 7.015 27.859 22.226 1.00 19.36 ? 239 TYR A CE1 1 ATOM 1517 C CE2 . TYR A 1 221 ? 8.297 25.832 22.423 1.00 20.15 ? 239 TYR A CE2 1 ATOM 1518 C CZ . TYR A 1 221 ? 8.062 27.055 21.818 1.00 20.73 ? 239 TYR A CZ 1 ATOM 1519 O OH . TYR A 1 221 ? 8.886 27.477 20.797 1.00 22.46 ? 239 TYR A OH 1 ATOM 1520 N N . VAL A 1 222 ? 4.383 27.166 28.267 1.00 13.38 ? 240 VAL A N 1 ATOM 1521 C CA . VAL A 1 222 ? 3.325 27.047 29.278 1.00 12.96 ? 240 VAL A CA 1 ATOM 1522 C C . VAL A 1 222 ? 2.380 28.221 29.109 1.00 13.33 ? 240 VAL A C 1 ATOM 1523 O O . VAL A 1 222 ? 2.820 29.377 28.987 1.00 12.88 ? 240 VAL A O 1 ATOM 1524 C CB . VAL A 1 222 ? 3.876 27.034 30.724 1.00 13.01 ? 240 VAL A CB 1 ATOM 1525 C CG1 . VAL A 1 222 ? 2.750 26.774 31.739 1.00 13.44 ? 240 VAL A CG1 1 ATOM 1526 C CG2 . VAL A 1 222 ? 4.970 25.974 30.859 1.00 13.66 ? 240 VAL A CG2 1 ATOM 1527 N N . THR A 1 223 ? 1.092 27.916 29.092 1.00 13.01 ? 241 THR A N 1 ATOM 1528 C CA . THR A 1 223 ? 0.061 28.943 29.069 1.00 13.97 ? 241 THR A CA 1 ATOM 1529 C C . THR A 1 223 ? -0.770 28.808 30.319 1.00 13.58 ? 241 THR A C 1 ATOM 1530 O O . THR A 1 223 ? -1.224 27.708 30.655 1.00 12.81 ? 241 THR A O 1 ATOM 1531 C CB . THR A 1 223 ? -0.847 28.769 27.841 1.00 15.13 ? 241 THR A CB 1 ATOM 1532 O OG1 . THR A 1 223 ? -0.066 28.949 26.657 1.00 19.09 ? 241 THR A OG1 1 ATOM 1533 C CG2 . THR A 1 223 ? -1.980 29.791 27.843 1.00 16.21 ? 241 THR A CG2 1 ATOM 1534 N N . VAL A 1 224 ? -0.967 29.927 31.008 1.00 12.98 ? 242 VAL A N 1 ATOM 1535 C CA . VAL A 1 224 ? -1.874 29.969 32.120 1.00 14.12 ? 242 VAL A CA 1 ATOM 1536 C C . VAL A 1 224 ? -2.890 31.053 31.732 1.00 14.14 ? 242 VAL A C 1 ATOM 1537 O O . VAL A 1 224 ? -2.518 32.206 31.521 1.00 14.17 ? 242 VAL A O 1 ATOM 1538 C CB . VAL A 1 224 ? -1.164 30.381 33.440 1.00 13.29 ? 242 VAL A CB 1 ATOM 1539 C CG1 . VAL A 1 224 ? -2.164 30.420 34.600 1.00 13.91 ? 242 VAL A CG1 1 ATOM 1540 C CG2 . VAL A 1 224 ? -0.006 29.436 33.775 1.00 13.52 ? 242 VAL A CG2 1 ATOM 1541 N N . ASP A 1 225 ? -4.159 30.674 31.655 1.00 14.71 ? 243 ASP A N 1 ATOM 1542 C CA . ASP A 1 225 ? -5.215 31.612 31.211 1.00 15.97 ? 243 ASP A CA 1 ATOM 1543 C C . ASP A 1 225 ? -6.401 31.558 32.164 1.00 15.63 ? 243 ASP A C 1 ATOM 1544 O O . ASP A 1 225 ? -7.131 30.573 32.162 1.00 17.01 ? 243 ASP A O 1 ATOM 1545 C CB . ASP A 1 225 ? -5.650 31.214 29.800 1.00 17.43 ? 243 ASP A CB 1 ATOM 1546 C CG . ASP A 1 225 ? -6.655 32.181 29.186 1.00 20.32 ? 243 ASP A CG 1 ATOM 1547 O OD1 . ASP A 1 225 ? -7.363 32.912 29.921 1.00 20.17 ? 243 ASP A OD1 1 ATOM 1548 O OD2 . ASP A 1 225 ? -6.725 32.203 27.937 1.00 23.89 ? 243 ASP A OD2 1 ATOM 1549 N N . THR A 1 226 ? -6.584 32.621 32.943 1.00 15.14 ? 244 THR A N 1 ATOM 1550 C CA . THR A 1 226 ? -7.688 32.772 33.905 1.00 15.08 ? 244 THR A CA 1 ATOM 1551 C C . THR A 1 226 ? -7.464 31.930 35.155 1.00 15.42 ? 244 THR A C 1 ATOM 1552 O O . THR A 1 226 ? -7.758 30.729 35.201 1.00 15.56 ? 244 THR A O 1 ATOM 1553 C CB . THR A 1 226 ? -9.082 32.510 33.289 1.00 15.94 ? 244 THR A CB 1 ATOM 1554 O OG1 . THR A 1 226 ? -9.172 33.179 32.028 1.00 16.91 ? 244 THR A OG1 1 ATOM 1555 C CG2 . THR A 1 226 ? -10.195 33.014 34.232 1.00 16.53 ? 244 THR A CG2 1 ATOM 1556 N N . ILE A 1 227 ? -6.928 32.585 36.165 1.00 14.74 ? 245 ILE A N 1 ATOM 1557 C CA . ILE A 1 227 ? -6.592 31.914 37.396 1.00 14.92 ? 245 ILE A CA 1 ATOM 1558 C C . ILE A 1 227 ? -6.837 32.876 38.538 1.00 15.43 ? 245 ILE A C 1 ATOM 1559 O O . ILE A 1 227 ? -6.605 34.094 38.415 1.00 15.60 ? 245 ILE A O 1 ATOM 1560 C CB . ILE A 1 227 ? -5.133 31.379 37.357 1.00 14.81 ? 245 ILE A CB 1 ATOM 1561 C CG1 . ILE A 1 227 ? -4.798 30.614 38.637 1.00 14.80 ? 245 ILE A CG1 1 ATOM 1562 C CG2 . ILE A 1 227 ? -4.125 32.515 37.137 1.00 14.87 ? 245 ILE A CG2 1 ATOM 1563 C CD1 . ILE A 1 227 ? -3.600 29.690 38.468 1.00 15.55 ? 245 ILE A CD1 1 ATOM 1564 N N . SER A 1 228 ? -7.365 32.340 39.632 1.00 15.46 ? 246 SER A N 1 ATOM 1565 C CA A SER A 1 228 ? -7.510 33.103 40.851 0.80 16.70 ? 246 SER A CA 1 ATOM 1566 C CA B SER A 1 228 ? -7.528 33.096 40.865 0.20 16.04 ? 246 SER A CA 1 ATOM 1567 C C . SER A 1 228 ? -6.691 32.432 41.944 1.00 16.85 ? 246 SER A C 1 ATOM 1568 O O . SER A 1 228 ? -6.773 31.216 42.124 1.00 16.40 ? 246 SER A O 1 ATOM 1569 C CB A SER A 1 228 ? -8.984 33.163 41.261 0.80 17.96 ? 246 SER A CB 1 ATOM 1570 C CB B SER A 1 228 ? -8.999 33.127 41.290 0.20 15.89 ? 246 SER A CB 1 ATOM 1571 O OG A SER A 1 228 ? -9.091 33.763 42.532 0.80 20.80 ? 246 SER A OG 1 ATOM 1572 O OG B SER A 1 228 ? -9.760 33.955 40.434 0.20 15.43 ? 246 SER A OG 1 ATOM 1573 N N . CYS A 1 229 ? -5.907 33.227 42.661 1.00 17.01 ? 247 CYS A N 1 ATOM 1574 C CA . CYS A 1 229 ? -5.026 32.717 43.723 1.00 18.13 ? 247 CYS A CA 1 ATOM 1575 C C . CYS A 1 229 ? -5.197 33.560 44.978 1.00 17.39 ? 247 CYS A C 1 ATOM 1576 O O . CYS A 1 229 ? -5.068 34.792 44.931 1.00 17.65 ? 247 CYS A O 1 ATOM 1577 C CB . CYS A 1 229 ? -3.552 32.785 43.300 1.00 21.17 ? 247 CYS A CB 1 ATOM 1578 S SG . CYS A 1 229 ? -3.208 32.295 41.586 1.00 29.12 ? 247 CYS A SG 1 ATOM 1579 N N . THR A 1 230 ? -5.450 32.901 46.104 1.00 16.08 ? 248 THR A N 1 ATOM 1580 C CA . THR A 1 230 ? -5.635 33.599 47.376 1.00 15.32 ? 248 THR A CA 1 ATOM 1581 C C . THR A 1 230 ? -4.647 33.075 48.403 1.00 15.05 ? 248 THR A C 1 ATOM 1582 O O . THR A 1 230 ? -4.599 31.876 48.652 1.00 14.61 ? 248 THR A O 1 ATOM 1583 C CB . THR A 1 230 ? -7.074 33.406 47.910 1.00 15.55 ? 248 THR A CB 1 ATOM 1584 O OG1 . THR A 1 230 ? -8.011 33.906 46.954 1.00 16.20 ? 248 THR A OG1 1 ATOM 1585 C CG2 . THR A 1 230 ? -7.267 34.142 49.207 1.00 15.34 ? 248 THR A CG2 1 ATOM 1586 N N . GLY A 1 231 ? -3.854 33.971 48.976 1.00 14.43 ? 249 GLY A N 1 ATOM 1587 C CA . GLY A 1 231 ? -2.902 33.603 50.012 1.00 14.95 ? 249 GLY A CA 1 ATOM 1588 C C . GLY A 1 231 ? -1.611 33.020 49.475 1.00 14.79 ? 249 GLY A C 1 ATOM 1589 O O . GLY A 1 231 ? -0.788 32.519 50.241 1.00 15.30 ? 249 GLY A O 1 ATOM 1590 N N . SER A 1 232 ? -1.416 33.132 48.162 1.00 15.42 ? 250 SER A N 1 ATOM 1591 C CA . SER A 1 232 ? -0.280 32.499 47.499 1.00 15.03 ? 250 SER A CA 1 ATOM 1592 C C . SER A 1 232 ? 1.011 33.334 47.549 1.00 15.57 ? 250 SER A C 1 ATOM 1593 O O . SER A 1 232 ? 1.039 34.424 48.111 1.00 15.82 ? 250 SER A O 1 ATOM 1594 C CB . SER A 1 232 ? -0.669 32.152 46.052 1.00 15.88 ? 250 SER A CB 1 ATOM 1595 O OG . SER A 1 232 ? -0.577 33.290 45.211 1.00 16.68 ? 250 SER A OG 1 ATOM 1596 N N . HIS A 1 233 ? 2.083 32.795 46.981 1.00 14.89 ? 251 HIS A N 1 ATOM 1597 C CA . HIS A 1 233 ? 3.325 33.541 46.804 1.00 16.02 ? 251 HIS A CA 1 ATOM 1598 C C . HIS A 1 233 ? 3.472 33.997 45.369 1.00 15.63 ? 251 HIS A C 1 ATOM 1599 O O . HIS A 1 233 ? 4.556 34.391 44.942 1.00 16.40 ? 251 HIS A O 1 ATOM 1600 C CB . HIS A 1 233 ? 4.500 32.682 47.229 1.00 16.17 ? 251 HIS A CB 1 ATOM 1601 C CG . HIS A 1 233 ? 4.547 32.397 48.711 1.00 17.87 ? 251 HIS A CG 1 ATOM 1602 N ND1 . HIS A 1 233 ? 5.565 31.713 49.282 1.00 18.57 ? 251 HIS A ND1 1 ATOM 1603 C CD2 . HIS A 1 233 ? 3.668 32.738 49.743 1.00 17.86 ? 251 HIS A CD2 1 ATOM 1604 C CE1 . HIS A 1 233 ? 5.349 31.617 50.609 1.00 19.44 ? 251 HIS A CE1 1 ATOM 1605 N NE2 . HIS A 1 233 ? 4.191 32.252 50.892 1.00 18.75 ? 251 HIS A NE2 1 ATOM 1606 N N . GLY A 1 234 ? 2.377 33.926 44.615 1.00 15.68 ? 252 GLY A N 1 ATOM 1607 C CA . GLY A 1 234 ? 2.292 34.493 43.263 1.00 15.32 ? 252 GLY A CA 1 ATOM 1608 C C . GLY A 1 234 ? 2.511 33.548 42.091 1.00 15.24 ? 252 GLY A C 1 ATOM 1609 O O . GLY A 1 234 ? 2.714 32.349 42.280 1.00 14.33 ? 252 GLY A O 1 ATOM 1610 N N . ILE A 1 235 ? 2.435 34.104 40.883 1.00 14.06 ? 253 ILE A N 1 ATOM 1611 C CA . ILE A 1 235 ? 2.783 33.396 39.653 1.00 14.39 ? 253 ILE A CA 1 ATOM 1612 C C . ILE A 1 235 ? 4.267 33.684 39.526 1.00 14.41 ? 253 ILE A C 1 ATOM 1613 O O . ILE A 1 235 ? 4.662 34.822 39.269 1.00 13.40 ? 253 ILE A O 1 ATOM 1614 C CB . ILE A 1 235 ? 2.014 33.981 38.443 1.00 15.13 ? 253 ILE A CB 1 ATOM 1615 C CG1 . ILE A 1 235 ? 0.497 33.885 38.630 1.00 16.77 ? 253 ILE A CG1 1 ATOM 1616 C CG2 . ILE A 1 235 ? 2.429 33.317 37.130 1.00 14.85 ? 253 ILE A CG2 1 ATOM 1617 C CD1 . ILE A 1 235 ? -0.066 32.489 38.697 1.00 16.64 ? 253 ILE A CD1 1 ATOM 1618 N N . SER A 1 236 ? 5.081 32.650 39.740 1.00 13.62 ? 254 SER A N 1 ATOM 1619 C CA . SER A 1 236 ? 6.473 32.841 40.086 1.00 14.40 ? 254 SER A CA 1 ATOM 1620 C C . SER A 1 236 ? 7.402 32.050 39.169 1.00 13.63 ? 254 SER A C 1 ATOM 1621 O O . SER A 1 236 ? 7.231 30.849 39.011 1.00 14.01 ? 254 SER A O 1 ATOM 1622 C CB . SER A 1 236 ? 6.648 32.363 41.541 1.00 15.49 ? 254 SER A CB 1 ATOM 1623 O OG . SER A 1 236 ? 7.918 32.696 42.066 1.00 19.17 ? 254 SER A OG 1 ATOM 1624 N N . VAL A 1 237 ? 8.362 32.722 38.537 1.00 12.85 ? 255 VAL A N 1 ATOM 1625 C CA . VAL A 1 237 ? 9.411 31.999 37.814 1.00 12.81 ? 255 VAL A CA 1 ATOM 1626 C C . VAL A 1 237 ? 10.496 31.659 38.829 1.00 12.71 ? 255 VAL A C 1 ATOM 1627 O O . VAL A 1 237 ? 11.081 32.544 39.468 1.00 12.75 ? 255 VAL A O 1 ATOM 1628 C CB . VAL A 1 237 ? 10.021 32.809 36.647 1.00 12.82 ? 255 VAL A CB 1 ATOM 1629 C CG1 . VAL A 1 237 ? 11.239 32.090 36.062 1.00 13.20 ? 255 VAL A CG1 1 ATOM 1630 C CG2 . VAL A 1 237 ? 8.978 33.055 35.554 1.00 13.22 ? 255 VAL A CG2 1 ATOM 1631 N N . GLY A 1 238 ? 10.783 30.375 38.964 1.00 13.22 ? 256 GLY A N 1 ATOM 1632 C CA . GLY A 1 238 ? 11.871 29.932 39.831 1.00 13.33 ? 256 GLY A CA 1 ATOM 1633 C C . GLY A 1 238 ? 11.440 29.209 41.108 1.00 15.15 ? 256 GLY A C 1 ATOM 1634 O O . GLY A 1 238 ? 10.286 28.757 41.220 1.00 15.31 ? 256 GLY A O 1 ATOM 1635 N N . SER A 1 239 ? 12.363 29.079 42.071 1.00 14.94 ? 257 SER A N 1 ATOM 1636 C CA . SER A 1 239 ? 13.729 29.614 41.926 1.00 15.15 ? 257 SER A CA 1 ATOM 1637 C C . SER A 1 239 ? 14.505 28.870 40.844 1.00 14.61 ? 257 SER A C 1 ATOM 1638 O O . SER A 1 239 ? 14.258 27.700 40.574 1.00 14.15 ? 257 SER A O 1 ATOM 1639 C CB . SER A 1 239 ? 14.506 29.507 43.234 1.00 16.57 ? 257 SER A CB 1 ATOM 1640 O OG . SER A 1 239 ? 14.610 28.156 43.636 1.00 17.52 ? 257 SER A OG 1 ATOM 1641 N N . LEU A 1 240 ? 15.452 29.572 40.241 1.00 13.94 ? 258 LEU A N 1 ATOM 1642 C CA . LEU A 1 240 ? 16.346 28.971 39.259 1.00 14.48 ? 258 LEU A CA 1 ATOM 1643 C C . LEU A 1 240 ? 17.779 29.185 39.719 1.00 14.82 ? 258 LEU A C 1 ATOM 1644 O O . LEU A 1 240 ? 18.077 30.186 40.363 1.00 14.89 ? 258 LEU A O 1 ATOM 1645 C CB . LEU A 1 240 ? 16.159 29.660 37.901 1.00 14.46 ? 258 LEU A CB 1 ATOM 1646 C CG . LEU A 1 240 ? 14.740 29.724 37.338 1.00 14.02 ? 258 LEU A CG 1 ATOM 1647 C CD1 . LEU A 1 240 ? 14.788 30.468 36.014 1.00 14.56 ? 258 LEU A CD1 1 ATOM 1648 C CD2 . LEU A 1 240 ? 14.141 28.331 37.163 1.00 13.88 ? 258 LEU A CD2 1 ATOM 1649 N N . GLY A 1 241 ? 18.643 28.233 39.387 1.00 16.16 ? 259 GLY A N 1 ATOM 1650 C CA . GLY A 1 241 ? 20.086 28.402 39.549 1.00 17.60 ? 259 GLY A CA 1 ATOM 1651 C C . GLY A 1 241 ? 20.688 27.827 40.822 1.00 18.75 ? 259 GLY A C 1 ATOM 1652 O O . GLY A 1 241 ? 21.858 28.064 41.099 1.00 18.83 ? 259 GLY A O 1 ATOM 1653 N N . LYS A 1 242 ? 19.907 27.055 41.589 1.00 19.72 ? 260 LYS A N 1 ATOM 1654 C CA . LYS A 1 242 ? 20.377 26.563 42.888 1.00 21.32 ? 260 LYS A CA 1 ATOM 1655 C C . LYS A 1 242 ? 21.674 25.767 42.755 1.00 21.54 ? 260 LYS A C 1 ATOM 1656 O O . LYS A 1 242 ? 22.619 25.996 43.517 1.00 22.14 ? 260 LYS A O 1 ATOM 1657 C CB . LYS A 1 242 ? 19.313 25.705 43.593 1.00 23.11 ? 260 LYS A CB 1 ATOM 1658 C CG . LYS A 1 242 ? 19.748 25.180 44.958 1.00 25.35 ? 260 LYS A CG 1 ATOM 1659 C CD . LYS A 1 242 ? 18.638 24.340 45.583 1.00 28.02 ? 260 LYS A CD 1 ATOM 1660 C CE . LYS A 1 242 ? 19.072 23.651 46.868 1.00 31.91 ? 260 LYS A CE 1 ATOM 1661 N NZ . LYS A 1 242 ? 19.723 24.592 47.817 1.00 34.53 ? 260 LYS A NZ 1 ATOM 1662 N N . SER A 1 243 ? 21.714 24.849 41.797 1.00 22.34 ? 261 SER A N 1 ATOM 1663 C CA . SER A 1 243 ? 22.873 23.964 41.659 1.00 24.01 ? 261 SER A CA 1 ATOM 1664 C C . SER A 1 243 ? 23.173 23.572 40.213 1.00 24.90 ? 261 SER A C 1 ATOM 1665 O O . SER A 1 243 ? 24.004 22.691 39.962 1.00 26.00 ? 261 SER A O 1 ATOM 1666 C CB . SER A 1 243 ? 22.688 22.720 42.528 1.00 25.69 ? 261 SER A CB 1 ATOM 1667 O OG . SER A 1 243 ? 21.579 21.975 42.078 1.00 29.62 ? 261 SER A OG 1 ATOM 1668 N N . SER A 1 244 ? 22.504 24.227 39.265 1.00 23.71 ? 262 SER A N 1 ATOM 1669 C CA . SER A 1 244 ? 22.709 23.959 37.844 1.00 23.82 ? 262 SER A CA 1 ATOM 1670 C C . SER A 1 244 ? 22.299 25.168 37.012 1.00 22.67 ? 262 SER A C 1 ATOM 1671 O O . SER A 1 244 ? 21.709 26.124 37.531 1.00 20.98 ? 262 SER A O 1 ATOM 1672 C CB . SER A 1 244 ? 21.924 22.717 37.404 1.00 26.26 ? 262 SER A CB 1 ATOM 1673 O OG . SER A 1 244 ? 20.559 22.839 37.779 1.00 31.09 ? 262 SER A OG 1 ATOM 1674 N N . ASP A 1 245 ? 22.641 25.127 35.729 1.00 21.68 ? 263 ASP A N 1 ATOM 1675 C CA . ASP A 1 245 ? 22.201 26.125 34.776 1.00 22.12 ? 263 ASP A CA 1 ATOM 1676 C C . ASP A 1 245 ? 20.765 25.780 34.414 1.00 20.36 ? 263 ASP A C 1 ATOM 1677 O O . ASP A 1 245 ? 20.494 24.696 33.901 1.00 20.66 ? 263 ASP A O 1 ATOM 1678 C CB . ASP A 1 245 ? 23.099 26.088 33.536 1.00 24.28 ? 263 ASP A CB 1 ATOM 1679 C CG . ASP A 1 245 ? 24.425 26.832 33.741 1.00 27.32 ? 263 ASP A CG 1 ATOM 1680 O OD1 . ASP A 1 245 ? 24.714 27.316 34.862 1.00 25.49 ? 263 ASP A OD1 1 ATOM 1681 O OD2 . ASP A 1 245 ? 25.188 26.949 32.748 1.00 30.43 ? 263 ASP A OD2 1 ATOM 1682 N N . ASP A 1 246 ? 19.849 26.698 34.699 1.00 17.87 ? 264 ASP A N 1 ATOM 1683 C CA . ASP A 1 246 ? 18.422 26.427 34.593 1.00 16.92 ? 264 ASP A CA 1 ATOM 1684 C C . ASP A 1 246 ? 17.777 27.430 33.655 1.00 16.74 ? 264 ASP A C 1 ATOM 1685 O O . ASP A 1 246 ? 18.141 28.608 33.668 1.00 16.51 ? 264 ASP A O 1 ATOM 1686 C CB . ASP A 1 246 ? 17.758 26.604 35.958 1.00 16.37 ? 264 ASP A CB 1 ATOM 1687 C CG . ASP A 1 246 ? 18.166 25.547 36.968 1.00 17.17 ? 264 ASP A CG 1 ATOM 1688 O OD1 . ASP A 1 246 ? 18.476 24.405 36.566 1.00 17.39 ? 264 ASP A OD1 1 ATOM 1689 O OD2 . ASP A 1 246 ? 18.140 25.860 38.179 1.00 17.00 ? 264 ASP A OD2 1 ATOM 1690 N N . SER A 1 247 ? 16.807 26.976 32.870 1.00 16.06 ? 265 SER A N 1 ATOM 1691 C CA . SER A 1 247 ? 16.080 27.888 31.996 1.00 17.19 ? 265 SER A CA 1 ATOM 1692 C C . SER A 1 247 ? 14.566 27.746 32.104 1.00 16.17 ? 265 SER A C 1 ATOM 1693 O O . SER A 1 247 ? 14.037 26.662 32.389 1.00 15.59 ? 265 SER A O 1 ATOM 1694 C CB . SER A 1 247 ? 16.516 27.723 30.543 1.00 20.42 ? 265 SER A CB 1 ATOM 1695 O OG . SER A 1 247 ? 15.895 26.591 29.990 1.00 24.51 ? 265 SER A OG 1 ATOM 1696 N N . VAL A 1 248 ? 13.881 28.867 31.893 1.00 14.48 ? 266 VAL A N 1 ATOM 1697 C CA . VAL A 1 248 ? 12.422 28.892 31.770 1.00 13.56 ? 266 VAL A CA 1 ATOM 1698 C C . VAL A 1 248 ? 12.156 29.739 30.535 1.00 13.36 ? 266 VAL A C 1 ATOM 1699 O O . VAL A 1 248 ? 12.702 30.849 30.422 1.00 13.35 ? 266 VAL A O 1 ATOM 1700 C CB . VAL A 1 248 ? 11.751 29.524 33.011 1.00 13.54 ? 266 VAL A CB 1 ATOM 1701 C CG1 . VAL A 1 248 ? 10.253 29.740 32.770 1.00 13.05 ? 266 VAL A CG1 1 ATOM 1702 C CG2 . VAL A 1 248 ? 11.937 28.631 34.230 1.00 13.34 ? 266 VAL A CG2 1 ATOM 1703 N N . LYS A 1 249 ? 11.377 29.223 29.594 1.00 13.22 ? 267 LYS A N 1 ATOM 1704 C CA . LYS A 1 249 ? 11.079 30.001 28.394 1.00 14.65 ? 267 LYS A CA 1 ATOM 1705 C C . LYS A 1 249 ? 9.690 29.859 27.838 1.00 13.83 ? 267 LYS A C 1 ATOM 1706 O O . LYS A 1 249 ? 9.008 28.850 28.072 1.00 12.80 ? 267 LYS A O 1 ATOM 1707 C CB . LYS A 1 249 ? 12.097 29.715 27.284 1.00 16.75 ? 267 LYS A CB 1 ATOM 1708 C CG . LYS A 1 249 ? 12.287 28.273 26.937 1.00 19.80 ? 267 LYS A CG 1 ATOM 1709 C CD . LYS A 1 249 ? 13.529 28.092 26.067 1.00 22.07 ? 267 LYS A CD 1 ATOM 1710 C CE . LYS A 1 249 ? 13.540 26.682 25.529 1.00 24.15 ? 267 LYS A CE 1 ATOM 1711 N NZ . LYS A 1 249 ? 14.703 26.475 24.621 1.00 25.84 ? 267 LYS A NZ 1 ATOM 1712 N N . ASN A 1 250 ? 9.278 30.876 27.083 1.00 13.31 ? 268 ASN A N 1 ATOM 1713 C CA . ASN A 1 250 ? 8.051 30.797 26.289 1.00 13.17 ? 268 ASN A CA 1 ATOM 1714 C C . ASN A 1 250 ? 6.837 30.530 27.175 1.00 13.06 ? 268 ASN A C 1 ATOM 1715 O O . ASN A 1 250 ? 6.091 29.539 27.009 1.00 12.71 ? 268 ASN A O 1 ATOM 1716 C CB . ASN A 1 250 ? 8.210 29.756 25.184 1.00 13.76 ? 268 ASN A CB 1 ATOM 1717 C CG . ASN A 1 250 ? 9.448 30.007 24.338 1.00 14.59 ? 268 ASN A CG 1 ATOM 1718 O OD1 . ASN A 1 250 ? 9.752 31.162 24.000 1.00 14.41 ? 268 ASN A OD1 1 ATOM 1719 N ND2 . ASN A 1 250 ? 10.186 28.940 24.015 1.00 14.48 ? 268 ASN A ND2 1 ATOM 1720 N N . ILE A 1 251 ? 6.648 31.456 28.107 1.00 12.37 ? 269 ILE A N 1 ATOM 1721 C CA . ILE A 1 251 ? 5.577 31.368 29.104 1.00 12.37 ? 269 ILE A CA 1 ATOM 1722 C C . ILE A 1 251 ? 4.593 32.499 28.869 1.00 12.88 ? 269 ILE A C 1 ATOM 1723 O O . ILE A 1 251 ? 5.006 33.656 28.698 1.00 12.89 ? 269 ILE A O 1 ATOM 1724 C CB . ILE A 1 251 ? 6.153 31.517 30.527 1.00 12.10 ? 269 ILE A CB 1 ATOM 1725 C CG1 . ILE A 1 251 ? 7.315 30.526 30.811 1.00 12.70 ? 269 ILE A CG1 1 ATOM 1726 C CG2 . ILE A 1 251 ? 5.057 31.460 31.589 1.00 12.10 ? 269 ILE A CG2 1 ATOM 1727 C CD1 . ILE A 1 251 ? 6.946 29.061 30.756 1.00 12.82 ? 269 ILE A CD1 1 ATOM 1728 N N . TYR A 1 252 ? 3.294 32.183 28.899 1.00 12.64 ? 270 TYR A N 1 ATOM 1729 C CA . TYR A 1 252 ? 2.285 33.224 28.744 1.00 13.28 ? 270 TYR A CA 1 ATOM 1730 C C . TYR A 1 252 ? 1.243 33.072 29.840 1.00 12.99 ? 270 TYR A C 1 ATOM 1731 O O . TYR A 1 252 ? 0.595 32.028 29.942 1.00 13.32 ? 270 TYR A O 1 ATOM 1732 C CB . TYR A 1 252 ? 1.644 33.143 27.354 1.00 14.41 ? 270 TYR A CB 1 ATOM 1733 C CG . TYR A 1 252 ? 0.634 34.241 27.140 1.00 15.82 ? 270 TYR A CG 1 ATOM 1734 C CD1 . TYR A 1 252 ? 1.053 35.545 26.857 1.00 17.13 ? 270 TYR A CD1 1 ATOM 1735 C CD2 . TYR A 1 252 ? -0.728 33.987 27.270 1.00 16.96 ? 270 TYR A CD2 1 ATOM 1736 C CE1 . TYR A 1 252 ? 0.127 36.574 26.691 1.00 18.35 ? 270 TYR A CE1 1 ATOM 1737 C CE2 . TYR A 1 252 ? -1.663 35.007 27.098 1.00 18.23 ? 270 TYR A CE2 1 ATOM 1738 C CZ . TYR A 1 252 ? -1.224 36.291 26.822 1.00 19.47 ? 270 TYR A CZ 1 ATOM 1739 O OH . TYR A 1 252 ? -2.146 37.311 26.680 1.00 21.46 ? 270 TYR A OH 1 ATOM 1740 N N . VAL A 1 253 ? 1.090 34.106 30.654 1.00 12.71 ? 271 VAL A N 1 ATOM 1741 C CA . VAL A 1 253 ? 0.136 34.079 31.761 1.00 12.69 ? 271 VAL A CA 1 ATOM 1742 C C . VAL A 1 253 ? -0.806 35.257 31.577 1.00 13.45 ? 271 VAL A C 1 ATOM 1743 O O . VAL A 1 253 ? -0.362 36.395 31.481 1.00 14.24 ? 271 VAL A O 1 ATOM 1744 C CB . VAL A 1 253 ? 0.813 34.220 33.126 1.00 12.79 ? 271 VAL A CB 1 ATOM 1745 C CG1 . VAL A 1 253 ? -0.247 34.199 34.227 1.00 13.16 ? 271 VAL A CG1 1 ATOM 1746 C CG2 . VAL A 1 253 ? 1.821 33.092 33.353 1.00 12.82 ? 271 VAL A CG2 1 ATOM 1747 N N . THR A 1 254 ? -2.096 34.984 31.525 1.00 13.29 ? 272 THR A N 1 ATOM 1748 C CA . THR A 1 254 ? -3.073 36.074 31.391 1.00 13.90 ? 272 THR A CA 1 ATOM 1749 C C . THR A 1 254 ? -4.278 35.855 32.303 1.00 14.03 ? 272 THR A C 1 ATOM 1750 O O . THR A 1 254 ? -4.654 34.717 32.581 1.00 14.07 ? 272 THR A O 1 ATOM 1751 C CB . THR A 1 254 ? -3.505 36.263 29.918 1.00 14.62 ? 272 THR A CB 1 ATOM 1752 O OG1 . THR A 1 254 ? -4.223 37.506 29.776 1.00 15.63 ? 272 THR A OG1 1 ATOM 1753 C CG2 . THR A 1 254 ? -4.362 35.066 29.420 1.00 15.19 ? 272 THR A CG2 1 ATOM 1754 N N . GLY A 1 255 ? -4.863 36.951 32.772 1.00 14.03 ? 273 GLY A N 1 ATOM 1755 C CA . GLY A 1 255 ? -6.122 36.888 33.523 1.00 14.34 ? 273 GLY A CA 1 ATOM 1756 C C . GLY A 1 255 ? -5.968 36.339 34.926 1.00 14.56 ? 273 GLY A C 1 ATOM 1757 O O . GLY A 1 255 ? -6.751 35.484 35.355 1.00 15.00 ? 273 GLY A O 1 ATOM 1758 N N . ALA A 1 256 ? -4.962 36.817 35.645 1.00 14.47 ? 274 ALA A N 1 ATOM 1759 C CA . ALA A 1 256 ? -4.702 36.336 37.001 1.00 15.65 ? 274 ALA A CA 1 ATOM 1760 C C . ALA A 1 256 ? -5.260 37.291 38.037 1.00 16.29 ? 274 ALA A C 1 ATOM 1761 O O . ALA A 1 256 ? -4.925 38.479 38.054 1.00 17.00 ? 274 ALA A O 1 ATOM 1762 C CB . ALA A 1 256 ? -3.210 36.152 37.234 1.00 15.58 ? 274 ALA A CB 1 ATOM 1763 N N . THR A 1 257 ? -6.103 36.768 38.908 1.00 15.89 ? 275 THR A N 1 ATOM 1764 C CA . THR A 1 257 ? -6.575 37.547 40.049 1.00 16.82 ? 275 THR A CA 1 ATOM 1765 C C . THR A 1 257 ? -5.832 37.054 41.276 1.00 17.26 ? 275 THR A C 1 ATOM 1766 O O . THR A 1 257 ? -6.032 35.914 41.722 1.00 16.93 ? 275 THR A O 1 ATOM 1767 C CB . THR A 1 257 ? -8.088 37.386 40.226 1.00 18.21 ? 275 THR A CB 1 ATOM 1768 O OG1 . THR A 1 257 ? -8.734 37.804 39.019 1.00 19.25 ? 275 THR A OG1 1 ATOM 1769 C CG2 . THR A 1 257 ? -8.603 38.241 41.428 1.00 18.55 ? 275 THR A CG2 1 ATOM 1770 N N . MET A 1 258 ? -4.964 37.919 41.803 1.00 16.29 ? 276 MET A N 1 ATOM 1771 C CA . MET A 1 258 ? -4.053 37.590 42.879 1.00 17.55 ? 276 MET A CA 1 ATOM 1772 C C . MET A 1 258 ? -4.495 38.336 44.135 1.00 18.72 ? 276 MET A C 1 ATOM 1773 O O . MET A 1 258 ? -4.409 39.572 44.210 1.00 20.62 ? 276 MET A O 1 ATOM 1774 C CB . MET A 1 258 ? -2.617 37.981 42.489 1.00 17.67 ? 276 MET A CB 1 ATOM 1775 C CG . MET A 1 258 ? -2.149 37.379 41.161 1.00 17.70 ? 276 MET A CG 1 ATOM 1776 S SD . MET A 1 258 ? -2.314 35.582 41.059 1.00 19.49 ? 276 MET A SD 1 ATOM 1777 C CE . MET A 1 258 ? -1.042 35.100 42.200 1.00 18.60 ? 276 MET A CE 1 ATOM 1778 N N . ILE A 1 259 ? -4.987 37.575 45.103 1.00 17.15 ? 277 ILE A N 1 ATOM 1779 C CA . ILE A 1 259 ? -5.605 38.122 46.302 1.00 16.84 ? 277 ILE A CA 1 ATOM 1780 C C . ILE A 1 259 ? -4.758 37.749 47.516 1.00 16.68 ? 277 ILE A C 1 ATOM 1781 O O . ILE A 1 259 ? -4.424 36.573 47.699 1.00 16.14 ? 277 ILE A O 1 ATOM 1782 C CB . ILE A 1 259 ? -7.026 37.524 46.481 1.00 17.15 ? 277 ILE A CB 1 ATOM 1783 C CG1 . ILE A 1 259 ? -7.892 37.810 45.246 1.00 17.89 ? 277 ILE A CG1 1 ATOM 1784 C CG2 . ILE A 1 259 ? -7.658 38.049 47.763 1.00 17.66 ? 277 ILE A CG2 1 ATOM 1785 C CD1 . ILE A 1 259 ? -9.111 36.912 45.102 1.00 19.96 ? 277 ILE A CD1 1 ATOM 1786 N N . ASN A 1 260 ? -4.394 38.735 48.338 1.00 15.86 ? 278 ASN A N 1 ATOM 1787 C CA . ASN A 1 260 ? -3.666 38.463 49.577 1.00 17.02 ? 278 ASN A CA 1 ATOM 1788 C C . ASN A 1 260 ? -2.426 37.609 49.364 1.00 16.75 ? 278 ASN A C 1 ATOM 1789 O O . ASN A 1 260 ? -2.119 36.739 50.179 1.00 17.40 ? 278 ASN A O 1 ATOM 1790 C CB . ASN A 1 260 ? -4.576 37.731 50.577 1.00 18.43 ? 278 ASN A CB 1 ATOM 1791 C CG . ASN A 1 260 ? -5.674 38.610 51.117 1.00 21.12 ? 278 ASN A CG 1 ATOM 1792 O OD1 . ASN A 1 260 ? -5.716 39.808 50.848 1.00 20.32 ? 278 ASN A OD1 1 ATOM 1793 N ND2 . ASN A 1 260 ? -6.585 38.010 51.880 1.00 22.97 ? 278 ASN A ND2 1 ATOM 1794 N N . SER A 1 261 ? -1.719 37.844 48.264 1.00 16.55 ? 279 SER A N 1 ATOM 1795 C CA A SER A 1 261 ? -0.534 37.068 47.947 0.50 16.15 ? 279 SER A CA 1 ATOM 1796 C CA B SER A 1 261 ? -0.516 37.064 47.978 0.50 16.85 ? 279 SER A CA 1 ATOM 1797 C C . SER A 1 261 ? 0.728 37.863 48.335 1.00 16.37 ? 279 SER A C 1 ATOM 1798 O O . SER A 1 261 ? 0.672 39.091 48.494 1.00 16.65 ? 279 SER A O 1 ATOM 1799 C CB A SER A 1 261 ? -0.563 36.661 46.466 0.50 15.99 ? 279 SER A CB 1 ATOM 1800 C CB B SER A 1 261 ? -0.468 36.599 46.522 0.50 17.72 ? 279 SER A CB 1 ATOM 1801 O OG A SER A 1 261 ? -1.666 35.774 46.209 0.50 14.89 ? 279 SER A OG 1 ATOM 1802 O OG B SER A 1 261 ? -0.616 37.672 45.629 0.50 19.26 ? 279 SER A OG 1 ATOM 1803 N N . THR A 1 262 ? 1.850 37.183 48.525 1.00 15.56 ? 280 THR A N 1 ATOM 1804 C CA . THR A 1 262 ? 3.065 37.923 48.900 1.00 15.77 ? 280 THR A CA 1 ATOM 1805 C C . THR A 1 262 ? 3.573 38.749 47.719 1.00 16.26 ? 280 THR A C 1 ATOM 1806 O O . THR A 1 262 ? 4.121 39.830 47.901 1.00 17.59 ? 280 THR A O 1 ATOM 1807 C CB . THR A 1 262 ? 4.190 37.006 49.421 1.00 16.17 ? 280 THR A CB 1 ATOM 1808 O OG1 . THR A 1 262 ? 4.467 36.001 48.445 1.00 16.00 ? 280 THR A OG1 1 ATOM 1809 C CG2 . THR A 1 262 ? 3.806 36.351 50.763 1.00 16.51 ? 280 THR A CG2 1 ATOM 1810 N N . LYS A 1 263 ? 3.418 38.213 46.517 1.00 16.74 ? 281 LYS A N 1 ATOM 1811 C CA . LYS A 1 263 ? 3.626 38.963 45.269 1.00 16.48 ? 281 LYS A CA 1 ATOM 1812 C C . LYS A 1 263 ? 2.599 38.440 44.292 1.00 15.73 ? 281 LYS A C 1 ATOM 1813 O O . LYS A 1 263 ? 2.202 37.275 44.367 1.00 16.67 ? 281 LYS A O 1 ATOM 1814 C CB . LYS A 1 263 ? 5.057 38.805 44.721 1.00 16.88 ? 281 LYS A CB 1 ATOM 1815 C CG . LYS A 1 263 ? 5.405 37.394 44.242 1.00 17.44 ? 281 LYS A CG 1 ATOM 1816 C CD . LYS A 1 263 ? 6.835 37.295 43.725 1.00 18.16 ? 281 LYS A CD 1 ATOM 1817 C CE . LYS A 1 263 ? 7.145 35.912 43.149 1.00 19.07 ? 281 LYS A CE 1 ATOM 1818 N NZ . LYS A 1 263 ? 7.242 34.876 44.209 1.00 19.61 ? 281 LYS A NZ 1 ATOM 1819 N N . ALA A 1 264 ? 2.125 39.291 43.393 1.00 14.76 ? 282 ALA A N 1 ATOM 1820 C CA . ALA A 1 264 ? 1.221 38.829 42.363 1.00 14.49 ? 282 ALA A CA 1 ATOM 1821 C C . ALA A 1 264 ? 2.008 38.003 41.346 1.00 13.89 ? 282 ALA A C 1 ATOM 1822 O O . ALA A 1 264 ? 1.548 36.981 40.854 1.00 13.47 ? 282 ALA A O 1 ATOM 1823 C CB . ALA A 1 264 ? 0.539 40.004 41.684 1.00 14.67 ? 282 ALA A CB 1 ATOM 1824 N N . ALA A 1 265 ? 3.221 38.448 41.060 1.00 13.80 ? 283 ALA A N 1 ATOM 1825 C CA . ALA A 1 265 ? 4.031 37.787 40.040 1.00 13.46 ? 283 ALA A CA 1 ATOM 1826 C C . ALA A 1 265 ? 5.478 38.117 40.272 1.00 13.28 ? 283 ALA A C 1 ATOM 1827 O O . ALA A 1 265 ? 5.798 39.141 40.883 1.00 13.44 ? 283 ALA A O 1 ATOM 1828 C CB . ALA A 1 265 ? 3.607 38.235 38.653 1.00 14.17 ? 283 ALA A CB 1 ATOM 1829 N N . GLY A 1 266 ? 6.373 37.245 39.815 1.00 12.88 ? 284 GLY A N 1 ATOM 1830 C CA . GLY A 1 266 ? 7.781 37.572 39.949 1.00 12.81 ? 284 GLY A CA 1 ATOM 1831 C C . GLY A 1 266 ? 8.726 36.545 39.376 1.00 13.07 ? 284 GLY A C 1 ATOM 1832 O O . GLY A 1 266 ? 8.302 35.518 38.825 1.00 12.49 ? 284 GLY A O 1 ATOM 1833 N N . ILE A 1 267 ? 10.010 36.875 39.498 1.00 12.81 ? 285 ILE A N 1 ATOM 1834 C CA . ILE A 1 267 ? 11.117 36.036 39.048 1.00 13.23 ? 285 ILE A CA 1 ATOM 1835 C C . ILE A 1 267 ? 12.110 35.922 40.199 1.00 13.59 ? 285 ILE A C 1 ATOM 1836 O O . ILE A 1 267 ? 12.434 36.934 40.829 1.00 14.14 ? 285 ILE A O 1 ATOM 1837 C CB . ILE A 1 267 ? 11.817 36.657 37.810 1.00 12.95 ? 285 ILE A CB 1 ATOM 1838 C CG1 . ILE A 1 267 ? 10.811 36.769 36.650 1.00 13.42 ? 285 ILE A CG1 1 ATOM 1839 C CG2 . ILE A 1 267 ? 13.013 35.786 37.390 1.00 13.03 ? 285 ILE A CG2 1 ATOM 1840 C CD1 . ILE A 1 267 ? 11.297 37.583 35.465 1.00 14.29 ? 285 ILE A CD1 1 ATOM 1841 N N . LYS A 1 268 ? 12.596 34.706 40.479 1.00 13.96 ? 286 LYS A N 1 ATOM 1842 C CA . LYS A 1 268 ? 13.543 34.499 41.572 1.00 15.27 ? 286 LYS A CA 1 ATOM 1843 C C . LYS A 1 268 ? 14.715 33.685 41.076 1.00 14.82 ? 286 LYS A C 1 ATOM 1844 O O . LYS A 1 268 ? 14.537 32.566 40.608 1.00 14.01 ? 286 LYS A O 1 ATOM 1845 C CB . LYS A 1 268 ? 12.942 33.686 42.726 1.00 17.72 ? 286 LYS A CB 1 ATOM 1846 C CG . LYS A 1 268 ? 11.559 34.044 43.189 1.00 20.93 ? 286 LYS A CG 1 ATOM 1847 C CD . LYS A 1 268 ? 11.274 33.370 44.533 1.00 22.09 ? 286 LYS A CD 1 ATOM 1848 C CE . LYS A 1 268 ? 11.287 31.854 44.453 1.00 23.16 ? 286 LYS A CE 1 ATOM 1849 N NZ . LYS A 1 268 ? 10.463 31.231 45.541 1.00 24.49 ? 286 LYS A NZ 1 ATOM 1850 N N . THR A 1 269 ? 15.923 34.226 41.190 1.00 14.68 ? 287 THR A N 1 ATOM 1851 C CA . THR A 1 269 ? 17.099 33.469 40.772 1.00 15.29 ? 287 THR A CA 1 ATOM 1852 C C . THR A 1 269 ? 18.158 33.535 41.866 1.00 15.02 ? 287 THR A C 1 ATOM 1853 O O . THR A 1 269 ? 18.263 34.519 42.581 1.00 14.39 ? 287 THR A O 1 ATOM 1854 C CB . THR A 1 269 ? 17.680 33.989 39.437 1.00 16.33 ? 287 THR A CB 1 ATOM 1855 O OG1 . THR A 1 269 ? 18.019 35.378 39.563 1.00 17.03 ? 287 THR A OG1 1 ATOM 1856 C CG2 . THR A 1 269 ? 16.648 33.834 38.300 1.00 16.63 ? 287 THR A CG2 1 ATOM 1857 N N . TYR A 1 270 ? 18.949 32.474 41.974 1.00 15.57 ? 288 TYR A N 1 ATOM 1858 C CA . TYR A 1 270 ? 20.077 32.453 42.887 1.00 17.09 ? 288 TYR A CA 1 ATOM 1859 C C . TYR A 1 270 ? 21.193 33.344 42.347 1.00 17.87 ? 288 TYR A C 1 ATOM 1860 O O . TYR A 1 270 ? 21.327 33.510 41.142 1.00 18.62 ? 288 TYR A O 1 ATOM 1861 C CB . TYR A 1 270 ? 20.600 31.028 43.031 1.00 17.20 ? 288 TYR A CB 1 ATOM 1862 C CG . TYR A 1 270 ? 19.797 30.197 44.008 1.00 17.95 ? 288 TYR A CG 1 ATOM 1863 C CD1 . TYR A 1 270 ? 18.641 29.522 43.601 1.00 18.41 ? 288 TYR A CD1 1 ATOM 1864 C CD2 . TYR A 1 270 ? 20.207 30.071 45.338 1.00 18.22 ? 288 TYR A CD2 1 ATOM 1865 C CE1 . TYR A 1 270 ? 17.901 28.756 44.504 1.00 18.67 ? 288 TYR A CE1 1 ATOM 1866 C CE2 . TYR A 1 270 ? 19.478 29.307 46.241 1.00 18.56 ? 288 TYR A CE2 1 ATOM 1867 C CZ . TYR A 1 270 ? 18.335 28.652 45.818 1.00 19.21 ? 288 TYR A CZ 1 ATOM 1868 O OH . TYR A 1 270 ? 17.623 27.892 46.729 1.00 19.76 ? 288 TYR A OH 1 ATOM 1869 N N . PRO A 1 271 ? 21.994 33.922 43.245 1.00 19.41 ? 289 PRO A N 1 ATOM 1870 C CA . PRO A 1 271 ? 23.168 34.661 42.765 1.00 19.97 ? 289 PRO A CA 1 ATOM 1871 C C . PRO A 1 271 ? 24.270 33.697 42.323 1.00 20.61 ? 289 PRO A C 1 ATOM 1872 O O . PRO A 1 271 ? 24.047 32.482 42.276 1.00 20.94 ? 289 PRO A O 1 ATOM 1873 C CB . PRO A 1 271 ? 23.598 35.443 44.002 1.00 20.73 ? 289 PRO A CB 1 ATOM 1874 C CG . PRO A 1 271 ? 23.200 34.548 45.133 1.00 20.45 ? 289 PRO A CG 1 ATOM 1875 C CD . PRO A 1 271 ? 21.845 34.014 44.708 1.00 19.83 ? 289 PRO A CD 1 ATOM 1876 N N . SER A 1 272 ? 25.452 34.222 41.993 1.00 22.14 ? 290 SER A N 1 ATOM 1877 C CA . SER A 1 272 ? 26.557 33.352 41.606 1.00 23.17 ? 290 SER A CA 1 ATOM 1878 C C . SER A 1 272 ? 27.282 32.817 42.850 1.00 25.07 ? 290 SER A C 1 ATOM 1879 O O . SER A 1 272 ? 26.818 33.001 43.977 1.00 24.39 ? 290 SER A O 1 ATOM 1880 C CB . SER A 1 272 ? 27.533 34.086 40.684 1.00 23.70 ? 290 SER A CB 1 ATOM 1881 O OG . SER A 1 272 ? 28.030 35.248 41.327 1.00 23.23 ? 290 SER A OG 1 ATOM 1882 N N . GLY A 1 273 ? 28.410 32.146 42.638 1.00 26.98 ? 291 GLY A N 1 ATOM 1883 C CA . GLY A 1 273 ? 29.191 31.598 43.752 1.00 27.87 ? 291 GLY A CA 1 ATOM 1884 C C . GLY A 1 273 ? 28.729 30.212 44.159 1.00 29.43 ? 291 GLY A C 1 ATOM 1885 O O . GLY A 1 273 ? 27.667 29.739 43.740 1.00 27.48 ? 291 GLY A O 1 ATOM 1886 N N . GLY A 1 274 ? 29.541 29.543 44.974 1.00 31.16 ? 292 GLY A N 1 ATOM 1887 C CA . GLY A 1 274 ? 29.214 28.208 45.448 1.00 30.92 ? 292 GLY A CA 1 ATOM 1888 C C . GLY A 1 274 ? 28.902 27.261 44.312 1.00 31.11 ? 292 GLY A C 1 ATOM 1889 O O . GLY A 1 274 ? 29.625 27.210 43.318 1.00 32.60 ? 292 GLY A O 1 ATOM 1890 N N . ASP A 1 275 ? 27.809 26.520 44.455 1.00 30.12 ? 293 ASP A N 1 ATOM 1891 C CA . ASP A 1 275 ? 27.398 25.550 43.453 1.00 29.91 ? 293 ASP A CA 1 ATOM 1892 C C . ASP A 1 275 ? 26.300 26.099 42.550 1.00 26.77 ? 293 ASP A C 1 ATOM 1893 O O . ASP A 1 275 ? 25.735 25.362 41.745 1.00 26.64 ? 293 ASP A O 1 ATOM 1894 C CB . ASP A 1 275 ? 26.912 24.267 44.134 1.00 34.48 ? 293 ASP A CB 1 ATOM 1895 C CG . ASP A 1 275 ? 28.052 23.453 44.722 1.00 39.18 ? 293 ASP A CG 1 ATOM 1896 O OD1 . ASP A 1 275 ? 29.232 23.814 44.498 1.00 40.93 ? 293 ASP A OD1 1 ATOM 1897 O OD2 . ASP A 1 275 ? 27.766 22.445 45.401 1.00 41.86 ? 293 ASP A OD2 1 ATOM 1898 N N . HIS A 1 276 ? 26.007 27.388 42.683 1.00 25.52 ? 294 HIS A N 1 ATOM 1899 C CA . HIS A 1 276 ? 24.915 27.994 41.916 1.00 23.19 ? 294 HIS A CA 1 ATOM 1900 C C . HIS A 1 276 ? 25.241 28.012 40.464 1.00 23.60 ? 294 HIS A C 1 ATOM 1901 O O . HIS A 1 276 ? 26.404 28.138 40.086 1.00 23.02 ? 294 HIS A O 1 ATOM 1902 C CB . HIS A 1 276 ? 24.628 29.411 42.384 1.00 23.25 ? 294 HIS A CB 1 ATOM 1903 C CG . HIS A 1 276 ? 24.325 29.523 43.857 1.00 23.04 ? 294 HIS A CG 1 ATOM 1904 N ND1 . HIS A 1 276 ? 23.527 28.645 44.505 1.00 24.50 ? 294 HIS A ND1 1 ATOM 1905 C CD2 . HIS A 1 276 ? 24.728 30.457 44.800 1.00 23.65 ? 294 HIS A CD2 1 ATOM 1906 C CE1 . HIS A 1 276 ? 23.449 28.989 45.807 1.00 24.05 ? 294 HIS A CE1 1 ATOM 1907 N NE2 . HIS A 1 276 ? 24.175 30.104 45.984 1.00 24.83 ? 294 HIS A NE2 1 ATOM 1908 N N . GLY A 1 277 ? 24.215 27.884 39.629 1.00 21.83 ? 295 GLY A N 1 ATOM 1909 C CA . GLY A 1 277 ? 24.375 27.998 38.192 1.00 21.50 ? 295 GLY A CA 1 ATOM 1910 C C . GLY A 1 277 ? 23.798 29.299 37.672 1.00 21.35 ? 295 GLY A C 1 ATOM 1911 O O . GLY A 1 277 ? 23.410 30.178 38.448 1.00 21.82 ? 295 GLY A O 1 ATOM 1912 N N . THR A 1 278 ? 23.748 29.433 36.352 1.00 22.05 ? 296 THR A N 1 ATOM 1913 C CA . THR A 1 278 ? 23.203 30.640 35.746 1.00 22.22 ? 296 THR A CA 1 ATOM 1914 C C . THR A 1 278 ? 21.779 30.340 35.335 1.00 20.43 ? 296 THR A C 1 ATOM 1915 O O . THR A 1 278 ? 21.450 29.208 34.973 1.00 21.58 ? 296 THR A O 1 ATOM 1916 C CB . THR A 1 278 ? 24.036 31.150 34.537 1.00 25.16 ? 296 THR A CB 1 ATOM 1917 O OG1 . THR A 1 278 ? 25.324 31.584 34.996 1.00 28.06 ? 296 THR A OG1 1 ATOM 1918 C CG2 . THR A 1 278 ? 23.347 32.348 33.850 1.00 25.28 ? 296 THR A CG2 1 ATOM 1919 N N . SER A 1 279 ? 20.934 31.354 35.436 1.00 17.86 ? 297 SER A N 1 ATOM 1920 C CA . SER A 1 279 ? 19.529 31.223 35.133 1.00 16.74 ? 297 SER A CA 1 ATOM 1921 C C . SER A 1 279 ? 19.243 31.982 33.853 1.00 15.97 ? 297 SER A C 1 ATOM 1922 O O . SER A 1 279 ? 19.718 33.100 33.685 1.00 16.08 ? 297 SER A O 1 ATOM 1923 C CB . SER A 1 279 ? 18.716 31.861 36.261 1.00 16.31 ? 297 SER A CB 1 ATOM 1924 O OG . SER A 1 279 ? 18.924 31.180 37.483 1.00 17.21 ? 297 SER A OG 1 ATOM 1925 N N . THR A 1 280 ? 18.453 31.381 32.978 1.00 15.32 ? 298 THR A N 1 ATOM 1926 C CA . THR A 1 280 ? 18.037 32.016 31.736 1.00 16.00 ? 298 THR A CA 1 ATOM 1927 C C . THR A 1 280 ? 16.524 32.034 31.689 1.00 16.15 ? 298 THR A C 1 ATOM 1928 O O . THR A 1 280 ? 15.881 30.991 31.806 1.00 16.02 ? 298 THR A O 1 ATOM 1929 C CB . THR A 1 280 ? 18.610 31.253 30.525 1.00 17.01 ? 298 THR A CB 1 ATOM 1930 O OG1 . THR A 1 280 ? 20.040 31.225 30.647 1.00 17.69 ? 298 THR A OG1 1 ATOM 1931 C CG2 . THR A 1 280 ? 18.239 31.917 29.220 1.00 17.79 ? 298 THR A CG2 1 ATOM 1932 N N . VAL A 1 281 ? 15.942 33.222 31.538 1.00 14.87 ? 299 VAL A N 1 ATOM 1933 C CA . VAL A 1 281 ? 14.490 33.307 31.438 1.00 14.03 ? 299 VAL A CA 1 ATOM 1934 C C . VAL A 1 281 ? 14.197 34.110 30.200 1.00 14.49 ? 299 VAL A C 1 ATOM 1935 O O . VAL A 1 281 ? 14.614 35.277 30.105 1.00 14.70 ? 299 VAL A O 1 ATOM 1936 C CB . VAL A 1 281 ? 13.862 33.990 32.669 1.00 14.17 ? 299 VAL A CB 1 ATOM 1937 C CG1 . VAL A 1 281 ? 12.331 33.984 32.566 1.00 14.14 ? 299 VAL A CG1 1 ATOM 1938 C CG2 . VAL A 1 281 ? 14.310 33.287 33.943 1.00 13.78 ? 299 VAL A CG2 1 ATOM 1939 N N . SER A 1 282 ? 13.499 33.503 29.245 1.00 13.96 ? 300 SER A N 1 ATOM 1940 C CA A SER A 1 282 ? 13.240 34.200 27.986 0.50 14.08 ? 300 SER A CA 1 ATOM 1941 C CA B SER A 1 282 ? 13.260 34.147 27.947 0.50 14.35 ? 300 SER A CA 1 ATOM 1942 C C . SER A 1 282 ? 11.803 34.089 27.517 1.00 14.12 ? 300 SER A C 1 ATOM 1943 O O . SER A 1 282 ? 11.193 33.026 27.568 1.00 13.87 ? 300 SER A O 1 ATOM 1944 C CB A SER A 1 282 ? 14.220 33.745 26.894 0.50 14.22 ? 300 SER A CB 1 ATOM 1945 C CB B SER A 1 282 ? 14.137 33.479 26.881 0.50 14.81 ? 300 SER A CB 1 ATOM 1946 O OG A SER A 1 282 ? 13.976 32.415 26.493 0.50 14.01 ? 300 SER A OG 1 ATOM 1947 O OG B SER A 1 282 ? 13.765 33.894 25.580 0.50 15.57 ? 300 SER A OG 1 ATOM 1948 N N . ASN A 1 283 ? 11.256 35.221 27.072 1.00 13.75 ? 301 ASN A N 1 ATOM 1949 C CA . ASN A 1 283 ? 9.901 35.265 26.534 1.00 13.65 ? 301 ASN A CA 1 ATOM 1950 C C . ASN A 1 283 ? 8.876 34.814 27.571 1.00 13.08 ? 301 ASN A C 1 ATOM 1951 O O . ASN A 1 283 ? 8.249 33.765 27.427 1.00 12.67 ? 301 ASN A O 1 ATOM 1952 C CB . ASN A 1 283 ? 9.796 34.452 25.240 1.00 14.67 ? 301 ASN A CB 1 ATOM 1953 C CG . ASN A 1 283 ? 8.388 34.412 24.673 1.00 15.93 ? 301 ASN A CG 1 ATOM 1954 O OD1 . ASN A 1 283 ? 7.581 35.324 24.885 1.00 16.03 ? 301 ASN A OD1 1 ATOM 1955 N ND2 . ASN A 1 283 ? 8.087 33.349 23.949 1.00 16.40 ? 301 ASN A ND2 1 ATOM 1956 N N . VAL A 1 284 ? 8.727 35.626 28.606 1.00 12.70 ? 302 VAL A N 1 ATOM 1957 C CA . VAL A 1 284 ? 7.729 35.387 29.636 1.00 12.63 ? 302 VAL A CA 1 ATOM 1958 C C . VAL A 1 284 ? 6.838 36.613 29.704 1.00 13.11 ? 302 VAL A C 1 ATOM 1959 O O . VAL A 1 284 ? 7.316 37.718 29.913 1.00 12.51 ? 302 VAL A O 1 ATOM 1960 C CB . VAL A 1 284 ? 8.371 35.098 31.001 1.00 12.75 ? 302 VAL A CB 1 ATOM 1961 C CG1 . VAL A 1 284 ? 7.295 34.951 32.069 1.00 12.53 ? 302 VAL A CG1 1 ATOM 1962 C CG2 . VAL A 1 284 ? 9.235 33.835 30.917 1.00 12.29 ? 302 VAL A CG2 1 ATOM 1963 N N . THR A 1 285 ? 5.537 36.400 29.537 1.00 13.46 ? 303 THR A N 1 ATOM 1964 C CA . THR A 1 285 ? 4.584 37.506 29.627 1.00 14.09 ? 303 THR A CA 1 ATOM 1965 C C . THR A 1 285 ? 3.605 37.292 30.778 1.00 14.43 ? 303 THR A C 1 ATOM 1966 O O . THR A 1 285 ? 3.025 36.214 30.902 1.00 14.35 ? 303 THR A O 1 ATOM 1967 C CB . THR A 1 285 ? 3.780 37.616 28.322 1.00 15.36 ? 303 THR A CB 1 ATOM 1968 O OG1 . THR A 1 285 ? 4.665 37.975 27.256 1.00 17.20 ? 303 THR A OG1 1 ATOM 1969 C CG2 . THR A 1 285 ? 2.669 38.691 28.454 1.00 15.35 ? 303 THR A CG2 1 ATOM 1970 N N . PHE A 1 286 ? 3.427 38.336 31.585 1.00 13.64 ? 304 PHE A N 1 ATOM 1971 C CA . PHE A 1 286 ? 2.443 38.368 32.652 1.00 13.94 ? 304 PHE A CA 1 ATOM 1972 C C . PHE A 1 286 ? 1.472 39.461 32.208 1.00 14.52 ? 304 PHE A C 1 ATOM 1973 O O . PHE A 1 286 ? 1.831 40.643 32.199 1.00 14.63 ? 304 PHE A O 1 ATOM 1974 C CB . PHE A 1 286 ? 3.072 38.790 33.974 1.00 14.18 ? 304 PHE A CB 1 ATOM 1975 C CG . PHE A 1 286 ? 4.233 37.935 34.434 1.00 14.53 ? 304 PHE A CG 1 ATOM 1976 C CD1 . PHE A 1 286 ? 5.541 38.243 34.044 1.00 14.93 ? 304 PHE A CD1 1 ATOM 1977 C CD2 . PHE A 1 286 ? 4.031 36.864 35.305 1.00 15.41 ? 304 PHE A CD2 1 ATOM 1978 C CE1 . PHE A 1 286 ? 6.617 37.474 34.495 1.00 14.17 ? 304 PHE A CE1 1 ATOM 1979 C CE2 . PHE A 1 286 ? 5.102 36.092 35.756 1.00 15.23 ? 304 PHE A CE2 1 ATOM 1980 C CZ . PHE A 1 286 ? 6.396 36.405 35.352 1.00 15.52 ? 304 PHE A CZ 1 ATOM 1981 N N . ASN A 1 287 ? 0.261 39.064 31.841 1.00 14.91 ? 305 ASN A N 1 ATOM 1982 C CA . ASN A 1 287 ? -0.732 39.993 31.281 1.00 15.37 ? 305 ASN A CA 1 ATOM 1983 C C . ASN A 1 287 ? -2.050 40.001 32.054 1.00 16.56 ? 305 ASN A C 1 ATOM 1984 O O . ASN A 1 287 ? -2.499 38.958 32.529 1.00 15.55 ? 305 ASN A O 1 ATOM 1985 C CB . ASN A 1 287 ? -1.009 39.620 29.825 1.00 16.46 ? 305 ASN A CB 1 ATOM 1986 C CG . ASN A 1 287 ? -1.991 40.566 29.160 1.00 17.24 ? 305 ASN A CG 1 ATOM 1987 O OD1 . ASN A 1 287 ? -1.719 41.765 29.010 1.00 17.15 ? 305 ASN A OD1 1 ATOM 1988 N ND2 . ASN A 1 287 ? -3.144 40.033 28.753 1.00 17.41 ? 305 ASN A ND2 1 ATOM 1989 N N . ASP A 1 288 ? -2.679 41.171 32.171 1.00 17.26 ? 306 ASP A N 1 ATOM 1990 C CA . ASP A 1 288 ? -4.040 41.241 32.729 1.00 18.83 ? 306 ASP A CA 1 ATOM 1991 C C . ASP A 1 288 ? -4.104 40.652 34.142 1.00 17.61 ? 306 ASP A C 1 ATOM 1992 O O . ASP A 1 288 ? -4.840 39.681 34.399 1.00 16.94 ? 306 ASP A O 1 ATOM 1993 C CB . ASP A 1 288 ? -5.029 40.503 31.815 1.00 21.47 ? 306 ASP A CB 1 ATOM 1994 C CG . ASP A 1 288 ? -5.498 41.339 30.636 1.00 26.38 ? 306 ASP A CG 1 ATOM 1995 O OD1 . ASP A 1 288 ? -5.059 42.506 30.480 1.00 29.58 ? 306 ASP A OD1 1 ATOM 1996 O OD2 . ASP A 1 288 ? -6.319 40.819 29.845 1.00 29.58 ? 306 ASP A OD2 1 ATOM 1997 N N . PHE A 1 289 ? -3.316 41.220 35.042 1.00 15.84 ? 307 PHE A N 1 ATOM 1998 C CA . PHE A 1 289 ? -3.341 40.838 36.445 1.00 16.84 ? 307 PHE A CA 1 ATOM 1999 C C . PHE A 1 289 ? -4.146 41.829 37.252 1.00 18.55 ? 307 PHE A C 1 ATOM 2000 O O . PHE A 1 289 ? -4.020 43.053 37.074 1.00 18.47 ? 307 PHE A O 1 ATOM 2001 C CB . PHE A 1 289 ? -1.944 40.792 37.053 1.00 14.97 ? 307 PHE A CB 1 ATOM 2002 C CG . PHE A 1 289 ? -1.209 39.494 36.828 1.00 14.68 ? 307 PHE A CG 1 ATOM 2003 C CD1 . PHE A 1 289 ? -0.992 39.001 35.541 1.00 14.89 ? 307 PHE A CD1 1 ATOM 2004 C CD2 . PHE A 1 289 ? -0.684 38.794 37.911 1.00 14.72 ? 307 PHE A CD2 1 ATOM 2005 C CE1 . PHE A 1 289 ? -0.295 37.813 35.336 1.00 14.44 ? 307 PHE A CE1 1 ATOM 2006 C CE2 . PHE A 1 289 ? 0.017 37.598 37.717 1.00 14.24 ? 307 PHE A CE2 1 ATOM 2007 C CZ . PHE A 1 289 ? 0.218 37.115 36.433 1.00 14.18 ? 307 PHE A CZ 1 ATOM 2008 N N . THR A 1 290 ? -4.958 41.285 38.146 1.00 18.21 ? 308 THR A N 1 ATOM 2009 C CA . THR A 1 290 ? -5.634 42.081 39.157 1.00 20.46 ? 308 THR A CA 1 ATOM 2010 C C . THR A 1 290 ? -4.963 41.809 40.486 1.00 20.66 ? 308 THR A C 1 ATOM 2011 O O . THR A 1 290 ? -4.864 40.657 40.927 1.00 19.99 ? 308 THR A O 1 ATOM 2012 C CB . THR A 1 290 ? -7.135 41.741 39.188 1.00 21.95 ? 308 THR A CB 1 ATOM 2013 O OG1 . THR A 1 290 ? -7.689 42.065 37.903 1.00 23.66 ? 308 THR A OG1 1 ATOM 2014 C CG2 . THR A 1 290 ? -7.854 42.538 40.265 1.00 23.45 ? 308 THR A CG2 1 ATOM 2015 N N . VAL A 1 291 ? -4.458 42.870 41.099 1.00 20.13 ? 309 VAL A N 1 ATOM 2016 C CA . VAL A 1 291 ? -3.792 42.793 42.380 1.00 22.15 ? 309 VAL A CA 1 ATOM 2017 C C . VAL A 1 291 ? -4.812 43.246 43.437 1.00 24.85 ? 309 VAL A C 1 ATOM 2018 O O . VAL A 1 291 ? -5.354 44.361 43.370 1.00 25.18 ? 309 VAL A O 1 ATOM 2019 C CB . VAL A 1 291 ? -2.522 43.683 42.399 1.00 23.25 ? 309 VAL A CB 1 ATOM 2020 C CG1 . VAL A 1 291 ? -1.785 43.570 43.726 1.00 25.17 ? 309 VAL A CG1 1 ATOM 2021 C CG2 . VAL A 1 291 ? -1.605 43.311 41.228 1.00 23.15 ? 309 VAL A CG2 1 ATOM 2022 N N . ASP A 1 292 ? -5.091 42.364 44.389 1.00 23.56 ? 310 ASP A N 1 ATOM 2023 C CA . ASP A 1 292 ? -6.026 42.667 45.469 1.00 22.92 ? 310 ASP A CA 1 ATOM 2024 C C . ASP A 1 292 ? -5.349 42.394 46.795 1.00 21.24 ? 310 ASP A C 1 ATOM 2025 O O . ASP A 1 292 ? -5.331 41.259 47.276 1.00 20.36 ? 310 ASP A O 1 ATOM 2026 C CB . ASP A 1 292 ? -7.302 41.834 45.297 1.00 25.18 ? 310 ASP A CB 1 ATOM 2027 C CG . ASP A 1 292 ? -8.297 42.013 46.442 1.00 27.26 ? 310 ASP A CG 1 ATOM 2028 O OD1 . ASP A 1 292 ? -8.038 42.812 47.372 1.00 28.37 ? 310 ASP A OD1 1 ATOM 2029 O OD2 . ASP A 1 292 ? -9.332 41.309 46.412 1.00 30.11 ? 310 ASP A OD2 1 ATOM 2030 N N . ASN A 1 293 ? -4.766 43.439 47.378 1.00 19.90 ? 311 ASN A N 1 ATOM 2031 C CA . ASN A 1 293 ? -4.144 43.348 48.690 1.00 20.51 ? 311 ASN A CA 1 ATOM 2032 C C . ASN A 1 293 ? -2.932 42.397 48.720 1.00 19.63 ? 311 ASN A C 1 ATOM 2033 O O . ASN A 1 293 ? -2.626 41.802 49.745 1.00 20.52 ? 311 ASN A O 1 ATOM 2034 C CB . ASN A 1 293 ? -5.192 42.941 49.758 1.00 21.49 ? 311 ASN A CB 1 ATOM 2035 C CG . ASN A 1 293 ? -4.734 43.249 51.163 1.00 23.53 ? 311 ASN A CG 1 ATOM 2036 O OD1 . ASN A 1 293 ? -4.212 44.327 51.426 1.00 23.13 ? 311 ASN A OD1 1 ATOM 2037 N ND2 . ASN A 1 293 ? -4.921 42.299 52.080 1.00 23.37 ? 311 ASN A ND2 1 ATOM 2038 N N . SER A 1 294 ? -2.239 42.267 47.589 1.00 19.18 ? 312 SER A N 1 ATOM 2039 C CA . SER A 1 294 ? -0.977 41.522 47.551 1.00 18.33 ? 312 SER A CA 1 ATOM 2040 C C . SER A 1 294 ? 0.181 42.440 47.944 1.00 18.27 ? 312 SER A C 1 ATOM 2041 O O . SER A 1 294 ? 0.102 43.649 47.733 1.00 19.26 ? 312 SER A O 1 ATOM 2042 C CB . SER A 1 294 ? -0.775 40.920 46.170 1.00 18.36 ? 312 SER A CB 1 ATOM 2043 O OG . SER A 1 294 ? -1.759 39.916 45.948 1.00 19.28 ? 312 SER A OG 1 ATOM 2044 N N . ASP A 1 295 ? 1.244 41.898 48.528 1.00 17.61 ? 313 ASP A N 1 ATOM 2045 C CA . ASP A 1 295 ? 2.289 42.774 49.085 1.00 18.28 ? 313 ASP A CA 1 ATOM 2046 C C . ASP A 1 295 ? 3.091 43.533 48.021 1.00 18.73 ? 313 ASP A C 1 ATOM 2047 O O . ASP A 1 295 ? 3.398 44.713 48.194 1.00 19.10 ? 313 ASP A O 1 ATOM 2048 C CB . ASP A 1 295 ? 3.209 42.021 50.043 1.00 18.92 ? 313 ASP A CB 1 ATOM 2049 C CG . ASP A 1 295 ? 2.451 41.377 51.199 1.00 20.12 ? 313 ASP A CG 1 ATOM 2050 O OD1 . ASP A 1 295 ? 1.445 41.956 51.668 1.00 20.43 ? 313 ASP A OD1 1 ATOM 2051 O OD2 . ASP A 1 295 ? 2.870 40.282 51.626 1.00 21.20 ? 313 ASP A OD2 1 ATOM 2052 N N . TYR A 1 296 ? 3.436 42.853 46.936 1.00 18.56 ? 314 TYR A N 1 ATOM 2053 C CA . TYR A 1 296 ? 4.005 43.492 45.755 1.00 17.94 ? 314 TYR A CA 1 ATOM 2054 C C . TYR A 1 296 ? 3.190 43.069 44.554 1.00 17.86 ? 314 TYR A C 1 ATOM 2055 O O . TYR A 1 296 ? 2.695 41.936 44.491 1.00 18.20 ? 314 TYR A O 1 ATOM 2056 C CB . TYR A 1 296 ? 5.445 43.024 45.512 1.00 18.02 ? 314 TYR A CB 1 ATOM 2057 C CG . TYR A 1 296 ? 6.514 43.538 46.444 1.00 18.41 ? 314 TYR A CG 1 ATOM 2058 C CD1 . TYR A 1 296 ? 6.644 44.902 46.726 1.00 18.51 ? 314 TYR A CD1 1 ATOM 2059 C CD2 . TYR A 1 296 ? 7.456 42.661 46.979 1.00 18.23 ? 314 TYR A CD2 1 ATOM 2060 C CE1 . TYR A 1 296 ? 7.655 45.360 47.560 1.00 19.33 ? 314 TYR A CE1 1 ATOM 2061 C CE2 . TYR A 1 296 ? 8.472 43.111 47.806 1.00 19.23 ? 314 TYR A CE2 1 ATOM 2062 C CZ . TYR A 1 296 ? 8.565 44.463 48.085 1.00 18.86 ? 314 TYR A CZ 1 ATOM 2063 O OH . TYR A 1 296 ? 9.576 44.901 48.913 1.00 20.02 ? 314 TYR A OH 1 ATOM 2064 N N . ALA A 1 297 ? 3.084 43.956 43.572 1.00 15.86 ? 315 ALA A N 1 ATOM 2065 C CA . ALA A 1 297 ? 2.485 43.616 42.306 1.00 15.85 ? 315 ALA A CA 1 ATOM 2066 C C . ALA A 1 297 ? 3.468 42.773 41.494 1.00 15.86 ? 315 ALA A C 1 ATOM 2067 O O . ALA A 1 297 ? 3.076 41.828 40.815 1.00 15.91 ? 315 ALA A O 1 ATOM 2068 C CB . ALA A 1 297 ? 2.123 44.878 41.540 1.00 16.55 ? 315 ALA A CB 1 ATOM 2069 N N . PHE A 1 298 ? 4.739 43.155 41.531 1.00 15.53 ? 316 PHE A N 1 ATOM 2070 C CA . PHE A 1 298 ? 5.773 42.405 40.808 1.00 15.85 ? 316 PHE A CA 1 ATOM 2071 C C . PHE A 1 298 ? 7.084 42.455 41.550 1.00 16.21 ? 316 PHE A C 1 ATOM 2072 O O . PHE A 1 298 ? 7.416 43.465 42.194 1.00 16.50 ? 316 PHE A O 1 ATOM 2073 C CB . PHE A 1 298 ? 5.945 42.932 39.378 1.00 16.35 ? 316 PHE A CB 1 ATOM 2074 C CG . PHE A 1 298 ? 6.595 41.941 38.456 1.00 16.85 ? 316 PHE A CG 1 ATOM 2075 C CD1 . PHE A 1 298 ? 5.834 40.954 37.837 1.00 17.16 ? 316 PHE A CD1 1 ATOM 2076 C CD2 . PHE A 1 298 ? 7.968 41.964 38.231 1.00 17.92 ? 316 PHE A CD2 1 ATOM 2077 C CE1 . PHE A 1 298 ? 6.429 40.013 36.999 1.00 17.88 ? 316 PHE A CE1 1 ATOM 2078 C CE2 . PHE A 1 298 ? 8.567 41.033 37.383 1.00 17.97 ? 316 PHE A CE2 1 ATOM 2079 C CZ . PHE A 1 298 ? 7.796 40.049 36.778 1.00 17.61 ? 316 PHE A CZ 1 ATOM 2080 N N . GLN A 1 299 ? 7.856 41.374 41.464 1.00 15.70 ? 317 GLN A N 1 ATOM 2081 C CA . GLN A 1 299 ? 9.109 41.341 42.179 1.00 16.04 ? 317 GLN A CA 1 ATOM 2082 C C . GLN A 1 299 ? 10.140 40.573 41.382 1.00 16.43 ? 317 GLN A C 1 ATOM 2083 O O . GLN A 1 299 ? 9.826 39.542 40.792 1.00 16.14 ? 317 GLN A O 1 ATOM 2084 C CB . GLN A 1 299 ? 8.918 40.713 43.566 1.00 16.62 ? 317 GLN A CB 1 ATOM 2085 C CG . GLN A 1 299 ? 10.180 40.685 44.405 1.00 17.81 ? 317 GLN A CG 1 ATOM 2086 C CD . GLN A 1 299 ? 9.958 40.167 45.808 1.00 19.03 ? 317 GLN A CD 1 ATOM 2087 O OE1 . GLN A 1 299 ? 8.903 39.599 46.121 1.00 20.02 ? 317 GLN A OE1 1 ATOM 2088 N NE2 . GLN A 1 299 ? 10.965 40.334 46.665 1.00 19.63 ? 317 GLN A NE2 1 ATOM 2089 N N . ILE A 1 300 ? 11.358 41.106 41.340 1.00 14.98 ? 318 ILE A N 1 ATOM 2090 C CA . ILE A 1 300 ? 12.481 40.350 40.835 1.00 15.13 ? 318 ILE A CA 1 ATOM 2091 C C . ILE A 1 300 ? 13.469 40.188 41.971 1.00 15.66 ? 318 ILE A C 1 ATOM 2092 O O . ILE A 1 300 ? 13.914 41.184 42.582 1.00 16.09 ? 318 ILE A O 1 ATOM 2093 C CB . ILE A 1 300 ? 13.163 41.035 39.636 1.00 15.25 ? 318 ILE A CB 1 ATOM 2094 C CG1 . ILE A 1 300 ? 12.188 41.127 38.445 1.00 15.85 ? 318 ILE A CG1 1 ATOM 2095 C CG2 . ILE A 1 300 ? 14.415 40.252 39.242 1.00 14.53 ? 318 ILE A CG2 1 ATOM 2096 C CD1 . ILE A 1 300 ? 12.726 41.960 37.294 1.00 16.64 ? 318 ILE A CD1 1 ATOM 2097 N N . GLN A 1 301 ? 13.811 38.932 42.242 1.00 15.11 ? 319 GLN A N 1 ATOM 2098 C CA . GLN A 1 301 ? 14.812 38.591 43.231 1.00 15.55 ? 319 GLN A CA 1 ATOM 2099 C C . GLN A 1 301 ? 16.002 38.000 42.518 1.00 15.73 ? 319 GLN A C 1 ATOM 2100 O O . GLN A 1 301 ? 15.853 37.055 41.741 1.00 15.29 ? 319 GLN A O 1 ATOM 2101 C CB . GLN A 1 301 ? 14.252 37.577 44.240 1.00 16.38 ? 319 GLN A CB 1 ATOM 2102 C CG . GLN A 1 301 ? 13.204 38.166 45.174 1.00 17.43 ? 319 GLN A CG 1 ATOM 2103 C CD . GLN A 1 301 ? 12.451 37.080 45.921 1.00 19.19 ? 319 GLN A CD 1 ATOM 2104 O OE1 . GLN A 1 301 ? 12.913 36.593 46.955 1.00 22.54 ? 319 GLN A OE1 1 ATOM 2105 N NE2 . GLN A 1 301 ? 11.308 36.683 45.393 1.00 19.10 ? 319 GLN A NE2 1 ATOM 2106 N N . SER A 1 302 ? 17.184 38.568 42.768 1.00 15.86 ? 320 SER A N 1 ATOM 2107 C CA . SER A 1 302 ? 18.415 38.083 42.155 1.00 17.10 ? 320 SER A CA 1 ATOM 2108 C C . SER A 1 302 ? 19.404 37.589 43.212 1.00 18.30 ? 320 SER A C 1 ATOM 2109 O O . SER A 1 302 ? 20.498 37.119 42.883 1.00 18.89 ? 320 SER A O 1 ATOM 2110 C CB . SER A 1 302 ? 19.068 39.195 41.336 1.00 17.43 ? 320 SER A CB 1 ATOM 2111 O OG . SER A 1 302 ? 19.350 40.312 42.159 1.00 17.18 ? 320 SER A OG 1 ATOM 2112 N N . CYS A 1 303 ? 19.009 37.701 44.473 1.00 20.12 ? 321 CYS A N 1 ATOM 2113 C CA . CYS A 1 303 ? 19.845 37.272 45.598 1.00 22.17 ? 321 CYS A CA 1 ATOM 2114 C C . CYS A 1 303 ? 19.100 36.179 46.379 1.00 21.74 ? 321 CYS A C 1 ATOM 2115 O O . CYS A 1 303 ? 19.197 36.085 47.609 1.00 21.07 ? 321 CYS A O 1 ATOM 2116 C CB . CYS A 1 303 ? 20.172 38.480 46.486 1.00 26.10 ? 321 CYS A CB 1 ATOM 2117 S SG . CYS A 1 303 ? 21.482 38.203 47.712 1.00 33.31 ? 321 CYS A SG 1 ATOM 2118 N N . TYR A 1 304 ? 18.348 35.353 45.656 1.00 20.37 ? 322 TYR A N 1 ATOM 2119 C CA . TYR A 1 304 ? 17.545 34.324 46.303 1.00 20.94 ? 322 TYR A CA 1 ATOM 2120 C C . TYR A 1 304 ? 18.417 33.328 47.060 1.00 21.51 ? 322 TYR A C 1 ATOM 2121 O O . TYR A 1 304 ? 19.412 32.833 46.525 1.00 21.69 ? 322 TYR A O 1 ATOM 2122 C CB . TYR A 1 304 ? 16.675 33.587 45.293 1.00 20.91 ? 322 TYR A CB 1 ATOM 2123 C CG . TYR A 1 304 ? 15.688 32.662 45.955 1.00 21.85 ? 322 TYR A CG 1 ATOM 2124 C CD1 . TYR A 1 304 ? 14.536 33.165 46.561 1.00 22.60 ? 322 TYR A CD1 1 ATOM 2125 C CD2 . TYR A 1 304 ? 15.911 31.286 45.985 1.00 21.93 ? 322 TYR A CD2 1 ATOM 2126 C CE1 . TYR A 1 304 ? 13.630 32.319 47.176 1.00 24.24 ? 322 TYR A CE1 1 ATOM 2127 C CE2 . TYR A 1 304 ? 15.009 30.425 46.595 1.00 23.57 ? 322 TYR A CE2 1 ATOM 2128 C CZ . TYR A 1 304 ? 13.872 30.952 47.183 1.00 24.37 ? 322 TYR A CZ 1 ATOM 2129 O OH . TYR A 1 304 ? 12.973 30.100 47.783 1.00 26.93 ? 322 TYR A OH 1 ATOM 2130 N N . GLY A 1 305 ? 18.035 33.047 48.304 1.00 22.48 ? 323 GLY A N 1 ATOM 2131 C CA . GLY A 1 305 ? 18.722 32.039 49.114 1.00 23.66 ? 323 GLY A CA 1 ATOM 2132 C C . GLY A 1 305 ? 20.024 32.506 49.740 1.00 25.20 ? 323 GLY A C 1 ATOM 2133 O O . GLY A 1 305 ? 20.750 31.707 50.326 1.00 26.81 ? 323 GLY A O 1 ATOM 2134 N N . GLU A 1 306 ? 20.332 33.792 49.612 1.00 25.47 ? 324 GLU A N 1 ATOM 2135 C CA . GLU A 1 306 ? 21.575 34.342 50.163 1.00 27.00 ? 324 GLU A CA 1 ATOM 2136 C C . GLU A 1 306 ? 21.317 35.725 50.752 1.00 29.15 ? 324 GLU A C 1 ATOM 2137 O O . GLU A 1 306 ? 20.205 36.242 50.648 1.00 27.90 ? 324 GLU A O 1 ATOM 2138 C CB . GLU A 1 306 ? 22.680 34.381 49.093 1.00 26.49 ? 324 GLU A CB 1 ATOM 2139 C CG . GLU A 1 306 ? 22.921 33.060 48.356 1.00 26.77 ? 324 GLU A CG 1 ATOM 2140 C CD . GLU A 1 306 ? 23.674 32.006 49.161 1.00 28.43 ? 324 GLU A CD 1 ATOM 2141 O OE1 . GLU A 1 306 ? 24.038 32.260 50.325 1.00 29.98 ? 324 GLU A OE1 1 ATOM 2142 O OE2 . GLU A 1 306 ? 23.923 30.908 48.623 1.00 28.96 ? 324 GLU A OE2 1 ATOM 2143 N N . ASP A 1 307 ? 22.318 36.314 51.409 1.00 32.01 ? 325 ASP A N 1 ATOM 2144 C CA . ASP A 1 307 ? 22.142 37.668 51.942 1.00 34.38 ? 325 ASP A CA 1 ATOM 2145 C C . ASP A 1 307 ? 22.853 38.741 51.116 1.00 34.76 ? 325 ASP A C 1 ATOM 2146 O O . ASP A 1 307 ? 23.597 38.430 50.185 1.00 33.20 ? 325 ASP A O 1 ATOM 2147 C CB . ASP A 1 307 ? 22.505 37.757 53.437 1.00 37.56 ? 325 ASP A CB 1 ATOM 2148 C CG . ASP A 1 307 ? 23.957 37.397 53.729 1.00 38.93 ? 325 ASP A CG 1 ATOM 2149 O OD1 . ASP A 1 307 ? 24.856 37.657 52.899 1.00 39.30 ? 325 ASP A OD1 1 ATOM 2150 O OD2 . ASP A 1 307 ? 24.202 36.858 54.827 1.00 42.46 ? 325 ASP A OD2 1 ATOM 2151 N N . ASP A 1 308 ? 22.608 40.002 51.470 1.00 37.35 ? 326 ASP A N 1 ATOM 2152 C CA . ASP A 1 308 ? 23.157 41.152 50.745 1.00 39.61 ? 326 ASP A CA 1 ATOM 2153 C C . ASP A 1 308 ? 24.674 41.134 50.600 1.00 39.55 ? 326 ASP A C 1 ATOM 2154 O O . ASP A 1 308 ? 25.190 41.407 49.516 1.00 38.95 ? 326 ASP A O 1 ATOM 2155 C CB . ASP A 1 308 ? 22.693 42.469 51.381 1.00 43.34 ? 326 ASP A CB 1 ATOM 2156 C CG . ASP A 1 308 ? 21.198 42.708 51.209 1.00 48.23 ? 326 ASP A CG 1 ATOM 2157 O OD1 . ASP A 1 308 ? 20.509 41.829 50.646 1.00 50.79 ? 326 ASP A OD1 1 ATOM 2158 O OD2 . ASP A 1 308 ? 20.703 43.776 51.634 1.00 50.64 ? 326 ASP A OD2 1 ATOM 2159 N N . ASP A 1 309 ? 25.387 40.814 51.681 1.00 39.04 ? 327 ASP A N 1 ATOM 2160 C CA . ASP A 1 309 ? 26.853 40.789 51.646 1.00 39.89 ? 327 ASP A CA 1 ATOM 2161 C C . ASP A 1 309 ? 27.396 39.714 50.717 1.00 36.53 ? 327 ASP A C 1 ATOM 2162 O O . ASP A 1 309 ? 28.417 39.917 50.051 1.00 37.12 ? 327 ASP A O 1 ATOM 2163 C CB . ASP A 1 309 ? 27.440 40.613 53.050 1.00 44.05 ? 327 ASP A CB 1 ATOM 2164 C CG . ASP A 1 309 ? 27.311 41.868 53.897 1.00 46.96 ? 327 ASP A CG 1 ATOM 2165 O OD1 . ASP A 1 309 ? 27.068 42.964 53.343 1.00 48.83 ? 327 ASP A OD1 1 ATOM 2166 O OD2 . ASP A 1 309 ? 27.451 41.753 55.129 1.00 50.13 ? 327 ASP A OD2 1 ATOM 2167 N N . TYR A 1 310 ? 26.708 38.575 50.679 1.00 33.73 ? 328 TYR A N 1 ATOM 2168 C CA . TYR A 1 310 ? 27.070 37.483 49.787 1.00 32.31 ? 328 TYR A CA 1 ATOM 2169 C C . TYR A 1 310 ? 26.932 37.937 48.335 1.00 31.11 ? 328 TYR A C 1 ATOM 2170 O O . TYR A 1 310 ? 27.794 37.653 47.492 1.00 31.37 ? 328 TYR A O 1 ATOM 2171 C CB . TYR A 1 310 ? 26.189 36.253 50.046 1.00 31.42 ? 328 TYR A CB 1 ATOM 2172 C CG . TYR A 1 310 ? 26.534 35.087 49.156 1.00 31.00 ? 328 TYR A CG 1 ATOM 2173 C CD1 . TYR A 1 310 ? 26.013 34.991 47.861 1.00 30.62 ? 328 TYR A CD1 1 ATOM 2174 C CD2 . TYR A 1 310 ? 27.398 34.088 49.594 1.00 30.60 ? 328 TYR A CD2 1 ATOM 2175 C CE1 . TYR A 1 310 ? 26.341 33.930 47.039 1.00 30.23 ? 328 TYR A CE1 1 ATOM 2176 C CE2 . TYR A 1 310 ? 27.734 33.022 48.778 1.00 31.24 ? 328 TYR A CE2 1 ATOM 2177 C CZ . TYR A 1 310 ? 27.201 32.948 47.504 1.00 30.96 ? 328 TYR A CZ 1 ATOM 2178 O OH . TYR A 1 310 ? 27.534 31.891 46.696 1.00 32.46 ? 328 TYR A OH 1 ATOM 2179 N N . CYS A 1 311 ? 25.848 38.650 48.050 1.00 31.82 ? 329 CYS A N 1 ATOM 2180 C CA . CYS A 1 311 ? 25.547 39.056 46.682 1.00 33.79 ? 329 CYS A CA 1 ATOM 2181 C C . CYS A 1 311 ? 26.436 40.189 46.186 1.00 35.53 ? 329 CYS A C 1 ATOM 2182 O O . CYS A 1 311 ? 26.663 40.319 44.983 1.00 34.10 ? 329 CYS A O 1 ATOM 2183 C CB . CYS A 1 311 ? 24.051 39.337 46.512 1.00 34.38 ? 329 CYS A CB 1 ATOM 2184 S SG . CYS A 1 311 ? 23.131 37.778 46.596 1.00 38.11 ? 329 CYS A SG 1 ATOM 2185 N N . GLU A 1 312 ? 26.957 40.990 47.115 1.00 37.03 ? 330 GLU A N 1 ATOM 2186 C CA . GLU A 1 312 ? 27.979 41.982 46.784 1.00 40.35 ? 330 GLU A CA 1 ATOM 2187 C C . GLU A 1 312 ? 29.246 41.313 46.249 1.00 38.56 ? 330 GLU A C 1 ATOM 2188 O O . GLU A 1 312 ? 29.824 41.775 45.267 1.00 40.90 ? 330 GLU A O 1 ATOM 2189 C CB . GLU A 1 312 ? 28.306 42.856 47.994 1.00 43.37 ? 330 GLU A CB 1 ATOM 2190 C CG . GLU A 1 312 ? 27.234 43.886 48.309 1.00 48.60 ? 330 GLU A CG 1 ATOM 2191 C CD . GLU A 1 312 ? 27.589 44.749 49.506 1.00 52.44 ? 330 GLU A CD 1 ATOM 2192 O OE1 . GLU A 1 312 ? 28.776 45.117 49.643 1.00 55.75 ? 330 GLU A OE1 1 ATOM 2193 O OE2 . GLU A 1 312 ? 26.680 45.061 50.308 1.00 53.96 ? 330 GLU A OE2 1 ATOM 2194 N N . GLU A 1 313 ? 29.657 40.218 46.883 1.00 37.77 ? 331 GLU A N 1 ATOM 2195 C CA . GLU A 1 313 ? 30.839 39.471 46.453 1.00 38.18 ? 331 GLU A CA 1 ATOM 2196 C C . GLU A 1 313 ? 30.538 38.464 45.339 1.00 35.21 ? 331 GLU A C 1 ATOM 2197 O O . GLU A 1 313 ? 31.435 38.075 44.590 1.00 32.95 ? 331 GLU A O 1 ATOM 2198 C CB . GLU A 1 313 ? 31.505 38.761 47.645 1.00 43.74 ? 331 GLU A CB 1 ATOM 2199 C CG . GLU A 1 313 ? 31.757 39.640 48.874 1.00 49.41 ? 331 GLU A CG 1 ATOM 2200 C CD . GLU A 1 313 ? 33.023 40.497 48.790 1.00 54.02 ? 331 GLU A CD 1 ATOM 2201 O OE1 . GLU A 1 313 ? 33.673 40.544 47.720 1.00 56.33 ? 331 GLU A OE1 1 ATOM 2202 O OE2 . GLU A 1 313 ? 33.376 41.134 49.812 1.00 55.87 ? 331 GLU A OE2 1 ATOM 2203 N N . ASN A 1 314 ? 29.275 38.042 45.234 1.00 32.25 ? 332 ASN A N 1 ATOM 2204 C CA . ASN A 1 314 ? 28.860 37.056 44.238 1.00 29.47 ? 332 ASN A CA 1 ATOM 2205 C C . ASN A 1 314 ? 27.628 37.545 43.477 1.00 28.21 ? 332 ASN A C 1 ATOM 2206 O O . ASN A 1 314 ? 26.504 37.126 43.785 1.00 26.11 ? 332 ASN A O 1 ATOM 2207 C CB . ASN A 1 314 ? 28.543 35.720 44.908 1.00 30.05 ? 332 ASN A CB 1 ATOM 2208 C CG . ASN A 1 314 ? 29.721 35.162 45.680 1.00 30.40 ? 332 ASN A CG 1 ATOM 2209 O OD1 . ASN A 1 314 ? 30.602 34.518 45.111 1.00 30.62 ? 332 ASN A OD1 1 ATOM 2210 N ND2 . ASN A 1 314 ? 29.731 35.392 46.983 1.00 29.69 ? 332 ASN A ND2 1 ATOM 2211 N N . PRO A 1 315 ? 27.830 38.432 42.490 1.00 26.61 ? 333 PRO A N 1 ATOM 2212 C CA . PRO A 1 315 ? 26.684 39.083 41.864 1.00 25.34 ? 333 PRO A CA 1 ATOM 2213 C C . PRO A 1 315 ? 25.815 38.109 41.070 1.00 23.23 ? 333 PRO A C 1 ATOM 2214 O O . PRO A 1 315 ? 26.291 37.066 40.605 1.00 22.44 ? 333 PRO A O 1 ATOM 2215 C CB . PRO A 1 315 ? 27.330 40.120 40.928 1.00 26.90 ? 333 PRO A CB 1 ATOM 2216 C CG . PRO A 1 315 ? 28.731 40.279 41.435 1.00 27.54 ? 333 PRO A CG 1 ATOM 2217 C CD . PRO A 1 315 ? 29.104 38.915 41.919 1.00 28.36 ? 333 PRO A CD 1 ATOM 2218 N N . GLY A 1 316 ? 24.542 38.457 40.933 1.00 21.55 ? 334 GLY A N 1 ATOM 2219 C CA . GLY A 1 316 ? 23.638 37.700 40.081 1.00 20.80 ? 334 GLY A CA 1 ATOM 2220 C C . GLY A 1 316 ? 23.954 37.985 38.623 1.00 20.01 ? 334 GLY A C 1 ATOM 2221 O O . GLY A 1 316 ? 24.305 39.115 38.266 1.00 19.76 ? 334 GLY A O 1 ATOM 2222 N N . ASN A 1 317 ? 23.852 36.958 37.783 1.00 18.95 ? 335 ASN A N 1 ATOM 2223 C CA . ASN A 1 317 ? 24.096 37.112 36.343 1.00 19.34 ? 335 ASN A CA 1 ATOM 2224 C C . ASN A 1 317 ? 23.008 36.469 35.494 1.00 17.67 ? 335 ASN A C 1 ATOM 2225 O O . ASN A 1 317 ? 23.237 36.027 34.361 1.00 16.48 ? 335 ASN A O 1 ATOM 2226 C CB . ASN A 1 317 ? 25.498 36.627 35.943 1.00 21.51 ? 335 ASN A CB 1 ATOM 2227 C CG . ASN A 1 317 ? 25.795 35.212 36.407 1.00 24.81 ? 335 ASN A CG 1 ATOM 2228 O OD1 . ASN A 1 317 ? 24.898 34.373 36.526 1.00 24.09 ? 335 ASN A OD1 1 ATOM 2229 N ND2 . ASN A 1 317 ? 27.074 34.945 36.697 1.00 27.75 ? 335 ASN A ND2 1 ATOM 2230 N N . ALA A 1 318 ? 21.795 36.444 36.044 1.00 16.91 ? 336 ALA A N 1 ATOM 2231 C CA . ALA A 1 318 ? 20.672 35.859 35.324 1.00 15.63 ? 336 ALA A CA 1 ATOM 2232 C C . ALA A 1 318 ? 20.439 36.585 33.995 1.00 15.64 ? 336 ALA A C 1 ATOM 2233 O O . ALA A 1 318 ? 20.589 37.801 33.899 1.00 16.98 ? 336 ALA A O 1 ATOM 2234 C CB . ALA A 1 318 ? 19.414 35.888 36.182 1.00 15.79 ? 336 ALA A CB 1 ATOM 2235 N N . LYS A 1 319 ? 20.104 35.821 32.968 1.00 14.87 ? 337 LYS A N 1 ATOM 2236 C CA . LYS A 1 319 ? 19.801 36.380 31.670 1.00 15.66 ? 337 LYS A CA 1 ATOM 2237 C C . LYS A 1 319 ? 18.300 36.388 31.452 1.00 14.85 ? 337 LYS A C 1 ATOM 2238 O O . LYS A 1 319 ? 17.729 35.377 31.050 1.00 14.43 ? 337 LYS A O 1 ATOM 2239 C CB . LYS A 1 319 ? 20.494 35.574 30.565 1.00 17.16 ? 337 LYS A CB 1 ATOM 2240 C CG . LYS A 1 319 ? 20.417 36.264 29.215 1.00 19.73 ? 337 LYS A CG 1 ATOM 2241 C CD . LYS A 1 319 ? 21.021 35.410 28.108 1.00 22.70 ? 337 LYS A CD 1 ATOM 2242 C CE . LYS A 1 319 ? 20.768 36.039 26.741 1.00 24.70 ? 337 LYS A CE 1 ATOM 2243 N NZ . LYS A 1 319 ? 21.495 35.274 25.676 1.00 26.91 ? 337 LYS A NZ 1 ATOM 2244 N N . LEU A 1 320 ? 17.679 37.534 31.727 1.00 14.88 ? 338 LEU A N 1 ATOM 2245 C CA . LEU A 1 320 ? 16.258 37.711 31.537 1.00 14.58 ? 338 LEU A CA 1 ATOM 2246 C C . LEU A 1 320 ? 16.061 38.518 30.270 1.00 15.23 ? 338 LEU A C 1 ATOM 2247 O O . LEU A 1 320 ? 16.601 39.620 30.141 1.00 15.09 ? 338 LEU A O 1 ATOM 2248 C CB . LEU A 1 320 ? 15.636 38.440 32.738 1.00 15.31 ? 338 LEU A CB 1 ATOM 2249 C CG . LEU A 1 320 ? 16.112 38.027 34.150 1.00 16.05 ? 338 LEU A CG 1 ATOM 2250 C CD1 . LEU A 1 320 ? 15.406 38.859 35.211 1.00 16.93 ? 338 LEU A CD1 1 ATOM 2251 C CD2 . LEU A 1 320 ? 15.904 36.549 34.432 1.00 15.98 ? 338 LEU A CD2 1 ATOM 2252 N N . THR A 1 321 ? 15.331 37.962 29.320 1.00 14.36 ? 339 THR A N 1 ATOM 2253 C CA . THR A 1 321 ? 15.051 38.686 28.081 1.00 15.46 ? 339 THR A CA 1 ATOM 2254 C C . THR A 1 321 ? 13.593 38.530 27.682 1.00 15.86 ? 339 THR A C 1 ATOM 2255 O O . THR A 1 321 ? 12.969 37.489 27.961 1.00 14.71 ? 339 THR A O 1 ATOM 2256 C CB . THR A 1 321 ? 15.960 38.221 26.907 1.00 16.54 ? 339 THR A CB 1 ATOM 2257 O OG1 . THR A 1 321 ? 15.801 36.814 26.708 1.00 17.23 ? 339 THR A OG1 1 ATOM 2258 C CG2 . THR A 1 321 ? 17.429 38.539 27.180 1.00 16.59 ? 339 THR A CG2 1 ATOM 2259 N N . ASP A 1 322 ? 13.057 39.566 27.033 1.00 15.46 ? 340 ASP A N 1 ATOM 2260 C CA A ASP A 1 322 ? 11.674 39.563 26.555 0.50 15.78 ? 340 ASP A CA 1 ATOM 2261 C CA B ASP A 1 322 ? 11.683 39.534 26.537 0.50 15.64 ? 340 ASP A CA 1 ATOM 2262 C C . ASP A 1 322 ? 10.709 39.179 27.671 1.00 15.45 ? 340 ASP A C 1 ATOM 2263 O O . ASP A 1 322 ? 9.829 38.316 27.503 1.00 15.36 ? 340 ASP A O 1 ATOM 2264 C CB A ASP A 1 322 ? 11.511 38.659 25.328 0.50 17.07 ? 340 ASP A CB 1 ATOM 2265 C CB B ASP A 1 322 ? 11.572 38.545 25.363 0.50 16.73 ? 340 ASP A CB 1 ATOM 2266 C CG A ASP A 1 322 ? 12.182 39.230 24.100 0.50 18.12 ? 340 ASP A CG 1 ATOM 2267 C CG B ASP A 1 322 ? 10.259 38.654 24.617 0.50 17.31 ? 340 ASP A CG 1 ATOM 2268 O OD1 A ASP A 1 322 ? 11.915 40.402 23.770 0.50 19.28 ? 340 ASP A OD1 1 ATOM 2269 O OD1 B ASP A 1 322 ? 9.616 39.722 24.665 0.50 18.94 ? 340 ASP A OD1 1 ATOM 2270 O OD2 A ASP A 1 322 ? 12.977 38.518 23.463 0.50 18.96 ? 340 ASP A OD2 1 ATOM 2271 O OD2 B ASP A 1 322 ? 9.863 37.661 23.979 0.50 18.40 ? 340 ASP A OD2 1 ATOM 2272 N N . ILE A 1 323 ? 10.883 39.836 28.811 1.00 14.47 ? 341 ILE A N 1 ATOM 2273 C CA . ILE A 1 323 ? 9.949 39.707 29.932 1.00 14.49 ? 341 ILE A CA 1 ATOM 2274 C C . ILE A 1 323 ? 8.963 40.857 29.773 1.00 14.32 ? 341 ILE A C 1 ATOM 2275 O O . ILE A 1 323 ? 9.363 42.013 29.642 1.00 14.24 ? 341 ILE A O 1 ATOM 2276 C CB . ILE A 1 323 ? 10.630 39.801 31.312 1.00 14.67 ? 341 ILE A CB 1 ATOM 2277 C CG1 . ILE A 1 323 ? 11.890 38.910 31.385 1.00 14.95 ? 341 ILE A CG1 1 ATOM 2278 C CG2 . ILE A 1 323 ? 9.613 39.507 32.431 1.00 14.79 ? 341 ILE A CG2 1 ATOM 2279 C CD1 . ILE A 1 323 ? 11.665 37.425 31.165 1.00 15.00 ? 341 ILE A CD1 1 ATOM 2280 N N . VAL A 1 324 ? 7.680 40.527 29.738 1.00 13.67 ? 342 VAL A N 1 ATOM 2281 C CA . VAL A 1 324 ? 6.651 41.553 29.533 1.00 14.22 ? 342 VAL A CA 1 ATOM 2282 C C . VAL A 1 324 ? 5.677 41.515 30.702 1.00 14.92 ? 342 VAL A C 1 ATOM 2283 O O . VAL A 1 324 ? 5.166 40.447 31.063 1.00 14.72 ? 342 VAL A O 1 ATOM 2284 C CB . VAL A 1 324 ? 5.912 41.337 28.201 1.00 14.64 ? 342 VAL A CB 1 ATOM 2285 C CG1 . VAL A 1 324 ? 4.734 42.314 28.079 1.00 15.04 ? 342 VAL A CG1 1 ATOM 2286 C CG2 . VAL A 1 324 ? 6.888 41.487 27.032 1.00 14.41 ? 342 VAL A CG2 1 ATOM 2287 N N . VAL A 1 325 ? 5.435 42.683 31.287 1.00 15.04 ? 343 VAL A N 1 ATOM 2288 C CA . VAL A 1 325 ? 4.477 42.829 32.379 1.00 15.57 ? 343 VAL A CA 1 ATOM 2289 C C . VAL A 1 325 ? 3.489 43.853 31.836 1.00 16.90 ? 343 VAL A C 1 ATOM 2290 O O . VAL A 1 325 ? 3.852 45.022 31.635 1.00 18.41 ? 343 VAL A O 1 ATOM 2291 C CB . VAL A 1 325 ? 5.177 43.326 33.662 1.00 15.54 ? 343 VAL A CB 1 ATOM 2292 C CG1 . VAL A 1 325 ? 4.187 43.695 34.767 1.00 16.25 ? 343 VAL A CG1 1 ATOM 2293 C CG2 . VAL A 1 325 ? 6.175 42.299 34.173 1.00 16.26 ? 343 VAL A CG2 1 ATOM 2294 N N . SER A 1 326 ? 2.262 43.418 31.572 1.00 16.52 ? 344 SER A N 1 ATOM 2295 C CA . SER A 1 326 ? 1.279 44.294 30.923 1.00 17.65 ? 344 SER A CA 1 ATOM 2296 C C . SER A 1 326 ? -0.090 44.235 31.583 1.00 18.13 ? 344 SER A C 1 ATOM 2297 O O . SER A 1 326 ? -0.554 43.163 31.967 1.00 16.66 ? 344 SER A O 1 ATOM 2298 C CB . SER A 1 326 ? 1.162 43.965 29.433 1.00 18.35 ? 344 SER A CB 1 ATOM 2299 O OG . SER A 1 326 ? 0.898 42.577 29.202 1.00 19.30 ? 344 SER A OG 1 ATOM 2300 N N . SER A 1 327 ? -0.722 45.403 31.714 1.00 18.92 ? 345 SER A N 1 ATOM 2301 C CA . SER A 1 327 ? -2.085 45.519 32.222 1.00 19.80 ? 345 SER A CA 1 ATOM 2302 C C . SER A 1 327 ? -2.219 44.943 33.617 1.00 19.35 ? 345 SER A C 1 ATOM 2303 O O . SER A 1 327 ? -2.920 43.944 33.815 1.00 19.35 ? 345 SER A O 1 ATOM 2304 C CB . SER A 1 327 ? -3.081 44.845 31.270 1.00 21.21 ? 345 SER A CB 1 ATOM 2305 O OG . SER A 1 327 ? -3.133 45.507 30.024 1.00 24.65 ? 345 SER A OG 1 ATOM 2306 N N . PHE A 1 328 ? -1.512 45.538 34.572 1.00 18.97 ? 346 PHE A N 1 ATOM 2307 C CA . PHE A 1 328 ? -1.685 45.207 35.975 1.00 18.85 ? 346 PHE A CA 1 ATOM 2308 C C . PHE A 1 328 ? -2.528 46.306 36.611 1.00 20.97 ? 346 PHE A C 1 ATOM 2309 O O . PHE A 1 328 ? -2.256 47.501 36.424 1.00 22.04 ? 346 PHE A O 1 ATOM 2310 C CB . PHE A 1 328 ? -0.344 45.134 36.701 1.00 17.27 ? 346 PHE A CB 1 ATOM 2311 C CG . PHE A 1 328 ? 0.345 43.793 36.609 1.00 16.46 ? 346 PHE A CG 1 ATOM 2312 C CD1 . PHE A 1 328 ? 0.485 43.132 35.388 1.00 16.58 ? 346 PHE A CD1 1 ATOM 2313 C CD2 . PHE A 1 328 ? 0.890 43.210 37.756 1.00 16.24 ? 346 PHE A CD2 1 ATOM 2314 C CE1 . PHE A 1 328 ? 1.140 41.905 35.313 1.00 15.95 ? 346 PHE A CE1 1 ATOM 2315 C CE2 . PHE A 1 328 ? 1.553 41.986 37.687 1.00 16.16 ? 346 PHE A CE2 1 ATOM 2316 C CZ . PHE A 1 328 ? 1.673 41.331 36.467 1.00 16.26 ? 346 PHE A CZ 1 ATOM 2317 N N . SER A 1 329 ? -3.527 45.906 37.381 1.00 20.29 ? 347 SER A N 1 ATOM 2318 C CA . SER A 1 329 ? -4.321 46.886 38.112 1.00 21.76 ? 347 SER A CA 1 ATOM 2319 C C . SER A 1 329 ? -4.580 46.435 39.539 1.00 22.23 ? 347 SER A C 1 ATOM 2320 O O . SER A 1 329 ? -4.279 45.294 39.908 1.00 20.99 ? 347 SER A O 1 ATOM 2321 C CB . SER A 1 329 ? -5.625 47.164 37.368 1.00 22.83 ? 347 SER A CB 1 ATOM 2322 O OG . SER A 1 329 ? -6.395 45.977 37.253 1.00 25.80 ? 347 SER A OG 1 ATOM 2323 N N . GLY A 1 330 ? -5.122 47.342 40.342 1.00 21.52 ? 348 GLY A N 1 ATOM 2324 C CA . GLY A 1 330 ? -5.486 47.033 41.706 1.00 22.09 ? 348 GLY A CA 1 ATOM 2325 C C . GLY A 1 330 ? -4.653 47.754 42.735 1.00 22.84 ? 348 GLY A C 1 ATOM 2326 O O . GLY A 1 330 ? -3.984 48.750 42.433 1.00 23.66 ? 348 GLY A O 1 ATOM 2327 N N . THR A 1 331 ? -4.699 47.234 43.957 1.00 22.18 ? 349 THR A N 1 ATOM 2328 C CA . THR A 1 331 ? -4.140 47.886 45.122 1.00 22.82 ? 349 THR A CA 1 ATOM 2329 C C . THR A 1 331 ? -3.345 46.861 45.899 1.00 22.75 ? 349 THR A C 1 ATOM 2330 O O . THR A 1 331 ? -3.835 45.755 46.159 1.00 22.69 ? 349 THR A O 1 ATOM 2331 C CB . THR A 1 331 ? -5.269 48.445 46.030 1.00 23.79 ? 349 THR A CB 1 ATOM 2332 O OG1 . THR A 1 331 ? -6.211 49.164 45.223 1.00 25.30 ? 349 THR A OG1 1 ATOM 2333 C CG2 . THR A 1 331 ? -4.718 49.377 47.087 1.00 25.08 ? 349 THR A CG2 1 ATOM 2334 N N . THR A 1 332 ? -2.126 47.233 46.277 1.00 21.27 ? 350 THR A N 1 ATOM 2335 C CA . THR A 1 332 ? -1.301 46.391 47.128 1.00 21.04 ? 350 THR A CA 1 ATOM 2336 C C . THR A 1 332 ? -1.740 46.502 48.592 1.00 21.40 ? 350 THR A C 1 ATOM 2337 O O . THR A 1 332 ? -2.616 47.298 48.931 1.00 20.64 ? 350 THR A O 1 ATOM 2338 C CB . THR A 1 332 ? 0.198 46.729 47.009 1.00 21.08 ? 350 THR A CB 1 ATOM 2339 O OG1 . THR A 1 332 ? 0.399 48.136 47.220 1.00 21.21 ? 350 THR A OG1 1 ATOM 2340 C CG2 . THR A 1 332 ? 0.746 46.332 45.625 1.00 19.80 ? 350 THR A CG2 1 ATOM 2341 N N . SER A 1 333 ? -1.118 45.697 49.443 1.00 21.36 ? 351 SER A N 1 ATOM 2342 C CA . SER A 1 333 ? -1.346 45.732 50.877 1.00 22.33 ? 351 SER A CA 1 ATOM 2343 C C . SER A 1 333 ? -0.628 46.918 51.527 1.00 23.05 ? 351 SER A C 1 ATOM 2344 O O . SER A 1 333 ? 0.136 47.629 50.870 1.00 22.28 ? 351 SER A O 1 ATOM 2345 C CB . SER A 1 333 ? -0.825 44.441 51.504 1.00 22.15 ? 351 SER A CB 1 ATOM 2346 O OG . SER A 1 333 ? 0.589 44.463 51.563 1.00 21.81 ? 351 SER A OG 1 ATOM 2347 N N . ASP A 1 334 ? -0.855 47.091 52.829 1.00 24.49 ? 352 ASP A N 1 ATOM 2348 C CA . ASP A 1 334 ? -0.152 48.087 53.644 1.00 25.74 ? 352 ASP A CA 1 ATOM 2349 C C . ASP A 1 334 ? 1.324 47.779 53.818 1.00 24.66 ? 352 ASP A C 1 ATOM 2350 O O . ASP A 1 334 ? 2.101 48.664 54.155 1.00 25.24 ? 352 ASP A O 1 ATOM 2351 C CB . ASP A 1 334 ? -0.756 48.144 55.057 1.00 28.82 ? 352 ASP A CB 1 ATOM 2352 C CG . ASP A 1 334 ? -2.163 48.674 55.075 1.00 32.81 ? 352 ASP A CG 1 ATOM 2353 O OD1 . ASP A 1 334 ? -2.510 49.528 54.228 1.00 35.10 ? 352 ASP A OD1 1 ATOM 2354 O OD2 . ASP A 1 334 ? -2.932 48.240 55.962 1.00 34.98 ? 352 ASP A OD2 1 ATOM 2355 N N . LYS A 1 335 ? 1.713 46.524 53.604 1.00 22.86 ? 353 LYS A N 1 ATOM 2356 C CA . LYS A 1 335 ? 2.995 46.050 54.094 1.00 22.17 ? 353 LYS A CA 1 ATOM 2357 C C . LYS A 1 335 ? 4.193 46.872 53.612 1.00 22.42 ? 353 LYS A C 1 ATOM 2358 O O . LYS A 1 335 ? 5.043 47.251 54.414 1.00 22.65 ? 353 LYS A O 1 ATOM 2359 C CB . LYS A 1 335 ? 3.212 44.582 53.738 1.00 22.46 ? 353 LYS A CB 1 ATOM 2360 C CG . LYS A 1 335 ? 4.513 44.046 54.297 1.00 23.50 ? 353 LYS A CG 1 ATOM 2361 C CD . LYS A 1 335 ? 4.660 42.561 54.045 1.00 23.11 ? 353 LYS A CD 1 ATOM 2362 C CE . LYS A 1 335 ? 5.901 42.045 54.748 1.00 23.92 ? 353 LYS A CE 1 ATOM 2363 N NZ . LYS A 1 335 ? 6.022 40.584 54.517 1.00 24.39 ? 353 LYS A NZ 1 ATOM 2364 N N . TYR A 1 336 ? 4.269 47.110 52.306 1.00 21.72 ? 354 TYR A N 1 ATOM 2365 C CA . TYR A 1 336 ? 5.429 47.807 51.732 1.00 21.62 ? 354 TYR A CA 1 ATOM 2366 C C . TYR A 1 336 ? 5.112 49.214 51.236 1.00 22.14 ? 354 TYR A C 1 ATOM 2367 O O . TYR A 1 336 ? 5.994 49.906 50.715 1.00 22.51 ? 354 TYR A O 1 ATOM 2368 C CB . TYR A 1 336 ? 6.044 46.985 50.597 1.00 21.11 ? 354 TYR A CB 1 ATOM 2369 C CG . TYR A 1 336 ? 6.604 45.657 51.040 1.00 21.26 ? 354 TYR A CG 1 ATOM 2370 C CD1 . TYR A 1 336 ? 7.645 45.590 51.968 1.00 22.23 ? 354 TYR A CD1 1 ATOM 2371 C CD2 . TYR A 1 336 ? 6.101 44.463 50.519 1.00 20.98 ? 354 TYR A CD2 1 ATOM 2372 C CE1 . TYR A 1 336 ? 8.171 44.364 52.368 1.00 23.15 ? 354 TYR A CE1 1 ATOM 2373 C CE2 . TYR A 1 336 ? 6.622 43.237 50.911 1.00 22.34 ? 354 TYR A CE2 1 ATOM 2374 C CZ . TYR A 1 336 ? 7.648 43.191 51.831 1.00 23.68 ? 354 TYR A CZ 1 ATOM 2375 O OH . TYR A 1 336 ? 8.158 41.971 52.215 1.00 25.04 ? 354 TYR A OH 1 ATOM 2376 N N . ASP A 1 337 ? 3.857 49.627 51.400 1.00 22.68 ? 355 ASP A N 1 ATOM 2377 C CA . ASP A 1 337 ? 3.409 50.970 51.059 1.00 23.69 ? 355 ASP A CA 1 ATOM 2378 C C . ASP A 1 337 ? 4.524 51.969 51.415 1.00 23.57 ? 355 ASP A C 1 ATOM 2379 O O . ASP A 1 337 ? 4.993 51.988 52.552 1.00 23.60 ? 355 ASP A O 1 ATOM 2380 C CB . ASP A 1 337 ? 2.118 51.264 51.836 1.00 23.68 ? 355 ASP A CB 1 ATOM 2381 C CG . ASP A 1 337 ? 1.368 52.477 51.314 1.00 25.04 ? 355 ASP A CG 1 ATOM 2382 O OD1 . ASP A 1 337 ? 2.008 53.407 50.780 1.00 26.22 ? 355 ASP A OD1 1 ATOM 2383 O OD2 . ASP A 1 337 ? 0.121 52.503 51.430 1.00 25.66 ? 355 ASP A OD2 1 ATOM 2384 N N . PRO A 1 338 ? 4.958 52.810 50.450 1.00 23.02 ? 356 PRO A N 1 ATOM 2385 C CA . PRO A 1 338 ? 4.439 53.146 49.117 1.00 21.75 ? 356 PRO A CA 1 ATOM 2386 C C . PRO A 1 338 ? 4.929 52.271 47.946 1.00 21.02 ? 356 PRO A C 1 ATOM 2387 O O . PRO A 1 338 ? 4.517 52.489 46.805 1.00 21.15 ? 356 PRO A O 1 ATOM 2388 C CB . PRO A 1 338 ? 4.963 54.567 48.917 1.00 21.61 ? 356 PRO A CB 1 ATOM 2389 C CG . PRO A 1 338 ? 6.283 54.544 49.604 1.00 22.27 ? 356 PRO A CG 1 ATOM 2390 C CD . PRO A 1 338 ? 6.128 53.641 50.799 1.00 23.29 ? 356 PRO A CD 1 ATOM 2391 N N . VAL A 1 339 ? 5.786 51.301 48.243 1.00 21.14 ? 357 VAL A N 1 ATOM 2392 C CA . VAL A 1 339 ? 6.405 50.465 47.213 1.00 19.76 ? 357 VAL A CA 1 ATOM 2393 C C . VAL A 1 339 ? 5.418 49.402 46.726 1.00 20.23 ? 357 VAL A C 1 ATOM 2394 O O . VAL A 1 339 ? 4.879 48.643 47.537 1.00 21.25 ? 357 VAL A O 1 ATOM 2395 C CB . VAL A 1 339 ? 7.700 49.805 47.743 1.00 20.41 ? 357 VAL A CB 1 ATOM 2396 C CG1 . VAL A 1 339 ? 8.346 48.939 46.667 1.00 19.17 ? 357 VAL A CG1 1 ATOM 2397 C CG2 . VAL A 1 339 ? 8.679 50.875 48.226 1.00 20.08 ? 357 VAL A CG2 1 ATOM 2398 N N . VAL A 1 340 ? 5.191 49.358 45.415 1.00 18.22 ? 358 VAL A N 1 ATOM 2399 C CA . VAL A 1 340 ? 4.278 48.372 44.810 1.00 18.13 ? 358 VAL A CA 1 ATOM 2400 C C . VAL A 1 340 ? 5.028 47.291 44.019 1.00 17.98 ? 358 VAL A C 1 ATOM 2401 O O . VAL A 1 340 ? 4.435 46.283 43.616 1.00 17.84 ? 358 VAL A O 1 ATOM 2402 C CB . VAL A 1 340 ? 3.230 49.045 43.904 1.00 17.98 ? 358 VAL A CB 1 ATOM 2403 C CG1 . VAL A 1 340 ? 2.400 50.052 44.703 1.00 17.66 ? 358 VAL A CG1 1 ATOM 2404 C CG2 . VAL A 1 340 ? 3.896 49.724 42.706 1.00 18.48 ? 358 VAL A CG2 1 ATOM 2405 N N . ALA A 1 341 ? 6.320 47.513 43.788 1.00 17.49 ? 359 ALA A N 1 ATOM 2406 C CA . ALA A 1 341 ? 7.155 46.540 43.062 1.00 16.97 ? 359 ALA A CA 1 ATOM 2407 C C . ALA A 1 341 ? 8.612 46.686 43.464 1.00 17.54 ? 359 ALA A C 1 ATOM 2408 O O . ALA A 1 341 ? 9.074 47.792 43.714 1.00 17.10 ? 359 ALA A O 1 ATOM 2409 C CB . ALA A 1 341 ? 6.995 46.716 41.558 1.00 17.06 ? 359 ALA A CB 1 ATOM 2410 N N . ASN A 1 342 ? 9.334 45.567 43.512 1.00 17.22 ? 360 ASN A N 1 ATOM 2411 C CA . ASN A 1 342 ? 10.741 45.560 43.892 1.00 17.49 ? 360 ASN A CA 1 ATOM 2412 C C . ASN A 1 342 ? 11.492 44.784 42.818 1.00 17.29 ? 360 ASN A C 1 ATOM 2413 O O . ASN A 1 342 ? 11.461 43.551 42.790 1.00 16.62 ? 360 ASN A O 1 ATOM 2414 C CB . ASN A 1 342 ? 10.920 44.899 45.268 1.00 18.02 ? 360 ASN A CB 1 ATOM 2415 C CG . ASN A 1 342 ? 12.276 45.195 45.899 1.00 19.72 ? 360 ASN A CG 1 ATOM 2416 O OD1 . ASN A 1 342 ? 13.263 45.467 45.209 1.00 19.45 ? 360 ASN A OD1 1 ATOM 2417 N ND2 . ASN A 1 342 ? 12.328 45.150 47.227 1.00 20.82 ? 360 ASN A ND2 1 ATOM 2418 N N . LEU A 1 343 ? 12.139 45.510 41.914 1.00 16.75 ? 361 LEU A N 1 ATOM 2419 C CA . LEU A 1 343 ? 12.776 44.896 40.751 1.00 16.80 ? 361 LEU A CA 1 ATOM 2420 C C . LEU A 1 343 ? 14.272 44.904 40.980 1.00 17.49 ? 361 LEU A C 1 ATOM 2421 O O . LEU A 1 343 ? 14.986 45.820 40.536 1.00 17.01 ? 361 LEU A O 1 ATOM 2422 C CB . LEU A 1 343 ? 12.402 45.649 39.468 1.00 17.44 ? 361 LEU A CB 1 ATOM 2423 C CG . LEU A 1 343 ? 10.926 45.989 39.224 1.00 18.52 ? 361 LEU A CG 1 ATOM 2424 C CD1 . LEU A 1 343 ? 10.716 46.722 37.905 1.00 19.63 ? 361 LEU A CD1 1 ATOM 2425 C CD2 . LEU A 1 343 ? 10.057 44.738 39.275 1.00 18.69 ? 361 LEU A CD2 1 ATOM 2426 N N . ASP A 1 344 ? 14.743 43.897 41.711 1.00 16.95 ? 362 ASP A N 1 ATOM 2427 C CA . ASP A 1 344 ? 16.150 43.805 42.041 1.00 17.94 ? 362 ASP A CA 1 ATOM 2428 C C . ASP A 1 344 ? 16.901 42.911 41.042 1.00 17.79 ? 362 ASP A C 1 ATOM 2429 O O . ASP A 1 344 ? 17.267 41.777 41.365 1.00 17.70 ? 362 ASP A O 1 ATOM 2430 C CB . ASP A 1 344 ? 16.353 43.308 43.482 1.00 18.90 ? 362 ASP A CB 1 ATOM 2431 C CG . ASP A 1 344 ? 17.753 43.605 44.004 1.00 20.75 ? 362 ASP A CG 1 ATOM 2432 O OD1 . ASP A 1 344 ? 18.262 44.715 43.730 1.00 22.38 ? 362 ASP A OD1 1 ATOM 2433 O OD2 . ASP A 1 344 ? 18.347 42.745 44.684 1.00 21.56 ? 362 ASP A OD2 1 ATOM 2434 N N . CYS A 1 345 ? 17.133 43.420 39.832 1.00 17.78 ? 363 CYS A N 1 ATOM 2435 C CA . CYS A 1 345 ? 17.899 42.645 38.848 1.00 18.55 ? 363 CYS A CA 1 ATOM 2436 C C . CYS A 1 345 ? 19.367 42.512 39.275 1.00 18.01 ? 363 CYS A C 1 ATOM 2437 O O . CYS A 1 345 ? 19.884 43.373 39.985 1.00 17.83 ? 363 CYS A O 1 ATOM 2438 C CB . CYS A 1 345 ? 17.789 43.254 37.449 1.00 19.37 ? 363 CYS A CB 1 ATOM 2439 S SG . CYS A 1 345 ? 16.315 42.652 36.582 1.00 21.80 ? 363 CYS A SG 1 ATOM 2440 N N . GLY A 1 346 ? 20.012 41.433 38.837 1.00 18.29 ? 364 GLY A N 1 ATOM 2441 C CA . GLY A 1 346 ? 21.392 41.146 39.218 1.00 18.87 ? 364 GLY A CA 1 ATOM 2442 C C . GLY A 1 346 ? 22.367 42.114 38.566 1.00 20.00 ? 364 GLY A C 1 ATOM 2443 O O . GLY A 1 346 ? 22.116 42.623 37.480 1.00 19.21 ? 364 GLY A O 1 ATOM 2444 N N . ALA A 1 347 ? 23.474 42.371 39.247 1.00 20.38 ? 365 ALA A N 1 ATOM 2445 C CA . ALA A 1 347 ? 24.452 43.354 38.775 1.00 21.34 ? 365 ALA A CA 1 ATOM 2446 C C . ALA A 1 347 ? 25.124 42.946 37.476 1.00 22.48 ? 365 ALA A C 1 ATOM 2447 O O . ALA A 1 347 ? 25.482 43.807 36.670 1.00 22.85 ? 365 ALA A O 1 ATOM 2448 C CB . ALA A 1 347 ? 25.500 43.610 39.849 1.00 21.43 ? 365 ALA A CB 1 ATOM 2449 N N . ASP A 1 348 ? 25.304 41.644 37.274 1.00 21.32 ? 366 ASP A N 1 ATOM 2450 C CA . ASP A 1 348 ? 25.978 41.135 36.082 1.00 22.45 ? 366 ASP A CA 1 ATOM 2451 C C . ASP A 1 348 ? 25.040 40.467 35.092 1.00 21.10 ? 366 ASP A C 1 ATOM 2452 O O . ASP A 1 348 ? 25.486 39.762 34.186 1.00 20.97 ? 366 ASP A O 1 ATOM 2453 C CB . ASP A 1 348 ? 27.056 40.125 36.474 1.00 23.97 ? 366 ASP A CB 1 ATOM 2454 C CG . ASP A 1 348 ? 28.217 40.763 37.200 1.00 25.65 ? 366 ASP A CG 1 ATOM 2455 O OD1 . ASP A 1 348 ? 28.193 41.998 37.405 1.00 28.06 ? 366 ASP A OD1 1 ATOM 2456 O OD2 . ASP A 1 348 ? 29.144 40.016 37.571 1.00 27.19 ? 366 ASP A OD2 1 ATOM 2457 N N . GLY A 1 349 ? 23.741 40.682 35.256 1.00 19.87 ? 367 GLY A N 1 ATOM 2458 C CA . GLY A 1 349 ? 22.794 39.994 34.404 1.00 18.77 ? 367 GLY A CA 1 ATOM 2459 C C . GLY A 1 349 ? 22.178 40.878 33.343 1.00 18.44 ? 367 GLY A C 1 ATOM 2460 O O . GLY A 1 349 ? 22.545 42.056 33.187 1.00 18.59 ? 367 GLY A O 1 ATOM 2461 N N . THR A 1 350 ? 21.238 40.301 32.617 1.00 17.15 ? 368 THR A N 1 ATOM 2462 C CA . THR A 1 350 ? 20.426 41.035 31.667 1.00 17.42 ? 368 THR A CA 1 ATOM 2463 C C . THR A 1 350 ? 19.036 41.133 32.264 1.00 17.46 ? 368 THR A C 1 ATOM 2464 O O . THR A 1 350 ? 18.487 40.133 32.730 1.00 16.95 ? 368 THR A O 1 ATOM 2465 C CB . THR A 1 350 ? 20.383 40.290 30.323 1.00 18.74 ? 368 THR A CB 1 ATOM 2466 O OG1 . THR A 1 350 ? 21.730 40.012 29.901 1.00 20.63 ? 368 THR A OG1 1 ATOM 2467 C CG2 . THR A 1 350 ? 19.704 41.118 29.259 1.00 18.99 ? 368 THR A CG2 1 ATOM 2468 N N . CYS A 1 351 ? 18.472 42.335 32.235 1.00 17.58 ? 369 CYS A N 1 ATOM 2469 C CA . CYS A 1 351 ? 17.199 42.614 32.893 1.00 17.56 ? 369 CYS A CA 1 ATOM 2470 C C . CYS A 1 351 ? 16.200 43.095 31.849 1.00 16.43 ? 369 CYS A C 1 ATOM 2471 O O . CYS A 1 351 ? 15.711 44.226 31.909 1.00 16.82 ? 369 CYS A O 1 ATOM 2472 C CB . CYS A 1 351 ? 17.424 43.667 33.981 1.00 18.75 ? 369 CYS A CB 1 ATOM 2473 S SG . CYS A 1 351 ? 16.008 43.975 35.073 1.00 21.24 ? 369 CYS A SG 1 ATOM 2474 N N . GLY A 1 352 ? 15.897 42.229 30.887 1.00 15.50 ? 370 GLY A N 1 ATOM 2475 C CA . GLY A 1 352 ? 15.121 42.617 29.724 1.00 15.50 ? 370 GLY A CA 1 ATOM 2476 C C . GLY A 1 352 ? 13.634 42.603 30.025 1.00 16.23 ? 370 GLY A C 1 ATOM 2477 O O . GLY A 1 352 ? 12.895 41.783 29.484 1.00 16.48 ? 370 GLY A O 1 ATOM 2478 N N . ILE A 1 353 ? 13.205 43.525 30.876 1.00 16.61 ? 371 ILE A N 1 ATOM 2479 C CA . ILE A 1 353 ? 11.792 43.616 31.250 1.00 17.34 ? 371 ILE A CA 1 ATOM 2480 C C . ILE A 1 353 ? 11.170 44.915 30.755 1.00 17.43 ? 371 ILE A C 1 ATOM 2481 O O . ILE A 1 353 ? 11.791 45.981 30.827 1.00 16.38 ? 371 ILE A O 1 ATOM 2482 C CB . ILE A 1 353 ? 11.567 43.374 32.769 1.00 18.83 ? 371 ILE A CB 1 ATOM 2483 C CG1 . ILE A 1 353 ? 10.081 43.527 33.147 1.00 19.69 ? 371 ILE A CG1 1 ATOM 2484 C CG2 . ILE A 1 353 ? 12.480 44.225 33.632 1.00 19.81 ? 371 ILE A CG2 1 ATOM 2485 C CD1 . ILE A 1 353 ? 9.761 43.052 34.557 1.00 21.35 ? 371 ILE A CD1 1 ATOM 2486 N N . SER A 1 354 ? 9.970 44.801 30.200 1.00 17.04 ? 372 SER A N 1 ATOM 2487 C CA A SER A 1 354 ? 9.188 45.949 29.734 0.50 17.52 ? 372 SER A CA 1 ATOM 2488 C CA B SER A 1 354 ? 9.220 45.995 29.838 0.50 17.86 ? 372 SER A CA 1 ATOM 2489 C C . SER A 1 354 ? 7.831 45.960 30.440 1.00 17.82 ? 372 SER A C 1 ATOM 2490 O O . SER A 1 354 ? 7.134 44.943 30.416 1.00 17.82 ? 372 SER A O 1 ATOM 2491 C CB A SER A 1 354 ? 8.993 45.853 28.220 0.50 17.56 ? 372 SER A CB 1 ATOM 2492 C CB B SER A 1 354 ? 9.195 46.252 28.328 0.50 18.51 ? 372 SER A CB 1 ATOM 2493 O OG A SER A 1 354 ? 8.253 46.950 27.711 0.50 18.45 ? 372 SER A OG 1 ATOM 2494 O OG B SER A 1 354 ? 8.973 45.077 27.590 0.50 20.13 ? 372 SER A OG 1 ATOM 2495 N N . ILE A 1 355 ? 7.465 47.093 31.028 1.00 17.30 ? 373 ILE A N 1 ATOM 2496 C CA . ILE A 1 355 ? 6.231 47.213 31.779 1.00 18.24 ? 373 ILE A CA 1 ATOM 2497 C C . ILE A 1 355 ? 5.327 48.231 31.102 1.00 19.60 ? 373 ILE A C 1 ATOM 2498 O O . ILE A 1 355 ? 5.780 49.321 30.734 1.00 19.17 ? 373 ILE A O 1 ATOM 2499 C CB . ILE A 1 355 ? 6.511 47.627 33.232 1.00 18.62 ? 373 ILE A CB 1 ATOM 2500 C CG1 . ILE A 1 355 ? 7.471 46.627 33.885 1.00 18.89 ? 373 ILE A CG1 1 ATOM 2501 C CG2 . ILE A 1 355 ? 5.207 47.724 34.027 1.00 18.98 ? 373 ILE A CG2 1 ATOM 2502 C CD1 . ILE A 1 355 ? 8.005 47.055 35.231 1.00 19.71 ? 373 ILE A CD1 1 ATOM 2503 N N . SER A 1 356 ? 4.063 47.868 30.916 1.00 19.03 ? 374 SER A N 1 ATOM 2504 C CA . SER A 1 356 ? 3.075 48.804 30.353 1.00 20.72 ? 374 SER A CA 1 ATOM 2505 C C . SER A 1 356 ? 1.725 48.621 31.045 1.00 21.12 ? 374 SER A C 1 ATOM 2506 O O . SER A 1 356 ? 1.436 47.554 31.591 1.00 19.17 ? 374 SER A O 1 ATOM 2507 C CB . SER A 1 356 ? 2.917 48.617 28.850 1.00 21.63 ? 374 SER A CB 1 ATOM 2508 O OG . SER A 1 356 ? 2.429 47.323 28.555 1.00 24.60 ? 374 SER A OG 1 ATOM 2509 N N . GLY A 1 357 ? 0.895 49.661 31.017 1.00 21.01 ? 375 GLY A N 1 ATOM 2510 C CA . GLY A 1 357 ? -0.415 49.596 31.668 1.00 21.94 ? 375 GLY A CA 1 ATOM 2511 C C . GLY A 1 357 ? -0.314 49.155 33.116 1.00 22.13 ? 375 GLY A C 1 ATOM 2512 O O . GLY A 1 357 ? -1.120 48.340 33.593 1.00 23.03 ? 375 GLY A O 1 ATOM 2513 N N . PHE A 1 358 ? 0.681 49.678 33.821 1.00 22.11 ? 376 PHE A N 1 ATOM 2514 C CA . PHE A 1 358 ? 0.905 49.311 35.206 1.00 23.64 ? 376 PHE A CA 1 ATOM 2515 C C . PHE A 1 358 ? 0.196 50.339 36.074 1.00 25.41 ? 376 PHE A C 1 ATOM 2516 O O . PHE A 1 358 ? 0.729 51.418 36.324 1.00 26.70 ? 376 PHE A O 1 ATOM 2517 C CB . PHE A 1 358 ? 2.404 49.297 35.491 1.00 24.00 ? 376 PHE A CB 1 ATOM 2518 C CG . PHE A 1 358 ? 2.779 48.674 36.802 1.00 24.50 ? 376 PHE A CG 1 ATOM 2519 C CD1 . PHE A 1 358 ? 2.841 47.293 36.941 1.00 23.87 ? 376 PHE A CD1 1 ATOM 2520 C CD2 . PHE A 1 358 ? 3.109 49.473 37.889 1.00 25.56 ? 376 PHE A CD2 1 ATOM 2521 C CE1 . PHE A 1 358 ? 3.206 46.720 38.148 1.00 25.45 ? 376 PHE A CE1 1 ATOM 2522 C CE2 . PHE A 1 358 ? 3.478 48.910 39.102 1.00 27.04 ? 376 PHE A CE2 1 ATOM 2523 C CZ . PHE A 1 358 ? 3.527 47.529 39.231 1.00 26.25 ? 376 PHE A CZ 1 ATOM 2524 N N . ASP A 1 359 ? -1.011 50.002 36.518 1.00 25.61 ? 377 ASP A N 1 ATOM 2525 C CA . ASP A 1 359 ? -1.890 50.971 37.178 1.00 28.25 ? 377 ASP A CA 1 ATOM 2526 C C . ASP A 1 359 ? -2.098 50.647 38.650 1.00 27.98 ? 377 ASP A C 1 ATOM 2527 O O . ASP A 1 359 ? -3.081 51.061 39.252 1.00 31.92 ? 377 ASP A O 1 ATOM 2528 C CB . ASP A 1 359 ? -3.238 51.036 36.456 1.00 31.03 ? 377 ASP A CB 1 ATOM 2529 C CG . ASP A 1 359 ? -3.127 51.625 35.051 1.00 36.23 ? 377 ASP A CG 1 ATOM 2530 O OD1 . ASP A 1 359 ? -2.106 52.283 34.745 1.00 39.51 ? 377 ASP A OD1 1 ATOM 2531 O OD2 . ASP A 1 359 ? -4.064 51.430 34.244 1.00 38.86 ? 377 ASP A OD2 1 ATOM 2532 N N . VAL A 1 360 ? -1.151 49.928 39.228 1.00 25.17 ? 378 VAL A N 1 ATOM 2533 C CA . VAL A 1 360 ? -1.239 49.487 40.610 1.00 24.19 ? 378 VAL A CA 1 ATOM 2534 C C . VAL A 1 360 ? -0.806 50.568 41.596 1.00 24.31 ? 378 VAL A C 1 ATOM 2535 O O . VAL A 1 360 ? 0.210 51.241 41.400 1.00 23.70 ? 378 VAL A O 1 ATOM 2536 C CB . VAL A 1 360 ? -0.418 48.190 40.813 1.00 23.81 ? 378 VAL A CB 1 ATOM 2537 C CG1 . VAL A 1 360 ? -0.598 47.658 42.225 1.00 25.48 ? 378 VAL A CG1 1 ATOM 2538 C CG2 . VAL A 1 360 ? -0.867 47.142 39.810 1.00 22.97 ? 378 VAL A CG2 1 ATOM 2539 N N . LYS A 1 361 ? -1.591 50.738 42.657 1.00 23.53 ? 379 LYS A N 1 ATOM 2540 C CA . LYS A 1 361 ? -1.275 51.700 43.705 1.00 24.25 ? 379 LYS A CA 1 ATOM 2541 C C . LYS A 1 361 ? -1.225 51.033 45.066 1.00 22.89 ? 379 LYS A C 1 ATOM 2542 O O . LYS A 1 361 ? -1.874 50.008 45.281 1.00 23.21 ? 379 LYS A O 1 ATOM 2543 C CB . LYS A 1 361 ? -2.323 52.822 43.712 1.00 26.25 ? 379 LYS A CB 1 ATOM 2544 C CG . LYS A 1 361 ? -2.211 53.766 42.521 1.00 30.27 ? 379 LYS A CG 1 ATOM 2545 C CD . LYS A 1 361 ? -3.409 54.700 42.424 1.00 34.18 ? 379 LYS A CD 1 ATOM 2546 C CE . LYS A 1 361 ? -3.057 55.972 41.660 1.00 37.64 ? 379 LYS A CE 1 ATOM 2547 N NZ . LYS A 1 361 ? -2.306 55.708 40.399 1.00 40.43 ? 379 LYS A NZ 1 ATOM 2548 N N . ALA A 1 362 ? -0.455 51.617 45.979 1.00 21.46 ? 380 ALA A N 1 ATOM 2549 C CA . ALA A 1 362 ? -0.471 51.229 47.380 1.00 21.75 ? 380 ALA A CA 1 ATOM 2550 C C . ALA A 1 362 ? -1.745 51.832 48.024 1.00 22.65 ? 380 ALA A C 1 ATOM 2551 O O . ALA A 1 362 ? -2.394 52.662 47.401 1.00 22.56 ? 380 ALA A O 1 ATOM 2552 C CB . ALA A 1 362 ? 0.791 51.718 48.065 1.00 21.31 ? 380 ALA A CB 1 ATOM 2553 N N . PRO A 1 363 ? -2.128 51.377 49.232 1.00 23.82 ? 381 PRO A N 1 ATOM 2554 C CA . PRO A 1 363 ? -3.323 51.937 49.892 1.00 24.87 ? 381 PRO A CA 1 ATOM 2555 C C . PRO A 1 363 ? -3.302 53.472 50.040 1.00 26.60 ? 381 PRO A C 1 ATOM 2556 O O . PRO A 1 363 ? -4.347 54.111 49.906 1.00 28.57 ? 381 PRO A O 1 ATOM 2557 C CB . PRO A 1 363 ? -3.304 51.246 51.255 1.00 25.02 ? 381 PRO A CB 1 ATOM 2558 C CG . PRO A 1 363 ? -2.745 49.887 50.930 1.00 23.67 ? 381 PRO A CG 1 ATOM 2559 C CD . PRO A 1 363 ? -1.626 50.196 49.963 1.00 23.31 ? 381 PRO A CD 1 ATOM 2560 N N . SER A 1 364 ? -2.125 54.037 50.296 1.00 27.72 ? 382 SER A N 1 ATOM 2561 C CA . SER A 1 364 ? -1.920 55.494 50.362 1.00 28.75 ? 382 SER A CA 1 ATOM 2562 C C . SER A 1 364 ? -2.203 56.238 49.054 1.00 29.40 ? 382 SER A C 1 ATOM 2563 O O . SER A 1 364 ? -2.326 57.467 49.050 1.00 30.29 ? 382 SER A O 1 ATOM 2564 C CB . SER A 1 364 ? -0.481 55.784 50.769 1.00 29.17 ? 382 SER A CB 1 ATOM 2565 O OG . SER A 1 364 ? 0.418 55.380 49.736 1.00 28.41 ? 382 SER A OG 1 ATOM 2566 N N . GLY A 1 365 ? -2.277 55.506 47.945 1.00 29.03 ? 383 GLY A N 1 ATOM 2567 C CA . GLY A 1 365 ? -2.430 56.111 46.625 1.00 27.25 ? 383 GLY A CA 1 ATOM 2568 C C . GLY A 1 365 ? -1.099 56.260 45.893 1.00 26.92 ? 383 GLY A C 1 ATOM 2569 O O . GLY A 1 365 ? -1.079 56.536 44.698 1.00 27.42 ? 383 GLY A O 1 ATOM 2570 N N . LYS A 1 366 ? 0.010 56.076 46.604 1.00 26.98 ? 384 LYS A N 1 ATOM 2571 C CA . LYS A 1 366 ? 1.339 56.146 45.987 1.00 29.23 ? 384 LYS A CA 1 ATOM 2572 C C . LYS A 1 366 ? 1.661 54.868 45.210 1.00 29.07 ? 384 LYS A C 1 ATOM 2573 O O . LYS A 1 366 ? 0.950 53.863 45.353 1.00 28.06 ? 384 LYS A O 1 ATOM 2574 C CB . LYS A 1 366 ? 2.399 56.437 47.042 1.00 31.37 ? 384 LYS A CB 1 ATOM 2575 C CG . LYS A 1 366 ? 2.328 57.874 47.536 1.00 33.91 ? 384 LYS A CG 1 ATOM 2576 C CD . LYS A 1 366 ? 3.060 58.054 48.849 1.00 37.18 ? 384 LYS A CD 1 ATOM 2577 C CE . LYS A 1 366 ? 2.993 59.505 49.295 1.00 38.86 ? 384 LYS A CE 1 ATOM 2578 N NZ . LYS A 1 366 ? 3.907 59.743 50.447 1.00 41.32 ? 384 LYS A NZ 1 ATOM 2579 N N . SER A 1 367 ? 2.712 54.910 44.383 1.00 27.96 ? 385 SER A N 1 ATOM 2580 C CA . SER A 1 367 ? 3.072 53.766 43.524 1.00 27.62 ? 385 SER A CA 1 ATOM 2581 C C . SER A 1 367 ? 4.563 53.711 43.181 1.00 26.69 ? 385 SER A C 1 ATOM 2582 O O . SER A 1 367 ? 4.970 53.757 42.011 1.00 28.18 ? 385 SER A O 1 ATOM 2583 C CB . SER A 1 367 ? 2.233 53.773 42.248 1.00 29.06 ? 385 SER A CB 1 ATOM 2584 O OG . SER A 1 367 ? 2.391 55.011 41.573 1.00 32.99 ? 385 SER A OG 1 ATOM 2585 N N . GLU A 1 368 ? 5.377 53.597 44.211 1.00 24.17 ? 386 GLU A N 1 ATOM 2586 C CA . GLU A 1 368 ? 6.808 53.572 44.049 1.00 24.16 ? 386 GLU A CA 1 ATOM 2587 C C . GLU A 1 368 ? 7.277 52.197 43.552 1.00 22.99 ? 386 GLU A C 1 ATOM 2588 O O . GLU A 1 368 ? 6.781 51.163 43.993 1.00 21.57 ? 386 GLU A O 1 ATOM 2589 C CB . GLU A 1 368 ? 7.425 53.907 45.394 1.00 26.73 ? 386 GLU A CB 1 ATOM 2590 C CG . GLU A 1 368 ? 8.917 54.131 45.421 1.00 31.25 ? 386 GLU A CG 1 ATOM 2591 C CD . GLU A 1 368 ? 9.370 54.645 46.776 1.00 33.27 ? 386 GLU A CD 1 ATOM 2592 O OE1 . GLU A 1 368 ? 8.725 55.577 47.305 1.00 36.49 ? 386 GLU A OE1 1 ATOM 2593 O OE2 . GLU A 1 368 ? 10.358 54.108 47.312 1.00 37.90 ? 386 GLU A OE2 1 ATOM 2594 N N . VAL A 1 369 ? 8.211 52.205 42.606 1.00 20.90 ? 387 VAL A N 1 ATOM 2595 C CA . VAL A 1 369 ? 8.827 50.975 42.112 1.00 20.59 ? 387 VAL A CA 1 ATOM 2596 C C . VAL A 1 369 ? 10.318 51.050 42.432 1.00 20.88 ? 387 VAL A C 1 ATOM 2597 O O . VAL A 1 369 ? 11.034 51.935 41.927 1.00 21.38 ? 387 VAL A O 1 ATOM 2598 C CB . VAL A 1 369 ? 8.584 50.798 40.593 1.00 20.34 ? 387 VAL A CB 1 ATOM 2599 C CG1 . VAL A 1 369 ? 9.323 49.572 40.052 1.00 20.29 ? 387 VAL A CG1 1 ATOM 2600 C CG2 . VAL A 1 369 ? 7.093 50.706 40.288 1.00 20.80 ? 387 VAL A CG2 1 ATOM 2601 N N . LEU A 1 370 ? 10.789 50.145 43.280 1.00 20.00 ? 388 LEU A N 1 ATOM 2602 C CA . LEU A 1 370 ? 12.206 50.067 43.593 1.00 20.45 ? 388 LEU A CA 1 ATOM 2603 C C . LEU A 1 370 ? 12.909 49.300 42.485 1.00 21.15 ? 388 LEU A C 1 ATOM 2604 O O . LEU A 1 370 ? 12.398 48.275 42.026 1.00 19.50 ? 388 LEU A O 1 ATOM 2605 C CB . LEU A 1 370 ? 12.444 49.367 44.927 1.00 21.27 ? 388 LEU A CB 1 ATOM 2606 C CG . LEU A 1 370 ? 11.846 50.036 46.168 1.00 22.32 ? 388 LEU A CG 1 ATOM 2607 C CD1 . LEU A 1 370 ? 12.321 49.268 47.383 1.00 21.73 ? 388 LEU A CD1 1 ATOM 2608 C CD2 . LEU A 1 370 ? 12.251 51.510 46.246 1.00 23.99 ? 388 LEU A CD2 1 ATOM 2609 N N . CYS A 1 371 ? 14.063 49.812 42.043 1.00 21.35 ? 389 CYS A N 1 ATOM 2610 C CA . CYS A 1 371 ? 14.797 49.185 40.934 1.00 21.51 ? 389 CYS A CA 1 ATOM 2611 C C . CYS A 1 371 ? 16.289 49.113 41.190 1.00 21.33 ? 389 CYS A C 1 ATOM 2612 O O . CYS A 1 371 ? 16.873 50.020 41.796 1.00 21.58 ? 389 CYS A O 1 ATOM 2613 C CB . CYS A 1 371 ? 14.606 49.970 39.640 1.00 23.67 ? 389 CYS A CB 1 ATOM 2614 S SG . CYS A 1 371 ? 12.915 50.177 39.054 1.00 25.76 ? 389 CYS A SG 1 ATOM 2615 N N . ALA A 1 372 ? 16.898 48.029 40.718 1.00 19.24 ? 390 ALA A N 1 ATOM 2616 C CA . ALA A 1 372 ? 18.342 47.947 40.578 1.00 19.34 ? 390 ALA A CA 1 ATOM 2617 C C . ALA A 1 372 ? 18.620 47.247 39.257 1.00 18.29 ? 390 ALA A C 1 ATOM 2618 O O . ALA A 1 372 ? 17.993 46.224 38.951 1.00 17.30 ? 390 ALA A O 1 ATOM 2619 C CB . ALA A 1 372 ? 18.959 47.173 41.733 1.00 19.02 ? 390 ALA A CB 1 ATOM 2620 N N . ASN A 1 373 ? 19.517 47.825 38.451 1.00 17.35 ? 391 ASN A N 1 ATOM 2621 C CA . ASN A 1 373 ? 19.972 47.194 37.204 1.00 16.18 ? 391 ASN A CA 1 ATOM 2622 C C . ASN A 1 373 ? 18.868 46.983 36.167 1.00 15.87 ? 391 ASN A C 1 ATOM 2623 O O . ASN A 1 373 ? 18.918 46.040 35.378 1.00 15.06 ? 391 ASN A O 1 ATOM 2624 C CB . ASN A 1 373 ? 20.710 45.879 37.497 1.00 16.73 ? 391 ASN A CB 1 ATOM 2625 C CG . ASN A 1 373 ? 21.873 46.074 38.431 1.00 18.15 ? 391 ASN A CG 1 ATOM 2626 O OD1 . ASN A 1 373 ? 22.847 46.756 38.080 1.00 18.08 ? 391 ASN A OD1 1 ATOM 2627 N ND2 . ASN A 1 373 ? 21.788 45.495 39.632 1.00 16.82 ? 391 ASN A ND2 1 ATOM 2628 N N . THR A 1 374 ? 17.886 47.881 36.180 1.00 16.14 ? 392 THR A N 1 ATOM 2629 C CA . THR A 1 374 ? 16.777 47.844 35.246 1.00 16.28 ? 392 THR A CA 1 ATOM 2630 C C . THR A 1 374 ? 17.113 48.687 34.025 1.00 15.97 ? 392 THR A C 1 ATOM 2631 O O . THR A 1 374 ? 17.900 49.638 34.122 1.00 15.97 ? 392 THR A O 1 ATOM 2632 C CB . THR A 1 374 ? 15.468 48.357 35.892 1.00 17.12 ? 392 THR A CB 1 ATOM 2633 O OG1 . THR A 1 374 ? 15.710 49.619 36.522 1.00 16.87 ? 392 THR A OG1 1 ATOM 2634 C CG2 . THR A 1 374 ? 14.956 47.360 36.951 1.00 17.00 ? 392 THR A CG2 1 ATOM 2635 N N . PRO A 1 375 ? 16.541 48.337 32.872 1.00 16.37 ? 393 PRO A N 1 ATOM 2636 C CA . PRO A 1 375 ? 16.900 48.969 31.598 1.00 16.60 ? 393 PRO A CA 1 ATOM 2637 C C . PRO A 1 375 ? 16.272 50.353 31.400 1.00 17.84 ? 393 PRO A C 1 ATOM 2638 O O . PRO A 1 375 ? 15.287 50.704 32.050 1.00 17.41 ? 393 PRO A O 1 ATOM 2639 C CB . PRO A 1 375 ? 16.328 48.006 30.562 1.00 17.33 ? 393 PRO A CB 1 ATOM 2640 C CG . PRO A 1 375 ? 15.166 47.367 31.249 1.00 16.74 ? 393 PRO A CG 1 ATOM 2641 C CD . PRO A 1 375 ? 15.571 47.240 32.683 1.00 16.46 ? 393 PRO A CD 1 ATOM 2642 N N . SER A 1 376 ? 16.836 51.119 30.473 1.00 18.27 ? 394 SER A N 1 ATOM 2643 C CA . SER A 1 376 ? 16.337 52.470 30.198 1.00 20.73 ? 394 SER A CA 1 ATOM 2644 C C . SER A 1 376 ? 14.920 52.483 29.635 1.00 23.00 ? 394 SER A C 1 ATOM 2645 O O . SER A 1 376 ? 14.229 53.491 29.735 1.00 27.00 ? 394 SER A O 1 ATOM 2646 C CB . SER A 1 376 ? 17.300 53.209 29.254 1.00 20.47 ? 394 SER A CB 1 ATOM 2647 O OG . SER A 1 376 ? 17.607 52.396 28.129 1.00 21.08 ? 394 SER A OG 1 ATOM 2648 N N . ASP A 1 377 ? 14.471 51.379 29.057 1.00 23.16 ? 395 ASP A N 1 ATOM 2649 C CA . ASP A 1 377 ? 13.133 51.363 28.460 1.00 26.14 ? 395 ASP A CA 1 ATOM 2650 C C . ASP A 1 377 ? 12.148 50.564 29.325 1.00 24.98 ? 395 ASP A C 1 ATOM 2651 O O . ASP A 1 377 ? 11.227 49.927 28.807 1.00 26.22 ? 395 ASP A O 1 ATOM 2652 C CB . ASP A 1 377 ? 13.185 50.799 27.028 1.00 28.05 ? 395 ASP A CB 1 ATOM 2653 C CG . ASP A 1 377 ? 13.581 49.303 26.982 1.00 30.06 ? 395 ASP A CG 1 ATOM 2654 O OD1 . ASP A 1 377 ? 14.175 48.793 27.958 1.00 29.58 ? 395 ASP A OD1 1 ATOM 2655 O OD2 . ASP A 1 377 ? 13.303 48.640 25.956 1.00 32.23 ? 395 ASP A OD2 1 ATOM 2656 N N . LEU A 1 378 ? 12.364 50.582 30.638 1.00 24.32 ? 396 LEU A N 1 ATOM 2657 C CA . LEU A 1 378 ? 11.545 49.777 31.562 1.00 22.98 ? 396 LEU A CA 1 ATOM 2658 C C . LEU A 1 378 ? 10.050 50.069 31.429 1.00 23.25 ? 396 LEU A C 1 ATOM 2659 O O . LEU A 1 378 ? 9.242 49.143 31.344 1.00 22.85 ? 396 LEU A O 1 ATOM 2660 C CB . LEU A 1 378 ? 11.995 49.983 33.002 1.00 21.51 ? 396 LEU A CB 1 ATOM 2661 C CG . LEU A 1 378 ? 11.226 49.182 34.058 1.00 20.93 ? 396 LEU A CG 1 ATOM 2662 C CD1 . LEU A 1 378 ? 11.490 47.692 33.888 1.00 21.39 ? 396 LEU A CD1 1 ATOM 2663 C CD2 . LEU A 1 378 ? 11.635 49.657 35.440 1.00 20.62 ? 396 LEU A CD2 1 ATOM 2664 N N . GLY A 1 379 ? 9.687 51.351 31.426 1.00 23.48 ? 397 GLY A N 1 ATOM 2665 C CA . GLY A 1 379 ? 8.298 51.747 31.222 1.00 24.74 ? 397 GLY A CA 1 ATOM 2666 C C . GLY A 1 379 ? 7.578 52.315 32.429 1.00 25.18 ? 397 GLY A C 1 ATOM 2667 O O . GLY A 1 379 ? 6.430 52.729 32.312 1.00 28.26 ? 397 GLY A O 1 ATOM 2668 N N . VAL A 1 380 ? 8.235 52.311 33.588 1.00 24.98 ? 398 VAL A N 1 ATOM 2669 C CA . VAL A 1 380 ? 7.741 52.968 34.802 1.00 25.08 ? 398 VAL A CA 1 ATOM 2670 C C . VAL A 1 380 ? 8.904 53.706 35.464 1.00 25.71 ? 398 VAL A C 1 ATOM 2671 O O . VAL A 1 380 ? 10.067 53.343 35.267 1.00 23.60 ? 398 VAL A O 1 ATOM 2672 C CB . VAL A 1 380 ? 7.115 51.984 35.830 1.00 25.20 ? 398 VAL A CB 1 ATOM 2673 C CG1 . VAL A 1 380 ? 5.898 51.276 35.247 1.00 25.08 ? 398 VAL A CG1 1 ATOM 2674 C CG2 . VAL A 1 380 ? 8.138 50.983 36.357 1.00 25.02 ? 398 VAL A CG2 1 ATOM 2675 N N . THR A 1 381 ? 8.588 54.728 36.252 1.00 25.44 ? 399 THR A N 1 ATOM 2676 C CA . THR A 1 381 ? 9.610 55.489 36.976 1.00 26.81 ? 399 THR A CA 1 ATOM 2677 C C . THR A 1 381 ? 10.206 54.654 38.103 1.00 27.38 ? 399 THR A C 1 ATOM 2678 O O . THR A 1 381 ? 9.472 54.020 38.860 1.00 29.17 ? 399 THR A O 1 ATOM 2679 C CB . THR A 1 381 ? 9.043 56.815 37.532 1.00 27.76 ? 399 THR A CB 1 ATOM 2680 O OG1 . THR A 1 381 ? 8.406 57.531 36.470 1.00 29.64 ? 399 THR A OG1 1 ATOM 2681 C CG2 . THR A 1 381 ? 10.158 57.688 38.101 1.00 27.87 ? 399 THR A CG2 1 ATOM 2682 N N . CYS A 1 382 ? 11.534 54.646 38.193 1.00 27.15 ? 400 CYS A N 1 ATOM 2683 C CA . CYS A 1 382 ? 12.255 53.876 39.201 1.00 28.08 ? 400 CYS A CA 1 ATOM 2684 C C . CYS A 1 382 ? 12.687 54.709 40.380 1.00 28.62 ? 400 CYS A C 1 ATOM 2685 O O . CYS A 1 382 ? 12.912 55.920 40.255 1.00 29.17 ? 400 CYS A O 1 ATOM 2686 C CB . CYS A 1 382 ? 13.501 53.212 38.607 1.00 28.71 ? 400 CYS A CB 1 ATOM 2687 S SG . CYS A 1 382 ? 13.139 51.711 37.674 1.00 33.17 ? 400 CYS A SG 1 ATOM 2688 N N . THR A 1 383 ? 12.808 54.034 41.516 1.00 26.58 ? 401 THR A N 1 ATOM 2689 C CA . THR A 1 383 ? 13.395 54.577 42.725 1.00 27.18 ? 401 THR A CA 1 ATOM 2690 C C . THR A 1 383 ? 14.475 53.595 43.156 1.00 27.82 ? 401 THR A C 1 ATOM 2691 O O . THR A 1 383 ? 14.270 52.384 43.122 1.00 25.33 ? 401 THR A O 1 ATOM 2692 C CB . THR A 1 383 ? 12.329 54.715 43.827 1.00 27.08 ? 401 THR A CB 1 ATOM 2693 O OG1 . THR A 1 383 ? 11.277 55.562 43.352 1.00 28.16 ? 401 THR A OG1 1 ATOM 2694 C CG2 . THR A 1 383 ? 12.921 55.298 45.112 1.00 29.14 ? 401 THR A CG2 1 ATOM 2695 N N . SER A 1 384 ? 15.635 54.107 43.546 1.00 27.76 ? 402 SER A N 1 ATOM 2696 C CA . SER A 1 384 ? 16.723 53.246 43.984 1.00 28.24 ? 402 SER A CA 1 ATOM 2697 C C . SER A 1 384 ? 16.397 52.615 45.337 1.00 28.02 ? 402 SER A C 1 ATOM 2698 O O . SER A 1 384 ? 15.558 53.120 46.098 1.00 28.18 ? 402 SER A O 1 ATOM 2699 C CB . SER A 1 384 ? 18.023 54.039 44.088 1.00 31.43 ? 402 SER A CB 1 ATOM 2700 O OG . SER A 1 384 ? 17.968 54.895 45.211 1.00 34.00 ? 402 SER A OG 1 ATOM 2701 N N . GLY A 1 385 ? 17.070 51.512 45.627 1.00 26.68 ? 403 GLY A N 1 ATOM 2702 C CA . GLY A 1 385 ? 16.930 50.837 46.901 1.00 26.85 ? 403 GLY A CA 1 ATOM 2703 C C . GLY A 1 385 ? 16.284 49.470 46.795 1.00 26.64 ? 403 GLY A C 1 ATOM 2704 O O . GLY A 1 385 ? 15.862 48.923 47.805 1.00 27.68 ? 403 GLY A O 1 ATOM 2705 N N . ALA A 1 386 ? 16.206 48.916 45.585 1.00 25.51 ? 404 ALA A N 1 ATOM 2706 C CA . ALA A 1 386 ? 15.727 47.533 45.405 1.00 24.52 ? 404 ALA A CA 1 ATOM 2707 C C . ALA A 1 386 ? 16.649 46.566 46.137 1.00 24.37 ? 404 ALA A C 1 ATOM 2708 O O . ALA A 1 386 ? 17.839 46.831 46.288 1.00 25.12 ? 404 ALA A O 1 ATOM 2709 C CB . ALA A 1 386 ? 15.638 47.172 43.924 1.00 23.62 ? 404 ALA A CB 1 ATOM 2710 N N . SER A 1 387 ? 16.103 45.452 46.612 1.00 23.79 ? 405 SER A N 1 ATOM 2711 C CA . SER A 1 387 ? 16.918 44.442 47.285 1.00 23.68 ? 405 SER A CA 1 ATOM 2712 C C . SER A 1 387 ? 16.227 43.090 47.157 1.00 23.51 ? 405 SER A C 1 ATOM 2713 O O . SER A 1 387 ? 15.035 43.037 46.852 1.00 23.33 ? 405 SER A O 1 ATOM 2714 C CB . SER A 1 387 ? 17.138 44.796 48.767 1.00 24.89 ? 405 SER A CB 1 ATOM 2715 O OG . SER A 1 387 ? 15.915 44.759 49.483 1.00 25.95 ? 405 SER A OG 1 ATOM 2716 N N . GLY A 1 388 ? 16.978 42.016 47.371 1.00 23.29 ? 406 GLY A N 1 ATOM 2717 C CA . GLY A 1 388 ? 16.426 40.659 47.293 1.00 24.20 ? 406 GLY A CA 1 ATOM 2718 C C . GLY A 1 388 ? 16.835 39.906 46.040 1.00 24.27 ? 406 GLY A C 1 ATOM 2719 O O . GLY A 1 388 ? 16.835 38.665 46.022 1.00 23.73 ? 406 GLY A O 1 ATOM 2720 O OXT . GLY A 1 388 ? 17.182 40.510 45.015 1.00 24.32 ? 406 GLY A OXT 1 HETATM 2721 C C1 . MAN B 2 . ? -19.392 0.445 37.694 1.00 23.43 ? 410 MAN A C1 1 HETATM 2722 C C2 . MAN B 2 . ? -19.614 0.783 36.221 1.00 26.47 ? 410 MAN A C2 1 HETATM 2723 C C3 . MAN B 2 . ? -20.087 2.224 36.051 1.00 26.38 ? 410 MAN A C3 1 HETATM 2724 C C4 . MAN B 2 . ? -21.248 2.545 36.989 1.00 27.11 ? 410 MAN A C4 1 HETATM 2725 C C5 . MAN B 2 . ? -20.907 2.142 38.436 1.00 26.82 ? 410 MAN A C5 1 HETATM 2726 C C6 . MAN B 2 . ? -22.060 2.365 39.409 1.00 29.08 ? 410 MAN A C6 1 HETATM 2727 O O2 . MAN B 2 . ? -20.590 -0.096 35.686 1.00 28.70 ? 410 MAN A O2 1 HETATM 2728 O O3 . MAN B 2 . ? -20.470 2.410 34.701 1.00 26.78 ? 410 MAN A O3 1 HETATM 2729 O O4 . MAN B 2 . ? -21.520 3.924 36.909 1.00 27.02 ? 410 MAN A O4 1 HETATM 2730 O O5 . MAN B 2 . ? -20.537 0.775 38.469 1.00 24.28 ? 410 MAN A O5 1 HETATM 2731 O O6 . MAN B 2 . ? -23.072 1.406 39.161 1.00 31.69 ? 410 MAN A O6 1 HETATM 2732 C C1 . NAG C 3 . ? -7.637 38.802 52.459 1.00 28.15 ? 411 NAG A C1 1 HETATM 2733 C C2 . NAG C 3 . ? -8.796 37.932 52.921 1.00 31.72 ? 411 NAG A C2 1 HETATM 2734 C C3 . NAG C 3 . ? -9.803 38.724 53.759 1.00 33.82 ? 411 NAG A C3 1 HETATM 2735 C C4 . NAG C 3 . ? -9.099 39.484 54.875 1.00 34.94 ? 411 NAG A C4 1 HETATM 2736 C C5 . NAG C 3 . ? -8.004 40.345 54.241 1.00 35.18 ? 411 NAG A C5 1 HETATM 2737 C C6 . NAG C 3 . ? -7.255 41.180 55.273 1.00 35.59 ? 411 NAG A C6 1 HETATM 2738 C C7 . NAG C 3 . ? -9.743 36.196 51.492 1.00 33.37 ? 411 NAG A C7 1 HETATM 2739 C C8 . NAG C 3 . ? -10.510 35.975 50.224 1.00 33.12 ? 411 NAG A C8 1 HETATM 2740 N N2 . NAG C 3 . ? -9.503 37.470 51.753 1.00 32.81 ? 411 NAG A N2 1 HETATM 2741 O O3 . NAG C 3 . ? -10.758 37.823 54.277 1.00 35.63 ? 411 NAG A O3 1 HETATM 2742 O O4 . NAG C 3 . ? -10.023 40.296 55.580 1.00 39.37 ? 411 NAG A O4 1 HETATM 2743 O O5 . NAG C 3 . ? -7.081 39.494 53.560 1.00 31.33 ? 411 NAG A O5 1 HETATM 2744 O O6 . NAG C 3 . ? -6.645 40.311 56.198 1.00 40.19 ? 411 NAG A O6 1 HETATM 2745 O O7 . NAG C 3 . ? -9.380 35.264 52.218 1.00 35.39 ? 411 NAG A O7 1 HETATM 2746 C C1 . NAG D 3 . ? 6.784 33.175 23.377 1.00 19.28 ? 412 NAG A C1 1 HETATM 2747 C C2 . NAG D 3 . ? 6.915 32.559 21.981 1.00 22.08 ? 412 NAG A C2 1 HETATM 2748 C C3 . NAG D 3 . ? 5.550 32.196 21.404 1.00 22.96 ? 412 NAG A C3 1 HETATM 2749 C C4 . NAG D 3 . ? 4.723 31.378 22.405 1.00 22.86 ? 412 NAG A C4 1 HETATM 2750 C C5 . NAG D 3 . ? 4.715 32.073 23.784 1.00 20.44 ? 412 NAG A C5 1 HETATM 2751 C C6 . NAG D 3 . ? 3.955 31.330 24.895 1.00 18.50 ? 412 NAG A C6 1 HETATM 2752 C C7 . NAG D 3 . ? 8.777 33.385 20.632 1.00 26.78 ? 412 NAG A C7 1 HETATM 2753 C C8 . NAG D 3 . ? 9.253 34.492 19.733 1.00 28.29 ? 412 NAG A C8 1 HETATM 2754 N N2 . NAG D 3 . ? 7.541 33.521 21.096 1.00 24.07 ? 412 NAG A N2 1 HETATM 2755 O O3 . NAG D 3 . ? 5.736 31.462 20.210 1.00 24.27 ? 412 NAG A O3 1 HETATM 2756 O O4 . NAG D 3 . ? 3.405 31.245 21.889 1.00 26.27 ? 412 NAG A O4 1 HETATM 2757 O O5 . NAG D 3 . ? 6.041 32.311 24.218 1.00 18.86 ? 412 NAG A O5 1 HETATM 2758 O O6 . NAG D 3 . ? 4.324 29.969 24.967 1.00 18.29 ? 412 NAG A O6 1 HETATM 2759 O O7 . NAG D 3 . ? 9.517 32.437 20.896 1.00 29.28 ? 412 NAG A O7 1 HETATM 2760 C C1 . NAG E 3 . ? 3.012 29.855 21.887 1.00 30.61 ? 413 NAG A C1 1 HETATM 2761 C C2 . NAG E 3 . ? 1.483 29.763 21.778 1.00 33.41 ? 413 NAG A C2 1 HETATM 2762 C C3 . NAG E 3 . ? 0.949 28.355 21.516 1.00 37.21 ? 413 NAG A C3 1 HETATM 2763 C C4 . NAG E 3 . ? 1.827 27.512 20.595 1.00 37.68 ? 413 NAG A C4 1 HETATM 2764 C C5 . NAG E 3 . ? 3.315 27.714 20.910 1.00 35.28 ? 413 NAG A C5 1 HETATM 2765 C C6 . NAG E 3 . ? 4.195 26.984 19.906 1.00 36.25 ? 413 NAG A C6 1 HETATM 2766 C C7 . NAG E 3 . ? 0.290 31.449 23.050 1.00 32.52 ? 413 NAG A C7 1 HETATM 2767 C C8 . NAG E 3 . ? -0.332 31.836 24.362 1.00 31.47 ? 413 NAG A C8 1 HETATM 2768 N N2 . NAG E 3 . ? 0.851 30.245 22.994 1.00 32.66 ? 413 NAG A N2 1 HETATM 2769 O O3 . NAG E 3 . ? -0.305 28.509 20.902 1.00 41.27 ? 413 NAG A O3 1 HETATM 2770 O O4 . NAG E 3 . ? 1.458 26.150 20.721 1.00 40.56 ? 413 NAG A O4 1 HETATM 2771 O O5 . NAG E 3 . ? 3.640 29.095 20.872 1.00 33.28 ? 413 NAG A O5 1 HETATM 2772 O O6 . NAG E 3 . ? 3.973 27.564 18.641 1.00 38.87 ? 413 NAG A O6 1 HETATM 2773 O O7 . NAG E 3 . ? 0.284 32.218 22.094 1.00 31.79 ? 413 NAG A O7 1 HETATM 2774 S S . SO4 F 4 . ? 11.723 27.501 45.610 1.00 29.69 ? 1407 SO4 A S 1 HETATM 2775 O O1 . SO4 F 4 . ? 10.848 28.098 46.641 1.00 32.74 ? 1407 SO4 A O1 1 HETATM 2776 O O2 . SO4 F 4 . ? 13.135 27.696 46.026 1.00 32.70 ? 1407 SO4 A O2 1 HETATM 2777 O O3 . SO4 F 4 . ? 11.404 28.187 44.349 1.00 30.45 ? 1407 SO4 A O3 1 HETATM 2778 O O4 . SO4 F 4 . ? 11.477 26.051 45.525 1.00 33.01 ? 1407 SO4 A O4 1 HETATM 2779 S S . SO4 G 4 . ? 8.463 6.668 46.976 1.00 17.00 ? 1408 SO4 A S 1 HETATM 2780 O O1 . SO4 G 4 . ? 9.233 6.713 48.245 1.00 17.57 ? 1408 SO4 A O1 1 HETATM 2781 O O2 . SO4 G 4 . ? 8.941 5.497 46.205 1.00 16.23 ? 1408 SO4 A O2 1 HETATM 2782 O O3 . SO4 G 4 . ? 8.720 7.922 46.237 1.00 16.07 ? 1408 SO4 A O3 1 HETATM 2783 O O4 . SO4 G 4 . ? 7.015 6.506 47.256 1.00 14.79 ? 1408 SO4 A O4 1 HETATM 2784 S S . SO4 H 4 . ? -14.658 21.153 53.255 1.00 41.13 ? 1409 SO4 A S 1 HETATM 2785 O O1 . SO4 H 4 . ? -14.048 22.364 52.658 1.00 40.51 ? 1409 SO4 A O1 1 HETATM 2786 O O2 . SO4 H 4 . ? -14.729 20.032 52.286 1.00 38.72 ? 1409 SO4 A O2 1 HETATM 2787 O O3 . SO4 H 4 . ? -16.032 21.474 53.686 1.00 43.52 ? 1409 SO4 A O3 1 HETATM 2788 O O4 . SO4 H 4 . ? -13.841 20.751 54.424 1.00 43.55 ? 1409 SO4 A O4 1 HETATM 2789 S S . SO4 I 4 . ? 9.187 32.537 48.646 1.00 49.04 ? 1410 SO4 A S 1 HETATM 2790 O O1 . SO4 I 4 . ? 9.375 32.872 50.075 1.00 52.46 ? 1410 SO4 A O1 1 HETATM 2791 O O2 . SO4 I 4 . ? 10.488 32.616 47.952 1.00 48.69 ? 1410 SO4 A O2 1 HETATM 2792 O O3 . SO4 I 4 . ? 8.261 33.532 48.064 1.00 48.50 ? 1410 SO4 A O3 1 HETATM 2793 O O4 . SO4 I 4 . ? 8.603 31.181 48.483 1.00 48.43 ? 1410 SO4 A O4 1 HETATM 2794 S S . SO4 J 4 . ? -6.147 42.307 26.727 1.00 73.37 ? 1411 SO4 A S 1 HETATM 2795 O O1 . SO4 J 4 . ? -7.025 42.766 27.826 1.00 70.68 ? 1411 SO4 A O1 1 HETATM 2796 O O2 . SO4 J 4 . ? -5.397 43.464 26.184 1.00 72.09 ? 1411 SO4 A O2 1 HETATM 2797 O O3 . SO4 J 4 . ? -6.967 41.705 25.651 1.00 74.05 ? 1411 SO4 A O3 1 HETATM 2798 O O4 . SO4 J 4 . ? -5.199 41.294 27.241 1.00 68.12 ? 1411 SO4 A O4 1 HETATM 2799 S S . SO4 K 4 . ? 13.699 29.224 22.106 1.00 47.24 ? 1412 SO4 A S 1 HETATM 2800 O O1 . SO4 K 4 . ? 13.990 30.364 23.010 1.00 47.52 ? 1412 SO4 A O1 1 HETATM 2801 O O2 . SO4 K 4 . ? 13.982 29.649 20.711 1.00 49.23 ? 1412 SO4 A O2 1 HETATM 2802 O O3 . SO4 K 4 . ? 12.283 28.798 22.199 1.00 41.32 ? 1412 SO4 A O3 1 HETATM 2803 O O4 . SO4 K 4 . ? 14.583 28.093 22.490 1.00 46.72 ? 1412 SO4 A O4 1 HETATM 2804 S S . SO4 L 4 . ? -8.121 -4.507 26.225 1.00 87.37 ? 1413 SO4 A S 1 HETATM 2805 O O1 . SO4 L 4 . ? -8.788 -3.184 26.233 1.00 87.30 ? 1413 SO4 A O1 1 HETATM 2806 O O2 . SO4 L 4 . ? -6.697 -4.335 26.585 1.00 83.13 ? 1413 SO4 A O2 1 HETATM 2807 O O3 . SO4 L 4 . ? -8.221 -5.101 24.872 1.00 87.65 ? 1413 SO4 A O3 1 HETATM 2808 O O4 . SO4 L 4 . ? -8.784 -5.403 27.200 1.00 84.80 ? 1413 SO4 A O4 1 HETATM 2809 C C1 . GOL M 5 . ? -10.785 16.865 56.866 1.00 47.36 ? 1414 GOL A C1 1 HETATM 2810 O O1 . GOL M 5 . ? -10.699 15.912 55.787 1.00 50.23 ? 1414 GOL A O1 1 HETATM 2811 C C2 . GOL M 5 . ? -12.139 17.580 56.926 1.00 47.48 ? 1414 GOL A C2 1 HETATM 2812 O O2 . GOL M 5 . ? -12.036 18.870 56.314 1.00 45.33 ? 1414 GOL A O2 1 HETATM 2813 C C3 . GOL M 5 . ? -13.242 16.796 56.220 1.00 47.63 ? 1414 GOL A C3 1 HETATM 2814 O O3 . GOL M 5 . ? -13.675 15.717 57.054 1.00 52.72 ? 1414 GOL A O3 1 HETATM 2815 O O . HOH N 6 . ? -11.791 25.647 55.396 1.00 39.89 ? 2001 HOH A O 1 HETATM 2816 O O . HOH N 6 . ? -11.201 -1.190 28.212 1.00 28.16 ? 2002 HOH A O 1 HETATM 2817 O O . HOH N 6 . ? -14.187 -3.022 25.387 1.00 42.67 ? 2003 HOH A O 1 HETATM 2818 O O . HOH N 6 . ? -15.260 2.522 27.501 1.00 36.28 ? 2004 HOH A O 1 HETATM 2819 O O . HOH N 6 . ? -17.895 -2.444 30.078 1.00 30.01 ? 2005 HOH A O 1 HETATM 2820 O O . HOH N 6 . ? -16.045 -3.935 32.971 1.00 41.31 ? 2006 HOH A O 1 HETATM 2821 O O . HOH N 6 . ? -12.817 -5.831 35.233 1.00 38.96 ? 2007 HOH A O 1 HETATM 2822 O O . HOH N 6 . ? -17.421 -2.582 37.299 1.00 31.96 ? 2008 HOH A O 1 HETATM 2823 O O . HOH N 6 . ? -17.820 -1.884 42.052 1.00 36.21 ? 2009 HOH A O 1 HETATM 2824 O O . HOH N 6 . ? -13.432 -3.122 38.826 1.00 39.41 ? 2010 HOH A O 1 HETATM 2825 O O . HOH N 6 . ? -18.099 -0.457 45.210 1.00 29.40 ? 2011 HOH A O 1 HETATM 2826 O O . HOH N 6 . ? -11.986 -3.111 41.629 1.00 24.91 ? 2012 HOH A O 1 HETATM 2827 O O . HOH N 6 . ? -11.216 -2.011 48.203 1.00 22.51 ? 2013 HOH A O 1 HETATM 2828 O O . HOH N 6 . ? -16.973 -3.946 49.198 1.00 40.74 ? 2014 HOH A O 1 HETATM 2829 O O . HOH N 6 . ? -12.309 0.812 52.232 1.00 16.56 ? 2015 HOH A O 1 HETATM 2830 O O . HOH N 6 . ? -14.371 2.689 50.227 1.00 19.07 ? 2016 HOH A O 1 HETATM 2831 O O . HOH N 6 . ? -19.223 2.186 54.413 1.00 43.23 ? 2017 HOH A O 1 HETATM 2832 O O . HOH N 6 . ? -16.806 4.510 56.615 1.00 38.49 ? 2018 HOH A O 1 HETATM 2833 O O . HOH N 6 . ? -14.277 4.508 57.670 1.00 32.50 ? 2019 HOH A O 1 HETATM 2834 O O . HOH N 6 . ? -6.794 5.196 57.083 1.00 30.86 ? 2020 HOH A O 1 HETATM 2835 O O . HOH N 6 . ? -2.059 0.043 52.826 1.00 17.16 ? 2021 HOH A O 1 HETATM 2836 O O . HOH N 6 . ? -20.228 0.617 48.023 1.00 38.65 ? 2022 HOH A O 1 HETATM 2837 O O . HOH N 6 . ? -8.100 7.844 56.292 1.00 29.25 ? 2023 HOH A O 1 HETATM 2838 O O . HOH N 6 . ? -3.979 4.459 57.072 1.00 28.86 ? 2024 HOH A O 1 HETATM 2839 O O . HOH N 6 . ? -2.768 -0.852 37.392 1.00 28.23 ? 2025 HOH A O 1 HETATM 2840 O O . HOH N 6 . ? -1.739 -0.718 43.486 1.00 19.40 ? 2026 HOH A O 1 HETATM 2841 O O . HOH N 6 . ? -11.852 -4.995 37.498 1.00 41.11 ? 2027 HOH A O 1 HETATM 2842 O O . HOH N 6 . ? -10.750 -5.628 41.955 1.00 38.59 ? 2028 HOH A O 1 HETATM 2843 O O . HOH N 6 . ? -8.592 -9.229 40.254 1.00 35.00 ? 2029 HOH A O 1 HETATM 2844 O O . HOH N 6 . ? -4.517 -1.054 31.666 1.00 33.43 ? 2030 HOH A O 1 HETATM 2845 O O . HOH N 6 . ? -7.229 3.378 22.619 1.00 39.40 ? 2031 HOH A O 1 HETATM 2846 O O . HOH N 6 . ? -8.412 -2.297 29.014 1.00 33.88 ? 2032 HOH A O 1 HETATM 2847 O O . HOH N 6 . ? -22.727 3.441 43.258 1.00 36.17 ? 2033 HOH A O 1 HETATM 2848 O O . HOH N 6 . ? -18.174 13.430 50.437 1.00 30.32 ? 2034 HOH A O 1 HETATM 2849 O O . HOH N 6 . ? -10.853 -0.612 25.437 1.00 44.17 ? 2035 HOH A O 1 HETATM 2850 O O . HOH N 6 . ? -4.856 2.455 24.239 1.00 35.34 ? 2036 HOH A O 1 HETATM 2851 O O . HOH N 6 . ? -1.945 0.290 24.760 1.00 46.24 ? 2037 HOH A O 1 HETATM 2852 O O . HOH N 6 . ? -19.660 3.038 46.769 1.00 28.97 ? 2038 HOH A O 1 HETATM 2853 O O . HOH N 6 . ? -17.355 13.071 53.015 1.00 36.34 ? 2039 HOH A O 1 HETATM 2854 O O . HOH N 6 . ? -20.746 1.419 42.903 1.00 37.90 ? 2040 HOH A O 1 HETATM 2855 O O . HOH N 6 . ? -10.766 6.190 27.234 1.00 38.58 ? 2041 HOH A O 1 HETATM 2856 O O . HOH N 6 . ? -4.110 -2.096 56.174 1.00 33.95 ? 2042 HOH A O 1 HETATM 2857 O O . HOH N 6 . ? -14.933 7.512 28.589 1.00 29.98 ? 2043 HOH A O 1 HETATM 2858 O O . HOH N 6 . ? 5.843 6.859 43.114 1.00 17.04 ? 2044 HOH A O 1 HETATM 2859 O O . HOH N 6 . ? -6.466 11.135 26.026 1.00 34.23 ? 2045 HOH A O 1 HETATM 2860 O O . HOH N 6 . ? -24.016 7.318 42.032 1.00 41.42 ? 2046 HOH A O 1 HETATM 2861 O O . HOH N 6 . ? -22.323 5.933 45.481 1.00 39.72 ? 2047 HOH A O 1 HETATM 2862 O O . HOH N 6 . ? -22.943 14.723 41.531 1.00 33.68 ? 2048 HOH A O 1 HETATM 2863 O O . HOH N 6 . ? -16.677 15.142 48.938 1.00 22.34 ? 2049 HOH A O 1 HETATM 2864 O O . HOH N 6 . ? -20.097 12.710 44.948 1.00 26.22 ? 2050 HOH A O 1 HETATM 2865 O O . HOH N 6 . ? -19.679 8.377 50.494 1.00 28.79 ? 2051 HOH A O 1 HETATM 2866 O O . HOH N 6 . ? -18.750 11.559 47.576 1.00 30.92 ? 2052 HOH A O 1 HETATM 2867 O O . HOH N 6 . ? -18.591 4.549 48.746 1.00 25.39 ? 2053 HOH A O 1 HETATM 2868 O O . HOH N 6 . ? -17.368 4.254 51.276 1.00 26.14 ? 2054 HOH A O 1 HETATM 2869 O O . HOH N 6 . ? -17.188 10.163 53.093 1.00 32.47 ? 2055 HOH A O 1 HETATM 2870 O O . HOH N 6 . ? 5.154 3.272 57.905 1.00 40.46 ? 2056 HOH A O 1 HETATM 2871 O O . HOH N 6 . ? 6.210 11.531 63.376 1.00 36.22 ? 2057 HOH A O 1 HETATM 2872 O O . HOH N 6 . ? -18.456 2.290 44.402 1.00 30.74 ? 2058 HOH A O 1 HETATM 2873 O O . HOH N 6 . ? 12.844 11.927 54.446 1.00 30.08 ? 2059 HOH A O 1 HETATM 2874 O O . HOH N 6 . ? -17.366 5.566 53.788 1.00 25.37 ? 2060 HOH A O 1 HETATM 2875 O O . HOH N 6 . ? -13.828 7.570 57.610 1.00 48.54 ? 2061 HOH A O 1 HETATM 2876 O O . HOH N 6 . ? -15.230 9.239 55.200 1.00 45.30 ? 2062 HOH A O 1 HETATM 2877 O O . HOH N 6 . ? 9.265 16.349 43.688 1.00 36.13 ? 2063 HOH A O 1 HETATM 2878 O O . HOH N 6 . ? 0.014 1.811 53.391 1.00 18.76 ? 2064 HOH A O 1 HETATM 2879 O O . HOH N 6 . ? -1.862 4.391 55.383 1.00 20.04 ? 2065 HOH A O 1 HETATM 2880 O O . HOH N 6 . ? -8.018 7.010 53.788 1.00 15.72 ? 2066 HOH A O 1 HETATM 2881 O O . HOH N 6 . ? -4.302 0.093 54.775 1.00 26.16 ? 2067 HOH A O 1 HETATM 2882 O O . HOH N 6 . ? -0.260 -0.038 47.754 0.50 25.82 ? 2068 HOH A O 1 HETATM 2883 O O . HOH N 6 . ? -0.802 1.938 43.382 1.00 13.90 ? 2069 HOH A O 1 HETATM 2884 O O . HOH N 6 . ? 1.262 1.726 46.175 1.00 17.64 ? 2070 HOH A O 1 HETATM 2885 O O . HOH N 6 . ? -1.888 1.590 37.247 1.00 23.82 ? 2071 HOH A O 1 HETATM 2886 O O . HOH N 6 . ? 2.306 5.993 36.759 1.00 22.42 ? 2072 HOH A O 1 HETATM 2887 O O . HOH N 6 . ? 4.306 5.679 38.743 1.00 31.25 ? 2073 HOH A O 1 HETATM 2888 O O . HOH N 6 . ? 4.418 4.590 42.317 1.00 14.15 ? 2074 HOH A O 1 HETATM 2889 O O . HOH N 6 . ? -16.722 20.054 45.219 1.00 29.75 ? 2075 HOH A O 1 HETATM 2890 O O . HOH N 6 . ? -17.997 17.497 48.298 1.00 28.39 ? 2076 HOH A O 1 HETATM 2891 O O . HOH N 6 . ? 3.037 3.909 32.052 1.00 22.57 ? 2077 HOH A O 1 HETATM 2892 O O . HOH N 6 . ? -14.869 16.365 50.455 1.00 24.27 ? 2078 HOH A O 1 HETATM 2893 O O . HOH N 6 . ? 0.411 4.933 28.826 1.00 23.37 ? 2079 HOH A O 1 HETATM 2894 O O . HOH N 6 . ? 0.420 3.804 26.301 1.00 38.22 ? 2080 HOH A O 1 HETATM 2895 O O . HOH N 6 . ? -1.435 5.457 24.772 1.00 36.57 ? 2081 HOH A O 1 HETATM 2896 O O . HOH N 6 . ? 4.886 25.822 59.505 1.00 22.55 ? 2082 HOH A O 1 HETATM 2897 O O . HOH N 6 . ? -7.700 9.126 27.319 1.00 27.43 ? 2083 HOH A O 1 HETATM 2898 O O . HOH N 6 . ? -2.226 9.478 23.434 1.00 37.11 ? 2084 HOH A O 1 HETATM 2899 O O . HOH N 6 . ? 7.456 25.869 58.965 1.00 33.91 ? 2085 HOH A O 1 HETATM 2900 O O . HOH N 6 . ? 10.545 25.187 57.900 1.00 33.37 ? 2086 HOH A O 1 HETATM 2901 O O . HOH N 6 . ? 11.163 21.874 53.030 1.00 42.01 ? 2087 HOH A O 1 HETATM 2902 O O . HOH N 6 . ? 12.126 24.593 55.831 1.00 39.64 ? 2088 HOH A O 1 HETATM 2903 O O . HOH N 6 . ? -19.251 6.948 32.417 1.00 33.25 ? 2089 HOH A O 1 HETATM 2904 O O . HOH N 6 . ? -18.866 10.060 35.482 1.00 17.17 ? 2090 HOH A O 1 HETATM 2905 O O . HOH N 6 . ? -18.205 7.117 29.662 1.00 40.28 ? 2091 HOH A O 1 HETATM 2906 O O . HOH N 6 . ? -17.007 14.064 46.505 1.00 22.00 ? 2092 HOH A O 1 HETATM 2907 O O . HOH N 6 . ? -13.153 9.908 56.694 1.00 49.12 ? 2093 HOH A O 1 HETATM 2908 O O . HOH N 6 . ? -10.544 8.844 57.264 1.00 43.33 ? 2094 HOH A O 1 HETATM 2909 O O . HOH N 6 . ? -9.459 11.386 58.605 1.00 40.78 ? 2095 HOH A O 1 HETATM 2910 O O . HOH N 6 . ? -9.367 14.066 57.703 1.00 36.40 ? 2096 HOH A O 1 HETATM 2911 O O . HOH N 6 . ? -10.623 24.146 57.711 1.00 41.50 ? 2097 HOH A O 1 HETATM 2912 O O . HOH N 6 . ? -1.903 12.521 53.424 1.00 13.57 ? 2098 HOH A O 1 HETATM 2913 O O . HOH N 6 . ? -6.008 9.065 57.879 1.00 18.99 ? 2099 HOH A O 1 HETATM 2914 O O . HOH N 6 . ? -3.714 7.506 58.515 1.00 21.13 ? 2100 HOH A O 1 HETATM 2915 O O . HOH N 6 . ? 0.253 13.112 55.097 1.00 16.28 ? 2101 HOH A O 1 HETATM 2916 O O . HOH N 6 . ? -0.825 10.562 60.407 1.00 19.80 ? 2102 HOH A O 1 HETATM 2917 O O . HOH N 6 . ? -2.359 8.105 61.079 1.00 35.60 ? 2103 HOH A O 1 HETATM 2918 O O . HOH N 6 . ? 2.579 3.778 59.060 1.00 30.11 ? 2104 HOH A O 1 HETATM 2919 O O . HOH N 6 . ? 2.039 7.566 60.924 1.00 25.21 ? 2105 HOH A O 1 HETATM 2920 O O . HOH N 6 . ? 0.917 2.103 56.141 1.00 28.08 ? 2106 HOH A O 1 HETATM 2921 O O . HOH N 6 . ? 14.186 18.275 36.246 1.00 49.73 ? 2107 HOH A O 1 HETATM 2922 O O . HOH N 6 . ? 1.704 12.619 62.581 1.00 33.69 ? 2108 HOH A O 1 HETATM 2923 O O . HOH N 6 . ? 5.557 10.641 60.915 1.00 25.78 ? 2109 HOH A O 1 HETATM 2924 O O . HOH N 6 . ? 7.469 4.474 55.390 1.00 39.24 ? 2110 HOH A O 1 HETATM 2925 O O . HOH N 6 . ? 8.682 6.498 57.861 1.00 34.40 ? 2111 HOH A O 1 HETATM 2926 O O . HOH N 6 . ? 3.624 3.868 61.625 1.00 40.85 ? 2112 HOH A O 1 HETATM 2927 O O . HOH N 6 . ? 8.201 6.240 53.356 1.00 27.87 ? 2113 HOH A O 1 HETATM 2928 O O . HOH N 6 . ? 2.420 1.286 49.182 1.00 18.10 ? 2114 HOH A O 1 HETATM 2929 O O . HOH N 6 . ? -11.897 29.110 46.246 1.00 31.56 ? 2115 HOH A O 1 HETATM 2930 O O . HOH N 6 . ? 10.613 12.727 56.038 1.00 16.39 ? 2116 HOH A O 1 HETATM 2931 O O . HOH N 6 . ? 9.759 9.489 59.073 1.00 43.67 ? 2117 HOH A O 1 HETATM 2932 O O . HOH N 6 . ? -3.117 28.936 58.013 1.00 30.83 ? 2118 HOH A O 1 HETATM 2933 O O . HOH N 6 . ? -7.077 17.038 61.609 1.00 44.33 ? 2119 HOH A O 1 HETATM 2934 O O . HOH N 6 . ? 11.086 9.368 47.220 1.00 25.69 ? 2120 HOH A O 1 HETATM 2935 O O . HOH N 6 . ? 9.089 13.648 49.653 1.00 22.32 ? 2121 HOH A O 1 HETATM 2936 O O . HOH N 6 . ? 12.784 11.258 49.862 1.00 36.99 ? 2122 HOH A O 1 HETATM 2937 O O . HOH N 6 . ? 8.508 2.917 47.472 1.00 13.78 ? 2123 HOH A O 1 HETATM 2938 O O . HOH N 6 . ? 9.686 5.295 50.648 1.00 32.55 ? 2124 HOH A O 1 HETATM 2939 O O . HOH N 6 . ? 6.070 2.611 54.003 1.00 15.04 ? 2125 HOH A O 1 HETATM 2940 O O . HOH N 6 . ? 1.141 31.807 56.930 1.00 35.26 ? 2126 HOH A O 1 HETATM 2941 O O . HOH N 6 . ? 8.783 26.663 56.657 1.00 35.57 ? 2127 HOH A O 1 HETATM 2942 O O . HOH N 6 . ? 5.401 8.059 45.645 1.00 11.95 ? 2128 HOH A O 1 HETATM 2943 O O . HOH N 6 . ? 7.430 15.216 45.388 1.00 23.28 ? 2129 HOH A O 1 HETATM 2944 O O . HOH N 6 . ? 10.126 8.416 43.481 1.00 28.34 ? 2130 HOH A O 1 HETATM 2945 O O . HOH N 6 . ? 10.996 13.093 45.311 1.00 37.82 ? 2131 HOH A O 1 HETATM 2946 O O . HOH N 6 . ? 14.209 20.318 28.355 1.00 34.07 ? 2132 HOH A O 1 HETATM 2947 O O . HOH N 6 . ? 6.189 9.002 41.261 1.00 21.50 ? 2133 HOH A O 1 HETATM 2948 O O . HOH N 6 . ? 2.893 10.681 32.616 1.00 11.19 ? 2134 HOH A O 1 HETATM 2949 O O . HOH N 6 . ? 8.616 8.067 33.774 1.00 28.27 ? 2135 HOH A O 1 HETATM 2950 O O . HOH N 6 . ? 7.841 10.019 28.756 1.00 31.80 ? 2136 HOH A O 1 HETATM 2951 O O . HOH N 6 . ? -11.005 31.588 45.837 1.00 32.09 ? 2137 HOH A O 1 HETATM 2952 O O . HOH N 6 . ? -6.625 32.631 52.259 1.00 32.89 ? 2138 HOH A O 1 HETATM 2953 O O . HOH N 6 . ? 5.266 10.100 25.622 1.00 39.55 ? 2139 HOH A O 1 HETATM 2954 O O . HOH N 6 . ? 2.103 4.649 24.458 1.00 47.07 ? 2140 HOH A O 1 HETATM 2955 O O . HOH N 6 . ? 13.409 23.226 40.964 1.00 37.31 ? 2141 HOH A O 1 HETATM 2956 O O . HOH N 6 . ? 15.210 21.088 38.080 1.00 38.90 ? 2142 HOH A O 1 HETATM 2957 O O . HOH N 6 . ? -6.392 13.300 27.372 1.00 30.32 ? 2143 HOH A O 1 HETATM 2958 O O . HOH N 6 . ? 14.407 23.748 28.149 1.00 41.26 ? 2144 HOH A O 1 HETATM 2959 O O . HOH N 6 . ? 11.631 19.967 23.732 1.00 42.43 ? 2145 HOH A O 1 HETATM 2960 O O . HOH N 6 . ? -16.440 10.374 27.461 1.00 33.05 ? 2146 HOH A O 1 HETATM 2961 O O . HOH N 6 . ? -10.225 36.900 34.812 1.00 39.49 ? 2147 HOH A O 1 HETATM 2962 O O . HOH N 6 . ? -11.170 32.371 49.461 1.00 37.57 ? 2148 HOH A O 1 HETATM 2963 O O . HOH N 6 . ? -12.284 35.851 46.770 1.00 42.23 ? 2149 HOH A O 1 HETATM 2964 O O . HOH N 6 . ? -23.519 18.747 38.440 1.00 18.03 ? 2150 HOH A O 1 HETATM 2965 O O . HOH N 6 . ? -21.317 19.463 41.137 1.00 39.40 ? 2151 HOH A O 1 HETATM 2966 O O . HOH N 6 . ? -17.419 21.971 40.339 1.00 39.60 ? 2152 HOH A O 1 HETATM 2967 O O . HOH N 6 . ? -15.549 18.925 43.051 1.00 18.90 ? 2153 HOH A O 1 HETATM 2968 O O . HOH N 6 . ? -18.961 17.086 45.965 1.00 27.46 ? 2154 HOH A O 1 HETATM 2969 O O . HOH N 6 . ? -21.668 17.627 45.141 1.00 46.54 ? 2155 HOH A O 1 HETATM 2970 O O . HOH N 6 . ? 19.989 26.840 30.758 1.00 29.95 ? 2156 HOH A O 1 HETATM 2971 O O . HOH N 6 . ? 17.522 28.730 27.464 1.00 42.88 ? 2157 HOH A O 1 HETATM 2972 O O . HOH N 6 . ? -8.470 17.243 54.619 1.00 15.59 ? 2158 HOH A O 1 HETATM 2973 O O . HOH N 6 . ? -13.103 15.500 52.433 1.00 17.96 ? 2159 HOH A O 1 HETATM 2974 O O . HOH N 6 . ? 3.435 35.595 24.204 1.00 30.09 ? 2160 HOH A O 1 HETATM 2975 O O . HOH N 6 . ? -4.356 14.895 58.548 1.00 13.00 ? 2161 HOH A O 1 HETATM 2976 O O . HOH N 6 . ? -1.412 14.676 56.719 1.00 12.42 ? 2162 HOH A O 1 HETATM 2977 O O . HOH N 6 . ? -6.146 13.311 59.867 1.00 42.89 ? 2163 HOH A O 1 HETATM 2978 O O . HOH N 6 . ? -7.139 10.899 59.532 1.00 47.85 ? 2164 HOH A O 1 HETATM 2979 O O . HOH N 6 . ? -6.495 17.818 56.427 1.00 20.02 ? 2165 HOH A O 1 HETATM 2980 O O . HOH N 6 . ? -7.253 20.617 57.444 1.00 19.59 ? 2166 HOH A O 1 HETATM 2981 O O . HOH N 6 . ? 1.083 15.367 62.813 1.00 22.39 ? 2167 HOH A O 1 HETATM 2982 O O . HOH N 6 . ? -1.674 17.030 64.120 1.00 39.38 ? 2168 HOH A O 1 HETATM 2983 O O . HOH N 6 . ? -5.150 11.759 62.204 1.00 45.55 ? 2169 HOH A O 1 HETATM 2984 O O . HOH N 6 . ? 15.833 29.007 50.126 1.00 44.60 ? 2170 HOH A O 1 HETATM 2985 O O . HOH N 6 . ? 3.026 24.015 58.751 1.00 19.66 ? 2171 HOH A O 1 HETATM 2986 O O . HOH N 6 . ? 3.574 20.989 65.377 1.00 27.77 ? 2172 HOH A O 1 HETATM 2987 O O . HOH N 6 . ? 8.991 23.987 59.853 1.00 24.47 ? 2173 HOH A O 1 HETATM 2988 O O . HOH N 6 . ? 18.002 33.313 26.259 1.00 25.00 ? 2174 HOH A O 1 HETATM 2989 O O . HOH N 6 . ? 6.509 26.483 63.259 1.00 38.07 ? 2175 HOH A O 1 HETATM 2990 O O . HOH N 6 . ? 10.443 24.039 62.366 1.00 35.73 ? 2176 HOH A O 1 HETATM 2991 O O . HOH N 6 . ? 12.392 22.000 62.601 1.00 29.19 ? 2177 HOH A O 1 HETATM 2992 O O . HOH N 6 . ? 9.696 14.807 64.312 1.00 40.57 ? 2178 HOH A O 1 HETATM 2993 O O . HOH N 6 . ? 11.863 18.747 54.407 1.00 31.23 ? 2179 HOH A O 1 HETATM 2994 O O . HOH N 6 . ? 12.587 22.268 55.247 1.00 34.66 ? 2180 HOH A O 1 HETATM 2995 O O . HOH N 6 . ? -6.463 48.816 51.311 1.00 39.72 ? 2181 HOH A O 1 HETATM 2996 O O . HOH N 6 . ? 11.641 13.035 58.774 1.00 32.65 ? 2182 HOH A O 1 HETATM 2997 O O . HOH N 6 . ? 14.529 15.298 55.297 1.00 37.18 ? 2183 HOH A O 1 HETATM 2998 O O . HOH N 6 . ? 12.425 47.656 50.558 1.00 30.56 ? 2184 HOH A O 1 HETATM 2999 O O . HOH N 6 . ? 8.351 18.842 53.522 1.00 18.67 ? 2185 HOH A O 1 HETATM 3000 O O . HOH N 6 . ? 2.964 13.823 54.243 1.00 15.00 ? 2186 HOH A O 1 HETATM 3001 O O . HOH N 6 . ? 13.576 12.740 51.941 1.00 41.57 ? 2187 HOH A O 1 HETATM 3002 O O . HOH N 6 . ? 11.687 17.589 50.917 1.00 42.43 ? 2188 HOH A O 1 HETATM 3003 O O . HOH N 6 . ? 8.654 17.883 50.935 1.00 27.91 ? 2189 HOH A O 1 HETATM 3004 O O . HOH N 6 . ? 5.353 18.088 47.386 1.00 14.99 ? 2190 HOH A O 1 HETATM 3005 O O . HOH N 6 . ? 8.416 16.315 47.776 1.00 35.04 ? 2191 HOH A O 1 HETATM 3006 O O . HOH N 6 . ? 8.942 21.166 52.107 1.00 37.80 ? 2192 HOH A O 1 HETATM 3007 O O . HOH N 6 . ? 26.878 34.307 53.425 1.00 38.79 ? 2193 HOH A O 1 HETATM 3008 O O . HOH N 6 . ? 0.831 17.242 48.522 1.00 10.16 ? 2194 HOH A O 1 HETATM 3009 O O . HOH N 6 . ? 27.990 43.921 41.997 1.00 36.12 ? 2195 HOH A O 1 HETATM 3010 O O . HOH N 6 . ? 6.549 17.636 43.022 1.00 25.21 ? 2196 HOH A O 1 HETATM 3011 O O . HOH N 6 . ? 30.562 36.108 38.266 1.00 43.37 ? 2197 HOH A O 1 HETATM 3012 O O . HOH N 6 . ? 10.595 12.595 37.578 1.00 33.38 ? 2198 HOH A O 1 HETATM 3013 O O . HOH N 6 . ? 10.435 11.075 39.668 1.00 46.11 ? 2199 HOH A O 1 HETATM 3014 O O . HOH N 6 . ? 10.678 15.209 41.851 1.00 34.74 ? 2200 HOH A O 1 HETATM 3015 O O . HOH N 6 . ? 6.096 15.818 38.672 1.00 18.75 ? 2201 HOH A O 1 HETATM 3016 O O . HOH N 6 . ? 9.936 10.405 34.222 1.00 32.76 ? 2202 HOH A O 1 HETATM 3017 O O . HOH N 6 . ? 6.834 12.973 26.696 1.00 26.42 ? 2203 HOH A O 1 HETATM 3018 O O . HOH N 6 . ? -4.758 14.964 25.848 1.00 30.82 ? 2204 HOH A O 1 HETATM 3019 O O . HOH N 6 . ? 9.422 48.380 53.900 1.00 43.27 ? 2205 HOH A O 1 HETATM 3020 O O . HOH N 6 . ? 10.270 51.605 51.213 1.00 39.61 ? 2206 HOH A O 1 HETATM 3021 O O . HOH N 6 . ? -4.293 17.322 27.033 1.00 35.04 ? 2207 HOH A O 1 HETATM 3022 O O . HOH N 6 . ? -8.564 19.775 30.870 1.00 34.88 ? 2208 HOH A O 1 HETATM 3023 O O . HOH N 6 . ? -14.172 22.570 39.412 1.00 28.23 ? 2209 HOH A O 1 HETATM 3024 O O . HOH N 6 . ? -14.601 21.439 42.009 1.00 29.61 ? 2210 HOH A O 1 HETATM 3025 O O . HOH N 6 . ? -16.467 19.964 47.701 1.00 23.99 ? 2211 HOH A O 1 HETATM 3026 O O . HOH N 6 . ? -15.998 23.462 48.202 1.00 47.04 ? 2212 HOH A O 1 HETATM 3027 O O . HOH N 6 . ? -12.427 25.306 50.756 1.00 42.13 ? 2213 HOH A O 1 HETATM 3028 O O . HOH N 6 . ? -9.470 23.220 52.341 1.00 18.89 ? 2214 HOH A O 1 HETATM 3029 O O . HOH N 6 . ? -9.565 22.175 56.376 1.00 35.96 ? 2215 HOH A O 1 HETATM 3030 O O . HOH N 6 . ? 7.764 56.992 41.764 1.00 41.43 ? 2216 HOH A O 1 HETATM 3031 O O . HOH N 6 . ? 7.882 19.305 47.335 1.00 29.99 ? 2217 HOH A O 1 HETATM 3032 O O . HOH N 6 . ? 7.957 21.766 48.819 1.00 28.09 ? 2218 HOH A O 1 HETATM 3033 O O . HOH N 6 . ? 22.498 48.775 41.982 1.00 37.69 ? 2219 HOH A O 1 HETATM 3034 O O . HOH N 6 . ? 8.062 20.347 38.899 1.00 26.79 ? 2220 HOH A O 1 HETATM 3035 O O . HOH N 6 . ? 10.793 20.518 38.571 1.00 30.51 ? 2221 HOH A O 1 HETATM 3036 O O . HOH N 6 . ? 12.350 16.394 35.133 1.00 18.62 ? 2222 HOH A O 1 HETATM 3037 O O . HOH N 6 . ? 9.589 12.435 28.464 1.00 31.04 ? 2223 HOH A O 1 HETATM 3038 O O . HOH N 6 . ? 10.857 11.092 31.834 1.00 30.51 ? 2224 HOH A O 1 HETATM 3039 O O . HOH N 6 . ? 8.330 17.776 26.473 1.00 21.85 ? 2225 HOH A O 1 HETATM 3040 O O . HOH N 6 . ? 4.534 17.576 21.932 1.00 46.62 ? 2226 HOH A O 1 HETATM 3041 O O . HOH N 6 . ? -2.459 19.019 25.212 1.00 38.90 ? 2227 HOH A O 1 HETATM 3042 O O . HOH N 6 . ? -0.142 21.062 22.362 1.00 44.11 ? 2228 HOH A O 1 HETATM 3043 O O . HOH N 6 . ? -1.512 22.239 26.476 1.00 30.79 ? 2229 HOH A O 1 HETATM 3044 O O . HOH N 6 . ? -14.163 27.136 35.899 1.00 40.73 ? 2230 HOH A O 1 HETATM 3045 O O . HOH N 6 . ? -12.197 26.942 38.798 1.00 44.26 ? 2231 HOH A O 1 HETATM 3046 O O . HOH N 6 . ? -10.101 27.192 45.341 1.00 24.00 ? 2232 HOH A O 1 HETATM 3047 O O . HOH N 6 . ? -5.017 28.650 53.615 1.00 25.11 ? 2233 HOH A O 1 HETATM 3048 O O . HOH N 6 . ? -10.939 27.787 50.762 1.00 25.10 ? 2234 HOH A O 1 HETATM 3049 O O . HOH N 6 . ? -9.789 30.211 53.164 1.00 34.64 ? 2235 HOH A O 1 HETATM 3050 O O . HOH N 6 . ? -5.142 27.880 56.531 1.00 18.16 ? 2236 HOH A O 1 HETATM 3051 O O . HOH N 6 . ? -7.656 27.525 61.692 1.00 37.51 ? 2237 HOH A O 1 HETATM 3052 O O . HOH N 6 . ? -10.019 24.135 64.459 1.00 38.96 ? 2238 HOH A O 1 HETATM 3053 O O . HOH N 6 . ? -7.948 16.994 58.870 1.00 38.05 ? 2239 HOH A O 1 HETATM 3054 O O . HOH N 6 . ? -4.402 30.139 68.954 1.00 42.91 ? 2240 HOH A O 1 HETATM 3055 O O . HOH N 6 . ? 6.701 29.174 53.752 1.00 47.99 ? 2241 HOH A O 1 HETATM 3056 O O . HOH N 6 . ? 3.152 30.860 56.016 1.00 29.94 ? 2242 HOH A O 1 HETATM 3057 O O . HOH N 6 . ? 4.774 27.995 52.207 1.00 18.21 ? 2243 HOH A O 1 HETATM 3058 O O . HOH N 6 . ? 8.392 25.920 54.150 1.00 28.64 ? 2244 HOH A O 1 HETATM 3059 O O . HOH N 6 . ? 7.129 25.191 47.923 1.00 21.80 ? 2245 HOH A O 1 HETATM 3060 O O . HOH N 6 . ? 10.728 25.839 51.399 1.00 49.64 ? 2246 HOH A O 1 HETATM 3061 O O . HOH N 6 . ? 8.268 28.688 50.105 1.00 30.42 ? 2247 HOH A O 1 HETATM 3062 O O . HOH N 6 . ? 9.074 27.966 52.653 1.00 46.04 ? 2248 HOH A O 1 HETATM 3063 O O . HOH N 6 . ? 8.024 23.009 45.478 1.00 30.85 ? 2249 HOH A O 1 HETATM 3064 O O . HOH N 6 . ? 7.853 26.704 44.388 1.00 21.16 ? 2250 HOH A O 1 HETATM 3065 O O . HOH N 6 . ? 7.551 20.047 43.002 1.00 36.29 ? 2251 HOH A O 1 HETATM 3066 O O . HOH N 6 . ? 11.766 19.229 36.002 1.00 31.67 ? 2252 HOH A O 1 HETATM 3067 O O . HOH N 6 . ? 13.516 13.859 29.678 1.00 47.29 ? 2253 HOH A O 1 HETATM 3068 O O . HOH N 6 . ? 12.490 17.096 27.708 1.00 31.51 ? 2254 HOH A O 1 HETATM 3069 O O . HOH N 6 . ? 10.461 18.763 27.946 1.00 22.96 ? 2255 HOH A O 1 HETATM 3070 O O . HOH N 6 . ? 5.119 23.004 29.404 1.00 23.70 ? 2256 HOH A O 1 HETATM 3071 O O . HOH N 6 . ? 11.513 21.167 28.270 1.00 18.16 ? 2257 HOH A O 1 HETATM 3072 O O . HOH N 6 . ? 7.452 19.083 22.663 1.00 34.08 ? 2258 HOH A O 1 HETATM 3073 O O . HOH N 6 . ? 9.477 22.122 21.530 1.00 48.68 ? 2259 HOH A O 1 HETATM 3074 O O . HOH N 6 . ? 0.972 25.821 26.295 1.00 29.81 ? 2260 HOH A O 1 HETATM 3075 O O . HOH N 6 . ? -3.319 26.592 25.677 1.00 34.07 ? 2261 HOH A O 1 HETATM 3076 O O . HOH N 6 . ? -12.354 29.676 37.140 1.00 38.54 ? 2262 HOH A O 1 HETATM 3077 O O . HOH N 6 . ? -10.229 31.263 37.828 1.00 24.48 ? 2263 HOH A O 1 HETATM 3078 O O . HOH N 6 . ? -8.494 32.020 44.810 1.00 19.72 ? 2264 HOH A O 1 HETATM 3079 O O . HOH N 6 . ? -4.715 30.911 51.953 1.00 25.86 ? 2265 HOH A O 1 HETATM 3080 O O . HOH N 6 . ? -1.667 32.219 52.992 1.00 24.82 ? 2266 HOH A O 1 HETATM 3081 O O . HOH N 6 . ? -1.712 30.429 55.713 1.00 43.82 ? 2267 HOH A O 1 HETATM 3082 O O . HOH N 6 . ? 1.146 33.967 51.601 1.00 34.18 ? 2268 HOH A O 1 HETATM 3083 O O . HOH N 6 . ? 2.953 32.913 53.334 1.00 33.26 ? 2269 HOH A O 1 HETATM 3084 O O . HOH N 6 . ? 8.285 28.553 46.930 1.00 34.28 ? 2270 HOH A O 1 HETATM 3085 O O . HOH N 6 . ? 7.826 32.371 45.378 1.00 23.32 ? 2271 HOH A O 1 HETATM 3086 O O . HOH N 6 . ? 8.907 30.380 42.904 1.00 26.07 ? 2272 HOH A O 1 HETATM 3087 O O . HOH N 6 . ? 13.028 25.722 42.058 1.00 24.23 ? 2273 HOH A O 1 HETATM 3088 O O . HOH N 6 . ? 12.681 21.284 36.908 1.00 30.43 ? 2274 HOH A O 1 HETATM 3089 O O . HOH N 6 . ? 16.798 24.026 32.713 1.00 16.74 ? 2275 HOH A O 1 HETATM 3090 O O . HOH N 6 . ? 15.632 20.303 34.859 1.00 49.79 ? 2276 HOH A O 1 HETATM 3091 O O . HOH N 6 . ? 13.149 25.798 29.344 1.00 15.83 ? 2277 HOH A O 1 HETATM 3092 O O . HOH N 6 . ? 11.918 25.844 22.424 1.00 34.00 ? 2278 HOH A O 1 HETATM 3093 O O . HOH N 6 . ? 11.656 22.157 25.617 1.00 26.73 ? 2279 HOH A O 1 HETATM 3094 O O . HOH N 6 . ? 7.591 29.686 19.196 1.00 47.82 ? 2280 HOH A O 1 HETATM 3095 O O . HOH N 6 . ? 2.241 28.362 25.571 1.00 30.00 ? 2281 HOH A O 1 HETATM 3096 O O . HOH N 6 . ? -1.548 28.523 24.344 1.00 35.30 ? 2282 HOH A O 1 HETATM 3097 O O . HOH N 6 . ? -8.342 35.241 29.264 1.00 32.31 ? 2283 HOH A O 1 HETATM 3098 O O . HOH N 6 . ? -7.088 34.482 26.296 1.00 44.13 ? 2284 HOH A O 1 HETATM 3099 O O . HOH N 6 . ? -4.048 32.407 26.265 1.00 44.49 ? 2285 HOH A O 1 HETATM 3100 O O . HOH N 6 . ? -9.784 36.064 32.206 1.00 36.13 ? 2286 HOH A O 1 HETATM 3101 O O . HOH N 6 . ? -8.935 35.842 37.019 1.00 19.66 ? 2287 HOH A O 1 HETATM 3102 O O . HOH N 6 . ? -10.386 33.856 37.959 1.00 24.39 ? 2288 HOH A O 1 HETATM 3103 O O . HOH N 6 . ? -10.443 34.137 47.504 1.00 31.18 ? 2289 HOH A O 1 HETATM 3104 O O . HOH N 6 . ? 16.877 26.578 41.682 1.00 25.01 ? 2290 HOH A O 1 HETATM 3105 O O . HOH N 6 . ? 15.686 25.110 43.878 1.00 42.26 ? 2291 HOH A O 1 HETATM 3106 O O . HOH N 6 . ? 15.389 26.496 46.317 1.00 32.97 ? 2292 HOH A O 1 HETATM 3107 O O . HOH N 6 . ? 19.468 24.050 40.019 1.00 25.08 ? 2293 HOH A O 1 HETATM 3108 O O . HOH N 6 . ? 23.967 25.054 45.730 1.00 34.01 ? 2294 HOH A O 1 HETATM 3109 O O . HOH N 6 . ? 22.227 26.401 47.934 1.00 48.63 ? 2295 HOH A O 1 HETATM 3110 O O . HOH N 6 . ? 26.732 22.540 41.289 1.00 43.22 ? 2296 HOH A O 1 HETATM 3111 O O . HOH N 6 . ? 26.516 24.538 39.039 1.00 45.29 ? 2297 HOH A O 1 HETATM 3112 O O . HOH N 6 . ? 20.364 21.011 45.389 1.00 54.36 ? 2298 HOH A O 1 HETATM 3113 O O . HOH N 6 . ? 17.682 22.172 37.957 1.00 33.16 ? 2299 HOH A O 1 HETATM 3114 O O . HOH N 6 . ? 24.287 22.577 34.606 1.00 36.80 ? 2300 HOH A O 1 HETATM 3115 O O . HOH N 6 . ? 18.422 22.526 34.592 1.00 23.56 ? 2301 HOH A O 1 HETATM 3116 O O . HOH N 6 . ? 18.779 24.445 31.019 1.00 38.61 ? 2302 HOH A O 1 HETATM 3117 O O . HOH N 6 . ? 27.316 28.085 35.000 1.00 30.43 ? 2303 HOH A O 1 HETATM 3118 O O . HOH N 6 . ? 24.425 26.049 30.374 1.00 40.56 ? 2304 HOH A O 1 HETATM 3119 O O . HOH N 6 . ? 20.910 29.150 32.089 1.00 22.77 ? 2305 HOH A O 1 HETATM 3120 O O . HOH N 6 . ? 16.656 26.117 26.898 1.00 45.31 ? 2306 HOH A O 1 HETATM 3121 O O . HOH N 6 . ? 14.290 23.350 25.309 1.00 41.94 ? 2307 HOH A O 1 HETATM 3122 O O . HOH N 6 . ? 12.432 32.066 24.217 1.00 22.57 ? 2308 HOH A O 1 HETATM 3123 O O . HOH N 6 . ? 5.169 35.030 26.257 1.00 17.08 ? 2309 HOH A O 1 HETATM 3124 O O . HOH N 6 . ? -4.711 37.005 26.213 1.00 35.53 ? 2310 HOH A O 1 HETATM 3125 O O . HOH N 6 . ? -0.838 39.792 25.997 1.00 28.08 ? 2311 HOH A O 1 HETATM 3126 O O . HOH N 6 . ? -6.836 37.577 29.937 1.00 24.85 ? 2312 HOH A O 1 HETATM 3127 O O . HOH N 6 . ? -7.273 39.801 35.862 1.00 24.62 ? 2313 HOH A O 1 HETATM 3128 O O . HOH N 6 . ? -10.475 39.773 38.948 1.00 36.13 ? 2314 HOH A O 1 HETATM 3129 O O . HOH N 6 . ? 0.168 36.261 51.625 1.00 37.49 ? 2315 HOH A O 1 HETATM 3130 O O . HOH N 6 . ? -8.157 41.222 49.851 1.00 32.21 ? 2316 HOH A O 1 HETATM 3131 O O . HOH N 6 . ? -5.826 35.318 52.681 1.00 28.92 ? 2317 HOH A O 1 HETATM 3132 O O . HOH N 6 . ? -0.953 40.094 51.562 1.00 38.95 ? 2318 HOH A O 1 HETATM 3133 O O . HOH N 6 . ? 6.489 39.928 49.255 1.00 32.07 ? 2319 HOH A O 1 HETATM 3134 O O . HOH N 6 . ? 6.927 35.904 47.886 1.00 40.14 ? 2320 HOH A O 1 HETATM 3135 O O . HOH N 6 . ? 9.098 35.379 46.158 1.00 27.81 ? 2321 HOH A O 1 HETATM 3136 O O . HOH N 6 . ? 10.214 37.175 42.908 1.00 18.15 ? 2322 HOH A O 1 HETATM 3137 O O . HOH N 6 . ? 20.525 35.994 40.329 1.00 18.62 ? 2323 HOH A O 1 HETATM 3138 O O . HOH N 6 . ? 16.404 37.478 38.889 1.00 20.82 ? 2324 HOH A O 1 HETATM 3139 O O . HOH N 6 . ? 21.063 31.845 39.011 1.00 18.17 ? 2325 HOH A O 1 HETATM 3140 O O . HOH N 6 . ? 23.321 34.388 39.294 1.00 22.21 ? 2326 HOH A O 1 HETATM 3141 O O . HOH N 6 . ? 18.365 27.731 49.388 1.00 43.46 ? 2327 HOH A O 1 HETATM 3142 O O . HOH N 6 . ? 30.729 34.631 42.198 1.00 35.03 ? 2328 HOH A O 1 HETATM 3143 O O . HOH N 6 . ? 32.177 31.746 46.001 1.00 41.43 ? 2329 HOH A O 1 HETATM 3144 O O . HOH N 6 . ? 28.911 27.762 40.600 1.00 38.86 ? 2330 HOH A O 1 HETATM 3145 O O . HOH N 6 . ? 26.256 27.041 46.653 1.00 35.61 ? 2331 HOH A O 1 HETATM 3146 O O . HOH N 6 . ? 27.641 30.975 38.233 1.00 39.45 ? 2332 HOH A O 1 HETATM 3147 O O . HOH N 6 . ? 25.227 32.448 38.708 1.00 26.65 ? 2333 HOH A O 1 HETATM 3148 O O . HOH N 6 . ? 22.025 33.501 36.801 1.00 24.65 ? 2334 HOH A O 1 HETATM 3149 O O . HOH N 6 . ? 21.805 31.718 28.624 1.00 38.90 ? 2335 HOH A O 1 HETATM 3150 O O . HOH N 6 . ? 17.263 35.083 28.133 1.00 17.91 ? 2336 HOH A O 1 HETATM 3151 O O . HOH N 6 . ? 16.355 31.033 26.295 1.00 26.61 ? 2337 HOH A O 1 HETATM 3152 O O . HOH N 6 . ? 14.212 36.404 24.532 1.00 27.74 ? 2338 HOH A O 1 HETATM 3153 O O . HOH N 6 . ? 7.740 37.375 22.219 1.00 40.82 ? 2339 HOH A O 1 HETATM 3154 O O . HOH N 6 . ? 7.300 38.034 26.331 1.00 22.59 ? 2340 HOH A O 1 HETATM 3155 O O . HOH N 6 . ? 3.689 39.807 25.476 1.00 34.83 ? 2341 HOH A O 1 HETATM 3156 O O . HOH N 6 . ? -2.973 43.714 27.759 1.00 33.52 ? 2342 HOH A O 1 HETATM 3157 O O . HOH N 6 . ? -6.248 44.894 29.808 1.00 46.58 ? 2343 HOH A O 1 HETATM 3158 O O . HOH N 6 . ? -6.612 38.752 27.247 1.00 40.90 ? 2344 HOH A O 1 HETATM 3159 O O . HOH N 6 . ? -7.653 39.517 31.991 1.00 38.09 ? 2345 HOH A O 1 HETATM 3160 O O . HOH N 6 . ? -5.717 44.406 35.090 1.00 24.96 ? 2346 HOH A O 1 HETATM 3161 O O . HOH N 6 . ? -8.136 44.711 42.895 1.00 36.79 ? 2347 HOH A O 1 HETATM 3162 O O . HOH N 6 . ? -7.219 45.770 47.513 1.00 42.28 ? 2348 HOH A O 1 HETATM 3163 O O . HOH N 6 . ? -9.801 40.632 43.528 1.00 33.19 ? 2349 HOH A O 1 HETATM 3164 O O . HOH N 6 . ? -5.066 46.723 49.780 1.00 29.39 ? 2350 HOH A O 1 HETATM 3165 O O . HOH N 6 . ? -3.230 45.689 53.747 1.00 26.62 ? 2351 HOH A O 1 HETATM 3166 O O . HOH N 6 . ? -4.271 42.740 55.245 1.00 48.89 ? 2352 HOH A O 1 HETATM 3167 O O . HOH N 6 . ? 2.645 46.259 50.239 1.00 19.81 ? 2353 HOH A O 1 HETATM 3168 O O . HOH N 6 . ? 0.482 41.787 54.294 1.00 33.37 ? 2354 HOH A O 1 HETATM 3169 O O . HOH N 6 . ? 1.110 38.483 52.797 1.00 45.30 ? 2355 HOH A O 1 HETATM 3170 O O . HOH N 6 . ? 5.447 39.594 51.865 1.00 25.70 ? 2356 HOH A O 1 HETATM 3171 O O . HOH N 6 . ? 10.963 43.088 50.154 1.00 28.72 ? 2357 HOH A O 1 HETATM 3172 O O . HOH N 6 . ? 9.880 47.445 49.747 1.00 29.04 ? 2358 HOH A O 1 HETATM 3173 O O . HOH N 6 . ? 8.237 38.077 48.192 1.00 39.48 ? 2359 HOH A O 1 HETATM 3174 O O . HOH N 6 . ? 13.206 41.597 45.323 1.00 21.65 ? 2360 HOH A O 1 HETATM 3175 O O . HOH N 6 . ? 10.934 39.833 49.391 1.00 42.83 ? 2361 HOH A O 1 HETATM 3176 O O . HOH N 6 . ? 13.244 42.102 48.821 1.00 38.47 ? 2362 HOH A O 1 HETATM 3177 O O . HOH N 6 . ? 11.452 34.891 48.939 1.00 37.73 ? 2363 HOH A O 1 HETATM 3178 O O . HOH N 6 . ? 13.758 39.231 49.305 1.00 41.23 ? 2364 HOH A O 1 HETATM 3179 O O . HOH N 6 . ? 15.546 37.423 48.109 1.00 25.98 ? 2365 HOH A O 1 HETATM 3180 O O . HOH N 6 . ? 21.532 41.170 43.397 1.00 30.89 ? 2366 HOH A O 1 HETATM 3181 O O . HOH N 6 . ? 11.731 30.669 50.211 1.00 39.98 ? 2367 HOH A O 1 HETATM 3182 O O . HOH N 6 . ? 16.070 34.561 49.665 1.00 36.46 ? 2368 HOH A O 1 HETATM 3183 O O . HOH N 6 . ? 21.992 31.381 53.020 1.00 47.03 ? 2369 HOH A O 1 HETATM 3184 O O . HOH N 6 . ? 20.675 29.047 49.852 1.00 42.37 ? 2370 HOH A O 1 HETATM 3185 O O . HOH N 6 . ? 24.230 34.275 52.217 1.00 31.83 ? 2371 HOH A O 1 HETATM 3186 O O . HOH N 6 . ? 24.224 40.885 54.323 1.00 44.27 ? 2372 HOH A O 1 HETATM 3187 O O . HOH N 6 . ? 20.546 40.516 53.543 1.00 45.88 ? 2373 HOH A O 1 HETATM 3188 O O . HOH N 6 . ? 24.089 42.695 47.284 1.00 44.31 ? 2374 HOH A O 1 HETATM 3189 O O . HOH N 6 . ? 19.681 42.095 47.896 1.00 34.99 ? 2375 HOH A O 1 HETATM 3190 O O . HOH N 6 . ? 26.105 42.225 43.230 1.00 27.40 ? 2376 HOH A O 1 HETATM 3191 O O . HOH N 6 . ? 31.754 34.420 48.870 1.00 44.20 ? 2377 HOH A O 1 HETATM 3192 O O . HOH N 6 . ? 23.909 41.207 41.877 1.00 24.73 ? 2378 HOH A O 1 HETATM 3193 O O . HOH N 6 . ? 20.828 37.927 38.449 1.00 17.06 ? 2379 HOH A O 1 HETATM 3194 O O . HOH N 6 . ? 29.052 37.208 36.372 1.00 29.53 ? 2380 HOH A O 1 HETATM 3195 O O . HOH N 6 . ? 19.025 39.891 35.581 1.00 24.85 ? 2381 HOH A O 1 HETATM 3196 O O . HOH N 6 . ? 24.081 35.380 26.540 1.00 41.06 ? 2382 HOH A O 1 HETATM 3197 O O . HOH N 6 . ? 20.654 32.463 26.152 1.00 35.42 ? 2383 HOH A O 1 HETATM 3198 O O . HOH N 6 . ? 9.684 42.323 24.761 1.00 37.82 ? 2384 HOH A O 1 HETATM 3199 O O . HOH N 6 . ? 13.970 41.795 23.529 1.00 42.69 ? 2385 HOH A O 1 HETATM 3200 O O . HOH N 6 . ? 10.668 42.979 27.248 1.00 17.04 ? 2386 HOH A O 1 HETATM 3201 O O . HOH N 6 . ? 1.802 46.265 33.992 1.00 35.72 ? 2387 HOH A O 1 HETATM 3202 O O . HOH N 6 . ? 4.586 45.683 28.477 1.00 29.29 ? 2388 HOH A O 1 HETATM 3203 O O . HOH N 6 . ? 1.276 41.684 26.669 1.00 26.56 ? 2389 HOH A O 1 HETATM 3204 O O . HOH N 6 . ? -0.538 47.283 28.897 1.00 32.09 ? 2390 HOH A O 1 HETATM 3205 O O . HOH N 6 . ? -3.978 48.546 33.918 1.00 29.77 ? 2391 HOH A O 1 HETATM 3206 O O . HOH N 6 . ? -8.069 46.039 39.869 1.00 39.70 ? 2392 HOH A O 1 HETATM 3207 O O . HOH N 6 . ? -6.011 49.962 39.460 1.00 37.33 ? 2393 HOH A O 1 HETATM 3208 O O . HOH N 6 . ? -8.151 47.229 44.455 1.00 38.14 ? 2394 HOH A O 1 HETATM 3209 O O . HOH N 6 . ? 2.308 48.709 48.735 1.00 23.67 ? 2395 HOH A O 1 HETATM 3210 O O . HOH N 6 . ? -0.401 44.433 54.902 1.00 37.90 ? 2396 HOH A O 1 HETATM 3211 O O . HOH N 6 . ? -4.940 48.422 53.464 1.00 46.96 ? 2397 HOH A O 1 HETATM 3212 O O . HOH N 6 . ? -0.845 51.748 53.873 1.00 37.23 ? 2398 HOH A O 1 HETATM 3213 O O . HOH N 6 . ? 4.095 39.598 56.341 1.00 46.57 ? 2399 HOH A O 1 HETATM 3214 O O . HOH N 6 . ? 8.598 49.390 51.328 1.00 27.75 ? 2400 HOH A O 1 HETATM 3215 O O . HOH N 6 . ? 9.996 41.799 54.706 1.00 40.88 ? 2401 HOH A O 1 HETATM 3216 O O . HOH N 6 . ? 3.041 55.315 52.344 1.00 33.06 ? 2402 HOH A O 1 HETATM 3217 O O . HOH N 6 . ? 14.379 46.738 48.941 1.00 28.63 ? 2403 HOH A O 1 HETATM 3218 O O . HOH N 6 . ? 20.464 45.741 45.160 1.00 43.39 ? 2404 HOH A O 1 HETATM 3219 O O . HOH N 6 . ? 21.594 41.947 46.151 1.00 42.09 ? 2405 HOH A O 1 HETATM 3220 O O . HOH N 6 . ? 18.280 39.212 37.980 1.00 18.77 ? 2406 HOH A O 1 HETATM 3221 O O . HOH N 6 . ? 20.350 42.291 35.416 1.00 21.81 ? 2407 HOH A O 1 HETATM 3222 O O . HOH N 6 . ? 24.358 43.924 34.305 1.00 33.52 ? 2408 HOH A O 1 HETATM 3223 O O . HOH N 6 . ? 27.335 45.682 36.948 1.00 43.75 ? 2409 HOH A O 1 HETATM 3224 O O . HOH N 6 . ? 24.109 39.959 31.181 1.00 23.45 ? 2410 HOH A O 1 HETATM 3225 O O . HOH N 6 . ? 29.244 43.402 39.493 1.00 40.05 ? 2411 HOH A O 1 HETATM 3226 O O . HOH N 6 . ? 31.237 41.857 38.465 1.00 47.02 ? 2412 HOH A O 1 HETATM 3227 O O . HOH N 6 . ? 24.041 42.926 31.084 1.00 18.66 ? 2413 HOH A O 1 HETATM 3228 O O . HOH N 6 . ? 21.889 39.323 27.135 1.00 27.44 ? 2414 HOH A O 1 HETATM 3229 O O . HOH N 6 . ? 13.154 44.042 27.044 1.00 20.56 ? 2415 HOH A O 1 HETATM 3230 O O . HOH N 6 . ? 13.611 46.208 28.665 1.00 20.40 ? 2416 HOH A O 1 HETATM 3231 O O . HOH N 6 . ? 5.903 45.254 25.853 1.00 46.49 ? 2417 HOH A O 1 HETATM 3232 O O . HOH N 6 . ? 1.488 52.206 29.411 1.00 36.79 ? 2418 HOH A O 1 HETATM 3233 O O . HOH N 6 . ? 2.344 51.904 33.046 1.00 30.41 ? 2419 HOH A O 1 HETATM 3234 O O . HOH N 6 . ? 1.001 52.494 39.178 1.00 36.63 ? 2420 HOH A O 1 HETATM 3235 O O . HOH N 6 . ? -6.624 50.112 36.241 1.00 47.01 ? 2421 HOH A O 1 HETATM 3236 O O . HOH N 6 . ? -4.973 53.064 46.225 1.00 34.33 ? 2422 HOH A O 1 HETATM 3237 O O . HOH N 6 . ? 0.603 56.875 42.373 1.00 36.69 ? 2423 HOH A O 1 HETATM 3238 O O . HOH N 6 . ? 4.151 57.579 44.165 1.00 38.81 ? 2424 HOH A O 1 HETATM 3239 O O . HOH N 6 . ? 4.207 52.718 39.357 1.00 43.84 ? 2425 HOH A O 1 HETATM 3240 O O . HOH N 6 . ? 6.573 54.219 39.328 1.00 34.20 ? 2426 HOH A O 1 HETATM 3241 O O . HOH N 6 . ? 9.268 54.626 41.612 1.00 24.59 ? 2427 HOH A O 1 HETATM 3242 O O . HOH N 6 . ? 18.589 50.148 43.887 1.00 28.62 ? 2428 HOH A O 1 HETATM 3243 O O . HOH N 6 . ? 17.861 50.602 38.181 1.00 28.03 ? 2429 HOH A O 1 HETATM 3244 O O . HOH N 6 . ? 21.066 49.978 39.731 1.00 29.38 ? 2430 HOH A O 1 HETATM 3245 O O . HOH N 6 . ? 25.403 47.007 38.831 1.00 33.57 ? 2431 HOH A O 1 HETATM 3246 O O . HOH N 6 . ? 23.586 46.051 41.814 1.00 35.57 ? 2432 HOH A O 1 HETATM 3247 O O . HOH N 6 . ? 19.807 50.678 35.744 1.00 29.77 ? 2433 HOH A O 1 HETATM 3248 O O . HOH N 6 . ? 14.991 51.583 34.819 1.00 21.33 ? 2434 HOH A O 1 HETATM 3249 O O . HOH N 6 . ? 12.789 53.423 32.158 1.00 40.33 ? 2435 HOH A O 1 HETATM 3250 O O . HOH N 6 . ? 14.727 56.168 29.693 1.00 38.66 ? 2436 HOH A O 1 HETATM 3251 O O . HOH N 6 . ? 16.262 52.080 25.680 1.00 24.71 ? 2437 HOH A O 1 HETATM 3252 O O . HOH N 6 . ? 10.344 53.157 27.437 1.00 44.95 ? 2438 HOH A O 1 HETATM 3253 O O . HOH N 6 . ? 12.902 53.319 34.817 1.00 26.01 ? 2439 HOH A O 1 HETATM 3254 O O . HOH N 6 . ? 5.874 55.651 36.316 1.00 39.65 ? 2440 HOH A O 1 HETATM 3255 O O . HOH N 6 . ? 13.231 56.360 36.068 1.00 34.53 ? 2441 HOH A O 1 HETATM 3256 O O . HOH N 6 . ? 16.005 57.257 43.590 1.00 39.44 ? 2442 HOH A O 1 HETATM 3257 O O . HOH N 6 . ? 12.947 50.485 50.936 1.00 46.34 ? 2443 HOH A O 1 HETATM 3258 O O . HOH N 6 . ? -22.609 -1.012 37.227 1.00 40.55 ? 2444 HOH A O 1 HETATM 3259 O O . HOH N 6 . ? -20.691 4.772 33.382 1.00 28.28 ? 2445 HOH A O 1 HETATM 3260 O O . HOH N 6 . ? -10.292 39.442 50.003 1.00 39.33 ? 2446 HOH A O 1 HETATM 3261 O O . HOH N 6 . ? -13.103 37.044 52.715 1.00 49.74 ? 2447 HOH A O 1 HETATM 3262 O O . HOH N 6 . ? 12.114 34.094 22.178 1.00 38.54 ? 2448 HOH A O 1 HETATM 3263 O O . HOH N 6 . ? 3.485 30.997 18.609 1.00 45.24 ? 2449 HOH A O 1 HETATM 3264 O O . HOH N 6 . ? 2.240 33.058 19.891 1.00 42.77 ? 2450 HOH A O 1 HETATM 3265 O O . HOH N 6 . ? 11.881 5.329 46.174 1.00 27.65 ? 2451 HOH A O 1 HETATM 3266 O O . HOH N 6 . ? 8.504 5.902 43.505 1.00 22.38 ? 2452 HOH A O 1 HETATM 3267 O O . HOH N 6 . ? -11.691 22.980 53.946 1.00 38.37 ? 2453 HOH A O 1 HETATM 3268 O O . HOH N 6 . ? -16.550 18.165 52.051 1.00 40.22 ? 2454 HOH A O 1 HETATM 3269 O O . HOH N 6 . ? -3.085 41.383 25.235 1.00 40.34 ? 2455 HOH A O 1 HETATM 3270 O O . HOH N 6 . ? 16.580 29.732 23.828 1.00 42.92 ? 2456 HOH A O 1 HETATM 3271 O O . HOH N 6 . ? -4.397 -4.609 28.196 1.00 41.55 ? 2457 HOH A O 1 HETATM 3272 O O . HOH N 6 . ? -14.408 13.907 54.386 1.00 33.39 ? 2458 HOH A O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ALA 1 19 ? ? ? A . n A 1 2 PRO 2 20 ? ? ? A . n A 1 3 SER 3 21 ? ? ? A . n A 1 4 LYS 4 22 ? ? ? A . n A 1 5 VAL 5 23 ? ? ? A . n A 1 6 GLN 6 24 ? ? ? A . n A 1 7 ARG 7 25 ? ? ? A . n A 1 8 ALA 8 26 ? ? ? A . n A 1 9 PRO 9 27 ? ? ? A . n A 1 10 ASP 10 28 ? ? ? A . n A 1 11 SER 11 29 ? ? ? A . n A 1 12 SER 12 30 ? ? ? A . n A 1 13 ILE 13 31 ? ? ? A . n A 1 14 HIS 14 32 ? ? ? A . n A 1 15 ALA 15 33 ? ? ? A . n A 1 16 ARG 16 34 ? ? ? A . n A 1 17 ALA 17 35 35 ALA ALA A . n A 1 18 VAL 18 36 36 VAL VAL A . n A 1 19 CYS 19 37 37 CYS CYS A . n A 1 20 THR 20 38 38 THR THR A . n A 1 21 PRO 21 39 39 PRO PRO A . n A 1 22 THR 22 40 40 THR THR A . n A 1 23 ALA 23 41 41 ALA ALA A . n A 1 24 GLY 24 42 42 GLY GLY A . n A 1 25 GLY 25 43 43 GLY GLY A . n A 1 26 ASP 26 44 44 ASP ASP A . n A 1 27 SER 27 45 45 SER SER A . n A 1 28 SER 28 46 46 SER SER A . n A 1 29 THR 29 47 47 THR THR A . n A 1 30 ASP 30 48 48 ASP ASP A . n A 1 31 ASP 31 49 49 ASP ASP A . n A 1 32 VAL 32 50 50 VAL VAL A . n A 1 33 PRO 33 51 51 PRO PRO A . n A 1 34 ALA 34 52 52 ALA ALA A . n A 1 35 ILE 35 53 53 ILE ILE A . n A 1 36 THR 36 54 54 THR THR A . n A 1 37 GLU 37 55 55 GLU GLU A . n A 1 38 ALA 38 56 56 ALA ALA A . n A 1 39 LEU 39 57 57 LEU LEU A . n A 1 40 SER 40 58 58 SER SER A . n A 1 41 SER 41 59 59 SER SER A . n A 1 42 CYS 42 60 60 CYS CYS A . n A 1 43 GLY 43 61 61 GLY GLY A . n A 1 44 ASN 44 62 62 ASN ASN A . n A 1 45 GLY 45 63 63 GLY GLY A . n A 1 46 GLY 46 64 64 GLY GLY A . n A 1 47 THR 47 65 65 THR THR A . n A 1 48 ILE 48 66 66 ILE ILE A . n A 1 49 VAL 49 67 67 VAL VAL A . n A 1 50 PHE 50 68 68 PHE PHE A . n A 1 51 PRO 51 69 69 PRO PRO A . n A 1 52 GLU 52 70 70 GLU GLU A . n A 1 53 GLY 53 71 71 GLY GLY A . n A 1 54 SER 54 72 72 SER SER A . n A 1 55 THR 55 73 73 THR THR A . n A 1 56 TYR 56 74 74 TYR TYR A . n A 1 57 TYR 57 75 75 TYR TYR A . n A 1 58 LEU 58 76 76 LEU LEU A . n A 1 59 ASN 59 77 77 ASN ASN A . n A 1 60 SER 60 78 78 SER SER A . n A 1 61 VAL 61 79 79 VAL VAL A . n A 1 62 LEU 62 80 80 LEU LEU A . n A 1 63 ASP 63 81 81 ASP ASP A . n A 1 64 LEU 64 82 82 LEU LEU A . n A 1 65 GLY 65 83 83 GLY GLY A . n A 1 66 SER 66 84 84 SER SER A . n A 1 67 CYS 67 85 85 CYS CYS A . n A 1 68 SER 68 86 86 SER SER A . n A 1 69 ASP 69 87 87 ASP ASP A . n A 1 70 CYS 70 88 88 CYS CYS A . n A 1 71 ASP 71 89 89 ASP ASP A . n A 1 72 ILE 72 90 90 ILE ILE A . n A 1 73 GLN 73 91 91 GLN GLN A . n A 1 74 VAL 74 92 92 VAL VAL 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 LEU 77 95 95 LEU LEU A . n A 1 78 LEU 78 96 96 LEU LEU A . n A 1 79 LYS 79 97 97 LYS LYS A . n A 1 80 PHE 80 98 98 PHE PHE A . n A 1 81 ALA 81 99 99 ALA ALA A . n A 1 82 SER 82 100 100 SER SER A . n A 1 83 ASP 83 101 101 ASP ASP A . n A 1 84 THR 84 102 102 THR THR A . n A 1 85 ASP 85 103 103 ASP ASP A . n A 1 86 TYR 86 104 104 TYR TYR A . n A 1 87 TRP 87 105 105 TRP TRP A . n A 1 88 SER 88 106 106 SER SER A . n A 1 89 GLY 89 107 107 GLY GLY A . n A 1 90 ARG 90 108 108 ARG ARG A . n A 1 91 THR 91 109 109 THR THR A . n A 1 92 ALA 92 110 110 ALA ALA A . n A 1 93 MET 93 111 111 MET MET A . n A 1 94 ILE 94 112 112 ILE ILE A . n A 1 95 SER 95 113 113 SER SER A . n A 1 96 VAL 96 114 114 VAL VAL A . n A 1 97 SER 97 115 115 SER SER A . n A 1 98 ASN 98 116 116 ASN ASN A . n A 1 99 VAL 99 117 117 VAL VAL A . n A 1 100 ASP 100 118 118 ASP ASP A . n A 1 101 GLY 101 119 119 GLY GLY A . n A 1 102 LEU 102 120 120 LEU LEU A . n A 1 103 LYS 103 121 121 LYS LYS A . n A 1 104 LEU 104 122 122 LEU LEU A . n A 1 105 ARG 105 123 123 ARG ARG A . n A 1 106 SER 106 124 124 SER SER A . n A 1 107 LEU 107 125 125 LEU LEU A . n A 1 108 THR 108 126 126 THR THR A . n A 1 109 GLY 109 127 127 GLY GLY A . n A 1 110 SER 110 128 128 SER SER A . n A 1 111 GLY 111 129 129 GLY GLY A . n A 1 112 VAL 112 130 130 VAL VAL A . n A 1 113 ILE 113 131 131 ILE ILE A . n A 1 114 ASP 114 132 132 ASP ASP A . n A 1 115 GLY 115 133 133 GLY GLY A . n A 1 116 ASN 116 134 134 ASN ASN A . n A 1 117 GLY 117 135 135 GLY GLY A . n A 1 118 GLN 118 136 136 GLN GLN A . n A 1 119 ASP 119 137 137 ASP ASP A . n A 1 120 ALA 120 138 138 ALA ALA A . n A 1 121 TRP 121 139 139 TRP TRP A . n A 1 122 ASP 122 140 140 ASP ASP A . n A 1 123 LEU 123 141 141 LEU LEU A . n A 1 124 PHE 124 142 142 PHE PHE A . n A 1 125 ALA 125 143 143 ALA ALA A . n A 1 126 SER 126 144 144 SER SER A . n A 1 127 ASP 127 145 145 ASP ASP A . n A 1 128 SER 128 146 146 SER SER A . n A 1 129 SER 129 147 147 SER SER A . n A 1 130 TYR 130 148 148 TYR TYR A . n A 1 131 SER 131 149 149 SER SER A . n A 1 132 ARG 132 150 150 ARG ARG A . n A 1 133 PRO 133 151 151 PRO PRO A . n A 1 134 THR 134 152 152 THR THR A . n A 1 135 LEU 135 153 153 LEU LEU A . n A 1 136 LEU 136 154 154 LEU LEU A . n A 1 137 TYR 137 155 155 TYR TYR A . n A 1 138 ILE 138 156 156 ILE ILE A . n A 1 139 THR 139 157 157 THR THR A . n A 1 140 GLY 140 158 158 GLY GLY A . n A 1 141 GLY 141 159 159 GLY GLY A . n A 1 142 SER 142 160 160 SER SER A . n A 1 143 ASN 143 161 161 ASN ASN A . n A 1 144 LEU 144 162 162 LEU LEU A . n A 1 145 GLU 145 163 163 GLU GLU A . n A 1 146 ILE 146 164 164 ILE ILE A . n A 1 147 SER 147 165 165 SER SER A . n A 1 148 GLY 148 166 166 GLY GLY A . n A 1 149 LEU 149 167 167 LEU LEU A . n A 1 150 ARG 150 168 168 ARG ARG A . n A 1 151 GLN 151 169 169 GLN GLN A . n A 1 152 LYS 152 170 170 LYS LYS 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 PRO 155 173 173 PRO PRO A . n A 1 156 ASN 156 174 174 ASN ASN A . n A 1 157 VAL 157 175 175 VAL VAL A . n A 1 158 PHE 158 176 176 PHE PHE A . n A 1 159 ASN 159 177 177 ASN ASN A . n A 1 160 SER 160 178 178 SER SER A . n A 1 161 VAL 161 179 179 VAL VAL A . n A 1 162 LYS 162 180 180 LYS LYS A . n A 1 163 GLY 163 181 181 GLY GLY A . n A 1 164 GLY 164 182 182 GLY GLY A . n A 1 165 ALA 165 183 183 ALA ALA A . n A 1 166 THR 166 184 184 THR THR A . n A 1 167 ASN 167 185 185 ASN ASN A . n A 1 168 VAL 168 186 186 VAL VAL A . n A 1 169 VAL 169 187 187 VAL VAL A . n A 1 170 PHE 170 188 188 PHE PHE A . n A 1 171 SER 171 189 189 SER SER A . n A 1 172 ASN 172 190 190 ASN ASN A . n A 1 173 LEU 173 191 191 LEU LEU A . n A 1 174 LYS 174 192 192 LYS LYS A . n A 1 175 MET 175 193 193 MET MET A . n A 1 176 ASP 176 194 194 ASP ASP A . n A 1 177 ALA 177 195 195 ALA ALA A . n A 1 178 ASN 178 196 196 ASN ASN A . n A 1 179 SER 179 197 197 SER SER A . n A 1 180 LYS 180 198 198 LYS LYS A . n A 1 181 SER 181 199 199 SER SER A . n A 1 182 ASP 182 200 200 ASP ASP A . n A 1 183 ASN 183 201 201 ASN ASN A . n A 1 184 PRO 184 202 202 PRO PRO A . n A 1 185 PRO 185 203 203 PRO PRO A . n A 1 186 LYS 186 204 204 LYS LYS A . n A 1 187 ASN 187 205 205 ASN ASN A . n A 1 188 THR 188 206 206 THR THR A . n A 1 189 ASP 189 207 207 ASP ASP A . n A 1 190 GLY 190 208 208 GLY GLY A . n A 1 191 PHE 191 209 209 PHE PHE A . n A 1 192 ASP 192 210 210 ASP ASP A . n A 1 193 ILE 193 211 211 ILE ILE A . n A 1 194 GLY 194 212 212 GLY GLY A . n A 1 195 GLU 195 213 213 GLU GLU A . n A 1 196 SER 196 214 214 SER SER A . n A 1 197 THR 197 215 215 THR THR A . n A 1 198 TYR 198 216 216 TYR TYR A . n A 1 199 VAL 199 217 217 VAL VAL A . n A 1 200 THR 200 218 218 THR THR A . n A 1 201 ILE 201 219 219 ILE ILE A . n A 1 202 THR 202 220 220 THR THR A . n A 1 203 GLU 203 221 221 GLU GLU A . n A 1 204 VAL 204 222 222 VAL VAL A . n A 1 205 THR 205 223 223 THR THR A . n A 1 206 VAL 206 224 224 VAL VAL A . n A 1 207 VAL 207 225 225 VAL VAL A . n A 1 208 ASN 208 226 226 ASN ASN A . n A 1 209 ASP 209 227 227 ASP ASP A . n A 1 210 ASP 210 228 228 ASP ASP A . n A 1 211 ASP 211 229 229 ASP ASP A . n A 1 212 CYS 212 230 230 CYS CYS A . n A 1 213 VAL 213 231 231 VAL VAL A . n A 1 214 ALA 214 232 232 ALA ALA A . n A 1 215 PHE 215 233 233 PHE PHE A . n A 1 216 LYS 216 234 234 LYS LYS A . n A 1 217 PRO 217 235 235 PRO PRO A . n A 1 218 SER 218 236 236 SER SER A . n A 1 219 SER 219 237 237 SER SER A . n A 1 220 ASN 220 238 238 ASN ASN A . n A 1 221 TYR 221 239 239 TYR TYR A . n A 1 222 VAL 222 240 240 VAL VAL A . n A 1 223 THR 223 241 241 THR THR A . n A 1 224 VAL 224 242 242 VAL VAL A . n A 1 225 ASP 225 243 243 ASP ASP A . n A 1 226 THR 226 244 244 THR THR A . n A 1 227 ILE 227 245 245 ILE ILE A . n A 1 228 SER 228 246 246 SER SER A . n A 1 229 CYS 229 247 247 CYS CYS A . n A 1 230 THR 230 248 248 THR THR A . n A 1 231 GLY 231 249 249 GLY GLY A . n A 1 232 SER 232 250 250 SER SER A . n A 1 233 HIS 233 251 251 HIS HIS A . n A 1 234 GLY 234 252 252 GLY GLY A . n A 1 235 ILE 235 253 253 ILE ILE A . n A 1 236 SER 236 254 254 SER SER A . n A 1 237 VAL 237 255 255 VAL VAL A . n A 1 238 GLY 238 256 256 GLY GLY A . n A 1 239 SER 239 257 257 SER SER A . n A 1 240 LEU 240 258 258 LEU LEU A . n A 1 241 GLY 241 259 259 GLY GLY A . n A 1 242 LYS 242 260 260 LYS LYS A . n A 1 243 SER 243 261 261 SER SER A . n A 1 244 SER 244 262 262 SER SER A . n A 1 245 ASP 245 263 263 ASP ASP A . n A 1 246 ASP 246 264 264 ASP ASP A . n A 1 247 SER 247 265 265 SER SER A . n A 1 248 VAL 248 266 266 VAL VAL A . n A 1 249 LYS 249 267 267 LYS LYS A . n A 1 250 ASN 250 268 268 ASN ASN A . n A 1 251 ILE 251 269 269 ILE ILE A . n A 1 252 TYR 252 270 270 TYR TYR A . n A 1 253 VAL 253 271 271 VAL VAL A . n A 1 254 THR 254 272 272 THR THR A . n A 1 255 GLY 255 273 273 GLY GLY A . n A 1 256 ALA 256 274 274 ALA ALA A . n A 1 257 THR 257 275 275 THR THR A . n A 1 258 MET 258 276 276 MET MET A . n A 1 259 ILE 259 277 277 ILE ILE A . n A 1 260 ASN 260 278 278 ASN ASN A . n A 1 261 SER 261 279 279 SER SER A . n A 1 262 THR 262 280 280 THR THR A . n A 1 263 LYS 263 281 281 LYS LYS A . n A 1 264 ALA 264 282 282 ALA ALA A . n A 1 265 ALA 265 283 283 ALA ALA A . n A 1 266 GLY 266 284 284 GLY GLY A . n A 1 267 ILE 267 285 285 ILE ILE A . n A 1 268 LYS 268 286 286 LYS LYS A . n A 1 269 THR 269 287 287 THR THR A . n A 1 270 TYR 270 288 288 TYR TYR A . n A 1 271 PRO 271 289 289 PRO PRO A . n A 1 272 SER 272 290 290 SER SER A . n A 1 273 GLY 273 291 291 GLY GLY A . n A 1 274 GLY 274 292 292 GLY GLY A . n A 1 275 ASP 275 293 293 ASP ASP A . n A 1 276 HIS 276 294 294 HIS HIS A . n A 1 277 GLY 277 295 295 GLY GLY A . n A 1 278 THR 278 296 296 THR THR A . n A 1 279 SER 279 297 297 SER SER A . n A 1 280 THR 280 298 298 THR THR A . n A 1 281 VAL 281 299 299 VAL VAL A . n A 1 282 SER 282 300 300 SER SER A . n A 1 283 ASN 283 301 301 ASN ASN A . n A 1 284 VAL 284 302 302 VAL VAL A . n A 1 285 THR 285 303 303 THR THR A . n A 1 286 PHE 286 304 304 PHE PHE A . n A 1 287 ASN 287 305 305 ASN ASN A . n A 1 288 ASP 288 306 306 ASP ASP A . n A 1 289 PHE 289 307 307 PHE PHE A . n A 1 290 THR 290 308 308 THR THR A . n A 1 291 VAL 291 309 309 VAL VAL A . n A 1 292 ASP 292 310 310 ASP ASP A . n A 1 293 ASN 293 311 311 ASN ASN A . n A 1 294 SER 294 312 312 SER SER A . n A 1 295 ASP 295 313 313 ASP ASP A . n A 1 296 TYR 296 314 314 TYR TYR A . n A 1 297 ALA 297 315 315 ALA ALA A . n A 1 298 PHE 298 316 316 PHE PHE A . n A 1 299 GLN 299 317 317 GLN GLN A . n A 1 300 ILE 300 318 318 ILE ILE A . n A 1 301 GLN 301 319 319 GLN GLN A . n A 1 302 SER 302 320 320 SER SER A . n A 1 303 CYS 303 321 321 CYS CYS A . n A 1 304 TYR 304 322 322 TYR TYR A . n A 1 305 GLY 305 323 323 GLY GLY A . n A 1 306 GLU 306 324 324 GLU GLU A . n A 1 307 ASP 307 325 325 ASP ASP A . n A 1 308 ASP 308 326 326 ASP ASP A . n A 1 309 ASP 309 327 327 ASP ASP A . n A 1 310 TYR 310 328 328 TYR TYR A . n A 1 311 CYS 311 329 329 CYS CYS A . n A 1 312 GLU 312 330 330 GLU GLU A . n A 1 313 GLU 313 331 331 GLU GLU A . n A 1 314 ASN 314 332 332 ASN ASN A . n A 1 315 PRO 315 333 333 PRO PRO A . n A 1 316 GLY 316 334 334 GLY GLY A . n A 1 317 ASN 317 335 335 ASN ASN A . n A 1 318 ALA 318 336 336 ALA ALA A . n A 1 319 LYS 319 337 337 LYS LYS A . n A 1 320 LEU 320 338 338 LEU LEU A . n A 1 321 THR 321 339 339 THR THR A . n A 1 322 ASP 322 340 340 ASP ASP A . n A 1 323 ILE 323 341 341 ILE ILE A . n A 1 324 VAL 324 342 342 VAL VAL A . n A 1 325 VAL 325 343 343 VAL VAL A . n A 1 326 SER 326 344 344 SER SER A . n A 1 327 SER 327 345 345 SER SER A . n A 1 328 PHE 328 346 346 PHE PHE A . n A 1 329 SER 329 347 347 SER SER A . n A 1 330 GLY 330 348 348 GLY GLY A . n A 1 331 THR 331 349 349 THR THR A . n A 1 332 THR 332 350 350 THR THR A . n A 1 333 SER 333 351 351 SER SER A . n A 1 334 ASP 334 352 352 ASP ASP A . n A 1 335 LYS 335 353 353 LYS LYS A . n A 1 336 TYR 336 354 354 TYR TYR A . n A 1 337 ASP 337 355 355 ASP ASP A . n A 1 338 PRO 338 356 356 PRO PRO A . n A 1 339 VAL 339 357 357 VAL VAL A . n A 1 340 VAL 340 358 358 VAL VAL A . n A 1 341 ALA 341 359 359 ALA ALA A . n A 1 342 ASN 342 360 360 ASN ASN A . n A 1 343 LEU 343 361 361 LEU LEU A . n A 1 344 ASP 344 362 362 ASP ASP A . n A 1 345 CYS 345 363 363 CYS CYS A . n A 1 346 GLY 346 364 364 GLY GLY A . n A 1 347 ALA 347 365 365 ALA ALA A . n A 1 348 ASP 348 366 366 ASP ASP A . n A 1 349 GLY 349 367 367 GLY GLY A . n A 1 350 THR 350 368 368 THR THR A . n A 1 351 CYS 351 369 369 CYS CYS A . n A 1 352 GLY 352 370 370 GLY GLY A . n A 1 353 ILE 353 371 371 ILE ILE A . n A 1 354 SER 354 372 372 SER SER A . n A 1 355 ILE 355 373 373 ILE ILE A . n A 1 356 SER 356 374 374 SER SER A . n A 1 357 GLY 357 375 375 GLY GLY A . n A 1 358 PHE 358 376 376 PHE PHE A . n A 1 359 ASP 359 377 377 ASP ASP A . n A 1 360 VAL 360 378 378 VAL VAL A . n A 1 361 LYS 361 379 379 LYS LYS A . n A 1 362 ALA 362 380 380 ALA ALA A . n A 1 363 PRO 363 381 381 PRO PRO A . n A 1 364 SER 364 382 382 SER SER A . n A 1 365 GLY 365 383 383 GLY GLY A . n A 1 366 LYS 366 384 384 LYS LYS A . n A 1 367 SER 367 385 385 SER SER A . n A 1 368 GLU 368 386 386 GLU GLU A . n A 1 369 VAL 369 387 387 VAL VAL A . n A 1 370 LEU 370 388 388 LEU LEU A . n A 1 371 CYS 371 389 389 CYS CYS A . n A 1 372 ALA 372 390 390 ALA ALA A . n A 1 373 ASN 373 391 391 ASN ASN A . n A 1 374 THR 374 392 392 THR THR A . n A 1 375 PRO 375 393 393 PRO PRO A . n A 1 376 SER 376 394 394 SER SER A . n A 1 377 ASP 377 395 395 ASP ASP A . n A 1 378 LEU 378 396 396 LEU LEU A . n A 1 379 GLY 379 397 397 GLY GLY A . n A 1 380 VAL 380 398 398 VAL VAL A . n A 1 381 THR 381 399 399 THR THR A . n A 1 382 CYS 382 400 400 CYS CYS A . n A 1 383 THR 383 401 401 THR THR A . n A 1 384 SER 384 402 402 SER SER A . n A 1 385 GLY 385 403 403 GLY GLY A . n A 1 386 ALA 386 404 404 ALA ALA A . n A 1 387 SER 387 405 405 SER SER A . n A 1 388 GLY 388 406 406 GLY GLY 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 MAN 1 410 410 MAN MAN A . C 3 NAG 1 411 411 NAG NAG A . D 3 NAG 1 412 412 NAG NAG A . E 3 NAG 2 413 413 NAG NAG A . F 4 SO4 1 1407 1407 SO4 SO4 A . G 4 SO4 1 1408 1408 SO4 SO4 A . H 4 SO4 1 1409 1409 SO4 SO4 A . I 4 SO4 1 1410 1410 SO4 SO4 A . J 4 SO4 1 1411 1411 SO4 SO4 A . K 4 SO4 1 1412 1412 SO4 SO4 A . L 4 SO4 1 1413 1413 SO4 SO4 A . M 5 GOL 1 1414 1414 GOL GOL A . N 6 HOH 1 2001 2001 HOH HOH A . N 6 HOH 2 2002 2002 HOH HOH A . N 6 HOH 3 2003 2003 HOH HOH A . N 6 HOH 4 2004 2004 HOH HOH A . N 6 HOH 5 2005 2005 HOH HOH A . N 6 HOH 6 2006 2006 HOH HOH A . N 6 HOH 7 2007 2007 HOH HOH A . N 6 HOH 8 2008 2008 HOH HOH A . N 6 HOH 9 2009 2009 HOH HOH A . N 6 HOH 10 2010 2010 HOH HOH A . N 6 HOH 11 2011 2011 HOH HOH A . N 6 HOH 12 2012 2012 HOH HOH A . N 6 HOH 13 2013 2013 HOH HOH A . N 6 HOH 14 2014 2014 HOH HOH A . N 6 HOH 15 2015 2015 HOH HOH A . N 6 HOH 16 2016 2016 HOH HOH A . N 6 HOH 17 2017 2017 HOH HOH A . N 6 HOH 18 2018 2018 HOH HOH A . N 6 HOH 19 2019 2019 HOH HOH A . N 6 HOH 20 2020 2020 HOH HOH A . N 6 HOH 21 2021 2021 HOH HOH A . N 6 HOH 22 2022 2022 HOH HOH A . N 6 HOH 23 2023 2023 HOH HOH A . N 6 HOH 24 2024 2024 HOH HOH A . N 6 HOH 25 2025 2025 HOH HOH A . N 6 HOH 26 2026 2026 HOH HOH A . N 6 HOH 27 2027 2027 HOH HOH A . N 6 HOH 28 2028 2028 HOH HOH A . N 6 HOH 29 2029 2029 HOH HOH A . N 6 HOH 30 2030 2030 HOH HOH A . N 6 HOH 31 2031 2031 HOH HOH A . N 6 HOH 32 2032 2032 HOH HOH A . N 6 HOH 33 2033 2033 HOH HOH A . N 6 HOH 34 2034 2034 HOH HOH A . N 6 HOH 35 2035 2035 HOH HOH A . N 6 HOH 36 2036 2036 HOH HOH A . N 6 HOH 37 2037 2037 HOH HOH A . N 6 HOH 38 2038 2038 HOH HOH A . N 6 HOH 39 2039 2039 HOH HOH A . N 6 HOH 40 2040 2040 HOH HOH A . N 6 HOH 41 2041 2041 HOH HOH A . N 6 HOH 42 2042 2042 HOH HOH A . N 6 HOH 43 2043 2043 HOH HOH A . N 6 HOH 44 2044 2044 HOH HOH A . N 6 HOH 45 2045 2045 HOH HOH A . N 6 HOH 46 2046 2046 HOH HOH A . N 6 HOH 47 2047 2047 HOH HOH A . N 6 HOH 48 2048 2048 HOH HOH A . N 6 HOH 49 2049 2049 HOH HOH A . N 6 HOH 50 2050 2050 HOH HOH A . N 6 HOH 51 2051 2051 HOH HOH A . N 6 HOH 52 2052 2052 HOH HOH A . N 6 HOH 53 2053 2053 HOH HOH A . N 6 HOH 54 2054 2054 HOH HOH A . N 6 HOH 55 2055 2055 HOH HOH A . N 6 HOH 56 2056 2056 HOH HOH A . N 6 HOH 57 2057 2057 HOH HOH A . N 6 HOH 58 2058 2058 HOH HOH A . N 6 HOH 59 2059 2059 HOH HOH A . N 6 HOH 60 2060 2060 HOH HOH A . N 6 HOH 61 2061 2061 HOH HOH A . N 6 HOH 62 2062 2062 HOH HOH A . N 6 HOH 63 2063 2063 HOH HOH A . N 6 HOH 64 2064 2064 HOH HOH A . N 6 HOH 65 2065 2065 HOH HOH A . N 6 HOH 66 2066 2066 HOH HOH A . N 6 HOH 67 2067 2067 HOH HOH A . N 6 HOH 68 2068 2068 HOH HOH A . N 6 HOH 69 2069 2069 HOH HOH A . N 6 HOH 70 2070 2070 HOH HOH A . N 6 HOH 71 2071 2071 HOH HOH A . N 6 HOH 72 2072 2072 HOH HOH A . N 6 HOH 73 2073 2073 HOH HOH A . N 6 HOH 74 2074 2074 HOH HOH A . N 6 HOH 75 2075 2075 HOH HOH A . N 6 HOH 76 2076 2076 HOH HOH A . N 6 HOH 77 2077 2077 HOH HOH A . N 6 HOH 78 2078 2078 HOH HOH A . N 6 HOH 79 2079 2079 HOH HOH A . N 6 HOH 80 2080 2080 HOH HOH A . N 6 HOH 81 2081 2081 HOH HOH A . N 6 HOH 82 2082 2082 HOH HOH A . N 6 HOH 83 2083 2083 HOH HOH A . N 6 HOH 84 2084 2084 HOH HOH A . N 6 HOH 85 2085 2085 HOH HOH A . N 6 HOH 86 2086 2086 HOH HOH A . N 6 HOH 87 2087 2087 HOH HOH A . N 6 HOH 88 2088 2088 HOH HOH A . N 6 HOH 89 2089 2089 HOH HOH A . N 6 HOH 90 2090 2090 HOH HOH A . N 6 HOH 91 2091 2091 HOH HOH A . N 6 HOH 92 2092 2092 HOH HOH A . N 6 HOH 93 2093 2093 HOH HOH A . N 6 HOH 94 2094 2094 HOH HOH A . N 6 HOH 95 2095 2095 HOH HOH A . N 6 HOH 96 2096 2096 HOH HOH A . N 6 HOH 97 2097 2097 HOH HOH A . N 6 HOH 98 2098 2098 HOH HOH A . N 6 HOH 99 2099 2099 HOH HOH A . N 6 HOH 100 2100 2100 HOH HOH A . N 6 HOH 101 2101 2101 HOH HOH A . N 6 HOH 102 2102 2102 HOH HOH A . N 6 HOH 103 2103 2103 HOH HOH A . N 6 HOH 104 2104 2104 HOH HOH A . N 6 HOH 105 2105 2105 HOH HOH A . N 6 HOH 106 2106 2106 HOH HOH A . N 6 HOH 107 2107 2107 HOH HOH A . N 6 HOH 108 2108 2108 HOH HOH A . N 6 HOH 109 2109 2109 HOH HOH A . N 6 HOH 110 2110 2110 HOH HOH A . N 6 HOH 111 2111 2111 HOH HOH A . N 6 HOH 112 2112 2112 HOH HOH A . N 6 HOH 113 2113 2113 HOH HOH A . N 6 HOH 114 2114 2114 HOH HOH A . N 6 HOH 115 2115 2115 HOH HOH A . N 6 HOH 116 2116 2116 HOH HOH A . N 6 HOH 117 2117 2117 HOH HOH A . N 6 HOH 118 2118 2118 HOH HOH A . N 6 HOH 119 2119 2119 HOH HOH A . N 6 HOH 120 2120 2120 HOH HOH A . N 6 HOH 121 2121 2121 HOH HOH A . N 6 HOH 122 2122 2122 HOH HOH A . N 6 HOH 123 2123 2123 HOH HOH A . N 6 HOH 124 2124 2124 HOH HOH A . N 6 HOH 125 2125 2125 HOH HOH A . N 6 HOH 126 2126 2126 HOH HOH A . N 6 HOH 127 2127 2127 HOH HOH A . N 6 HOH 128 2128 2128 HOH HOH A . N 6 HOH 129 2129 2129 HOH HOH A . N 6 HOH 130 2130 2130 HOH HOH A . N 6 HOH 131 2131 2131 HOH HOH A . N 6 HOH 132 2132 2132 HOH HOH A . N 6 HOH 133 2133 2133 HOH HOH A . N 6 HOH 134 2134 2134 HOH HOH A . N 6 HOH 135 2135 2135 HOH HOH A . N 6 HOH 136 2136 2136 HOH HOH A . N 6 HOH 137 2137 2137 HOH HOH A . N 6 HOH 138 2138 2138 HOH HOH A . N 6 HOH 139 2139 2139 HOH HOH A . N 6 HOH 140 2140 2140 HOH HOH A . N 6 HOH 141 2141 2141 HOH HOH A . N 6 HOH 142 2142 2142 HOH HOH A . N 6 HOH 143 2143 2143 HOH HOH A . N 6 HOH 144 2144 2144 HOH HOH A . N 6 HOH 145 2145 2145 HOH HOH A . N 6 HOH 146 2146 2146 HOH HOH A . N 6 HOH 147 2147 2147 HOH HOH A . N 6 HOH 148 2148 2148 HOH HOH A . N 6 HOH 149 2149 2149 HOH HOH A . N 6 HOH 150 2150 2150 HOH HOH A . N 6 HOH 151 2151 2151 HOH HOH A . N 6 HOH 152 2152 2152 HOH HOH A . N 6 HOH 153 2153 2153 HOH HOH A . N 6 HOH 154 2154 2154 HOH HOH A . N 6 HOH 155 2155 2155 HOH HOH A . N 6 HOH 156 2156 2156 HOH HOH A . N 6 HOH 157 2157 2157 HOH HOH A . N 6 HOH 158 2158 2158 HOH HOH A . N 6 HOH 159 2159 2159 HOH HOH A . N 6 HOH 160 2160 2160 HOH HOH A . N 6 HOH 161 2161 2161 HOH HOH A . N 6 HOH 162 2162 2162 HOH HOH A . N 6 HOH 163 2163 2163 HOH HOH A . N 6 HOH 164 2164 2164 HOH HOH A . N 6 HOH 165 2165 2165 HOH HOH A . N 6 HOH 166 2166 2166 HOH HOH A . N 6 HOH 167 2167 2167 HOH HOH A . N 6 HOH 168 2168 2168 HOH HOH A . N 6 HOH 169 2169 2169 HOH HOH A . N 6 HOH 170 2170 2170 HOH HOH A . N 6 HOH 171 2171 2171 HOH HOH A . N 6 HOH 172 2172 2172 HOH HOH A . N 6 HOH 173 2173 2173 HOH HOH A . N 6 HOH 174 2174 2174 HOH HOH A . N 6 HOH 175 2175 2175 HOH HOH A . N 6 HOH 176 2176 2176 HOH HOH A . N 6 HOH 177 2177 2177 HOH HOH A . N 6 HOH 178 2178 2178 HOH HOH A . N 6 HOH 179 2179 2179 HOH HOH A . N 6 HOH 180 2180 2180 HOH HOH A . N 6 HOH 181 2181 2181 HOH HOH A . N 6 HOH 182 2182 2182 HOH HOH A . N 6 HOH 183 2183 2183 HOH HOH A . N 6 HOH 184 2184 2184 HOH HOH A . N 6 HOH 185 2185 2185 HOH HOH A . N 6 HOH 186 2186 2186 HOH HOH A . N 6 HOH 187 2187 2187 HOH HOH A . N 6 HOH 188 2188 2188 HOH HOH A . N 6 HOH 189 2189 2189 HOH HOH A . N 6 HOH 190 2190 2190 HOH HOH A . N 6 HOH 191 2191 2191 HOH HOH A . N 6 HOH 192 2192 2192 HOH HOH A . N 6 HOH 193 2193 2193 HOH HOH A . N 6 HOH 194 2194 2194 HOH HOH A . N 6 HOH 195 2195 2195 HOH HOH A . N 6 HOH 196 2196 2196 HOH HOH A . N 6 HOH 197 2197 2197 HOH HOH A . N 6 HOH 198 2198 2198 HOH HOH A . N 6 HOH 199 2199 2199 HOH HOH A . N 6 HOH 200 2200 2200 HOH HOH A . N 6 HOH 201 2201 2201 HOH HOH A . N 6 HOH 202 2202 2202 HOH HOH A . N 6 HOH 203 2203 2203 HOH HOH A . N 6 HOH 204 2204 2204 HOH HOH A . N 6 HOH 205 2205 2205 HOH HOH A . N 6 HOH 206 2206 2206 HOH HOH A . N 6 HOH 207 2207 2207 HOH HOH A . N 6 HOH 208 2208 2208 HOH HOH A . N 6 HOH 209 2209 2209 HOH HOH A . N 6 HOH 210 2210 2210 HOH HOH A . N 6 HOH 211 2211 2211 HOH HOH A . N 6 HOH 212 2212 2212 HOH HOH A . N 6 HOH 213 2213 2213 HOH HOH A . N 6 HOH 214 2214 2214 HOH HOH A . N 6 HOH 215 2215 2215 HOH HOH A . N 6 HOH 216 2216 2216 HOH HOH A . N 6 HOH 217 2217 2217 HOH HOH A . N 6 HOH 218 2218 2218 HOH HOH A . N 6 HOH 219 2219 2219 HOH HOH A . N 6 HOH 220 2220 2220 HOH HOH A . N 6 HOH 221 2221 2221 HOH HOH A . N 6 HOH 222 2222 2222 HOH HOH A . N 6 HOH 223 2223 2223 HOH HOH A . N 6 HOH 224 2224 2224 HOH HOH A . N 6 HOH 225 2225 2225 HOH HOH A . N 6 HOH 226 2226 2226 HOH HOH A . N 6 HOH 227 2227 2227 HOH HOH A . N 6 HOH 228 2228 2228 HOH HOH A . N 6 HOH 229 2229 2229 HOH HOH A . N 6 HOH 230 2230 2230 HOH HOH A . N 6 HOH 231 2231 2231 HOH HOH A . N 6 HOH 232 2232 2232 HOH HOH A . N 6 HOH 233 2233 2233 HOH HOH A . N 6 HOH 234 2234 2234 HOH HOH A . N 6 HOH 235 2235 2235 HOH HOH A . N 6 HOH 236 2236 2236 HOH HOH A . N 6 HOH 237 2237 2237 HOH HOH A . N 6 HOH 238 2238 2238 HOH HOH A . N 6 HOH 239 2239 2239 HOH HOH A . N 6 HOH 240 2240 2240 HOH HOH A . N 6 HOH 241 2241 2241 HOH HOH A . N 6 HOH 242 2242 2242 HOH HOH A . N 6 HOH 243 2243 2243 HOH HOH A . N 6 HOH 244 2244 2244 HOH HOH A . N 6 HOH 245 2245 2245 HOH HOH A . N 6 HOH 246 2246 2246 HOH HOH A . N 6 HOH 247 2247 2247 HOH HOH A . N 6 HOH 248 2248 2248 HOH HOH A . N 6 HOH 249 2249 2249 HOH HOH A . N 6 HOH 250 2250 2250 HOH HOH A . N 6 HOH 251 2251 2251 HOH HOH A . N 6 HOH 252 2252 2252 HOH HOH A . N 6 HOH 253 2253 2253 HOH HOH A . N 6 HOH 254 2254 2254 HOH HOH A . N 6 HOH 255 2255 2255 HOH HOH A . N 6 HOH 256 2256 2256 HOH HOH A . N 6 HOH 257 2257 2257 HOH HOH A . N 6 HOH 258 2258 2258 HOH HOH A . N 6 HOH 259 2259 2259 HOH HOH A . N 6 HOH 260 2260 2260 HOH HOH A . N 6 HOH 261 2261 2261 HOH HOH A . N 6 HOH 262 2262 2262 HOH HOH A . N 6 HOH 263 2263 2263 HOH HOH A . N 6 HOH 264 2264 2264 HOH HOH A . N 6 HOH 265 2265 2265 HOH HOH A . N 6 HOH 266 2266 2266 HOH HOH A . N 6 HOH 267 2267 2267 HOH HOH A . N 6 HOH 268 2268 2268 HOH HOH A . N 6 HOH 269 2269 2269 HOH HOH A . N 6 HOH 270 2270 2270 HOH HOH A . N 6 HOH 271 2271 2271 HOH HOH A . N 6 HOH 272 2272 2272 HOH HOH A . N 6 HOH 273 2273 2273 HOH HOH A . N 6 HOH 274 2274 2274 HOH HOH A . N 6 HOH 275 2275 2275 HOH HOH A . N 6 HOH 276 2276 2276 HOH HOH A . N 6 HOH 277 2277 2277 HOH HOH A . N 6 HOH 278 2278 2278 HOH HOH A . N 6 HOH 279 2279 2279 HOH HOH A . N 6 HOH 280 2280 2280 HOH HOH A . N 6 HOH 281 2281 2281 HOH HOH A . N 6 HOH 282 2282 2282 HOH HOH A . N 6 HOH 283 2283 2283 HOH HOH A . N 6 HOH 284 2284 2284 HOH HOH A . N 6 HOH 285 2285 2285 HOH HOH A . N 6 HOH 286 2286 2286 HOH HOH A . N 6 HOH 287 2287 2287 HOH HOH A . N 6 HOH 288 2288 2288 HOH HOH A . N 6 HOH 289 2289 2289 HOH HOH A . N 6 HOH 290 2290 2290 HOH HOH A . N 6 HOH 291 2291 2291 HOH HOH A . N 6 HOH 292 2292 2292 HOH HOH A . N 6 HOH 293 2293 2293 HOH HOH A . N 6 HOH 294 2294 2294 HOH HOH A . N 6 HOH 295 2295 2295 HOH HOH A . N 6 HOH 296 2296 2296 HOH HOH A . N 6 HOH 297 2297 2297 HOH HOH A . N 6 HOH 298 2298 2298 HOH HOH A . N 6 HOH 299 2299 2299 HOH HOH A . N 6 HOH 300 2300 2300 HOH HOH A . N 6 HOH 301 2301 2301 HOH HOH A . N 6 HOH 302 2302 2302 HOH HOH A . N 6 HOH 303 2303 2303 HOH HOH A . N 6 HOH 304 2304 2304 HOH HOH A . N 6 HOH 305 2305 2305 HOH HOH A . N 6 HOH 306 2306 2306 HOH HOH A . N 6 HOH 307 2307 2307 HOH HOH A . N 6 HOH 308 2308 2308 HOH HOH A . N 6 HOH 309 2309 2309 HOH HOH A . N 6 HOH 310 2310 2310 HOH HOH A . N 6 HOH 311 2311 2311 HOH HOH A . N 6 HOH 312 2312 2312 HOH HOH A . N 6 HOH 313 2313 2313 HOH HOH A . N 6 HOH 314 2314 2314 HOH HOH A . N 6 HOH 315 2315 2315 HOH HOH A . N 6 HOH 316 2316 2316 HOH HOH A . N 6 HOH 317 2317 2317 HOH HOH A . N 6 HOH 318 2318 2318 HOH HOH A . N 6 HOH 319 2319 2319 HOH HOH A . N 6 HOH 320 2320 2320 HOH HOH A . N 6 HOH 321 2321 2321 HOH HOH A . N 6 HOH 322 2322 2322 HOH HOH A . N 6 HOH 323 2323 2323 HOH HOH A . N 6 HOH 324 2324 2324 HOH HOH A . N 6 HOH 325 2325 2325 HOH HOH A . N 6 HOH 326 2326 2326 HOH HOH A . N 6 HOH 327 2327 2327 HOH HOH A . N 6 HOH 328 2328 2328 HOH HOH A . N 6 HOH 329 2329 2329 HOH HOH A . N 6 HOH 330 2330 2330 HOH HOH A . N 6 HOH 331 2331 2331 HOH HOH A . N 6 HOH 332 2332 2332 HOH HOH A . N 6 HOH 333 2333 2333 HOH HOH A . N 6 HOH 334 2334 2334 HOH HOH A . N 6 HOH 335 2335 2335 HOH HOH A . N 6 HOH 336 2336 2336 HOH HOH A . N 6 HOH 337 2337 2337 HOH HOH A . N 6 HOH 338 2338 2338 HOH HOH A . N 6 HOH 339 2339 2339 HOH HOH A . N 6 HOH 340 2340 2340 HOH HOH A . N 6 HOH 341 2341 2341 HOH HOH A . N 6 HOH 342 2342 2342 HOH HOH A . N 6 HOH 343 2343 2343 HOH HOH A . N 6 HOH 344 2344 2344 HOH HOH A . N 6 HOH 345 2345 2345 HOH HOH A . N 6 HOH 346 2346 2346 HOH HOH A . N 6 HOH 347 2347 2347 HOH HOH A . N 6 HOH 348 2348 2348 HOH HOH A . N 6 HOH 349 2349 2349 HOH HOH A . N 6 HOH 350 2350 2350 HOH HOH A . N 6 HOH 351 2351 2351 HOH HOH A . N 6 HOH 352 2352 2352 HOH HOH A . N 6 HOH 353 2353 2353 HOH HOH A . N 6 HOH 354 2354 2354 HOH HOH A . N 6 HOH 355 2355 2355 HOH HOH A . N 6 HOH 356 2356 2356 HOH HOH A . N 6 HOH 357 2357 2357 HOH HOH A . N 6 HOH 358 2358 2358 HOH HOH A . N 6 HOH 359 2359 2359 HOH HOH A . N 6 HOH 360 2360 2360 HOH HOH A . N 6 HOH 361 2361 2361 HOH HOH A . N 6 HOH 362 2362 2362 HOH HOH A . N 6 HOH 363 2363 2363 HOH HOH A . N 6 HOH 364 2364 2364 HOH HOH A . N 6 HOH 365 2365 2365 HOH HOH A . N 6 HOH 366 2366 2366 HOH HOH A . N 6 HOH 367 2367 2367 HOH HOH A . N 6 HOH 368 2368 2368 HOH HOH A . N 6 HOH 369 2369 2369 HOH HOH A . N 6 HOH 370 2370 2370 HOH HOH A . N 6 HOH 371 2371 2371 HOH HOH A . N 6 HOH 372 2372 2372 HOH HOH A . N 6 HOH 373 2373 2373 HOH HOH A . N 6 HOH 374 2374 2374 HOH HOH A . N 6 HOH 375 2375 2375 HOH HOH A . N 6 HOH 376 2376 2376 HOH HOH A . N 6 HOH 377 2377 2377 HOH HOH A . N 6 HOH 378 2378 2378 HOH HOH A . N 6 HOH 379 2379 2379 HOH HOH A . N 6 HOH 380 2380 2380 HOH HOH A . N 6 HOH 381 2381 2381 HOH HOH A . N 6 HOH 382 2382 2382 HOH HOH A . N 6 HOH 383 2383 2383 HOH HOH A . N 6 HOH 384 2384 2384 HOH HOH A . N 6 HOH 385 2385 2385 HOH HOH A . N 6 HOH 386 2386 2386 HOH HOH A . N 6 HOH 387 2387 2387 HOH HOH A . N 6 HOH 388 2388 2388 HOH HOH A . N 6 HOH 389 2389 2389 HOH HOH A . N 6 HOH 390 2390 2390 HOH HOH A . N 6 HOH 391 2391 2391 HOH HOH A . N 6 HOH 392 2392 2392 HOH HOH A . N 6 HOH 393 2393 2393 HOH HOH A . N 6 HOH 394 2394 2394 HOH HOH A . N 6 HOH 395 2395 2395 HOH HOH A . N 6 HOH 396 2396 2396 HOH HOH A . N 6 HOH 397 2397 2397 HOH HOH A . N 6 HOH 398 2398 2398 HOH HOH A . N 6 HOH 399 2399 2399 HOH HOH A . N 6 HOH 400 2400 2400 HOH HOH A . N 6 HOH 401 2401 2401 HOH HOH A . N 6 HOH 402 2402 2402 HOH HOH A . N 6 HOH 403 2403 2403 HOH HOH A . N 6 HOH 404 2404 2404 HOH HOH A . N 6 HOH 405 2405 2405 HOH HOH A . N 6 HOH 406 2406 2406 HOH HOH A . N 6 HOH 407 2407 2407 HOH HOH A . N 6 HOH 408 2408 2408 HOH HOH A . N 6 HOH 409 2409 2409 HOH HOH A . N 6 HOH 410 2410 2410 HOH HOH A . N 6 HOH 411 2411 2411 HOH HOH A . N 6 HOH 412 2412 2412 HOH HOH A . N 6 HOH 413 2413 2413 HOH HOH A . N 6 HOH 414 2414 2414 HOH HOH A . N 6 HOH 415 2415 2415 HOH HOH A . N 6 HOH 416 2416 2416 HOH HOH A . N 6 HOH 417 2417 2417 HOH HOH A . N 6 HOH 418 2418 2418 HOH HOH A . N 6 HOH 419 2419 2419 HOH HOH A . N 6 HOH 420 2420 2420 HOH HOH A . N 6 HOH 421 2421 2421 HOH HOH A . N 6 HOH 422 2422 2422 HOH HOH A . N 6 HOH 423 2423 2423 HOH HOH A . N 6 HOH 424 2424 2424 HOH HOH A . N 6 HOH 425 2425 2425 HOH HOH A . N 6 HOH 426 2426 2426 HOH HOH A . N 6 HOH 427 2427 2427 HOH HOH A . N 6 HOH 428 2428 2428 HOH HOH A . N 6 HOH 429 2429 2429 HOH HOH A . N 6 HOH 430 2430 2430 HOH HOH A . N 6 HOH 431 2431 2431 HOH HOH A . N 6 HOH 432 2432 2432 HOH HOH A . N 6 HOH 433 2433 2433 HOH HOH A . N 6 HOH 434 2434 2434 HOH HOH A . N 6 HOH 435 2435 2435 HOH HOH A . N 6 HOH 436 2436 2436 HOH HOH A . N 6 HOH 437 2437 2437 HOH HOH A . N 6 HOH 438 2438 2438 HOH HOH A . N 6 HOH 439 2439 2439 HOH HOH A . N 6 HOH 440 2440 2440 HOH HOH A . N 6 HOH 441 2441 2441 HOH HOH A . N 6 HOH 442 2442 2442 HOH HOH A . N 6 HOH 443 2443 2443 HOH HOH A . N 6 HOH 444 2444 2444 HOH HOH A . N 6 HOH 445 2445 2445 HOH HOH A . N 6 HOH 446 2446 2446 HOH HOH A . N 6 HOH 447 2447 2447 HOH HOH A . N 6 HOH 448 2448 2448 HOH HOH A . N 6 HOH 449 2449 2449 HOH HOH A . N 6 HOH 450 2450 2450 HOH HOH A . N 6 HOH 451 2451 2451 HOH HOH A . N 6 HOH 452 2452 2452 HOH HOH A . N 6 HOH 453 2453 2453 HOH HOH A . N 6 HOH 454 2454 2454 HOH HOH A . N 6 HOH 455 2455 2455 HOH HOH A . N 6 HOH 456 2456 2456 HOH HOH A . N 6 HOH 457 2457 2457 HOH HOH A . N 6 HOH 458 2458 2458 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 THR 20 A THR 38 ? THR 'GLYCOSYLATION SITE' 2 A ASN 260 A ASN 278 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 283 A ASN 301 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # 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 2013-09-25 2 'Structure model' 1 1 2013-12-04 # _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 ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.6.0117 ? 1 iMOSFLM 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 PHASER phasing . ? 4 # 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 ASP A 101 ? ? 0.32 79.02 2 1 ASN A 174 ? ? -154.17 -128.73 3 1 ASN A 185 ? ? 60.74 66.92 4 1 SER A 199 ? ? -124.61 -165.16 5 1 GLU A 213 ? ? -58.81 106.45 6 1 ASN A 226 ? ? -156.92 -159.68 7 1 THR A 244 ? ? 75.54 96.38 8 1 SER A 261 ? ? -147.16 10.13 9 1 ASP A 355 ? ? -37.45 125.98 10 1 SER A 385 ? ? -152.74 60.57 # 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 ALA 19 ? A ALA 1 2 1 Y 1 A PRO 20 ? A PRO 2 3 1 Y 1 A SER 21 ? A SER 3 4 1 Y 1 A LYS 22 ? A LYS 4 5 1 Y 1 A VAL 23 ? A VAL 5 6 1 Y 1 A GLN 24 ? A GLN 6 7 1 Y 1 A ARG 25 ? A ARG 7 8 1 Y 1 A ALA 26 ? A ALA 8 9 1 Y 1 A PRO 27 ? A PRO 9 10 1 Y 1 A ASP 28 ? A ASP 10 11 1 Y 1 A SER 29 ? A SER 11 12 1 Y 1 A SER 30 ? A SER 12 13 1 Y 1 A ILE 31 ? A ILE 13 14 1 Y 1 A HIS 32 ? A HIS 14 15 1 Y 1 A ALA 33 ? A ALA 15 16 1 Y 1 A ARG 34 ? A ARG 16 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 ALPHA-D-MANNOSE MAN 3 N-ACETYL-D-GLUCOSAMINE NAG 4 'SULFATE ION' SO4 5 GLYCEROL GOL 6 water HOH #