data_1QNS # _entry.id 1QNS # _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 1QNS PDBE EBI-4279 WWPDB D_1290004279 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 1QNO unspecified 'THE 3-D STRUCTURE OF A TRICHODERMA REESEI B-MANNANASE FROM GLYCOSIDE HYDROLASE FAMILY 5' PDB 1QNP unspecified 'THE 3-D STRUCTURE OF A TRICHODERMA REESEI B-MANNANASE FROM GLYCOSIDE HYDROLASE FAMILY 5' PDB 1QNQ unspecified 'THE 3-D STRUCTURE OF A TRICHODERMA REESEI B-MANNANASE FROM GLYCOSIDE HYDROLASE FAMILY 5' PDB 1QNR unspecified 'THE 3-D STRUCTURE OF A TRICHODERMA REESEI B-MANNANASE FROM GLYCOSIDE HYDROLASE FAMILY 5' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1QNS _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 1999-10-20 _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 'Sabini, E.' 1 'Schubert, H.' 2 'Murshudov, G.' 3 'Wilson, K.S.' 4 'Siika-Aho, M.' 5 'Penttila, M.' 6 # _citation.id primary _citation.title 'The Three-Dimensional Structure of a Trichoderma Reesei Beta-Mannanase from Glycoside Hydrolase Family 5' _citation.journal_abbrev 'Acta Crystallogr.,Sect.D' _citation.journal_volume 56 _citation.page_first 3 _citation.page_last ? _citation.year 2000 _citation.journal_id_ASTM ABCRE6 _citation.country DK _citation.journal_id_ISSN 0907-4449 _citation.journal_id_CSD 0766 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 10666621 _citation.pdbx_database_id_DOI 10.1107/S0907444999013943 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Sabini, E.' 1 primary 'Schubert, H.' 2 primary 'Murshudov, G.' 3 primary 'Wilson, K.S.' 4 primary 'Siika-Aho, M.' 5 primary 'Penttila, M.' 6 # _cell.entry_id 1QNS _cell.length_a 50.180 _cell.length_b 54.600 _cell.length_c 60.760 _cell.angle_alpha 90.00 _cell.angle_beta 111.23 _cell.angle_gamma 90.00 _cell.Z_PDB 2 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1QNS _symmetry.space_group_name_H-M 'P 1 21 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 4 # 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-1,4-B-D-MANNANASE 37747.137 1 3.2.1.78 ? 'CATALYTIC DOMAIN, RESIDUES 28-371' ? 2 non-polymer syn 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL 122.143 1 ? ? ? ? 3 non-polymer syn 'SULFATE ION' 96.063 1 ? ? ? ? 4 non-polymer syn GLYCEROL 92.094 3 ? ? ? ? 5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 6 water nat water 18.015 457 ? ? ? ? # _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 ;ASSFVTISGTQFNIDGKVGYFAGTNCYWCSFLTNHADVDSTFSHISSSGLKVVRVWGFNDVNTQPSPGQIWFQKLSATGS TINTGADGLQTLDYVVQSAEQHNLKLIIPFVNNWSDYGGINAYVNAFGGNATTWYTNTAAQTQYRKYVQAVVSRYANSTA IFAWELGNEPRCNGCSTDVIVQWATSVSQYVKSLDSNHLVTLGDEGLGLSTGDGAYPYTYGEGTDFAKNVQIKSLDFGTF HLYPDSWGTNYTWGNGWIQTHAAACLAAGKPCVFEEYGAQQNPCTNEAPWQTTSLTTRGMGGDMFWQWGDTFANGAQSNS DPYTVWYNSSNWQCLVKNHVDAIN ; _entity_poly.pdbx_seq_one_letter_code_can ;ASSFVTISGTQFNIDGKVGYFAGTNCYWCSFLTNHADVDSTFSHISSSGLKVVRVWGFNDVNTQPSPGQIWFQKLSATGS TINTGADGLQTLDYVVQSAEQHNLKLIIPFVNNWSDYGGINAYVNAFGGNATTWYTNTAAQTQYRKYVQAVVSRYANSTA IFAWELGNEPRCNGCSTDVIVQWATSVSQYVKSLDSNHLVTLGDEGLGLSTGDGAYPYTYGEGTDFAKNVQIKSLDFGTF HLYPDSWGTNYTWGNGWIQTHAAACLAAGKPCVFEEYGAQQNPCTNEAPWQTTSLTTRGMGGDMFWQWGDTFANGAQSNS DPYTVWYNSSNWQCLVKNHVDAIN ; _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 SER n 1 3 SER n 1 4 PHE n 1 5 VAL n 1 6 THR n 1 7 ILE n 1 8 SER n 1 9 GLY n 1 10 THR n 1 11 GLN n 1 12 PHE n 1 13 ASN n 1 14 ILE n 1 15 ASP n 1 16 GLY n 1 17 LYS n 1 18 VAL n 1 19 GLY n 1 20 TYR n 1 21 PHE n 1 22 ALA n 1 23 GLY n 1 24 THR n 1 25 ASN n 1 26 CYS n 1 27 TYR n 1 28 TRP n 1 29 CYS n 1 30 SER n 1 31 PHE n 1 32 LEU n 1 33 THR n 1 34 ASN n 1 35 HIS n 1 36 ALA n 1 37 ASP n 1 38 VAL n 1 39 ASP n 1 40 SER n 1 41 THR n 1 42 PHE n 1 43 SER n 1 44 HIS n 1 45 ILE n 1 46 SER n 1 47 SER n 1 48 SER n 1 49 GLY n 1 50 LEU n 1 51 LYS n 1 52 VAL n 1 53 VAL n 1 54 ARG n 1 55 VAL n 1 56 TRP n 1 57 GLY n 1 58 PHE n 1 59 ASN n 1 60 ASP n 1 61 VAL n 1 62 ASN n 1 63 THR n 1 64 GLN n 1 65 PRO n 1 66 SER n 1 67 PRO n 1 68 GLY n 1 69 GLN n 1 70 ILE n 1 71 TRP n 1 72 PHE n 1 73 GLN n 1 74 LYS n 1 75 LEU n 1 76 SER n 1 77 ALA n 1 78 THR n 1 79 GLY n 1 80 SER n 1 81 THR n 1 82 ILE n 1 83 ASN n 1 84 THR n 1 85 GLY n 1 86 ALA n 1 87 ASP n 1 88 GLY n 1 89 LEU n 1 90 GLN n 1 91 THR n 1 92 LEU n 1 93 ASP n 1 94 TYR n 1 95 VAL n 1 96 VAL n 1 97 GLN n 1 98 SER n 1 99 ALA n 1 100 GLU n 1 101 GLN n 1 102 HIS n 1 103 ASN n 1 104 LEU n 1 105 LYS n 1 106 LEU n 1 107 ILE n 1 108 ILE n 1 109 PRO n 1 110 PHE n 1 111 VAL n 1 112 ASN n 1 113 ASN n 1 114 TRP n 1 115 SER n 1 116 ASP n 1 117 TYR n 1 118 GLY n 1 119 GLY n 1 120 ILE n 1 121 ASN n 1 122 ALA n 1 123 TYR n 1 124 VAL n 1 125 ASN n 1 126 ALA n 1 127 PHE n 1 128 GLY n 1 129 GLY n 1 130 ASN n 1 131 ALA n 1 132 THR n 1 133 THR n 1 134 TRP n 1 135 TYR n 1 136 THR n 1 137 ASN n 1 138 THR n 1 139 ALA n 1 140 ALA n 1 141 GLN n 1 142 THR n 1 143 GLN n 1 144 TYR n 1 145 ARG n 1 146 LYS n 1 147 TYR n 1 148 VAL n 1 149 GLN n 1 150 ALA n 1 151 VAL n 1 152 VAL n 1 153 SER n 1 154 ARG n 1 155 TYR n 1 156 ALA n 1 157 ASN n 1 158 SER n 1 159 THR n 1 160 ALA n 1 161 ILE n 1 162 PHE n 1 163 ALA n 1 164 TRP n 1 165 GLU n 1 166 LEU n 1 167 GLY n 1 168 ASN n 1 169 GLU n 1 170 PRO n 1 171 ARG n 1 172 CYS n 1 173 ASN n 1 174 GLY n 1 175 CYS n 1 176 SER n 1 177 THR n 1 178 ASP n 1 179 VAL n 1 180 ILE n 1 181 VAL n 1 182 GLN n 1 183 TRP n 1 184 ALA n 1 185 THR n 1 186 SER n 1 187 VAL n 1 188 SER n 1 189 GLN n 1 190 TYR n 1 191 VAL n 1 192 LYS n 1 193 SER n 1 194 LEU n 1 195 ASP n 1 196 SER n 1 197 ASN n 1 198 HIS n 1 199 LEU n 1 200 VAL n 1 201 THR n 1 202 LEU n 1 203 GLY n 1 204 ASP n 1 205 GLU n 1 206 GLY n 1 207 LEU n 1 208 GLY n 1 209 LEU n 1 210 SER n 1 211 THR n 1 212 GLY n 1 213 ASP n 1 214 GLY n 1 215 ALA n 1 216 TYR n 1 217 PRO n 1 218 TYR n 1 219 THR n 1 220 TYR n 1 221 GLY n 1 222 GLU n 1 223 GLY n 1 224 THR n 1 225 ASP n 1 226 PHE n 1 227 ALA n 1 228 LYS n 1 229 ASN n 1 230 VAL n 1 231 GLN n 1 232 ILE n 1 233 LYS n 1 234 SER n 1 235 LEU n 1 236 ASP n 1 237 PHE n 1 238 GLY n 1 239 THR n 1 240 PHE n 1 241 HIS n 1 242 LEU n 1 243 TYR n 1 244 PRO n 1 245 ASP n 1 246 SER n 1 247 TRP n 1 248 GLY n 1 249 THR n 1 250 ASN n 1 251 TYR n 1 252 THR n 1 253 TRP n 1 254 GLY n 1 255 ASN n 1 256 GLY n 1 257 TRP n 1 258 ILE n 1 259 GLN n 1 260 THR n 1 261 HIS n 1 262 ALA n 1 263 ALA n 1 264 ALA n 1 265 CYS n 1 266 LEU n 1 267 ALA n 1 268 ALA n 1 269 GLY n 1 270 LYS n 1 271 PRO n 1 272 CYS n 1 273 VAL n 1 274 PHE n 1 275 GLU n 1 276 GLU n 1 277 TYR n 1 278 GLY n 1 279 ALA n 1 280 GLN n 1 281 GLN n 1 282 ASN n 1 283 PRO n 1 284 CYS n 1 285 THR n 1 286 ASN n 1 287 GLU n 1 288 ALA n 1 289 PRO n 1 290 TRP n 1 291 GLN n 1 292 THR n 1 293 THR n 1 294 SER n 1 295 LEU n 1 296 THR n 1 297 THR n 1 298 ARG n 1 299 GLY n 1 300 MET n 1 301 GLY n 1 302 GLY n 1 303 ASP n 1 304 MET n 1 305 PHE n 1 306 TRP n 1 307 GLN n 1 308 TRP n 1 309 GLY n 1 310 ASP n 1 311 THR n 1 312 PHE n 1 313 ALA n 1 314 ASN n 1 315 GLY n 1 316 ALA n 1 317 GLN n 1 318 SER n 1 319 ASN n 1 320 SER n 1 321 ASP n 1 322 PRO n 1 323 TYR n 1 324 THR n 1 325 VAL n 1 326 TRP n 1 327 TYR n 1 328 ASN n 1 329 SER n 1 330 SER n 1 331 ASN n 1 332 TRP n 1 333 GLN n 1 334 CYS n 1 335 LEU n 1 336 VAL n 1 337 LYS n 1 338 ASN n 1 339 HIS n 1 340 VAL n 1 341 ASP n 1 342 ALA n 1 343 ILE n 1 344 ASN 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 ALKO4330 _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 'TRICHODERMA REESEI' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 51453 _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 'TRICHODERMA REESEI' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 51453 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene 'CBH1 PROMOTER' _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 ALKO4330 _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 SECRETED _entity_src_gen.pdbx_host_org_vector_type INTEGRATIVE _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 Q99036_HYPJE _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession Q99036 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1QNS _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 344 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession Q99036 _struct_ref_seq.db_align_beg 28 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 371 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 1 _struct_ref_seq.pdbx_auth_seq_align_end 344 # 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 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 TRS non-polymer . 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL 'TRIS BUFFER' 'C4 H12 N O3 1' 122.143 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 1QNS _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 1.9 _exptl_crystal.density_percent_sol 36 _exptl_crystal.description ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 8.50 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '2M AMMONIUM SULPHATE 0.1M TRIS-HCL PH 8.5' # _diffrn.id 1 _diffrn.ambient_temp 110.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC CCD' _diffrn_detector.pdbx_collection_date ? _diffrn_detector.details MIRRORS # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'SI(111)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.87 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SRS BEAMLINE PX9.6' _diffrn_source.pdbx_synchrotron_site SRS _diffrn_source.pdbx_synchrotron_beamline PX9.6 _diffrn_source.pdbx_wavelength 0.87 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 1QNS _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 20.000 _reflns.d_resolution_high 1.500 _reflns.number_obs 40304 _reflns.number_all ? _reflns.percent_possible_obs 84.1 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.04200 _reflns.pdbx_netI_over_sigmaI 22.4000 _reflns.B_iso_Wilson_estimate 10.334 _reflns.pdbx_redundancy 2.400 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.50 _reflns_shell.d_res_low 1.53 _reflns_shell.percent_possible_all 52.4 _reflns_shell.Rmerge_I_obs 0.01000 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 8.400 _reflns_shell.pdbx_redundancy 1.40 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 1QNS _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 60810 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 20.0 _refine.ls_d_res_high 1.50 _refine.ls_percent_reflns_obs 84.1 _refine.ls_R_factor_obs ? _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.111 _refine.ls_R_factor_R_free 0.157 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean 12.8 _refine.aniso_B[1][1] -0.242 _refine.aniso_B[2][2] 0.282 _refine.aniso_B[3][3] -0.031 _refine.aniso_B[1][2] 0.000 _refine.aniso_B[1][3] 0.550 _refine.aniso_B[2][3] 0.000 _refine.solvent_model_details ? _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct OTHER _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.07540 _refine.pdbx_overall_ESU_R_Free 0.06391 _refine.overall_SU_ML 0.03482 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 0.91031 _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 2669 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 87 _refine_hist.number_atoms_solvent 457 _refine_hist.number_atoms_total 3213 _refine_hist.d_res_high 1.50 _refine_hist.d_res_low 20.0 # 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 p_bond_d 0.013 0.020 ? ? 'X-RAY DIFFRACTION' ? p_angle_d 0.029 0.040 ? ? 'X-RAY DIFFRACTION' ? p_angle_deg ? ? ? ? 'X-RAY DIFFRACTION' ? p_planar_d 0.032 0.050 ? ? 'X-RAY DIFFRACTION' ? p_hb_or_metal_coord ? ? ? ? 'X-RAY DIFFRACTION' ? p_mcbond_it 2.080 2.000 ? ? 'X-RAY DIFFRACTION' ? p_mcangle_it 2.770 3.000 ? ? 'X-RAY DIFFRACTION' ? p_scbond_it 2.447 2.000 ? ? 'X-RAY DIFFRACTION' ? p_scangle_it 3.216 3.000 ? ? 'X-RAY DIFFRACTION' ? p_plane_restr 0.0269 ? ? ? 'X-RAY DIFFRACTION' ? p_chiral_restr 0.114 0.150 ? ? 'X-RAY DIFFRACTION' ? p_singtor_nbd 0.166 0.300 ? ? 'X-RAY DIFFRACTION' ? p_multtor_nbd 0.257 0.300 ? ? 'X-RAY DIFFRACTION' ? p_xhyhbond_nbd ? ? ? ? 'X-RAY DIFFRACTION' ? p_xyhbond_nbd ? ? ? ? 'X-RAY DIFFRACTION' ? p_planar_tor 5.0 7.0 ? ? 'X-RAY DIFFRACTION' ? p_staggered_tor 11.7 15.0 ? ? 'X-RAY DIFFRACTION' ? p_orthonormal_tor ? ? ? ? 'X-RAY DIFFRACTION' ? p_transverse_tor 36.7 20.0 ? ? 'X-RAY DIFFRACTION' ? p_special_tor 15.0 ? ? ? 'X-RAY DIFFRACTION' ? # _struct.entry_id 1QNS _struct.title 'The 3-D structure of a Trichoderma reesei b-mannanase from glycoside hydrolase family 5' _struct.pdbx_descriptor 'ENDO-1,4-B-D-MANNANASE (E.C.3.2.1.78)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1QNS _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, MANNANASE, ANOMALOUS SCATTERING' # 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 4 ? E N N 4 ? F N N 4 ? G N N 5 ? H N N 5 ? I N N 5 ? J N N 5 ? K 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 TYR A 27 ? LEU A 32 ? TYR A 27 LEU A 32 5 ? 6 HELX_P HELX_P2 2 ASN A 34 ? SER A 48 ? ASN A 34 SER A 48 1 ? 15 HELX_P HELX_P3 3 GLY A 88 ? HIS A 102 ? GLY A 88 HIS A 102 1 ? 15 HELX_P HELX_P4 4 GLY A 118 ? GLY A 128 ? GLY A 118 GLY A 128 1 ? 11 HELX_P HELX_P5 5 THR A 132 ? THR A 136 ? THR A 132 THR A 136 5 ? 5 HELX_P HELX_P6 6 ASN A 137 ? ALA A 156 ? ASN A 137 ALA A 156 1 ? 20 HELX_P HELX_P7 7 THR A 177 ? ASP A 195 ? THR A 177 ASP A 195 1 ? 19 HELX_P HELX_P8 8 ALA A 215 ? THR A 219 ? ALA A 215 THR A 219 5 ? 5 HELX_P HELX_P9 9 ASP A 225 ? GLN A 231 ? ASP A 225 GLN A 231 1 ? 7 HELX_P HELX_P10 10 TYR A 243 ? GLY A 248 ? TYR A 243 GLY A 248 1 ? 6 HELX_P HELX_P11 11 THR A 252 ? ALA A 268 ? THR A 252 ALA A 268 1 ? 17 HELX_P HELX_P12 12 ASN A 282 ? THR A 296 ? ASN A 282 THR A 296 1 ? 15 HELX_P HELX_P13 13 SER A 329 ? VAL A 336 ? SER A 329 VAL A 336 1 ? 8 HELX_P HELX_P14 14 VAL A 336 ? ASN A 344 ? VAL A 336 ASN A 344 1 ? 9 # _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 26 SG ? ? ? 1_555 A CYS 29 SG ? ? A CYS 26 A CYS 29 1_555 ? ? ? ? ? ? ? 2.035 ? disulf2 disulf ? ? A CYS 172 SG ? ? ? 1_555 A CYS 175 SG ? ? A CYS 172 A CYS 175 1_555 ? ? ? ? ? ? ? 2.092 ? disulf3 disulf ? ? A CYS 265 SG ? ? ? 1_555 A CYS 272 SG ? ? A CYS 265 A CYS 272 1_555 ? ? ? ? ? ? ? 2.098 ? disulf4 disulf ? ? A CYS 284 SG ? ? ? 1_555 A CYS 334 SG ? ? A CYS 284 A CYS 334 1_555 ? ? ? ? ? ? ? 2.068 ? covale1 covale ? ? A ASN 130 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 130 A NAG 430 1_555 ? ? ? ? ? ? ? 1.588 ? covale2 covale ? ? A ASN 157 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 157 A NAG 431 1_555 ? ? ? ? ? ? ? 1.594 ? covale3 covale ? ? A ASN 250 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 250 A NAG 432 1_555 ? ? ? ? ? ? ? 1.594 ? covale4 covale ? ? A ASN 328 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 328 A NAG 433 1_555 ? ? ? ? ? ? ? 1.601 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id TRP _struct_mon_prot_cis.label_seq_id 306 _struct_mon_prot_cis.label_asym_id A _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code ? _struct_mon_prot_cis.auth_comp_id TRP _struct_mon_prot_cis.auth_seq_id 306 _struct_mon_prot_cis.auth_asym_id A _struct_mon_prot_cis.pdbx_label_comp_id_2 GLN _struct_mon_prot_cis.pdbx_label_seq_id_2 307 _struct_mon_prot_cis.pdbx_label_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_ins_code_2 ? _struct_mon_prot_cis.pdbx_auth_comp_id_2 GLN _struct_mon_prot_cis.pdbx_auth_seq_id_2 307 _struct_mon_prot_cis.pdbx_auth_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle 5.88 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 2 ? B ? 8 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel B 1 2 ? parallel B 2 3 ? parallel B 3 4 ? parallel B 4 5 ? parallel B 5 6 ? parallel B 6 7 ? parallel B 7 8 ? parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 THR A 6 ? SER A 8 ? THR A 6 SER A 8 A 2 GLN A 11 ? ASN A 13 ? GLN A 11 ASN A 13 B 1 LEU A 199 ? THR A 201 ? LEU A 199 THR A 201 B 2 ILE A 161 ? GLU A 165 ? ILE A 161 GLU A 165 B 3 LYS A 105 ? PRO A 109 ? LYS A 105 PRO A 109 B 4 VAL A 52 ? TRP A 56 ? VAL A 52 TRP A 56 B 5 PHE A 21 ? ASN A 25 ? PHE A 21 ASN A 25 B 6 MET A 300 ? PHE A 305 ? MET A 300 PHE A 305 B 7 CYS A 272 ? TYR A 277 ? CYS A 272 TYR A 277 B 8 GLY A 238 ? LEU A 242 ? GLY A 238 LEU A 242 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O THR A 6 ? O THR A 6 N ASN A 13 ? N ASN A 13 B 1 2 O LEU A 199 ? O LEU A 199 N TRP A 164 ? N TRP A 164 B 2 3 O PHE A 162 ? O PHE A 162 N LEU A 106 ? N LEU A 106 B 3 4 O LYS A 105 ? O LYS A 105 N VAL A 53 ? N VAL A 53 B 4 5 O VAL A 52 ? O VAL A 52 N THR A 24 ? N THR A 24 B 5 6 O PHE A 21 ? O PHE A 21 N ASP A 303 ? N ASP A 303 B 6 7 O GLY A 301 ? O GLY A 301 N CYS A 272 ? N CYS A 272 B 7 8 O VAL A 273 ? O VAL A 273 N GLY A 238 ? N GLY A 238 # 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 402' AC2 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE TRS A 401' AC3 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GOL A 410' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE GOL A 411' AC5 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE GOL A 412' AC6 Software ? ? ? ? 6 'Binding site for Mono-Saccharide NAG A 430 bound to ASN A 130' AC7 Software ? ? ? ? 9 'Binding site for Mono-Saccharide NAG A 431 bound to ASN A 157' AC8 Software ? ? ? ? 3 'Binding site for Mono-Saccharide NAG A 432 bound to ASN A 250' AC9 Software ? ? ? ? 6 'Binding site for Mono-Saccharide NAG A 433 bound to ASN A 328' # 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 ASN A 282 ? ASN A 282 . ? 1_555 ? 2 AC1 7 PRO A 283 ? PRO A 283 . ? 1_555 ? 3 AC1 7 CYS A 284 ? CYS A 284 . ? 1_555 ? 4 AC1 7 THR A 285 ? THR A 285 . ? 1_555 ? 5 AC1 7 HOH K . ? HOH A 2440 . ? 1_555 ? 6 AC1 7 HOH K . ? HOH A 2441 . ? 1_555 ? 7 AC1 7 HOH K . ? HOH A 2442 . ? 1_555 ? 8 AC2 12 ASN A 168 ? ASN A 168 . ? 1_555 ? 9 AC2 12 GLU A 169 ? GLU A 169 . ? 1_555 ? 10 AC2 12 TYR A 243 ? TYR A 243 . ? 1_555 ? 11 AC2 12 GLU A 276 ? GLU A 276 . ? 1_555 ? 12 AC2 12 TRP A 306 ? TRP A 306 . ? 1_555 ? 13 AC2 12 GOL D . ? GOL A 410 . ? 1_555 ? 14 AC2 12 GOL E . ? GOL A 411 . ? 1_555 ? 15 AC2 12 GOL F . ? GOL A 412 . ? 1_555 ? 16 AC2 12 HOH K . ? HOH A 2205 . ? 1_555 ? 17 AC2 12 HOH K . ? HOH A 2405 . ? 1_555 ? 18 AC2 12 HOH K . ? HOH A 2439 . ? 1_555 ? 19 AC2 12 HOH K . ? HOH A 2444 . ? 1_555 ? 20 AC3 8 TYR A 27 ? TYR A 27 . ? 1_555 ? 21 AC3 8 TRP A 56 ? TRP A 56 . ? 1_555 ? 22 AC3 8 ASP A 116 ? ASP A 116 . ? 1_555 ? 23 AC3 8 TRS B . ? TRS A 401 . ? 1_555 ? 24 AC3 8 HOH K . ? HOH A 2205 . ? 1_555 ? 25 AC3 8 HOH K . ? HOH A 2404 . ? 1_555 ? 26 AC3 8 HOH K . ? HOH A 2439 . ? 1_555 ? 27 AC3 8 HOH K . ? HOH A 2443 . ? 1_555 ? 28 AC4 4 TRP A 114 ? TRP A 114 . ? 1_555 ? 29 AC4 4 ASP A 116 ? ASP A 116 . ? 1_555 ? 30 AC4 4 TRS B . ? TRS A 401 . ? 1_555 ? 31 AC4 4 HOH K . ? HOH A 2439 . ? 1_555 ? 32 AC5 9 GLU A 169 ? GLU A 169 . ? 1_555 ? 33 AC5 9 ARG A 171 ? ARG A 171 . ? 1_555 ? 34 AC5 9 GLU A 205 ? GLU A 205 . ? 1_555 ? 35 AC5 9 TYR A 243 ? TYR A 243 . ? 1_555 ? 36 AC5 9 SER A 246 ? SER A 246 . ? 1_555 ? 37 AC5 9 TRP A 247 ? TRP A 247 . ? 1_555 ? 38 AC5 9 TRS B . ? TRS A 401 . ? 1_555 ? 39 AC5 9 HOH K . ? HOH A 2444 . ? 1_555 ? 40 AC5 9 HOH K . ? HOH A 2445 . ? 1_555 ? 41 AC6 6 ASN A 130 ? ASN A 130 . ? 1_555 ? 42 AC6 6 THR A 133 ? THR A 133 . ? 1_555 ? 43 AC6 6 HOH K . ? HOH A 2229 . ? 1_555 ? 44 AC6 6 HOH K . ? HOH A 2446 . ? 1_555 ? 45 AC6 6 HOH K . ? HOH A 2447 . ? 1_555 ? 46 AC6 6 HOH K . ? HOH A 2448 . ? 1_555 ? 47 AC7 9 ASN A 157 ? ASN A 157 . ? 1_555 ? 48 AC7 9 ASP A 195 ? ASP A 195 . ? 1_555 ? 49 AC7 9 SER A 196 ? SER A 196 . ? 1_555 ? 50 AC7 9 ASN A 197 ? ASN A 197 . ? 1_555 ? 51 AC7 9 HOH K . ? HOH A 2449 . ? 1_555 ? 52 AC7 9 HOH K . ? HOH A 2450 . ? 1_555 ? 53 AC7 9 HOH K . ? HOH A 2451 . ? 1_555 ? 54 AC7 9 HOH K . ? HOH A 2452 . ? 1_555 ? 55 AC7 9 HOH K . ? HOH A 2453 . ? 1_555 ? 56 AC8 3 ASP A 213 ? ASP A 213 . ? 1_555 ? 57 AC8 3 ASN A 250 ? ASN A 250 . ? 1_555 ? 58 AC8 3 THR A 252 ? THR A 252 . ? 1_555 ? 59 AC9 6 ARG A 145 ? ARG A 145 . ? 1_455 ? 60 AC9 6 TYR A 190 ? TYR A 190 . ? 1_455 ? 61 AC9 6 ASN A 328 ? ASN A 328 . ? 1_555 ? 62 AC9 6 HOH K . ? HOH A 2241 . ? 1_455 ? 63 AC9 6 HOH K . ? HOH A 2455 . ? 1_555 ? 64 AC9 6 HOH K . ? HOH A 2456 . ? 1_555 ? # _database_PDB_matrix.entry_id 1QNS _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 1QNS _atom_sites.fract_transf_matrix[1][1] 0.019928 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.007742 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.018315 _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] 0.017656 _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 1 ? -1.645 52.319 11.123 1.00 41.64 ? 1 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? -0.242 52.389 10.629 1.00 41.56 ? 1 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? 0.264 51.048 10.116 1.00 40.58 ? 1 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? -0.399 50.005 10.210 1.00 41.19 ? 1 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? 0.662 52.837 11.775 1.00 42.42 ? 1 ALA A CB 1 ATOM 6 N N . SER A 1 2 ? 1.455 51.092 9.540 1.00 38.32 ? 2 SER A N 1 ATOM 7 C CA . SER A 1 2 ? 2.159 49.911 9.054 1.00 35.82 ? 2 SER A CA 1 ATOM 8 C C . SER A 1 2 ? 3.640 50.121 9.402 1.00 33.38 ? 2 SER A C 1 ATOM 9 O O . SER A 1 2 ? 4.324 50.906 8.733 1.00 35.79 ? 2 SER A O 1 ATOM 10 C CB . SER A 1 2 ? 2.079 49.635 7.552 1.00 36.51 ? 2 SER A CB 1 ATOM 11 O OG . SER A 1 2 ? 2.621 48.315 7.325 1.00 35.89 ? 2 SER A OG 1 ATOM 12 N N . SER A 1 3 ? 4.073 49.581 10.535 1.00 28.10 ? 3 SER A N 1 ATOM 13 C CA . SER A 1 3 ? 5.452 49.853 10.997 1.00 25.10 ? 3 SER A CA 1 ATOM 14 C C . SER A 1 3 ? 6.156 48.528 11.133 1.00 20.31 ? 3 SER A C 1 ATOM 15 O O . SER A 1 3 ? 5.459 47.500 11.034 1.00 20.46 ? 3 SER A O 1 ATOM 16 C CB . SER A 1 3 ? 5.364 50.584 12.351 1.00 23.95 ? 3 SER A CB 1 ATOM 17 O OG A SER A 1 3 ? 4.519 49.858 13.242 0.50 22.97 ? 3 SER A OG 1 ATOM 18 O OG B SER A 1 3 ? 4.086 51.231 12.356 0.50 23.53 ? 3 SER A OG 1 ATOM 19 N N . PHE A 1 4 ? 7.448 48.540 11.558 1.00 14.93 ? 4 PHE A N 1 ATOM 20 C CA . PHE A 1 4 ? 8.039 47.195 11.720 1.00 12.49 ? 4 PHE A CA 1 ATOM 21 C C . PHE A 1 4 ? 7.565 46.593 13.046 1.00 12.78 ? 4 PHE A C 1 ATOM 22 O O . PHE A 1 4 ? 7.339 47.330 14.044 1.00 13.24 ? 4 PHE A O 1 ATOM 23 C CB . PHE A 1 4 ? 9.578 47.319 11.802 1.00 11.74 ? 4 PHE A CB 1 ATOM 24 C CG . PHE A 1 4 ? 10.202 47.703 10.489 1.00 11.23 ? 4 PHE A CG 1 ATOM 25 C CD1 . PHE A 1 4 ? 10.119 46.889 9.367 1.00 11.16 ? 4 PHE A CD1 1 ATOM 26 C CD2 . PHE A 1 4 ? 10.882 48.910 10.323 1.00 11.56 ? 4 PHE A CD2 1 ATOM 27 C CE1 . PHE A 1 4 ? 10.661 47.224 8.164 1.00 12.08 ? 4 PHE A CE1 1 ATOM 28 C CE2 . PHE A 1 4 ? 11.455 49.256 9.112 1.00 12.61 ? 4 PHE A CE2 1 ATOM 29 C CZ . PHE A 1 4 ? 11.380 48.395 8.049 1.00 12.14 ? 4 PHE A CZ 1 ATOM 30 N N . VAL A 1 5 ? 7.329 45.274 13.081 1.00 11.46 ? 5 VAL A N 1 ATOM 31 C CA . VAL A 1 5 ? 6.871 44.647 14.307 1.00 12.01 ? 5 VAL A CA 1 ATOM 32 C C . VAL A 1 5 ? 8.002 44.644 15.325 1.00 12.22 ? 5 VAL A C 1 ATOM 33 O O . VAL A 1 5 ? 9.125 44.236 15.010 1.00 12.38 ? 5 VAL A O 1 ATOM 34 C CB . VAL A 1 5 ? 6.390 43.210 14.083 1.00 11.01 ? 5 VAL A CB 1 ATOM 35 C CG1 . VAL A 1 5 ? 6.021 42.485 15.388 1.00 12.07 ? 5 VAL A CG1 1 ATOM 36 C CG2 . VAL A 1 5 ? 5.200 43.153 13.141 1.00 12.65 ? 5 VAL A CG2 1 ATOM 37 N N . THR A 1 6 ? 7.685 45.094 16.532 1.00 10.73 ? 6 THR A N 1 ATOM 38 C CA . THR A 1 6 ? 8.637 45.188 17.624 1.00 12.51 ? 6 THR A CA 1 ATOM 39 C C . THR A 1 6 ? 8.042 44.609 18.904 1.00 11.81 ? 6 THR A C 1 ATOM 40 O O . THR A 1 6 ? 6.887 44.140 18.953 1.00 11.81 ? 6 THR A O 1 ATOM 41 C CB . THR A 1 6 ? 9.055 46.655 17.898 1.00 13.35 ? 6 THR A CB 1 ATOM 42 O OG1 . THR A 1 6 ? 7.866 47.394 18.252 1.00 15.67 ? 6 THR A OG1 1 ATOM 43 C CG2 . THR A 1 6 ? 9.782 47.266 16.708 1.00 14.80 ? 6 THR A CG2 1 ATOM 44 N N . ILE A 1 7 ? 8.855 44.539 19.947 1.00 13.12 ? 7 ILE A N 1 ATOM 45 C CA . ILE A 1 7 ? 8.492 44.127 21.286 1.00 13.02 ? 7 ILE A CA 1 ATOM 46 C C . ILE A 1 7 ? 8.465 45.330 22.217 1.00 15.41 ? 7 ILE A C 1 ATOM 47 O O . ILE A 1 7 ? 9.454 46.084 22.233 1.00 18.00 ? 7 ILE A O 1 ATOM 48 C CB . ILE A 1 7 ? 9.395 42.988 21.789 1.00 14.04 ? 7 ILE A CB 1 ATOM 49 C CG1 . ILE A 1 7 ? 9.126 41.725 20.945 1.00 15.81 ? 7 ILE A CG1 1 ATOM 50 C CG2 . ILE A 1 7 ? 9.179 42.683 23.267 1.00 15.42 ? 7 ILE A CG2 1 ATOM 51 C CD1 . ILE A 1 7 ? 10.205 40.663 21.055 1.00 17.04 ? 7 ILE A CD1 1 ATOM 52 N N . SER A 1 8 ? 7.380 45.470 22.944 1.00 18.57 ? 8 SER A N 1 ATOM 53 C CA . SER A 1 8 ? 7.277 46.588 23.913 1.00 20.39 ? 8 SER A CA 1 ATOM 54 C C . SER A 1 8 ? 6.976 45.891 25.226 1.00 22.78 ? 8 SER A C 1 ATOM 55 O O . SER A 1 8 ? 6.019 45.099 25.392 1.00 22.83 ? 8 SER A O 1 ATOM 56 C CB . SER A 1 8 ? 6.162 47.515 23.497 1.00 21.86 ? 8 SER A CB 1 ATOM 57 O OG A SER A 1 8 ? 6.091 48.668 24.317 0.50 23.68 ? 8 SER A OG 1 ATOM 58 O OG B SER A 1 8 ? 6.300 48.158 22.252 0.50 24.26 ? 8 SER A OG 1 ATOM 59 N N . GLY A 1 9 ? 7.907 46.011 26.215 1.00 23.72 ? 9 GLY A N 1 ATOM 60 C CA . GLY A 1 9 ? 7.592 45.234 27.449 1.00 25.09 ? 9 GLY A CA 1 ATOM 61 C C . GLY A 1 9 ? 7.678 43.759 27.133 1.00 24.74 ? 9 GLY A C 1 ATOM 62 O O . GLY A 1 9 ? 8.676 43.402 26.485 1.00 24.65 ? 9 GLY A O 1 ATOM 63 N N . THR A 1 10 ? 6.785 42.868 27.544 1.00 26.17 ? 10 THR A N 1 ATOM 64 C CA . THR A 1 10 ? 6.830 41.475 27.147 1.00 28.12 ? 10 THR A CA 1 ATOM 65 C C . THR A 1 10 ? 5.627 41.191 26.210 1.00 26.29 ? 10 THR A C 1 ATOM 66 O O . THR A 1 10 ? 5.167 40.069 26.128 1.00 25.79 ? 10 THR A O 1 ATOM 67 C CB . THR A 1 10 ? 6.773 40.360 28.189 1.00 30.06 ? 10 THR A CB 1 ATOM 68 O OG1 . THR A 1 10 ? 5.713 40.731 29.079 1.00 32.15 ? 10 THR A OG1 1 ATOM 69 C CG2 . THR A 1 10 ? 8.128 40.194 28.875 1.00 30.82 ? 10 THR A CG2 1 ATOM 70 N N . GLN A 1 11 ? 5.269 42.246 25.470 1.00 23.48 ? 11 GLN A N 1 ATOM 71 C CA . GLN A 1 11 ? 4.199 42.133 24.492 1.00 21.68 ? 11 GLN A CA 1 ATOM 72 C C . GLN A 1 11 ? 4.695 42.532 23.125 1.00 18.53 ? 11 GLN A C 1 ATOM 73 O O . GLN A 1 11 ? 5.709 43.247 22.965 1.00 20.87 ? 11 GLN A O 1 ATOM 74 C CB . GLN A 1 11 ? 3.027 43.072 24.863 1.00 23.20 ? 11 GLN A CB 1 ATOM 75 C CG . GLN A 1 11 ? 2.482 42.829 26.252 1.00 25.91 ? 11 GLN A CG 1 ATOM 76 C CD . GLN A 1 11 ? 1.259 43.681 26.529 1.00 29.04 ? 11 GLN A CD 1 ATOM 77 O OE1 . GLN A 1 11 ? 0.199 43.288 26.092 1.00 31.02 ? 11 GLN A OE1 1 ATOM 78 N NE2 . GLN A 1 11 ? 1.485 44.797 27.196 1.00 31.54 ? 11 GLN A NE2 1 ATOM 79 N N . PHE A 1 12 ? 3.932 42.141 22.096 1.00 12.80 ? 12 PHE A N 1 ATOM 80 C CA . PHE A 1 12 ? 4.252 42.583 20.757 1.00 11.11 ? 12 PHE A CA 1 ATOM 81 C C . PHE A 1 12 ? 3.536 43.895 20.413 1.00 12.26 ? 12 PHE A C 1 ATOM 82 O O . PHE A 1 12 ? 2.430 44.135 20.858 1.00 14.10 ? 12 PHE A O 1 ATOM 83 C CB . PHE A 1 12 ? 3.919 41.541 19.690 1.00 9.66 ? 12 PHE A CB 1 ATOM 84 C CG . PHE A 1 12 ? 4.795 40.317 19.802 1.00 9.70 ? 12 PHE A CG 1 ATOM 85 C CD1 . PHE A 1 12 ? 6.091 40.300 19.330 1.00 9.88 ? 12 PHE A CD1 1 ATOM 86 C CD2 . PHE A 1 12 ? 4.294 39.181 20.424 1.00 8.94 ? 12 PHE A CD2 1 ATOM 87 C CE1 . PHE A 1 12 ? 6.877 39.164 19.465 1.00 10.08 ? 12 PHE A CE1 1 ATOM 88 C CE2 . PHE A 1 12 ? 5.072 38.062 20.547 1.00 10.23 ? 12 PHE A CE2 1 ATOM 89 C CZ . PHE A 1 12 ? 6.390 38.036 20.087 1.00 10.18 ? 12 PHE A CZ 1 ATOM 90 N N . ASN A 1 13 ? 4.201 44.716 19.619 1.00 11.92 ? 13 ASN A N 1 ATOM 91 C CA . ASN A 1 13 ? 3.652 45.980 19.115 1.00 12.64 ? 13 ASN A CA 1 ATOM 92 C C . ASN A 1 13 ? 3.528 45.779 17.602 1.00 13.32 ? 13 ASN A C 1 ATOM 93 O O . ASN A 1 13 ? 4.527 45.698 16.863 1.00 12.75 ? 13 ASN A O 1 ATOM 94 C CB . ASN A 1 13 ? 4.644 47.107 19.449 1.00 14.46 ? 13 ASN A CB 1 ATOM 95 C CG . ASN A 1 13 ? 4.187 48.447 18.922 1.00 17.36 ? 13 ASN A CG 1 ATOM 96 O OD1 . ASN A 1 13 ? 3.453 48.527 17.929 1.00 17.75 ? 13 ASN A OD1 1 ATOM 97 N ND2 . ASN A 1 13 ? 4.653 49.542 19.524 1.00 19.89 ? 13 ASN A ND2 1 ATOM 98 N N . ILE A 1 14 ? 2.289 45.651 17.128 1.00 12.18 ? 14 ILE A N 1 ATOM 99 C CA . ILE A 1 14 ? 1.941 45.398 15.740 1.00 12.01 ? 14 ILE A CA 1 ATOM 100 C C . ILE A 1 14 ? 1.217 46.627 15.218 1.00 13.20 ? 14 ILE A C 1 ATOM 101 O O . ILE A 1 14 ? 0.139 46.976 15.704 1.00 13.26 ? 14 ILE A O 1 ATOM 102 C CB . ILE A 1 14 ? 1.057 44.129 15.592 1.00 11.34 ? 14 ILE A CB 1 ATOM 103 C CG1 . ILE A 1 14 ? 1.738 42.880 16.222 1.00 11.52 ? 14 ILE A CG1 1 ATOM 104 C CG2 . ILE A 1 14 ? 0.700 43.864 14.111 1.00 12.59 ? 14 ILE A CG2 1 ATOM 105 C CD1 . ILE A 1 14 ? 0.823 41.693 16.266 1.00 12.54 ? 14 ILE A CD1 1 ATOM 106 N N . ASP A 1 15 ? 1.838 47.373 14.316 1.00 14.38 ? 15 ASP A N 1 ATOM 107 C CA . ASP A 1 15 ? 1.262 48.594 13.744 1.00 14.41 ? 15 ASP A CA 1 ATOM 108 C C . ASP A 1 15 ? 0.871 49.581 14.816 1.00 15.63 ? 15 ASP A C 1 ATOM 109 O O . ASP A 1 15 ? -0.163 50.255 14.706 1.00 17.91 ? 15 ASP A O 1 ATOM 110 C CB . ASP A 1 15 ? 0.172 48.250 12.763 1.00 16.11 ? 15 ASP A CB 1 ATOM 111 C CG . ASP A 1 15 ? 0.707 47.472 11.545 1.00 18.18 ? 15 ASP A CG 1 ATOM 112 O OD1 . ASP A 1 15 ? 1.901 47.600 11.181 1.00 18.88 ? 15 ASP A OD1 1 ATOM 113 O OD2 . ASP A 1 15 ? -0.107 46.756 10.925 1.00 20.53 ? 15 ASP A OD2 1 ATOM 114 N N . GLY A 1 16 ? 1.651 49.665 15.876 1.00 16.37 ? 16 GLY A N 1 ATOM 115 C CA . GLY A 1 16 ? 1.408 50.641 16.942 1.00 18.14 ? 16 GLY A CA 1 ATOM 116 C C . GLY A 1 16 ? 0.518 50.189 18.060 1.00 18.42 ? 16 GLY A C 1 ATOM 117 O O . GLY A 1 16 ? 0.316 50.864 19.089 1.00 21.72 ? 16 GLY A O 1 ATOM 118 N N . LYS A 1 17 ? -0.098 49.018 17.899 1.00 16.91 ? 17 LYS A N 1 ATOM 119 C CA . LYS A 1 17 ? -0.940 48.428 18.913 1.00 17.82 ? 17 LYS A CA 1 ATOM 120 C C . LYS A 1 17 ? -0.191 47.390 19.718 1.00 14.99 ? 17 LYS A C 1 ATOM 121 O O . LYS A 1 17 ? 0.279 46.369 19.159 1.00 15.23 ? 17 LYS A O 1 ATOM 122 C CB . LYS A 1 17 ? -2.195 47.763 18.283 1.00 20.57 ? 17 LYS A CB 1 ATOM 123 C CG A LYS A 1 17 ? -3.118 48.757 17.602 0.50 24.18 ? 17 LYS A CG 1 ATOM 124 C CG B LYS A 1 17 ? -2.872 48.847 17.418 0.50 23.90 ? 17 LYS A CG 1 ATOM 125 C CD A LYS A 1 17 ? -3.834 49.603 18.656 0.50 25.77 ? 17 LYS A CD 1 ATOM 126 C CD B LYS A 1 17 ? -3.241 50.065 18.272 0.50 25.14 ? 17 LYS A CD 1 ATOM 127 C CE A LYS A 1 17 ? -4.386 50.884 18.052 0.50 27.02 ? 17 LYS A CE 1 ATOM 128 C CE B LYS A 1 17 ? -3.254 51.341 17.457 0.50 27.40 ? 17 LYS A CE 1 ATOM 129 N NZ A LYS A 1 17 ? -5.162 51.632 19.085 0.50 27.89 ? 17 LYS A NZ 1 ATOM 130 N NZ B LYS A 1 17 ? -4.206 52.348 18.005 0.50 27.55 ? 17 LYS A NZ 1 ATOM 131 N N . VAL A 1 18 ? -0.115 47.624 21.014 1.00 14.54 ? 18 VAL A N 1 ATOM 132 C CA . VAL A 1 18 ? 0.571 46.724 21.923 1.00 15.59 ? 18 VAL A CA 1 ATOM 133 C C . VAL A 1 18 ? -0.463 45.853 22.603 1.00 16.03 ? 18 VAL A C 1 ATOM 134 O O . VAL A 1 18 ? -1.434 46.279 23.258 1.00 18.87 ? 18 VAL A O 1 ATOM 135 C CB . VAL A 1 18 ? 1.345 47.521 22.984 1.00 18.05 ? 18 VAL A CB 1 ATOM 136 C CG1 . VAL A 1 18 ? 2.009 46.594 23.986 1.00 19.86 ? 18 VAL A CG1 1 ATOM 137 C CG2 . VAL A 1 18 ? 2.339 48.451 22.308 1.00 19.92 ? 18 VAL A CG2 1 ATOM 138 N N . GLY A 1 19 ? -0.287 44.540 22.463 1.00 14.92 ? 19 GLY A N 1 ATOM 139 C CA . GLY A 1 19 ? -1.227 43.618 23.077 1.00 15.30 ? 19 GLY A CA 1 ATOM 140 C C . GLY A 1 19 ? -1.182 42.227 22.428 1.00 13.11 ? 19 GLY A C 1 ATOM 141 O O . GLY A 1 19 ? -0.482 42.039 21.447 1.00 14.34 ? 19 GLY A O 1 ATOM 142 N N . TYR A 1 20 ? -1.899 41.323 23.058 1.00 13.23 ? 20 TYR A N 1 ATOM 143 C CA . TYR A 1 20 ? -1.972 39.920 22.626 1.00 11.82 ? 20 TYR A CA 1 ATOM 144 C C . TYR A 1 20 ? -2.520 39.822 21.205 1.00 12.01 ? 20 TYR A C 1 ATOM 145 O O . TYR A 1 20 ? -3.416 40.549 20.798 1.00 14.27 ? 20 TYR A O 1 ATOM 146 C CB . TYR A 1 20 ? -2.875 39.167 23.612 1.00 12.03 ? 20 TYR A CB 1 ATOM 147 C CG . TYR A 1 20 ? -2.817 37.645 23.472 1.00 11.26 ? 20 TYR A CG 1 ATOM 148 C CD1 . TYR A 1 20 ? -3.669 36.980 22.593 1.00 10.96 ? 20 TYR A CD1 1 ATOM 149 C CD2 . TYR A 1 20 ? -1.933 36.901 24.235 1.00 12.15 ? 20 TYR A CD2 1 ATOM 150 C CE1 . TYR A 1 20 ? -3.626 35.592 22.479 1.00 10.71 ? 20 TYR A CE1 1 ATOM 151 C CE2 . TYR A 1 20 ? -1.870 35.513 24.121 1.00 11.98 ? 20 TYR A CE2 1 ATOM 152 C CZ . TYR A 1 20 ? -2.687 34.878 23.229 1.00 10.81 ? 20 TYR A CZ 1 ATOM 153 O OH . TYR A 1 20 ? -2.653 33.498 23.156 1.00 10.77 ? 20 TYR A OH 1 ATOM 154 N N . PHE A 1 21 ? -2.015 38.847 20.420 1.00 10.44 ? 21 PHE A N 1 ATOM 155 C CA . PHE A 1 21 ? -2.507 38.626 19.074 1.00 9.67 ? 21 PHE A CA 1 ATOM 156 C C . PHE A 1 21 ? -2.899 37.159 18.873 1.00 10.72 ? 21 PHE A C 1 ATOM 157 O O . PHE A 1 21 ? -2.311 36.265 19.467 1.00 10.67 ? 21 PHE A O 1 ATOM 158 C CB . PHE A 1 21 ? -1.497 39.022 17.992 1.00 11.40 ? 21 PHE A CB 1 ATOM 159 C CG . PHE A 1 21 ? -0.355 38.059 17.792 1.00 9.99 ? 21 PHE A CG 1 ATOM 160 C CD1 . PHE A 1 21 ? -0.431 36.968 16.929 1.00 8.71 ? 21 PHE A CD1 1 ATOM 161 C CD2 . PHE A 1 21 ? 0.840 38.244 18.510 1.00 9.88 ? 21 PHE A CD2 1 ATOM 162 C CE1 . PHE A 1 21 ? 0.626 36.085 16.827 1.00 10.21 ? 21 PHE A CE1 1 ATOM 163 C CE2 . PHE A 1 21 ? 1.886 37.353 18.343 1.00 9.76 ? 21 PHE A CE2 1 ATOM 164 C CZ . PHE A 1 21 ? 1.817 36.280 17.489 1.00 10.23 ? 21 PHE A CZ 1 ATOM 165 N N . ALA A 1 22 ? -3.849 36.978 17.948 1.00 10.67 ? 22 ALA A N 1 ATOM 166 C CA . ALA A 1 22 ? -4.115 35.628 17.441 1.00 10.00 ? 22 ALA A CA 1 ATOM 167 C C . ALA A 1 22 ? -3.721 35.558 15.978 1.00 8.82 ? 22 ALA A C 1 ATOM 168 O O . ALA A 1 22 ? -3.866 36.528 15.199 1.00 9.59 ? 22 ALA A O 1 ATOM 169 C CB . ALA A 1 22 ? -5.596 35.259 17.606 1.00 12.70 ? 22 ALA A CB 1 ATOM 170 N N . GLY A 1 23 ? -3.155 34.419 15.556 1.00 7.32 ? 23 GLY A N 1 ATOM 171 C CA . GLY A 1 23 ? -2.813 34.187 14.170 1.00 8.24 ? 23 GLY A CA 1 ATOM 172 C C . GLY A 1 23 ? -3.066 32.733 13.767 1.00 7.86 ? 23 GLY A C 1 ATOM 173 O O . GLY A 1 23 ? -3.756 31.991 14.477 1.00 7.99 ? 23 GLY A O 1 ATOM 174 N N . THR A 1 24 ? -2.501 32.338 12.623 1.00 6.99 ? 24 THR A N 1 ATOM 175 C CA . THR A 1 24 ? -2.708 30.989 12.141 1.00 7.20 ? 24 THR A CA 1 ATOM 176 C C . THR A 1 24 ? -1.529 30.515 11.313 1.00 7.22 ? 24 THR A C 1 ATOM 177 O O . THR A 1 24 ? -0.760 31.336 10.825 1.00 8.43 ? 24 THR A O 1 ATOM 178 C CB . THR A 1 24 ? -4.001 30.880 11.289 1.00 7.77 ? 24 THR A CB 1 ATOM 179 O OG1 . THR A 1 24 ? -4.290 29.499 10.967 1.00 8.48 ? 24 THR A OG1 1 ATOM 180 C CG2 . THR A 1 24 ? -3.905 31.636 9.980 1.00 8.18 ? 24 THR A CG2 1 ATOM 181 N N . ASN A 1 25 ? -1.398 29.221 11.127 1.00 6.97 ? 25 ASN A N 1 ATOM 182 C CA . ASN A 1 25 ? -0.442 28.598 10.258 1.00 7.62 ? 25 ASN A CA 1 ATOM 183 C C . ASN A 1 25 ? -1.073 28.387 8.893 1.00 7.20 ? 25 ASN A C 1 ATOM 184 O O . ASN A 1 25 ? -2.197 27.825 8.810 1.00 7.65 ? 25 ASN A O 1 ATOM 185 C CB . ASN A 1 25 ? 0.080 27.229 10.760 1.00 7.22 ? 25 ASN A CB 1 ATOM 186 C CG . ASN A 1 25 ? 1.040 27.456 11.910 1.00 8.99 ? 25 ASN A CG 1 ATOM 187 O OD1 . ASN A 1 25 ? 2.265 27.561 11.765 1.00 8.02 ? 25 ASN A OD1 1 ATOM 188 N ND2 . ASN A 1 25 ? 0.508 27.568 13.132 1.00 8.45 ? 25 ASN A ND2 1 ATOM 189 N N . CYS A 1 26 ? -0.392 28.774 7.827 1.00 7.26 ? 26 CYS A N 1 ATOM 190 C CA . CYS A 1 26 ? -0.822 28.526 6.458 1.00 7.85 ? 26 CYS A CA 1 ATOM 191 C C . CYS A 1 26 ? 0.399 28.175 5.640 1.00 7.81 ? 26 CYS A C 1 ATOM 192 O O . CYS A 1 26 ? 0.879 28.998 4.822 1.00 8.45 ? 26 CYS A O 1 ATOM 193 C CB . CYS A 1 26 ? -1.592 29.731 5.871 1.00 8.85 ? 26 CYS A CB 1 ATOM 194 S SG . CYS A 1 26 ? -2.269 29.331 4.211 1.00 10.04 ? 26 CYS A SG 1 ATOM 195 N N . TYR A 1 27 ? 1.025 27.010 5.897 1.00 7.48 ? 27 TYR A N 1 ATOM 196 C CA . TYR A 1 27 ? 2.297 26.713 5.229 1.00 7.79 ? 27 TYR A CA 1 ATOM 197 C C . TYR A 1 27 ? 2.174 26.795 3.703 1.00 8.05 ? 27 TYR A C 1 ATOM 198 O O . TYR A 1 27 ? 3.114 27.231 3.001 1.00 9.60 ? 27 TYR A O 1 ATOM 199 C CB . TYR A 1 27 ? 2.857 25.312 5.584 1.00 8.78 ? 27 TYR A CB 1 ATOM 200 C CG . TYR A 1 27 ? 2.212 24.130 4.921 1.00 8.49 ? 27 TYR A CG 1 ATOM 201 C CD1 . TYR A 1 27 ? 2.655 23.713 3.651 1.00 9.19 ? 27 TYR A CD1 1 ATOM 202 C CD2 . TYR A 1 27 ? 1.204 23.402 5.538 1.00 9.06 ? 27 TYR A CD2 1 ATOM 203 C CE1 . TYR A 1 27 ? 2.056 22.645 3.015 1.00 8.93 ? 27 TYR A CE1 1 ATOM 204 C CE2 . TYR A 1 27 ? 0.588 22.340 4.902 1.00 9.96 ? 27 TYR A CE2 1 ATOM 205 C CZ . TYR A 1 27 ? 1.035 21.953 3.654 1.00 9.30 ? 27 TYR A CZ 1 ATOM 206 O OH . TYR A 1 27 ? 0.419 20.878 3.032 1.00 12.69 ? 27 TYR A OH 1 ATOM 207 N N . TRP A 1 28 ? 1.027 26.359 3.219 1.00 8.40 ? 28 TRP A N 1 ATOM 208 C CA . TRP A 1 28 ? 0.744 26.118 1.816 1.00 8.91 ? 28 TRP A CA 1 ATOM 209 C C . TRP A 1 28 ? 0.458 27.419 1.075 1.00 9.09 ? 28 TRP A C 1 ATOM 210 O O . TRP A 1 28 ? 0.458 27.445 -0.154 1.00 9.36 ? 28 TRP A O 1 ATOM 211 C CB . TRP A 1 28 ? -0.416 25.112 1.695 1.00 8.50 ? 28 TRP A CB 1 ATOM 212 C CG . TRP A 1 28 ? -1.629 25.442 2.528 1.00 8.55 ? 28 TRP A CG 1 ATOM 213 C CD1 . TRP A 1 28 ? -1.900 24.900 3.745 1.00 8.68 ? 28 TRP A CD1 1 ATOM 214 C CD2 . TRP A 1 28 ? -2.709 26.353 2.251 1.00 8.56 ? 28 TRP A CD2 1 ATOM 215 N NE1 . TRP A 1 28 ? -3.064 25.412 4.281 1.00 8.91 ? 28 TRP A NE1 1 ATOM 216 C CE2 . TRP A 1 28 ? -3.579 26.291 3.358 1.00 9.21 ? 28 TRP A CE2 1 ATOM 217 C CE3 . TRP A 1 28 ? -2.982 27.232 1.185 1.00 7.87 ? 28 TRP A CE3 1 ATOM 218 C CZ2 . TRP A 1 28 ? -4.759 27.060 3.405 1.00 9.05 ? 28 TRP A CZ2 1 ATOM 219 C CZ3 . TRP A 1 28 ? -4.143 27.987 1.233 1.00 8.82 ? 28 TRP A CZ3 1 ATOM 220 C CH2 . TRP A 1 28 ? -4.995 27.884 2.354 1.00 9.07 ? 28 TRP A CH2 1 ATOM 221 N N . CYS A 1 29 ? 0.227 28.533 1.773 1.00 9.14 ? 29 CYS A N 1 ATOM 222 C CA . CYS A 1 29 ? 0.000 29.809 1.133 1.00 9.87 ? 29 CYS A CA 1 ATOM 223 C C . CYS A 1 29 ? 1.170 30.212 0.251 1.00 10.09 ? 29 CYS A C 1 ATOM 224 O O . CYS A 1 29 ? 1.029 30.772 -0.829 1.00 10.95 ? 29 CYS A O 1 ATOM 225 C CB . CYS A 1 29 ? -0.276 30.850 2.255 1.00 12.24 ? 29 CYS A CB 1 ATOM 226 S SG . CYS A 1 29 ? -1.928 30.920 2.986 1.00 13.24 ? 29 CYS A SG 1 ATOM 227 N N . SER A 1 30 ? 2.410 29.847 0.657 1.00 10.40 ? 30 SER A N 1 ATOM 228 C CA . SER A 1 30 ? 3.601 30.157 -0.097 1.00 10.84 ? 30 SER A CA 1 ATOM 229 C C . SER A 1 30 ? 3.743 29.476 -1.452 1.00 11.47 ? 30 SER A C 1 ATOM 230 O O . SER A 1 30 ? 4.619 29.892 -2.228 1.00 11.22 ? 30 SER A O 1 ATOM 231 C CB . SER A 1 30 ? 4.829 29.631 0.731 1.00 12.89 ? 30 SER A CB 1 ATOM 232 O OG . SER A 1 30 ? 4.827 30.320 1.937 1.00 13.10 ? 30 SER A OG 1 ATOM 233 N N . PHE A 1 31 ? 2.960 28.401 -1.697 1.00 9.96 ? 31 PHE A N 1 ATOM 234 C CA . PHE A 1 31 ? 3.079 27.611 -2.918 1.00 12.11 ? 31 PHE A CA 1 ATOM 235 C C . PHE A 1 31 ? 1.904 27.741 -3.873 1.00 13.45 ? 31 PHE A C 1 ATOM 236 O O . PHE A 1 31 ? 1.761 27.016 -4.859 1.00 16.80 ? 31 PHE A O 1 ATOM 237 C CB . PHE A 1 31 ? 3.273 26.122 -2.538 1.00 11.81 ? 31 PHE A CB 1 ATOM 238 C CG . PHE A 1 31 ? 4.343 25.867 -1.498 1.00 9.49 ? 31 PHE A CG 1 ATOM 239 C CD1 . PHE A 1 31 ? 5.522 26.618 -1.475 1.00 10.64 ? 31 PHE A CD1 1 ATOM 240 C CD2 . PHE A 1 31 ? 4.206 24.861 -0.559 1.00 9.67 ? 31 PHE A CD2 1 ATOM 241 C CE1 . PHE A 1 31 ? 6.470 26.386 -0.487 1.00 11.07 ? 31 PHE A CE1 1 ATOM 242 C CE2 . PHE A 1 31 ? 5.171 24.561 0.368 1.00 10.01 ? 31 PHE A CE2 1 ATOM 243 C CZ . PHE A 1 31 ? 6.307 25.355 0.405 1.00 10.72 ? 31 PHE A CZ 1 ATOM 244 N N . LEU A 1 32 ? 1.014 28.656 -3.541 1.00 11.49 ? 32 LEU A N 1 ATOM 245 C CA . LEU A 1 32 ? -0.128 28.912 -4.438 1.00 12.98 ? 32 LEU A CA 1 ATOM 246 C C . LEU A 1 32 ? 0.386 29.605 -5.700 1.00 16.54 ? 32 LEU A C 1 ATOM 247 O O . LEU A 1 32 ? 1.035 30.629 -5.603 1.00 18.62 ? 32 LEU A O 1 ATOM 248 C CB . LEU A 1 32 ? -1.141 29.798 -3.702 1.00 12.90 ? 32 LEU A CB 1 ATOM 249 C CG . LEU A 1 32 ? -1.803 29.145 -2.496 1.00 11.10 ? 32 LEU A CG 1 ATOM 250 C CD1 . LEU A 1 32 ? -2.561 30.220 -1.699 1.00 11.08 ? 32 LEU A CD1 1 ATOM 251 C CD2 . LEU A 1 32 ? -2.765 28.000 -2.838 1.00 13.87 ? 32 LEU A CD2 1 ATOM 252 N N . THR A 1 33 ? -0.038 29.117 -6.868 1.00 18.98 ? 33 THR A N 1 ATOM 253 C CA . THR A 1 33 ? 0.429 29.797 -8.101 1.00 21.79 ? 33 THR A CA 1 ATOM 254 C C . THR A 1 33 ? -0.585 30.787 -8.657 1.00 22.08 ? 33 THR A C 1 ATOM 255 O O . THR A 1 33 ? -0.182 31.656 -9.452 1.00 25.31 ? 33 THR A O 1 ATOM 256 C CB . THR A 1 33 ? 0.807 28.788 -9.180 1.00 25.09 ? 33 THR A CB 1 ATOM 257 O OG1 . THR A 1 33 ? -0.295 27.896 -9.431 1.00 26.58 ? 33 THR A OG1 1 ATOM 258 C CG2 . THR A 1 33 ? 2.040 28.034 -8.711 1.00 25.86 ? 33 THR A CG2 1 ATOM 259 N N . ASN A 1 34 ? -1.835 30.700 -8.240 1.00 18.11 ? 34 ASN A N 1 ATOM 260 C CA . ASN A 1 34 ? -2.851 31.647 -8.667 1.00 17.30 ? 34 ASN A CA 1 ATOM 261 C C . ASN A 1 34 ? -2.894 32.759 -7.609 1.00 17.29 ? 34 ASN A C 1 ATOM 262 O O . ASN A 1 34 ? -3.321 32.488 -6.470 1.00 15.51 ? 34 ASN A O 1 ATOM 263 C CB . ASN A 1 34 ? -4.209 30.963 -8.824 1.00 19.52 ? 34 ASN A CB 1 ATOM 264 C CG . ASN A 1 34 ? -5.250 31.898 -9.414 1.00 23.69 ? 34 ASN A CG 1 ATOM 265 O OD1 . ASN A 1 34 ? -5.097 33.124 -9.480 1.00 25.15 ? 34 ASN A OD1 1 ATOM 266 N ND2 . ASN A 1 34 ? -6.298 31.265 -9.928 1.00 26.16 ? 34 ASN A ND2 1 ATOM 267 N N . HIS A 1 35 ? -2.528 33.971 -7.995 1.00 17.50 ? 35 HIS A N 1 ATOM 268 C CA . HIS A 1 35 ? -2.583 35.133 -7.125 1.00 19.45 ? 35 HIS A CA 1 ATOM 269 C C . HIS A 1 35 ? -3.919 35.369 -6.463 1.00 17.10 ? 35 HIS A C 1 ATOM 270 O O . HIS A 1 35 ? -4.007 35.773 -5.275 1.00 17.73 ? 35 HIS A O 1 ATOM 271 C CB . HIS A 1 35 ? -2.304 36.471 -7.884 1.00 22.01 ? 35 HIS A CB 1 ATOM 272 C CG . HIS A 1 35 ? -0.866 36.554 -8.281 1.00 24.12 ? 35 HIS A CG 1 ATOM 273 N ND1 . HIS A 1 35 ? -0.357 37.589 -9.060 1.00 26.66 ? 35 HIS A ND1 1 ATOM 274 C CD2 . HIS A 1 35 ? 0.150 35.702 -8.022 1.00 23.21 ? 35 HIS A CD2 1 ATOM 275 C CE1 . HIS A 1 35 ? 0.942 37.342 -9.239 1.00 27.20 ? 35 HIS A CE1 1 ATOM 276 N NE2 . HIS A 1 35 ? 1.265 36.220 -8.626 1.00 24.78 ? 35 HIS A NE2 1 ATOM 277 N N . ALA A 1 36 ? -4.988 35.090 -7.181 1.00 16.45 ? 36 ALA A N 1 ATOM 278 C CA . ALA A 1 36 ? -6.330 35.256 -6.642 1.00 15.99 ? 36 ALA A CA 1 ATOM 279 C C . ALA A 1 36 ? -6.540 34.381 -5.404 1.00 14.06 ? 36 ALA A C 1 ATOM 280 O O . ALA A 1 36 ? -7.297 34.763 -4.504 1.00 14.34 ? 36 ALA A O 1 ATOM 281 C CB . ALA A 1 36 ? -7.389 34.919 -7.680 1.00 16.88 ? 36 ALA A CB 1 ATOM 282 N N . ASP A 1 37 ? -5.895 33.218 -5.332 1.00 12.59 ? 37 ASP A N 1 ATOM 283 C CA . ASP A 1 37 ? -6.106 32.302 -4.194 1.00 11.41 ? 37 ASP A CA 1 ATOM 284 C C . ASP A 1 37 ? -5.370 32.804 -2.965 1.00 10.97 ? 37 ASP A C 1 ATOM 285 O O . ASP A 1 37 ? -5.778 32.587 -1.830 1.00 10.63 ? 37 ASP A O 1 ATOM 286 C CB . ASP A 1 37 ? -5.637 30.903 -4.621 1.00 11.39 ? 37 ASP A CB 1 ATOM 287 C CG . ASP A 1 37 ? -6.415 30.314 -5.768 1.00 13.44 ? 37 ASP A CG 1 ATOM 288 O OD1 . ASP A 1 37 ? -7.549 30.783 -6.034 1.00 14.43 ? 37 ASP A OD1 1 ATOM 289 O OD2 . ASP A 1 37 ? -5.895 29.308 -6.359 1.00 15.70 ? 37 ASP A OD2 1 ATOM 290 N N . VAL A 1 38 ? -4.214 33.456 -3.185 1.00 11.00 ? 38 VAL A N 1 ATOM 291 C CA . VAL A 1 38 ? -3.528 34.080 -2.057 1.00 10.96 ? 38 VAL A CA 1 ATOM 292 C C . VAL A 1 38 ? -4.442 35.177 -1.499 1.00 10.50 ? 38 VAL A C 1 ATOM 293 O O . VAL A 1 38 ? -4.631 35.278 -0.273 1.00 10.42 ? 38 VAL A O 1 ATOM 294 C CB . VAL A 1 38 ? -2.175 34.665 -2.474 1.00 11.08 ? 38 VAL A CB 1 ATOM 295 C CG1 . VAL A 1 38 ? -1.534 35.433 -1.316 1.00 12.03 ? 38 VAL A CG1 1 ATOM 296 C CG2 . VAL A 1 38 ? -1.205 33.611 -2.974 1.00 11.38 ? 38 VAL A CG2 1 ATOM 297 N N . ASP A 1 39 ? -4.957 36.029 -2.394 1.00 10.83 ? 39 ASP A N 1 ATOM 298 C CA . ASP A 1 39 ? -5.776 37.154 -1.904 1.00 11.42 ? 39 ASP A CA 1 ATOM 299 C C . ASP A 1 39 ? -7.054 36.694 -1.223 1.00 10.94 ? 39 ASP A C 1 ATOM 300 O O . ASP A 1 39 ? -7.423 37.268 -0.207 1.00 11.28 ? 39 ASP A O 1 ATOM 301 C CB . ASP A 1 39 ? -6.070 38.055 -3.095 1.00 12.61 ? 39 ASP A CB 1 ATOM 302 C CG . ASP A 1 39 ? -4.816 38.792 -3.613 1.00 14.47 ? 39 ASP A CG 1 ATOM 303 O OD1 . ASP A 1 39 ? -3.903 39.153 -2.849 1.00 18.27 ? 39 ASP A OD1 1 ATOM 304 O OD2 . ASP A 1 39 ? -4.909 39.083 -4.787 1.00 19.17 ? 39 ASP A OD2 1 ATOM 305 N N . SER A 1 40 ? -7.750 35.671 -1.742 1.00 10.46 ? 40 SER A N 1 ATOM 306 C CA . SER A 1 40 ? -8.991 35.250 -1.083 1.00 10.11 ? 40 SER A CA 1 ATOM 307 C C . SER A 1 40 ? -8.684 34.692 0.305 1.00 9.08 ? 40 SER A C 1 ATOM 308 O O . SER A 1 40 ? -9.390 34.953 1.285 1.00 9.85 ? 40 SER A O 1 ATOM 309 C CB . SER A 1 40 ? -9.839 34.275 -1.914 1.00 9.72 ? 40 SER A CB 1 ATOM 310 O OG . SER A 1 40 ? -9.109 33.122 -2.279 1.00 10.70 ? 40 SER A OG 1 ATOM 311 N N . THR A 1 41 ? -7.595 33.899 0.387 1.00 8.48 ? 41 THR A N 1 ATOM 312 C CA . THR A 1 41 ? -7.250 33.303 1.659 1.00 8.43 ? 41 THR A CA 1 ATOM 313 C C . THR A 1 41 ? -6.901 34.381 2.699 1.00 8.06 ? 41 THR A C 1 ATOM 314 O O . THR A 1 41 ? -7.348 34.359 3.846 1.00 8.97 ? 41 THR A O 1 ATOM 315 C CB . THR A 1 41 ? -6.094 32.296 1.468 1.00 9.66 ? 41 THR A CB 1 ATOM 316 O OG1 . THR A 1 41 ? -6.534 31.309 0.497 1.00 10.20 ? 41 THR A OG1 1 ATOM 317 C CG2 . THR A 1 41 ? -5.739 31.637 2.784 1.00 10.36 ? 41 THR A CG2 1 ATOM 318 N N . PHE A 1 42 ? -6.010 35.314 2.292 1.00 8.35 ? 42 PHE A N 1 ATOM 319 C CA . PHE A 1 42 ? -5.635 36.427 3.184 1.00 9.07 ? 42 PHE A CA 1 ATOM 320 C C . PHE A 1 42 ? -6.789 37.344 3.542 1.00 9.67 ? 42 PHE A C 1 ATOM 321 O O . PHE A 1 42 ? -6.847 37.817 4.679 1.00 11.07 ? 42 PHE A O 1 ATOM 322 C CB . PHE A 1 42 ? -4.426 37.155 2.587 1.00 9.15 ? 42 PHE A CB 1 ATOM 323 C CG . PHE A 1 42 ? -3.107 36.463 2.836 1.00 9.18 ? 42 PHE A CG 1 ATOM 324 C CD1 . PHE A 1 42 ? -3.001 35.196 3.382 1.00 9.38 ? 42 PHE A CD1 1 ATOM 325 C CD2 . PHE A 1 42 ? -1.937 37.160 2.518 1.00 10.07 ? 42 PHE A CD2 1 ATOM 326 C CE1 . PHE A 1 42 ? -1.758 34.625 3.613 1.00 10.17 ? 42 PHE A CE1 1 ATOM 327 C CE2 . PHE A 1 42 ? -0.713 36.571 2.760 1.00 11.57 ? 42 PHE A CE2 1 ATOM 328 C CZ . PHE A 1 42 ? -0.613 35.321 3.333 1.00 10.35 ? 42 PHE A CZ 1 ATOM 329 N N . SER A 1 43 ? -7.709 37.564 2.597 1.00 9.81 ? 43 SER A N 1 ATOM 330 C CA . SER A 1 43 ? -8.894 38.332 2.939 1.00 9.92 ? 43 SER A CA 1 ATOM 331 C C . SER A 1 43 ? -9.673 37.666 4.057 1.00 9.46 ? 43 SER A C 1 ATOM 332 O O . SER A 1 43 ? -10.100 38.323 5.021 1.00 10.22 ? 43 SER A O 1 ATOM 333 C CB . SER A 1 43 ? -9.872 38.407 1.757 1.00 12.03 ? 43 SER A CB 1 ATOM 334 O OG . SER A 1 43 ? -10.980 39.231 2.072 1.00 16.15 ? 43 SER A OG 1 ATOM 335 N N . HIS A 1 44 ? -9.815 36.333 3.997 1.00 9.04 ? 44 HIS A N 1 ATOM 336 C CA . HIS A 1 44 ? -10.562 35.606 5.018 1.00 8.78 ? 44 HIS A CA 1 ATOM 337 C C . HIS A 1 44 ? -9.860 35.627 6.369 1.00 9.20 ? 44 HIS A C 1 ATOM 338 O O . HIS A 1 44 ? -10.488 35.762 7.430 1.00 9.32 ? 44 HIS A O 1 ATOM 339 C CB . HIS A 1 44 ? -10.781 34.163 4.573 1.00 8.56 ? 44 HIS A CB 1 ATOM 340 C CG . HIS A 1 44 ? -11.536 34.007 3.299 1.00 7.72 ? 44 HIS A CG 1 ATOM 341 N ND1 . HIS A 1 44 ? -11.375 32.849 2.524 1.00 8.89 ? 44 HIS A ND1 1 ATOM 342 C CD2 . HIS A 1 44 ? -12.398 34.816 2.626 1.00 9.44 ? 44 HIS A CD2 1 ATOM 343 C CE1 . HIS A 1 44 ? -12.134 32.997 1.437 1.00 11.26 ? 44 HIS A CE1 1 ATOM 344 N NE2 . HIS A 1 44 ? -12.757 34.160 1.470 1.00 11.28 ? 44 HIS A NE2 1 ATOM 345 N N . ILE A 1 45 ? -8.516 35.445 6.341 1.00 8.31 ? 45 ILE A N 1 ATOM 346 C CA . ILE A 1 45 ? -7.764 35.519 7.592 1.00 9.01 ? 45 ILE A CA 1 ATOM 347 C C . ILE A 1 45 ? -7.910 36.909 8.236 1.00 9.40 ? 45 ILE A C 1 ATOM 348 O O . ILE A 1 45 ? -8.134 37.041 9.440 1.00 9.61 ? 45 ILE A O 1 ATOM 349 C CB . ILE A 1 45 ? -6.293 35.130 7.320 1.00 9.22 ? 45 ILE A CB 1 ATOM 350 C CG1 . ILE A 1 45 ? -6.206 33.650 6.948 1.00 8.05 ? 45 ILE A CG1 1 ATOM 351 C CG2 . ILE A 1 45 ? -5.381 35.449 8.492 1.00 8.86 ? 45 ILE A CG2 1 ATOM 352 C CD1 . ILE A 1 45 ? -4.820 33.187 6.520 1.00 8.73 ? 45 ILE A CD1 1 ATOM 353 N N . SER A 1 46 ? -7.726 37.968 7.444 1.00 9.24 ? 46 SER A N 1 ATOM 354 C CA . SER A 1 46 ? -7.841 39.335 7.918 1.00 9.74 ? 46 SER A CA 1 ATOM 355 C C . SER A 1 46 ? -9.230 39.653 8.464 1.00 10.51 ? 46 SER A C 1 ATOM 356 O O . SER A 1 46 ? -9.380 40.219 9.546 1.00 11.85 ? 46 SER A O 1 ATOM 357 C CB . SER A 1 46 ? -7.451 40.300 6.774 1.00 13.03 ? 46 SER A CB 1 ATOM 358 O OG . SER A 1 46 ? -7.562 41.640 7.303 1.00 17.06 ? 46 SER A OG 1 ATOM 359 N N . SER A 1 47 ? -10.268 39.260 7.704 1.00 10.70 ? 47 SER A N 1 ATOM 360 C CA . SER A 1 47 ? -11.644 39.582 8.147 1.00 12.73 ? 47 SER A CA 1 ATOM 361 C C . SER A 1 47 ? -12.036 38.789 9.388 1.00 11.17 ? 47 SER A C 1 ATOM 362 O O . SER A 1 47 ? -12.873 39.232 10.194 1.00 12.79 ? 47 SER A O 1 ATOM 363 C CB . SER A 1 47 ? -12.649 39.402 7.026 1.00 15.93 ? 47 SER A CB 1 ATOM 364 O OG . SER A 1 47 ? -12.809 38.079 6.650 1.00 17.46 ? 47 SER A OG 1 ATOM 365 N N . SER A 1 48 ? -11.363 37.656 9.650 1.00 10.52 ? 48 SER A N 1 ATOM 366 C CA . SER A 1 48 ? -11.592 36.890 10.865 1.00 10.54 ? 48 SER A CA 1 ATOM 367 C C . SER A 1 48 ? -10.960 37.548 12.079 1.00 11.39 ? 48 SER A C 1 ATOM 368 O O . SER A 1 48 ? -11.223 37.147 13.212 1.00 14.30 ? 48 SER A O 1 ATOM 369 C CB . SER A 1 48 ? -10.966 35.499 10.676 1.00 10.77 ? 48 SER A CB 1 ATOM 370 O OG . SER A 1 48 ? -11.659 34.740 9.713 1.00 10.76 ? 48 SER A OG 1 ATOM 371 N N . GLY A 1 49 ? -10.103 38.548 11.874 1.00 10.58 ? 49 GLY A N 1 ATOM 372 C CA . GLY A 1 49 ? -9.450 39.221 12.991 1.00 11.53 ? 49 GLY A CA 1 ATOM 373 C C . GLY A 1 49 ? -8.076 38.712 13.373 1.00 10.97 ? 49 GLY A C 1 ATOM 374 O O . GLY A 1 49 ? -7.512 39.170 14.381 1.00 12.53 ? 49 GLY A O 1 ATOM 375 N N . LEU A 1 50 ? -7.533 37.792 12.585 1.00 10.60 ? 50 LEU A N 1 ATOM 376 C CA . LEU A 1 50 ? -6.175 37.308 12.867 1.00 9.07 ? 50 LEU A CA 1 ATOM 377 C C . LEU A 1 50 ? -5.193 38.308 12.282 1.00 9.28 ? 50 LEU A C 1 ATOM 378 O O . LEU A 1 50 ? -5.441 38.932 11.236 1.00 11.87 ? 50 LEU A O 1 ATOM 379 C CB . LEU A 1 50 ? -6.079 35.952 12.162 1.00 10.30 ? 50 LEU A CB 1 ATOM 380 C CG . LEU A 1 50 ? -7.000 34.868 12.732 1.00 10.64 ? 50 LEU A CG 1 ATOM 381 C CD1 . LEU A 1 50 ? -6.813 33.582 11.931 1.00 12.14 ? 50 LEU A CD1 1 ATOM 382 C CD2 . LEU A 1 50 ? -6.771 34.578 14.205 1.00 10.35 ? 50 LEU A CD2 1 ATOM 383 N N . LYS A 1 51 ? -4.041 38.417 12.952 1.00 8.68 ? 51 LYS A N 1 ATOM 384 C CA . LYS A 1 51 ? -3.060 39.427 12.548 1.00 9.52 ? 51 LYS A CA 1 ATOM 385 C C . LYS A 1 51 ? -1.775 38.924 11.954 1.00 9.19 ? 51 LYS A C 1 ATOM 386 O O . LYS A 1 51 ? -0.989 39.660 11.322 1.00 9.25 ? 51 LYS A O 1 ATOM 387 C CB . LYS A 1 51 ? -2.715 40.309 13.784 1.00 11.42 ? 51 LYS A CB 1 ATOM 388 C CG . LYS A 1 51 ? -3.868 41.280 14.139 1.00 12.49 ? 51 LYS A CG 1 ATOM 389 C CD . LYS A 1 51 ? -3.394 42.228 15.262 1.00 16.24 ? 51 LYS A CD 1 ATOM 390 C CE . LYS A 1 51 ? -4.522 43.187 15.613 1.00 18.06 ? 51 LYS A CE 1 ATOM 391 N NZ . LYS A 1 51 ? -4.095 44.200 16.640 1.00 20.10 ? 51 LYS A NZ 1 ATOM 392 N N . VAL A 1 52 ? -1.473 37.644 12.191 1.00 9.41 ? 52 VAL A N 1 ATOM 393 C CA . VAL A 1 52 ? -0.205 37.011 11.841 1.00 8.86 ? 52 VAL A CA 1 ATOM 394 C C . VAL A 1 52 ? -0.418 35.662 11.190 1.00 7.97 ? 52 VAL A C 1 ATOM 395 O O . VAL A 1 52 ? -1.269 34.867 11.647 1.00 8.92 ? 52 VAL A O 1 ATOM 396 C CB . VAL A 1 52 ? 0.690 36.850 13.104 1.00 8.85 ? 52 VAL A CB 1 ATOM 397 C CG1 . VAL A 1 52 ? 2.089 36.351 12.711 1.00 10.03 ? 52 VAL A CG1 1 ATOM 398 C CG2 . VAL A 1 52 ? 0.814 38.153 13.907 1.00 11.06 ? 52 VAL A CG2 1 ATOM 399 N N . VAL A 1 53 ? 0.310 35.381 10.130 1.00 8.28 ? 53 VAL A N 1 ATOM 400 C CA . VAL A 1 53 ? 0.276 34.127 9.389 1.00 7.25 ? 53 VAL A CA 1 ATOM 401 C C . VAL A 1 53 ? 1.687 33.540 9.299 1.00 6.97 ? 53 VAL A C 1 ATOM 402 O O . VAL A 1 53 ? 2.637 34.238 8.967 1.00 8.52 ? 53 VAL A O 1 ATOM 403 C CB . VAL A 1 53 ? -0.342 34.285 7.977 1.00 8.00 ? 53 VAL A CB 1 ATOM 404 C CG1 . VAL A 1 53 ? -0.609 32.903 7.353 1.00 10.53 ? 53 VAL A CG1 1 ATOM 405 C CG2 . VAL A 1 53 ? -1.620 35.079 8.004 1.00 10.98 ? 53 VAL A CG2 1 ATOM 406 N N . ARG A 1 54 ? 1.791 32.233 9.564 1.00 7.11 ? 54 ARG A N 1 ATOM 407 C CA . ARG A 1 54 ? 3.065 31.505 9.441 1.00 6.18 ? 54 ARG A CA 1 ATOM 408 C C . ARG A 1 54 ? 3.059 30.747 8.117 1.00 7.72 ? 54 ARG A C 1 ATOM 409 O O . ARG A 1 54 ? 2.147 29.940 7.889 1.00 8.70 ? 54 ARG A O 1 ATOM 410 C CB . ARG A 1 54 ? 3.301 30.632 10.678 1.00 7.29 ? 54 ARG A CB 1 ATOM 411 C CG . ARG A 1 54 ? 4.635 29.871 10.647 1.00 7.71 ? 54 ARG A CG 1 ATOM 412 C CD . ARG A 1 54 ? 4.972 29.532 12.083 1.00 6.64 ? 54 ARG A CD 1 ATOM 413 N NE . ARG A 1 54 ? 6.146 28.688 12.240 1.00 7.29 ? 54 ARG A NE 1 ATOM 414 C CZ . ARG A 1 54 ? 6.151 27.369 12.301 1.00 7.11 ? 54 ARG A CZ 1 ATOM 415 N NH1 . ARG A 1 54 ? 5.060 26.652 12.121 1.00 7.53 ? 54 ARG A NH1 1 ATOM 416 N NH2 . ARG A 1 54 ? 7.285 26.718 12.531 1.00 7.06 ? 54 ARG A NH2 1 ATOM 417 N N . VAL A 1 55 ? 4.027 31.027 7.247 1.00 6.45 ? 55 VAL A N 1 ATOM 418 C CA . VAL A 1 55 ? 4.082 30.421 5.901 1.00 6.63 ? 55 VAL A CA 1 ATOM 419 C C . VAL A 1 55 ? 5.451 29.803 5.676 1.00 7.62 ? 55 VAL A C 1 ATOM 420 O O . VAL A 1 55 ? 6.429 30.274 6.301 1.00 8.13 ? 55 VAL A O 1 ATOM 421 C CB . VAL A 1 55 ? 3.748 31.444 4.804 1.00 7.52 ? 55 VAL A CB 1 ATOM 422 C CG1 . VAL A 1 55 ? 2.382 32.108 5.026 1.00 9.15 ? 55 VAL A CG1 1 ATOM 423 C CG2 . VAL A 1 55 ? 4.839 32.532 4.678 1.00 8.96 ? 55 VAL A CG2 1 ATOM 424 N N . TRP A 1 56 ? 5.553 28.730 4.881 1.00 6.76 ? 56 TRP A N 1 ATOM 425 C CA . TRP A 1 56 ? 6.896 28.176 4.627 1.00 6.93 ? 56 TRP A CA 1 ATOM 426 C C . TRP A 1 56 ? 7.746 29.149 3.804 1.00 7.71 ? 56 TRP A C 1 ATOM 427 O O . TRP A 1 56 ? 7.343 29.643 2.761 1.00 9.12 ? 56 TRP A O 1 ATOM 428 C CB . TRP A 1 56 ? 6.838 26.811 3.981 1.00 8.13 ? 56 TRP A CB 1 ATOM 429 C CG . TRP A 1 56 ? 6.405 25.668 4.846 1.00 8.02 ? 56 TRP A CG 1 ATOM 430 C CD1 . TRP A 1 56 ? 6.233 24.392 4.377 1.00 8.23 ? 56 TRP A CD1 1 ATOM 431 C CD2 . TRP A 1 56 ? 6.228 25.586 6.274 1.00 8.03 ? 56 TRP A CD2 1 ATOM 432 N NE1 . TRP A 1 56 ? 5.980 23.515 5.411 1.00 8.40 ? 56 TRP A NE1 1 ATOM 433 C CE2 . TRP A 1 56 ? 5.916 24.240 6.585 1.00 8.32 ? 56 TRP A CE2 1 ATOM 434 C CE3 . TRP A 1 56 ? 6.233 26.517 7.313 1.00 7.94 ? 56 TRP A CE3 1 ATOM 435 C CZ2 . TRP A 1 56 ? 5.705 23.768 7.877 1.00 8.45 ? 56 TRP A CZ2 1 ATOM 436 C CZ3 . TRP A 1 56 ? 5.959 26.060 8.589 1.00 8.04 ? 56 TRP A CZ3 1 ATOM 437 C CH2 . TRP A 1 56 ? 5.721 24.695 8.904 1.00 7.18 ? 56 TRP A CH2 1 ATOM 438 N N . GLY A 1 57 ? 9.003 29.365 4.219 1.00 7.13 ? 57 GLY A N 1 ATOM 439 C CA . GLY A 1 57 ? 9.967 30.155 3.445 1.00 7.96 ? 57 GLY A CA 1 ATOM 440 C C . GLY A 1 57 ? 10.958 29.301 2.648 1.00 7.99 ? 57 GLY A C 1 ATOM 441 O O . GLY A 1 57 ? 11.972 29.834 2.193 1.00 10.68 ? 57 GLY A O 1 ATOM 442 N N . PHE A 1 58 ? 10.643 28.049 2.460 1.00 7.67 ? 58 PHE A N 1 ATOM 443 C CA . PHE A 1 58 ? 11.446 27.057 1.818 1.00 8.05 ? 58 PHE A CA 1 ATOM 444 C C . PHE A 1 58 ? 10.653 26.165 0.883 1.00 7.76 ? 58 PHE A C 1 ATOM 445 O O . PHE A 1 58 ? 9.460 25.965 1.119 1.00 8.17 ? 58 PHE A O 1 ATOM 446 C CB . PHE A 1 58 ? 12.157 26.142 2.861 1.00 9.26 ? 58 PHE A CB 1 ATOM 447 C CG . PHE A 1 58 ? 11.219 25.491 3.859 1.00 7.42 ? 58 PHE A CG 1 ATOM 448 C CD1 . PHE A 1 58 ? 10.522 24.321 3.531 1.00 7.91 ? 58 PHE A CD1 1 ATOM 449 C CD2 . PHE A 1 58 ? 11.011 26.083 5.090 1.00 8.11 ? 58 PHE A CD2 1 ATOM 450 C CE1 . PHE A 1 58 ? 9.634 23.781 4.439 1.00 7.78 ? 58 PHE A CE1 1 ATOM 451 C CE2 . PHE A 1 58 ? 10.116 25.542 6.016 1.00 7.40 ? 58 PHE A CE2 1 ATOM 452 C CZ . PHE A 1 58 ? 9.449 24.375 5.688 1.00 7.24 ? 58 PHE A CZ 1 ATOM 453 N N . ASN A 1 59 ? 11.338 25.540 -0.081 1.00 8.95 ? 59 ASN A N 1 ATOM 454 C CA . ASN A 1 59 ? 10.799 24.501 -0.938 1.00 8.50 ? 59 ASN A CA 1 ATOM 455 C C . ASN A 1 59 ? 12.037 23.956 -1.652 1.00 9.05 ? 59 ASN A C 1 ATOM 456 O O . ASN A 1 59 ? 12.463 24.424 -2.696 1.00 9.69 ? 59 ASN A O 1 ATOM 457 C CB . ASN A 1 59 ? 9.695 25.011 -1.865 1.00 10.17 ? 59 ASN A CB 1 ATOM 458 C CG . ASN A 1 59 ? 8.969 23.856 -2.541 1.00 10.65 ? 59 ASN A CG 1 ATOM 459 O OD1 . ASN A 1 59 ? 9.600 22.852 -2.882 1.00 14.32 ? 59 ASN A OD1 1 ATOM 460 N ND2 . ASN A 1 59 ? 7.686 23.988 -2.777 1.00 11.03 ? 59 ASN A ND2 1 ATOM 461 N N . ASP A 1 60 ? 12.647 22.964 -0.969 1.00 9.36 ? 60 ASP A N 1 ATOM 462 C CA . ASP A 1 60 ? 13.934 22.406 -1.355 1.00 10.07 ? 60 ASP A CA 1 ATOM 463 C C . ASP A 1 60 ? 13.767 21.115 -2.118 1.00 9.21 ? 60 ASP A C 1 ATOM 464 O O . ASP A 1 60 ? 13.002 20.232 -1.722 1.00 10.62 ? 60 ASP A O 1 ATOM 465 C CB . ASP A 1 60 ? 14.737 22.134 -0.065 1.00 10.49 ? 60 ASP A CB 1 ATOM 466 C CG . ASP A 1 60 ? 15.171 23.423 0.627 1.00 9.11 ? 60 ASP A CG 1 ATOM 467 O OD1 . ASP A 1 60 ? 15.754 24.295 -0.088 1.00 10.27 ? 60 ASP A OD1 1 ATOM 468 O OD2 . ASP A 1 60 ? 14.989 23.573 1.863 1.00 11.25 ? 60 ASP A OD2 1 ATOM 469 N N . VAL A 1 61 ? 14.517 20.981 -3.192 1.00 11.09 ? 61 VAL A N 1 ATOM 470 C CA . VAL A 1 61 ? 14.513 19.811 -4.048 1.00 11.03 ? 61 VAL A CA 1 ATOM 471 C C . VAL A 1 61 ? 15.956 19.368 -4.362 1.00 11.93 ? 61 VAL A C 1 ATOM 472 O O . VAL A 1 61 ? 16.875 20.165 -4.283 1.00 12.10 ? 61 VAL A O 1 ATOM 473 C CB . VAL A 1 61 ? 13.761 20.021 -5.403 1.00 11.95 ? 61 VAL A CB 1 ATOM 474 C CG1 . VAL A 1 61 ? 12.332 20.441 -5.137 1.00 13.32 ? 61 VAL A CG1 1 ATOM 475 C CG2 . VAL A 1 61 ? 14.459 21.080 -6.269 1.00 12.44 ? 61 VAL A CG2 1 ATOM 476 N N . ASN A 1 62 ? 16.095 18.127 -4.777 1.00 13.31 ? 62 ASN A N 1 ATOM 477 C CA . ASN A 1 62 ? 17.340 17.564 -5.286 1.00 13.21 ? 62 ASN A CA 1 ATOM 478 C C . ASN A 1 62 ? 17.251 17.388 -6.804 1.00 16.73 ? 62 ASN A C 1 ATOM 479 O O . ASN A 1 62 ? 18.266 17.420 -7.460 1.00 20.91 ? 62 ASN A O 1 ATOM 480 C CB . ASN A 1 62 ? 17.781 16.279 -4.609 1.00 13.41 ? 62 ASN A CB 1 ATOM 481 C CG . ASN A 1 62 ? 18.017 16.477 -3.123 1.00 12.67 ? 62 ASN A CG 1 ATOM 482 O OD1 . ASN A 1 62 ? 17.350 15.904 -2.265 1.00 13.30 ? 62 ASN A OD1 1 ATOM 483 N ND2 . ASN A 1 62 ? 18.990 17.300 -2.765 1.00 13.24 ? 62 ASN A ND2 1 ATOM 484 N N . THR A 1 63 ? 16.046 17.188 -7.328 1.00 19.13 ? 63 THR A N 1 ATOM 485 C CA . THR A 1 63 ? 15.808 17.019 -8.750 1.00 23.24 ? 63 THR A CA 1 ATOM 486 C C . THR A 1 63 ? 14.808 18.125 -9.097 1.00 23.98 ? 63 THR A C 1 ATOM 487 O O . THR A 1 63 ? 13.851 18.323 -8.341 1.00 23.44 ? 63 THR A O 1 ATOM 488 C CB . THR A 1 63 ? 15.217 15.652 -9.115 1.00 27.45 ? 63 THR A CB 1 ATOM 489 O OG1 . THR A 1 63 ? 13.957 15.545 -8.471 1.00 32.34 ? 63 THR A OG1 1 ATOM 490 C CG2 . THR A 1 63 ? 16.007 14.447 -8.627 1.00 27.94 ? 63 THR A CG2 1 ATOM 491 N N . GLN A 1 64 ? 14.981 18.799 -10.209 1.00 26.94 ? 64 GLN A N 1 ATOM 492 C CA . GLN A 1 64 ? 13.971 19.815 -10.534 1.00 29.29 ? 64 GLN A CA 1 ATOM 493 C C . GLN A 1 64 ? 12.636 19.142 -10.796 1.00 29.03 ? 64 GLN A C 1 ATOM 494 O O . GLN A 1 64 ? 12.620 18.085 -11.420 1.00 30.47 ? 64 GLN A O 1 ATOM 495 C CB . GLN A 1 64 ? 14.330 20.614 -11.783 1.00 32.03 ? 64 GLN A CB 1 ATOM 496 C CG . GLN A 1 64 ? 14.687 22.033 -11.409 1.00 35.01 ? 64 GLN A CG 1 ATOM 497 C CD . GLN A 1 64 ? 14.990 22.871 -12.629 1.00 35.17 ? 64 GLN A CD 1 ATOM 498 O OE1 . GLN A 1 64 ? 14.087 23.230 -13.373 1.00 35.67 ? 64 GLN A OE1 1 ATOM 499 N NE2 . GLN A 1 64 ? 16.266 23.178 -12.764 1.00 35.82 ? 64 GLN A NE2 1 ATOM 500 N N . PRO A 1 65 ? 11.568 19.758 -10.335 1.00 27.09 ? 65 PRO A N 1 ATOM 501 C CA . PRO A 1 65 ? 10.255 19.166 -10.512 1.00 27.40 ? 65 PRO A CA 1 ATOM 502 C C . PRO A 1 65 ? 9.833 19.327 -11.967 1.00 28.63 ? 65 PRO A C 1 ATOM 503 O O . PRO A 1 65 ? 10.499 20.009 -12.735 1.00 26.42 ? 65 PRO A O 1 ATOM 504 C CB . PRO A 1 65 ? 9.351 19.951 -9.586 1.00 27.02 ? 65 PRO A CB 1 ATOM 505 C CG . PRO A 1 65 ? 10.036 21.276 -9.455 1.00 26.44 ? 65 PRO A CG 1 ATOM 506 C CD . PRO A 1 65 ? 11.505 20.991 -9.529 1.00 26.08 ? 65 PRO A CD 1 ATOM 507 N N . SER A 1 66 ? 8.702 18.677 -12.266 1.00 29.20 ? 66 SER A N 1 ATOM 508 C CA . SER A 1 66 ? 8.151 18.870 -13.604 1.00 29.85 ? 66 SER A CA 1 ATOM 509 C C . SER A 1 66 ? 8.034 20.369 -13.873 1.00 28.81 ? 66 SER A C 1 ATOM 510 O O . SER A 1 66 ? 7.652 21.204 -13.036 1.00 26.36 ? 66 SER A O 1 ATOM 511 C CB . SER A 1 66 ? 6.747 18.250 -13.705 1.00 30.83 ? 66 SER A CB 1 ATOM 512 O OG . SER A 1 66 ? 6.753 16.940 -13.114 1.00 32.62 ? 66 SER A OG 1 ATOM 513 N N . PRO A 1 67 ? 8.279 20.759 -15.109 1.00 29.34 ? 67 PRO A N 1 ATOM 514 C CA . PRO A 1 67 ? 8.109 22.129 -15.546 1.00 29.25 ? 67 PRO A CA 1 ATOM 515 C C . PRO A 1 67 ? 6.754 22.671 -15.115 1.00 27.65 ? 67 PRO A C 1 ATOM 516 O O . PRO A 1 67 ? 5.680 22.070 -15.310 1.00 28.76 ? 67 PRO A O 1 ATOM 517 C CB . PRO A 1 67 ? 8.293 21.996 -17.050 1.00 31.04 ? 67 PRO A CB 1 ATOM 518 C CG . PRO A 1 67 ? 9.279 20.869 -17.184 1.00 31.92 ? 67 PRO A CG 1 ATOM 519 C CD . PRO A 1 67 ? 8.736 19.845 -16.207 1.00 30.88 ? 67 PRO A CD 1 ATOM 520 N N . GLY A 1 68 ? 6.730 23.822 -14.462 1.00 26.04 ? 68 GLY A N 1 ATOM 521 C CA . GLY A 1 68 ? 5.582 24.501 -13.908 1.00 23.69 ? 68 GLY A CA 1 ATOM 522 C C . GLY A 1 68 ? 5.404 24.356 -12.403 1.00 22.31 ? 68 GLY A C 1 ATOM 523 O O . GLY A 1 68 ? 4.703 25.159 -11.744 1.00 22.76 ? 68 GLY A O 1 ATOM 524 N N . GLN A 1 69 ? 5.992 23.317 -11.827 1.00 21.33 ? 69 GLN A N 1 ATOM 525 C CA . GLN A 1 69 ? 5.916 23.094 -10.383 1.00 20.54 ? 69 GLN A CA 1 ATOM 526 C C . GLN A 1 69 ? 6.836 24.051 -9.633 1.00 19.17 ? 69 GLN A C 1 ATOM 527 O O . GLN A 1 69 ? 7.857 24.495 -10.174 1.00 18.89 ? 69 GLN A O 1 ATOM 528 C CB . GLN A 1 69 ? 6.231 21.645 -10.011 1.00 23.18 ? 69 GLN A CB 1 ATOM 529 C CG . GLN A 1 69 ? 5.184 20.669 -10.558 1.00 25.91 ? 69 GLN A CG 1 ATOM 530 C CD . GLN A 1 69 ? 3.777 20.998 -10.131 1.00 29.34 ? 69 GLN A CD 1 ATOM 531 O OE1 . GLN A 1 69 ? 3.484 21.242 -8.964 1.00 30.34 ? 69 GLN A OE1 1 ATOM 532 N NE2 . GLN A 1 69 ? 2.866 21.025 -11.102 1.00 30.71 ? 69 GLN A NE2 1 ATOM 533 N N . ILE A 1 70 ? 6.423 24.416 -8.429 1.00 18.58 ? 70 ILE A N 1 ATOM 534 C CA . ILE A 1 70 ? 7.185 25.367 -7.630 1.00 17.48 ? 70 ILE A CA 1 ATOM 535 C C . ILE A 1 70 ? 8.356 24.698 -6.924 1.00 16.64 ? 70 ILE A C 1 ATOM 536 O O . ILE A 1 70 ? 8.330 23.573 -6.430 1.00 19.13 ? 70 ILE A O 1 ATOM 537 C CB . ILE A 1 70 ? 6.272 26.009 -6.567 1.00 18.48 ? 70 ILE A CB 1 ATOM 538 C CG1 . ILE A 1 70 ? 5.064 26.674 -7.246 1.00 21.82 ? 70 ILE A CG1 1 ATOM 539 C CG2 . ILE A 1 70 ? 6.980 26.986 -5.641 1.00 19.24 ? 70 ILE A CG2 1 ATOM 540 C CD1 . ILE A 1 70 ? 5.440 27.679 -8.301 1.00 23.85 ? 70 ILE A CD1 1 ATOM 541 N N . TRP A 1 71 ? 9.470 25.430 -6.982 1.00 14.38 ? 71 TRP A N 1 ATOM 542 C CA . TRP A 1 71 ? 10.660 25.056 -6.238 1.00 12.81 ? 71 TRP A CA 1 ATOM 543 C C . TRP A 1 71 ? 11.430 26.307 -5.857 1.00 11.89 ? 71 TRP A C 1 ATOM 544 O O . TRP A 1 71 ? 11.525 27.183 -6.710 1.00 13.38 ? 71 TRP A O 1 ATOM 545 C CB . TRP A 1 71 ? 11.515 24.064 -7.008 1.00 13.64 ? 71 TRP A CB 1 ATOM 546 C CG . TRP A 1 71 ? 12.071 24.490 -8.320 1.00 14.62 ? 71 TRP A CG 1 ATOM 547 C CD1 . TRP A 1 71 ? 11.389 24.589 -9.500 1.00 15.06 ? 71 TRP A CD1 1 ATOM 548 C CD2 . TRP A 1 71 ? 13.409 24.899 -8.609 1.00 14.94 ? 71 TRP A CD2 1 ATOM 549 N NE1 . TRP A 1 71 ? 12.215 25.029 -10.502 1.00 16.27 ? 71 TRP A NE1 1 ATOM 550 C CE2 . TRP A 1 71 ? 13.470 25.235 -9.975 1.00 15.29 ? 71 TRP A CE2 1 ATOM 551 C CE3 . TRP A 1 71 ? 14.565 25.035 -7.828 1.00 14.95 ? 71 TRP A CE3 1 ATOM 552 C CZ2 . TRP A 1 71 ? 14.656 25.671 -10.575 1.00 15.46 ? 71 TRP A CZ2 1 ATOM 553 C CZ3 . TRP A 1 71 ? 15.736 25.472 -8.435 1.00 15.84 ? 71 TRP A CZ3 1 ATOM 554 C CH2 . TRP A 1 71 ? 15.772 25.787 -9.794 1.00 16.38 ? 71 TRP A CH2 1 ATOM 555 N N . PHE A 1 72 ? 11.942 26.456 -4.632 1.00 10.51 ? 72 PHE A N 1 ATOM 556 C CA . PHE A 1 72 ? 12.743 27.634 -4.279 1.00 11.07 ? 72 PHE A CA 1 ATOM 557 C C . PHE A 1 72 ? 14.245 27.382 -4.320 1.00 10.48 ? 72 PHE A C 1 ATOM 558 O O . PHE A 1 72 ? 14.993 28.341 -4.565 1.00 10.14 ? 72 PHE A O 1 ATOM 559 C CB . PHE A 1 72 ? 12.338 28.140 -2.895 1.00 10.48 ? 72 PHE A CB 1 ATOM 560 C CG . PHE A 1 72 ? 10.902 28.586 -2.677 1.00 9.98 ? 72 PHE A CG 1 ATOM 561 C CD1 . PHE A 1 72 ? 10.080 28.909 -3.730 1.00 10.86 ? 72 PHE A CD1 1 ATOM 562 C CD2 . PHE A 1 72 ? 10.426 28.816 -1.392 1.00 10.13 ? 72 PHE A CD2 1 ATOM 563 C CE1 . PHE A 1 72 ? 8.767 29.323 -3.550 1.00 11.38 ? 72 PHE A CE1 1 ATOM 564 C CE2 . PHE A 1 72 ? 9.133 29.246 -1.175 1.00 10.57 ? 72 PHE A CE2 1 ATOM 565 C CZ . PHE A 1 72 ? 8.320 29.522 -2.263 1.00 10.39 ? 72 PHE A CZ 1 ATOM 566 N N . GLN A 1 73 ? 14.701 26.154 -4.132 1.00 10.68 ? 73 GLN A N 1 ATOM 567 C CA . GLN A 1 73 ? 16.134 25.866 -4.150 1.00 9.25 ? 73 GLN A CA 1 ATOM 568 C C . GLN A 1 73 ? 16.375 24.418 -4.559 1.00 10.41 ? 73 GLN A C 1 ATOM 569 O O . GLN A 1 73 ? 15.701 23.512 -4.060 1.00 10.86 ? 73 GLN A O 1 ATOM 570 C CB . GLN A 1 73 ? 16.688 26.115 -2.744 1.00 9.35 ? 73 GLN A CB 1 ATOM 571 C CG . GLN A 1 73 ? 18.173 25.902 -2.615 1.00 10.45 ? 73 GLN A CG 1 ATOM 572 C CD . GLN A 1 73 ? 18.735 26.292 -1.280 1.00 9.91 ? 73 GLN A CD 1 ATOM 573 O OE1 . GLN A 1 73 ? 19.790 26.947 -1.182 1.00 11.36 ? 73 GLN A OE1 1 ATOM 574 N NE2 . GLN A 1 73 ? 18.154 25.886 -0.157 1.00 9.08 ? 73 GLN A NE2 1 ATOM 575 N N . LYS A 1 74 ? 17.358 24.199 -5.415 1.00 10.78 ? 74 LYS A N 1 ATOM 576 C CA . LYS A 1 74 ? 17.799 22.883 -5.849 1.00 12.29 ? 74 LYS A CA 1 ATOM 577 C C . LYS A 1 74 ? 19.174 22.691 -5.214 1.00 11.79 ? 74 LYS A C 1 ATOM 578 O O . LYS A 1 74 ? 20.122 23.468 -5.445 1.00 13.32 ? 74 LYS A O 1 ATOM 579 C CB . LYS A 1 74 ? 17.883 22.721 -7.362 1.00 13.44 ? 74 LYS A CB 1 ATOM 580 C CG . LYS A 1 74 ? 18.489 21.388 -7.784 1.00 16.59 ? 74 LYS A CG 1 ATOM 581 C CD . LYS A 1 74 ? 18.523 21.178 -9.295 1.00 20.87 ? 74 LYS A CD 1 ATOM 582 C CE . LYS A 1 74 ? 19.476 20.003 -9.569 1.00 24.80 ? 74 LYS A CE 1 ATOM 583 N NZ . LYS A 1 74 ? 19.569 19.741 -11.045 1.00 28.72 ? 74 LYS A NZ 1 ATOM 584 N N . LEU A 1 75 ? 19.282 21.654 -4.404 1.00 11.76 ? 75 LEU A N 1 ATOM 585 C CA . LEU A 1 75 ? 20.492 21.317 -3.669 1.00 12.80 ? 75 LEU A CA 1 ATOM 586 C C . LEU A 1 75 ? 21.238 20.184 -4.368 1.00 13.30 ? 75 LEU A C 1 ATOM 587 O O . LEU A 1 75 ? 20.716 19.101 -4.547 1.00 13.56 ? 75 LEU A O 1 ATOM 588 C CB . LEU A 1 75 ? 20.125 20.932 -2.229 1.00 12.42 ? 75 LEU A CB 1 ATOM 589 C CG . LEU A 1 75 ? 19.483 22.091 -1.445 1.00 13.34 ? 75 LEU A CG 1 ATOM 590 C CD1 . LEU A 1 75 ? 18.851 21.631 -0.167 1.00 15.13 ? 75 LEU A CD1 1 ATOM 591 C CD2 . LEU A 1 75 ? 20.516 23.173 -1.171 1.00 13.03 ? 75 LEU A CD2 1 ATOM 592 N N . SER A 1 76 ? 22.469 20.480 -4.743 1.00 12.75 ? 76 SER A N 1 ATOM 593 C CA . SER A 1 76 ? 23.330 19.559 -5.464 1.00 12.54 ? 76 SER A CA 1 ATOM 594 C C . SER A 1 76 ? 24.751 19.674 -4.967 1.00 12.32 ? 76 SER A C 1 ATOM 595 O O . SER A 1 76 ? 25.294 20.780 -4.839 1.00 13.78 ? 76 SER A O 1 ATOM 596 C CB . SER A 1 76 ? 23.281 19.944 -6.974 1.00 15.12 ? 76 SER A CB 1 ATOM 597 O OG . SER A 1 76 ? 24.334 19.310 -7.671 1.00 18.29 ? 76 SER A OG 1 ATOM 598 N N . ALA A 1 77 ? 25.449 18.532 -4.974 1.00 12.39 ? 77 ALA A N 1 ATOM 599 C CA . ALA A 1 77 ? 26.867 18.473 -4.678 1.00 14.47 ? 77 ALA A CA 1 ATOM 600 C C . ALA A 1 77 ? 27.711 19.183 -5.709 1.00 14.70 ? 77 ALA A C 1 ATOM 601 O O . ALA A 1 77 ? 28.890 19.495 -5.432 1.00 18.25 ? 77 ALA A O 1 ATOM 602 C CB . ALA A 1 77 ? 27.255 16.989 -4.727 1.00 17.35 ? 77 ALA A CB 1 ATOM 603 N N . THR A 1 78 ? 27.188 19.443 -6.898 1.00 13.44 ? 78 THR A N 1 ATOM 604 C CA . THR A 1 78 ? 27.977 20.103 -7.935 1.00 14.76 ? 78 THR A CA 1 ATOM 605 C C . THR A 1 78 ? 27.532 21.507 -8.245 1.00 15.31 ? 78 THR A C 1 ATOM 606 O O . THR A 1 78 ? 27.858 22.066 -9.298 1.00 15.93 ? 78 THR A O 1 ATOM 607 C CB . THR A 1 78 ? 28.054 19.247 -9.188 1.00 15.60 ? 78 THR A CB 1 ATOM 608 O OG1 . THR A 1 78 ? 26.740 19.052 -9.723 1.00 16.54 ? 78 THR A OG1 1 ATOM 609 C CG2 . THR A 1 78 ? 28.728 17.906 -8.857 1.00 15.44 ? 78 THR A CG2 1 ATOM 610 N N . GLY A 1 79 ? 26.797 22.128 -7.325 1.00 16.27 ? 79 GLY A N 1 ATOM 611 C CA . GLY A 1 79 ? 26.392 23.524 -7.482 1.00 15.83 ? 79 GLY A CA 1 ATOM 612 C C . GLY A 1 79 ? 24.864 23.573 -7.334 1.00 14.25 ? 79 GLY A C 1 ATOM 613 O O . GLY A 1 79 ? 24.128 23.014 -8.124 1.00 16.05 ? 79 GLY A O 1 ATOM 614 N N . SER A 1 80 ? 24.479 24.338 -6.328 1.00 13.21 ? 80 SER A N 1 ATOM 615 C CA . SER A 1 80 ? 23.057 24.517 -5.996 1.00 13.10 ? 80 SER A CA 1 ATOM 616 C C . SER A 1 80 ? 22.529 25.726 -6.731 1.00 13.19 ? 80 SER A C 1 ATOM 617 O O . SER A 1 80 ? 23.273 26.635 -7.112 1.00 14.91 ? 80 SER A O 1 ATOM 618 C CB . SER A 1 80 ? 22.952 24.592 -4.484 1.00 13.21 ? 80 SER A CB 1 ATOM 619 O OG . SER A 1 80 ? 23.312 23.354 -3.883 1.00 13.10 ? 80 SER A OG 1 ATOM 620 N N . THR A 1 81 ? 21.208 25.791 -6.874 1.00 13.33 ? 81 THR A N 1 ATOM 621 C CA . THR A 1 81 ? 20.539 26.878 -7.561 1.00 13.58 ? 81 THR A CA 1 ATOM 622 C C . THR A 1 81 ? 19.346 27.408 -6.719 1.00 12.31 ? 81 THR A C 1 ATOM 623 O O . THR A 1 81 ? 18.525 26.621 -6.217 1.00 14.57 ? 81 THR A O 1 ATOM 624 C CB . THR A 1 81 ? 19.972 26.362 -8.885 1.00 17.01 ? 81 THR A CB 1 ATOM 625 O OG1 . THR A 1 81 ? 20.983 25.849 -9.777 1.00 19.53 ? 81 THR A OG1 1 ATOM 626 C CG2 . THR A 1 81 ? 19.306 27.541 -9.618 1.00 18.15 ? 81 THR A CG2 1 ATOM 627 N N . ILE A 1 82 ? 19.300 28.706 -6.545 1.00 11.88 ? 82 ILE A N 1 ATOM 628 C CA . ILE A 1 82 ? 18.210 29.386 -5.835 1.00 11.18 ? 82 ILE A CA 1 ATOM 629 C C . ILE A 1 82 ? 17.329 29.966 -6.942 1.00 12.05 ? 82 ILE A C 1 ATOM 630 O O . ILE A 1 82 ? 17.796 30.718 -7.788 1.00 14.57 ? 82 ILE A O 1 ATOM 631 C CB . ILE A 1 82 ? 18.688 30.435 -4.796 1.00 12.48 ? 82 ILE A CB 1 ATOM 632 C CG1 . ILE A 1 82 ? 19.495 29.762 -3.691 1.00 12.52 ? 82 ILE A CG1 1 ATOM 633 C CG2 . ILE A 1 82 ? 17.482 31.189 -4.258 1.00 12.63 ? 82 ILE A CG2 1 ATOM 634 C CD1 . ILE A 1 82 ? 20.363 30.677 -2.845 1.00 14.37 ? 82 ILE A CD1 1 ATOM 635 N N . ASN A 1 83 ? 16.062 29.533 -6.989 1.00 11.24 ? 83 ASN A N 1 ATOM 636 C CA . ASN A 1 83 ? 15.131 29.915 -8.034 1.00 12.26 ? 83 ASN A CA 1 ATOM 637 C C . ASN A 1 83 ? 14.405 31.228 -7.752 1.00 13.91 ? 83 ASN A C 1 ATOM 638 O O . ASN A 1 83 ? 13.547 31.305 -6.863 1.00 13.75 ? 83 ASN A O 1 ATOM 639 C CB . ASN A 1 83 ? 14.074 28.809 -8.240 1.00 12.94 ? 83 ASN A CB 1 ATOM 640 C CG . ASN A 1 83 ? 13.190 29.017 -9.440 1.00 13.77 ? 83 ASN A CG 1 ATOM 641 O OD1 . ASN A 1 83 ? 13.432 29.939 -10.237 1.00 14.93 ? 83 ASN A OD1 1 ATOM 642 N ND2 . ASN A 1 83 ? 12.158 28.179 -9.509 1.00 14.11 ? 83 ASN A ND2 1 ATOM 643 N N . THR A 1 84 ? 14.775 32.297 -8.479 1.00 16.11 ? 84 THR A N 1 ATOM 644 C CA . THR A 1 84 ? 14.127 33.577 -8.333 1.00 16.69 ? 84 THR A CA 1 ATOM 645 C C . THR A 1 84 ? 13.181 33.874 -9.497 1.00 17.08 ? 84 THR A C 1 ATOM 646 O O . THR A 1 84 ? 12.719 35.016 -9.638 1.00 20.10 ? 84 THR A O 1 ATOM 647 C CB . THR A 1 84 ? 15.132 34.752 -8.225 1.00 18.02 ? 84 THR A CB 1 ATOM 648 O OG1 . THR A 1 84 ? 15.898 34.767 -9.422 1.00 20.30 ? 84 THR A OG1 1 ATOM 649 C CG2 . THR A 1 84 ? 16.022 34.600 -7.011 1.00 18.60 ? 84 THR A CG2 1 ATOM 650 N N . GLY A 1 85 ? 12.814 32.843 -10.239 1.00 16.94 ? 85 GLY A N 1 ATOM 651 C CA . GLY A 1 85 ? 11.888 33.000 -11.355 1.00 18.89 ? 85 GLY A CA 1 ATOM 652 C C . GLY A 1 85 ? 10.432 32.826 -10.918 1.00 18.51 ? 85 GLY A C 1 ATOM 653 O O . GLY A 1 85 ? 10.067 32.809 -9.742 1.00 17.65 ? 85 GLY A O 1 ATOM 654 N N . ALA A 1 86 ? 9.544 32.815 -11.924 1.00 20.43 ? 86 ALA A N 1 ATOM 655 C CA . ALA A 1 86 ? 8.110 32.792 -11.702 1.00 20.01 ? 86 ALA A CA 1 ATOM 656 C C . ALA A 1 86 ? 7.634 31.563 -10.955 1.00 20.08 ? 86 ALA A C 1 ATOM 657 O O . ALA A 1 86 ? 6.644 31.682 -10.221 1.00 23.10 ? 86 ALA A O 1 ATOM 658 C CB . ALA A 1 86 ? 7.371 32.897 -13.040 1.00 18.96 ? 86 ALA A CB 1 ATOM 659 N N . ASP A 1 87 ? 8.235 30.417 -11.149 1.00 18.19 ? 87 ASP A N 1 ATOM 660 C CA . ASP A 1 87 ? 7.963 29.161 -10.485 1.00 17.99 ? 87 ASP A CA 1 ATOM 661 C C . ASP A 1 87 ? 8.858 29.008 -9.237 1.00 17.35 ? 87 ASP A C 1 ATOM 662 O O . ASP A 1 87 ? 8.937 27.909 -8.671 1.00 18.21 ? 87 ASP A O 1 ATOM 663 C CB . ASP A 1 87 ? 8.200 27.962 -11.406 1.00 19.76 ? 87 ASP A CB 1 ATOM 664 C CG . ASP A 1 87 ? 9.549 27.930 -12.076 1.00 22.21 ? 87 ASP A CG 1 ATOM 665 O OD1 . ASP A 1 87 ? 10.431 28.783 -11.831 1.00 21.96 ? 87 ASP A OD1 1 ATOM 666 O OD2 . ASP A 1 87 ? 9.751 27.007 -12.906 1.00 27.16 ? 87 ASP A OD2 1 ATOM 667 N N . GLY A 1 88 ? 9.480 30.102 -8.806 1.00 15.56 ? 88 GLY A N 1 ATOM 668 C CA . GLY A 1 88 ? 10.313 30.099 -7.620 1.00 15.18 ? 88 GLY A CA 1 ATOM 669 C C . GLY A 1 88 ? 9.909 31.171 -6.619 1.00 14.69 ? 88 GLY A C 1 ATOM 670 O O . GLY A 1 88 ? 8.703 31.319 -6.315 1.00 14.04 ? 88 GLY A O 1 ATOM 671 N N . LEU A 1 89 ? 10.836 31.941 -6.090 1.00 13.92 ? 89 LEU A N 1 ATOM 672 C CA . LEU A 1 89 ? 10.624 32.934 -5.059 1.00 14.56 ? 89 LEU A CA 1 ATOM 673 C C . LEU A 1 89 ? 9.690 34.070 -5.435 1.00 15.44 ? 89 LEU A C 1 ATOM 674 O O . LEU A 1 89 ? 9.198 34.754 -4.527 1.00 16.60 ? 89 LEU A O 1 ATOM 675 C CB . LEU A 1 89 ? 11.941 33.470 -4.478 1.00 15.65 ? 89 LEU A CB 1 ATOM 676 C CG . LEU A 1 89 ? 12.707 32.473 -3.587 1.00 16.06 ? 89 LEU A CG 1 ATOM 677 C CD1 . LEU A 1 89 ? 14.117 32.999 -3.341 1.00 15.84 ? 89 LEU A CD1 1 ATOM 678 C CD2 . LEU A 1 89 ? 11.970 32.214 -2.295 1.00 16.23 ? 89 LEU A CD2 1 ATOM 679 N N . GLN A 1 90 ? 9.384 34.248 -6.737 1.00 15.41 ? 90 GLN A N 1 ATOM 680 C CA . GLN A 1 90 ? 8.349 35.193 -7.124 1.00 16.83 ? 90 GLN A CA 1 ATOM 681 C C . GLN A 1 90 ? 7.013 34.777 -6.526 1.00 16.03 ? 90 GLN A C 1 ATOM 682 O O . GLN A 1 90 ? 6.174 35.686 -6.312 1.00 17.15 ? 90 GLN A O 1 ATOM 683 C CB . GLN A 1 90 ? 8.308 35.338 -8.640 1.00 18.23 ? 90 GLN A CB 1 ATOM 684 C CG . GLN A 1 90 ? 9.490 36.119 -9.188 1.00 20.67 ? 90 GLN A CG 1 ATOM 685 C CD . GLN A 1 90 ? 9.387 36.213 -10.709 1.00 23.56 ? 90 GLN A CD 1 ATOM 686 O OE1 . GLN A 1 90 ? 8.298 36.218 -11.277 1.00 25.83 ? 90 GLN A OE1 1 ATOM 687 N NE2 . GLN A 1 90 ? 10.535 36.287 -11.377 1.00 25.10 ? 90 GLN A NE2 1 ATOM 688 N N . THR A 1 91 ? 6.757 33.508 -6.249 1.00 16.15 ? 91 THR A N 1 ATOM 689 C CA . THR A 1 91 ? 5.496 33.095 -5.611 1.00 16.60 ? 91 THR A CA 1 ATOM 690 C C . THR A 1 91 ? 5.448 33.639 -4.187 1.00 16.57 ? 91 THR A C 1 ATOM 691 O O . THR A 1 91 ? 4.474 34.207 -3.705 1.00 17.79 ? 91 THR A O 1 ATOM 692 C CB . THR A 1 91 ? 5.181 31.593 -5.641 1.00 19.24 ? 91 THR A CB 1 ATOM 693 O OG1 A THR A 1 91 ? 5.757 30.831 -4.571 0.50 20.18 ? 91 THR A OG1 1 ATOM 694 O OG1 B THR A 1 91 ? 3.956 31.343 -5.015 0.50 21.16 ? 91 THR A OG1 1 ATOM 695 C CG2 A THR A 1 91 ? 5.638 31.034 -7.009 0.50 16.36 ? 91 THR A CG2 1 ATOM 696 C CG2 B THR A 1 91 ? 6.234 30.775 -4.897 0.50 20.65 ? 91 THR A CG2 1 ATOM 697 N N . LEU A 1 92 ? 6.581 33.543 -3.458 1.00 14.79 ? 92 LEU A N 1 ATOM 698 C CA . LEU A 1 92 ? 6.646 34.117 -2.101 1.00 13.37 ? 92 LEU A CA 1 ATOM 699 C C . LEU A 1 92 ? 6.586 35.643 -2.134 1.00 12.61 ? 92 LEU A C 1 ATOM 700 O O . LEU A 1 92 ? 5.999 36.284 -1.229 1.00 11.75 ? 92 LEU A O 1 ATOM 701 C CB . LEU A 1 92 ? 7.923 33.620 -1.415 1.00 12.35 ? 92 LEU A CB 1 ATOM 702 C CG . LEU A 1 92 ? 8.075 33.989 0.063 1.00 11.57 ? 92 LEU A CG 1 ATOM 703 C CD1 . LEU A 1 92 ? 6.918 33.441 0.881 1.00 14.21 ? 92 LEU A CD1 1 ATOM 704 C CD2 . LEU A 1 92 ? 9.409 33.462 0.580 1.00 12.00 ? 92 LEU A CD2 1 ATOM 705 N N . ASP A 1 93 ? 7.107 36.287 -3.189 1.00 13.73 ? 93 ASP A N 1 ATOM 706 C CA . ASP A 1 93 ? 6.990 37.737 -3.291 1.00 13.25 ? 93 ASP A CA 1 ATOM 707 C C . ASP A 1 93 ? 5.530 38.198 -3.273 1.00 13.53 ? 93 ASP A C 1 ATOM 708 O O . ASP A 1 93 ? 5.185 39.188 -2.622 1.00 12.08 ? 93 ASP A O 1 ATOM 709 C CB . ASP A 1 93 ? 7.611 38.259 -4.594 1.00 14.11 ? 93 ASP A CB 1 ATOM 710 C CG . ASP A 1 93 ? 9.105 38.176 -4.743 1.00 15.71 ? 93 ASP A CG 1 ATOM 711 O OD1 . ASP A 1 93 ? 9.792 37.891 -3.750 1.00 15.16 ? 93 ASP A OD1 1 ATOM 712 O OD2 . ASP A 1 93 ? 9.618 38.449 -5.855 1.00 18.07 ? 93 ASP A OD2 1 ATOM 713 N N . TYR A 1 94 ? 4.667 37.474 -3.989 1.00 12.55 ? 94 TYR A N 1 ATOM 714 C CA . TYR A 1 94 ? 3.261 37.860 -4.019 1.00 12.04 ? 94 TYR A CA 1 ATOM 715 C C . TYR A 1 94 ? 2.591 37.663 -2.666 1.00 12.14 ? 94 TYR A C 1 ATOM 716 O O . TYR A 1 94 ? 1.738 38.444 -2.278 1.00 12.55 ? 94 TYR A O 1 ATOM 717 C CB . TYR A 1 94 ? 2.515 37.110 -5.126 1.00 11.94 ? 94 TYR A CB 1 ATOM 718 C CG . TYR A 1 94 ? 1.139 37.749 -5.311 1.00 12.96 ? 94 TYR A CG 1 ATOM 719 C CD1 . TYR A 1 94 ? 0.995 38.824 -6.166 1.00 15.63 ? 94 TYR A CD1 1 ATOM 720 C CD2 . TYR A 1 94 ? 0.034 37.254 -4.653 1.00 13.52 ? 94 TYR A CD2 1 ATOM 721 C CE1 . TYR A 1 94 ? -0.266 39.401 -6.320 1.00 18.17 ? 94 TYR A CE1 1 ATOM 722 C CE2 . TYR A 1 94 ? -1.196 37.859 -4.789 1.00 13.24 ? 94 TYR A CE2 1 ATOM 723 C CZ . TYR A 1 94 ? -1.355 38.899 -5.644 1.00 17.66 ? 94 TYR A CZ 1 ATOM 724 O OH . TYR A 1 94 ? -2.577 39.507 -5.844 1.00 20.32 ? 94 TYR A OH 1 ATOM 725 N N . VAL A 1 95 ? 3.009 36.635 -1.923 1.00 11.44 ? 95 VAL A N 1 ATOM 726 C CA . VAL A 1 95 ? 2.545 36.389 -0.573 1.00 10.69 ? 95 VAL A CA 1 ATOM 727 C C . VAL A 1 95 ? 2.861 37.557 0.336 1.00 9.72 ? 95 VAL A C 1 ATOM 728 O O . VAL A 1 95 ? 2.001 38.059 1.095 1.00 9.41 ? 95 VAL A O 1 ATOM 729 C CB . VAL A 1 95 ? 3.081 35.053 -0.036 1.00 10.66 ? 95 VAL A CB 1 ATOM 730 C CG1 . VAL A 1 95 ? 2.649 34.872 1.422 1.00 12.56 ? 95 VAL A CG1 1 ATOM 731 C CG2 . VAL A 1 95 ? 2.454 33.964 -0.894 1.00 14.62 ? 95 VAL A CG2 1 ATOM 732 N N . VAL A 1 96 ? 4.108 38.044 0.266 1.00 10.46 ? 96 VAL A N 1 ATOM 733 C CA . VAL A 1 96 ? 4.482 39.192 1.082 1.00 11.29 ? 96 VAL A CA 1 ATOM 734 C C . VAL A 1 96 ? 3.713 40.438 0.603 1.00 12.62 ? 96 VAL A C 1 ATOM 735 O O . VAL A 1 96 ? 3.207 41.181 1.447 1.00 13.70 ? 96 VAL A O 1 ATOM 736 C CB . VAL A 1 96 ? 6.000 39.424 1.025 1.00 11.29 ? 96 VAL A CB 1 ATOM 737 C CG1 . VAL A 1 96 ? 6.390 40.691 1.774 1.00 13.66 ? 96 VAL A CG1 1 ATOM 738 C CG2 . VAL A 1 96 ? 6.723 38.195 1.576 1.00 12.46 ? 96 VAL A CG2 1 ATOM 739 N N . GLN A 1 97 ? 3.530 40.667 -0.693 1.00 12.53 ? 97 GLN A N 1 ATOM 740 C CA . GLN A 1 97 ? 2.743 41.788 -1.244 1.00 14.33 ? 97 GLN A CA 1 ATOM 741 C C . GLN A 1 97 ? 1.310 41.728 -0.731 1.00 13.91 ? 97 GLN A C 1 ATOM 742 O O . GLN A 1 97 ? 0.741 42.733 -0.311 1.00 14.16 ? 97 GLN A O 1 ATOM 743 C CB . GLN A 1 97 ? 2.759 41.772 -2.785 1.00 16.69 ? 97 GLN A CB 1 ATOM 744 C CG A GLN A 1 97 ? 4.109 41.751 -3.360 0.50 18.87 ? 97 GLN A CG 1 ATOM 745 C CG B GLN A 1 97 ? 1.949 42.853 -3.505 0.50 14.86 ? 97 GLN A CG 1 ATOM 746 C CD A GLN A 1 97 ? 5.099 42.835 -3.470 0.50 18.25 ? 97 GLN A CD 1 ATOM 747 C CD B GLN A 1 97 ? 1.593 42.738 -4.982 0.50 14.10 ? 97 GLN A CD 1 ATOM 748 O OE1 A GLN A 1 97 ? 5.832 42.828 -4.487 0.50 18.07 ? 97 GLN A OE1 1 ATOM 749 O OE1 B GLN A 1 97 ? 0.597 43.277 -5.493 0.50 16.03 ? 97 GLN A OE1 1 ATOM 750 N NE2 A GLN A 1 97 ? 5.252 43.643 -2.436 0.50 16.46 ? 97 GLN A NE2 1 ATOM 751 N NE2 B GLN A 1 97 ? 2.223 41.988 -5.840 0.50 10.74 ? 97 GLN A NE2 1 ATOM 752 N N . SER A 1 98 ? 0.725 40.523 -0.725 1.00 11.99 ? 98 SER A N 1 ATOM 753 C CA . SER A 1 98 ? -0.654 40.360 -0.279 1.00 11.36 ? 98 SER A CA 1 ATOM 754 C C . SER A 1 98 ? -0.822 40.548 1.216 1.00 10.44 ? 98 SER A C 1 ATOM 755 O O . SER A 1 98 ? -1.804 41.073 1.728 1.00 11.46 ? 98 SER A O 1 ATOM 756 C CB . SER A 1 98 ? -1.177 39.007 -0.739 1.00 10.91 ? 98 SER A CB 1 ATOM 757 O OG . SER A 1 98 ? -2.561 38.873 -0.427 1.00 12.59 ? 98 SER A OG 1 ATOM 758 N N . ALA A 1 99 ? 0.200 40.129 1.981 1.00 10.54 ? 99 ALA A N 1 ATOM 759 C CA . ALA A 1 99 ? 0.206 40.402 3.412 1.00 11.44 ? 99 ALA A CA 1 ATOM 760 C C . ALA A 1 99 ? 0.255 41.931 3.628 1.00 12.78 ? 99 ALA A C 1 ATOM 761 O O . ALA A 1 99 ? -0.518 42.450 4.464 1.00 14.45 ? 99 ALA A O 1 ATOM 762 C CB . ALA A 1 99 ? 1.353 39.701 4.129 1.00 10.92 ? 99 ALA A CB 1 ATOM 763 N N . GLU A 1 100 ? 1.080 42.653 2.881 1.00 13.19 ? 100 GLU A N 1 ATOM 764 C CA . GLU A 1 100 ? 1.156 44.136 2.969 1.00 15.05 ? 100 GLU A CA 1 ATOM 765 C C . GLU A 1 100 ? -0.213 44.748 2.659 1.00 15.95 ? 100 GLU A C 1 ATOM 766 O O . GLU A 1 100 ? -0.728 45.617 3.379 1.00 18.62 ? 100 GLU A O 1 ATOM 767 C CB . GLU A 1 100 ? 2.198 44.664 1.983 1.00 17.93 ? 100 GLU A CB 1 ATOM 768 C CG . GLU A 1 100 ? 3.665 44.365 2.267 1.00 19.14 ? 100 GLU A CG 1 ATOM 769 C CD . GLU A 1 100 ? 4.677 44.759 1.228 1.00 22.03 ? 100 GLU A CD 1 ATOM 770 O OE1 . GLU A 1 100 ? 4.397 45.141 0.067 1.00 21.19 ? 100 GLU A OE1 1 ATOM 771 O OE2 . GLU A 1 100 ? 5.895 44.677 1.583 1.00 23.59 ? 100 GLU A OE2 1 ATOM 772 N N . GLN A 1 101 ? -0.911 44.212 1.671 1.00 12.88 ? 101 GLN A N 1 ATOM 773 C CA . GLN A 1 101 ? -2.212 44.747 1.284 1.00 13.73 ? 101 GLN A CA 1 ATOM 774 C C . GLN A 1 101 ? -3.264 44.489 2.350 1.00 14.39 ? 101 GLN A C 1 ATOM 775 O O . GLN A 1 101 ? -4.131 45.368 2.559 1.00 16.43 ? 101 GLN A O 1 ATOM 776 C CB . GLN A 1 101 ? -2.646 44.079 -0.003 1.00 14.18 ? 101 GLN A CB 1 ATOM 777 C CG . GLN A 1 101 ? -4.073 44.397 -0.455 1.00 15.82 ? 101 GLN A CG 1 ATOM 778 C CD . GLN A 1 101 ? -4.333 43.771 -1.818 1.00 17.82 ? 101 GLN A CD 1 ATOM 779 O OE1 . GLN A 1 101 ? -3.436 43.595 -2.665 1.00 20.93 ? 101 GLN A OE1 1 ATOM 780 N NE2 . GLN A 1 101 ? -5.582 43.426 -1.988 1.00 16.62 ? 101 GLN A NE2 1 ATOM 781 N N . HIS A 1 102 ? -3.266 43.281 2.919 1.00 14.68 ? 102 HIS A N 1 ATOM 782 C CA . HIS A 1 102 ? -4.275 42.829 3.869 1.00 14.95 ? 102 HIS A CA 1 ATOM 783 C C . HIS A 1 102 ? -4.004 43.136 5.329 1.00 16.79 ? 102 HIS A C 1 ATOM 784 O O . HIS A 1 102 ? -4.665 42.633 6.231 1.00 17.89 ? 102 HIS A O 1 ATOM 785 C CB . HIS A 1 102 ? -4.638 41.353 3.645 1.00 15.56 ? 102 HIS A CB 1 ATOM 786 C CG . HIS A 1 102 ? -5.285 41.081 2.325 1.00 11.82 ? 102 HIS A CG 1 ATOM 787 N ND1 . HIS A 1 102 ? -4.591 40.676 1.218 1.00 14.92 ? 102 HIS A ND1 1 ATOM 788 C CD2 . HIS A 1 102 ? -6.615 41.173 1.960 1.00 12.60 ? 102 HIS A CD2 1 ATOM 789 C CE1 . HIS A 1 102 ? -5.404 40.528 0.182 1.00 14.64 ? 102 HIS A CE1 1 ATOM 790 N NE2 . HIS A 1 102 ? -6.612 40.819 0.635 1.00 14.78 ? 102 HIS A NE2 1 ATOM 791 N N . ASN A 1 103 ? -2.944 43.881 5.574 1.00 17.47 ? 103 ASN A N 1 ATOM 792 C CA . ASN A 1 103 ? -2.570 44.278 6.923 1.00 20.00 ? 103 ASN A CA 1 ATOM 793 C C . ASN A 1 103 ? -2.286 43.064 7.807 1.00 16.83 ? 103 ASN A C 1 ATOM 794 O O . ASN A 1 103 ? -2.655 42.997 8.982 1.00 18.11 ? 103 ASN A O 1 ATOM 795 C CB . ASN A 1 103 ? -3.678 45.146 7.562 1.00 23.23 ? 103 ASN A CB 1 ATOM 796 C CG . ASN A 1 103 ? -4.010 46.366 6.707 1.00 27.91 ? 103 ASN A CG 1 ATOM 797 O OD1 . ASN A 1 103 ? -5.207 46.625 6.531 1.00 33.70 ? 103 ASN A OD1 1 ATOM 798 N ND2 . ASN A 1 103 ? -2.986 47.061 6.247 1.00 28.36 ? 103 ASN A ND2 1 ATOM 799 N N . LEU A 1 104 ? -1.540 42.134 7.220 1.00 12.25 ? 104 LEU A N 1 ATOM 800 C CA . LEU A 1 104 ? -1.111 40.916 7.915 1.00 11.40 ? 104 LEU A CA 1 ATOM 801 C C . LEU A 1 104 ? 0.409 40.895 8.061 1.00 9.62 ? 104 LEU A C 1 ATOM 802 O O . LEU A 1 104 ? 1.092 41.536 7.240 1.00 11.72 ? 104 LEU A O 1 ATOM 803 C CB . LEU A 1 104 ? -1.522 39.623 7.170 1.00 10.86 ? 104 LEU A CB 1 ATOM 804 C CG . LEU A 1 104 ? -3.048 39.444 7.062 1.00 9.80 ? 104 LEU A CG 1 ATOM 805 C CD1 . LEU A 1 104 ? -3.325 38.279 6.127 1.00 11.94 ? 104 LEU A CD1 1 ATOM 806 C CD2 . LEU A 1 104 ? -3.629 39.201 8.442 1.00 10.77 ? 104 LEU A CD2 1 ATOM 807 N N . LYS A 1 105 ? 0.881 40.222 9.096 1.00 8.32 ? 105 LYS A N 1 ATOM 808 C CA . LYS A 1 105 ? 2.343 40.062 9.302 1.00 8.76 ? 105 LYS A CA 1 ATOM 809 C C . LYS A 1 105 ? 2.658 38.567 9.126 1.00 9.07 ? 105 LYS A C 1 ATOM 810 O O . LYS A 1 105 ? 1.825 37.703 9.430 1.00 11.89 ? 105 LYS A O 1 ATOM 811 C CB . LYS A 1 105 ? 2.752 40.485 10.718 1.00 9.16 ? 105 LYS A CB 1 ATOM 812 C CG . LYS A 1 105 ? 2.257 41.889 11.107 1.00 8.63 ? 105 LYS A CG 1 ATOM 813 C CD . LYS A 1 105 ? 2.852 42.975 10.194 1.00 9.07 ? 105 LYS A CD 1 ATOM 814 C CE . LYS A 1 105 ? 2.485 44.363 10.664 1.00 11.80 ? 105 LYS A CE 1 ATOM 815 N NZ . LYS A 1 105 ? 2.793 45.403 9.631 1.00 15.25 ? 105 LYS A NZ 1 ATOM 816 N N . LEU A 1 106 ? 3.868 38.240 8.693 1.00 7.96 ? 106 LEU A N 1 ATOM 817 C CA . LEU A 1 106 ? 4.278 36.875 8.394 1.00 7.97 ? 106 LEU A CA 1 ATOM 818 C C . LEU A 1 106 ? 5.450 36.391 9.242 1.00 7.58 ? 106 LEU A C 1 ATOM 819 O O . LEU A 1 106 ? 6.460 37.082 9.388 1.00 7.73 ? 106 LEU A O 1 ATOM 820 C CB . LEU A 1 106 ? 4.739 36.778 6.925 1.00 8.90 ? 106 LEU A CB 1 ATOM 821 C CG . LEU A 1 106 ? 3.681 37.162 5.881 1.00 8.54 ? 106 LEU A CG 1 ATOM 822 C CD1 . LEU A 1 106 ? 4.289 37.204 4.484 1.00 13.23 ? 106 LEU A CD1 1 ATOM 823 C CD2 . LEU A 1 106 ? 2.485 36.236 5.938 1.00 10.78 ? 106 LEU A CD2 1 ATOM 824 N N . ILE A 1 107 ? 5.349 35.154 9.710 1.00 6.72 ? 107 ILE A N 1 ATOM 825 C CA . ILE A 1 107 ? 6.499 34.422 10.303 1.00 7.35 ? 107 ILE A CA 1 ATOM 826 C C . ILE A 1 107 ? 6.981 33.471 9.221 1.00 8.46 ? 107 ILE A C 1 ATOM 827 O O . ILE A 1 107 ? 6.218 32.668 8.679 1.00 8.01 ? 107 ILE A O 1 ATOM 828 C CB . ILE A 1 107 ? 6.157 33.702 11.606 1.00 7.30 ? 107 ILE A CB 1 ATOM 829 C CG1 . ILE A 1 107 ? 5.802 34.685 12.704 1.00 7.83 ? 107 ILE A CG1 1 ATOM 830 C CG2 . ILE A 1 107 ? 7.319 32.820 12.049 1.00 9.46 ? 107 ILE A CG2 1 ATOM 831 C CD1 . ILE A 1 107 ? 5.265 34.068 13.987 1.00 9.88 ? 107 ILE A CD1 1 ATOM 832 N N . ILE A 1 108 ? 8.285 33.559 8.878 1.00 7.97 ? 108 ILE A N 1 ATOM 833 C CA . ILE A 1 108 ? 8.848 32.779 7.761 1.00 7.66 ? 108 ILE A CA 1 ATOM 834 C C . ILE A 1 108 ? 10.064 31.968 8.164 1.00 8.00 ? 108 ILE A C 1 ATOM 835 O O . ILE A 1 108 ? 11.166 32.564 8.324 1.00 8.57 ? 108 ILE A O 1 ATOM 836 C CB . ILE A 1 108 ? 9.203 33.748 6.585 1.00 7.50 ? 108 ILE A CB 1 ATOM 837 C CG1 . ILE A 1 108 ? 7.981 34.590 6.138 1.00 9.07 ? 108 ILE A CG1 1 ATOM 838 C CG2 . ILE A 1 108 ? 9.732 32.936 5.404 1.00 9.22 ? 108 ILE A CG2 1 ATOM 839 C CD1 . ILE A 1 108 ? 8.209 35.496 4.966 1.00 11.18 ? 108 ILE A CD1 1 ATOM 840 N N . PRO A 1 109 ? 9.963 30.647 8.346 1.00 8.07 ? 109 PRO A N 1 ATOM 841 C CA . PRO A 1 109 ? 11.113 29.780 8.558 1.00 7.45 ? 109 PRO A CA 1 ATOM 842 C C . PRO A 1 109 ? 11.844 29.477 7.257 1.00 8.31 ? 109 PRO A C 1 ATOM 843 O O . PRO A 1 109 ? 11.280 29.295 6.175 1.00 8.63 ? 109 PRO A O 1 ATOM 844 C CB . PRO A 1 109 ? 10.480 28.503 9.159 1.00 6.99 ? 109 PRO A CB 1 ATOM 845 C CG . PRO A 1 109 ? 9.114 28.447 8.547 1.00 9.89 ? 109 PRO A CG 1 ATOM 846 C CD . PRO A 1 109 ? 8.699 29.897 8.456 1.00 8.63 ? 109 PRO A CD 1 ATOM 847 N N . PHE A 1 110 ? 13.185 29.254 7.361 1.00 8.01 ? 110 PHE A N 1 ATOM 848 C CA . PHE A 1 110 ? 14.047 29.060 6.208 1.00 7.74 ? 110 PHE A CA 1 ATOM 849 C C . PHE A 1 110 ? 14.328 27.645 5.769 1.00 7.45 ? 110 PHE A C 1 ATOM 850 O O . PHE A 1 110 ? 14.808 27.467 4.650 1.00 8.79 ? 110 PHE A O 1 ATOM 851 C CB . PHE A 1 110 ? 15.430 29.729 6.474 1.00 8.09 ? 110 PHE A CB 1 ATOM 852 C CG . PHE A 1 110 ? 15.391 31.210 6.790 1.00 7.74 ? 110 PHE A CG 1 ATOM 853 C CD1 . PHE A 1 110 ? 14.895 32.115 5.838 1.00 10.12 ? 110 PHE A CD1 1 ATOM 854 C CD2 . PHE A 1 110 ? 15.863 31.685 8.007 1.00 8.76 ? 110 PHE A CD2 1 ATOM 855 C CE1 . PHE A 1 110 ? 14.860 33.483 6.149 1.00 9.15 ? 110 PHE A CE1 1 ATOM 856 C CE2 . PHE A 1 110 ? 15.823 33.051 8.290 1.00 8.07 ? 110 PHE A CE2 1 ATOM 857 C CZ . PHE A 1 110 ? 15.311 33.952 7.350 1.00 8.92 ? 110 PHE A CZ 1 ATOM 858 N N . VAL A 1 111 ? 14.073 26.668 6.656 1.00 8.06 ? 111 VAL A N 1 ATOM 859 C CA . VAL A 1 111 ? 14.341 25.266 6.342 1.00 7.28 ? 111 VAL A CA 1 ATOM 860 C C . VAL A 1 111 ? 13.395 24.415 7.209 1.00 7.02 ? 111 VAL A C 1 ATOM 861 O O . VAL A 1 111 ? 12.979 24.867 8.302 1.00 7.87 ? 111 VAL A O 1 ATOM 862 C CB . VAL A 1 111 ? 15.816 24.868 6.618 1.00 7.90 ? 111 VAL A CB 1 ATOM 863 C CG1 . VAL A 1 111 ? 16.207 24.937 8.100 1.00 7.26 ? 111 VAL A CG1 1 ATOM 864 C CG2 . VAL A 1 111 ? 16.122 23.480 6.076 1.00 8.24 ? 111 VAL A CG2 1 ATOM 865 N N . ASN A 1 112 ? 13.033 23.221 6.750 1.00 7.26 ? 112 ASN A N 1 ATOM 866 C CA . ASN A 1 112 ? 12.241 22.294 7.542 1.00 6.98 ? 112 ASN A CA 1 ATOM 867 C C . ASN A 1 112 ? 13.176 21.309 8.255 1.00 7.97 ? 112 ASN A C 1 ATOM 868 O O . ASN A 1 112 ? 14.071 20.680 7.637 1.00 7.91 ? 112 ASN A O 1 ATOM 869 C CB . ASN A 1 112 ? 11.280 21.509 6.641 1.00 7.04 ? 112 ASN A CB 1 ATOM 870 C CG . ASN A 1 112 ? 10.059 20.972 7.382 1.00 6.57 ? 112 ASN A CG 1 ATOM 871 O OD1 . ASN A 1 112 ? 9.978 21.084 8.602 1.00 7.61 ? 112 ASN A OD1 1 ATOM 872 N ND2 . ASN A 1 112 ? 9.137 20.456 6.609 1.00 8.26 ? 112 ASN A ND2 1 ATOM 873 N N . ASN A 1 113 ? 12.873 20.984 9.525 1.00 7.07 ? 113 ASN A N 1 ATOM 874 C CA . ASN A 1 113 ? 13.553 19.854 10.159 1.00 7.15 ? 113 ASN A CA 1 ATOM 875 C C . ASN A 1 113 ? 13.153 18.563 9.448 1.00 7.69 ? 113 ASN A C 1 ATOM 876 O O . ASN A 1 113 ? 13.930 17.631 9.256 1.00 9.81 ? 113 ASN A O 1 ATOM 877 C CB . ASN A 1 113 ? 13.159 19.745 11.630 1.00 8.24 ? 113 ASN A CB 1 ATOM 878 C CG . ASN A 1 113 ? 13.919 18.663 12.360 1.00 8.90 ? 113 ASN A CG 1 ATOM 879 O OD1 . ASN A 1 113 ? 15.124 18.848 12.597 1.00 9.52 ? 113 ASN A OD1 1 ATOM 880 N ND2 . ASN A 1 113 ? 13.260 17.584 12.776 1.00 9.25 ? 113 ASN A ND2 1 ATOM 881 N N . TRP A 1 114 ? 11.876 18.451 9.070 1.00 7.53 ? 114 TRP A N 1 ATOM 882 C CA . TRP A 1 114 ? 11.268 17.299 8.444 1.00 7.58 ? 114 TRP A CA 1 ATOM 883 C C . TRP A 1 114 ? 11.451 17.264 6.942 1.00 7.97 ? 114 TRP A C 1 ATOM 884 O O . TRP A 1 114 ? 11.800 18.290 6.334 1.00 8.33 ? 114 TRP A O 1 ATOM 885 C CB . TRP A 1 114 ? 9.747 17.227 8.789 1.00 7.84 ? 114 TRP A CB 1 ATOM 886 C CG . TRP A 1 114 ? 9.520 17.442 10.246 1.00 7.18 ? 114 TRP A CG 1 ATOM 887 C CD1 . TRP A 1 114 ? 8.857 18.508 10.799 1.00 7.89 ? 114 TRP A CD1 1 ATOM 888 C CD2 . TRP A 1 114 ? 9.929 16.636 11.360 1.00 8.50 ? 114 TRP A CD2 1 ATOM 889 N NE1 . TRP A 1 114 ? 8.816 18.431 12.168 1.00 8.78 ? 114 TRP A NE1 1 ATOM 890 C CE2 . TRP A 1 114 ? 9.515 17.293 12.535 1.00 8.57 ? 114 TRP A CE2 1 ATOM 891 C CE3 . TRP A 1 114 ? 10.669 15.459 11.473 1.00 9.67 ? 114 TRP A CE3 1 ATOM 892 C CZ2 . TRP A 1 114 ? 9.757 16.773 13.779 1.00 9.58 ? 114 TRP A CZ2 1 ATOM 893 C CZ3 . TRP A 1 114 ? 10.886 14.931 12.736 1.00 10.58 ? 114 TRP A CZ3 1 ATOM 894 C CH2 . TRP A 1 114 ? 10.449 15.597 13.884 1.00 10.49 ? 114 TRP A CH2 1 ATOM 895 N N . SER A 1 115 ? 11.235 16.091 6.302 1.00 8.61 ? 115 SER A N 1 ATOM 896 C CA . SER A 1 115 ? 11.529 15.961 4.880 1.00 9.71 ? 115 SER A CA 1 ATOM 897 C C . SER A 1 115 ? 10.459 16.495 3.940 1.00 10.46 ? 115 SER A C 1 ATOM 898 O O . SER A 1 115 ? 10.696 16.527 2.732 1.00 12.11 ? 115 SER A O 1 ATOM 899 C CB . SER A 1 115 ? 11.868 14.516 4.558 1.00 11.01 ? 115 SER A CB 1 ATOM 900 O OG A SER A 1 115 ? 12.910 14.047 5.395 0.50 14.22 ? 115 SER A OG 1 ATOM 901 O OG B SER A 1 115 ? 10.815 13.649 4.865 0.50 10.58 ? 115 SER A OG 1 ATOM 902 N N . ASP A 1 116 ? 9.373 17.048 4.501 1.00 9.44 ? 116 ASP A N 1 ATOM 903 C CA . ASP A 1 116 ? 8.366 17.681 3.665 1.00 9.56 ? 116 ASP A CA 1 ATOM 904 C C . ASP A 1 116 ? 8.931 18.942 3.044 1.00 8.33 ? 116 ASP A C 1 ATOM 905 O O . ASP A 1 116 ? 9.435 19.833 3.758 1.00 9.60 ? 116 ASP A O 1 ATOM 906 C CB . ASP A 1 116 ? 7.121 17.980 4.514 1.00 8.92 ? 116 ASP A CB 1 ATOM 907 C CG . ASP A 1 116 ? 6.715 16.759 5.336 1.00 11.27 ? 116 ASP A CG 1 ATOM 908 O OD1 . ASP A 1 116 ? 6.277 15.739 4.787 1.00 15.16 ? 116 ASP A OD1 1 ATOM 909 O OD2 . ASP A 1 116 ? 6.844 16.786 6.591 1.00 11.27 ? 116 ASP A OD2 1 ATOM 910 N N . TYR A 1 117 ? 8.779 19.055 1.713 1.00 7.82 ? 117 TYR A N 1 ATOM 911 C CA . TYR A 1 117 ? 9.367 20.193 0.976 1.00 7.76 ? 117 TYR A CA 1 ATOM 912 C C . TYR A 1 117 ? 10.878 20.274 1.181 1.00 8.79 ? 117 TYR A C 1 ATOM 913 O O . TYR A 1 117 ? 11.515 21.302 1.176 1.00 10.17 ? 117 TYR A O 1 ATOM 914 C CB . TYR A 1 117 ? 8.630 21.514 1.286 1.00 8.53 ? 117 TYR A CB 1 ATOM 915 C CG . TYR A 1 117 ? 7.130 21.332 1.052 1.00 9.62 ? 117 TYR A CG 1 ATOM 916 C CD1 . TYR A 1 117 ? 6.629 21.363 -0.242 1.00 10.10 ? 117 TYR A CD1 1 ATOM 917 C CD2 . TYR A 1 117 ? 6.258 21.124 2.103 1.00 9.77 ? 117 TYR A CD2 1 ATOM 918 C CE1 . TYR A 1 117 ? 5.280 21.149 -0.493 1.00 11.63 ? 117 TYR A CE1 1 ATOM 919 C CE2 . TYR A 1 117 ? 4.890 20.878 1.851 1.00 11.52 ? 117 TYR A CE2 1 ATOM 920 C CZ . TYR A 1 117 ? 4.456 20.894 0.562 1.00 12.19 ? 117 TYR A CZ 1 ATOM 921 O OH . TYR A 1 117 ? 3.084 20.689 0.334 1.00 14.84 ? 117 TYR A OH 1 ATOM 922 N N . GLY A 1 118 ? 11.468 19.060 1.205 1.00 9.49 ? 118 GLY A N 1 ATOM 923 C CA . GLY A 1 118 ? 12.896 18.838 1.198 1.00 9.07 ? 118 GLY A CA 1 ATOM 924 C C . GLY A 1 118 ? 13.552 18.660 2.533 1.00 9.91 ? 118 GLY A C 1 ATOM 925 O O . GLY A 1 118 ? 14.000 17.578 2.930 1.00 9.75 ? 118 GLY A O 1 ATOM 926 N N . GLY A 1 119 ? 13.613 19.782 3.261 1.00 9.57 ? 119 GLY A N 1 ATOM 927 C CA . GLY A 1 119 ? 14.127 19.787 4.596 1.00 8.55 ? 119 GLY A CA 1 ATOM 928 C C . GLY A 1 119 ? 15.622 19.489 4.703 1.00 8.98 ? 119 GLY A C 1 ATOM 929 O O . GLY A 1 119 ? 16.348 19.415 3.721 1.00 10.41 ? 119 GLY A O 1 ATOM 930 N N . ILE A 1 120 ? 16.006 19.254 5.961 1.00 8.91 ? 120 ILE A N 1 ATOM 931 C CA . ILE A 1 120 ? 17.375 18.865 6.255 1.00 8.21 ? 120 ILE A CA 1 ATOM 932 C C . ILE A 1 120 ? 17.727 17.660 5.385 1.00 8.53 ? 120 ILE A C 1 ATOM 933 O O . ILE A 1 120 ? 18.881 17.606 4.924 1.00 9.75 ? 120 ILE A O 1 ATOM 934 C CB . ILE A 1 120 ? 17.539 18.586 7.762 1.00 8.31 ? 120 ILE A CB 1 ATOM 935 C CG1 . ILE A 1 120 ? 17.564 19.898 8.568 1.00 8.93 ? 120 ILE A CG1 1 ATOM 936 C CG2 . ILE A 1 120 ? 18.745 17.692 8.032 1.00 9.77 ? 120 ILE A CG2 1 ATOM 937 C CD1 . ILE A 1 120 ? 17.648 19.806 10.063 1.00 9.18 ? 120 ILE A CD1 1 ATOM 938 N N . ASN A 1 121 ? 16.799 16.718 5.157 1.00 9.00 ? 121 ASN A N 1 ATOM 939 C CA . ASN A 1 121 ? 17.132 15.548 4.336 1.00 9.51 ? 121 ASN A CA 1 ATOM 940 C C . ASN A 1 121 ? 17.566 15.938 2.927 1.00 10.31 ? 121 ASN A C 1 ATOM 941 O O . ASN A 1 121 ? 18.437 15.247 2.353 1.00 10.67 ? 121 ASN A O 1 ATOM 942 C CB . ASN A 1 121 ? 15.941 14.603 4.305 1.00 10.74 ? 121 ASN A CB 1 ATOM 943 C CG . ASN A 1 121 ? 16.190 13.343 3.494 1.00 11.81 ? 121 ASN A CG 1 ATOM 944 O OD1 . ASN A 1 121 ? 15.596 13.111 2.425 1.00 16.97 ? 121 ASN A OD1 1 ATOM 945 N ND2 . ASN A 1 121 ? 17.026 12.521 4.110 1.00 12.69 ? 121 ASN A ND2 1 ATOM 946 N N . ALA A 1 122 ? 17.021 17.001 2.331 1.00 10.80 ? 122 ALA A N 1 ATOM 947 C CA . ALA A 1 122 ? 17.444 17.416 0.980 1.00 10.19 ? 122 ALA A CA 1 ATOM 948 C C . ALA A 1 122 ? 18.893 17.907 1.003 1.00 11.16 ? 122 ALA A C 1 ATOM 949 O O . ALA A 1 122 ? 19.648 17.671 0.053 1.00 11.77 ? 122 ALA A O 1 ATOM 950 C CB . ALA A 1 122 ? 16.488 18.447 0.398 1.00 11.55 ? 122 ALA A CB 1 ATOM 951 N N . TYR A 1 123 ? 19.296 18.571 2.087 1.00 10.57 ? 123 TYR A N 1 ATOM 952 C CA . TYR A 1 123 ? 20.704 18.972 2.254 1.00 10.27 ? 123 TYR A CA 1 ATOM 953 C C . TYR A 1 123 ? 21.558 17.740 2.460 1.00 12.15 ? 123 TYR A C 1 ATOM 954 O O . TYR A 1 123 ? 22.678 17.695 1.920 1.00 12.51 ? 123 TYR A O 1 ATOM 955 C CB . TYR A 1 123 ? 20.838 19.928 3.440 1.00 10.24 ? 123 TYR A CB 1 ATOM 956 C CG . TYR A 1 123 ? 20.322 21.337 3.261 1.00 9.62 ? 123 TYR A CG 1 ATOM 957 C CD1 . TYR A 1 123 ? 18.971 21.641 3.413 1.00 11.52 ? 123 TYR A CD1 1 ATOM 958 C CD2 . TYR A 1 123 ? 21.191 22.383 2.940 1.00 9.76 ? 123 TYR A CD2 1 ATOM 959 C CE1 . TYR A 1 123 ? 18.514 22.940 3.267 1.00 10.70 ? 123 TYR A CE1 1 ATOM 960 C CE2 . TYR A 1 123 ? 20.748 23.693 2.785 1.00 10.76 ? 123 TYR A CE2 1 ATOM 961 C CZ . TYR A 1 123 ? 19.403 23.956 2.956 1.00 10.14 ? 123 TYR A CZ 1 ATOM 962 O OH . TYR A 1 123 ? 19.007 25.268 2.820 1.00 9.64 ? 123 TYR A OH 1 ATOM 963 N N . VAL A 1 124 ? 21.117 16.756 3.245 1.00 11.15 ? 124 VAL A N 1 ATOM 964 C CA . VAL A 1 124 ? 21.909 15.539 3.459 1.00 12.41 ? 124 VAL A CA 1 ATOM 965 C C . VAL A 1 124 ? 22.107 14.805 2.144 1.00 12.50 ? 124 VAL A C 1 ATOM 966 O O . VAL A 1 124 ? 23.199 14.292 1.832 1.00 12.79 ? 124 VAL A O 1 ATOM 967 C CB . VAL A 1 124 ? 21.173 14.617 4.470 1.00 12.62 ? 124 VAL A CB 1 ATOM 968 C CG1 . VAL A 1 124 ? 21.801 13.227 4.495 1.00 13.82 ? 124 VAL A CG1 1 ATOM 969 C CG2 . VAL A 1 124 ? 21.185 15.247 5.858 1.00 13.34 ? 124 VAL A CG2 1 ATOM 970 N N . ASN A 1 125 ? 21.121 14.764 1.238 1.00 12.33 ? 125 ASN A N 1 ATOM 971 C CA . ASN A 1 125 ? 21.247 14.083 -0.036 1.00 12.62 ? 125 ASN A CA 1 ATOM 972 C C . ASN A 1 125 ? 22.371 14.724 -0.879 1.00 13.51 ? 125 ASN A C 1 ATOM 973 O O . ASN A 1 125 ? 23.092 13.978 -1.546 1.00 16.03 ? 125 ASN A O 1 ATOM 974 C CB . ASN A 1 125 ? 19.950 14.138 -0.844 1.00 13.43 ? 125 ASN A CB 1 ATOM 975 C CG . ASN A 1 125 ? 18.854 13.216 -0.366 1.00 13.98 ? 125 ASN A CG 1 ATOM 976 O OD1 . ASN A 1 125 ? 19.166 12.213 0.364 1.00 18.00 ? 125 ASN A OD1 1 ATOM 977 N ND2 . ASN A 1 125 ? 17.657 13.487 -0.765 1.00 12.70 ? 125 ASN A ND2 1 ATOM 978 N N . ALA A 1 126 ? 22.472 16.049 -0.808 1.00 13.01 ? 126 ALA A N 1 ATOM 979 C CA . ALA A 1 126 ? 23.467 16.767 -1.573 1.00 13.89 ? 126 ALA A CA 1 ATOM 980 C C . ALA A 1 126 ? 24.840 16.808 -0.924 1.00 14.28 ? 126 ALA A C 1 ATOM 981 O O . ALA A 1 126 ? 25.859 16.750 -1.634 1.00 17.53 ? 126 ALA A O 1 ATOM 982 C CB . ALA A 1 126 ? 22.995 18.218 -1.787 1.00 12.91 ? 126 ALA A CB 1 ATOM 983 N N . PHE A 1 127 ? 24.919 16.992 0.379 1.00 13.43 ? 127 PHE A N 1 ATOM 984 C CA . PHE A 1 127 ? 26.133 17.309 1.110 1.00 13.34 ? 127 PHE A CA 1 ATOM 985 C C . PHE A 1 127 ? 26.647 16.261 2.054 1.00 14.12 ? 127 PHE A C 1 ATOM 986 O O . PHE A 1 127 ? 27.662 16.476 2.757 1.00 16.39 ? 127 PHE A O 1 ATOM 987 C CB . PHE A 1 127 ? 25.910 18.678 1.798 1.00 13.09 ? 127 PHE A CB 1 ATOM 988 C CG . PHE A 1 127 ? 25.529 19.779 0.847 1.00 13.99 ? 127 PHE A CG 1 ATOM 989 C CD1 . PHE A 1 127 ? 26.285 20.154 -0.235 1.00 15.63 ? 127 PHE A CD1 1 ATOM 990 C CD2 . PHE A 1 127 ? 24.332 20.458 1.063 1.00 13.84 ? 127 PHE A CD2 1 ATOM 991 C CE1 . PHE A 1 127 ? 25.870 21.145 -1.095 1.00 16.59 ? 127 PHE A CE1 1 ATOM 992 C CE2 . PHE A 1 127 ? 23.895 21.446 0.219 1.00 13.98 ? 127 PHE A CE2 1 ATOM 993 C CZ . PHE A 1 127 ? 24.669 21.807 -0.869 1.00 15.83 ? 127 PHE A CZ 1 ATOM 994 N N . GLY A 1 128 ? 25.965 15.117 2.109 1.00 14.12 ? 128 GLY A N 1 ATOM 995 C CA . GLY A 1 128 ? 26.395 14.012 2.947 1.00 15.01 ? 128 GLY A CA 1 ATOM 996 C C . GLY A 1 128 ? 26.111 14.199 4.416 1.00 14.93 ? 128 GLY A C 1 ATOM 997 O O . GLY A 1 128 ? 25.274 15.022 4.827 1.00 15.10 ? 128 GLY A O 1 ATOM 998 N N . GLY A 1 129 ? 26.739 13.376 5.260 1.00 17.05 ? 129 GLY A N 1 ATOM 999 C CA . GLY A 1 129 ? 26.461 13.390 6.685 1.00 16.47 ? 129 GLY A CA 1 ATOM 1000 C C . GLY A 1 129 ? 25.077 12.761 6.932 1.00 16.05 ? 129 GLY A C 1 ATOM 1001 O O . GLY A 1 129 ? 24.532 11.938 6.210 1.00 16.46 ? 129 GLY A O 1 ATOM 1002 N N . ASN A 1 130 ? 24.464 13.261 8.012 1.00 15.06 ? 130 ASN A N 1 ATOM 1003 C CA . ASN A 1 130 ? 23.114 12.814 8.371 1.00 13.66 ? 130 ASN A CA 1 ATOM 1004 C C . ASN A 1 130 ? 22.346 13.969 9.006 1.00 11.83 ? 130 ASN A C 1 ATOM 1005 O O . ASN A 1 130 ? 22.830 15.099 9.074 1.00 12.54 ? 130 ASN A O 1 ATOM 1006 C CB . ASN A 1 130 ? 23.149 11.486 9.142 1.00 14.67 ? 130 ASN A CB 1 ATOM 1007 C CG . ASN A 1 130 ? 23.772 11.763 10.467 1.00 15.56 ? 130 ASN A CG 1 ATOM 1008 O OD1 . ASN A 1 130 ? 23.845 12.805 11.106 1.00 14.33 ? 130 ASN A OD1 1 ATOM 1009 N ND2 . ASN A 1 130 ? 24.355 10.653 11.066 1.00 18.47 ? 130 ASN A ND2 1 ATOM 1010 N N . ALA A 1 131 ? 21.113 13.692 9.478 1.00 11.49 ? 131 ALA A N 1 ATOM 1011 C CA . ALA A 1 131 ? 20.295 14.765 10.007 1.00 11.78 ? 131 ALA A CA 1 ATOM 1012 C C . ALA A 1 131 ? 20.787 15.460 11.248 1.00 10.32 ? 131 ALA A C 1 ATOM 1013 O O . ALA A 1 131 ? 20.307 16.582 11.537 1.00 12.65 ? 131 ALA A O 1 ATOM 1014 C CB . ALA A 1 131 ? 18.873 14.176 10.227 1.00 13.40 ? 131 ALA A CB 1 ATOM 1015 N N . THR A 1 132 ? 21.705 14.855 11.997 1.00 12.01 ? 132 THR A N 1 ATOM 1016 C CA . THR A 1 132 ? 22.243 15.486 13.208 1.00 12.25 ? 132 THR A CA 1 ATOM 1017 C C . THR A 1 132 ? 23.582 16.157 12.928 1.00 12.04 ? 132 THR A C 1 ATOM 1018 O O . THR A 1 132 ? 23.871 17.215 13.506 1.00 14.75 ? 132 THR A O 1 ATOM 1019 C CB . THR A 1 132 ? 22.306 14.549 14.411 1.00 12.64 ? 132 THR A CB 1 ATOM 1020 O OG1 . THR A 1 132 ? 23.136 13.412 14.057 1.00 15.21 ? 132 THR A OG1 1 ATOM 1021 C CG2 . THR A 1 132 ? 20.915 14.057 14.809 1.00 12.16 ? 132 THR A CG2 1 ATOM 1022 N N . THR A 1 133 ? 24.341 15.675 11.960 1.00 10.69 ? 133 THR A N 1 ATOM 1023 C CA . THR A 1 133 ? 25.569 16.350 11.578 1.00 12.18 ? 133 THR A CA 1 ATOM 1024 C C . THR A 1 133 ? 25.296 17.529 10.655 1.00 12.04 ? 133 THR A C 1 ATOM 1025 O O . THR A 1 133 ? 26.170 18.386 10.465 1.00 11.97 ? 133 THR A O 1 ATOM 1026 C CB . THR A 1 133 ? 26.585 15.421 10.879 1.00 13.93 ? 133 THR A CB 1 ATOM 1027 O OG1 . THR A 1 133 ? 26.159 15.061 9.556 1.00 14.58 ? 133 THR A OG1 1 ATOM 1028 C CG2 . THR A 1 133 ? 26.908 14.207 11.726 1.00 17.04 ? 133 THR A CG2 1 ATOM 1029 N N . TRP A 1 134 ? 24.052 17.712 10.187 1.00 11.05 ? 134 TRP A N 1 ATOM 1030 C CA . TRP A 1 134 ? 23.714 18.833 9.308 1.00 9.46 ? 134 TRP A CA 1 ATOM 1031 C C . TRP A 1 134 ? 24.123 20.180 9.877 1.00 9.05 ? 134 TRP A C 1 ATOM 1032 O O . TRP A 1 134 ? 24.646 21.065 9.148 1.00 9.68 ? 134 TRP A O 1 ATOM 1033 C CB . TRP A 1 134 ? 22.200 18.825 9.065 1.00 9.66 ? 134 TRP A CB 1 ATOM 1034 C CG . TRP A 1 134 ? 21.747 19.971 8.184 1.00 8.79 ? 134 TRP A CG 1 ATOM 1035 C CD1 . TRP A 1 134 ? 21.745 20.017 6.833 1.00 8.66 ? 134 TRP A CD1 1 ATOM 1036 C CD2 . TRP A 1 134 ? 21.149 21.206 8.627 1.00 8.14 ? 134 TRP A CD2 1 ATOM 1037 N NE1 . TRP A 1 134 ? 21.266 21.229 6.372 1.00 9.60 ? 134 TRP A NE1 1 ATOM 1038 C CE2 . TRP A 1 134 ? 20.909 21.969 7.459 1.00 8.98 ? 134 TRP A CE2 1 ATOM 1039 C CE3 . TRP A 1 134 ? 20.866 21.760 9.863 1.00 8.87 ? 134 TRP A CE3 1 ATOM 1040 C CZ2 . TRP A 1 134 ? 20.313 23.235 7.518 1.00 9.07 ? 134 TRP A CZ2 1 ATOM 1041 C CZ3 . TRP A 1 134 ? 20.275 23.011 9.933 1.00 8.76 ? 134 TRP A CZ3 1 ATOM 1042 C CH2 . TRP A 1 134 ? 20.043 23.739 8.769 1.00 9.06 ? 134 TRP A CH2 1 ATOM 1043 N N . TYR A 1 135 ? 23.923 20.369 11.183 1.00 9.39 ? 135 TYR A N 1 ATOM 1044 C CA . TYR A 1 135 ? 24.187 21.633 11.876 1.00 9.95 ? 135 TYR A CA 1 ATOM 1045 C C . TYR A 1 135 ? 25.633 22.119 11.776 1.00 10.58 ? 135 TYR A C 1 ATOM 1046 O O . TYR A 1 135 ? 25.894 23.323 11.845 1.00 11.35 ? 135 TYR A O 1 ATOM 1047 C CB . TYR A 1 135 ? 23.799 21.534 13.371 1.00 9.55 ? 135 TYR A CB 1 ATOM 1048 C CG . TYR A 1 135 ? 22.292 21.341 13.501 1.00 9.80 ? 135 TYR A CG 1 ATOM 1049 C CD1 . TYR A 1 135 ? 21.428 22.426 13.413 1.00 9.36 ? 135 TYR A CD1 1 ATOM 1050 C CD2 . TYR A 1 135 ? 21.744 20.094 13.712 1.00 9.44 ? 135 TYR A CD2 1 ATOM 1051 C CE1 . TYR A 1 135 ? 20.065 22.248 13.519 1.00 9.55 ? 135 TYR A CE1 1 ATOM 1052 C CE2 . TYR A 1 135 ? 20.368 19.902 13.807 1.00 9.78 ? 135 TYR A CE2 1 ATOM 1053 C CZ . TYR A 1 135 ? 19.533 20.998 13.721 1.00 9.51 ? 135 TYR A CZ 1 ATOM 1054 O OH . TYR A 1 135 ? 18.145 20.851 13.795 1.00 9.40 ? 135 TYR A OH 1 ATOM 1055 N N . THR A 1 136 ? 26.540 21.132 11.597 1.00 11.22 ? 136 THR A N 1 ATOM 1056 C CA . THR A 1 136 ? 27.969 21.455 11.507 1.00 12.25 ? 136 THR A CA 1 ATOM 1057 C C . THR A 1 136 ? 28.595 20.953 10.215 1.00 11.18 ? 136 THR A C 1 ATOM 1058 O O . THR A 1 136 ? 29.838 20.918 10.097 1.00 13.12 ? 136 THR A O 1 ATOM 1059 C CB . THR A 1 136 ? 28.712 20.858 12.724 1.00 12.96 ? 136 THR A CB 1 ATOM 1060 O OG1 . THR A 1 136 ? 28.529 19.425 12.716 1.00 14.45 ? 136 THR A OG1 1 ATOM 1061 C CG2 . THR A 1 136 ? 28.239 21.422 14.048 1.00 15.77 ? 136 THR A CG2 1 ATOM 1062 N N . ASN A 1 137 ? 27.815 20.686 9.191 1.00 10.74 ? 137 ASN A N 1 ATOM 1063 C CA . ASN A 1 137 ? 28.280 20.287 7.858 1.00 11.25 ? 137 ASN A CA 1 ATOM 1064 C C . ASN A 1 137 ? 28.567 21.570 7.079 1.00 11.27 ? 137 ASN A C 1 ATOM 1065 O O . ASN A 1 137 ? 27.687 22.384 6.795 1.00 12.15 ? 137 ASN A O 1 ATOM 1066 C CB . ASN A 1 137 ? 27.188 19.432 7.212 1.00 12.87 ? 137 ASN A CB 1 ATOM 1067 C CG . ASN A 1 137 ? 27.474 19.022 5.789 1.00 13.57 ? 137 ASN A CG 1 ATOM 1068 O OD1 . ASN A 1 137 ? 28.001 19.792 4.968 1.00 14.92 ? 137 ASN A OD1 1 ATOM 1069 N ND2 . ASN A 1 137 ? 27.106 17.790 5.487 1.00 16.45 ? 137 ASN A ND2 1 ATOM 1070 N N . THR A 1 138 ? 29.877 21.826 6.832 1.00 11.80 ? 138 THR A N 1 ATOM 1071 C CA . THR A 1 138 ? 30.239 23.134 6.250 1.00 12.42 ? 138 THR A CA 1 ATOM 1072 C C . THR A 1 138 ? 29.560 23.406 4.915 1.00 12.64 ? 138 THR A C 1 ATOM 1073 O O . THR A 1 138 ? 29.052 24.518 4.705 1.00 12.27 ? 138 THR A O 1 ATOM 1074 C CB . THR A 1 138 ? 31.767 23.260 6.078 1.00 15.63 ? 138 THR A CB 1 ATOM 1075 O OG1 . THR A 1 138 ? 32.359 22.976 7.360 1.00 17.40 ? 138 THR A OG1 1 ATOM 1076 C CG2 . THR A 1 138 ? 32.173 24.658 5.638 1.00 16.78 ? 138 THR A CG2 1 ATOM 1077 N N . ALA A 1 139 ? 29.558 22.439 4.006 1.00 12.04 ? 139 ALA A N 1 ATOM 1078 C CA . ALA A 1 139 ? 28.899 22.676 2.715 1.00 11.78 ? 139 ALA A CA 1 ATOM 1079 C C . ALA A 1 139 ? 27.403 22.934 2.890 1.00 10.75 ? 139 ALA A C 1 ATOM 1080 O O . ALA A 1 139 ? 26.845 23.780 2.180 1.00 12.54 ? 139 ALA A O 1 ATOM 1081 C CB . ALA A 1 139 ? 29.190 21.533 1.764 1.00 12.73 ? 139 ALA A CB 1 ATOM 1082 N N . ALA A 1 140 ? 26.753 22.142 3.758 1.00 10.06 ? 140 ALA A N 1 ATOM 1083 C CA . ALA A 1 140 ? 25.322 22.353 3.939 1.00 9.80 ? 140 ALA A CA 1 ATOM 1084 C C . ALA A 1 140 ? 25.002 23.696 4.556 1.00 10.03 ? 140 ALA A C 1 ATOM 1085 O O . ALA A 1 140 ? 24.095 24.399 4.116 1.00 11.05 ? 140 ALA A O 1 ATOM 1086 C CB . ALA A 1 140 ? 24.728 21.248 4.824 1.00 10.94 ? 140 ALA A CB 1 ATOM 1087 N N . GLN A 1 141 ? 25.781 24.121 5.537 1.00 9.01 ? 141 GLN A N 1 ATOM 1088 C CA . GLN A 1 141 ? 25.566 25.395 6.223 1.00 8.78 ? 141 GLN A CA 1 ATOM 1089 C C . GLN A 1 141 ? 25.890 26.580 5.294 1.00 9.76 ? 141 GLN A C 1 ATOM 1090 O O . GLN A 1 141 ? 25.184 27.598 5.350 1.00 10.64 ? 141 GLN A O 1 ATOM 1091 C CB . GLN A 1 141 ? 26.342 25.456 7.528 1.00 9.33 ? 141 GLN A CB 1 ATOM 1092 C CG . GLN A 1 141 ? 25.805 24.550 8.634 1.00 9.57 ? 141 GLN A CG 1 ATOM 1093 C CD . GLN A 1 141 ? 24.345 24.796 8.894 1.00 10.00 ? 141 GLN A CD 1 ATOM 1094 O OE1 . GLN A 1 141 ? 23.938 25.942 9.140 1.00 9.88 ? 141 GLN A OE1 1 ATOM 1095 N NE2 . GLN A 1 141 ? 23.543 23.741 8.829 1.00 10.35 ? 141 GLN A NE2 1 ATOM 1096 N N . THR A 1 142 ? 26.898 26.427 4.438 1.00 10.82 ? 142 THR A N 1 ATOM 1097 C CA . THR A 1 142 ? 27.224 27.481 3.487 1.00 11.65 ? 142 THR A CA 1 ATOM 1098 C C . THR A 1 142 ? 26.083 27.726 2.498 1.00 10.23 ? 142 THR A C 1 ATOM 1099 O O . THR A 1 142 ? 25.650 28.891 2.314 1.00 10.38 ? 142 THR A O 1 ATOM 1100 C CB . THR A 1 142 ? 28.505 27.133 2.712 1.00 13.87 ? 142 THR A CB 1 ATOM 1101 O OG1 . THR A 1 142 ? 29.555 27.135 3.695 1.00 15.48 ? 142 THR A OG1 1 ATOM 1102 C CG2 . THR A 1 142 ? 28.804 28.199 1.671 1.00 15.83 ? 142 THR A CG2 1 ATOM 1103 N N . GLN A 1 143 ? 25.476 26.629 2.033 1.00 10.11 ? 143 GLN A N 1 ATOM 1104 C CA . GLN A 1 143 ? 24.324 26.806 1.127 1.00 9.04 ? 143 GLN A CA 1 ATOM 1105 C C . GLN A 1 143 ? 23.110 27.303 1.891 1.00 9.75 ? 143 GLN A C 1 ATOM 1106 O O . GLN A 1 143 ? 22.378 28.170 1.384 1.00 8.91 ? 143 GLN A O 1 ATOM 1107 C CB . GLN A 1 143 ? 24.062 25.514 0.346 1.00 9.90 ? 143 GLN A CB 1 ATOM 1108 C CG . GLN A 1 143 ? 23.002 25.707 -0.711 1.00 10.13 ? 143 GLN A CG 1 ATOM 1109 C CD . GLN A 1 143 ? 23.364 26.677 -1.806 1.00 10.89 ? 143 GLN A CD 1 ATOM 1110 O OE1 . GLN A 1 143 ? 24.538 26.832 -2.204 1.00 13.42 ? 143 GLN A OE1 1 ATOM 1111 N NE2 . GLN A 1 143 ? 22.378 27.403 -2.345 1.00 10.15 ? 143 GLN A NE2 1 ATOM 1112 N N . TYR A 1 144 ? 22.859 26.754 3.071 1.00 9.06 ? 144 TYR A N 1 ATOM 1113 C CA . TYR A 1 144 ? 21.727 27.251 3.882 1.00 8.71 ? 144 TYR A CA 1 ATOM 1114 C C . TYR A 1 144 ? 21.854 28.753 4.091 1.00 8.44 ? 144 TYR A C 1 ATOM 1115 O O . TYR A 1 144 ? 20.865 29.522 3.952 1.00 9.77 ? 144 TYR A O 1 ATOM 1116 C CB . TYR A 1 144 ? 21.646 26.500 5.215 1.00 9.11 ? 144 TYR A CB 1 ATOM 1117 C CG . TYR A 1 144 ? 20.746 27.076 6.280 1.00 8.22 ? 144 TYR A CG 1 ATOM 1118 C CD1 . TYR A 1 144 ? 19.351 26.968 6.215 1.00 9.35 ? 144 TYR A CD1 1 ATOM 1119 C CD2 . TYR A 1 144 ? 21.280 27.706 7.403 1.00 9.03 ? 144 TYR A CD2 1 ATOM 1120 C CE1 . TYR A 1 144 ? 18.581 27.504 7.220 1.00 8.18 ? 144 TYR A CE1 1 ATOM 1121 C CE2 . TYR A 1 144 ? 20.489 28.252 8.397 1.00 9.56 ? 144 TYR A CE2 1 ATOM 1122 C CZ . TYR A 1 144 ? 19.111 28.137 8.309 1.00 8.51 ? 144 TYR A CZ 1 ATOM 1123 O OH . TYR A 1 144 ? 18.378 28.711 9.327 1.00 9.76 ? 144 TYR A OH 1 ATOM 1124 N N . ARG A 1 145 ? 23.041 29.264 4.471 1.00 9.39 ? 145 ARG A N 1 ATOM 1125 C CA . ARG A 1 145 ? 23.203 30.713 4.666 1.00 10.35 ? 145 ARG A CA 1 ATOM 1126 C C . ARG A 1 145 ? 23.053 31.505 3.368 1.00 9.33 ? 145 ARG A C 1 ATOM 1127 O O . ARG A 1 145 ? 22.516 32.637 3.411 1.00 10.35 ? 145 ARG A O 1 ATOM 1128 C CB . ARG A 1 145 ? 24.564 31.026 5.303 1.00 11.96 ? 145 ARG A CB 1 ATOM 1129 C CG . ARG A 1 145 ? 24.577 30.533 6.756 0.70 12.69 ? 145 ARG A CG 1 ATOM 1130 C CD . ARG A 1 145 ? 25.886 31.112 7.391 0.70 15.36 ? 145 ARG A CD 1 ATOM 1131 N NE . ARG A 1 145 ? 25.834 30.708 8.777 0.70 15.78 ? 145 ARG A NE 1 ATOM 1132 C CZ . ARG A 1 145 ? 26.266 31.360 9.826 0.70 13.53 ? 145 ARG A CZ 1 ATOM 1133 N NH1 . ARG A 1 145 ? 26.979 32.491 9.639 0.70 13.18 ? 145 ARG A NH1 1 ATOM 1134 N NH2 . ARG A 1 145 ? 26.035 30.763 10.990 0.70 14.91 ? 145 ARG A NH2 1 ATOM 1135 N N . LYS A 1 146 ? 23.437 30.936 2.227 1.00 8.92 ? 146 LYS A N 1 ATOM 1136 C CA . LYS A 1 146 ? 23.207 31.590 0.937 1.00 10.80 ? 146 LYS A CA 1 ATOM 1137 C C . LYS A 1 146 ? 21.690 31.714 0.709 1.00 10.85 ? 146 LYS A C 1 ATOM 1138 O O . LYS A 1 146 ? 21.241 32.752 0.214 1.00 11.70 ? 146 LYS A O 1 ATOM 1139 C CB . LYS A 1 146 ? 23.849 30.794 -0.198 1.00 12.67 ? 146 LYS A CB 1 ATOM 1140 C CG A LYS A 1 146 ? 25.337 30.998 -0.397 0.50 14.80 ? 146 LYS A CG 1 ATOM 1141 C CG B LYS A 1 146 ? 23.902 31.474 -1.535 0.50 12.87 ? 146 LYS A CG 1 ATOM 1142 C CD A LYS A 1 146 ? 25.848 30.234 -1.621 0.50 16.76 ? 146 LYS A CD 1 ATOM 1143 C CD B LYS A 1 146 ? 24.776 30.678 -2.515 0.50 15.53 ? 146 LYS A CD 1 ATOM 1144 C CE A LYS A 1 146 ? 25.262 30.707 -2.925 0.50 19.31 ? 146 LYS A CE 1 ATOM 1145 C CE B LYS A 1 146 ? 24.743 31.316 -3.897 0.50 17.05 ? 146 LYS A CE 1 ATOM 1146 N NZ A LYS A 1 146 ? 26.126 30.446 -4.112 0.50 22.57 ? 146 LYS A NZ 1 ATOM 1147 N NZ B LYS A 1 146 ? 25.455 30.497 -4.921 0.50 18.28 ? 146 LYS A NZ 1 ATOM 1148 N N . TYR A 1 147 ? 20.964 30.650 1.089 1.00 10.19 ? 147 TYR A N 1 ATOM 1149 C CA . TYR A 1 147 ? 19.506 30.704 0.919 1.00 10.15 ? 147 TYR A CA 1 ATOM 1150 C C . TYR A 1 147 ? 18.873 31.690 1.879 1.00 9.19 ? 147 TYR A C 1 ATOM 1151 O O . TYR A 1 147 ? 18.013 32.502 1.464 1.00 10.34 ? 147 TYR A O 1 ATOM 1152 C CB . TYR A 1 147 ? 18.906 29.277 1.135 1.00 9.95 ? 147 TYR A CB 1 ATOM 1153 C CG . TYR A 1 147 ? 17.424 29.337 0.829 1.00 9.86 ? 147 TYR A CG 1 ATOM 1154 C CD1 . TYR A 1 147 ? 16.990 29.541 -0.477 1.00 9.87 ? 147 TYR A CD1 1 ATOM 1155 C CD2 . TYR A 1 147 ? 16.472 29.190 1.844 1.00 10.04 ? 147 TYR A CD2 1 ATOM 1156 C CE1 . TYR A 1 147 ? 15.649 29.645 -0.770 1.00 9.40 ? 147 TYR A CE1 1 ATOM 1157 C CE2 . TYR A 1 147 ? 15.123 29.312 1.542 1.00 8.33 ? 147 TYR A CE2 1 ATOM 1158 C CZ . TYR A 1 147 ? 14.723 29.532 0.254 1.00 8.88 ? 147 TYR A CZ 1 ATOM 1159 O OH . TYR A 1 147 ? 13.339 29.665 -0.041 1.00 9.06 ? 147 TYR A OH 1 ATOM 1160 N N . VAL A 1 148 ? 19.305 31.741 3.128 1.00 8.78 ? 148 VAL A N 1 ATOM 1161 C CA . VAL A 1 148 ? 18.861 32.754 4.092 1.00 9.30 ? 148 VAL A CA 1 ATOM 1162 C C . VAL A 1 148 ? 19.082 34.146 3.501 1.00 9.87 ? 148 VAL A C 1 ATOM 1163 O O . VAL A 1 148 ? 18.178 35.005 3.543 1.00 10.83 ? 148 VAL A O 1 ATOM 1164 C CB . VAL A 1 148 ? 19.575 32.580 5.440 1.00 8.83 ? 148 VAL A CB 1 ATOM 1165 C CG1 . VAL A 1 148 ? 19.260 33.748 6.396 1.00 10.28 ? 148 VAL A CG1 1 ATOM 1166 C CG2 . VAL A 1 148 ? 19.158 31.290 6.131 1.00 9.04 ? 148 VAL A CG2 1 ATOM 1167 N N . GLN A 1 149 ? 20.282 34.449 2.980 1.00 11.56 ? 149 GLN A N 1 ATOM 1168 C CA . GLN A 1 149 ? 20.521 35.753 2.380 1.00 11.43 ? 149 GLN A CA 1 ATOM 1169 C C . GLN A 1 149 ? 19.587 36.069 1.221 1.00 11.24 ? 149 GLN A C 1 ATOM 1170 O O . GLN A 1 149 ? 19.073 37.207 1.106 1.00 12.57 ? 149 GLN A O 1 ATOM 1171 C CB . GLN A 1 149 ? 21.996 35.912 1.947 1.00 14.23 ? 149 GLN A CB 1 ATOM 1172 C CG . GLN A 1 149 ? 22.341 37.339 1.550 1.00 14.88 ? 149 GLN A CG 1 ATOM 1173 C CD . GLN A 1 149 ? 21.997 37.855 0.186 1.00 18.59 ? 149 GLN A CD 1 ATOM 1174 O OE1 . GLN A 1 149 ? 21.832 37.087 -0.768 1.00 19.57 ? 149 GLN A OE1 1 ATOM 1175 N NE2 . GLN A 1 149 ? 21.910 39.186 -0.022 1.00 20.89 ? 149 GLN A NE2 1 ATOM 1176 N N . ALA A 1 150 ? 19.288 35.069 0.421 1.00 10.12 ? 150 ALA A N 1 ATOM 1177 C CA . ALA A 1 150 ? 18.429 35.250 -0.741 1.00 10.58 ? 150 ALA A CA 1 ATOM 1178 C C . ALA A 1 150 ? 17.006 35.613 -0.331 1.00 12.95 ? 150 ALA A C 1 ATOM 1179 O O . ALA A 1 150 ? 16.328 36.401 -1.005 1.00 14.90 ? 150 ALA A O 1 ATOM 1180 C CB . ALA A 1 150 ? 18.432 34.028 -1.664 1.00 11.53 ? 150 ALA A CB 1 ATOM 1181 N N . VAL A 1 151 ? 16.524 35.006 0.776 1.00 11.16 ? 151 VAL A N 1 ATOM 1182 C CA . VAL A 1 151 ? 15.150 35.321 1.187 1.00 10.27 ? 151 VAL A CA 1 ATOM 1183 C C . VAL A 1 151 ? 15.140 36.630 1.972 1.00 9.71 ? 151 VAL A C 1 ATOM 1184 O O . VAL A 1 151 ? 14.345 37.538 1.647 1.00 11.01 ? 151 VAL A O 1 ATOM 1185 C CB . VAL A 1 151 ? 14.622 34.180 2.055 1.00 11.18 ? 151 VAL A CB 1 ATOM 1186 C CG1 . VAL A 1 151 ? 13.255 34.536 2.673 1.00 11.39 ? 151 VAL A CG1 1 ATOM 1187 C CG2 . VAL A 1 151 ? 14.447 32.913 1.220 1.00 12.46 ? 151 VAL A CG2 1 ATOM 1188 N N . VAL A 1 152 ? 16.019 36.769 2.974 1.00 9.81 ? 152 VAL A N 1 ATOM 1189 C CA . VAL A 1 152 ? 16.008 37.986 3.787 1.00 9.55 ? 152 VAL A CA 1 ATOM 1190 C C . VAL A 1 152 ? 16.224 39.244 2.964 1.00 11.84 ? 152 VAL A C 1 ATOM 1191 O O . VAL A 1 152 ? 15.524 40.243 3.187 1.00 11.62 ? 152 VAL A O 1 ATOM 1192 C CB . VAL A 1 152 ? 17.058 37.952 4.932 1.00 10.75 ? 152 VAL A CB 1 ATOM 1193 C CG1 . VAL A 1 152 ? 17.161 39.281 5.673 1.00 11.26 ? 152 VAL A CG1 1 ATOM 1194 C CG2 . VAL A 1 152 ? 16.682 36.848 5.908 1.00 10.48 ? 152 VAL A CG2 1 ATOM 1195 N N . SER A 1 153 ? 17.110 39.203 1.975 1.00 11.68 ? 153 SER A N 1 ATOM 1196 C CA . SER A 1 153 ? 17.366 40.438 1.204 1.00 13.12 ? 153 SER A CA 1 ATOM 1197 C C . SER A 1 153 ? 16.181 40.887 0.382 1.00 13.33 ? 153 SER A C 1 ATOM 1198 O O . SER A 1 153 ? 16.148 42.062 0.018 1.00 16.69 ? 153 SER A O 1 ATOM 1199 C CB . SER A 1 153 ? 18.619 40.212 0.370 1.00 15.42 ? 153 SER A CB 1 ATOM 1200 O OG . SER A 1 153 ? 18.445 39.239 -0.626 1.00 15.54 ? 153 SER A OG 1 ATOM 1201 N N . ARG A 1 154 ? 15.257 39.979 0.074 1.00 12.11 ? 154 ARG A N 1 ATOM 1202 C CA . ARG A 1 154 ? 14.093 40.405 -0.681 1.00 12.50 ? 154 ARG A CA 1 ATOM 1203 C C . ARG A 1 154 ? 13.137 41.244 0.154 1.00 13.59 ? 154 ARG A C 1 ATOM 1204 O O . ARG A 1 154 ? 12.370 42.049 -0.406 1.00 16.60 ? 154 ARG A O 1 ATOM 1205 C CB . ARG A 1 154 ? 13.296 39.190 -1.219 1.00 13.67 ? 154 ARG A CB 1 ATOM 1206 C CG . ARG A 1 154 ? 14.105 38.389 -2.210 1.00 14.43 ? 154 ARG A CG 1 ATOM 1207 C CD . ARG A 1 154 ? 13.432 37.151 -2.805 1.00 13.60 ? 154 ARG A CD 1 ATOM 1208 N NE . ARG A 1 154 ? 12.582 37.406 -3.977 1.00 13.50 ? 154 ARG A NE 1 ATOM 1209 C CZ . ARG A 1 154 ? 13.095 37.520 -5.198 1.00 14.02 ? 154 ARG A CZ 1 ATOM 1210 N NH1 . ARG A 1 154 ? 14.394 37.353 -5.427 1.00 13.48 ? 154 ARG A NH1 1 ATOM 1211 N NH2 . ARG A 1 154 ? 12.335 37.787 -6.264 1.00 15.54 ? 154 ARG A NH2 1 ATOM 1212 N N . TYR A 1 155 ? 13.042 40.891 1.453 1.00 11.19 ? 155 TYR A N 1 ATOM 1213 C CA . TYR A 1 155 ? 11.973 41.481 2.263 1.00 10.11 ? 155 TYR A CA 1 ATOM 1214 C C . TYR A 1 155 ? 12.437 42.249 3.467 1.00 9.38 ? 155 TYR A C 1 ATOM 1215 O O . TYR A 1 155 ? 11.682 42.620 4.360 1.00 10.60 ? 155 TYR A O 1 ATOM 1216 C CB . TYR A 1 155 ? 10.948 40.415 2.724 1.00 11.38 ? 155 TYR A CB 1 ATOM 1217 C CG . TYR A 1 155 ? 10.570 39.413 1.658 1.00 11.33 ? 155 TYR A CG 1 ATOM 1218 C CD1 . TYR A 1 155 ? 9.980 39.786 0.462 1.00 9.94 ? 155 TYR A CD1 1 ATOM 1219 C CD2 . TYR A 1 155 ? 10.861 38.066 1.796 1.00 12.86 ? 155 TYR A CD2 1 ATOM 1220 C CE1 . TYR A 1 155 ? 9.707 38.923 -0.565 1.00 11.14 ? 155 TYR A CE1 1 ATOM 1221 C CE2 . TYR A 1 155 ? 10.599 37.159 0.790 1.00 13.84 ? 155 TYR A CE2 1 ATOM 1222 C CZ . TYR A 1 155 ? 9.998 37.576 -0.378 1.00 12.99 ? 155 TYR A CZ 1 ATOM 1223 O OH . TYR A 1 155 ? 9.782 36.676 -1.376 1.00 13.17 ? 155 TYR A OH 1 ATOM 1224 N N . ALA A 1 156 ? 13.765 42.541 3.561 1.00 10.37 ? 156 ALA A N 1 ATOM 1225 C CA . ALA A 1 156 ? 14.331 43.171 4.735 1.00 9.20 ? 156 ALA A CA 1 ATOM 1226 C C . ALA A 1 156 ? 13.700 44.508 5.107 1.00 9.74 ? 156 ALA A C 1 ATOM 1227 O O . ALA A 1 156 ? 13.708 44.853 6.290 1.00 10.37 ? 156 ALA A O 1 ATOM 1228 C CB . ALA A 1 156 ? 15.865 43.321 4.608 1.00 10.65 ? 156 ALA A CB 1 ATOM 1229 N N . ASN A 1 157 ? 13.211 45.253 4.125 1.00 10.38 ? 157 ASN A N 1 ATOM 1230 C CA . ASN A 1 157 ? 12.631 46.546 4.369 1.00 9.02 ? 157 ASN A CA 1 ATOM 1231 C C . ASN A 1 157 ? 11.107 46.573 4.283 1.00 8.94 ? 157 ASN A C 1 ATOM 1232 O O . ASN A 1 157 ? 10.486 47.632 4.322 1.00 9.29 ? 157 ASN A O 1 ATOM 1233 C CB . ASN A 1 157 ? 13.235 47.654 3.438 1.00 8.15 ? 157 ASN A CB 1 ATOM 1234 C CG . ASN A 1 157 ? 14.696 47.669 3.536 1.00 8.86 ? 157 ASN A CG 1 ATOM 1235 O OD1 . ASN A 1 157 ? 15.517 46.898 3.024 1.00 10.54 ? 157 ASN A OD1 1 ATOM 1236 N ND2 . ASN A 1 157 ? 15.153 48.614 4.370 1.00 8.39 ? 157 ASN A ND2 1 ATOM 1237 N N . SER A 1 158 ? 10.519 45.362 4.257 1.00 9.30 ? 158 SER A N 1 ATOM 1238 C CA . SER A 1 158 ? 9.050 45.271 4.253 1.00 8.76 ? 158 SER A CA 1 ATOM 1239 C C . SER A 1 158 ? 8.492 45.289 5.675 1.00 9.64 ? 158 SER A C 1 ATOM 1240 O O . SER A 1 158 ? 8.988 44.534 6.520 1.00 10.52 ? 158 SER A O 1 ATOM 1241 C CB . SER A 1 158 ? 8.642 43.921 3.629 1.00 10.45 ? 158 SER A CB 1 ATOM 1242 O OG . SER A 1 158 ? 7.198 43.752 3.772 1.00 11.46 ? 158 SER A OG 1 ATOM 1243 N N . THR A 1 159 ? 7.436 46.047 5.935 1.00 9.68 ? 159 THR A N 1 ATOM 1244 C CA . THR A 1 159 ? 6.802 46.043 7.253 1.00 11.16 ? 159 THR A CA 1 ATOM 1245 C C . THR A 1 159 ? 5.891 44.817 7.434 1.00 10.47 ? 159 THR A C 1 ATOM 1246 O O . THR A 1 159 ? 5.400 44.653 8.548 1.00 11.00 ? 159 THR A O 1 ATOM 1247 C CB . THR A 1 159 ? 6.015 47.323 7.541 1.00 12.97 ? 159 THR A CB 1 ATOM 1248 O OG1 . THR A 1 159 ? 5.032 47.407 6.532 1.00 17.40 ? 159 THR A OG1 1 ATOM 1249 C CG2 . THR A 1 159 ? 6.914 48.542 7.472 1.00 14.65 ? 159 THR A CG2 1 ATOM 1250 N N . ALA A 1 160 ? 5.746 43.951 6.436 1.00 9.51 ? 160 ALA A N 1 ATOM 1251 C CA . ALA A 1 160 ? 4.886 42.793 6.649 1.00 9.49 ? 160 ALA A CA 1 ATOM 1252 C C . ALA A 1 160 ? 5.560 41.593 7.264 1.00 9.87 ? 160 ALA A C 1 ATOM 1253 O O . ALA A 1 160 ? 4.874 40.594 7.451 1.00 10.47 ? 160 ALA A O 1 ATOM 1254 C CB . ALA A 1 160 ? 4.301 42.391 5.295 1.00 10.16 ? 160 ALA A CB 1 ATOM 1255 N N . ILE A 1 161 ? 6.854 41.627 7.544 1.00 9.06 ? 161 ILE A N 1 ATOM 1256 C CA . ILE A 1 161 ? 7.493 40.476 8.180 1.00 8.60 ? 161 ILE A CA 1 ATOM 1257 C C . ILE A 1 161 ? 7.375 40.629 9.698 1.00 9.72 ? 161 ILE A C 1 ATOM 1258 O O . ILE A 1 161 ? 7.816 41.592 10.322 1.00 10.83 ? 161 ILE A O 1 ATOM 1259 C CB . ILE A 1 161 ? 8.973 40.362 7.765 1.00 8.93 ? 161 ILE A CB 1 ATOM 1260 C CG1 . ILE A 1 161 ? 9.151 40.340 6.247 1.00 9.34 ? 161 ILE A CG1 1 ATOM 1261 C CG2 . ILE A 1 161 ? 9.665 39.185 8.459 1.00 10.93 ? 161 ILE A CG2 1 ATOM 1262 C CD1 . ILE A 1 161 ? 8.435 39.206 5.553 1.00 11.27 ? 161 ILE A CD1 1 ATOM 1263 N N . PHE A 1 162 ? 6.721 39.661 10.344 1.00 8.13 ? 162 PHE A N 1 ATOM 1264 C CA . PHE A 1 162 ? 6.633 39.561 11.789 1.00 8.94 ? 162 PHE A CA 1 ATOM 1265 C C . PHE A 1 162 ? 8.005 39.179 12.378 1.00 8.84 ? 162 PHE A C 1 ATOM 1266 O O . PHE A 1 162 ? 8.554 39.848 13.268 1.00 8.96 ? 162 PHE A O 1 ATOM 1267 C CB . PHE A 1 162 ? 5.590 38.543 12.272 1.00 9.23 ? 162 PHE A CB 1 ATOM 1268 C CG . PHE A 1 162 ? 5.329 38.564 13.751 1.00 7.75 ? 162 PHE A CG 1 ATOM 1269 C CD1 . PHE A 1 162 ? 6.129 37.868 14.639 1.00 9.09 ? 162 PHE A CD1 1 ATOM 1270 C CD2 . PHE A 1 162 ? 4.243 39.254 14.275 1.00 8.75 ? 162 PHE A CD2 1 ATOM 1271 C CE1 . PHE A 1 162 ? 5.874 37.867 15.998 1.00 10.40 ? 162 PHE A CE1 1 ATOM 1272 C CE2 . PHE A 1 162 ? 3.978 39.265 15.626 1.00 9.28 ? 162 PHE A CE2 1 ATOM 1273 C CZ . PHE A 1 162 ? 4.813 38.599 16.513 1.00 9.88 ? 162 PHE A CZ 1 ATOM 1274 N N . ALA A 1 163 ? 8.541 38.081 11.864 1.00 9.40 ? 163 ALA A N 1 ATOM 1275 C CA . ALA A 1 163 ? 9.853 37.596 12.271 1.00 7.15 ? 163 ALA A CA 1 ATOM 1276 C C . ALA A 1 163 ? 10.383 36.607 11.225 1.00 7.79 ? 163 ALA A C 1 ATOM 1277 O O . ALA A 1 163 ? 9.674 35.804 10.592 1.00 8.97 ? 163 ALA A O 1 ATOM 1278 C CB . ALA A 1 163 ? 9.752 36.864 13.606 1.00 9.05 ? 163 ALA A CB 1 ATOM 1279 N N . TRP A 1 164 ? 11.722 36.594 11.164 1.00 7.98 ? 164 TRP A N 1 ATOM 1280 C CA . TRP A 1 164 ? 12.478 35.524 10.498 1.00 7.81 ? 164 TRP A CA 1 ATOM 1281 C C . TRP A 1 164 ? 12.569 34.371 11.526 1.00 8.57 ? 164 TRP A C 1 ATOM 1282 O O . TRP A 1 164 ? 12.733 34.582 12.723 1.00 9.33 ? 164 TRP A O 1 ATOM 1283 C CB . TRP A 1 164 ? 13.896 35.989 10.162 1.00 7.92 ? 164 TRP A CB 1 ATOM 1284 C CG . TRP A 1 164 ? 13.901 37.108 9.158 1.00 7.96 ? 164 TRP A CG 1 ATOM 1285 C CD1 . TRP A 1 164 ? 14.423 38.356 9.355 1.00 8.75 ? 164 TRP A CD1 1 ATOM 1286 C CD2 . TRP A 1 164 ? 13.286 37.127 7.867 1.00 8.38 ? 164 TRP A CD2 1 ATOM 1287 N NE1 . TRP A 1 164 ? 14.225 39.139 8.246 1.00 8.65 ? 164 TRP A NE1 1 ATOM 1288 C CE2 . TRP A 1 164 ? 13.497 38.416 7.327 1.00 8.93 ? 164 TRP A CE2 1 ATOM 1289 C CE3 . TRP A 1 164 ? 12.568 36.201 7.111 1.00 9.68 ? 164 TRP A CE3 1 ATOM 1290 C CZ2 . TRP A 1 164 ? 13.029 38.813 6.058 1.00 9.88 ? 164 TRP A CZ2 1 ATOM 1291 C CZ3 . TRP A 1 164 ? 12.089 36.571 5.868 1.00 9.80 ? 164 TRP A CZ3 1 ATOM 1292 C CH2 . TRP A 1 164 ? 12.336 37.871 5.355 1.00 10.70 ? 164 TRP A CH2 1 ATOM 1293 N N . GLU A 1 165 ? 12.541 33.133 10.998 1.00 7.56 ? 165 GLU A N 1 ATOM 1294 C CA . GLU A 1 165 ? 12.562 31.945 11.843 1.00 7.13 ? 165 GLU A CA 1 ATOM 1295 C C . GLU A 1 165 ? 13.603 30.975 11.301 1.00 5.81 ? 165 GLU A C 1 ATOM 1296 O O . GLU A 1 165 ? 13.647 30.677 10.101 1.00 7.15 ? 165 GLU A O 1 ATOM 1297 C CB . GLU A 1 165 ? 11.156 31.343 11.926 1.00 7.03 ? 165 GLU A CB 1 ATOM 1298 C CG . GLU A 1 165 ? 11.059 30.104 12.824 1.00 7.90 ? 165 GLU A CG 1 ATOM 1299 C CD . GLU A 1 165 ? 9.593 29.893 13.184 1.00 8.09 ? 165 GLU A CD 1 ATOM 1300 O OE1 . GLU A 1 165 ? 8.934 29.235 12.368 1.00 8.07 ? 165 GLU A OE1 1 ATOM 1301 O OE2 . GLU A 1 165 ? 9.213 30.491 14.222 1.00 8.77 ? 165 GLU A OE2 1 ATOM 1302 N N . LEU A 1 166 ? 14.520 30.548 12.216 1.00 6.79 ? 166 LEU A N 1 ATOM 1303 C CA . LEU A 1 166 ? 15.645 29.749 11.689 1.00 7.20 ? 166 LEU A CA 1 ATOM 1304 C C . LEU A 1 166 ? 15.198 28.463 11.041 1.00 8.31 ? 166 LEU A C 1 ATOM 1305 O O . LEU A 1 166 ? 15.773 28.102 9.974 1.00 8.38 ? 166 LEU A O 1 ATOM 1306 C CB . LEU A 1 166 ? 16.659 29.502 12.801 1.00 7.55 ? 166 LEU A CB 1 ATOM 1307 C CG . LEU A 1 166 ? 17.142 30.735 13.580 1.00 8.34 ? 166 LEU A CG 1 ATOM 1308 C CD1 . LEU A 1 166 ? 18.357 30.347 14.420 1.00 9.10 ? 166 LEU A CD1 1 ATOM 1309 C CD2 . LEU A 1 166 ? 17.450 31.913 12.684 1.00 9.90 ? 166 LEU A CD2 1 ATOM 1310 N N . GLY A 1 167 ? 14.198 27.776 11.582 1.00 7.26 ? 167 GLY A N 1 ATOM 1311 C CA . GLY A 1 167 ? 13.707 26.596 10.874 1.00 7.91 ? 167 GLY A CA 1 ATOM 1312 C C . GLY A 1 167 ? 12.345 26.201 11.456 1.00 8.09 ? 167 GLY A C 1 ATOM 1313 O O . GLY A 1 167 ? 11.927 26.766 12.474 1.00 8.47 ? 167 GLY A O 1 ATOM 1314 N N . ASN A 1 168 ? 11.708 25.234 10.782 1.00 7.17 ? 168 ASN A N 1 ATOM 1315 C CA . ASN A 1 168 ? 10.488 24.654 11.336 1.00 7.23 ? 168 ASN A CA 1 ATOM 1316 C C . ASN A 1 168 ? 10.862 23.426 12.182 1.00 7.17 ? 168 ASN A C 1 ATOM 1317 O O . ASN A 1 168 ? 11.329 22.394 11.675 1.00 7.72 ? 168 ASN A O 1 ATOM 1318 C CB . ASN A 1 168 ? 9.563 24.180 10.230 1.00 6.43 ? 168 ASN A CB 1 ATOM 1319 C CG . ASN A 1 168 ? 8.316 23.519 10.786 1.00 6.45 ? 168 ASN A CG 1 ATOM 1320 O OD1 . ASN A 1 168 ? 7.687 24.096 11.690 1.00 7.04 ? 168 ASN A OD1 1 ATOM 1321 N ND2 . ASN A 1 168 ? 8.013 22.336 10.291 1.00 7.56 ? 168 ASN A ND2 1 ATOM 1322 N N . GLU A 1 169 ? 10.656 23.560 13.484 1.00 6.33 ? 169 GLU A N 1 ATOM 1323 C CA . GLU A 1 169 ? 10.850 22.495 14.464 1.00 7.48 ? 169 GLU A CA 1 ATOM 1324 C C . GLU A 1 169 ? 12.222 21.828 14.445 1.00 7.66 ? 169 GLU A C 1 ATOM 1325 O O . GLU A 1 169 ? 12.345 20.601 14.477 1.00 7.72 ? 169 GLU A O 1 ATOM 1326 C CB . GLU A 1 169 ? 9.764 21.395 14.304 1.00 8.08 ? 169 GLU A CB 1 ATOM 1327 C CG . GLU A 1 169 ? 8.373 22.015 14.393 1.00 7.34 ? 169 GLU A CG 1 ATOM 1328 C CD . GLU A 1 169 ? 7.193 21.066 14.459 1.00 8.11 ? 169 GLU A CD 1 ATOM 1329 O OE1 . GLU A 1 169 ? 7.201 20.004 13.785 1.00 8.42 ? 169 GLU A OE1 1 ATOM 1330 O OE2 . GLU A 1 169 ? 6.176 21.421 15.150 1.00 8.50 ? 169 GLU A OE2 1 ATOM 1331 N N . PRO A 1 170 ? 13.306 22.615 14.440 1.00 7.14 ? 170 PRO A N 1 ATOM 1332 C CA . PRO A 1 170 ? 14.640 22.010 14.450 1.00 7.30 ? 170 PRO A CA 1 ATOM 1333 C C . PRO A 1 170 ? 14.789 21.063 15.644 1.00 7.11 ? 170 PRO A C 1 ATOM 1334 O O . PRO A 1 170 ? 14.476 21.413 16.778 1.00 8.43 ? 170 PRO A O 1 ATOM 1335 C CB . PRO A 1 170 ? 15.569 23.220 14.577 1.00 7.18 ? 170 PRO A CB 1 ATOM 1336 C CG . PRO A 1 170 ? 14.766 24.311 15.173 1.00 8.53 ? 170 PRO A CG 1 ATOM 1337 C CD . PRO A 1 170 ? 13.388 24.085 14.583 1.00 8.14 ? 170 PRO A CD 1 ATOM 1338 N N . ARG A 1 171 ? 15.389 19.888 15.370 1.00 7.33 ? 171 ARG A N 1 ATOM 1339 C CA . ARG A 1 171 ? 15.727 18.909 16.403 1.00 7.37 ? 171 ARG A CA 1 ATOM 1340 C C . ARG A 1 171 ? 17.121 18.373 16.079 1.00 8.62 ? 171 ARG A C 1 ATOM 1341 O O . ARG A 1 171 ? 17.610 18.417 14.954 1.00 9.21 ? 171 ARG A O 1 ATOM 1342 C CB . ARG A 1 171 ? 14.761 17.718 16.452 1.00 7.71 ? 171 ARG A CB 1 ATOM 1343 C CG . ARG A 1 171 ? 13.311 18.007 16.766 1.00 8.57 ? 171 ARG A CG 1 ATOM 1344 C CD . ARG A 1 171 ? 12.565 16.667 16.775 1.00 8.80 ? 171 ARG A CD 1 ATOM 1345 N NE . ARG A 1 171 ? 11.184 16.850 17.239 1.00 8.03 ? 171 ARG A NE 1 ATOM 1346 C CZ . ARG A 1 171 ? 10.414 15.793 17.580 1.00 8.96 ? 171 ARG A CZ 1 ATOM 1347 N NH1 . ARG A 1 171 ? 10.861 14.547 17.512 1.00 9.76 ? 171 ARG A NH1 1 ATOM 1348 N NH2 . ARG A 1 171 ? 9.160 16.063 17.953 1.00 9.57 ? 171 ARG A NH2 1 ATOM 1349 N N . CYS A 1 172 ? 17.774 17.802 17.091 1.00 9.44 ? 172 CYS A N 1 ATOM 1350 C CA . CYS A 1 172 ? 19.045 17.072 16.893 1.00 10.05 ? 172 CYS A CA 1 ATOM 1351 C C . CYS A 1 172 ? 18.896 15.844 17.793 1.00 10.14 ? 172 CYS A C 1 ATOM 1352 O O . CYS A 1 172 ? 19.253 15.882 18.971 1.00 11.81 ? 172 CYS A O 1 ATOM 1353 C CB . CYS A 1 172 ? 20.180 18.039 17.222 1.00 11.10 ? 172 CYS A CB 1 ATOM 1354 S SG . CYS A 1 172 ? 21.819 17.502 16.658 1.00 11.70 ? 172 CYS A SG 1 ATOM 1355 N N . ASN A 1 173 ? 18.258 14.818 17.253 1.00 10.43 ? 173 ASN A N 1 ATOM 1356 C CA . ASN A 1 173 ? 17.926 13.640 18.044 1.00 11.82 ? 173 ASN A CA 1 ATOM 1357 C C . ASN A 1 173 ? 19.129 13.012 18.727 1.00 12.26 ? 173 ASN A C 1 ATOM 1358 O O . ASN A 1 173 ? 20.056 12.576 18.045 1.00 13.17 ? 173 ASN A O 1 ATOM 1359 C CB . ASN A 1 173 ? 17.249 12.617 17.094 1.00 12.93 ? 173 ASN A CB 1 ATOM 1360 C CG . ASN A 1 173 ? 16.819 11.376 17.865 1.00 15.41 ? 173 ASN A CG 1 ATOM 1361 O OD1 . ASN A 1 173 ? 17.483 10.339 17.724 1.00 19.86 ? 173 ASN A OD1 1 ATOM 1362 N ND2 . ASN A 1 173 ? 15.762 11.438 18.635 1.00 14.75 ? 173 ASN A ND2 1 ATOM 1363 N N . GLY A 1 174 ? 19.055 12.900 20.069 1.00 12.24 ? 174 GLY A N 1 ATOM 1364 C CA . GLY A 1 174 ? 20.144 12.299 20.824 1.00 13.01 ? 174 GLY A CA 1 ATOM 1365 C C . GLY A 1 174 ? 21.390 13.159 20.939 1.00 14.27 ? 174 GLY A C 1 ATOM 1366 O O . GLY A 1 174 ? 22.341 12.711 21.587 1.00 16.37 ? 174 GLY A O 1 ATOM 1367 N N . CYS A 1 175 ? 21.374 14.393 20.399 1.00 12.47 ? 175 CYS A N 1 ATOM 1368 C CA . CYS A 1 175 ? 22.576 15.212 20.459 1.00 13.43 ? 175 CYS A CA 1 ATOM 1369 C C . CYS A 1 175 ? 22.699 15.957 21.770 1.00 12.82 ? 175 CYS A C 1 ATOM 1370 O O . CYS A 1 175 ? 21.728 16.187 22.512 1.00 13.45 ? 175 CYS A O 1 ATOM 1371 C CB . CYS A 1 175 ? 22.488 16.317 19.387 1.00 14.84 ? 175 CYS A CB 1 ATOM 1372 S SG . CYS A 1 175 ? 22.195 15.741 17.722 1.00 13.78 ? 175 CYS A SG 1 ATOM 1373 N N . SER A 1 176 ? 23.923 16.450 22.070 1.00 13.42 ? 176 SER A N 1 ATOM 1374 C CA . SER A 1 176 ? 24.103 17.425 23.139 1.00 12.70 ? 176 SER A CA 1 ATOM 1375 C C . SER A 1 176 ? 23.214 18.623 22.762 1.00 12.43 ? 176 SER A C 1 ATOM 1376 O O . SER A 1 176 ? 23.210 19.028 21.587 1.00 13.43 ? 176 SER A O 1 ATOM 1377 C CB . SER A 1 176 ? 25.535 17.950 23.151 1.00 14.29 ? 176 SER A CB 1 ATOM 1378 O OG . SER A 1 176 ? 25.670 19.101 23.948 1.00 16.18 ? 176 SER A OG 1 ATOM 1379 N N . THR A 1 177 ? 22.576 19.242 23.739 1.00 12.14 ? 177 THR A N 1 ATOM 1380 C CA . THR A 1 177 ? 21.745 20.416 23.445 1.00 11.66 ? 177 THR A CA 1 ATOM 1381 C C . THR A 1 177 ? 22.589 21.621 23.000 1.00 11.87 ? 177 THR A C 1 ATOM 1382 O O . THR A 1 177 ? 22.050 22.547 22.392 1.00 12.40 ? 177 THR A O 1 ATOM 1383 C CB . THR A 1 177 ? 20.932 20.817 24.682 1.00 13.10 ? 177 THR A CB 1 ATOM 1384 O OG1 . THR A 1 177 ? 21.838 21.199 25.717 1.00 14.48 ? 177 THR A OG1 1 ATOM 1385 C CG2 . THR A 1 177 ? 19.983 19.693 25.093 1.00 13.29 ? 177 THR A CG2 1 ATOM 1386 N N . ASP A 1 178 ? 23.907 21.587 23.200 1.00 11.46 ? 178 ASP A N 1 ATOM 1387 C CA . ASP A 1 178 ? 24.761 22.675 22.760 1.00 12.42 ? 178 ASP A CA 1 ATOM 1388 C C . ASP A 1 178 ? 24.878 22.765 21.247 1.00 11.97 ? 178 ASP A C 1 ATOM 1389 O O . ASP A 1 178 ? 25.279 23.828 20.700 1.00 11.69 ? 178 ASP A O 1 ATOM 1390 C CB . ASP A 1 178 ? 26.146 22.540 23.422 1.00 15.27 ? 178 ASP A CB 1 ATOM 1391 C CG . ASP A 1 178 ? 27.023 23.781 23.225 1.00 18.19 ? 178 ASP A CG 1 ATOM 1392 O OD1 . ASP A 1 178 ? 26.582 24.859 23.653 1.00 19.63 ? 178 ASP A OD1 1 ATOM 1393 O OD2 . ASP A 1 178 ? 28.098 23.559 22.639 1.00 20.93 ? 178 ASP A OD2 1 ATOM 1394 N N . VAL A 1 179 ? 24.639 21.694 20.485 1.00 12.40 ? 179 VAL A N 1 ATOM 1395 C CA . VAL A 1 179 ? 24.732 21.785 19.026 1.00 11.75 ? 179 VAL A CA 1 ATOM 1396 C C . VAL A 1 179 ? 23.749 22.831 18.502 1.00 11.47 ? 179 VAL A C 1 ATOM 1397 O O . VAL A 1 179 ? 24.155 23.746 17.782 1.00 11.21 ? 179 VAL A O 1 ATOM 1398 C CB . VAL A 1 179 ? 24.525 20.435 18.343 1.00 11.75 ? 179 VAL A CB 1 ATOM 1399 C CG1 . VAL A 1 179 ? 24.535 20.519 16.813 1.00 12.37 ? 179 VAL A CG1 1 ATOM 1400 C CG2 . VAL A 1 179 ? 25.551 19.394 18.767 1.00 12.80 ? 179 VAL A CG2 1 ATOM 1401 N N . ILE A 1 180 ? 22.476 22.721 18.864 1.00 11.18 ? 180 ILE A N 1 ATOM 1402 C CA . ILE A 1 180 ? 21.498 23.741 18.435 1.00 9.80 ? 180 ILE A CA 1 ATOM 1403 C C . ILE A 1 180 ? 21.763 25.057 19.120 1.00 9.37 ? 180 ILE A C 1 ATOM 1404 O O . ILE A 1 180 ? 21.586 26.113 18.466 1.00 10.73 ? 180 ILE A O 1 ATOM 1405 C CB . ILE A 1 180 ? 20.069 23.209 18.603 1.00 9.69 ? 180 ILE A CB 1 ATOM 1406 C CG1 . ILE A 1 180 ? 19.819 22.204 17.474 1.00 9.73 ? 180 ILE A CG1 1 ATOM 1407 C CG2 . ILE A 1 180 ? 19.069 24.382 18.581 1.00 11.21 ? 180 ILE A CG2 1 ATOM 1408 C CD1 . ILE A 1 180 ? 18.522 21.483 17.512 1.00 9.53 ? 180 ILE A CD1 1 ATOM 1409 N N . VAL A 1 181 ? 22.242 25.109 20.386 1.00 9.81 ? 181 VAL A N 1 ATOM 1410 C CA . VAL A 1 181 ? 22.560 26.449 20.922 1.00 10.82 ? 181 VAL A CA 1 ATOM 1411 C C . VAL A 1 181 ? 23.601 27.174 20.063 1.00 10.11 ? 181 VAL A C 1 ATOM 1412 O O . VAL A 1 181 ? 23.411 28.351 19.716 1.00 12.12 ? 181 VAL A O 1 ATOM 1413 C CB . VAL A 1 181 ? 23.065 26.386 22.366 1.00 11.40 ? 181 VAL A CB 1 ATOM 1414 C CG1 . VAL A 1 181 ? 23.485 27.776 22.882 1.00 13.05 ? 181 VAL A CG1 1 ATOM 1415 C CG2 . VAL A 1 181 ? 21.967 25.861 23.284 1.00 13.11 ? 181 VAL A CG2 1 ATOM 1416 N N . GLN A 1 182 ? 24.700 26.498 19.734 1.00 10.06 ? 182 GLN A N 1 ATOM 1417 C CA . GLN A 1 182 ? 25.739 27.189 18.966 1.00 10.98 ? 182 GLN A CA 1 ATOM 1418 C C . GLN A 1 182 ? 25.306 27.544 17.560 1.00 10.80 ? 182 GLN A C 1 ATOM 1419 O O . GLN A 1 182 ? 25.665 28.618 17.044 1.00 11.96 ? 182 GLN A O 1 ATOM 1420 C CB . GLN A 1 182 ? 27.035 26.390 18.968 1.00 12.24 ? 182 GLN A CB 1 ATOM 1421 C CG . GLN A 1 182 ? 27.733 26.138 20.303 1.00 15.32 ? 182 GLN A CG 1 ATOM 1422 C CD . GLN A 1 182 ? 27.829 27.402 21.132 1.00 17.07 ? 182 GLN A CD 1 ATOM 1423 O OE1 . GLN A 1 182 ? 28.289 28.415 20.565 1.00 19.18 ? 182 GLN A OE1 1 ATOM 1424 N NE2 . GLN A 1 182 ? 27.407 27.409 22.376 1.00 18.97 ? 182 GLN A NE2 1 ATOM 1425 N N . TRP A 1 183 ? 24.582 26.634 16.900 1.00 10.51 ? 183 TRP A N 1 ATOM 1426 C CA . TRP A 1 183 ? 24.093 26.899 15.541 1.00 9.56 ? 183 TRP A CA 1 ATOM 1427 C C . TRP A 1 183 ? 23.107 28.076 15.577 1.00 9.90 ? 183 TRP A C 1 ATOM 1428 O O . TRP A 1 183 ? 23.212 29.009 14.770 1.00 11.37 ? 183 TRP A O 1 ATOM 1429 C CB . TRP A 1 183 ? 23.374 25.618 15.057 1.00 9.88 ? 183 TRP A CB 1 ATOM 1430 C CG . TRP A 1 183 ? 22.677 25.769 13.756 1.00 9.61 ? 183 TRP A CG 1 ATOM 1431 C CD1 . TRP A 1 183 ? 23.256 25.739 12.514 1.00 9.55 ? 183 TRP A CD1 1 ATOM 1432 C CD2 . TRP A 1 183 ? 21.265 25.969 13.547 1.00 9.55 ? 183 TRP A CD2 1 ATOM 1433 N NE1 . TRP A 1 183 ? 22.319 25.958 11.532 1.00 10.15 ? 183 TRP A NE1 1 ATOM 1434 C CE2 . TRP A 1 183 ? 21.088 26.098 12.165 1.00 8.99 ? 183 TRP A CE2 1 ATOM 1435 C CE3 . TRP A 1 183 ? 20.170 26.057 14.415 1.00 10.25 ? 183 TRP A CE3 1 ATOM 1436 C CZ2 . TRP A 1 183 ? 19.812 26.295 11.617 1.00 10.06 ? 183 TRP A CZ2 1 ATOM 1437 C CZ3 . TRP A 1 183 ? 18.916 26.250 13.858 1.00 9.63 ? 183 TRP A CZ3 1 ATOM 1438 C CH2 . TRP A 1 183 ? 18.762 26.370 12.486 1.00 8.61 ? 183 TRP A CH2 1 ATOM 1439 N N . ALA A 1 184 ? 22.149 28.007 16.523 1.00 9.27 ? 184 ALA A N 1 ATOM 1440 C CA . ALA A 1 184 ? 21.152 29.088 16.580 1.00 9.81 ? 184 ALA A CA 1 ATOM 1441 C C . ALA A 1 184 ? 21.770 30.443 16.902 1.00 9.44 ? 184 ALA A C 1 ATOM 1442 O O . ALA A 1 184 ? 21.343 31.473 16.375 1.00 10.60 ? 184 ALA A O 1 ATOM 1443 C CB . ALA A 1 184 ? 20.062 28.715 17.572 1.00 11.44 ? 184 ALA A CB 1 ATOM 1444 N N . THR A 1 185 ? 22.782 30.469 17.743 1.00 10.56 ? 185 THR A N 1 ATOM 1445 C CA . THR A 1 185 ? 23.525 31.682 18.061 1.00 11.04 ? 185 THR A CA 1 ATOM 1446 C C . THR A 1 185 ? 24.153 32.255 16.804 1.00 10.87 ? 185 THR A C 1 ATOM 1447 O O . THR A 1 185 ? 23.957 33.439 16.460 1.00 11.27 ? 185 THR A O 1 ATOM 1448 C CB . THR A 1 185 ? 24.587 31.371 19.145 1.00 11.57 ? 185 THR A CB 1 ATOM 1449 O OG1 . THR A 1 185 ? 23.914 30.967 20.337 1.00 11.92 ? 185 THR A OG1 1 ATOM 1450 C CG2 . THR A 1 185 ? 25.431 32.597 19.426 1.00 13.91 ? 185 THR A CG2 1 ATOM 1451 N N . SER A 1 186 ? 24.913 31.415 16.090 1.00 9.69 ? 186 SER A N 1 ATOM 1452 C CA . SER A 1 186 ? 25.593 31.892 14.877 1.00 10.52 ? 186 SER A CA 1 ATOM 1453 C C . SER A 1 186 ? 24.623 32.313 13.765 1.00 9.24 ? 186 SER A C 1 ATOM 1454 O O . SER A 1 186 ? 24.811 33.374 13.146 1.00 10.22 ? 186 SER A O 1 ATOM 1455 C CB . SER A 1 186 ? 26.493 30.794 14.328 1.00 13.73 ? 186 SER A CB 1 ATOM 1456 O OG . SER A 1 186 ? 27.272 31.328 13.261 1.00 18.30 ? 186 SER A OG 1 ATOM 1457 N N . VAL A 1 187 ? 23.593 31.504 13.504 1.00 8.81 ? 187 VAL A N 1 ATOM 1458 C CA . VAL A 1 187 ? 22.696 31.851 12.389 1.00 8.68 ? 187 VAL A CA 1 ATOM 1459 C C . VAL A 1 187 ? 21.846 33.055 12.772 1.00 8.54 ? 187 VAL A C 1 ATOM 1460 O O . VAL A 1 187 ? 21.665 33.891 11.869 1.00 9.21 ? 187 VAL A O 1 ATOM 1461 C CB . VAL A 1 187 ? 21.813 30.662 12.012 1.00 8.56 ? 187 VAL A CB 1 ATOM 1462 C CG1 . VAL A 1 187 ? 20.798 30.990 10.943 1.00 10.83 ? 187 VAL A CG1 1 ATOM 1463 C CG2 . VAL A 1 187 ? 22.644 29.484 11.512 1.00 10.19 ? 187 VAL A CG2 1 ATOM 1464 N N . SER A 1 188 ? 21.401 33.203 14.014 1.00 8.33 ? 188 SER A N 1 ATOM 1465 C CA . SER A 1 188 ? 20.580 34.419 14.310 1.00 8.95 ? 188 SER A CA 1 ATOM 1466 C C . SER A 1 188 ? 21.435 35.658 14.223 1.00 8.45 ? 188 SER A C 1 ATOM 1467 O O . SER A 1 188 ? 20.998 36.711 13.791 1.00 9.81 ? 188 SER A O 1 ATOM 1468 C CB . SER A 1 188 ? 19.829 34.248 15.642 1.00 8.74 ? 188 SER A CB 1 ATOM 1469 O OG . SER A 1 188 ? 20.727 34.053 16.730 1.00 9.25 ? 188 SER A OG 1 ATOM 1470 N N . GLN A 1 189 ? 22.701 35.586 14.684 1.00 9.12 ? 189 GLN A N 1 ATOM 1471 C CA . GLN A 1 189 ? 23.629 36.707 14.459 1.00 9.06 ? 189 GLN A CA 1 ATOM 1472 C C . GLN A 1 189 ? 23.746 37.082 12.986 1.00 9.16 ? 189 GLN A C 1 ATOM 1473 O O . GLN A 1 189 ? 23.727 38.269 12.579 1.00 10.90 ? 189 GLN A O 1 ATOM 1474 C CB . GLN A 1 189 ? 25.012 36.400 15.025 1.00 11.63 ? 189 GLN A CB 1 ATOM 1475 C CG . GLN A 1 189 ? 25.143 36.414 16.525 1.00 12.66 ? 189 GLN A CG 1 ATOM 1476 C CD . GLN A 1 189 ? 26.513 35.976 17.022 1.00 14.14 ? 189 GLN A CD 1 ATOM 1477 O OE1 . GLN A 1 189 ? 27.483 35.868 16.258 1.00 19.95 ? 189 GLN A OE1 1 ATOM 1478 N NE2 . GLN A 1 189 ? 26.569 35.785 18.318 1.00 13.56 ? 189 GLN A NE2 1 ATOM 1479 N N . TYR A 1 190 ? 23.830 36.055 12.121 1.00 8.24 ? 190 TYR A N 1 ATOM 1480 C CA . TYR A 1 190 ? 23.905 36.290 10.675 1.00 9.17 ? 190 TYR A CA 1 ATOM 1481 C C . TYR A 1 190 ? 22.656 37.005 10.167 1.00 9.26 ? 190 TYR A C 1 ATOM 1482 O O . TYR A 1 190 ? 22.733 37.962 9.396 1.00 9.62 ? 190 TYR A O 1 ATOM 1483 C CB . TYR A 1 190 ? 24.132 34.976 9.922 1.00 9.89 ? 190 TYR A CB 1 ATOM 1484 C CG . TYR A 1 190 ? 24.249 35.136 8.421 1.00 10.73 ? 190 TYR A CG 1 ATOM 1485 C CD1 . TYR A 1 190 ? 25.202 35.977 7.830 1.00 10.97 ? 190 TYR A CD1 1 ATOM 1486 C CD2 . TYR A 1 190 ? 23.405 34.454 7.560 1.00 11.47 ? 190 TYR A CD2 1 ATOM 1487 C CE1 . TYR A 1 190 ? 25.277 36.147 6.478 1.00 12.94 ? 190 TYR A CE1 1 ATOM 1488 C CE2 . TYR A 1 190 ? 23.500 34.580 6.182 1.00 12.45 ? 190 TYR A CE2 1 ATOM 1489 C CZ . TYR A 1 190 ? 24.427 35.442 5.648 1.00 12.61 ? 190 TYR A CZ 1 ATOM 1490 O OH . TYR A 1 190 ? 24.491 35.603 4.279 1.00 14.31 ? 190 TYR A OH 1 ATOM 1491 N N . VAL A 1 191 ? 21.465 36.508 10.558 1.00 9.38 ? 191 VAL A N 1 ATOM 1492 C CA . VAL A 1 191 ? 20.228 37.180 10.125 1.00 9.86 ? 191 VAL A CA 1 ATOM 1493 C C . VAL A 1 191 ? 20.200 38.626 10.583 1.00 9.89 ? 191 VAL A C 1 ATOM 1494 O O . VAL A 1 191 ? 19.857 39.518 9.770 1.00 10.01 ? 191 VAL A O 1 ATOM 1495 C CB . VAL A 1 191 ? 19.023 36.400 10.642 1.00 10.73 ? 191 VAL A CB 1 ATOM 1496 C CG1 . VAL A 1 191 ? 17.732 37.126 10.208 1.00 9.32 ? 191 VAL A CG1 1 ATOM 1497 C CG2 . VAL A 1 191 ? 18.937 34.993 10.082 1.00 9.68 ? 191 VAL A CG2 1 ATOM 1498 N N . LYS A 1 192 ? 20.612 38.899 11.812 1.00 10.23 ? 192 LYS A N 1 ATOM 1499 C CA . LYS A 1 192 ? 20.643 40.301 12.308 1.00 10.12 ? 192 LYS A CA 1 ATOM 1500 C C . LYS A 1 192 ? 21.624 41.164 11.511 1.00 10.46 ? 192 LYS A C 1 ATOM 1501 O O . LYS A 1 192 ? 21.438 42.373 11.340 1.00 13.86 ? 192 LYS A O 1 ATOM 1502 C CB . LYS A 1 192 ? 20.947 40.299 13.810 1.00 11.40 ? 192 LYS A CB 1 ATOM 1503 C CG . LYS A 1 192 ? 19.827 39.721 14.680 1.00 12.32 ? 192 LYS A CG 1 ATOM 1504 C CD . LYS A 1 192 ? 18.584 40.595 14.691 1.00 12.89 ? 192 LYS A CD 1 ATOM 1505 C CE . LYS A 1 192 ? 17.656 40.182 15.835 1.00 13.93 ? 192 LYS A CE 1 ATOM 1506 N NZ . LYS A 1 192 ? 16.425 41.036 15.903 1.00 15.41 ? 192 LYS A NZ 1 ATOM 1507 N N . SER A 1 193 ? 22.687 40.555 10.967 1.00 10.83 ? 193 SER A N 1 ATOM 1508 C CA . SER A 1 193 ? 23.645 41.274 10.120 1.00 10.04 ? 193 SER A CA 1 ATOM 1509 C C . SER A 1 193 ? 23.104 41.639 8.740 1.00 10.63 ? 193 SER A C 1 ATOM 1510 O O . SER A 1 193 ? 23.663 42.540 8.103 1.00 12.26 ? 193 SER A O 1 ATOM 1511 C CB . SER A 1 193 ? 24.942 40.459 9.999 1.00 10.85 ? 193 SER A CB 1 ATOM 1512 O OG . SER A 1 193 ? 24.906 39.491 8.975 1.00 12.08 ? 193 SER A OG 1 ATOM 1513 N N . LEU A 1 194 ? 22.034 40.938 8.328 1.00 10.22 ? 194 LEU A N 1 ATOM 1514 C CA . LEU A 1 194 ? 21.403 41.201 7.054 1.00 9.90 ? 194 LEU A CA 1 ATOM 1515 C C . LEU A 1 194 ? 20.202 42.144 7.158 1.00 9.33 ? 194 LEU A C 1 ATOM 1516 O O . LEU A 1 194 ? 19.776 42.663 6.131 1.00 10.78 ? 194 LEU A O 1 ATOM 1517 C CB . LEU A 1 194 ? 20.860 39.875 6.486 1.00 9.11 ? 194 LEU A CB 1 ATOM 1518 C CG . LEU A 1 194 ? 21.907 38.801 6.212 1.00 10.72 ? 194 LEU A CG 1 ATOM 1519 C CD1 . LEU A 1 194 ? 21.248 37.539 5.669 1.00 13.80 ? 194 LEU A CD1 1 ATOM 1520 C CD2 . LEU A 1 194 ? 22.982 39.331 5.252 1.00 15.07 ? 194 LEU A CD2 1 ATOM 1521 N N . ASP A 1 195 ? 19.651 42.240 8.342 1.00 8.92 ? 195 ASP A N 1 ATOM 1522 C CA . ASP A 1 195 ? 18.375 42.955 8.530 1.00 8.77 ? 195 ASP A CA 1 ATOM 1523 C C . ASP A 1 195 ? 18.306 43.372 9.996 1.00 9.80 ? 195 ASP A C 1 ATOM 1524 O O . ASP A 1 195 ? 18.178 42.559 10.913 1.00 10.17 ? 195 ASP A O 1 ATOM 1525 C CB . ASP A 1 195 ? 17.237 41.977 8.202 1.00 10.29 ? 195 ASP A CB 1 ATOM 1526 C CG . ASP A 1 195 ? 15.836 42.518 8.401 1.00 10.42 ? 195 ASP A CG 1 ATOM 1527 O OD1 . ASP A 1 195 ? 15.591 43.500 9.107 1.00 9.91 ? 195 ASP A OD1 1 ATOM 1528 O OD2 . ASP A 1 195 ? 14.904 41.849 7.852 1.00 10.13 ? 195 ASP A OD2 1 ATOM 1529 N N . SER A 1 196 ? 18.314 44.696 10.239 1.00 9.22 ? 196 SER A N 1 ATOM 1530 C CA . SER A 1 196 ? 18.193 45.228 11.588 1.00 10.55 ? 196 SER A CA 1 ATOM 1531 C C . SER A 1 196 ? 16.795 45.748 11.927 1.00 12.14 ? 196 SER A C 1 ATOM 1532 O O . SER A 1 196 ? 16.576 46.367 12.967 1.00 14.17 ? 196 SER A O 1 ATOM 1533 C CB . SER A 1 196 ? 19.191 46.371 11.834 1.00 12.12 ? 196 SER A CB 1 ATOM 1534 O OG . SER A 1 196 ? 18.902 47.479 11.023 1.00 15.21 ? 196 SER A OG 1 ATOM 1535 N N . ASN A 1 197 ? 15.851 45.501 10.989 1.00 10.04 ? 197 ASN A N 1 ATOM 1536 C CA . ASN A 1 197 ? 14.483 45.949 11.224 1.00 9.87 ? 197 ASN A CA 1 ATOM 1537 C C . ASN A 1 197 ? 13.593 44.896 11.888 1.00 10.35 ? 197 ASN A C 1 ATOM 1538 O O . ASN A 1 197 ? 12.621 45.301 12.528 1.00 11.10 ? 197 ASN A O 1 ATOM 1539 C CB . ASN A 1 197 ? 13.826 46.264 9.860 1.00 9.55 ? 197 ASN A CB 1 ATOM 1540 C CG . ASN A 1 197 ? 14.548 47.375 9.109 1.00 9.16 ? 197 ASN A CG 1 ATOM 1541 O OD1 . ASN A 1 197 ? 14.911 48.391 9.709 1.00 12.00 ? 197 ASN A OD1 1 ATOM 1542 N ND2 . ASN A 1 197 ? 14.767 47.135 7.817 1.00 10.41 ? 197 ASN A ND2 1 ATOM 1543 N N . HIS A 1 198 ? 13.930 43.626 11.702 1.00 9.87 ? 198 HIS A N 1 ATOM 1544 C CA . HIS A 1 198 ? 13.010 42.558 12.105 1.00 8.76 ? 198 HIS A CA 1 ATOM 1545 C C . HIS A 1 198 ? 13.440 41.671 13.249 1.00 8.72 ? 198 HIS A C 1 ATOM 1546 O O . HIS A 1 198 ? 14.623 41.386 13.502 1.00 10.66 ? 198 HIS A O 1 ATOM 1547 C CB . HIS A 1 198 ? 12.715 41.680 10.871 1.00 8.83 ? 198 HIS A CB 1 ATOM 1548 C CG . HIS A 1 198 ? 11.983 42.386 9.770 1.00 8.89 ? 198 HIS A CG 1 ATOM 1549 N ND1 . HIS A 1 198 ? 10.722 42.965 9.870 1.00 11.43 ? 198 HIS A ND1 1 ATOM 1550 C CD2 . HIS A 1 198 ? 12.422 42.608 8.526 1.00 7.45 ? 198 HIS A CD2 1 ATOM 1551 C CE1 . HIS A 1 198 ? 10.472 43.516 8.667 1.00 6.74 ? 198 HIS A CE1 1 ATOM 1552 N NE2 . HIS A 1 198 ? 11.462 43.262 7.836 1.00 11.65 ? 198 HIS A NE2 1 ATOM 1553 N N . LEU A 1 199 ? 12.449 41.131 13.949 1.00 7.94 ? 199 LEU A N 1 ATOM 1554 C CA . LEU A 1 199 ? 12.593 40.151 15.011 1.00 7.83 ? 199 LEU A CA 1 ATOM 1555 C C . LEU A 1 199 ? 13.035 38.806 14.425 1.00 8.22 ? 199 LEU A C 1 ATOM 1556 O O . LEU A 1 199 ? 12.806 38.517 13.262 1.00 8.55 ? 199 LEU A O 1 ATOM 1557 C CB . LEU A 1 199 ? 11.256 39.921 15.717 1.00 8.59 ? 199 LEU A CB 1 ATOM 1558 C CG . LEU A 1 199 ? 10.651 41.154 16.366 1.00 9.05 ? 199 LEU A CG 1 ATOM 1559 C CD1 . LEU A 1 199 ? 9.242 40.815 16.886 1.00 10.15 ? 199 LEU A CD1 1 ATOM 1560 C CD2 . LEU A 1 199 ? 11.544 41.698 17.457 1.00 10.12 ? 199 LEU A CD2 1 ATOM 1561 N N . VAL A 1 200 ? 13.768 37.997 15.195 1.00 8.95 ? 200 VAL A N 1 ATOM 1562 C CA . VAL A 1 200 ? 14.249 36.665 14.831 1.00 8.37 ? 200 VAL A CA 1 ATOM 1563 C C . VAL A 1 200 ? 13.868 35.668 15.945 1.00 7.74 ? 200 VAL A C 1 ATOM 1564 O O . VAL A 1 200 ? 13.981 35.983 17.128 1.00 8.72 ? 200 VAL A O 1 ATOM 1565 C CB . VAL A 1 200 ? 15.754 36.670 14.611 1.00 7.99 ? 200 VAL A CB 1 ATOM 1566 C CG1 . VAL A 1 200 ? 16.293 35.308 14.178 1.00 9.18 ? 200 VAL A CG1 1 ATOM 1567 C CG2 . VAL A 1 200 ? 16.194 37.733 13.586 1.00 8.92 ? 200 VAL A CG2 1 ATOM 1568 N N . THR A 1 201 ? 13.485 34.460 15.561 1.00 8.04 ? 201 THR A N 1 ATOM 1569 C CA . THR A 1 201 ? 13.120 33.404 16.508 1.00 7.82 ? 201 THR A CA 1 ATOM 1570 C C . THR A 1 201 ? 13.635 32.059 15.983 1.00 7.25 ? 201 THR A C 1 ATOM 1571 O O . THR A 1 201 ? 13.940 31.886 14.813 1.00 7.98 ? 201 THR A O 1 ATOM 1572 C CB . THR A 1 201 ? 11.609 33.427 16.819 1.00 8.13 ? 201 THR A CB 1 ATOM 1573 O OG1 . THR A 1 201 ? 11.350 32.552 17.917 1.00 9.48 ? 201 THR A OG1 1 ATOM 1574 C CG2 . THR A 1 201 ? 10.825 33.003 15.613 1.00 8.77 ? 201 THR A CG2 1 ATOM 1575 N N . LEU A 1 202 ? 13.647 31.042 16.859 1.00 7.88 ? 202 LEU A N 1 ATOM 1576 C CA . LEU A 1 202 ? 14.195 29.747 16.478 1.00 7.47 ? 202 LEU A CA 1 ATOM 1577 C C . LEU A 1 202 ? 13.216 28.897 15.655 1.00 8.41 ? 202 LEU A C 1 ATOM 1578 O O . LEU A 1 202 ? 13.638 28.251 14.683 1.00 8.82 ? 202 LEU A O 1 ATOM 1579 C CB . LEU A 1 202 ? 14.635 29.015 17.753 1.00 8.71 ? 202 LEU A CB 1 ATOM 1580 C CG . LEU A 1 202 ? 15.255 27.609 17.599 1.00 8.23 ? 202 LEU A CG 1 ATOM 1581 C CD1 . LEU A 1 202 ? 16.392 27.562 16.576 1.00 8.43 ? 202 LEU A CD1 1 ATOM 1582 C CD2 . LEU A 1 202 ? 15.772 27.102 18.946 1.00 9.68 ? 202 LEU A CD2 1 ATOM 1583 N N . GLY A 1 203 ? 11.938 28.787 16.081 1.00 7.11 ? 203 GLY A N 1 ATOM 1584 C CA . GLY A 1 203 ? 10.982 27.914 15.448 1.00 7.70 ? 203 GLY A CA 1 ATOM 1585 C C . GLY A 1 203 ? 10.868 26.521 16.053 1.00 7.34 ? 203 GLY A C 1 ATOM 1586 O O . GLY A 1 203 ? 10.231 25.623 15.462 1.00 8.31 ? 203 GLY A O 1 ATOM 1587 N N . ASP A 1 204 ? 11.578 26.290 17.162 1.00 7.86 ? 204 ASP A N 1 ATOM 1588 C CA . ASP A 1 204 ? 11.487 24.997 17.839 1.00 7.70 ? 204 ASP A CA 1 ATOM 1589 C C . ASP A 1 204 ? 10.139 24.753 18.471 1.00 8.13 ? 204 ASP A C 1 ATOM 1590 O O . ASP A 1 204 ? 9.287 25.635 18.674 1.00 7.93 ? 204 ASP A O 1 ATOM 1591 C CB . ASP A 1 204 ? 12.599 24.929 18.919 1.00 9.26 ? 204 ASP A CB 1 ATOM 1592 C CG . ASP A 1 204 ? 12.403 25.970 20.000 1.00 11.89 ? 204 ASP A CG 1 ATOM 1593 O OD1 . ASP A 1 204 ? 12.302 27.166 19.624 1.00 11.98 ? 204 ASP A OD1 1 ATOM 1594 O OD2 . ASP A 1 204 ? 12.300 25.601 21.205 1.00 13.95 ? 204 ASP A OD2 1 ATOM 1595 N N . GLU A 1 205 ? 9.899 23.491 18.807 1.00 8.24 ? 205 GLU A N 1 ATOM 1596 C CA . GLU A 1 205 ? 8.697 23.018 19.472 1.00 8.63 ? 205 GLU A CA 1 ATOM 1597 C C . GLU A 1 205 ? 8.651 23.268 20.964 1.00 8.73 ? 205 GLU A C 1 ATOM 1598 O O . GLU A 1 205 ? 7.600 23.088 21.586 1.00 8.40 ? 205 GLU A O 1 ATOM 1599 C CB . GLU A 1 205 ? 8.609 21.485 19.269 1.00 8.57 ? 205 GLU A CB 1 ATOM 1600 C CG . GLU A 1 205 ? 8.456 21.058 17.824 1.00 7.94 ? 205 GLU A CG 1 ATOM 1601 C CD . GLU A 1 205 ? 8.910 19.628 17.634 1.00 8.05 ? 205 GLU A CD 1 ATOM 1602 O OE1 . GLU A 1 205 ? 10.125 19.391 17.506 1.00 10.63 ? 205 GLU A OE1 1 ATOM 1603 O OE2 . GLU A 1 205 ? 8.039 18.677 17.635 1.00 9.45 ? 205 GLU A OE2 1 ATOM 1604 N N . GLY A 1 206 ? 9.788 23.662 21.560 1.00 9.08 ? 206 GLY A N 1 ATOM 1605 C CA . GLY A 1 206 ? 9.876 23.907 22.973 1.00 9.86 ? 206 GLY A CA 1 ATOM 1606 C C . GLY A 1 206 ? 10.308 22.695 23.785 1.00 8.62 ? 206 GLY A C 1 ATOM 1607 O O . GLY A 1 206 ? 10.203 22.707 25.020 1.00 9.80 ? 206 GLY A O 1 ATOM 1608 N N . LEU A 1 207 ? 10.818 21.654 23.118 1.00 7.90 ? 207 LEU A N 1 ATOM 1609 C CA . LEU A 1 207 ? 11.200 20.466 23.893 1.00 7.60 ? 207 LEU A CA 1 ATOM 1610 C C . LEU A 1 207 ? 12.396 20.740 24.805 1.00 9.22 ? 207 LEU A C 1 ATOM 1611 O O . LEU A 1 207 ? 13.273 21.554 24.507 1.00 9.62 ? 207 LEU A O 1 ATOM 1612 C CB . LEU A 1 207 ? 11.493 19.286 22.962 1.00 8.09 ? 207 LEU A CB 1 ATOM 1613 C CG . LEU A 1 207 ? 10.451 19.022 21.840 1.00 8.47 ? 207 LEU A CG 1 ATOM 1614 C CD1 . LEU A 1 207 ? 10.917 17.858 20.952 1.00 8.59 ? 207 LEU A CD1 1 ATOM 1615 C CD2 . LEU A 1 207 ? 9.075 18.793 22.396 1.00 9.32 ? 207 LEU A CD2 1 ATOM 1616 N N . GLY A 1 208 ? 12.430 20.071 25.943 1.00 9.04 ? 208 GLY A N 1 ATOM 1617 C CA . GLY A 1 208 ? 13.493 20.143 26.919 1.00 9.77 ? 208 GLY A CA 1 ATOM 1618 C C . GLY A 1 208 ? 13.288 21.276 27.902 1.00 10.01 ? 208 GLY A C 1 ATOM 1619 O O . GLY A 1 208 ? 13.788 22.389 27.670 1.00 10.82 ? 208 GLY A O 1 ATOM 1620 N N . LEU A 1 209 ? 12.581 21.020 28.994 1.00 9.74 ? 209 LEU A N 1 ATOM 1621 C CA . LEU A 1 209 ? 12.281 22.042 30.003 1.00 9.82 ? 209 LEU A CA 1 ATOM 1622 C C . LEU A 1 209 ? 12.038 21.316 31.319 1.00 12.25 ? 209 LEU A C 1 ATOM 1623 O O . LEU A 1 209 ? 11.153 20.471 31.426 1.00 12.56 ? 209 LEU A O 1 ATOM 1624 C CB . LEU A 1 209 ? 11.092 22.888 29.523 1.00 10.45 ? 209 LEU A CB 1 ATOM 1625 C CG . LEU A 1 209 ? 10.614 24.019 30.421 1.00 10.54 ? 209 LEU A CG 1 ATOM 1626 C CD1 . LEU A 1 209 ? 11.740 25.001 30.719 1.00 11.24 ? 209 LEU A CD1 1 ATOM 1627 C CD2 . LEU A 1 209 ? 9.429 24.778 29.851 1.00 12.13 ? 209 LEU A CD2 1 ATOM 1628 N N . SER A 1 210 ? 12.833 21.650 32.332 1.00 12.45 ? 210 SER A N 1 ATOM 1629 C CA . SER A 1 210 ? 12.859 20.871 33.568 1.00 14.17 ? 210 SER A CA 1 ATOM 1630 C C . SER A 1 210 ? 11.772 21.150 34.587 1.00 14.16 ? 210 SER A C 1 ATOM 1631 O O . SER A 1 210 ? 11.633 20.450 35.602 1.00 17.05 ? 210 SER A O 1 ATOM 1632 C CB . SER A 1 210 ? 14.279 21.038 34.164 1.00 15.82 ? 210 SER A CB 1 ATOM 1633 O OG . SER A 1 210 ? 15.212 20.332 33.313 1.00 16.08 ? 210 SER A OG 1 ATOM 1634 N N . THR A 1 211 ? 10.915 22.134 34.318 1.00 14.53 ? 211 THR A N 1 ATOM 1635 C CA . THR A 1 211 ? 9.855 22.523 35.235 1.00 14.94 ? 211 THR A CA 1 ATOM 1636 C C . THR A 1 211 ? 8.533 21.805 34.999 1.00 14.43 ? 211 THR A C 1 ATOM 1637 O O . THR A 1 211 ? 7.528 22.107 35.628 1.00 14.86 ? 211 THR A O 1 ATOM 1638 C CB . THR A 1 211 ? 9.622 24.044 35.092 1.00 15.07 ? 211 THR A CB 1 ATOM 1639 O OG1 . THR A 1 211 ? 9.433 24.299 33.697 1.00 13.39 ? 211 THR A OG1 1 ATOM 1640 C CG2 . THR A 1 211 ? 10.799 24.846 35.620 1.00 15.98 ? 211 THR A CG2 1 ATOM 1641 N N . GLY A 1 212 ? 8.523 20.831 34.112 1.00 14.73 ? 212 GLY A N 1 ATOM 1642 C CA . GLY A 1 212 ? 7.363 20.048 33.762 1.00 15.73 ? 212 GLY A CA 1 ATOM 1643 C C . GLY A 1 212 ? 7.164 18.805 34.608 1.00 16.10 ? 212 GLY A C 1 ATOM 1644 O O . GLY A 1 212 ? 7.712 18.727 35.706 1.00 17.98 ? 212 GLY A O 1 ATOM 1645 N N . ASP A 1 213 ? 6.425 17.864 34.021 1.00 14.25 ? 213 ASP A N 1 ATOM 1646 C CA . ASP A 1 213 ? 6.054 16.628 34.722 1.00 14.86 ? 213 ASP A CA 1 ATOM 1647 C C . ASP A 1 213 ? 6.882 15.435 34.295 1.00 15.23 ? 213 ASP A C 1 ATOM 1648 O O . ASP A 1 213 ? 6.541 14.330 34.659 1.00 17.17 ? 213 ASP A O 1 ATOM 1649 C CB . ASP A 1 213 ? 4.579 16.366 34.527 1.00 15.97 ? 213 ASP A CB 1 ATOM 1650 C CG . ASP A 1 213 ? 4.138 15.884 33.162 1.00 15.86 ? 213 ASP A CG 1 ATOM 1651 O OD1 . ASP A 1 213 ? 4.908 15.994 32.191 1.00 14.05 ? 213 ASP A OD1 1 ATOM 1652 O OD2 . ASP A 1 213 ? 2.983 15.410 33.068 1.00 18.72 ? 213 ASP A OD2 1 ATOM 1653 N N . GLY A 1 214 ? 7.943 15.631 33.524 1.00 14.13 ? 214 GLY A N 1 ATOM 1654 C CA . GLY A 1 214 ? 8.781 14.502 33.133 1.00 14.73 ? 214 GLY A CA 1 ATOM 1655 C C . GLY A 1 214 ? 8.306 13.708 31.954 1.00 12.73 ? 214 GLY A C 1 ATOM 1656 O O . GLY A 1 214 ? 9.015 12.747 31.542 1.00 14.89 ? 214 GLY A O 1 ATOM 1657 N N . ALA A 1 215 ? 7.204 14.067 31.307 1.00 12.44 ? 215 ALA A N 1 ATOM 1658 C CA . ALA A 1 215 ? 6.811 13.413 30.065 1.00 12.07 ? 215 ALA A CA 1 ATOM 1659 C C . ALA A 1 215 ? 7.909 13.642 29.027 1.00 11.10 ? 215 ALA A C 1 ATOM 1660 O O . ALA A 1 215 ? 8.664 14.619 29.071 1.00 10.57 ? 215 ALA A O 1 ATOM 1661 C CB . ALA A 1 215 ? 5.472 13.941 29.564 1.00 12.19 ? 215 ALA A CB 1 ATOM 1662 N N . TYR A 1 216 ? 8.004 12.773 28.011 1.00 11.02 ? 216 TYR A N 1 ATOM 1663 C CA . TYR A 1 216 ? 9.064 12.867 27.011 1.00 10.55 ? 216 TYR A CA 1 ATOM 1664 C C . TYR A 1 216 ? 9.286 14.240 26.419 1.00 9.56 ? 216 TYR A C 1 ATOM 1665 O O . TYR A 1 216 ? 10.460 14.643 26.328 1.00 10.16 ? 216 TYR A O 1 ATOM 1666 C CB . TYR A 1 216 ? 8.948 11.805 25.918 1.00 9.79 ? 216 TYR A CB 1 ATOM 1667 C CG . TYR A 1 216 ? 10.122 11.854 24.943 1.00 8.80 ? 216 TYR A CG 1 ATOM 1668 C CD1 . TYR A 1 216 ? 11.358 11.332 25.306 1.00 10.14 ? 216 TYR A CD1 1 ATOM 1669 C CD2 . TYR A 1 216 ? 10.001 12.417 23.676 1.00 11.21 ? 216 TYR A CD2 1 ATOM 1670 C CE1 . TYR A 1 216 ? 12.417 11.367 24.434 1.00 11.23 ? 216 TYR A CE1 1 ATOM 1671 C CE2 . TYR A 1 216 ? 11.085 12.495 22.807 1.00 11.87 ? 216 TYR A CE2 1 ATOM 1672 C CZ . TYR A 1 216 ? 12.291 11.927 23.171 1.00 12.18 ? 216 TYR A CZ 1 ATOM 1673 O OH . TYR A 1 216 ? 13.390 11.969 22.330 1.00 12.63 ? 216 TYR A OH 1 ATOM 1674 N N . PRO A 1 217 ? 8.270 15.042 26.077 1.00 9.36 ? 217 PRO A N 1 ATOM 1675 C CA . PRO A 1 217 ? 8.548 16.362 25.499 1.00 8.61 ? 217 PRO A CA 1 ATOM 1676 C C . PRO A 1 217 ? 9.319 17.264 26.426 1.00 9.13 ? 217 PRO A C 1 ATOM 1677 O O . PRO A 1 217 ? 10.010 18.180 25.922 1.00 9.31 ? 217 PRO A O 1 ATOM 1678 C CB . PRO A 1 217 ? 7.152 16.916 25.235 1.00 9.05 ? 217 PRO A CB 1 ATOM 1679 C CG . PRO A 1 217 ? 6.310 15.683 25.012 1.00 9.66 ? 217 PRO A CG 1 ATOM 1680 C CD . PRO A 1 217 ? 6.845 14.677 26.005 1.00 9.23 ? 217 PRO A CD 1 ATOM 1681 N N . TYR A 1 218 ? 9.224 17.104 27.764 1.00 8.73 ? 218 TYR A N 1 ATOM 1682 C CA . TYR A 1 218 ? 10.028 17.907 28.691 1.00 9.76 ? 218 TYR A CA 1 ATOM 1683 C C . TYR A 1 218 ? 11.460 17.363 28.855 1.00 9.95 ? 218 TYR A C 1 ATOM 1684 O O . TYR A 1 218 ? 12.283 18.133 29.366 1.00 10.47 ? 218 TYR A O 1 ATOM 1685 C CB . TYR A 1 218 ? 9.337 17.879 30.066 1.00 10.75 ? 218 TYR A CB 1 ATOM 1686 C CG . TYR A 1 218 ? 8.073 18.716 30.232 1.00 9.60 ? 218 TYR A CG 1 ATOM 1687 C CD1 . TYR A 1 218 ? 8.162 20.096 30.177 1.00 10.70 ? 218 TYR A CD1 1 ATOM 1688 C CD2 . TYR A 1 218 ? 6.840 18.117 30.488 1.00 9.98 ? 218 TYR A CD2 1 ATOM 1689 C CE1 . TYR A 1 218 ? 7.036 20.889 30.376 1.00 11.05 ? 218 TYR A CE1 1 ATOM 1690 C CE2 . TYR A 1 218 ? 5.714 18.901 30.672 1.00 10.63 ? 218 TYR A CE2 1 ATOM 1691 C CZ . TYR A 1 218 ? 5.812 20.271 30.596 1.00 11.68 ? 218 TYR A CZ 1 ATOM 1692 O OH . TYR A 1 218 ? 4.700 21.081 30.803 1.00 11.89 ? 218 TYR A OH 1 ATOM 1693 N N . THR A 1 219 ? 11.750 16.132 28.422 1.00 11.18 ? 219 THR A N 1 ATOM 1694 C CA . THR A 1 219 ? 13.123 15.618 28.561 1.00 13.43 ? 219 THR A CA 1 ATOM 1695 C C . THR A 1 219 ? 13.997 16.168 27.435 1.00 13.02 ? 219 THR A C 1 ATOM 1696 O O . THR A 1 219 ? 13.586 16.940 26.563 1.00 10.38 ? 219 THR A O 1 ATOM 1697 C CB . THR A 1 219 ? 13.063 14.067 28.523 1.00 18.53 ? 219 THR A CB 1 ATOM 1698 O OG1 A THR A 1 219 ? 12.255 13.536 29.569 0.50 15.32 ? 219 THR A OG1 1 ATOM 1699 O OG1 B THR A 1 219 ? 14.033 13.588 29.425 0.50 23.65 ? 219 THR A OG1 1 ATOM 1700 C CG2 A THR A 1 219 ? 14.446 13.405 28.575 0.50 19.15 ? 219 THR A CG2 1 ATOM 1701 C CG2 B THR A 1 219 ? 13.003 13.614 27.106 0.50 11.40 ? 219 THR A CG2 1 ATOM 1702 N N . TYR A 1 220 ? 15.266 15.781 27.444 1.00 14.25 ? 220 TYR A N 1 ATOM 1703 C CA . TYR A 1 220 ? 16.298 16.261 26.517 1.00 13.39 ? 220 TYR A CA 1 ATOM 1704 C C . TYR A 1 220 ? 16.731 15.177 25.545 1.00 15.40 ? 220 TYR A C 1 ATOM 1705 O O . TYR A 1 220 ? 17.912 14.861 25.357 1.00 19.86 ? 220 TYR A O 1 ATOM 1706 C CB . TYR A 1 220 ? 17.511 16.796 27.298 1.00 13.62 ? 220 TYR A CB 1 ATOM 1707 C CG . TYR A 1 220 ? 17.049 17.900 28.240 1.00 13.23 ? 220 TYR A CG 1 ATOM 1708 C CD1 . TYR A 1 220 ? 16.951 19.212 27.812 1.00 12.13 ? 220 TYR A CD1 1 ATOM 1709 C CD2 . TYR A 1 220 ? 16.660 17.609 29.541 1.00 15.97 ? 220 TYR A CD2 1 ATOM 1710 C CE1 . TYR A 1 220 ? 16.504 20.193 28.640 1.00 11.42 ? 220 TYR A CE1 1 ATOM 1711 C CE2 . TYR A 1 220 ? 16.179 18.617 30.380 1.00 15.95 ? 220 TYR A CE2 1 ATOM 1712 C CZ . TYR A 1 220 ? 16.120 19.926 29.933 1.00 13.53 ? 220 TYR A CZ 1 ATOM 1713 O OH . TYR A 1 220 ? 15.712 20.929 30.761 1.00 15.75 ? 220 TYR A OH 1 ATOM 1714 N N . GLY A 1 221 ? 15.775 14.524 24.873 1.00 11.97 ? 221 GLY A N 1 ATOM 1715 C CA . GLY A 1 221 ? 16.060 13.531 23.887 1.00 12.33 ? 221 GLY A CA 1 ATOM 1716 C C . GLY A 1 221 ? 16.157 14.029 22.448 1.00 10.14 ? 221 GLY A C 1 ATOM 1717 O O . GLY A 1 221 ? 16.601 13.303 21.545 1.00 12.08 ? 221 GLY A O 1 ATOM 1718 N N . GLU A 1 222 ? 15.725 15.283 22.213 1.00 9.65 ? 222 GLU A N 1 ATOM 1719 C CA . GLU A 1 222 ? 15.676 15.853 20.887 1.00 10.07 ? 222 GLU A CA 1 ATOM 1720 C C . GLU A 1 222 ? 16.664 16.974 20.657 1.00 9.07 ? 222 GLU A C 1 ATOM 1721 O O . GLU A 1 222 ? 16.578 17.724 19.674 1.00 10.29 ? 222 GLU A O 1 ATOM 1722 C CB . GLU A 1 222 ? 14.241 16.298 20.531 1.00 9.42 ? 222 GLU A CB 1 ATOM 1723 C CG . GLU A 1 222 ? 13.294 15.100 20.553 1.00 10.09 ? 222 GLU A CG 1 ATOM 1724 C CD . GLU A 1 222 ? 13.619 13.945 19.619 1.00 10.60 ? 222 GLU A CD 1 ATOM 1725 O OE1 . GLU A 1 222 ? 14.313 14.139 18.612 1.00 10.90 ? 222 GLU A OE1 1 ATOM 1726 O OE2 . GLU A 1 222 ? 13.109 12.824 19.899 1.00 11.59 ? 222 GLU A OE2 1 ATOM 1727 N N . GLY A 1 223 ? 17.679 17.052 21.528 1.00 10.59 ? 223 GLY A N 1 ATOM 1728 C CA . GLY A 1 223 ? 18.738 18.034 21.322 1.00 10.96 ? 223 GLY A CA 1 ATOM 1729 C C . GLY A 1 223 ? 18.399 19.467 21.599 1.00 10.22 ? 223 GLY A C 1 ATOM 1730 O O . GLY A 1 223 ? 19.179 20.373 21.255 1.00 12.09 ? 223 GLY A O 1 ATOM 1731 N N . THR A 1 224 ? 17.267 19.755 22.218 1.00 9.79 ? 224 THR A N 1 ATOM 1732 C CA . THR A 1 224 ? 16.924 21.147 22.509 1.00 8.85 ? 224 THR A CA 1 ATOM 1733 C C . THR A 1 224 ? 16.728 21.350 24.003 1.00 9.61 ? 224 THR A C 1 ATOM 1734 O O . THR A 1 224 ? 16.240 20.482 24.736 1.00 10.32 ? 224 THR A O 1 ATOM 1735 C CB . THR A 1 224 ? 15.682 21.644 21.741 1.00 9.04 ? 224 THR A CB 1 ATOM 1736 O OG1 . THR A 1 224 ? 14.544 20.852 22.092 1.00 10.19 ? 224 THR A OG1 1 ATOM 1737 C CG2 . THR A 1 224 ? 15.862 21.533 20.228 1.00 10.31 ? 224 THR A CG2 1 ATOM 1738 N N . ASP A 1 225 ? 17.141 22.525 24.513 1.00 10.23 ? 225 ASP A N 1 ATOM 1739 C CA . ASP A 1 225 ? 16.961 23.001 25.883 1.00 10.43 ? 225 ASP A CA 1 ATOM 1740 C C . ASP A 1 225 ? 16.293 24.388 25.740 1.00 9.55 ? 225 ASP A C 1 ATOM 1741 O O . ASP A 1 225 ? 16.917 25.355 25.325 1.00 10.36 ? 225 ASP A O 1 ATOM 1742 C CB . ASP A 1 225 ? 18.330 23.093 26.561 1.00 11.33 ? 225 ASP A CB 1 ATOM 1743 C CG . ASP A 1 225 ? 18.299 23.522 28.018 1.00 13.14 ? 225 ASP A CG 1 ATOM 1744 O OD1 . ASP A 1 225 ? 17.494 24.441 28.294 1.00 14.56 ? 225 ASP A OD1 1 ATOM 1745 O OD2 . ASP A 1 225 ? 19.097 23.014 28.834 1.00 15.96 ? 225 ASP A OD2 1 ATOM 1746 N N . PHE A 1 226 ? 15.007 24.406 26.038 1.00 8.97 ? 226 PHE A N 1 ATOM 1747 C CA . PHE A 1 226 ? 14.217 25.615 25.863 1.00 10.09 ? 226 PHE A CA 1 ATOM 1748 C C . PHE A 1 226 ? 14.774 26.827 26.584 1.00 11.07 ? 226 PHE A C 1 ATOM 1749 O O . PHE A 1 226 ? 14.880 27.869 25.947 1.00 12.19 ? 226 PHE A O 1 ATOM 1750 C CB . PHE A 1 226 ? 12.756 25.385 26.268 1.00 11.35 ? 226 PHE A CB 1 ATOM 1751 C CG . PHE A 1 226 ? 11.832 26.511 25.884 1.00 9.85 ? 226 PHE A CG 1 ATOM 1752 C CD1 . PHE A 1 226 ? 11.499 26.754 24.552 1.00 9.49 ? 226 PHE A CD1 1 ATOM 1753 C CD2 . PHE A 1 226 ? 11.324 27.395 26.852 1.00 9.75 ? 226 PHE A CD2 1 ATOM 1754 C CE1 . PHE A 1 226 ? 10.652 27.792 24.199 1.00 8.36 ? 226 PHE A CE1 1 ATOM 1755 C CE2 . PHE A 1 226 ? 10.454 28.417 26.499 1.00 10.25 ? 226 PHE A CE2 1 ATOM 1756 C CZ . PHE A 1 226 ? 10.129 28.613 25.172 1.00 10.25 ? 226 PHE A CZ 1 ATOM 1757 N N . ALA A 1 227 ? 15.074 26.695 27.859 1.00 12.19 ? 227 ALA A N 1 ATOM 1758 C CA . ALA A 1 227 ? 15.586 27.836 28.623 1.00 14.11 ? 227 ALA A CA 1 ATOM 1759 C C . ALA A 1 227 ? 16.930 28.305 28.085 1.00 16.31 ? 227 ALA A C 1 ATOM 1760 O O . ALA A 1 227 ? 17.183 29.530 27.984 1.00 19.15 ? 227 ALA A O 1 ATOM 1761 C CB . ALA A 1 227 ? 15.702 27.412 30.083 1.00 15.97 ? 227 ALA A CB 1 ATOM 1762 N N . LYS A 1 228 ? 17.784 27.404 27.639 1.00 13.19 ? 228 LYS A N 1 ATOM 1763 C CA . LYS A 1 228 ? 19.074 27.819 27.068 1.00 14.76 ? 228 LYS A CA 1 ATOM 1764 C C . LYS A 1 228 ? 18.849 28.564 25.757 1.00 13.49 ? 228 LYS A C 1 ATOM 1765 O O . LYS A 1 228 ? 19.488 29.577 25.428 1.00 17.72 ? 228 LYS A O 1 ATOM 1766 C CB . LYS A 1 228 ? 20.075 26.686 26.830 1.00 16.85 ? 228 LYS A CB 1 ATOM 1767 C CG . LYS A 1 228 ? 20.657 26.075 28.130 1.00 19.20 ? 228 LYS A CG 1 ATOM 1768 C CD . LYS A 1 228 ? 21.759 25.078 27.762 1.00 23.11 ? 228 LYS A CD 1 ATOM 1769 C CE . LYS A 1 228 ? 22.274 24.375 29.025 1.00 26.55 ? 228 LYS A CE 1 ATOM 1770 N NZ . LYS A 1 228 ? 23.038 25.392 29.779 1.00 31.90 ? 228 LYS A NZ 1 ATOM 1771 N N . ASN A 1 229 ? 17.940 28.058 24.901 1.00 11.36 ? 229 ASN A N 1 ATOM 1772 C CA . ASN A 1 229 ? 17.724 28.677 23.614 1.00 11.24 ? 229 ASN A CA 1 ATOM 1773 C C . ASN A 1 229 ? 17.104 30.070 23.721 1.00 12.43 ? 229 ASN A C 1 ATOM 1774 O O . ASN A 1 229 ? 17.569 30.999 23.036 1.00 12.04 ? 229 ASN A O 1 ATOM 1775 C CB . ASN A 1 229 ? 16.807 27.828 22.737 1.00 11.22 ? 229 ASN A CB 1 ATOM 1776 C CG . ASN A 1 229 ? 17.395 26.502 22.328 1.00 11.61 ? 229 ASN A CG 1 ATOM 1777 O OD1 . ASN A 1 229 ? 18.608 26.362 22.252 1.00 13.33 ? 229 ASN A OD1 1 ATOM 1778 N ND2 . ASN A 1 229 ? 16.593 25.467 22.026 1.00 12.42 ? 229 ASN A ND2 1 ATOM 1779 N N . VAL A 1 230 ? 16.142 30.222 24.626 1.00 12.21 ? 230 VAL A N 1 ATOM 1780 C CA . VAL A 1 230 ? 15.498 31.545 24.686 1.00 14.03 ? 230 VAL A CA 1 ATOM 1781 C C . VAL A 1 230 ? 16.386 32.610 25.307 1.00 14.28 ? 230 VAL A C 1 ATOM 1782 O O . VAL A 1 230 ? 16.053 33.790 25.159 1.00 16.67 ? 230 VAL A O 1 ATOM 1783 C CB . VAL A 1 230 ? 14.120 31.568 25.349 1.00 16.17 ? 230 VAL A CB 1 ATOM 1784 C CG1 . VAL A 1 230 ? 13.157 30.699 24.585 1.00 18.19 ? 230 VAL A CG1 1 ATOM 1785 C CG2 . VAL A 1 230 ? 14.174 31.188 26.814 1.00 15.52 ? 230 VAL A CG2 1 ATOM 1786 N N . GLN A 1 231 ? 17.478 32.259 25.950 1.00 13.92 ? 231 GLN A N 1 ATOM 1787 C CA . GLN A 1 231 ? 18.424 33.232 26.480 1.00 15.95 ? 231 GLN A CA 1 ATOM 1788 C C . GLN A 1 231 ? 19.404 33.730 25.443 1.00 13.39 ? 231 GLN A C 1 ATOM 1789 O O . GLN A 1 231 ? 20.156 34.679 25.705 1.00 15.98 ? 231 GLN A O 1 ATOM 1790 C CB . GLN A 1 231 ? 19.094 32.618 27.742 1.00 19.88 ? 231 GLN A CB 1 ATOM 1791 C CG A GLN A 1 231 ? 18.060 32.666 28.877 0.50 22.61 ? 231 GLN A CG 1 ATOM 1792 C CG B GLN A 1 231 ? 18.067 32.288 28.823 0.50 23.61 ? 231 GLN A CG 1 ATOM 1793 C CD A GLN A 1 231 ? 18.000 31.488 29.818 0.50 24.22 ? 231 GLN A CD 1 ATOM 1794 C CD B GLN A 1 231 ? 18.610 32.082 30.218 0.50 25.93 ? 231 GLN A CD 1 ATOM 1795 O OE1 A GLN A 1 231 ? 16.882 31.100 30.236 0.50 23.85 ? 231 GLN A OE1 1 ATOM 1796 O OE1 B GLN A 1 231 ? 18.275 31.117 30.930 0.50 27.37 ? 231 GLN A OE1 1 ATOM 1797 N NE2 A GLN A 1 231 ? 19.164 30.916 30.143 0.50 25.39 ? 231 GLN A NE2 1 ATOM 1798 N NE2 B GLN A 1 231 ? 19.451 32.990 30.687 0.50 25.76 ? 231 GLN A NE2 1 ATOM 1799 N N . ILE A 1 232 ? 19.449 33.175 24.225 1.00 10.75 ? 232 ILE A N 1 ATOM 1800 C CA . ILE A 1 232 ? 20.317 33.641 23.164 1.00 10.69 ? 232 ILE A CA 1 ATOM 1801 C C . ILE A 1 232 ? 19.942 35.076 22.826 1.00 10.79 ? 232 ILE A C 1 ATOM 1802 O O . ILE A 1 232 ? 18.786 35.409 22.580 1.00 11.82 ? 232 ILE A O 1 ATOM 1803 C CB . ILE A 1 232 ? 20.237 32.697 21.934 1.00 10.68 ? 232 ILE A CB 1 ATOM 1804 C CG1 . ILE A 1 232 ? 20.773 31.295 22.272 1.00 11.89 ? 232 ILE A CG1 1 ATOM 1805 C CG2 . ILE A 1 232 ? 20.946 33.288 20.715 1.00 11.66 ? 232 ILE A CG2 1 ATOM 1806 C CD1 . ILE A 1 232 ? 20.521 30.253 21.205 1.00 12.64 ? 232 ILE A CD1 1 ATOM 1807 N N . LYS A 1 233 ? 20.925 35.997 22.818 1.00 12.68 ? 233 LYS A N 1 ATOM 1808 C CA . LYS A 1 233 ? 20.687 37.410 22.705 1.00 13.69 ? 233 LYS A CA 1 ATOM 1809 C C . LYS A 1 233 ? 20.044 37.818 21.384 1.00 12.24 ? 233 LYS A C 1 ATOM 1810 O O . LYS A 1 233 ? 19.246 38.757 21.376 1.00 12.41 ? 233 LYS A O 1 ATOM 1811 C CB . LYS A 1 233 ? 22.031 38.199 22.841 1.00 17.22 ? 233 LYS A CB 1 ATOM 1812 C CG . LYS A 1 233 ? 22.754 38.028 24.161 1.00 22.05 ? 233 LYS A CG 1 ATOM 1813 C CD . LYS A 1 233 ? 24.165 38.553 24.120 1.00 25.90 ? 233 LYS A CD 1 ATOM 1814 C CE . LYS A 1 233 ? 24.446 39.653 23.106 1.00 27.86 ? 233 LYS A CE 1 ATOM 1815 N NZ . LYS A 1 233 ? 25.677 40.397 23.602 1.00 29.82 ? 233 LYS A NZ 1 ATOM 1816 N N . SER A 1 234 ? 20.429 37.123 20.309 1.00 11.86 ? 234 SER A N 1 ATOM 1817 C CA . SER A 1 234 ? 19.960 37.409 18.967 1.00 10.61 ? 234 SER A CA 1 ATOM 1818 C C . SER A 1 234 ? 18.668 36.689 18.589 1.00 9.46 ? 234 SER A C 1 ATOM 1819 O O . SER A 1 234 ? 18.272 36.744 17.417 1.00 11.56 ? 234 SER A O 1 ATOM 1820 C CB . SER A 1 234 ? 21.070 37.092 17.998 1.00 11.79 ? 234 SER A CB 1 ATOM 1821 O OG . SER A 1 234 ? 21.773 35.920 18.334 1.00 12.61 ? 234 SER A OG 1 ATOM 1822 N N . LEU A 1 235 ? 18.017 36.058 19.574 1.00 9.23 ? 235 LEU A N 1 ATOM 1823 C CA . LEU A 1 235 ? 16.648 35.546 19.420 1.00 9.50 ? 235 LEU A CA 1 ATOM 1824 C C . LEU A 1 235 ? 15.753 36.449 20.269 1.00 9.74 ? 235 LEU A C 1 ATOM 1825 O O . LEU A 1 235 ? 16.040 36.674 21.460 1.00 12.36 ? 235 LEU A O 1 ATOM 1826 C CB . LEU A 1 235 ? 16.491 34.097 19.837 1.00 9.16 ? 235 LEU A CB 1 ATOM 1827 C CG . LEU A 1 235 ? 17.333 33.084 19.050 1.00 10.07 ? 235 LEU A CG 1 ATOM 1828 C CD1 . LEU A 1 235 ? 17.185 31.675 19.620 1.00 11.67 ? 235 LEU A CD1 1 ATOM 1829 C CD2 . LEU A 1 235 ? 16.935 33.088 17.578 1.00 10.87 ? 235 LEU A CD2 1 ATOM 1830 N N . ASP A 1 236 ? 14.700 37.035 19.679 1.00 8.92 ? 236 ASP A N 1 ATOM 1831 C CA . ASP A 1 236 ? 13.915 38.046 20.376 1.00 9.25 ? 236 ASP A CA 1 ATOM 1832 C C . ASP A 1 236 ? 12.734 37.509 21.180 1.00 9.77 ? 236 ASP A C 1 ATOM 1833 O O . ASP A 1 236 ? 12.218 38.212 22.071 1.00 11.18 ? 236 ASP A O 1 ATOM 1834 C CB . ASP A 1 236 ? 13.408 39.092 19.352 1.00 10.61 ? 236 ASP A CB 1 ATOM 1835 C CG . ASP A 1 236 ? 14.583 39.771 18.679 1.00 11.03 ? 236 ASP A CG 1 ATOM 1836 O OD1 . ASP A 1 236 ? 15.334 40.468 19.392 1.00 15.24 ? 236 ASP A OD1 1 ATOM 1837 O OD2 . ASP A 1 236 ? 14.738 39.611 17.459 1.00 10.55 ? 236 ASP A OD2 1 ATOM 1838 N N . PHE A 1 237 ? 12.249 36.311 20.883 1.00 9.36 ? 237 PHE A N 1 ATOM 1839 C CA . PHE A 1 237 ? 11.113 35.705 21.554 1.00 9.27 ? 237 PHE A CA 1 ATOM 1840 C C . PHE A 1 237 ? 11.196 34.196 21.403 1.00 8.85 ? 237 PHE A C 1 ATOM 1841 O O . PHE A 1 237 ? 11.890 33.709 20.505 1.00 9.51 ? 237 PHE A O 1 ATOM 1842 C CB . PHE A 1 237 ? 9.779 36.253 21.058 1.00 9.24 ? 237 PHE A CB 1 ATOM 1843 C CG . PHE A 1 237 ? 9.442 36.026 19.609 1.00 8.43 ? 237 PHE A CG 1 ATOM 1844 C CD1 . PHE A 1 237 ? 9.831 36.909 18.617 1.00 8.60 ? 237 PHE A CD1 1 ATOM 1845 C CD2 . PHE A 1 237 ? 8.726 34.891 19.241 1.00 9.12 ? 237 PHE A CD2 1 ATOM 1846 C CE1 . PHE A 1 237 ? 9.473 36.723 17.284 1.00 10.09 ? 237 PHE A CE1 1 ATOM 1847 C CE2 . PHE A 1 237 ? 8.382 34.684 17.916 1.00 8.48 ? 237 PHE A CE2 1 ATOM 1848 C CZ . PHE A 1 237 ? 8.755 35.578 16.915 1.00 8.79 ? 237 PHE A CZ 1 ATOM 1849 N N . GLY A 1 238 ? 10.485 33.495 22.275 1.00 8.71 ? 238 GLY A N 1 ATOM 1850 C CA . GLY A 1 238 ? 10.488 32.030 22.233 1.00 8.93 ? 238 GLY A CA 1 ATOM 1851 C C . GLY A 1 238 ? 9.275 31.509 21.475 1.00 8.88 ? 238 GLY A C 1 ATOM 1852 O O . GLY A 1 238 ? 8.240 32.177 21.348 1.00 9.43 ? 238 GLY A O 1 ATOM 1853 N N . THR A 1 239 ? 9.425 30.328 20.906 1.00 8.05 ? 239 THR A N 1 ATOM 1854 C CA . THR A 1 239 ? 8.344 29.609 20.261 1.00 8.55 ? 239 THR A CA 1 ATOM 1855 C C . THR A 1 239 ? 8.165 28.251 20.932 1.00 8.71 ? 239 THR A C 1 ATOM 1856 O O . THR A 1 239 ? 9.150 27.567 21.283 1.00 7.94 ? 239 THR A O 1 ATOM 1857 C CB . THR A 1 239 ? 8.615 29.355 18.759 1.00 9.04 ? 239 THR A CB 1 ATOM 1858 O OG1 . THR A 1 239 ? 9.896 28.737 18.591 1.00 10.24 ? 239 THR A OG1 1 ATOM 1859 C CG2 . THR A 1 239 ? 8.622 30.632 17.928 1.00 9.04 ? 239 THR A CG2 1 ATOM 1860 N N . PHE A 1 240 ? 6.943 27.764 20.962 1.00 7.78 ? 240 PHE A N 1 ATOM 1861 C CA . PHE A 1 240 ? 6.683 26.362 21.340 1.00 8.05 ? 240 PHE A CA 1 ATOM 1862 C C . PHE A 1 240 ? 5.424 25.874 20.629 1.00 8.10 ? 240 PHE A C 1 ATOM 1863 O O . PHE A 1 240 ? 4.562 26.679 20.247 1.00 8.66 ? 240 PHE A O 1 ATOM 1864 C CB . PHE A 1 240 ? 6.573 26.095 22.836 1.00 7.82 ? 240 PHE A CB 1 ATOM 1865 C CG . PHE A 1 240 ? 5.448 26.856 23.525 1.00 9.00 ? 240 PHE A CG 1 ATOM 1866 C CD1 . PHE A 1 240 ? 5.566 28.133 23.989 1.00 10.71 ? 240 PHE A CD1 1 ATOM 1867 C CD2 . PHE A 1 240 ? 4.238 26.179 23.683 1.00 9.88 ? 240 PHE A CD2 1 ATOM 1868 C CE1 . PHE A 1 240 ? 4.483 28.735 24.631 1.00 10.24 ? 240 PHE A CE1 1 ATOM 1869 C CE2 . PHE A 1 240 ? 3.162 26.773 24.319 1.00 10.31 ? 240 PHE A CE2 1 ATOM 1870 C CZ . PHE A 1 240 ? 3.295 28.064 24.784 1.00 10.39 ? 240 PHE A CZ 1 ATOM 1871 N N . HIS A 1 241 ? 5.409 24.573 20.355 1.00 7.17 ? 241 HIS A N 1 ATOM 1872 C CA . HIS A 1 241 ? 4.322 23.905 19.620 1.00 6.72 ? 241 HIS A CA 1 ATOM 1873 C C . HIS A 1 241 ? 3.677 22.839 20.527 1.00 7.58 ? 241 HIS A C 1 ATOM 1874 O O . HIS A 1 241 ? 4.230 22.568 21.589 1.00 8.99 ? 241 HIS A O 1 ATOM 1875 C CB . HIS A 1 241 ? 4.865 23.250 18.333 1.00 7.13 ? 241 HIS A CB 1 ATOM 1876 C CG . HIS A 1 241 ? 5.567 24.184 17.374 1.00 6.97 ? 241 HIS A CG 1 ATOM 1877 N ND1 . HIS A 1 241 ? 6.105 23.762 16.160 1.00 7.01 ? 241 HIS A ND1 1 ATOM 1878 C CD2 . HIS A 1 241 ? 5.753 25.534 17.404 1.00 8.41 ? 241 HIS A CD2 1 ATOM 1879 C CE1 . HIS A 1 241 ? 6.613 24.839 15.551 1.00 6.96 ? 241 HIS A CE1 1 ATOM 1880 N NE2 . HIS A 1 241 ? 6.413 25.914 16.284 1.00 8.32 ? 241 HIS A NE2 1 ATOM 1881 N N . LEU A 1 242 ? 2.522 22.277 20.126 1.00 7.75 ? 242 LEU A N 1 ATOM 1882 C CA . LEU A 1 242 ? 1.830 21.377 21.057 1.00 7.10 ? 242 LEU A CA 1 ATOM 1883 C C . LEU A 1 242 ? 0.978 20.346 20.304 1.00 8.60 ? 242 LEU A C 1 ATOM 1884 O O . LEU A 1 242 ? 0.018 20.700 19.598 1.00 8.80 ? 242 LEU A O 1 ATOM 1885 C CB . LEU A 1 242 ? 0.943 22.183 22.018 1.00 8.15 ? 242 LEU A CB 1 ATOM 1886 C CG . LEU A 1 242 ? 0.008 21.357 22.915 1.00 9.50 ? 242 LEU A CG 1 ATOM 1887 C CD1 . LEU A 1 242 ? 0.767 20.393 23.819 1.00 8.99 ? 242 LEU A CD1 1 ATOM 1888 C CD2 . LEU A 1 242 ? -0.882 22.303 23.744 1.00 11.28 ? 242 LEU A CD2 1 ATOM 1889 N N . TYR A 1 243 ? 1.341 19.050 20.420 1.00 8.68 ? 243 TYR A N 1 ATOM 1890 C CA . TYR A 1 243 ? 0.604 17.974 19.778 1.00 9.42 ? 243 TYR A CA 1 ATOM 1891 C C . TYR A 1 243 ? 0.503 16.738 20.662 1.00 9.81 ? 243 TYR A C 1 ATOM 1892 O O . TYR A 1 243 ? 1.210 15.744 20.467 1.00 11.28 ? 243 TYR A O 1 ATOM 1893 C CB . TYR A 1 243 ? 1.232 17.569 18.428 1.00 9.85 ? 243 TYR A CB 1 ATOM 1894 C CG . TYR A 1 243 ? 1.164 18.636 17.344 1.00 8.93 ? 243 TYR A CG 1 ATOM 1895 C CD1 . TYR A 1 243 ? -0.004 18.879 16.632 1.00 10.88 ? 243 TYR A CD1 1 ATOM 1896 C CD2 . TYR A 1 243 ? 2.219 19.502 17.117 1.00 8.52 ? 243 TYR A CD2 1 ATOM 1897 C CE1 . TYR A 1 243 ? -0.074 19.837 15.647 1.00 8.73 ? 243 TYR A CE1 1 ATOM 1898 C CE2 . TYR A 1 243 ? 2.160 20.500 16.171 1.00 9.36 ? 243 TYR A CE2 1 ATOM 1899 C CZ . TYR A 1 243 ? 1.015 20.671 15.425 1.00 7.76 ? 243 TYR A CZ 1 ATOM 1900 O OH . TYR A 1 243 ? 0.929 21.624 14.456 1.00 8.50 ? 243 TYR A OH 1 ATOM 1901 N N . PRO A 1 244 ? -0.424 16.742 21.631 1.00 10.80 ? 244 PRO A N 1 ATOM 1902 C CA . PRO A 1 244 ? -0.627 15.581 22.506 1.00 11.43 ? 244 PRO A CA 1 ATOM 1903 C C . PRO A 1 244 ? -0.879 14.274 21.767 1.00 12.99 ? 244 PRO A C 1 ATOM 1904 O O . PRO A 1 244 ? -0.349 13.210 22.176 1.00 14.20 ? 244 PRO A O 1 ATOM 1905 C CB . PRO A 1 244 ? -1.817 15.998 23.375 1.00 13.70 ? 244 PRO A CB 1 ATOM 1906 C CG . PRO A 1 244 ? -1.699 17.490 23.404 1.00 13.28 ? 244 PRO A CG 1 ATOM 1907 C CD . PRO A 1 244 ? -1.328 17.857 21.993 1.00 11.45 ? 244 PRO A CD 1 ATOM 1908 N N . ASP A 1 245 ? -1.600 14.315 20.641 1.00 13.76 ? 245 ASP A N 1 ATOM 1909 C CA . ASP A 1 245 ? -1.853 13.091 19.865 1.00 16.23 ? 245 ASP A CA 1 ATOM 1910 C C . ASP A 1 245 ? -0.624 12.475 19.240 1.00 16.66 ? 245 ASP A C 1 ATOM 1911 O O . ASP A 1 245 ? -0.594 11.266 18.961 1.00 21.61 ? 245 ASP A O 1 ATOM 1912 C CB . ASP A 1 245 ? -2.707 13.366 18.595 1.00 21.71 ? 245 ASP A CB 1 ATOM 1913 C CG . ASP A 1 245 ? -4.085 13.853 18.859 1.00 23.03 ? 245 ASP A CG 1 ATOM 1914 O OD1 . ASP A 1 245 ? -4.813 13.127 19.557 1.00 27.04 ? 245 ASP A OD1 1 ATOM 1915 O OD2 . ASP A 1 245 ? -4.405 14.926 18.331 1.00 21.89 ? 245 ASP A OD2 1 ATOM 1916 N N . SER A 1 246 ? 0.403 13.310 18.961 1.00 13.35 ? 246 SER A N 1 ATOM 1917 C CA . SER A 1 246 ? 1.631 12.797 18.388 1.00 14.12 ? 246 SER A CA 1 ATOM 1918 C C . SER A 1 246 ? 2.631 12.429 19.485 1.00 13.46 ? 246 SER A C 1 ATOM 1919 O O . SER A 1 246 ? 3.575 11.677 19.211 1.00 16.45 ? 246 SER A O 1 ATOM 1920 C CB . SER A 1 246 ? 2.276 13.954 17.576 1.00 16.28 ? 246 SER A CB 1 ATOM 1921 O OG . SER A 1 246 ? 1.326 14.385 16.606 1.00 22.64 ? 246 SER A OG 1 ATOM 1922 N N . TRP A 1 247 ? 2.432 12.997 20.669 1.00 12.03 ? 247 TRP A N 1 ATOM 1923 C CA . TRP A 1 247 ? 3.416 12.898 21.734 1.00 11.59 ? 247 TRP A CA 1 ATOM 1924 C C . TRP A 1 247 ? 3.080 11.947 22.871 1.00 12.80 ? 247 TRP A C 1 ATOM 1925 O O . TRP A 1 247 ? 3.856 11.756 23.801 1.00 14.40 ? 247 TRP A O 1 ATOM 1926 C CB . TRP A 1 247 ? 3.644 14.301 22.343 1.00 11.22 ? 247 TRP A CB 1 ATOM 1927 C CG . TRP A 1 247 ? 4.241 15.324 21.409 1.00 10.19 ? 247 TRP A CG 1 ATOM 1928 C CD1 . TRP A 1 247 ? 4.749 15.105 20.148 1.00 10.79 ? 247 TRP A CD1 1 ATOM 1929 C CD2 . TRP A 1 247 ? 4.420 16.720 21.669 1.00 10.31 ? 247 TRP A CD2 1 ATOM 1930 N NE1 . TRP A 1 247 ? 5.246 16.269 19.613 1.00 10.98 ? 247 TRP A NE1 1 ATOM 1931 C CE2 . TRP A 1 247 ? 5.028 17.285 20.524 1.00 11.15 ? 247 TRP A CE2 1 ATOM 1932 C CE3 . TRP A 1 247 ? 4.062 17.539 22.743 1.00 9.78 ? 247 TRP A CE3 1 ATOM 1933 C CZ2 . TRP A 1 247 ? 5.357 18.640 20.448 1.00 11.02 ? 247 TRP A CZ2 1 ATOM 1934 C CZ3 . TRP A 1 247 ? 4.433 18.896 22.678 1.00 9.69 ? 247 TRP A CZ3 1 ATOM 1935 C CH2 . TRP A 1 247 ? 5.031 19.422 21.531 1.00 10.75 ? 247 TRP A CH2 1 ATOM 1936 N N . GLY A 1 248 ? 1.925 11.309 22.764 1.00 13.82 ? 248 GLY A N 1 ATOM 1937 C CA . GLY A 1 248 ? 1.499 10.340 23.759 1.00 14.85 ? 248 GLY A CA 1 ATOM 1938 C C . GLY A 1 248 ? 1.030 10.910 25.081 1.00 16.53 ? 248 GLY A C 1 ATOM 1939 O O . GLY A 1 248 ? 1.065 10.235 26.128 1.00 19.98 ? 248 GLY A O 1 ATOM 1940 N N . THR A 1 249 ? 0.624 12.175 25.116 1.00 13.27 ? 249 THR A N 1 ATOM 1941 C CA . THR A 1 249 ? 0.096 12.803 26.321 1.00 14.34 ? 249 THR A CA 1 ATOM 1942 C C . THR A 1 249 ? -1.415 13.030 26.134 1.00 14.85 ? 249 THR A C 1 ATOM 1943 O O . THR A 1 249 ? -1.928 12.978 25.006 1.00 14.90 ? 249 THR A O 1 ATOM 1944 C CB . THR A 1 249 ? 0.798 14.131 26.674 1.00 16.36 ? 249 THR A CB 1 ATOM 1945 O OG1 . THR A 1 249 ? 0.593 15.006 25.559 1.00 18.54 ? 249 THR A OG1 1 ATOM 1946 C CG2 . THR A 1 249 ? 2.281 13.910 26.837 1.00 18.36 ? 249 THR A CG2 1 ATOM 1947 N N . ASN A 1 250 ? -2.082 13.370 27.234 1.00 15.73 ? 250 ASN A N 1 ATOM 1948 C CA . ASN A 1 250 ? -3.510 13.668 27.073 1.00 15.94 ? 250 ASN A CA 1 ATOM 1949 C C . ASN A 1 250 ? -3.646 15.150 26.697 1.00 14.11 ? 250 ASN A C 1 ATOM 1950 O O . ASN A 1 250 ? -2.696 15.953 26.725 1.00 14.60 ? 250 ASN A O 1 ATOM 1951 C CB . ASN A 1 250 ? -4.388 13.294 28.224 1.00 18.31 ? 250 ASN A CB 1 ATOM 1952 C CG . ASN A 1 250 ? -4.105 14.073 29.433 1.00 22.35 ? 250 ASN A CG 1 ATOM 1953 O OD1 . ASN A 1 250 ? -3.745 15.230 29.517 1.00 20.32 ? 250 ASN A OD1 1 ATOM 1954 N ND2 . ASN A 1 250 ? -4.315 13.382 30.606 1.00 28.91 ? 250 ASN A ND2 1 ATOM 1955 N N . TYR A 1 251 ? -4.820 15.585 26.290 1.00 14.05 ? 251 TYR A N 1 ATOM 1956 C CA . TYR A 1 251 ? -5.018 16.959 25.842 1.00 13.15 ? 251 TYR A CA 1 ATOM 1957 C C . TYR A 1 251 ? -4.895 17.962 26.958 1.00 12.98 ? 251 TYR A C 1 ATOM 1958 O O . TYR A 1 251 ? -4.291 19.029 26.791 1.00 13.11 ? 251 TYR A O 1 ATOM 1959 C CB . TYR A 1 251 ? -6.384 17.063 25.151 1.00 14.55 ? 251 TYR A CB 1 ATOM 1960 C CG . TYR A 1 251 ? -6.463 16.337 23.835 1.00 15.31 ? 251 TYR A CG 1 ATOM 1961 C CD1 . TYR A 1 251 ? -5.581 16.486 22.797 1.00 16.61 ? 251 TYR A CD1 1 ATOM 1962 C CD2 . TYR A 1 251 ? -7.530 15.447 23.614 1.00 18.01 ? 251 TYR A CD2 1 ATOM 1963 C CE1 . TYR A 1 251 ? -5.707 15.822 21.598 1.00 17.22 ? 251 TYR A CE1 1 ATOM 1964 C CE2 . TYR A 1 251 ? -7.669 14.804 22.416 1.00 19.28 ? 251 TYR A CE2 1 ATOM 1965 C CZ . TYR A 1 251 ? -6.771 14.979 21.391 1.00 18.46 ? 251 TYR A CZ 1 ATOM 1966 O OH . TYR A 1 251 ? -6.915 14.294 20.198 1.00 18.04 ? 251 TYR A OH 1 ATOM 1967 N N . THR A 1 252 ? -5.403 17.683 28.164 1.00 12.99 ? 252 THR A N 1 ATOM 1968 C CA . THR A 1 252 ? -5.363 18.619 29.269 1.00 14.29 ? 252 THR A CA 1 ATOM 1969 C C . THR A 1 252 ? -3.953 18.915 29.775 1.00 14.31 ? 252 THR A C 1 ATOM 1970 O O . THR A 1 252 ? -3.732 20.034 30.278 1.00 14.85 ? 252 THR A O 1 ATOM 1971 C CB . THR A 1 252 ? -6.285 18.218 30.438 1.00 16.36 ? 252 THR A CB 1 ATOM 1972 O OG1 A THR A 1 252 ? -5.834 16.915 30.895 0.50 17.63 ? 252 THR A OG1 1 ATOM 1973 O OG1 B THR A 1 252 ? -6.716 19.498 31.007 0.50 17.21 ? 252 THR A OG1 1 ATOM 1974 C CG2 A THR A 1 252 ? -7.722 18.076 30.036 0.50 16.49 ? 252 THR A CG2 1 ATOM 1975 C CG2 B THR A 1 252 ? -5.709 17.409 31.566 0.50 16.81 ? 252 THR A CG2 1 ATOM 1976 N N . TRP A 1 253 ? -3.020 18.011 29.520 1.00 13.27 ? 253 TRP A N 1 ATOM 1977 C CA . TRP A 1 253 ? -1.593 18.236 29.807 1.00 11.74 ? 253 TRP A CA 1 ATOM 1978 C C . TRP A 1 253 ? -1.078 19.454 29.058 1.00 11.32 ? 253 TRP A C 1 ATOM 1979 O O . TRP A 1 253 ? -0.069 20.067 29.434 1.00 12.67 ? 253 TRP A O 1 ATOM 1980 C CB . TRP A 1 253 ? -0.855 16.971 29.402 1.00 12.29 ? 253 TRP A CB 1 ATOM 1981 C CG . TRP A 1 253 ? 0.640 16.962 29.403 1.00 11.99 ? 253 TRP A CG 1 ATOM 1982 C CD1 . TRP A 1 253 ? 1.444 16.516 30.416 1.00 12.24 ? 253 TRP A CD1 1 ATOM 1983 C CD2 . TRP A 1 253 ? 1.525 17.366 28.336 1.00 10.48 ? 253 TRP A CD2 1 ATOM 1984 N NE1 . TRP A 1 253 ? 2.764 16.630 30.041 1.00 12.16 ? 253 TRP A NE1 1 ATOM 1985 C CE2 . TRP A 1 253 ? 2.842 17.148 28.775 1.00 10.79 ? 253 TRP A CE2 1 ATOM 1986 C CE3 . TRP A 1 253 ? 1.308 17.846 27.056 1.00 10.80 ? 253 TRP A CE3 1 ATOM 1987 C CZ2 . TRP A 1 253 ? 3.959 17.456 27.986 1.00 10.25 ? 253 TRP A CZ2 1 ATOM 1988 C CZ3 . TRP A 1 253 ? 2.398 18.183 26.257 1.00 9.91 ? 253 TRP A CZ3 1 ATOM 1989 C CH2 . TRP A 1 253 ? 3.702 17.953 26.732 1.00 9.98 ? 253 TRP A CH2 1 ATOM 1990 N N . GLY A 1 254 ? -1.725 19.836 27.956 1.00 11.11 ? 254 GLY A N 1 ATOM 1991 C CA . GLY A 1 254 ? -1.321 21.005 27.199 1.00 8.58 ? 254 GLY A CA 1 ATOM 1992 C C . GLY A 1 254 ? -1.370 22.307 27.978 1.00 9.55 ? 254 GLY A C 1 ATOM 1993 O O . GLY A 1 254 ? -0.587 23.229 27.683 1.00 10.34 ? 254 GLY A O 1 ATOM 1994 N N . ASN A 1 255 ? -2.242 22.452 28.972 1.00 10.73 ? 255 ASN A N 1 ATOM 1995 C CA . ASN A 1 255 ? -2.324 23.654 29.772 1.00 10.54 ? 255 ASN A CA 1 ATOM 1996 C C . ASN A 1 255 ? -1.033 23.894 30.540 1.00 10.57 ? 255 ASN A C 1 ATOM 1997 O O . ASN A 1 255 ? -0.461 24.993 30.518 1.00 11.47 ? 255 ASN A O 1 ATOM 1998 C CB . ASN A 1 255 ? -3.542 23.655 30.707 1.00 12.39 ? 255 ASN A CB 1 ATOM 1999 C CG . ASN A 1 255 ? -4.807 23.642 29.874 1.00 14.68 ? 255 ASN A CG 1 ATOM 2000 O OD1 . ASN A 1 255 ? -5.175 24.581 29.156 1.00 14.03 ? 255 ASN A OD1 1 ATOM 2001 N ND2 . ASN A 1 255 ? -5.518 22.510 29.995 1.00 18.02 ? 255 ASN A ND2 1 ATOM 2002 N N . GLY A 1 256 ? -0.531 22.835 31.172 1.00 11.04 ? 256 GLY A N 1 ATOM 2003 C CA . GLY A 1 256 ? 0.747 22.931 31.877 1.00 10.37 ? 256 GLY A CA 1 ATOM 2004 C C . GLY A 1 256 ? 1.922 23.160 30.927 1.00 10.76 ? 256 GLY A C 1 ATOM 2005 O O . GLY A 1 256 ? 2.853 23.889 31.265 1.00 10.97 ? 256 GLY A O 1 ATOM 2006 N N . TRP A 1 257 ? 1.874 22.612 29.716 1.00 9.57 ? 257 TRP A N 1 ATOM 2007 C CA . TRP A 1 257 ? 2.897 22.876 28.709 1.00 9.05 ? 257 TRP A CA 1 ATOM 2008 C C . TRP A 1 257 ? 2.930 24.354 28.371 1.00 8.98 ? 257 TRP A C 1 ATOM 2009 O O . TRP A 1 257 ? 4.008 24.976 28.304 1.00 9.12 ? 257 TRP A O 1 ATOM 2010 C CB . TRP A 1 257 ? 2.560 22.054 27.474 1.00 9.50 ? 257 TRP A CB 1 ATOM 2011 C CG . TRP A 1 257 ? 3.567 22.143 26.355 1.00 8.86 ? 257 TRP A CG 1 ATOM 2012 C CD1 . TRP A 1 257 ? 3.430 22.795 25.167 1.00 9.77 ? 257 TRP A CD1 1 ATOM 2013 C CD2 . TRP A 1 257 ? 4.847 21.497 26.296 1.00 8.55 ? 257 TRP A CD2 1 ATOM 2014 N NE1 . TRP A 1 257 ? 4.535 22.607 24.368 1.00 9.21 ? 257 TRP A NE1 1 ATOM 2015 C CE2 . TRP A 1 257 ? 5.421 21.800 25.050 1.00 8.37 ? 257 TRP A CE2 1 ATOM 2016 C CE3 . TRP A 1 257 ? 5.553 20.690 27.159 1.00 9.04 ? 257 TRP A CE3 1 ATOM 2017 C CZ2 . TRP A 1 257 ? 6.670 21.308 24.663 1.00 8.51 ? 257 TRP A CZ2 1 ATOM 2018 C CZ3 . TRP A 1 257 ? 6.805 20.187 26.784 1.00 8.79 ? 257 TRP A CZ3 1 ATOM 2019 C CH2 . TRP A 1 257 ? 7.351 20.538 25.550 1.00 9.05 ? 257 TRP A CH2 1 ATOM 2020 N N . ILE A 1 258 ? 1.784 25.031 28.227 1.00 9.84 ? 258 ILE A N 1 ATOM 2021 C CA . ILE A 1 258 ? 1.753 26.462 27.957 1.00 9.57 ? 258 ILE A CA 1 ATOM 2022 C C . ILE A 1 258 ? 2.314 27.237 29.161 1.00 9.35 ? 258 ILE A C 1 ATOM 2023 O O . ILE A 1 258 ? 3.141 28.143 28.978 1.00 10.80 ? 258 ILE A O 1 ATOM 2024 C CB . ILE A 1 258 ? 0.313 26.943 27.647 1.00 9.33 ? 258 ILE A CB 1 ATOM 2025 C CG1 . ILE A 1 258 ? -0.203 26.297 26.352 1.00 8.89 ? 258 ILE A CG1 1 ATOM 2026 C CG2 . ILE A 1 258 ? 0.241 28.453 27.584 1.00 11.78 ? 258 ILE A CG2 1 ATOM 2027 C CD1 . ILE A 1 258 ? -1.724 26.225 26.261 1.00 11.11 ? 258 ILE A CD1 1 ATOM 2028 N N . GLN A 1 259 ? 1.872 26.903 30.374 1.00 10.63 ? 259 GLN A N 1 ATOM 2029 C CA . GLN A 1 259 ? 2.271 27.624 31.573 1.00 11.21 ? 259 GLN A CA 1 ATOM 2030 C C . GLN A 1 259 ? 3.773 27.543 31.815 1.00 11.34 ? 259 GLN A C 1 ATOM 2031 O O . GLN A 1 259 ? 4.398 28.563 32.125 1.00 11.65 ? 259 GLN A O 1 ATOM 2032 C CB . GLN A 1 259 ? 1.532 27.078 32.810 1.00 13.49 ? 259 GLN A CB 1 ATOM 2033 C CG . GLN A 1 259 ? 0.035 27.411 32.748 1.00 16.83 ? 259 GLN A CG 1 ATOM 2034 C CD . GLN A 1 259 ? -0.778 26.666 33.789 1.00 21.24 ? 259 GLN A CD 1 ATOM 2035 O OE1 . GLN A 1 259 ? -0.494 25.535 34.187 1.00 23.15 ? 259 GLN A OE1 1 ATOM 2036 N NE2 . GLN A 1 259 ? -1.800 27.407 34.200 1.00 24.06 ? 259 GLN A NE2 1 ATOM 2037 N N . THR A 1 260 ? 4.369 26.350 31.636 1.00 10.58 ? 260 THR A N 1 ATOM 2038 C CA . THR A 1 260 ? 5.788 26.226 31.917 1.00 10.13 ? 260 THR A CA 1 ATOM 2039 C C . THR A 1 260 ? 6.603 26.994 30.909 1.00 9.62 ? 260 THR A C 1 ATOM 2040 O O . THR A 1 260 ? 7.639 27.619 31.221 1.00 10.00 ? 260 THR A O 1 ATOM 2041 C CB . THR A 1 260 ? 6.262 24.772 31.987 1.00 11.32 ? 260 THR A CB 1 ATOM 2042 O OG1 . THR A 1 260 ? 5.885 24.108 30.761 1.00 11.90 ? 260 THR A OG1 1 ATOM 2043 C CG2 . THR A 1 260 ? 5.695 24.003 33.175 1.00 12.37 ? 260 THR A CG2 1 ATOM 2044 N N . HIS A 1 261 ? 6.211 26.965 29.632 1.00 9.21 ? 261 HIS A N 1 ATOM 2045 C CA . HIS A 1 261 ? 6.952 27.676 28.592 1.00 9.38 ? 261 HIS A CA 1 ATOM 2046 C C . HIS A 1 261 ? 6.811 29.173 28.790 1.00 8.97 ? 261 HIS A C 1 ATOM 2047 O O . HIS A 1 261 ? 7.800 29.928 28.674 1.00 10.89 ? 261 HIS A O 1 ATOM 2048 C CB . HIS A 1 261 ? 6.499 27.210 27.178 1.00 10.17 ? 261 HIS A CB 1 ATOM 2049 C CG . HIS A 1 261 ? 7.120 25.882 26.870 1.00 8.63 ? 261 HIS A CG 1 ATOM 2050 N ND1 . HIS A 1 261 ? 6.543 24.695 27.327 1.00 8.72 ? 261 HIS A ND1 1 ATOM 2051 C CD2 . HIS A 1 261 ? 8.256 25.530 26.210 1.00 8.79 ? 261 HIS A CD2 1 ATOM 2052 C CE1 . HIS A 1 261 ? 7.341 23.673 26.944 1.00 8.59 ? 261 HIS A CE1 1 ATOM 2053 N NE2 . HIS A 1 261 ? 8.370 24.175 26.255 1.00 8.90 ? 261 HIS A NE2 1 ATOM 2054 N N . ALA A 1 262 ? 5.602 29.670 29.070 1.00 9.21 ? 262 ALA A N 1 ATOM 2055 C CA . ALA A 1 262 ? 5.400 31.084 29.327 1.00 10.08 ? 262 ALA A CA 1 ATOM 2056 C C . ALA A 1 262 ? 6.303 31.616 30.436 1.00 11.03 ? 262 ALA A C 1 ATOM 2057 O O . ALA A 1 262 ? 6.928 32.696 30.314 1.00 11.99 ? 262 ALA A O 1 ATOM 2058 C CB . ALA A 1 262 ? 3.953 31.401 29.672 1.00 11.38 ? 262 ALA A CB 1 ATOM 2059 N N . ALA A 1 263 ? 6.390 30.815 31.504 1.00 11.39 ? 263 ALA A N 1 ATOM 2060 C CA . ALA A 1 263 ? 7.251 31.225 32.621 1.00 11.86 ? 263 ALA A CA 1 ATOM 2061 C C . ALA A 1 263 ? 8.713 31.284 32.222 1.00 11.43 ? 263 ALA A C 1 ATOM 2062 O O . ALA A 1 263 ? 9.452 32.160 32.704 1.00 13.71 ? 263 ALA A O 1 ATOM 2063 C CB . ALA A 1 263 ? 7.012 30.277 33.777 1.00 12.76 ? 263 ALA A CB 1 ATOM 2064 N N . ALA A 1 264 ? 9.173 30.344 31.395 1.00 11.25 ? 264 ALA A N 1 ATOM 2065 C CA . ALA A 1 264 ? 10.565 30.362 30.935 1.00 11.76 ? 264 ALA A CA 1 ATOM 2066 C C . ALA A 1 264 ? 10.845 31.537 30.015 1.00 10.85 ? 264 ALA A C 1 ATOM 2067 O O . ALA A 1 264 ? 11.908 32.193 30.139 1.00 13.56 ? 264 ALA A O 1 ATOM 2068 C CB . ALA A 1 264 ? 10.890 29.033 30.281 1.00 12.48 ? 264 ALA A CB 1 ATOM 2069 N N . CYS A 1 265 ? 9.900 31.925 29.149 1.00 10.99 ? 265 CYS A N 1 ATOM 2070 C CA . CYS A 1 265 ? 10.071 33.124 28.339 1.00 13.08 ? 265 CYS A CA 1 ATOM 2071 C C . CYS A 1 265 ? 10.146 34.360 29.233 1.00 13.22 ? 265 CYS A C 1 ATOM 2072 O O . CYS A 1 265 ? 11.042 35.204 29.115 1.00 13.58 ? 265 CYS A O 1 ATOM 2073 C CB . CYS A 1 265 ? 8.899 33.298 27.340 1.00 12.47 ? 265 CYS A CB 1 ATOM 2074 S SG . CYS A 1 265 ? 9.104 32.263 25.885 1.00 12.59 ? 265 CYS A SG 1 ATOM 2075 N N . LEU A 1 266 ? 9.226 34.472 30.175 1.00 13.71 ? 266 LEU A N 1 ATOM 2076 C CA . LEU A 1 266 ? 9.174 35.656 31.062 1.00 13.99 ? 266 LEU A CA 1 ATOM 2077 C C . LEU A 1 266 ? 10.408 35.731 31.920 1.00 14.58 ? 266 LEU A C 1 ATOM 2078 O O . LEU A 1 266 ? 10.930 36.845 32.117 1.00 14.97 ? 266 LEU A O 1 ATOM 2079 C CB . LEU A 1 266 ? 7.898 35.609 31.900 1.00 15.49 ? 266 LEU A CB 1 ATOM 2080 C CG . LEU A 1 266 ? 7.646 36.795 32.855 1.00 18.54 ? 266 LEU A CG 1 ATOM 2081 C CD1 . LEU A 1 266 ? 7.531 38.100 32.094 1.00 19.27 ? 266 LEU A CD1 1 ATOM 2082 C CD2 . LEU A 1 266 ? 6.369 36.530 33.644 1.00 21.49 ? 266 LEU A CD2 1 ATOM 2083 N N . ALA A 1 267 ? 10.949 34.592 32.342 1.00 13.45 ? 267 ALA A N 1 ATOM 2084 C CA . ALA A 1 267 ? 12.213 34.592 33.107 1.00 15.39 ? 267 ALA A CA 1 ATOM 2085 C C . ALA A 1 267 ? 13.385 35.084 32.269 1.00 15.41 ? 267 ALA A C 1 ATOM 2086 O O . ALA A 1 267 ? 14.362 35.632 32.819 1.00 17.37 ? 267 ALA A O 1 ATOM 2087 C CB . ALA A 1 267 ? 12.504 33.228 33.667 1.00 16.35 ? 267 ALA A CB 1 ATOM 2088 N N . ALA A 1 268 ? 13.357 34.870 30.947 1.00 13.95 ? 268 ALA A N 1 ATOM 2089 C CA . ALA A 1 268 ? 14.372 35.357 30.028 1.00 12.98 ? 268 ALA A CA 1 ATOM 2090 C C . ALA A 1 268 ? 14.079 36.766 29.534 1.00 12.72 ? 268 ALA A C 1 ATOM 2091 O O . ALA A 1 268 ? 14.792 37.357 28.695 1.00 13.81 ? 268 ALA A O 1 ATOM 2092 C CB . ALA A 1 268 ? 14.494 34.422 28.825 1.00 14.10 ? 268 ALA A CB 1 ATOM 2093 N N . GLY A 1 269 ? 13.010 37.388 30.032 1.00 12.33 ? 269 GLY A N 1 ATOM 2094 C CA . GLY A 1 269 ? 12.607 38.721 29.728 1.00 11.35 ? 269 GLY A CA 1 ATOM 2095 C C . GLY A 1 269 ? 11.955 39.026 28.389 1.00 10.55 ? 269 GLY A C 1 ATOM 2096 O O . GLY A 1 269 ? 11.957 40.180 27.894 1.00 11.96 ? 269 GLY A O 1 ATOM 2097 N N . LYS A 1 270 ? 11.380 37.956 27.806 1.00 11.75 ? 270 LYS A N 1 ATOM 2098 C CA . LYS A 1 270 ? 10.858 38.002 26.449 1.00 11.21 ? 270 LYS A CA 1 ATOM 2099 C C . LYS A 1 270 ? 9.493 37.349 26.348 1.00 10.60 ? 270 LYS A C 1 ATOM 2100 O O . LYS A 1 270 ? 9.110 36.525 27.181 1.00 11.60 ? 270 LYS A O 1 ATOM 2101 C CB . LYS A 1 270 ? 11.807 37.184 25.550 1.00 12.19 ? 270 LYS A CB 1 ATOM 2102 C CG . LYS A 1 270 ? 13.240 37.667 25.524 1.00 12.49 ? 270 LYS A CG 1 ATOM 2103 C CD . LYS A 1 270 ? 14.159 36.698 24.773 1.00 12.17 ? 270 LYS A CD 1 ATOM 2104 C CE . LYS A 1 270 ? 15.592 37.160 24.946 1.00 12.17 ? 270 LYS A CE 1 ATOM 2105 N NZ . LYS A 1 270 ? 16.590 36.371 24.193 1.00 11.30 ? 270 LYS A NZ 1 ATOM 2106 N N . PRO A 1 271 ? 8.715 37.730 25.329 1.00 10.75 ? 271 PRO A N 1 ATOM 2107 C CA . PRO A 1 271 ? 7.460 37.023 25.075 1.00 10.51 ? 271 PRO A CA 1 ATOM 2108 C C . PRO A 1 271 ? 7.698 35.631 24.514 1.00 9.70 ? 271 PRO A C 1 ATOM 2109 O O . PRO A 1 271 ? 8.732 35.327 23.935 1.00 10.93 ? 271 PRO A O 1 ATOM 2110 C CB . PRO A 1 271 ? 6.741 37.863 24.007 1.00 11.68 ? 271 PRO A CB 1 ATOM 2111 C CG . PRO A 1 271 ? 7.683 38.984 23.681 1.00 11.31 ? 271 PRO A CG 1 ATOM 2112 C CD . PRO A 1 271 ? 9.022 38.701 24.268 1.00 10.74 ? 271 PRO A CD 1 ATOM 2113 N N . CYS A 1 272 ? 6.673 34.772 24.640 1.00 10.26 ? 272 CYS A N 1 ATOM 2114 C CA . CYS A 1 272 ? 6.557 33.474 24.018 1.00 10.96 ? 272 CYS A CA 1 ATOM 2115 C C . CYS A 1 272 ? 5.404 33.585 22.965 1.00 10.30 ? 272 CYS A C 1 ATOM 2116 O O . CYS A 1 272 ? 4.409 34.293 23.194 1.00 11.15 ? 272 CYS A O 1 ATOM 2117 C CB . CYS A 1 272 ? 6.069 32.421 25.012 1.00 13.18 ? 272 CYS A CB 1 ATOM 2118 S SG . CYS A 1 272 ? 7.286 31.251 25.613 1.00 13.57 ? 272 CYS A SG 1 ATOM 2119 N N . VAL A 1 273 ? 5.547 32.819 21.898 1.00 9.43 ? 273 VAL A N 1 ATOM 2120 C CA . VAL A 1 273 ? 4.507 32.616 20.888 1.00 8.99 ? 273 VAL A CA 1 ATOM 2121 C C . VAL A 1 273 ? 4.163 31.118 20.891 1.00 8.68 ? 273 VAL A C 1 ATOM 2122 O O . VAL A 1 273 ? 5.032 30.253 20.684 1.00 8.60 ? 273 VAL A O 1 ATOM 2123 C CB . VAL A 1 273 ? 4.854 33.091 19.478 1.00 9.91 ? 273 VAL A CB 1 ATOM 2124 C CG1 . VAL A 1 273 ? 3.747 32.743 18.471 1.00 11.06 ? 273 VAL A CG1 1 ATOM 2125 C CG2 . VAL A 1 273 ? 5.072 34.602 19.453 1.00 12.38 ? 273 VAL A CG2 1 ATOM 2126 N N . PHE A 1 274 ? 2.905 30.806 21.144 1.00 8.71 ? 274 PHE A N 1 ATOM 2127 C CA . PHE A 1 274 ? 2.315 29.474 21.095 1.00 7.34 ? 274 PHE A CA 1 ATOM 2128 C C . PHE A 1 274 ? 2.048 29.268 19.602 1.00 8.32 ? 274 PHE A C 1 ATOM 2129 O O . PHE A 1 274 ? 0.945 29.558 19.119 1.00 8.94 ? 274 PHE A O 1 ATOM 2130 C CB . PHE A 1 274 ? 1.059 29.485 21.965 1.00 7.77 ? 274 PHE A CB 1 ATOM 2131 C CG . PHE A 1 274 ? 0.267 28.221 22.123 1.00 7.94 ? 274 PHE A CG 1 ATOM 2132 C CD1 . PHE A 1 274 ? 0.778 26.964 21.929 1.00 8.74 ? 274 PHE A CD1 1 ATOM 2133 C CD2 . PHE A 1 274 ? -1.051 28.310 22.548 1.00 9.29 ? 274 PHE A CD2 1 ATOM 2134 C CE1 . PHE A 1 274 ? 0.006 25.836 22.142 1.00 10.12 ? 274 PHE A CE1 1 ATOM 2135 C CE2 . PHE A 1 274 ? -1.841 27.182 22.777 1.00 9.14 ? 274 PHE A CE2 1 ATOM 2136 C CZ . PHE A 1 274 ? -1.298 25.945 22.569 1.00 10.64 ? 274 PHE A CZ 1 ATOM 2137 N N . GLU A 1 275 ? 3.036 28.726 18.901 1.00 6.83 ? 275 GLU A N 1 ATOM 2138 C CA . GLU A 1 275 ? 3.144 28.906 17.450 1.00 7.46 ? 275 GLU A CA 1 ATOM 2139 C C . GLU A 1 275 ? 2.500 27.834 16.587 1.00 7.48 ? 275 GLU A C 1 ATOM 2140 O O . GLU A 1 275 ? 2.207 28.098 15.412 1.00 7.18 ? 275 GLU A O 1 ATOM 2141 C CB . GLU A 1 275 ? 4.637 29.065 17.112 1.00 7.19 ? 275 GLU A CB 1 ATOM 2142 C CG . GLU A 1 275 ? 4.954 29.338 15.646 1.00 8.64 ? 275 GLU A CG 1 ATOM 2143 C CD . GLU A 1 275 ? 6.432 29.424 15.362 1.00 7.72 ? 275 GLU A CD 1 ATOM 2144 O OE1 . GLU A 1 275 ? 7.151 28.429 15.658 1.00 7.98 ? 275 GLU A OE1 1 ATOM 2145 O OE2 . GLU A 1 275 ? 6.837 30.462 14.748 1.00 8.58 ? 275 GLU A OE2 1 ATOM 2146 N N . GLU A 1 276 ? 2.300 26.629 17.166 1.00 6.63 ? 276 GLU A N 1 ATOM 2147 C CA . GLU A 1 276 ? 1.527 25.585 16.523 1.00 6.43 ? 276 GLU A CA 1 ATOM 2148 C C . GLU A 1 276 ? 0.780 24.815 17.598 1.00 6.95 ? 276 GLU A C 1 ATOM 2149 O O . GLU A 1 276 ? 1.377 24.549 18.645 1.00 8.20 ? 276 GLU A O 1 ATOM 2150 C CB . GLU A 1 276 ? 2.312 24.531 15.741 1.00 7.20 ? 276 GLU A CB 1 ATOM 2151 C CG . GLU A 1 276 ? 3.102 24.967 14.548 1.00 6.93 ? 276 GLU A CG 1 ATOM 2152 C CD . GLU A 1 276 ? 3.745 23.807 13.800 1.00 8.70 ? 276 GLU A CD 1 ATOM 2153 O OE1 . GLU A 1 276 ? 3.309 22.641 13.994 1.00 8.45 ? 276 GLU A OE1 1 ATOM 2154 O OE2 . GLU A 1 276 ? 4.693 24.047 13.027 1.00 8.25 ? 276 GLU A OE2 1 ATOM 2155 N N . TYR A 1 277 ? -0.432 24.375 17.323 1.00 7.49 ? 277 TYR A N 1 ATOM 2156 C CA . TYR A 1 277 ? -1.135 23.456 18.221 1.00 7.86 ? 277 TYR A CA 1 ATOM 2157 C C . TYR A 1 277 ? -2.309 22.857 17.442 1.00 7.98 ? 277 TYR A C 1 ATOM 2158 O O . TYR A 1 277 ? -2.904 23.481 16.593 1.00 9.11 ? 277 TYR A O 1 ATOM 2159 C CB . TYR A 1 277 ? -1.590 24.133 19.505 1.00 7.47 ? 277 TYR A CB 1 ATOM 2160 C CG . TYR A 1 277 ? -2.502 25.336 19.355 1.00 7.29 ? 277 TYR A CG 1 ATOM 2161 C CD1 . TYR A 1 277 ? -3.891 25.188 19.273 1.00 7.81 ? 277 TYR A CD1 1 ATOM 2162 C CD2 . TYR A 1 277 ? -2.014 26.630 19.288 1.00 8.31 ? 277 TYR A CD2 1 ATOM 2163 C CE1 . TYR A 1 277 ? -4.718 26.290 19.169 1.00 8.83 ? 277 TYR A CE1 1 ATOM 2164 C CE2 . TYR A 1 277 ? -2.815 27.740 19.154 1.00 8.91 ? 277 TYR A CE2 1 ATOM 2165 C CZ . TYR A 1 277 ? -4.189 27.579 19.057 1.00 9.11 ? 277 TYR A CZ 1 ATOM 2166 O OH . TYR A 1 277 ? -4.997 28.681 18.961 1.00 10.00 ? 277 TYR A OH 1 ATOM 2167 N N . GLY A 1 278 ? -2.668 21.637 17.865 1.00 9.81 ? 278 GLY A N 1 ATOM 2168 C CA . GLY A 1 278 ? -3.845 20.997 17.261 1.00 9.97 ? 278 GLY A CA 1 ATOM 2169 C C . GLY A 1 278 ? -4.234 19.767 18.074 1.00 11.23 ? 278 GLY A C 1 ATOM 2170 O O . GLY A 1 278 ? -3.395 19.152 18.734 1.00 10.73 ? 278 GLY A O 1 ATOM 2171 N N . ALA A 1 279 ? -5.488 19.362 17.858 1.00 12.06 ? 279 ALA A N 1 ATOM 2172 C CA . ALA A 1 279 ? -6.040 18.123 18.431 1.00 13.01 ? 279 ALA A CA 1 ATOM 2173 C C . ALA A 1 279 ? -6.766 17.414 17.290 1.00 13.93 ? 279 ALA A C 1 ATOM 2174 O O . ALA A 1 279 ? -7.632 18.074 16.701 1.00 16.02 ? 279 ALA A O 1 ATOM 2175 C CB . ALA A 1 279 ? -6.921 18.418 19.608 1.00 11.75 ? 279 ALA A CB 1 ATOM 2176 N N . GLN A 1 280 ? -6.535 16.099 17.140 1.00 16.39 ? 280 GLN A N 1 ATOM 2177 C CA . GLN A 1 280 ? -7.242 15.402 16.042 1.00 17.44 ? 280 GLN A CA 1 ATOM 2178 C C . GLN A 1 280 ? -8.682 15.078 16.434 1.00 17.59 ? 280 GLN A C 1 ATOM 2179 O O . GLN A 1 280 ? -9.577 15.015 15.571 1.00 18.93 ? 280 GLN A O 1 ATOM 2180 C CB . GLN A 1 280 ? -6.480 14.113 15.705 1.00 21.34 ? 280 GLN A CB 1 ATOM 2181 C CG . GLN A 1 280 ? -5.172 14.415 14.983 1.00 26.28 ? 280 GLN A CG 1 ATOM 2182 C CD . GLN A 1 280 ? -4.439 13.178 14.511 1.00 31.69 ? 280 GLN A CD 1 ATOM 2183 O OE1 . GLN A 1 280 ? -3.267 12.954 14.846 1.00 35.00 ? 280 GLN A OE1 1 ATOM 2184 N NE2 . GLN A 1 280 ? -5.173 12.392 13.735 1.00 32.70 ? 280 GLN A NE2 1 ATOM 2185 N N . GLN A 1 281 ? -8.899 14.795 17.713 1.00 17.14 ? 281 GLN A N 1 ATOM 2186 C CA . GLN A 1 281 ? -10.235 14.458 18.180 1.00 19.15 ? 281 GLN A CA 1 ATOM 2187 C C . GLN A 1 281 ? -10.863 15.645 18.879 1.00 17.39 ? 281 GLN A C 1 ATOM 2188 O O . GLN A 1 281 ? -10.216 16.289 19.722 1.00 18.70 ? 281 GLN A O 1 ATOM 2189 C CB . GLN A 1 281 ? -10.187 13.312 19.219 1.00 23.76 ? 281 GLN A CB 1 ATOM 2190 C CG A GLN A 1 281 ? -9.467 12.061 18.725 0.50 27.29 ? 281 GLN A CG 1 ATOM 2191 C CG B GLN A 1 281 ? -9.511 12.055 18.683 0.50 28.00 ? 281 GLN A CG 1 ATOM 2192 C CD A GLN A 1 281 ? -10.189 11.510 17.502 0.50 29.40 ? 281 GLN A CD 1 ATOM 2193 C CD B GLN A 1 281 ? -9.455 10.910 19.667 0.50 30.80 ? 281 GLN A CD 1 ATOM 2194 O OE1 A GLN A 1 281 ? -11.408 11.351 17.561 0.50 30.84 ? 281 GLN A OE1 1 ATOM 2195 O OE1 B GLN A 1 281 ? -8.619 10.003 19.551 0.50 33.13 ? 281 GLN A OE1 1 ATOM 2196 N NE2 A GLN A 1 281 ? -9.444 11.274 16.433 0.50 30.15 ? 281 GLN A NE2 1 ATOM 2197 N NE2 B GLN A 1 281 ? -10.338 10.923 20.657 0.50 31.91 ? 281 GLN A NE2 1 ATOM 2198 N N . ASN A 1 282 ? -12.130 15.962 18.591 1.00 17.98 ? 282 ASN A N 1 ATOM 2199 C CA . ASN A 1 282 ? -12.878 16.998 19.282 1.00 17.37 ? 282 ASN A CA 1 ATOM 2200 C C . ASN A 1 282 ? -12.066 18.273 19.534 1.00 15.62 ? 282 ASN A C 1 ATOM 2201 O O . ASN A 1 282 ? -11.909 18.768 20.645 1.00 16.08 ? 282 ASN A O 1 ATOM 2202 C CB . ASN A 1 282 ? -13.404 16.462 20.619 1.00 19.54 ? 282 ASN A CB 1 ATOM 2203 C CG . ASN A 1 282 ? -14.153 15.146 20.490 1.00 21.57 ? 282 ASN A CG 1 ATOM 2204 O OD1 . ASN A 1 282 ? -13.648 14.078 20.883 1.00 23.32 ? 282 ASN A OD1 1 ATOM 2205 N ND2 . ASN A 1 282 ? -15.289 15.253 19.820 1.00 22.17 ? 282 ASN A ND2 1 ATOM 2206 N N . PRO A 1 283 ? -11.656 18.917 18.457 1.00 14.27 ? 283 PRO A N 1 ATOM 2207 C CA . PRO A 1 283 ? -10.819 20.130 18.553 1.00 13.29 ? 283 PRO A CA 1 ATOM 2208 C C . PRO A 1 283 ? -11.481 21.305 19.243 1.00 13.84 ? 283 PRO A C 1 ATOM 2209 O O . PRO A 1 283 ? -10.806 22.019 20.002 1.00 14.07 ? 283 PRO A O 1 ATOM 2210 C CB . PRO A 1 283 ? -10.418 20.446 17.122 1.00 15.39 ? 283 PRO A CB 1 ATOM 2211 C CG . PRO A 1 283 ? -11.474 19.800 16.297 1.00 15.70 ? 283 PRO A CG 1 ATOM 2212 C CD . PRO A 1 283 ? -11.799 18.519 17.034 1.00 14.68 ? 283 PRO A CD 1 ATOM 2213 N N . CYS A 1 284 ? -12.795 21.504 19.080 1.00 13.68 ? 284 CYS A N 1 ATOM 2214 C CA . CYS A 1 284 ? -13.412 22.624 19.799 1.00 14.59 ? 284 CYS A CA 1 ATOM 2215 C C . CYS A 1 284 ? -13.354 22.420 21.315 1.00 15.50 ? 284 CYS A C 1 ATOM 2216 O O . CYS A 1 284 ? -12.910 23.309 22.039 1.00 17.32 ? 284 CYS A O 1 ATOM 2217 C CB . CYS A 1 284 ? -14.855 22.790 19.356 1.00 15.53 ? 284 CYS A CB 1 ATOM 2218 S SG . CYS A 1 284 ? -15.770 24.087 20.152 1.00 17.01 ? 284 CYS A SG 1 ATOM 2219 N N . THR A 1 285 ? -13.714 21.192 21.767 1.00 15.55 ? 285 THR A N 1 ATOM 2220 C CA . THR A 1 285 ? -13.625 20.888 23.191 1.00 17.35 ? 285 THR A CA 1 ATOM 2221 C C . THR A 1 285 ? -12.215 20.922 23.767 1.00 15.48 ? 285 THR A C 1 ATOM 2222 O O . THR A 1 285 ? -12.005 21.469 24.860 1.00 15.76 ? 285 THR A O 1 ATOM 2223 C CB . THR A 1 285 ? -14.261 19.499 23.429 1.00 18.92 ? 285 THR A CB 1 ATOM 2224 O OG1 . THR A 1 285 ? -15.645 19.596 23.019 1.00 21.54 ? 285 THR A OG1 1 ATOM 2225 C CG2 . THR A 1 285 ? -14.197 19.009 24.861 1.00 20.49 ? 285 THR A CG2 1 ATOM 2226 N N . ASN A 1 286 ? -11.275 20.311 23.052 1.00 13.84 ? 286 ASN A N 1 ATOM 2227 C CA . ASN A 1 286 ? -9.937 20.125 23.555 1.00 13.05 ? 286 ASN A CA 1 ATOM 2228 C C . ASN A 1 286 ? -9.006 21.315 23.383 1.00 11.66 ? 286 ASN A C 1 ATOM 2229 O O . ASN A 1 286 ? -8.107 21.420 24.227 1.00 13.09 ? 286 ASN A O 1 ATOM 2230 C CB . ASN A 1 286 ? -9.345 18.840 22.936 1.00 13.76 ? 286 ASN A CB 1 ATOM 2231 C CG . ASN A 1 286 ? -10.089 17.605 23.447 1.00 18.11 ? 286 ASN A CG 1 ATOM 2232 O OD1 . ASN A 1 286 ? -10.336 17.411 24.633 1.00 19.28 ? 286 ASN A OD1 1 ATOM 2233 N ND2 . ASN A 1 286 ? -10.397 16.721 22.504 1.00 20.05 ? 286 ASN A ND2 1 ATOM 2234 N N . GLU A 1 287 ? -9.168 22.132 22.345 1.00 11.71 ? 287 GLU A N 1 ATOM 2235 C CA . GLU A 1 287 ? -8.259 23.240 22.088 1.00 10.99 ? 287 GLU A CA 1 ATOM 2236 C C . GLU A 1 287 ? -8.700 24.556 22.717 1.00 11.85 ? 287 GLU A C 1 ATOM 2237 O O . GLU A 1 287 ? -7.877 25.412 23.063 1.00 12.73 ? 287 GLU A O 1 ATOM 2238 C CB . GLU A 1 287 ? -7.986 23.493 20.590 1.00 11.68 ? 287 GLU A CB 1 ATOM 2239 C CG . GLU A 1 287 ? -7.470 22.254 19.842 1.00 12.35 ? 287 GLU A CG 1 ATOM 2240 C CD . GLU A 1 287 ? -7.154 22.530 18.407 1.00 13.90 ? 287 GLU A CD 1 ATOM 2241 O OE1 . GLU A 1 287 ? -6.730 23.661 18.090 1.00 14.50 ? 287 GLU A OE1 1 ATOM 2242 O OE2 . GLU A 1 287 ? -7.346 21.617 17.580 1.00 14.48 ? 287 GLU A OE2 1 ATOM 2243 N N . ALA A 1 288 ? -10.016 24.758 22.928 1.00 12.47 ? 288 ALA A N 1 ATOM 2244 C CA . ALA A 1 288 ? -10.479 25.983 23.562 1.00 12.97 ? 288 ALA A CA 1 ATOM 2245 C C . ALA A 1 288 ? -9.825 26.296 24.894 1.00 13.44 ? 288 ALA A C 1 ATOM 2246 O O . ALA A 1 288 ? -9.375 27.428 25.159 1.00 13.59 ? 288 ALA A O 1 ATOM 2247 C CB . ALA A 1 288 ? -11.997 25.974 23.666 1.00 14.83 ? 288 ALA A CB 1 ATOM 2248 N N . PRO A 1 289 ? -9.654 25.304 25.778 1.00 12.96 ? 289 PRO A N 1 ATOM 2249 C CA . PRO A 1 289 ? -8.983 25.583 27.043 1.00 14.32 ? 289 PRO A CA 1 ATOM 2250 C C . PRO A 1 289 ? -7.557 26.066 26.856 1.00 12.37 ? 289 PRO A C 1 ATOM 2251 O O . PRO A 1 289 ? -7.077 26.880 27.637 1.00 12.39 ? 289 PRO A O 1 ATOM 2252 C CB . PRO A 1 289 ? -9.025 24.241 27.778 1.00 14.99 ? 289 PRO A CB 1 ATOM 2253 C CG . PRO A 1 289 ? -10.170 23.487 27.188 1.00 16.43 ? 289 PRO A CG 1 ATOM 2254 C CD . PRO A 1 289 ? -10.267 23.956 25.747 1.00 14.87 ? 289 PRO A CD 1 ATOM 2255 N N . TRP A 1 290 ? -6.867 25.527 25.839 1.00 11.27 ? 290 TRP A N 1 ATOM 2256 C CA . TRP A 1 290 ? -5.498 25.971 25.569 1.00 10.55 ? 290 TRP A CA 1 ATOM 2257 C C . TRP A 1 290 ? -5.436 27.443 25.168 1.00 10.96 ? 290 TRP A C 1 ATOM 2258 O O . TRP A 1 290 ? -4.564 28.208 25.604 1.00 11.02 ? 290 TRP A O 1 ATOM 2259 C CB . TRP A 1 290 ? -4.883 25.116 24.455 1.00 10.48 ? 290 TRP A CB 1 ATOM 2260 C CG . TRP A 1 290 ? -4.818 23.652 24.649 1.00 9.97 ? 290 TRP A CG 1 ATOM 2261 C CD1 . TRP A 1 290 ? -4.936 22.917 25.811 1.00 9.88 ? 290 TRP A CD1 1 ATOM 2262 C CD2 . TRP A 1 290 ? -4.552 22.707 23.602 1.00 8.73 ? 290 TRP A CD2 1 ATOM 2263 N NE1 . TRP A 1 290 ? -4.808 21.583 25.537 1.00 9.68 ? 290 TRP A NE1 1 ATOM 2264 C CE2 . TRP A 1 290 ? -4.576 21.422 24.189 1.00 9.64 ? 290 TRP A CE2 1 ATOM 2265 C CE3 . TRP A 1 290 ? -4.322 22.818 22.220 1.00 9.90 ? 290 TRP A CE3 1 ATOM 2266 C CZ2 . TRP A 1 290 ? -4.348 20.257 23.449 1.00 10.29 ? 290 TRP A CZ2 1 ATOM 2267 C CZ3 . TRP A 1 290 ? -4.132 21.659 21.474 1.00 9.40 ? 290 TRP A CZ3 1 ATOM 2268 C CH2 . TRP A 1 290 ? -4.136 20.389 22.097 1.00 10.56 ? 290 TRP A CH2 1 ATOM 2269 N N . GLN A 1 291 ? -6.400 27.834 24.333 1.00 10.33 ? 291 GLN A N 1 ATOM 2270 C CA . GLN A 1 291 ? -6.480 29.234 23.889 1.00 10.53 ? 291 GLN A CA 1 ATOM 2271 C C . GLN A 1 291 ? -6.733 30.162 25.087 1.00 11.40 ? 291 GLN A C 1 ATOM 2272 O O . GLN A 1 291 ? -6.092 31.190 25.255 1.00 12.00 ? 291 GLN A O 1 ATOM 2273 C CB . GLN A 1 291 ? -7.618 29.389 22.877 1.00 10.29 ? 291 GLN A CB 1 ATOM 2274 C CG . GLN A 1 291 ? -7.331 28.639 21.572 1.00 10.85 ? 291 GLN A CG 1 ATOM 2275 C CD . GLN A 1 291 ? -8.357 28.895 20.503 1.00 11.90 ? 291 GLN A CD 1 ATOM 2276 O OE1 . GLN A 1 291 ? -9.548 29.071 20.871 1.00 13.32 ? 291 GLN A OE1 1 ATOM 2277 N NE2 . GLN A 1 291 ? -7.919 28.903 19.254 1.00 10.24 ? 291 GLN A NE2 1 ATOM 2278 N N . THR A 1 292 ? -7.614 29.736 26.011 1.00 11.60 ? 292 THR A N 1 ATOM 2279 C CA . THR A 1 292 ? -7.839 30.536 27.215 1.00 12.63 ? 292 THR A CA 1 ATOM 2280 C C . THR A 1 292 ? -6.613 30.575 28.109 1.00 12.13 ? 292 THR A C 1 ATOM 2281 O O . THR A 1 292 ? -6.265 31.662 28.629 1.00 12.20 ? 292 THR A O 1 ATOM 2282 C CB . THR A 1 292 ? -9.047 29.981 27.982 1.00 14.12 ? 292 THR A CB 1 ATOM 2283 O OG1 . THR A 1 292 ? -10.207 30.158 27.153 1.00 15.20 ? 292 THR A OG1 1 ATOM 2284 C CG2 . THR A 1 292 ? -9.265 30.672 29.324 1.00 15.55 ? 292 THR A CG2 1 ATOM 2285 N N . THR A 1 293 ? -5.934 29.447 28.291 1.00 11.82 ? 293 THR A N 1 ATOM 2286 C CA . THR A 1 293 ? -4.721 29.446 29.112 1.00 11.16 ? 293 THR A CA 1 ATOM 2287 C C . THR A 1 293 ? -3.688 30.393 28.534 1.00 12.05 ? 293 THR A C 1 ATOM 2288 O O . THR A 1 293 ? -3.117 31.221 29.236 1.00 13.13 ? 293 THR A O 1 ATOM 2289 C CB . THR A 1 293 ? -4.169 28.017 29.231 1.00 10.73 ? 293 THR A CB 1 ATOM 2290 O OG1 . THR A 1 293 ? -5.140 27.185 29.899 1.00 12.66 ? 293 THR A OG1 1 ATOM 2291 C CG2 . THR A 1 293 ? -2.878 28.001 30.030 1.00 12.65 ? 293 THR A CG2 1 ATOM 2292 N N . SER A 1 294 ? -3.480 30.331 27.208 1.00 10.93 ? 294 SER A N 1 ATOM 2293 C CA . SER A 1 294 ? -2.489 31.228 26.589 1.00 10.08 ? 294 SER A CA 1 ATOM 2294 C C . SER A 1 294 ? -2.844 32.691 26.746 1.00 11.86 ? 294 SER A C 1 ATOM 2295 O O . SER A 1 294 ? -1.994 33.498 27.143 1.00 12.47 ? 294 SER A O 1 ATOM 2296 C CB . SER A 1 294 ? -2.369 30.829 25.113 1.00 10.24 ? 294 SER A CB 1 ATOM 2297 O OG . SER A 1 294 ? -1.281 31.545 24.519 1.00 10.41 ? 294 SER A OG 1 ATOM 2298 N N . LEU A 1 295 ? -4.116 33.050 26.529 1.00 11.52 ? 295 LEU A N 1 ATOM 2299 C CA . LEU A 1 295 ? -4.567 34.432 26.627 1.00 13.26 ? 295 LEU A CA 1 ATOM 2300 C C . LEU A 1 295 ? -4.408 34.966 28.047 1.00 12.93 ? 295 LEU A C 1 ATOM 2301 O O . LEU A 1 295 ? -4.089 36.160 28.215 1.00 16.32 ? 295 LEU A O 1 ATOM 2302 C CB . LEU A 1 295 ? -6.048 34.511 26.156 1.00 13.39 ? 295 LEU A CB 1 ATOM 2303 C CG . LEU A 1 295 ? -6.733 35.864 26.282 1.00 14.43 ? 295 LEU A CG 1 ATOM 2304 C CD1 . LEU A 1 295 ? -5.940 36.943 25.554 1.00 16.45 ? 295 LEU A CD1 1 ATOM 2305 C CD2 . LEU A 1 295 ? -8.157 35.744 25.728 1.00 15.82 ? 295 LEU A CD2 1 ATOM 2306 N N . THR A 1 296 ? -4.526 34.126 29.061 1.00 12.47 ? 296 THR A N 1 ATOM 2307 C CA . THR A 1 296 ? -4.511 34.577 30.438 1.00 15.26 ? 296 THR A CA 1 ATOM 2308 C C . THR A 1 296 ? -3.222 34.288 31.199 1.00 15.74 ? 296 THR A C 1 ATOM 2309 O O . THR A 1 296 ? -3.195 34.451 32.431 1.00 19.25 ? 296 THR A O 1 ATOM 2310 C CB . THR A 1 296 ? -5.715 33.975 31.196 1.00 16.12 ? 296 THR A CB 1 ATOM 2311 O OG1 . THR A 1 296 ? -5.646 32.557 31.241 1.00 17.37 ? 296 THR A OG1 1 ATOM 2312 C CG2 . THR A 1 296 ? -7.062 34.395 30.611 1.00 16.23 ? 296 THR A CG2 1 ATOM 2313 N N . THR A 1 297 ? -2.155 33.871 30.511 1.00 14.31 ? 297 THR A N 1 ATOM 2314 C CA . THR A 1 297 ? -0.895 33.586 31.187 1.00 14.03 ? 297 THR A CA 1 ATOM 2315 C C . THR A 1 297 ? 0.184 34.619 30.868 1.00 14.20 ? 297 THR A C 1 ATOM 2316 O O . THR A 1 297 ? 0.493 34.936 29.711 1.00 15.03 ? 297 THR A O 1 ATOM 2317 C CB . THR A 1 297 ? -0.378 32.185 30.847 1.00 13.63 ? 297 THR A CB 1 ATOM 2318 O OG1 . THR A 1 297 ? -1.325 31.188 31.246 1.00 15.19 ? 297 THR A OG1 1 ATOM 2319 C CG2 . THR A 1 297 ? 0.925 31.853 31.536 1.00 15.82 ? 297 THR A CG2 1 ATOM 2320 N N . ARG A 1 298 ? 0.748 35.192 31.948 1.00 14.40 ? 298 ARG A N 1 ATOM 2321 C CA . ARG A 1 298 ? 1.804 36.190 31.762 1.00 16.49 ? 298 ARG A CA 1 ATOM 2322 C C . ARG A 1 298 ? 2.992 35.547 31.021 1.00 14.80 ? 298 ARG A C 1 ATOM 2323 O O . ARG A 1 298 ? 3.377 34.441 31.363 1.00 15.45 ? 298 ARG A O 1 ATOM 2324 C CB . ARG A 1 298 ? 2.298 36.719 33.113 1.00 21.51 ? 298 ARG A CB 1 ATOM 2325 C CG . ARG A 1 298 ? 1.417 37.811 33.698 1.00 27.70 ? 298 ARG A CG 1 ATOM 2326 C CD . ARG A 1 298 ? 1.839 39.203 33.267 1.00 32.13 ? 298 ARG A CD 1 ATOM 2327 N NE . ARG A 1 298 ? 3.277 39.579 33.277 1.00 33.25 ? 298 ARG A NE 1 ATOM 2328 C CZ . ARG A 1 298 ? 3.639 40.697 32.638 1.00 33.28 ? 298 ARG A CZ 1 ATOM 2329 N NH1 . ARG A 1 298 ? 2.683 41.453 32.045 1.00 33.16 ? 298 ARG A NH1 1 ATOM 2330 N NH2 . ARG A 1 298 ? 4.878 41.127 32.474 1.00 32.92 ? 298 ARG A NH2 1 ATOM 2331 N N . GLY A 1 299 ? 3.564 36.308 30.094 1.00 13.33 ? 299 GLY A N 1 ATOM 2332 C CA . GLY A 1 299 ? 4.678 35.786 29.292 1.00 13.93 ? 299 GLY A CA 1 ATOM 2333 C C . GLY A 1 299 ? 4.229 35.398 27.891 1.00 12.72 ? 299 GLY A C 1 ATOM 2334 O O . GLY A 1 299 ? 5.048 35.291 26.977 1.00 14.10 ? 299 GLY A O 1 ATOM 2335 N N . MET A 1 300 ? 2.942 35.130 27.689 1.00 11.92 ? 300 MET A N 1 ATOM 2336 C CA . MET A 1 300 ? 2.461 34.790 26.365 1.00 10.53 ? 300 MET A CA 1 ATOM 2337 C C . MET A 1 300 ? 2.088 36.029 25.538 1.00 12.69 ? 300 MET A C 1 ATOM 2338 O O . MET A 1 300 ? 1.261 36.831 25.987 1.00 16.87 ? 300 MET A O 1 ATOM 2339 C CB . MET A 1 300 ? 1.198 33.941 26.450 1.00 10.68 ? 300 MET A CB 1 ATOM 2340 C CG . MET A 1 300 ? 1.422 32.581 27.061 1.00 10.43 ? 300 MET A CG 1 ATOM 2341 S SD . MET A 1 300 ? 2.720 31.602 26.293 1.00 9.09 ? 300 MET A SD 1 ATOM 2342 C CE . MET A 1 300 ? 2.203 31.727 24.573 1.00 10.48 ? 300 MET A CE 1 ATOM 2343 N N . GLY A 1 301 ? 2.667 36.189 24.371 1.00 9.99 ? 301 GLY A N 1 ATOM 2344 C CA . GLY A 1 301 ? 2.365 37.268 23.470 1.00 10.38 ? 301 GLY A CA 1 ATOM 2345 C C . GLY A 1 301 ? 1.350 37.006 22.389 1.00 10.23 ? 301 GLY A C 1 ATOM 2346 O O . GLY A 1 301 ? 0.789 37.966 21.833 1.00 10.51 ? 301 GLY A O 1 ATOM 2347 N N . GLY A 1 302 ? 1.091 35.719 22.103 1.00 9.03 ? 302 GLY A N 1 ATOM 2348 C CA . GLY A 1 302 ? 0.109 35.407 21.067 1.00 9.41 ? 302 GLY A CA 1 ATOM 2349 C C . GLY A 1 302 ? 0.098 33.904 20.830 1.00 9.21 ? 302 GLY A C 1 ATOM 2350 O O . GLY A 1 302 ? 0.957 33.159 21.346 1.00 9.91 ? 302 GLY A O 1 ATOM 2351 N N . ASP A 1 303 ? -0.870 33.489 20.015 1.00 8.20 ? 303 ASP A N 1 ATOM 2352 C CA . ASP A 1 303 ? -1.040 32.076 19.676 1.00 8.71 ? 303 ASP A CA 1 ATOM 2353 C C . ASP A 1 303 ? -1.514 31.897 18.235 1.00 8.43 ? 303 ASP A C 1 ATOM 2354 O O . ASP A 1 303 ? -2.143 32.768 17.647 1.00 9.20 ? 303 ASP A O 1 ATOM 2355 C CB . ASP A 1 303 ? -1.996 31.326 20.633 1.00 9.44 ? 303 ASP A CB 1 ATOM 2356 C CG . ASP A 1 303 ? -3.460 31.699 20.396 1.00 9.47 ? 303 ASP A CG 1 ATOM 2357 O OD1 . ASP A 1 303 ? -4.081 31.086 19.508 1.00 10.45 ? 303 ASP A OD1 1 ATOM 2358 O OD2 . ASP A 1 303 ? -3.938 32.605 21.103 1.00 11.67 ? 303 ASP A OD2 1 ATOM 2359 N N . MET A 1 304 ? -1.065 30.759 17.635 1.00 7.97 ? 304 MET A N 1 ATOM 2360 C CA . MET A 1 304 ? -1.316 30.473 16.209 1.00 8.26 ? 304 MET A CA 1 ATOM 2361 C C . MET A 1 304 ? -1.658 29.003 16.050 1.00 8.43 ? 304 MET A C 1 ATOM 2362 O O . MET A 1 304 ? -0.804 28.129 16.127 1.00 9.05 ? 304 MET A O 1 ATOM 2363 C CB . MET A 1 304 ? -0.115 30.826 15.312 1.00 8.89 ? 304 MET A CB 1 ATOM 2364 C CG . MET A 1 304 ? 0.414 32.217 15.599 1.00 10.03 ? 304 MET A CG 1 ATOM 2365 S SD . MET A 1 304 ? 1.919 32.736 14.817 1.00 9.53 ? 304 MET A SD 1 ATOM 2366 C CE . MET A 1 304 ? 1.393 32.737 13.101 1.00 10.72 ? 304 MET A CE 1 ATOM 2367 N N . PHE A 1 305 ? -2.929 28.685 15.798 1.00 8.33 ? 305 PHE A N 1 ATOM 2368 C CA . PHE A 1 305 ? -3.330 27.295 15.629 1.00 8.68 ? 305 PHE A CA 1 ATOM 2369 C C . PHE A 1 305 ? -2.776 26.711 14.326 1.00 8.21 ? 305 PHE A C 1 ATOM 2370 O O . PHE A 1 305 ? -2.541 27.432 13.331 1.00 7.59 ? 305 PHE A O 1 ATOM 2371 C CB . PHE A 1 305 ? -4.871 27.149 15.701 1.00 9.47 ? 305 PHE A CB 1 ATOM 2372 C CG . PHE A 1 305 ? -5.634 27.773 14.565 1.00 9.22 ? 305 PHE A CG 1 ATOM 2373 C CD1 . PHE A 1 305 ? -6.033 29.096 14.633 1.00 9.79 ? 305 PHE A CD1 1 ATOM 2374 C CD2 . PHE A 1 305 ? -5.945 27.040 13.410 1.00 9.21 ? 305 PHE A CD2 1 ATOM 2375 C CE1 . PHE A 1 305 ? -6.766 29.662 13.600 1.00 10.87 ? 305 PHE A CE1 1 ATOM 2376 C CE2 . PHE A 1 305 ? -6.714 27.578 12.404 1.00 11.67 ? 305 PHE A CE2 1 ATOM 2377 C CZ . PHE A 1 305 ? -7.080 28.900 12.498 1.00 10.36 ? 305 PHE A CZ 1 ATOM 2378 N N . TRP A 1 306 ? -2.619 25.391 14.336 1.00 6.54 ? 306 TRP A N 1 ATOM 2379 C CA . TRP A 1 306 ? -2.317 24.606 13.119 1.00 6.82 ? 306 TRP A CA 1 ATOM 2380 C C . TRP A 1 306 ? -3.612 23.882 12.755 1.00 6.97 ? 306 TRP A C 1 ATOM 2381 O O . TRP A 1 306 ? -4.052 23.048 13.546 1.00 8.64 ? 306 TRP A O 1 ATOM 2382 C CB . TRP A 1 306 ? -1.198 23.596 13.400 1.00 6.94 ? 306 TRP A CB 1 ATOM 2383 C CG . TRP A 1 306 ? -0.802 22.844 12.176 1.00 7.11 ? 306 TRP A CG 1 ATOM 2384 C CD1 . TRP A 1 306 ? -1.444 21.716 11.680 1.00 7.99 ? 306 TRP A CD1 1 ATOM 2385 C CD2 . TRP A 1 306 ? 0.240 23.134 11.224 1.00 7.88 ? 306 TRP A CD2 1 ATOM 2386 N NE1 . TRP A 1 306 ? -0.845 21.300 10.511 1.00 8.30 ? 306 TRP A NE1 1 ATOM 2387 C CE2 . TRP A 1 306 ? 0.182 22.156 10.203 1.00 7.30 ? 306 TRP A CE2 1 ATOM 2388 C CE3 . TRP A 1 306 ? 1.220 24.117 11.127 1.00 7.44 ? 306 TRP A CE3 1 ATOM 2389 C CZ2 . TRP A 1 306 ? 1.048 22.131 9.116 1.00 8.10 ? 306 TRP A CZ2 1 ATOM 2390 C CZ3 . TRP A 1 306 ? 2.119 24.082 10.056 1.00 7.51 ? 306 TRP A CZ3 1 ATOM 2391 C CH2 . TRP A 1 306 ? 2.021 23.106 9.055 1.00 7.19 ? 306 TRP A CH2 1 ATOM 2392 N N . GLN A 1 307 ? -4.240 24.204 11.639 1.00 7.81 ? 307 GLN A N 1 ATOM 2393 C CA . GLN A 1 307 ? -3.825 25.100 10.598 1.00 6.22 ? 307 GLN A CA 1 ATOM 2394 C C . GLN A 1 307 ? -5.037 25.626 9.803 1.00 7.24 ? 307 GLN A C 1 ATOM 2395 O O . GLN A 1 307 ? -6.128 25.021 9.905 1.00 8.17 ? 307 GLN A O 1 ATOM 2396 C CB . GLN A 1 307 ? -2.893 24.430 9.565 1.00 7.40 ? 307 GLN A CB 1 ATOM 2397 C CG . GLN A 1 307 ? -3.531 23.301 8.763 1.00 8.41 ? 307 GLN A CG 1 ATOM 2398 C CD . GLN A 1 307 ? -2.687 22.770 7.630 1.00 9.10 ? 307 GLN A CD 1 ATOM 2399 O OE1 . GLN A 1 307 ? -1.963 23.554 6.974 1.00 9.10 ? 307 GLN A OE1 1 ATOM 2400 N NE2 . GLN A 1 307 ? -2.791 21.470 7.370 1.00 9.45 ? 307 GLN A NE2 1 ATOM 2401 N N . TRP A 1 308 ? -4.852 26.714 9.092 1.00 7.12 ? 308 TRP A N 1 ATOM 2402 C CA . TRP A 1 308 ? -5.923 27.266 8.251 1.00 7.37 ? 308 TRP A CA 1 ATOM 2403 C C . TRP A 1 308 ? -6.219 26.322 7.098 1.00 7.78 ? 308 TRP A C 1 ATOM 2404 O O . TRP A 1 308 ? -5.307 25.770 6.478 1.00 8.47 ? 308 TRP A O 1 ATOM 2405 C CB . TRP A 1 308 ? -5.436 28.607 7.686 1.00 7.59 ? 308 TRP A CB 1 ATOM 2406 C CG . TRP A 1 308 ? -6.519 29.451 7.077 1.00 8.11 ? 308 TRP A CG 1 ATOM 2407 C CD1 . TRP A 1 308 ? -6.853 29.562 5.764 1.00 8.03 ? 308 TRP A CD1 1 ATOM 2408 C CD2 . TRP A 1 308 ? -7.442 30.255 7.817 1.00 7.93 ? 308 TRP A CD2 1 ATOM 2409 N NE1 . TRP A 1 308 ? -7.923 30.435 5.622 1.00 8.54 ? 308 TRP A NE1 1 ATOM 2410 C CE2 . TRP A 1 308 ? -8.301 30.856 6.873 1.00 8.18 ? 308 TRP A CE2 1 ATOM 2411 C CE3 . TRP A 1 308 ? -7.571 30.584 9.176 1.00 7.91 ? 308 TRP A CE3 1 ATOM 2412 C CZ2 . TRP A 1 308 ? -9.310 31.761 7.248 1.00 8.08 ? 308 TRP A CZ2 1 ATOM 2413 C CZ3 . TRP A 1 308 ? -8.583 31.438 9.552 1.00 9.00 ? 308 TRP A CZ3 1 ATOM 2414 C CH2 . TRP A 1 308 ? -9.440 32.015 8.586 1.00 9.37 ? 308 TRP A CH2 1 ATOM 2415 N N . GLY A 1 309 ? -7.511 26.148 6.784 1.00 7.74 ? 309 GLY A N 1 ATOM 2416 C CA . GLY A 1 309 ? -7.965 25.501 5.562 1.00 8.50 ? 309 GLY A CA 1 ATOM 2417 C C . GLY A 1 309 ? -8.879 26.477 4.808 1.00 8.11 ? 309 GLY A C 1 ATOM 2418 O O . GLY A 1 309 ? -9.603 27.240 5.453 1.00 9.00 ? 309 GLY A O 1 ATOM 2419 N N . ASP A 1 310 ? -8.779 26.451 3.471 1.00 7.82 ? 310 ASP A N 1 ATOM 2420 C CA . ASP A 1 310 ? -9.628 27.360 2.714 1.00 8.36 ? 310 ASP A CA 1 ATOM 2421 C C . ASP A 1 310 ? -9.917 26.749 1.360 1.00 8.74 ? 310 ASP A C 1 ATOM 2422 O O . ASP A 1 310 ? -9.417 25.661 0.992 1.00 9.54 ? 310 ASP A O 1 ATOM 2423 C CB . ASP A 1 310 ? -8.996 28.754 2.580 1.00 9.20 ? 310 ASP A CB 1 ATOM 2424 C CG . ASP A 1 310 ? -10.021 29.887 2.684 1.00 7.75 ? 310 ASP A CG 1 ATOM 2425 O OD1 . ASP A 1 310 ? -11.132 29.748 2.112 1.00 9.94 ? 310 ASP A OD1 1 ATOM 2426 O OD2 . ASP A 1 310 ? -9.613 30.936 3.259 1.00 10.01 ? 310 ASP A OD2 1 ATOM 2427 N N . THR A 1 311 ? -10.772 27.401 0.590 1.00 8.62 ? 311 THR A N 1 ATOM 2428 C CA . THR A 1 311 ? -11.181 26.944 -0.728 1.00 9.61 ? 311 THR A CA 1 ATOM 2429 C C . THR A 1 311 ? -11.145 28.133 -1.675 1.00 8.89 ? 311 THR A C 1 ATOM 2430 O O . THR A 1 311 ? -11.096 29.305 -1.243 1.00 10.29 ? 311 THR A O 1 ATOM 2431 C CB . THR A 1 311 ? -12.565 26.280 -0.772 1.00 10.01 ? 311 THR A CB 1 ATOM 2432 O OG1 . THR A 1 311 ? -13.550 27.272 -0.524 1.00 11.18 ? 311 THR A OG1 1 ATOM 2433 C CG2 . THR A 1 311 ? -12.705 25.146 0.243 1.00 10.53 ? 311 THR A CG2 1 ATOM 2434 N N . PHE A 1 312 ? -11.040 27.893 -2.964 1.00 8.83 ? 312 PHE A N 1 ATOM 2435 C CA . PHE A 1 312 ? -10.698 28.857 -3.994 1.00 9.44 ? 312 PHE A CA 1 ATOM 2436 C C . PHE A 1 312 ? -11.847 29.106 -4.964 1.00 10.48 ? 312 PHE A C 1 ATOM 2437 O O . PHE A 1 312 ? -12.791 28.309 -5.064 1.00 10.99 ? 312 PHE A O 1 ATOM 2438 C CB . PHE A 1 312 ? -9.422 28.383 -4.716 1.00 9.80 ? 312 PHE A CB 1 ATOM 2439 C CG . PHE A 1 312 ? -8.296 28.045 -3.759 1.00 9.51 ? 312 PHE A CG 1 ATOM 2440 C CD1 . PHE A 1 312 ? -7.962 28.875 -2.683 1.00 10.21 ? 312 PHE A CD1 1 ATOM 2441 C CD2 . PHE A 1 312 ? -7.602 26.881 -3.892 1.00 10.94 ? 312 PHE A CD2 1 ATOM 2442 C CE1 . PHE A 1 312 ? -6.978 28.530 -1.790 1.00 10.53 ? 312 PHE A CE1 1 ATOM 2443 C CE2 . PHE A 1 312 ? -6.606 26.538 -2.981 1.00 11.36 ? 312 PHE A CE2 1 ATOM 2444 C CZ . PHE A 1 312 ? -6.247 27.371 -1.939 1.00 10.60 ? 312 PHE A CZ 1 ATOM 2445 N N . ALA A 1 313 ? -11.687 30.159 -5.763 1.00 11.45 ? 313 ALA A N 1 ATOM 2446 C CA . ALA A 1 313 ? -12.779 30.531 -6.682 1.00 12.08 ? 313 ALA A CA 1 ATOM 2447 C C . ALA A 1 313 ? -13.093 29.440 -7.701 1.00 12.64 ? 313 ALA A C 1 ATOM 2448 O O . ALA A 1 313 ? -14.261 29.348 -8.172 1.00 15.03 ? 313 ALA A O 1 ATOM 2449 C CB . ALA A 1 313 ? -12.431 31.837 -7.384 1.00 14.24 ? 313 ALA A CB 1 ATOM 2450 N N . ASN A 1 314 ? -12.136 28.608 -8.072 1.00 12.34 ? 314 ASN A N 1 ATOM 2451 C CA . ASN A 1 314 ? -12.397 27.542 -9.029 1.00 13.70 ? 314 ASN A CA 1 ATOM 2452 C C . ASN A 1 314 ? -13.007 26.276 -8.417 1.00 12.39 ? 314 ASN A C 1 ATOM 2453 O O . ASN A 1 314 ? -13.207 25.275 -9.111 1.00 13.52 ? 314 ASN A O 1 ATOM 2454 C CB . ASN A 1 314 ? -11.132 27.128 -9.754 1.00 14.91 ? 314 ASN A CB 1 ATOM 2455 C CG . ASN A 1 314 ? -10.101 26.448 -8.914 1.00 15.48 ? 314 ASN A CG 1 ATOM 2456 O OD1 . ASN A 1 314 ? -10.128 26.530 -7.680 1.00 13.25 ? 314 ASN A OD1 1 ATOM 2457 N ND2 . ASN A 1 314 ? -9.150 25.714 -9.528 1.00 20.47 ? 314 ASN A ND2 1 ATOM 2458 N N . GLY A 1 315 ? -13.249 26.265 -7.101 1.00 9.54 ? 315 GLY A N 1 ATOM 2459 C CA . GLY A 1 315 ? -13.822 25.128 -6.437 1.00 10.31 ? 315 GLY A CA 1 ATOM 2460 C C . GLY A 1 315 ? -12.774 24.167 -5.868 1.00 9.65 ? 315 GLY A C 1 ATOM 2461 O O . GLY A 1 315 ? -13.183 23.165 -5.295 1.00 11.57 ? 315 GLY A O 1 ATOM 2462 N N . ALA A 1 316 ? -11.488 24.410 -6.054 1.00 9.57 ? 316 ALA A N 1 ATOM 2463 C CA . ALA A 1 316 ? -10.502 23.539 -5.425 1.00 9.31 ? 316 ALA A CA 1 ATOM 2464 C C . ALA A 1 316 ? -10.342 23.942 -3.949 1.00 9.33 ? 316 ALA A C 1 ATOM 2465 O O . ALA A 1 316 ? -10.494 25.105 -3.539 1.00 10.34 ? 316 ALA A O 1 ATOM 2466 C CB . ALA A 1 316 ? -9.179 23.747 -6.131 1.00 10.60 ? 316 ALA A CB 1 ATOM 2467 N N . GLN A 1 317 ? -9.988 22.945 -3.143 1.00 8.97 ? 317 GLN A N 1 ATOM 2468 C CA . GLN A 1 317 ? -9.641 23.161 -1.743 1.00 9.21 ? 317 GLN A CA 1 ATOM 2469 C C . GLN A 1 317 ? -8.112 23.204 -1.598 1.00 9.05 ? 317 GLN A C 1 ATOM 2470 O O . GLN A 1 317 ? -7.332 22.671 -2.401 1.00 11.27 ? 317 GLN A O 1 ATOM 2471 C CB . GLN A 1 317 ? -10.250 22.102 -0.821 1.00 10.63 ? 317 GLN A CB 1 ATOM 2472 C CG . GLN A 1 317 ? -9.578 20.749 -0.953 1.00 13.53 ? 317 GLN A CG 1 ATOM 2473 C CD . GLN A 1 317 ? -10.353 19.624 -0.280 1.00 14.90 ? 317 GLN A CD 1 ATOM 2474 O OE1 . GLN A 1 317 ? -11.579 19.629 -0.373 1.00 16.41 ? 317 GLN A OE1 1 ATOM 2475 N NE2 . GLN A 1 317 ? -9.658 18.707 0.388 1.00 16.76 ? 317 GLN A NE2 1 ATOM 2476 N N . SER A 1 318 ? -7.716 23.854 -0.501 1.00 8.14 ? 318 SER A N 1 ATOM 2477 C CA . SER A 1 318 ? -6.320 23.925 -0.107 1.00 8.09 ? 318 SER A CA 1 ATOM 2478 C C . SER A 1 318 ? -5.816 22.563 0.354 1.00 9.36 ? 318 SER A C 1 ATOM 2479 O O . SER A 1 318 ? -6.586 21.665 0.658 1.00 10.12 ? 318 SER A O 1 ATOM 2480 C CB . SER A 1 318 ? -6.138 24.925 1.063 1.00 9.28 ? 318 SER A CB 1 ATOM 2481 O OG . SER A 1 318 ? -6.765 24.449 2.256 1.00 8.76 ? 318 SER A OG 1 ATOM 2482 N N . ASN A 1 319 ? -4.495 22.470 0.441 1.00 10.42 ? 319 ASN A N 1 ATOM 2483 C CA . ASN A 1 319 ? -3.862 21.366 1.159 1.00 10.87 ? 319 ASN A CA 1 ATOM 2484 C C . ASN A 1 319 ? -4.459 21.322 2.569 1.00 9.38 ? 319 ASN A C 1 ATOM 2485 O O . ASN A 1 319 ? -4.914 22.330 3.123 1.00 10.49 ? 319 ASN A O 1 ATOM 2486 C CB . ASN A 1 319 ? -2.346 21.643 1.266 1.00 12.82 ? 319 ASN A CB 1 ATOM 2487 C CG . ASN A 1 319 ? -1.567 21.353 0.009 1.00 16.17 ? 319 ASN A CG 1 ATOM 2488 O OD1 . ASN A 1 319 ? -2.082 21.310 -1.115 1.00 20.55 ? 319 ASN A OD1 1 ATOM 2489 N ND2 . ASN A 1 319 ? -0.268 21.134 0.142 1.00 17.87 ? 319 ASN A ND2 1 ATOM 2490 N N . SER A 1 320 ? -4.514 20.143 3.184 1.00 9.97 ? 320 SER A N 1 ATOM 2491 C CA . SER A 1 320 ? -5.073 19.973 4.514 1.00 10.48 ? 320 SER A CA 1 ATOM 2492 C C . SER A 1 320 ? -4.566 18.724 5.220 1.00 9.63 ? 320 SER A C 1 ATOM 2493 O O . SER A 1 320 ? -3.856 17.919 4.583 1.00 10.59 ? 320 SER A O 1 ATOM 2494 C CB . SER A 1 320 ? -6.598 19.888 4.413 1.00 12.18 ? 320 SER A CB 1 ATOM 2495 O OG . SER A 1 320 ? -6.955 18.701 3.707 1.00 12.77 ? 320 SER A OG 1 ATOM 2496 N N . ASP A 1 321 ? -4.886 18.606 6.496 1.00 10.06 ? 321 ASP A N 1 ATOM 2497 C CA . ASP A 1 321 ? -4.528 17.434 7.305 1.00 10.46 ? 321 ASP A CA 1 ATOM 2498 C C . ASP A 1 321 ? -5.606 17.287 8.362 1.00 10.31 ? 321 ASP A C 1 ATOM 2499 O O . ASP A 1 321 ? -6.583 18.074 8.407 1.00 11.69 ? 321 ASP A O 1 ATOM 2500 C CB . ASP A 1 321 ? -3.095 17.568 7.816 1.00 10.10 ? 321 ASP A CB 1 ATOM 2501 C CG . ASP A 1 321 ? -2.825 18.601 8.899 1.00 11.06 ? 321 ASP A CG 1 ATOM 2502 O OD1 . ASP A 1 321 ? -3.809 19.174 9.400 1.00 11.06 ? 321 ASP A OD1 1 ATOM 2503 O OD2 . ASP A 1 321 ? -1.616 18.820 9.200 1.00 12.61 ? 321 ASP A OD2 1 ATOM 2504 N N . PRO A 1 322 ? -5.515 16.351 9.293 1.00 12.46 ? 322 PRO A N 1 ATOM 2505 C CA . PRO A 1 322 ? -6.551 16.138 10.287 1.00 13.92 ? 322 PRO A CA 1 ATOM 2506 C C . PRO A 1 322 ? -6.726 17.266 11.291 1.00 13.70 ? 322 PRO A C 1 ATOM 2507 O O . PRO A 1 322 ? -7.744 17.308 12.009 1.00 16.76 ? 322 PRO A O 1 ATOM 2508 C CB . PRO A 1 322 ? -6.153 14.844 10.980 1.00 15.02 ? 322 PRO A CB 1 ATOM 2509 C CG . PRO A 1 322 ? -5.447 14.120 9.892 1.00 15.70 ? 322 PRO A CG 1 ATOM 2510 C CD . PRO A 1 322 ? -4.556 15.213 9.257 1.00 14.16 ? 322 PRO A CD 1 ATOM 2511 N N . TYR A 1 323 ? -5.793 18.225 11.340 1.00 10.73 ? 323 TYR A N 1 ATOM 2512 C CA . TYR A 1 323 ? -5.885 19.372 12.210 1.00 10.03 ? 323 TYR A CA 1 ATOM 2513 C C . TYR A 1 323 ? -6.506 20.586 11.532 1.00 9.47 ? 323 TYR A C 1 ATOM 2514 O O . TYR A 1 323 ? -6.839 21.566 12.232 1.00 11.29 ? 323 TYR A O 1 ATOM 2515 C CB . TYR A 1 323 ? -4.460 19.789 12.629 1.00 10.53 ? 323 TYR A CB 1 ATOM 2516 C CG . TYR A 1 323 ? -3.728 18.718 13.415 1.00 10.90 ? 323 TYR A CG 1 ATOM 2517 C CD1 . TYR A 1 323 ? -4.121 18.359 14.697 1.00 11.02 ? 323 TYR A CD1 1 ATOM 2518 C CD2 . TYR A 1 323 ? -2.631 18.094 12.849 1.00 11.60 ? 323 TYR A CD2 1 ATOM 2519 C CE1 . TYR A 1 323 ? -3.422 17.390 15.410 1.00 12.85 ? 323 TYR A CE1 1 ATOM 2520 C CE2 . TYR A 1 323 ? -1.938 17.111 13.550 1.00 13.54 ? 323 TYR A CE2 1 ATOM 2521 C CZ . TYR A 1 323 ? -2.353 16.762 14.817 1.00 13.76 ? 323 TYR A CZ 1 ATOM 2522 O OH . TYR A 1 323 ? -1.638 15.790 15.496 1.00 16.10 ? 323 TYR A OH 1 ATOM 2523 N N . THR A 1 324 ? -6.721 20.575 10.231 1.00 9.65 ? 324 THR A N 1 ATOM 2524 C CA . THR A 1 324 ? -7.240 21.731 9.537 1.00 9.12 ? 324 THR A CA 1 ATOM 2525 C C . THR A 1 324 ? -8.539 22.251 10.108 1.00 9.63 ? 324 THR A C 1 ATOM 2526 O O . THR A 1 324 ? -9.484 21.474 10.379 1.00 10.37 ? 324 THR A O 1 ATOM 2527 C CB . THR A 1 324 ? -7.431 21.369 8.028 1.00 8.82 ? 324 THR A CB 1 ATOM 2528 O OG1 . THR A 1 324 ? -6.144 21.120 7.473 1.00 9.51 ? 324 THR A OG1 1 ATOM 2529 C CG2 . THR A 1 324 ? -8.200 22.437 7.287 1.00 9.70 ? 324 THR A CG2 1 ATOM 2530 N N . VAL A 1 325 ? -8.600 23.558 10.281 1.00 9.07 ? 325 VAL A N 1 ATOM 2531 C CA . VAL A 1 325 ? -9.810 24.262 10.687 1.00 9.69 ? 325 VAL A CA 1 ATOM 2532 C C . VAL A 1 325 ? -10.220 25.028 9.428 1.00 9.13 ? 325 VAL A C 1 ATOM 2533 O O . VAL A 1 325 ? -9.583 26.011 8.986 1.00 9.53 ? 325 VAL A O 1 ATOM 2534 C CB . VAL A 1 325 ? -9.593 25.245 11.839 1.00 10.90 ? 325 VAL A CB 1 ATOM 2535 C CG1 . VAL A 1 325 ? -10.891 25.983 12.209 1.00 12.50 ? 325 VAL A CG1 1 ATOM 2536 C CG2 . VAL A 1 325 ? -9.061 24.550 13.063 1.00 12.75 ? 325 VAL A CG2 1 ATOM 2537 N N . TRP A 1 326 ? -11.318 24.618 8.798 1.00 8.84 ? 326 TRP A N 1 ATOM 2538 C CA . TRP A 1 326 ? -11.756 25.184 7.536 1.00 9.57 ? 326 TRP A CA 1 ATOM 2539 C C . TRP A 1 326 ? -12.454 26.513 7.730 1.00 9.80 ? 326 TRP A C 1 ATOM 2540 O O . TRP A 1 326 ? -13.324 26.680 8.605 1.00 10.58 ? 326 TRP A O 1 ATOM 2541 C CB . TRP A 1 326 ? -12.730 24.229 6.832 1.00 10.31 ? 326 TRP A CB 1 ATOM 2542 C CG . TRP A 1 326 ? -12.039 22.972 6.369 1.00 8.86 ? 326 TRP A CG 1 ATOM 2543 C CD1 . TRP A 1 326 ? -12.063 21.754 7.017 1.00 11.30 ? 326 TRP A CD1 1 ATOM 2544 C CD2 . TRP A 1 326 ? -11.233 22.790 5.202 1.00 9.89 ? 326 TRP A CD2 1 ATOM 2545 N NE1 . TRP A 1 326 ? -11.322 20.833 6.316 1.00 12.45 ? 326 TRP A NE1 1 ATOM 2546 C CE2 . TRP A 1 326 ? -10.800 21.460 5.201 1.00 10.63 ? 326 TRP A CE2 1 ATOM 2547 C CE3 . TRP A 1 326 ? -10.825 23.633 4.168 1.00 10.74 ? 326 TRP A CE3 1 ATOM 2548 C CZ2 . TRP A 1 326 ? -9.979 20.938 4.199 1.00 10.14 ? 326 TRP A CZ2 1 ATOM 2549 C CZ3 . TRP A 1 326 ? -9.998 23.128 3.169 1.00 9.96 ? 326 TRP A CZ3 1 ATOM 2550 C CH2 . TRP A 1 326 ? -9.585 21.780 3.190 1.00 9.81 ? 326 TRP A CH2 1 ATOM 2551 N N . TYR A 1 327 ? -12.088 27.545 6.973 1.00 9.50 ? 327 TYR A N 1 ATOM 2552 C CA . TYR A 1 327 ? -12.754 28.839 7.082 1.00 9.57 ? 327 TYR A CA 1 ATOM 2553 C C . TYR A 1 327 ? -14.276 28.705 6.987 1.00 9.98 ? 327 TYR A C 1 ATOM 2554 O O . TYR A 1 327 ? -14.816 27.947 6.176 1.00 10.15 ? 327 TYR A O 1 ATOM 2555 C CB . TYR A 1 327 ? -12.259 29.766 5.963 1.00 10.79 ? 327 TYR A CB 1 ATOM 2556 C CG . TYR A 1 327 ? -12.944 31.112 5.943 1.00 10.21 ? 327 TYR A CG 1 ATOM 2557 C CD1 . TYR A 1 327 ? -12.874 31.982 7.021 1.00 10.69 ? 327 TYR A CD1 1 ATOM 2558 C CD2 . TYR A 1 327 ? -13.644 31.470 4.804 1.00 10.43 ? 327 TYR A CD2 1 ATOM 2559 C CE1 . TYR A 1 327 ? -13.517 33.209 6.962 1.00 11.08 ? 327 TYR A CE1 1 ATOM 2560 C CE2 . TYR A 1 327 ? -14.335 32.665 4.781 1.00 12.04 ? 327 TYR A CE2 1 ATOM 2561 C CZ . TYR A 1 327 ? -14.191 33.554 5.820 1.00 12.71 ? 327 TYR A CZ 1 ATOM 2562 O OH . TYR A 1 327 ? -14.884 34.737 5.771 1.00 15.75 ? 327 TYR A OH 1 ATOM 2563 N N . ASN A 1 328 ? -14.978 29.450 7.871 1.00 9.63 ? 328 ASN A N 1 ATOM 2564 C CA . ASN A 1 328 ? -16.413 29.519 7.906 1.00 11.62 ? 328 ASN A CA 1 ATOM 2565 C C . ASN A 1 328 ? -17.125 28.300 8.455 1.00 12.59 ? 328 ASN A C 1 ATOM 2566 O O . ASN A 1 328 ? -18.365 28.288 8.519 1.00 15.95 ? 328 ASN A O 1 ATOM 2567 C CB . ASN A 1 328 ? -17.026 29.834 6.529 1.00 15.19 ? 328 ASN A CB 1 ATOM 2568 C CG . ASN A 1 328 ? -17.435 31.248 6.495 1.00 14.96 ? 328 ASN A CG 1 ATOM 2569 O OD1 . ASN A 1 328 ? -17.332 32.116 7.321 1.00 16.99 ? 328 ASN A OD1 1 ATOM 2570 N ND2 . ASN A 1 328 ? -18.118 31.546 5.342 1.00 17.37 ? 328 ASN A ND2 1 ATOM 2571 N N . SER A 1 329 ? -16.371 27.301 8.934 1.00 9.33 ? 329 SER A N 1 ATOM 2572 C CA . SER A 1 329 ? -16.948 26.107 9.525 1.00 10.33 ? 329 SER A CA 1 ATOM 2573 C C . SER A 1 329 ? -17.341 26.326 10.983 1.00 11.19 ? 329 SER A C 1 ATOM 2574 O O . SER A 1 329 ? -16.997 27.331 11.600 1.00 11.88 ? 329 SER A O 1 ATOM 2575 C CB . SER A 1 329 ? -15.939 24.946 9.466 1.00 11.19 ? 329 SER A CB 1 ATOM 2576 O OG . SER A 1 329 ? -14.800 25.162 10.326 1.00 11.24 ? 329 SER A OG 1 ATOM 2577 N N . SER A 1 330 ? -17.967 25.275 11.583 1.00 10.92 ? 330 SER A N 1 ATOM 2578 C CA . SER A 1 330 ? -18.299 25.303 13.000 1.00 11.65 ? 330 SER A CA 1 ATOM 2579 C C . SER A 1 330 ? -17.021 25.411 13.841 1.00 12.28 ? 330 SER A C 1 ATOM 2580 O O . SER A 1 330 ? -17.030 26.076 14.886 1.00 13.03 ? 330 SER A O 1 ATOM 2581 C CB . SER A 1 330 ? -19.132 24.083 13.410 1.00 14.21 ? 330 SER A CB 1 ATOM 2582 O OG A SER A 1 330 ? -18.538 22.847 13.214 0.50 14.34 ? 330 SER A OG 1 ATOM 2583 O OG B SER A 1 330 ? -20.244 24.101 12.509 0.50 16.43 ? 330 SER A OG 1 ATOM 2584 N N . ASN A 1 331 ? -15.932 24.748 13.437 1.00 11.23 ? 331 ASN A N 1 ATOM 2585 C CA . ASN A 1 331 ? -14.703 24.834 14.235 1.00 11.51 ? 331 ASN A CA 1 ATOM 2586 C C . ASN A 1 331 ? -14.050 26.200 14.020 1.00 8.93 ? 331 ASN A C 1 ATOM 2587 O O . ASN A 1 331 ? -13.349 26.647 14.938 1.00 10.46 ? 331 ASN A O 1 ATOM 2588 C CB . ASN A 1 331 ? -13.773 23.675 13.913 1.00 14.14 ? 331 ASN A CB 1 ATOM 2589 C CG . ASN A 1 331 ? -14.244 22.341 14.500 1.00 16.68 ? 331 ASN A CG 1 ATOM 2590 O OD1 . ASN A 1 331 ? -13.827 21.256 14.037 1.00 23.22 ? 331 ASN A OD1 1 ATOM 2591 N ND2 . ASN A 1 331 ? -15.022 22.458 15.533 1.00 19.08 ? 331 ASN A ND2 1 ATOM 2592 N N . TRP A 1 332 ? -14.219 26.860 12.891 1.00 8.97 ? 332 TRP A N 1 ATOM 2593 C CA . TRP A 1 332 ? -13.808 28.264 12.712 1.00 8.76 ? 332 TRP A CA 1 ATOM 2594 C C . TRP A 1 332 ? -14.577 29.147 13.688 1.00 10.02 ? 332 TRP A C 1 ATOM 2595 O O . TRP A 1 332 ? -13.991 30.018 14.335 1.00 10.42 ? 332 TRP A O 1 ATOM 2596 C CB . TRP A 1 332 ? -13.956 28.689 11.243 1.00 10.07 ? 332 TRP A CB 1 ATOM 2597 C CG . TRP A 1 332 ? -13.825 30.166 11.023 1.00 11.26 ? 332 TRP A CG 1 ATOM 2598 C CD1 . TRP A 1 332 ? -12.705 30.870 10.716 1.00 11.17 ? 332 TRP A CD1 1 ATOM 2599 C CD2 . TRP A 1 332 ? -14.866 31.180 11.138 1.00 11.21 ? 332 TRP A CD2 1 ATOM 2600 N NE1 . TRP A 1 332 ? -12.967 32.216 10.594 1.00 11.99 ? 332 TRP A NE1 1 ATOM 2601 C CE2 . TRP A 1 332 ? -14.286 32.420 10.851 1.00 12.07 ? 332 TRP A CE2 1 ATOM 2602 C CE3 . TRP A 1 332 ? -16.238 31.079 11.422 1.00 12.06 ? 332 TRP A CE3 1 ATOM 2603 C CZ2 . TRP A 1 332 ? -15.014 33.608 10.885 1.00 13.61 ? 332 TRP A CZ2 1 ATOM 2604 C CZ3 . TRP A 1 332 ? -16.956 32.258 11.429 1.00 15.10 ? 332 TRP A CZ3 1 ATOM 2605 C CH2 . TRP A 1 332 ? -16.353 33.495 11.176 1.00 14.59 ? 332 TRP A CH2 1 ATOM 2606 N N . GLN A 1 333 ? -15.892 28.925 13.898 1.00 10.23 ? 333 GLN A N 1 ATOM 2607 C CA . GLN A 1 333 ? -16.637 29.728 14.881 1.00 12.84 ? 333 GLN A CA 1 ATOM 2608 C C . GLN A 1 333 ? -16.046 29.483 16.253 1.00 12.57 ? 333 GLN A C 1 ATOM 2609 O O . GLN A 1 333 ? -15.819 30.453 16.976 1.00 13.58 ? 333 GLN A O 1 ATOM 2610 C CB . GLN A 1 333 ? -18.128 29.333 14.867 1.00 12.96 ? 333 GLN A CB 1 ATOM 2611 C CG A GLN A 1 333 ? -19.101 29.773 15.965 0.70 16.48 ? 333 GLN A CG 1 ATOM 2612 C CG B GLN A 1 333 ? -18.910 30.316 15.744 0.30 11.76 ? 333 GLN A CG 1 ATOM 2613 C CD A GLN A 1 333 ? -20.519 29.226 16.050 0.70 18.83 ? 333 GLN A CD 1 ATOM 2614 C CD B GLN A 1 333 ? -18.965 31.769 15.371 0.30 10.57 ? 333 GLN A CD 1 ATOM 2615 O OE1 A GLN A 1 333 ? -21.411 29.566 16.910 0.70 20.23 ? 333 GLN A OE1 1 ATOM 2616 O OE1 B GLN A 1 333 ? -18.664 32.652 16.195 0.30 11.76 ? 333 GLN A OE1 1 ATOM 2617 N NE2 A GLN A 1 333 ? -20.905 28.300 15.166 0.70 16.57 ? 333 GLN A NE2 1 ATOM 2618 N NE2 B GLN A 1 333 ? -19.445 32.135 14.190 0.30 10.66 ? 333 GLN A NE2 1 ATOM 2619 N N . CYS A 1 334 ? -15.789 28.224 16.627 1.00 11.94 ? 334 CYS A N 1 ATOM 2620 C CA . CYS A 1 334 ? -15.329 27.946 17.984 1.00 12.81 ? 334 CYS A CA 1 ATOM 2621 C C . CYS A 1 334 ? -13.901 28.415 18.263 1.00 12.53 ? 334 CYS A C 1 ATOM 2622 O O . CYS A 1 334 ? -13.652 28.923 19.340 1.00 13.13 ? 334 CYS A O 1 ATOM 2623 C CB . CYS A 1 334 ? -15.421 26.411 18.204 1.00 14.80 ? 334 CYS A CB 1 ATOM 2624 S SG . CYS A 1 334 ? -14.765 25.858 19.794 1.00 15.29 ? 334 CYS A SG 1 ATOM 2625 N N . LEU A 1 335 ? -12.976 28.143 17.331 1.00 11.11 ? 335 LEU A N 1 ATOM 2626 C CA . LEU A 1 335 ? -11.562 28.359 17.590 1.00 10.45 ? 335 LEU A CA 1 ATOM 2627 C C . LEU A 1 335 ? -10.976 29.595 16.961 1.00 9.37 ? 335 LEU A C 1 ATOM 2628 O O . LEU A 1 335 ? -9.814 29.908 17.251 1.00 11.08 ? 335 LEU A O 1 ATOM 2629 C CB . LEU A 1 335 ? -10.787 27.117 17.088 1.00 11.43 ? 335 LEU A CB 1 ATOM 2630 C CG . LEU A 1 335 ? -11.146 25.814 17.800 1.00 11.70 ? 335 LEU A CG 1 ATOM 2631 C CD1 . LEU A 1 335 ? -10.471 24.611 17.124 1.00 13.55 ? 335 LEU A CD1 1 ATOM 2632 C CD2 . LEU A 1 335 ? -10.885 25.838 19.293 1.00 13.06 ? 335 LEU A CD2 1 ATOM 2633 N N . VAL A 1 336 ? -11.697 30.285 16.085 1.00 10.65 ? 336 VAL A N 1 ATOM 2634 C CA . VAL A 1 336 ? -11.248 31.498 15.444 1.00 10.02 ? 336 VAL A CA 1 ATOM 2635 C C . VAL A 1 336 ? -12.140 32.690 15.839 1.00 11.21 ? 336 VAL A C 1 ATOM 2636 O O . VAL A 1 336 ? -11.702 33.483 16.702 1.00 12.09 ? 336 VAL A O 1 ATOM 2637 C CB . VAL A 1 336 ? -11.134 31.403 13.906 1.00 8.63 ? 336 VAL A CB 1 ATOM 2638 C CG1 . VAL A 1 336 ? -10.497 32.697 13.418 1.00 10.29 ? 336 VAL A CG1 1 ATOM 2639 C CG2 . VAL A 1 336 ? -10.244 30.188 13.562 1.00 10.01 ? 336 VAL A CG2 1 ATOM 2640 N N . LYS A 1 337 ? -13.411 32.718 15.429 1.00 12.18 ? 337 LYS A N 1 ATOM 2641 C CA . LYS A 1 337 ? -14.231 33.885 15.781 1.00 13.56 ? 337 LYS A CA 1 ATOM 2642 C C . LYS A 1 337 ? -14.410 34.012 17.277 1.00 12.39 ? 337 LYS A C 1 ATOM 2643 O O . LYS A 1 337 ? -14.201 35.155 17.759 1.00 13.47 ? 337 LYS A O 1 ATOM 2644 C CB . LYS A 1 337 ? -15.584 33.749 15.070 1.00 16.44 ? 337 LYS A CB 1 ATOM 2645 C CG . LYS A 1 337 ? -16.465 34.980 15.288 1.00 22.91 ? 337 LYS A CG 1 ATOM 2646 C CD . LYS A 1 337 ? -17.807 34.889 14.629 1.00 29.15 ? 337 LYS A CD 1 ATOM 2647 C CE . LYS A 1 337 ? -18.903 35.638 15.391 1.00 32.62 ? 337 LYS A CE 1 ATOM 2648 N NZ . LYS A 1 337 ? -18.465 36.959 15.937 1.00 34.72 ? 337 LYS A NZ 1 ATOM 2649 N N . ASN A 1 338 ? -14.722 32.975 18.040 1.00 12.06 ? 338 ASN A N 1 ATOM 2650 C CA . ASN A 1 338 ? -14.964 33.150 19.487 1.00 12.02 ? 338 ASN A CA 1 ATOM 2651 C C . ASN A 1 338 ? -13.670 33.548 20.194 1.00 12.73 ? 338 ASN A C 1 ATOM 2652 O O . ASN A 1 338 ? -13.717 34.276 21.217 1.00 14.19 ? 338 ASN A O 1 ATOM 2653 C CB . ASN A 1 338 ? -15.562 31.911 20.140 1.00 14.03 ? 338 ASN A CB 1 ATOM 2654 C CG . ASN A 1 338 ? -16.981 31.503 19.768 1.00 15.12 ? 338 ASN A CG 1 ATOM 2655 O OD1 . ASN A 1 338 ? -17.425 30.379 20.128 1.00 19.13 ? 338 ASN A OD1 1 ATOM 2656 N ND2 . ASN A 1 338 ? -17.611 32.376 19.049 1.00 14.12 ? 338 ASN A ND2 1 ATOM 2657 N N . HIS A 1 339 ? -12.531 33.036 19.721 1.00 11.58 ? 339 HIS A N 1 ATOM 2658 C CA . HIS A 1 339 ? -11.246 33.384 20.355 1.00 11.82 ? 339 HIS A CA 1 ATOM 2659 C C . HIS A 1 339 ? -10.854 34.828 20.097 1.00 11.99 ? 339 HIS A C 1 ATOM 2660 O O . HIS A 1 339 ? -10.484 35.541 21.035 1.00 12.98 ? 339 HIS A O 1 ATOM 2661 C CB . HIS A 1 339 ? -10.162 32.441 19.845 1.00 11.56 ? 339 HIS A CB 1 ATOM 2662 C CG . HIS A 1 339 ? -8.841 32.650 20.508 1.00 10.56 ? 339 HIS A CG 1 ATOM 2663 N ND1 . HIS A 1 339 ? -8.697 32.817 21.883 1.00 9.74 ? 339 HIS A ND1 1 ATOM 2664 C CD2 . HIS A 1 339 ? -7.580 32.614 19.965 1.00 10.42 ? 339 HIS A CD2 1 ATOM 2665 C CE1 . HIS A 1 339 ? -7.383 32.916 22.120 1.00 11.38 ? 339 HIS A CE1 1 ATOM 2666 N NE2 . HIS A 1 339 ? -6.698 32.767 20.985 1.00 11.62 ? 339 HIS A NE2 1 ATOM 2667 N N . VAL A 1 340 ? -10.949 35.282 18.845 1.00 13.05 ? 340 VAL A N 1 ATOM 2668 C CA . VAL A 1 340 ? -10.681 36.678 18.512 1.00 13.88 ? 340 VAL A CA 1 ATOM 2669 C C . VAL A 1 340 ? -11.621 37.594 19.304 1.00 15.32 ? 340 VAL A C 1 ATOM 2670 O O . VAL A 1 340 ? -11.209 38.643 19.809 1.00 15.45 ? 340 VAL A O 1 ATOM 2671 C CB . VAL A 1 340 ? -10.879 36.915 17.001 1.00 13.94 ? 340 VAL A CB 1 ATOM 2672 C CG1 . VAL A 1 340 ? -10.955 38.367 16.587 1.00 18.84 ? 340 VAL A CG1 1 ATOM 2673 C CG2 . VAL A 1 340 ? -9.707 36.245 16.248 1.00 12.85 ? 340 VAL A CG2 1 ATOM 2674 N N . ASP A 1 341 ? -12.881 37.177 19.502 1.00 14.42 ? 341 ASP A N 1 ATOM 2675 C CA . ASP A 1 341 ? -13.842 37.983 20.264 1.00 15.44 ? 341 ASP A CA 1 ATOM 2676 C C . ASP A 1 341 ? -13.416 38.113 21.716 1.00 16.64 ? 341 ASP A C 1 ATOM 2677 O O . ASP A 1 341 ? -13.634 39.137 22.358 1.00 19.82 ? 341 ASP A O 1 ATOM 2678 C CB . ASP A 1 341 ? -15.253 37.399 20.179 1.00 18.65 ? 341 ASP A CB 1 ATOM 2679 C CG . ASP A 1 341 ? -15.965 37.638 18.870 1.00 22.17 ? 341 ASP A CG 1 ATOM 2680 O OD1 . ASP A 1 341 ? -15.506 38.488 18.085 1.00 23.76 ? 341 ASP A OD1 1 ATOM 2681 O OD2 . ASP A 1 341 ? -17.008 36.973 18.651 1.00 25.92 ? 341 ASP A OD2 1 ATOM 2682 N N . ALA A 1 342 ? -12.803 37.067 22.296 1.00 16.30 ? 342 ALA A N 1 ATOM 2683 C CA . ALA A 1 342 ? -12.376 37.045 23.684 1.00 16.22 ? 342 ALA A CA 1 ATOM 2684 C C . ALA A 1 342 ? -11.133 37.893 23.894 1.00 17.44 ? 342 ALA A C 1 ATOM 2685 O O . ALA A 1 342 ? -10.874 38.386 25.009 1.00 19.04 ? 342 ALA A O 1 ATOM 2686 C CB . ALA A 1 342 ? -12.071 35.605 24.102 1.00 17.10 ? 342 ALA A CB 1 ATOM 2687 N N . ILE A 1 343 ? -10.303 38.006 22.845 1.00 17.70 ? 343 ILE A N 1 ATOM 2688 C CA . ILE A 1 343 ? -9.078 38.802 22.933 1.00 18.63 ? 343 ILE A CA 1 ATOM 2689 C C . ILE A 1 343 ? -9.462 40.271 22.939 1.00 23.84 ? 343 ILE A C 1 ATOM 2690 O O . ILE A 1 343 ? -8.862 41.034 23.676 1.00 22.12 ? 343 ILE A O 1 ATOM 2691 C CB . ILE A 1 343 ? -8.157 38.498 21.721 1.00 18.58 ? 343 ILE A CB 1 ATOM 2692 C CG1 . ILE A 1 343 ? -7.632 37.074 21.848 1.00 17.06 ? 343 ILE A CG1 1 ATOM 2693 C CG2 . ILE A 1 343 ? -7.023 39.512 21.636 1.00 19.66 ? 343 ILE A CG2 1 ATOM 2694 C CD1 . ILE A 1 343 ? -6.977 36.524 20.577 1.00 15.68 ? 343 ILE A CD1 1 ATOM 2695 N N . ASN A 1 344 ? -10.469 40.588 22.137 1.00 28.77 ? 344 ASN A N 1 ATOM 2696 C CA . ASN A 1 344 ? -10.923 41.938 21.917 1.00 37.23 ? 344 ASN A CA 1 ATOM 2697 C C . ASN A 1 344 ? -11.999 41.861 20.820 1.00 40.35 ? 344 ASN A C 1 ATOM 2698 O O . ASN A 1 344 ? -13.112 41.454 21.205 1.00 43.94 ? 344 ASN A O 1 ATOM 2699 C CB . ASN A 1 344 ? -9.760 42.777 21.360 1.00 41.27 ? 344 ASN A CB 1 ATOM 2700 C CG . ASN A 1 344 ? -9.579 44.031 22.191 1.00 44.87 ? 344 ASN A CG 1 ATOM 2701 O OD1 . ASN A 1 344 ? -9.984 44.078 23.361 1.00 47.39 ? 344 ASN A OD1 1 ATOM 2702 N ND2 . ASN A 1 344 ? -8.940 45.021 21.585 1.00 46.66 ? 344 ASN A ND2 1 ATOM 2703 O OXT . ASN A 1 344 ? -11.619 42.216 19.687 1.00 20.00 ? 344 ASN A OXT 1 HETATM 2704 C C . TRS B 2 . ? 3.901 19.986 11.757 1.00 7.20 ? 401 TRS A C 1 HETATM 2705 C C1 . TRS B 2 . ? 4.920 18.954 11.193 1.00 9.56 ? 401 TRS A C1 1 HETATM 2706 C C2 . TRS B 2 . ? 4.178 21.330 11.092 1.00 8.04 ? 401 TRS A C2 1 HETATM 2707 C C3 . TRS B 2 . ? 2.458 19.656 11.624 1.00 8.83 ? 401 TRS A C3 1 HETATM 2708 N N . TRS B 2 . ? 4.264 20.119 13.260 1.00 8.24 ? 401 TRS A N 1 HETATM 2709 O O1 . TRS B 2 . ? 4.755 18.778 9.791 1.00 10.58 ? 401 TRS A O1 1 HETATM 2710 O O2 . TRS B 2 . ? 5.479 21.870 11.557 1.00 8.38 ? 401 TRS A O2 1 HETATM 2711 O O3 . TRS B 2 . ? 2.218 18.403 12.225 1.00 13.64 ? 401 TRS A O3 1 HETATM 2712 S S . SO4 C 3 . ? -15.877 19.070 19.196 1.00 26.78 ? 402 SO4 A S 1 HETATM 2713 O O1 . SO4 C 3 . ? -14.881 19.587 18.119 1.00 26.54 ? 402 SO4 A O1 1 HETATM 2714 O O2 . SO4 C 3 . ? -16.236 17.670 18.885 1.00 29.30 ? 402 SO4 A O2 1 HETATM 2715 O O3 . SO4 C 3 . ? -17.110 19.929 19.123 1.00 26.71 ? 402 SO4 A O3 1 HETATM 2716 O O4 . SO4 C 3 . ? -15.245 19.236 20.524 1.00 26.09 ? 402 SO4 A O4 1 HETATM 2717 C C1 . GOL D 4 . ? 3.837 20.728 6.259 1.00 20.67 ? 410 GOL A C1 1 HETATM 2718 O O1 . GOL D 4 . ? 5.193 20.675 5.811 1.00 12.91 ? 410 GOL A O1 1 HETATM 2719 C C2 . GOL D 4 . ? 2.867 19.669 5.903 1.00 28.09 ? 410 GOL A C2 1 HETATM 2720 O O2 . GOL D 4 . ? 3.132 18.961 4.696 1.00 30.24 ? 410 GOL A O2 1 HETATM 2721 C C3 . GOL D 4 . ? 2.816 18.628 7.035 1.00 32.15 ? 410 GOL A C3 1 HETATM 2722 O O3 . GOL D 4 . ? 3.615 17.606 6.358 1.00 36.91 ? 410 GOL A O3 1 HETATM 2723 C C1 . GOL E 4 . ? 6.927 15.066 8.950 0.50 24.28 ? 411 GOL A C1 1 HETATM 2724 O O1 . GOL E 4 . ? 5.953 14.728 8.001 0.50 21.70 ? 411 GOL A O1 1 HETATM 2725 C C2 . GOL E 4 . ? 6.551 15.180 10.399 0.50 25.79 ? 411 GOL A C2 1 HETATM 2726 O O2 . GOL E 4 . ? 5.123 15.269 10.606 0.50 28.11 ? 411 GOL A O2 1 HETATM 2727 C C3 . GOL E 4 . ? 7.127 14.013 11.212 0.50 26.86 ? 411 GOL A C3 1 HETATM 2728 O O3 . GOL E 4 . ? 7.219 12.826 10.397 0.50 28.71 ? 411 GOL A O3 1 HETATM 2729 C C1 . GOL F 4 . ? 6.720 15.866 16.140 0.50 19.32 ? 412 GOL A C1 1 HETATM 2730 O O1 . GOL F 4 . ? 5.958 16.304 17.206 0.50 19.43 ? 412 GOL A O1 1 HETATM 2731 C C2 . GOL F 4 . ? 5.902 15.805 14.892 0.50 17.29 ? 412 GOL A C2 1 HETATM 2732 O O2 . GOL F 4 . ? 4.716 14.995 15.093 0.50 20.30 ? 412 GOL A O2 1 HETATM 2733 C C3 . GOL F 4 . ? 5.574 17.198 14.444 0.50 11.48 ? 412 GOL A C3 1 HETATM 2734 O O3 . GOL F 4 . ? 4.404 17.717 15.107 0.50 6.61 ? 412 GOL A O3 1 HETATM 2735 C C1 . NAG G 5 . ? 25.143 10.436 12.428 1.00 24.09 ? 430 NAG A C1 1 HETATM 2736 C C2 . NAG G 5 . ? 24.892 9.129 13.141 1.00 28.76 ? 430 NAG A C2 1 HETATM 2737 C C3 . NAG G 5 . ? 25.667 9.223 14.436 1.00 30.62 ? 430 NAG A C3 1 HETATM 2738 C C4 . NAG G 5 . ? 27.134 9.520 14.072 1.00 30.54 ? 430 NAG A C4 1 HETATM 2739 C C5 . NAG G 5 . ? 27.266 10.852 13.289 1.00 28.77 ? 430 NAG A C5 1 HETATM 2740 C C6 . NAG G 5 . ? 28.709 11.065 12.887 1.00 30.56 ? 430 NAG A C6 1 HETATM 2741 C C7 . NAG G 5 . ? 22.818 7.783 12.942 1.00 33.59 ? 430 NAG A C7 1 HETATM 2742 C C8 . NAG G 5 . ? 21.363 7.755 13.203 1.00 33.23 ? 430 NAG A C8 1 HETATM 2743 N N2 . NAG G 5 . ? 23.442 8.933 13.307 1.00 30.94 ? 430 NAG A N2 1 HETATM 2744 O O3 . NAG G 5 . ? 25.559 7.926 15.002 1.00 32.80 ? 430 NAG A O3 1 HETATM 2745 O O4 . NAG G 5 . ? 27.951 9.641 15.241 1.00 31.83 ? 430 NAG A O4 1 HETATM 2746 O O5 . NAG G 5 . ? 26.511 10.669 12.088 1.00 25.46 ? 430 NAG A O5 1 HETATM 2747 O O6 . NAG G 5 . ? 29.160 10.022 12.094 1.00 33.27 ? 430 NAG A O6 1 HETATM 2748 O O7 . NAG G 5 . ? 23.357 6.876 12.455 1.00 34.94 ? 430 NAG A O7 1 HETATM 2749 C C1 . NAG H 5 . ? 16.656 48.967 4.767 1.00 9.77 ? 431 NAG A C1 1 HETATM 2750 C C2 . NAG H 5 . ? 16.990 50.431 4.647 1.00 10.13 ? 431 NAG A C2 1 HETATM 2751 C C3 . NAG H 5 . ? 18.417 50.592 5.112 1.00 10.01 ? 431 NAG A C3 1 HETATM 2752 C C4 . NAG H 5 . ? 18.587 49.998 6.532 1.00 9.14 ? 431 NAG A C4 1 HETATM 2753 C C5 . NAG H 5 . ? 18.167 48.501 6.495 1.00 9.86 ? 431 NAG A C5 1 HETATM 2754 C C6 . NAG H 5 . ? 18.218 47.887 7.896 1.00 10.44 ? 431 NAG A C6 1 HETATM 2755 C C7 . NAG H 5 . ? 16.155 51.921 2.829 1.00 12.51 ? 431 NAG A C7 1 HETATM 2756 C C8 . NAG H 5 . ? 16.215 52.158 1.357 1.00 12.89 ? 431 NAG A C8 1 HETATM 2757 N N2 . NAG H 5 . ? 16.830 50.812 3.220 1.00 10.66 ? 431 NAG A N2 1 HETATM 2758 O O3 . NAG H 5 . ? 18.696 52.005 5.152 1.00 12.32 ? 431 NAG A O3 1 HETATM 2759 O O4 . NAG H 5 . ? 19.979 50.051 6.826 1.00 11.72 ? 431 NAG A O4 1 HETATM 2760 O O5 . NAG H 5 . ? 16.778 48.481 6.100 1.00 9.68 ? 431 NAG A O5 1 HETATM 2761 O O6 . NAG H 5 . ? 17.996 46.477 7.865 1.00 11.77 ? 431 NAG A O6 1 HETATM 2762 O O7 . NAG H 5 . ? 15.594 52.606 3.629 1.00 14.12 ? 431 NAG A O7 1 HETATM 2763 C C1 . NAG I 5 . ? -4.272 13.451 32.198 1.00 38.98 ? 432 NAG A C1 1 HETATM 2764 C C2 . NAG I 5 . ? -5.419 13.342 33.140 1.00 41.68 ? 432 NAG A C2 1 HETATM 2765 C C3 . NAG I 5 . ? -5.145 14.021 34.457 1.00 43.90 ? 432 NAG A C3 1 HETATM 2766 C C4 . NAG I 5 . ? -3.675 13.723 34.839 1.00 45.63 ? 432 NAG A C4 1 HETATM 2767 C C5 . NAG I 5 . ? -2.700 14.305 33.797 1.00 45.11 ? 432 NAG A C5 1 HETATM 2768 C C6 . NAG I 5 . ? -1.242 13.950 34.053 1.00 45.81 ? 432 NAG A C6 1 HETATM 2769 C C7 . NAG I 5 . ? -7.436 13.169 31.686 1.00 40.42 ? 432 NAG A C7 1 HETATM 2770 C C8 . NAG I 5 . ? -8.766 13.785 31.395 1.00 40.04 ? 432 NAG A C8 1 HETATM 2771 N N2 . NAG I 5 . ? -6.628 13.913 32.489 1.00 40.13 ? 432 NAG A N2 1 HETATM 2772 O O3 . NAG I 5 . ? -6.046 13.453 35.403 1.00 43.17 ? 432 NAG A O3 1 HETATM 2773 O O4 . NAG I 5 . ? -3.397 14.334 36.111 1.00 47.04 ? 432 NAG A O4 1 HETATM 2774 O O5 . NAG I 5 . ? -2.947 13.760 32.512 1.00 42.86 ? 432 NAG A O5 1 HETATM 2775 O O6 . NAG I 5 . ? -0.489 14.216 32.905 1.00 45.99 ? 432 NAG A O6 1 HETATM 2776 O O7 . NAG I 5 . ? -7.136 12.128 31.286 1.00 38.90 ? 432 NAG A O7 1 HETATM 2777 C C1 . NAG J 5 . ? -18.854 32.832 4.736 1.00 20.41 ? 433 NAG A C1 1 HETATM 2778 C C2 . NAG J 5 . ? -18.995 32.931 3.246 1.00 23.65 ? 433 NAG A C2 1 HETATM 2779 C C3 . NAG J 5 . ? -19.712 34.202 2.904 1.00 26.03 ? 433 NAG A C3 1 HETATM 2780 C C4 . NAG J 5 . ? -21.013 34.159 3.735 1.00 25.19 ? 433 NAG A C4 1 HETATM 2781 C C5 . NAG J 5 . ? -20.823 34.003 5.245 1.00 23.22 ? 433 NAG A C5 1 HETATM 2782 C C6 . NAG J 5 . ? -22.130 33.777 6.006 1.00 23.49 ? 433 NAG A C6 1 HETATM 2783 C C7 . NAG J 5 . ? -17.326 31.956 1.737 1.00 29.73 ? 433 NAG A C7 1 HETATM 2784 C C8 . NAG J 5 . ? -15.969 32.157 1.134 1.00 29.75 ? 433 NAG A C8 1 HETATM 2785 N N2 . NAG J 5 . ? -17.640 32.919 2.630 1.00 26.30 ? 433 NAG A N2 1 HETATM 2786 O O3 . NAG J 5 . ? -19.918 34.053 1.488 1.00 27.08 ? 433 NAG A O3 1 HETATM 2787 O O4 . NAG J 5 . ? -21.659 35.435 3.555 1.00 29.10 ? 433 NAG A O4 1 HETATM 2788 O O5 . NAG J 5 . ? -20.084 32.800 5.476 1.00 21.25 ? 433 NAG A O5 1 HETATM 2789 O O6 . NAG J 5 . ? -21.877 33.872 7.389 1.00 24.46 ? 433 NAG A O6 1 HETATM 2790 O O7 . NAG J 5 . ? -18.037 31.079 1.483 1.00 33.22 ? 433 NAG A O7 1 HETATM 2791 O O . HOH K 6 . ? 6.165 52.318 7.455 1.00 34.20 ? 2001 HOH A O 1 HETATM 2792 O O . HOH K 6 . ? 2.075 46.233 5.237 1.00 36.22 ? 2002 HOH A O 1 HETATM 2793 O O . HOH K 6 . ? 10.913 49.955 14.595 1.00 30.52 ? 2003 HOH A O 1 HETATM 2794 O O . HOH K 6 . ? 13.218 45.201 17.373 1.00 42.00 ? 2004 HOH A O 1 HETATM 2795 O O . HOH K 6 . ? 4.840 48.437 15.435 1.00 36.22 ? 2005 HOH A O 1 HETATM 2796 O O . HOH K 6 . ? 4.272 46.537 13.305 1.00 21.26 ? 2006 HOH A O 1 HETATM 2797 O O . HOH K 6 . ? 12.051 49.131 19.251 1.00 34.03 ? 2007 HOH A O 1 HETATM 2798 O O . HOH K 6 . ? 12.844 42.859 24.342 1.00 25.07 ? 2008 HOH A O 1 HETATM 2799 O O . HOH K 6 . ? 8.720 51.033 12.241 1.00 31.14 ? 2009 HOH A O 1 HETATM 2800 O O . HOH K 6 . ? 11.948 44.514 15.257 1.00 17.10 ? 2010 HOH A O 1 HETATM 2801 O O . HOH K 6 . ? 7.967 49.145 20.307 1.00 29.78 ? 2011 HOH A O 1 HETATM 2802 O O . HOH K 6 . ? 10.498 48.474 21.271 1.00 31.40 ? 2012 HOH A O 1 HETATM 2803 O O . HOH K 6 . ? 11.769 45.025 19.527 1.00 23.00 ? 2013 HOH A O 1 HETATM 2804 O O . HOH K 6 . ? 4.996 48.462 26.730 1.00 42.92 ? 2014 HOH A O 1 HETATM 2805 O O . HOH K 6 . ? 5.483 51.009 23.095 1.00 50.30 ? 2015 HOH A O 1 HETATM 2806 O O . HOH K 6 . ? 10.747 41.616 25.744 1.00 25.76 ? 2016 HOH A O 1 HETATM 2807 O O . HOH K 6 . ? 4.441 42.920 29.468 1.00 38.80 ? 2017 HOH A O 1 HETATM 2808 O O . HOH K 6 . ? 4.000 46.389 27.641 1.00 42.64 ? 2018 HOH A O 1 HETATM 2809 O O . HOH K 6 . ? -3.532 23.913 -3.864 1.00 49.38 ? 2019 HOH A O 1 HETATM 2810 O O . HOH K 6 . ? 4.229 52.346 18.434 1.00 34.97 ? 2020 HOH A O 1 HETATM 2811 O O . HOH K 6 . ? -12.678 30.725 -11.230 1.00 37.27 ? 2021 HOH A O 1 HETATM 2812 O O . HOH K 6 . ? -2.889 32.338 -12.348 1.00 43.94 ? 2022 HOH A O 1 HETATM 2813 O O . HOH K 6 . ? -10.857 34.882 -8.502 1.00 29.25 ? 2023 HOH A O 1 HETATM 2814 O O . HOH K 6 . ? -13.017 34.685 -4.606 1.00 37.90 ? 2024 HOH A O 1 HETATM 2815 O O . HOH K 6 . ? 3.955 32.517 -14.535 1.00 56.03 ? 2025 HOH A O 1 HETATM 2816 O O . HOH K 6 . ? -10.325 32.155 32.810 1.00 46.33 ? 2026 HOH A O 1 HETATM 2817 O O . HOH K 6 . ? -2.360 45.878 15.059 1.00 17.89 ? 2027 HOH A O 1 HETATM 2818 O O . HOH K 6 . ? -2.370 50.692 13.439 1.00 29.52 ? 2028 HOH A O 1 HETATM 2819 O O . HOH K 6 . ? -2.166 44.903 12.464 1.00 24.71 ? 2029 HOH A O 1 HETATM 2820 O O . HOH K 6 . ? -0.775 46.015 8.637 1.00 33.08 ? 2030 HOH A O 1 HETATM 2821 O O . HOH K 6 . ? 16.099 11.753 11.493 1.00 29.90 ? 2031 HOH A O 1 HETATM 2822 O O . HOH K 6 . ? -0.408 43.638 19.119 1.00 22.22 ? 2032 HOH A O 1 HETATM 2823 O O . HOH K 6 . ? 29.286 19.565 17.187 1.00 27.12 ? 2033 HOH A O 1 HETATM 2824 O O . HOH K 6 . ? -1.392 49.992 22.087 1.00 25.80 ? 2034 HOH A O 1 HETATM 2825 O O . HOH K 6 . ? -4.691 42.808 21.975 1.00 30.11 ? 2035 HOH A O 1 HETATM 2826 O O . HOH K 6 . ? -4.897 41.440 18.692 1.00 32.30 ? 2036 HOH A O 1 HETATM 2827 O O . HOH K 6 . ? -3.671 42.274 25.226 1.00 28.64 ? 2037 HOH A O 1 HETATM 2828 O O . HOH K 6 . ? -5.380 39.192 16.676 1.00 20.26 ? 2038 HOH A O 1 HETATM 2829 O O . HOH K 6 . ? 10.039 16.284 -1.027 1.00 38.16 ? 2039 HOH A O 1 HETATM 2830 O O . HOH K 6 . ? -5.072 31.461 16.879 1.00 12.88 ? 2040 HOH A O 1 HETATM 2831 O O . HOH K 6 . ? -1.446 19.689 4.754 1.00 17.92 ? 2041 HOH A O 1 HETATM 2832 O O . HOH K 6 . ? -0.474 25.448 -1.889 1.00 19.00 ? 2042 HOH A O 1 HETATM 2833 O O . HOH K 6 . ? 12.796 27.606 37.499 1.00 47.85 ? 2043 HOH A O 1 HETATM 2834 O O . HOH K 6 . ? 19.895 33.941 -5.401 1.00 37.67 ? 2044 HOH A O 1 HETATM 2835 O O . HOH K 6 . ? 2.280 24.401 -5.895 1.00 36.63 ? 2045 HOH A O 1 HETATM 2836 O O . HOH K 6 . ? -1.008 24.763 -4.517 1.00 35.42 ? 2046 HOH A O 1 HETATM 2837 O O . HOH K 6 . ? 16.885 28.137 -12.551 1.00 49.90 ? 2047 HOH A O 1 HETATM 2838 O O . HOH K 6 . ? 1.860 31.553 -3.294 1.00 32.83 ? 2048 HOH A O 1 HETATM 2839 O O . HOH K 6 . ? -1.598 26.235 -6.602 1.00 41.77 ? 2049 HOH A O 1 HETATM 2840 O O . HOH K 6 . ? -2.000 28.805 -11.598 1.00 53.82 ? 2050 HOH A O 1 HETATM 2841 O O . HOH K 6 . ? -9.747 30.845 -10.479 1.00 35.81 ? 2051 HOH A O 1 HETATM 2842 O O . HOH K 6 . ? 5.529 35.433 -14.795 1.00 52.66 ? 2052 HOH A O 1 HETATM 2843 O O . HOH K 6 . ? 8.031 29.622 37.383 1.00 41.93 ? 2053 HOH A O 1 HETATM 2844 O O . HOH K 6 . ? 5.535 31.207 37.356 1.00 36.98 ? 2054 HOH A O 1 HETATM 2845 O O . HOH K 6 . ? -1.981 34.499 -10.891 1.00 25.52 ? 2055 HOH A O 1 HETATM 2846 O O . HOH K 6 . ? 0.696 34.671 -11.831 1.00 49.74 ? 2056 HOH A O 1 HETATM 2847 O O . HOH K 6 . ? 2.523 33.761 -8.059 1.00 39.86 ? 2057 HOH A O 1 HETATM 2848 O O . HOH K 6 . ? -9.316 36.847 -4.931 1.00 22.72 ? 2058 HOH A O 1 HETATM 2849 O O . HOH K 6 . ? -10.685 34.569 -5.865 1.00 20.16 ? 2059 HOH A O 1 HETATM 2850 O O . HOH K 6 . ? -9.267 29.791 -8.083 1.00 17.34 ? 2060 HOH A O 1 HETATM 2851 O O . HOH K 6 . ? -9.670 32.141 -4.858 1.00 13.24 ? 2061 HOH A O 1 HETATM 2852 O O . HOH K 6 . ? -7.213 27.407 -7.626 1.00 24.36 ? 2062 HOH A O 1 HETATM 2853 O O . HOH K 6 . ? -3.227 28.556 -6.459 1.00 21.08 ? 2063 HOH A O 1 HETATM 2854 O O . HOH K 6 . ? -13.050 31.753 30.160 1.00 55.34 ? 2064 HOH A O 1 HETATM 2855 O O . HOH K 6 . ? -10.884 33.704 30.910 1.00 39.30 ? 2065 HOH A O 1 HETATM 2856 O O . HOH K 6 . ? -9.154 37.390 28.982 1.00 39.15 ? 2066 HOH A O 1 HETATM 2857 O O . HOH K 6 . ? -6.263 38.927 -6.989 1.00 52.00 ? 2067 HOH A O 1 HETATM 2858 O O . HOH K 6 . ? -10.178 38.204 -2.388 1.00 25.27 ? 2068 HOH A O 1 HETATM 2859 O O . HOH K 6 . ? -9.396 31.353 -0.262 1.00 10.50 ? 2069 HOH A O 1 HETATM 2860 O O . HOH K 6 . ? 16.155 14.212 8.179 1.00 22.09 ? 2070 HOH A O 1 HETATM 2861 O O . HOH K 6 . ? 14.450 13.897 11.532 1.00 18.43 ? 2071 HOH A O 1 HETATM 2862 O O . HOH K 6 . ? 12.450 12.826 9.953 1.00 29.31 ? 2072 HOH A O 1 HETATM 2863 O O . HOH K 6 . ? -10.432 41.404 4.142 1.00 36.89 ? 2073 HOH A O 1 HETATM 2864 O O . HOH K 6 . ? -14.436 35.244 -0.429 1.00 28.42 ? 2074 HOH A O 1 HETATM 2865 O O . HOH K 6 . ? -9.702 43.328 9.001 1.00 43.16 ? 2075 HOH A O 1 HETATM 2866 O O . HOH K 6 . ? -7.862 43.181 4.625 1.00 32.24 ? 2076 HOH A O 1 HETATM 2867 O O . HOH K 6 . ? -5.608 42.507 9.290 1.00 35.07 ? 2077 HOH A O 1 HETATM 2868 O O . HOH K 6 . ? -10.556 42.630 6.629 1.00 53.83 ? 2078 HOH A O 1 HETATM 2869 O O . HOH K 6 . ? -13.012 38.074 3.829 1.00 19.56 ? 2079 HOH A O 1 HETATM 2870 O O . HOH K 6 . ? -12.645 41.084 12.584 1.00 35.92 ? 2080 HOH A O 1 HETATM 2871 O O . HOH K 6 . ? -14.636 36.551 8.281 1.00 30.01 ? 2081 HOH A O 1 HETATM 2872 O O . HOH K 6 . ? -15.270 37.382 11.345 1.00 29.63 ? 2082 HOH A O 1 HETATM 2873 O O . HOH K 6 . ? 17.850 12.352 13.369 1.00 22.04 ? 2083 HOH A O 1 HETATM 2874 O O . HOH K 6 . ? 27.693 17.715 15.845 1.00 47.64 ? 2084 HOH A O 1 HETATM 2875 O O . HOH K 6 . ? 26.122 15.401 17.658 1.00 40.62 ? 2085 HOH A O 1 HETATM 2876 O O . HOH K 6 . ? -13.809 36.442 13.728 1.00 26.11 ? 2086 HOH A O 1 HETATM 2877 O O . HOH K 6 . ? -8.004 41.765 15.295 1.00 26.71 ? 2087 HOH A O 1 HETATM 2878 O O . HOH K 6 . ? -7.065 41.121 11.012 1.00 24.97 ? 2088 HOH A O 1 HETATM 2879 O O . HOH K 6 . ? 30.446 24.455 -0.464 1.00 17.41 ? 2089 HOH A O 1 HETATM 2880 O O . HOH K 6 . ? -2.776 43.029 18.810 1.00 40.32 ? 2090 HOH A O 1 HETATM 2881 O O . HOH K 6 . ? -5.616 46.591 16.833 1.00 35.78 ? 2091 HOH A O 1 HETATM 2882 O O . HOH K 6 . ? 28.069 26.994 10.644 1.00 32.79 ? 2092 HOH A O 1 HETATM 2883 O O . HOH K 6 . ? 25.421 34.893 -0.189 1.00 32.79 ? 2093 HOH A O 1 HETATM 2884 O O . HOH K 6 . ? 18.951 36.155 -4.975 1.00 27.37 ? 2094 HOH A O 1 HETATM 2885 O O . HOH K 6 . ? 15.475 41.608 -3.939 1.00 45.26 ? 2095 HOH A O 1 HETATM 2886 O O . HOH K 6 . ? 17.037 47.955 -0.406 1.00 34.94 ? 2096 HOH A O 1 HETATM 2887 O O . HOH K 6 . ? 5.966 22.124 -4.291 1.00 23.86 ? 2097 HOH A O 1 HETATM 2888 O O . HOH K 6 . ? 10.280 20.575 -1.970 1.00 24.45 ? 2098 HOH A O 1 HETATM 2889 O O . HOH K 6 . ? 8.886 19.973 -3.351 1.00 35.17 ? 2099 HOH A O 1 HETATM 2890 O O . HOH K 6 . ? 12.320 17.670 -2.070 1.00 33.56 ? 2100 HOH A O 1 HETATM 2891 O O . HOH K 6 . ? 13.334 22.706 3.808 1.00 8.94 ? 2101 HOH A O 1 HETATM 2892 O O . HOH K 6 . ? 14.092 26.432 -0.234 1.00 10.52 ? 2102 HOH A O 1 HETATM 2893 O O . HOH K 6 . ? 14.707 15.854 -1.285 1.00 19.40 ? 2103 HOH A O 1 HETATM 2894 O O . HOH K 6 . ? 13.962 16.204 -5.201 1.00 24.11 ? 2104 HOH A O 1 HETATM 2895 O O . HOH K 6 . ? 8.626 11.952 15.014 1.00 62.55 ? 2105 HOH A O 1 HETATM 2896 O O . HOH K 6 . ? 7.283 12.703 20.892 1.00 20.42 ? 2106 HOH A O 1 HETATM 2897 O O . HOH K 6 . ? 11.458 17.528 -7.158 1.00 39.23 ? 2107 HOH A O 1 HETATM 2898 O O . HOH K 6 . ? 15.403 13.769 -5.957 1.00 42.48 ? 2108 HOH A O 1 HETATM 2899 O O . HOH K 6 . ? 10.906 15.550 -11.328 1.00 44.11 ? 2109 HOH A O 1 HETATM 2900 O O . HOH K 6 . ? 24.089 27.808 26.641 1.00 30.14 ? 2110 HOH A O 1 HETATM 2901 O O . HOH K 6 . ? 28.535 22.130 17.771 1.00 19.89 ? 2111 HOH A O 1 HETATM 2902 O O . HOH K 6 . ? 31.670 26.261 21.340 1.00 27.49 ? 2112 HOH A O 1 HETATM 2903 O O . HOH K 6 . ? 11.032 22.708 -13.242 1.00 29.59 ? 2113 HOH A O 1 HETATM 2904 O O . HOH K 6 . ? 27.199 32.107 22.989 1.00 34.71 ? 2114 HOH A O 1 HETATM 2905 O O . HOH K 6 . ? 7.231 17.435 -9.637 1.00 29.96 ? 2115 HOH A O 1 HETATM 2906 O O . HOH K 6 . ? 4.560 17.002 -11.410 1.00 35.00 ? 2116 HOH A O 1 HETATM 2907 O O . HOH K 6 . ? 23.453 32.129 25.201 1.00 28.90 ? 2117 HOH A O 1 HETATM 2908 O O . HOH K 6 . ? 3.782 20.863 -13.818 1.00 27.36 ? 2118 HOH A O 1 HETATM 2909 O O . HOH K 6 . ? 27.495 39.195 12.811 1.00 49.67 ? 2119 HOH A O 1 HETATM 2910 O O . HOH K 6 . ? 24.611 42.913 13.288 1.00 43.16 ? 2120 HOH A O 1 HETATM 2911 O O . HOH K 6 . ? 4.119 23.058 -7.221 1.00 30.81 ? 2121 HOH A O 1 HETATM 2912 O O . HOH K 6 . ? 22.648 46.479 13.476 1.00 46.03 ? 2122 HOH A O 1 HETATM 2913 O O . HOH K 6 . ? 8.354 20.806 -6.049 1.00 36.55 ? 2123 HOH A O 1 HETATM 2914 O O . HOH K 6 . ? 17.930 51.562 10.246 1.00 35.27 ? 2124 HOH A O 1 HETATM 2915 O O . HOH K 6 . ? 18.245 51.917 14.136 1.00 66.36 ? 2125 HOH A O 1 HETATM 2916 O O . HOH K 6 . ? 14.154 47.630 16.186 1.00 49.47 ? 2126 HOH A O 1 HETATM 2917 O O . HOH K 6 . ? 20.905 17.098 -6.450 1.00 31.52 ? 2127 HOH A O 1 HETATM 2918 O O . HOH K 6 . ? 14.384 26.084 33.497 1.00 26.86 ? 2128 HOH A O 1 HETATM 2919 O O . HOH K 6 . ? 14.574 25.459 36.075 1.00 34.35 ? 2129 HOH A O 1 HETATM 2920 O O . HOH K 6 . ? 24.506 16.893 -8.716 1.00 29.06 ? 2130 HOH A O 1 HETATM 2921 O O . HOH K 6 . ? 22.762 19.385 -10.451 1.00 45.37 ? 2131 HOH A O 1 HETATM 2922 O O . HOH K 6 . ? 9.237 15.804 37.303 1.00 29.31 ? 2132 HOH A O 1 HETATM 2923 O O . HOH K 6 . ? 2.930 21.821 34.809 1.00 45.00 ? 2133 HOH A O 1 HETATM 2924 O O . HOH K 6 . ? 28.376 22.202 -4.437 1.00 23.75 ? 2134 HOH A O 1 HETATM 2925 O O . HOH K 6 . ? 31.144 17.960 -5.619 1.00 13.22 ? 2135 HOH A O 1 HETATM 2926 O O . HOH K 6 . ? 23.767 16.122 -5.418 1.00 29.78 ? 2136 HOH A O 1 HETATM 2927 O O . HOH K 6 . ? 29.678 20.432 -2.640 1.00 24.84 ? 2137 HOH A O 1 HETATM 2928 O O . HOH K 6 . ? 24.793 21.178 -10.232 1.00 25.62 ? 2138 HOH A O 1 HETATM 2929 O O . HOH K 6 . ? 21.733 23.260 -9.131 1.00 23.01 ? 2139 HOH A O 1 HETATM 2930 O O . HOH K 6 . ? 26.060 23.535 -3.694 1.00 24.88 ? 2140 HOH A O 1 HETATM 2931 O O . HOH K 6 . ? 25.727 26.647 -8.533 1.00 32.46 ? 2141 HOH A O 1 HETATM 2932 O O . HOH K 6 . ? 26.472 25.944 -4.899 1.00 32.35 ? 2142 HOH A O 1 HETATM 2933 O O . HOH K 6 . ? 13.289 10.932 15.267 1.00 34.66 ? 2143 HOH A O 1 HETATM 2934 O O . HOH K 6 . ? 21.616 30.299 -7.447 1.00 27.56 ? 2144 HOH A O 1 HETATM 2935 O O . HOH K 6 . ? 19.457 32.906 -7.700 1.00 31.09 ? 2145 HOH A O 1 HETATM 2936 O O . HOH K 6 . ? 13.318 29.346 -12.877 1.00 49.67 ? 2146 HOH A O 1 HETATM 2937 O O . HOH K 6 . ? 13.534 28.818 32.859 1.00 26.97 ? 2147 HOH A O 1 HETATM 2938 O O . HOH K 6 . ? 20.854 36.718 33.007 1.00 33.60 ? 2148 HOH A O 1 HETATM 2939 O O . HOH K 6 . ? 16.549 31.809 -10.852 1.00 25.62 ? 2149 HOH A O 1 HETATM 2940 O O . HOH K 6 . ? 18.829 34.699 -9.404 1.00 39.23 ? 2150 HOH A O 1 HETATM 2941 O O . HOH K 6 . ? 13.124 37.669 -9.108 1.00 25.64 ? 2151 HOH A O 1 HETATM 2942 O O . HOH K 6 . ? 24.483 38.952 19.302 1.00 30.29 ? 2152 HOH A O 1 HETATM 2943 O O . HOH K 6 . ? 26.029 35.873 23.847 1.00 42.06 ? 2153 HOH A O 1 HETATM 2944 O O . HOH K 6 . ? 10.649 33.033 -14.588 1.00 33.25 ? 2154 HOH A O 1 HETATM 2945 O O . HOH K 6 . ? 4.964 33.764 -9.891 1.00 35.94 ? 2155 HOH A O 1 HETATM 2946 O O . HOH K 6 . ? 12.162 26.088 -13.364 1.00 29.81 ? 2156 HOH A O 1 HETATM 2947 O O . HOH K 6 . ? 9.135 24.449 -12.625 1.00 25.16 ? 2157 HOH A O 1 HETATM 2948 O O . HOH K 6 . ? 5.413 38.354 -7.653 1.00 28.25 ? 2158 HOH A O 1 HETATM 2949 O O . HOH K 6 . ? 10.077 35.978 -14.325 1.00 58.23 ? 2159 HOH A O 1 HETATM 2950 O O . HOH K 6 . ? 5.585 35.873 -11.287 1.00 39.23 ? 2160 HOH A O 1 HETATM 2951 O O . HOH K 6 . ? -0.640 10.489 29.810 1.00 57.90 ? 2161 HOH A O 1 HETATM 2952 O O . HOH K 6 . ? 1.945 33.646 -5.110 1.00 20.97 ? 2162 HOH A O 1 HETATM 2953 O O . HOH K 6 . ? -9.759 16.427 28.761 1.00 35.58 ? 2163 HOH A O 1 HETATM 2954 O O . HOH K 6 . ? 11.269 41.052 -4.793 1.00 45.15 ? 2164 HOH A O 1 HETATM 2955 O O . HOH K 6 . ? 8.222 39.544 -7.893 1.00 26.39 ? 2165 HOH A O 1 HETATM 2956 O O . HOH K 6 . ? 7.379 27.134 35.755 1.00 25.53 ? 2166 HOH A O 1 HETATM 2957 O O . HOH K 6 . ? 0.726 29.971 35.235 1.00 33.33 ? 2167 HOH A O 1 HETATM 2958 O O . HOH K 6 . ? 3.894 29.252 36.209 1.00 34.95 ? 2168 HOH A O 1 HETATM 2959 O O . HOH K 6 . ? 5.970 33.326 35.584 1.00 26.16 ? 2169 HOH A O 1 HETATM 2960 O O . HOH K 6 . ? 10.320 30.705 36.230 1.00 42.11 ? 2170 HOH A O 1 HETATM 2961 O O . HOH K 6 . ? 7.144 42.397 -6.732 1.00 27.99 ? 2171 HOH A O 1 HETATM 2962 O O . HOH K 6 . ? 1.292 41.625 -8.542 1.00 32.34 ? 2172 HOH A O 1 HETATM 2963 O O . HOH K 6 . ? 6.872 41.434 -2.268 1.00 29.51 ? 2173 HOH A O 1 HETATM 2964 O O . HOH K 6 . ? 0.367 40.875 -3.778 1.00 28.52 ? 2174 HOH A O 1 HETATM 2965 O O . HOH K 6 . ? 4.463 40.546 -5.913 1.00 32.74 ? 2175 HOH A O 1 HETATM 2966 O O . HOH K 6 . ? 9.170 42.059 -3.479 1.00 42.49 ? 2176 HOH A O 1 HETATM 2967 O O . HOH K 6 . ? 2.612 45.546 -1.559 1.00 23.02 ? 2177 HOH A O 1 HETATM 2968 O O . HOH K 6 . ? 7.832 42.982 -0.372 1.00 31.25 ? 2178 HOH A O 1 HETATM 2969 O O . HOH K 6 . ? -2.282 41.337 -3.456 1.00 26.98 ? 2179 HOH A O 1 HETATM 2970 O O . HOH K 6 . ? -6.968 45.425 2.526 1.00 29.64 ? 2180 HOH A O 1 HETATM 2971 O O . HOH K 6 . ? -4.260 47.609 3.890 1.00 40.23 ? 2181 HOH A O 1 HETATM 2972 O O . HOH K 6 . ? -16.317 26.702 23.080 1.00 23.95 ? 2182 HOH A O 1 HETATM 2973 O O . HOH K 6 . ? -8.177 39.300 0.252 1.00 98.55 ? 2183 HOH A O 1 HETATM 2974 O O . HOH K 6 . ? -8.704 40.498 -1.432 1.00 25.55 ? 2184 HOH A O 1 HETATM 2975 O O . HOH K 6 . ? -7.988 24.727 31.949 1.00 46.31 ? 2185 HOH A O 1 HETATM 2976 O O . HOH K 6 . ? -10.986 27.080 29.902 1.00 28.56 ? 2186 HOH A O 1 HETATM 2977 O O . HOH K 6 . ? -12.733 29.433 24.046 1.00 21.46 ? 2187 HOH A O 1 HETATM 2978 O O . HOH K 6 . ? -3.192 49.793 4.156 1.00 41.16 ? 2188 HOH A O 1 HETATM 2979 O O . HOH K 6 . ? -1.302 42.554 11.339 1.00 16.86 ? 2189 HOH A O 1 HETATM 2980 O O . HOH K 6 . ? -13.470 33.210 27.097 1.00 36.92 ? 2190 HOH A O 1 HETATM 2981 O O . HOH K 6 . ? -10.120 34.624 28.570 1.00 32.09 ? 2191 HOH A O 1 HETATM 2982 O O . HOH K 6 . ? 1.428 44.327 7.209 1.00 18.18 ? 2192 HOH A O 1 HETATM 2983 O O . HOH K 6 . ? 2.001 33.527 35.734 1.00 39.88 ? 2193 HOH A O 1 HETATM 2984 O O . HOH K 6 . ? 14.490 16.223 6.847 1.00 10.49 ? 2194 HOH A O 1 HETATM 2985 O O . HOH K 6 . ? 14.495 14.978 14.067 1.00 10.77 ? 2195 HOH A O 1 HETATM 2986 O O . HOH K 6 . ? 15.843 16.012 10.421 1.00 13.87 ? 2196 HOH A O 1 HETATM 2987 O O . HOH K 6 . ? -13.539 21.997 2.510 1.00 36.65 ? 2197 HOH A O 1 HETATM 2988 O O . HOH K 6 . ? 8.136 13.766 3.969 1.00 23.22 ? 2198 HOH A O 1 HETATM 2989 O O . HOH K 6 . ? 10.710 13.786 8.059 1.00 22.07 ? 2199 HOH A O 1 HETATM 2990 O O . HOH K 6 . ? 11.196 14.350 0.680 1.00 29.52 ? 2200 HOH A O 1 HETATM 2991 O O . HOH K 6 . ? 8.777 11.447 6.604 1.00 39.28 ? 2201 HOH A O 1 HETATM 2992 O O . HOH K 6 . ? 13.199 11.258 5.360 1.00 79.63 ? 2202 HOH A O 1 HETATM 2993 O O . HOH K 6 . ? 13.536 13.604 7.796 1.00 47.34 ? 2203 HOH A O 1 HETATM 2994 O O . HOH K 6 . ? -14.834 23.854 3.954 1.00 28.11 ? 2204 HOH A O 1 HETATM 2995 O O . HOH K 6 . ? 6.609 19.245 7.771 1.00 9.33 ? 2205 HOH A O 1 HETATM 2996 O O . HOH K 6 . ? -19.335 35.428 10.355 1.00 37.24 ? 2206 HOH A O 1 HETATM 2997 O O . HOH K 6 . ? -19.260 23.456 17.811 1.00 25.19 ? 2207 HOH A O 1 HETATM 2998 O O . HOH K 6 . ? 1.826 21.019 -2.172 1.00 20.83 ? 2208 HOH A O 1 HETATM 2999 O O . HOH K 6 . ? 7.663 16.967 0.030 1.00 17.62 ? 2209 HOH A O 1 HETATM 3000 O O . HOH K 6 . ? 13.887 15.304 1.337 1.00 15.40 ? 2210 HOH A O 1 HETATM 3001 O O . HOH K 6 . ? -14.866 31.046 23.247 1.00 29.98 ? 2211 HOH A O 1 HETATM 3002 O O . HOH K 6 . ? -15.378 32.531 25.456 1.00 46.46 ? 2212 HOH A O 1 HETATM 3003 O O . HOH K 6 . ? 15.261 11.657 -0.179 1.00 36.18 ? 2213 HOH A O 1 HETATM 3004 O O . HOH K 6 . ? 19.030 11.109 2.995 1.00 32.27 ? 2214 HOH A O 1 HETATM 3005 O O . HOH K 6 . ? 18.145 13.083 6.572 1.00 19.33 ? 2215 HOH A O 1 HETATM 3006 O O . HOH K 6 . ? 16.334 25.554 3.127 1.00 10.48 ? 2216 HOH A O 1 HETATM 3007 O O . HOH K 6 . ? 23.801 11.534 1.436 1.00 28.45 ? 2217 HOH A O 1 HETATM 3008 O O . HOH K 6 . ? 25.231 13.471 -3.134 1.00 30.74 ? 2218 HOH A O 1 HETATM 3009 O O . HOH K 6 . ? 21.075 9.742 -0.687 1.00 47.35 ? 2219 HOH A O 1 HETATM 3010 O O . HOH K 6 . ? 29.775 18.143 1.876 1.00 39.90 ? 2220 HOH A O 1 HETATM 3011 O O . HOH K 6 . ? 24.613 16.525 7.031 1.00 14.17 ? 2221 HOH A O 1 HETATM 3012 O O . HOH K 6 . ? 22.329 10.007 6.152 1.00 34.74 ? 2222 HOH A O 1 HETATM 3013 O O . HOH K 6 . ? 24.964 10.631 3.641 1.00 35.76 ? 2223 HOH A O 1 HETATM 3014 O O . HOH K 6 . ? 20.264 11.284 11.689 1.00 39.82 ? 2224 HOH A O 1 HETATM 3015 O O . HOH K 6 . ? 17.602 16.849 12.400 1.00 12.51 ? 2225 HOH A O 1 HETATM 3016 O O . HOH K 6 . ? 19.877 11.257 7.909 1.00 22.30 ? 2226 HOH A O 1 HETATM 3017 O O . HOH K 6 . ? 25.628 13.697 15.072 1.00 30.32 ? 2227 HOH A O 1 HETATM 3018 O O . HOH K 6 . ? 26.171 18.625 13.994 1.00 22.16 ? 2228 HOH A O 1 HETATM 3019 O O . HOH K 6 . ? 21.896 11.141 13.995 1.00 34.82 ? 2229 HOH A O 1 HETATM 3020 O O . HOH K 6 . ? 28.299 16.068 8.045 1.00 23.83 ? 2230 HOH A O 1 HETATM 3021 O O . HOH K 6 . ? 29.422 17.683 10.482 1.00 27.36 ? 2231 HOH A O 1 HETATM 3022 O O . HOH K 6 . ? 31.197 23.219 9.864 1.00 17.18 ? 2232 HOH A O 1 HETATM 3023 O O . HOH K 6 . ? 32.033 18.835 10.223 1.00 37.97 ? 2233 HOH A O 1 HETATM 3024 O O . HOH K 6 . ? 34.674 22.319 6.666 1.00 32.12 ? 2234 HOH A O 1 HETATM 3025 O O . HOH K 6 . ? 31.733 19.627 7.207 1.00 24.46 ? 2235 HOH A O 1 HETATM 3026 O O . HOH K 6 . ? 31.046 19.901 4.173 1.00 23.65 ? 2236 HOH A O 1 HETATM 3027 O O . HOH K 6 . ? 27.718 24.494 -0.421 1.00 20.61 ? 2237 HOH A O 1 HETATM 3028 O O . HOH K 6 . ? 32.885 22.603 2.627 1.00 32.23 ? 2238 HOH A O 1 HETATM 3029 O O . HOH K 6 . ? 25.567 28.065 9.944 1.00 16.31 ? 2239 HOH A O 1 HETATM 3030 O O . HOH K 6 . ? 31.560 25.077 1.868 1.00 26.77 ? 2240 HOH A O 1 HETATM 3031 O O . HOH K 6 . ? 31.662 29.022 3.623 1.00 27.89 ? 2241 HOH A O 1 HETATM 3032 O O . HOH K 6 . ? 27.056 31.302 2.529 1.00 16.78 ? 2242 HOH A O 1 HETATM 3033 O O . HOH K 6 . ? 22.986 28.813 -4.900 1.00 19.86 ? 2243 HOH A O 1 HETATM 3034 O O . HOH K 6 . ? 27.007 27.111 -1.118 1.00 19.88 ? 2244 HOH A O 1 HETATM 3035 O O . HOH K 6 . ? 22.550 34.429 -1.457 1.00 19.30 ? 2245 HOH A O 1 HETATM 3036 O O . HOH K 6 . ? 22.374 41.300 2.112 1.00 22.01 ? 2246 HOH A O 1 HETATM 3037 O O . HOH K 6 . ? 16.770 37.015 -3.634 1.00 15.78 ? 2247 HOH A O 1 HETATM 3038 O O . HOH K 6 . ? 17.785 56.157 5.637 1.00 70.54 ? 2248 HOH A O 1 HETATM 3039 O O . HOH K 6 . ? -19.437 40.448 4.323 1.00 39.54 ? 2249 HOH A O 1 HETATM 3040 O O . HOH K 6 . ? -22.851 33.633 -1.470 1.00 34.90 ? 2250 HOH A O 1 HETATM 3041 O O . HOH K 6 . ? 18.824 43.667 1.736 1.00 21.13 ? 2251 HOH A O 1 HETATM 3042 O O . HOH K 6 . ? 17.355 39.762 -3.428 1.00 28.93 ? 2252 HOH A O 1 HETATM 3043 O O . HOH K 6 . ? 14.686 44.111 -0.807 1.00 30.03 ? 2253 HOH A O 1 HETATM 3044 O O . HOH K 6 . ? 15.891 38.259 -7.722 1.00 27.01 ? 2254 HOH A O 1 HETATM 3045 O O . HOH K 6 . ? 10.308 43.426 -1.287 1.00 29.64 ? 2255 HOH A O 1 HETATM 3046 O O . HOH K 6 . ? 15.550 46.105 0.324 1.00 31.49 ? 2256 HOH A O 1 HETATM 3047 O O . HOH K 6 . ? 18.094 45.856 3.142 1.00 14.81 ? 2257 HOH A O 1 HETATM 3048 O O . HOH K 6 . ? 7.594 44.259 10.290 1.00 11.03 ? 2258 HOH A O 1 HETATM 3049 O O . HOH K 6 . ? 9.876 42.317 13.043 1.00 9.69 ? 2259 HOH A O 1 HETATM 3050 O O . HOH K 6 . ? 7.902 13.763 19.060 1.00 21.43 ? 2260 HOH A O 1 HETATM 3051 O O . HOH K 6 . ? 9.381 11.951 17.643 1.00 31.31 ? 2261 HOH A O 1 HETATM 3052 O O . HOH K 6 . ? 18.420 8.779 20.577 1.00 25.71 ? 2262 HOH A O 1 HETATM 3053 O O . HOH K 6 . ? 14.834 9.300 20.524 1.00 29.86 ? 2263 HOH A O 1 HETATM 3054 O O . HOH K 6 . ? 16.326 7.611 18.273 1.00 55.18 ? 2264 HOH A O 1 HETATM 3055 O O . HOH K 6 . ? 22.765 11.918 18.026 1.00 32.07 ? 2265 HOH A O 1 HETATM 3056 O O . HOH K 6 . ? 20.131 10.547 16.037 1.00 42.40 ? 2266 HOH A O 1 HETATM 3057 O O . HOH K 6 . ? 17.302 14.906 14.479 1.00 11.19 ? 2267 HOH A O 1 HETATM 3058 O O . HOH K 6 . ? 25.726 20.929 26.882 1.00 46.49 ? 2268 HOH A O 1 HETATM 3059 O O . HOH K 6 . ? 26.090 15.755 20.163 1.00 25.98 ? 2269 HOH A O 1 HETATM 3060 O O . HOH K 6 . ? 23.963 22.812 26.377 1.00 23.72 ? 2270 HOH A O 1 HETATM 3061 O O . HOH K 6 . ? 20.998 21.133 28.241 1.00 27.09 ? 2271 HOH A O 1 HETATM 3062 O O . HOH K 6 . ? 23.390 18.059 26.573 1.00 24.90 ? 2272 HOH A O 1 HETATM 3063 O O . HOH K 6 . ? 30.022 25.410 23.388 1.00 30.51 ? 2273 HOH A O 1 HETATM 3064 O O . HOH K 6 . ? 28.456 21.938 20.562 1.00 30.66 ? 2274 HOH A O 1 HETATM 3065 O O . HOH K 6 . ? 24.751 25.256 25.560 1.00 23.68 ? 2275 HOH A O 1 HETATM 3066 O O . HOH K 6 . ? 26.634 23.668 16.377 1.00 14.89 ? 2276 HOH A O 1 HETATM 3067 O O . HOH K 6 . ? 28.837 30.991 21.202 1.00 32.05 ? 2277 HOH A O 1 HETATM 3068 O O . HOH K 6 . ? 24.600 32.197 22.755 1.00 19.72 ? 2278 HOH A O 1 HETATM 3069 O O . HOH K 6 . ? 27.207 34.308 12.080 1.00 16.99 ? 2279 HOH A O 1 HETATM 3070 O O . HOH K 6 . ? 29.028 35.082 19.808 1.00 29.78 ? 2280 HOH A O 1 HETATM 3071 O O . HOH K 6 . ? 28.626 37.435 14.471 1.00 40.49 ? 2281 HOH A O 1 HETATM 3072 O O . HOH K 6 . ? 24.830 40.308 14.051 1.00 22.53 ? 2282 HOH A O 1 HETATM 3073 O O . HOH K 6 . ? 26.015 37.675 3.349 1.00 23.67 ? 2283 HOH A O 1 HETATM 3074 O O . HOH K 6 . ? 27.209 36.917 11.166 1.00 21.79 ? 2284 HOH A O 1 HETATM 3075 O O . HOH K 6 . ? 25.726 33.693 2.535 1.00 16.60 ? 2285 HOH A O 1 HETATM 3076 O O . HOH K 6 . ? 14.493 43.526 16.168 1.00 30.74 ? 2286 HOH A O 1 HETATM 3077 O O . HOH K 6 . ? 21.148 44.160 13.471 1.00 27.61 ? 2287 HOH A O 1 HETATM 3078 O O . HOH K 6 . ? 26.959 39.393 7.138 1.00 27.96 ? 2288 HOH A O 1 HETATM 3079 O O . HOH K 6 . ? 20.003 41.948 3.396 1.00 16.88 ? 2289 HOH A O 1 HETATM 3080 O O . HOH K 6 . ? 16.220 40.529 11.242 1.00 13.41 ? 2290 HOH A O 1 HETATM 3081 O O . HOH K 6 . ? 17.130 49.294 12.429 1.00 38.21 ? 2291 HOH A O 1 HETATM 3082 O O . HOH K 6 . ? 20.711 49.285 11.474 1.00 33.08 ? 2292 HOH A O 1 HETATM 3083 O O . HOH K 6 . ? 14.225 49.503 12.091 1.00 18.85 ? 2293 HOH A O 1 HETATM 3084 O O . HOH K 6 . ? 15.698 50.877 8.867 1.00 17.51 ? 2294 HOH A O 1 HETATM 3085 O O . HOH K 6 . ? 12.644 47.957 13.761 1.00 18.84 ? 2295 HOH A O 1 HETATM 3086 O O . HOH K 6 . ? 13.807 27.621 22.624 1.00 25.25 ? 2296 HOH A O 1 HETATM 3087 O O . HOH K 6 . ? 13.744 24.116 22.958 1.00 13.11 ? 2297 HOH A O 1 HETATM 3088 O O . HOH K 6 . ? 12.188 29.312 21.141 1.00 12.45 ? 2298 HOH A O 1 HETATM 3089 O O . HOH K 6 . ? 11.868 21.422 17.851 1.00 8.92 ? 2299 HOH A O 1 HETATM 3090 O O . HOH K 6 . ? 17.291 23.175 33.296 1.00 25.06 ? 2300 HOH A O 1 HETATM 3091 O O . HOH K 6 . ? 13.697 22.928 36.699 1.00 34.07 ? 2301 HOH A O 1 HETATM 3092 O O . HOH K 6 . ? 15.954 17.965 34.014 1.00 23.60 ? 2302 HOH A O 1 HETATM 3093 O O . HOH K 6 . ? 14.866 23.765 32.096 1.00 16.51 ? 2303 HOH A O 1 HETATM 3094 O O . HOH K 6 . ? 5.235 20.792 36.448 1.00 39.37 ? 2304 HOH A O 1 HETATM 3095 O O . HOH K 6 . ? 4.776 18.322 37.801 1.00 40.47 ? 2305 HOH A O 1 HETATM 3096 O O . HOH K 6 . ? 9.499 19.612 37.516 1.00 26.82 ? 2306 HOH A O 1 HETATM 3097 O O . HOH K 6 . ? 6.721 15.854 37.952 1.00 41.43 ? 2307 HOH A O 1 HETATM 3098 O O . HOH K 6 . ? 1.533 18.726 33.595 1.00 45.69 ? 2308 HOH A O 1 HETATM 3099 O O . HOH K 6 . ? 3.361 19.345 35.343 1.00 58.57 ? 2309 HOH A O 1 HETATM 3100 O O . HOH K 6 . ? 5.846 13.299 37.029 1.00 27.09 ? 2310 HOH A O 1 HETATM 3101 O O . HOH K 6 . ? 9.421 10.083 30.731 1.00 13.16 ? 2311 HOH A O 1 HETATM 3102 O O . HOH K 6 . ? 9.919 17.984 33.399 1.00 20.10 ? 2312 HOH A O 1 HETATM 3103 O O . HOH K 6 . ? 6.203 10.543 27.951 1.00 19.82 ? 2313 HOH A O 1 HETATM 3104 O O . HOH K 6 . ? 2.204 19.846 31.288 1.00 19.26 ? 2314 HOH A O 1 HETATM 3105 O O . HOH K 6 . ? 13.019 17.462 32.043 1.00 21.65 ? 2315 HOH A O 1 HETATM 3106 O O . HOH K 6 . ? 12.878 15.456 24.268 1.00 18.64 ? 2316 HOH A O 1 HETATM 3107 O O . HOH K 6 . ? 19.175 14.915 22.834 1.00 16.97 ? 2317 HOH A O 1 HETATM 3108 O O . HOH K 6 . ? 11.894 10.865 18.512 1.00 29.97 ? 2318 HOH A O 1 HETATM 3109 O O . HOH K 6 . ? 13.359 13.502 16.186 1.00 11.59 ? 2319 HOH A O 1 HETATM 3110 O O . HOH K 6 . ? 21.439 20.144 19.734 1.00 10.64 ? 2320 HOH A O 1 HETATM 3111 O O . HOH K 6 . ? 15.054 17.998 23.842 1.00 13.17 ? 2321 HOH A O 1 HETATM 3112 O O . HOH K 6 . ? 12.281 21.764 20.597 1.00 9.49 ? 2322 HOH A O 1 HETATM 3113 O O . HOH K 6 . ? 18.666 21.470 31.200 1.00 28.20 ? 2323 HOH A O 1 HETATM 3114 O O . HOH K 6 . ? 18.611 24.823 31.178 1.00 29.02 ? 2324 HOH A O 1 HETATM 3115 O O . HOH K 6 . ? 15.040 24.162 29.399 1.00 13.63 ? 2325 HOH A O 1 HETATM 3116 O O . HOH K 6 . ? 22.085 29.969 26.206 1.00 23.14 ? 2326 HOH A O 1 HETATM 3117 O O . HOH K 6 . ? 19.156 23.647 22.541 1.00 12.03 ? 2327 HOH A O 1 HETATM 3118 O O . HOH K 6 . ? 18.829 35.540 30.419 1.00 31.01 ? 2328 HOH A O 1 HETATM 3119 O O . HOH K 6 . ? 21.775 30.902 28.771 1.00 29.88 ? 2329 HOH A O 1 HETATM 3120 O O . HOH K 6 . ? 17.754 29.299 32.865 1.00 43.93 ? 2330 HOH A O 1 HETATM 3121 O O . HOH K 6 . ? 14.203 30.802 30.907 1.00 23.94 ? 2331 HOH A O 1 HETATM 3122 O O . HOH K 6 . ? 26.222 40.383 26.202 1.00 33.41 ? 2332 HOH A O 1 HETATM 3123 O O . HOH K 6 . ? 17.323 39.182 23.254 1.00 18.49 ? 2333 HOH A O 1 HETATM 3124 O O . HOH K 6 . ? 24.043 34.903 22.497 1.00 21.18 ? 2334 HOH A O 1 HETATM 3125 O O . HOH K 6 . ? 24.027 36.173 19.864 1.00 14.60 ? 2335 HOH A O 1 HETATM 3126 O O . HOH K 6 . ? 13.326 40.624 23.022 1.00 25.89 ? 2336 HOH A O 1 HETATM 3127 O O . HOH K 6 . ? 14.794 43.125 18.791 1.00 39.70 ? 2337 HOH A O 1 HETATM 3128 O O . HOH K 6 . ? 15.818 40.939 22.063 1.00 24.23 ? 2338 HOH A O 1 HETATM 3129 O O . HOH K 6 . ? 18.120 40.520 19.465 1.00 17.90 ? 2339 HOH A O 1 HETATM 3130 O O . HOH K 6 . ? 13.510 31.410 19.839 1.00 11.88 ? 2340 HOH A O 1 HETATM 3131 O O . HOH K 6 . ? -4.547 12.305 22.823 1.00 49.75 ? 2341 HOH A O 1 HETATM 3132 O O . HOH K 6 . ? -6.038 10.840 17.881 1.00 47.53 ? 2342 HOH A O 1 HETATM 3133 O O . HOH K 6 . ? 0.033 9.860 21.093 1.00 36.32 ? 2343 HOH A O 1 HETATM 3134 O O . HOH K 6 . ? 0.817 12.398 14.833 1.00 45.96 ? 2344 HOH A O 1 HETATM 3135 O O . HOH K 6 . ? 8.004 14.812 21.284 1.00 26.25 ? 2345 HOH A O 1 HETATM 3136 O O . HOH K 6 . ? 6.597 12.044 23.471 1.00 17.23 ? 2346 HOH A O 1 HETATM 3137 O O . HOH K 6 . ? 4.187 10.425 26.259 1.00 37.98 ? 2347 HOH A O 1 HETATM 3138 O O . HOH K 6 . ? -4.242 10.206 30.155 1.00 40.64 ? 2348 HOH A O 1 HETATM 3139 O O . HOH K 6 . ? -0.737 13.186 29.892 1.00 20.92 ? 2349 HOH A O 1 HETATM 3140 O O . HOH K 6 . ? -6.637 13.166 25.952 1.00 39.02 ? 2350 HOH A O 1 HETATM 3141 O O . HOH K 6 . ? -8.025 21.289 29.276 1.00 23.12 ? 2351 HOH A O 1 HETATM 3142 O O . HOH K 6 . ? -7.343 15.346 28.389 1.00 24.97 ? 2352 HOH A O 1 HETATM 3143 O O . HOH K 6 . ? -1.931 20.712 32.513 1.00 19.85 ? 2353 HOH A O 1 HETATM 3144 O O . HOH K 6 . ? 4.615 26.930 35.317 1.00 37.62 ? 2354 HOH A O 1 HETATM 3145 O O . HOH K 6 . ? 2.238 24.436 35.382 1.00 40.52 ? 2355 HOH A O 1 HETATM 3146 O O . HOH K 6 . ? 3.237 30.441 33.817 1.00 17.16 ? 2356 HOH A O 1 HETATM 3147 O O . HOH K 6 . ? 9.063 27.055 33.540 1.00 13.72 ? 2357 HOH A O 1 HETATM 3148 O O . HOH K 6 . ? 8.754 33.481 35.107 1.00 19.69 ? 2358 HOH A O 1 HETATM 3149 O O . HOH K 6 . ? 11.039 28.780 34.085 1.00 27.37 ? 2359 HOH A O 1 HETATM 3150 O O . HOH K 6 . ? 11.035 37.874 34.633 1.00 19.62 ? 2360 HOH A O 1 HETATM 3151 O O . HOH K 6 . ? 17.472 36.631 28.300 1.00 17.52 ? 2361 HOH A O 1 HETATM 3152 O O . HOH K 6 . ? -2.230 16.644 18.907 1.00 17.78 ? 2362 HOH A O 1 HETATM 3153 O O . HOH K 6 . ? -7.701 11.878 12.562 1.00 35.90 ? 2363 HOH A O 1 HETATM 3154 O O . HOH K 6 . ? -11.413 16.956 13.596 1.00 33.41 ? 2364 HOH A O 1 HETATM 3155 O O . HOH K 6 . ? -11.547 13.986 22.897 1.00 30.23 ? 2365 HOH A O 1 HETATM 3156 O O . HOH K 6 . ? -14.533 11.451 20.894 1.00 53.50 ? 2366 HOH A O 1 HETATM 3157 O O . HOH K 6 . ? -13.612 14.537 16.715 1.00 27.67 ? 2367 HOH A O 1 HETATM 3158 O O . HOH K 6 . ? -15.032 24.325 23.694 1.00 21.41 ? 2368 HOH A O 1 HETATM 3159 O O . HOH K 6 . ? -13.525 21.982 27.024 1.00 33.17 ? 2369 HOH A O 1 HETATM 3160 O O . HOH K 6 . ? -12.337 15.518 25.778 1.00 52.02 ? 2370 HOH A O 1 HETATM 3161 O O . HOH K 6 . ? -9.599 18.317 27.051 1.00 22.74 ? 2371 HOH A O 1 HETATM 3162 O O . HOH K 6 . ? -7.658 20.279 26.694 1.00 17.22 ? 2372 HOH A O 1 HETATM 3163 O O . HOH K 6 . ? -6.499 21.415 14.986 1.00 26.28 ? 2373 HOH A O 1 HETATM 3164 O O . HOH K 6 . ? -5.861 23.755 15.753 1.00 21.11 ? 2374 HOH A O 1 HETATM 3165 O O . HOH K 6 . ? -8.252 27.065 30.323 1.00 20.26 ? 2375 HOH A O 1 HETATM 3166 O O . HOH K 6 . ? -12.058 28.567 21.511 1.00 19.99 ? 2376 HOH A O 1 HETATM 3167 O O . HOH K 6 . ? -10.755 32.864 26.600 1.00 21.20 ? 2377 HOH A O 1 HETATM 3168 O O . HOH K 6 . ? -12.376 28.291 26.958 1.00 56.40 ? 2378 HOH A O 1 HETATM 3169 O O . HOH K 6 . ? -5.067 26.632 32.738 1.00 39.54 ? 2379 HOH A O 1 HETATM 3170 O O . HOH K 6 . ? -2.274 39.055 27.447 1.00 41.92 ? 2380 HOH A O 1 HETATM 3171 O O . HOH K 6 . ? -4.666 30.880 33.300 1.00 54.97 ? 2381 HOH A O 1 HETATM 3172 O O . HOH K 6 . ? -1.493 37.823 30.650 1.00 47.30 ? 2382 HOH A O 1 HETATM 3173 O O . HOH K 6 . ? -1.178 36.540 27.910 1.00 24.21 ? 2383 HOH A O 1 HETATM 3174 O O . HOH K 6 . ? -1.975 30.303 33.640 1.00 26.48 ? 2384 HOH A O 1 HETATM 3175 O O . HOH K 6 . ? 4.045 32.979 33.661 1.00 21.81 ? 2385 HOH A O 1 HETATM 3176 O O . HOH K 6 . ? -0.071 34.318 34.640 1.00 26.86 ? 2386 HOH A O 1 HETATM 3177 O O . HOH K 6 . ? 2.900 38.877 28.912 1.00 34.36 ? 2387 HOH A O 1 HETATM 3178 O O . HOH K 6 . ? 1.598 40.488 22.341 1.00 20.65 ? 2388 HOH A O 1 HETATM 3179 O O . HOH K 6 . ? -0.140 25.412 7.935 1.00 7.74 ? 2389 HOH A O 1 HETATM 3180 O O . HOH K 6 . ? -5.353 23.147 5.738 1.00 9.60 ? 2390 HOH A O 1 HETATM 3181 O O . HOH K 6 . ? -13.617 28.715 2.040 1.00 22.98 ? 2391 HOH A O 1 HETATM 3182 O O . HOH K 6 . ? -13.053 31.256 -1.262 1.00 25.00 ? 2392 HOH A O 1 HETATM 3183 O O . HOH K 6 . ? -16.164 31.281 -8.518 1.00 42.15 ? 2393 HOH A O 1 HETATM 3184 O O . HOH K 6 . ? -13.146 24.754 -11.763 1.00 22.38 ? 2394 HOH A O 1 HETATM 3185 O O . HOH K 6 . ? -12.831 17.385 -1.248 1.00 12.93 ? 2395 HOH A O 1 HETATM 3186 O O . HOH K 6 . ? -13.970 21.480 0.031 1.00 30.20 ? 2396 HOH A O 1 HETATM 3187 O O . HOH K 6 . ? -6.575 20.205 -3.407 1.00 18.57 ? 2397 HOH A O 1 HETATM 3188 O O . HOH K 6 . ? -5.760 23.212 -4.829 1.00 41.75 ? 2398 HOH A O 1 HETATM 3189 O O . HOH K 6 . ? -0.842 22.258 -3.552 1.00 43.05 ? 2399 HOH A O 1 HETATM 3190 O O . HOH K 6 . ? -3.210 24.517 -1.230 1.00 15.55 ? 2400 HOH A O 1 HETATM 3191 O O . HOH K 6 . ? -3.955 20.739 -3.150 1.00 43.77 ? 2401 HOH A O 1 HETATM 3192 O O . HOH K 6 . ? -8.651 17.133 5.330 1.00 31.54 ? 2402 HOH A O 1 HETATM 3193 O O . HOH K 6 . ? -6.945 19.022 1.090 1.00 18.04 ? 2403 HOH A O 1 HETATM 3194 O O . HOH K 6 . ? -0.099 19.228 6.913 1.00 22.85 ? 2404 HOH A O 1 HETATM 3195 O O . HOH K 6 . ? 0.101 17.221 10.436 1.00 27.55 ? 2405 HOH A O 1 HETATM 3196 O O . HOH K 6 . ? -8.936 18.443 14.170 1.00 21.81 ? 2406 HOH A O 1 HETATM 3197 O O . HOH K 6 . ? -10.034 20.940 13.271 1.00 28.77 ? 2407 HOH A O 1 HETATM 3198 O O . HOH K 6 . ? -9.986 18.854 9.754 1.00 33.52 ? 2408 HOH A O 1 HETATM 3199 O O . HOH K 6 . ? -10.383 28.719 9.558 1.00 13.04 ? 2409 HOH A O 1 HETATM 3200 O O . HOH K 6 . ? -10.437 18.095 7.097 1.00 32.09 ? 2410 HOH A O 1 HETATM 3201 O O . HOH K 6 . ? -13.020 22.800 10.327 1.00 14.63 ? 2411 HOH A O 1 HETATM 3202 O O . HOH K 6 . ? -18.142 36.295 5.686 1.00 41.08 ? 2412 HOH A O 1 HETATM 3203 O O . HOH K 6 . ? -16.126 35.693 3.078 1.00 29.38 ? 2413 HOH A O 1 HETATM 3204 O O . HOH K 6 . ? -13.607 26.586 3.983 1.00 18.08 ? 2414 HOH A O 1 HETATM 3205 O O . HOH K 6 . ? -17.385 34.929 8.028 1.00 31.78 ? 2415 HOH A O 1 HETATM 3206 O O . HOH K 6 . ? -20.248 30.239 9.457 1.00 34.62 ? 2416 HOH A O 1 HETATM 3207 O O . HOH K 6 . ? -20.391 26.775 7.303 1.00 31.95 ? 2417 HOH A O 1 HETATM 3208 O O . HOH K 6 . ? -20.829 25.149 9.223 1.00 28.32 ? 2418 HOH A O 1 HETATM 3209 O O . HOH K 6 . ? -16.186 22.368 11.694 1.00 16.12 ? 2419 HOH A O 1 HETATM 3210 O O . HOH K 6 . ? -19.122 26.097 16.901 1.00 21.48 ? 2420 HOH A O 1 HETATM 3211 O O . HOH K 6 . ? -22.560 25.178 12.603 1.00 35.45 ? 2421 HOH A O 1 HETATM 3212 O O . HOH K 6 . ? -20.297 33.815 12.110 1.00 36.46 ? 2422 HOH A O 1 HETATM 3213 O O . HOH K 6 . ? -22.068 25.775 15.260 1.00 31.68 ? 2423 HOH A O 1 HETATM 3214 O O . HOH K 6 . ? -21.680 32.951 16.722 1.00 32.61 ? 2424 HOH A O 1 HETATM 3215 O O . HOH K 6 . ? -7.890 31.921 16.472 1.00 13.28 ? 2425 HOH A O 1 HETATM 3216 O O . HOH K 6 . ? -18.462 32.227 22.745 1.00 53.56 ? 2426 HOH A O 1 HETATM 3217 O O . HOH K 6 . ? -12.896 31.810 23.187 1.00 33.67 ? 2427 HOH A O 1 HETATM 3218 O O . HOH K 6 . ? -15.776 34.767 22.999 1.00 28.95 ? 2428 HOH A O 1 HETATM 3219 O O . HOH K 6 . ? -15.459 28.887 21.699 1.00 19.97 ? 2429 HOH A O 1 HETATM 3220 O O . HOH K 6 . ? -20.431 31.808 18.721 1.00 24.50 ? 2430 HOH A O 1 HETATM 3221 O O . HOH K 6 . ? -18.946 27.646 19.123 1.00 24.45 ? 2431 HOH A O 1 HETATM 3222 O O . HOH K 6 . ? -10.577 32.329 23.885 1.00 16.31 ? 2432 HOH A O 1 HETATM 3223 O O . HOH K 6 . ? -9.560 40.608 18.821 1.00 29.35 ? 2433 HOH A O 1 HETATM 3224 O O . HOH K 6 . ? -15.018 38.606 15.112 1.00 52.94 ? 2434 HOH A O 1 HETATM 3225 O O . HOH K 6 . ? -18.374 34.950 19.481 1.00 37.03 ? 2435 HOH A O 1 HETATM 3226 O O . HOH K 6 . ? -13.680 43.466 22.689 1.00 41.84 ? 2436 HOH A O 1 HETATM 3227 O O . HOH K 6 . ? -11.526 44.383 25.594 1.00 75.84 ? 2437 HOH A O 1 HETATM 3228 O O . HOH K 6 . ? 1.123 15.254 12.561 1.00 40.84 ? 2438 HOH A O 1 HETATM 3229 O O . HOH K 6 . ? 2.894 16.752 9.279 1.00 34.68 ? 2439 HOH A O 1 HETATM 3230 O O . HOH K 6 . ? -17.230 21.709 17.019 1.00 31.64 ? 2440 HOH A O 1 HETATM 3231 O O . HOH K 6 . ? -15.167 18.825 15.513 1.00 32.08 ? 2441 HOH A O 1 HETATM 3232 O O . HOH K 6 . ? -17.962 21.261 21.515 1.00 39.77 ? 2442 HOH A O 1 HETATM 3233 O O . HOH K 6 . ? 3.650 15.002 5.772 1.00 29.22 ? 2443 HOH A O 1 HETATM 3234 O O . HOH K 6 . ? 1.753 16.752 14.675 1.00 21.31 ? 2444 HOH A O 1 HETATM 3235 O O . HOH K 6 . ? 5.505 19.437 16.892 1.00 11.74 ? 2445 HOH A O 1 HETATM 3236 O O . HOH K 6 . ? 27.109 11.381 16.738 1.00 52.02 ? 2446 HOH A O 1 HETATM 3237 O O . HOH K 6 . ? 27.388 11.323 9.458 1.00 38.08 ? 2447 HOH A O 1 HETATM 3238 O O . HOH K 6 . ? 23.347 7.148 16.480 1.00 46.55 ? 2448 HOH A O 1 HETATM 3239 O O . HOH K 6 . ? 14.557 54.979 3.012 1.00 14.22 ? 2449 HOH A O 1 HETATM 3240 O O . HOH K 6 . ? 20.363 52.204 8.483 1.00 29.74 ? 2450 HOH A O 1 HETATM 3241 O O . HOH K 6 . ? 17.175 53.818 6.759 1.00 29.60 ? 2451 HOH A O 1 HETATM 3242 O O . HOH K 6 . ? 19.396 53.281 2.733 1.00 20.41 ? 2452 HOH A O 1 HETATM 3243 O O . HOH K 6 . ? 18.610 49.364 1.403 1.00 17.44 ? 2453 HOH A O 1 HETATM 3244 O O . HOH K 6 . ? -5.546 9.694 32.658 1.00 50.72 ? 2454 HOH A O 1 HETATM 3245 O O . HOH K 6 . ? -21.466 36.386 8.702 1.00 28.65 ? 2455 HOH A O 1 HETATM 3246 O O . HOH K 6 . ? -21.427 31.864 0.400 1.00 28.68 ? 2456 HOH A O 1 HETATM 3247 O O . HOH K 6 . ? -19.784 38.245 2.983 1.00 46.55 ? 2457 HOH A O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ALA 1 1 1 ALA ALA A . n A 1 2 SER 2 2 2 SER SER A . n A 1 3 SER 3 3 3 SER SER A . n A 1 4 PHE 4 4 4 PHE PHE A . n A 1 5 VAL 5 5 5 VAL VAL A . n A 1 6 THR 6 6 6 THR THR A . n A 1 7 ILE 7 7 7 ILE ILE A . n A 1 8 SER 8 8 8 SER SER A . n A 1 9 GLY 9 9 9 GLY GLY A . n A 1 10 THR 10 10 10 THR THR A . n A 1 11 GLN 11 11 11 GLN GLN A . n A 1 12 PHE 12 12 12 PHE PHE A . n A 1 13 ASN 13 13 13 ASN ASN A . n A 1 14 ILE 14 14 14 ILE ILE A . n A 1 15 ASP 15 15 15 ASP ASP A . n A 1 16 GLY 16 16 16 GLY GLY A . n A 1 17 LYS 17 17 17 LYS LYS A . n A 1 18 VAL 18 18 18 VAL VAL A . n A 1 19 GLY 19 19 19 GLY GLY A . n A 1 20 TYR 20 20 20 TYR TYR A . n A 1 21 PHE 21 21 21 PHE PHE A . n A 1 22 ALA 22 22 22 ALA ALA A . n A 1 23 GLY 23 23 23 GLY GLY A . n A 1 24 THR 24 24 24 THR THR A . n A 1 25 ASN 25 25 25 ASN ASN A . n A 1 26 CYS 26 26 26 CYS CYS A . n A 1 27 TYR 27 27 27 TYR TYR A . n A 1 28 TRP 28 28 28 TRP TRP A . n A 1 29 CYS 29 29 29 CYS CYS A . n A 1 30 SER 30 30 30 SER SER A . n A 1 31 PHE 31 31 31 PHE PHE A . n A 1 32 LEU 32 32 32 LEU LEU A . n A 1 33 THR 33 33 33 THR THR A . n A 1 34 ASN 34 34 34 ASN ASN A . n A 1 35 HIS 35 35 35 HIS HIS A . n A 1 36 ALA 36 36 36 ALA ALA A . n A 1 37 ASP 37 37 37 ASP ASP A . n A 1 38 VAL 38 38 38 VAL VAL A . n A 1 39 ASP 39 39 39 ASP ASP A . n A 1 40 SER 40 40 40 SER SER A . n A 1 41 THR 41 41 41 THR THR A . n A 1 42 PHE 42 42 42 PHE PHE A . n A 1 43 SER 43 43 43 SER SER A . n A 1 44 HIS 44 44 44 HIS HIS A . n A 1 45 ILE 45 45 45 ILE ILE A . n A 1 46 SER 46 46 46 SER SER A . n A 1 47 SER 47 47 47 SER SER A . n A 1 48 SER 48 48 48 SER SER A . n A 1 49 GLY 49 49 49 GLY GLY A . n A 1 50 LEU 50 50 50 LEU LEU A . n A 1 51 LYS 51 51 51 LYS LYS A . n A 1 52 VAL 52 52 52 VAL VAL A . n A 1 53 VAL 53 53 53 VAL VAL A . n A 1 54 ARG 54 54 54 ARG ARG A . n A 1 55 VAL 55 55 55 VAL VAL A . n A 1 56 TRP 56 56 56 TRP TRP A . n A 1 57 GLY 57 57 57 GLY GLY A . n A 1 58 PHE 58 58 58 PHE PHE A . n A 1 59 ASN 59 59 59 ASN ASN A . n A 1 60 ASP 60 60 60 ASP ASP A . n A 1 61 VAL 61 61 61 VAL VAL A . n A 1 62 ASN 62 62 62 ASN ASN A . n A 1 63 THR 63 63 63 THR THR A . n A 1 64 GLN 64 64 64 GLN GLN A . n A 1 65 PRO 65 65 65 PRO PRO A . n A 1 66 SER 66 66 66 SER SER A . n A 1 67 PRO 67 67 67 PRO PRO A . n A 1 68 GLY 68 68 68 GLY GLY A . n A 1 69 GLN 69 69 69 GLN GLN A . n A 1 70 ILE 70 70 70 ILE ILE A . n A 1 71 TRP 71 71 71 TRP TRP A . n A 1 72 PHE 72 72 72 PHE PHE A . n A 1 73 GLN 73 73 73 GLN GLN A . n A 1 74 LYS 74 74 74 LYS LYS A . n A 1 75 LEU 75 75 75 LEU LEU A . n A 1 76 SER 76 76 76 SER SER A . n A 1 77 ALA 77 77 77 ALA ALA A . n A 1 78 THR 78 78 78 THR THR A . n A 1 79 GLY 79 79 79 GLY GLY A . n A 1 80 SER 80 80 80 SER SER A . n A 1 81 THR 81 81 81 THR THR A . n A 1 82 ILE 82 82 82 ILE ILE A . n A 1 83 ASN 83 83 83 ASN ASN A . n A 1 84 THR 84 84 84 THR THR A . n A 1 85 GLY 85 85 85 GLY GLY A . n A 1 86 ALA 86 86 86 ALA ALA A . n A 1 87 ASP 87 87 87 ASP ASP A . n A 1 88 GLY 88 88 88 GLY GLY A . n A 1 89 LEU 89 89 89 LEU LEU A . n A 1 90 GLN 90 90 90 GLN GLN A . n A 1 91 THR 91 91 91 THR THR A . n A 1 92 LEU 92 92 92 LEU LEU A . n A 1 93 ASP 93 93 93 ASP ASP A . n A 1 94 TYR 94 94 94 TYR TYR A . n A 1 95 VAL 95 95 95 VAL VAL A . n A 1 96 VAL 96 96 96 VAL VAL A . n A 1 97 GLN 97 97 97 GLN GLN A . n A 1 98 SER 98 98 98 SER SER A . n A 1 99 ALA 99 99 99 ALA ALA A . n A 1 100 GLU 100 100 100 GLU GLU A . n A 1 101 GLN 101 101 101 GLN GLN A . n A 1 102 HIS 102 102 102 HIS HIS A . n A 1 103 ASN 103 103 103 ASN ASN A . n A 1 104 LEU 104 104 104 LEU LEU A . n A 1 105 LYS 105 105 105 LYS LYS A . n A 1 106 LEU 106 106 106 LEU LEU A . n A 1 107 ILE 107 107 107 ILE ILE A . n A 1 108 ILE 108 108 108 ILE ILE A . n A 1 109 PRO 109 109 109 PRO PRO A . n A 1 110 PHE 110 110 110 PHE PHE A . n A 1 111 VAL 111 111 111 VAL VAL A . n A 1 112 ASN 112 112 112 ASN ASN A . n A 1 113 ASN 113 113 113 ASN ASN A . n A 1 114 TRP 114 114 114 TRP TRP A . n A 1 115 SER 115 115 115 SER SER A . n A 1 116 ASP 116 116 116 ASP ASP A . n A 1 117 TYR 117 117 117 TYR TYR A . n A 1 118 GLY 118 118 118 GLY GLY A . n A 1 119 GLY 119 119 119 GLY GLY A . n A 1 120 ILE 120 120 120 ILE ILE A . n A 1 121 ASN 121 121 121 ASN ASN A . n A 1 122 ALA 122 122 122 ALA ALA A . n A 1 123 TYR 123 123 123 TYR TYR A . n A 1 124 VAL 124 124 124 VAL VAL A . n A 1 125 ASN 125 125 125 ASN ASN A . n A 1 126 ALA 126 126 126 ALA ALA A . n A 1 127 PHE 127 127 127 PHE PHE A . n A 1 128 GLY 128 128 128 GLY GLY A . n A 1 129 GLY 129 129 129 GLY GLY A . n A 1 130 ASN 130 130 130 ASN ASN A . n A 1 131 ALA 131 131 131 ALA ALA A . n A 1 132 THR 132 132 132 THR THR A . n A 1 133 THR 133 133 133 THR THR A . n A 1 134 TRP 134 134 134 TRP TRP A . n A 1 135 TYR 135 135 135 TYR TYR A . n A 1 136 THR 136 136 136 THR THR A . n A 1 137 ASN 137 137 137 ASN ASN A . n A 1 138 THR 138 138 138 THR THR A . n A 1 139 ALA 139 139 139 ALA ALA A . n A 1 140 ALA 140 140 140 ALA ALA A . n A 1 141 GLN 141 141 141 GLN GLN A . n A 1 142 THR 142 142 142 THR THR A . n A 1 143 GLN 143 143 143 GLN GLN A . n A 1 144 TYR 144 144 144 TYR TYR A . n A 1 145 ARG 145 145 145 ARG ARG A . n A 1 146 LYS 146 146 146 LYS LYS A . n A 1 147 TYR 147 147 147 TYR TYR A . n A 1 148 VAL 148 148 148 VAL VAL A . n A 1 149 GLN 149 149 149 GLN GLN A . n A 1 150 ALA 150 150 150 ALA ALA A . n A 1 151 VAL 151 151 151 VAL VAL A . n A 1 152 VAL 152 152 152 VAL VAL A . n A 1 153 SER 153 153 153 SER SER A . n A 1 154 ARG 154 154 154 ARG ARG A . n A 1 155 TYR 155 155 155 TYR TYR A . n A 1 156 ALA 156 156 156 ALA ALA A . n A 1 157 ASN 157 157 157 ASN ASN A . n A 1 158 SER 158 158 158 SER SER A . n A 1 159 THR 159 159 159 THR THR A . n A 1 160 ALA 160 160 160 ALA ALA A . n A 1 161 ILE 161 161 161 ILE ILE A . n A 1 162 PHE 162 162 162 PHE PHE A . n A 1 163 ALA 163 163 163 ALA ALA A . n A 1 164 TRP 164 164 164 TRP TRP A . n A 1 165 GLU 165 165 165 GLU GLU A . n A 1 166 LEU 166 166 166 LEU LEU A . n A 1 167 GLY 167 167 167 GLY GLY A . n A 1 168 ASN 168 168 168 ASN ASN A . n A 1 169 GLU 169 169 169 GLU GLU A . n A 1 170 PRO 170 170 170 PRO PRO A . n A 1 171 ARG 171 171 171 ARG ARG A . n A 1 172 CYS 172 172 172 CYS CYS A . n A 1 173 ASN 173 173 173 ASN ASN A . n A 1 174 GLY 174 174 174 GLY GLY A . n A 1 175 CYS 175 175 175 CYS CYS A . n A 1 176 SER 176 176 176 SER SER A . n A 1 177 THR 177 177 177 THR THR A . n A 1 178 ASP 178 178 178 ASP ASP A . n A 1 179 VAL 179 179 179 VAL VAL A . n A 1 180 ILE 180 180 180 ILE ILE A . n A 1 181 VAL 181 181 181 VAL VAL A . n A 1 182 GLN 182 182 182 GLN GLN A . n A 1 183 TRP 183 183 183 TRP TRP A . n A 1 184 ALA 184 184 184 ALA ALA A . n A 1 185 THR 185 185 185 THR THR A . n A 1 186 SER 186 186 186 SER SER A . n A 1 187 VAL 187 187 187 VAL VAL A . n A 1 188 SER 188 188 188 SER SER A . n A 1 189 GLN 189 189 189 GLN GLN A . n A 1 190 TYR 190 190 190 TYR TYR A . n A 1 191 VAL 191 191 191 VAL VAL A . n A 1 192 LYS 192 192 192 LYS LYS A . n A 1 193 SER 193 193 193 SER SER A . n A 1 194 LEU 194 194 194 LEU LEU A . n A 1 195 ASP 195 195 195 ASP ASP A . n A 1 196 SER 196 196 196 SER SER A . n A 1 197 ASN 197 197 197 ASN ASN A . n A 1 198 HIS 198 198 198 HIS HIS A . n A 1 199 LEU 199 199 199 LEU LEU A . n A 1 200 VAL 200 200 200 VAL VAL A . n A 1 201 THR 201 201 201 THR THR A . n A 1 202 LEU 202 202 202 LEU LEU A . n A 1 203 GLY 203 203 203 GLY GLY A . n A 1 204 ASP 204 204 204 ASP ASP A . n A 1 205 GLU 205 205 205 GLU GLU A . n A 1 206 GLY 206 206 206 GLY GLY A . n A 1 207 LEU 207 207 207 LEU LEU A . n A 1 208 GLY 208 208 208 GLY GLY A . n A 1 209 LEU 209 209 209 LEU LEU A . n A 1 210 SER 210 210 210 SER SER A . n A 1 211 THR 211 211 211 THR THR A . n A 1 212 GLY 212 212 212 GLY GLY A . n A 1 213 ASP 213 213 213 ASP ASP A . n A 1 214 GLY 214 214 214 GLY GLY A . n A 1 215 ALA 215 215 215 ALA ALA A . n A 1 216 TYR 216 216 216 TYR TYR A . n A 1 217 PRO 217 217 217 PRO PRO A . n A 1 218 TYR 218 218 218 TYR TYR A . n A 1 219 THR 219 219 219 THR THR A . n A 1 220 TYR 220 220 220 TYR TYR A . n A 1 221 GLY 221 221 221 GLY GLY A . n A 1 222 GLU 222 222 222 GLU GLU A . n A 1 223 GLY 223 223 223 GLY GLY A . n A 1 224 THR 224 224 224 THR THR A . n A 1 225 ASP 225 225 225 ASP ASP A . n A 1 226 PHE 226 226 226 PHE PHE A . n A 1 227 ALA 227 227 227 ALA ALA A . n A 1 228 LYS 228 228 228 LYS LYS A . n A 1 229 ASN 229 229 229 ASN ASN A . n A 1 230 VAL 230 230 230 VAL VAL A . n A 1 231 GLN 231 231 231 GLN GLN A . n A 1 232 ILE 232 232 232 ILE ILE A . n A 1 233 LYS 233 233 233 LYS LYS A . n A 1 234 SER 234 234 234 SER SER A . n A 1 235 LEU 235 235 235 LEU LEU A . n A 1 236 ASP 236 236 236 ASP ASP A . n A 1 237 PHE 237 237 237 PHE PHE A . n A 1 238 GLY 238 238 238 GLY GLY A . n A 1 239 THR 239 239 239 THR THR A . n A 1 240 PHE 240 240 240 PHE PHE A . n A 1 241 HIS 241 241 241 HIS HIS A . n A 1 242 LEU 242 242 242 LEU LEU A . n A 1 243 TYR 243 243 243 TYR TYR A . n A 1 244 PRO 244 244 244 PRO PRO A . n A 1 245 ASP 245 245 245 ASP ASP A . n A 1 246 SER 246 246 246 SER SER A . n A 1 247 TRP 247 247 247 TRP TRP A . n A 1 248 GLY 248 248 248 GLY GLY A . n A 1 249 THR 249 249 249 THR THR A . n A 1 250 ASN 250 250 250 ASN ASN A . n A 1 251 TYR 251 251 251 TYR TYR A . n A 1 252 THR 252 252 252 THR THR A . n A 1 253 TRP 253 253 253 TRP TRP A . n A 1 254 GLY 254 254 254 GLY GLY A . n A 1 255 ASN 255 255 255 ASN ASN A . n A 1 256 GLY 256 256 256 GLY GLY A . n A 1 257 TRP 257 257 257 TRP TRP A . n A 1 258 ILE 258 258 258 ILE ILE A . n A 1 259 GLN 259 259 259 GLN GLN A . n A 1 260 THR 260 260 260 THR THR A . n A 1 261 HIS 261 261 261 HIS HIS A . n A 1 262 ALA 262 262 262 ALA ALA A . n A 1 263 ALA 263 263 263 ALA ALA A . n A 1 264 ALA 264 264 264 ALA ALA A . n A 1 265 CYS 265 265 265 CYS CYS A . n A 1 266 LEU 266 266 266 LEU LEU A . n A 1 267 ALA 267 267 267 ALA ALA A . n A 1 268 ALA 268 268 268 ALA ALA A . n A 1 269 GLY 269 269 269 GLY GLY A . n A 1 270 LYS 270 270 270 LYS LYS A . n A 1 271 PRO 271 271 271 PRO PRO A . n A 1 272 CYS 272 272 272 CYS CYS A . n A 1 273 VAL 273 273 273 VAL VAL A . n A 1 274 PHE 274 274 274 PHE PHE A . n A 1 275 GLU 275 275 275 GLU GLU A . n A 1 276 GLU 276 276 276 GLU GLU A . n A 1 277 TYR 277 277 277 TYR TYR A . n A 1 278 GLY 278 278 278 GLY GLY A . n A 1 279 ALA 279 279 279 ALA ALA A . n A 1 280 GLN 280 280 280 GLN GLN A . n A 1 281 GLN 281 281 281 GLN GLN A . n A 1 282 ASN 282 282 282 ASN ASN A . n A 1 283 PRO 283 283 283 PRO PRO A . n A 1 284 CYS 284 284 284 CYS CYS A . n A 1 285 THR 285 285 285 THR THR A . n A 1 286 ASN 286 286 286 ASN ASN A . n A 1 287 GLU 287 287 287 GLU GLU A . n A 1 288 ALA 288 288 288 ALA ALA A . n A 1 289 PRO 289 289 289 PRO PRO A . n A 1 290 TRP 290 290 290 TRP TRP A . n A 1 291 GLN 291 291 291 GLN GLN A . n A 1 292 THR 292 292 292 THR THR A . n A 1 293 THR 293 293 293 THR THR A . n A 1 294 SER 294 294 294 SER SER A . n A 1 295 LEU 295 295 295 LEU LEU A . n A 1 296 THR 296 296 296 THR THR A . n A 1 297 THR 297 297 297 THR THR A . n A 1 298 ARG 298 298 298 ARG ARG A . n A 1 299 GLY 299 299 299 GLY GLY A . n A 1 300 MET 300 300 300 MET MET A . n A 1 301 GLY 301 301 301 GLY GLY A . n A 1 302 GLY 302 302 302 GLY GLY A . n A 1 303 ASP 303 303 303 ASP ASP A . n A 1 304 MET 304 304 304 MET MET A . n A 1 305 PHE 305 305 305 PHE PHE A . n A 1 306 TRP 306 306 306 TRP TRP A . n A 1 307 GLN 307 307 307 GLN GLN A . n A 1 308 TRP 308 308 308 TRP TRP A . n A 1 309 GLY 309 309 309 GLY GLY A . n A 1 310 ASP 310 310 310 ASP ASP A . n A 1 311 THR 311 311 311 THR THR A . n A 1 312 PHE 312 312 312 PHE PHE A . n A 1 313 ALA 313 313 313 ALA ALA A . n A 1 314 ASN 314 314 314 ASN ASN A . n A 1 315 GLY 315 315 315 GLY GLY A . n A 1 316 ALA 316 316 316 ALA ALA A . n A 1 317 GLN 317 317 317 GLN GLN A . n A 1 318 SER 318 318 318 SER SER A . n A 1 319 ASN 319 319 319 ASN ASN A . n A 1 320 SER 320 320 320 SER SER A . n A 1 321 ASP 321 321 321 ASP ASP A . n A 1 322 PRO 322 322 322 PRO PRO A . n A 1 323 TYR 323 323 323 TYR TYR A . n A 1 324 THR 324 324 324 THR THR A . n A 1 325 VAL 325 325 325 VAL VAL A . n A 1 326 TRP 326 326 326 TRP TRP A . n A 1 327 TYR 327 327 327 TYR TYR A . n A 1 328 ASN 328 328 328 ASN ASN A . n A 1 329 SER 329 329 329 SER SER A . n A 1 330 SER 330 330 330 SER SER A . n A 1 331 ASN 331 331 331 ASN ASN A . n A 1 332 TRP 332 332 332 TRP TRP A . n A 1 333 GLN 333 333 333 GLN GLN A . n A 1 334 CYS 334 334 334 CYS CYS A . n A 1 335 LEU 335 335 335 LEU LEU A . n A 1 336 VAL 336 336 336 VAL VAL A . n A 1 337 LYS 337 337 337 LYS LYS A . n A 1 338 ASN 338 338 338 ASN ASN A . n A 1 339 HIS 339 339 339 HIS HIS A . n A 1 340 VAL 340 340 340 VAL VAL A . n A 1 341 ASP 341 341 341 ASP ASP A . n A 1 342 ALA 342 342 342 ALA ALA A . n A 1 343 ILE 343 343 343 ILE ILE A . n A 1 344 ASN 344 344 344 ASN ASN 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 TRS 1 401 401 TRS TRS A . C 3 SO4 1 402 402 SO4 SO4 A . D 4 GOL 1 410 410 GOL GOL A . E 4 GOL 1 411 411 GOL GOL A . F 4 GOL 1 412 412 GOL GOL A . G 5 NAG 1 430 430 NAG NAG A . H 5 NAG 1 431 431 NAG NAG A . I 5 NAG 1 432 432 NAG NAG A . J 5 NAG 1 433 433 NAG NAG A . K 6 HOH 1 2001 2001 HOH HOH A . K 6 HOH 2 2002 2002 HOH HOH A . K 6 HOH 3 2003 2003 HOH HOH A . K 6 HOH 4 2004 2004 HOH HOH A . K 6 HOH 5 2005 2005 HOH HOH A . K 6 HOH 6 2006 2006 HOH HOH A . K 6 HOH 7 2007 2007 HOH HOH A . K 6 HOH 8 2008 2008 HOH HOH A . K 6 HOH 9 2009 2009 HOH HOH A . K 6 HOH 10 2010 2010 HOH HOH A . K 6 HOH 11 2011 2011 HOH HOH A . K 6 HOH 12 2012 2012 HOH HOH A . K 6 HOH 13 2013 2013 HOH HOH A . K 6 HOH 14 2014 2014 HOH HOH A . K 6 HOH 15 2015 2015 HOH HOH A . K 6 HOH 16 2016 2016 HOH HOH A . K 6 HOH 17 2017 2017 HOH HOH A . K 6 HOH 18 2018 2018 HOH HOH A . K 6 HOH 19 2019 2019 HOH HOH A . K 6 HOH 20 2020 2020 HOH HOH A . K 6 HOH 21 2021 2021 HOH HOH A . K 6 HOH 22 2022 2022 HOH HOH A . K 6 HOH 23 2023 2023 HOH HOH A . K 6 HOH 24 2024 2024 HOH HOH A . K 6 HOH 25 2025 2025 HOH HOH A . K 6 HOH 26 2026 2026 HOH HOH A . K 6 HOH 27 2027 2027 HOH HOH A . K 6 HOH 28 2028 2028 HOH HOH A . K 6 HOH 29 2029 2029 HOH HOH A . K 6 HOH 30 2030 2030 HOH HOH A . K 6 HOH 31 2031 2031 HOH HOH A . K 6 HOH 32 2032 2032 HOH HOH A . K 6 HOH 33 2033 2033 HOH HOH A . K 6 HOH 34 2034 2034 HOH HOH A . K 6 HOH 35 2035 2035 HOH HOH A . K 6 HOH 36 2036 2036 HOH HOH A . K 6 HOH 37 2037 2037 HOH HOH A . K 6 HOH 38 2038 2038 HOH HOH A . K 6 HOH 39 2039 2039 HOH HOH A . K 6 HOH 40 2040 2040 HOH HOH A . K 6 HOH 41 2041 2041 HOH HOH A . K 6 HOH 42 2042 2042 HOH HOH A . K 6 HOH 43 2043 2043 HOH HOH A . K 6 HOH 44 2044 2044 HOH HOH A . K 6 HOH 45 2045 2045 HOH HOH A . K 6 HOH 46 2046 2046 HOH HOH A . K 6 HOH 47 2047 2047 HOH HOH A . K 6 HOH 48 2048 2048 HOH HOH A . K 6 HOH 49 2049 2049 HOH HOH A . K 6 HOH 50 2050 2050 HOH HOH A . K 6 HOH 51 2051 2051 HOH HOH A . K 6 HOH 52 2052 2052 HOH HOH A . K 6 HOH 53 2053 2053 HOH HOH A . K 6 HOH 54 2054 2054 HOH HOH A . K 6 HOH 55 2055 2055 HOH HOH A . K 6 HOH 56 2056 2056 HOH HOH A . K 6 HOH 57 2057 2057 HOH HOH A . K 6 HOH 58 2058 2058 HOH HOH A . K 6 HOH 59 2059 2059 HOH HOH A . K 6 HOH 60 2060 2060 HOH HOH A . K 6 HOH 61 2061 2061 HOH HOH A . K 6 HOH 62 2062 2062 HOH HOH A . K 6 HOH 63 2063 2063 HOH HOH A . K 6 HOH 64 2064 2064 HOH HOH A . K 6 HOH 65 2065 2065 HOH HOH A . K 6 HOH 66 2066 2066 HOH HOH A . K 6 HOH 67 2067 2067 HOH HOH A . K 6 HOH 68 2068 2068 HOH HOH A . K 6 HOH 69 2069 2069 HOH HOH A . K 6 HOH 70 2070 2070 HOH HOH A . K 6 HOH 71 2071 2071 HOH HOH A . K 6 HOH 72 2072 2072 HOH HOH A . K 6 HOH 73 2073 2073 HOH HOH A . K 6 HOH 74 2074 2074 HOH HOH A . K 6 HOH 75 2075 2075 HOH HOH A . K 6 HOH 76 2076 2076 HOH HOH A . K 6 HOH 77 2077 2077 HOH HOH A . K 6 HOH 78 2078 2078 HOH HOH A . K 6 HOH 79 2079 2079 HOH HOH A . K 6 HOH 80 2080 2080 HOH HOH A . K 6 HOH 81 2081 2081 HOH HOH A . K 6 HOH 82 2082 2082 HOH HOH A . K 6 HOH 83 2083 2083 HOH HOH A . K 6 HOH 84 2084 2084 HOH HOH A . K 6 HOH 85 2085 2085 HOH HOH A . K 6 HOH 86 2086 2086 HOH HOH A . K 6 HOH 87 2087 2087 HOH HOH A . K 6 HOH 88 2088 2088 HOH HOH A . K 6 HOH 89 2089 2089 HOH HOH A . K 6 HOH 90 2090 2090 HOH HOH A . K 6 HOH 91 2091 2091 HOH HOH A . K 6 HOH 92 2092 2092 HOH HOH A . K 6 HOH 93 2093 2093 HOH HOH A . K 6 HOH 94 2094 2094 HOH HOH A . K 6 HOH 95 2095 2095 HOH HOH A . K 6 HOH 96 2096 2096 HOH HOH A . K 6 HOH 97 2097 2097 HOH HOH A . K 6 HOH 98 2098 2098 HOH HOH A . K 6 HOH 99 2099 2099 HOH HOH A . K 6 HOH 100 2100 2100 HOH HOH A . K 6 HOH 101 2101 2101 HOH HOH A . K 6 HOH 102 2102 2102 HOH HOH A . K 6 HOH 103 2103 2103 HOH HOH A . K 6 HOH 104 2104 2104 HOH HOH A . K 6 HOH 105 2105 2105 HOH HOH A . K 6 HOH 106 2106 2106 HOH HOH A . K 6 HOH 107 2107 2107 HOH HOH A . K 6 HOH 108 2108 2108 HOH HOH A . K 6 HOH 109 2109 2109 HOH HOH A . K 6 HOH 110 2110 2110 HOH HOH A . K 6 HOH 111 2111 2111 HOH HOH A . K 6 HOH 112 2112 2112 HOH HOH A . K 6 HOH 113 2113 2113 HOH HOH A . K 6 HOH 114 2114 2114 HOH HOH A . K 6 HOH 115 2115 2115 HOH HOH A . K 6 HOH 116 2116 2116 HOH HOH A . K 6 HOH 117 2117 2117 HOH HOH A . K 6 HOH 118 2118 2118 HOH HOH A . K 6 HOH 119 2119 2119 HOH HOH A . K 6 HOH 120 2120 2120 HOH HOH A . K 6 HOH 121 2121 2121 HOH HOH A . K 6 HOH 122 2122 2122 HOH HOH A . K 6 HOH 123 2123 2123 HOH HOH A . K 6 HOH 124 2124 2124 HOH HOH A . K 6 HOH 125 2125 2125 HOH HOH A . K 6 HOH 126 2126 2126 HOH HOH A . K 6 HOH 127 2127 2127 HOH HOH A . K 6 HOH 128 2128 2128 HOH HOH A . K 6 HOH 129 2129 2129 HOH HOH A . K 6 HOH 130 2130 2130 HOH HOH A . K 6 HOH 131 2131 2131 HOH HOH A . K 6 HOH 132 2132 2132 HOH HOH A . K 6 HOH 133 2133 2133 HOH HOH A . K 6 HOH 134 2134 2134 HOH HOH A . K 6 HOH 135 2135 2135 HOH HOH A . K 6 HOH 136 2136 2136 HOH HOH A . K 6 HOH 137 2137 2137 HOH HOH A . K 6 HOH 138 2138 2138 HOH HOH A . K 6 HOH 139 2139 2139 HOH HOH A . K 6 HOH 140 2140 2140 HOH HOH A . K 6 HOH 141 2141 2141 HOH HOH A . K 6 HOH 142 2142 2142 HOH HOH A . K 6 HOH 143 2143 2143 HOH HOH A . K 6 HOH 144 2144 2144 HOH HOH A . K 6 HOH 145 2145 2145 HOH HOH A . K 6 HOH 146 2146 2146 HOH HOH A . K 6 HOH 147 2147 2147 HOH HOH A . K 6 HOH 148 2148 2148 HOH HOH A . K 6 HOH 149 2149 2149 HOH HOH A . K 6 HOH 150 2150 2150 HOH HOH A . K 6 HOH 151 2151 2151 HOH HOH A . K 6 HOH 152 2152 2152 HOH HOH A . K 6 HOH 153 2153 2153 HOH HOH A . K 6 HOH 154 2154 2154 HOH HOH A . K 6 HOH 155 2155 2155 HOH HOH A . K 6 HOH 156 2156 2156 HOH HOH A . K 6 HOH 157 2157 2157 HOH HOH A . K 6 HOH 158 2158 2158 HOH HOH A . K 6 HOH 159 2159 2159 HOH HOH A . K 6 HOH 160 2160 2160 HOH HOH A . K 6 HOH 161 2161 2161 HOH HOH A . K 6 HOH 162 2162 2162 HOH HOH A . K 6 HOH 163 2163 2163 HOH HOH A . K 6 HOH 164 2164 2164 HOH HOH A . K 6 HOH 165 2165 2165 HOH HOH A . K 6 HOH 166 2166 2166 HOH HOH A . K 6 HOH 167 2167 2167 HOH HOH A . K 6 HOH 168 2168 2168 HOH HOH A . K 6 HOH 169 2169 2169 HOH HOH A . K 6 HOH 170 2170 2170 HOH HOH A . K 6 HOH 171 2171 2171 HOH HOH A . K 6 HOH 172 2172 2172 HOH HOH A . K 6 HOH 173 2173 2173 HOH HOH A . K 6 HOH 174 2174 2174 HOH HOH A . K 6 HOH 175 2175 2175 HOH HOH A . K 6 HOH 176 2176 2176 HOH HOH A . K 6 HOH 177 2177 2177 HOH HOH A . K 6 HOH 178 2178 2178 HOH HOH A . K 6 HOH 179 2179 2179 HOH HOH A . K 6 HOH 180 2180 2180 HOH HOH A . K 6 HOH 181 2181 2181 HOH HOH A . K 6 HOH 182 2182 2182 HOH HOH A . K 6 HOH 183 2183 2183 HOH HOH A . K 6 HOH 184 2184 2184 HOH HOH A . K 6 HOH 185 2185 2185 HOH HOH A . K 6 HOH 186 2186 2186 HOH HOH A . K 6 HOH 187 2187 2187 HOH HOH A . K 6 HOH 188 2188 2188 HOH HOH A . K 6 HOH 189 2189 2189 HOH HOH A . K 6 HOH 190 2190 2190 HOH HOH A . K 6 HOH 191 2191 2191 HOH HOH A . K 6 HOH 192 2192 2192 HOH HOH A . K 6 HOH 193 2193 2193 HOH HOH A . K 6 HOH 194 2194 2194 HOH HOH A . K 6 HOH 195 2195 2195 HOH HOH A . K 6 HOH 196 2196 2196 HOH HOH A . K 6 HOH 197 2197 2197 HOH HOH A . K 6 HOH 198 2198 2198 HOH HOH A . K 6 HOH 199 2199 2199 HOH HOH A . K 6 HOH 200 2200 2200 HOH HOH A . K 6 HOH 201 2201 2201 HOH HOH A . K 6 HOH 202 2202 2202 HOH HOH A . K 6 HOH 203 2203 2203 HOH HOH A . K 6 HOH 204 2204 2204 HOH HOH A . K 6 HOH 205 2205 2205 HOH HOH A . K 6 HOH 206 2206 2206 HOH HOH A . K 6 HOH 207 2207 2207 HOH HOH A . K 6 HOH 208 2208 2208 HOH HOH A . K 6 HOH 209 2209 2209 HOH HOH A . K 6 HOH 210 2210 2210 HOH HOH A . K 6 HOH 211 2211 2211 HOH HOH A . K 6 HOH 212 2212 2212 HOH HOH A . K 6 HOH 213 2213 2213 HOH HOH A . K 6 HOH 214 2214 2214 HOH HOH A . K 6 HOH 215 2215 2215 HOH HOH A . K 6 HOH 216 2216 2216 HOH HOH A . K 6 HOH 217 2217 2217 HOH HOH A . K 6 HOH 218 2218 2218 HOH HOH A . K 6 HOH 219 2219 2219 HOH HOH A . K 6 HOH 220 2220 2220 HOH HOH A . K 6 HOH 221 2221 2221 HOH HOH A . K 6 HOH 222 2222 2222 HOH HOH A . K 6 HOH 223 2223 2223 HOH HOH A . K 6 HOH 224 2224 2224 HOH HOH A . K 6 HOH 225 2225 2225 HOH HOH A . K 6 HOH 226 2226 2226 HOH HOH A . K 6 HOH 227 2227 2227 HOH HOH A . K 6 HOH 228 2228 2228 HOH HOH A . K 6 HOH 229 2229 2229 HOH HOH A . K 6 HOH 230 2230 2230 HOH HOH A . K 6 HOH 231 2231 2231 HOH HOH A . K 6 HOH 232 2232 2232 HOH HOH A . K 6 HOH 233 2233 2233 HOH HOH A . K 6 HOH 234 2234 2234 HOH HOH A . K 6 HOH 235 2235 2235 HOH HOH A . K 6 HOH 236 2236 2236 HOH HOH A . K 6 HOH 237 2237 2237 HOH HOH A . K 6 HOH 238 2238 2238 HOH HOH A . K 6 HOH 239 2239 2239 HOH HOH A . K 6 HOH 240 2240 2240 HOH HOH A . K 6 HOH 241 2241 2241 HOH HOH A . K 6 HOH 242 2242 2242 HOH HOH A . K 6 HOH 243 2243 2243 HOH HOH A . K 6 HOH 244 2244 2244 HOH HOH A . K 6 HOH 245 2245 2245 HOH HOH A . K 6 HOH 246 2246 2246 HOH HOH A . K 6 HOH 247 2247 2247 HOH HOH A . K 6 HOH 248 2248 2248 HOH HOH A . K 6 HOH 249 2249 2249 HOH HOH A . K 6 HOH 250 2250 2250 HOH HOH A . K 6 HOH 251 2251 2251 HOH HOH A . K 6 HOH 252 2252 2252 HOH HOH A . K 6 HOH 253 2253 2253 HOH HOH A . K 6 HOH 254 2254 2254 HOH HOH A . K 6 HOH 255 2255 2255 HOH HOH A . K 6 HOH 256 2256 2256 HOH HOH A . K 6 HOH 257 2257 2257 HOH HOH A . K 6 HOH 258 2258 2258 HOH HOH A . K 6 HOH 259 2259 2259 HOH HOH A . K 6 HOH 260 2260 2260 HOH HOH A . K 6 HOH 261 2261 2261 HOH HOH A . K 6 HOH 262 2262 2262 HOH HOH A . K 6 HOH 263 2263 2263 HOH HOH A . K 6 HOH 264 2264 2264 HOH HOH A . K 6 HOH 265 2265 2265 HOH HOH A . K 6 HOH 266 2266 2266 HOH HOH A . K 6 HOH 267 2267 2267 HOH HOH A . K 6 HOH 268 2268 2268 HOH HOH A . K 6 HOH 269 2269 2269 HOH HOH A . K 6 HOH 270 2270 2270 HOH HOH A . K 6 HOH 271 2271 2271 HOH HOH A . K 6 HOH 272 2272 2272 HOH HOH A . K 6 HOH 273 2273 2273 HOH HOH A . K 6 HOH 274 2274 2274 HOH HOH A . K 6 HOH 275 2275 2275 HOH HOH A . K 6 HOH 276 2276 2276 HOH HOH A . K 6 HOH 277 2277 2277 HOH HOH A . K 6 HOH 278 2278 2278 HOH HOH A . K 6 HOH 279 2279 2279 HOH HOH A . K 6 HOH 280 2280 2280 HOH HOH A . K 6 HOH 281 2281 2281 HOH HOH A . K 6 HOH 282 2282 2282 HOH HOH A . K 6 HOH 283 2283 2283 HOH HOH A . K 6 HOH 284 2284 2284 HOH HOH A . K 6 HOH 285 2285 2285 HOH HOH A . K 6 HOH 286 2286 2286 HOH HOH A . K 6 HOH 287 2287 2287 HOH HOH A . K 6 HOH 288 2288 2288 HOH HOH A . K 6 HOH 289 2289 2289 HOH HOH A . K 6 HOH 290 2290 2290 HOH HOH A . K 6 HOH 291 2291 2291 HOH HOH A . K 6 HOH 292 2292 2292 HOH HOH A . K 6 HOH 293 2293 2293 HOH HOH A . K 6 HOH 294 2294 2294 HOH HOH A . K 6 HOH 295 2295 2295 HOH HOH A . K 6 HOH 296 2296 2296 HOH HOH A . K 6 HOH 297 2297 2297 HOH HOH A . K 6 HOH 298 2298 2298 HOH HOH A . K 6 HOH 299 2299 2299 HOH HOH A . K 6 HOH 300 2300 2300 HOH HOH A . K 6 HOH 301 2301 2301 HOH HOH A . K 6 HOH 302 2302 2302 HOH HOH A . K 6 HOH 303 2303 2303 HOH HOH A . K 6 HOH 304 2304 2304 HOH HOH A . K 6 HOH 305 2305 2305 HOH HOH A . K 6 HOH 306 2306 2306 HOH HOH A . K 6 HOH 307 2307 2307 HOH HOH A . K 6 HOH 308 2308 2308 HOH HOH A . K 6 HOH 309 2309 2309 HOH HOH A . K 6 HOH 310 2310 2310 HOH HOH A . K 6 HOH 311 2311 2311 HOH HOH A . K 6 HOH 312 2312 2312 HOH HOH A . K 6 HOH 313 2313 2313 HOH HOH A . K 6 HOH 314 2314 2314 HOH HOH A . K 6 HOH 315 2315 2315 HOH HOH A . K 6 HOH 316 2316 2316 HOH HOH A . K 6 HOH 317 2317 2317 HOH HOH A . K 6 HOH 318 2318 2318 HOH HOH A . K 6 HOH 319 2319 2319 HOH HOH A . K 6 HOH 320 2320 2320 HOH HOH A . K 6 HOH 321 2321 2321 HOH HOH A . K 6 HOH 322 2322 2322 HOH HOH A . K 6 HOH 323 2323 2323 HOH HOH A . K 6 HOH 324 2324 2324 HOH HOH A . K 6 HOH 325 2325 2325 HOH HOH A . K 6 HOH 326 2326 2326 HOH HOH A . K 6 HOH 327 2327 2327 HOH HOH A . K 6 HOH 328 2328 2328 HOH HOH A . K 6 HOH 329 2329 2329 HOH HOH A . K 6 HOH 330 2330 2330 HOH HOH A . K 6 HOH 331 2331 2331 HOH HOH A . K 6 HOH 332 2332 2332 HOH HOH A . K 6 HOH 333 2333 2333 HOH HOH A . K 6 HOH 334 2334 2334 HOH HOH A . K 6 HOH 335 2335 2335 HOH HOH A . K 6 HOH 336 2336 2336 HOH HOH A . K 6 HOH 337 2337 2337 HOH HOH A . K 6 HOH 338 2338 2338 HOH HOH A . K 6 HOH 339 2339 2339 HOH HOH A . K 6 HOH 340 2340 2340 HOH HOH A . K 6 HOH 341 2341 2341 HOH HOH A . K 6 HOH 342 2342 2342 HOH HOH A . K 6 HOH 343 2343 2343 HOH HOH A . K 6 HOH 344 2344 2344 HOH HOH A . K 6 HOH 345 2345 2345 HOH HOH A . K 6 HOH 346 2346 2346 HOH HOH A . K 6 HOH 347 2347 2347 HOH HOH A . K 6 HOH 348 2348 2348 HOH HOH A . K 6 HOH 349 2349 2349 HOH HOH A . K 6 HOH 350 2350 2350 HOH HOH A . K 6 HOH 351 2351 2351 HOH HOH A . K 6 HOH 352 2352 2352 HOH HOH A . K 6 HOH 353 2353 2353 HOH HOH A . K 6 HOH 354 2354 2354 HOH HOH A . K 6 HOH 355 2355 2355 HOH HOH A . K 6 HOH 356 2356 2356 HOH HOH A . K 6 HOH 357 2357 2357 HOH HOH A . K 6 HOH 358 2358 2358 HOH HOH A . K 6 HOH 359 2359 2359 HOH HOH A . K 6 HOH 360 2360 2360 HOH HOH A . K 6 HOH 361 2361 2361 HOH HOH A . K 6 HOH 362 2362 2362 HOH HOH A . K 6 HOH 363 2363 2363 HOH HOH A . K 6 HOH 364 2364 2364 HOH HOH A . K 6 HOH 365 2365 2365 HOH HOH A . K 6 HOH 366 2366 2366 HOH HOH A . K 6 HOH 367 2367 2367 HOH HOH A . K 6 HOH 368 2368 2368 HOH HOH A . K 6 HOH 369 2369 2369 HOH HOH A . K 6 HOH 370 2370 2370 HOH HOH A . K 6 HOH 371 2371 2371 HOH HOH A . K 6 HOH 372 2372 2372 HOH HOH A . K 6 HOH 373 2373 2373 HOH HOH A . K 6 HOH 374 2374 2374 HOH HOH A . K 6 HOH 375 2375 2375 HOH HOH A . K 6 HOH 376 2376 2376 HOH HOH A . K 6 HOH 377 2377 2377 HOH HOH A . K 6 HOH 378 2378 2378 HOH HOH A . K 6 HOH 379 2379 2379 HOH HOH A . K 6 HOH 380 2380 2380 HOH HOH A . K 6 HOH 381 2381 2381 HOH HOH A . K 6 HOH 382 2382 2382 HOH HOH A . K 6 HOH 383 2383 2383 HOH HOH A . K 6 HOH 384 2384 2384 HOH HOH A . K 6 HOH 385 2385 2385 HOH HOH A . K 6 HOH 386 2386 2386 HOH HOH A . K 6 HOH 387 2387 2387 HOH HOH A . K 6 HOH 388 2388 2388 HOH HOH A . K 6 HOH 389 2389 2389 HOH HOH A . K 6 HOH 390 2390 2390 HOH HOH A . K 6 HOH 391 2391 2391 HOH HOH A . K 6 HOH 392 2392 2392 HOH HOH A . K 6 HOH 393 2393 2393 HOH HOH A . K 6 HOH 394 2394 2394 HOH HOH A . K 6 HOH 395 2395 2395 HOH HOH A . K 6 HOH 396 2396 2396 HOH HOH A . K 6 HOH 397 2397 2397 HOH HOH A . K 6 HOH 398 2398 2398 HOH HOH A . K 6 HOH 399 2399 2399 HOH HOH A . K 6 HOH 400 2400 2400 HOH HOH A . K 6 HOH 401 2401 2401 HOH HOH A . K 6 HOH 402 2402 2402 HOH HOH A . K 6 HOH 403 2403 2403 HOH HOH A . K 6 HOH 404 2404 2404 HOH HOH A . K 6 HOH 405 2405 2405 HOH HOH A . K 6 HOH 406 2406 2406 HOH HOH A . K 6 HOH 407 2407 2407 HOH HOH A . K 6 HOH 408 2408 2408 HOH HOH A . K 6 HOH 409 2409 2409 HOH HOH A . K 6 HOH 410 2410 2410 HOH HOH A . K 6 HOH 411 2411 2411 HOH HOH A . K 6 HOH 412 2412 2412 HOH HOH A . K 6 HOH 413 2413 2413 HOH HOH A . K 6 HOH 414 2414 2414 HOH HOH A . K 6 HOH 415 2415 2415 HOH HOH A . K 6 HOH 416 2416 2416 HOH HOH A . K 6 HOH 417 2417 2417 HOH HOH A . K 6 HOH 418 2418 2418 HOH HOH A . K 6 HOH 419 2419 2419 HOH HOH A . K 6 HOH 420 2420 2420 HOH HOH A . K 6 HOH 421 2421 2421 HOH HOH A . K 6 HOH 422 2422 2422 HOH HOH A . K 6 HOH 423 2423 2423 HOH HOH A . K 6 HOH 424 2424 2424 HOH HOH A . K 6 HOH 425 2425 2425 HOH HOH A . K 6 HOH 426 2426 2426 HOH HOH A . K 6 HOH 427 2427 2427 HOH HOH A . K 6 HOH 428 2428 2428 HOH HOH A . K 6 HOH 429 2429 2429 HOH HOH A . K 6 HOH 430 2430 2430 HOH HOH A . K 6 HOH 431 2431 2431 HOH HOH A . K 6 HOH 432 2432 2432 HOH HOH A . K 6 HOH 433 2433 2433 HOH HOH A . K 6 HOH 434 2434 2434 HOH HOH A . K 6 HOH 435 2435 2435 HOH HOH A . K 6 HOH 436 2436 2436 HOH HOH A . K 6 HOH 437 2437 2437 HOH HOH A . K 6 HOH 438 2438 2438 HOH HOH A . K 6 HOH 439 2439 2439 HOH HOH A . K 6 HOH 440 2440 2440 HOH HOH A . K 6 HOH 441 2441 2441 HOH HOH A . K 6 HOH 442 2442 2442 HOH HOH A . K 6 HOH 443 2443 2443 HOH HOH A . K 6 HOH 444 2444 2444 HOH HOH A . K 6 HOH 445 2445 2445 HOH HOH A . K 6 HOH 446 2446 2446 HOH HOH A . K 6 HOH 447 2447 2447 HOH HOH A . K 6 HOH 448 2448 2448 HOH HOH A . K 6 HOH 449 2449 2449 HOH HOH A . K 6 HOH 450 2450 2450 HOH HOH A . K 6 HOH 451 2451 2451 HOH HOH A . K 6 HOH 452 2452 2452 HOH HOH A . K 6 HOH 453 2453 2453 HOH HOH A . K 6 HOH 454 2454 2454 HOH HOH A . K 6 HOH 455 2455 2455 HOH HOH A . K 6 HOH 456 2456 2456 HOH HOH A . K 6 HOH 457 2457 2457 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 130 A ASN 130 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 157 A ASN 157 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 250 A ASN 250 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 328 A ASN 328 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details 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 # _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 2000-10-19 2 'Structure model' 1 1 2013-01-30 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Atomic model' 2 2 'Structure model' 'Database references' 3 2 'Structure model' 'Derived calculations' 4 2 'Structure model' 'Non-polymer description' 5 2 'Structure model' Other 6 2 'Structure model' 'Structure summary' 7 2 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement . ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O A HOH 2098 ? ? O A HOH 2099 ? ? 2.05 2 1 O A HOH 2211 ? ? O A HOH 2427 ? ? 2.11 3 1 O A HOH 2183 ? ? O A HOH 2184 ? ? 2.13 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 CG2 _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 THR _pdbx_validate_symm_contact.auth_seq_id_1 219 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 A _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 GLY _pdbx_validate_symm_contact.auth_seq_id_2 269 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 2_646 _pdbx_validate_symm_contact.dist 1.86 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CB A ASP 39 ? ? CG A ASP 39 ? ? OD2 A ASP 39 ? ? 112.14 118.30 -6.16 0.90 N 2 1 CB A GLN 97 ? ? CG A GLN 97 ? A CD A GLN 97 ? A 129.60 111.60 18.00 2.60 N 3 1 NH1 A ARG 145 ? ? CZ A ARG 145 ? ? NH2 A ARG 145 ? ? 126.14 119.40 6.74 1.10 N 4 1 NE A ARG 145 ? ? CZ A ARG 145 ? ? NH2 A ARG 145 ? ? 114.91 120.30 -5.39 0.50 N 5 1 NE A ARG 171 ? ? CZ A ARG 171 ? ? NH2 A ARG 171 ? ? 116.57 120.30 -3.73 0.50 N 6 1 CB A TYR 251 ? ? CG A TYR 251 ? ? CD1 A TYR 251 ? ? 125.18 121.00 4.18 0.60 N 7 1 NE A ARG 298 ? ? CZ A ARG 298 ? ? NH2 A ARG 298 ? ? 125.79 120.30 5.49 0.50 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 59 ? ? -169.53 88.04 2 1 TYR A 220 ? ? -110.28 50.97 # _pdbx_validate_chiral.id 1 _pdbx_validate_chiral.PDB_model_num 1 _pdbx_validate_chiral.auth_atom_id C1 _pdbx_validate_chiral.label_alt_id ? _pdbx_validate_chiral.auth_asym_id A _pdbx_validate_chiral.auth_comp_id NAG _pdbx_validate_chiral.auth_seq_id 432 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details PLANAR _pdbx_validate_chiral.omega . # loop_ _pdbx_distant_solvent_atoms.id _pdbx_distant_solvent_atoms.PDB_model_num _pdbx_distant_solvent_atoms.auth_atom_id _pdbx_distant_solvent_atoms.label_alt_id _pdbx_distant_solvent_atoms.auth_asym_id _pdbx_distant_solvent_atoms.auth_comp_id _pdbx_distant_solvent_atoms.auth_seq_id _pdbx_distant_solvent_atoms.PDB_ins_code _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance _pdbx_distant_solvent_atoms.neighbor_ligand_distance 1 1 O ? A HOH 2043 ? 6.06 . 2 1 O ? A HOH 2054 ? 5.93 . # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL TRS 3 'SULFATE ION' SO4 4 GLYCEROL GOL 5 N-ACETYL-D-GLUCOSAMINE NAG 6 water HOH #