data_1QNQ # _entry.id 1QNQ # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.280 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 1QNQ PDBE EBI-4240 WWPDB D_1290004240 # 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 1QNR unspecified 'THE 3-D STRUCTURE OF A TRICHODERMA REESEI B-MANNANASE FROM GLYCOSIDE HYDROLASE FAMILY 5' PDB 1QNS 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 1QNQ _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 1QNQ _cell.length_a 51.130 _cell.length_b 54.290 _cell.length_c 61.050 _cell.angle_alpha 90.00 _cell.angle_beta 110.21 _cell.angle_gamma 90.00 _cell.Z_PDB 2 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1QNQ _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 ;2,2':6',2''-TERPYRIDINE PLATINUM(II) Chloride ; 463.799 2 ? ? ? ? 3 non-polymer syn 'SULFATE ION' 96.063 2 ? ? ? ? 4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 5 water nat water 18.015 654 ? ? ? ? # _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 _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 1QNQ _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 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 TPT non-polymer . ;2,2':6',2''-TERPYRIDINE PLATINUM(II) Chloride ; ? 'C15 H11 Cl N3 Pt 1' 463.799 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 1QNQ _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.0 _exptl_crystal.density_percent_sol 38 _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 1QNQ _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 20.000 _reflns.d_resolution_high 1.650 _reflns.number_obs 60810 _reflns.number_all ? _reflns.percent_possible_obs 91.0 _reflns.pdbx_Rmerge_I_obs 0.03900 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 18.4000 _reflns.B_iso_Wilson_estimate 10.334 _reflns.pdbx_redundancy 2.000 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.65 _reflns_shell.d_res_low 1.71 _reflns_shell.percent_possible_all 73.4 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value 0.07100 _reflns_shell.meanI_over_sigI_obs 9.800 _reflns_shell.pdbx_redundancy 1.20 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 1QNQ _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 1.65 _refine.ls_percent_reflns_obs 91 _refine.ls_R_factor_obs ? _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.115 _refine.ls_R_factor_R_free 0.160 _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 10.9 _refine.aniso_B[1][1] -2.126 _refine.aniso_B[2][2] -0.077 _refine.aniso_B[3][3] 2.053 _refine.aniso_B[1][2] 0.000 _refine.aniso_B[1][3] -1.465 _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 0.19 _refine.pdbx_overall_ESU_R_Free 0.08 _refine.overall_SU_ML 0.05 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 1.36 _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 104 _refine_hist.number_atoms_solvent 654 _refine_hist.number_atoms_total 3427 _refine_hist.d_res_high 1.65 _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 0.035 0.040 ? ? 'X-RAY DIFFRACTION' ? p_angle_deg ? ? ? ? 'X-RAY DIFFRACTION' ? p_planar_d 0.040 0.050 ? ? 'X-RAY DIFFRACTION' ? p_hb_or_metal_coord ? ? ? ? 'X-RAY DIFFRACTION' ? p_mcbond_it 1.645 2.000 ? ? 'X-RAY DIFFRACTION' ? p_mcangle_it 2.077 3.000 ? ? 'X-RAY DIFFRACTION' ? p_scbond_it 1.867 2.000 ? ? 'X-RAY DIFFRACTION' ? p_scangle_it 2.503 3.000 ? ? 'X-RAY DIFFRACTION' ? p_plane_restr 0.0236 ? ? ? 'X-RAY DIFFRACTION' ? p_chiral_restr 0.110 0.150 ? ? 'X-RAY DIFFRACTION' ? p_singtor_nbd 0.158 0.300 ? ? 'X-RAY DIFFRACTION' ? p_multtor_nbd 0.249 0.300 ? ? 'X-RAY DIFFRACTION' ? p_xhyhbond_nbd ? ? ? ? 'X-RAY DIFFRACTION' ? p_xyhbond_nbd ? ? ? ? 'X-RAY DIFFRACTION' ? p_planar_tor 4.5 7.0 ? ? 'X-RAY DIFFRACTION' ? p_staggered_tor 11.4 15.0 ? ? 'X-RAY DIFFRACTION' ? p_orthonormal_tor ? ? ? ? 'X-RAY DIFFRACTION' ? p_transverse_tor 34.8 20.0 ? ? 'X-RAY DIFFRACTION' ? p_special_tor 15.0 ? ? ? 'X-RAY DIFFRACTION' ? # _struct.entry_id 1QNQ _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 1QNQ _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, MANNANASE, TRICHODERMA REESEI, 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 2 ? D N N 3 ? E N N 3 ? F N N 4 ? G N N 4 ? H N N 4 ? I N N 4 ? J N N 5 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 TYR A 27 ? PHE A 31 ? TYR A 27 PHE A 31 5 ? 5 HELX_P HELX_P2 2 ASN A 34 ? SER A 48 ? ASN A 34 SER A 48 1 ? 15 HELX_P HELX_P3 3 LEU A 89 ? HIS A 102 ? LEU A 89 HIS A 102 1 ? 14 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 ? ? ? ? ? ? ? 2.047 ? disulf2 disulf ? ? A CYS 172 SG ? ? ? 1_555 A CYS 175 SG ? ? A CYS 172 A CYS 175 1_555 ? ? ? ? ? ? ? 2.079 ? disulf3 disulf ? ? A CYS 265 SG ? ? ? 1_555 A CYS 272 SG ? ? A CYS 265 A CYS 272 1_555 ? ? ? ? ? ? ? 2.076 ? disulf4 disulf ? ? A CYS 284 SG ? ? ? 1_555 A CYS 334 SG ? ? A CYS 284 A CYS 334 1_555 ? ? ? ? ? ? ? 2.092 ? covale1 covale ? ? A ASN 130 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 130 A NAG 430 1_555 ? ? ? ? ? ? ? 1.613 ? covale2 covale ? ? A ASN 157 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 157 A NAG 431 1_555 ? ? ? ? ? ? ? 1.619 ? covale3 covale ? ? A ASN 250 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 250 A NAG 432 1_555 ? ? ? ? ? ? ? 1.613 ? covale4 covale ? ? A ASN 328 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 328 A NAG 433 1_555 ? ? ? ? ? ? ? 1.621 ? metalc1 metalc ? ? B TPT . PT1 ? ? ? 1_555 J HOH . O ? ? A TPT 401 A HOH 2619 1_555 ? ? ? ? ? ? ? 2.365 ? metalc2 metalc ? ? C TPT . PT1 ? ? ? 1_555 J HOH . O ? ? A TPT 402 A HOH 2620 1_555 ? ? ? ? ? ? ? 2.170 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # _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 1.16 # 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 ? ? ? ? 10 'BINDING SITE FOR RESIDUE SO4 A 411' AC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 A 412' AC3 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE TPT A 401' AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE TPT A 402' AC5 Software ? ? ? ? 3 'Binding site for Mono-Saccharide NAG A 430 bound to ASN A 130' AC6 Software ? ? ? ? 9 'Binding site for Mono-Saccharide NAG A 431 bound to ASN A 157' AC7 Software ? ? ? ? 6 'Binding site for Mono-Saccharide NAG A 432 bound to ASN A 250' AC8 Software ? ? ? ? 9 '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 10 SER A 246 ? SER A 246 . ? 1_555 ? 2 AC1 10 GLN A 280 ? GLN A 280 . ? 1_555 ? 3 AC1 10 TPT B . ? TPT A 401 . ? 1_555 ? 4 AC1 10 HOH J . ? HOH A 2587 . ? 1_555 ? 5 AC1 10 HOH J . ? HOH A 2621 . ? 1_555 ? 6 AC1 10 HOH J . ? HOH A 2622 . ? 1_555 ? 7 AC1 10 HOH J . ? HOH A 2623 . ? 1_555 ? 8 AC1 10 HOH J . ? HOH A 2624 . ? 1_555 ? 9 AC1 10 HOH J . ? HOH A 2625 . ? 1_555 ? 10 AC1 10 HOH J . ? HOH A 2626 . ? 1_555 ? 11 AC2 7 ASN A 282 ? ASN A 282 . ? 1_555 ? 12 AC2 7 PRO A 283 ? PRO A 283 . ? 1_555 ? 13 AC2 7 CYS A 284 ? CYS A 284 . ? 1_555 ? 14 AC2 7 THR A 285 ? THR A 285 . ? 1_555 ? 15 AC2 7 HOH J . ? HOH A 2604 . ? 1_555 ? 16 AC2 7 HOH J . ? HOH A 2627 . ? 1_555 ? 17 AC2 7 HOH J . ? HOH A 2628 . ? 1_555 ? 18 AC3 7 TYR A 243 ? TYR A 243 . ? 1_555 ? 19 AC3 7 SER A 246 ? SER A 246 . ? 1_555 ? 20 AC3 7 ASP A 321 ? ASP A 321 . ? 1_555 ? 21 AC3 7 TYR A 323 ? TYR A 323 . ? 1_555 ? 22 AC3 7 TPT C . ? TPT A 402 . ? 1_555 ? 23 AC3 7 SO4 D . ? SO4 A 411 . ? 1_555 ? 24 AC3 7 HOH J . ? HOH A 2619 . ? 1_555 ? 25 AC4 6 TRP A 114 ? TRP A 114 . ? 1_555 ? 26 AC4 6 ASP A 116 ? ASP A 116 . ? 1_555 ? 27 AC4 6 GLU A 169 ? GLU A 169 . ? 1_555 ? 28 AC4 6 TPT B . ? TPT A 401 . ? 1_555 ? 29 AC4 6 HOH J . ? HOH A 2619 . ? 1_555 ? 30 AC4 6 HOH J . ? HOH A 2620 . ? 1_555 ? 31 AC5 3 ASN A 130 ? ASN A 130 . ? 1_555 ? 32 AC5 3 HOH J . ? HOH A 2631 . ? 1_555 ? 33 AC5 3 HOH J . ? HOH A 2632 . ? 1_555 ? 34 AC6 9 ASN A 157 ? ASN A 157 . ? 1_555 ? 35 AC6 9 SER A 196 ? SER A 196 . ? 1_555 ? 36 AC6 9 ASN A 197 ? ASN A 197 . ? 1_555 ? 37 AC6 9 HOH J . ? HOH A 2637 . ? 1_555 ? 38 AC6 9 HOH J . ? HOH A 2638 . ? 1_555 ? 39 AC6 9 HOH J . ? HOH A 2639 . ? 1_555 ? 40 AC6 9 HOH J . ? HOH A 2641 . ? 1_555 ? 41 AC6 9 HOH J . ? HOH A 2642 . ? 1_555 ? 42 AC6 9 HOH J . ? HOH A 2643 . ? 1_555 ? 43 AC7 6 ASP A 213 ? ASP A 213 . ? 1_555 ? 44 AC7 6 ASN A 250 ? ASN A 250 . ? 1_555 ? 45 AC7 6 THR A 252 ? THR A 252 . ? 1_555 ? 46 AC7 6 TRP A 253 ? TRP A 253 . ? 1_555 ? 47 AC7 6 HOH J . ? HOH A 2647 . ? 1_555 ? 48 AC7 6 HOH J . ? HOH A 2648 . ? 1_555 ? 49 AC8 9 ARG A 145 ? ARG A 145 . ? 1_455 ? 50 AC8 9 TYR A 190 ? TYR A 190 . ? 1_455 ? 51 AC8 9 ASN A 328 ? ASN A 328 . ? 1_555 ? 52 AC8 9 HOH J . ? HOH A 2148 . ? 1_555 ? 53 AC8 9 HOH J . ? HOH A 2385 . ? 1_455 ? 54 AC8 9 HOH J . ? HOH A 2440 . ? 1_455 ? 55 AC8 9 HOH J . ? HOH A 2652 . ? 1_555 ? 56 AC8 9 HOH J . ? HOH A 2653 . ? 1_555 ? 57 AC8 9 HOH J . ? HOH A 2654 . ? 1_555 ? # _database_PDB_matrix.entry_id 1QNQ _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 1QNQ _atom_sites.fract_transf_matrix[1][1] 0.019558 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.007200 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.018419 _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] 0.017455 _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 PT 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 ? -1.568 52.524 11.916 1.00 20.12 ? 1 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? -0.120 52.696 11.606 1.00 21.07 ? 1 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? 0.458 51.438 10.951 1.00 20.51 ? 1 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? -0.168 50.376 10.991 1.00 19.65 ? 1 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? 0.639 53.018 12.892 1.00 20.95 ? 1 ALA A CB 1 ATOM 6 N N . SER A 1 2 ? 1.609 51.571 10.322 1.00 19.71 ? 2 SER A N 1 ATOM 7 C CA . SER A 1 2 ? 2.329 50.460 9.683 1.00 18.99 ? 2 SER A CA 1 ATOM 8 C C . SER A 1 2 ? 3.796 50.559 10.127 1.00 18.98 ? 2 SER A C 1 ATOM 9 O O . SER A 1 2 ? 4.545 51.409 9.604 1.00 18.35 ? 2 SER A O 1 ATOM 10 C CB . SER A 1 2 ? 2.273 50.523 8.169 1.00 19.17 ? 2 SER A CB 1 ATOM 11 O OG . SER A 1 2 ? 1.001 50.506 7.606 1.00 19.34 ? 2 SER A OG 1 ATOM 12 N N . SER A 1 3 ? 4.203 49.738 11.107 1.00 16.93 ? 3 SER A N 1 ATOM 13 C CA . SER A 1 3 ? 5.558 49.855 11.648 1.00 16.57 ? 3 SER A CA 1 ATOM 14 C C . SER A 1 3 ? 6.245 48.500 11.785 1.00 13.94 ? 3 SER A C 1 ATOM 15 O O . SER A 1 3 ? 5.601 47.431 11.640 1.00 12.40 ? 3 SER A O 1 ATOM 16 C CB . SER A 1 3 ? 5.518 50.544 13.019 1.00 17.43 ? 3 SER A CB 1 ATOM 17 O OG A SER A 1 3 ? 4.646 49.900 13.900 0.50 17.48 ? 3 SER A OG 1 ATOM 18 O OG B SER A 1 3 ? 4.466 51.496 13.077 0.50 17.22 ? 3 SER A OG 1 ATOM 19 N N . PHE A 1 4 ? 7.549 48.546 12.113 1.00 11.17 ? 4 PHE A N 1 ATOM 20 C CA . PHE A 1 4 ? 8.278 47.296 12.323 1.00 10.32 ? 4 PHE A CA 1 ATOM 21 C C . PHE A 1 4 ? 7.850 46.646 13.656 1.00 10.58 ? 4 PHE A C 1 ATOM 22 O O . PHE A 1 4 ? 7.720 47.329 14.690 1.00 9.04 ? 4 PHE A O 1 ATOM 23 C CB . PHE A 1 4 ? 9.809 47.523 12.335 1.00 9.66 ? 4 PHE A CB 1 ATOM 24 C CG . PHE A 1 4 ? 10.460 47.975 11.061 1.00 10.35 ? 4 PHE A CG 1 ATOM 25 C CD1 . PHE A 1 4 ? 10.400 47.227 9.897 1.00 10.15 ? 4 PHE A CD1 1 ATOM 26 C CD2 . PHE A 1 4 ? 11.159 49.185 11.003 1.00 11.86 ? 4 PHE A CD2 1 ATOM 27 C CE1 . PHE A 1 4 ? 11.001 47.650 8.721 1.00 10.10 ? 4 PHE A CE1 1 ATOM 28 C CE2 . PHE A 1 4 ? 11.742 49.612 9.839 1.00 9.95 ? 4 PHE A CE2 1 ATOM 29 C CZ . PHE A 1 4 ? 11.680 48.860 8.701 1.00 10.59 ? 4 PHE A CZ 1 ATOM 30 N N . VAL A 1 5 ? 7.644 45.333 13.682 1.00 8.80 ? 5 VAL A N 1 ATOM 31 C CA . VAL A 1 5 ? 7.272 44.602 14.913 1.00 9.48 ? 5 VAL A CA 1 ATOM 32 C C . VAL A 1 5 ? 8.427 44.590 15.923 1.00 9.34 ? 5 VAL A C 1 ATOM 33 O O . VAL A 1 5 ? 9.557 44.236 15.571 1.00 8.79 ? 5 VAL A O 1 ATOM 34 C CB . VAL A 1 5 ? 6.826 43.154 14.639 1.00 9.31 ? 5 VAL A CB 1 ATOM 35 C CG1 . VAL A 1 5 ? 6.503 42.390 15.933 1.00 10.92 ? 5 VAL A CG1 1 ATOM 36 C CG2 . VAL A 1 5 ? 5.565 43.053 13.760 1.00 10.50 ? 5 VAL A CG2 1 ATOM 37 N N . THR A 1 6 ? 8.207 45.004 17.161 1.00 9.07 ? 6 THR A N 1 ATOM 38 C CA . THR A 1 6 ? 9.209 45.090 18.227 1.00 10.13 ? 6 THR A CA 1 ATOM 39 C C . THR A 1 6 ? 8.714 44.472 19.542 1.00 11.10 ? 6 THR A C 1 ATOM 40 O O . THR A 1 6 ? 7.547 44.069 19.659 1.00 9.00 ? 6 THR A O 1 ATOM 41 C CB . THR A 1 6 ? 9.591 46.556 18.536 1.00 10.51 ? 6 THR A CB 1 ATOM 42 O OG1 . THR A 1 6 ? 8.411 47.344 18.849 1.00 11.21 ? 6 THR A OG1 1 ATOM 43 C CG2 . THR A 1 6 ? 10.304 47.203 17.356 1.00 11.11 ? 6 THR A CG2 1 ATOM 44 N N . ILE A 1 7 ? 9.623 44.367 20.519 1.00 10.83 ? 7 ILE A N 1 ATOM 45 C CA . ILE A 1 7 ? 9.289 43.945 21.866 1.00 15.60 ? 7 ILE A CA 1 ATOM 46 C C . ILE A 1 7 ? 9.124 45.162 22.790 1.00 15.43 ? 7 ILE A C 1 ATOM 47 O O . ILE A 1 7 ? 9.916 46.084 22.699 1.00 16.93 ? 7 ILE A O 1 ATOM 48 C CB . ILE A 1 7 ? 10.313 42.915 22.388 1.00 18.54 ? 7 ILE A CB 1 ATOM 49 C CG1 . ILE A 1 7 ? 9.772 41.559 21.856 1.00 20.29 ? 7 ILE A CG1 1 ATOM 50 C CG2 . ILE A 1 7 ? 10.411 42.900 23.906 1.00 18.58 ? 7 ILE A CG2 1 ATOM 51 C CD1 . ILE A 1 7 ? 10.659 40.380 21.694 1.00 21.66 ? 7 ILE A CD1 1 ATOM 52 N N . SER A 1 8 ? 8.108 45.198 23.642 1.00 14.47 ? 8 SER A N 1 ATOM 53 C CA . SER A 1 8 ? 7.839 46.241 24.624 1.00 15.89 ? 8 SER A CA 1 ATOM 54 C C . SER A 1 8 ? 7.762 45.582 26.004 1.00 14.53 ? 8 SER A C 1 ATOM 55 O O . SER A 1 8 ? 6.779 44.900 26.320 1.00 12.87 ? 8 SER A O 1 ATOM 56 C CB . SER A 1 8 ? 6.569 47.058 24.349 1.00 18.17 ? 8 SER A CB 1 ATOM 57 O OG . SER A 1 8 ? 6.346 48.037 25.380 1.00 20.08 ? 8 SER A OG 1 ATOM 58 N N . GLY A 1 9 ? 8.853 45.711 26.789 1.00 12.30 ? 9 GLY A N 1 ATOM 59 C CA . GLY A 1 9 ? 8.815 45.020 28.098 1.00 14.25 ? 9 GLY A CA 1 ATOM 60 C C . GLY A 1 9 ? 8.700 43.523 27.936 1.00 14.57 ? 9 GLY A C 1 ATOM 61 O O . GLY A 1 9 ? 9.463 42.898 27.204 1.00 13.28 ? 9 GLY A O 1 ATOM 62 N N . THR A 1 10 ? 7.725 42.898 28.605 1.00 16.32 ? 10 THR A N 1 ATOM 63 C CA . THR A 1 10 ? 7.474 41.482 28.536 1.00 17.10 ? 10 THR A CA 1 ATOM 64 C C . THR A 1 10 ? 6.543 41.027 27.419 1.00 18.23 ? 10 THR A C 1 ATOM 65 O O . THR A 1 10 ? 6.131 39.843 27.325 1.00 17.45 ? 10 THR A O 1 ATOM 66 C CB . THR A 1 10 ? 6.919 41.014 29.919 1.00 18.06 ? 10 THR A CB 1 ATOM 67 O OG1 . THR A 1 10 ? 5.675 41.691 30.150 1.00 18.45 ? 10 THR A OG1 1 ATOM 68 C CG2 . THR A 1 10 ? 7.839 41.309 31.129 1.00 17.45 ? 10 THR A CG2 1 ATOM 69 N N . GLN A 1 11 ? 6.097 41.894 26.494 1.00 18.45 ? 11 GLN A N 1 ATOM 70 C CA . GLN A 1 11 ? 5.094 41.666 25.476 1.00 17.73 ? 11 GLN A CA 1 ATOM 71 C C . GLN A 1 11 ? 5.469 42.110 24.058 1.00 15.70 ? 11 GLN A C 1 ATOM 72 O O . GLN A 1 11 ? 6.543 42.718 23.929 1.00 16.79 ? 11 GLN A O 1 ATOM 73 C CB . GLN A 1 11 ? 3.832 42.507 25.865 1.00 17.77 ? 11 GLN A CB 1 ATOM 74 C CG . GLN A 1 11 ? 3.370 42.381 27.298 1.00 18.25 ? 11 GLN A CG 1 ATOM 75 C CD . GLN A 1 11 ? 2.154 43.178 27.685 1.00 20.55 ? 11 GLN A CD 1 ATOM 76 O OE1 . GLN A 1 11 ? 2.253 44.310 28.194 1.00 20.43 ? 11 GLN A OE1 1 ATOM 77 N NE2 . GLN A 1 11 ? 0.995 42.562 27.426 1.00 21.29 ? 11 GLN A NE2 1 ATOM 78 N N . PHE A 1 12 ? 4.683 41.893 23.016 1.00 13.39 ? 12 PHE A N 1 ATOM 79 C CA . PHE A 1 12 ? 4.902 42.369 21.663 1.00 12.83 ? 12 PHE A CA 1 ATOM 80 C C . PHE A 1 12 ? 4.173 43.669 21.302 1.00 13.22 ? 12 PHE A C 1 ATOM 81 O O . PHE A 1 12 ? 3.079 43.939 21.798 1.00 13.12 ? 12 PHE A O 1 ATOM 82 C CB . PHE A 1 12 ? 4.483 41.315 20.609 1.00 12.34 ? 12 PHE A CB 1 ATOM 83 C CG . PHE A 1 12 ? 5.333 40.058 20.611 1.00 13.00 ? 12 PHE A CG 1 ATOM 84 C CD1 . PHE A 1 12 ? 6.609 40.066 20.078 1.00 11.66 ? 12 PHE A CD1 1 ATOM 85 C CD2 . PHE A 1 12 ? 4.874 38.870 21.148 1.00 11.38 ? 12 PHE A CD2 1 ATOM 86 C CE1 . PHE A 1 12 ? 7.389 38.918 20.061 1.00 11.30 ? 12 PHE A CE1 1 ATOM 87 C CE2 . PHE A 1 12 ? 5.645 37.716 21.153 1.00 11.45 ? 12 PHE A CE2 1 ATOM 88 C CZ . PHE A 1 12 ? 6.924 37.748 20.624 1.00 9.13 ? 12 PHE A CZ 1 ATOM 89 N N . ASN A 1 13 ? 4.732 44.478 20.413 1.00 12.08 ? 13 ASN A N 1 ATOM 90 C CA . ASN A 1 13 ? 4.157 45.747 19.931 1.00 13.40 ? 13 ASN A CA 1 ATOM 91 C C . ASN A 1 13 ? 3.936 45.641 18.425 1.00 13.20 ? 13 ASN A C 1 ATOM 92 O O . ASN A 1 13 ? 4.911 45.568 17.657 1.00 11.91 ? 13 ASN A O 1 ATOM 93 C CB . ASN A 1 13 ? 5.099 46.896 20.282 1.00 16.24 ? 13 ASN A CB 1 ATOM 94 C CG . ASN A 1 13 ? 4.652 48.281 19.913 1.00 19.09 ? 13 ASN A CG 1 ATOM 95 O OD1 . ASN A 1 13 ? 3.764 48.455 19.077 1.00 20.03 ? 13 ASN A OD1 1 ATOM 96 N ND2 . ASN A 1 13 ? 5.244 49.316 20.517 1.00 19.54 ? 13 ASN A ND2 1 ATOM 97 N N . ILE A 1 14 ? 2.678 45.551 17.984 1.00 12.27 ? 14 ILE A N 1 ATOM 98 C CA . ILE A 1 14 ? 2.295 45.378 16.586 1.00 11.50 ? 14 ILE A CA 1 ATOM 99 C C . ILE A 1 14 ? 1.538 46.608 16.071 1.00 12.30 ? 14 ILE A C 1 ATOM 100 O O . ILE A 1 14 ? 0.439 46.920 16.554 1.00 11.46 ? 14 ILE A O 1 ATOM 101 C CB . ILE A 1 14 ? 1.371 44.132 16.415 1.00 11.08 ? 14 ILE A CB 1 ATOM 102 C CG1 . ILE A 1 14 ? 1.973 42.841 16.955 1.00 11.64 ? 14 ILE A CG1 1 ATOM 103 C CG2 . ILE A 1 14 ? 1.008 43.931 14.939 1.00 10.73 ? 14 ILE A CG2 1 ATOM 104 C CD1 . ILE A 1 14 ? 1.138 41.568 16.836 1.00 11.76 ? 14 ILE A CD1 1 ATOM 105 N N . ASP A 1 15 ? 2.145 47.354 15.165 1.00 12.53 ? 15 ASP A N 1 ATOM 106 C CA . ASP A 1 15 ? 1.585 48.610 14.644 1.00 13.80 ? 15 ASP A CA 1 ATOM 107 C C . ASP A 1 15 ? 1.159 49.574 15.752 1.00 15.57 ? 15 ASP A C 1 ATOM 108 O O . ASP A 1 15 ? 0.190 50.342 15.659 1.00 15.50 ? 15 ASP A O 1 ATOM 109 C CB . ASP A 1 15 ? 0.462 48.308 13.658 1.00 12.57 ? 15 ASP A CB 1 ATOM 110 C CG . ASP A 1 15 ? 0.954 47.610 12.401 1.00 13.01 ? 15 ASP A CG 1 ATOM 111 O OD1 . ASP A 1 15 ? 2.090 47.787 11.934 1.00 11.59 ? 15 ASP A OD1 1 ATOM 112 O OD2 . ASP A 1 15 ? 0.163 46.831 11.836 1.00 14.37 ? 15 ASP A OD2 1 ATOM 113 N N . GLY A 1 16 ? 1.933 49.633 16.838 1.00 15.76 ? 16 GLY A N 1 ATOM 114 C CA . GLY A 1 16 ? 1.711 50.539 17.941 1.00 16.74 ? 16 GLY A CA 1 ATOM 115 C C . GLY A 1 16 ? 0.858 50.048 19.078 1.00 17.81 ? 16 GLY A C 1 ATOM 116 O O . GLY A 1 16 ? 0.768 50.732 20.113 1.00 18.43 ? 16 GLY A O 1 ATOM 117 N N . LYS A 1 17 ? 0.212 48.899 18.889 1.00 16.37 ? 17 LYS A N 1 ATOM 118 C CA . LYS A 1 17 ? -0.603 48.254 19.897 1.00 17.79 ? 17 LYS A CA 1 ATOM 119 C C . LYS A 1 17 ? 0.155 47.185 20.695 1.00 16.19 ? 17 LYS A C 1 ATOM 120 O O . LYS A 1 17 ? 0.580 46.209 20.077 1.00 15.01 ? 17 LYS A O 1 ATOM 121 C CB . LYS A 1 17 ? -1.804 47.558 19.210 1.00 20.53 ? 17 LYS A CB 1 ATOM 122 C CG . LYS A 1 17 ? -2.487 48.531 18.231 1.00 25.60 ? 17 LYS A CG 1 ATOM 123 C CD . LYS A 1 17 ? -3.244 49.555 19.083 1.00 30.25 ? 17 LYS A CD 1 ATOM 124 C CE . LYS A 1 17 ? -3.662 50.771 18.289 1.00 33.61 ? 17 LYS A CE 1 ATOM 125 N NZ . LYS A 1 17 ? -4.220 51.811 19.215 1.00 36.21 ? 17 LYS A NZ 1 ATOM 126 N N . VAL A 1 18 ? 0.281 47.350 22.004 1.00 14.93 ? 18 VAL A N 1 ATOM 127 C CA . VAL A 1 18 ? 0.963 46.362 22.857 1.00 14.60 ? 18 VAL A CA 1 ATOM 128 C C . VAL A 1 18 ? -0.016 45.398 23.507 1.00 15.73 ? 18 VAL A C 1 ATOM 129 O O . VAL A 1 18 ? -1.008 45.842 24.121 1.00 15.95 ? 18 VAL A O 1 ATOM 130 C CB . VAL A 1 18 ? 1.727 47.115 23.985 1.00 14.59 ? 18 VAL A CB 1 ATOM 131 C CG1 . VAL A 1 18 ? 2.349 46.161 24.989 1.00 14.42 ? 18 VAL A CG1 1 ATOM 132 C CG2 . VAL A 1 18 ? 2.745 48.047 23.349 1.00 14.99 ? 18 VAL A CG2 1 ATOM 133 N N . GLY A 1 19 ? 0.221 44.083 23.416 1.00 14.39 ? 19 GLY A N 1 ATOM 134 C CA . GLY A 1 19 ? -0.654 43.098 24.022 1.00 15.13 ? 19 GLY A CA 1 ATOM 135 C C . GLY A 1 19 ? -0.718 41.749 23.297 1.00 12.99 ? 19 GLY A C 1 ATOM 136 O O . GLY A 1 19 ? -0.109 41.604 22.250 1.00 11.77 ? 19 GLY A O 1 ATOM 137 N N . TYR A 1 20 ? -1.451 40.805 23.839 1.00 12.41 ? 20 TYR A N 1 ATOM 138 C CA . TYR A 1 20 ? -1.633 39.447 23.324 1.00 11.08 ? 20 TYR A CA 1 ATOM 139 C C . TYR A 1 20 ? -2.212 39.391 21.907 1.00 11.24 ? 20 TYR A C 1 ATOM 140 O O . TYR A 1 20 ? -3.120 40.177 21.580 1.00 12.05 ? 20 TYR A O 1 ATOM 141 C CB . TYR A 1 20 ? -2.550 38.632 24.270 1.00 11.13 ? 20 TYR A CB 1 ATOM 142 C CG . TYR A 1 20 ? -2.489 37.127 24.055 1.00 11.63 ? 20 TYR A CG 1 ATOM 143 C CD1 . TYR A 1 20 ? -1.531 36.348 24.697 1.00 10.79 ? 20 TYR A CD1 1 ATOM 144 C CD2 . TYR A 1 20 ? -3.387 36.490 23.197 1.00 11.18 ? 20 TYR A CD2 1 ATOM 145 C CE1 . TYR A 1 20 ? -1.480 34.975 24.470 1.00 11.19 ? 20 TYR A CE1 1 ATOM 146 C CE2 . TYR A 1 20 ? -3.355 35.117 22.979 1.00 10.86 ? 20 TYR A CE2 1 ATOM 147 C CZ . TYR A 1 20 ? -2.360 34.375 23.606 1.00 12.08 ? 20 TYR A CZ 1 ATOM 148 O OH . TYR A 1 20 ? -2.291 32.996 23.405 1.00 11.46 ? 20 TYR A OH 1 ATOM 149 N N . PHE A 1 21 ? -1.709 38.514 21.046 1.00 9.88 ? 21 PHE A N 1 ATOM 150 C CA . PHE A 1 21 ? -2.171 38.294 19.685 1.00 9.48 ? 21 PHE A CA 1 ATOM 151 C C . PHE A 1 21 ? -2.567 36.848 19.369 1.00 9.84 ? 21 PHE A C 1 ATOM 152 O O . PHE A 1 21 ? -2.058 35.905 19.971 1.00 9.82 ? 21 PHE A O 1 ATOM 153 C CB . PHE A 1 21 ? -1.140 38.749 18.614 1.00 9.02 ? 21 PHE A CB 1 ATOM 154 C CG . PHE A 1 21 ? 0.037 37.827 18.384 1.00 8.99 ? 21 PHE A CG 1 ATOM 155 C CD1 . PHE A 1 21 ? -0.087 36.761 17.500 1.00 8.63 ? 21 PHE A CD1 1 ATOM 156 C CD2 . PHE A 1 21 ? 1.254 38.008 18.993 1.00 9.78 ? 21 PHE A CD2 1 ATOM 157 C CE1 . PHE A 1 21 ? 0.949 35.849 17.272 1.00 8.14 ? 21 PHE A CE1 1 ATOM 158 C CE2 . PHE A 1 21 ? 2.307 37.132 18.782 1.00 9.82 ? 21 PHE A CE2 1 ATOM 159 C CZ . PHE A 1 21 ? 2.157 36.052 17.933 1.00 9.50 ? 21 PHE A CZ 1 ATOM 160 N N . ALA A 1 22 ? -3.490 36.680 18.420 1.00 8.63 ? 22 ALA A N 1 ATOM 161 C CA . ALA A 1 22 ? -3.800 35.373 17.827 1.00 8.58 ? 22 ALA A CA 1 ATOM 162 C C . ALA A 1 22 ? -3.457 35.343 16.323 1.00 8.85 ? 22 ALA A C 1 ATOM 163 O O . ALA A 1 22 ? -3.618 36.329 15.583 1.00 8.37 ? 22 ALA A O 1 ATOM 164 C CB . ALA A 1 22 ? -5.268 34.995 17.969 1.00 9.06 ? 22 ALA A CB 1 ATOM 165 N N . GLY A 1 23 ? -3.001 34.175 15.867 1.00 6.18 ? 23 GLY A N 1 ATOM 166 C CA . GLY A 1 23 ? -2.679 33.959 14.445 1.00 7.78 ? 23 GLY A CA 1 ATOM 167 C C . GLY A 1 23 ? -2.904 32.519 13.970 1.00 7.49 ? 23 GLY A C 1 ATOM 168 O O . GLY A 1 23 ? -3.580 31.737 14.646 1.00 7.59 ? 23 GLY A O 1 ATOM 169 N N . THR A 1 24 ? -2.391 32.182 12.782 1.00 6.55 ? 24 THR A N 1 ATOM 170 C CA . THR A 1 24 ? -2.573 30.822 12.231 1.00 7.46 ? 24 THR A CA 1 ATOM 171 C C . THR A 1 24 ? -1.383 30.381 11.371 1.00 8.03 ? 24 THR A C 1 ATOM 172 O O . THR A 1 24 ? -0.541 31.203 10.983 1.00 6.77 ? 24 THR A O 1 ATOM 173 C CB . THR A 1 24 ? -3.864 30.740 11.383 1.00 6.98 ? 24 THR A CB 1 ATOM 174 O OG1 . THR A 1 24 ? -4.177 29.382 11.042 1.00 6.93 ? 24 THR A OG1 1 ATOM 175 C CG2 . THR A 1 24 ? -3.746 31.505 10.058 1.00 7.81 ? 24 THR A CG2 1 ATOM 176 N N . ASN A 1 25 ? -1.303 29.088 11.063 1.00 7.54 ? 25 ASN A N 1 ATOM 177 C CA . ASN A 1 25 ? -0.297 28.507 10.184 1.00 5.94 ? 25 ASN A CA 1 ATOM 178 C C . ASN A 1 25 ? -0.887 28.297 8.776 1.00 6.55 ? 25 ASN A C 1 ATOM 179 O O . ASN A 1 25 ? -2.033 27.808 8.660 1.00 7.51 ? 25 ASN A O 1 ATOM 180 C CB . ASN A 1 25 ? 0.255 27.149 10.701 1.00 6.96 ? 25 ASN A CB 1 ATOM 181 C CG . ASN A 1 25 ? 1.213 27.259 11.872 1.00 8.08 ? 25 ASN A CG 1 ATOM 182 O OD1 . ASN A 1 25 ? 2.440 27.299 11.665 1.00 5.96 ? 25 ASN A OD1 1 ATOM 183 N ND2 . ASN A 1 25 ? 0.686 27.303 13.108 1.00 6.52 ? 25 ASN A ND2 1 ATOM 184 N N . CYS A 1 26 ? -0.167 28.660 7.732 1.00 4.80 ? 26 CYS A N 1 ATOM 185 C CA . CYS A 1 26 ? -0.547 28.451 6.312 1.00 6.35 ? 26 CYS A CA 1 ATOM 186 C C . CYS A 1 26 ? 0.722 28.220 5.483 1.00 7.11 ? 26 CYS A C 1 ATOM 187 O O . CYS A 1 26 ? 1.123 29.040 4.644 1.00 7.89 ? 26 CYS A O 1 ATOM 188 C CB . CYS A 1 26 ? -1.319 29.645 5.712 1.00 6.59 ? 26 CYS A CB 1 ATOM 189 S SG . CYS A 1 26 ? -2.013 29.356 4.055 1.00 7.15 ? 26 CYS A SG 1 ATOM 190 N N . TYR A 1 27 ? 1.368 27.044 5.627 1.00 5.37 ? 27 TYR A N 1 ATOM 191 C CA . TYR A 1 27 ? 2.603 26.699 4.936 1.00 7.25 ? 27 TYR A CA 1 ATOM 192 C C . TYR A 1 27 ? 2.411 26.837 3.420 1.00 7.91 ? 27 TYR A C 1 ATOM 193 O O . TYR A 1 27 ? 3.271 27.361 2.688 1.00 7.63 ? 27 TYR A O 1 ATOM 194 C CB . TYR A 1 27 ? 3.184 25.294 5.294 1.00 7.98 ? 27 TYR A CB 1 ATOM 195 C CG . TYR A 1 27 ? 2.542 24.129 4.577 1.00 7.85 ? 27 TYR A CG 1 ATOM 196 C CD1 . TYR A 1 27 ? 2.946 23.719 3.307 1.00 6.37 ? 27 TYR A CD1 1 ATOM 197 C CD2 . TYR A 1 27 ? 1.492 23.425 5.159 1.00 7.19 ? 27 TYR A CD2 1 ATOM 198 C CE1 . TYR A 1 27 ? 2.322 22.681 2.644 1.00 6.65 ? 27 TYR A CE1 1 ATOM 199 C CE2 . TYR A 1 27 ? 0.857 22.372 4.508 1.00 7.03 ? 27 TYR A CE2 1 ATOM 200 C CZ . TYR A 1 27 ? 1.270 22.029 3.235 1.00 6.47 ? 27 TYR A CZ 1 ATOM 201 O OH . TYR A 1 27 ? 0.604 20.962 2.607 1.00 6.88 ? 27 TYR A OH 1 ATOM 202 N N . TRP A 1 28 ? 1.259 26.380 2.937 1.00 6.50 ? 28 TRP A N 1 ATOM 203 C CA . TRP A 1 28 ? 0.865 26.283 1.553 1.00 7.27 ? 28 TRP A CA 1 ATOM 204 C C . TRP A 1 28 ? 0.605 27.615 0.881 1.00 8.73 ? 28 TRP A C 1 ATOM 205 O O . TRP A 1 28 ? 0.581 27.667 -0.341 1.00 9.32 ? 28 TRP A O 1 ATOM 206 C CB . TRP A 1 28 ? -0.331 25.326 1.397 1.00 7.41 ? 28 TRP A CB 1 ATOM 207 C CG . TRP A 1 28 ? -1.538 25.622 2.238 1.00 6.17 ? 28 TRP A CG 1 ATOM 208 C CD1 . TRP A 1 28 ? -1.880 25.061 3.447 1.00 5.62 ? 28 TRP A CD1 1 ATOM 209 C CD2 . TRP A 1 28 ? -2.581 26.573 1.954 1.00 6.99 ? 28 TRP A CD2 1 ATOM 210 N NE1 . TRP A 1 28 ? -3.054 25.610 3.914 1.00 6.02 ? 28 TRP A NE1 1 ATOM 211 C CE2 . TRP A 1 28 ? -3.502 26.536 3.011 1.00 7.21 ? 28 TRP A CE2 1 ATOM 212 C CE3 . TRP A 1 28 ? -2.827 27.449 0.897 1.00 7.30 ? 28 TRP A CE3 1 ATOM 213 C CZ2 . TRP A 1 28 ? -4.635 27.344 3.033 1.00 8.05 ? 28 TRP A CZ2 1 ATOM 214 C CZ3 . TRP A 1 28 ? -3.938 28.276 0.938 1.00 6.70 ? 28 TRP A CZ3 1 ATOM 215 C CH2 . TRP A 1 28 ? -4.849 28.221 2.001 1.00 6.93 ? 28 TRP A CH2 1 ATOM 216 N N . CYS A 1 29 ? 0.436 28.703 1.628 1.00 7.84 ? 29 CYS A N 1 ATOM 217 C CA . CYS A 1 29 ? 0.222 30.043 1.092 1.00 8.40 ? 29 CYS A CA 1 ATOM 218 C C . CYS A 1 29 ? 1.411 30.501 0.253 1.00 9.27 ? 29 CYS A C 1 ATOM 219 O O . CYS A 1 29 ? 1.254 31.375 -0.635 1.00 8.92 ? 29 CYS A O 1 ATOM 220 C CB . CYS A 1 29 ? -0.101 30.975 2.260 1.00 8.09 ? 29 CYS A CB 1 ATOM 221 S SG . CYS A 1 29 ? -1.776 31.076 2.970 1.00 7.53 ? 29 CYS A SG 1 ATOM 222 N N . SER A 1 30 ? 2.615 29.949 0.454 1.00 8.19 ? 30 SER A N 1 ATOM 223 C CA . SER A 1 30 ? 3.833 30.282 -0.246 1.00 8.64 ? 30 SER A CA 1 ATOM 224 C C . SER A 1 30 ? 3.984 29.705 -1.638 1.00 8.89 ? 30 SER A C 1 ATOM 225 O O . SER A 1 30 ? 4.928 30.050 -2.351 1.00 8.50 ? 30 SER A O 1 ATOM 226 C CB . SER A 1 30 ? 5.062 29.794 0.591 1.00 9.33 ? 30 SER A CB 1 ATOM 227 O OG . SER A 1 30 ? 5.079 30.492 1.840 1.00 7.54 ? 30 SER A OG 1 ATOM 228 N N . PHE A 1 31 ? 3.188 28.716 -2.015 1.00 8.77 ? 31 PHE A N 1 ATOM 229 C CA . PHE A 1 31 ? 3.287 27.958 -3.253 1.00 9.53 ? 31 PHE A CA 1 ATOM 230 C C . PHE A 1 31 ? 2.055 28.095 -4.139 1.00 11.35 ? 31 PHE A C 1 ATOM 231 O O . PHE A 1 31 ? 1.559 27.091 -4.685 1.00 12.50 ? 31 PHE A O 1 ATOM 232 C CB . PHE A 1 31 ? 3.602 26.476 -2.903 1.00 9.34 ? 31 PHE A CB 1 ATOM 233 C CG . PHE A 1 31 ? 4.677 26.194 -1.873 1.00 7.73 ? 31 PHE A CG 1 ATOM 234 C CD1 . PHE A 1 31 ? 5.862 26.887 -1.787 1.00 8.29 ? 31 PHE A CD1 1 ATOM 235 C CD2 . PHE A 1 31 ? 4.495 25.177 -0.925 1.00 6.99 ? 31 PHE A CD2 1 ATOM 236 C CE1 . PHE A 1 31 ? 6.821 26.617 -0.831 1.00 7.76 ? 31 PHE A CE1 1 ATOM 237 C CE2 . PHE A 1 31 ? 5.424 24.877 0.042 1.00 7.02 ? 31 PHE A CE2 1 ATOM 238 C CZ . PHE A 1 31 ? 6.597 25.617 0.111 1.00 7.27 ? 31 PHE A CZ 1 ATOM 239 N N . LEU A 1 32 ? 1.591 29.314 -4.369 1.00 9.86 ? 32 LEU A N 1 ATOM 240 C CA . LEU A 1 32 ? 0.446 29.618 -5.236 1.00 11.60 ? 32 LEU A CA 1 ATOM 241 C C . LEU A 1 32 ? 0.896 30.390 -6.472 1.00 13.19 ? 32 LEU A C 1 ATOM 242 O O . LEU A 1 32 ? 1.596 31.407 -6.357 1.00 15.06 ? 32 LEU A O 1 ATOM 243 C CB . LEU A 1 32 ? -0.665 30.320 -4.414 1.00 9.74 ? 32 LEU A CB 1 ATOM 244 C CG . LEU A 1 32 ? -1.281 29.509 -3.270 1.00 10.54 ? 32 LEU A CG 1 ATOM 245 C CD1 . LEU A 1 32 ? -2.082 30.367 -2.304 1.00 9.57 ? 32 LEU A CD1 1 ATOM 246 C CD2 . LEU A 1 32 ? -2.177 28.362 -3.733 1.00 11.54 ? 32 LEU A CD2 1 ATOM 247 N N . THR A 1 33 ? 0.550 29.950 -7.681 1.00 12.51 ? 33 THR A N 1 ATOM 248 C CA . THR A 1 33 ? 0.938 30.593 -8.921 1.00 13.36 ? 33 THR A CA 1 ATOM 249 C C . THR A 1 33 ? 0.004 31.730 -9.350 1.00 14.15 ? 33 THR A C 1 ATOM 250 O O . THR A 1 33 ? 0.429 32.522 -10.197 1.00 16.59 ? 33 THR A O 1 ATOM 251 C CB . THR A 1 33 ? 1.112 29.610 -10.095 1.00 13.94 ? 33 THR A CB 1 ATOM 252 O OG1 . THR A 1 33 ? -0.093 28.880 -10.331 1.00 14.27 ? 33 THR A OG1 1 ATOM 253 C CG2 . THR A 1 33 ? 2.240 28.612 -9.829 1.00 13.21 ? 33 THR A CG2 1 ATOM 254 N N . ASN A 1 34 ? -1.186 31.842 -8.812 1.00 12.09 ? 34 ASN A N 1 ATOM 255 C CA . ASN A 1 34 ? -2.114 32.968 -9.082 1.00 12.03 ? 34 ASN A CA 1 ATOM 256 C C . ASN A 1 34 ? -2.178 33.829 -7.811 1.00 10.93 ? 34 ASN A C 1 ATOM 257 O O . ASN A 1 34 ? -2.710 33.384 -6.778 1.00 9.69 ? 34 ASN A O 1 ATOM 258 C CB . ASN A 1 34 ? -3.500 32.464 -9.421 1.00 13.50 ? 34 ASN A CB 1 ATOM 259 C CG . ASN A 1 34 ? -4.546 33.548 -9.687 1.00 14.47 ? 34 ASN A CG 1 ATOM 260 O OD1 . ASN A 1 34 ? -4.301 34.755 -9.627 1.00 13.65 ? 34 ASN A OD1 1 ATOM 261 N ND2 . ASN A 1 34 ? -5.755 33.076 -9.991 1.00 15.51 ? 34 ASN A ND2 1 ATOM 262 N N . HIS A 1 35 ? -1.737 35.081 -7.875 1.00 9.12 ? 35 HIS A N 1 ATOM 263 C CA . HIS A 1 35 ? -1.722 35.911 -6.675 1.00 9.87 ? 35 HIS A CA 1 ATOM 264 C C . HIS A 1 35 ? -3.122 36.188 -6.130 1.00 9.63 ? 35 HIS A C 1 ATOM 265 O O . HIS A 1 35 ? -3.252 36.411 -4.919 1.00 9.03 ? 35 HIS A O 1 ATOM 266 C CB . HIS A 1 35 ? -0.964 37.218 -6.860 1.00 10.84 ? 35 HIS A CB 1 ATOM 267 C CG . HIS A 1 35 ? -1.766 38.291 -7.559 1.00 11.05 ? 35 HIS A CG 1 ATOM 268 N ND1 . HIS A 1 35 ? -2.649 39.143 -6.914 1.00 9.94 ? 35 HIS A ND1 1 ATOM 269 C CD2 . HIS A 1 35 ? -1.762 38.584 -8.864 1.00 12.31 ? 35 HIS A CD2 1 ATOM 270 C CE1 . HIS A 1 35 ? -3.222 39.922 -7.808 1.00 11.67 ? 35 HIS A CE1 1 ATOM 271 N NE2 . HIS A 1 35 ? -2.667 39.595 -8.949 1.00 10.58 ? 35 HIS A NE2 1 ATOM 272 N N . ALA A 1 36 ? -4.168 36.091 -6.950 1.00 8.94 ? 36 ALA A N 1 ATOM 273 C CA . ALA A 1 36 ? -5.522 36.311 -6.458 1.00 10.48 ? 36 ALA A CA 1 ATOM 274 C C . ALA A 1 36 ? -5.940 35.253 -5.428 1.00 10.02 ? 36 ALA A C 1 ATOM 275 O O . ALA A 1 36 ? -6.786 35.581 -4.603 1.00 9.30 ? 36 ALA A O 1 ATOM 276 C CB . ALA A 1 36 ? -6.536 36.298 -7.575 1.00 11.97 ? 36 ALA A CB 1 ATOM 277 N N . ASP A 1 37 ? -5.390 34.047 -5.460 1.00 9.64 ? 37 ASP A N 1 ATOM 278 C CA . ASP A 1 37 ? -5.660 32.994 -4.506 1.00 8.11 ? 37 ASP A CA 1 ATOM 279 C C . ASP A 1 37 ? -5.012 33.272 -3.142 1.00 9.08 ? 37 ASP A C 1 ATOM 280 O O . ASP A 1 37 ? -5.607 32.987 -2.079 1.00 7.50 ? 37 ASP A O 1 ATOM 281 C CB . ASP A 1 37 ? -5.188 31.639 -5.080 1.00 9.20 ? 37 ASP A CB 1 ATOM 282 C CG . ASP A 1 37 ? -5.994 31.134 -6.261 1.00 11.06 ? 37 ASP A CG 1 ATOM 283 O OD1 . ASP A 1 37 ? -7.119 31.605 -6.524 1.00 11.77 ? 37 ASP A OD1 1 ATOM 284 O OD2 . ASP A 1 37 ? -5.495 30.199 -6.944 1.00 12.98 ? 37 ASP A OD2 1 ATOM 285 N N . VAL A 1 38 ? -3.838 33.904 -3.091 1.00 8.05 ? 38 VAL A N 1 ATOM 286 C CA . VAL A 1 38 ? -3.205 34.380 -1.878 1.00 8.95 ? 38 VAL A CA 1 ATOM 287 C C . VAL A 1 38 ? -4.066 35.501 -1.260 1.00 8.51 ? 38 VAL A C 1 ATOM 288 O O . VAL A 1 38 ? -4.406 35.532 -0.063 1.00 6.53 ? 38 VAL A O 1 ATOM 289 C CB . VAL A 1 38 ? -1.769 34.924 -2.076 1.00 9.99 ? 38 VAL A CB 1 ATOM 290 C CG1 . VAL A 1 38 ? -1.177 35.379 -0.745 1.00 11.76 ? 38 VAL A CG1 1 ATOM 291 C CG2 . VAL A 1 38 ? -0.837 33.926 -2.769 1.00 11.25 ? 38 VAL A CG2 1 ATOM 292 N N . ASP A 1 39 ? -4.498 36.442 -2.091 1.00 8.31 ? 39 ASP A N 1 ATOM 293 C CA . ASP A 1 39 ? -5.292 37.605 -1.684 1.00 9.24 ? 39 ASP A CA 1 ATOM 294 C C . ASP A 1 39 ? -6.672 37.265 -1.118 1.00 9.22 ? 39 ASP A C 1 ATOM 295 O O . ASP A 1 39 ? -7.067 37.878 -0.102 1.00 8.90 ? 39 ASP A O 1 ATOM 296 C CB . ASP A 1 39 ? -5.371 38.641 -2.818 1.00 9.24 ? 39 ASP A CB 1 ATOM 297 C CG . ASP A 1 39 ? -4.059 39.274 -3.252 1.00 11.38 ? 39 ASP A CG 1 ATOM 298 O OD1 . ASP A 1 39 ? -3.059 39.320 -2.492 1.00 12.30 ? 39 ASP A OD1 1 ATOM 299 O OD2 . ASP A 1 39 ? -3.981 39.685 -4.439 1.00 10.72 ? 39 ASP A OD2 1 ATOM 300 N N . SER A 1 40 ? -7.401 36.301 -1.678 1.00 7.85 ? 40 SER A N 1 ATOM 301 C CA . SER A 1 40 ? -8.707 35.905 -1.133 1.00 7.57 ? 40 SER A CA 1 ATOM 302 C C . SER A 1 40 ? -8.524 35.239 0.230 1.00 7.40 ? 40 SER A C 1 ATOM 303 O O . SER A 1 40 ? -9.259 35.533 1.174 1.00 7.26 ? 40 SER A O 1 ATOM 304 C CB . SER A 1 40 ? -9.513 35.045 -2.096 1.00 8.23 ? 40 SER A CB 1 ATOM 305 O OG . SER A 1 40 ? -8.874 33.863 -2.502 1.00 7.77 ? 40 SER A OG 1 ATOM 306 N N . THR A 1 41 ? -7.491 34.421 0.372 1.00 7.03 ? 41 THR A N 1 ATOM 307 C CA . THR A 1 41 ? -7.185 33.756 1.654 1.00 6.73 ? 41 THR A CA 1 ATOM 308 C C . THR A 1 41 ? -6.823 34.774 2.740 1.00 8.08 ? 41 THR A C 1 ATOM 309 O O . THR A 1 41 ? -7.336 34.747 3.867 1.00 5.89 ? 41 THR A O 1 ATOM 310 C CB . THR A 1 41 ? -6.070 32.707 1.445 1.00 6.95 ? 41 THR A CB 1 ATOM 311 O OG1 . THR A 1 41 ? -6.458 31.758 0.431 1.00 6.76 ? 41 THR A OG1 1 ATOM 312 C CG2 . THR A 1 41 ? -5.820 31.926 2.720 1.00 5.93 ? 41 THR A CG2 1 ATOM 313 N N . PHE A 1 42 ? -5.933 35.726 2.446 1.00 7.82 ? 42 PHE A N 1 ATOM 314 C CA . PHE A 1 42 ? -5.559 36.781 3.403 1.00 7.82 ? 42 PHE A CA 1 ATOM 315 C C . PHE A 1 42 ? -6.679 37.751 3.742 1.00 7.77 ? 42 PHE A C 1 ATOM 316 O O . PHE A 1 42 ? -6.761 38.249 4.886 1.00 6.53 ? 42 PHE A O 1 ATOM 317 C CB . PHE A 1 42 ? -4.267 37.434 2.943 1.00 8.33 ? 42 PHE A CB 1 ATOM 318 C CG . PHE A 1 42 ? -2.971 36.725 3.287 1.00 9.60 ? 42 PHE A CG 1 ATOM 319 C CD1 . PHE A 1 42 ? -2.934 35.383 3.638 1.00 9.28 ? 42 PHE A CD1 1 ATOM 320 C CD2 . PHE A 1 42 ? -1.785 37.430 3.248 1.00 9.71 ? 42 PHE A CD2 1 ATOM 321 C CE1 . PHE A 1 42 ? -1.718 34.768 3.971 1.00 9.53 ? 42 PHE A CE1 1 ATOM 322 C CE2 . PHE A 1 42 ? -0.577 36.829 3.568 1.00 11.44 ? 42 PHE A CE2 1 ATOM 323 C CZ . PHE A 1 42 ? -0.542 35.480 3.917 1.00 10.90 ? 42 PHE A CZ 1 ATOM 324 N N . SER A 1 43 ? -7.617 38.016 2.816 1.00 6.93 ? 43 SER A N 1 ATOM 325 C CA . SER A 1 43 ? -8.818 38.786 3.108 1.00 8.08 ? 43 SER A CA 1 ATOM 326 C C . SER A 1 43 ? -9.634 38.112 4.218 1.00 7.49 ? 43 SER A C 1 ATOM 327 O O . SER A 1 43 ? -10.111 38.761 5.156 1.00 7.09 ? 43 SER A O 1 ATOM 328 C CB . SER A 1 43 ? -9.704 38.905 1.872 1.00 8.38 ? 43 SER A CB 1 ATOM 329 O OG A SER A 1 43 ? -9.125 39.744 0.886 0.50 8.21 ? 43 SER A OG 1 ATOM 330 O OG B SER A 1 43 ? -10.823 39.733 2.139 0.50 9.81 ? 43 SER A OG 1 ATOM 331 N N . HIS A 1 44 ? -9.814 36.788 4.134 1.00 7.57 ? 44 HIS A N 1 ATOM 332 C CA . HIS A 1 44 ? -10.534 36.005 5.141 1.00 8.28 ? 44 HIS A CA 1 ATOM 333 C C . HIS A 1 44 ? -9.855 35.953 6.516 1.00 8.25 ? 44 HIS A C 1 ATOM 334 O O . HIS A 1 44 ? -10.479 36.039 7.593 1.00 7.78 ? 44 HIS A O 1 ATOM 335 C CB . HIS A 1 44 ? -10.799 34.555 4.671 1.00 7.69 ? 44 HIS A CB 1 ATOM 336 C CG . HIS A 1 44 ? -11.513 34.418 3.349 1.00 9.32 ? 44 HIS A CG 1 ATOM 337 N ND1 . HIS A 1 44 ? -11.442 33.355 2.472 1.00 8.59 ? 44 HIS A ND1 1 ATOM 338 C CD2 . HIS A 1 44 ? -12.293 35.372 2.784 1.00 10.78 ? 44 HIS A CD2 1 ATOM 339 C CE1 . HIS A 1 44 ? -12.228 33.658 1.399 1.00 9.77 ? 44 HIS A CE1 1 ATOM 340 N NE2 . HIS A 1 44 ? -12.737 34.871 1.586 1.00 10.28 ? 44 HIS A NE2 1 ATOM 341 N N . ILE A 1 45 ? -8.521 35.751 6.533 1.00 7.03 ? 45 ILE A N 1 ATOM 342 C CA . ILE A 1 45 ? -7.770 35.763 7.800 1.00 6.70 ? 45 ILE A CA 1 ATOM 343 C C . ILE A 1 45 ? -7.899 37.122 8.479 1.00 8.22 ? 45 ILE A C 1 ATOM 344 O O . ILE A 1 45 ? -8.130 37.190 9.686 1.00 7.58 ? 45 ILE A O 1 ATOM 345 C CB . ILE A 1 45 ? -6.285 35.380 7.508 1.00 6.50 ? 45 ILE A CB 1 ATOM 346 C CG1 . ILE A 1 45 ? -6.197 33.914 7.060 1.00 6.24 ? 45 ILE A CG1 1 ATOM 347 C CG2 . ILE A 1 45 ? -5.330 35.651 8.682 1.00 7.44 ? 45 ILE A CG2 1 ATOM 348 C CD1 . ILE A 1 45 ? -4.812 33.359 6.713 1.00 6.34 ? 45 ILE A CD1 1 ATOM 349 N N . SER A 1 46 ? -7.757 38.238 7.753 1.00 7.47 ? 46 SER A N 1 ATOM 350 C CA . SER A 1 46 ? -7.856 39.591 8.316 1.00 8.90 ? 46 SER A CA 1 ATOM 351 C C . SER A 1 46 ? -9.256 39.924 8.811 1.00 9.89 ? 46 SER A C 1 ATOM 352 O O . SER A 1 46 ? -9.452 40.436 9.929 1.00 9.22 ? 46 SER A O 1 ATOM 353 C CB . SER A 1 46 ? -7.365 40.633 7.296 1.00 11.12 ? 46 SER A CB 1 ATOM 354 O OG . SER A 1 46 ? -7.579 41.992 7.725 1.00 11.55 ? 46 SER A OG 1 ATOM 355 N N . SER A 1 47 ? -10.294 39.587 8.067 1.00 10.15 ? 47 SER A N 1 ATOM 356 C CA . SER A 1 47 ? -11.654 39.896 8.539 1.00 11.63 ? 47 SER A CA 1 ATOM 357 C C . SER A 1 47 ? -12.020 39.045 9.741 1.00 11.01 ? 47 SER A C 1 ATOM 358 O O . SER A 1 47 ? -12.921 39.431 10.501 1.00 11.52 ? 47 SER A O 1 ATOM 359 C CB . SER A 1 47 ? -12.656 39.840 7.397 1.00 13.25 ? 47 SER A CB 1 ATOM 360 O OG . SER A 1 47 ? -12.813 38.532 6.930 1.00 13.41 ? 47 SER A OG 1 ATOM 361 N N . SER A 1 48 ? -11.371 37.897 9.967 1.00 9.44 ? 48 SER A N 1 ATOM 362 C CA . SER A 1 48 ? -11.573 37.042 11.126 1.00 8.62 ? 48 SER A CA 1 ATOM 363 C C . SER A 1 48 ? -10.959 37.677 12.395 1.00 9.18 ? 48 SER A C 1 ATOM 364 O O . SER A 1 48 ? -11.222 37.241 13.515 1.00 9.74 ? 48 SER A O 1 ATOM 365 C CB . SER A 1 48 ? -11.004 35.646 10.878 1.00 9.78 ? 48 SER A CB 1 ATOM 366 O OG . SER A 1 48 ? -11.634 34.850 9.866 1.00 8.50 ? 48 SER A OG 1 ATOM 367 N N . GLY A 1 49 ? -10.114 38.673 12.306 1.00 8.81 ? 49 GLY A N 1 ATOM 368 C CA . GLY A 1 49 ? -9.461 39.333 13.419 1.00 9.51 ? 49 GLY A CA 1 ATOM 369 C C . GLY A 1 49 ? -8.084 38.799 13.806 1.00 9.98 ? 49 GLY A C 1 ATOM 370 O O . GLY A 1 49 ? -7.546 39.193 14.848 1.00 9.94 ? 49 GLY A O 1 ATOM 371 N N . LEU A 1 50 ? -7.510 37.903 13.038 1.00 8.79 ? 50 LEU A N 1 ATOM 372 C CA . LEU A 1 50 ? -6.166 37.339 13.248 1.00 9.04 ? 50 LEU A CA 1 ATOM 373 C C . LEU A 1 50 ? -5.095 38.338 12.804 1.00 10.12 ? 50 LEU A C 1 ATOM 374 O O . LEU A 1 50 ? -5.380 39.078 11.853 1.00 10.03 ? 50 LEU A O 1 ATOM 375 C CB . LEU A 1 50 ? -6.025 35.994 12.549 1.00 8.95 ? 50 LEU A CB 1 ATOM 376 C CG . LEU A 1 50 ? -6.887 34.848 13.046 1.00 9.22 ? 50 LEU A CG 1 ATOM 377 C CD1 . LEU A 1 50 ? -6.666 33.556 12.239 1.00 9.31 ? 50 LEU A CD1 1 ATOM 378 C CD2 . LEU A 1 50 ? -6.677 34.501 14.508 1.00 9.17 ? 50 LEU A CD2 1 ATOM 379 N N . LYS A 1 51 ? -3.897 38.393 13.421 1.00 9.71 ? 51 LYS A N 1 ATOM 380 C CA . LYS A 1 51 ? -2.909 39.410 13.062 1.00 9.49 ? 51 LYS A CA 1 ATOM 381 C C . LYS A 1 51 ? -1.610 38.879 12.461 1.00 9.15 ? 51 LYS A C 1 ATOM 382 O O . LYS A 1 51 ? -0.809 39.653 11.864 1.00 7.83 ? 51 LYS A O 1 ATOM 383 C CB . LYS A 1 51 ? -2.575 40.265 14.333 1.00 10.07 ? 51 LYS A CB 1 ATOM 384 C CG . LYS A 1 51 ? -3.650 41.235 14.808 1.00 13.32 ? 51 LYS A CG 1 ATOM 385 C CD . LYS A 1 51 ? -3.221 42.281 15.849 1.00 14.31 ? 51 LYS A CD 1 ATOM 386 C CE . LYS A 1 51 ? -4.352 43.217 16.248 1.00 15.94 ? 51 LYS A CE 1 ATOM 387 N NZ . LYS A 1 51 ? -3.975 44.305 17.208 1.00 16.63 ? 51 LYS A NZ 1 ATOM 388 N N . VAL A 1 52 ? -1.310 37.579 12.639 1.00 7.02 ? 52 VAL A N 1 ATOM 389 C CA . VAL A 1 52 ? -0.052 36.976 12.206 1.00 7.82 ? 52 VAL A CA 1 ATOM 390 C C . VAL A 1 52 ? -0.240 35.626 11.513 1.00 7.77 ? 52 VAL A C 1 ATOM 391 O O . VAL A 1 52 ? -1.137 34.837 11.896 1.00 6.80 ? 52 VAL A O 1 ATOM 392 C CB . VAL A 1 52 ? 0.867 36.758 13.455 1.00 8.57 ? 52 VAL A CB 1 ATOM 393 C CG1 . VAL A 1 52 ? 2.207 36.140 13.129 1.00 8.69 ? 52 VAL A CG1 1 ATOM 394 C CG2 . VAL A 1 52 ? 1.128 38.065 14.230 1.00 8.61 ? 52 VAL A CG2 1 ATOM 395 N N . VAL A 1 53 ? 0.524 35.338 10.479 1.00 7.21 ? 53 VAL A N 1 ATOM 396 C CA . VAL A 1 53 ? 0.517 34.087 9.714 1.00 7.17 ? 53 VAL A CA 1 ATOM 397 C C . VAL A 1 53 ? 1.938 33.504 9.567 1.00 8.24 ? 53 VAL A C 1 ATOM 398 O O . VAL A 1 53 ? 2.879 34.259 9.286 1.00 7.62 ? 53 VAL A O 1 ATOM 399 C CB . VAL A 1 53 ? -0.087 34.270 8.290 1.00 7.06 ? 53 VAL A CB 1 ATOM 400 C CG1 . VAL A 1 53 ? -0.378 32.983 7.528 1.00 7.59 ? 53 VAL A CG1 1 ATOM 401 C CG2 . VAL A 1 53 ? -1.346 35.145 8.272 1.00 7.66 ? 53 VAL A CG2 1 ATOM 402 N N . ARG A 1 54 ? 2.120 32.198 9.782 1.00 6.18 ? 54 ARG A N 1 ATOM 403 C CA . ARG A 1 54 ? 3.394 31.467 9.619 1.00 5.96 ? 54 ARG A CA 1 ATOM 404 C C . ARG A 1 54 ? 3.384 30.787 8.249 1.00 5.97 ? 54 ARG A C 1 ATOM 405 O O . ARG A 1 54 ? 2.438 30.016 7.975 1.00 6.23 ? 54 ARG A O 1 ATOM 406 C CB . ARG A 1 54 ? 3.638 30.491 10.789 1.00 5.29 ? 54 ARG A CB 1 ATOM 407 C CG . ARG A 1 54 ? 4.957 29.680 10.756 1.00 5.10 ? 54 ARG A CG 1 ATOM 408 C CD . ARG A 1 54 ? 5.391 29.208 12.136 1.00 6.71 ? 54 ARG A CD 1 ATOM 409 N NE . ARG A 1 54 ? 6.536 28.303 12.244 1.00 5.93 ? 54 ARG A NE 1 ATOM 410 C CZ . ARG A 1 54 ? 6.483 26.980 12.254 1.00 6.93 ? 54 ARG A CZ 1 ATOM 411 N NH1 . ARG A 1 54 ? 5.332 26.303 12.129 1.00 5.85 ? 54 ARG A NH1 1 ATOM 412 N NH2 . ARG A 1 54 ? 7.604 26.249 12.386 1.00 7.29 ? 54 ARG A NH2 1 ATOM 413 N N . VAL A 1 55 ? 4.381 31.026 7.370 1.00 4.89 ? 55 VAL A N 1 ATOM 414 C CA . VAL A 1 55 ? 4.409 30.518 6.003 1.00 5.70 ? 55 VAL A CA 1 ATOM 415 C C . VAL A 1 55 ? 5.802 29.970 5.655 1.00 6.97 ? 55 VAL A C 1 ATOM 416 O O . VAL A 1 55 ? 6.769 30.416 6.308 1.00 7.60 ? 55 VAL A O 1 ATOM 417 C CB . VAL A 1 55 ? 4.036 31.573 4.936 1.00 5.65 ? 55 VAL A CB 1 ATOM 418 C CG1 . VAL A 1 55 ? 2.651 32.199 5.161 1.00 7.23 ? 55 VAL A CG1 1 ATOM 419 C CG2 . VAL A 1 55 ? 5.048 32.734 4.846 1.00 6.61 ? 55 VAL A CG2 1 ATOM 420 N N . TRP A 1 56 ? 5.953 29.017 4.751 1.00 5.99 ? 56 TRP A N 1 ATOM 421 C CA . TRP A 1 56 ? 7.297 28.450 4.497 1.00 5.83 ? 56 TRP A CA 1 ATOM 422 C C . TRP A 1 56 ? 8.180 29.410 3.688 1.00 7.97 ? 56 TRP A C 1 ATOM 423 O O . TRP A 1 56 ? 7.745 29.987 2.699 1.00 7.56 ? 56 TRP A O 1 ATOM 424 C CB . TRP A 1 56 ? 7.224 27.053 3.842 1.00 5.23 ? 56 TRP A CB 1 ATOM 425 C CG . TRP A 1 56 ? 6.864 25.831 4.643 1.00 5.78 ? 56 TRP A CG 1 ATOM 426 C CD1 . TRP A 1 56 ? 6.684 24.568 4.118 1.00 6.61 ? 56 TRP A CD1 1 ATOM 427 C CD2 . TRP A 1 56 ? 6.644 25.694 6.057 1.00 6.29 ? 56 TRP A CD2 1 ATOM 428 N NE1 . TRP A 1 56 ? 6.381 23.669 5.129 1.00 6.09 ? 56 TRP A NE1 1 ATOM 429 C CE2 . TRP A 1 56 ? 6.356 24.341 6.319 1.00 5.47 ? 56 TRP A CE2 1 ATOM 430 C CE3 . TRP A 1 56 ? 6.625 26.581 7.127 1.00 5.69 ? 56 TRP A CE3 1 ATOM 431 C CZ2 . TRP A 1 56 ? 6.119 23.857 7.606 1.00 5.09 ? 56 TRP A CZ2 1 ATOM 432 C CZ3 . TRP A 1 56 ? 6.357 26.128 8.412 1.00 6.53 ? 56 TRP A CZ3 1 ATOM 433 C CH2 . TRP A 1 56 ? 6.127 24.754 8.645 1.00 5.45 ? 56 TRP A CH2 1 ATOM 434 N N . GLY A 1 57 ? 9.456 29.537 4.067 1.00 6.96 ? 57 GLY A N 1 ATOM 435 C CA . GLY A 1 57 ? 10.447 30.300 3.314 1.00 6.99 ? 57 GLY A CA 1 ATOM 436 C C . GLY A 1 57 ? 11.400 29.450 2.490 1.00 8.44 ? 57 GLY A C 1 ATOM 437 O O . GLY A 1 57 ? 12.431 29.996 2.049 1.00 7.89 ? 57 GLY A O 1 ATOM 438 N N . PHE A 1 58 ? 11.100 28.173 2.259 1.00 7.04 ? 58 PHE A N 1 ATOM 439 C CA . PHE A 1 58 ? 11.886 27.171 1.564 1.00 6.33 ? 58 PHE A CA 1 ATOM 440 C C . PHE A 1 58 ? 11.094 26.267 0.621 1.00 8.05 ? 58 PHE A C 1 ATOM 441 O O . PHE A 1 58 ? 9.880 26.085 0.818 1.00 6.80 ? 58 PHE A O 1 ATOM 442 C CB . PHE A 1 58 ? 12.565 26.209 2.605 1.00 7.07 ? 58 PHE A CB 1 ATOM 443 C CG . PHE A 1 58 ? 11.651 25.541 3.605 1.00 7.12 ? 58 PHE A CG 1 ATOM 444 C CD1 . PHE A 1 58 ? 10.988 24.359 3.269 1.00 6.88 ? 58 PHE A CD1 1 ATOM 445 C CD2 . PHE A 1 58 ? 11.416 26.035 4.871 1.00 6.39 ? 58 PHE A CD2 1 ATOM 446 C CE1 . PHE A 1 58 ? 10.122 23.715 4.133 1.00 6.15 ? 58 PHE A CE1 1 ATOM 447 C CE2 . PHE A 1 58 ? 10.564 25.397 5.763 1.00 6.18 ? 58 PHE A CE2 1 ATOM 448 C CZ . PHE A 1 58 ? 9.901 24.232 5.406 1.00 6.43 ? 58 PHE A CZ 1 ATOM 449 N N . ASN A 1 59 ? 11.782 25.694 -0.384 1.00 6.78 ? 59 ASN A N 1 ATOM 450 C CA . ASN A 1 59 ? 11.238 24.676 -1.290 1.00 8.37 ? 59 ASN A CA 1 ATOM 451 C C . ASN A 1 59 ? 12.471 24.086 -2.001 1.00 8.87 ? 59 ASN A C 1 ATOM 452 O O . ASN A 1 59 ? 12.888 24.541 -3.067 1.00 8.39 ? 59 ASN A O 1 ATOM 453 C CB . ASN A 1 59 ? 10.137 25.168 -2.215 1.00 7.58 ? 59 ASN A CB 1 ATOM 454 C CG . ASN A 1 59 ? 9.324 24.087 -2.887 1.00 10.16 ? 59 ASN A CG 1 ATOM 455 O OD1 . ASN A 1 59 ? 9.853 23.012 -3.126 1.00 12.16 ? 59 ASN A OD1 1 ATOM 456 N ND2 . ASN A 1 59 ? 8.043 24.259 -3.224 1.00 10.20 ? 59 ASN A ND2 1 ATOM 457 N N . ASP A 1 60 ? 13.108 23.115 -1.350 1.00 8.12 ? 60 ASP A N 1 ATOM 458 C CA . ASP A 1 60 ? 14.362 22.491 -1.756 1.00 7.62 ? 60 ASP A CA 1 ATOM 459 C C . ASP A 1 60 ? 14.245 21.194 -2.549 1.00 8.55 ? 60 ASP A C 1 ATOM 460 O O . ASP A 1 60 ? 13.445 20.322 -2.200 1.00 7.66 ? 60 ASP A O 1 ATOM 461 C CB . ASP A 1 60 ? 15.185 22.243 -0.467 1.00 7.79 ? 60 ASP A CB 1 ATOM 462 C CG . ASP A 1 60 ? 15.686 23.481 0.256 1.00 9.19 ? 60 ASP A CG 1 ATOM 463 O OD1 . ASP A 1 60 ? 16.285 24.343 -0.434 1.00 10.04 ? 60 ASP A OD1 1 ATOM 464 O OD2 . ASP A 1 60 ? 15.516 23.582 1.498 1.00 8.20 ? 60 ASP A OD2 1 ATOM 465 N N . VAL A 1 61 ? 15.012 21.042 -3.639 1.00 8.17 ? 61 VAL A N 1 ATOM 466 C CA . VAL A 1 61 ? 15.023 19.880 -4.510 1.00 9.93 ? 61 VAL A CA 1 ATOM 467 C C . VAL A 1 61 ? 16.443 19.450 -4.876 1.00 10.71 ? 61 VAL A C 1 ATOM 468 O O . VAL A 1 61 ? 17.363 20.248 -4.759 1.00 9.98 ? 61 VAL A O 1 ATOM 469 C CB . VAL A 1 61 ? 14.256 20.135 -5.839 1.00 10.98 ? 61 VAL A CB 1 ATOM 470 C CG1 . VAL A 1 61 ? 12.823 20.613 -5.613 1.00 11.34 ? 61 VAL A CG1 1 ATOM 471 C CG2 . VAL A 1 61 ? 14.918 21.184 -6.751 1.00 8.69 ? 61 VAL A CG2 1 ATOM 472 N N . ASN A 1 62 ? 16.618 18.219 -5.373 1.00 11.97 ? 62 ASN A N 1 ATOM 473 C CA . ASN A 1 62 ? 17.902 17.748 -5.894 1.00 13.30 ? 62 ASN A CA 1 ATOM 474 C C . ASN A 1 62 ? 17.813 17.649 -7.432 1.00 15.76 ? 62 ASN A C 1 ATOM 475 O O . ASN A 1 62 ? 18.851 17.663 -8.105 1.00 16.47 ? 62 ASN A O 1 ATOM 476 C CB . ASN A 1 62 ? 18.400 16.465 -5.274 1.00 11.96 ? 62 ASN A CB 1 ATOM 477 C CG . ASN A 1 62 ? 18.747 16.566 -3.783 1.00 12.98 ? 62 ASN A CG 1 ATOM 478 O OD1 . ASN A 1 62 ? 18.089 15.833 -2.996 1.00 12.17 ? 62 ASN A OD1 1 ATOM 479 N ND2 . ASN A 1 62 ? 19.682 17.387 -3.370 1.00 11.77 ? 62 ASN A ND2 1 ATOM 480 N N . THR A 1 63 ? 16.599 17.597 -7.955 1.00 16.44 ? 63 THR A N 1 ATOM 481 C CA . THR A 1 63 ? 16.314 17.584 -9.400 1.00 19.18 ? 63 THR A CA 1 ATOM 482 C C . THR A 1 63 ? 15.119 18.522 -9.650 1.00 19.26 ? 63 THR A C 1 ATOM 483 O O . THR A 1 63 ? 14.159 18.552 -8.868 1.00 18.44 ? 63 THR A O 1 ATOM 484 C CB . THR A 1 63 ? 16.070 16.184 -9.965 1.00 21.52 ? 63 THR A CB 1 ATOM 485 O OG1 . THR A 1 63 ? 15.943 16.243 -11.409 1.00 23.90 ? 63 THR A OG1 1 ATOM 486 C CG2 . THR A 1 63 ? 14.776 15.543 -9.461 1.00 21.99 ? 63 THR A CG2 1 ATOM 487 N N . GLN A 1 64 ? 15.178 19.340 -10.699 1.00 19.47 ? 64 GLN A N 1 ATOM 488 C CA . GLN A 1 64 ? 14.094 20.268 -10.994 1.00 21.15 ? 64 GLN A CA 1 ATOM 489 C C . GLN A 1 64 ? 12.782 19.518 -11.252 1.00 21.02 ? 64 GLN A C 1 ATOM 490 O O . GLN A 1 64 ? 12.835 18.460 -11.873 1.00 21.98 ? 64 GLN A O 1 ATOM 491 C CB . GLN A 1 64 ? 14.367 21.098 -12.255 1.00 22.49 ? 64 GLN A CB 1 ATOM 492 C CG . GLN A 1 64 ? 15.241 22.313 -12.036 1.00 24.13 ? 64 GLN A CG 1 ATOM 493 C CD . GLN A 1 64 ? 15.399 23.150 -13.288 1.00 25.36 ? 64 GLN A CD 1 ATOM 494 O OE1 . GLN A 1 64 ? 14.430 23.559 -13.954 1.00 25.38 ? 64 GLN A OE1 1 ATOM 495 N NE2 . GLN A 1 64 ? 16.674 23.412 -13.551 1.00 26.04 ? 64 GLN A NE2 1 ATOM 496 N N . PRO A 1 65 ? 11.677 20.080 -10.822 1.00 19.86 ? 65 PRO A N 1 ATOM 497 C CA . PRO A 1 65 ? 10.356 19.498 -10.998 1.00 19.49 ? 65 PRO A CA 1 ATOM 498 C C . PRO A 1 65 ? 9.823 19.665 -12.416 1.00 19.78 ? 65 PRO A C 1 ATOM 499 O O . PRO A 1 65 ? 10.524 20.205 -13.269 1.00 17.56 ? 65 PRO A O 1 ATOM 500 C CB . PRO A 1 65 ? 9.497 20.245 -9.981 1.00 18.40 ? 65 PRO A CB 1 ATOM 501 C CG . PRO A 1 65 ? 10.139 21.601 -9.930 1.00 17.84 ? 65 PRO A CG 1 ATOM 502 C CD . PRO A 1 65 ? 11.619 21.350 -10.038 1.00 18.95 ? 65 PRO A CD 1 ATOM 503 N N . SER A 1 66 ? 8.632 19.101 -12.697 1.00 20.84 ? 66 SER A N 1 ATOM 504 C CA . SER A 1 66 ? 8.063 19.259 -14.042 1.00 23.38 ? 66 SER A CA 1 ATOM 505 C C . SER A 1 66 ? 7.944 20.752 -14.354 1.00 22.96 ? 66 SER A C 1 ATOM 506 O O . SER A 1 66 ? 7.586 21.542 -13.493 1.00 21.76 ? 66 SER A O 1 ATOM 507 C CB . SER A 1 66 ? 6.662 18.648 -14.147 1.00 24.82 ? 66 SER A CB 1 ATOM 508 O OG . SER A 1 66 ? 6.528 17.364 -13.565 1.00 26.16 ? 66 SER A OG 1 ATOM 509 N N . PRO A 1 67 ? 8.213 21.160 -15.589 1.00 23.08 ? 67 PRO A N 1 ATOM 510 C CA . PRO A 1 67 ? 8.075 22.537 -16.011 1.00 22.49 ? 67 PRO A CA 1 ATOM 511 C C . PRO A 1 67 ? 6.727 23.138 -15.638 1.00 20.58 ? 67 PRO A C 1 ATOM 512 O O . PRO A 1 67 ? 5.699 22.542 -15.977 1.00 19.67 ? 67 PRO A O 1 ATOM 513 C CB . PRO A 1 67 ? 8.253 22.403 -17.529 1.00 23.97 ? 67 PRO A CB 1 ATOM 514 C CG . PRO A 1 67 ? 9.208 21.268 -17.692 1.00 24.59 ? 67 PRO A CG 1 ATOM 515 C CD . PRO A 1 67 ? 8.703 20.266 -16.670 1.00 24.55 ? 67 PRO A CD 1 ATOM 516 N N . GLY A 1 68 ? 6.699 24.244 -14.913 1.00 17.50 ? 68 GLY A N 1 ATOM 517 C CA . GLY A 1 68 ? 5.514 24.921 -14.414 1.00 17.11 ? 68 GLY A CA 1 ATOM 518 C C . GLY A 1 68 ? 5.377 24.814 -12.897 1.00 15.25 ? 68 GLY A C 1 ATOM 519 O O . GLY A 1 68 ? 4.693 25.631 -12.267 1.00 16.29 ? 68 GLY A O 1 ATOM 520 N N . GLN A 1 69 ? 5.997 23.827 -12.294 1.00 13.78 ? 69 GLN A N 1 ATOM 521 C CA . GLN A 1 69 ? 5.958 23.558 -10.864 1.00 13.76 ? 69 GLN A CA 1 ATOM 522 C C . GLN A 1 69 ? 6.964 24.466 -10.146 1.00 13.85 ? 69 GLN A C 1 ATOM 523 O O . GLN A 1 69 ? 7.961 24.861 -10.737 1.00 13.50 ? 69 GLN A O 1 ATOM 524 C CB . GLN A 1 69 ? 6.195 22.092 -10.496 1.00 14.78 ? 69 GLN A CB 1 ATOM 525 C CG . GLN A 1 69 ? 5.115 21.114 -10.969 1.00 17.19 ? 69 GLN A CG 1 ATOM 526 C CD . GLN A 1 69 ? 3.699 21.483 -10.583 1.00 18.99 ? 69 GLN A CD 1 ATOM 527 O OE1 . GLN A 1 69 ? 3.318 21.689 -9.427 1.00 19.34 ? 69 GLN A OE1 1 ATOM 528 N NE2 . GLN A 1 69 ? 2.832 21.558 -11.588 1.00 20.11 ? 69 GLN A NE2 1 ATOM 529 N N . ILE A 1 70 ? 6.684 24.821 -8.903 1.00 12.30 ? 70 ILE A N 1 ATOM 530 C CA . ILE A 1 70 ? 7.507 25.756 -8.123 1.00 12.03 ? 70 ILE A CA 1 ATOM 531 C C . ILE A 1 70 ? 8.723 25.101 -7.466 1.00 12.33 ? 70 ILE A C 1 ATOM 532 O O . ILE A 1 70 ? 8.614 23.981 -6.968 1.00 12.13 ? 70 ILE A O 1 ATOM 533 C CB . ILE A 1 70 ? 6.610 26.390 -7.034 1.00 11.78 ? 70 ILE A CB 1 ATOM 534 C CG1 . ILE A 1 70 ? 5.474 27.188 -7.694 1.00 11.83 ? 70 ILE A CG1 1 ATOM 535 C CG2 . ILE A 1 70 ? 7.382 27.268 -6.047 1.00 11.76 ? 70 ILE A CG2 1 ATOM 536 C CD1 . ILE A 1 70 ? 4.334 27.587 -6.787 1.00 12.99 ? 70 ILE A CD1 1 ATOM 537 N N . TRP A 1 71 ? 9.860 25.805 -7.447 1.00 11.14 ? 71 TRP A N 1 ATOM 538 C CA . TRP A 1 71 ? 11.063 25.383 -6.727 1.00 10.63 ? 71 TRP A CA 1 ATOM 539 C C . TRP A 1 71 ? 11.888 26.592 -6.331 1.00 9.74 ? 71 TRP A C 1 ATOM 540 O O . TRP A 1 71 ? 11.990 27.514 -7.160 1.00 8.56 ? 71 TRP A O 1 ATOM 541 C CB . TRP A 1 71 ? 11.860 24.348 -7.551 1.00 11.76 ? 71 TRP A CB 1 ATOM 542 C CG . TRP A 1 71 ? 12.447 24.841 -8.841 1.00 13.00 ? 71 TRP A CG 1 ATOM 543 C CD1 . TRP A 1 71 ? 11.772 25.002 -10.036 1.00 12.60 ? 71 TRP A CD1 1 ATOM 544 C CD2 . TRP A 1 71 ? 13.802 25.250 -9.089 1.00 13.71 ? 71 TRP A CD2 1 ATOM 545 N NE1 . TRP A 1 71 ? 12.636 25.494 -10.986 1.00 13.01 ? 71 TRP A NE1 1 ATOM 546 C CE2 . TRP A 1 71 ? 13.870 25.658 -10.434 1.00 14.06 ? 71 TRP A CE2 1 ATOM 547 C CE3 . TRP A 1 71 ? 14.947 25.341 -8.289 1.00 13.58 ? 71 TRP A CE3 1 ATOM 548 C CZ2 . TRP A 1 71 ? 15.059 26.127 -11.013 1.00 14.94 ? 71 TRP A CZ2 1 ATOM 549 C CZ3 . TRP A 1 71 ? 16.120 25.802 -8.865 1.00 14.21 ? 71 TRP A CZ3 1 ATOM 550 C CH2 . TRP A 1 71 ? 16.167 26.202 -10.206 1.00 14.35 ? 71 TRP A CH2 1 ATOM 551 N N . PHE A 1 72 ? 12.380 26.708 -5.081 1.00 7.87 ? 72 PHE A N 1 ATOM 552 C CA . PHE A 1 72 ? 13.151 27.875 -4.653 1.00 8.61 ? 72 PHE A CA 1 ATOM 553 C C . PHE A 1 72 ? 14.671 27.642 -4.725 1.00 8.54 ? 72 PHE A C 1 ATOM 554 O O . PHE A 1 72 ? 15.458 28.578 -4.937 1.00 9.48 ? 72 PHE A O 1 ATOM 555 C CB . PHE A 1 72 ? 12.714 28.296 -3.233 1.00 8.64 ? 72 PHE A CB 1 ATOM 556 C CG . PHE A 1 72 ? 11.307 28.787 -2.979 1.00 9.17 ? 72 PHE A CG 1 ATOM 557 C CD1 . PHE A 1 72 ? 10.435 29.104 -4.001 1.00 8.48 ? 72 PHE A CD1 1 ATOM 558 C CD2 . PHE A 1 72 ? 10.848 28.965 -1.686 1.00 8.54 ? 72 PHE A CD2 1 ATOM 559 C CE1 . PHE A 1 72 ? 9.145 29.551 -3.715 1.00 6.47 ? 72 PHE A CE1 1 ATOM 560 C CE2 . PHE A 1 72 ? 9.564 29.391 -1.355 1.00 8.30 ? 72 PHE A CE2 1 ATOM 561 C CZ . PHE A 1 72 ? 8.709 29.696 -2.411 1.00 7.59 ? 72 PHE A CZ 1 ATOM 562 N N . GLN A 1 73 ? 15.167 26.440 -4.558 1.00 8.64 ? 73 GLN A N 1 ATOM 563 C CA . GLN A 1 73 ? 16.591 26.108 -4.532 1.00 9.02 ? 73 GLN A CA 1 ATOM 564 C C . GLN A 1 73 ? 16.901 24.687 -4.977 1.00 9.62 ? 73 GLN A C 1 ATOM 565 O O . GLN A 1 73 ? 16.274 23.749 -4.496 1.00 8.57 ? 73 GLN A O 1 ATOM 566 C CB . GLN A 1 73 ? 17.143 26.312 -3.085 1.00 9.49 ? 73 GLN A CB 1 ATOM 567 C CG . GLN A 1 73 ? 18.639 26.130 -2.924 1.00 8.84 ? 73 GLN A CG 1 ATOM 568 C CD . GLN A 1 73 ? 19.284 26.472 -1.600 1.00 10.55 ? 73 GLN A CD 1 ATOM 569 O OE1 . GLN A 1 73 ? 20.339 27.128 -1.448 1.00 9.54 ? 73 GLN A OE1 1 ATOM 570 N NE2 . GLN A 1 73 ? 18.650 26.017 -0.522 1.00 9.22 ? 73 GLN A NE2 1 ATOM 571 N N . LYS A 1 74 ? 17.928 24.477 -5.825 1.00 9.08 ? 74 LYS A N 1 ATOM 572 C CA . LYS A 1 74 ? 18.383 23.163 -6.271 1.00 10.16 ? 74 LYS A CA 1 ATOM 573 C C . LYS A 1 74 ? 19.768 22.875 -5.660 1.00 10.59 ? 74 LYS A C 1 ATOM 574 O O . LYS A 1 74 ? 20.709 23.632 -5.921 1.00 9.65 ? 74 LYS A O 1 ATOM 575 C CB . LYS A 1 74 ? 18.437 23.039 -7.806 1.00 12.08 ? 74 LYS A CB 1 ATOM 576 C CG . LYS A 1 74 ? 19.094 21.751 -8.319 1.00 15.97 ? 74 LYS A CG 1 ATOM 577 C CD . LYS A 1 74 ? 18.920 21.589 -9.828 1.00 21.18 ? 74 LYS A CD 1 ATOM 578 C CE . LYS A 1 74 ? 19.891 20.558 -10.377 1.00 24.89 ? 74 LYS A CE 1 ATOM 579 N NZ . LYS A 1 74 ? 19.834 20.440 -11.868 1.00 27.70 ? 74 LYS A NZ 1 ATOM 580 N N . LEU A 1 75 ? 19.872 21.854 -4.808 1.00 9.98 ? 75 LEU A N 1 ATOM 581 C CA . LEU A 1 75 ? 21.106 21.501 -4.101 1.00 10.01 ? 75 LEU A CA 1 ATOM 582 C C . LEU A 1 75 ? 21.935 20.448 -4.834 1.00 10.14 ? 75 LEU A C 1 ATOM 583 O O . LEU A 1 75 ? 21.448 19.350 -5.115 1.00 9.48 ? 75 LEU A O 1 ATOM 584 C CB . LEU A 1 75 ? 20.778 21.085 -2.663 1.00 10.26 ? 75 LEU A CB 1 ATOM 585 C CG . LEU A 1 75 ? 20.042 22.170 -1.839 1.00 12.38 ? 75 LEU A CG 1 ATOM 586 C CD1 . LEU A 1 75 ? 19.335 21.658 -0.625 1.00 14.70 ? 75 LEU A CD1 1 ATOM 587 C CD2 . LEU A 1 75 ? 21.017 23.277 -1.456 1.00 10.81 ? 75 LEU A CD2 1 ATOM 588 N N . SER A 1 76 ? 23.181 20.803 -5.161 1.00 9.38 ? 76 SER A N 1 ATOM 589 C CA . SER A 1 76 ? 24.094 19.910 -5.905 1.00 10.06 ? 76 SER A CA 1 ATOM 590 C C . SER A 1 76 ? 25.568 20.090 -5.531 1.00 12.31 ? 76 SER A C 1 ATOM 591 O O . SER A 1 76 ? 26.037 21.223 -5.446 1.00 11.18 ? 76 SER A O 1 ATOM 592 C CB . SER A 1 76 ? 24.000 20.232 -7.417 1.00 11.20 ? 76 SER A CB 1 ATOM 593 O OG . SER A 1 76 ? 25.043 19.579 -8.175 1.00 13.34 ? 76 SER A OG 1 ATOM 594 N N . ALA A 1 77 ? 26.364 19.017 -5.441 1.00 12.89 ? 77 ALA A N 1 ATOM 595 C CA . ALA A 1 77 ? 27.789 19.100 -5.186 1.00 15.61 ? 77 ALA A CA 1 ATOM 596 C C . ALA A 1 77 ? 28.614 19.737 -6.285 1.00 15.58 ? 77 ALA A C 1 ATOM 597 O O . ALA A 1 77 ? 29.808 20.067 -6.087 1.00 16.64 ? 77 ALA A O 1 ATOM 598 C CB . ALA A 1 77 ? 28.377 17.692 -4.933 1.00 17.89 ? 77 ALA A CB 1 ATOM 599 N N . THR A 1 78 ? 28.033 19.928 -7.464 1.00 13.72 ? 78 THR A N 1 ATOM 600 C CA . THR A 1 78 ? 28.707 20.581 -8.580 1.00 15.78 ? 78 THR A CA 1 ATOM 601 C C . THR A 1 78 ? 28.258 22.023 -8.824 1.00 15.06 ? 78 THR A C 1 ATOM 602 O O . THR A 1 78 ? 28.602 22.633 -9.864 1.00 14.59 ? 78 THR A O 1 ATOM 603 C CB . THR A 1 78 ? 28.548 19.760 -9.857 1.00 17.92 ? 78 THR A CB 1 ATOM 604 O OG1 . THR A 1 78 ? 27.180 19.731 -10.304 1.00 18.82 ? 78 THR A OG1 1 ATOM 605 C CG2 . THR A 1 78 ? 29.012 18.333 -9.567 1.00 20.91 ? 78 THR A CG2 1 ATOM 606 N N . GLY A 1 79 ? 27.577 22.612 -7.859 1.00 14.27 ? 79 GLY A N 1 ATOM 607 C CA . GLY A 1 79 ? 27.107 23.997 -7.943 1.00 13.05 ? 79 GLY A CA 1 ATOM 608 C C . GLY A 1 79 ? 25.586 24.108 -7.799 1.00 12.75 ? 79 GLY A C 1 ATOM 609 O O . GLY A 1 79 ? 24.854 23.645 -8.696 1.00 12.03 ? 79 GLY A O 1 ATOM 610 N N . SER A 1 80 ? 25.152 24.714 -6.709 1.00 11.08 ? 80 SER A N 1 ATOM 611 C CA . SER A 1 80 ? 23.702 24.871 -6.447 1.00 10.90 ? 80 SER A CA 1 ATOM 612 C C . SER A 1 80 ? 23.089 26.095 -7.086 1.00 11.32 ? 80 SER A C 1 ATOM 613 O O . SER A 1 80 ? 23.817 27.042 -7.411 1.00 11.88 ? 80 SER A O 1 ATOM 614 C CB . SER A 1 80 ? 23.508 24.883 -4.929 1.00 11.24 ? 80 SER A CB 1 ATOM 615 O OG . SER A 1 80 ? 23.959 23.705 -4.286 1.00 10.46 ? 80 SER A OG 1 ATOM 616 N N . THR A 1 81 ? 21.777 26.094 -7.352 1.00 11.67 ? 81 THR A N 1 ATOM 617 C CA . THR A 1 81 ? 21.075 27.205 -7.997 1.00 12.15 ? 81 THR A CA 1 ATOM 618 C C . THR A 1 81 ? 19.915 27.754 -7.165 1.00 12.60 ? 81 THR A C 1 ATOM 619 O O . THR A 1 81 ? 19.060 26.963 -6.722 1.00 13.07 ? 81 THR A O 1 ATOM 620 C CB . THR A 1 81 ? 20.515 26.722 -9.366 1.00 14.47 ? 81 THR A CB 1 ATOM 621 O OG1 . THR A 1 81 ? 21.579 26.221 -10.202 1.00 16.07 ? 81 THR A OG1 1 ATOM 622 C CG2 . THR A 1 81 ? 19.820 27.864 -10.104 1.00 15.12 ? 81 THR A CG2 1 ATOM 623 N N . ILE A 1 82 ? 19.871 29.064 -6.927 1.00 12.57 ? 82 ILE A N 1 ATOM 624 C CA . ILE A 1 82 ? 18.748 29.714 -6.211 1.00 12.29 ? 82 ILE A CA 1 ATOM 625 C C . ILE A 1 82 ? 17.851 30.356 -7.286 1.00 13.25 ? 82 ILE A C 1 ATOM 626 O O . ILE A 1 82 ? 18.342 31.139 -8.145 1.00 13.32 ? 82 ILE A O 1 ATOM 627 C CB . ILE A 1 82 ? 19.194 30.699 -5.128 1.00 12.03 ? 82 ILE A CB 1 ATOM 628 C CG1 . ILE A 1 82 ? 20.048 30.037 -4.053 1.00 10.44 ? 82 ILE A CG1 1 ATOM 629 C CG2 . ILE A 1 82 ? 17.987 31.446 -4.534 1.00 10.40 ? 82 ILE A CG2 1 ATOM 630 C CD1 . ILE A 1 82 ? 20.834 30.950 -3.121 1.00 9.86 ? 82 ILE A CD1 1 ATOM 631 N N . ASN A 1 83 ? 16.574 29.989 -7.339 1.00 12.20 ? 83 ASN A N 1 ATOM 632 C CA . ASN A 1 83 ? 15.626 30.441 -8.358 1.00 12.05 ? 83 ASN A CA 1 ATOM 633 C C . ASN A 1 83 ? 14.834 31.689 -8.000 1.00 13.03 ? 83 ASN A C 1 ATOM 634 O O . ASN A 1 83 ? 13.968 31.676 -7.131 1.00 11.09 ? 83 ASN A O 1 ATOM 635 C CB . ASN A 1 83 ? 14.668 29.292 -8.702 1.00 11.27 ? 83 ASN A CB 1 ATOM 636 C CG . ASN A 1 83 ? 13.680 29.585 -9.826 1.00 12.19 ? 83 ASN A CG 1 ATOM 637 O OD1 . ASN A 1 83 ? 13.833 30.467 -10.656 1.00 11.43 ? 83 ASN A OD1 1 ATOM 638 N ND2 . ASN A 1 83 ? 12.635 28.779 -9.918 1.00 11.02 ? 83 ASN A ND2 1 ATOM 639 N N . THR A 1 84 ? 15.097 32.788 -8.715 1.00 15.15 ? 84 THR A N 1 ATOM 640 C CA . THR A 1 84 ? 14.437 34.071 -8.510 1.00 15.31 ? 84 THR A CA 1 ATOM 641 C C . THR A 1 84 ? 13.456 34.373 -9.635 1.00 15.85 ? 84 THR A C 1 ATOM 642 O O . THR A 1 84 ? 12.880 35.474 -9.724 1.00 15.30 ? 84 THR A O 1 ATOM 643 C CB . THR A 1 84 ? 15.451 35.241 -8.388 1.00 16.10 ? 84 THR A CB 1 ATOM 644 O OG1 . THR A 1 84 ? 16.166 35.370 -9.633 1.00 16.88 ? 84 THR A OG1 1 ATOM 645 C CG2 . THR A 1 84 ? 16.440 35.030 -7.268 1.00 16.24 ? 84 THR A CG2 1 ATOM 646 N N . GLY A 1 85 ? 13.190 33.376 -10.460 1.00 15.34 ? 85 GLY A N 1 ATOM 647 C CA . GLY A 1 85 ? 12.271 33.419 -11.569 1.00 16.52 ? 85 GLY A CA 1 ATOM 648 C C . GLY A 1 85 ? 10.795 33.361 -11.218 1.00 16.89 ? 85 GLY A C 1 ATOM 649 O O . GLY A 1 85 ? 10.405 33.297 -10.044 1.00 15.90 ? 85 GLY A O 1 ATOM 650 N N . ALA A 1 86 ? 9.941 33.323 -12.253 1.00 16.32 ? 86 ALA A N 1 ATOM 651 C CA . ALA A 1 86 ? 8.495 33.322 -12.078 1.00 16.17 ? 86 ALA A CA 1 ATOM 652 C C . ALA A 1 86 ? 7.928 32.112 -11.336 1.00 15.29 ? 86 ALA A C 1 ATOM 653 O O . ALA A 1 86 ? 6.911 32.224 -10.630 1.00 15.40 ? 86 ALA A O 1 ATOM 654 C CB . ALA A 1 86 ? 7.761 33.474 -13.417 1.00 16.09 ? 86 ALA A CB 1 ATOM 655 N N . ASP A 1 87 ? 8.589 30.969 -11.467 1.00 12.45 ? 87 ASP A N 1 ATOM 656 C CA . ASP A 1 87 ? 8.287 29.710 -10.836 1.00 13.11 ? 87 ASP A CA 1 ATOM 657 C C . ASP A 1 87 ? 9.204 29.481 -9.609 1.00 11.59 ? 87 ASP A C 1 ATOM 658 O O . ASP A 1 87 ? 9.273 28.342 -9.178 1.00 10.39 ? 87 ASP A O 1 ATOM 659 C CB . ASP A 1 87 ? 8.458 28.502 -11.767 1.00 14.35 ? 87 ASP A CB 1 ATOM 660 C CG . ASP A 1 87 ? 9.811 28.416 -12.465 1.00 15.99 ? 87 ASP A CG 1 ATOM 661 O OD1 . ASP A 1 87 ? 10.734 29.239 -12.263 1.00 14.72 ? 87 ASP A OD1 1 ATOM 662 O OD2 . ASP A 1 87 ? 10.026 27.478 -13.296 1.00 16.55 ? 87 ASP A OD2 1 ATOM 663 N N . GLY A 1 88 ? 9.844 30.510 -9.117 1.00 10.05 ? 88 GLY A N 1 ATOM 664 C CA . GLY A 1 88 ? 10.706 30.500 -7.938 1.00 10.76 ? 88 GLY A CA 1 ATOM 665 C C . GLY A 1 88 ? 10.273 31.447 -6.824 1.00 10.68 ? 88 GLY A C 1 ATOM 666 O O . GLY A 1 88 ? 9.081 31.565 -6.521 1.00 9.02 ? 88 GLY A O 1 ATOM 667 N N . LEU A 1 89 ? 11.190 32.244 -6.263 1.00 9.46 ? 89 LEU A N 1 ATOM 668 C CA . LEU A 1 89 ? 10.943 33.148 -5.141 1.00 9.70 ? 89 LEU A CA 1 ATOM 669 C C . LEU A 1 89 ? 9.917 34.251 -5.442 1.00 9.59 ? 89 LEU A C 1 ATOM 670 O O . LEU A 1 89 ? 9.363 34.808 -4.493 1.00 8.89 ? 89 LEU A O 1 ATOM 671 C CB . LEU A 1 89 ? 12.269 33.707 -4.580 1.00 9.76 ? 89 LEU A CB 1 ATOM 672 C CG . LEU A 1 89 ? 13.135 32.730 -3.766 1.00 10.72 ? 89 LEU A CG 1 ATOM 673 C CD1 . LEU A 1 89 ? 14.560 33.208 -3.539 1.00 12.55 ? 89 LEU A CD1 1 ATOM 674 C CD2 . LEU A 1 89 ? 12.430 32.477 -2.429 1.00 9.45 ? 89 LEU A CD2 1 ATOM 675 N N . GLN A 1 90 ? 9.551 34.508 -6.708 1.00 9.53 ? 90 GLN A N 1 ATOM 676 C CA . GLN A 1 90 ? 8.419 35.413 -6.964 1.00 10.61 ? 90 GLN A CA 1 ATOM 677 C C . GLN A 1 90 ? 7.123 34.919 -6.338 1.00 9.54 ? 90 GLN A C 1 ATOM 678 O O . GLN A 1 90 ? 6.253 35.786 -6.065 1.00 9.32 ? 90 GLN A O 1 ATOM 679 C CB . GLN A 1 90 ? 8.294 35.621 -8.479 1.00 13.09 ? 90 GLN A CB 1 ATOM 680 C CG . GLN A 1 90 ? 9.417 36.504 -9.014 1.00 14.82 ? 90 GLN A CG 1 ATOM 681 C CD . GLN A 1 90 ? 9.374 36.774 -10.495 1.00 17.53 ? 90 GLN A CD 1 ATOM 682 O OE1 . GLN A 1 90 ? 8.321 36.929 -11.107 1.00 17.29 ? 90 GLN A OE1 1 ATOM 683 N NE2 . GLN A 1 90 ? 10.547 36.848 -11.142 1.00 17.87 ? 90 GLN A NE2 1 ATOM 684 N N . THR A 1 91 ? 6.862 33.638 -6.076 1.00 8.83 ? 91 THR A N 1 ATOM 685 C CA . THR A 1 91 ? 5.612 33.228 -5.408 1.00 9.66 ? 91 THR A CA 1 ATOM 686 C C . THR A 1 91 ? 5.681 33.548 -3.918 1.00 10.17 ? 91 THR A C 1 ATOM 687 O O . THR A 1 91 ? 4.631 33.800 -3.314 1.00 11.08 ? 91 THR A O 1 ATOM 688 C CB . THR A 1 91 ? 5.129 31.775 -5.658 1.00 8.97 ? 91 THR A CB 1 ATOM 689 O OG1 . THR A 1 91 ? 6.052 30.881 -5.002 1.00 8.80 ? 91 THR A OG1 1 ATOM 690 C CG2 . THR A 1 91 ? 5.203 31.413 -7.140 1.00 10.53 ? 91 THR A CG2 1 ATOM 691 N N . LEU A 1 92 ? 6.855 33.594 -3.263 1.00 9.26 ? 92 LEU A N 1 ATOM 692 C CA . LEU A 1 92 ? 6.971 34.081 -1.881 1.00 8.57 ? 92 LEU A CA 1 ATOM 693 C C . LEU A 1 92 ? 6.807 35.606 -1.879 1.00 9.79 ? 92 LEU A C 1 ATOM 694 O O . LEU A 1 92 ? 6.177 36.161 -0.955 1.00 7.17 ? 92 LEU A O 1 ATOM 695 C CB . LEU A 1 92 ? 8.317 33.649 -1.278 1.00 9.79 ? 92 LEU A CB 1 ATOM 696 C CG . LEU A 1 92 ? 8.567 33.955 0.205 1.00 10.13 ? 92 LEU A CG 1 ATOM 697 C CD1 . LEU A 1 92 ? 7.589 33.275 1.136 1.00 11.50 ? 92 LEU A CD1 1 ATOM 698 C CD2 . LEU A 1 92 ? 9.995 33.540 0.588 1.00 10.73 ? 92 LEU A CD2 1 ATOM 699 N N . ASP A 1 93 ? 7.278 36.335 -2.912 1.00 9.17 ? 93 ASP A N 1 ATOM 700 C CA . ASP A 1 93 ? 7.016 37.776 -3.001 1.00 9.72 ? 93 ASP A CA 1 ATOM 701 C C . ASP A 1 93 ? 5.507 38.075 -2.937 1.00 10.05 ? 93 ASP A C 1 ATOM 702 O O . ASP A 1 93 ? 5.067 39.027 -2.279 1.00 9.00 ? 93 ASP A O 1 ATOM 703 C CB . ASP A 1 93 ? 7.605 38.385 -4.269 1.00 10.48 ? 93 ASP A CB 1 ATOM 704 C CG . ASP A 1 93 ? 9.105 38.442 -4.447 1.00 11.19 ? 93 ASP A CG 1 ATOM 705 O OD1 . ASP A 1 93 ? 9.853 38.149 -3.487 1.00 9.04 ? 93 ASP A OD1 1 ATOM 706 O OD2 . ASP A 1 93 ? 9.545 38.849 -5.572 1.00 11.21 ? 93 ASP A OD2 1 ATOM 707 N N . TYR A 1 94 ? 4.668 37.292 -3.618 1.00 9.11 ? 94 TYR A N 1 ATOM 708 C CA . TYR A 1 94 ? 3.205 37.415 -3.576 1.00 10.31 ? 94 TYR A CA 1 ATOM 709 C C . TYR A 1 94 ? 2.669 37.415 -2.160 1.00 9.28 ? 94 TYR A C 1 ATOM 710 O O . TYR A 1 94 ? 1.738 38.173 -1.859 1.00 9.23 ? 94 TYR A O 1 ATOM 711 C CB . TYR A 1 94 ? 2.519 36.305 -4.363 1.00 11.61 ? 94 TYR A CB 1 ATOM 712 C CG . TYR A 1 94 ? 2.541 36.172 -5.857 1.00 13.49 ? 94 TYR A CG 1 ATOM 713 C CD1 . TYR A 1 94 ? 2.765 37.236 -6.714 1.00 14.59 ? 94 TYR A CD1 1 ATOM 714 C CD2 . TYR A 1 94 ? 2.287 34.922 -6.435 1.00 13.75 ? 94 TYR A CD2 1 ATOM 715 C CE1 . TYR A 1 94 ? 2.715 37.046 -8.102 1.00 16.33 ? 94 TYR A CE1 1 ATOM 716 C CE2 . TYR A 1 94 ? 2.243 34.725 -7.810 1.00 15.25 ? 94 TYR A CE2 1 ATOM 717 C CZ . TYR A 1 94 ? 2.467 35.812 -8.639 1.00 15.53 ? 94 TYR A CZ 1 ATOM 718 O OH . TYR A 1 94 ? 2.385 35.640 -10.024 1.00 15.54 ? 94 TYR A OH 1 ATOM 719 N N . VAL A 1 95 ? 3.180 36.555 -1.269 1.00 9.39 ? 95 VAL A N 1 ATOM 720 C CA . VAL A 1 95 ? 2.767 36.498 0.130 1.00 10.24 ? 95 VAL A CA 1 ATOM 721 C C . VAL A 1 95 ? 3.184 37.734 0.930 1.00 10.18 ? 95 VAL A C 1 ATOM 722 O O . VAL A 1 95 ? 2.385 38.246 1.719 1.00 8.76 ? 95 VAL A O 1 ATOM 723 C CB . VAL A 1 95 ? 3.290 35.234 0.855 1.00 12.26 ? 95 VAL A CB 1 ATOM 724 C CG1 . VAL A 1 95 ? 2.719 35.115 2.260 1.00 13.26 ? 95 VAL A CG1 1 ATOM 725 C CG2 . VAL A 1 95 ? 2.931 33.975 0.096 1.00 12.77 ? 95 VAL A CG2 1 ATOM 726 N N . VAL A 1 96 ? 4.420 38.249 0.824 1.00 9.39 ? 96 VAL A N 1 ATOM 727 C CA . VAL A 1 96 ? 4.825 39.449 1.547 1.00 8.68 ? 96 VAL A CA 1 ATOM 728 C C . VAL A 1 96 ? 4.002 40.674 1.101 1.00 9.67 ? 96 VAL A C 1 ATOM 729 O O . VAL A 1 96 ? 3.526 41.460 1.933 1.00 9.13 ? 96 VAL A O 1 ATOM 730 C CB . VAL A 1 96 ? 6.345 39.665 1.390 1.00 7.99 ? 96 VAL A CB 1 ATOM 731 C CG1 . VAL A 1 96 ? 6.772 40.964 2.071 1.00 9.04 ? 96 VAL A CG1 1 ATOM 732 C CG2 . VAL A 1 96 ? 7.139 38.517 1.983 1.00 8.09 ? 96 VAL A CG2 1 ATOM 733 N N . GLN A 1 97 ? 3.744 40.805 -0.189 1.00 9.28 ? 97 GLN A N 1 ATOM 734 C CA . GLN A 1 97 ? 2.940 41.873 -0.784 1.00 10.07 ? 97 GLN A CA 1 ATOM 735 C C . GLN A 1 97 ? 1.510 41.782 -0.272 1.00 10.10 ? 97 GLN A C 1 ATOM 736 O O . GLN A 1 97 ? 0.937 42.788 0.172 1.00 9.01 ? 97 GLN A O 1 ATOM 737 C CB . GLN A 1 97 ? 3.005 41.824 -2.323 1.00 10.60 ? 97 GLN A CB 1 ATOM 738 C CG . GLN A 1 97 ? 4.424 42.083 -2.863 1.00 11.77 ? 97 GLN A CG 1 ATOM 739 C CD . GLN A 1 97 ? 4.777 41.598 -4.243 1.00 13.63 ? 97 GLN A CD 1 ATOM 740 O OE1 . GLN A 1 97 ? 5.926 41.664 -4.758 1.00 14.88 ? 97 GLN A OE1 1 ATOM 741 N NE2 . GLN A 1 97 ? 3.825 41.040 -4.964 1.00 13.00 ? 97 GLN A NE2 1 ATOM 742 N N . SER A 1 98 ? 0.906 40.575 -0.271 1.00 9.20 ? 98 SER A N 1 ATOM 743 C CA . SER A 1 98 ? -0.455 40.415 0.247 1.00 9.43 ? 98 SER A CA 1 ATOM 744 C C . SER A 1 98 ? -0.588 40.769 1.727 1.00 10.06 ? 98 SER A C 1 ATOM 745 O O . SER A 1 98 ? -1.614 41.323 2.195 1.00 8.86 ? 98 SER A O 1 ATOM 746 C CB . SER A 1 98 ? -0.973 38.980 -0.019 1.00 9.90 ? 98 SER A CB 1 ATOM 747 O OG . SER A 1 98 ? -2.404 38.910 0.164 1.00 8.19 ? 98 SER A OG 1 ATOM 748 N N . ALA A 1 99 ? 0.433 40.470 2.539 1.00 8.56 ? 99 ALA A N 1 ATOM 749 C CA . ALA A 1 99 ? 0.436 40.820 3.953 1.00 10.22 ? 99 ALA A CA 1 ATOM 750 C C . ALA A 1 99 ? 0.434 42.340 4.132 1.00 9.76 ? 99 ALA A C 1 ATOM 751 O O . ALA A 1 99 ? -0.299 42.838 4.991 1.00 8.44 ? 99 ALA A O 1 ATOM 752 C CB . ALA A 1 99 ? 1.626 40.215 4.706 1.00 10.27 ? 99 ALA A CB 1 ATOM 753 N N . GLU A 1 100 ? 1.228 43.063 3.363 1.00 9.17 ? 100 GLU A N 1 ATOM 754 C CA . GLU A 1 100 ? 1.225 44.538 3.422 1.00 8.81 ? 100 GLU A CA 1 ATOM 755 C C . GLU A 1 100 ? -0.171 45.079 3.092 1.00 10.51 ? 100 GLU A C 1 ATOM 756 O O . GLU A 1 100 ? -0.658 46.001 3.755 1.00 10.53 ? 100 GLU A O 1 ATOM 757 C CB . GLU A 1 100 ? 2.235 45.083 2.395 1.00 8.43 ? 100 GLU A CB 1 ATOM 758 C CG . GLU A 1 100 ? 3.696 44.749 2.673 1.00 9.04 ? 100 GLU A CG 1 ATOM 759 C CD . GLU A 1 100 ? 4.685 45.189 1.618 1.00 9.55 ? 100 GLU A CD 1 ATOM 760 O OE1 . GLU A 1 100 ? 4.332 45.391 0.419 1.00 8.39 ? 100 GLU A OE1 1 ATOM 761 O OE2 . GLU A 1 100 ? 5.929 45.320 1.929 1.00 10.74 ? 100 GLU A OE2 1 ATOM 762 N N . GLN A 1 101 ? -0.814 44.534 2.061 1.00 9.95 ? 101 GLN A N 1 ATOM 763 C CA . GLN A 1 101 ? -2.149 44.997 1.658 1.00 10.87 ? 101 GLN A CA 1 ATOM 764 C C . GLN A 1 101 ? -3.279 44.614 2.594 1.00 11.22 ? 101 GLN A C 1 ATOM 765 O O . GLN A 1 101 ? -4.363 45.288 2.559 1.00 12.10 ? 101 GLN A O 1 ATOM 766 C CB . GLN A 1 101 ? -2.443 44.511 0.207 1.00 10.18 ? 101 GLN A CB 1 ATOM 767 C CG . GLN A 1 101 ? -1.516 45.136 -0.842 1.00 10.97 ? 101 GLN A CG 1 ATOM 768 C CD . GLN A 1 101 ? -1.523 44.410 -2.182 1.00 13.98 ? 101 GLN A CD 1 ATOM 769 O OE1 . GLN A 1 101 ? -2.592 44.055 -2.721 1.00 13.87 ? 101 GLN A OE1 1 ATOM 770 N NE2 . GLN A 1 101 ? -0.309 44.200 -2.718 1.00 11.80 ? 101 GLN A NE2 1 ATOM 771 N N . HIS A 1 102 ? -3.163 43.585 3.425 1.00 8.82 ? 102 HIS A N 1 ATOM 772 C CA . HIS A 1 102 ? -4.266 43.179 4.307 1.00 8.85 ? 102 HIS A CA 1 ATOM 773 C C . HIS A 1 102 ? -3.929 43.357 5.777 1.00 9.55 ? 102 HIS A C 1 ATOM 774 O O . HIS A 1 102 ? -4.553 42.792 6.669 1.00 11.11 ? 102 HIS A O 1 ATOM 775 C CB . HIS A 1 102 ? -4.699 41.723 4.000 1.00 9.92 ? 102 HIS A CB 1 ATOM 776 C CG . HIS A 1 102 ? -5.194 41.480 2.598 1.00 11.03 ? 102 HIS A CG 1 ATOM 777 N ND1 . HIS A 1 102 ? -4.312 41.168 1.583 1.00 9.54 ? 102 HIS A ND1 1 ATOM 778 C CD2 . HIS A 1 102 ? -6.431 41.479 2.019 1.00 10.45 ? 102 HIS A CD2 1 ATOM 779 C CE1 . HIS A 1 102 ? -4.972 41.021 0.447 1.00 10.20 ? 102 HIS A CE1 1 ATOM 780 N NE2 . HIS A 1 102 ? -6.250 41.205 0.675 1.00 9.61 ? 102 HIS A NE2 1 ATOM 781 N N . ASN A 1 103 ? -2.901 44.126 6.098 1.00 9.07 ? 103 ASN A N 1 ATOM 782 C CA . ASN A 1 103 ? -2.505 44.474 7.462 1.00 11.38 ? 103 ASN A CA 1 ATOM 783 C C . ASN A 1 103 ? -2.148 43.277 8.314 1.00 9.82 ? 103 ASN A C 1 ATOM 784 O O . ASN A 1 103 ? -2.535 43.217 9.482 1.00 11.21 ? 103 ASN A O 1 ATOM 785 C CB . ASN A 1 103 ? -3.577 45.390 8.105 1.00 14.90 ? 103 ASN A CB 1 ATOM 786 C CG . ASN A 1 103 ? -4.007 46.599 7.290 1.00 18.58 ? 103 ASN A CG 1 ATOM 787 O OD1 . ASN A 1 103 ? -3.221 47.312 6.668 1.00 19.12 ? 103 ASN A OD1 1 ATOM 788 N ND2 . ASN A 1 103 ? -5.327 46.875 7.276 1.00 19.69 ? 103 ASN A ND2 1 ATOM 789 N N . LEU A 1 104 ? -1.357 42.322 7.781 1.00 8.14 ? 104 LEU A N 1 ATOM 790 C CA . LEU A 1 104 ? -0.900 41.129 8.504 1.00 7.19 ? 104 LEU A CA 1 ATOM 791 C C . LEU A 1 104 ? 0.629 41.052 8.642 1.00 8.42 ? 104 LEU A C 1 ATOM 792 O O . LEU A 1 104 ? 1.332 41.667 7.850 1.00 9.30 ? 104 LEU A O 1 ATOM 793 C CB . LEU A 1 104 ? -1.377 39.837 7.771 1.00 8.61 ? 104 LEU A CB 1 ATOM 794 C CG . LEU A 1 104 ? -2.902 39.688 7.619 1.00 9.44 ? 104 LEU A CG 1 ATOM 795 C CD1 . LEU A 1 104 ? -3.271 38.535 6.680 1.00 8.27 ? 104 LEU A CD1 1 ATOM 796 C CD2 . LEU A 1 104 ? -3.528 39.466 8.992 1.00 9.75 ? 104 LEU A CD2 1 ATOM 797 N N . LYS A 1 105 ? 1.174 40.303 9.608 1.00 7.07 ? 105 LYS A N 1 ATOM 798 C CA . LYS A 1 105 ? 2.625 40.114 9.781 1.00 7.14 ? 105 LYS A CA 1 ATOM 799 C C . LYS A 1 105 ? 2.977 38.634 9.588 1.00 8.08 ? 105 LYS A C 1 ATOM 800 O O . LYS A 1 105 ? 2.116 37.776 9.845 1.00 9.11 ? 105 LYS A O 1 ATOM 801 C CB . LYS A 1 105 ? 3.020 40.534 11.208 1.00 7.25 ? 105 LYS A CB 1 ATOM 802 C CG . LYS A 1 105 ? 2.596 41.943 11.645 1.00 7.98 ? 105 LYS A CG 1 ATOM 803 C CD . LYS A 1 105 ? 3.199 43.087 10.842 1.00 9.81 ? 105 LYS A CD 1 ATOM 804 C CE . LYS A 1 105 ? 2.660 44.449 11.280 1.00 9.81 ? 105 LYS A CE 1 ATOM 805 N NZ . LYS A 1 105 ? 3.121 45.559 10.419 1.00 10.05 ? 105 LYS A NZ 1 ATOM 806 N N . LEU A 1 106 ? 4.199 38.287 9.182 1.00 7.02 ? 106 LEU A N 1 ATOM 807 C CA . LEU A 1 106 ? 4.607 36.925 8.880 1.00 7.58 ? 106 LEU A CA 1 ATOM 808 C C . LEU A 1 106 ? 5.792 36.348 9.653 1.00 8.05 ? 106 LEU A C 1 ATOM 809 O O . LEU A 1 106 ? 6.806 37.033 9.783 1.00 7.60 ? 106 LEU A O 1 ATOM 810 C CB . LEU A 1 106 ? 5.013 36.872 7.383 1.00 7.72 ? 106 LEU A CB 1 ATOM 811 C CG . LEU A 1 106 ? 4.003 37.354 6.342 1.00 7.57 ? 106 LEU A CG 1 ATOM 812 C CD1 . LEU A 1 106 ? 4.613 37.372 4.954 1.00 7.15 ? 106 LEU A CD1 1 ATOM 813 C CD2 . LEU A 1 106 ? 2.732 36.478 6.337 1.00 6.34 ? 106 LEU A CD2 1 ATOM 814 N N . ILE A 1 107 ? 5.731 35.095 10.078 1.00 6.79 ? 107 ILE A N 1 ATOM 815 C CA . ILE A 1 107 ? 6.889 34.350 10.661 1.00 7.52 ? 107 ILE A CA 1 ATOM 816 C C . ILE A 1 107 ? 7.377 33.415 9.546 1.00 8.01 ? 107 ILE A C 1 ATOM 817 O O . ILE A 1 107 ? 6.561 32.643 8.982 1.00 8.70 ? 107 ILE A O 1 ATOM 818 C CB . ILE A 1 107 ? 6.482 33.596 11.944 1.00 7.84 ? 107 ILE A CB 1 ATOM 819 C CG1 . ILE A 1 107 ? 6.176 34.574 13.087 1.00 7.53 ? 107 ILE A CG1 1 ATOM 820 C CG2 . ILE A 1 107 ? 7.611 32.651 12.375 1.00 8.05 ? 107 ILE A CG2 1 ATOM 821 C CD1 . ILE A 1 107 ? 5.802 33.942 14.437 1.00 8.05 ? 107 ILE A CD1 1 ATOM 822 N N . ILE A 1 108 ? 8.647 33.431 9.141 1.00 7.17 ? 108 ILE A N 1 ATOM 823 C CA . ILE A 1 108 ? 9.214 32.695 8.021 1.00 7.09 ? 108 ILE A CA 1 ATOM 824 C C . ILE A 1 108 ? 10.479 31.884 8.323 1.00 7.87 ? 108 ILE A C 1 ATOM 825 O O . ILE A 1 108 ? 11.559 32.488 8.445 1.00 7.53 ? 108 ILE A O 1 ATOM 826 C CB . ILE A 1 108 ? 9.559 33.703 6.868 1.00 7.91 ? 108 ILE A CB 1 ATOM 827 C CG1 . ILE A 1 108 ? 8.392 34.603 6.456 1.00 8.35 ? 108 ILE A CG1 1 ATOM 828 C CG2 . ILE A 1 108 ? 10.050 32.980 5.607 1.00 9.15 ? 108 ILE A CG2 1 ATOM 829 C CD1 . ILE A 1 108 ? 8.519 35.554 5.276 1.00 7.80 ? 108 ILE A CD1 1 ATOM 830 N N . PRO A 1 109 ? 10.425 30.564 8.379 1.00 6.18 ? 109 PRO A N 1 ATOM 831 C CA . PRO A 1 109 ? 11.579 29.671 8.535 1.00 7.44 ? 109 PRO A CA 1 ATOM 832 C C . PRO A 1 109 ? 12.333 29.409 7.232 1.00 7.64 ? 109 PRO A C 1 ATOM 833 O O . PRO A 1 109 ? 11.732 29.352 6.154 1.00 7.49 ? 109 PRO A O 1 ATOM 834 C CB . PRO A 1 109 ? 10.962 28.397 9.096 1.00 8.64 ? 109 PRO A CB 1 ATOM 835 C CG . PRO A 1 109 ? 9.592 28.359 8.510 1.00 8.07 ? 109 PRO A CG 1 ATOM 836 C CD . PRO A 1 109 ? 9.131 29.793 8.405 1.00 8.56 ? 109 PRO A CD 1 ATOM 837 N N . PHE A 1 110 ? 13.667 29.177 7.294 1.00 6.62 ? 110 PHE A N 1 ATOM 838 C CA . PHE A 1 110 ? 14.546 29.017 6.152 1.00 6.59 ? 110 PHE A CA 1 ATOM 839 C C . PHE A 1 110 ? 14.862 27.609 5.680 1.00 6.20 ? 110 PHE A C 1 ATOM 840 O O . PHE A 1 110 ? 15.373 27.437 4.543 1.00 6.00 ? 110 PHE A O 1 ATOM 841 C CB . PHE A 1 110 ? 15.892 29.751 6.472 1.00 7.17 ? 110 PHE A CB 1 ATOM 842 C CG . PHE A 1 110 ? 15.896 31.214 6.792 1.00 7.48 ? 110 PHE A CG 1 ATOM 843 C CD1 . PHE A 1 110 ? 15.471 32.153 5.877 1.00 7.77 ? 110 PHE A CD1 1 ATOM 844 C CD2 . PHE A 1 110 ? 16.396 31.696 7.987 1.00 7.48 ? 110 PHE A CD2 1 ATOM 845 C CE1 . PHE A 1 110 ? 15.473 33.509 6.143 1.00 9.38 ? 110 PHE A CE1 1 ATOM 846 C CE2 . PHE A 1 110 ? 16.398 33.039 8.305 1.00 8.64 ? 110 PHE A CE2 1 ATOM 847 C CZ . PHE A 1 110 ? 15.981 33.968 7.355 1.00 8.44 ? 110 PHE A CZ 1 ATOM 848 N N . VAL A 1 111 ? 14.616 26.595 6.497 1.00 6.32 ? 111 VAL A N 1 ATOM 849 C CA . VAL A 1 111 ? 14.831 25.164 6.184 1.00 7.33 ? 111 VAL A CA 1 ATOM 850 C C . VAL A 1 111 ? 13.913 24.254 7.034 1.00 7.84 ? 111 VAL A C 1 ATOM 851 O O . VAL A 1 111 ? 13.513 24.634 8.129 1.00 6.31 ? 111 VAL A O 1 ATOM 852 C CB . VAL A 1 111 ? 16.280 24.742 6.421 1.00 8.39 ? 111 VAL A CB 1 ATOM 853 C CG1 . VAL A 1 111 ? 16.634 24.747 7.912 1.00 6.77 ? 111 VAL A CG1 1 ATOM 854 C CG2 . VAL A 1 111 ? 16.691 23.410 5.847 1.00 7.89 ? 111 VAL A CG2 1 ATOM 855 N N . ASN A 1 112 ? 13.589 23.054 6.589 1.00 6.68 ? 112 ASN A N 1 ATOM 856 C CA . ASN A 1 112 ? 12.837 22.045 7.325 1.00 6.37 ? 112 ASN A CA 1 ATOM 857 C C . ASN A 1 112 ? 13.721 20.970 7.961 1.00 6.88 ? 112 ASN A C 1 ATOM 858 O O . ASN A 1 112 ? 14.640 20.473 7.300 1.00 5.30 ? 112 ASN A O 1 ATOM 859 C CB . ASN A 1 112 ? 11.807 21.338 6.414 1.00 6.66 ? 112 ASN A CB 1 ATOM 860 C CG . ASN A 1 112 ? 10.617 20.737 7.162 1.00 7.82 ? 112 ASN A CG 1 ATOM 861 O OD1 . ASN A 1 112 ? 10.560 20.655 8.394 1.00 7.37 ? 112 ASN A OD1 1 ATOM 862 N ND2 . ASN A 1 112 ? 9.603 20.225 6.434 1.00 7.45 ? 112 ASN A ND2 1 ATOM 863 N N . ASN A 1 113 ? 13.444 20.582 9.237 1.00 5.99 ? 113 ASN A N 1 ATOM 864 C CA . ASN A 1 113 ? 14.148 19.418 9.810 1.00 5.49 ? 113 ASN A CA 1 ATOM 865 C C . ASN A 1 113 ? 13.656 18.146 9.107 1.00 7.29 ? 113 ASN A C 1 ATOM 866 O O . ASN A 1 113 ? 14.454 17.215 8.836 1.00 7.65 ? 113 ASN A O 1 ATOM 867 C CB . ASN A 1 113 ? 13.845 19.282 11.329 1.00 5.67 ? 113 ASN A CB 1 ATOM 868 C CG . ASN A 1 113 ? 14.702 18.241 12.028 1.00 7.72 ? 113 ASN A CG 1 ATOM 869 O OD1 . ASN A 1 113 ? 15.887 18.446 12.262 1.00 7.89 ? 113 ASN A OD1 1 ATOM 870 N ND2 . ASN A 1 113 ? 14.140 17.071 12.379 1.00 7.50 ? 113 ASN A ND2 1 ATOM 871 N N . TRP A 1 114 ? 12.366 18.099 8.767 1.00 6.94 ? 114 TRP A N 1 ATOM 872 C CA . TRP A 1 114 ? 11.706 16.932 8.158 1.00 8.41 ? 114 TRP A CA 1 ATOM 873 C C . TRP A 1 114 ? 11.870 16.945 6.633 1.00 8.80 ? 114 TRP A C 1 ATOM 874 O O . TRP A 1 114 ? 12.238 17.995 6.092 1.00 8.87 ? 114 TRP A O 1 ATOM 875 C CB . TRP A 1 114 ? 10.240 16.697 8.612 1.00 9.68 ? 114 TRP A CB 1 ATOM 876 C CG . TRP A 1 114 ? 10.094 16.813 10.119 1.00 6.68 ? 114 TRP A CG 1 ATOM 877 C CD1 . TRP A 1 114 ? 9.543 17.869 10.792 1.00 7.69 ? 114 TRP A CD1 1 ATOM 878 C CD2 . TRP A 1 114 ? 10.719 15.999 11.104 1.00 8.49 ? 114 TRP A CD2 1 ATOM 879 N NE1 . TRP A 1 114 ? 9.749 17.737 12.152 1.00 8.28 ? 114 TRP A NE1 1 ATOM 880 C CE2 . TRP A 1 114 ? 10.467 16.581 12.362 1.00 9.02 ? 114 TRP A CE2 1 ATOM 881 C CE3 . TRP A 1 114 ? 11.409 14.777 11.051 1.00 6.25 ? 114 TRP A CE3 1 ATOM 882 C CZ2 . TRP A 1 114 ? 10.905 15.974 13.544 1.00 10.61 ? 114 TRP A CZ2 1 ATOM 883 C CZ3 . TRP A 1 114 ? 11.851 14.190 12.225 1.00 6.65 ? 114 TRP A CZ3 1 ATOM 884 C CH2 . TRP A 1 114 ? 11.609 14.828 13.461 1.00 8.29 ? 114 TRP A CH2 1 ATOM 885 N N . SER A 1 115 ? 11.625 15.849 5.913 1.00 7.37 ? 115 SER A N 1 ATOM 886 C CA . SER A 1 115 ? 11.902 15.791 4.464 1.00 7.64 ? 115 SER A CA 1 ATOM 887 C C . SER A 1 115 ? 10.842 16.360 3.532 1.00 9.60 ? 115 SER A C 1 ATOM 888 O O . SER A 1 115 ? 10.971 16.306 2.289 1.00 9.78 ? 115 SER A O 1 ATOM 889 C CB . SER A 1 115 ? 12.275 14.355 4.035 1.00 8.44 ? 115 SER A CB 1 ATOM 890 O OG A SER A 1 115 ? 13.380 13.881 4.799 0.50 6.69 ? 115 SER A OG 1 ATOM 891 O OG B SER A 1 115 ? 11.364 13.407 4.548 0.50 11.45 ? 115 SER A OG 1 ATOM 892 N N . ASP A 1 116 ? 9.778 16.921 4.071 1.00 9.18 ? 116 ASP A N 1 ATOM 893 C CA . ASP A 1 116 ? 8.726 17.591 3.279 1.00 9.28 ? 116 ASP A CA 1 ATOM 894 C C . ASP A 1 116 ? 9.275 18.876 2.678 1.00 7.74 ? 116 ASP A C 1 ATOM 895 O O . ASP A 1 116 ? 9.839 19.709 3.385 1.00 6.42 ? 116 ASP A O 1 ATOM 896 C CB . ASP A 1 116 ? 7.510 17.831 4.159 1.00 9.83 ? 116 ASP A CB 1 ATOM 897 C CG . ASP A 1 116 ? 6.975 16.591 4.862 1.00 11.40 ? 116 ASP A CG 1 ATOM 898 O OD1 . ASP A 1 116 ? 6.685 15.574 4.174 1.00 9.75 ? 116 ASP A OD1 1 ATOM 899 O OD2 . ASP A 1 116 ? 6.872 16.583 6.120 1.00 10.07 ? 116 ASP A OD2 1 ATOM 900 N N . TYR A 1 117 ? 9.156 19.055 1.365 1.00 6.14 ? 117 TYR A N 1 ATOM 901 C CA . TYR A 1 117 ? 9.703 20.176 0.622 1.00 6.74 ? 117 TYR A CA 1 ATOM 902 C C . TYR A 1 117 ? 11.250 20.175 0.767 1.00 7.74 ? 117 TYR A C 1 ATOM 903 O O . TYR A 1 117 ? 11.890 21.228 0.797 1.00 6.64 ? 117 TYR A O 1 ATOM 904 C CB . TYR A 1 117 ? 8.983 21.513 0.895 1.00 6.79 ? 117 TYR A CB 1 ATOM 905 C CG . TYR A 1 117 ? 7.480 21.433 0.606 1.00 6.36 ? 117 TYR A CG 1 ATOM 906 C CD1 . TYR A 1 117 ? 6.993 21.540 -0.682 1.00 6.64 ? 117 TYR A CD1 1 ATOM 907 C CD2 . TYR A 1 117 ? 6.573 21.123 1.603 1.00 5.30 ? 117 TYR A CD2 1 ATOM 908 C CE1 . TYR A 1 117 ? 5.629 21.382 -0.962 1.00 8.09 ? 117 TYR A CE1 1 ATOM 909 C CE2 . TYR A 1 117 ? 5.205 20.942 1.324 1.00 7.22 ? 117 TYR A CE2 1 ATOM 910 C CZ . TYR A 1 117 ? 4.742 21.085 0.050 1.00 8.17 ? 117 TYR A CZ 1 ATOM 911 O OH . TYR A 1 117 ? 3.378 20.934 -0.242 1.00 9.11 ? 117 TYR A OH 1 ATOM 912 N N . GLY A 1 118 ? 11.839 18.984 0.736 1.00 7.70 ? 118 GLY A N 1 ATOM 913 C CA . GLY A 1 118 ? 13.283 18.772 0.700 1.00 7.31 ? 118 GLY A CA 1 ATOM 914 C C . GLY A 1 118 ? 13.971 18.547 2.039 1.00 7.91 ? 118 GLY A C 1 ATOM 915 O O . GLY A 1 118 ? 14.478 17.470 2.383 1.00 7.77 ? 118 GLY A O 1 ATOM 916 N N . GLY A 1 119 ? 14.032 19.585 2.848 1.00 7.45 ? 119 GLY A N 1 ATOM 917 C CA . GLY A 1 119 ? 14.610 19.639 4.166 1.00 7.47 ? 119 GLY A CA 1 ATOM 918 C C . GLY A 1 119 ? 16.097 19.333 4.295 1.00 7.64 ? 119 GLY A C 1 ATOM 919 O O . GLY A 1 119 ? 16.804 19.279 3.314 1.00 8.23 ? 119 GLY A O 1 ATOM 920 N N . ILE A 1 120 ? 16.577 19.033 5.511 1.00 5.69 ? 120 ILE A N 1 ATOM 921 C CA . ILE A 1 120 ? 17.955 18.622 5.769 1.00 6.56 ? 120 ILE A CA 1 ATOM 922 C C . ILE A 1 120 ? 18.347 17.452 4.861 1.00 8.23 ? 120 ILE A C 1 ATOM 923 O O . ILE A 1 120 ? 19.499 17.386 4.396 1.00 7.78 ? 120 ILE A O 1 ATOM 924 C CB . ILE A 1 120 ? 18.156 18.358 7.274 1.00 5.83 ? 120 ILE A CB 1 ATOM 925 C CG1 . ILE A 1 120 ? 18.220 19.655 8.068 1.00 6.02 ? 120 ILE A CG1 1 ATOM 926 C CG2 . ILE A 1 120 ? 19.430 17.528 7.529 1.00 5.39 ? 120 ILE A CG2 1 ATOM 927 C CD1 . ILE A 1 120 ? 18.363 19.579 9.572 1.00 6.90 ? 120 ILE A CD1 1 ATOM 928 N N . ASN A 1 121 ? 17.449 16.499 4.576 1.00 7.87 ? 121 ASN A N 1 ATOM 929 C CA . ASN A 1 121 ? 17.721 15.380 3.688 1.00 8.78 ? 121 ASN A CA 1 ATOM 930 C C . ASN A 1 121 ? 18.185 15.790 2.299 1.00 8.73 ? 121 ASN A C 1 ATOM 931 O O . ASN A 1 121 ? 19.054 15.101 1.720 1.00 7.71 ? 121 ASN A O 1 ATOM 932 C CB . ASN A 1 121 ? 16.495 14.438 3.606 1.00 9.18 ? 121 ASN A CB 1 ATOM 933 C CG . ASN A 1 121 ? 16.773 13.182 2.813 1.00 11.06 ? 121 ASN A CG 1 ATOM 934 O OD1 . ASN A 1 121 ? 16.207 12.906 1.730 1.00 14.16 ? 121 ASN A OD1 1 ATOM 935 N ND2 . ASN A 1 121 ? 17.661 12.341 3.334 1.00 7.50 ? 121 ASN A ND2 1 ATOM 936 N N . ALA A 1 122 ? 17.629 16.872 1.715 1.00 7.54 ? 122 ALA A N 1 ATOM 937 C CA . ALA A 1 122 ? 18.099 17.309 0.397 1.00 6.60 ? 122 ALA A CA 1 ATOM 938 C C . ALA A 1 122 ? 19.536 17.836 0.475 1.00 7.86 ? 122 ALA A C 1 ATOM 939 O O . ALA A 1 122 ? 20.279 17.639 -0.485 1.00 8.20 ? 122 ALA A O 1 ATOM 940 C CB . ALA A 1 122 ? 17.168 18.346 -0.195 1.00 7.59 ? 122 ALA A CB 1 ATOM 941 N N . TYR A 1 123 ? 19.944 18.468 1.572 1.00 7.97 ? 123 TYR A N 1 ATOM 942 C CA . TYR A 1 123 ? 21.335 18.886 1.755 1.00 7.68 ? 123 TYR A CA 1 ATOM 943 C C . TYR A 1 123 ? 22.214 17.634 1.902 1.00 8.53 ? 123 TYR A C 1 ATOM 944 O O . TYR A 1 123 ? 23.358 17.582 1.387 1.00 7.98 ? 123 TYR A O 1 ATOM 945 C CB . TYR A 1 123 ? 21.485 19.858 2.934 1.00 6.47 ? 123 TYR A CB 1 ATOM 946 C CG . TYR A 1 123 ? 21.009 21.287 2.813 1.00 7.17 ? 123 TYR A CG 1 ATOM 947 C CD1 . TYR A 1 123 ? 19.649 21.593 2.937 1.00 7.35 ? 123 TYR A CD1 1 ATOM 948 C CD2 . TYR A 1 123 ? 21.878 22.360 2.617 1.00 6.98 ? 123 TYR A CD2 1 ATOM 949 C CE1 . TYR A 1 123 ? 19.180 22.896 2.867 1.00 7.24 ? 123 TYR A CE1 1 ATOM 950 C CE2 . TYR A 1 123 ? 21.415 23.672 2.525 1.00 7.54 ? 123 TYR A CE2 1 ATOM 951 C CZ . TYR A 1 123 ? 20.056 23.937 2.662 1.00 7.51 ? 123 TYR A CZ 1 ATOM 952 O OH . TYR A 1 123 ? 19.634 25.257 2.551 1.00 7.74 ? 123 TYR A OH 1 ATOM 953 N N . VAL A 1 124 ? 21.778 16.597 2.623 1.00 7.36 ? 124 VAL A N 1 ATOM 954 C CA . VAL A 1 124 ? 22.546 15.351 2.816 1.00 10.39 ? 124 VAL A CA 1 ATOM 955 C C . VAL A 1 124 ? 22.822 14.626 1.509 1.00 11.51 ? 124 VAL A C 1 ATOM 956 O O . VAL A 1 124 ? 23.938 14.154 1.192 1.00 10.16 ? 124 VAL A O 1 ATOM 957 C CB . VAL A 1 124 ? 21.867 14.404 3.837 1.00 10.45 ? 124 VAL A CB 1 ATOM 958 C CG1 . VAL A 1 124 ? 22.522 13.012 3.844 1.00 10.53 ? 124 VAL A CG1 1 ATOM 959 C CG2 . VAL A 1 124 ? 21.956 15.009 5.243 1.00 10.42 ? 124 VAL A CG2 1 ATOM 960 N N . ASN A 1 125 ? 21.832 14.562 0.617 1.00 11.25 ? 125 ASN A N 1 ATOM 961 C CA . ASN A 1 125 ? 22.011 13.923 -0.693 1.00 12.36 ? 125 ASN A CA 1 ATOM 962 C C . ASN A 1 125 ? 23.122 14.604 -1.486 1.00 12.21 ? 125 ASN A C 1 ATOM 963 O O . ASN A 1 125 ? 23.931 13.944 -2.140 1.00 10.83 ? 125 ASN A O 1 ATOM 964 C CB . ASN A 1 125 ? 20.698 13.962 -1.478 1.00 14.24 ? 125 ASN A CB 1 ATOM 965 C CG . ASN A 1 125 ? 19.695 12.905 -1.052 1.00 16.47 ? 125 ASN A CG 1 ATOM 966 O OD1 . ASN A 1 125 ? 18.469 13.031 -1.318 1.00 18.39 ? 125 ASN A OD1 1 ATOM 967 N ND2 . ASN A 1 125 ? 20.151 11.846 -0.439 1.00 16.13 ? 125 ASN A ND2 1 ATOM 968 N N . ALA A 1 126 ? 23.159 15.929 -1.466 1.00 10.44 ? 126 ALA A N 1 ATOM 969 C CA . ALA A 1 126 ? 24.174 16.674 -2.210 1.00 10.98 ? 126 ALA A CA 1 ATOM 970 C C . ALA A 1 126 ? 25.568 16.721 -1.607 1.00 12.14 ? 126 ALA A C 1 ATOM 971 O O . ALA A 1 126 ? 26.542 16.635 -2.383 1.00 12.23 ? 126 ALA A O 1 ATOM 972 C CB . ALA A 1 126 ? 23.636 18.105 -2.324 1.00 9.79 ? 126 ALA A CB 1 ATOM 973 N N . PHE A 1 127 ? 25.686 16.926 -0.300 1.00 10.69 ? 127 PHE A N 1 ATOM 974 C CA . PHE A 1 127 ? 26.953 17.214 0.366 1.00 11.02 ? 127 PHE A CA 1 ATOM 975 C C . PHE A 1 127 ? 27.540 16.135 1.264 1.00 12.04 ? 127 PHE A C 1 ATOM 976 O O . PHE A 1 127 ? 28.602 16.322 1.909 1.00 12.92 ? 127 PHE A O 1 ATOM 977 C CB . PHE A 1 127 ? 26.766 18.553 1.152 1.00 11.37 ? 127 PHE A CB 1 ATOM 978 C CG . PHE A 1 127 ? 26.259 19.707 0.326 1.00 11.55 ? 127 PHE A CG 1 ATOM 979 C CD1 . PHE A 1 127 ? 26.923 20.162 -0.794 1.00 12.83 ? 127 PHE A CD1 1 ATOM 980 C CD2 . PHE A 1 127 ? 25.063 20.351 0.652 1.00 11.23 ? 127 PHE A CD2 1 ATOM 981 C CE1 . PHE A 1 127 ? 26.447 21.203 -1.564 1.00 13.01 ? 127 PHE A CE1 1 ATOM 982 C CE2 . PHE A 1 127 ? 24.567 21.410 -0.106 1.00 12.48 ? 127 PHE A CE2 1 ATOM 983 C CZ . PHE A 1 127 ? 25.265 21.825 -1.226 1.00 13.64 ? 127 PHE A CZ 1 ATOM 984 N N . GLY A 1 128 ? 26.885 14.998 1.402 1.00 10.91 ? 128 GLY A N 1 ATOM 985 C CA . GLY A 1 128 ? 27.290 13.877 2.238 1.00 11.19 ? 128 GLY A CA 1 ATOM 986 C C . GLY A 1 128 ? 26.987 13.981 3.734 1.00 12.38 ? 128 GLY A C 1 ATOM 987 O O . GLY A 1 128 ? 26.196 14.805 4.215 1.00 11.31 ? 128 GLY A O 1 ATOM 988 N N . GLY A 1 129 ? 27.566 13.065 4.512 1.00 12.46 ? 129 GLY A N 1 ATOM 989 C CA . GLY A 1 129 ? 27.358 12.997 5.965 1.00 13.06 ? 129 GLY A CA 1 ATOM 990 C C . GLY A 1 129 ? 25.959 12.481 6.292 1.00 13.14 ? 129 GLY A C 1 ATOM 991 O O . GLY A 1 129 ? 25.449 11.624 5.538 1.00 13.06 ? 129 GLY A O 1 ATOM 992 N N . ASN A 1 130 ? 25.351 12.962 7.392 1.00 11.71 ? 130 ASN A N 1 ATOM 993 C CA . ASN A 1 130 ? 23.987 12.493 7.711 1.00 11.27 ? 130 ASN A CA 1 ATOM 994 C C . ASN A 1 130 ? 23.149 13.562 8.416 1.00 10.86 ? 130 ASN A C 1 ATOM 995 O O . ASN A 1 130 ? 23.615 14.729 8.473 1.00 9.69 ? 130 ASN A O 1 ATOM 996 C CB . ASN A 1 130 ? 24.048 11.128 8.429 1.00 11.41 ? 130 ASN A CB 1 ATOM 997 C CG . ASN A 1 130 ? 24.646 11.301 9.784 1.00 14.14 ? 130 ASN A CG 1 ATOM 998 O OD1 . ASN A 1 130 ? 24.748 12.328 10.420 1.00 10.61 ? 130 ASN A OD1 1 ATOM 999 N ND2 . ASN A 1 130 ? 25.243 10.203 10.358 1.00 18.99 ? 130 ASN A ND2 1 ATOM 1000 N N . ALA A 1 131 ? 21.943 13.281 8.910 1.00 9.52 ? 131 ALA A N 1 ATOM 1001 C CA . ALA A 1 131 ? 21.085 14.294 9.518 1.00 9.54 ? 131 ALA A CA 1 ATOM 1002 C C . ALA A 1 131 ? 21.590 14.966 10.785 1.00 9.65 ? 131 ALA A C 1 ATOM 1003 O O . ALA A 1 131 ? 21.124 16.088 11.093 1.00 7.27 ? 131 ALA A O 1 ATOM 1004 C CB . ALA A 1 131 ? 19.680 13.688 9.736 1.00 8.75 ? 131 ALA A CB 1 ATOM 1005 N N . THR A 1 132 ? 22.517 14.351 11.522 1.00 8.89 ? 132 THR A N 1 ATOM 1006 C CA . THR A 1 132 ? 23.098 14.963 12.716 1.00 9.60 ? 132 THR A CA 1 ATOM 1007 C C . THR A 1 132 ? 24.402 15.691 12.432 1.00 10.93 ? 132 THR A C 1 ATOM 1008 O O . THR A 1 132 ? 24.718 16.684 13.120 1.00 12.84 ? 132 THR A O 1 ATOM 1009 C CB . THR A 1 132 ? 23.260 13.988 13.901 1.00 10.46 ? 132 THR A CB 1 ATOM 1010 O OG1 . THR A 1 132 ? 24.066 12.859 13.523 1.00 11.58 ? 132 THR A OG1 1 ATOM 1011 C CG2 . THR A 1 132 ? 21.906 13.479 14.416 1.00 11.65 ? 132 THR A CG2 1 ATOM 1012 N N . THR A 1 133 ? 25.175 15.289 11.437 1.00 10.24 ? 133 THR A N 1 ATOM 1013 C CA . THR A 1 133 ? 26.408 15.990 11.083 1.00 10.15 ? 133 THR A CA 1 ATOM 1014 C C . THR A 1 133 ? 26.123 17.214 10.198 1.00 9.00 ? 133 THR A C 1 ATOM 1015 O O . THR A 1 133 ? 27.020 18.056 9.977 1.00 9.08 ? 133 THR A O 1 ATOM 1016 C CB . THR A 1 133 ? 27.449 15.099 10.401 1.00 11.62 ? 133 THR A CB 1 ATOM 1017 O OG1 . THR A 1 133 ? 27.039 14.639 9.101 1.00 11.97 ? 133 THR A OG1 1 ATOM 1018 C CG2 . THR A 1 133 ? 27.750 13.826 11.180 1.00 14.51 ? 133 THR A CG2 1 ATOM 1019 N N . TRP A 1 134 ? 24.904 17.422 9.718 1.00 7.21 ? 134 TRP A N 1 ATOM 1020 C CA . TRP A 1 134 ? 24.525 18.564 8.887 1.00 7.56 ? 134 TRP A CA 1 ATOM 1021 C C . TRP A 1 134 ? 24.924 19.906 9.502 1.00 9.03 ? 134 TRP A C 1 ATOM 1022 O O . TRP A 1 134 ? 25.483 20.784 8.795 1.00 6.87 ? 134 TRP A O 1 ATOM 1023 C CB . TRP A 1 134 ? 22.986 18.565 8.617 1.00 7.61 ? 134 TRP A CB 1 ATOM 1024 C CG . TRP A 1 134 ? 22.507 19.746 7.795 1.00 7.26 ? 134 TRP A CG 1 ATOM 1025 C CD1 . TRP A 1 134 ? 22.509 19.844 6.427 1.00 6.56 ? 134 TRP A CD1 1 ATOM 1026 C CD2 . TRP A 1 134 ? 21.930 20.965 8.282 1.00 8.43 ? 134 TRP A CD2 1 ATOM 1027 N NE1 . TRP A 1 134 ? 21.991 21.078 6.046 1.00 7.00 ? 134 TRP A NE1 1 ATOM 1028 C CE2 . TRP A 1 134 ? 21.619 21.773 7.163 1.00 8.41 ? 134 TRP A CE2 1 ATOM 1029 C CE3 . TRP A 1 134 ? 21.655 21.487 9.549 1.00 9.84 ? 134 TRP A CE3 1 ATOM 1030 C CZ2 . TRP A 1 134 ? 21.072 23.047 7.285 1.00 9.40 ? 134 TRP A CZ2 1 ATOM 1031 C CZ3 . TRP A 1 134 ? 21.096 22.746 9.684 1.00 9.19 ? 134 TRP A CZ3 1 ATOM 1032 C CH2 . TRP A 1 134 ? 20.791 23.536 8.538 1.00 10.97 ? 134 TRP A CH2 1 ATOM 1033 N N . TYR A 1 135 ? 24.743 20.082 10.821 1.00 8.27 ? 135 TYR A N 1 ATOM 1034 C CA . TYR A 1 135 ? 25.021 21.294 11.565 1.00 9.04 ? 135 TYR A CA 1 ATOM 1035 C C . TYR A 1 135 ? 26.476 21.773 11.450 1.00 10.16 ? 135 TYR A C 1 ATOM 1036 O O . TYR A 1 135 ? 26.800 22.990 11.576 1.00 9.71 ? 135 TYR A O 1 ATOM 1037 C CB . TYR A 1 135 ? 24.626 21.165 13.068 1.00 8.83 ? 135 TYR A CB 1 ATOM 1038 C CG . TYR A 1 135 ? 23.136 20.937 13.255 1.00 8.58 ? 135 TYR A CG 1 ATOM 1039 C CD1 . TYR A 1 135 ? 22.250 22.009 13.194 1.00 6.81 ? 135 TYR A CD1 1 ATOM 1040 C CD2 . TYR A 1 135 ? 22.604 19.699 13.461 1.00 8.11 ? 135 TYR A CD2 1 ATOM 1041 C CE1 . TYR A 1 135 ? 20.870 21.862 13.325 1.00 6.87 ? 135 TYR A CE1 1 ATOM 1042 C CE2 . TYR A 1 135 ? 21.219 19.508 13.569 1.00 7.66 ? 135 TYR A CE2 1 ATOM 1043 C CZ . TYR A 1 135 ? 20.360 20.593 13.503 1.00 7.16 ? 135 TYR A CZ 1 ATOM 1044 O OH . TYR A 1 135 ? 18.984 20.416 13.614 1.00 5.46 ? 135 TYR A OH 1 ATOM 1045 N N . THR A 1 136 ? 27.408 20.832 11.266 1.00 9.14 ? 136 THR A N 1 ATOM 1046 C CA . THR A 1 136 ? 28.837 21.084 11.125 1.00 9.89 ? 136 THR A CA 1 ATOM 1047 C C . THR A 1 136 ? 29.465 20.728 9.777 1.00 9.80 ? 136 THR A C 1 ATOM 1048 O O . THR A 1 136 ? 30.725 20.700 9.627 1.00 9.64 ? 136 THR A O 1 ATOM 1049 C CB . THR A 1 136 ? 29.650 20.383 12.246 1.00 9.61 ? 136 THR A CB 1 ATOM 1050 O OG1 . THR A 1 136 ? 29.504 18.951 12.206 1.00 9.97 ? 136 THR A OG1 1 ATOM 1051 C CG2 . THR A 1 136 ? 29.282 20.905 13.620 1.00 11.98 ? 136 THR A CG2 1 ATOM 1052 N N . ASN A 1 137 ? 28.671 20.386 8.769 1.00 7.28 ? 137 ASN A N 1 ATOM 1053 C CA . ASN A 1 137 ? 29.144 20.119 7.394 1.00 7.84 ? 137 ASN A CA 1 ATOM 1054 C C . ASN A 1 137 ? 29.465 21.422 6.672 1.00 9.20 ? 137 ASN A C 1 ATOM 1055 O O . ASN A 1 137 ? 28.621 22.301 6.421 1.00 9.10 ? 137 ASN A O 1 ATOM 1056 C CB . ASN A 1 137 ? 28.038 19.308 6.689 1.00 8.82 ? 137 ASN A CB 1 ATOM 1057 C CG . ASN A 1 137 ? 28.340 18.875 5.281 1.00 10.94 ? 137 ASN A CG 1 ATOM 1058 O OD1 . ASN A 1 137 ? 28.640 19.667 4.400 1.00 12.10 ? 137 ASN A OD1 1 ATOM 1059 N ND2 . ASN A 1 137 ? 28.247 17.609 4.931 1.00 11.98 ? 137 ASN A ND2 1 ATOM 1060 N N . THR A 1 138 ? 30.761 21.654 6.335 1.00 9.75 ? 138 THR A N 1 ATOM 1061 C CA . THR A 1 138 ? 31.174 22.933 5.771 1.00 11.06 ? 138 THR A CA 1 ATOM 1062 C C . THR A 1 138 ? 30.475 23.333 4.482 1.00 10.54 ? 138 THR A C 1 ATOM 1063 O O . THR A 1 138 ? 29.946 24.462 4.380 1.00 9.66 ? 138 THR A O 1 ATOM 1064 C CB . THR A 1 138 ? 32.715 22.917 5.607 1.00 12.67 ? 138 THR A CB 1 ATOM 1065 O OG1 . THR A 1 138 ? 33.322 22.585 6.876 1.00 13.57 ? 138 THR A OG1 1 ATOM 1066 C CG2 . THR A 1 138 ? 33.326 24.220 5.147 1.00 13.11 ? 138 THR A CG2 1 ATOM 1067 N N . ALA A 1 139 ? 30.349 22.448 3.504 1.00 10.25 ? 139 ALA A N 1 ATOM 1068 C CA . ALA A 1 139 ? 29.683 22.801 2.235 1.00 10.83 ? 139 ALA A CA 1 ATOM 1069 C C . ALA A 1 139 ? 28.182 23.043 2.406 1.00 9.95 ? 139 ALA A C 1 ATOM 1070 O O . ALA A 1 139 ? 27.590 23.954 1.783 1.00 8.27 ? 139 ALA A O 1 ATOM 1071 C CB . ALA A 1 139 ? 29.893 21.741 1.163 1.00 10.63 ? 139 ALA A CB 1 ATOM 1072 N N . ALA A 1 140 ? 27.565 22.232 3.277 1.00 8.72 ? 140 ALA A N 1 ATOM 1073 C CA . ALA A 1 140 ? 26.116 22.462 3.510 1.00 9.02 ? 140 ALA A CA 1 ATOM 1074 C C . ALA A 1 140 ? 25.826 23.797 4.181 1.00 9.10 ? 140 ALA A C 1 ATOM 1075 O O . ALA A 1 140 ? 24.875 24.495 3.804 1.00 8.15 ? 140 ALA A O 1 ATOM 1076 C CB . ALA A 1 140 ? 25.558 21.311 4.339 1.00 8.99 ? 140 ALA A CB 1 ATOM 1077 N N . GLN A 1 141 ? 26.586 24.166 5.214 1.00 8.35 ? 141 GLN A N 1 ATOM 1078 C CA . GLN A 1 141 ? 26.428 25.439 5.909 1.00 9.13 ? 141 GLN A CA 1 ATOM 1079 C C . GLN A 1 141 ? 26.765 26.631 5.020 1.00 9.63 ? 141 GLN A C 1 ATOM 1080 O O . GLN A 1 141 ? 26.074 27.653 5.109 1.00 9.71 ? 141 GLN A O 1 ATOM 1081 C CB . GLN A 1 141 ? 27.228 25.462 7.227 1.00 10.22 ? 141 GLN A CB 1 ATOM 1082 C CG . GLN A 1 141 ? 26.682 24.519 8.298 1.00 9.96 ? 141 GLN A CG 1 ATOM 1083 C CD . GLN A 1 141 ? 25.221 24.713 8.641 1.00 10.17 ? 141 GLN A CD 1 ATOM 1084 O OE1 . GLN A 1 141 ? 24.790 25.836 8.929 1.00 8.46 ? 141 GLN A OE1 1 ATOM 1085 N NE2 . GLN A 1 141 ? 24.478 23.609 8.591 1.00 9.60 ? 141 GLN A NE2 1 ATOM 1086 N N . THR A 1 142 ? 27.774 26.541 4.140 1.00 8.74 ? 142 THR A N 1 ATOM 1087 C CA . THR A 1 142 ? 28.067 27.633 3.207 1.00 10.09 ? 142 THR A CA 1 ATOM 1088 C C . THR A 1 142 ? 26.862 27.898 2.289 1.00 10.28 ? 142 THR A C 1 ATOM 1089 O O . THR A 1 142 ? 26.476 29.064 2.088 1.00 8.38 ? 142 THR A O 1 ATOM 1090 C CB . THR A 1 142 ? 29.335 27.310 2.368 1.00 11.43 ? 142 THR A CB 1 ATOM 1091 O OG1 . THR A 1 142 ? 30.504 27.255 3.228 1.00 12.07 ? 142 THR A OG1 1 ATOM 1092 C CG2 . THR A 1 142 ? 29.575 28.340 1.275 1.00 11.28 ? 142 THR A CG2 1 ATOM 1093 N N . GLN A 1 143 ? 26.197 26.852 1.780 1.00 9.55 ? 143 GLN A N 1 ATOM 1094 C CA . GLN A 1 143 ? 25.038 27.050 0.896 1.00 8.98 ? 143 GLN A CA 1 ATOM 1095 C C . GLN A 1 143 ? 23.811 27.522 1.668 1.00 9.44 ? 143 GLN A C 1 ATOM 1096 O O . GLN A 1 143 ? 23.060 28.363 1.138 1.00 7.44 ? 143 GLN A O 1 ATOM 1097 C CB . GLN A 1 143 ? 24.742 25.784 0.073 1.00 10.22 ? 143 GLN A CB 1 ATOM 1098 C CG . GLN A 1 143 ? 23.673 25.979 -0.996 1.00 10.31 ? 143 GLN A CG 1 ATOM 1099 C CD . GLN A 1 143 ? 23.994 26.993 -2.068 1.00 12.07 ? 143 GLN A CD 1 ATOM 1100 O OE1 . GLN A 1 143 ? 25.174 27.164 -2.479 1.00 12.30 ? 143 GLN A OE1 1 ATOM 1101 N NE2 . GLN A 1 143 ? 22.999 27.706 -2.594 1.00 9.94 ? 143 GLN A NE2 1 ATOM 1102 N N . TYR A 1 144 ? 23.584 27.023 2.893 1.00 8.73 ? 144 TYR A N 1 ATOM 1103 C CA . TYR A 1 144 ? 22.455 27.478 3.717 1.00 9.14 ? 144 TYR A CA 1 ATOM 1104 C C . TYR A 1 144 ? 22.537 28.975 3.976 1.00 8.64 ? 144 TYR A C 1 ATOM 1105 O O . TYR A 1 144 ? 21.548 29.712 3.902 1.00 6.36 ? 144 TYR A O 1 ATOM 1106 C CB . TYR A 1 144 ? 22.362 26.679 5.030 1.00 8.29 ? 144 TYR A CB 1 ATOM 1107 C CG . TYR A 1 144 ? 21.442 27.173 6.132 1.00 8.16 ? 144 TYR A CG 1 ATOM 1108 C CD1 . TYR A 1 144 ? 20.073 26.939 6.099 1.00 7.10 ? 144 TYR A CD1 1 ATOM 1109 C CD2 . TYR A 1 144 ? 21.926 27.846 7.245 1.00 9.54 ? 144 TYR A CD2 1 ATOM 1110 C CE1 . TYR A 1 144 ? 19.241 27.386 7.109 1.00 7.00 ? 144 TYR A CE1 1 ATOM 1111 C CE2 . TYR A 1 144 ? 21.116 28.278 8.276 1.00 9.16 ? 144 TYR A CE2 1 ATOM 1112 C CZ . TYR A 1 144 ? 19.747 28.057 8.207 1.00 8.90 ? 144 TYR A CZ 1 ATOM 1113 O OH . TYR A 1 144 ? 18.956 28.539 9.235 1.00 7.58 ? 144 TYR A OH 1 ATOM 1114 N N . ARG A 1 145 ? 23.724 29.484 4.322 1.00 8.90 ? 145 ARG A N 1 ATOM 1115 C CA . ARG A 1 145 ? 23.967 30.888 4.582 1.00 9.52 ? 145 ARG A CA 1 ATOM 1116 C C . ARG A 1 145 ? 23.778 31.737 3.314 1.00 9.51 ? 145 ARG A C 1 ATOM 1117 O O . ARG A 1 145 ? 23.230 32.848 3.369 1.00 8.42 ? 145 ARG A O 1 ATOM 1118 C CB . ARG A 1 145 ? 25.337 31.163 5.200 1.00 9.40 ? 145 ARG A CB 1 ATOM 1119 C CG . ARG A 1 145 ? 25.513 30.694 6.631 1.00 12.63 ? 145 ARG A CG 1 ATOM 1120 C CD . ARG A 1 145 ? 26.878 31.125 7.244 1.00 14.67 ? 145 ARG A CD 1 ATOM 1121 N NE . ARG A 1 145 ? 26.802 30.727 8.637 1.00 16.64 ? 145 ARG A NE 1 ATOM 1122 C CZ . ARG A 1 145 ? 27.208 31.365 9.713 1.00 17.17 ? 145 ARG A CZ 1 ATOM 1123 N NH1 . ARG A 1 145 ? 27.787 32.580 9.671 1.00 15.79 ? 145 ARG A NH1 1 ATOM 1124 N NH2 . ARG A 1 145 ? 26.977 30.710 10.848 1.00 18.51 ? 145 ARG A NH2 1 ATOM 1125 N N . LYS A 1 146 ? 24.145 31.232 2.137 1.00 9.33 ? 146 LYS A N 1 ATOM 1126 C CA . LYS A 1 146 ? 23.847 31.937 0.884 1.00 10.57 ? 146 LYS A CA 1 ATOM 1127 C C . LYS A 1 146 ? 22.328 32.022 0.635 1.00 10.51 ? 146 LYS A C 1 ATOM 1128 O O . LYS A 1 146 ? 21.834 33.074 0.167 1.00 9.20 ? 146 LYS A O 1 ATOM 1129 C CB . LYS A 1 146 ? 24.477 31.242 -0.316 1.00 13.32 ? 146 LYS A CB 1 ATOM 1130 C CG . LYS A 1 146 ? 25.960 31.447 -0.565 1.00 17.94 ? 146 LYS A CG 1 ATOM 1131 C CD . LYS A 1 146 ? 26.356 30.955 -1.966 1.00 22.34 ? 146 LYS A CD 1 ATOM 1132 C CE . LYS A 1 146 ? 25.334 31.296 -3.024 1.00 25.89 ? 146 LYS A CE 1 ATOM 1133 N NZ . LYS A 1 146 ? 25.843 31.725 -4.358 1.00 29.39 ? 146 LYS A NZ 1 ATOM 1134 N N . TYR A 1 147 ? 21.600 30.951 0.955 1.00 8.89 ? 147 TYR A N 1 ATOM 1135 C CA . TYR A 1 147 ? 20.121 30.959 0.821 1.00 7.55 ? 147 TYR A CA 1 ATOM 1136 C C . TYR A 1 147 ? 19.504 31.955 1.790 1.00 8.88 ? 147 TYR A C 1 ATOM 1137 O O . TYR A 1 147 ? 18.622 32.764 1.419 1.00 7.99 ? 147 TYR A O 1 ATOM 1138 C CB . TYR A 1 147 ? 19.543 29.516 0.876 1.00 7.09 ? 147 TYR A CB 1 ATOM 1139 C CG . TYR A 1 147 ? 18.034 29.497 0.614 1.00 8.07 ? 147 TYR A CG 1 ATOM 1140 C CD1 . TYR A 1 147 ? 17.572 29.709 -0.678 1.00 8.12 ? 147 TYR A CD1 1 ATOM 1141 C CD2 . TYR A 1 147 ? 17.109 29.360 1.633 1.00 8.98 ? 147 TYR A CD2 1 ATOM 1142 C CE1 . TYR A 1 147 ? 16.214 29.817 -0.960 1.00 8.18 ? 147 TYR A CE1 1 ATOM 1143 C CE2 . TYR A 1 147 ? 15.741 29.447 1.361 1.00 8.23 ? 147 TYR A CE2 1 ATOM 1144 C CZ . TYR A 1 147 ? 15.310 29.683 0.068 1.00 7.60 ? 147 TYR A CZ 1 ATOM 1145 O OH . TYR A 1 147 ? 13.949 29.803 -0.243 1.00 7.08 ? 147 TYR A OH 1 ATOM 1146 N N . VAL A 1 148 ? 19.951 32.039 3.052 1.00 8.80 ? 148 VAL A N 1 ATOM 1147 C CA . VAL A 1 148 ? 19.505 33.035 4.024 1.00 7.71 ? 148 VAL A CA 1 ATOM 1148 C C . VAL A 1 148 ? 19.685 34.461 3.471 1.00 9.66 ? 148 VAL A C 1 ATOM 1149 O O . VAL A 1 148 ? 18.741 35.246 3.537 1.00 8.65 ? 148 VAL A O 1 ATOM 1150 C CB . VAL A 1 148 ? 20.201 32.900 5.403 1.00 7.46 ? 148 VAL A CB 1 ATOM 1151 C CG1 . VAL A 1 148 ? 19.898 34.072 6.346 1.00 7.56 ? 148 VAL A CG1 1 ATOM 1152 C CG2 . VAL A 1 148 ? 19.855 31.583 6.112 1.00 6.76 ? 148 VAL A CG2 1 ATOM 1153 N N . GLN A 1 149 ? 20.855 34.816 2.873 1.00 9.94 ? 149 GLN A N 1 ATOM 1154 C CA . GLN A 1 149 ? 21.032 36.173 2.343 1.00 10.44 ? 149 GLN A CA 1 ATOM 1155 C C . GLN A 1 149 ? 20.094 36.442 1.162 1.00 10.22 ? 149 GLN A C 1 ATOM 1156 O O . GLN A 1 149 ? 19.570 37.564 1.076 1.00 10.53 ? 149 GLN A O 1 ATOM 1157 C CB . GLN A 1 149 ? 22.486 36.501 1.936 1.00 10.56 ? 149 GLN A CB 1 ATOM 1158 C CG . GLN A 1 149 ? 22.710 37.950 1.514 1.00 11.36 ? 149 GLN A CG 1 ATOM 1159 C CD . GLN A 1 149 ? 24.127 38.453 1.394 1.00 13.07 ? 149 GLN A CD 1 ATOM 1160 O OE1 . GLN A 1 149 ? 25.075 37.702 1.198 1.00 13.84 ? 149 GLN A OE1 1 ATOM 1161 N NE2 . GLN A 1 149 ? 24.344 39.785 1.491 1.00 13.55 ? 149 GLN A NE2 1 ATOM 1162 N N . ALA A 1 150 ? 19.878 35.464 0.295 1.00 8.12 ? 150 ALA A N 1 ATOM 1163 C CA . ALA A 1 150 ? 18.949 35.655 -0.834 1.00 9.03 ? 150 ALA A CA 1 ATOM 1164 C C . ALA A 1 150 ? 17.515 35.964 -0.388 1.00 10.41 ? 150 ALA A C 1 ATOM 1165 O O . ALA A 1 150 ? 16.831 36.728 -1.080 1.00 10.90 ? 150 ALA A O 1 ATOM 1166 C CB . ALA A 1 150 ? 18.958 34.483 -1.779 1.00 8.16 ? 150 ALA A CB 1 ATOM 1167 N N . VAL A 1 151 ? 17.021 35.331 0.671 1.00 10.14 ? 151 VAL A N 1 ATOM 1168 C CA . VAL A 1 151 ? 15.670 35.618 1.168 1.00 8.98 ? 151 VAL A CA 1 ATOM 1169 C C . VAL A 1 151 ? 15.631 36.930 1.945 1.00 9.53 ? 151 VAL A C 1 ATOM 1170 O O . VAL A 1 151 ? 14.795 37.790 1.657 1.00 8.32 ? 151 VAL A O 1 ATOM 1171 C CB . VAL A 1 151 ? 15.175 34.447 2.058 1.00 8.97 ? 151 VAL A CB 1 ATOM 1172 C CG1 . VAL A 1 151 ? 13.799 34.750 2.677 1.00 8.07 ? 151 VAL A CG1 1 ATOM 1173 C CG2 . VAL A 1 151 ? 15.077 33.180 1.209 1.00 8.92 ? 151 VAL A CG2 1 ATOM 1174 N N . VAL A 1 152 ? 16.546 37.141 2.921 1.00 7.83 ? 152 VAL A N 1 ATOM 1175 C CA . VAL A 1 152 ? 16.487 38.333 3.788 1.00 8.33 ? 152 VAL A CA 1 ATOM 1176 C C . VAL A 1 152 ? 16.629 39.617 2.998 1.00 8.92 ? 152 VAL A C 1 ATOM 1177 O O . VAL A 1 152 ? 15.907 40.608 3.253 1.00 9.30 ? 152 VAL A O 1 ATOM 1178 C CB . VAL A 1 152 ? 17.526 38.242 4.943 1.00 7.90 ? 152 VAL A CB 1 ATOM 1179 C CG1 . VAL A 1 152 ? 17.657 39.535 5.749 1.00 8.39 ? 152 VAL A CG1 1 ATOM 1180 C CG2 . VAL A 1 152 ? 17.142 37.100 5.908 1.00 7.68 ? 152 VAL A CG2 1 ATOM 1181 N N . SER A 1 153 ? 17.550 39.650 2.048 1.00 9.58 ? 153 SER A N 1 ATOM 1182 C CA . SER A 1 153 ? 17.800 40.831 1.217 1.00 10.82 ? 153 SER A CA 1 ATOM 1183 C C . SER A 1 153 ? 16.575 41.264 0.392 1.00 11.61 ? 153 SER A C 1 ATOM 1184 O O . SER A 1 153 ? 16.560 42.437 0.005 1.00 11.24 ? 153 SER A O 1 ATOM 1185 C CB . SER A 1 153 ? 19.028 40.624 0.345 1.00 12.12 ? 153 SER A CB 1 ATOM 1186 O OG . SER A 1 153 ? 18.823 39.637 -0.669 1.00 11.85 ? 153 SER A OG 1 ATOM 1187 N N . ARG A 1 154 ? 15.578 40.420 0.136 1.00 9.50 ? 154 ARG A N 1 ATOM 1188 C CA . ARG A 1 154 ? 14.377 40.850 -0.578 1.00 9.26 ? 154 ARG A CA 1 ATOM 1189 C C . ARG A 1 154 ? 13.433 41.653 0.302 1.00 9.25 ? 154 ARG A C 1 ATOM 1190 O O . ARG A 1 154 ? 12.681 42.504 -0.230 1.00 9.81 ? 154 ARG A O 1 ATOM 1191 C CB . ARG A 1 154 ? 13.584 39.653 -1.173 1.00 9.16 ? 154 ARG A CB 1 ATOM 1192 C CG . ARG A 1 154 ? 14.355 38.739 -2.089 1.00 9.37 ? 154 ARG A CG 1 ATOM 1193 C CD . ARG A 1 154 ? 13.584 37.593 -2.697 1.00 10.09 ? 154 ARG A CD 1 ATOM 1194 N NE . ARG A 1 154 ? 12.813 37.883 -3.897 1.00 10.64 ? 154 ARG A NE 1 ATOM 1195 C CZ . ARG A 1 154 ? 13.212 37.986 -5.138 1.00 12.36 ? 154 ARG A CZ 1 ATOM 1196 N NH1 . ARG A 1 154 ? 14.518 37.814 -5.395 1.00 12.26 ? 154 ARG A NH1 1 ATOM 1197 N NH2 . ARG A 1 154 ? 12.361 38.270 -6.131 1.00 11.88 ? 154 ARG A NH2 1 ATOM 1198 N N . TYR A 1 155 ? 13.330 41.344 1.609 1.00 8.57 ? 155 TYR A N 1 ATOM 1199 C CA . TYR A 1 155 ? 12.313 41.877 2.485 1.00 8.84 ? 155 TYR A CA 1 ATOM 1200 C C . TYR A 1 155 ? 12.820 42.611 3.713 1.00 8.95 ? 155 TYR A C 1 ATOM 1201 O O . TYR A 1 155 ? 12.022 42.951 4.597 1.00 8.55 ? 155 TYR A O 1 ATOM 1202 C CB . TYR A 1 155 ? 11.344 40.716 2.950 1.00 8.46 ? 155 TYR A CB 1 ATOM 1203 C CG . TYR A 1 155 ? 10.974 39.713 1.867 1.00 8.06 ? 155 TYR A CG 1 ATOM 1204 C CD1 . TYR A 1 155 ? 10.352 40.080 0.682 1.00 8.80 ? 155 TYR A CD1 1 ATOM 1205 C CD2 . TYR A 1 155 ? 11.272 38.361 1.992 1.00 8.73 ? 155 TYR A CD2 1 ATOM 1206 C CE1 . TYR A 1 155 ? 10.047 39.174 -0.329 1.00 9.12 ? 155 TYR A CE1 1 ATOM 1207 C CE2 . TYR A 1 155 ? 11.002 37.430 0.993 1.00 10.82 ? 155 TYR A CE2 1 ATOM 1208 C CZ . TYR A 1 155 ? 10.354 37.841 -0.163 1.00 11.12 ? 155 TYR A CZ 1 ATOM 1209 O OH . TYR A 1 155 ? 10.050 36.901 -1.135 1.00 10.84 ? 155 TYR A OH 1 ATOM 1210 N N . ALA A 1 156 ? 14.104 42.893 3.898 1.00 10.14 ? 156 ALA A N 1 ATOM 1211 C CA . ALA A 1 156 ? 14.630 43.529 5.132 1.00 9.31 ? 156 ALA A CA 1 ATOM 1212 C C . ALA A 1 156 ? 14.027 44.865 5.518 1.00 10.35 ? 156 ALA A C 1 ATOM 1213 O O . ALA A 1 156 ? 13.994 45.179 6.746 1.00 8.20 ? 156 ALA A O 1 ATOM 1214 C CB . ALA A 1 156 ? 16.161 43.625 5.039 1.00 8.38 ? 156 ALA A CB 1 ATOM 1215 N N . ASN A 1 157 ? 13.494 45.639 4.551 1.00 9.26 ? 157 ASN A N 1 ATOM 1216 C CA . ASN A 1 157 ? 12.866 46.913 4.819 1.00 9.81 ? 157 ASN A CA 1 ATOM 1217 C C . ASN A 1 157 ? 11.340 46.908 4.736 1.00 9.82 ? 157 ASN A C 1 ATOM 1218 O O . ASN A 1 157 ? 10.733 47.961 4.935 1.00 9.75 ? 157 ASN A O 1 ATOM 1219 C CB . ASN A 1 157 ? 13.428 48.044 3.934 1.00 9.91 ? 157 ASN A CB 1 ATOM 1220 C CG . ASN A 1 157 ? 14.903 48.135 4.106 1.00 10.79 ? 157 ASN A CG 1 ATOM 1221 O OD1 . ASN A 1 157 ? 15.802 47.427 3.631 1.00 12.23 ? 157 ASN A OD1 1 ATOM 1222 N ND2 . ASN A 1 157 ? 15.396 49.125 4.909 1.00 8.86 ? 157 ASN A ND2 1 ATOM 1223 N N . SER A 1 158 ? 10.728 45.736 4.522 1.00 8.66 ? 158 SER A N 1 ATOM 1224 C CA . SER A 1 158 ? 9.271 45.630 4.607 1.00 8.35 ? 158 SER A CA 1 ATOM 1225 C C . SER A 1 158 ? 8.754 45.591 6.042 1.00 9.12 ? 158 SER A C 1 ATOM 1226 O O . SER A 1 158 ? 9.279 44.853 6.896 1.00 8.66 ? 158 SER A O 1 ATOM 1227 C CB . SER A 1 158 ? 8.763 44.386 3.869 1.00 8.19 ? 158 SER A CB 1 ATOM 1228 O OG . SER A 1 158 ? 7.351 44.190 4.135 1.00 6.54 ? 158 SER A OG 1 ATOM 1229 N N . THR A 1 159 ? 7.661 46.328 6.339 1.00 8.42 ? 159 THR A N 1 ATOM 1230 C CA . THR A 1 159 ? 7.015 46.324 7.632 1.00 8.53 ? 159 THR A CA 1 ATOM 1231 C C . THR A 1 159 ? 6.125 45.094 7.851 1.00 8.36 ? 159 THR A C 1 ATOM 1232 O O . THR A 1 159 ? 5.618 44.921 8.962 1.00 8.60 ? 159 THR A O 1 ATOM 1233 C CB . THR A 1 159 ? 6.207 47.605 7.942 1.00 9.20 ? 159 THR A CB 1 ATOM 1234 O OG1 . THR A 1 159 ? 5.328 47.949 6.832 1.00 9.36 ? 159 THR A OG1 1 ATOM 1235 C CG2 . THR A 1 159 ? 7.152 48.771 8.223 1.00 9.82 ? 159 THR A CG2 1 ATOM 1236 N N . ALA A 1 160 ? 5.952 44.189 6.907 1.00 8.07 ? 160 ALA A N 1 ATOM 1237 C CA . ALA A 1 160 ? 5.147 42.983 7.069 1.00 9.31 ? 160 ALA A CA 1 ATOM 1238 C C . ALA A 1 160 ? 5.836 41.778 7.721 1.00 10.42 ? 160 ALA A C 1 ATOM 1239 O O . ALA A 1 160 ? 5.125 40.774 7.971 1.00 8.87 ? 160 ALA A O 1 ATOM 1240 C CB . ALA A 1 160 ? 4.523 42.569 5.722 1.00 10.28 ? 160 ALA A CB 1 ATOM 1241 N N . ILE A 1 161 ? 7.135 41.800 8.010 1.00 9.10 ? 161 ILE A N 1 ATOM 1242 C CA . ILE A 1 161 ? 7.802 40.647 8.656 1.00 9.12 ? 161 ILE A CA 1 ATOM 1243 C C . ILE A 1 161 ? 7.679 40.690 10.178 1.00 9.45 ? 161 ILE A C 1 ATOM 1244 O O . ILE A 1 161 ? 8.107 41.669 10.795 1.00 8.56 ? 161 ILE A O 1 ATOM 1245 C CB . ILE A 1 161 ? 9.300 40.587 8.259 1.00 10.36 ? 161 ILE A CB 1 ATOM 1246 C CG1 . ILE A 1 161 ? 9.534 40.669 6.747 1.00 9.17 ? 161 ILE A CG1 1 ATOM 1247 C CG2 . ILE A 1 161 ? 10.004 39.372 8.852 1.00 8.96 ? 161 ILE A CG2 1 ATOM 1248 C CD1 . ILE A 1 161 ? 8.778 39.608 5.945 1.00 10.82 ? 161 ILE A CD1 1 ATOM 1249 N N . PHE A 1 162 ? 7.115 39.679 10.840 1.00 8.52 ? 162 PHE A N 1 ATOM 1250 C CA . PHE A 1 162 ? 7.069 39.579 12.302 1.00 8.42 ? 162 PHE A CA 1 ATOM 1251 C C . PHE A 1 162 ? 8.458 39.122 12.805 1.00 9.62 ? 162 PHE A C 1 ATOM 1252 O O . PHE A 1 162 ? 9.067 39.745 13.706 1.00 9.29 ? 162 PHE A O 1 ATOM 1253 C CB . PHE A 1 162 ? 6.001 38.594 12.796 1.00 8.73 ? 162 PHE A CB 1 ATOM 1254 C CG . PHE A 1 162 ? 5.722 38.533 14.281 1.00 9.46 ? 162 PHE A CG 1 ATOM 1255 C CD1 . PHE A 1 162 ? 6.561 37.853 15.151 1.00 8.92 ? 162 PHE A CD1 1 ATOM 1256 C CD2 . PHE A 1 162 ? 4.596 39.129 14.831 1.00 9.25 ? 162 PHE A CD2 1 ATOM 1257 C CE1 . PHE A 1 162 ? 6.302 37.822 16.511 1.00 8.18 ? 162 PHE A CE1 1 ATOM 1258 C CE2 . PHE A 1 162 ? 4.321 39.099 16.169 1.00 7.79 ? 162 PHE A CE2 1 ATOM 1259 C CZ . PHE A 1 162 ? 5.173 38.428 17.027 1.00 7.94 ? 162 PHE A CZ 1 ATOM 1260 N N . ALA A 1 163 ? 8.958 38.015 12.245 1.00 7.91 ? 163 ALA A N 1 ATOM 1261 C CA . ALA A 1 163 ? 10.312 37.511 12.558 1.00 7.90 ? 163 ALA A CA 1 ATOM 1262 C C . ALA A 1 163 ? 10.894 36.541 11.542 1.00 8.17 ? 163 ALA A C 1 ATOM 1263 O O . ALA A 1 163 ? 10.150 35.785 10.901 1.00 7.91 ? 163 ALA A O 1 ATOM 1264 C CB . ALA A 1 163 ? 10.353 36.786 13.920 1.00 7.78 ? 163 ALA A CB 1 ATOM 1265 N N . TRP A 1 164 ? 12.240 36.478 11.466 1.00 6.47 ? 164 TRP A N 1 ATOM 1266 C CA . TRP A 1 164 ? 12.933 35.419 10.725 1.00 6.77 ? 164 TRP A CA 1 ATOM 1267 C C . TRP A 1 164 ? 13.071 34.220 11.682 1.00 6.80 ? 164 TRP A C 1 ATOM 1268 O O . TRP A 1 164 ? 13.264 34.437 12.888 1.00 8.24 ? 164 TRP A O 1 ATOM 1269 C CB . TRP A 1 164 ? 14.319 35.885 10.286 1.00 6.86 ? 164 TRP A CB 1 ATOM 1270 C CG . TRP A 1 164 ? 14.302 37.069 9.360 1.00 8.13 ? 164 TRP A CG 1 ATOM 1271 C CD1 . TRP A 1 164 ? 14.864 38.284 9.608 1.00 8.22 ? 164 TRP A CD1 1 ATOM 1272 C CD2 . TRP A 1 164 ? 13.716 37.138 8.063 1.00 9.28 ? 164 TRP A CD2 1 ATOM 1273 N NE1 . TRP A 1 164 ? 14.617 39.144 8.535 1.00 8.93 ? 164 TRP A NE1 1 ATOM 1274 C CE2 . TRP A 1 164 ? 13.912 38.439 7.586 1.00 8.71 ? 164 TRP A CE2 1 ATOM 1275 C CE3 . TRP A 1 164 ? 12.977 36.241 7.277 1.00 8.84 ? 164 TRP A CE3 1 ATOM 1276 C CZ2 . TRP A 1 164 ? 13.478 38.866 6.325 1.00 10.43 ? 164 TRP A CZ2 1 ATOM 1277 C CZ3 . TRP A 1 164 ? 12.520 36.676 6.024 1.00 10.41 ? 164 TRP A CZ3 1 ATOM 1278 C CH2 . TRP A 1 164 ? 12.786 37.983 5.572 1.00 10.67 ? 164 TRP A CH2 1 ATOM 1279 N N . GLU A 1 165 ? 12.997 32.995 11.170 1.00 5.74 ? 165 GLU A N 1 ATOM 1280 C CA . GLU A 1 165 ? 13.075 31.758 11.965 1.00 6.61 ? 165 GLU A CA 1 ATOM 1281 C C . GLU A 1 165 ? 14.125 30.809 11.412 1.00 6.49 ? 165 GLU A C 1 ATOM 1282 O O . GLU A 1 165 ? 14.135 30.551 10.197 1.00 6.22 ? 165 GLU A O 1 ATOM 1283 C CB . GLU A 1 165 ? 11.685 31.120 12.044 1.00 6.05 ? 165 GLU A CB 1 ATOM 1284 C CG . GLU A 1 165 ? 11.482 29.845 12.837 1.00 6.81 ? 165 GLU A CG 1 ATOM 1285 C CD . GLU A 1 165 ? 10.011 29.613 13.208 1.00 8.55 ? 165 GLU A CD 1 ATOM 1286 O OE1 . GLU A 1 165 ? 9.574 30.130 14.278 1.00 5.97 ? 165 GLU A OE1 1 ATOM 1287 O OE2 . GLU A 1 165 ? 9.327 28.898 12.431 1.00 6.80 ? 165 GLU A OE2 1 ATOM 1288 N N . LEU A 1 166 ? 15.065 30.263 12.240 1.00 7.13 ? 166 LEU A N 1 ATOM 1289 C CA . LEU A 1 166 ? 16.157 29.456 11.697 1.00 6.16 ? 166 LEU A CA 1 ATOM 1290 C C . LEU A 1 166 ? 15.694 28.170 11.023 1.00 7.03 ? 166 LEU A C 1 ATOM 1291 O O . LEU A 1 166 ? 16.242 27.809 9.969 1.00 6.50 ? 166 LEU A O 1 ATOM 1292 C CB . LEU A 1 166 ? 17.210 29.225 12.808 1.00 5.96 ? 166 LEU A CB 1 ATOM 1293 C CG . LEU A 1 166 ? 17.742 30.426 13.585 1.00 8.60 ? 166 LEU A CG 1 ATOM 1294 C CD1 . LEU A 1 166 ? 19.024 30.033 14.347 1.00 7.76 ? 166 LEU A CD1 1 ATOM 1295 C CD2 . LEU A 1 166 ? 18.009 31.651 12.717 1.00 8.78 ? 166 LEU A CD2 1 ATOM 1296 N N . GLY A 1 167 ? 14.688 27.433 11.534 1.00 6.24 ? 167 GLY A N 1 ATOM 1297 C CA . GLY A 1 167 ? 14.161 26.270 10.860 1.00 5.54 ? 167 GLY A CA 1 ATOM 1298 C C . GLY A 1 167 ? 12.817 25.789 11.427 1.00 6.04 ? 167 GLY A C 1 ATOM 1299 O O . GLY A 1 167 ? 12.391 26.288 12.464 1.00 5.95 ? 167 GLY A O 1 ATOM 1300 N N . ASN A 1 168 ? 12.208 24.784 10.796 1.00 5.04 ? 168 ASN A N 1 ATOM 1301 C CA . ASN A 1 168 ? 10.972 24.159 11.302 1.00 5.79 ? 168 ASN A CA 1 ATOM 1302 C C . ASN A 1 168 ? 11.387 22.904 12.104 1.00 7.05 ? 168 ASN A C 1 ATOM 1303 O O . ASN A 1 168 ? 11.887 21.933 11.537 1.00 5.21 ? 168 ASN A O 1 ATOM 1304 C CB . ASN A 1 168 ? 10.001 23.748 10.185 1.00 5.75 ? 168 ASN A CB 1 ATOM 1305 C CG . ASN A 1 168 ? 8.780 22.949 10.643 1.00 7.14 ? 168 ASN A CG 1 ATOM 1306 O OD1 . ASN A 1 168 ? 8.053 23.457 11.518 1.00 8.19 ? 168 ASN A OD1 1 ATOM 1307 N ND2 . ASN A 1 168 ? 8.467 21.758 10.167 1.00 7.74 ? 168 ASN A ND2 1 ATOM 1308 N N . GLU A 1 169 ? 11.298 22.974 13.432 1.00 5.88 ? 169 GLU A N 1 ATOM 1309 C CA . GLU A 1 169 ? 11.539 21.901 14.368 1.00 7.44 ? 169 GLU A CA 1 ATOM 1310 C C . GLU A 1 169 ? 12.936 21.324 14.346 1.00 7.46 ? 169 GLU A C 1 ATOM 1311 O O . GLU A 1 169 ? 13.129 20.092 14.299 1.00 6.10 ? 169 GLU A O 1 ATOM 1312 C CB . GLU A 1 169 ? 10.455 20.800 14.211 1.00 7.38 ? 169 GLU A CB 1 ATOM 1313 C CG . GLU A 1 169 ? 9.011 21.248 14.409 1.00 8.28 ? 169 GLU A CG 1 ATOM 1314 C CD . GLU A 1 169 ? 7.984 20.150 14.627 1.00 8.93 ? 169 GLU A CD 1 ATOM 1315 O OE1 . GLU A 1 169 ? 8.267 18.936 14.405 1.00 8.75 ? 169 GLU A OE1 1 ATOM 1316 O OE2 . GLU A 1 169 ? 6.832 20.439 15.065 1.00 7.44 ? 169 GLU A OE2 1 ATOM 1317 N N . PRO A 1 170 ? 13.992 22.145 14.361 1.00 6.88 ? 170 PRO A N 1 ATOM 1318 C CA . PRO A 1 170 ? 15.347 21.575 14.388 1.00 6.03 ? 170 PRO A CA 1 ATOM 1319 C C . PRO A 1 170 ? 15.575 20.561 15.510 1.00 7.69 ? 170 PRO A C 1 ATOM 1320 O O . PRO A 1 170 ? 15.238 20.852 16.665 1.00 6.05 ? 170 PRO A O 1 ATOM 1321 C CB . PRO A 1 170 ? 16.277 22.794 14.530 1.00 6.73 ? 170 PRO A CB 1 ATOM 1322 C CG . PRO A 1 170 ? 15.384 23.859 15.077 1.00 7.78 ? 170 PRO A CG 1 ATOM 1323 C CD . PRO A 1 170 ? 14.008 23.603 14.517 1.00 6.26 ? 170 PRO A CD 1 ATOM 1324 N N . ARG A 1 171 ? 16.132 19.389 15.202 1.00 5.46 ? 171 ARG A N 1 ATOM 1325 C CA . ARG A 1 171 ? 16.514 18.352 16.154 1.00 6.74 ? 171 ARG A CA 1 ATOM 1326 C C . ARG A 1 171 ? 17.920 17.811 15.881 1.00 7.24 ? 171 ARG A C 1 ATOM 1327 O O . ARG A 1 171 ? 18.365 17.874 14.735 1.00 7.50 ? 171 ARG A O 1 ATOM 1328 C CB . ARG A 1 171 ? 15.574 17.138 16.192 1.00 6.70 ? 171 ARG A CB 1 ATOM 1329 C CG . ARG A 1 171 ? 14.135 17.350 16.658 1.00 5.97 ? 171 ARG A CG 1 ATOM 1330 C CD . ARG A 1 171 ? 13.346 16.028 16.692 1.00 5.57 ? 171 ARG A CD 1 ATOM 1331 N NE . ARG A 1 171 ? 11.969 16.108 17.183 1.00 5.58 ? 171 ARG A NE 1 ATOM 1332 C CZ . ARG A 1 171 ? 11.205 15.057 17.481 1.00 7.48 ? 171 ARG A CZ 1 ATOM 1333 N NH1 . ARG A 1 171 ? 11.637 13.796 17.351 1.00 7.59 ? 171 ARG A NH1 1 ATOM 1334 N NH2 . ARG A 1 171 ? 9.950 15.221 17.906 1.00 8.40 ? 171 ARG A NH2 1 ATOM 1335 N N . CYS A 1 172 ? 18.582 17.203 16.847 1.00 8.17 ? 172 CYS A N 1 ATOM 1336 C CA . CYS A 1 172 ? 19.870 16.498 16.668 1.00 8.35 ? 172 CYS A CA 1 ATOM 1337 C C . CYS A 1 172 ? 19.735 15.210 17.497 1.00 9.23 ? 172 CYS A C 1 ATOM 1338 O O . CYS A 1 172 ? 20.065 15.182 18.680 1.00 7.76 ? 172 CYS A O 1 ATOM 1339 C CB . CYS A 1 172 ? 21.096 17.326 16.989 1.00 8.20 ? 172 CYS A CB 1 ATOM 1340 S SG . CYS A 1 172 ? 22.735 16.803 16.393 1.00 7.46 ? 172 CYS A SG 1 ATOM 1341 N N . ASN A 1 173 ? 19.199 14.151 16.896 1.00 8.59 ? 173 ASN A N 1 ATOM 1342 C CA . ASN A 1 173 ? 18.833 12.929 17.665 1.00 8.50 ? 173 ASN A CA 1 ATOM 1343 C C . ASN A 1 173 ? 19.992 12.246 18.369 1.00 9.64 ? 173 ASN A C 1 ATOM 1344 O O . ASN A 1 173 ? 20.948 11.844 17.700 1.00 9.20 ? 173 ASN A O 1 ATOM 1345 C CB . ASN A 1 173 ? 18.088 11.956 16.730 1.00 10.04 ? 173 ASN A CB 1 ATOM 1346 C CG . ASN A 1 173 ? 17.728 10.647 17.439 1.00 11.95 ? 173 ASN A CG 1 ATOM 1347 O OD1 . ASN A 1 173 ? 18.366 9.606 17.235 1.00 14.95 ? 173 ASN A OD1 1 ATOM 1348 N ND2 . ASN A 1 173 ? 16.717 10.623 18.289 1.00 12.45 ? 173 ASN A ND2 1 ATOM 1349 N N . GLY A 1 174 ? 19.947 12.164 19.715 1.00 7.95 ? 174 GLY A N 1 ATOM 1350 C CA . GLY A 1 174 ? 21.027 11.562 20.489 1.00 8.73 ? 174 GLY A CA 1 ATOM 1351 C C . GLY A 1 174 ? 22.256 12.427 20.694 1.00 10.25 ? 174 GLY A C 1 ATOM 1352 O O . GLY A 1 174 ? 23.266 11.930 21.221 1.00 11.19 ? 174 GLY A O 1 ATOM 1353 N N . CYS A 1 175 ? 22.322 13.650 20.181 1.00 8.64 ? 175 CYS A N 1 ATOM 1354 C CA . CYS A 1 175 ? 23.502 14.476 20.233 1.00 9.30 ? 175 CYS A CA 1 ATOM 1355 C C . CYS A 1 175 ? 23.655 15.221 21.564 1.00 10.11 ? 175 CYS A C 1 ATOM 1356 O O . CYS A 1 175 ? 22.689 15.443 22.304 1.00 8.95 ? 175 CYS A O 1 ATOM 1357 C CB . CYS A 1 175 ? 23.415 15.603 19.152 1.00 7.85 ? 175 CYS A CB 1 ATOM 1358 S SG . CYS A 1 175 ? 23.149 15.050 17.431 1.00 8.38 ? 175 CYS A SG 1 ATOM 1359 N N . SER A 1 176 ? 24.876 15.718 21.818 1.00 10.22 ? 176 SER A N 1 ATOM 1360 C CA . SER A 1 176 ? 25.044 16.668 22.930 1.00 9.04 ? 176 SER A CA 1 ATOM 1361 C C . SER A 1 176 ? 24.146 17.871 22.590 1.00 9.34 ? 176 SER A C 1 ATOM 1362 O O . SER A 1 176 ? 24.141 18.294 21.419 1.00 8.34 ? 176 SER A O 1 ATOM 1363 C CB . SER A 1 176 ? 26.495 17.160 22.967 1.00 10.39 ? 176 SER A CB 1 ATOM 1364 O OG . SER A 1 176 ? 26.658 18.286 23.819 1.00 12.51 ? 176 SER A OG 1 ATOM 1365 N N . THR A 1 177 ? 23.542 18.529 23.562 1.00 9.22 ? 177 THR A N 1 ATOM 1366 C CA . THR A 1 177 ? 22.719 19.726 23.338 1.00 8.44 ? 177 THR A CA 1 ATOM 1367 C C . THR A 1 177 ? 23.543 20.928 22.881 1.00 9.00 ? 177 THR A C 1 ATOM 1368 O O . THR A 1 177 ? 22.995 21.905 22.297 1.00 7.95 ? 177 THR A O 1 ATOM 1369 C CB . THR A 1 177 ? 21.884 20.074 24.589 1.00 9.10 ? 177 THR A CB 1 ATOM 1370 O OG1 . THR A 1 177 ? 22.776 20.394 25.668 1.00 11.68 ? 177 THR A OG1 1 ATOM 1371 C CG2 . THR A 1 177 ? 20.933 18.984 25.037 1.00 8.85 ? 177 THR A CG2 1 ATOM 1372 N N . ASP A 1 178 ? 24.873 20.924 23.075 1.00 9.75 ? 178 ASP A N 1 ATOM 1373 C CA . ASP A 1 178 ? 25.745 21.996 22.614 1.00 11.11 ? 178 ASP A CA 1 ATOM 1374 C C . ASP A 1 178 ? 25.857 22.116 21.103 1.00 8.84 ? 178 ASP A C 1 ATOM 1375 O O . ASP A 1 178 ? 26.259 23.184 20.619 1.00 7.77 ? 178 ASP A O 1 ATOM 1376 C CB . ASP A 1 178 ? 27.157 21.841 23.219 1.00 14.02 ? 178 ASP A CB 1 ATOM 1377 C CG . ASP A 1 178 ? 27.999 23.108 23.131 1.00 16.28 ? 178 ASP A CG 1 ATOM 1378 O OD1 . ASP A 1 178 ? 27.572 24.179 23.580 1.00 16.72 ? 178 ASP A OD1 1 ATOM 1379 O OD2 . ASP A 1 178 ? 29.123 22.989 22.591 1.00 18.77 ? 178 ASP A OD2 1 ATOM 1380 N N . VAL A 1 179 ? 25.530 21.075 20.333 1.00 7.50 ? 179 VAL A N 1 ATOM 1381 C CA . VAL A 1 179 ? 25.636 21.191 18.859 1.00 8.17 ? 179 VAL A CA 1 ATOM 1382 C C . VAL A 1 179 ? 24.666 22.266 18.370 1.00 8.80 ? 179 VAL A C 1 ATOM 1383 O O . VAL A 1 179 ? 25.085 23.205 17.691 1.00 8.54 ? 179 VAL A O 1 ATOM 1384 C CB . VAL A 1 179 ? 25.393 19.847 18.173 1.00 9.57 ? 179 VAL A CB 1 ATOM 1385 C CG1 . VAL A 1 179 ? 25.453 19.996 16.656 1.00 11.12 ? 179 VAL A CG1 1 ATOM 1386 C CG2 . VAL A 1 179 ? 26.456 18.807 18.571 1.00 8.59 ? 179 VAL A CG2 1 ATOM 1387 N N . ILE A 1 180 ? 23.390 22.161 18.701 1.00 8.55 ? 180 ILE A N 1 ATOM 1388 C CA . ILE A 1 180 ? 22.405 23.202 18.334 1.00 7.91 ? 180 ILE A CA 1 ATOM 1389 C C . ILE A 1 180 ? 22.680 24.520 19.028 1.00 8.71 ? 180 ILE A C 1 ATOM 1390 O O . ILE A 1 180 ? 22.509 25.589 18.380 1.00 7.37 ? 180 ILE A O 1 ATOM 1391 C CB . ILE A 1 180 ? 20.958 22.661 18.482 1.00 7.37 ? 180 ILE A CB 1 ATOM 1392 C CG1 . ILE A 1 180 ? 20.709 21.721 17.293 1.00 7.57 ? 180 ILE A CG1 1 ATOM 1393 C CG2 . ILE A 1 180 ? 19.896 23.750 18.504 1.00 6.80 ? 180 ILE A CG2 1 ATOM 1394 C CD1 . ILE A 1 180 ? 19.423 20.938 17.330 1.00 6.63 ? 180 ILE A CD1 1 ATOM 1395 N N . VAL A 1 181 ? 23.165 24.573 20.281 1.00 8.45 ? 181 VAL A N 1 ATOM 1396 C CA . VAL A 1 181 ? 23.473 25.883 20.865 1.00 8.95 ? 181 VAL A CA 1 ATOM 1397 C C . VAL A 1 181 ? 24.521 26.647 20.042 1.00 9.37 ? 181 VAL A C 1 ATOM 1398 O O . VAL A 1 181 ? 24.323 27.820 19.696 1.00 8.66 ? 181 VAL A O 1 ATOM 1399 C CB . VAL A 1 181 ? 23.919 25.798 22.330 1.00 10.21 ? 181 VAL A CB 1 ATOM 1400 C CG1 . VAL A 1 181 ? 24.391 27.171 22.813 1.00 8.80 ? 181 VAL A CG1 1 ATOM 1401 C CG2 . VAL A 1 181 ? 22.824 25.288 23.248 1.00 10.03 ? 181 VAL A CG2 1 ATOM 1402 N N . GLN A 1 182 ? 25.655 26.009 19.704 1.00 9.28 ? 182 GLN A N 1 ATOM 1403 C CA . GLN A 1 182 ? 26.689 26.715 18.920 1.00 9.32 ? 182 GLN A CA 1 ATOM 1404 C C . GLN A 1 182 ? 26.221 27.085 17.511 1.00 8.89 ? 182 GLN A C 1 ATOM 1405 O O . GLN A 1 182 ? 26.553 28.167 17.000 1.00 9.08 ? 182 GLN A O 1 ATOM 1406 C CB . GLN A 1 182 ? 27.991 25.926 18.916 1.00 10.08 ? 182 GLN A CB 1 ATOM 1407 C CG . GLN A 1 182 ? 28.700 25.656 20.234 1.00 11.69 ? 182 GLN A CG 1 ATOM 1408 C CD . GLN A 1 182 ? 28.838 26.826 21.156 1.00 13.20 ? 182 GLN A CD 1 ATOM 1409 O OE1 . GLN A 1 182 ? 29.326 27.903 20.730 1.00 14.68 ? 182 GLN A OE1 1 ATOM 1410 N NE2 . GLN A 1 182 ? 28.444 26.756 22.413 1.00 14.47 ? 182 GLN A NE2 1 ATOM 1411 N N . TRP A 1 183 ? 25.476 26.229 16.812 1.00 8.17 ? 183 TRP A N 1 ATOM 1412 C CA . TRP A 1 183 ? 24.967 26.489 15.461 1.00 8.30 ? 183 TRP A CA 1 ATOM 1413 C C . TRP A 1 183 ? 24.006 27.675 15.472 1.00 9.08 ? 183 TRP A C 1 ATOM 1414 O O . TRP A 1 183 ? 24.156 28.613 14.673 1.00 8.36 ? 183 TRP A O 1 ATOM 1415 C CB . TRP A 1 183 ? 24.299 25.245 14.861 1.00 8.41 ? 183 TRP A CB 1 ATOM 1416 C CG . TRP A 1 183 ? 23.525 25.448 13.576 1.00 7.87 ? 183 TRP A CG 1 ATOM 1417 C CD1 . TRP A 1 183 ? 24.046 25.508 12.308 1.00 8.49 ? 183 TRP A CD1 1 ATOM 1418 C CD2 . TRP A 1 183 ? 22.106 25.666 13.440 1.00 7.31 ? 183 TRP A CD2 1 ATOM 1419 N NE1 . TRP A 1 183 ? 23.049 25.750 11.391 1.00 7.06 ? 183 TRP A NE1 1 ATOM 1420 C CE2 . TRP A 1 183 ? 21.836 25.829 12.071 1.00 7.47 ? 183 TRP A CE2 1 ATOM 1421 C CE3 . TRP A 1 183 ? 21.050 25.681 14.351 1.00 7.26 ? 183 TRP A CE3 1 ATOM 1422 C CZ2 . TRP A 1 183 ? 20.543 26.026 11.575 1.00 7.74 ? 183 TRP A CZ2 1 ATOM 1423 C CZ3 . TRP A 1 183 ? 19.755 25.886 13.865 1.00 7.41 ? 183 TRP A CZ3 1 ATOM 1424 C CH2 . TRP A 1 183 ? 19.505 26.058 12.491 1.00 6.91 ? 183 TRP A CH2 1 ATOM 1425 N N . ALA A 1 184 ? 23.043 27.634 16.400 1.00 8.37 ? 184 ALA A N 1 ATOM 1426 C CA . ALA A 1 184 ? 22.057 28.730 16.492 1.00 8.10 ? 184 ALA A CA 1 ATOM 1427 C C . ALA A 1 184 ? 22.655 30.083 16.895 1.00 9.04 ? 184 ALA A C 1 ATOM 1428 O O . ALA A 1 184 ? 22.211 31.112 16.384 1.00 8.18 ? 184 ALA A O 1 ATOM 1429 C CB . ALA A 1 184 ? 20.935 28.347 17.451 1.00 8.48 ? 184 ALA A CB 1 ATOM 1430 N N . THR A 1 185 ? 23.671 30.083 17.764 1.00 8.04 ? 185 THR A N 1 ATOM 1431 C CA . THR A 1 185 ? 24.339 31.336 18.158 1.00 9.76 ? 185 THR A CA 1 ATOM 1432 C C . THR A 1 185 ? 24.973 32.003 16.953 1.00 9.83 ? 185 THR A C 1 ATOM 1433 O O . THR A 1 185 ? 24.759 33.198 16.662 1.00 9.90 ? 185 THR A O 1 ATOM 1434 C CB . THR A 1 185 ? 25.392 31.006 19.239 1.00 10.42 ? 185 THR A CB 1 ATOM 1435 O OG1 . THR A 1 185 ? 24.755 30.482 20.410 1.00 10.78 ? 185 THR A OG1 1 ATOM 1436 C CG2 . THR A 1 185 ? 26.219 32.242 19.601 1.00 10.50 ? 185 THR A CG2 1 ATOM 1437 N N . SER A 1 186 ? 25.732 31.266 16.160 1.00 10.74 ? 186 SER A N 1 ATOM 1438 C CA . SER A 1 186 ? 26.418 31.751 14.978 1.00 12.12 ? 186 SER A CA 1 ATOM 1439 C C . SER A 1 186 ? 25.479 32.195 13.843 1.00 11.30 ? 186 SER A C 1 ATOM 1440 O O . SER A 1 186 ? 25.644 33.282 13.273 1.00 10.24 ? 186 SER A O 1 ATOM 1441 C CB . SER A 1 186 ? 27.396 30.689 14.431 1.00 14.41 ? 186 SER A CB 1 ATOM 1442 O OG . SER A 1 186 ? 28.184 31.288 13.393 1.00 17.55 ? 186 SER A OG 1 ATOM 1443 N N . VAL A 1 187 ? 24.454 31.412 13.565 1.00 8.93 ? 187 VAL A N 1 ATOM 1444 C CA . VAL A 1 187 ? 23.487 31.736 12.504 1.00 8.69 ? 187 VAL A CA 1 ATOM 1445 C C . VAL A 1 187 ? 22.629 32.934 12.875 1.00 8.10 ? 187 VAL A C 1 ATOM 1446 O O . VAL A 1 187 ? 22.399 33.830 12.018 1.00 8.42 ? 187 VAL A O 1 ATOM 1447 C CB . VAL A 1 187 ? 22.617 30.519 12.107 1.00 8.63 ? 187 VAL A CB 1 ATOM 1448 C CG1 . VAL A 1 187 ? 21.524 30.923 11.112 1.00 9.06 ? 187 VAL A CG1 1 ATOM 1449 C CG2 . VAL A 1 187 ? 23.404 29.393 11.451 1.00 8.99 ? 187 VAL A CG2 1 ATOM 1450 N N . SER A 1 188 ? 22.180 33.077 14.115 1.00 7.02 ? 188 SER A N 1 ATOM 1451 C CA . SER A 1 188 ? 21.352 34.246 14.496 1.00 8.65 ? 188 SER A CA 1 ATOM 1452 C C . SER A 1 188 ? 22.182 35.529 14.501 1.00 9.84 ? 188 SER A C 1 ATOM 1453 O O . SER A 1 188 ? 21.668 36.567 14.084 1.00 9.17 ? 188 SER A O 1 ATOM 1454 C CB . SER A 1 188 ? 20.606 34.033 15.813 1.00 8.39 ? 188 SER A CB 1 ATOM 1455 O OG . SER A 1 188 ? 21.498 33.765 16.924 1.00 7.75 ? 188 SER A OG 1 ATOM 1456 N N . GLN A 1 189 ? 23.481 35.455 14.834 1.00 9.94 ? 189 GLN A N 1 ATOM 1457 C CA . GLN A 1 189 ? 24.382 36.601 14.672 1.00 11.22 ? 189 GLN A CA 1 ATOM 1458 C C . GLN A 1 189 ? 24.455 37.032 13.206 1.00 10.91 ? 189 GLN A C 1 ATOM 1459 O O . GLN A 1 189 ? 24.441 38.246 12.863 1.00 11.43 ? 189 GLN A O 1 ATOM 1460 C CB . GLN A 1 189 ? 25.777 36.236 15.208 1.00 14.48 ? 189 GLN A CB 1 ATOM 1461 C CG . GLN A 1 189 ? 26.096 36.326 16.657 1.00 18.60 ? 189 GLN A CG 1 ATOM 1462 C CD . GLN A 1 189 ? 27.458 35.809 17.105 1.00 21.25 ? 189 GLN A CD 1 ATOM 1463 O OE1 . GLN A 1 189 ? 28.376 35.595 16.301 1.00 22.02 ? 189 GLN A OE1 1 ATOM 1464 N NE2 . GLN A 1 189 ? 27.648 35.594 18.413 1.00 21.74 ? 189 GLN A NE2 1 ATOM 1465 N N . TYR A 1 190 ? 24.536 36.081 12.287 1.00 10.05 ? 190 TYR A N 1 ATOM 1466 C CA . TYR A 1 190 ? 24.572 36.341 10.849 1.00 10.72 ? 190 TYR A CA 1 ATOM 1467 C C . TYR A 1 190 ? 23.278 37.013 10.365 1.00 11.13 ? 190 TYR A C 1 ATOM 1468 O O . TYR A 1 190 ? 23.367 38.002 9.601 1.00 9.82 ? 190 TYR A O 1 ATOM 1469 C CB . TYR A 1 190 ? 24.916 35.132 9.991 1.00 10.67 ? 190 TYR A CB 1 ATOM 1470 C CG . TYR A 1 190 ? 24.974 35.315 8.487 1.00 11.64 ? 190 TYR A CG 1 ATOM 1471 C CD1 . TYR A 1 190 ? 25.895 36.235 7.950 1.00 12.51 ? 190 TYR A CD1 1 ATOM 1472 C CD2 . TYR A 1 190 ? 24.144 34.654 7.597 1.00 12.71 ? 190 TYR A CD2 1 ATOM 1473 C CE1 . TYR A 1 190 ? 25.990 36.428 6.579 1.00 13.16 ? 190 TYR A CE1 1 ATOM 1474 C CE2 . TYR A 1 190 ? 24.217 34.859 6.227 1.00 12.67 ? 190 TYR A CE2 1 ATOM 1475 C CZ . TYR A 1 190 ? 25.166 35.733 5.724 1.00 14.44 ? 190 TYR A CZ 1 ATOM 1476 O OH . TYR A 1 190 ? 25.293 35.966 4.355 1.00 16.17 ? 190 TYR A OH 1 ATOM 1477 N N . VAL A 1 191 ? 22.111 36.529 10.760 1.00 8.95 ? 191 VAL A N 1 ATOM 1478 C CA . VAL A 1 191 ? 20.851 37.191 10.352 1.00 10.13 ? 191 VAL A CA 1 ATOM 1479 C C . VAL A 1 191 ? 20.793 38.647 10.823 1.00 10.84 ? 191 VAL A C 1 ATOM 1480 O O . VAL A 1 191 ? 20.488 39.548 10.028 1.00 10.35 ? 191 VAL A O 1 ATOM 1481 C CB . VAL A 1 191 ? 19.603 36.444 10.843 1.00 10.25 ? 191 VAL A CB 1 ATOM 1482 C CG1 . VAL A 1 191 ? 18.273 37.124 10.454 1.00 10.88 ? 191 VAL A CG1 1 ATOM 1483 C CG2 . VAL A 1 191 ? 19.601 35.025 10.302 1.00 9.91 ? 191 VAL A CG2 1 ATOM 1484 N N . LYS A 1 192 ? 21.165 38.954 12.062 1.00 11.13 ? 192 LYS A N 1 ATOM 1485 C CA . LYS A 1 192 ? 21.196 40.319 12.596 1.00 11.27 ? 192 LYS A CA 1 ATOM 1486 C C . LYS A 1 192 ? 22.191 41.194 11.834 1.00 12.07 ? 192 LYS A C 1 ATOM 1487 O O . LYS A 1 192 ? 21.939 42.386 11.715 1.00 12.89 ? 192 LYS A O 1 ATOM 1488 C CB . LYS A 1 192 ? 21.441 40.292 14.121 1.00 11.47 ? 192 LYS A CB 1 ATOM 1489 C CG . LYS A 1 192 ? 20.238 39.756 14.903 1.00 13.99 ? 192 LYS A CG 1 ATOM 1490 C CD . LYS A 1 192 ? 20.096 40.145 16.348 1.00 15.82 ? 192 LYS A CD 1 ATOM 1491 C CE . LYS A 1 192 ? 18.744 39.713 16.943 1.00 17.85 ? 192 LYS A CE 1 ATOM 1492 N NZ . LYS A 1 192 ? 18.504 40.480 18.207 1.00 19.71 ? 192 LYS A NZ 1 ATOM 1493 N N . SER A 1 193 ? 23.258 40.662 11.240 1.00 10.22 ? 193 SER A N 1 ATOM 1494 C CA . SER A 1 193 ? 24.209 41.436 10.437 1.00 11.16 ? 193 SER A CA 1 ATOM 1495 C C . SER A 1 193 ? 23.618 41.870 9.090 1.00 11.93 ? 193 SER A C 1 ATOM 1496 O O . SER A 1 193 ? 24.210 42.741 8.418 1.00 11.65 ? 193 SER A O 1 ATOM 1497 C CB . SER A 1 193 ? 25.501 40.646 10.229 1.00 11.89 ? 193 SER A CB 1 ATOM 1498 O OG . SER A 1 193 ? 25.516 39.679 9.188 1.00 10.80 ? 193 SER A OG 1 ATOM 1499 N N . LEU A 1 194 ? 22.549 41.210 8.660 1.00 10.41 ? 194 LEU A N 1 ATOM 1500 C CA . LEU A 1 194 ? 21.868 41.484 7.399 1.00 10.50 ? 194 LEU A CA 1 ATOM 1501 C C . LEU A 1 194 ? 20.629 42.370 7.544 1.00 10.94 ? 194 LEU A C 1 ATOM 1502 O O . LEU A 1 194 ? 20.163 42.934 6.540 1.00 10.17 ? 194 LEU A O 1 ATOM 1503 C CB . LEU A 1 194 ? 21.427 40.171 6.696 1.00 10.52 ? 194 LEU A CB 1 ATOM 1504 C CG . LEU A 1 194 ? 22.512 39.176 6.283 1.00 12.32 ? 194 LEU A CG 1 ATOM 1505 C CD1 . LEU A 1 194 ? 21.938 37.900 5.658 1.00 12.86 ? 194 LEU A CD1 1 ATOM 1506 C CD2 . LEU A 1 194 ? 23.531 39.799 5.350 1.00 13.31 ? 194 LEU A CD2 1 ATOM 1507 N N . ASP A 1 195 ? 20.071 42.506 8.732 1.00 9.68 ? 195 ASP A N 1 ATOM 1508 C CA . ASP A 1 195 ? 18.787 43.180 8.980 1.00 9.37 ? 195 ASP A CA 1 ATOM 1509 C C . ASP A 1 195 ? 18.670 43.567 10.450 1.00 11.10 ? 195 ASP A C 1 ATOM 1510 O O . ASP A 1 195 ? 18.569 42.718 11.353 1.00 9.68 ? 195 ASP A O 1 ATOM 1511 C CB . ASP A 1 195 ? 17.605 42.274 8.557 1.00 9.09 ? 195 ASP A CB 1 ATOM 1512 C CG . ASP A 1 195 ? 16.193 42.684 8.806 1.00 8.85 ? 195 ASP A CG 1 ATOM 1513 O OD1 . ASP A 1 195 ? 15.940 43.658 9.531 1.00 8.95 ? 195 ASP A OD1 1 ATOM 1514 O OD2 . ASP A 1 195 ? 15.204 42.023 8.294 1.00 8.77 ? 195 ASP A OD2 1 ATOM 1515 N N . SER A 1 196 ? 18.733 44.888 10.703 1.00 10.85 ? 196 SER A N 1 ATOM 1516 C CA . SER A 1 196 ? 18.587 45.402 12.062 1.00 12.72 ? 196 SER A CA 1 ATOM 1517 C C . SER A 1 196 ? 17.188 45.891 12.368 1.00 12.88 ? 196 SER A C 1 ATOM 1518 O O . SER A 1 196 ? 16.983 46.418 13.469 1.00 14.24 ? 196 SER A O 1 ATOM 1519 C CB . SER A 1 196 ? 19.625 46.499 12.324 1.00 13.72 ? 196 SER A CB 1 ATOM 1520 O OG . SER A 1 196 ? 19.449 47.657 11.508 1.00 16.39 ? 196 SER A OG 1 ATOM 1521 N N . ASN A 1 197 ? 16.211 45.725 11.448 1.00 10.48 ? 197 ASN A N 1 ATOM 1522 C CA . ASN A 1 197 ? 14.864 46.145 11.695 1.00 9.59 ? 197 ASN A CA 1 ATOM 1523 C C . ASN A 1 197 ? 13.976 45.072 12.325 1.00 9.34 ? 197 ASN A C 1 ATOM 1524 O O . ASN A 1 197 ? 13.026 45.456 13.045 1.00 8.19 ? 197 ASN A O 1 ATOM 1525 C CB . ASN A 1 197 ? 14.159 46.500 10.337 1.00 9.76 ? 197 ASN A CB 1 ATOM 1526 C CG . ASN A 1 197 ? 14.884 47.607 9.582 1.00 11.43 ? 197 ASN A CG 1 ATOM 1527 O OD1 . ASN A 1 197 ? 15.248 48.616 10.196 1.00 10.93 ? 197 ASN A OD1 1 ATOM 1528 N ND2 . ASN A 1 197 ? 15.112 47.471 8.282 1.00 10.68 ? 197 ASN A ND2 1 ATOM 1529 N N . HIS A 1 198 ? 14.283 43.793 12.115 1.00 8.40 ? 198 HIS A N 1 ATOM 1530 C CA . HIS A 1 198 ? 13.427 42.685 12.574 1.00 8.82 ? 198 HIS A CA 1 ATOM 1531 C C . HIS A 1 198 ? 13.874 41.710 13.659 1.00 8.36 ? 198 HIS A C 1 ATOM 1532 O O . HIS A 1 198 ? 15.047 41.513 13.974 1.00 8.30 ? 198 HIS A O 1 ATOM 1533 C CB . HIS A 1 198 ? 13.047 41.874 11.305 1.00 8.87 ? 198 HIS A CB 1 ATOM 1534 C CG . HIS A 1 198 ? 12.296 42.616 10.234 1.00 9.29 ? 198 HIS A CG 1 ATOM 1535 N ND1 . HIS A 1 198 ? 12.785 42.800 8.951 1.00 7.82 ? 198 HIS A ND1 1 ATOM 1536 C CD2 . HIS A 1 198 ? 11.106 43.218 10.254 1.00 9.85 ? 198 HIS A CD2 1 ATOM 1537 C CE1 . HIS A 1 198 ? 11.899 43.468 8.234 1.00 8.07 ? 198 HIS A CE1 1 ATOM 1538 N NE2 . HIS A 1 198 ? 10.867 43.760 8.989 1.00 8.87 ? 198 HIS A NE2 1 ATOM 1539 N N . LEU A 1 199 ? 12.942 41.055 14.318 1.00 7.94 ? 199 LEU A N 1 ATOM 1540 C CA . LEU A 1 199 ? 13.145 40.053 15.367 1.00 7.68 ? 199 LEU A CA 1 ATOM 1541 C C . LEU A 1 199 ? 13.598 38.718 14.773 1.00 8.16 ? 199 LEU A C 1 ATOM 1542 O O . LEU A 1 199 ? 13.364 38.434 13.587 1.00 7.31 ? 199 LEU A O 1 ATOM 1543 C CB . LEU A 1 199 ? 11.846 39.858 16.179 1.00 8.42 ? 199 LEU A CB 1 ATOM 1544 C CG . LEU A 1 199 ? 11.240 41.047 16.918 1.00 9.20 ? 199 LEU A CG 1 ATOM 1545 C CD1 . LEU A 1 199 ? 9.908 40.682 17.586 1.00 9.92 ? 199 LEU A CD1 1 ATOM 1546 C CD2 . LEU A 1 199 ? 12.205 41.682 17.920 1.00 8.56 ? 199 LEU A CD2 1 ATOM 1547 N N . VAL A 1 200 ? 14.230 37.841 15.554 1.00 6.85 ? 200 VAL A N 1 ATOM 1548 C CA . VAL A 1 200 ? 14.782 36.528 15.166 1.00 8.50 ? 200 VAL A CA 1 ATOM 1549 C C . VAL A 1 200 ? 14.461 35.461 16.226 1.00 8.06 ? 200 VAL A C 1 ATOM 1550 O O . VAL A 1 200 ? 14.548 35.760 17.420 1.00 8.36 ? 200 VAL A O 1 ATOM 1551 C CB . VAL A 1 200 ? 16.305 36.563 14.934 1.00 8.93 ? 200 VAL A CB 1 ATOM 1552 C CG1 . VAL A 1 200 ? 16.841 35.214 14.441 1.00 7.63 ? 200 VAL A CG1 1 ATOM 1553 C CG2 . VAL A 1 200 ? 16.753 37.632 13.946 1.00 8.87 ? 200 VAL A CG2 1 ATOM 1554 N N . THR A 1 201 ? 14.062 34.246 15.852 1.00 6.84 ? 201 THR A N 1 ATOM 1555 C CA . THR A 1 201 ? 13.693 33.143 16.740 1.00 6.09 ? 201 THR A CA 1 ATOM 1556 C C . THR A 1 201 ? 14.170 31.790 16.202 1.00 6.44 ? 201 THR A C 1 ATOM 1557 O O . THR A 1 201 ? 14.522 31.675 15.009 1.00 4.67 ? 201 THR A O 1 ATOM 1558 C CB . THR A 1 201 ? 12.143 33.156 17.005 1.00 5.49 ? 201 THR A CB 1 ATOM 1559 O OG1 . THR A 1 201 ? 11.848 32.292 18.124 1.00 5.42 ? 201 THR A OG1 1 ATOM 1560 C CG2 . THR A 1 201 ? 11.345 32.717 15.795 1.00 6.16 ? 201 THR A CG2 1 ATOM 1561 N N . LEU A 1 202 ? 14.207 30.692 16.992 1.00 5.74 ? 202 LEU A N 1 ATOM 1562 C CA . LEU A 1 202 ? 14.724 29.393 16.556 1.00 4.87 ? 202 LEU A CA 1 ATOM 1563 C C . LEU A 1 202 ? 13.770 28.500 15.735 1.00 5.68 ? 202 LEU A C 1 ATOM 1564 O O . LEU A 1 202 ? 14.166 27.962 14.703 1.00 4.64 ? 202 LEU A O 1 ATOM 1565 C CB . LEU A 1 202 ? 15.218 28.623 17.805 1.00 5.95 ? 202 LEU A CB 1 ATOM 1566 C CG . LEU A 1 202 ? 15.866 27.250 17.651 1.00 6.26 ? 202 LEU A CG 1 ATOM 1567 C CD1 . LEU A 1 202 ? 17.020 27.261 16.652 1.00 6.68 ? 202 LEU A CD1 1 ATOM 1568 C CD2 . LEU A 1 202 ? 16.365 26.721 19.011 1.00 7.58 ? 202 LEU A CD2 1 ATOM 1569 N N . GLY A 1 203 ? 12.505 28.343 16.215 1.00 6.20 ? 203 GLY A N 1 ATOM 1570 C CA . GLY A 1 203 ? 11.570 27.441 15.522 1.00 5.30 ? 203 GLY A CA 1 ATOM 1571 C C . GLY A 1 203 ? 11.482 26.014 16.071 1.00 6.51 ? 203 GLY A C 1 ATOM 1572 O O . GLY A 1 203 ? 10.824 25.128 15.470 1.00 6.12 ? 203 GLY A O 1 ATOM 1573 N N . ASP A 1 204 ? 12.123 25.756 17.214 1.00 6.24 ? 204 ASP A N 1 ATOM 1574 C CA . ASP A 1 204 ? 12.084 24.450 17.865 1.00 6.41 ? 204 ASP A CA 1 ATOM 1575 C C . ASP A 1 204 ? 10.733 24.099 18.473 1.00 6.82 ? 204 ASP A C 1 ATOM 1576 O O . ASP A 1 204 ? 9.943 24.975 18.737 1.00 5.47 ? 204 ASP A O 1 ATOM 1577 C CB . ASP A 1 204 ? 13.156 24.338 18.982 1.00 6.71 ? 204 ASP A CB 1 ATOM 1578 C CG . ASP A 1 204 ? 12.996 25.419 20.043 1.00 9.23 ? 204 ASP A CG 1 ATOM 1579 O OD1 . ASP A 1 204 ? 12.960 26.626 19.715 1.00 8.49 ? 204 ASP A OD1 1 ATOM 1580 O OD2 . ASP A 1 204 ? 12.932 25.036 21.241 1.00 9.69 ? 204 ASP A OD2 1 ATOM 1581 N N . GLU A 1 205 ? 10.516 22.830 18.792 1.00 6.48 ? 205 GLU A N 1 ATOM 1582 C CA . GLU A 1 205 ? 9.328 22.295 19.433 1.00 6.94 ? 205 GLU A CA 1 ATOM 1583 C C . GLU A 1 205 ? 9.266 22.603 20.944 1.00 6.72 ? 205 GLU A C 1 ATOM 1584 O O . GLU A 1 205 ? 8.204 22.461 21.567 1.00 6.08 ? 205 GLU A O 1 ATOM 1585 C CB . GLU A 1 205 ? 9.269 20.765 19.297 1.00 7.70 ? 205 GLU A CB 1 ATOM 1586 C CG . GLU A 1 205 ? 9.107 20.240 17.846 1.00 7.97 ? 205 GLU A CG 1 ATOM 1587 C CD . GLU A 1 205 ? 9.595 18.804 17.732 1.00 8.74 ? 205 GLU A CD 1 ATOM 1588 O OE1 . GLU A 1 205 ? 10.819 18.609 17.527 1.00 7.31 ? 205 GLU A OE1 1 ATOM 1589 O OE2 . GLU A 1 205 ? 8.808 17.822 17.858 1.00 8.70 ? 205 GLU A OE2 1 ATOM 1590 N N . GLY A 1 206 ? 10.401 22.952 21.547 1.00 5.95 ? 206 GLY A N 1 ATOM 1591 C CA . GLY A 1 206 ? 10.495 23.210 22.977 1.00 5.18 ? 206 GLY A CA 1 ATOM 1592 C C . GLY A 1 206 ? 10.964 22.028 23.822 1.00 7.34 ? 206 GLY A C 1 ATOM 1593 O O . GLY A 1 206 ? 10.862 22.048 25.077 1.00 7.38 ? 206 GLY A O 1 ATOM 1594 N N . LEU A 1 207 ? 11.503 20.974 23.213 1.00 6.05 ? 207 LEU A N 1 ATOM 1595 C CA . LEU A 1 207 ? 11.902 19.774 23.955 1.00 7.33 ? 207 LEU A CA 1 ATOM 1596 C C . LEU A 1 207 ? 13.058 20.014 24.914 1.00 8.20 ? 207 LEU A C 1 ATOM 1597 O O . LEU A 1 207 ? 13.948 20.806 24.590 1.00 7.25 ? 207 LEU A O 1 ATOM 1598 C CB . LEU A 1 207 ? 12.240 18.614 22.987 1.00 7.98 ? 207 LEU A CB 1 ATOM 1599 C CG . LEU A 1 207 ? 11.232 18.334 21.855 1.00 7.84 ? 207 LEU A CG 1 ATOM 1600 C CD1 . LEU A 1 207 ? 11.700 17.182 20.956 1.00 7.77 ? 207 LEU A CD1 1 ATOM 1601 C CD2 . LEU A 1 207 ? 9.844 18.013 22.379 1.00 8.88 ? 207 LEU A CD2 1 ATOM 1602 N N . GLY A 1 208 ? 13.073 19.343 26.073 1.00 7.30 ? 208 GLY A N 1 ATOM 1603 C CA . GLY A 1 208 ? 14.172 19.439 27.029 1.00 7.34 ? 208 GLY A CA 1 ATOM 1604 C C . GLY A 1 208 ? 13.975 20.535 28.078 1.00 8.35 ? 208 GLY A C 1 ATOM 1605 O O . GLY A 1 208 ? 14.552 21.615 27.891 1.00 7.54 ? 208 GLY A O 1 ATOM 1606 N N . LEU A 1 209 ? 13.282 20.248 29.179 1.00 7.52 ? 209 LEU A N 1 ATOM 1607 C CA . LEU A 1 209 ? 12.974 21.203 30.245 1.00 7.53 ? 209 LEU A CA 1 ATOM 1608 C C . LEU A 1 209 ? 12.698 20.459 31.560 1.00 9.37 ? 209 LEU A C 1 ATOM 1609 O O . LEU A 1 209 ? 11.822 19.591 31.689 1.00 8.91 ? 209 LEU A O 1 ATOM 1610 C CB . LEU A 1 209 ? 11.785 22.091 29.823 1.00 7.15 ? 209 LEU A CB 1 ATOM 1611 C CG . LEU A 1 209 ? 11.290 23.206 30.739 1.00 7.41 ? 209 LEU A CG 1 ATOM 1612 C CD1 . LEU A 1 209 ? 12.356 24.261 31.010 1.00 7.90 ? 209 LEU A CD1 1 ATOM 1613 C CD2 . LEU A 1 209 ? 10.062 23.910 30.113 1.00 8.15 ? 209 LEU A CD2 1 ATOM 1614 N N . SER A 1 210 ? 13.477 20.793 32.601 1.00 9.34 ? 210 SER A N 1 ATOM 1615 C CA . SER A 1 210 ? 13.475 20.030 33.858 1.00 10.99 ? 210 SER A CA 1 ATOM 1616 C C . SER A 1 210 ? 12.405 20.351 34.886 1.00 12.08 ? 210 SER A C 1 ATOM 1617 O O . SER A 1 210 ? 12.297 19.657 35.917 1.00 13.14 ? 210 SER A O 1 ATOM 1618 C CB . SER A 1 210 ? 14.870 20.180 34.503 1.00 12.28 ? 210 SER A CB 1 ATOM 1619 O OG . SER A 1 210 ? 15.903 19.538 33.755 1.00 10.82 ? 210 SER A OG 1 ATOM 1620 N N . THR A 1 211 ? 11.560 21.332 34.662 1.00 11.70 ? 211 THR A N 1 ATOM 1621 C CA . THR A 1 211 ? 10.465 21.750 35.539 1.00 11.38 ? 211 THR A CA 1 ATOM 1622 C C . THR A 1 211 ? 9.138 21.039 35.297 1.00 12.01 ? 211 THR A C 1 ATOM 1623 O O . THR A 1 211 ? 8.148 21.408 35.951 1.00 11.24 ? 211 THR A O 1 ATOM 1624 C CB . THR A 1 211 ? 10.280 23.274 35.395 1.00 12.38 ? 211 THR A CB 1 ATOM 1625 O OG1 . THR A 1 211 ? 10.069 23.572 34.001 1.00 10.77 ? 211 THR A OG1 1 ATOM 1626 C CG2 . THR A 1 211 ? 11.462 24.062 35.927 1.00 13.49 ? 211 THR A CG2 1 ATOM 1627 N N . GLY A 1 212 ? 9.039 20.073 34.401 1.00 12.06 ? 212 GLY A N 1 ATOM 1628 C CA . GLY A 1 212 ? 7.877 19.306 34.054 1.00 13.50 ? 212 GLY A CA 1 ATOM 1629 C C . GLY A 1 212 ? 7.561 18.033 34.816 1.00 12.47 ? 212 GLY A C 1 ATOM 1630 O O . GLY A 1 212 ? 8.051 17.869 35.943 1.00 12.92 ? 212 GLY A O 1 ATOM 1631 N N . ASP A 1 213 ? 6.796 17.106 34.232 1.00 10.95 ? 213 ASP A N 1 ATOM 1632 C CA . ASP A 1 213 ? 6.434 15.849 34.883 1.00 12.83 ? 213 ASP A CA 1 ATOM 1633 C C . ASP A 1 213 ? 7.299 14.663 34.439 1.00 13.40 ? 213 ASP A C 1 ATOM 1634 O O . ASP A 1 213 ? 7.046 13.515 34.856 1.00 13.33 ? 213 ASP A O 1 ATOM 1635 C CB . ASP A 1 213 ? 4.963 15.529 34.659 1.00 13.15 ? 213 ASP A CB 1 ATOM 1636 C CG . ASP A 1 213 ? 4.589 15.104 33.252 1.00 14.10 ? 213 ASP A CG 1 ATOM 1637 O OD1 . ASP A 1 213 ? 5.378 15.232 32.294 1.00 11.05 ? 213 ASP A OD1 1 ATOM 1638 O OD2 . ASP A 1 213 ? 3.449 14.606 33.101 1.00 16.61 ? 213 ASP A OD2 1 ATOM 1639 N N . GLY A 1 214 ? 8.307 14.894 33.601 1.00 12.54 ? 214 GLY A N 1 ATOM 1640 C CA . GLY A 1 214 ? 9.203 13.820 33.175 1.00 11.90 ? 214 GLY A CA 1 ATOM 1641 C C . GLY A 1 214 ? 8.797 12.984 31.975 1.00 11.63 ? 214 GLY A C 1 ATOM 1642 O O . GLY A 1 214 ? 9.542 12.050 31.597 1.00 11.75 ? 214 GLY A O 1 ATOM 1643 N N . ALA A 1 215 ? 7.678 13.281 31.328 1.00 9.50 ? 215 ALA A N 1 ATOM 1644 C CA . ALA A 1 215 ? 7.307 12.619 30.066 1.00 10.51 ? 215 ALA A CA 1 ATOM 1645 C C . ALA A 1 215 ? 8.423 12.810 29.030 1.00 10.15 ? 215 ALA A C 1 ATOM 1646 O O . ALA A 1 215 ? 9.145 13.795 29.125 1.00 9.48 ? 215 ALA A O 1 ATOM 1647 C CB . ALA A 1 215 ? 5.984 13.173 29.554 1.00 11.15 ? 215 ALA A CB 1 ATOM 1648 N N . TYR A 1 216 ? 8.529 11.983 27.973 1.00 10.12 ? 216 TYR A N 1 ATOM 1649 C CA . TYR A 1 216 ? 9.591 12.106 26.967 1.00 11.14 ? 216 TYR A CA 1 ATOM 1650 C C . TYR A 1 216 ? 9.833 13.482 26.394 1.00 9.28 ? 216 TYR A C 1 ATOM 1651 O O . TYR A 1 216 ? 11.021 13.847 26.276 1.00 7.82 ? 216 TYR A O 1 ATOM 1652 C CB . TYR A 1 216 ? 9.490 11.062 25.831 1.00 13.25 ? 216 TYR A CB 1 ATOM 1653 C CG . TYR A 1 216 ? 10.702 11.057 24.893 1.00 14.71 ? 216 TYR A CG 1 ATOM 1654 C CD1 . TYR A 1 216 ? 11.914 10.521 25.282 1.00 14.43 ? 216 TYR A CD1 1 ATOM 1655 C CD2 . TYR A 1 216 ? 10.645 11.617 23.631 1.00 16.82 ? 216 TYR A CD2 1 ATOM 1656 C CE1 . TYR A 1 216 ? 13.033 10.534 24.447 1.00 15.28 ? 216 TYR A CE1 1 ATOM 1657 C CE2 . TYR A 1 216 ? 11.739 11.644 22.775 1.00 16.51 ? 216 TYR A CE2 1 ATOM 1658 C CZ . TYR A 1 216 ? 12.944 11.097 23.198 1.00 17.01 ? 216 TYR A CZ 1 ATOM 1659 O OH . TYR A 1 216 ? 14.052 11.137 22.351 1.00 17.78 ? 216 TYR A OH 1 ATOM 1660 N N . PRO A 1 217 ? 8.842 14.280 26.036 1.00 7.79 ? 217 PRO A N 1 ATOM 1661 C CA . PRO A 1 217 ? 9.109 15.626 25.501 1.00 7.41 ? 217 PRO A CA 1 ATOM 1662 C C . PRO A 1 217 ? 9.900 16.528 26.425 1.00 7.82 ? 217 PRO A C 1 ATOM 1663 O O . PRO A 1 217 ? 10.602 17.446 25.944 1.00 7.48 ? 217 PRO A O 1 ATOM 1664 C CB . PRO A 1 217 ? 7.726 16.170 25.141 1.00 8.48 ? 217 PRO A CB 1 ATOM 1665 C CG . PRO A 1 217 ? 6.895 14.939 24.926 1.00 8.06 ? 217 PRO A CG 1 ATOM 1666 C CD . PRO A 1 217 ? 7.394 13.956 25.974 1.00 9.30 ? 217 PRO A CD 1 ATOM 1667 N N . TYR A 1 218 ? 9.852 16.301 27.754 1.00 5.96 ? 218 TYR A N 1 ATOM 1668 C CA . TYR A 1 218 ? 10.613 17.067 28.750 1.00 7.73 ? 218 TYR A CA 1 ATOM 1669 C C . TYR A 1 218 ? 12.062 16.562 28.926 1.00 7.76 ? 218 TYR A C 1 ATOM 1670 O O . TYR A 1 218 ? 12.927 17.285 29.484 1.00 7.06 ? 218 TYR A O 1 ATOM 1671 C CB . TYR A 1 218 ? 9.917 17.049 30.116 1.00 9.03 ? 218 TYR A CB 1 ATOM 1672 C CG . TYR A 1 218 ? 8.671 17.889 30.349 1.00 9.77 ? 218 TYR A CG 1 ATOM 1673 C CD1 . TYR A 1 218 ? 8.766 19.280 30.357 1.00 9.33 ? 218 TYR A CD1 1 ATOM 1674 C CD2 . TYR A 1 218 ? 7.414 17.355 30.574 1.00 9.34 ? 218 TYR A CD2 1 ATOM 1675 C CE1 . TYR A 1 218 ? 7.678 20.113 30.564 1.00 9.89 ? 218 TYR A CE1 1 ATOM 1676 C CE2 . TYR A 1 218 ? 6.314 18.166 30.793 1.00 10.07 ? 218 TYR A CE2 1 ATOM 1677 C CZ . TYR A 1 218 ? 6.435 19.547 30.781 1.00 11.27 ? 218 TYR A CZ 1 ATOM 1678 O OH . TYR A 1 218 ? 5.315 20.341 31.012 1.00 9.89 ? 218 TYR A OH 1 ATOM 1679 N N . THR A 1 219 ? 12.384 15.374 28.459 1.00 7.61 ? 219 THR A N 1 ATOM 1680 C CA . THR A 1 219 ? 13.740 14.806 28.527 1.00 8.88 ? 219 THR A CA 1 ATOM 1681 C C . THR A 1 219 ? 14.653 15.261 27.411 1.00 8.86 ? 219 THR A C 1 ATOM 1682 O O . THR A 1 219 ? 14.260 16.115 26.583 1.00 8.60 ? 219 THR A O 1 ATOM 1683 C CB . THR A 1 219 ? 13.768 13.266 28.664 1.00 9.79 ? 219 THR A CB 1 ATOM 1684 O OG1 . THR A 1 219 ? 13.466 12.701 27.382 1.00 10.36 ? 219 THR A OG1 1 ATOM 1685 C CG2 . THR A 1 219 ? 12.770 12.737 29.684 1.00 10.37 ? 219 THR A CG2 1 ATOM 1686 N N . TYR A 1 220 ? 15.905 14.779 27.422 1.00 8.35 ? 220 TYR A N 1 ATOM 1687 C CA . TYR A 1 220 ? 16.971 15.321 26.553 1.00 8.64 ? 220 TYR A CA 1 ATOM 1688 C C . TYR A 1 220 ? 17.514 14.354 25.512 1.00 9.38 ? 220 TYR A C 1 ATOM 1689 O O . TYR A 1 220 ? 18.721 14.227 25.330 1.00 10.93 ? 220 TYR A O 1 ATOM 1690 C CB . TYR A 1 220 ? 18.098 15.934 27.421 1.00 7.49 ? 220 TYR A CB 1 ATOM 1691 C CG . TYR A 1 220 ? 17.664 17.035 28.383 1.00 9.16 ? 220 TYR A CG 1 ATOM 1692 C CD1 . TYR A 1 220 ? 17.639 18.371 28.006 1.00 8.52 ? 220 TYR A CD1 1 ATOM 1693 C CD2 . TYR A 1 220 ? 17.219 16.757 29.657 1.00 10.06 ? 220 TYR A CD2 1 ATOM 1694 C CE1 . TYR A 1 220 ? 17.241 19.389 28.853 1.00 9.15 ? 220 TYR A CE1 1 ATOM 1695 C CE2 . TYR A 1 220 ? 16.801 17.764 30.531 1.00 9.89 ? 220 TYR A CE2 1 ATOM 1696 C CZ . TYR A 1 220 ? 16.798 19.069 30.126 1.00 9.58 ? 220 TYR A CZ 1 ATOM 1697 O OH . TYR A 1 220 ? 16.401 20.087 30.983 1.00 9.77 ? 220 TYR A OH 1 ATOM 1698 N N . GLY A 1 221 ? 16.637 13.719 24.736 1.00 8.62 ? 221 GLY A N 1 ATOM 1699 C CA . GLY A 1 221 ? 17.041 12.772 23.699 1.00 9.22 ? 221 GLY A CA 1 ATOM 1700 C C . GLY A 1 221 ? 17.046 13.285 22.258 1.00 9.53 ? 221 GLY A C 1 ATOM 1701 O O . GLY A 1 221 ? 17.432 12.496 21.375 1.00 7.44 ? 221 GLY A O 1 ATOM 1702 N N . GLU A 1 222 ? 16.693 14.552 22.026 1.00 7.96 ? 222 GLU A N 1 ATOM 1703 C CA . GLU A 1 222 ? 16.625 15.109 20.675 1.00 7.33 ? 222 GLU A CA 1 ATOM 1704 C C . GLU A 1 222 ? 17.567 16.286 20.447 1.00 8.72 ? 222 GLU A C 1 ATOM 1705 O O . GLU A 1 222 ? 17.404 17.054 19.476 1.00 8.45 ? 222 GLU A O 1 ATOM 1706 C CB . GLU A 1 222 ? 15.177 15.526 20.345 1.00 7.39 ? 222 GLU A CB 1 ATOM 1707 C CG . GLU A 1 222 ? 14.197 14.349 20.364 1.00 9.48 ? 222 GLU A CG 1 ATOM 1708 C CD . GLU A 1 222 ? 14.489 13.176 19.443 1.00 10.44 ? 222 GLU A CD 1 ATOM 1709 O OE1 . GLU A 1 222 ? 15.216 13.275 18.431 1.00 10.12 ? 222 GLU A OE1 1 ATOM 1710 O OE2 . GLU A 1 222 ? 14.007 12.047 19.670 1.00 10.59 ? 222 GLU A OE2 1 ATOM 1711 N N . GLY A 1 223 ? 18.601 16.412 21.289 1.00 6.94 ? 223 GLY A N 1 ATOM 1712 C CA . GLY A 1 223 ? 19.648 17.401 21.112 1.00 7.12 ? 223 GLY A CA 1 ATOM 1713 C C . GLY A 1 223 ? 19.302 18.848 21.451 1.00 8.54 ? 223 GLY A C 1 ATOM 1714 O O . GLY A 1 223 ? 20.060 19.767 21.116 1.00 8.37 ? 223 GLY A O 1 ATOM 1715 N N . THR A 1 224 ? 18.169 19.073 22.126 1.00 6.45 ? 224 THR A N 1 ATOM 1716 C CA . THR A 1 224 ? 17.769 20.417 22.527 1.00 6.77 ? 224 THR A CA 1 ATOM 1717 C C . THR A 1 224 ? 17.576 20.614 24.034 1.00 7.10 ? 224 THR A C 1 ATOM 1718 O O . THR A 1 224 ? 17.083 19.748 24.743 1.00 6.98 ? 224 THR A O 1 ATOM 1719 C CB . THR A 1 224 ? 16.509 20.909 21.786 1.00 7.13 ? 224 THR A CB 1 ATOM 1720 O OG1 . THR A 1 224 ? 15.363 20.105 22.125 1.00 6.64 ? 224 THR A OG1 1 ATOM 1721 C CG2 . THR A 1 224 ? 16.694 20.889 20.278 1.00 6.45 ? 224 THR A CG2 1 ATOM 1722 N N . ASP A 1 225 ? 17.960 21.795 24.532 1.00 5.73 ? 225 ASP A N 1 ATOM 1723 C CA . ASP A 1 225 ? 17.783 22.286 25.909 1.00 6.79 ? 225 ASP A CA 1 ATOM 1724 C C . ASP A 1 225 ? 17.079 23.646 25.841 1.00 6.19 ? 225 ASP A C 1 ATOM 1725 O O . ASP A 1 225 ? 17.678 24.650 25.420 1.00 6.21 ? 225 ASP A O 1 ATOM 1726 C CB . ASP A 1 225 ? 19.108 22.304 26.669 1.00 7.02 ? 225 ASP A CB 1 ATOM 1727 C CG . ASP A 1 225 ? 19.134 22.767 28.106 1.00 9.76 ? 225 ASP A CG 1 ATOM 1728 O OD1 . ASP A 1 225 ? 18.335 23.652 28.476 1.00 9.09 ? 225 ASP A OD1 1 ATOM 1729 O OD2 . ASP A 1 225 ? 20.006 22.299 28.924 1.00 10.16 ? 225 ASP A OD2 1 ATOM 1730 N N . PHE A 1 226 ? 15.773 23.694 26.178 1.00 6.31 ? 226 PHE A N 1 ATOM 1731 C CA . PHE A 1 226 ? 14.937 24.881 26.031 1.00 6.91 ? 226 PHE A CA 1 ATOM 1732 C C . PHE A 1 226 ? 15.479 26.104 26.774 1.00 8.87 ? 226 PHE A C 1 ATOM 1733 O O . PHE A 1 226 ? 15.569 27.178 26.173 1.00 7.11 ? 226 PHE A O 1 ATOM 1734 C CB . PHE A 1 226 ? 13.461 24.681 26.399 1.00 7.39 ? 226 PHE A CB 1 ATOM 1735 C CG . PHE A 1 226 ? 12.514 25.817 26.067 1.00 9.35 ? 226 PHE A CG 1 ATOM 1736 C CD1 . PHE A 1 226 ? 12.136 26.055 24.756 1.00 8.56 ? 226 PHE A CD1 1 ATOM 1737 C CD2 . PHE A 1 226 ? 11.999 26.659 27.059 1.00 9.10 ? 226 PHE A CD2 1 ATOM 1738 C CE1 . PHE A 1 226 ? 11.289 27.092 24.417 1.00 8.59 ? 226 PHE A CE1 1 ATOM 1739 C CE2 . PHE A 1 226 ? 11.123 27.678 26.741 1.00 9.15 ? 226 PHE A CE2 1 ATOM 1740 C CZ . PHE A 1 226 ? 10.775 27.918 25.411 1.00 8.40 ? 226 PHE A CZ 1 ATOM 1741 N N . ALA A 1 227 ? 15.838 25.974 28.062 1.00 9.22 ? 227 ALA A N 1 ATOM 1742 C CA . ALA A 1 227 ? 16.391 27.138 28.770 1.00 10.61 ? 227 ALA A CA 1 ATOM 1743 C C . ALA A 1 227 ? 17.685 27.652 28.174 1.00 11.86 ? 227 ALA A C 1 ATOM 1744 O O . ALA A 1 227 ? 17.867 28.886 27.996 1.00 13.50 ? 227 ALA A O 1 ATOM 1745 C CB . ALA A 1 227 ? 16.509 26.819 30.257 1.00 11.34 ? 227 ALA A CB 1 ATOM 1746 N N . LYS A 1 228 ? 18.607 26.790 27.785 1.00 10.31 ? 228 LYS A N 1 ATOM 1747 C CA . LYS A 1 228 ? 19.853 27.222 27.151 1.00 11.44 ? 228 LYS A CA 1 ATOM 1748 C C . LYS A 1 228 ? 19.615 27.930 25.823 1.00 11.14 ? 228 LYS A C 1 ATOM 1749 O O . LYS A 1 228 ? 20.323 28.906 25.516 1.00 12.62 ? 228 LYS A O 1 ATOM 1750 C CB . LYS A 1 228 ? 20.856 26.099 26.940 1.00 14.81 ? 228 LYS A CB 1 ATOM 1751 C CG . LYS A 1 228 ? 21.559 25.600 28.182 1.00 19.10 ? 228 LYS A CG 1 ATOM 1752 C CD . LYS A 1 228 ? 22.708 24.675 27.739 1.00 23.59 ? 228 LYS A CD 1 ATOM 1753 C CE . LYS A 1 228 ? 23.464 24.150 28.958 1.00 27.45 ? 228 LYS A CE 1 ATOM 1754 N NZ . LYS A 1 228 ? 23.933 25.259 29.852 1.00 29.80 ? 228 LYS A NZ 1 ATOM 1755 N N . ASN A 1 229 ? 18.688 27.426 25.008 1.00 8.26 ? 229 ASN A N 1 ATOM 1756 C CA . ASN A 1 229 ? 18.417 28.029 23.701 1.00 9.58 ? 229 ASN A CA 1 ATOM 1757 C C . ASN A 1 229 ? 17.788 29.410 23.837 1.00 10.45 ? 229 ASN A C 1 ATOM 1758 O O . ASN A 1 229 ? 18.175 30.373 23.129 1.00 10.10 ? 229 ASN A O 1 ATOM 1759 C CB . ASN A 1 229 ? 17.495 27.093 22.895 1.00 8.78 ? 229 ASN A CB 1 ATOM 1760 C CG . ASN A 1 229 ? 18.165 25.834 22.374 1.00 10.12 ? 229 ASN A CG 1 ATOM 1761 O OD1 . ASN A 1 229 ? 19.363 25.800 22.142 1.00 10.32 ? 229 ASN A OD1 1 ATOM 1762 N ND2 . ASN A 1 229 ? 17.435 24.733 22.133 1.00 8.29 ? 229 ASN A ND2 1 ATOM 1763 N N . VAL A 1 230 ? 16.797 29.565 24.723 1.00 9.76 ? 230 VAL A N 1 ATOM 1764 C CA . VAL A 1 230 ? 16.137 30.861 24.906 1.00 11.06 ? 230 VAL A CA 1 ATOM 1765 C C . VAL A 1 230 ? 17.019 31.949 25.518 1.00 11.70 ? 230 VAL A C 1 ATOM 1766 O O . VAL A 1 230 ? 16.681 33.130 25.314 1.00 12.43 ? 230 VAL A O 1 ATOM 1767 C CB . VAL A 1 230 ? 14.779 30.893 25.626 1.00 11.85 ? 230 VAL A CB 1 ATOM 1768 C CG1 A VAL A 1 230 ? 13.739 30.128 24.826 0.50 12.26 ? 230 VAL A CG1 1 ATOM 1769 C CG1 B VAL A 1 230 ? 13.893 32.047 25.188 0.50 12.18 ? 230 VAL A CG1 1 ATOM 1770 C CG2 A VAL A 1 230 ? 14.830 30.405 27.072 0.50 8.18 ? 230 VAL A CG2 1 ATOM 1771 C CG2 B VAL A 1 230 ? 14.025 29.599 25.320 0.50 12.49 ? 230 VAL A CG2 1 ATOM 1772 N N . GLN A 1 231 ? 18.123 31.584 26.176 1.00 10.12 ? 231 GLN A N 1 ATOM 1773 C CA . GLN A 1 231 ? 19.100 32.535 26.678 1.00 12.12 ? 231 GLN A CA 1 ATOM 1774 C C . GLN A 1 231 ? 20.152 32.969 25.674 1.00 10.48 ? 231 GLN A C 1 ATOM 1775 O O . GLN A 1 231 ? 20.928 33.900 25.968 1.00 9.05 ? 231 GLN A O 1 ATOM 1776 C CB . GLN A 1 231 ? 19.717 31.962 27.985 1.00 16.39 ? 231 GLN A CB 1 ATOM 1777 C CG . GLN A 1 231 ? 18.648 31.790 29.040 1.00 21.93 ? 231 GLN A CG 1 ATOM 1778 C CD . GLN A 1 231 ? 18.772 30.876 30.218 1.00 26.22 ? 231 GLN A CD 1 ATOM 1779 O OE1 . GLN A 1 231 ? 19.853 30.544 30.699 1.00 28.80 ? 231 GLN A OE1 1 ATOM 1780 N NE2 . GLN A 1 231 ? 17.618 30.420 30.754 1.00 27.18 ? 231 GLN A NE2 1 ATOM 1781 N N . ILE A 1 232 ? 20.156 32.442 24.453 1.00 8.59 ? 232 ILE A N 1 ATOM 1782 C CA . ILE A 1 232 ? 21.101 32.900 23.405 1.00 9.26 ? 232 ILE A CA 1 ATOM 1783 C C . ILE A 1 232 ? 20.871 34.393 23.134 1.00 9.11 ? 232 ILE A C 1 ATOM 1784 O O . ILE A 1 232 ? 19.724 34.815 22.937 1.00 6.89 ? 232 ILE A O 1 ATOM 1785 C CB . ILE A 1 232 ? 20.931 31.982 22.176 1.00 9.10 ? 232 ILE A CB 1 ATOM 1786 C CG1 . ILE A 1 232 ? 21.423 30.550 22.433 1.00 9.46 ? 232 ILE A CG1 1 ATOM 1787 C CG2 . ILE A 1 232 ? 21.687 32.581 20.976 1.00 9.32 ? 232 ILE A CG2 1 ATOM 1788 C CD1 . ILE A 1 232 ? 21.193 29.516 21.339 1.00 9.10 ? 232 ILE A CD1 1 ATOM 1789 N N . LYS A 1 233 ? 21.923 35.243 23.132 1.00 7.56 ? 233 LYS A N 1 ATOM 1790 C CA . LYS A 1 233 ? 21.731 36.691 23.061 1.00 10.61 ? 233 LYS A CA 1 ATOM 1791 C C . LYS A 1 233 ? 21.098 37.251 21.795 1.00 10.34 ? 233 LYS A C 1 ATOM 1792 O O . LYS A 1 233 ? 20.354 38.247 21.857 1.00 10.01 ? 233 LYS A O 1 ATOM 1793 C CB . LYS A 1 233 ? 23.107 37.380 23.302 1.00 14.28 ? 233 LYS A CB 1 ATOM 1794 C CG . LYS A 1 233 ? 23.624 36.968 24.670 1.00 20.79 ? 233 LYS A CG 1 ATOM 1795 C CD . LYS A 1 233 ? 25.062 37.262 24.984 1.00 25.36 ? 233 LYS A CD 1 ATOM 1796 C CE . LYS A 1 233 ? 25.608 38.522 24.385 1.00 28.96 ? 233 LYS A CE 1 ATOM 1797 N NZ . LYS A 1 233 ? 25.840 38.423 22.915 1.00 32.12 ? 233 LYS A NZ 1 ATOM 1798 N N . SER A 1 234 ? 21.318 36.589 20.659 1.00 10.93 ? 234 SER A N 1 ATOM 1799 C CA . SER A 1 234 ? 20.816 36.996 19.354 1.00 11.27 ? 234 SER A CA 1 ATOM 1800 C C . SER A 1 234 ? 19.479 36.357 18.970 1.00 11.32 ? 234 SER A C 1 ATOM 1801 O O . SER A 1 234 ? 19.050 36.470 17.803 1.00 11.28 ? 234 SER A O 1 ATOM 1802 C CB . SER A 1 234 ? 21.888 36.812 18.267 1.00 12.87 ? 234 SER A CB 1 ATOM 1803 O OG . SER A 1 234 ? 22.733 35.668 18.524 1.00 14.49 ? 234 SER A OG 1 ATOM 1804 N N . LEU A 1 235 ? 18.773 35.749 19.909 1.00 9.92 ? 235 LEU A N 1 ATOM 1805 C CA . LEU A 1 235 ? 17.390 35.299 19.730 1.00 9.25 ? 235 LEU A CA 1 ATOM 1806 C C . LEU A 1 235 ? 16.491 36.191 20.606 1.00 10.51 ? 235 LEU A C 1 ATOM 1807 O O . LEU A 1 235 ? 16.835 36.477 21.783 1.00 10.09 ? 235 LEU A O 1 ATOM 1808 C CB . LEU A 1 235 ? 17.161 33.805 20.055 1.00 8.19 ? 235 LEU A CB 1 ATOM 1809 C CG . LEU A 1 235 ? 17.918 32.791 19.195 1.00 9.00 ? 235 LEU A CG 1 ATOM 1810 C CD1 . LEU A 1 235 ? 17.726 31.365 19.714 1.00 9.80 ? 235 LEU A CD1 1 ATOM 1811 C CD2 . LEU A 1 235 ? 17.505 32.857 17.723 1.00 7.54 ? 235 LEU A CD2 1 ATOM 1812 N N . ASP A 1 236 ? 15.329 36.641 20.125 1.00 8.79 ? 236 ASP A N 1 ATOM 1813 C CA . ASP A 1 236 ? 14.537 37.646 20.832 1.00 9.35 ? 236 ASP A CA 1 ATOM 1814 C C . ASP A 1 236 ? 13.335 37.137 21.616 1.00 9.32 ? 236 ASP A C 1 ATOM 1815 O O . ASP A 1 236 ? 12.828 37.816 22.517 1.00 8.40 ? 236 ASP A O 1 ATOM 1816 C CB . ASP A 1 236 ? 14.133 38.707 19.765 1.00 9.75 ? 236 ASP A CB 1 ATOM 1817 C CG . ASP A 1 236 ? 15.296 39.415 19.110 1.00 12.05 ? 236 ASP A CG 1 ATOM 1818 O OD1 . ASP A 1 236 ? 16.248 39.904 19.812 1.00 13.40 ? 236 ASP A OD1 1 ATOM 1819 O OD2 . ASP A 1 236 ? 15.332 39.517 17.861 1.00 9.82 ? 236 ASP A OD2 1 ATOM 1820 N N . PHE A 1 237 ? 12.837 35.945 21.300 1.00 8.22 ? 237 PHE A N 1 ATOM 1821 C CA . PHE A 1 237 ? 11.688 35.309 21.946 1.00 8.45 ? 237 PHE A CA 1 ATOM 1822 C C . PHE A 1 237 ? 11.739 33.789 21.763 1.00 7.70 ? 237 PHE A C 1 ATOM 1823 O O . PHE A 1 237 ? 12.424 33.284 20.852 1.00 6.52 ? 237 PHE A O 1 ATOM 1824 C CB . PHE A 1 237 ? 10.354 35.942 21.477 1.00 8.32 ? 237 PHE A CB 1 ATOM 1825 C CG . PHE A 1 237 ? 9.947 35.707 20.027 1.00 9.01 ? 237 PHE A CG 1 ATOM 1826 C CD1 . PHE A 1 237 ? 9.282 34.590 19.611 1.00 9.36 ? 237 PHE A CD1 1 ATOM 1827 C CD2 . PHE A 1 237 ? 10.305 36.635 19.053 1.00 8.37 ? 237 PHE A CD2 1 ATOM 1828 C CE1 . PHE A 1 237 ? 8.928 34.369 18.275 1.00 8.74 ? 237 PHE A CE1 1 ATOM 1829 C CE2 . PHE A 1 237 ? 9.984 36.429 17.724 1.00 7.17 ? 237 PHE A CE2 1 ATOM 1830 C CZ . PHE A 1 237 ? 9.238 35.319 17.318 1.00 6.96 ? 237 PHE A CZ 1 ATOM 1831 N N . GLY A 1 238 ? 11.063 33.018 22.631 1.00 5.95 ? 238 GLY A N 1 ATOM 1832 C CA . GLY A 1 238 ? 10.987 31.569 22.558 1.00 7.06 ? 238 GLY A CA 1 ATOM 1833 C C . GLY A 1 238 ? 9.816 31.031 21.732 1.00 8.12 ? 238 GLY A C 1 ATOM 1834 O O . GLY A 1 238 ? 8.759 31.708 21.656 1.00 7.87 ? 238 GLY A O 1 ATOM 1835 N N . THR A 1 239 ? 10.002 29.844 21.119 1.00 6.99 ? 239 THR A N 1 ATOM 1836 C CA . THR A 1 239 ? 8.912 29.125 20.450 1.00 7.37 ? 239 THR A CA 1 ATOM 1837 C C . THR A 1 239 ? 8.670 27.712 20.999 1.00 7.69 ? 239 THR A C 1 ATOM 1838 O O . THR A 1 239 ? 9.636 27.045 21.440 1.00 6.13 ? 239 THR A O 1 ATOM 1839 C CB . THR A 1 239 ? 9.197 28.943 18.931 1.00 6.90 ? 239 THR A CB 1 ATOM 1840 O OG1 . THR A 1 239 ? 10.508 28.349 18.738 1.00 6.36 ? 239 THR A OG1 1 ATOM 1841 C CG2 . THR A 1 239 ? 9.158 30.256 18.182 1.00 6.09 ? 239 THR A CG2 1 ATOM 1842 N N . PHE A 1 240 ? 7.442 27.176 20.975 1.00 6.23 ? 240 PHE A N 1 ATOM 1843 C CA . PHE A 1 240 ? 7.209 25.752 21.309 1.00 5.77 ? 240 PHE A CA 1 ATOM 1844 C C . PHE A 1 240 ? 5.969 25.255 20.548 1.00 7.23 ? 240 PHE A C 1 ATOM 1845 O O . PHE A 1 240 ? 5.104 26.063 20.141 1.00 7.02 ? 240 PHE A O 1 ATOM 1846 C CB . PHE A 1 240 ? 7.094 25.507 22.819 1.00 6.72 ? 240 PHE A CB 1 ATOM 1847 C CG . PHE A 1 240 ? 5.955 26.179 23.551 1.00 7.22 ? 240 PHE A CG 1 ATOM 1848 C CD1 . PHE A 1 240 ? 6.073 27.432 24.129 1.00 7.54 ? 240 PHE A CD1 1 ATOM 1849 C CD2 . PHE A 1 240 ? 4.739 25.530 23.698 1.00 7.57 ? 240 PHE A CD2 1 ATOM 1850 C CE1 . PHE A 1 240 ? 4.994 28.012 24.793 1.00 8.20 ? 240 PHE A CE1 1 ATOM 1851 C CE2 . PHE A 1 240 ? 3.659 26.096 24.361 1.00 7.65 ? 240 PHE A CE2 1 ATOM 1852 C CZ . PHE A 1 240 ? 3.777 27.355 24.910 1.00 7.28 ? 240 PHE A CZ 1 ATOM 1853 N N . HIS A 1 241 ? 5.929 23.958 20.276 1.00 6.06 ? 241 HIS A N 1 ATOM 1854 C CA . HIS A 1 241 ? 4.845 23.262 19.560 1.00 7.52 ? 241 HIS A CA 1 ATOM 1855 C C . HIS A 1 241 ? 4.115 22.257 20.460 1.00 8.49 ? 241 HIS A C 1 ATOM 1856 O O . HIS A 1 241 ? 4.615 21.972 21.553 1.00 8.94 ? 241 HIS A O 1 ATOM 1857 C CB . HIS A 1 241 ? 5.393 22.579 18.310 1.00 7.31 ? 241 HIS A CB 1 ATOM 1858 C CG . HIS A 1 241 ? 6.066 23.420 17.248 1.00 8.54 ? 241 HIS A CG 1 ATOM 1859 N ND1 . HIS A 1 241 ? 6.477 22.901 16.022 1.00 7.32 ? 241 HIS A ND1 1 ATOM 1860 C CD2 . HIS A 1 241 ? 6.379 24.722 17.219 1.00 8.24 ? 241 HIS A CD2 1 ATOM 1861 C CE1 . HIS A 1 241 ? 7.022 23.906 15.318 1.00 8.25 ? 241 HIS A CE1 1 ATOM 1862 N NE2 . HIS A 1 241 ? 6.974 25.025 15.999 1.00 7.70 ? 241 HIS A NE2 1 ATOM 1863 N N . LEU A 1 242 ? 3.010 21.628 20.066 1.00 7.52 ? 242 LEU A N 1 ATOM 1864 C CA . LEU A 1 242 ? 2.253 20.689 20.915 1.00 7.50 ? 242 LEU A CA 1 ATOM 1865 C C . LEU A 1 242 ? 1.424 19.665 20.115 1.00 8.44 ? 242 LEU A C 1 ATOM 1866 O O . LEU A 1 242 ? 0.441 20.056 19.453 1.00 6.64 ? 242 LEU A O 1 ATOM 1867 C CB . LEU A 1 242 ? 1.392 21.442 21.922 1.00 6.36 ? 242 LEU A CB 1 ATOM 1868 C CG . LEU A 1 242 ? 0.428 20.638 22.805 1.00 7.67 ? 242 LEU A CG 1 ATOM 1869 C CD1 . LEU A 1 242 ? 1.274 19.731 23.709 1.00 6.13 ? 242 LEU A CD1 1 ATOM 1870 C CD2 . LEU A 1 242 ? -0.487 21.534 23.636 1.00 9.19 ? 242 LEU A CD2 1 ATOM 1871 N N . TYR A 1 243 ? 1.775 18.369 20.205 1.00 7.85 ? 243 TYR A N 1 ATOM 1872 C CA . TYR A 1 243 ? 1.038 17.288 19.494 1.00 9.10 ? 243 TYR A CA 1 ATOM 1873 C C . TYR A 1 243 ? 0.951 16.019 20.352 1.00 9.77 ? 243 TYR A C 1 ATOM 1874 O O . TYR A 1 243 ? 1.688 15.017 20.188 1.00 9.04 ? 243 TYR A O 1 ATOM 1875 C CB . TYR A 1 243 ? 1.767 16.989 18.173 1.00 9.47 ? 243 TYR A CB 1 ATOM 1876 C CG . TYR A 1 243 ? 1.712 17.966 17.020 1.00 10.42 ? 243 TYR A CG 1 ATOM 1877 C CD1 . TYR A 1 243 ? 0.552 18.039 16.254 1.00 10.72 ? 243 TYR A CD1 1 ATOM 1878 C CD2 . TYR A 1 243 ? 2.754 18.822 16.686 1.00 9.84 ? 243 TYR A CD2 1 ATOM 1879 C CE1 . TYR A 1 243 ? 0.429 18.902 15.175 1.00 10.99 ? 243 TYR A CE1 1 ATOM 1880 C CE2 . TYR A 1 243 ? 2.668 19.698 15.619 1.00 10.58 ? 243 TYR A CE2 1 ATOM 1881 C CZ . TYR A 1 243 ? 1.505 19.704 14.853 1.00 12.30 ? 243 TYR A CZ 1 ATOM 1882 O OH . TYR A 1 243 ? 1.359 20.572 13.795 1.00 12.95 ? 243 TYR A OH 1 ATOM 1883 N N . PRO A 1 244 ? 0.052 15.983 21.326 1.00 9.69 ? 244 PRO A N 1 ATOM 1884 C CA . PRO A 1 244 ? -0.131 14.872 22.264 1.00 12.09 ? 244 PRO A CA 1 ATOM 1885 C C . PRO A 1 244 ? -0.385 13.503 21.680 1.00 14.07 ? 244 PRO A C 1 ATOM 1886 O O . PRO A 1 244 ? 0.152 12.501 22.195 1.00 14.63 ? 244 PRO A O 1 ATOM 1887 C CB . PRO A 1 244 ? -1.283 15.249 23.179 1.00 12.91 ? 244 PRO A CB 1 ATOM 1888 C CG . PRO A 1 244 ? -1.462 16.703 22.999 1.00 12.81 ? 244 PRO A CG 1 ATOM 1889 C CD . PRO A 1 244 ? -0.922 17.060 21.647 1.00 10.18 ? 244 PRO A CD 1 ATOM 1890 N N . ASP A 1 245 ? -1.102 13.423 20.576 1.00 15.67 ? 245 ASP A N 1 ATOM 1891 C CA . ASP A 1 245 ? -1.391 12.131 19.949 1.00 18.76 ? 245 ASP A CA 1 ATOM 1892 C C . ASP A 1 245 ? -0.170 11.537 19.280 1.00 18.70 ? 245 ASP A C 1 ATOM 1893 O O . ASP A 1 245 ? -0.192 10.331 19.036 1.00 21.28 ? 245 ASP A O 1 ATOM 1894 C CB . ASP A 1 245 ? -2.524 12.261 18.946 1.00 21.28 ? 245 ASP A CB 1 ATOM 1895 C CG . ASP A 1 245 ? -3.888 12.511 19.543 1.00 24.18 ? 245 ASP A CG 1 ATOM 1896 O OD1 . ASP A 1 245 ? -4.233 12.008 20.641 1.00 26.39 ? 245 ASP A OD1 1 ATOM 1897 O OD2 . ASP A 1 245 ? -4.644 13.259 18.912 1.00 26.09 ? 245 ASP A OD2 1 ATOM 1898 N N . SER A 1 246 ? 0.885 12.296 18.980 1.00 17.79 ? 246 SER A N 1 ATOM 1899 C CA . SER A 1 246 ? 2.085 11.758 18.381 1.00 17.83 ? 246 SER A CA 1 ATOM 1900 C C . SER A 1 246 ? 3.120 11.479 19.478 1.00 17.41 ? 246 SER A C 1 ATOM 1901 O O . SER A 1 246 ? 4.032 10.679 19.316 1.00 19.03 ? 246 SER A O 1 ATOM 1902 C CB . SER A 1 246 ? 2.705 12.728 17.360 1.00 19.76 ? 246 SER A CB 1 ATOM 1903 O OG . SER A 1 246 ? 1.770 13.299 16.445 1.00 19.56 ? 246 SER A OG 1 ATOM 1904 N N . TRP A 1 247 ? 3.021 12.125 20.630 1.00 15.37 ? 247 TRP A N 1 ATOM 1905 C CA . TRP A 1 247 ? 3.946 12.086 21.730 1.00 16.64 ? 247 TRP A CA 1 ATOM 1906 C C . TRP A 1 247 ? 3.612 11.098 22.844 1.00 17.72 ? 247 TRP A C 1 ATOM 1907 O O . TRP A 1 247 ? 4.352 10.977 23.835 1.00 17.62 ? 247 TRP A O 1 ATOM 1908 C CB . TRP A 1 247 ? 4.055 13.527 22.281 1.00 14.58 ? 247 TRP A CB 1 ATOM 1909 C CG . TRP A 1 247 ? 4.674 14.554 21.386 1.00 14.30 ? 247 TRP A CG 1 ATOM 1910 C CD1 . TRP A 1 247 ? 5.279 14.360 20.165 1.00 14.69 ? 247 TRP A CD1 1 ATOM 1911 C CD2 . TRP A 1 247 ? 4.827 15.961 21.656 1.00 12.82 ? 247 TRP A CD2 1 ATOM 1912 N NE1 . TRP A 1 247 ? 5.759 15.517 19.668 1.00 13.81 ? 247 TRP A NE1 1 ATOM 1913 C CE2 . TRP A 1 247 ? 5.519 16.540 20.559 1.00 12.52 ? 247 TRP A CE2 1 ATOM 1914 C CE3 . TRP A 1 247 ? 4.450 16.778 22.733 1.00 10.98 ? 247 TRP A CE3 1 ATOM 1915 C CZ2 . TRP A 1 247 ? 5.819 17.890 20.497 1.00 10.97 ? 247 TRP A CZ2 1 ATOM 1916 C CZ3 . TRP A 1 247 ? 4.782 18.135 22.663 1.00 10.21 ? 247 TRP A CZ3 1 ATOM 1917 C CH2 . TRP A 1 247 ? 5.454 18.679 21.564 1.00 10.18 ? 247 TRP A CH2 1 ATOM 1918 N N . GLY A 1 248 ? 2.452 10.453 22.782 1.00 18.12 ? 248 GLY A N 1 ATOM 1919 C CA . GLY A 1 248 ? 2.045 9.500 23.815 1.00 19.69 ? 248 GLY A CA 1 ATOM 1920 C C . GLY A 1 248 ? 1.511 10.094 25.108 1.00 20.55 ? 248 GLY A C 1 ATOM 1921 O O . GLY A 1 248 ? 1.493 9.396 26.134 1.00 23.14 ? 248 GLY A O 1 ATOM 1922 N N . THR A 1 249 ? 1.107 11.351 25.137 1.00 18.10 ? 249 THR A N 1 ATOM 1923 C CA . THR A 1 249 ? 0.539 11.990 26.306 1.00 17.91 ? 249 THR A CA 1 ATOM 1924 C C . THR A 1 249 ? -0.958 12.243 26.108 1.00 18.34 ? 249 THR A C 1 ATOM 1925 O O . THR A 1 249 ? -1.468 12.131 24.978 1.00 18.33 ? 249 THR A O 1 ATOM 1926 C CB . THR A 1 249 ? 1.228 13.326 26.648 1.00 17.23 ? 249 THR A CB 1 ATOM 1927 O OG1 . THR A 1 249 ? 1.097 14.240 25.533 1.00 16.36 ? 249 THR A OG1 1 ATOM 1928 C CG2 . THR A 1 249 ? 2.694 13.094 26.953 1.00 17.85 ? 249 THR A CG2 1 ATOM 1929 N N . ASN A 1 250 ? -1.676 12.598 27.166 1.00 18.42 ? 250 ASN A N 1 ATOM 1930 C CA . ASN A 1 250 ? -3.104 12.928 26.964 1.00 19.86 ? 250 ASN A CA 1 ATOM 1931 C C . ASN A 1 250 ? -3.317 14.407 26.664 1.00 18.33 ? 250 ASN A C 1 ATOM 1932 O O . ASN A 1 250 ? -2.388 15.214 26.741 1.00 16.44 ? 250 ASN A O 1 ATOM 1933 C CB . ASN A 1 250 ? -3.952 12.476 28.137 1.00 23.13 ? 250 ASN A CB 1 ATOM 1934 C CG . ASN A 1 250 ? -3.657 13.242 29.387 1.00 27.04 ? 250 ASN A CG 1 ATOM 1935 O OD1 . ASN A 1 250 ? -3.358 14.417 29.469 1.00 26.65 ? 250 ASN A OD1 1 ATOM 1936 N ND2 . ASN A 1 250 ? -3.765 12.539 30.553 1.00 31.32 ? 250 ASN A ND2 1 ATOM 1937 N N . TYR A 1 251 ? -4.558 14.777 26.329 1.00 17.13 ? 251 TYR A N 1 ATOM 1938 C CA . TYR A 1 251 ? -4.844 16.151 25.922 1.00 16.91 ? 251 TYR A CA 1 ATOM 1939 C C . TYR A 1 251 ? -4.693 17.168 27.049 1.00 16.73 ? 251 TYR A C 1 ATOM 1940 O O . TYR A 1 251 ? -4.055 18.231 26.858 1.00 15.44 ? 251 TYR A O 1 ATOM 1941 C CB . TYR A 1 251 ? -6.202 16.290 25.194 1.00 17.71 ? 251 TYR A CB 1 ATOM 1942 C CG . TYR A 1 251 ? -6.358 15.491 23.923 1.00 19.66 ? 251 TYR A CG 1 ATOM 1943 C CD1 . TYR A 1 251 ? -5.565 15.713 22.815 1.00 20.04 ? 251 TYR A CD1 1 ATOM 1944 C CD2 . TYR A 1 251 ? -7.321 14.472 23.821 1.00 20.82 ? 251 TYR A CD2 1 ATOM 1945 C CE1 . TYR A 1 251 ? -5.661 14.995 21.648 1.00 20.62 ? 251 TYR A CE1 1 ATOM 1946 C CE2 . TYR A 1 251 ? -7.438 13.755 22.643 1.00 21.40 ? 251 TYR A CE2 1 ATOM 1947 C CZ . TYR A 1 251 ? -6.630 14.009 21.571 1.00 21.44 ? 251 TYR A CZ 1 ATOM 1948 O OH . TYR A 1 251 ? -6.751 13.289 20.398 1.00 21.84 ? 251 TYR A OH 1 ATOM 1949 N N . THR A 1 252 ? -5.110 16.858 28.291 1.00 16.00 ? 252 THR A N 1 ATOM 1950 C CA . THR A 1 252 ? -5.033 17.818 29.376 1.00 16.71 ? 252 THR A CA 1 ATOM 1951 C C . THR A 1 252 ? -3.614 18.108 29.855 1.00 14.42 ? 252 THR A C 1 ATOM 1952 O O . THR A 1 252 ? -3.402 19.182 30.422 1.00 12.33 ? 252 THR A O 1 ATOM 1953 C CB . THR A 1 252 ? -5.929 17.465 30.584 1.00 19.95 ? 252 THR A CB 1 ATOM 1954 O OG1 . THR A 1 252 ? -5.542 16.214 31.135 1.00 21.83 ? 252 THR A OG1 1 ATOM 1955 C CG2 . THR A 1 252 ? -7.388 17.333 30.196 1.00 20.70 ? 252 THR A CG2 1 ATOM 1956 N N . TRP A 1 253 ? -2.656 17.254 29.508 1.00 11.11 ? 253 TRP A N 1 ATOM 1957 C CA . TRP A 1 253 ? -1.226 17.460 29.796 1.00 11.10 ? 253 TRP A CA 1 ATOM 1958 C C . TRP A 1 253 ? -0.710 18.701 29.084 1.00 10.66 ? 253 TRP A C 1 ATOM 1959 O O . TRP A 1 253 ? 0.266 19.300 29.536 1.00 9.66 ? 253 TRP A O 1 ATOM 1960 C CB . TRP A 1 253 ? -0.430 16.220 29.423 1.00 10.53 ? 253 TRP A CB 1 ATOM 1961 C CG . TRP A 1 253 ? 1.061 16.190 29.424 1.00 10.17 ? 253 TRP A CG 1 ATOM 1962 C CD1 . TRP A 1 253 ? 1.894 15.764 30.440 1.00 9.37 ? 253 TRP A CD1 1 ATOM 1963 C CD2 . TRP A 1 253 ? 1.928 16.590 28.351 1.00 9.19 ? 253 TRP A CD2 1 ATOM 1964 N NE1 . TRP A 1 253 ? 3.204 15.899 30.063 1.00 8.38 ? 253 TRP A NE1 1 ATOM 1965 C CE2 . TRP A 1 253 ? 3.246 16.437 28.790 1.00 9.07 ? 253 TRP A CE2 1 ATOM 1966 C CE3 . TRP A 1 253 ? 1.692 17.120 27.084 1.00 9.47 ? 253 TRP A CE3 1 ATOM 1967 C CZ2 . TRP A 1 253 ? 4.363 16.705 27.976 1.00 9.40 ? 253 TRP A CZ2 1 ATOM 1968 C CZ3 . TRP A 1 253 ? 2.791 17.412 26.278 1.00 8.63 ? 253 TRP A CZ3 1 ATOM 1969 C CH2 . TRP A 1 253 ? 4.116 17.215 26.732 1.00 9.78 ? 253 TRP A CH2 1 ATOM 1970 N N . GLY A 1 254 ? -1.343 19.101 27.969 1.00 10.40 ? 254 GLY A N 1 ATOM 1971 C CA . GLY A 1 254 ? -0.966 20.315 27.277 1.00 10.01 ? 254 GLY A CA 1 ATOM 1972 C C . GLY A 1 254 ? -1.025 21.602 28.090 1.00 9.94 ? 254 GLY A C 1 ATOM 1973 O O . GLY A 1 254 ? -0.253 22.551 27.818 1.00 8.17 ? 254 GLY A O 1 ATOM 1974 N N . ASN A 1 255 ? -1.898 21.700 29.108 1.00 8.92 ? 255 ASN A N 1 ATOM 1975 C CA . ASN A 1 255 ? -1.962 22.917 29.903 1.00 10.16 ? 255 ASN A CA 1 ATOM 1976 C C . ASN A 1 255 ? -0.676 23.144 30.704 1.00 10.24 ? 255 ASN A C 1 ATOM 1977 O O . ASN A 1 255 ? -0.129 24.252 30.718 1.00 9.41 ? 255 ASN A O 1 ATOM 1978 C CB . ASN A 1 255 ? -3.175 22.875 30.841 1.00 12.24 ? 255 ASN A CB 1 ATOM 1979 C CG . ASN A 1 255 ? -4.485 22.839 30.055 1.00 13.66 ? 255 ASN A CG 1 ATOM 1980 O OD1 . ASN A 1 255 ? -4.820 23.766 29.313 1.00 13.42 ? 255 ASN A OD1 1 ATOM 1981 N ND2 . ASN A 1 255 ? -5.248 21.767 30.135 1.00 14.79 ? 255 ASN A ND2 1 ATOM 1982 N N . GLY A 1 256 ? -0.187 22.087 31.335 1.00 8.99 ? 256 GLY A N 1 ATOM 1983 C CA . GLY A 1 256 ? 1.109 22.153 32.031 1.00 9.90 ? 256 GLY A CA 1 ATOM 1984 C C . GLY A 1 256 ? 2.287 22.412 31.101 1.00 9.49 ? 256 GLY A C 1 ATOM 1985 O O . GLY A 1 256 ? 3.278 23.080 31.493 1.00 9.96 ? 256 GLY A O 1 ATOM 1986 N N . TRP A 1 257 ? 2.267 21.875 29.884 1.00 7.58 ? 257 TRP A N 1 ATOM 1987 C CA . TRP A 1 257 ? 3.324 22.140 28.887 1.00 8.08 ? 257 TRP A CA 1 ATOM 1988 C C . TRP A 1 257 ? 3.397 23.635 28.569 1.00 7.82 ? 257 TRP A C 1 ATOM 1989 O O . TRP A 1 257 ? 4.465 24.251 28.503 1.00 6.46 ? 257 TRP A O 1 ATOM 1990 C CB . TRP A 1 257 ? 3.082 21.322 27.613 1.00 8.74 ? 257 TRP A CB 1 ATOM 1991 C CG . TRP A 1 257 ? 4.089 21.395 26.489 1.00 8.73 ? 257 TRP A CG 1 ATOM 1992 C CD1 . TRP A 1 257 ? 3.955 22.052 25.317 1.00 8.85 ? 257 TRP A CD1 1 ATOM 1993 C CD2 . TRP A 1 257 ? 5.355 20.733 26.401 1.00 7.89 ? 257 TRP A CD2 1 ATOM 1994 N NE1 . TRP A 1 257 ? 5.062 21.913 24.506 1.00 8.68 ? 257 TRP A NE1 1 ATOM 1995 C CE2 . TRP A 1 257 ? 5.948 21.089 25.169 1.00 8.66 ? 257 TRP A CE2 1 ATOM 1996 C CE3 . TRP A 1 257 ? 6.081 19.906 27.277 1.00 7.37 ? 257 TRP A CE3 1 ATOM 1997 C CZ2 . TRP A 1 257 ? 7.203 20.593 24.773 1.00 7.57 ? 257 TRP A CZ2 1 ATOM 1998 C CZ3 . TRP A 1 257 ? 7.325 19.447 26.875 1.00 6.42 ? 257 TRP A CZ3 1 ATOM 1999 C CH2 . TRP A 1 257 ? 7.875 19.786 25.635 1.00 8.40 ? 257 TRP A CH2 1 ATOM 2000 N N . ILE A 1 258 ? 2.258 24.300 28.417 1.00 7.86 ? 258 ILE A N 1 ATOM 2001 C CA . ILE A 1 258 ? 2.168 25.745 28.189 1.00 8.15 ? 258 ILE A CA 1 ATOM 2002 C C . ILE A 1 258 ? 2.738 26.507 29.405 1.00 9.36 ? 258 ILE A C 1 ATOM 2003 O O . ILE A 1 258 ? 3.570 27.434 29.272 1.00 7.82 ? 258 ILE A O 1 ATOM 2004 C CB . ILE A 1 258 ? 0.723 26.175 27.869 1.00 8.93 ? 258 ILE A CB 1 ATOM 2005 C CG1 . ILE A 1 258 ? 0.173 25.611 26.554 1.00 10.12 ? 258 ILE A CG1 1 ATOM 2006 C CG2 . ILE A 1 258 ? 0.670 27.716 27.827 1.00 8.36 ? 258 ILE A CG2 1 ATOM 2007 C CD1 . ILE A 1 258 ? -1.342 25.647 26.365 1.00 11.79 ? 258 ILE A CD1 1 ATOM 2008 N N . GLN A 1 259 ? 2.327 26.150 30.626 1.00 9.55 ? 259 GLN A N 1 ATOM 2009 C CA . GLN A 1 259 ? 2.743 26.833 31.842 1.00 10.81 ? 259 GLN A CA 1 ATOM 2010 C C . GLN A 1 259 ? 4.247 26.756 32.111 1.00 9.29 ? 259 GLN A C 1 ATOM 2011 O O . GLN A 1 259 ? 4.862 27.793 32.421 1.00 7.43 ? 259 GLN A O 1 ATOM 2012 C CB . GLN A 1 259 ? 1.931 26.328 33.048 1.00 13.23 ? 259 GLN A CB 1 ATOM 2013 C CG . GLN A 1 259 ? 0.445 26.654 32.992 1.00 15.78 ? 259 GLN A CG 1 ATOM 2014 C CD . GLN A 1 259 ? -0.397 25.975 34.047 1.00 19.89 ? 259 GLN A CD 1 ATOM 2015 O OE1 . GLN A 1 259 ? -0.130 24.842 34.457 1.00 21.03 ? 259 GLN A OE1 1 ATOM 2016 N NE2 . GLN A 1 259 ? -1.452 26.625 34.530 1.00 21.50 ? 259 GLN A NE2 1 ATOM 2017 N N . THR A 1 260 ? 4.865 25.587 31.964 1.00 7.62 ? 260 THR A N 1 ATOM 2018 C CA . THR A 1 260 ? 6.307 25.473 32.186 1.00 7.79 ? 260 THR A CA 1 ATOM 2019 C C . THR A 1 260 ? 7.119 26.269 31.175 1.00 7.19 ? 260 THR A C 1 ATOM 2020 O O . THR A 1 260 ? 8.158 26.894 31.516 1.00 6.87 ? 260 THR A O 1 ATOM 2021 C CB . THR A 1 260 ? 6.773 24.004 32.228 1.00 8.22 ? 260 THR A CB 1 ATOM 2022 O OG1 . THR A 1 260 ? 6.366 23.337 31.013 1.00 7.81 ? 260 THR A OG1 1 ATOM 2023 C CG2 . THR A 1 260 ? 6.180 23.258 33.417 1.00 9.24 ? 260 THR A CG2 1 ATOM 2024 N N . HIS A 1 261 ? 6.733 26.267 29.890 1.00 6.67 ? 261 HIS A N 1 ATOM 2025 C CA . HIS A 1 261 ? 7.456 27.026 28.869 1.00 7.31 ? 261 HIS A CA 1 ATOM 2026 C C . HIS A 1 261 ? 7.358 28.537 29.069 1.00 7.61 ? 261 HIS A C 1 ATOM 2027 O O . HIS A 1 261 ? 8.356 29.291 28.988 1.00 7.15 ? 261 HIS A O 1 ATOM 2028 C CB . HIS A 1 261 ? 7.031 26.552 27.450 1.00 6.40 ? 261 HIS A CB 1 ATOM 2029 C CG . HIS A 1 261 ? 7.637 25.206 27.110 1.00 5.35 ? 261 HIS A CG 1 ATOM 2030 N ND1 . HIS A 1 261 ? 7.084 24.003 27.490 1.00 6.70 ? 261 HIS A ND1 1 ATOM 2031 C CD2 . HIS A 1 261 ? 8.763 24.901 26.426 1.00 5.70 ? 261 HIS A CD2 1 ATOM 2032 C CE1 . HIS A 1 261 ? 7.860 23.014 27.085 1.00 6.18 ? 261 HIS A CE1 1 ATOM 2033 N NE2 . HIS A 1 261 ? 8.904 23.523 26.401 1.00 4.80 ? 261 HIS A NE2 1 ATOM 2034 N N . ALA A 1 262 ? 6.181 29.058 29.394 1.00 7.50 ? 262 ALA A N 1 ATOM 2035 C CA . ALA A 1 262 ? 5.936 30.448 29.701 1.00 7.71 ? 262 ALA A CA 1 ATOM 2036 C C . ALA A 1 262 ? 6.838 30.928 30.857 1.00 8.02 ? 262 ALA A C 1 ATOM 2037 O O . ALA A 1 262 ? 7.476 31.971 30.700 1.00 7.08 ? 262 ALA A O 1 ATOM 2038 C CB . ALA A 1 262 ? 4.480 30.702 30.106 1.00 6.77 ? 262 ALA A CB 1 ATOM 2039 N N . ALA A 1 263 ? 6.993 30.111 31.913 1.00 7.38 ? 263 ALA A N 1 ATOM 2040 C CA . ALA A 1 263 ? 7.864 30.487 33.030 1.00 8.47 ? 263 ALA A CA 1 ATOM 2041 C C . ALA A 1 263 ? 9.349 30.532 32.653 1.00 9.61 ? 263 ALA A C 1 ATOM 2042 O O . ALA A 1 263 ? 10.105 31.410 33.134 1.00 7.92 ? 263 ALA A O 1 ATOM 2043 C CB . ALA A 1 263 ? 7.631 29.508 34.189 1.00 8.21 ? 263 ALA A CB 1 ATOM 2044 N N . ALA A 1 264 ? 9.795 29.619 31.797 1.00 8.87 ? 264 ALA A N 1 ATOM 2045 C CA . ALA A 1 264 ? 11.179 29.602 31.307 1.00 8.64 ? 264 ALA A CA 1 ATOM 2046 C C . ALA A 1 264 ? 11.458 30.787 30.404 1.00 9.21 ? 264 ALA A C 1 ATOM 2047 O O . ALA A 1 264 ? 12.530 31.409 30.539 1.00 8.22 ? 264 ALA A O 1 ATOM 2048 C CB . ALA A 1 264 ? 11.480 28.274 30.629 1.00 8.72 ? 264 ALA A CB 1 ATOM 2049 N N . CYS A 1 265 ? 10.508 31.200 29.552 1.00 8.40 ? 265 CYS A N 1 ATOM 2050 C CA . CYS A 1 265 ? 10.671 32.407 28.757 1.00 8.14 ? 265 CYS A CA 1 ATOM 2051 C C . CYS A 1 265 ? 10.822 33.631 29.677 1.00 8.42 ? 265 CYS A C 1 ATOM 2052 O O . CYS A 1 265 ? 11.765 34.424 29.533 1.00 7.63 ? 265 CYS A O 1 ATOM 2053 C CB . CYS A 1 265 ? 9.482 32.607 27.782 1.00 7.93 ? 265 CYS A CB 1 ATOM 2054 S SG . CYS A 1 265 ? 9.662 31.660 26.238 1.00 7.25 ? 265 CYS A SG 1 ATOM 2055 N N . LEU A 1 266 ? 9.930 33.807 30.655 1.00 7.84 ? 266 LEU A N 1 ATOM 2056 C CA . LEU A 1 266 ? 9.980 34.940 31.583 1.00 9.24 ? 266 LEU A CA 1 ATOM 2057 C C . LEU A 1 266 ? 11.234 34.952 32.450 1.00 9.99 ? 266 LEU A C 1 ATOM 2058 O O . LEU A 1 266 ? 11.823 36.021 32.690 1.00 8.96 ? 266 LEU A O 1 ATOM 2059 C CB . LEU A 1 266 ? 8.702 34.963 32.440 1.00 10.94 ? 266 LEU A CB 1 ATOM 2060 C CG . LEU A 1 266 ? 8.410 36.122 33.395 1.00 13.89 ? 266 LEU A CG 1 ATOM 2061 C CD1 . LEU A 1 266 ? 8.405 37.472 32.691 1.00 14.72 ? 266 LEU A CD1 1 ATOM 2062 C CD2 . LEU A 1 266 ? 7.066 35.890 34.097 1.00 15.17 ? 266 LEU A CD2 1 ATOM 2063 N N . ALA A 1 267 ? 11.748 33.794 32.875 1.00 9.67 ? 267 ALA A N 1 ATOM 2064 C CA . ALA A 1 267 ? 13.026 33.738 33.595 1.00 9.60 ? 267 ALA A CA 1 ATOM 2065 C C . ALA A 1 267 ? 14.228 34.191 32.773 1.00 10.47 ? 267 ALA A C 1 ATOM 2066 O O . ALA A 1 267 ? 15.239 34.652 33.326 1.00 11.23 ? 267 ALA A O 1 ATOM 2067 C CB . ALA A 1 267 ? 13.228 32.320 34.162 1.00 10.25 ? 267 ALA A CB 1 ATOM 2068 N N . ALA A 1 268 ? 14.186 34.131 31.446 1.00 8.54 ? 268 ALA A N 1 ATOM 2069 C CA . ALA A 1 268 ? 15.160 34.627 30.504 1.00 8.29 ? 268 ALA A CA 1 ATOM 2070 C C . ALA A 1 268 ? 14.895 36.076 30.062 1.00 8.65 ? 268 ALA A C 1 ATOM 2071 O O . ALA A 1 268 ? 15.678 36.597 29.248 1.00 9.19 ? 268 ALA A O 1 ATOM 2072 C CB . ALA A 1 268 ? 15.240 33.697 29.293 1.00 8.80 ? 268 ALA A CB 1 ATOM 2073 N N . GLY A 1 269 ? 13.823 36.703 30.551 1.00 6.41 ? 269 GLY A N 1 ATOM 2074 C CA . GLY A 1 269 ? 13.539 38.093 30.228 1.00 8.22 ? 269 GLY A CA 1 ATOM 2075 C C . GLY A 1 269 ? 12.786 38.344 28.935 1.00 7.96 ? 269 GLY A C 1 ATOM 2076 O O . GLY A 1 269 ? 12.785 39.490 28.494 1.00 7.07 ? 269 GLY A O 1 ATOM 2077 N N . LYS A 1 270 ? 12.152 37.328 28.347 1.00 7.53 ? 270 LYS A N 1 ATOM 2078 C CA . LYS A 1 270 ? 11.550 37.410 27.015 1.00 6.53 ? 270 LYS A CA 1 ATOM 2079 C C . LYS A 1 270 ? 10.140 36.810 26.932 1.00 8.18 ? 270 LYS A C 1 ATOM 2080 O O . LYS A 1 270 ? 9.765 36.022 27.806 1.00 7.14 ? 270 LYS A O 1 ATOM 2081 C CB . LYS A 1 270 ? 12.494 36.548 26.112 1.00 6.45 ? 270 LYS A CB 1 ATOM 2082 C CG . LYS A 1 270 ? 13.955 36.956 26.020 1.00 6.98 ? 270 LYS A CG 1 ATOM 2083 C CD . LYS A 1 270 ? 14.904 36.115 25.166 1.00 7.06 ? 270 LYS A CD 1 ATOM 2084 C CE . LYS A 1 270 ? 16.341 36.552 25.305 1.00 6.94 ? 270 LYS A CE 1 ATOM 2085 N NZ . LYS A 1 270 ? 17.363 35.791 24.548 1.00 8.01 ? 270 LYS A NZ 1 ATOM 2086 N N . PRO A 1 271 ? 9.333 37.116 25.908 1.00 8.51 ? 271 PRO A N 1 ATOM 2087 C CA . PRO A 1 271 ? 8.069 36.405 25.675 1.00 9.35 ? 271 PRO A CA 1 ATOM 2088 C C . PRO A 1 271 ? 8.240 35.050 24.985 1.00 9.42 ? 271 PRO A C 1 ATOM 2089 O O . PRO A 1 271 ? 9.268 34.761 24.375 1.00 8.65 ? 271 PRO A O 1 ATOM 2090 C CB . PRO A 1 271 ? 7.317 37.304 24.684 1.00 10.04 ? 271 PRO A CB 1 ATOM 2091 C CG . PRO A 1 271 ? 8.260 38.352 24.225 1.00 9.83 ? 271 PRO A CG 1 ATOM 2092 C CD . PRO A 1 271 ? 9.614 38.061 24.822 1.00 8.45 ? 271 PRO A CD 1 ATOM 2093 N N . CYS A 1 272 ? 7.234 34.189 25.028 1.00 8.33 ? 272 CYS A N 1 ATOM 2094 C CA . CYS A 1 272 ? 7.105 32.916 24.334 1.00 8.54 ? 272 CYS A CA 1 ATOM 2095 C C . CYS A 1 272 ? 5.944 33.053 23.310 1.00 9.39 ? 272 CYS A C 1 ATOM 2096 O O . CYS A 1 272 ? 4.952 33.777 23.527 1.00 7.27 ? 272 CYS A O 1 ATOM 2097 C CB . CYS A 1 272 ? 6.671 31.777 25.285 1.00 8.65 ? 272 CYS A CB 1 ATOM 2098 S SG . CYS A 1 272 ? 7.880 30.625 25.984 1.00 8.16 ? 272 CYS A SG 1 ATOM 2099 N N . VAL A 1 273 ? 6.013 32.312 22.201 1.00 8.50 ? 273 VAL A N 1 ATOM 2100 C CA . VAL A 1 273 ? 4.932 32.174 21.224 1.00 8.03 ? 273 VAL A CA 1 ATOM 2101 C C . VAL A 1 273 ? 4.569 30.683 21.122 1.00 8.96 ? 273 VAL A C 1 ATOM 2102 O O . VAL A 1 273 ? 5.469 29.891 20.816 1.00 8.90 ? 273 VAL A O 1 ATOM 2103 C CB . VAL A 1 273 ? 5.316 32.714 19.836 1.00 7.68 ? 273 VAL A CB 1 ATOM 2104 C CG1 . VAL A 1 273 ? 4.279 32.420 18.727 1.00 8.19 ? 273 VAL A CG1 1 ATOM 2105 C CG2 . VAL A 1 273 ? 5.614 34.199 19.858 1.00 6.12 ? 273 VAL A CG2 1 ATOM 2106 N N . PHE A 1 274 ? 3.310 30.311 21.341 1.00 7.67 ? 274 PHE A N 1 ATOM 2107 C CA . PHE A 1 274 ? 2.762 28.950 21.193 1.00 8.34 ? 274 PHE A CA 1 ATOM 2108 C C . PHE A 1 274 ? 2.438 28.784 19.698 1.00 8.67 ? 274 PHE A C 1 ATOM 2109 O O . PHE A 1 274 ? 1.331 29.062 19.223 1.00 7.66 ? 274 PHE A O 1 ATOM 2110 C CB . PHE A 1 274 ? 1.518 28.844 22.067 1.00 8.71 ? 274 PHE A CB 1 ATOM 2111 C CG . PHE A 1 274 ? 0.699 27.599 22.211 1.00 8.71 ? 274 PHE A CG 1 ATOM 2112 C CD1 . PHE A 1 274 ? 1.196 26.344 21.935 1.00 10.45 ? 274 PHE A CD1 1 ATOM 2113 C CD2 . PHE A 1 274 ? -0.610 27.657 22.696 1.00 9.91 ? 274 PHE A CD2 1 ATOM 2114 C CE1 . PHE A 1 274 ? 0.452 25.197 22.076 1.00 9.95 ? 274 PHE A CE1 1 ATOM 2115 C CE2 . PHE A 1 274 ? -1.390 26.517 22.839 1.00 10.19 ? 274 PHE A CE2 1 ATOM 2116 C CZ . PHE A 1 274 ? -0.845 25.290 22.529 1.00 9.66 ? 274 PHE A CZ 1 ATOM 2117 N N . GLU A 1 275 ? 3.430 28.383 18.915 1.00 8.18 ? 275 GLU A N 1 ATOM 2118 C CA . GLU A 1 275 ? 3.486 28.495 17.467 1.00 9.85 ? 275 GLU A CA 1 ATOM 2119 C C . GLU A 1 275 ? 2.835 27.469 16.565 1.00 9.15 ? 275 GLU A C 1 ATOM 2120 O O . GLU A 1 275 ? 2.522 27.849 15.407 1.00 7.52 ? 275 GLU A O 1 ATOM 2121 C CB . GLU A 1 275 ? 5.008 28.632 17.158 1.00 12.06 ? 275 GLU A CB 1 ATOM 2122 C CG . GLU A 1 275 ? 5.499 28.378 15.778 1.00 12.43 ? 275 GLU A CG 1 ATOM 2123 C CD . GLU A 1 275 ? 6.955 28.662 15.473 1.00 9.65 ? 275 GLU A CD 1 ATOM 2124 O OE1 . GLU A 1 275 ? 7.182 29.828 15.080 1.00 8.89 ? 275 GLU A OE1 1 ATOM 2125 O OE2 . GLU A 1 275 ? 7.783 27.743 15.579 1.00 8.02 ? 275 GLU A OE2 1 ATOM 2126 N N . GLU A 1 276 ? 2.609 26.247 17.007 1.00 7.95 ? 276 GLU A N 1 ATOM 2127 C CA . GLU A 1 276 ? 1.984 25.183 16.213 1.00 9.04 ? 276 GLU A CA 1 ATOM 2128 C C . GLU A 1 276 ? 1.337 24.149 17.116 1.00 10.07 ? 276 GLU A C 1 ATOM 2129 O O . GLU A 1 276 ? 2.091 23.677 17.996 1.00 12.10 ? 276 GLU A O 1 ATOM 2130 C CB . GLU A 1 276 ? 3.068 24.548 15.331 1.00 10.56 ? 276 GLU A CB 1 ATOM 2131 C CG . GLU A 1 276 ? 2.773 23.444 14.392 1.00 12.10 ? 276 GLU A CG 1 ATOM 2132 C CD . GLU A 1 276 ? 3.840 22.984 13.442 1.00 11.70 ? 276 GLU A CD 1 ATOM 2133 O OE1 . GLU A 1 276 ? 4.851 23.623 12.990 1.00 8.64 ? 276 GLU A OE1 1 ATOM 2134 O OE2 . GLU A 1 276 ? 3.638 21.806 13.068 1.00 14.54 ? 276 GLU A OE2 1 ATOM 2135 N N . TYR A 1 277 ? 0.040 23.846 17.011 1.00 8.52 ? 277 TYR A N 1 ATOM 2136 C CA . TYR A 1 277 ? -0.601 22.857 17.873 1.00 9.11 ? 277 TYR A CA 1 ATOM 2137 C C . TYR A 1 277 ? -1.799 22.189 17.159 1.00 9.86 ? 277 TYR A C 1 ATOM 2138 O O . TYR A 1 277 ? -2.424 22.847 16.329 1.00 8.41 ? 277 TYR A O 1 ATOM 2139 C CB . TYR A 1 277 ? -1.097 23.471 19.179 1.00 9.60 ? 277 TYR A CB 1 ATOM 2140 C CG . TYR A 1 277 ? -1.992 24.700 19.143 1.00 10.92 ? 277 TYR A CG 1 ATOM 2141 C CD1 . TYR A 1 277 ? -1.490 25.987 19.140 1.00 9.92 ? 277 TYR A CD1 1 ATOM 2142 C CD2 . TYR A 1 277 ? -3.376 24.562 19.125 1.00 9.58 ? 277 TYR A CD2 1 ATOM 2143 C CE1 . TYR A 1 277 ? -2.300 27.103 19.126 1.00 10.90 ? 277 TYR A CE1 1 ATOM 2144 C CE2 . TYR A 1 277 ? -4.220 25.667 19.099 1.00 10.98 ? 277 TYR A CE2 1 ATOM 2145 C CZ . TYR A 1 277 ? -3.680 26.935 19.088 1.00 10.23 ? 277 TYR A CZ 1 ATOM 2146 O OH . TYR A 1 277 ? -4.519 28.030 19.071 1.00 8.99 ? 277 TYR A OH 1 ATOM 2147 N N . GLY A 1 278 ? -2.099 20.934 17.517 1.00 7.82 ? 278 GLY A N 1 ATOM 2148 C CA . GLY A 1 278 ? -3.273 20.231 16.998 1.00 9.20 ? 278 GLY A CA 1 ATOM 2149 C C . GLY A 1 278 ? -3.620 18.950 17.768 1.00 10.85 ? 278 GLY A C 1 ATOM 2150 O O . GLY A 1 278 ? -2.772 18.341 18.390 1.00 9.99 ? 278 GLY A O 1 ATOM 2151 N N . ALA A 1 279 ? -4.885 18.537 17.725 1.00 10.78 ? 279 ALA A N 1 ATOM 2152 C CA . ALA A 1 279 ? -5.365 17.258 18.264 1.00 12.77 ? 279 ALA A CA 1 ATOM 2153 C C . ALA A 1 279 ? -6.074 16.463 17.156 1.00 14.25 ? 279 ALA A C 1 ATOM 2154 O O . ALA A 1 279 ? -6.797 17.041 16.341 1.00 13.19 ? 279 ALA A O 1 ATOM 2155 C CB . ALA A 1 279 ? -6.364 17.512 19.376 1.00 12.64 ? 279 ALA A CB 1 ATOM 2156 N N . GLN A 1 280 ? -5.850 15.173 17.039 1.00 18.17 ? 280 GLN A N 1 ATOM 2157 C CA . GLN A 1 280 ? -6.357 14.361 15.927 1.00 21.47 ? 280 GLN A CA 1 ATOM 2158 C C . GLN A 1 280 ? -7.845 14.038 16.060 1.00 22.90 ? 280 GLN A C 1 ATOM 2159 O O . GLN A 1 280 ? -8.580 13.862 15.058 1.00 23.64 ? 280 GLN A O 1 ATOM 2160 C CB . GLN A 1 280 ? -5.486 13.099 15.743 1.00 23.46 ? 280 GLN A CB 1 ATOM 2161 C CG . GLN A 1 280 ? -4.100 13.274 15.183 1.00 23.99 ? 280 GLN A CG 1 ATOM 2162 C CD . GLN A 1 280 ? -3.238 12.053 14.945 1.00 25.18 ? 280 GLN A CD 1 ATOM 2163 O OE1 . GLN A 1 280 ? -3.692 10.985 14.539 1.00 26.13 ? 280 GLN A OE1 1 ATOM 2164 N NE2 . GLN A 1 280 ? -1.928 12.096 15.157 1.00 23.90 ? 280 GLN A NE2 1 ATOM 2165 N N . GLN A 1 281 ? -8.309 13.948 17.299 1.00 21.80 ? 281 GLN A N 1 ATOM 2166 C CA . GLN A 1 281 ? -9.692 13.680 17.654 1.00 23.02 ? 281 GLN A CA 1 ATOM 2167 C C . GLN A 1 281 ? -10.344 14.869 18.355 1.00 19.95 ? 281 GLN A C 1 ATOM 2168 O O . GLN A 1 281 ? -9.694 15.543 19.149 1.00 17.46 ? 281 GLN A O 1 ATOM 2169 C CB . GLN A 1 281 ? -9.799 12.476 18.613 1.00 26.93 ? 281 GLN A CB 1 ATOM 2170 C CG . GLN A 1 281 ? -9.717 11.119 17.958 1.00 32.84 ? 281 GLN A CG 1 ATOM 2171 C CD . GLN A 1 281 ? -8.369 10.645 17.502 1.00 37.11 ? 281 GLN A CD 1 ATOM 2172 O OE1 . GLN A 1 281 ? -7.395 10.506 18.259 1.00 39.76 ? 281 GLN A OE1 1 ATOM 2173 N NE2 . GLN A 1 281 ? -8.266 10.349 16.207 1.00 38.17 ? 281 GLN A NE2 1 ATOM 2174 N N . ASN A 1 282 ? -11.620 15.133 18.070 1.00 18.42 ? 282 ASN A N 1 ATOM 2175 C CA . ASN A 1 282 ? -12.409 16.182 18.686 1.00 17.22 ? 282 ASN A CA 1 ATOM 2176 C C . ASN A 1 282 ? -11.696 17.499 18.962 1.00 15.22 ? 282 ASN A C 1 ATOM 2177 O O . ASN A 1 282 ? -11.536 17.946 20.114 1.00 14.20 ? 282 ASN A O 1 ATOM 2178 C CB . ASN A 1 282 ? -13.027 15.616 19.973 1.00 18.48 ? 282 ASN A CB 1 ATOM 2179 C CG . ASN A 1 282 ? -13.865 14.368 19.807 1.00 20.93 ? 282 ASN A CG 1 ATOM 2180 O OD1 . ASN A 1 282 ? -13.499 13.336 20.396 1.00 22.02 ? 282 ASN A OD1 1 ATOM 2181 N ND2 . ASN A 1 282 ? -14.920 14.345 19.002 1.00 20.04 ? 282 ASN A ND2 1 ATOM 2182 N N . PRO A 1 283 ? -11.277 18.225 17.923 1.00 13.56 ? 283 PRO A N 1 ATOM 2183 C CA . PRO A 1 283 ? -10.502 19.452 18.094 1.00 13.41 ? 283 PRO A CA 1 ATOM 2184 C C . PRO A 1 283 ? -11.149 20.582 18.847 1.00 13.78 ? 283 PRO A C 1 ATOM 2185 O O . PRO A 1 283 ? -10.429 21.283 19.605 1.00 11.92 ? 283 PRO A O 1 ATOM 2186 C CB . PRO A 1 283 ? -10.063 19.840 16.678 1.00 14.26 ? 283 PRO A CB 1 ATOM 2187 C CG . PRO A 1 283 ? -11.040 19.158 15.781 1.00 14.15 ? 283 PRO A CG 1 ATOM 2188 C CD . PRO A 1 283 ? -11.435 17.877 16.498 1.00 13.32 ? 283 PRO A CD 1 ATOM 2189 N N . CYS A 1 284 ? -12.438 20.880 18.621 1.00 13.77 ? 284 CYS A N 1 ATOM 2190 C CA . CYS A 1 284 ? -13.081 21.944 19.404 1.00 14.39 ? 284 CYS A CA 1 ATOM 2191 C C . CYS A 1 284 ? -13.054 21.653 20.900 1.00 14.17 ? 284 CYS A C 1 ATOM 2192 O O . CYS A 1 284 ? -12.700 22.491 21.741 1.00 13.47 ? 284 CYS A O 1 ATOM 2193 C CB . CYS A 1 284 ? -14.493 22.216 18.842 1.00 13.15 ? 284 CYS A CB 1 ATOM 2194 S SG . CYS A 1 284 ? -15.531 23.293 19.846 1.00 11.95 ? 284 CYS A SG 1 ATOM 2195 N N . THR A 1 285 ? -13.410 20.455 21.343 1.00 14.49 ? 285 THR A N 1 ATOM 2196 C CA . THR A 1 285 ? -13.386 20.066 22.755 1.00 16.19 ? 285 THR A CA 1 ATOM 2197 C C . THR A 1 285 ? -11.988 20.132 23.363 1.00 15.51 ? 285 THR A C 1 ATOM 2198 O O . THR A 1 285 ? -11.778 20.672 24.458 1.00 15.94 ? 285 THR A O 1 ATOM 2199 C CB . THR A 1 285 ? -13.921 18.620 22.897 1.00 18.22 ? 285 THR A CB 1 ATOM 2200 O OG1 . THR A 1 285 ? -15.318 18.574 22.525 1.00 19.73 ? 285 THR A OG1 1 ATOM 2201 C CG2 . THR A 1 285 ? -13.801 18.077 24.317 1.00 19.20 ? 285 THR A CG2 1 ATOM 2202 N N . ASN A 1 286 ? -10.997 19.559 22.690 1.00 14.29 ? 286 ASN A N 1 ATOM 2203 C CA . ASN A 1 286 ? -9.644 19.420 23.190 1.00 13.45 ? 286 ASN A CA 1 ATOM 2204 C C . ASN A 1 286 ? -8.711 20.621 23.018 1.00 13.44 ? 286 ASN A C 1 ATOM 2205 O O . ASN A 1 286 ? -7.904 20.816 23.947 1.00 12.88 ? 286 ASN A O 1 ATOM 2206 C CB . ASN A 1 286 ? -9.019 18.139 22.607 1.00 14.63 ? 286 ASN A CB 1 ATOM 2207 C CG . ASN A 1 286 ? -9.765 16.887 23.049 1.00 16.76 ? 286 ASN A CG 1 ATOM 2208 O OD1 . ASN A 1 286 ? -10.167 16.749 24.214 1.00 18.07 ? 286 ASN A OD1 1 ATOM 2209 N ND2 . ASN A 1 286 ? -9.908 15.947 22.123 1.00 17.43 ? 286 ASN A ND2 1 ATOM 2210 N N . GLU A 1 287 ? -8.876 21.435 21.969 1.00 10.10 ? 287 GLU A N 1 ATOM 2211 C CA . GLU A 1 287 ? -7.993 22.600 21.813 1.00 10.15 ? 287 GLU A CA 1 ATOM 2212 C C . GLU A 1 287 ? -8.415 23.911 22.450 1.00 10.50 ? 287 GLU A C 1 ATOM 2213 O O . GLU A 1 287 ? -7.595 24.787 22.825 1.00 9.83 ? 287 GLU A O 1 ATOM 2214 C CB . GLU A 1 287 ? -7.741 22.815 20.304 1.00 9.86 ? 287 GLU A CB 1 ATOM 2215 C CG . GLU A 1 287 ? -7.068 21.645 19.613 1.00 10.47 ? 287 GLU A CG 1 ATOM 2216 C CD . GLU A 1 287 ? -6.742 21.848 18.147 1.00 11.63 ? 287 GLU A CD 1 ATOM 2217 O OE1 . GLU A 1 287 ? -6.425 22.967 17.674 1.00 11.64 ? 287 GLU A OE1 1 ATOM 2218 O OE2 . GLU A 1 287 ? -6.796 20.844 17.393 1.00 12.43 ? 287 GLU A OE2 1 ATOM 2219 N N . ALA A 1 288 ? -9.724 24.129 22.615 1.00 10.29 ? 288 ALA A N 1 ATOM 2220 C CA . ALA A 1 288 ? -10.241 25.321 23.268 1.00 11.58 ? 288 ALA A CA 1 ATOM 2221 C C . ALA A 1 288 ? -9.674 25.587 24.646 1.00 11.29 ? 288 ALA A C 1 ATOM 2222 O O . ALA A 1 288 ? -9.295 26.750 24.896 1.00 11.73 ? 288 ALA A O 1 ATOM 2223 C CB . ALA A 1 288 ? -11.769 25.355 23.219 1.00 12.19 ? 288 ALA A CB 1 ATOM 2224 N N . PRO A 1 289 ? -9.521 24.639 25.542 1.00 11.97 ? 289 PRO A N 1 ATOM 2225 C CA . PRO A 1 289 ? -8.903 24.887 26.854 1.00 13.07 ? 289 PRO A CA 1 ATOM 2226 C C . PRO A 1 289 ? -7.444 25.342 26.767 1.00 12.83 ? 289 PRO A C 1 ATOM 2227 O O . PRO A 1 289 ? -6.989 26.204 27.570 1.00 11.42 ? 289 PRO A O 1 ATOM 2228 C CB . PRO A 1 289 ? -9.102 23.600 27.629 1.00 13.53 ? 289 PRO A CB 1 ATOM 2229 C CG . PRO A 1 289 ? -10.150 22.840 26.904 1.00 13.29 ? 289 PRO A CG 1 ATOM 2230 C CD . PRO A 1 289 ? -10.057 23.262 25.448 1.00 12.98 ? 289 PRO A CD 1 ATOM 2231 N N . TRP A 1 290 ? -6.694 24.867 25.763 1.00 10.62 ? 290 TRP A N 1 ATOM 2232 C CA . TRP A 1 290 ? -5.300 25.290 25.547 1.00 10.43 ? 290 TRP A CA 1 ATOM 2233 C C . TRP A 1 290 ? -5.199 26.791 25.227 1.00 9.73 ? 290 TRP A C 1 ATOM 2234 O O . TRP A 1 290 ? -4.307 27.515 25.687 1.00 8.47 ? 290 TRP A O 1 ATOM 2235 C CB . TRP A 1 290 ? -4.563 24.499 24.473 1.00 8.25 ? 290 TRP A CB 1 ATOM 2236 C CG . TRP A 1 290 ? -4.510 22.998 24.574 1.00 8.16 ? 290 TRP A CG 1 ATOM 2237 C CD1 . TRP A 1 290 ? -4.688 22.259 25.719 1.00 7.71 ? 290 TRP A CD1 1 ATOM 2238 C CD2 . TRP A 1 290 ? -4.240 22.060 23.537 1.00 8.86 ? 290 TRP A CD2 1 ATOM 2239 N NE1 . TRP A 1 290 ? -4.556 20.930 25.449 1.00 7.55 ? 290 TRP A NE1 1 ATOM 2240 C CE2 . TRP A 1 290 ? -4.281 20.763 24.116 1.00 8.53 ? 290 TRP A CE2 1 ATOM 2241 C CE3 . TRP A 1 290 ? -3.962 22.168 22.179 1.00 9.35 ? 290 TRP A CE3 1 ATOM 2242 C CZ2 . TRP A 1 290 ? -4.066 19.600 23.394 1.00 9.24 ? 290 TRP A CZ2 1 ATOM 2243 C CZ3 . TRP A 1 290 ? -3.755 20.995 21.430 1.00 9.19 ? 290 TRP A CZ3 1 ATOM 2244 C CH2 . TRP A 1 290 ? -3.801 19.744 22.046 1.00 8.73 ? 290 TRP A CH2 1 ATOM 2245 N N . GLN A 1 291 ? -6.101 27.274 24.369 1.00 9.22 ? 291 GLN A N 1 ATOM 2246 C CA . GLN A 1 291 ? -6.232 28.658 23.967 1.00 10.65 ? 291 GLN A CA 1 ATOM 2247 C C . GLN A 1 291 ? -6.474 29.568 25.175 1.00 12.21 ? 291 GLN A C 1 ATOM 2248 O O . GLN A 1 291 ? -5.781 30.598 25.346 1.00 11.63 ? 291 GLN A O 1 ATOM 2249 C CB . GLN A 1 291 ? -7.292 28.822 22.846 1.00 10.35 ? 291 GLN A CB 1 ATOM 2250 C CG . GLN A 1 291 ? -6.958 28.113 21.541 1.00 11.14 ? 291 GLN A CG 1 ATOM 2251 C CD . GLN A 1 291 ? -7.954 28.348 20.425 1.00 11.51 ? 291 GLN A CD 1 ATOM 2252 O OE1 . GLN A 1 291 ? -9.158 28.461 20.741 1.00 11.45 ? 291 GLN A OE1 1 ATOM 2253 N NE2 . GLN A 1 291 ? -7.533 28.432 19.178 1.00 10.10 ? 291 GLN A NE2 1 ATOM 2254 N N . THR A 1 292 ? -7.338 29.184 26.103 1.00 12.90 ? 292 THR A N 1 ATOM 2255 C CA . THR A 1 292 ? -7.611 29.940 27.330 1.00 13.33 ? 292 THR A CA 1 ATOM 2256 C C . THR A 1 292 ? -6.408 29.943 28.274 1.00 13.05 ? 292 THR A C 1 ATOM 2257 O O . THR A 1 292 ? -6.019 30.981 28.834 1.00 11.52 ? 292 THR A O 1 ATOM 2258 C CB . THR A 1 292 ? -8.826 29.334 28.042 1.00 14.38 ? 292 THR A CB 1 ATOM 2259 O OG1 . THR A 1 292 ? -10.003 29.419 27.210 1.00 14.30 ? 292 THR A OG1 1 ATOM 2260 C CG2 . THR A 1 292 ? -9.067 30.003 29.393 1.00 12.61 ? 292 THR A CG2 1 ATOM 2261 N N . THR A 1 293 ? -5.737 28.819 28.451 1.00 13.45 ? 293 THR A N 1 ATOM 2262 C CA . THR A 1 293 ? -4.518 28.751 29.275 1.00 12.75 ? 293 THR A CA 1 ATOM 2263 C C . THR A 1 293 ? -3.462 29.718 28.758 1.00 12.18 ? 293 THR A C 1 ATOM 2264 O O . THR A 1 293 ? -2.892 30.497 29.541 1.00 12.50 ? 293 THR A O 1 ATOM 2265 C CB . THR A 1 293 ? -3.981 27.314 29.393 1.00 12.92 ? 293 THR A CB 1 ATOM 2266 O OG1 . THR A 1 293 ? -4.956 26.487 30.092 1.00 11.92 ? 293 THR A OG1 1 ATOM 2267 C CG2 . THR A 1 293 ? -2.688 27.169 30.174 1.00 11.80 ? 293 THR A CG2 1 ATOM 2268 N N . SER A 1 294 ? -3.176 29.721 27.450 1.00 10.24 ? 294 SER A N 1 ATOM 2269 C CA . SER A 1 294 ? -2.172 30.661 26.896 1.00 9.50 ? 294 SER A CA 1 ATOM 2270 C C . SER A 1 294 ? -2.536 32.124 27.093 1.00 10.39 ? 294 SER A C 1 ATOM 2271 O O . SER A 1 294 ? -1.710 32.934 27.537 1.00 9.07 ? 294 SER A O 1 ATOM 2272 C CB . SER A 1 294 ? -1.961 30.316 25.421 1.00 9.16 ? 294 SER A CB 1 ATOM 2273 O OG . SER A 1 294 ? -0.885 30.983 24.787 1.00 9.03 ? 294 SER A OG 1 ATOM 2274 N N . LEU A 1 295 ? -3.816 32.498 26.847 1.00 9.08 ? 295 LEU A N 1 ATOM 2275 C CA . LEU A 1 295 ? -4.261 33.870 27.033 1.00 11.39 ? 295 LEU A CA 1 ATOM 2276 C C . LEU A 1 295 ? -4.058 34.341 28.466 1.00 12.47 ? 295 LEU A C 1 ATOM 2277 O O . LEU A 1 295 ? -3.728 35.511 28.674 1.00 13.00 ? 295 LEU A O 1 ATOM 2278 C CB . LEU A 1 295 ? -5.751 33.997 26.635 1.00 12.09 ? 295 LEU A CB 1 ATOM 2279 C CG . LEU A 1 295 ? -6.460 35.325 26.820 1.00 14.13 ? 295 LEU A CG 1 ATOM 2280 C CD1 . LEU A 1 295 ? -5.753 36.440 26.057 1.00 14.67 ? 295 LEU A CD1 1 ATOM 2281 C CD2 . LEU A 1 295 ? -7.931 35.255 26.406 1.00 15.47 ? 295 LEU A CD2 1 ATOM 2282 N N . THR A 1 296 ? -4.282 33.463 29.453 1.00 13.08 ? 296 THR A N 1 ATOM 2283 C CA . THR A 1 296 ? -4.223 33.873 30.854 1.00 14.53 ? 296 THR A CA 1 ATOM 2284 C C . THR A 1 296 ? -2.958 33.495 31.625 1.00 15.66 ? 296 THR A C 1 ATOM 2285 O O . THR A 1 296 ? -3.023 33.567 32.873 1.00 15.88 ? 296 THR A O 1 ATOM 2286 C CB . THR A 1 296 ? -5.434 33.290 31.619 1.00 16.49 ? 296 THR A CB 1 ATOM 2287 O OG1 . THR A 1 296 ? -5.410 31.871 31.578 1.00 17.22 ? 296 THR A OG1 1 ATOM 2288 C CG2 . THR A 1 296 ? -6.768 33.742 31.041 1.00 15.85 ? 296 THR A CG2 1 ATOM 2289 N N . THR A 1 297 ? -1.858 33.150 30.971 1.00 13.74 ? 297 THR A N 1 ATOM 2290 C CA . THR A 1 297 ? -0.591 32.821 31.618 1.00 12.68 ? 297 THR A CA 1 ATOM 2291 C C . THR A 1 297 ? 0.473 33.897 31.379 1.00 12.94 ? 297 THR A C 1 ATOM 2292 O O . THR A 1 297 ? 0.803 34.260 30.236 1.00 12.70 ? 297 THR A O 1 ATOM 2293 C CB . THR A 1 297 ? -0.040 31.448 31.190 1.00 11.62 ? 297 THR A CB 1 ATOM 2294 O OG1 . THR A 1 297 ? -0.989 30.414 31.520 1.00 11.24 ? 297 THR A OG1 1 ATOM 2295 C CG2 . THR A 1 297 ? 1.300 31.093 31.857 1.00 10.68 ? 297 THR A CG2 1 ATOM 2296 N N . ARG A 1 298 ? 1.094 34.394 32.477 1.00 12.09 ? 298 ARG A N 1 ATOM 2297 C CA . ARG A 1 298 ? 2.137 35.415 32.336 1.00 13.71 ? 298 ARG A CA 1 ATOM 2298 C C . ARG A 1 298 ? 3.368 34.877 31.578 1.00 13.30 ? 298 ARG A C 1 ATOM 2299 O O . ARG A 1 298 ? 3.807 33.766 31.895 1.00 12.83 ? 298 ARG A O 1 ATOM 2300 C CB . ARG A 1 298 ? 2.577 35.971 33.704 1.00 16.95 ? 298 ARG A CB 1 ATOM 2301 C CG . ARG A 1 298 ? 1.493 36.616 34.547 1.00 22.19 ? 298 ARG A CG 1 ATOM 2302 C CD . ARG A 1 298 ? 0.829 37.845 33.979 1.00 28.38 ? 298 ARG A CD 1 ATOM 2303 N NE . ARG A 1 298 ? -0.276 37.573 33.085 1.00 32.78 ? 298 ARG A NE 1 ATOM 2304 C CZ . ARG A 1 298 ? -1.484 37.063 33.233 1.00 34.89 ? 298 ARG A CZ 1 ATOM 2305 N NH1 . ARG A 1 298 ? -1.977 36.639 34.392 1.00 36.34 ? 298 ARG A NH1 1 ATOM 2306 N NH2 . ARG A 1 298 ? -2.232 36.976 32.137 1.00 35.61 ? 298 ARG A NH2 1 ATOM 2307 N N . GLY A 1 299 ? 3.893 35.617 30.600 1.00 11.30 ? 299 GLY A N 1 ATOM 2308 C CA . GLY A 1 299 ? 5.058 35.131 29.826 1.00 12.91 ? 299 GLY A CA 1 ATOM 2309 C C . GLY A 1 299 ? 4.669 34.704 28.407 1.00 12.52 ? 299 GLY A C 1 ATOM 2310 O O . GLY A 1 299 ? 5.515 34.543 27.500 1.00 12.14 ? 299 GLY A O 1 ATOM 2311 N N . MET A 1 300 ? 3.375 34.507 28.170 1.00 11.46 ? 300 MET A N 1 ATOM 2312 C CA . MET A 1 300 ? 2.867 34.154 26.846 1.00 11.11 ? 300 MET A CA 1 ATOM 2313 C C . MET A 1 300 ? 2.453 35.388 26.037 1.00 12.79 ? 300 MET A C 1 ATOM 2314 O O . MET A 1 300 ? 1.526 36.105 26.436 1.00 14.42 ? 300 MET A O 1 ATOM 2315 C CB . MET A 1 300 ? 1.652 33.227 26.946 1.00 9.39 ? 300 MET A CB 1 ATOM 2316 C CG . MET A 1 300 ? 1.911 31.807 27.410 1.00 8.23 ? 300 MET A CG 1 ATOM 2317 S SD . MET A 1 300 ? 3.252 30.855 26.608 1.00 7.83 ? 300 MET A SD 1 ATOM 2318 C CE . MET A 1 300 ? 2.827 31.207 24.874 1.00 8.58 ? 300 MET A CE 1 ATOM 2319 N N . GLY A 1 301 ? 3.033 35.596 24.855 1.00 10.62 ? 301 GLY A N 1 ATOM 2320 C CA . GLY A 1 301 ? 2.692 36.738 24.018 1.00 10.69 ? 301 GLY A CA 1 ATOM 2321 C C . GLY A 1 301 ? 1.733 36.500 22.869 1.00 9.46 ? 301 GLY A C 1 ATOM 2322 O O . GLY A 1 301 ? 1.156 37.477 22.371 1.00 10.29 ? 301 GLY A O 1 ATOM 2323 N N . GLY A 1 302 ? 1.533 35.262 22.472 1.00 8.24 ? 302 GLY A N 1 ATOM 2324 C CA . GLY A 1 302 ? 0.561 34.945 21.387 1.00 6.88 ? 302 GLY A CA 1 ATOM 2325 C C . GLY A 1 302 ? 0.498 33.444 21.123 1.00 8.54 ? 302 GLY A C 1 ATOM 2326 O O . GLY A 1 302 ? 1.368 32.725 21.607 1.00 7.61 ? 302 GLY A O 1 ATOM 2327 N N . ASP A 1 303 ? -0.459 33.021 20.286 1.00 8.11 ? 303 ASP A N 1 ATOM 2328 C CA . ASP A 1 303 ? -0.621 31.623 19.877 1.00 8.26 ? 303 ASP A CA 1 ATOM 2329 C C . ASP A 1 303 ? -1.108 31.483 18.435 1.00 9.09 ? 303 ASP A C 1 ATOM 2330 O O . ASP A 1 303 ? -1.781 32.368 17.909 1.00 8.06 ? 303 ASP A O 1 ATOM 2331 C CB . ASP A 1 303 ? -1.570 30.845 20.800 1.00 9.33 ? 303 ASP A CB 1 ATOM 2332 C CG . ASP A 1 303 ? -3.044 31.174 20.595 1.00 10.42 ? 303 ASP A CG 1 ATOM 2333 O OD1 . ASP A 1 303 ? -3.751 30.561 19.735 1.00 8.96 ? 303 ASP A OD1 1 ATOM 2334 O OD2 . ASP A 1 303 ? -3.516 32.078 21.305 1.00 9.10 ? 303 ASP A OD2 1 ATOM 2335 N N . MET A 1 304 ? -0.735 30.403 17.717 1.00 8.81 ? 304 MET A N 1 ATOM 2336 C CA . MET A 1 304 ? -1.131 30.150 16.319 1.00 9.19 ? 304 MET A CA 1 ATOM 2337 C C . MET A 1 304 ? -1.501 28.691 16.072 1.00 9.37 ? 304 MET A C 1 ATOM 2338 O O . MET A 1 304 ? -0.608 27.833 16.094 1.00 8.50 ? 304 MET A O 1 ATOM 2339 C CB . MET A 1 304 ? 0.064 30.496 15.382 1.00 10.47 ? 304 MET A CB 1 ATOM 2340 C CG . MET A 1 304 ? 0.525 31.919 15.611 1.00 12.17 ? 304 MET A CG 1 ATOM 2341 S SD . MET A 1 304 ? 2.177 32.418 15.202 1.00 14.64 ? 304 MET A SD 1 ATOM 2342 C CE . MET A 1 304 ? 1.811 32.563 13.438 1.00 16.25 ? 304 MET A CE 1 ATOM 2343 N N . PHE A 1 305 ? -2.771 28.312 15.858 1.00 8.52 ? 305 PHE A N 1 ATOM 2344 C CA . PHE A 1 305 ? -3.131 26.922 15.563 1.00 8.19 ? 305 PHE A CA 1 ATOM 2345 C C . PHE A 1 305 ? -2.643 26.357 14.224 1.00 7.72 ? 305 PHE A C 1 ATOM 2346 O O . PHE A 1 305 ? -2.388 27.115 13.260 1.00 6.83 ? 305 PHE A O 1 ATOM 2347 C CB . PHE A 1 305 ? -4.683 26.773 15.651 1.00 8.71 ? 305 PHE A CB 1 ATOM 2348 C CG . PHE A 1 305 ? -5.487 27.473 14.589 1.00 9.48 ? 305 PHE A CG 1 ATOM 2349 C CD1 . PHE A 1 305 ? -5.899 28.778 14.722 1.00 10.44 ? 305 PHE A CD1 1 ATOM 2350 C CD2 . PHE A 1 305 ? -5.886 26.783 13.450 1.00 9.68 ? 305 PHE A CD2 1 ATOM 2351 C CE1 . PHE A 1 305 ? -6.650 29.425 13.747 1.00 9.75 ? 305 PHE A CE1 1 ATOM 2352 C CE2 . PHE A 1 305 ? -6.620 27.420 12.443 1.00 8.22 ? 305 PHE A CE2 1 ATOM 2353 C CZ . PHE A 1 305 ? -7.022 28.728 12.606 1.00 8.75 ? 305 PHE A CZ 1 ATOM 2354 N N . TRP A 1 306 ? -2.458 25.032 14.120 1.00 5.62 ? 306 TRP A N 1 ATOM 2355 C CA . TRP A 1 306 ? -2.214 24.287 12.872 1.00 5.92 ? 306 TRP A CA 1 ATOM 2356 C C . TRP A 1 306 ? -3.528 23.616 12.466 1.00 6.62 ? 306 TRP A C 1 ATOM 2357 O O . TRP A 1 306 ? -4.037 22.813 13.262 1.00 6.89 ? 306 TRP A O 1 ATOM 2358 C CB . TRP A 1 306 ? -1.076 23.239 13.047 1.00 6.07 ? 306 TRP A CB 1 ATOM 2359 C CG . TRP A 1 306 ? -0.653 22.576 11.766 1.00 6.65 ? 306 TRP A CG 1 ATOM 2360 C CD1 . TRP A 1 306 ? -1.309 21.503 11.201 1.00 7.15 ? 306 TRP A CD1 1 ATOM 2361 C CD2 . TRP A 1 306 ? 0.418 22.882 10.873 1.00 6.17 ? 306 TRP A CD2 1 ATOM 2362 N NE1 . TRP A 1 306 ? -0.684 21.133 10.014 1.00 7.06 ? 306 TRP A NE1 1 ATOM 2363 C CE2 . TRP A 1 306 ? 0.402 21.969 9.819 1.00 7.04 ? 306 TRP A CE2 1 ATOM 2364 C CE3 . TRP A 1 306 ? 1.457 23.834 10.914 1.00 6.61 ? 306 TRP A CE3 1 ATOM 2365 C CZ2 . TRP A 1 306 ? 1.332 21.992 8.787 1.00 7.68 ? 306 TRP A CZ2 1 ATOM 2366 C CZ3 . TRP A 1 306 ? 2.414 23.852 9.895 1.00 5.57 ? 306 TRP A CZ3 1 ATOM 2367 C CH2 . TRP A 1 306 ? 2.332 22.947 8.825 1.00 6.54 ? 306 TRP A CH2 1 ATOM 2368 N N . GLN A 1 307 ? -4.167 23.924 11.339 1.00 5.87 ? 307 GLN A N 1 ATOM 2369 C CA . GLN A 1 307 ? -3.721 24.895 10.338 1.00 6.28 ? 307 GLN A CA 1 ATOM 2370 C C . GLN A 1 307 ? -4.961 25.487 9.602 1.00 7.74 ? 307 GLN A C 1 ATOM 2371 O O . GLN A 1 307 ? -6.069 24.870 9.623 1.00 6.96 ? 307 GLN A O 1 ATOM 2372 C CB . GLN A 1 307 ? -2.814 24.282 9.259 1.00 4.94 ? 307 GLN A CB 1 ATOM 2373 C CG . GLN A 1 307 ? -3.414 23.204 8.358 1.00 6.62 ? 307 GLN A CG 1 ATOM 2374 C CD . GLN A 1 307 ? -2.590 22.800 7.143 1.00 8.26 ? 307 GLN A CD 1 ATOM 2375 O OE1 . GLN A 1 307 ? -1.763 23.532 6.595 1.00 6.56 ? 307 GLN A OE1 1 ATOM 2376 N NE2 . GLN A 1 307 ? -2.830 21.564 6.674 1.00 7.18 ? 307 GLN A NE2 1 ATOM 2377 N N . TRP A 1 308 ? -4.792 26.579 8.864 1.00 7.84 ? 308 TRP A N 1 ATOM 2378 C CA . TRP A 1 308 ? -5.864 27.200 8.051 1.00 7.77 ? 308 TRP A CA 1 ATOM 2379 C C . TRP A 1 308 ? -6.204 26.353 6.821 1.00 8.73 ? 308 TRP A C 1 ATOM 2380 O O . TRP A 1 308 ? -5.313 25.790 6.182 1.00 8.44 ? 308 TRP A O 1 ATOM 2381 C CB . TRP A 1 308 ? -5.435 28.606 7.550 1.00 7.23 ? 308 TRP A CB 1 ATOM 2382 C CG . TRP A 1 308 ? -6.487 29.528 6.989 1.00 7.25 ? 308 TRP A CG 1 ATOM 2383 C CD1 . TRP A 1 308 ? -6.832 29.739 5.674 1.00 7.37 ? 308 TRP A CD1 1 ATOM 2384 C CD2 . TRP A 1 308 ? -7.398 30.328 7.763 1.00 7.23 ? 308 TRP A CD2 1 ATOM 2385 N NE1 . TRP A 1 308 ? -7.899 30.628 5.585 1.00 6.84 ? 308 TRP A NE1 1 ATOM 2386 C CE2 . TRP A 1 308 ? -8.249 31.009 6.870 1.00 7.15 ? 308 TRP A CE2 1 ATOM 2387 C CE3 . TRP A 1 308 ? -7.556 30.581 9.137 1.00 7.31 ? 308 TRP A CE3 1 ATOM 2388 C CZ2 . TRP A 1 308 ? -9.247 31.888 7.297 1.00 7.07 ? 308 TRP A CZ2 1 ATOM 2389 C CZ3 . TRP A 1 308 ? -8.538 31.455 9.576 1.00 7.88 ? 308 TRP A CZ3 1 ATOM 2390 C CH2 . TRP A 1 308 ? -9.407 32.101 8.643 1.00 8.62 ? 308 TRP A CH2 1 ATOM 2391 N N . GLY A 1 309 ? -7.486 26.279 6.429 1.00 8.27 ? 309 GLY A N 1 ATOM 2392 C CA . GLY A 1 309 ? -7.909 25.689 5.162 1.00 7.44 ? 309 GLY A CA 1 ATOM 2393 C C . GLY A 1 309 ? -8.832 26.674 4.417 1.00 8.31 ? 309 GLY A C 1 ATOM 2394 O O . GLY A 1 309 ? -9.583 27.360 5.113 1.00 7.54 ? 309 GLY A O 1 ATOM 2395 N N . ASP A 1 310 ? -8.789 26.723 3.060 1.00 6.65 ? 310 ASP A N 1 ATOM 2396 C CA . ASP A 1 310 ? -9.651 27.701 2.366 1.00 7.06 ? 310 ASP A CA 1 ATOM 2397 C C . ASP A 1 310 ? -9.929 27.231 0.933 1.00 8.04 ? 310 ASP A C 1 ATOM 2398 O O . ASP A 1 310 ? -9.430 26.162 0.503 1.00 7.23 ? 310 ASP A O 1 ATOM 2399 C CB . ASP A 1 310 ? -8.981 29.085 2.357 1.00 7.79 ? 310 ASP A CB 1 ATOM 2400 C CG . ASP A 1 310 ? -9.901 30.281 2.512 1.00 9.66 ? 310 ASP A CG 1 ATOM 2401 O OD1 . ASP A 1 310 ? -11.014 30.227 1.917 1.00 9.27 ? 310 ASP A OD1 1 ATOM 2402 O OD2 . ASP A 1 310 ? -9.605 31.313 3.183 1.00 7.18 ? 310 ASP A OD2 1 ATOM 2403 N N . THR A 1 311 ? -10.762 27.942 0.167 1.00 6.98 ? 311 THR A N 1 ATOM 2404 C CA . THR A 1 311 ? -11.159 27.578 -1.195 1.00 9.19 ? 311 THR A CA 1 ATOM 2405 C C . THR A 1 311 ? -11.043 28.801 -2.125 1.00 10.33 ? 311 THR A C 1 ATOM 2406 O O . THR A 1 311 ? -11.007 29.951 -1.653 1.00 9.37 ? 311 THR A O 1 ATOM 2407 C CB . THR A 1 311 ? -12.589 26.979 -1.275 1.00 10.89 ? 311 THR A CB 1 ATOM 2408 O OG1 . THR A 1 311 ? -13.554 27.983 -0.960 1.00 10.47 ? 311 THR A OG1 1 ATOM 2409 C CG2 . THR A 1 311 ? -12.781 25.819 -0.302 1.00 11.23 ? 311 THR A CG2 1 ATOM 2410 N N . PHE A 1 312 ? -10.908 28.609 -3.438 1.00 9.93 ? 312 PHE A N 1 ATOM 2411 C CA . PHE A 1 312 ? -10.584 29.657 -4.400 1.00 10.40 ? 312 PHE A CA 1 ATOM 2412 C C . PHE A 1 312 ? -11.684 29.992 -5.403 1.00 11.80 ? 312 PHE A C 1 ATOM 2413 O O . PHE A 1 312 ? -12.683 29.259 -5.529 1.00 9.67 ? 312 PHE A O 1 ATOM 2414 C CB . PHE A 1 312 ? -9.266 29.272 -5.135 1.00 9.81 ? 312 PHE A CB 1 ATOM 2415 C CG . PHE A 1 312 ? -8.165 28.783 -4.232 1.00 10.95 ? 312 PHE A CG 1 ATOM 2416 C CD1 . PHE A 1 312 ? -7.727 29.550 -3.153 1.00 10.97 ? 312 PHE A CD1 1 ATOM 2417 C CD2 . PHE A 1 312 ? -7.518 27.590 -4.475 1.00 10.94 ? 312 PHE A CD2 1 ATOM 2418 C CE1 . PHE A 1 312 ? -6.736 29.107 -2.309 1.00 10.08 ? 312 PHE A CE1 1 ATOM 2419 C CE2 . PHE A 1 312 ? -6.508 27.134 -3.647 1.00 11.67 ? 312 PHE A CE2 1 ATOM 2420 C CZ . PHE A 1 312 ? -6.091 27.900 -2.563 1.00 10.96 ? 312 PHE A CZ 1 ATOM 2421 N N . ALA A 1 313 ? -11.485 31.055 -6.189 1.00 13.23 ? 313 ALA A N 1 ATOM 2422 C CA . ALA A 1 313 ? -12.459 31.505 -7.189 1.00 13.95 ? 313 ALA A CA 1 ATOM 2423 C C . ALA A 1 313 ? -12.877 30.449 -8.213 1.00 15.52 ? 313 ALA A C 1 ATOM 2424 O O . ALA A 1 313 ? -14.045 30.435 -8.673 1.00 16.47 ? 313 ALA A O 1 ATOM 2425 C CB . ALA A 1 313 ? -11.950 32.780 -7.875 1.00 14.78 ? 313 ALA A CB 1 ATOM 2426 N N . ASN A 1 314 ? -12.026 29.493 -8.553 1.00 14.28 ? 314 ASN A N 1 ATOM 2427 C CA . ASN A 1 314 ? -12.304 28.430 -9.501 1.00 15.97 ? 314 ASN A CA 1 ATOM 2428 C C . ASN A 1 314 ? -12.993 27.206 -8.917 1.00 15.63 ? 314 ASN A C 1 ATOM 2429 O O . ASN A 1 314 ? -13.178 26.220 -9.655 1.00 15.79 ? 314 ASN A O 1 ATOM 2430 C CB . ASN A 1 314 ? -11.000 27.980 -10.186 1.00 17.90 ? 314 ASN A CB 1 ATOM 2431 C CG . ASN A 1 314 ? -9.970 27.394 -9.261 1.00 19.19 ? 314 ASN A CG 1 ATOM 2432 O OD1 . ASN A 1 314 ? -10.054 27.327 -8.040 1.00 16.61 ? 314 ASN A OD1 1 ATOM 2433 N ND2 . ASN A 1 314 ? -8.862 26.900 -9.846 1.00 22.22 ? 314 ASN A ND2 1 ATOM 2434 N N . GLY A 1 315 ? -13.294 27.185 -7.620 1.00 13.44 ? 315 GLY A N 1 ATOM 2435 C CA . GLY A 1 315 ? -13.953 26.041 -7.004 1.00 12.15 ? 315 GLY A CA 1 ATOM 2436 C C . GLY A 1 315 ? -12.988 25.014 -6.435 1.00 11.52 ? 315 GLY A C 1 ATOM 2437 O O . GLY A 1 315 ? -13.417 23.993 -5.898 1.00 11.93 ? 315 GLY A O 1 ATOM 2438 N N . ALA A 1 316 ? -11.679 25.232 -6.607 1.00 8.96 ? 316 ALA A N 1 ATOM 2439 C CA . ALA A 1 316 ? -10.764 24.261 -5.975 1.00 8.86 ? 316 ALA A CA 1 ATOM 2440 C C . ALA A 1 316 ? -10.518 24.598 -4.501 1.00 10.08 ? 316 ALA A C 1 ATOM 2441 O O . ALA A 1 316 ? -10.536 25.778 -4.141 1.00 10.15 ? 316 ALA A O 1 ATOM 2442 C CB . ALA A 1 316 ? -9.420 24.296 -6.689 1.00 9.74 ? 316 ALA A CB 1 ATOM 2443 N N . GLN A 1 317 ? -10.143 23.599 -3.710 1.00 8.46 ? 317 GLN A N 1 ATOM 2444 C CA . GLN A 1 317 ? -9.758 23.758 -2.305 1.00 8.46 ? 317 GLN A CA 1 ATOM 2445 C C . GLN A 1 317 ? -8.232 23.696 -2.109 1.00 8.93 ? 317 GLN A C 1 ATOM 2446 O O . GLN A 1 317 ? -7.520 23.099 -2.913 1.00 8.24 ? 317 GLN A O 1 ATOM 2447 C CB . GLN A 1 317 ? -10.414 22.707 -1.401 1.00 9.29 ? 317 GLN A CB 1 ATOM 2448 C CG . GLN A 1 317 ? -9.978 21.253 -1.482 1.00 10.14 ? 317 GLN A CG 1 ATOM 2449 C CD . GLN A 1 317 ? -10.885 20.280 -0.719 1.00 9.56 ? 317 GLN A CD 1 ATOM 2450 O OE1 . GLN A 1 317 ? -12.123 20.375 -0.712 1.00 9.84 ? 317 GLN A OE1 1 ATOM 2451 N NE2 . GLN A 1 317 ? -10.277 19.296 -0.051 1.00 8.61 ? 317 GLN A NE2 1 ATOM 2452 N N . SER A 1 318 ? -7.734 24.305 -1.026 1.00 6.75 ? 318 SER A N 1 ATOM 2453 C CA . SER A 1 318 ? -6.299 24.260 -0.727 1.00 7.88 ? 318 SER A CA 1 ATOM 2454 C C . SER A 1 318 ? -5.795 22.892 -0.299 1.00 7.58 ? 318 SER A C 1 ATOM 2455 O O . SER A 1 318 ? -6.575 22.007 0.051 1.00 6.51 ? 318 SER A O 1 ATOM 2456 C CB . SER A 1 318 ? -6.064 25.217 0.467 1.00 7.79 ? 318 SER A CB 1 ATOM 2457 O OG . SER A 1 318 ? -6.682 24.747 1.669 1.00 7.79 ? 318 SER A OG 1 ATOM 2458 N N . ASN A 1 319 ? -4.454 22.794 -0.144 1.00 7.18 ? 319 ASN A N 1 ATOM 2459 C CA . ASN A 1 319 ? -3.872 21.603 0.476 1.00 9.20 ? 319 ASN A CA 1 ATOM 2460 C C . ASN A 1 319 ? -4.554 21.404 1.854 1.00 10.59 ? 319 ASN A C 1 ATOM 2461 O O . ASN A 1 319 ? -4.836 22.402 2.512 1.00 9.95 ? 319 ASN A O 1 ATOM 2462 C CB . ASN A 1 319 ? -2.363 21.759 0.648 1.00 9.11 ? 319 ASN A CB 1 ATOM 2463 C CG . ASN A 1 319 ? -1.496 21.645 -0.592 1.00 10.29 ? 319 ASN A CG 1 ATOM 2464 O OD1 . ASN A 1 319 ? -1.945 21.709 -1.731 1.00 9.45 ? 319 ASN A OD1 1 ATOM 2465 N ND2 . ASN A 1 319 ? -0.160 21.491 -0.434 1.00 8.48 ? 319 ASN A ND2 1 ATOM 2466 N N . SER A 1 320 ? -4.801 20.185 2.312 1.00 10.37 ? 320 SER A N 1 ATOM 2467 C CA . SER A 1 320 ? -5.378 19.853 3.594 1.00 10.48 ? 320 SER A CA 1 ATOM 2468 C C . SER A 1 320 ? -4.670 18.709 4.344 1.00 11.06 ? 320 SER A C 1 ATOM 2469 O O . SER A 1 320 ? -3.768 18.047 3.793 1.00 11.65 ? 320 SER A O 1 ATOM 2470 C CB . SER A 1 320 ? -6.856 19.460 3.424 1.00 12.68 ? 320 SER A CB 1 ATOM 2471 O OG . SER A 1 320 ? -7.041 18.301 2.622 1.00 12.16 ? 320 SER A OG 1 ATOM 2472 N N . ASP A 1 321 ? -4.980 18.517 5.618 1.00 9.54 ? 321 ASP A N 1 ATOM 2473 C CA . ASP A 1 321 ? -4.453 17.382 6.433 1.00 10.07 ? 321 ASP A CA 1 ATOM 2474 C C . ASP A 1 321 ? -5.456 17.065 7.534 1.00 10.48 ? 321 ASP A C 1 ATOM 2475 O O . ASP A 1 321 ? -6.513 17.715 7.644 1.00 8.53 ? 321 ASP A O 1 ATOM 2476 C CB . ASP A 1 321 ? -3.026 17.568 6.920 1.00 9.75 ? 321 ASP A CB 1 ATOM 2477 C CG . ASP A 1 321 ? -2.756 18.561 8.042 1.00 9.87 ? 321 ASP A CG 1 ATOM 2478 O OD1 . ASP A 1 321 ? -3.734 19.048 8.654 1.00 8.10 ? 321 ASP A OD1 1 ATOM 2479 O OD2 . ASP A 1 321 ? -1.560 18.861 8.353 1.00 10.19 ? 321 ASP A OD2 1 ATOM 2480 N N . PRO A 1 322 ? -5.207 16.130 8.454 1.00 10.63 ? 322 PRO A N 1 ATOM 2481 C CA . PRO A 1 322 ? -6.166 15.835 9.520 1.00 11.85 ? 322 PRO A CA 1 ATOM 2482 C C . PRO A 1 322 ? -6.486 16.972 10.479 1.00 11.88 ? 322 PRO A C 1 ATOM 2483 O O . PRO A 1 322 ? -7.462 16.915 11.256 1.00 11.71 ? 322 PRO A O 1 ATOM 2484 C CB . PRO A 1 322 ? -5.570 14.628 10.247 1.00 12.83 ? 322 PRO A CB 1 ATOM 2485 C CG . PRO A 1 322 ? -4.582 14.036 9.297 1.00 12.75 ? 322 PRO A CG 1 ATOM 2486 C CD . PRO A 1 322 ? -4.049 15.217 8.477 1.00 11.60 ? 322 PRO A CD 1 ATOM 2487 N N . TYR A 1 323 ? -5.701 18.045 10.506 1.00 9.69 ? 323 TYR A N 1 ATOM 2488 C CA . TYR A 1 323 ? -5.845 19.157 11.427 1.00 9.75 ? 323 TYR A CA 1 ATOM 2489 C C . TYR A 1 323 ? -6.520 20.394 10.813 1.00 9.77 ? 323 TYR A C 1 ATOM 2490 O O . TYR A 1 323 ? -6.770 21.403 11.485 1.00 10.10 ? 323 TYR A O 1 ATOM 2491 C CB . TYR A 1 323 ? -4.445 19.509 12.007 1.00 8.96 ? 323 TYR A CB 1 ATOM 2492 C CG . TYR A 1 323 ? -3.654 18.379 12.653 1.00 8.38 ? 323 TYR A CG 1 ATOM 2493 C CD1 . TYR A 1 323 ? -3.882 17.957 13.965 1.00 8.46 ? 323 TYR A CD1 1 ATOM 2494 C CD2 . TYR A 1 323 ? -2.654 17.728 11.943 1.00 8.98 ? 323 TYR A CD2 1 ATOM 2495 C CE1 . TYR A 1 323 ? -3.158 16.922 14.557 1.00 9.05 ? 323 TYR A CE1 1 ATOM 2496 C CE2 . TYR A 1 323 ? -1.928 16.670 12.496 1.00 9.14 ? 323 TYR A CE2 1 ATOM 2497 C CZ . TYR A 1 323 ? -2.174 16.298 13.800 1.00 8.99 ? 323 TYR A CZ 1 ATOM 2498 O OH . TYR A 1 323 ? -1.463 15.242 14.322 1.00 10.33 ? 323 TYR A OH 1 ATOM 2499 N N . THR A 1 324 ? -6.838 20.363 9.515 1.00 8.41 ? 324 THR A N 1 ATOM 2500 C CA . THR A 1 324 ? -7.366 21.556 8.850 1.00 8.09 ? 324 THR A CA 1 ATOM 2501 C C . THR A 1 324 ? -8.618 22.143 9.482 1.00 9.05 ? 324 THR A C 1 ATOM 2502 O O . THR A 1 324 ? -9.557 21.382 9.778 1.00 8.84 ? 324 THR A O 1 ATOM 2503 C CB . THR A 1 324 ? -7.610 21.215 7.355 1.00 9.27 ? 324 THR A CB 1 ATOM 2504 O OG1 . THR A 1 324 ? -6.349 20.933 6.720 1.00 8.22 ? 324 THR A OG1 1 ATOM 2505 C CG2 . THR A 1 324 ? -8.342 22.334 6.626 1.00 9.66 ? 324 THR A CG2 1 ATOM 2506 N N . VAL A 1 325 ? -8.658 23.473 9.668 1.00 7.17 ? 325 VAL A N 1 ATOM 2507 C CA . VAL A 1 325 ? -9.829 24.212 10.149 1.00 7.38 ? 325 VAL A CA 1 ATOM 2508 C C . VAL A 1 325 ? -10.302 25.061 8.964 1.00 7.43 ? 325 VAL A C 1 ATOM 2509 O O . VAL A 1 325 ? -9.641 26.011 8.543 1.00 5.56 ? 325 VAL A O 1 ATOM 2510 C CB . VAL A 1 325 ? -9.573 25.093 11.370 1.00 8.10 ? 325 VAL A CB 1 ATOM 2511 C CG1 . VAL A 1 325 ? -10.776 25.937 11.793 1.00 8.90 ? 325 VAL A CG1 1 ATOM 2512 C CG2 . VAL A 1 325 ? -9.062 24.299 12.557 1.00 8.34 ? 325 VAL A CG2 1 ATOM 2513 N N . TRP A 1 326 ? -11.391 24.666 8.293 1.00 8.03 ? 326 TRP A N 1 ATOM 2514 C CA . TRP A 1 326 ? -11.883 25.334 7.109 1.00 9.50 ? 326 TRP A CA 1 ATOM 2515 C C . TRP A 1 326 ? -12.555 26.665 7.410 1.00 9.90 ? 326 TRP A C 1 ATOM 2516 O O . TRP A 1 326 ? -13.406 26.771 8.332 1.00 9.29 ? 326 TRP A O 1 ATOM 2517 C CB . TRP A 1 326 ? -12.846 24.403 6.324 1.00 9.53 ? 326 TRP A CB 1 ATOM 2518 C CG . TRP A 1 326 ? -12.303 23.114 5.789 1.00 9.39 ? 326 TRP A CG 1 ATOM 2519 C CD1 . TRP A 1 326 ? -12.495 21.858 6.279 1.00 10.33 ? 326 TRP A CD1 1 ATOM 2520 C CD2 . TRP A 1 326 ? -11.458 22.932 4.628 1.00 9.58 ? 326 TRP A CD2 1 ATOM 2521 N NE1 . TRP A 1 326 ? -11.820 20.913 5.526 1.00 10.51 ? 326 TRP A NE1 1 ATOM 2522 C CE2 . TRP A 1 326 ? -11.167 21.570 4.498 1.00 10.14 ? 326 TRP A CE2 1 ATOM 2523 C CE3 . TRP A 1 326 ? -10.905 23.834 3.696 1.00 9.20 ? 326 TRP A CE3 1 ATOM 2524 C CZ2 . TRP A 1 326 ? -10.368 21.064 3.475 1.00 11.12 ? 326 TRP A CZ2 1 ATOM 2525 C CZ3 . TRP A 1 326 ? -10.089 23.324 2.693 1.00 10.32 ? 326 TRP A CZ3 1 ATOM 2526 C CH2 . TRP A 1 326 ? -9.819 21.954 2.565 1.00 10.31 ? 326 TRP A CH2 1 ATOM 2527 N N . TYR A 1 327 ? -12.233 27.736 6.669 1.00 8.99 ? 327 TYR A N 1 ATOM 2528 C CA . TYR A 1 327 ? -12.858 29.043 6.890 1.00 9.18 ? 327 TYR A CA 1 ATOM 2529 C C . TYR A 1 327 ? -14.400 28.961 6.847 1.00 10.87 ? 327 TYR A C 1 ATOM 2530 O O . TYR A 1 327 ? -14.959 28.295 5.970 1.00 10.76 ? 327 TYR A O 1 ATOM 2531 C CB . TYR A 1 327 ? -12.388 30.080 5.840 1.00 8.94 ? 327 TYR A CB 1 ATOM 2532 C CG . TYR A 1 327 ? -13.045 31.440 5.947 1.00 8.87 ? 327 TYR A CG 1 ATOM 2533 C CD1 . TYR A 1 327 ? -12.958 32.208 7.101 1.00 9.12 ? 327 TYR A CD1 1 ATOM 2534 C CD2 . TYR A 1 327 ? -13.817 31.947 4.894 1.00 8.04 ? 327 TYR A CD2 1 ATOM 2535 C CE1 . TYR A 1 327 ? -13.572 33.435 7.190 1.00 10.78 ? 327 TYR A CE1 1 ATOM 2536 C CE2 . TYR A 1 327 ? -14.424 33.196 4.985 1.00 10.75 ? 327 TYR A CE2 1 ATOM 2537 C CZ . TYR A 1 327 ? -14.326 33.927 6.145 1.00 11.61 ? 327 TYR A CZ 1 ATOM 2538 O OH . TYR A 1 327 ? -14.938 35.170 6.251 1.00 12.48 ? 327 TYR A OH 1 ATOM 2539 N N . ASN A 1 328 ? -15.060 29.596 7.812 1.00 9.58 ? 328 ASN A N 1 ATOM 2540 C CA . ASN A 1 328 ? -16.507 29.672 7.927 1.00 11.39 ? 328 ASN A CA 1 ATOM 2541 C C . ASN A 1 328 ? -17.222 28.418 8.429 1.00 12.28 ? 328 ASN A C 1 ATOM 2542 O O . ASN A 1 328 ? -18.465 28.422 8.548 1.00 14.62 ? 328 ASN A O 1 ATOM 2543 C CB . ASN A 1 328 ? -17.133 30.181 6.620 1.00 13.53 ? 328 ASN A CB 1 ATOM 2544 C CG . ASN A 1 328 ? -17.497 31.623 6.592 1.00 16.63 ? 328 ASN A CG 1 ATOM 2545 O OD1 . ASN A 1 328 ? -17.399 32.476 7.452 1.00 15.64 ? 328 ASN A OD1 1 ATOM 2546 N ND2 . ASN A 1 328 ? -18.082 32.114 5.440 1.00 20.87 ? 328 ASN A ND2 1 ATOM 2547 N N . SER A 1 329 ? -16.515 27.346 8.774 1.00 10.09 ? 329 SER A N 1 ATOM 2548 C CA . SER A 1 329 ? -17.046 26.106 9.315 1.00 10.50 ? 329 SER A CA 1 ATOM 2549 C C . SER A 1 329 ? -17.381 26.189 10.810 1.00 10.07 ? 329 SER A C 1 ATOM 2550 O O . SER A 1 329 ? -17.074 27.182 11.453 1.00 9.15 ? 329 SER A O 1 ATOM 2551 C CB . SER A 1 329 ? -16.025 24.968 9.125 1.00 11.24 ? 329 SER A CB 1 ATOM 2552 O OG . SER A 1 329 ? -14.909 25.107 10.024 1.00 10.58 ? 329 SER A OG 1 ATOM 2553 N N . SER A 1 330 ? -17.984 25.133 11.372 1.00 9.42 ? 330 SER A N 1 ATOM 2554 C CA . SER A 1 330 ? -18.292 25.054 12.801 1.00 10.66 ? 330 SER A CA 1 ATOM 2555 C C . SER A 1 330 ? -17.022 25.093 13.643 1.00 9.63 ? 330 SER A C 1 ATOM 2556 O O . SER A 1 330 ? -17.004 25.712 14.724 1.00 9.11 ? 330 SER A O 1 ATOM 2557 C CB . SER A 1 330 ? -19.022 23.722 13.057 1.00 13.22 ? 330 SER A CB 1 ATOM 2558 O OG A SER A 1 330 ? -20.225 23.748 12.281 0.50 13.95 ? 330 SER A OG 1 ATOM 2559 O OG B SER A 1 330 ? -19.278 23.477 14.418 0.50 15.09 ? 330 SER A OG 1 ATOM 2560 N N . ASN A 1 331 ? -15.937 24.506 13.153 1.00 10.24 ? 331 ASN A N 1 ATOM 2561 C CA . ASN A 1 331 ? -14.653 24.574 13.855 1.00 10.89 ? 331 ASN A CA 1 ATOM 2562 C C . ASN A 1 331 ? -13.986 25.951 13.706 1.00 10.26 ? 331 ASN A C 1 ATOM 2563 O O . ASN A 1 331 ? -13.303 26.367 14.676 1.00 8.30 ? 331 ASN A O 1 ATOM 2564 C CB . ASN A 1 331 ? -13.712 23.440 13.473 1.00 11.86 ? 331 ASN A CB 1 ATOM 2565 C CG . ASN A 1 331 ? -14.002 22.067 14.018 1.00 14.58 ? 331 ASN A CG 1 ATOM 2566 O OD1 . ASN A 1 331 ? -13.500 21.022 13.550 1.00 17.80 ? 331 ASN A OD1 1 ATOM 2567 N ND2 . ASN A 1 331 ? -14.830 21.964 15.051 1.00 12.73 ? 331 ASN A ND2 1 ATOM 2568 N N . TRP A 1 332 ? -14.215 26.725 12.642 1.00 9.21 ? 332 TRP A N 1 ATOM 2569 C CA . TRP A 1 332 ? -13.813 28.139 12.589 1.00 9.71 ? 332 TRP A CA 1 ATOM 2570 C C . TRP A 1 332 ? -14.581 28.914 13.674 1.00 10.18 ? 332 TRP A C 1 ATOM 2571 O O . TRP A 1 332 ? -14.019 29.754 14.383 1.00 8.55 ? 332 TRP A O 1 ATOM 2572 C CB . TRP A 1 332 ? -14.036 28.743 11.191 1.00 9.02 ? 332 TRP A CB 1 ATOM 2573 C CG . TRP A 1 332 ? -13.883 30.224 11.015 1.00 9.97 ? 332 TRP A CG 1 ATOM 2574 C CD1 . TRP A 1 332 ? -12.747 30.918 10.701 1.00 8.89 ? 332 TRP A CD1 1 ATOM 2575 C CD2 . TRP A 1 332 ? -14.894 31.224 11.184 1.00 9.44 ? 332 TRP A CD2 1 ATOM 2576 N NE1 . TRP A 1 332 ? -12.973 32.271 10.649 1.00 8.95 ? 332 TRP A NE1 1 ATOM 2577 C CE2 . TRP A 1 332 ? -14.322 32.475 10.941 1.00 10.22 ? 332 TRP A CE2 1 ATOM 2578 C CE3 . TRP A 1 332 ? -16.268 31.127 11.518 1.00 10.32 ? 332 TRP A CE3 1 ATOM 2579 C CZ2 . TRP A 1 332 ? -15.037 33.660 11.034 1.00 12.00 ? 332 TRP A CZ2 1 ATOM 2580 C CZ3 . TRP A 1 332 ? -16.972 32.330 11.587 1.00 12.75 ? 332 TRP A CZ3 1 ATOM 2581 C CH2 . TRP A 1 332 ? -16.369 33.556 11.349 1.00 12.28 ? 332 TRP A CH2 1 ATOM 2582 N N . GLN A 1 333 ? -15.878 28.683 13.887 1.00 10.10 ? 333 GLN A N 1 ATOM 2583 C CA . GLN A 1 333 ? -16.634 29.361 14.946 1.00 11.48 ? 333 GLN A CA 1 ATOM 2584 C C . GLN A 1 333 ? -16.022 29.053 16.318 1.00 11.73 ? 333 GLN A C 1 ATOM 2585 O O . GLN A 1 333 ? -15.783 29.975 17.115 1.00 12.14 ? 333 GLN A O 1 ATOM 2586 C CB . GLN A 1 333 ? -18.115 28.938 14.891 1.00 12.62 ? 333 GLN A CB 1 ATOM 2587 C CG . GLN A 1 333 ? -19.077 29.515 15.912 1.00 17.91 ? 333 GLN A CG 1 ATOM 2588 C CD . GLN A 1 333 ? -20.465 28.881 15.861 1.00 22.64 ? 333 GLN A CD 1 ATOM 2589 O OE1 . GLN A 1 333 ? -20.865 28.129 14.963 1.00 24.54 ? 333 GLN A OE1 1 ATOM 2590 N NE2 . GLN A 1 333 ? -21.326 29.156 16.879 1.00 22.92 ? 333 GLN A NE2 1 ATOM 2591 N N . CYS A 1 334 ? -15.666 27.813 16.629 1.00 11.66 ? 334 CYS A N 1 ATOM 2592 C CA . CYS A 1 334 ? -15.185 27.434 17.960 1.00 10.81 ? 334 CYS A CA 1 ATOM 2593 C C . CYS A 1 334 ? -13.734 27.843 18.256 1.00 11.57 ? 334 CYS A C 1 ATOM 2594 O O . CYS A 1 334 ? -13.469 28.230 19.395 1.00 11.67 ? 334 CYS A O 1 ATOM 2595 C CB . CYS A 1 334 ? -15.288 25.914 18.170 1.00 11.01 ? 334 CYS A CB 1 ATOM 2596 S SG . CYS A 1 334 ? -14.590 25.152 19.655 1.00 10.72 ? 334 CYS A SG 1 ATOM 2597 N N . LEU A 1 335 ? -12.856 27.720 17.286 1.00 10.64 ? 335 LEU A N 1 ATOM 2598 C CA . LEU A 1 335 ? -11.412 27.936 17.481 1.00 10.65 ? 335 LEU A CA 1 ATOM 2599 C C . LEU A 1 335 ? -10.830 29.217 16.921 1.00 10.47 ? 335 LEU A C 1 ATOM 2600 O O . LEU A 1 335 ? -9.658 29.577 17.199 1.00 9.96 ? 335 LEU A O 1 ATOM 2601 C CB . LEU A 1 335 ? -10.652 26.702 16.950 1.00 10.50 ? 335 LEU A CB 1 ATOM 2602 C CG . LEU A 1 335 ? -10.909 25.299 17.528 1.00 10.80 ? 335 LEU A CG 1 ATOM 2603 C CD1 . LEU A 1 335 ? -10.159 24.171 16.840 1.00 11.20 ? 335 LEU A CD1 1 ATOM 2604 C CD2 . LEU A 1 335 ? -10.570 25.315 19.025 1.00 12.20 ? 335 LEU A CD2 1 ATOM 2605 N N . VAL A 1 336 ? -11.577 30.014 16.158 1.00 9.41 ? 336 VAL A N 1 ATOM 2606 C CA . VAL A 1 336 ? -11.125 31.279 15.591 1.00 8.87 ? 336 VAL A CA 1 ATOM 2607 C C . VAL A 1 336 ? -12.042 32.394 16.116 1.00 10.47 ? 336 VAL A C 1 ATOM 2608 O O . VAL A 1 336 ? -11.605 33.212 16.924 1.00 9.83 ? 336 VAL A O 1 ATOM 2609 C CB . VAL A 1 336 ? -11.064 31.284 14.056 1.00 8.71 ? 336 VAL A CB 1 ATOM 2610 C CG1 . VAL A 1 336 ? -10.449 32.588 13.504 1.00 8.52 ? 336 VAL A CG1 1 ATOM 2611 C CG2 . VAL A 1 336 ? -10.237 30.114 13.503 1.00 7.73 ? 336 VAL A CG2 1 ATOM 2612 N N . LYS A 1 337 ? -13.304 32.500 15.682 1.00 10.52 ? 337 LYS A N 1 ATOM 2613 C CA . LYS A 1 337 ? -14.167 33.605 16.150 1.00 12.98 ? 337 LYS A CA 1 ATOM 2614 C C . LYS A 1 337 ? -14.290 33.711 17.667 1.00 11.90 ? 337 LYS A C 1 ATOM 2615 O O . LYS A 1 337 ? -14.123 34.799 18.254 1.00 12.25 ? 337 LYS A O 1 ATOM 2616 C CB . LYS A 1 337 ? -15.571 33.494 15.539 1.00 15.96 ? 337 LYS A CB 1 ATOM 2617 C CG . LYS A 1 337 ? -16.441 34.713 15.884 1.00 21.55 ? 337 LYS A CG 1 ATOM 2618 C CD . LYS A 1 337 ? -17.869 34.657 15.445 1.00 25.94 ? 337 LYS A CD 1 ATOM 2619 C CE . LYS A 1 337 ? -18.816 35.603 16.187 1.00 29.01 ? 337 LYS A CE 1 ATOM 2620 N NZ . LYS A 1 337 ? -18.396 37.030 16.201 1.00 31.39 ? 337 LYS A NZ 1 ATOM 2621 N N . ASN A 1 338 ? -14.594 32.611 18.347 1.00 11.62 ? 338 ASN A N 1 ATOM 2622 C CA . ASN A 1 338 ? -14.763 32.645 19.800 1.00 12.48 ? 338 ASN A CA 1 ATOM 2623 C C . ASN A 1 338 ? -13.460 33.033 20.511 1.00 12.22 ? 338 ASN A C 1 ATOM 2624 O O . ASN A 1 338 ? -13.556 33.679 21.560 1.00 11.34 ? 338 ASN A O 1 ATOM 2625 C CB . ASN A 1 338 ? -15.342 31.363 20.381 1.00 13.09 ? 338 ASN A CB 1 ATOM 2626 C CG . ASN A 1 338 ? -16.783 31.021 20.050 1.00 14.55 ? 338 ASN A CG 1 ATOM 2627 O OD1 . ASN A 1 338 ? -17.494 31.817 19.448 1.00 14.52 ? 338 ASN A OD1 1 ATOM 2628 N ND2 . ASN A 1 338 ? -17.262 29.808 20.392 1.00 13.90 ? 338 ASN A ND2 1 ATOM 2629 N N . HIS A 1 339 ? -12.288 32.651 19.991 1.00 11.17 ? 339 HIS A N 1 ATOM 2630 C CA . HIS A 1 339 ? -10.989 32.998 20.609 1.00 9.27 ? 339 HIS A CA 1 ATOM 2631 C C . HIS A 1 339 ? -10.654 34.472 20.393 1.00 10.61 ? 339 HIS A C 1 ATOM 2632 O O . HIS A 1 339 ? -10.348 35.179 21.358 1.00 10.29 ? 339 HIS A O 1 ATOM 2633 C CB . HIS A 1 339 ? -9.856 32.085 20.115 1.00 8.68 ? 339 HIS A CB 1 ATOM 2634 C CG . HIS A 1 339 ? -8.509 32.244 20.748 1.00 9.96 ? 339 HIS A CG 1 ATOM 2635 N ND1 . HIS A 1 339 ? -8.355 32.382 22.108 1.00 9.94 ? 339 HIS A ND1 1 ATOM 2636 C CD2 . HIS A 1 339 ? -7.266 32.249 20.202 1.00 8.81 ? 339 HIS A CD2 1 ATOM 2637 C CE1 . HIS A 1 339 ? -7.055 32.480 22.389 1.00 9.67 ? 339 HIS A CE1 1 ATOM 2638 N NE2 . HIS A 1 339 ? -6.379 32.404 21.260 1.00 9.33 ? 339 HIS A NE2 1 ATOM 2639 N N . VAL A 1 340 ? -10.820 34.985 19.166 1.00 10.42 ? 340 VAL A N 1 ATOM 2640 C CA . VAL A 1 340 ? -10.661 36.411 18.892 1.00 11.96 ? 340 VAL A CA 1 ATOM 2641 C C . VAL A 1 340 ? -11.589 37.264 19.771 1.00 13.60 ? 340 VAL A C 1 ATOM 2642 O O . VAL A 1 340 ? -11.150 38.300 20.300 1.00 11.65 ? 340 VAL A O 1 ATOM 2643 C CB . VAL A 1 340 ? -10.910 36.691 17.396 1.00 12.45 ? 340 VAL A CB 1 ATOM 2644 C CG1 . VAL A 1 340 ? -11.027 38.183 17.106 1.00 11.24 ? 340 VAL A CG1 1 ATOM 2645 C CG2 . VAL A 1 340 ? -9.777 36.100 16.552 1.00 10.98 ? 340 VAL A CG2 1 ATOM 2646 N N . ASP A 1 341 ? -12.840 36.833 19.986 1.00 14.05 ? 341 ASP A N 1 ATOM 2647 C CA . ASP A 1 341 ? -13.763 37.581 20.850 1.00 17.21 ? 341 ASP A CA 1 ATOM 2648 C C . ASP A 1 341 ? -13.311 37.627 22.310 1.00 18.00 ? 341 ASP A C 1 ATOM 2649 O O . ASP A 1 341 ? -13.533 38.639 23.010 1.00 19.10 ? 341 ASP A O 1 ATOM 2650 C CB . ASP A 1 341 ? -15.182 37.011 20.738 1.00 18.86 ? 341 ASP A CB 1 ATOM 2651 C CG . ASP A 1 341 ? -15.897 37.266 19.435 1.00 20.46 ? 341 ASP A CG 1 ATOM 2652 O OD1 . ASP A 1 341 ? -15.483 38.137 18.635 1.00 20.42 ? 341 ASP A OD1 1 ATOM 2653 O OD2 . ASP A 1 341 ? -16.909 36.558 19.171 1.00 21.06 ? 341 ASP A OD2 1 ATOM 2654 N N . ALA A 1 342 ? -12.618 36.606 22.810 1.00 16.81 ? 342 ALA A N 1 ATOM 2655 C CA . ALA A 1 342 ? -12.112 36.588 24.182 1.00 16.88 ? 342 ALA A CA 1 ATOM 2656 C C . ALA A 1 342 ? -10.883 37.466 24.375 1.00 18.22 ? 342 ALA A C 1 ATOM 2657 O O . ALA A 1 342 ? -10.654 37.943 25.503 1.00 18.86 ? 342 ALA A O 1 ATOM 2658 C CB . ALA A 1 342 ? -11.807 35.168 24.631 1.00 15.61 ? 342 ALA A CB 1 ATOM 2659 N N . ILE A 1 343 ? -10.085 37.709 23.356 1.00 19.20 ? 343 ILE A N 1 ATOM 2660 C CA . ILE A 1 343 ? -8.916 38.576 23.425 1.00 22.23 ? 343 ILE A CA 1 ATOM 2661 C C . ILE A 1 343 ? -9.376 40.037 23.435 1.00 27.28 ? 343 ILE A C 1 ATOM 2662 O O . ILE A 1 343 ? -8.772 40.848 24.154 1.00 26.58 ? 343 ILE A O 1 ATOM 2663 C CB . ILE A 1 343 ? -7.916 38.254 22.290 1.00 20.58 ? 343 ILE A CB 1 ATOM 2664 C CG1 . ILE A 1 343 ? -7.410 36.818 22.414 1.00 18.58 ? 343 ILE A CG1 1 ATOM 2665 C CG2 . ILE A 1 343 ? -6.768 39.256 22.253 1.00 21.37 ? 343 ILE A CG2 1 ATOM 2666 C CD1 . ILE A 1 343 ? -6.807 36.208 21.164 1.00 17.35 ? 343 ILE A CD1 1 ATOM 2667 N N . ASN A 1 344 ? -10.461 40.372 22.728 1.00 32.06 ? 344 ASN A N 1 ATOM 2668 C CA . ASN A 1 344 ? -11.030 41.714 22.740 1.00 37.77 ? 344 ASN A CA 1 ATOM 2669 C C . ASN A 1 344 ? -12.492 41.850 22.304 1.00 39.47 ? 344 ASN A C 1 ATOM 2670 O O . ASN A 1 344 ? -13.170 42.822 22.716 1.00 40.88 ? 344 ASN A O 1 ATOM 2671 C CB . ASN A 1 344 ? -10.198 42.648 21.834 1.00 41.17 ? 344 ASN A CB 1 ATOM 2672 C CG . ASN A 1 344 ? -9.447 43.644 22.697 1.00 43.94 ? 344 ASN A CG 1 ATOM 2673 O OD1 . ASN A 1 344 ? -10.037 44.217 23.619 1.00 45.31 ? 344 ASN A OD1 1 ATOM 2674 N ND2 . ASN A 1 344 ? -8.165 43.810 22.403 1.00 44.92 ? 344 ASN A ND2 1 ATOM 2675 O OXT . ASN A 1 344 ? -12.990 40.987 21.541 1.00 20.00 ? 344 ASN A OXT 1 HETATM 2676 PT PT1 . TPT B 2 . ? 3.280 13.510 10.916 1.00 12.63 ? 401 TPT A PT1 1 HETATM 2677 N N1 . TPT B 2 . ? 4.420 12.068 11.844 1.00 11.02 ? 401 TPT A N1 1 HETATM 2678 N N2 . TPT B 2 . ? 3.551 14.237 12.744 1.00 9.93 ? 401 TPT A N2 1 HETATM 2679 N N3 . TPT B 2 . ? 2.261 15.259 10.800 1.00 12.10 ? 401 TPT A N3 1 HETATM 2680 C C1 . TPT B 2 . ? 4.850 10.937 11.266 1.00 12.31 ? 401 TPT A C1 1 HETATM 2681 C C2 . TPT B 2 . ? 5.651 10.031 11.921 1.00 12.91 ? 401 TPT A C2 1 HETATM 2682 C C3 . TPT B 2 . ? 6.040 10.308 13.237 1.00 13.90 ? 401 TPT A C3 1 HETATM 2683 C C4 . TPT B 2 . ? 5.636 11.459 13.822 1.00 11.37 ? 401 TPT A C4 1 HETATM 2684 C C5 . TPT B 2 . ? 4.772 12.340 13.153 1.00 11.05 ? 401 TPT A C5 1 HETATM 2685 C C6 . TPT B 2 . ? 4.268 13.618 13.689 1.00 11.74 ? 401 TPT A C6 1 HETATM 2686 C C7 . TPT B 2 . ? 4.570 14.170 14.917 1.00 12.38 ? 401 TPT A C7 1 HETATM 2687 C C8 . TPT B 2 . ? 4.009 15.386 15.225 1.00 12.11 ? 401 TPT A C8 1 HETATM 2688 C C9 . TPT B 2 . ? 3.277 16.068 14.288 1.00 12.56 ? 401 TPT A C9 1 HETATM 2689 C C10 . TPT B 2 . ? 3.078 15.491 13.043 1.00 12.87 ? 401 TPT A C10 1 HETATM 2690 C C11 . TPT B 2 . ? 2.295 16.042 11.920 1.00 12.97 ? 401 TPT A C11 1 HETATM 2691 C C12 . TPT B 2 . ? 1.692 17.297 11.913 1.00 14.17 ? 401 TPT A C12 1 HETATM 2692 C C13 . TPT B 2 . ? 0.998 17.719 10.797 1.00 13.62 ? 401 TPT A C13 1 HETATM 2693 C C14 . TPT B 2 . ? 0.948 16.919 9.620 1.00 12.78 ? 401 TPT A C14 1 HETATM 2694 C C15 . TPT B 2 . ? 1.616 15.701 9.696 1.00 12.58 ? 401 TPT A C15 1 HETATM 2695 PT PT1 . TPT C 2 . ? 7.635 14.906 13.191 1.00 15.20 ? 402 TPT A PT1 1 HETATM 2696 N N1 . TPT C 2 . ? 8.645 13.158 13.408 1.00 13.20 ? 402 TPT A N1 1 HETATM 2697 N N2 . TPT C 2 . ? 7.561 14.170 11.330 1.00 10.01 ? 402 TPT A N2 1 HETATM 2698 N N3 . TPT C 2 . ? 6.474 16.362 12.330 1.00 13.55 ? 402 TPT A N3 1 HETATM 2699 C C1 . TPT C 2 . ? 9.298 12.725 14.514 1.00 14.46 ? 402 TPT A C1 1 HETATM 2700 C C2 . TPT C 2 . ? 10.010 11.563 14.496 1.00 13.55 ? 402 TPT A C2 1 HETATM 2701 C C3 . TPT C 2 . ? 10.110 10.813 13.309 1.00 14.63 ? 402 TPT A C3 1 HETATM 2702 C C4 . TPT C 2 . ? 9.515 11.317 12.178 1.00 14.64 ? 402 TPT A C4 1 HETATM 2703 C C5 . TPT C 2 . ? 8.769 12.494 12.210 1.00 14.10 ? 402 TPT A C5 1 HETATM 2704 C C6 . TPT C 2 . ? 8.123 13.102 11.042 1.00 10.43 ? 402 TPT A C6 1 HETATM 2705 C C7 . TPT C 2 . ? 8.093 12.566 9.715 1.00 13.60 ? 402 TPT A C7 1 HETATM 2706 C C8 . TPT C 2 . ? 7.368 13.338 8.829 1.00 12.91 ? 402 TPT A C8 1 HETATM 2707 C C9 . TPT C 2 . ? 6.768 14.556 9.167 1.00 11.76 ? 402 TPT A C9 1 HETATM 2708 C C10 . TPT C 2 . ? 6.948 15.041 10.436 1.00 11.46 ? 402 TPT A C10 1 HETATM 2709 C C11 . TPT C 2 . ? 6.299 16.262 11.012 1.00 12.73 ? 402 TPT A C11 1 HETATM 2710 C C12 . TPT C 2 . ? 5.452 17.074 10.270 1.00 11.66 ? 402 TPT A C12 1 HETATM 2711 C C13 . TPT C 2 . ? 4.961 18.251 10.879 1.00 12.59 ? 402 TPT A C13 1 HETATM 2712 C C14 . TPT C 2 . ? 5.231 18.423 12.260 1.00 13.97 ? 402 TPT A C14 1 HETATM 2713 C C15 . TPT C 2 . ? 6.005 17.510 12.907 1.00 15.28 ? 402 TPT A C15 1 HETATM 2714 S S . SO4 D 3 . ? 1.464 10.650 13.785 1.00 14.56 ? 411 SO4 A S 1 HETATM 2715 O O1 . SO4 D 3 . ? 1.767 12.082 14.098 1.00 16.92 ? 411 SO4 A O1 1 HETATM 2716 O O2 . SO4 D 3 . ? 1.105 10.541 12.322 1.00 17.94 ? 411 SO4 A O2 1 HETATM 2717 O O3 . SO4 D 3 . ? 0.290 10.126 14.574 1.00 17.13 ? 411 SO4 A O3 1 HETATM 2718 O O4 . SO4 D 3 . ? 2.647 9.792 14.076 1.00 18.33 ? 411 SO4 A O4 1 HETATM 2719 S S . SO4 E 3 . ? -15.455 18.320 18.464 1.00 22.69 ? 412 SO4 A S 1 HETATM 2720 O O1 . SO4 E 3 . ? -14.551 18.945 17.423 1.00 23.85 ? 412 SO4 A O1 1 HETATM 2721 O O2 . SO4 E 3 . ? -15.809 16.904 18.182 1.00 23.82 ? 412 SO4 A O2 1 HETATM 2722 O O3 . SO4 E 3 . ? -16.806 19.077 18.394 1.00 22.04 ? 412 SO4 A O3 1 HETATM 2723 O O4 . SO4 E 3 . ? -14.932 18.531 19.833 1.00 22.74 ? 412 SO4 A O4 1 HETATM 2724 C C1 . NAG F 4 . ? 26.175 9.817 11.616 1.00 28.87 ? 430 NAG A C1 1 HETATM 2725 C C2 . NAG F 4 . ? 25.830 8.670 12.537 1.00 34.19 ? 430 NAG A C2 1 HETATM 2726 C C3 . NAG F 4 . ? 26.583 8.840 13.826 1.00 34.94 ? 430 NAG A C3 1 HETATM 2727 C C4 . NAG F 4 . ? 28.078 9.012 13.498 1.00 34.84 ? 430 NAG A C4 1 HETATM 2728 C C5 . NAG F 4 . ? 28.451 10.095 12.462 1.00 33.71 ? 430 NAG A C5 1 HETATM 2729 C C6 . NAG F 4 . ? 29.776 9.592 11.883 1.00 35.46 ? 430 NAG A C6 1 HETATM 2730 C C7 . NAG F 4 . ? 23.595 7.556 12.507 1.00 41.25 ? 430 NAG A C7 1 HETATM 2731 C C8 . NAG F 4 . ? 22.140 7.714 12.741 1.00 42.04 ? 430 NAG A C8 1 HETATM 2732 N N2 . NAG F 4 . ? 24.369 8.645 12.706 1.00 37.56 ? 430 NAG A N2 1 HETATM 2733 O O3 . NAG F 4 . ? 26.512 7.606 14.547 1.00 35.51 ? 430 NAG A O3 1 HETATM 2734 O O4 . NAG F 4 . ? 28.811 9.314 14.705 1.00 35.22 ? 430 NAG A O4 1 HETATM 2735 O O5 . NAG F 4 . ? 27.529 10.122 11.421 1.00 31.20 ? 430 NAG A O5 1 HETATM 2736 O O6 . NAG F 4 . ? 30.485 10.461 11.113 1.00 37.19 ? 430 NAG A O6 1 HETATM 2737 O O7 . NAG F 4 . ? 24.054 6.549 12.175 1.00 42.95 ? 430 NAG A O7 1 HETATM 2738 C C1 . NAG G 4 . ? 16.865 49.616 5.382 1.00 10.82 ? 431 NAG A C1 1 HETATM 2739 C C2 . NAG G 4 . ? 17.252 51.063 5.225 1.00 10.70 ? 431 NAG A C2 1 HETATM 2740 C C3 . NAG G 4 . ? 18.694 51.211 5.679 1.00 12.20 ? 431 NAG A C3 1 HETATM 2741 C C4 . NAG G 4 . ? 18.841 50.567 7.080 1.00 13.11 ? 431 NAG A C4 1 HETATM 2742 C C5 . NAG G 4 . ? 18.444 49.074 7.067 1.00 13.71 ? 431 NAG A C5 1 HETATM 2743 C C6 . NAG G 4 . ? 18.514 48.405 8.433 1.00 14.57 ? 431 NAG A C6 1 HETATM 2744 C C7 . NAG G 4 . ? 16.386 52.601 3.461 1.00 14.22 ? 431 NAG A C7 1 HETATM 2745 C C8 . NAG G 4 . ? 16.341 52.829 1.985 1.00 13.95 ? 431 NAG A C8 1 HETATM 2746 N N2 . NAG G 4 . ? 17.061 51.465 3.805 1.00 11.21 ? 431 NAG A N2 1 HETATM 2747 O O3 . NAG G 4 . ? 18.894 52.621 5.690 1.00 12.79 ? 431 NAG A O3 1 HETATM 2748 O O4 . NAG G 4 . ? 20.239 50.665 7.508 1.00 15.33 ? 431 NAG A O4 1 HETATM 2749 O O5 . NAG G 4 . ? 17.060 49.036 6.682 1.00 11.62 ? 431 NAG A O5 1 HETATM 2750 O O6 . NAG G 4 . ? 18.467 46.991 8.375 1.00 15.92 ? 431 NAG A O6 1 HETATM 2751 O O7 . NAG G 4 . ? 15.902 53.332 4.222 1.00 15.70 ? 431 NAG A O7 1 HETATM 2752 C C1 . NAG H 4 . ? -3.765 12.502 32.166 1.00 38.32 ? 432 NAG A C1 1 HETATM 2753 C C2 . NAG H 4 . ? -4.915 12.839 33.073 1.00 40.36 ? 432 NAG A C2 1 HETATM 2754 C C3 . NAG H 4 . ? -4.539 13.618 34.310 1.00 41.19 ? 432 NAG A C3 1 HETATM 2755 C C4 . NAG H 4 . ? -3.091 13.224 34.700 1.00 41.83 ? 432 NAG A C4 1 HETATM 2756 C C5 . NAG H 4 . ? -2.148 13.726 33.580 1.00 41.77 ? 432 NAG A C5 1 HETATM 2757 C C6 . NAG H 4 . ? -0.698 13.337 33.844 1.00 42.03 ? 432 NAG A C6 1 HETATM 2758 C C7 . NAG H 4 . ? -6.977 12.918 31.678 1.00 41.16 ? 432 NAG A C7 1 HETATM 2759 C C8 . NAG H 4 . ? -8.306 13.578 31.633 1.00 40.91 ? 432 NAG A C8 1 HETATM 2760 N N2 . NAG H 4 . ? -5.976 13.576 32.324 1.00 40.73 ? 432 NAG A N2 1 HETATM 2761 O O3 . NAG H 4 . ? -5.420 13.224 35.356 1.00 40.57 ? 432 NAG A O3 1 HETATM 2762 O O4 . NAG H 4 . ? -2.708 13.849 35.925 1.00 41.89 ? 432 NAG A O4 1 HETATM 2763 O O5 . NAG H 4 . ? -2.500 13.099 32.379 1.00 40.52 ? 432 NAG A O5 1 HETATM 2764 O O6 . NAG H 4 . ? 0.068 13.495 32.698 1.00 41.62 ? 432 NAG A O6 1 HETATM 2765 O O7 . NAG H 4 . ? -6.764 11.887 31.216 1.00 40.89 ? 432 NAG A O7 1 HETATM 2766 C C1 . NAG I 4 . ? -18.843 33.396 4.804 1.00 25.90 ? 433 NAG A C1 1 HETATM 2767 C C2 . NAG I 4 . ? -19.000 33.782 3.344 1.00 28.16 ? 433 NAG A C2 1 HETATM 2768 C C3 . NAG I 4 . ? -19.652 35.130 3.181 1.00 29.26 ? 433 NAG A C3 1 HETATM 2769 C C4 . NAG I 4 . ? -20.972 35.115 3.990 1.00 28.90 ? 433 NAG A C4 1 HETATM 2770 C C5 . NAG I 4 . ? -20.730 34.747 5.475 1.00 27.92 ? 433 NAG A C5 1 HETATM 2771 C C6 . NAG I 4 . ? -22.058 34.534 6.208 1.00 27.26 ? 433 NAG A C6 1 HETATM 2772 C C7 . NAG I 4 . ? -17.256 32.589 2.071 1.00 30.74 ? 433 NAG A C7 1 HETATM 2773 C C8 . NAG I 4 . ? -15.967 32.636 1.332 1.00 29.76 ? 433 NAG A C8 1 HETATM 2774 N N2 . NAG I 4 . ? -17.662 33.730 2.688 1.00 29.13 ? 433 NAG A N2 1 HETATM 2775 O O3 . NAG I 4 . ? -19.946 35.280 1.782 1.00 30.19 ? 433 NAG A O3 1 HETATM 2776 O O4 . NAG I 4 . ? -21.581 36.412 3.934 1.00 28.49 ? 433 NAG A O4 1 HETATM 2777 O O5 . NAG I 4 . ? -20.082 33.489 5.540 1.00 26.84 ? 433 NAG A O5 1 HETATM 2778 O O6 . NAG I 4 . ? -21.876 34.378 7.582 1.00 25.04 ? 433 NAG A O6 1 HETATM 2779 O O7 . NAG I 4 . ? -17.850 31.604 2.099 1.00 32.21 ? 433 NAG A O7 1 HETATM 2780 O O . HOH J 5 . ? -2.105 52.248 9.122 1.00 23.04 ? 2001 HOH A O 1 HETATM 2781 O O . HOH J 5 . ? -2.308 55.004 13.588 1.00 17.84 ? 2002 HOH A O 1 HETATM 2782 O O . HOH J 5 . ? -0.623 56.930 14.016 1.00 30.34 ? 2003 HOH A O 1 HETATM 2783 O O . HOH J 5 . ? -0.442 57.436 17.183 1.00 55.98 ? 2004 HOH A O 1 HETATM 2784 O O . HOH J 5 . ? 6.008 52.654 7.476 1.00 19.11 ? 2005 HOH A O 1 HETATM 2785 O O . HOH J 5 . ? -0.828 48.534 8.225 1.00 22.37 ? 2006 HOH A O 1 HETATM 2786 O O . HOH J 5 . ? 2.956 54.320 10.441 1.00 20.04 ? 2007 HOH A O 1 HETATM 2787 O O . HOH J 5 . ? 1.415 54.244 16.381 1.00 48.19 ? 2008 HOH A O 1 HETATM 2788 O O . HOH J 5 . ? 10.891 52.303 13.437 1.00 28.20 ? 2009 HOH A O 1 HETATM 2789 O O . HOH J 5 . ? 11.257 50.106 15.263 1.00 24.26 ? 2010 HOH A O 1 HETATM 2790 O O . HOH J 5 . ? 13.910 45.435 17.749 1.00 21.36 ? 2011 HOH A O 1 HETATM 2791 O O . HOH J 5 . ? 11.268 50.736 19.244 1.00 61.51 ? 2012 HOH A O 1 HETATM 2792 O O . HOH J 5 . ? 15.524 49.429 20.113 1.00 22.40 ? 2013 HOH A O 1 HETATM 2793 O O . HOH J 5 . ? 0.082 41.611 34.409 1.00 41.68 ? 2014 HOH A O 1 HETATM 2794 O O . HOH J 5 . ? 3.404 52.579 15.207 1.00 46.76 ? 2015 HOH A O 1 HETATM 2795 O O . HOH J 5 . ? 5.165 48.343 16.344 1.00 22.57 ? 2016 HOH A O 1 HETATM 2796 O O . HOH J 5 . ? 5.330 51.010 16.957 1.00 48.35 ? 2017 HOH A O 1 HETATM 2797 O O . HOH J 5 . ? 13.066 48.544 19.412 1.00 30.90 ? 2018 HOH A O 1 HETATM 2798 O O . HOH J 5 . ? 8.602 51.283 12.403 1.00 22.96 ? 2019 HOH A O 1 HETATM 2799 O O . HOH J 5 . ? 8.572 49.983 15.378 1.00 25.88 ? 2020 HOH A O 1 HETATM 2800 O O . HOH J 5 . ? 1.538 42.139 31.393 1.00 38.34 ? 2021 HOH A O 1 HETATM 2801 O O . HOH J 5 . ? -0.306 47.374 32.070 1.00 65.16 ? 2022 HOH A O 1 HETATM 2802 O O . HOH J 5 . ? -3.851 42.933 25.737 1.00 67.54 ? 2023 HOH A O 1 HETATM 2803 O O . HOH J 5 . ? 12.282 44.556 15.746 1.00 12.68 ? 2024 HOH A O 1 HETATM 2804 O O . HOH J 5 . ? -12.427 31.857 -11.821 1.00 34.20 ? 2025 HOH A O 1 HETATM 2805 O O . HOH J 5 . ? 7.569 49.909 17.693 1.00 47.18 ? 2026 HOH A O 1 HETATM 2806 O O . HOH J 5 . ? 8.528 48.704 21.418 1.00 22.10 ? 2027 HOH A O 1 HETATM 2807 O O . HOH J 5 . ? -2.535 53.735 16.001 1.00 31.25 ? 2028 HOH A O 1 HETATM 2808 O O . HOH J 5 . ? 12.567 45.017 20.033 1.00 14.13 ? 2029 HOH A O 1 HETATM 2809 O O . HOH J 5 . ? 12.017 47.633 21.840 1.00 36.04 ? 2030 HOH A O 1 HETATM 2810 O O . HOH J 5 . ? 4.903 45.604 28.424 1.00 23.99 ? 2031 HOH A O 1 HETATM 2811 O O . HOH J 5 . ? 5.319 47.989 27.816 1.00 33.73 ? 2032 HOH A O 1 HETATM 2812 O O . HOH J 5 . ? 8.380 50.318 24.655 1.00 49.73 ? 2033 HOH A O 1 HETATM 2813 O O . HOH J 5 . ? -4.960 40.399 27.641 1.00 47.54 ? 2034 HOH A O 1 HETATM 2814 O O . HOH J 5 . ? -3.954 44.938 21.740 1.00 56.19 ? 2035 HOH A O 1 HETATM 2815 O O . HOH J 5 . ? -6.975 49.839 21.429 1.00 55.79 ? 2036 HOH A O 1 HETATM 2816 O O . HOH J 5 . ? 10.669 47.840 25.991 1.00 14.68 ? 2037 HOH A O 1 HETATM 2817 O O . HOH J 5 . ? 5.169 44.731 30.617 1.00 30.77 ? 2038 HOH A O 1 HETATM 2818 O O . HOH J 5 . ? 3.802 40.353 31.935 1.00 19.88 ? 2039 HOH A O 1 HETATM 2819 O O . HOH J 5 . ? 6.549 44.272 30.995 1.00 15.57 ? 2040 HOH A O 1 HETATM 2820 O O . HOH J 5 . ? 3.850 38.266 27.400 1.00 18.31 ? 2041 HOH A O 1 HETATM 2821 O O . HOH J 5 . ? 9.126 29.812 -16.100 1.00 77.23 ? 2042 HOH A O 1 HETATM 2822 O O . HOH J 5 . ? 0.782 46.814 28.887 1.00 57.88 ? 2043 HOH A O 1 HETATM 2823 O O . HOH J 5 . ? 1.351 39.526 26.245 1.00 20.00 ? 2044 HOH A O 1 HETATM 2824 O O . HOH J 5 . ? -1.935 44.433 27.742 1.00 49.20 ? 2045 HOH A O 1 HETATM 2825 O O . HOH J 5 . ? 2.226 40.286 23.594 1.00 15.92 ? 2046 HOH A O 1 HETATM 2826 O O . HOH J 5 . ? 6.323 51.118 23.235 1.00 54.79 ? 2047 HOH A O 1 HETATM 2827 O O . HOH J 5 . ? 5.179 52.575 19.434 1.00 54.60 ? 2048 HOH A O 1 HETATM 2828 O O . HOH J 5 . ? 2.526 32.182 -13.941 1.00 37.07 ? 2049 HOH A O 1 HETATM 2829 O O . HOH J 5 . ? -10.096 36.320 -9.055 1.00 23.64 ? 2050 HOH A O 1 HETATM 2830 O O . HOH J 5 . ? -9.533 31.982 -10.842 1.00 22.04 ? 2051 HOH A O 1 HETATM 2831 O O . HOH J 5 . ? -8.214 34.552 -13.495 1.00 29.23 ? 2052 HOH A O 1 HETATM 2832 O O . HOH J 5 . ? -8.254 30.551 -12.929 1.00 43.99 ? 2053 HOH A O 1 HETATM 2833 O O . HOH J 5 . ? -2.157 46.169 15.645 1.00 10.54 ? 2054 HOH A O 1 HETATM 2834 O O . HOH J 5 . ? -3.466 24.605 -4.654 1.00 15.33 ? 2055 HOH A O 1 HETATM 2835 O O . HOH J 5 . ? 4.564 46.543 14.120 1.00 12.82 ? 2056 HOH A O 1 HETATM 2836 O O . HOH J 5 . ? -1.909 45.149 13.077 1.00 15.99 ? 2057 HOH A O 1 HETATM 2837 O O . HOH J 5 . ? -0.177 46.318 9.316 1.00 17.60 ? 2058 HOH A O 1 HETATM 2838 O O . HOH J 5 . ? -2.107 50.844 14.286 1.00 18.85 ? 2059 HOH A O 1 HETATM 2839 O O . HOH J 5 . ? 14.665 7.896 8.128 1.00 35.80 ? 2060 HOH A O 1 HETATM 2840 O O . HOH J 5 . ? -8.577 28.107 -20.387 1.00 70.87 ? 2061 HOH A O 1 HETATM 2841 O O . HOH J 5 . ? -10.606 33.844 33.782 1.00 50.21 ? 2062 HOH A O 1 HETATM 2842 O O . HOH J 5 . ? -12.058 43.900 5.331 1.00 22.62 ? 2063 HOH A O 1 HETATM 2843 O O . HOH J 5 . ? -8.361 42.810 4.205 1.00 29.77 ? 2064 HOH A O 1 HETATM 2844 O O . HOH J 5 . ? -12.262 38.332 -1.692 1.00 25.04 ? 2065 HOH A O 1 HETATM 2845 O O . HOH J 5 . ? -16.369 36.441 0.391 1.00 32.98 ? 2066 HOH A O 1 HETATM 2846 O O . HOH J 5 . ? 0.025 43.384 19.868 1.00 18.70 ? 2067 HOH A O 1 HETATM 2847 O O . HOH J 5 . ? -6.156 53.872 17.713 1.00 58.25 ? 2068 HOH A O 1 HETATM 2848 O O . HOH J 5 . ? -14.927 38.677 1.988 1.00 61.61 ? 2069 HOH A O 1 HETATM 2849 O O . HOH J 5 . ? -9.410 46.227 6.424 1.00 20.66 ? 2070 HOH A O 1 HETATM 2850 O O . HOH J 5 . ? -13.199 40.536 15.299 1.00 49.28 ? 2071 HOH A O 1 HETATM 2851 O O . HOH J 5 . ? -18.514 37.018 12.206 1.00 45.27 ? 2072 HOH A O 1 HETATM 2852 O O . HOH J 5 . ? -0.897 49.942 23.324 1.00 28.01 ? 2073 HOH A O 1 HETATM 2853 O O . HOH J 5 . ? -11.323 41.847 17.476 1.00 36.98 ? 2074 HOH A O 1 HETATM 2854 O O . HOH J 5 . ? -8.103 43.864 17.322 1.00 44.92 ? 2075 HOH A O 1 HETATM 2855 O O . HOH J 5 . ? 30.194 18.941 16.877 1.00 27.25 ? 2076 HOH A O 1 HETATM 2856 O O . HOH J 5 . ? -6.170 47.370 20.267 1.00 52.25 ? 2077 HOH A O 1 HETATM 2857 O O . HOH J 5 . ? -2.404 41.069 26.924 1.00 33.75 ? 2078 HOH A O 1 HETATM 2858 O O . HOH J 5 . ? -4.304 41.453 19.409 1.00 25.26 ? 2079 HOH A O 1 HETATM 2859 O O . HOH J 5 . ? -4.574 42.185 23.334 1.00 23.71 ? 2080 HOH A O 1 HETATM 2860 O O . HOH J 5 . ? 5.065 20.414 8.309 1.00 10.94 ? 2081 HOH A O 1 HETATM 2861 O O . HOH J 5 . ? -4.790 39.136 17.413 1.00 21.07 ? 2082 HOH A O 1 HETATM 2862 O O . HOH J 5 . ? 15.679 13.709 -6.093 1.00 52.64 ? 2083 HOH A O 1 HETATM 2863 O O . HOH J 5 . ? 22.556 15.705 -5.343 1.00 37.67 ? 2084 HOH A O 1 HETATM 2864 O O . HOH J 5 . ? 22.206 15.447 -7.924 1.00 45.97 ? 2085 HOH A O 1 HETATM 2865 O O . HOH J 5 . ? 24.262 4.324 16.551 1.00 80.94 ? 2086 HOH A O 1 HETATM 2866 O O . HOH J 5 . ? 17.193 28.719 -13.287 1.00 47.87 ? 2087 HOH A O 1 HETATM 2867 O O . HOH J 5 . ? 33.653 23.917 27.123 1.00 60.91 ? 2088 HOH A O 1 HETATM 2868 O O . HOH J 5 . ? 33.987 26.651 25.582 1.00 55.75 ? 2089 HOH A O 1 HETATM 2869 O O . HOH J 5 . ? 26.431 31.535 27.214 1.00 33.89 ? 2090 HOH A O 1 HETATM 2870 O O . HOH J 5 . ? 5.971 29.432 -15.114 1.00 35.33 ? 2091 HOH A O 1 HETATM 2871 O O . HOH J 5 . ? -1.378 19.806 4.224 1.00 7.59 ? 2092 HOH A O 1 HETATM 2872 O O . HOH J 5 . ? 18.933 52.781 17.722 1.00 58.70 ? 2093 HOH A O 1 HETATM 2873 O O . HOH J 5 . ? -0.296 25.616 -2.247 1.00 12.30 ? 2094 HOH A O 1 HETATM 2874 O O . HOH J 5 . ? 24.864 19.838 -13.645 1.00 61.03 ? 2095 HOH A O 1 HETATM 2875 O O . HOH J 5 . ? 2.243 31.977 -3.206 1.00 11.81 ? 2096 HOH A O 1 HETATM 2876 O O . HOH J 5 . ? 29.046 23.670 -2.785 1.00 44.47 ? 2097 HOH A O 1 HETATM 2877 O O . HOH J 5 . ? 30.400 18.890 -1.429 1.00 25.55 ? 2098 HOH A O 1 HETATM 2878 O O . HOH J 5 . ? 15.197 24.933 36.400 1.00 22.90 ? 2099 HOH A O 1 HETATM 2879 O O . HOH J 5 . ? 8.665 28.720 37.776 1.00 44.51 ? 2100 HOH A O 1 HETATM 2880 O O . HOH J 5 . ? 28.224 22.381 -13.709 1.00 77.08 ? 2101 HOH A O 1 HETATM 2881 O O . HOH J 5 . ? 24.517 30.161 -9.541 1.00 39.72 ? 2102 HOH A O 1 HETATM 2882 O O . HOH J 5 . ? 28.546 26.609 -10.899 1.00 54.64 ? 2103 HOH A O 1 HETATM 2883 O O . HOH J 5 . ? 13.631 10.149 12.183 1.00 70.93 ? 2104 HOH A O 1 HETATM 2884 O O . HOH J 5 . ? 0.311 26.167 -7.255 1.00 19.92 ? 2105 HOH A O 1 HETATM 2885 O O . HOH J 5 . ? 1.555 24.219 -4.889 1.00 27.04 ? 2106 HOH A O 1 HETATM 2886 O O . HOH J 5 . ? 25.216 25.673 -12.945 1.00 57.61 ? 2107 HOH A O 1 HETATM 2887 O O . HOH J 5 . ? 20.360 34.594 -5.539 1.00 40.90 ? 2108 HOH A O 1 HETATM 2888 O O . HOH J 5 . ? 14.894 32.836 -14.038 1.00 74.31 ? 2109 HOH A O 1 HETATM 2889 O O . HOH J 5 . ? 15.769 29.435 35.415 1.00 43.10 ? 2110 HOH A O 1 HETATM 2890 O O . HOH J 5 . ? 2.977 32.723 -11.251 1.00 24.29 ? 2111 HOH A O 1 HETATM 2891 O O . HOH J 5 . ? -1.000 33.468 -12.768 1.00 24.27 ? 2112 HOH A O 1 HETATM 2892 O O . HOH J 5 . ? -2.006 30.144 -12.613 1.00 33.15 ? 2113 HOH A O 1 HETATM 2893 O O . HOH J 5 . ? -1.745 27.459 -8.067 1.00 28.14 ? 2114 HOH A O 1 HETATM 2894 O O . HOH J 5 . ? 9.306 33.385 -17.038 1.00 31.93 ? 2115 HOH A O 1 HETATM 2895 O O . HOH J 5 . ? -6.218 29.947 -10.868 1.00 42.49 ? 2116 HOH A O 1 HETATM 2896 O O . HOH J 5 . ? -8.308 34.623 -10.746 1.00 17.53 ? 2117 HOH A O 1 HETATM 2897 O O . HOH J 5 . ? 5.073 6.567 22.557 1.00 63.55 ? 2118 HOH A O 1 HETATM 2898 O O . HOH J 5 . ? 9.242 40.413 -9.875 1.00 34.47 ? 2119 HOH A O 1 HETATM 2899 O O . HOH J 5 . ? 10.189 41.852 -7.979 1.00 49.82 ? 2120 HOH A O 1 HETATM 2900 O O . HOH J 5 . ? 0.947 26.809 37.586 1.00 53.02 ? 2121 HOH A O 1 HETATM 2901 O O . HOH J 5 . ? 6.322 30.589 38.170 1.00 37.17 ? 2122 HOH A O 1 HETATM 2902 O O . HOH J 5 . ? 13.133 26.704 38.025 1.00 34.87 ? 2123 HOH A O 1 HETATM 2903 O O . HOH J 5 . ? -8.626 38.149 -5.123 1.00 26.54 ? 2124 HOH A O 1 HETATM 2904 O O . HOH J 5 . ? -10.032 35.699 -6.287 1.00 23.89 ? 2125 HOH A O 1 HETATM 2905 O O . HOH J 5 . ? 0.958 40.711 -8.606 1.00 17.63 ? 2126 HOH A O 1 HETATM 2906 O O . HOH J 5 . ? -2.768 29.609 -7.312 1.00 17.62 ? 2127 HOH A O 1 HETATM 2907 O O . HOH J 5 . ? -4.041 27.084 -6.474 1.00 28.83 ? 2128 HOH A O 1 HETATM 2908 O O . HOH J 5 . ? -8.943 30.578 -8.515 1.00 13.45 ? 2129 HOH A O 1 HETATM 2909 O O . HOH J 5 . ? -2.991 45.953 -7.114 1.00 13.13 ? 2130 HOH A O 1 HETATM 2910 O O . HOH J 5 . ? -11.891 23.630 30.441 1.00 44.64 ? 2131 HOH A O 1 HETATM 2911 O O . HOH J 5 . ? -6.432 40.280 -5.581 1.00 10.98 ? 2132 HOH A O 1 HETATM 2912 O O . HOH J 5 . ? -12.227 30.307 31.884 1.00 36.98 ? 2133 HOH A O 1 HETATM 2913 O O . HOH J 5 . ? -10.746 32.595 31.439 1.00 43.52 ? 2134 HOH A O 1 HETATM 2914 O O . HOH J 5 . ? -9.358 33.029 -5.238 1.00 10.85 ? 2135 HOH A O 1 HETATM 2915 O O . HOH J 5 . ? -9.261 31.973 -0.478 1.00 7.78 ? 2136 HOH A O 1 HETATM 2916 O O . HOH J 5 . ? 16.983 14.108 7.523 1.00 14.73 ? 2137 HOH A O 1 HETATM 2917 O O . HOH J 5 . ? 15.301 13.284 10.972 1.00 14.51 ? 2138 HOH A O 1 HETATM 2918 O O . HOH J 5 . ? -9.633 27.161 -17.002 1.00 80.94 ? 2139 HOH A O 1 HETATM 2919 O O . HOH J 5 . ? -12.530 28.931 -13.736 1.00 42.26 ? 2140 HOH A O 1 HETATM 2920 O O . HOH J 5 . ? -18.035 26.875 -12.847 1.00 72.40 ? 2141 HOH A O 1 HETATM 2921 O O . HOH J 5 . ? 13.349 12.269 8.859 1.00 26.97 ? 2142 HOH A O 1 HETATM 2922 O O . HOH J 5 . ? 12.459 9.306 5.805 1.00 39.53 ? 2143 HOH A O 1 HETATM 2923 O O . HOH J 5 . ? 15.605 11.653 7.449 1.00 42.62 ? 2144 HOH A O 1 HETATM 2924 O O . HOH J 5 . ? -12.200 40.747 -0.147 1.00 35.49 ? 2145 HOH A O 1 HETATM 2925 O O . HOH J 5 . ? -10.618 41.624 4.728 1.00 22.54 ? 2146 HOH A O 1 HETATM 2926 O O . HOH J 5 . ? -10.537 42.991 2.339 1.00 51.29 ? 2147 HOH A O 1 HETATM 2927 O O . HOH J 5 . ? -14.524 34.679 0.019 1.00 3.17 ? 2148 HOH A O 1 HETATM 2928 O O . HOH J 5 . ? 21.805 9.402 2.783 1.00 34.17 ? 2149 HOH A O 1 HETATM 2929 O O . HOH J 5 . ? -9.658 43.450 9.054 1.00 27.28 ? 2150 HOH A O 1 HETATM 2930 O O . HOH J 5 . ? -5.673 42.765 9.566 1.00 20.91 ? 2151 HOH A O 1 HETATM 2931 O O . HOH J 5 . ? -7.389 44.504 5.996 1.00 37.39 ? 2152 HOH A O 1 HETATM 2932 O O . HOH J 5 . ? 30.925 15.019 6.025 1.00 31.66 ? 2153 HOH A O 1 HETATM 2933 O O . HOH J 5 . ? -13.167 38.623 4.039 1.00 22.45 ? 2154 HOH A O 1 HETATM 2934 O O . HOH J 5 . ? -12.749 41.314 12.783 1.00 33.50 ? 2155 HOH A O 1 HETATM 2935 O O . HOH J 5 . ? -15.482 37.391 11.760 1.00 34.52 ? 2156 HOH A O 1 HETATM 2936 O O . HOH J 5 . ? 28.643 10.186 1.918 1.00 21.72 ? 2157 HOH A O 1 HETATM 2937 O O . HOH J 5 . ? 31.643 10.007 5.067 1.00 22.37 ? 2158 HOH A O 1 HETATM 2938 O O . HOH J 5 . ? 18.170 9.051 8.758 1.00 81.90 ? 2159 HOH A O 1 HETATM 2939 O O . HOH J 5 . ? 18.801 11.697 12.832 1.00 15.39 ? 2160 HOH A O 1 HETATM 2940 O O . HOH J 5 . ? -13.983 36.524 14.038 1.00 20.68 ? 2161 HOH A O 1 HETATM 2941 O O . HOH J 5 . ? 26.182 12.445 17.144 1.00 36.00 ? 2162 HOH A O 1 HETATM 2942 O O . HOH J 5 . ? 27.070 14.830 17.425 1.00 26.05 ? 2163 HOH A O 1 HETATM 2943 O O . HOH J 5 . ? 28.979 14.780 14.231 1.00 53.98 ? 2164 HOH A O 1 HETATM 2944 O O . HOH J 5 . ? 30.288 12.960 8.210 1.00 40.99 ? 2165 HOH A O 1 HETATM 2945 O O . HOH J 5 . ? -8.235 41.575 16.006 1.00 35.93 ? 2166 HOH A O 1 HETATM 2946 O O . HOH J 5 . ? 28.675 17.170 15.427 1.00 37.51 ? 2167 HOH A O 1 HETATM 2947 O O . HOH J 5 . ? 28.984 26.840 10.549 1.00 22.67 ? 2168 HOH A O 1 HETATM 2948 O O . HOH J 5 . ? 31.582 14.636 10.682 1.00 35.07 ? 2169 HOH A O 1 HETATM 2949 O O . HOH J 5 . ? 30.481 25.349 8.709 1.00 20.56 ? 2170 HOH A O 1 HETATM 2950 O O . HOH J 5 . ? 35.534 16.898 8.741 1.00 92.12 ? 2171 HOH A O 1 HETATM 2951 O O . HOH J 5 . ? -7.101 41.337 11.532 1.00 16.96 ? 2172 HOH A O 1 HETATM 2952 O O . HOH J 5 . ? 32.978 16.342 6.839 1.00 37.24 ? 2173 HOH A O 1 HETATM 2953 O O . HOH J 5 . ? 36.113 21.143 3.654 1.00 21.24 ? 2174 HOH A O 1 HETATM 2954 O O . HOH J 5 . ? -2.693 43.623 19.651 1.00 27.60 ? 2175 HOH A O 1 HETATM 2955 O O . HOH J 5 . ? -5.541 46.822 17.502 1.00 44.96 ? 2176 HOH A O 1 HETATM 2956 O O . HOH J 5 . ? 33.711 21.352 2.177 1.00 24.98 ? 2177 HOH A O 1 HETATM 2957 O O . HOH J 5 . ? 31.249 24.898 -0.807 1.00 15.53 ? 2178 HOH A O 1 HETATM 2958 O O . HOH J 5 . ? 29.445 28.976 6.585 1.00 29.54 ? 2179 HOH A O 1 HETATM 2959 O O . HOH J 5 . ? 33.311 23.828 1.697 1.00 31.33 ? 2180 HOH A O 1 HETATM 2960 O O . HOH J 5 . ? 35.734 24.967 2.540 1.00 40.37 ? 2181 HOH A O 1 HETATM 2961 O O . HOH J 5 . ? 29.583 28.748 -3.074 1.00 30.81 ? 2182 HOH A O 1 HETATM 2962 O O . HOH J 5 . ? 22.831 34.058 -4.647 1.00 31.59 ? 2183 HOH A O 1 HETATM 2963 O O . HOH J 5 . ? 5.865 20.831 5.273 1.00 15.23 ? 2184 HOH A O 1 HETATM 2964 O O . HOH J 5 . ? 18.867 44.736 2.599 1.00 20.88 ? 2185 HOH A O 1 HETATM 2965 O O . HOH J 5 . ? 16.288 44.594 -3.725 1.00 40.65 ? 2186 HOH A O 1 HETATM 2966 O O . HOH J 5 . ? 15.467 42.121 -3.869 1.00 32.68 ? 2187 HOH A O 1 HETATM 2967 O O . HOH J 5 . ? 10.202 43.919 -4.065 1.00 16.23 ? 2188 HOH A O 1 HETATM 2968 O O . HOH J 5 . ? 14.043 45.992 -2.951 1.00 31.52 ? 2189 HOH A O 1 HETATM 2969 O O . HOH J 5 . ? 14.436 41.572 -6.367 1.00 34.52 ? 2190 HOH A O 1 HETATM 2970 O O . HOH J 5 . ? 18.878 38.221 -7.576 1.00 42.55 ? 2191 HOH A O 1 HETATM 2971 O O . HOH J 5 . ? -2.917 6.068 29.742 1.00 62.22 ? 2192 HOH A O 1 HETATM 2972 O O . HOH J 5 . ? 6.279 22.197 -4.718 1.00 17.45 ? 2193 HOH A O 1 HETATM 2973 O O . HOH J 5 . ? 9.237 19.960 -3.756 1.00 31.42 ? 2194 HOH A O 1 HETATM 2974 O O . HOH J 5 . ? 10.763 20.867 -2.292 1.00 29.64 ? 2195 HOH A O 1 HETATM 2975 O O . HOH J 5 . ? 13.855 22.617 3.482 1.00 5.90 ? 2196 HOH A O 1 HETATM 2976 O O . HOH J 5 . ? 14.612 26.568 -0.500 1.00 6.27 ? 2197 HOH A O 1 HETATM 2977 O O . HOH J 5 . ? 11.736 18.359 -2.944 1.00 25.36 ? 2198 HOH A O 1 HETATM 2978 O O . HOH J 5 . ? 21.380 17.631 -7.222 1.00 26.40 ? 2199 HOH A O 1 HETATM 2979 O O . HOH J 5 . ? 15.199 15.685 -1.937 1.00 18.43 ? 2200 HOH A O 1 HETATM 2980 O O . HOH J 5 . ? 14.501 16.195 -5.861 1.00 17.41 ? 2201 HOH A O 1 HETATM 2981 O O . HOH J 5 . ? 6.976 10.244 16.797 1.00 34.19 ? 2202 HOH A O 1 HETATM 2982 O O . HOH J 5 . ? 9.197 8.655 16.859 1.00 52.41 ? 2203 HOH A O 1 HETATM 2983 O O . HOH J 5 . ? 19.397 7.850 20.502 1.00 17.70 ? 2204 HOH A O 1 HETATM 2984 O O . HOH J 5 . ? 22.374 7.771 19.604 1.00 41.49 ? 2205 HOH A O 1 HETATM 2985 O O . HOH J 5 . ? 22.737 7.124 16.901 1.00 54.98 ? 2206 HOH A O 1 HETATM 2986 O O . HOH J 5 . ? 16.829 11.122 11.130 1.00 27.15 ? 2207 HOH A O 1 HETATM 2987 O O . HOH J 5 . ? 18.651 16.846 -12.488 1.00 52.23 ? 2208 HOH A O 1 HETATM 2988 O O . HOH J 5 . ? 17.832 14.166 -13.708 1.00 82.50 ? 2209 HOH A O 1 HETATM 2989 O O . HOH J 5 . ? 11.681 17.842 -7.853 1.00 21.60 ? 2210 HOH A O 1 HETATM 2990 O O . HOH J 5 . ? 27.748 13.084 21.258 1.00 32.32 ? 2211 HOH A O 1 HETATM 2991 O O . HOH J 5 . ? 29.871 17.019 20.163 1.00 56.66 ? 2212 HOH A O 1 HETATM 2992 O O . HOH J 5 . ? 11.115 16.063 -11.793 1.00 41.85 ? 2213 HOH A O 1 HETATM 2993 O O . HOH J 5 . ? 17.880 26.176 -14.079 1.00 69.43 ? 2214 HOH A O 1 HETATM 2994 O O . HOH J 5 . ? 14.356 17.334 -13.887 1.00 34.63 ? 2215 HOH A O 1 HETATM 2995 O O . HOH J 5 . ? 11.831 23.931 -16.303 1.00 58.82 ? 2216 HOH A O 1 HETATM 2996 O O . HOH J 5 . ? 25.287 27.539 26.580 1.00 27.17 ? 2217 HOH A O 1 HETATM 2997 O O . HOH J 5 . ? 29.493 21.543 17.515 1.00 13.28 ? 2218 HOH A O 1 HETATM 2998 O O . HOH J 5 . ? 32.105 22.481 20.275 1.00 28.29 ? 2219 HOH A O 1 HETATM 2999 O O . HOH J 5 . ? 32.335 23.022 24.785 1.00 32.66 ? 2220 HOH A O 1 HETATM 3000 O O . HOH J 5 . ? 32.648 25.527 21.254 1.00 25.68 ? 2221 HOH A O 1 HETATM 3001 O O . HOH J 5 . ? 31.067 27.239 25.009 1.00 56.25 ? 2222 HOH A O 1 HETATM 3002 O O . HOH J 5 . ? 12.145 18.827 -15.429 1.00 39.06 ? 2223 HOH A O 1 HETATM 3003 O O . HOH J 5 . ? 11.242 22.994 -13.729 1.00 16.54 ? 2224 HOH A O 1 HETATM 3004 O O . HOH J 5 . ? 28.299 31.789 23.174 1.00 28.28 ? 2225 HOH A O 1 HETATM 3005 O O . HOH J 5 . ? 25.146 29.965 25.499 1.00 34.96 ? 2226 HOH A O 1 HETATM 3006 O O . HOH J 5 . ? 4.293 17.478 -11.770 1.00 20.24 ? 2227 HOH A O 1 HETATM 3007 O O . HOH J 5 . ? 7.041 18.006 -9.992 1.00 24.41 ? 2228 HOH A O 1 HETATM 3008 O O . HOH J 5 . ? 3.574 21.349 -14.433 1.00 14.73 ? 2229 HOH A O 1 HETATM 3009 O O . HOH J 5 . ? 30.702 33.905 12.182 1.00 27.37 ? 2230 HOH A O 1 HETATM 3010 O O . HOH J 5 . ? 9.129 26.130 -16.840 1.00 59.27 ? 2231 HOH A O 1 HETATM 3011 O O . HOH J 5 . ? 4.754 28.559 -12.618 1.00 22.08 ? 2232 HOH A O 1 HETATM 3012 O O . HOH J 5 . ? 27.724 41.790 13.245 1.00 66.33 ? 2233 HOH A O 1 HETATM 3013 O O . HOH J 5 . ? 24.141 40.014 17.205 1.00 55.55 ? 2234 HOH A O 1 HETATM 3014 O O . HOH J 5 . ? 24.268 43.076 14.532 1.00 44.57 ? 2235 HOH A O 1 HETATM 3015 O O . HOH J 5 . ? 30.362 37.562 20.234 1.00 63.44 ? 2236 HOH A O 1 HETATM 3016 O O . HOH J 5 . ? 9.206 24.747 -13.235 1.00 17.41 ? 2237 HOH A O 1 HETATM 3017 O O . HOH J 5 . ? 4.197 23.564 -7.703 1.00 16.04 ? 2238 HOH A O 1 HETATM 3018 O O . HOH J 5 . ? 28.748 39.235 12.759 1.00 31.84 ? 2239 HOH A O 1 HETATM 3019 O O . HOH J 5 . ? 19.478 44.078 15.529 1.00 23.72 ? 2240 HOH A O 1 HETATM 3020 O O . HOH J 5 . ? 23.121 46.623 14.101 1.00 31.12 ? 2241 HOH A O 1 HETATM 3021 O O . HOH J 5 . ? 26.517 44.464 12.299 1.00 34.22 ? 2242 HOH A O 1 HETATM 3022 O O . HOH J 5 . ? 9.723 21.564 -5.955 1.00 30.02 ? 2243 HOH A O 1 HETATM 3023 O O . HOH J 5 . ? 7.436 21.623 -6.774 1.00 26.74 ? 2244 HOH A O 1 HETATM 3024 O O . HOH J 5 . ? 14.738 47.618 16.494 1.00 37.51 ? 2245 HOH A O 1 HETATM 3025 O O . HOH J 5 . ? 20.489 47.781 17.576 1.00 64.86 ? 2246 HOH A O 1 HETATM 3026 O O . HOH J 5 . ? 17.932 49.116 18.328 1.00 40.96 ? 2247 HOH A O 1 HETATM 3027 O O . HOH J 5 . ? 18.317 52.107 11.008 1.00 39.23 ? 2248 HOH A O 1 HETATM 3028 O O . HOH J 5 . ? 22.376 22.354 -12.336 1.00 44.73 ? 2249 HOH A O 1 HETATM 3029 O O . HOH J 5 . ? 18.043 19.103 -13.817 1.00 62.14 ? 2250 HOH A O 1 HETATM 3030 O O . HOH J 5 . ? 21.330 17.802 -10.517 1.00 69.35 ? 2251 HOH A O 1 HETATM 3031 O O . HOH J 5 . ? 23.286 19.968 -11.378 1.00 46.26 ? 2252 HOH A O 1 HETATM 3032 O O . HOH J 5 . ? 15.123 25.474 33.747 1.00 18.35 ? 2253 HOH A O 1 HETATM 3033 O O . HOH J 5 . ? 2.913 18.326 35.919 1.00 71.40 ? 2254 HOH A O 1 HETATM 3034 O O . HOH J 5 . ? 3.407 20.854 35.206 1.00 31.58 ? 2255 HOH A O 1 HETATM 3035 O O . HOH J 5 . ? 8.005 26.221 36.233 1.00 19.98 ? 2256 HOH A O 1 HETATM 3036 O O . HOH J 5 . ? 30.429 21.145 -3.138 1.00 20.34 ? 2257 HOH A O 1 HETATM 3037 O O . HOH J 5 . ? 25.185 16.374 -5.810 1.00 23.88 ? 2258 HOH A O 1 HETATM 3038 O O . HOH J 5 . ? 25.720 22.363 -11.166 1.00 51.42 ? 2259 HOH A O 1 HETATM 3039 O O . HOH J 5 . ? 14.619 14.561 33.433 1.00 47.79 ? 2260 HOH A O 1 HETATM 3040 O O . HOH J 5 . ? 26.343 27.415 -8.742 1.00 34.67 ? 2261 HOH A O 1 HETATM 3041 O O . HOH J 5 . ? 26.584 24.273 -3.722 1.00 17.69 ? 2262 HOH A O 1 HETATM 3042 O O . HOH J 5 . ? 26.578 26.810 -5.256 1.00 36.06 ? 2263 HOH A O 1 HETATM 3043 O O . HOH J 5 . ? 13.909 10.294 14.883 1.00 27.68 ? 2264 HOH A O 1 HETATM 3044 O O . HOH J 5 . ? 11.932 8.678 16.112 1.00 60.17 ? 2265 HOH A O 1 HETATM 3045 O O . HOH J 5 . ? 22.242 23.595 -9.685 1.00 15.10 ? 2266 HOH A O 1 HETATM 3046 O O . HOH J 5 . ? 20.503 25.294 -12.910 1.00 39.06 ? 2267 HOH A O 1 HETATM 3047 O O . HOH J 5 . ? 23.632 28.092 -11.214 1.00 51.86 ? 2268 HOH A O 1 HETATM 3048 O O . HOH J 5 . ? 17.788 26.007 33.798 1.00 51.54 ? 2269 HOH A O 1 HETATM 3049 O O . HOH J 5 . ? 20.019 33.600 -8.001 1.00 21.09 ? 2270 HOH A O 1 HETATM 3050 O O . HOH J 5 . ? 22.059 30.755 -8.083 1.00 21.57 ? 2271 HOH A O 1 HETATM 3051 O O . HOH J 5 . ? 14.195 28.159 33.439 1.00 20.96 ? 2272 HOH A O 1 HETATM 3052 O O . HOH J 5 . ? 15.282 36.400 -12.130 1.00 55.82 ? 2273 HOH A O 1 HETATM 3053 O O . HOH J 5 . ? 16.756 32.453 -11.344 1.00 25.20 ? 2274 HOH A O 1 HETATM 3054 O O . HOH J 5 . ? 18.979 35.631 -9.739 1.00 39.55 ? 2275 HOH A O 1 HETATM 3055 O O . HOH J 5 . ? 13.153 38.321 -9.002 1.00 21.01 ? 2276 HOH A O 1 HETATM 3056 O O . HOH J 5 . ? 22.605 42.403 18.480 1.00 30.36 ? 2277 HOH A O 1 HETATM 3057 O O . HOH J 5 . ? 27.146 35.017 24.275 1.00 52.62 ? 2278 HOH A O 1 HETATM 3058 O O . HOH J 5 . ? 16.369 44.095 18.295 1.00 43.23 ? 2279 HOH A O 1 HETATM 3059 O O . HOH J 5 . ? 5.213 34.436 -10.843 1.00 24.23 ? 2280 HOH A O 1 HETATM 3060 O O . HOH J 5 . ? 4.644 30.559 -10.669 1.00 23.38 ? 2281 HOH A O 1 HETATM 3061 O O . HOH J 5 . ? 11.230 34.090 -15.107 1.00 34.54 ? 2282 HOH A O 1 HETATM 3062 O O . HOH J 5 . ? 12.588 26.550 -14.029 1.00 25.78 ? 2283 HOH A O 1 HETATM 3063 O O . HOH J 5 . ? 5.912 38.250 -7.674 1.00 14.14 ? 2284 HOH A O 1 HETATM 3064 O O . HOH J 5 . ? 5.677 37.250 -10.434 1.00 17.03 ? 2285 HOH A O 1 HETATM 3065 O O . HOH J 5 . ? 7.923 8.350 23.792 1.00 39.39 ? 2286 HOH A O 1 HETATM 3066 O O . HOH J 5 . ? -1.942 8.854 27.352 1.00 62.19 ? 2287 HOH A O 1 HETATM 3067 O O . HOH J 5 . ? -0.728 9.532 30.296 1.00 49.35 ? 2288 HOH A O 1 HETATM 3068 O O . HOH J 5 . ? 7.793 40.389 -7.132 1.00 18.29 ? 2289 HOH A O 1 HETATM 3069 O O . HOH J 5 . ? 1.263 29.229 35.845 1.00 29.74 ? 2290 HOH A O 1 HETATM 3070 O O . HOH J 5 . ? 4.548 28.481 36.948 1.00 36.02 ? 2291 HOH A O 1 HETATM 3071 O O . HOH J 5 . ? -0.358 39.138 -3.727 1.00 10.93 ? 2292 HOH A O 1 HETATM 3072 O O . HOH J 5 . ? 3.327 37.809 -11.634 1.00 24.15 ? 2293 HOH A O 1 HETATM 3073 O O . HOH J 5 . ? 10.636 30.455 36.903 1.00 31.27 ? 2294 HOH A O 1 HETATM 3074 O O . HOH J 5 . ? 6.717 32.621 36.099 1.00 18.89 ? 2295 HOH A O 1 HETATM 3075 O O . HOH J 5 . ? 12.487 28.874 36.699 1.00 34.64 ? 2296 HOH A O 1 HETATM 3076 O O . HOH J 5 . ? 1.153 40.599 -5.605 1.00 19.76 ? 2297 HOH A O 1 HETATM 3077 O O . HOH J 5 . ? 19.638 34.509 31.015 1.00 20.02 ? 2298 HOH A O 1 HETATM 3078 O O . HOH J 5 . ? 19.337 35.319 35.869 1.00 45.18 ? 2299 HOH A O 1 HETATM 3079 O O . HOH J 5 . ? 0.534 47.496 5.877 1.00 23.45 ? 2300 HOH A O 1 HETATM 3080 O O . HOH J 5 . ? 2.111 45.404 -1.409 1.00 9.09 ? 2301 HOH A O 1 HETATM 3081 O O . HOH J 5 . ? -6.783 46.010 3.526 1.00 24.04 ? 2302 HOH A O 1 HETATM 3082 O O . HOH J 5 . ? -2.843 42.244 -4.830 1.00 9.80 ? 2303 HOH A O 1 HETATM 3083 O O . HOH J 5 . ? -0.269 43.052 -5.661 1.00 15.75 ? 2304 HOH A O 1 HETATM 3084 O O . HOH J 5 . ? -3.911 46.236 -4.325 1.00 18.35 ? 2305 HOH A O 1 HETATM 3085 O O . HOH J 5 . ? -13.342 16.246 13.274 1.00 52.40 ? 2306 HOH A O 1 HETATM 3086 O O . HOH J 5 . ? -11.821 18.172 11.936 1.00 29.64 ? 2307 HOH A O 1 HETATM 3087 O O . HOH J 5 . ? -14.249 13.885 24.223 1.00 63.61 ? 2308 HOH A O 1 HETATM 3088 O O . HOH J 5 . ? -7.913 41.267 -1.745 1.00 14.26 ? 2309 HOH A O 1 HETATM 3089 O O . HOH J 5 . ? -17.053 21.915 23.126 1.00 30.38 ? 2310 HOH A O 1 HETATM 3090 O O . HOH J 5 . ? -13.895 24.425 26.352 1.00 48.70 ? 2311 HOH A O 1 HETATM 3091 O O . HOH J 5 . ? -16.213 25.769 22.890 1.00 15.60 ? 2312 HOH A O 1 HETATM 3092 O O . HOH J 5 . ? -16.401 19.858 26.568 1.00 58.07 ? 2313 HOH A O 1 HETATM 3093 O O . HOH J 5 . ? -11.687 19.018 28.108 1.00 38.12 ? 2314 HOH A O 1 HETATM 3094 O O . HOH J 5 . ? -1.116 42.738 11.936 1.00 13.29 ? 2315 HOH A O 1 HETATM 3095 O O . HOH J 5 . ? -3.664 49.530 4.860 1.00 22.79 ? 2316 HOH A O 1 HETATM 3096 O O . HOH J 5 . ? -13.503 29.393 23.731 1.00 31.74 ? 2317 HOH A O 1 HETATM 3097 O O . HOH J 5 . ? -8.011 23.720 31.923 1.00 34.90 ? 2318 HOH A O 1 HETATM 3098 O O . HOH J 5 . ? -10.966 26.172 29.909 1.00 23.66 ? 2319 HOH A O 1 HETATM 3099 O O . HOH J 5 . ? 1.718 44.630 7.783 1.00 11.85 ? 2320 HOH A O 1 HETATM 3100 O O . HOH J 5 . ? -13.881 29.771 29.274 1.00 58.10 ? 2321 HOH A O 1 HETATM 3101 O O . HOH J 5 . ? -13.534 32.476 26.931 1.00 36.14 ? 2322 HOH A O 1 HETATM 3102 O O . HOH J 5 . ? -10.439 33.843 28.947 1.00 28.58 ? 2323 HOH A O 1 HETATM 3103 O O . HOH J 5 . ? -6.548 38.278 31.345 1.00 75.46 ? 2324 HOH A O 1 HETATM 3104 O O . HOH J 5 . ? -0.675 38.991 29.498 1.00 25.45 ? 2325 HOH A O 1 HETATM 3105 O O . HOH J 5 . ? 2.804 33.062 36.583 1.00 29.02 ? 2326 HOH A O 1 HETATM 3106 O O . HOH J 5 . ? -15.610 30.826 -2.294 1.00 35.52 ? 2327 HOH A O 1 HETATM 3107 O O . HOH J 5 . ? -12.825 34.093 -3.865 1.00 34.47 ? 2328 HOH A O 1 HETATM 3108 O O . HOH J 5 . ? 16.557 15.621 9.955 1.00 6.97 ? 2329 HOH A O 1 HETATM 3109 O O . HOH J 5 . ? 14.982 15.860 6.297 1.00 7.21 ? 2330 HOH A O 1 HETATM 3110 O O . HOH J 5 . ? 15.341 14.366 13.709 1.00 10.32 ? 2331 HOH A O 1 HETATM 3111 O O . HOH J 5 . ? -9.462 27.998 -13.891 1.00 37.27 ? 2332 HOH A O 1 HETATM 3112 O O . HOH J 5 . ? -14.976 27.781 -13.011 1.00 54.71 ? 2333 HOH A O 1 HETATM 3113 O O . HOH J 5 . ? -14.291 24.839 -16.346 1.00 83.41 ? 2334 HOH A O 1 HETATM 3114 O O . HOH J 5 . ? -13.860 22.943 2.055 1.00 27.40 ? 2335 HOH A O 1 HETATM 3115 O O . HOH J 5 . ? 9.378 12.075 2.620 1.00 14.14 ? 2336 HOH A O 1 HETATM 3116 O O . HOH J 5 . ? 13.878 11.075 4.330 1.00 26.27 ? 2337 HOH A O 1 HETATM 3117 O O . HOH J 5 . ? 11.052 13.235 7.398 1.00 11.32 ? 2338 HOH A O 1 HETATM 3118 O O . HOH J 5 . ? 10.160 15.026 0.007 1.00 34.90 ? 2339 HOH A O 1 HETATM 3119 O O . HOH J 5 . ? 4.155 16.161 6.938 1.00 12.67 ? 2340 HOH A O 1 HETATM 3120 O O . HOH J 5 . ? 7.192 18.884 7.716 1.00 14.23 ? 2341 HOH A O 1 HETATM 3121 O O . HOH J 5 . ? 5.220 16.212 1.844 1.00 14.49 ? 2342 HOH A O 1 HETATM 3122 O O . HOH J 5 . ? -11.822 14.900 4.883 1.00 29.86 ? 2343 HOH A O 1 HETATM 3123 O O . HOH J 5 . ? -19.686 39.481 4.885 1.00 50.48 ? 2344 HOH A O 1 HETATM 3124 O O . HOH J 5 . ? 8.748 17.118 -1.344 1.00 33.16 ? 2345 HOH A O 1 HETATM 3125 O O . HOH J 5 . ? 2.137 21.349 -2.717 1.00 14.52 ? 2346 HOH A O 1 HETATM 3126 O O . HOH J 5 . ? 6.723 17.619 0.077 1.00 16.86 ? 2347 HOH A O 1 HETATM 3127 O O . HOH J 5 . ? -14.012 19.578 9.442 1.00 32.48 ? 2348 HOH A O 1 HETATM 3128 O O . HOH J 5 . ? -19.523 35.510 10.248 1.00 35.82 ? 2349 HOH A O 1 HETATM 3129 O O . HOH J 5 . ? 14.410 15.121 0.689 1.00 9.35 ? 2350 HOH A O 1 HETATM 3130 O O . HOH J 5 . ? -18.124 19.852 13.987 1.00 42.63 ? 2351 HOH A O 1 HETATM 3131 O O . HOH J 5 . ? 16.117 9.405 3.467 1.00 50.95 ? 2352 HOH A O 1 HETATM 3132 O O . HOH J 5 . ? 16.163 11.351 -0.016 1.00 39.34 ? 2353 HOH A O 1 HETATM 3133 O O . HOH J 5 . ? 18.947 12.760 5.841 1.00 13.61 ? 2354 HOH A O 1 HETATM 3134 O O . HOH J 5 . ? -18.024 34.006 22.776 1.00 67.51 ? 2355 HOH A O 1 HETATM 3135 O O . HOH J 5 . ? -8.521 37.638 29.542 1.00 62.56 ? 2356 HOH A O 1 HETATM 3136 O O . HOH J 5 . ? 24.560 18.017 4.297 1.00 23.56 ? 2357 HOH A O 1 HETATM 3137 O O . HOH J 5 . ? 16.972 25.629 2.874 1.00 6.25 ? 2358 HOH A O 1 HETATM 3138 O O . HOH J 5 . ? 22.461 10.035 -1.113 1.00 30.60 ? 2359 HOH A O 1 HETATM 3139 O O . HOH J 5 . ? 19.404 10.281 1.856 1.00 22.09 ? 2360 HOH A O 1 HETATM 3140 O O . HOH J 5 . ? 28.796 14.757 -2.085 1.00 12.01 ? 2361 HOH A O 1 HETATM 3141 O O . HOH J 5 . ? 30.712 18.009 1.174 1.00 19.68 ? 2362 HOH A O 1 HETATM 3142 O O . HOH J 5 . ? 30.974 15.140 3.330 1.00 28.66 ? 2363 HOH A O 1 HETATM 3143 O O . HOH J 5 . ? 25.441 16.276 6.564 1.00 9.62 ? 2364 HOH A O 1 HETATM 3144 O O . HOH J 5 . ? 25.865 10.337 2.943 1.00 19.76 ? 2365 HOH A O 1 HETATM 3145 O O . HOH J 5 . ? 30.098 11.641 3.511 1.00 21.06 ? 2366 HOH A O 1 HETATM 3146 O O . HOH J 5 . ? 22.924 9.646 5.310 1.00 24.20 ? 2367 HOH A O 1 HETATM 3147 O O . HOH J 5 . ? 25.612 7.660 8.460 1.00 34.37 ? 2368 HOH A O 1 HETATM 3148 O O . HOH J 5 . ? 20.683 10.926 7.224 1.00 20.02 ? 2369 HOH A O 1 HETATM 3149 O O . HOH J 5 . ? 18.412 16.443 12.018 1.00 9.15 ? 2370 HOH A O 1 HETATM 3150 O O . HOH J 5 . ? 21.245 10.635 10.839 1.00 37.41 ? 2371 HOH A O 1 HETATM 3151 O O . HOH J 5 . ? 26.633 13.212 14.591 1.00 25.39 ? 2372 HOH A O 1 HETATM 3152 O O . HOH J 5 . ? 26.330 16.183 15.276 1.00 39.92 ? 2373 HOH A O 1 HETATM 3153 O O . HOH J 5 . ? 29.089 15.950 7.563 1.00 20.00 ? 2374 HOH A O 1 HETATM 3154 O O . HOH J 5 . ? 28.422 24.944 12.625 1.00 28.05 ? 2375 HOH A O 1 HETATM 3155 O O . HOH J 5 . ? 27.059 18.334 13.603 1.00 25.43 ? 2376 HOH A O 1 HETATM 3156 O O . HOH J 5 . ? 33.068 18.893 9.724 1.00 29.10 ? 2377 HOH A O 1 HETATM 3157 O O . HOH J 5 . ? 30.431 17.416 9.908 1.00 19.90 ? 2378 HOH A O 1 HETATM 3158 O O . HOH J 5 . ? 32.184 23.012 9.463 1.00 10.21 ? 2379 HOH A O 1 HETATM 3159 O O . HOH J 5 . ? 35.182 20.496 6.251 1.00 24.38 ? 2380 HOH A O 1 HETATM 3160 O O . HOH J 5 . ? 32.502 19.129 6.308 1.00 23.42 ? 2381 HOH A O 1 HETATM 3161 O O . HOH J 5 . ? 28.545 24.746 -0.672 1.00 11.44 ? 2382 HOH A O 1 HETATM 3162 O O . HOH J 5 . ? 31.843 19.821 3.458 1.00 13.45 ? 2383 HOH A O 1 HETATM 3163 O O . HOH J 5 . ? 26.480 27.996 9.829 1.00 14.27 ? 2384 HOH A O 1 HETATM 3164 O O . HOH J 5 . ? 32.471 29.235 3.543 1.00 31.75 ? 2385 HOH A O 1 HETATM 3165 O O . HOH J 5 . ? 27.951 31.515 2.534 1.00 10.32 ? 2386 HOH A O 1 HETATM 3166 O O . HOH J 5 . ? 32.463 26.142 1.564 1.00 40.25 ? 2387 HOH A O 1 HETATM 3167 O O . HOH J 5 . ? 31.093 26.648 6.136 1.00 22.32 ? 2388 HOH A O 1 HETATM 3168 O O . HOH J 5 . ? 23.619 29.316 -5.194 1.00 16.70 ? 2389 HOH A O 1 HETATM 3169 O O . HOH J 5 . ? 27.763 27.390 -1.517 1.00 15.60 ? 2390 HOH A O 1 HETATM 3170 O O . HOH J 5 . ? 23.307 31.949 -6.172 1.00 33.90 ? 2391 HOH A O 1 HETATM 3171 O O . HOH J 5 . ? 26.469 34.533 -6.043 1.00 52.04 ? 2392 HOH A O 1 HETATM 3172 O O . HOH J 5 . ? 26.557 29.099 -4.508 1.00 33.88 ? 2393 HOH A O 1 HETATM 3173 O O . HOH J 5 . ? 26.184 34.961 -3.068 1.00 77.13 ? 2394 HOH A O 1 HETATM 3174 O O . HOH J 5 . ? 23.057 34.642 -1.868 1.00 14.66 ? 2395 HOH A O 1 HETATM 3175 O O . HOH J 5 . ? 5.273 6.366 13.787 1.00 29.85 ? 2396 HOH A O 1 HETATM 3176 O O . HOH J 5 . ? 25.716 35.268 0.005 1.00 20.41 ? 2397 HOH A O 1 HETATM 3177 O O . HOH J 5 . ? 26.896 38.434 -0.852 1.00 14.17 ? 2398 HOH A O 1 HETATM 3178 O O . HOH J 5 . ? 17.033 37.480 -3.848 1.00 12.53 ? 2399 HOH A O 1 HETATM 3179 O O . HOH J 5 . ? 17.647 40.341 -3.351 1.00 22.92 ? 2400 HOH A O 1 HETATM 3180 O O . HOH J 5 . ? 16.425 45.223 1.437 1.00 19.33 ? 2401 HOH A O 1 HETATM 3181 O O . HOH J 5 . ? 18.219 43.784 -1.889 1.00 27.68 ? 2402 HOH A O 1 HETATM 3182 O O . HOH J 5 . ? 28.393 10.841 18.705 1.00 63.39 ? 2403 HOH A O 1 HETATM 3183 O O . HOH J 5 . ? 17.749 56.682 1.015 1.00 52.59 ? 2404 HOH A O 1 HETATM 3184 O O . HOH J 5 . ? 15.926 39.125 -7.892 1.00 24.57 ? 2405 HOH A O 1 HETATM 3185 O O . HOH J 5 . ? 11.937 44.806 -1.854 1.00 13.83 ? 2406 HOH A O 1 HETATM 3186 O O . HOH J 5 . ? -4.187 8.706 28.838 1.00 66.00 ? 2407 HOH A O 1 HETATM 3187 O O . HOH J 5 . ? -19.898 31.217 -1.587 1.00 61.26 ? 2408 HOH A O 1 HETATM 3188 O O . HOH J 5 . ? 18.397 46.706 4.078 1.00 34.30 ? 2409 HOH A O 1 HETATM 3189 O O . HOH J 5 . ? 16.787 48.239 0.412 1.00 21.18 ? 2410 HOH A O 1 HETATM 3190 O O . HOH J 5 . ? 3.212 46.481 6.162 1.00 22.46 ? 2411 HOH A O 1 HETATM 3191 O O . HOH J 5 . ? 7.881 44.401 10.683 1.00 8.78 ? 2412 HOH A O 1 HETATM 3192 O O . HOH J 5 . ? 10.276 42.336 13.451 1.00 8.40 ? 2413 HOH A O 1 HETATM 3193 O O . HOH J 5 . ? 10.148 11.366 18.201 1.00 25.97 ? 2414 HOH A O 1 HETATM 3194 O O . HOH J 5 . ? 7.149 13.399 17.300 1.00 4.34 ? 2415 HOH A O 1 HETATM 3195 O O . HOH J 5 . ? 23.839 11.251 17.510 1.00 18.32 ? 2416 HOH A O 1 HETATM 3196 O O . HOH J 5 . ? 18.292 14.236 14.015 1.00 6.74 ? 2417 HOH A O 1 HETATM 3197 O O . HOH J 5 . ? 16.761 9.272 14.102 1.00 63.26 ? 2418 HOH A O 1 HETATM 3198 O O . HOH J 5 . ? 17.171 6.860 17.057 1.00 71.02 ? 2419 HOH A O 1 HETATM 3199 O O . HOH J 5 . ? 20.608 9.363 15.403 1.00 46.68 ? 2420 HOH A O 1 HETATM 3200 O O . HOH J 5 . ? 20.608 8.130 18.029 1.00 34.02 ? 2421 HOH A O 1 HETATM 3201 O O . HOH J 5 . ? 25.660 12.089 22.993 1.00 18.28 ? 2422 HOH A O 1 HETATM 3202 O O . HOH J 5 . ? 24.823 9.645 20.081 1.00 38.59 ? 2423 HOH A O 1 HETATM 3203 O O . HOH J 5 . ? 29.282 19.048 21.833 1.00 34.90 ? 2424 HOH A O 1 HETATM 3204 O O . HOH J 5 . ? 27.119 15.251 19.908 1.00 18.15 ? 2425 HOH A O 1 HETATM 3205 O O . HOH J 5 . ? 24.973 22.131 26.360 1.00 22.45 ? 2426 HOH A O 1 HETATM 3206 O O . HOH J 5 . ? 28.802 24.683 26.899 1.00 74.52 ? 2427 HOH A O 1 HETATM 3207 O O . HOH J 5 . ? 31.024 24.865 23.394 1.00 24.47 ? 2428 HOH A O 1 HETATM 3208 O O . HOH J 5 . ? 29.391 21.313 20.320 1.00 22.16 ? 2429 HOH A O 1 HETATM 3209 O O . HOH J 5 . ? 25.758 24.602 25.736 1.00 23.89 ? 2430 HOH A O 1 HETATM 3210 O O . HOH J 5 . ? 27.644 23.200 16.178 1.00 11.37 ? 2431 HOH A O 1 HETATM 3211 O O . HOH J 5 . ? 28.538 28.775 24.904 1.00 41.49 ? 2432 HOH A O 1 HETATM 3212 O O . HOH J 5 . ? 30.073 30.422 21.503 1.00 33.33 ? 2433 HOH A O 1 HETATM 3213 O O . HOH J 5 . ? 32.129 27.304 19.082 1.00 18.83 ? 2434 HOH A O 1 HETATM 3214 O O . HOH J 5 . ? 25.596 31.392 22.978 1.00 14.59 ? 2435 HOH A O 1 HETATM 3215 O O . HOH J 5 . ? 28.069 34.280 12.116 1.00 13.62 ? 2436 HOH A O 1 HETATM 3216 O O . HOH J 5 . ? 30.025 34.871 20.028 1.00 31.42 ? 2437 HOH A O 1 HETATM 3217 O O . HOH J 5 . ? 29.797 32.890 16.833 1.00 31.89 ? 2438 HOH A O 1 HETATM 3218 O O . HOH J 5 . ? 25.264 40.457 14.331 1.00 21.23 ? 2439 HOH A O 1 HETATM 3219 O O . HOH J 5 . ? 27.123 38.062 3.535 1.00 18.10 ? 2440 HOH A O 1 HETATM 3220 O O . HOH J 5 . ? 27.864 37.085 11.408 1.00 13.80 ? 2441 HOH A O 1 HETATM 3221 O O . HOH J 5 . ? 26.459 33.997 2.642 1.00 15.91 ? 2442 HOH A O 1 HETATM 3222 O O . HOH J 5 . ? 19.688 43.327 18.047 1.00 23.85 ? 2443 HOH A O 1 HETATM 3223 O O . HOH J 5 . ? 21.640 44.174 13.913 1.00 23.66 ? 2444 HOH A O 1 HETATM 3224 O O . HOH J 5 . ? 28.022 39.391 7.714 1.00 31.53 ? 2445 HOH A O 1 HETATM 3225 O O . HOH J 5 . ? 26.646 44.017 9.124 1.00 23.24 ? 2446 HOH A O 1 HETATM 3226 O O . HOH J 5 . ? 19.989 42.364 3.642 1.00 9.67 ? 2447 HOH A O 1 HETATM 3227 O O . HOH J 5 . ? 17.695 42.652 13.951 1.00 26.17 ? 2448 HOH A O 1 HETATM 3228 O O . HOH J 5 . ? 16.680 40.497 11.533 1.00 13.31 ? 2449 HOH A O 1 HETATM 3229 O O . HOH J 5 . ? 20.855 49.838 11.928 1.00 37.22 ? 2450 HOH A O 1 HETATM 3230 O O . HOH J 5 . ? 17.214 49.514 13.120 1.00 33.53 ? 2451 HOH A O 1 HETATM 3231 O O . HOH J 5 . ? 18.006 46.401 16.154 1.00 33.94 ? 2452 HOH A O 1 HETATM 3232 O O . HOH J 5 . ? 15.740 51.391 9.440 1.00 21.41 ? 2453 HOH A O 1 HETATM 3233 O O . HOH J 5 . ? 14.604 49.906 12.625 1.00 18.14 ? 2454 HOH A O 1 HETATM 3234 O O . HOH J 5 . ? 13.014 48.216 14.291 1.00 14.74 ? 2455 HOH A O 1 HETATM 3235 O O . HOH J 5 . ? 15.489 44.218 15.806 1.00 49.41 ? 2456 HOH A O 1 HETATM 3236 O O . HOH J 5 . ? 14.401 27.211 22.972 1.00 36.91 ? 2457 HOH A O 1 HETATM 3237 O O . HOH J 5 . ? 14.536 23.471 23.016 1.00 8.08 ? 2458 HOH A O 1 HETATM 3238 O O . HOH J 5 . ? 12.848 28.786 21.352 1.00 7.19 ? 2459 HOH A O 1 HETATM 3239 O O . HOH J 5 . ? 12.571 20.840 17.788 1.00 5.92 ? 2460 HOH A O 1 HETATM 3240 O O . HOH J 5 . ? 6.175 18.005 16.759 1.00 8.80 ? 2461 HOH A O 1 HETATM 3241 O O . HOH J 5 . ? 18.170 22.228 33.481 1.00 25.93 ? 2462 HOH A O 1 HETATM 3242 O O . HOH J 5 . ? 15.606 16.771 35.074 1.00 25.14 ? 2463 HOH A O 1 HETATM 3243 O O . HOH J 5 . ? 13.208 16.976 36.615 1.00 25.62 ? 2464 HOH A O 1 HETATM 3244 O O . HOH J 5 . ? 15.629 22.956 32.494 1.00 8.86 ? 2465 HOH A O 1 HETATM 3245 O O . HOH J 5 . ? 9.621 26.327 33.869 1.00 9.94 ? 2466 HOH A O 1 HETATM 3246 O O . HOH J 5 . ? 5.473 20.238 36.799 1.00 43.13 ? 2467 HOH A O 1 HETATM 3247 O O . HOH J 5 . ? 5.464 17.162 38.291 1.00 44.96 ? 2468 HOH A O 1 HETATM 3248 O O . HOH J 5 . ? 10.110 18.654 37.621 1.00 18.57 ? 2469 HOH A O 1 HETATM 3249 O O . HOH J 5 . ? 10.367 17.311 33.598 1.00 12.04 ? 2470 HOH A O 1 HETATM 3250 O O . HOH J 5 . ? 6.613 12.931 37.485 1.00 31.75 ? 2471 HOH A O 1 HETATM 3251 O O . HOH J 5 . ? 2.216 13.920 37.192 1.00 57.11 ? 2472 HOH A O 1 HETATM 3252 O O . HOH J 5 . ? 11.349 15.320 35.562 1.00 21.65 ? 2473 HOH A O 1 HETATM 3253 O O . HOH J 5 . ? 10.314 9.354 30.919 1.00 7.04 ? 2474 HOH A O 1 HETATM 3254 O O . HOH J 5 . ? 15.147 8.586 20.801 1.00 36.17 ? 2475 HOH A O 1 HETATM 3255 O O . HOH J 5 . ? 6.757 9.604 28.063 1.00 17.35 ? 2476 HOH A O 1 HETATM 3256 O O . HOH J 5 . ? 4.030 19.162 33.048 1.00 31.23 ? 2477 HOH A O 1 HETATM 3257 O O . HOH J 5 . ? 13.194 16.654 32.416 1.00 13.85 ? 2478 HOH A O 1 HETATM 3258 O O . HOH J 5 . ? 13.721 14.996 24.113 1.00 17.97 ? 2479 HOH A O 1 HETATM 3259 O O . HOH J 5 . ? 20.032 14.192 22.749 1.00 7.85 ? 2480 HOH A O 1 HETATM 3260 O O . HOH J 5 . ? 18.082 9.770 21.845 1.00 12.65 ? 2481 HOH A O 1 HETATM 3261 O O . HOH J 5 . ? 12.827 9.948 18.357 1.00 32.88 ? 2482 HOH A O 1 HETATM 3262 O O . HOH J 5 . ? 14.252 12.804 15.824 1.00 8.36 ? 2483 HOH A O 1 HETATM 3263 O O . HOH J 5 . ? 22.287 19.537 19.578 1.00 7.48 ? 2484 HOH A O 1 HETATM 3264 O O . HOH J 5 . ? 15.998 17.156 23.745 1.00 9.00 ? 2485 HOH A O 1 HETATM 3265 O O . HOH J 5 . ? 13.016 21.097 20.591 1.00 5.19 ? 2486 HOH A O 1 HETATM 3266 O O . HOH J 5 . ? 19.536 24.287 31.251 1.00 18.26 ? 2487 HOH A O 1 HETATM 3267 O O . HOH J 5 . ? 15.833 23.473 29.674 1.00 9.06 ? 2488 HOH A O 1 HETATM 3268 O O . HOH J 5 . ? 22.254 20.883 28.418 1.00 21.91 ? 2489 HOH A O 1 HETATM 3269 O O . HOH J 5 . ? 22.860 27.891 31.112 1.00 56.83 ? 2490 HOH A O 1 HETATM 3270 O O . HOH J 5 . ? 22.701 29.730 26.411 1.00 21.43 ? 2491 HOH A O 1 HETATM 3271 O O . HOH J 5 . ? 20.084 23.002 22.499 1.00 9.12 ? 2492 HOH A O 1 HETATM 3272 O O . HOH J 5 . ? 20.332 26.996 31.361 1.00 38.32 ? 2493 HOH A O 1 HETATM 3273 O O . HOH J 5 . ? 18.704 28.717 33.338 1.00 36.41 ? 2494 HOH A O 1 HETATM 3274 O O . HOH J 5 . ? 14.956 29.889 31.154 1.00 16.00 ? 2495 HOH A O 1 HETATM 3275 O O . HOH J 5 . ? 22.662 30.026 29.151 1.00 31.09 ? 2496 HOH A O 1 HETATM 3276 O O . HOH J 5 . ? 23.125 34.274 27.812 1.00 26.00 ? 2497 HOH A O 1 HETATM 3277 O O . HOH J 5 . ? 28.639 37.590 23.012 1.00 65.59 ? 2498 HOH A O 1 HETATM 3278 O O . HOH J 5 . ? 18.357 38.596 23.859 1.00 10.10 ? 2499 HOH A O 1 HETATM 3279 O O . HOH J 5 . ? 24.740 34.023 23.418 1.00 24.86 ? 2500 HOH A O 1 HETATM 3280 O O . HOH J 5 . ? 20.594 40.640 20.273 1.00 25.64 ? 2501 HOH A O 1 HETATM 3281 O O . HOH J 5 . ? 24.886 35.708 20.101 1.00 25.12 ? 2502 HOH A O 1 HETATM 3282 O O . HOH J 5 . ? 16.990 40.434 22.476 1.00 20.46 ? 2503 HOH A O 1 HETATM 3283 O O . HOH J 5 . ? 13.382 40.061 24.243 1.00 21.14 ? 2504 HOH A O 1 HETATM 3284 O O . HOH J 5 . ? 16.325 41.847 16.877 1.00 33.72 ? 2505 HOH A O 1 HETATM 3285 O O . HOH J 5 . ? 14.164 31.001 20.046 1.00 7.67 ? 2506 HOH A O 1 HETATM 3286 O O . HOH J 5 . ? -4.123 9.030 22.490 1.00 87.14 ? 2507 HOH A O 1 HETATM 3287 O O . HOH J 5 . ? -2.643 8.645 17.210 1.00 50.42 ? 2508 HOH A O 1 HETATM 3288 O O . HOH J 5 . ? -4.053 12.300 23.384 1.00 29.49 ? 2509 HOH A O 1 HETATM 3289 O O . HOH J 5 . ? -0.615 14.365 16.810 1.00 17.93 ? 2510 HOH A O 1 HETATM 3290 O O . HOH J 5 . ? 6.450 8.955 20.056 1.00 53.39 ? 2511 HOH A O 1 HETATM 3291 O O . HOH J 5 . ? 7.142 11.241 23.225 1.00 44.44 ? 2512 HOH A O 1 HETATM 3292 O O . HOH J 5 . ? 4.595 9.373 26.382 1.00 43.13 ? 2513 HOH A O 1 HETATM 3293 O O . HOH J 5 . ? 0.911 6.888 28.700 1.00 84.16 ? 2514 HOH A O 1 HETATM 3294 O O . HOH J 5 . ? -1.001 7.049 25.423 1.00 73.75 ? 2515 HOH A O 1 HETATM 3295 O O . HOH J 5 . ? 3.469 6.798 26.647 1.00 52.68 ? 2516 HOH A O 1 HETATM 3296 O O . HOH J 5 . ? -1.513 9.579 23.301 1.00 33.52 ? 2517 HOH A O 1 HETATM 3297 O O . HOH J 5 . ? -6.463 11.907 26.030 1.00 39.27 ? 2518 HOH A O 1 HETATM 3298 O O . HOH J 5 . ? -7.018 14.512 28.387 1.00 25.01 ? 2519 HOH A O 1 HETATM 3299 O O . HOH J 5 . ? 2.083 18.796 31.685 1.00 25.28 ? 2520 HOH A O 1 HETATM 3300 O O . HOH J 5 . ? -7.907 20.581 29.088 1.00 21.62 ? 2521 HOH A O 1 HETATM 3301 O O . HOH J 5 . ? -1.594 19.854 32.834 1.00 17.88 ? 2522 HOH A O 1 HETATM 3302 O O . HOH J 5 . ? -3.361 25.903 37.325 1.00 56.82 ? 2523 HOH A O 1 HETATM 3303 O O . HOH J 5 . ? 5.160 26.232 35.664 1.00 33.86 ? 2524 HOH A O 1 HETATM 3304 O O . HOH J 5 . ? 2.414 23.762 35.807 1.00 54.38 ? 2525 HOH A O 1 HETATM 3305 O O . HOH J 5 . ? -1.758 22.517 34.598 1.00 48.83 ? 2526 HOH A O 1 HETATM 3306 O O . HOH J 5 . ? 3.754 29.675 34.267 1.00 11.25 ? 2527 HOH A O 1 HETATM 3307 O O . HOH J 5 . ? 9.462 32.620 35.599 1.00 10.64 ? 2528 HOH A O 1 HETATM 3308 O O . HOH J 5 . ? 11.615 28.049 34.416 1.00 21.10 ? 2529 HOH A O 1 HETATM 3309 O O . HOH J 5 . ? 18.021 34.160 33.423 1.00 34.54 ? 2530 HOH A O 1 HETATM 3310 O O . HOH J 5 . ? 18.302 35.765 28.895 1.00 10.66 ? 2531 HOH A O 1 HETATM 3311 O O . HOH J 5 . ? 11.462 40.833 26.378 1.00 13.93 ? 2532 HOH A O 1 HETATM 3312 O O . HOH J 5 . ? 7.610 37.490 29.123 1.00 21.05 ? 2533 HOH A O 1 HETATM 3313 O O . HOH J 5 . ? 5.524 21.570 10.922 1.00 8.63 ? 2534 HOH A O 1 HETATM 3314 O O . HOH J 5 . ? -1.911 15.636 18.741 1.00 15.70 ? 2535 HOH A O 1 HETATM 3315 O O . HOH J 5 . ? -8.344 17.933 14.001 1.00 20.06 ? 2536 HOH A O 1 HETATM 3316 O O . HOH J 5 . ? -11.627 13.014 13.504 1.00 49.58 ? 2537 HOH A O 1 HETATM 3317 O O . HOH J 5 . ? -4.117 8.043 13.628 1.00 38.79 ? 2538 HOH A O 1 HETATM 3318 O O . HOH J 5 . ? -8.150 12.915 12.262 1.00 50.53 ? 2539 HOH A O 1 HETATM 3319 O O . HOH J 5 . ? -10.586 15.826 13.339 1.00 27.39 ? 2540 HOH A O 1 HETATM 3320 O O . HOH J 5 . ? -7.866 10.497 13.671 1.00 38.10 ? 2541 HOH A O 1 HETATM 3321 O O . HOH J 5 . ? -5.904 9.262 15.166 1.00 41.78 ? 2542 HOH A O 1 HETATM 3322 O O . HOH J 5 . ? -17.323 12.045 19.958 1.00 65.17 ? 2543 HOH A O 1 HETATM 3323 O O . HOH J 5 . ? -11.320 13.099 22.383 1.00 24.86 ? 2544 HOH A O 1 HETATM 3324 O O . HOH J 5 . ? -13.642 10.619 19.940 1.00 50.20 ? 2545 HOH A O 1 HETATM 3325 O O . HOH J 5 . ? -13.095 13.653 15.762 1.00 30.23 ? 2546 HOH A O 1 HETATM 3326 O O . HOH J 5 . ? -14.777 23.474 23.477 1.00 14.98 ? 2547 HOH A O 1 HETATM 3327 O O . HOH J 5 . ? -13.456 21.060 26.747 1.00 24.15 ? 2548 HOH A O 1 HETATM 3328 O O . HOH J 5 . ? -11.825 14.787 25.204 1.00 34.53 ? 2549 HOH A O 1 HETATM 3329 O O . HOH J 5 . ? -9.576 17.700 26.816 1.00 16.56 ? 2550 HOH A O 1 HETATM 3330 O O . HOH J 5 . ? -7.509 19.520 26.492 1.00 14.48 ? 2551 HOH A O 1 HETATM 3331 O O . HOH J 5 . ? -6.323 22.993 15.026 1.00 13.13 ? 2552 HOH A O 1 HETATM 3332 O O . HOH J 5 . ? -10.972 29.255 23.904 1.00 30.73 ? 2553 HOH A O 1 HETATM 3333 O O . HOH J 5 . ? -8.190 26.062 30.343 1.00 16.87 ? 2554 HOH A O 1 HETATM 3334 O O . HOH J 5 . ? -11.665 28.559 21.530 1.00 34.72 ? 2555 HOH A O 1 HETATM 3335 O O . HOH J 5 . ? -10.741 32.206 26.816 1.00 16.10 ? 2556 HOH A O 1 HETATM 3336 O O . HOH J 5 . ? -12.191 27.611 27.767 1.00 41.36 ? 2557 HOH A O 1 HETATM 3337 O O . HOH J 5 . ? -5.228 26.455 32.944 1.00 38.35 ? 2558 HOH A O 1 HETATM 3338 O O . HOH J 5 . ? -4.685 38.282 29.260 1.00 31.28 ? 2559 HOH A O 1 HETATM 3339 O O . HOH J 5 . ? -4.616 29.844 33.794 1.00 36.42 ? 2560 HOH A O 1 HETATM 3340 O O . HOH J 5 . ? -8.756 30.817 33.070 1.00 48.00 ? 2561 HOH A O 1 HETATM 3341 O O . HOH J 5 . ? -0.788 35.937 28.398 1.00 16.86 ? 2562 HOH A O 1 HETATM 3342 O O . HOH J 5 . ? -1.892 29.497 33.936 1.00 22.97 ? 2563 HOH A O 1 HETATM 3343 O O . HOH J 5 . ? -5.524 36.565 33.387 1.00 33.06 ? 2564 HOH A O 1 HETATM 3344 O O . HOH J 5 . ? 4.621 32.307 34.128 1.00 15.29 ? 2565 HOH A O 1 HETATM 3345 O O . HOH J 5 . ? 0.339 33.315 35.172 1.00 19.03 ? 2566 HOH A O 1 HETATM 3346 O O . HOH J 5 . ? 2.980 38.175 29.903 1.00 21.32 ? 2567 HOH A O 1 HETATM 3347 O O . HOH J 5 . ? -4.907 31.099 17.158 1.00 8.77 ? 2568 HOH A O 1 HETATM 3348 O O . HOH J 5 . ? 0.058 25.244 7.787 1.00 5.24 ? 2569 HOH A O 1 HETATM 3349 O O . HOH J 5 . ? -13.670 29.271 1.760 1.00 17.30 ? 2570 HOH A O 1 HETATM 3350 O O . HOH J 5 . ? -12.855 32.231 -1.858 1.00 27.84 ? 2571 HOH A O 1 HETATM 3351 O O . HOH J 5 . ? -15.968 29.575 -10.856 1.00 54.20 ? 2572 HOH A O 1 HETATM 3352 O O . HOH J 5 . ? -6.795 26.928 -12.656 1.00 44.69 ? 2573 HOH A O 1 HETATM 3353 O O . HOH J 5 . ? -13.415 25.212 -12.392 1.00 33.19 ? 2574 HOH A O 1 HETATM 3354 O O . HOH J 5 . ? -14.283 22.271 -0.380 1.00 19.75 ? 2575 HOH A O 1 HETATM 3355 O O . HOH J 5 . ? -13.454 18.009 -1.559 1.00 9.56 ? 2576 HOH A O 1 HETATM 3356 O O . HOH J 5 . ? -5.894 23.413 -5.353 1.00 11.36 ? 2577 HOH A O 1 HETATM 3357 O O . HOH J 5 . ? -6.508 20.460 -3.693 1.00 8.58 ? 2578 HOH A O 1 HETATM 3358 O O . HOH J 5 . ? -0.950 22.949 -4.421 1.00 25.55 ? 2579 HOH A O 1 HETATM 3359 O O . HOH J 5 . ? -3.613 21.280 -3.974 1.00 13.93 ? 2580 HOH A O 1 HETATM 3360 O O . HOH J 5 . ? -2.987 24.953 -1.831 1.00 8.99 ? 2581 HOH A O 1 HETATM 3361 O O . HOH J 5 . ? -8.143 15.530 2.876 1.00 23.88 ? 2582 HOH A O 1 HETATM 3362 O O . HOH J 5 . ? -7.356 19.263 0.135 1.00 9.06 ? 2583 HOH A O 1 HETATM 3363 O O . HOH J 5 . ? 0.280 18.616 6.235 1.00 9.89 ? 2584 HOH A O 1 HETATM 3364 O O . HOH J 5 . ? -9.182 17.930 6.326 1.00 19.74 ? 2585 HOH A O 1 HETATM 3365 O O . HOH J 5 . ? -10.444 16.385 10.102 1.00 32.23 ? 2586 HOH A O 1 HETATM 3366 O O . HOH J 5 . ? 0.131 13.835 12.696 1.00 15.66 ? 2587 HOH A O 1 HETATM 3367 O O . HOH J 5 . ? -8.296 21.057 13.845 1.00 17.54 ? 2588 HOH A O 1 HETATM 3368 O O . HOH J 5 . ? -10.746 20.898 12.405 1.00 15.05 ? 2589 HOH A O 1 HETATM 3369 O O . HOH J 5 . ? -10.472 18.778 8.701 1.00 20.37 ? 2590 HOH A O 1 HETATM 3370 O O . HOH J 5 . ? -5.516 23.077 5.176 1.00 7.27 ? 2591 HOH A O 1 HETATM 3371 O O . HOH J 5 . ? -10.428 28.722 9.330 1.00 8.72 ? 2592 HOH A O 1 HETATM 3372 O O . HOH J 5 . ? -12.636 17.885 5.810 1.00 23.62 ? 2593 HOH A O 1 HETATM 3373 O O . HOH J 5 . ? -17.873 37.245 5.791 1.00 39.28 ? 2594 HOH A O 1 HETATM 3374 O O . HOH J 5 . ? -16.049 36.539 3.946 1.00 26.63 ? 2595 HOH A O 1 HETATM 3375 O O . HOH J 5 . ? -17.406 27.277 5.127 1.00 23.29 ? 2596 HOH A O 1 HETATM 3376 O O . HOH J 5 . ? -13.737 27.077 3.566 1.00 13.94 ? 2597 HOH A O 1 HETATM 3377 O O . HOH J 5 . ? -14.801 36.951 8.721 1.00 21.48 ? 2598 HOH A O 1 HETATM 3378 O O . HOH J 5 . ? -20.435 30.164 9.747 1.00 28.30 ? 2599 HOH A O 1 HETATM 3379 O O . HOH J 5 . ? -17.533 35.093 8.325 1.00 27.19 ? 2600 HOH A O 1 HETATM 3380 O O . HOH J 5 . ? -13.097 22.694 9.904 1.00 9.92 ? 2601 HOH A O 1 HETATM 3381 O O . HOH J 5 . ? -19.166 22.707 17.495 1.00 19.19 ? 2602 HOH A O 1 HETATM 3382 O O . HOH J 5 . ? -19.143 25.564 16.769 1.00 13.65 ? 2603 HOH A O 1 HETATM 3383 O O . HOH J 5 . ? -17.202 21.234 16.213 1.00 31.83 ? 2604 HOH A O 1 HETATM 3384 O O . HOH J 5 . ? -16.123 22.148 11.171 1.00 11.47 ? 2605 HOH A O 1 HETATM 3385 O O . HOH J 5 . ? -20.742 28.578 12.129 1.00 42.18 ? 2606 HOH A O 1 HETATM 3386 O O . HOH J 5 . ? -21.954 25.374 15.214 1.00 22.75 ? 2607 HOH A O 1 HETATM 3387 O O . HOH J 5 . ? -15.170 28.164 21.732 1.00 17.97 ? 2608 HOH A O 1 HETATM 3388 O O . HOH J 5 . ? -7.676 31.670 16.544 1.00 9.85 ? 2609 HOH A O 1 HETATM 3389 O O . HOH J 5 . ? -20.350 31.581 19.063 1.00 22.87 ? 2610 HOH A O 1 HETATM 3390 O O . HOH J 5 . ? -15.429 33.698 23.602 1.00 35.48 ? 2611 HOH A O 1 HETATM 3391 O O . HOH J 5 . ? -10.231 31.789 24.166 1.00 15.37 ? 2612 HOH A O 1 HETATM 3392 O O . HOH J 5 . ? -9.238 40.307 19.339 1.00 22.26 ? 2613 HOH A O 1 HETATM 3393 O O . HOH J 5 . ? -14.807 38.085 16.111 1.00 27.69 ? 2614 HOH A O 1 HETATM 3394 O O . HOH J 5 . ? -18.286 34.379 20.100 1.00 34.69 ? 2615 HOH A O 1 HETATM 3395 O O . HOH J 5 . ? -11.119 36.974 28.041 1.00 32.38 ? 2616 HOH A O 1 HETATM 3396 O O . HOH J 5 . ? -8.490 39.516 27.228 1.00 42.08 ? 2617 HOH A O 1 HETATM 3397 O O . HOH J 5 . ? -6.458 42.974 20.311 1.00 44.83 ? 2618 HOH A O 1 HETATM 3398 O O . HOH J 5 . ? 5.435 14.111 11.684 1.00 46.45 ? 2619 HOH A O 1 HETATM 3399 O O . HOH J 5 . ? 7.708 15.702 15.208 1.00 12.43 ? 2620 HOH A O 1 HETATM 3400 O O . HOH J 5 . ? 4.255 9.202 16.269 1.00 24.87 ? 2621 HOH A O 1 HETATM 3401 O O . HOH J 5 . ? 3.300 7.662 12.477 1.00 16.00 ? 2622 HOH A O 1 HETATM 3402 O O . HOH J 5 . ? -1.463 8.185 13.546 1.00 28.39 ? 2623 HOH A O 1 HETATM 3403 O O . HOH J 5 . ? 0.449 8.608 10.595 1.00 15.13 ? 2624 HOH A O 1 HETATM 3404 O O . HOH J 5 . ? -1.118 11.847 10.886 1.00 20.83 ? 2625 HOH A O 1 HETATM 3405 O O . HOH J 5 . ? 0.573 8.396 16.652 1.00 38.36 ? 2626 HOH A O 1 HETATM 3406 O O . HOH J 5 . ? -14.686 18.134 14.500 1.00 23.56 ? 2627 HOH A O 1 HETATM 3407 O O . HOH J 5 . ? -17.656 20.295 20.868 1.00 47.97 ? 2628 HOH A O 1 HETATM 3408 O O . HOH J 5 . ? 28.810 7.330 9.848 1.00 37.22 ? 2629 HOH A O 1 HETATM 3409 O O . HOH J 5 . ? 29.610 12.517 15.852 1.00 72.00 ? 2630 HOH A O 1 HETATM 3410 O O . HOH J 5 . ? 28.258 11.289 8.857 1.00 31.46 ? 2631 HOH A O 1 HETATM 3411 O O . HOH J 5 . ? 22.910 10.379 13.992 1.00 51.34 ? 2632 HOH A O 1 HETATM 3412 O O . HOH J 5 . ? 26.544 5.625 10.367 1.00 52.04 ? 2633 HOH A O 1 HETATM 3413 O O . HOH J 5 . ? 23.887 3.735 10.801 1.00 63.45 ? 2634 HOH A O 1 HETATM 3414 O O . HOH J 5 . ? 30.728 6.154 14.540 1.00 69.76 ? 2635 HOH A O 1 HETATM 3415 O O . HOH J 5 . ? 22.012 54.037 5.313 1.00 34.86 ? 2636 HOH A O 1 HETATM 3416 O O . HOH J 5 . ? 14.524 55.652 3.546 1.00 11.67 ? 2637 HOH A O 1 HETATM 3417 O O . HOH J 5 . ? 20.649 52.411 9.529 1.00 27.79 ? 2638 HOH A O 1 HETATM 3418 O O . HOH J 5 . ? 17.274 54.957 6.918 1.00 28.16 ? 2639 HOH A O 1 HETATM 3419 O O . HOH J 5 . ? 19.562 54.115 2.879 1.00 27.27 ? 2640 HOH A O 1 HETATM 3420 O O . HOH J 5 . ? 18.662 49.692 1.906 1.00 13.22 ? 2641 HOH A O 1 HETATM 3421 O O . HOH J 5 . ? 19.057 45.552 6.102 1.00 18.89 ? 2642 HOH A O 1 HETATM 3422 O O . HOH J 5 . ? 22.017 50.021 5.124 1.00 29.58 ? 2643 HOH A O 1 HETATM 3423 O O . HOH J 5 . ? -5.231 9.017 32.192 1.00 47.54 ? 2644 HOH A O 1 HETATM 3424 O O . HOH J 5 . ? 0.008 16.783 33.416 1.00 51.21 ? 2645 HOH A O 1 HETATM 3425 O O . HOH J 5 . ? -7.343 9.938 28.853 1.00 36.02 ? 2646 HOH A O 1 HETATM 3426 O O . HOH J 5 . ? -6.193 13.740 38.062 1.00 58.31 ? 2647 HOH A O 1 HETATM 3427 O O . HOH J 5 . ? -0.279 12.309 29.983 1.00 14.37 ? 2648 HOH A O 1 HETATM 3428 O O . HOH J 5 . ? 2.337 12.191 30.763 1.00 25.53 ? 2649 HOH A O 1 HETATM 3429 O O . HOH J 5 . ? -16.970 28.393 1.272 1.00 36.20 ? 2650 HOH A O 1 HETATM 3430 O O . HOH J 5 . ? -21.551 32.447 0.453 1.00 24.81 ? 2651 HOH A O 1 HETATM 3431 O O . HOH J 5 . ? -21.646 37.011 8.652 1.00 27.24 ? 2652 HOH A O 1 HETATM 3432 O O . HOH J 5 . ? -21.729 31.083 5.048 1.00 29.11 ? 2653 HOH A O 1 HETATM 3433 O O . HOH J 5 . ? -19.819 32.966 9.042 1.00 22.47 ? 2654 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 TPT 1 401 401 TPT TPT A . C 2 TPT 1 402 402 TPT TPT A . D 3 SO4 1 411 411 SO4 SO4 A . E 3 SO4 1 412 412 SO4 SO4 A . F 4 NAG 1 430 430 NAG NAG A . G 4 NAG 1 431 431 NAG NAG A . H 4 NAG 1 432 432 NAG NAG A . I 4 NAG 1 433 433 NAG NAG A . J 5 HOH 1 2001 2001 HOH HOH A . J 5 HOH 2 2002 2002 HOH HOH A . J 5 HOH 3 2003 2003 HOH HOH A . J 5 HOH 4 2004 2004 HOH HOH A . J 5 HOH 5 2005 2005 HOH HOH A . J 5 HOH 6 2006 2006 HOH HOH A . J 5 HOH 7 2007 2007 HOH HOH A . J 5 HOH 8 2008 2008 HOH HOH A . J 5 HOH 9 2009 2009 HOH HOH A . J 5 HOH 10 2010 2010 HOH HOH A . J 5 HOH 11 2011 2011 HOH HOH A . J 5 HOH 12 2012 2012 HOH HOH A . J 5 HOH 13 2013 2013 HOH HOH A . J 5 HOH 14 2014 2014 HOH HOH A . J 5 HOH 15 2015 2015 HOH HOH A . J 5 HOH 16 2016 2016 HOH HOH A . J 5 HOH 17 2017 2017 HOH HOH A . J 5 HOH 18 2018 2018 HOH HOH A . J 5 HOH 19 2019 2019 HOH HOH A . J 5 HOH 20 2020 2020 HOH HOH A . J 5 HOH 21 2021 2021 HOH HOH A . J 5 HOH 22 2022 2022 HOH HOH A . J 5 HOH 23 2023 2023 HOH HOH A . J 5 HOH 24 2024 2024 HOH HOH A . J 5 HOH 25 2025 2025 HOH HOH A . J 5 HOH 26 2026 2026 HOH HOH A . J 5 HOH 27 2027 2027 HOH HOH A . J 5 HOH 28 2028 2028 HOH HOH A . J 5 HOH 29 2029 2029 HOH HOH A . J 5 HOH 30 2030 2030 HOH HOH A . J 5 HOH 31 2031 2031 HOH HOH A . J 5 HOH 32 2032 2032 HOH HOH A . J 5 HOH 33 2033 2033 HOH HOH A . J 5 HOH 34 2034 2034 HOH HOH A . J 5 HOH 35 2035 2035 HOH HOH A . J 5 HOH 36 2036 2036 HOH HOH A . J 5 HOH 37 2037 2037 HOH HOH A . J 5 HOH 38 2038 2038 HOH HOH A . J 5 HOH 39 2039 2039 HOH HOH A . J 5 HOH 40 2040 2040 HOH HOH A . J 5 HOH 41 2041 2041 HOH HOH A . J 5 HOH 42 2042 2042 HOH HOH A . J 5 HOH 43 2043 2043 HOH HOH A . J 5 HOH 44 2044 2044 HOH HOH A . J 5 HOH 45 2045 2045 HOH HOH A . J 5 HOH 46 2046 2046 HOH HOH A . J 5 HOH 47 2047 2047 HOH HOH A . J 5 HOH 48 2048 2048 HOH HOH A . J 5 HOH 49 2049 2049 HOH HOH A . J 5 HOH 50 2050 2050 HOH HOH A . J 5 HOH 51 2051 2051 HOH HOH A . J 5 HOH 52 2052 2052 HOH HOH A . J 5 HOH 53 2053 2053 HOH HOH A . J 5 HOH 54 2054 2054 HOH HOH A . J 5 HOH 55 2055 2055 HOH HOH A . J 5 HOH 56 2056 2056 HOH HOH A . J 5 HOH 57 2057 2057 HOH HOH A . J 5 HOH 58 2058 2058 HOH HOH A . J 5 HOH 59 2059 2059 HOH HOH A . J 5 HOH 60 2060 2060 HOH HOH A . J 5 HOH 61 2061 2061 HOH HOH A . J 5 HOH 62 2062 2062 HOH HOH A . J 5 HOH 63 2063 2063 HOH HOH A . J 5 HOH 64 2064 2064 HOH HOH A . J 5 HOH 65 2065 2065 HOH HOH A . J 5 HOH 66 2066 2066 HOH HOH A . J 5 HOH 67 2067 2067 HOH HOH A . J 5 HOH 68 2068 2068 HOH HOH A . J 5 HOH 69 2069 2069 HOH HOH A . J 5 HOH 70 2070 2070 HOH HOH A . J 5 HOH 71 2071 2071 HOH HOH A . J 5 HOH 72 2072 2072 HOH HOH A . J 5 HOH 73 2073 2073 HOH HOH A . J 5 HOH 74 2074 2074 HOH HOH A . J 5 HOH 75 2075 2075 HOH HOH A . J 5 HOH 76 2076 2076 HOH HOH A . J 5 HOH 77 2077 2077 HOH HOH A . J 5 HOH 78 2078 2078 HOH HOH A . J 5 HOH 79 2079 2079 HOH HOH A . J 5 HOH 80 2080 2080 HOH HOH A . J 5 HOH 81 2081 2081 HOH HOH A . J 5 HOH 82 2082 2082 HOH HOH A . J 5 HOH 83 2083 2083 HOH HOH A . J 5 HOH 84 2084 2084 HOH HOH A . J 5 HOH 85 2085 2085 HOH HOH A . J 5 HOH 86 2086 2086 HOH HOH A . J 5 HOH 87 2087 2087 HOH HOH A . J 5 HOH 88 2088 2088 HOH HOH A . J 5 HOH 89 2089 2089 HOH HOH A . J 5 HOH 90 2090 2090 HOH HOH A . J 5 HOH 91 2091 2091 HOH HOH A . J 5 HOH 92 2092 2092 HOH HOH A . J 5 HOH 93 2093 2093 HOH HOH A . J 5 HOH 94 2094 2094 HOH HOH A . J 5 HOH 95 2095 2095 HOH HOH A . J 5 HOH 96 2096 2096 HOH HOH A . J 5 HOH 97 2097 2097 HOH HOH A . J 5 HOH 98 2098 2098 HOH HOH A . J 5 HOH 99 2099 2099 HOH HOH A . J 5 HOH 100 2100 2100 HOH HOH A . J 5 HOH 101 2101 2101 HOH HOH A . J 5 HOH 102 2102 2102 HOH HOH A . J 5 HOH 103 2103 2103 HOH HOH A . J 5 HOH 104 2104 2104 HOH HOH A . J 5 HOH 105 2105 2105 HOH HOH A . J 5 HOH 106 2106 2106 HOH HOH A . J 5 HOH 107 2107 2107 HOH HOH A . J 5 HOH 108 2108 2108 HOH HOH A . J 5 HOH 109 2109 2109 HOH HOH A . J 5 HOH 110 2110 2110 HOH HOH A . J 5 HOH 111 2111 2111 HOH HOH A . J 5 HOH 112 2112 2112 HOH HOH A . J 5 HOH 113 2113 2113 HOH HOH A . J 5 HOH 114 2114 2114 HOH HOH A . J 5 HOH 115 2115 2115 HOH HOH A . J 5 HOH 116 2116 2116 HOH HOH A . J 5 HOH 117 2117 2117 HOH HOH A . J 5 HOH 118 2118 2118 HOH HOH A . J 5 HOH 119 2119 2119 HOH HOH A . J 5 HOH 120 2120 2120 HOH HOH A . J 5 HOH 121 2121 2121 HOH HOH A . J 5 HOH 122 2122 2122 HOH HOH A . J 5 HOH 123 2123 2123 HOH HOH A . J 5 HOH 124 2124 2124 HOH HOH A . J 5 HOH 125 2125 2125 HOH HOH A . J 5 HOH 126 2126 2126 HOH HOH A . J 5 HOH 127 2127 2127 HOH HOH A . J 5 HOH 128 2128 2128 HOH HOH A . J 5 HOH 129 2129 2129 HOH HOH A . J 5 HOH 130 2130 2130 HOH HOH A . J 5 HOH 131 2131 2131 HOH HOH A . J 5 HOH 132 2132 2132 HOH HOH A . J 5 HOH 133 2133 2133 HOH HOH A . J 5 HOH 134 2134 2134 HOH HOH A . J 5 HOH 135 2135 2135 HOH HOH A . J 5 HOH 136 2136 2136 HOH HOH A . J 5 HOH 137 2137 2137 HOH HOH A . J 5 HOH 138 2138 2138 HOH HOH A . J 5 HOH 139 2139 2139 HOH HOH A . J 5 HOH 140 2140 2140 HOH HOH A . J 5 HOH 141 2141 2141 HOH HOH A . J 5 HOH 142 2142 2142 HOH HOH A . J 5 HOH 143 2143 2143 HOH HOH A . J 5 HOH 144 2144 2144 HOH HOH A . J 5 HOH 145 2145 2145 HOH HOH A . J 5 HOH 146 2146 2146 HOH HOH A . J 5 HOH 147 2147 2147 HOH HOH A . J 5 HOH 148 2148 2148 HOH HOH A . J 5 HOH 149 2149 2149 HOH HOH A . J 5 HOH 150 2150 2150 HOH HOH A . J 5 HOH 151 2151 2151 HOH HOH A . J 5 HOH 152 2152 2152 HOH HOH A . J 5 HOH 153 2153 2153 HOH HOH A . J 5 HOH 154 2154 2154 HOH HOH A . J 5 HOH 155 2155 2155 HOH HOH A . J 5 HOH 156 2156 2156 HOH HOH A . J 5 HOH 157 2157 2157 HOH HOH A . J 5 HOH 158 2158 2158 HOH HOH A . J 5 HOH 159 2159 2159 HOH HOH A . J 5 HOH 160 2160 2160 HOH HOH A . J 5 HOH 161 2161 2161 HOH HOH A . J 5 HOH 162 2162 2162 HOH HOH A . J 5 HOH 163 2163 2163 HOH HOH A . J 5 HOH 164 2164 2164 HOH HOH A . J 5 HOH 165 2165 2165 HOH HOH A . J 5 HOH 166 2166 2166 HOH HOH A . J 5 HOH 167 2167 2167 HOH HOH A . J 5 HOH 168 2168 2168 HOH HOH A . J 5 HOH 169 2169 2169 HOH HOH A . J 5 HOH 170 2170 2170 HOH HOH A . J 5 HOH 171 2171 2171 HOH HOH A . J 5 HOH 172 2172 2172 HOH HOH A . J 5 HOH 173 2173 2173 HOH HOH A . J 5 HOH 174 2174 2174 HOH HOH A . J 5 HOH 175 2175 2175 HOH HOH A . J 5 HOH 176 2176 2176 HOH HOH A . J 5 HOH 177 2177 2177 HOH HOH A . J 5 HOH 178 2178 2178 HOH HOH A . J 5 HOH 179 2179 2179 HOH HOH A . J 5 HOH 180 2180 2180 HOH HOH A . J 5 HOH 181 2181 2181 HOH HOH A . J 5 HOH 182 2182 2182 HOH HOH A . J 5 HOH 183 2183 2183 HOH HOH A . J 5 HOH 184 2184 2184 HOH HOH A . J 5 HOH 185 2185 2185 HOH HOH A . J 5 HOH 186 2186 2186 HOH HOH A . J 5 HOH 187 2187 2187 HOH HOH A . J 5 HOH 188 2188 2188 HOH HOH A . J 5 HOH 189 2189 2189 HOH HOH A . J 5 HOH 190 2190 2190 HOH HOH A . J 5 HOH 191 2191 2191 HOH HOH A . J 5 HOH 192 2192 2192 HOH HOH A . J 5 HOH 193 2193 2193 HOH HOH A . J 5 HOH 194 2194 2194 HOH HOH A . J 5 HOH 195 2195 2195 HOH HOH A . J 5 HOH 196 2196 2196 HOH HOH A . J 5 HOH 197 2197 2197 HOH HOH A . J 5 HOH 198 2198 2198 HOH HOH A . J 5 HOH 199 2199 2199 HOH HOH A . J 5 HOH 200 2200 2200 HOH HOH A . J 5 HOH 201 2201 2201 HOH HOH A . J 5 HOH 202 2202 2202 HOH HOH A . J 5 HOH 203 2203 2203 HOH HOH A . J 5 HOH 204 2204 2204 HOH HOH A . J 5 HOH 205 2205 2205 HOH HOH A . J 5 HOH 206 2206 2206 HOH HOH A . J 5 HOH 207 2207 2207 HOH HOH A . J 5 HOH 208 2208 2208 HOH HOH A . J 5 HOH 209 2209 2209 HOH HOH A . J 5 HOH 210 2210 2210 HOH HOH A . J 5 HOH 211 2211 2211 HOH HOH A . J 5 HOH 212 2212 2212 HOH HOH A . J 5 HOH 213 2213 2213 HOH HOH A . J 5 HOH 214 2214 2214 HOH HOH A . J 5 HOH 215 2215 2215 HOH HOH A . J 5 HOH 216 2216 2216 HOH HOH A . J 5 HOH 217 2217 2217 HOH HOH A . J 5 HOH 218 2218 2218 HOH HOH A . J 5 HOH 219 2219 2219 HOH HOH A . J 5 HOH 220 2220 2220 HOH HOH A . J 5 HOH 221 2221 2221 HOH HOH A . J 5 HOH 222 2222 2222 HOH HOH A . J 5 HOH 223 2223 2223 HOH HOH A . J 5 HOH 224 2224 2224 HOH HOH A . J 5 HOH 225 2225 2225 HOH HOH A . J 5 HOH 226 2226 2226 HOH HOH A . J 5 HOH 227 2227 2227 HOH HOH A . J 5 HOH 228 2228 2228 HOH HOH A . J 5 HOH 229 2229 2229 HOH HOH A . J 5 HOH 230 2230 2230 HOH HOH A . J 5 HOH 231 2231 2231 HOH HOH A . J 5 HOH 232 2232 2232 HOH HOH A . J 5 HOH 233 2233 2233 HOH HOH A . J 5 HOH 234 2234 2234 HOH HOH A . J 5 HOH 235 2235 2235 HOH HOH A . J 5 HOH 236 2236 2236 HOH HOH A . J 5 HOH 237 2237 2237 HOH HOH A . J 5 HOH 238 2238 2238 HOH HOH A . J 5 HOH 239 2239 2239 HOH HOH A . J 5 HOH 240 2240 2240 HOH HOH A . J 5 HOH 241 2241 2241 HOH HOH A . J 5 HOH 242 2242 2242 HOH HOH A . J 5 HOH 243 2243 2243 HOH HOH A . J 5 HOH 244 2244 2244 HOH HOH A . J 5 HOH 245 2245 2245 HOH HOH A . J 5 HOH 246 2246 2246 HOH HOH A . J 5 HOH 247 2247 2247 HOH HOH A . J 5 HOH 248 2248 2248 HOH HOH A . J 5 HOH 249 2249 2249 HOH HOH A . J 5 HOH 250 2250 2250 HOH HOH A . J 5 HOH 251 2251 2251 HOH HOH A . J 5 HOH 252 2252 2252 HOH HOH A . J 5 HOH 253 2253 2253 HOH HOH A . J 5 HOH 254 2254 2254 HOH HOH A . J 5 HOH 255 2255 2255 HOH HOH A . J 5 HOH 256 2256 2256 HOH HOH A . J 5 HOH 257 2257 2257 HOH HOH A . J 5 HOH 258 2258 2258 HOH HOH A . J 5 HOH 259 2259 2259 HOH HOH A . J 5 HOH 260 2260 2260 HOH HOH A . J 5 HOH 261 2261 2261 HOH HOH A . J 5 HOH 262 2262 2262 HOH HOH A . J 5 HOH 263 2263 2263 HOH HOH A . J 5 HOH 264 2264 2264 HOH HOH A . J 5 HOH 265 2265 2265 HOH HOH A . J 5 HOH 266 2266 2266 HOH HOH A . J 5 HOH 267 2267 2267 HOH HOH A . J 5 HOH 268 2268 2268 HOH HOH A . J 5 HOH 269 2269 2269 HOH HOH A . J 5 HOH 270 2270 2270 HOH HOH A . J 5 HOH 271 2271 2271 HOH HOH A . J 5 HOH 272 2272 2272 HOH HOH A . J 5 HOH 273 2273 2273 HOH HOH A . J 5 HOH 274 2274 2274 HOH HOH A . J 5 HOH 275 2275 2275 HOH HOH A . J 5 HOH 276 2276 2276 HOH HOH A . J 5 HOH 277 2277 2277 HOH HOH A . J 5 HOH 278 2278 2278 HOH HOH A . J 5 HOH 279 2279 2279 HOH HOH A . J 5 HOH 280 2280 2280 HOH HOH A . J 5 HOH 281 2281 2281 HOH HOH A . J 5 HOH 282 2282 2282 HOH HOH A . J 5 HOH 283 2283 2283 HOH HOH A . J 5 HOH 284 2284 2284 HOH HOH A . J 5 HOH 285 2285 2285 HOH HOH A . J 5 HOH 286 2286 2286 HOH HOH A . J 5 HOH 287 2287 2287 HOH HOH A . J 5 HOH 288 2288 2288 HOH HOH A . J 5 HOH 289 2289 2289 HOH HOH A . J 5 HOH 290 2290 2290 HOH HOH A . J 5 HOH 291 2291 2291 HOH HOH A . J 5 HOH 292 2292 2292 HOH HOH A . J 5 HOH 293 2293 2293 HOH HOH A . J 5 HOH 294 2294 2294 HOH HOH A . J 5 HOH 295 2295 2295 HOH HOH A . J 5 HOH 296 2296 2296 HOH HOH A . J 5 HOH 297 2297 2297 HOH HOH A . J 5 HOH 298 2298 2298 HOH HOH A . J 5 HOH 299 2299 2299 HOH HOH A . J 5 HOH 300 2300 2300 HOH HOH A . J 5 HOH 301 2301 2301 HOH HOH A . J 5 HOH 302 2302 2302 HOH HOH A . J 5 HOH 303 2303 2303 HOH HOH A . J 5 HOH 304 2304 2304 HOH HOH A . J 5 HOH 305 2305 2305 HOH HOH A . J 5 HOH 306 2306 2306 HOH HOH A . J 5 HOH 307 2307 2307 HOH HOH A . J 5 HOH 308 2308 2308 HOH HOH A . J 5 HOH 309 2309 2309 HOH HOH A . J 5 HOH 310 2310 2310 HOH HOH A . J 5 HOH 311 2311 2311 HOH HOH A . J 5 HOH 312 2312 2312 HOH HOH A . J 5 HOH 313 2313 2313 HOH HOH A . J 5 HOH 314 2314 2314 HOH HOH A . J 5 HOH 315 2315 2315 HOH HOH A . J 5 HOH 316 2316 2316 HOH HOH A . J 5 HOH 317 2317 2317 HOH HOH A . J 5 HOH 318 2318 2318 HOH HOH A . J 5 HOH 319 2319 2319 HOH HOH A . J 5 HOH 320 2320 2320 HOH HOH A . J 5 HOH 321 2321 2321 HOH HOH A . J 5 HOH 322 2322 2322 HOH HOH A . J 5 HOH 323 2323 2323 HOH HOH A . J 5 HOH 324 2324 2324 HOH HOH A . J 5 HOH 325 2325 2325 HOH HOH A . J 5 HOH 326 2326 2326 HOH HOH A . J 5 HOH 327 2327 2327 HOH HOH A . J 5 HOH 328 2328 2328 HOH HOH A . J 5 HOH 329 2329 2329 HOH HOH A . J 5 HOH 330 2330 2330 HOH HOH A . J 5 HOH 331 2331 2331 HOH HOH A . J 5 HOH 332 2332 2332 HOH HOH A . J 5 HOH 333 2333 2333 HOH HOH A . J 5 HOH 334 2334 2334 HOH HOH A . J 5 HOH 335 2335 2335 HOH HOH A . J 5 HOH 336 2336 2336 HOH HOH A . J 5 HOH 337 2337 2337 HOH HOH A . J 5 HOH 338 2338 2338 HOH HOH A . J 5 HOH 339 2339 2339 HOH HOH A . J 5 HOH 340 2340 2340 HOH HOH A . J 5 HOH 341 2341 2341 HOH HOH A . J 5 HOH 342 2342 2342 HOH HOH A . J 5 HOH 343 2343 2343 HOH HOH A . J 5 HOH 344 2344 2344 HOH HOH A . J 5 HOH 345 2345 2345 HOH HOH A . J 5 HOH 346 2346 2346 HOH HOH A . J 5 HOH 347 2347 2347 HOH HOH A . J 5 HOH 348 2348 2348 HOH HOH A . J 5 HOH 349 2349 2349 HOH HOH A . J 5 HOH 350 2350 2350 HOH HOH A . J 5 HOH 351 2351 2351 HOH HOH A . J 5 HOH 352 2352 2352 HOH HOH A . J 5 HOH 353 2353 2353 HOH HOH A . J 5 HOH 354 2354 2354 HOH HOH A . J 5 HOH 355 2355 2355 HOH HOH A . J 5 HOH 356 2356 2356 HOH HOH A . J 5 HOH 357 2357 2357 HOH HOH A . J 5 HOH 358 2358 2358 HOH HOH A . J 5 HOH 359 2359 2359 HOH HOH A . J 5 HOH 360 2360 2360 HOH HOH A . J 5 HOH 361 2361 2361 HOH HOH A . J 5 HOH 362 2362 2362 HOH HOH A . J 5 HOH 363 2363 2363 HOH HOH A . J 5 HOH 364 2364 2364 HOH HOH A . J 5 HOH 365 2365 2365 HOH HOH A . J 5 HOH 366 2366 2366 HOH HOH A . J 5 HOH 367 2367 2367 HOH HOH A . J 5 HOH 368 2368 2368 HOH HOH A . J 5 HOH 369 2369 2369 HOH HOH A . J 5 HOH 370 2370 2370 HOH HOH A . J 5 HOH 371 2371 2371 HOH HOH A . J 5 HOH 372 2372 2372 HOH HOH A . J 5 HOH 373 2373 2373 HOH HOH A . J 5 HOH 374 2374 2374 HOH HOH A . J 5 HOH 375 2375 2375 HOH HOH A . J 5 HOH 376 2376 2376 HOH HOH A . J 5 HOH 377 2377 2377 HOH HOH A . J 5 HOH 378 2378 2378 HOH HOH A . J 5 HOH 379 2379 2379 HOH HOH A . J 5 HOH 380 2380 2380 HOH HOH A . J 5 HOH 381 2381 2381 HOH HOH A . J 5 HOH 382 2382 2382 HOH HOH A . J 5 HOH 383 2383 2383 HOH HOH A . J 5 HOH 384 2384 2384 HOH HOH A . J 5 HOH 385 2385 2385 HOH HOH A . J 5 HOH 386 2386 2386 HOH HOH A . J 5 HOH 387 2387 2387 HOH HOH A . J 5 HOH 388 2388 2388 HOH HOH A . J 5 HOH 389 2389 2389 HOH HOH A . J 5 HOH 390 2390 2390 HOH HOH A . J 5 HOH 391 2391 2391 HOH HOH A . J 5 HOH 392 2392 2392 HOH HOH A . J 5 HOH 393 2393 2393 HOH HOH A . J 5 HOH 394 2394 2394 HOH HOH A . J 5 HOH 395 2395 2395 HOH HOH A . J 5 HOH 396 2396 2396 HOH HOH A . J 5 HOH 397 2397 2397 HOH HOH A . J 5 HOH 398 2398 2398 HOH HOH A . J 5 HOH 399 2399 2399 HOH HOH A . J 5 HOH 400 2400 2400 HOH HOH A . J 5 HOH 401 2401 2401 HOH HOH A . J 5 HOH 402 2402 2402 HOH HOH A . J 5 HOH 403 2403 2403 HOH HOH A . J 5 HOH 404 2404 2404 HOH HOH A . J 5 HOH 405 2405 2405 HOH HOH A . J 5 HOH 406 2406 2406 HOH HOH A . J 5 HOH 407 2407 2407 HOH HOH A . J 5 HOH 408 2408 2408 HOH HOH A . J 5 HOH 409 2409 2409 HOH HOH A . J 5 HOH 410 2410 2410 HOH HOH A . J 5 HOH 411 2411 2411 HOH HOH A . J 5 HOH 412 2412 2412 HOH HOH A . J 5 HOH 413 2413 2413 HOH HOH A . J 5 HOH 414 2414 2414 HOH HOH A . J 5 HOH 415 2415 2415 HOH HOH A . J 5 HOH 416 2416 2416 HOH HOH A . J 5 HOH 417 2417 2417 HOH HOH A . J 5 HOH 418 2418 2418 HOH HOH A . J 5 HOH 419 2419 2419 HOH HOH A . J 5 HOH 420 2420 2420 HOH HOH A . J 5 HOH 421 2421 2421 HOH HOH A . J 5 HOH 422 2422 2422 HOH HOH A . J 5 HOH 423 2423 2423 HOH HOH A . J 5 HOH 424 2424 2424 HOH HOH A . J 5 HOH 425 2425 2425 HOH HOH A . J 5 HOH 426 2426 2426 HOH HOH A . J 5 HOH 427 2427 2427 HOH HOH A . J 5 HOH 428 2428 2428 HOH HOH A . J 5 HOH 429 2429 2429 HOH HOH A . J 5 HOH 430 2430 2430 HOH HOH A . J 5 HOH 431 2431 2431 HOH HOH A . J 5 HOH 432 2432 2432 HOH HOH A . J 5 HOH 433 2433 2433 HOH HOH A . J 5 HOH 434 2434 2434 HOH HOH A . J 5 HOH 435 2435 2435 HOH HOH A . J 5 HOH 436 2436 2436 HOH HOH A . J 5 HOH 437 2437 2437 HOH HOH A . J 5 HOH 438 2438 2438 HOH HOH A . J 5 HOH 439 2439 2439 HOH HOH A . J 5 HOH 440 2440 2440 HOH HOH A . J 5 HOH 441 2441 2441 HOH HOH A . J 5 HOH 442 2442 2442 HOH HOH A . J 5 HOH 443 2443 2443 HOH HOH A . J 5 HOH 444 2444 2444 HOH HOH A . J 5 HOH 445 2445 2445 HOH HOH A . J 5 HOH 446 2446 2446 HOH HOH A . J 5 HOH 447 2447 2447 HOH HOH A . J 5 HOH 448 2448 2448 HOH HOH A . J 5 HOH 449 2449 2449 HOH HOH A . J 5 HOH 450 2450 2450 HOH HOH A . J 5 HOH 451 2451 2451 HOH HOH A . J 5 HOH 452 2452 2452 HOH HOH A . J 5 HOH 453 2453 2453 HOH HOH A . J 5 HOH 454 2454 2454 HOH HOH A . J 5 HOH 455 2455 2455 HOH HOH A . J 5 HOH 456 2456 2456 HOH HOH A . J 5 HOH 457 2457 2457 HOH HOH A . J 5 HOH 458 2458 2458 HOH HOH A . J 5 HOH 459 2459 2459 HOH HOH A . J 5 HOH 460 2460 2460 HOH HOH A . J 5 HOH 461 2461 2461 HOH HOH A . J 5 HOH 462 2462 2462 HOH HOH A . J 5 HOH 463 2463 2463 HOH HOH A . J 5 HOH 464 2464 2464 HOH HOH A . J 5 HOH 465 2465 2465 HOH HOH A . J 5 HOH 466 2466 2466 HOH HOH A . J 5 HOH 467 2467 2467 HOH HOH A . J 5 HOH 468 2468 2468 HOH HOH A . J 5 HOH 469 2469 2469 HOH HOH A . J 5 HOH 470 2470 2470 HOH HOH A . J 5 HOH 471 2471 2471 HOH HOH A . J 5 HOH 472 2472 2472 HOH HOH A . J 5 HOH 473 2473 2473 HOH HOH A . J 5 HOH 474 2474 2474 HOH HOH A . J 5 HOH 475 2475 2475 HOH HOH A . J 5 HOH 476 2476 2476 HOH HOH A . J 5 HOH 477 2477 2477 HOH HOH A . J 5 HOH 478 2478 2478 HOH HOH A . J 5 HOH 479 2479 2479 HOH HOH A . J 5 HOH 480 2480 2480 HOH HOH A . J 5 HOH 481 2481 2481 HOH HOH A . J 5 HOH 482 2482 2482 HOH HOH A . J 5 HOH 483 2483 2483 HOH HOH A . J 5 HOH 484 2484 2484 HOH HOH A . J 5 HOH 485 2485 2485 HOH HOH A . J 5 HOH 486 2486 2486 HOH HOH A . J 5 HOH 487 2487 2487 HOH HOH A . J 5 HOH 488 2488 2488 HOH HOH A . J 5 HOH 489 2489 2489 HOH HOH A . J 5 HOH 490 2490 2490 HOH HOH A . J 5 HOH 491 2491 2491 HOH HOH A . J 5 HOH 492 2492 2492 HOH HOH A . J 5 HOH 493 2493 2493 HOH HOH A . J 5 HOH 494 2494 2494 HOH HOH A . J 5 HOH 495 2495 2495 HOH HOH A . J 5 HOH 496 2496 2496 HOH HOH A . J 5 HOH 497 2497 2497 HOH HOH A . J 5 HOH 498 2498 2498 HOH HOH A . J 5 HOH 499 2499 2499 HOH HOH A . J 5 HOH 500 2500 2500 HOH HOH A . J 5 HOH 501 2501 2501 HOH HOH A . J 5 HOH 502 2502 2502 HOH HOH A . J 5 HOH 503 2503 2503 HOH HOH A . J 5 HOH 504 2504 2504 HOH HOH A . J 5 HOH 505 2505 2505 HOH HOH A . J 5 HOH 506 2506 2506 HOH HOH A . J 5 HOH 507 2507 2507 HOH HOH A . J 5 HOH 508 2508 2508 HOH HOH A . J 5 HOH 509 2509 2509 HOH HOH A . J 5 HOH 510 2510 2510 HOH HOH A . J 5 HOH 511 2511 2511 HOH HOH A . J 5 HOH 512 2512 2512 HOH HOH A . J 5 HOH 513 2513 2513 HOH HOH A . J 5 HOH 514 2514 2514 HOH HOH A . J 5 HOH 515 2515 2515 HOH HOH A . J 5 HOH 516 2516 2516 HOH HOH A . J 5 HOH 517 2517 2517 HOH HOH A . J 5 HOH 518 2518 2518 HOH HOH A . J 5 HOH 519 2519 2519 HOH HOH A . J 5 HOH 520 2520 2520 HOH HOH A . J 5 HOH 521 2521 2521 HOH HOH A . J 5 HOH 522 2522 2522 HOH HOH A . J 5 HOH 523 2523 2523 HOH HOH A . J 5 HOH 524 2524 2524 HOH HOH A . J 5 HOH 525 2525 2525 HOH HOH A . J 5 HOH 526 2526 2526 HOH HOH A . J 5 HOH 527 2527 2527 HOH HOH A . J 5 HOH 528 2528 2528 HOH HOH A . J 5 HOH 529 2529 2529 HOH HOH A . J 5 HOH 530 2530 2530 HOH HOH A . J 5 HOH 531 2531 2531 HOH HOH A . J 5 HOH 532 2532 2532 HOH HOH A . J 5 HOH 533 2533 2533 HOH HOH A . J 5 HOH 534 2534 2534 HOH HOH A . J 5 HOH 535 2535 2535 HOH HOH A . J 5 HOH 536 2536 2536 HOH HOH A . J 5 HOH 537 2537 2537 HOH HOH A . J 5 HOH 538 2538 2538 HOH HOH A . J 5 HOH 539 2539 2539 HOH HOH A . J 5 HOH 540 2540 2540 HOH HOH A . J 5 HOH 541 2541 2541 HOH HOH A . J 5 HOH 542 2542 2542 HOH HOH A . J 5 HOH 543 2543 2543 HOH HOH A . J 5 HOH 544 2544 2544 HOH HOH A . J 5 HOH 545 2545 2545 HOH HOH A . J 5 HOH 546 2546 2546 HOH HOH A . J 5 HOH 547 2547 2547 HOH HOH A . J 5 HOH 548 2548 2548 HOH HOH A . J 5 HOH 549 2549 2549 HOH HOH A . J 5 HOH 550 2550 2550 HOH HOH A . J 5 HOH 551 2551 2551 HOH HOH A . J 5 HOH 552 2552 2552 HOH HOH A . J 5 HOH 553 2553 2553 HOH HOH A . J 5 HOH 554 2554 2554 HOH HOH A . J 5 HOH 555 2555 2555 HOH HOH A . J 5 HOH 556 2556 2556 HOH HOH A . J 5 HOH 557 2557 2557 HOH HOH A . J 5 HOH 558 2558 2558 HOH HOH A . J 5 HOH 559 2559 2559 HOH HOH A . J 5 HOH 560 2560 2560 HOH HOH A . J 5 HOH 561 2561 2561 HOH HOH A . J 5 HOH 562 2562 2562 HOH HOH A . J 5 HOH 563 2563 2563 HOH HOH A . J 5 HOH 564 2564 2564 HOH HOH A . J 5 HOH 565 2565 2565 HOH HOH A . J 5 HOH 566 2566 2566 HOH HOH A . J 5 HOH 567 2567 2567 HOH HOH A . J 5 HOH 568 2568 2568 HOH HOH A . J 5 HOH 569 2569 2569 HOH HOH A . J 5 HOH 570 2570 2570 HOH HOH A . J 5 HOH 571 2571 2571 HOH HOH A . J 5 HOH 572 2572 2572 HOH HOH A . J 5 HOH 573 2573 2573 HOH HOH A . J 5 HOH 574 2574 2574 HOH HOH A . J 5 HOH 575 2575 2575 HOH HOH A . J 5 HOH 576 2576 2576 HOH HOH A . J 5 HOH 577 2577 2577 HOH HOH A . J 5 HOH 578 2578 2578 HOH HOH A . J 5 HOH 579 2579 2579 HOH HOH A . J 5 HOH 580 2580 2580 HOH HOH A . J 5 HOH 581 2581 2581 HOH HOH A . J 5 HOH 582 2582 2582 HOH HOH A . J 5 HOH 583 2583 2583 HOH HOH A . J 5 HOH 584 2584 2584 HOH HOH A . J 5 HOH 585 2585 2585 HOH HOH A . J 5 HOH 586 2586 2586 HOH HOH A . J 5 HOH 587 2587 2587 HOH HOH A . J 5 HOH 588 2588 2588 HOH HOH A . J 5 HOH 589 2589 2589 HOH HOH A . J 5 HOH 590 2590 2590 HOH HOH A . J 5 HOH 591 2591 2591 HOH HOH A . J 5 HOH 592 2592 2592 HOH HOH A . J 5 HOH 593 2593 2593 HOH HOH A . J 5 HOH 594 2594 2594 HOH HOH A . J 5 HOH 595 2595 2595 HOH HOH A . J 5 HOH 596 2596 2596 HOH HOH A . J 5 HOH 597 2597 2597 HOH HOH A . J 5 HOH 598 2598 2598 HOH HOH A . J 5 HOH 599 2599 2599 HOH HOH A . J 5 HOH 600 2600 2600 HOH HOH A . J 5 HOH 601 2601 2601 HOH HOH A . J 5 HOH 602 2602 2602 HOH HOH A . J 5 HOH 603 2603 2603 HOH HOH A . J 5 HOH 604 2604 2604 HOH HOH A . J 5 HOH 605 2605 2605 HOH HOH A . J 5 HOH 606 2606 2606 HOH HOH A . J 5 HOH 607 2607 2607 HOH HOH A . J 5 HOH 608 2608 2608 HOH HOH A . J 5 HOH 609 2609 2609 HOH HOH A . J 5 HOH 610 2610 2610 HOH HOH A . J 5 HOH 611 2611 2611 HOH HOH A . J 5 HOH 612 2612 2612 HOH HOH A . J 5 HOH 613 2613 2613 HOH HOH A . J 5 HOH 614 2614 2614 HOH HOH A . J 5 HOH 615 2615 2615 HOH HOH A . J 5 HOH 616 2616 2616 HOH HOH A . J 5 HOH 617 2617 2617 HOH HOH A . J 5 HOH 618 2618 2618 HOH HOH A . J 5 HOH 619 2619 2619 HOH HOH A . J 5 HOH 620 2620 2620 HOH HOH A . J 5 HOH 621 2621 2621 HOH HOH A . J 5 HOH 622 2622 2622 HOH HOH A . J 5 HOH 623 2623 2623 HOH HOH A . J 5 HOH 624 2624 2624 HOH HOH A . J 5 HOH 625 2625 2625 HOH HOH A . J 5 HOH 626 2626 2626 HOH HOH A . J 5 HOH 627 2627 2627 HOH HOH A . J 5 HOH 628 2628 2628 HOH HOH A . J 5 HOH 629 2629 2629 HOH HOH A . J 5 HOH 630 2630 2630 HOH HOH A . J 5 HOH 631 2631 2631 HOH HOH A . J 5 HOH 632 2632 2632 HOH HOH A . J 5 HOH 633 2633 2633 HOH HOH A . J 5 HOH 634 2634 2634 HOH HOH A . J 5 HOH 635 2635 2635 HOH HOH A . J 5 HOH 636 2636 2636 HOH HOH A . J 5 HOH 637 2637 2637 HOH HOH A . J 5 HOH 638 2638 2638 HOH HOH A . J 5 HOH 639 2639 2639 HOH HOH A . J 5 HOH 640 2640 2640 HOH HOH A . J 5 HOH 641 2641 2641 HOH HOH A . J 5 HOH 642 2642 2642 HOH HOH A . J 5 HOH 643 2643 2643 HOH HOH A . J 5 HOH 644 2644 2644 HOH HOH A . J 5 HOH 645 2645 2645 HOH HOH A . J 5 HOH 646 2646 2646 HOH HOH A . J 5 HOH 647 2647 2647 HOH HOH A . J 5 HOH 648 2648 2648 HOH HOH A . J 5 HOH 649 2649 2649 HOH HOH A . J 5 HOH 650 2650 2650 HOH HOH A . J 5 HOH 651 2651 2651 HOH HOH A . J 5 HOH 652 2652 2652 HOH HOH A . J 5 HOH 653 2653 2653 HOH HOH A . J 5 HOH 654 2654 2654 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 PQS _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 # _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_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? J HOH . ? A HOH 2619 ? 1_555 PT1 ? B TPT . ? A TPT 401 ? 1_555 N1 ? B TPT . ? A TPT 401 ? 1_555 61.8 ? 2 O ? J HOH . ? A HOH 2619 ? 1_555 PT1 ? B TPT . ? A TPT 401 ? 1_555 N2 ? B TPT . ? A TPT 401 ? 1_555 58.9 ? 3 N1 ? B TPT . ? A TPT 401 ? 1_555 PT1 ? B TPT . ? A TPT 401 ? 1_555 N2 ? B TPT . ? A TPT 401 ? 1_555 76.5 ? 4 O ? J HOH . ? A HOH 2619 ? 1_555 PT1 ? B TPT . ? A TPT 401 ? 1_555 N3 ? B TPT . ? A TPT 401 ? 1_555 104.9 ? 5 N1 ? B TPT . ? A TPT 401 ? 1_555 PT1 ? B TPT . ? A TPT 401 ? 1_555 N3 ? B TPT . ? A TPT 401 ? 1_555 155.2 ? 6 N2 ? B TPT . ? A TPT 401 ? 1_555 PT1 ? B TPT . ? A TPT 401 ? 1_555 N3 ? B TPT . ? A TPT 401 ? 1_555 78.8 ? 7 O ? J HOH . ? A HOH 2620 ? 1_555 PT1 ? C TPT . ? A TPT 402 ? 1_555 N1 ? C TPT . ? A TPT 402 ? 1_555 101.5 ? 8 O ? J HOH . ? A HOH 2620 ? 1_555 PT1 ? C TPT . ? A TPT 402 ? 1_555 N2 ? C TPT . ? A TPT 402 ? 1_555 179.8 ? 9 N1 ? C TPT . ? A TPT 402 ? 1_555 PT1 ? C TPT . ? A TPT 402 ? 1_555 N2 ? C TPT . ? A TPT 402 ? 1_555 78.5 ? 10 O ? J HOH . ? A HOH 2620 ? 1_555 PT1 ? C TPT . ? A TPT 402 ? 1_555 N3 ? C TPT . ? A TPT 402 ? 1_555 98.6 ? 11 N1 ? C TPT . ? A TPT 402 ? 1_555 PT1 ? C TPT . ? A TPT 402 ? 1_555 N3 ? C TPT . ? A TPT 402 ? 1_555 159.6 ? 12 N2 ? C TPT . ? A TPT 402 ? 1_555 PT1 ? C TPT . ? A TPT 402 ? 1_555 N3 ? C TPT . ? A TPT 402 ? 1_555 81.4 ? # 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 3 'Structure model' 1 2 2017-06-28 # _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' 'Database references' 2 2 'Structure model' 'Derived calculations' 3 2 'Structure model' 'Non-polymer description' 4 2 'Structure model' Other 5 2 'Structure model' 'Structure summary' 6 2 'Structure model' 'Version format compliance' 7 3 'Structure model' 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 3 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_software.name' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement . ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 ARP/wARP phasing . ? 4 # 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 2038 ? ? O A HOH 2040 ? ? 1.50 2 1 N2 A TPT 402 ? ? O A HOH 2619 ? ? 2.16 3 1 N2 A TPT 401 ? ? O A HOH 2619 ? ? 2.17 4 1 C10 A TPT 402 ? ? O A HOH 2619 ? ? 2.17 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 O _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 HOH _pdbx_validate_symm_contact.auth_seq_id_1 2066 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _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 HOH _pdbx_validate_symm_contact.auth_seq_id_2 2353 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 2_555 _pdbx_validate_symm_contact.dist 2.10 # 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 CA A CYS 29 ? ? CB A CYS 29 ? ? SG A CYS 29 ? ? 121.72 114.20 7.52 1.10 N 2 1 CE1 A HIS 35 ? ? NE2 A HIS 35 ? ? CD2 A HIS 35 ? ? 114.40 109.00 5.40 0.70 N 3 1 CA A TYR 94 ? ? CB A TYR 94 ? ? CG A TYR 94 ? ? 124.91 113.40 11.51 1.90 N 4 1 NE A ARG 145 ? ? CZ A ARG 145 ? ? NH2 A ARG 145 ? ? 113.92 120.30 -6.38 0.50 N 5 1 CA A CYS 272 ? ? CB A CYS 272 ? ? SG A CYS 272 ? ? 121.26 114.20 7.06 1.10 N 6 1 CD A ARG 298 ? ? NE A ARG 298 ? ? CZ A ARG 298 ? ? 134.62 123.60 11.02 1.40 N 7 1 NE A ARG 298 ? ? CZ A ARG 298 ? ? NH1 A ARG 298 ? ? 124.11 120.30 3.81 0.50 N 8 1 NE A ARG 298 ? ? CZ A ARG 298 ? ? NH2 A ARG 298 ? ? 116.60 120.30 -3.70 0.50 N 9 1 CB A ASP 310 ? ? CG A ASP 310 ? ? OD2 A ASP 310 ? ? 123.72 118.30 5.42 0.90 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 ? ? -165.87 84.45 2 1 ASP A 195 ? ? -161.02 110.18 3 1 TYR A 220 ? ? -115.37 50.74 4 1 ASN A 282 ? ? 38.67 65.88 5 1 VAL A 336 ? ? -120.43 -71.73 # 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 2004 ? 7.07 . 2 1 O ? A HOH 2013 ? 7.02 . 3 1 O ? A HOH 2060 ? 6.97 . 4 1 O ? A HOH 2061 ? 10.61 . 5 1 O ? A HOH 2062 ? 5.98 . 6 1 O ? A HOH 2088 ? 6.47 . 7 1 O ? A HOH 2089 ? 6.39 . 8 1 O ? A HOH 2090 ? 6.12 . 9 1 O ? A HOH 2093 ? 7.90 . 10 1 O ? A HOH 2104 ? . 5.95 11 1 O ? A HOH 2122 ? 6.31 . 12 1 O ? A HOH 2123 ? 5.95 . 13 1 O ? A HOH 2139 ? 7.20 . 14 1 O ? A HOH 2141 ? 5.85 . 15 1 O ? A HOH 2171 ? 6.19 . 16 1 O ? A HOH 2192 ? 6.58 . 17 1 O ? A HOH 2207 ? 5.98 . 18 1 O ? A HOH 2334 ? 6.92 . 19 1 O ? A HOH 2343 ? 6.05 . # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 ;2,2':6',2''-TERPYRIDINE PLATINUM(II) Chloride ; TPT 3 'SULFATE ION' SO4 4 N-ACETYL-D-GLUCOSAMINE NAG 5 water HOH #