data_3TGT # _entry.id 3TGT # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.287 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3TGT RCSB RCSB067459 WWPDB D_1000067459 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3TGQ . unspecified PDB 3TGR . unspecified PDB 3TGS . unspecified PDB 3TIH . unspecified # _pdbx_database_status.entry_id 3TGT _pdbx_database_status.status_code REL _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.recvd_initial_deposition_date 2011-08-17 _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Kwon, Y.D.' 1 'Kwong, P.D.' 2 # _citation.id primary _citation.title ;Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops. ; _citation.journal_abbrev Proc.Natl.Acad.Sci.USA _citation.journal_volume 109 _citation.page_first 5663 _citation.page_last 5668 _citation.year 2012 _citation.journal_id_ASTM PNASA6 _citation.country US _citation.journal_id_ISSN 0027-8424 _citation.journal_id_CSD 0040 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 22451932 _citation.pdbx_database_id_DOI 10.1073/pnas.1112391109 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Kwon, Y.D.' 1 primary 'Finzi, A.' 2 primary 'Wu, X.' 3 primary 'Dogo-Isonagie, C.' 4 primary 'Lee, L.K.' 5 primary 'Moore, L.R.' 6 primary 'Schmidt, S.D.' 7 primary 'Stuckey, J.' 8 primary 'Yang, Y.' 9 primary 'Zhou, T.' 10 primary 'Zhu, J.' 11 primary 'Vicic, D.A.' 12 primary 'Debnath, A.K.' 13 primary 'Shapiro, L.' 14 primary 'Bewley, C.A.' 15 primary 'Mascola, J.R.' 16 primary 'Sodroski, J.G.' 17 primary 'Kwong, P.D.' 18 # _cell.entry_id 3TGT _cell.length_a 63.556 _cell.length_b 66.944 _cell.length_c 88.029 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3TGT _symmetry.space_group_name_H-M 'P 21 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'HIV-1 clade A/E 93TH057 gp120' 39211.434 1 ? ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 10 ? ? ? ? 3 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305 1 ? ? ? ? 4 water nat water 18.015 148 ? ? ? ? # _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 ;VWKDADTTLFCASDAKAHETEVHNVWATHACVPTDPNPQEIHLENVTENFNMWKNNMVEQMQEDVISLWDQSLQPCVKLT GGSVIKQACPKISFDPIPIHYCTPAGYVILKCNDKNFNGTGPCKNVSSVQCTHGIKPVVSTQLLLNGSLAEEEIIIRSEN LTNNAKTIIVHLNKSVEINCTRPSNGGSGSGGDIRKAYCEINGTKWNKVLKQVTEKLKEHFNNKTIIFQPPSGGDLEITM HHFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRDGG ANNTSNETFRPGGGNIKDNWRSELYKYKVVQIE ; _entity_poly.pdbx_seq_one_letter_code_can ;VWKDADTTLFCASDAKAHETEVHNVWATHACVPTDPNPQEIHLENVTENFNMWKNNMVEQMQEDVISLWDQSLQPCVKLT GGSVIKQACPKISFDPIPIHYCTPAGYVILKCNDKNFNGTGPCKNVSSVQCTHGIKPVVSTQLLLNGSLAEEEIIIRSEN LTNNAKTIIVHLNKSVEINCTRPSNGGSGSGGDIRKAYCEINGTKWNKVLKQVTEKLKEHFNNKTIIFQPPSGGDLEITM HHFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRDGG ANNTSNETFRPGGGNIKDNWRSELYKYKVVQIE ; _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 VAL n 1 2 TRP n 1 3 LYS n 1 4 ASP n 1 5 ALA n 1 6 ASP n 1 7 THR n 1 8 THR n 1 9 LEU n 1 10 PHE n 1 11 CYS n 1 12 ALA n 1 13 SER n 1 14 ASP n 1 15 ALA n 1 16 LYS n 1 17 ALA n 1 18 HIS n 1 19 GLU n 1 20 THR n 1 21 GLU n 1 22 VAL n 1 23 HIS n 1 24 ASN n 1 25 VAL n 1 26 TRP n 1 27 ALA n 1 28 THR n 1 29 HIS n 1 30 ALA n 1 31 CYS n 1 32 VAL n 1 33 PRO n 1 34 THR n 1 35 ASP n 1 36 PRO n 1 37 ASN n 1 38 PRO n 1 39 GLN n 1 40 GLU n 1 41 ILE n 1 42 HIS n 1 43 LEU n 1 44 GLU n 1 45 ASN n 1 46 VAL n 1 47 THR n 1 48 GLU n 1 49 ASN n 1 50 PHE n 1 51 ASN n 1 52 MET n 1 53 TRP n 1 54 LYS n 1 55 ASN n 1 56 ASN n 1 57 MET n 1 58 VAL n 1 59 GLU n 1 60 GLN n 1 61 MET n 1 62 GLN n 1 63 GLU n 1 64 ASP n 1 65 VAL n 1 66 ILE n 1 67 SER n 1 68 LEU n 1 69 TRP n 1 70 ASP n 1 71 GLN n 1 72 SER n 1 73 LEU n 1 74 GLN n 1 75 PRO n 1 76 CYS n 1 77 VAL n 1 78 LYS n 1 79 LEU n 1 80 THR n 1 81 GLY n 1 82 GLY n 1 83 SER n 1 84 VAL n 1 85 ILE n 1 86 LYS n 1 87 GLN n 1 88 ALA n 1 89 CYS n 1 90 PRO n 1 91 LYS n 1 92 ILE n 1 93 SER n 1 94 PHE n 1 95 ASP n 1 96 PRO n 1 97 ILE n 1 98 PRO n 1 99 ILE n 1 100 HIS n 1 101 TYR n 1 102 CYS n 1 103 THR n 1 104 PRO n 1 105 ALA n 1 106 GLY n 1 107 TYR n 1 108 VAL n 1 109 ILE n 1 110 LEU n 1 111 LYS n 1 112 CYS n 1 113 ASN n 1 114 ASP n 1 115 LYS n 1 116 ASN n 1 117 PHE n 1 118 ASN n 1 119 GLY n 1 120 THR n 1 121 GLY n 1 122 PRO n 1 123 CYS n 1 124 LYS n 1 125 ASN n 1 126 VAL n 1 127 SER n 1 128 SER n 1 129 VAL n 1 130 GLN n 1 131 CYS n 1 132 THR n 1 133 HIS n 1 134 GLY n 1 135 ILE n 1 136 LYS n 1 137 PRO n 1 138 VAL n 1 139 VAL n 1 140 SER n 1 141 THR n 1 142 GLN n 1 143 LEU n 1 144 LEU n 1 145 LEU n 1 146 ASN n 1 147 GLY n 1 148 SER n 1 149 LEU n 1 150 ALA n 1 151 GLU n 1 152 GLU n 1 153 GLU n 1 154 ILE n 1 155 ILE n 1 156 ILE n 1 157 ARG n 1 158 SER n 1 159 GLU n 1 160 ASN n 1 161 LEU n 1 162 THR n 1 163 ASN n 1 164 ASN n 1 165 ALA n 1 166 LYS n 1 167 THR n 1 168 ILE n 1 169 ILE n 1 170 VAL n 1 171 HIS n 1 172 LEU n 1 173 ASN n 1 174 LYS n 1 175 SER n 1 176 VAL n 1 177 GLU n 1 178 ILE n 1 179 ASN n 1 180 CYS n 1 181 THR n 1 182 ARG n 1 183 PRO n 1 184 SER n 1 185 ASN n 1 186 GLY n 1 187 GLY n 1 188 SER n 1 189 GLY n 1 190 SER n 1 191 GLY n 1 192 GLY n 1 193 ASP n 1 194 ILE n 1 195 ARG n 1 196 LYS n 1 197 ALA n 1 198 TYR n 1 199 CYS n 1 200 GLU n 1 201 ILE n 1 202 ASN n 1 203 GLY n 1 204 THR n 1 205 LYS n 1 206 TRP n 1 207 ASN n 1 208 LYS n 1 209 VAL n 1 210 LEU n 1 211 LYS n 1 212 GLN n 1 213 VAL n 1 214 THR n 1 215 GLU n 1 216 LYS n 1 217 LEU n 1 218 LYS n 1 219 GLU n 1 220 HIS n 1 221 PHE n 1 222 ASN n 1 223 ASN n 1 224 LYS n 1 225 THR n 1 226 ILE n 1 227 ILE n 1 228 PHE n 1 229 GLN n 1 230 PRO n 1 231 PRO n 1 232 SER n 1 233 GLY n 1 234 GLY n 1 235 ASP n 1 236 LEU n 1 237 GLU n 1 238 ILE n 1 239 THR n 1 240 MET n 1 241 HIS n 1 242 HIS n 1 243 PHE n 1 244 ASN n 1 245 CYS n 1 246 ARG n 1 247 GLY n 1 248 GLU n 1 249 PHE n 1 250 PHE n 1 251 TYR n 1 252 CYS n 1 253 ASN n 1 254 THR n 1 255 THR n 1 256 GLN n 1 257 LEU n 1 258 PHE n 1 259 ASN n 1 260 ASN n 1 261 THR n 1 262 CYS n 1 263 ILE n 1 264 GLY n 1 265 ASN n 1 266 GLU n 1 267 THR n 1 268 MET n 1 269 LYS n 1 270 GLY n 1 271 CYS n 1 272 ASN n 1 273 GLY n 1 274 THR n 1 275 ILE n 1 276 THR n 1 277 LEU n 1 278 PRO n 1 279 CYS n 1 280 LYS n 1 281 ILE n 1 282 LYS n 1 283 GLN n 1 284 ILE n 1 285 ILE n 1 286 ASN n 1 287 MET n 1 288 TRP n 1 289 GLN n 1 290 GLY n 1 291 THR n 1 292 GLY n 1 293 GLN n 1 294 ALA n 1 295 MET n 1 296 TYR n 1 297 ALA n 1 298 PRO n 1 299 PRO n 1 300 ILE n 1 301 ASP n 1 302 GLY n 1 303 LYS n 1 304 ILE n 1 305 ASN n 1 306 CYS n 1 307 VAL n 1 308 SER n 1 309 ASN n 1 310 ILE n 1 311 THR n 1 312 GLY n 1 313 ILE n 1 314 LEU n 1 315 LEU n 1 316 THR n 1 317 ARG n 1 318 ASP n 1 319 GLY n 1 320 GLY n 1 321 ALA n 1 322 ASN n 1 323 ASN n 1 324 THR n 1 325 SER n 1 326 ASN n 1 327 GLU n 1 328 THR n 1 329 PHE n 1 330 ARG n 1 331 PRO n 1 332 GLY n 1 333 GLY n 1 334 GLY n 1 335 ASN n 1 336 ILE n 1 337 LYS n 1 338 ASP n 1 339 ASN n 1 340 TRP n 1 341 ARG n 1 342 SER n 1 343 GLU n 1 344 LEU n 1 345 TYR n 1 346 LYS n 1 347 TYR n 1 348 LYS n 1 349 VAL n 1 350 VAL n 1 351 GLN n 1 352 ILE n 1 353 GLU 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 HIV-1 _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'HIV-1 env' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Human immunodeficiency virus 1' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 11676 _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 'HOMO SAPIENS' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 9606 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line 'HEK 293' _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type plasmid _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name pVRC8400 _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name PDB _struct_ref.db_code 3TGT _struct_ref.pdbx_db_accession 3TGT _struct_ref.entity_id 1 _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 3TGT _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 353 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession 3TGT _struct_ref_seq.db_align_beg 44 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 492 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 44 _struct_ref_seq.pdbx_auth_seq_align_end 492 # 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 EPE non-polymer . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S' 238.305 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 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 3TGT _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.39 _exptl_crystal.density_percent_sol 48.49 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.5 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '14% PEG 1500, 12% PEG 400, 0.1M HEPES, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 7.5' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type 'MAR scanner 300 mm plate' _diffrn_detector.pdbx_collection_date 2010-07-16 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'APS BEAMLINE 22-BM' _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 22-BM _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 3TGT _reflns.observed_criterion_sigma_I 0.0 _reflns.observed_criterion_sigma_F 0.0 _reflns.d_resolution_low 50 _reflns.d_resolution_high 1.9 _reflns.number_obs 30907 _reflns.number_all 32465 _reflns.percent_possible_obs 95.2 _reflns.pdbx_Rmerge_I_obs 0.084 _reflns.pdbx_Rsym_value 0.074 _reflns.pdbx_netI_over_sigmaI 38.5 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 6.8 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? # loop_ _reflns_shell.pdbx_diffrn_id _reflns_shell.pdbx_ordinal _reflns_shell.d_res_high _reflns_shell.d_res_low _reflns_shell.percent_possible_all _reflns_shell.Rmerge_I_obs _reflns_shell.pdbx_Rsym_value _reflns_shell.meanI_over_sigI_obs _reflns_shell.pdbx_redundancy _reflns_shell.percent_possible_obs _reflns_shell.number_unique_all _reflns_shell.number_measured_all _reflns_shell.number_measured_obs _reflns_shell.number_unique_obs _reflns_shell.pdbx_chi_squared 1 1 1.90 1.93 86.5 0.615 0.555 2.1 5.5 ? ? ? ? ? ? 1 2 1.93 1.97 89.9 0.498 0.452 2.7 5.8 ? ? ? ? ? ? 1 3 1.97 2.01 95.2 0.479 0.416 3.1 6.0 ? ? ? ? ? ? 1 4 2.01 2.05 97.8 0.419 0.368 3.7 6.4 ? ? ? ? ? ? 1 5 2.05 2.09 99.5 0.377 0.339 4.9 6.7 ? ? ? ? ? ? 1 6 2.09 2.14 99.8 0.327 0.269 6.3 6.9 ? ? ? ? ? ? 1 7 2.14 2.19 100.0 0.296 0.265 7.3 7.1 ? ? ? ? ? ? 1 8 2.19 2.25 100.0 0.257 0.226 9.6 7.2 ? ? ? ? ? ? 1 9 2.25 2.32 100.0 0.219 0.197 11.9 7.3 ? ? ? ? ? ? 1 10 2.32 2.39 99.9 0.190 0.172 15.5 7.3 ? ? ? ? ? ? 1 11 2.39 2.48 100.0 0.171 0.155 16.5 7.2 ? ? ? ? ? ? 1 12 2.48 2.58 100.0 0.144 0.137 20.9 7.2 ? ? ? ? ? ? 1 13 2.58 2.70 100.0 0.129 0.126 24.6 7.2 ? ? ? ? ? ? 1 14 2.70 2.84 99.9 0.115 0.116 28.7 7.1 ? ? ? ? ? ? 1 15 2.84 3.02 100.0 0.101 0.103 34.5 7.1 ? ? ? ? ? ? 1 16 3.02 3.25 99.9 0.091 0.093 41.9 6.9 ? ? ? ? ? ? 1 17 3.25 3.58 100.0 0.085 0.090 46.2 6.6 ? ? ? ? ? ? 1 18 3.58 4.09 99.9 0.075 0.081 51.3 6.3 ? ? ? ? ? ? 1 19 4.09 5.16 99.9 0.067 0.075 57.3 6.6 ? ? ? ? ? ? 1 20 5.16 50.00 98.1 0.053 0.062 57.9 6.4 ? ? ? ? ? ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 3TGT _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 29250 _refine.ls_number_reflns_all 31824 _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.11 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 24.571 _refine.ls_d_res_high 1.9 _refine.ls_percent_reflns_obs 91.91 _refine.ls_R_factor_obs 0.1910 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.1890 _refine.ls_R_factor_R_free 0.2307 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.91 _refine.ls_number_reflns_R_free 1437 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min 1.000 _refine.occupancy_max 1.000 _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] 10.7220 _refine.aniso_B[2][2] -4.9969 _refine.aniso_B[3][3] -5.7251 _refine.aniso_B[1][2] -0.0000 _refine.aniso_B[1][3] -0.0000 _refine.aniso_B[2][3] -0.0000 _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol 0.329 _refine.solvent_model_param_bsol 36.441 _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.24 _refine.pdbx_overall_phase_error 23.44 _refine.overall_SU_B ? _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.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2677 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 155 _refine_hist.number_atoms_solvent 148 _refine_hist.number_atoms_total 2980 _refine_hist.d_res_high 1.9 _refine_hist.d_res_low 24.571 # 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 f_bond_d 0.007 ? ? 2921 'X-RAY DIFFRACTION' ? f_angle_d 1.198 ? ? 3960 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 15.937 ? ? 1105 'X-RAY DIFFRACTION' ? f_chiral_restr 0.069 ? ? 462 'X-RAY DIFFRACTION' ? f_plane_restr 0.004 ? ? 492 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all _refine_ls_shell.redundancy_reflns_obs _refine_ls_shell.number_reflns_obs 'X-RAY DIFFRACTION' . 1.8676 1.9343 1817 0.2349 61.00 0.2307 . . 83 . . . . 'X-RAY DIFFRACTION' . 1.9343 2.0117 2475 0.2176 84.00 0.2760 . . 152 . . . . 'X-RAY DIFFRACTION' . 2.0117 2.1032 2717 0.2093 92.00 0.3130 . . 166 . . . . 'X-RAY DIFFRACTION' . 2.1032 2.2140 2814 0.2029 94.00 0.2610 . . 144 . . . . 'X-RAY DIFFRACTION' . 2.2140 2.3526 2858 0.1970 95.00 0.2560 . . 141 . . . . 'X-RAY DIFFRACTION' . 2.3526 2.5341 2896 0.2037 97.00 0.2440 . . 158 . . . . 'X-RAY DIFFRACTION' . 2.5341 2.7888 2953 0.1966 98.00 0.2692 . . 152 . . . . 'X-RAY DIFFRACTION' . 2.7888 3.1916 3038 0.1973 99.00 0.2095 . . 142 . . . . 'X-RAY DIFFRACTION' . 3.1916 4.0182 3055 0.1776 99.00 0.2326 . . 145 . . . . 'X-RAY DIFFRACTION' . 4.0182 24.5735 3190 0.1747 99.00 0.1972 . . 154 . . . . # _struct.entry_id 3TGT _struct.title 'Crystal structure of unliganded HIV-1 clade A/E strain 93TH057 gp120 core' _struct.pdbx_descriptor 'HIV-1 clade A/E 93TH057 gp120' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3TGT _struct_keywords.text 'HIV-1 gp120, unliganded structure, clade A/E 93TH057, VIRAL PROTEIN' _struct_keywords.pdbx_keywords 'VIRAL PROTEIN' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 2 ? E N N 2 ? F N N 2 ? G N N 2 ? H N N 2 ? I N N 2 ? J N N 2 ? K N N 2 ? L N N 3 ? M N N 4 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 GLU A 21 ? CYS A 31 ? GLU A 64 CYS A 74 1 ? 11 HELX_P HELX_P2 2 ASN A 55 ? LEU A 73 ? ASN A 98 LEU A 116 1 ? 19 HELX_P HELX_P3 3 GLY A 203 ? PHE A 221 ? GLY A 335 PHE A 353 1 ? 19 HELX_P HELX_P4 4 ASP A 235 ? MET A 240 ? ASP A 368 MET A 373 1 ? 6 HELX_P HELX_P5 5 THR A 254 ? ILE A 263 ? THR A 387 ILE A 396 5 ? 10 HELX_P HELX_P6 6 GLY A 320 ? THR A 324 ? GLY A 459 THR A 463 5 ? 5 HELX_P HELX_P7 7 ASN A 335 ? TYR A 345 ? ASN A 474 TYR A 484 1 ? 11 # _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 11 SG ? ? ? 1_555 A CYS 31 SG ? ? A CYS 54 A CYS 74 1_555 ? ? ? ? ? ? ? 2.058 ? disulf2 disulf ? ? A CYS 76 SG ? ? ? 1_555 A CYS 89 SG ? ? A CYS 119 A CYS 205 1_555 ? ? ? ? ? ? ? 2.031 ? disulf3 disulf ? ? A CYS 102 SG ? ? ? 1_555 A CYS 131 SG ? ? A CYS 218 A CYS 247 1_555 ? ? ? ? ? ? ? 2.045 ? disulf4 disulf ? ? A CYS 112 SG ? ? ? 1_555 A CYS 123 SG ? ? A CYS 228 A CYS 239 1_555 ? ? ? ? ? ? ? 2.079 ? disulf5 disulf ? ? A CYS 180 SG ? ? ? 1_555 A CYS 199 SG ? ? A CYS 296 A CYS 331 1_555 ? ? ? ? ? ? ? 2.047 ? disulf6 disulf ? ? A CYS 245 SG ? ? ? 1_555 A CYS 306 SG ? ? A CYS 378 A CYS 445 1_555 ? ? ? ? ? ? ? 2.029 ? disulf7 disulf ? ? A CYS 252 SG ? ? ? 1_555 A CYS 279 SG ? ? A CYS 385 A CYS 418 1_555 ? ? ? ? ? ? ? 2.036 ? disulf8 disulf ? ? A CYS 262 SG ? ? ? 1_555 A CYS 271 SG ? ? A CYS 395 A CYS 410 1_555 ? ? ? ? ? ? ? 2.034 ? covale1 covale ? ? A ASN 118 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 234 A NAG 734 1_555 ? ? ? ? ? ? ? 1.309 ? covale2 covale ? ? A ASN 202 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 334 A NAG 834 1_555 ? ? ? ? ? ? ? 1.434 ? covale3 covale ? ? A ASN 253 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 386 A NAG 886 1_555 ? ? ? ? ? ? ? 1.436 ? covale4 covale ? ? A ASN 309 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 448 A NAG 948 1_555 ? ? ? ? ? ? ? 1.437 ? covale5 covale ? ? A ASN 173 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 289 A NAG 789 1_555 ? ? ? ? ? ? ? 1.445 ? covale6 covale ? ? A ASN 125 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 241 A NAG 741 1_555 ? ? ? ? ? ? ? 1.446 ? covale7 covale ? ? A ASN 146 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 262 A NAG 762 1_555 ? ? ? ? ? ? ? 1.448 ? covale8 covale ? ? A ASN 179 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 295 A NAG 795 1_555 ? ? ? ? ? ? ? 1.449 ? covale9 covale ? ? A ASN 259 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 392 A NAG 892 1_555 ? ? ? ? ? ? ? 1.451 ? covale10 covale ? ? A ASN 160 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 276 A NAG 776 1_555 ? ? ? ? ? ? ? 1.491 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 5 ? B ? 3 ? C ? 2 ? D ? 4 ? E ? 5 ? F ? 7 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel B 1 2 ? parallel B 2 3 ? anti-parallel C 1 2 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 4 5 ? parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 4 5 ? anti-parallel F 5 6 ? anti-parallel F 6 7 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 TRP A 2 ? ASP A 4 ? TRP A 45 ASP A 47 A 2 TYR A 347 ? ILE A 352 ? TYR A 486 ILE A 491 A 3 TYR A 107 ? CYS A 112 ? TYR A 223 CYS A 228 A 4 VAL A 126 ? VAL A 129 ? VAL A 242 VAL A 245 A 5 GLU A 40 ? HIS A 42 ? GLU A 83 HIS A 85 B 1 VAL A 32 ? PRO A 33 ? VAL A 75 PRO A 76 B 2 PHE A 10 ? SER A 13 ? PHE A 53 SER A 56 B 3 HIS A 100 ? CYS A 102 ? HIS A 216 CYS A 218 C 1 GLU A 48 ? ASN A 51 ? GLU A 91 ASN A 94 C 2 THR A 120 ? CYS A 123 ? THR A 236 CYS A 239 D 1 SER A 83 ? LYS A 86 ? SER A 199 LYS A 202 D 2 VAL A 77 ? THR A 80 ? VAL A 120 THR A 123 D 3 GLN A 293 ? MET A 295 ? GLN A 432 MET A 434 D 4 ILE A 284 ? ASN A 286 ? ILE A 423 ASN A 425 E 1 LEU A 143 ? LEU A 145 ? LEU A 259 LEU A 261 E 2 ILE A 304 ? ARG A 317 ? ILE A 443 ARG A 456 E 3 ILE A 168 ? ARG A 182 ? ILE A 284 ARG A 298 E 4 ASN A 326 ? PRO A 331 ? ASN A 465 PRO A 470 E 5 THR A 225 ? PHE A 228 ? THR A 358 PHE A 361 F 1 ILE A 155 ? ARG A 157 ? ILE A 271 ARG A 273 F 2 ILE A 168 ? ARG A 182 ? ILE A 284 ARG A 298 F 3 ILE A 304 ? ARG A 317 ? ILE A 443 ARG A 456 F 4 LYS A 196 ? ASN A 202 ? LYS A 328 ASN A 334 F 5 THR A 274 ? ILE A 281 ? THR A 413 ILE A 420 F 6 GLU A 248 ? CYS A 252 ? GLU A 381 CYS A 385 F 7 HIS A 241 ? CYS A 245 ? HIS A 374 CYS A 378 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N LYS A 3 ? N LYS A 46 O GLN A 351 ? O GLN A 490 A 2 3 O LYS A 348 ? O LYS A 487 N LEU A 110 ? N LEU A 226 A 3 4 N LYS A 111 ? N LYS A 227 O SER A 127 ? O SER A 243 A 4 5 O SER A 128 ? O SER A 244 N ILE A 41 ? N ILE A 84 B 1 2 O VAL A 32 ? O VAL A 75 N CYS A 11 ? N CYS A 54 B 2 3 N ALA A 12 ? N ALA A 55 O HIS A 100 ? O HIS A 216 C 1 2 N PHE A 50 ? N PHE A 93 O GLY A 121 ? O GLY A 237 D 1 2 O SER A 83 ? O SER A 199 N THR A 80 ? N THR A 123 D 2 3 N LEU A 79 ? N LEU A 122 O GLN A 293 ? O GLN A 432 D 3 4 O ALA A 294 ? O ALA A 433 N ILE A 285 ? N ILE A 424 E 1 2 N LEU A 144 ? N LEU A 260 O THR A 311 ? O THR A 450 E 2 3 O ILE A 313 ? O ILE A 452 N VAL A 170 ? N VAL A 286 E 4 5 O PHE A 329 ? O PHE A 468 N ILE A 227 ? N ILE A 360 F 1 2 N ILE A 155 ? N ILE A 271 O HIS A 171 ? O HIS A 287 F 2 3 N VAL A 170 ? N VAL A 286 O ILE A 313 ? O ILE A 452 F 4 5 N ILE A 201 ? N ILE A 333 O ILE A 275 ? O ILE A 414 F 5 6 O LYS A 280 ? O LYS A 419 N TYR A 251 ? N TYR A 384 F 6 7 O PHE A 250 ? O PHE A 383 N PHE A 243 ? N PHE A 376 # 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 ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 734' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 741' AC3 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE NAG A 762' AC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 776' AC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 789' AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 795' AC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 834' AC8 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 886' AC9 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 892' BC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 948' BC2 Software ? ? ? ? 14 'BINDING SITE FOR RESIDUE EPE A 1' # 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 6 HIS A 18 ? HIS A 61 . ? 2_555 ? 2 AC1 6 ASN A 118 ? ASN A 234 . ? 1_555 ? 3 AC1 6 THR A 120 ? THR A 236 . ? 1_555 ? 4 AC1 6 ILE A 156 ? ILE A 272 . ? 1_555 ? 5 AC1 6 HIS A 220 ? HIS A 352 . ? 1_555 ? 6 AC1 6 HOH M . ? HOH A 504 . ? 1_555 ? 7 AC2 3 ASN A 113 ? ASN A 229 . ? 1_555 ? 8 AC2 3 ASN A 125 ? ASN A 241 . ? 1_555 ? 9 AC2 3 NAG H . ? NAG A 834 . ? 3_654 ? 10 AC3 11 HOH M . ? HOH A 34 . ? 1_555 ? 11 AC3 11 HOH M . ? HOH A 39 . ? 1_555 ? 12 AC3 11 HOH M . ? HOH A 42 . ? 1_555 ? 13 AC3 11 LYS A 136 ? LYS A 252 . ? 1_555 ? 14 AC3 11 ASN A 146 ? ASN A 262 . ? 1_555 ? 15 AC3 11 ARG A 246 ? ARG A 379 . ? 1_555 ? 16 AC3 11 CYS A 306 ? CYS A 445 . ? 1_555 ? 17 AC3 11 VAL A 307 ? VAL A 446 . ? 1_555 ? 18 AC3 11 SER A 308 ? SER A 447 . ? 1_555 ? 19 AC3 11 HOH M . ? HOH A 535 . ? 1_555 ? 20 AC3 11 NAG K . ? NAG A 948 . ? 1_555 ? 21 AC4 3 GLY A 82 ? GLY A 198 . ? 4_545 ? 22 AC4 3 ASN A 160 ? ASN A 276 . ? 1_555 ? 23 AC4 3 ASN A 163 ? ASN A 279 . ? 1_555 ? 24 AC5 5 GLU A 152 ? GLU A 268 . ? 1_555 ? 25 AC5 5 GLU A 153 ? GLU A 269 . ? 1_555 ? 26 AC5 5 ILE A 154 ? ILE A 270 . ? 1_555 ? 27 AC5 5 ASN A 173 ? ASN A 289 . ? 1_555 ? 28 AC5 5 HOH M . ? HOH A 550 . ? 1_555 ? 29 AC6 4 ASN A 179 ? ASN A 295 . ? 1_555 ? 30 AC6 4 TYR A 198 ? TYR A 330 . ? 1_555 ? 31 AC6 4 GLU A 200 ? GLU A 332 . ? 1_555 ? 32 AC6 4 HOH M . ? HOH A 525 . ? 1_555 ? 33 AC7 6 PRO A 38 ? PRO A 81 . ? 3_644 ? 34 AC7 6 GLU A 40 ? GLU A 83 . ? 3_644 ? 35 AC7 6 ASN A 202 ? ASN A 334 . ? 1_555 ? 36 AC7 6 LYS A 205 ? LYS A 337 . ? 1_555 ? 37 AC7 6 THR A 274 ? THR A 413 . ? 1_555 ? 38 AC7 6 NAG C . ? NAG A 741 . ? 3_644 ? 39 AC8 2 ASN A 253 ? ASN A 386 . ? 1_555 ? 40 AC8 2 THR A 255 ? THR A 388 . ? 1_555 ? 41 AC9 6 THR A 255 ? THR A 388 . ? 1_555 ? 42 AC9 6 GLN A 256 ? GLN A 389 . ? 1_555 ? 43 AC9 6 ASN A 259 ? ASN A 392 . ? 1_555 ? 44 AC9 6 THR A 261 ? THR A 394 . ? 1_555 ? 45 AC9 6 LYS A 269 ? LYS A 408 . ? 1_555 ? 46 AC9 6 CYS A 271 ? CYS A 410 . ? 1_555 ? 47 BC1 5 ASN A 146 ? ASN A 262 . ? 1_555 ? 48 BC1 5 LEU A 149 ? LEU A 265 . ? 1_555 ? 49 BC1 5 SER A 175 ? SER A 291 . ? 1_555 ? 50 BC1 5 ASN A 309 ? ASN A 448 . ? 1_555 ? 51 BC1 5 NAG D . ? NAG A 762 . ? 1_555 ? 52 BC2 14 LEU A 9 ? LEU A 52 . ? 1_555 ? 53 BC2 14 CYS A 11 ? CYS A 54 . ? 1_555 ? 54 BC2 14 ALA A 30 ? ALA A 73 . ? 1_555 ? 55 BC2 14 GLN A 60 ? GLN A 103 . ? 1_555 ? 56 BC2 14 ASP A 64 ? ASP A 107 . ? 1_555 ? 57 BC2 14 TYR A 101 ? TYR A 217 . ? 1_555 ? 58 BC2 14 ARG A 195 ? ARG A 327 . ? 3_554 ? 59 BC2 14 LYS A 280 ? LYS A 419 . ? 3_554 ? 60 BC2 14 ILE A 281 ? ILE A 420 . ? 3_554 ? 61 BC2 14 LYS A 282 ? LYS A 421 . ? 3_554 ? 62 BC2 14 GLN A 283 ? GLN A 422 . ? 3_554 ? 63 BC2 14 ILE A 284 ? ILE A 423 . ? 3_554 ? 64 BC2 14 HOH M . ? HOH A 519 . ? 1_555 ? 65 BC2 14 HOH M . ? HOH A 521 . ? 1_555 ? # _atom_sites.entry_id 3TGT _atom_sites.fract_transf_matrix[1][1] 0.015734 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.014938 _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] 0.011360 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . VAL A 1 1 ? 24.217 17.988 -1.032 1.00 69.68 ? 44 VAL A N 1 ATOM 2 C CA . VAL A 1 1 ? 23.810 17.080 0.039 1.00 70.70 ? 44 VAL A CA 1 ATOM 3 C C . VAL A 1 1 ? 22.387 16.568 -0.192 1.00 67.04 ? 44 VAL A C 1 ATOM 4 O O . VAL A 1 1 ? 21.572 17.236 -0.834 1.00 65.85 ? 44 VAL A O 1 ATOM 5 C CB . VAL A 1 1 ? 23.920 17.750 1.411 1.00 71.65 ? 44 VAL A CB 1 ATOM 6 C CG1 . VAL A 1 1 ? 23.612 16.748 2.529 1.00 74.12 ? 44 VAL A CG1 1 ATOM 7 C CG2 . VAL A 1 1 ? 25.313 18.354 1.585 1.00 70.29 ? 44 VAL A CG2 1 ATOM 8 N N . TRP A 1 2 ? 22.093 15.385 0.341 1.00 62.92 ? 45 TRP A N 1 ATOM 9 C CA . TRP A 1 2 ? 20.904 14.636 -0.065 1.00 56.11 ? 45 TRP A CA 1 ATOM 10 C C . TRP A 1 2 ? 20.377 13.715 1.041 1.00 53.52 ? 45 TRP A C 1 ATOM 11 O O . TRP A 1 2 ? 21.036 13.512 2.064 1.00 52.59 ? 45 TRP A O 1 ATOM 12 C CB . TRP A 1 2 ? 21.234 13.814 -1.314 1.00 54.58 ? 45 TRP A CB 1 ATOM 13 C CG . TRP A 1 2 ? 22.425 12.926 -1.115 1.00 57.92 ? 45 TRP A CG 1 ATOM 14 C CD1 . TRP A 1 2 ? 22.461 11.741 -0.433 1.00 57.70 ? 45 TRP A CD1 1 ATOM 15 C CD2 . TRP A 1 2 ? 23.758 13.156 -1.589 1.00 62.94 ? 45 TRP A CD2 1 ATOM 16 N NE1 . TRP A 1 2 ? 23.734 11.222 -0.454 1.00 57.47 ? 45 TRP A NE1 1 ATOM 17 C CE2 . TRP A 1 2 ? 24.549 12.072 -1.152 1.00 59.19 ? 45 TRP A CE2 1 ATOM 18 C CE3 . TRP A 1 2 ? 24.361 14.176 -2.335 1.00 69.06 ? 45 TRP A CE3 1 ATOM 19 C CZ2 . TRP A 1 2 ? 25.913 11.979 -1.432 1.00 60.27 ? 45 TRP A CZ2 1 ATOM 20 C CZ3 . TRP A 1 2 ? 25.719 14.081 -2.615 1.00 70.06 ? 45 TRP A CZ3 1 ATOM 21 C CH2 . TRP A 1 2 ? 26.477 12.986 -2.167 1.00 65.46 ? 45 TRP A CH2 1 ATOM 22 N N . LYS A 1 3 ? 19.182 13.171 0.825 1.00 51.42 ? 46 LYS A N 1 ATOM 23 C CA . LYS A 1 3 ? 18.561 12.205 1.735 1.00 49.30 ? 46 LYS A CA 1 ATOM 24 C C . LYS A 1 3 ? 17.774 11.190 0.901 1.00 47.24 ? 46 LYS A C 1 ATOM 25 O O . LYS A 1 3 ? 17.197 11.552 -0.125 1.00 43.34 ? 46 LYS A O 1 ATOM 26 C CB . LYS A 1 3 ? 17.619 12.908 2.710 1.00 49.57 ? 46 LYS A CB 1 ATOM 27 C CG . LYS A 1 3 ? 18.358 13.725 3.773 1.00 73.07 ? 46 LYS A CG 1 ATOM 28 C CD . LYS A 1 3 ? 17.412 14.398 4.780 1.00 84.82 ? 46 LYS A CD 1 ATOM 29 C CE . LYS A 1 3 ? 18.172 15.373 5.690 1.00 90.13 ? 46 LYS A CE 1 ATOM 30 N NZ . LYS A 1 3 ? 17.284 16.137 6.616 1.00 91.76 ? 46 LYS A NZ 1 ATOM 31 N N . ASP A 1 4 ? 17.763 9.928 1.329 1.00 46.92 ? 47 ASP A N 1 ATOM 32 C CA . ASP A 1 4 ? 16.975 8.901 0.647 1.00 48.32 ? 47 ASP A CA 1 ATOM 33 C C . ASP A 1 4 ? 15.534 9.396 0.536 1.00 50.27 ? 47 ASP A C 1 ATOM 34 O O . ASP A 1 4 ? 14.944 9.839 1.527 1.00 47.59 ? 47 ASP A O 1 ATOM 35 C CB . ASP A 1 4 ? 16.975 7.578 1.431 1.00 50.48 ? 47 ASP A CB 1 ATOM 36 C CG . ASP A 1 4 ? 18.348 6.928 1.530 1.00 53.06 ? 47 ASP A CG 1 ATOM 37 O OD1 . ASP A 1 4 ? 19.300 7.372 0.860 1.00 52.11 ? 47 ASP A OD1 1 ATOM 38 O OD2 . ASP A 1 4 ? 18.467 5.938 2.282 1.00 57.63 ? 47 ASP A OD2 1 ATOM 39 N N . ALA A 1 5 ? 14.959 9.300 -0.657 1.00 48.63 ? 48 ALA A N 1 ATOM 40 C CA . ALA A 1 5 ? 13.586 9.749 -0.870 1.00 44.54 ? 48 ALA A CA 1 ATOM 41 C C . ALA A 1 5 ? 12.938 8.921 -1.956 1.00 42.80 ? 48 ALA A C 1 ATOM 42 O O . ALA A 1 5 ? 13.622 8.335 -2.794 1.00 42.83 ? 48 ALA A O 1 ATOM 43 C CB . ALA A 1 5 ? 13.562 11.208 -1.260 1.00 47.29 ? 48 ALA A CB 1 ATOM 44 N N . ASP A 1 6 ? 11.613 8.872 -1.941 1.00 44.19 ? 49 ASP A N 1 ATOM 45 C CA . ASP A 1 6 ? 10.870 8.302 -3.057 1.00 41.17 ? 49 ASP A CA 1 ATOM 46 C C . ASP A 1 6 ? 10.201 9.430 -3.828 1.00 43.60 ? 49 ASP A C 1 ATOM 47 O O . ASP A 1 6 ? 9.719 10.404 -3.235 1.00 48.88 ? 49 ASP A O 1 ATOM 48 C CB . ASP A 1 6 ? 9.814 7.311 -2.565 1.00 41.33 ? 49 ASP A CB 1 ATOM 49 C CG . ASP A 1 6 ? 10.424 6.075 -1.921 1.00 47.61 ? 49 ASP A CG 1 ATOM 50 O OD1 . ASP A 1 6 ? 11.584 5.730 -2.251 1.00 48.13 ? 49 ASP A OD1 1 ATOM 51 O OD2 . ASP A 1 6 ? 9.737 5.454 -1.084 1.00 48.64 ? 49 ASP A OD2 1 ATOM 52 N N . THR A 1 7 ? 10.190 9.303 -5.146 1.00 40.13 ? 50 THR A N 1 ATOM 53 C CA . THR A 1 7 ? 9.416 10.191 -5.994 1.00 39.72 ? 50 THR A CA 1 ATOM 54 C C . THR A 1 7 ? 9.061 9.450 -7.282 1.00 36.88 ? 50 THR A C 1 ATOM 55 O O . THR A 1 7 ? 9.640 8.405 -7.592 1.00 35.41 ? 50 THR A O 1 ATOM 56 C CB . THR A 1 7 ? 10.190 11.473 -6.328 1.00 41.77 ? 50 THR A CB 1 ATOM 57 O OG1 . THR A 1 7 ? 9.291 12.461 -6.841 1.00 44.78 ? 50 THR A OG1 1 ATOM 58 C CG2 . THR A 1 7 ? 11.283 11.202 -7.344 1.00 43.98 ? 50 THR A CG2 1 ATOM 59 N N . THR A 1 8 ? 8.106 9.984 -8.032 1.00 40.10 ? 51 THR A N 1 ATOM 60 C CA . THR A 1 8 ? 7.728 9.384 -9.314 1.00 37.08 ? 51 THR A CA 1 ATOM 61 C C . THR A 1 8 ? 8.814 9.604 -10.374 1.00 37.76 ? 51 THR A C 1 ATOM 62 O O . THR A 1 8 ? 9.101 10.731 -10.751 1.00 38.09 ? 51 THR A O 1 ATOM 63 C CB . THR A 1 8 ? 6.390 9.972 -9.840 1.00 41.30 ? 51 THR A CB 1 ATOM 64 O OG1 . THR A 1 8 ? 5.364 9.792 -8.854 1.00 44.90 ? 51 THR A OG1 1 ATOM 65 C CG2 . THR A 1 8 ? 5.963 9.266 -11.124 1.00 44.15 ? 51 THR A CG2 1 ATOM 66 N N . LEU A 1 9 ? 9.419 8.524 -10.851 1.00 33.62 ? 52 LEU A N 1 ATOM 67 C CA . LEU A 1 9 ? 10.414 8.608 -11.925 1.00 34.78 ? 52 LEU A CA 1 ATOM 68 C C . LEU A 1 9 ? 9.752 8.833 -13.275 1.00 37.25 ? 52 LEU A C 1 ATOM 69 O O . LEU A 1 9 ? 8.538 8.674 -13.415 1.00 35.82 ? 52 LEU A O 1 ATOM 70 C CB . LEU A 1 9 ? 11.219 7.304 -12.003 1.00 26.69 ? 52 LEU A CB 1 ATOM 71 C CG . LEU A 1 9 ? 11.866 6.931 -10.670 1.00 33.49 ? 52 LEU A CG 1 ATOM 72 C CD1 . LEU A 1 9 ? 12.446 5.531 -10.691 1.00 38.56 ? 52 LEU A CD1 1 ATOM 73 C CD2 . LEU A 1 9 ? 12.923 7.964 -10.288 1.00 43.55 ? 52 LEU A CD2 1 ATOM 74 N N . PHE A 1 10 ? 10.549 9.183 -14.279 1.00 27.76 ? 53 PHE A N 1 ATOM 75 C CA . PHE A 1 10 ? 10.043 9.098 -15.630 1.00 31.11 ? 53 PHE A CA 1 ATOM 76 C C . PHE A 1 10 ? 10.943 8.153 -16.409 1.00 34.66 ? 53 PHE A C 1 ATOM 77 O O . PHE A 1 10 ? 11.991 7.734 -15.910 1.00 33.72 ? 53 PHE A O 1 ATOM 78 C CB . PHE A 1 10 ? 9.920 10.468 -16.315 1.00 32.07 ? 53 PHE A CB 1 ATOM 79 C CG . PHE A 1 10 ? 11.221 11.168 -16.541 1.00 32.56 ? 53 PHE A CG 1 ATOM 80 C CD1 . PHE A 1 10 ? 11.751 12.014 -15.561 1.00 35.32 ? 53 PHE A CD1 1 ATOM 81 C CD2 . PHE A 1 10 ? 11.898 11.021 -17.742 1.00 30.25 ? 53 PHE A CD2 1 ATOM 82 C CE1 . PHE A 1 10 ? 12.956 12.680 -15.768 1.00 39.83 ? 53 PHE A CE1 1 ATOM 83 C CE2 . PHE A 1 10 ? 13.094 11.685 -17.975 1.00 35.46 ? 53 PHE A CE2 1 ATOM 84 C CZ . PHE A 1 10 ? 13.630 12.520 -16.982 1.00 40.24 ? 53 PHE A CZ 1 ATOM 85 N N . CYS A 1 11 ? 10.525 7.786 -17.609 1.00 29.92 ? 54 CYS A N 1 ATOM 86 C CA . CYS A 1 11 ? 11.358 6.915 -18.422 1.00 29.07 ? 54 CYS A CA 1 ATOM 87 C C . CYS A 1 11 ? 11.863 7.595 -19.689 1.00 34.64 ? 54 CYS A C 1 ATOM 88 O O . CYS A 1 11 ? 11.261 8.551 -20.200 1.00 36.64 ? 54 CYS A O 1 ATOM 89 C CB . CYS A 1 11 ? 10.638 5.608 -18.751 1.00 32.23 ? 54 CYS A CB 1 ATOM 90 S SG . CYS A 1 11 ? 9.064 5.802 -19.635 1.00 35.64 ? 54 CYS A SG 1 ATOM 91 N N . ALA A 1 12 ? 12.976 7.069 -20.188 1.00 31.36 ? 55 ALA A N 1 ATOM 92 C CA . ALA A 1 12 ? 13.578 7.514 -21.429 1.00 32.89 ? 55 ALA A CA 1 ATOM 93 C C . ALA A 1 12 ? 13.954 6.269 -22.220 1.00 35.11 ? 55 ALA A C 1 ATOM 94 O O . ALA A 1 12 ? 14.254 5.228 -21.630 1.00 35.22 ? 55 ALA A O 1 ATOM 95 C CB . ALA A 1 12 ? 14.802 8.389 -21.160 1.00 34.76 ? 55 ALA A CB 1 ATOM 96 N N . SER A 1 13 ? 13.918 6.383 -23.548 1.00 34.52 ? 56 SER A N 1 ATOM 97 C CA . SER A 1 13 ? 14.244 5.283 -24.457 1.00 35.67 ? 56 SER A CA 1 ATOM 98 C C . SER A 1 13 ? 14.595 5.795 -25.857 1.00 36.34 ? 56 SER A C 1 ATOM 99 O O . SER A 1 13 ? 14.394 6.972 -26.182 1.00 33.33 ? 56 SER A O 1 ATOM 100 C CB . SER A 1 13 ? 13.062 4.329 -24.597 1.00 35.04 ? 56 SER A CB 1 ATOM 101 O OG . SER A 1 13 ? 12.173 4.812 -25.593 1.00 35.78 ? 56 SER A OG 1 ATOM 102 N N . ASP A 1 14 ? 15.090 4.884 -26.684 1.00 39.54 ? 57 ASP A N 1 ATOM 103 C CA . ASP A 1 14 ? 15.356 5.169 -28.086 1.00 41.53 ? 57 ASP A CA 1 ATOM 104 C C . ASP A 1 14 ? 14.308 4.530 -28.990 1.00 42.74 ? 57 ASP A C 1 ATOM 105 O O . ASP A 1 14 ? 14.611 4.166 -30.128 1.00 41.62 ? 57 ASP A O 1 ATOM 106 C CB . ASP A 1 14 ? 16.759 4.696 -28.483 1.00 43.27 ? 57 ASP A CB 1 ATOM 107 C CG . ASP A 1 14 ? 17.857 5.484 -27.785 1.00 46.86 ? 57 ASP A CG 1 ATOM 108 O OD1 . ASP A 1 14 ? 17.702 6.718 -27.632 1.00 42.43 ? 57 ASP A OD1 1 ATOM 109 O OD2 . ASP A 1 14 ? 18.862 4.865 -27.369 1.00 50.32 ? 57 ASP A OD2 1 ATOM 110 N N . ALA A 1 15 ? 13.085 4.395 -28.479 1.00 36.08 ? 58 ALA A N 1 ATOM 111 C CA . ALA A 1 15 ? 11.987 3.843 -29.269 1.00 35.12 ? 58 ALA A CA 1 ATOM 112 C C . ALA A 1 15 ? 11.880 4.560 -30.615 1.00 40.29 ? 58 ALA A C 1 ATOM 113 O O . ALA A 1 15 ? 12.077 5.769 -30.702 1.00 38.10 ? 58 ALA A O 1 ATOM 114 C CB . ALA A 1 15 ? 10.679 3.951 -28.514 1.00 34.78 ? 58 ALA A CB 1 ATOM 115 N N . LYS A 1 16 ? 11.556 3.798 -31.656 1.00 38.73 ? 59 LYS A N 1 ATOM 116 C CA . LYS A 1 16 ? 11.364 4.338 -32.989 1.00 47.00 ? 59 LYS A CA 1 ATOM 117 C C . LYS A 1 16 ? 9.880 4.590 -33.213 1.00 43.18 ? 59 LYS A C 1 ATOM 118 O O . LYS A 1 16 ? 9.065 3.700 -33.004 1.00 35.32 ? 59 LYS A O 1 ATOM 119 C CB . LYS A 1 16 ? 11.914 3.356 -34.020 1.00 50.88 ? 59 LYS A CB 1 ATOM 120 C CG . LYS A 1 16 ? 13.421 3.165 -33.898 1.00 65.28 ? 59 LYS A CG 1 ATOM 121 C CD . LYS A 1 16 ? 13.850 1.725 -34.134 1.00 75.74 ? 59 LYS A CD 1 ATOM 122 C CE . LYS A 1 16 ? 13.512 0.814 -32.940 1.00 86.71 ? 59 LYS A CE 1 ATOM 123 N NZ . LYS A 1 16 ? 14.325 1.067 -31.699 1.00 82.44 ? 59 LYS A NZ 1 ATOM 124 N N . ALA A 1 17 ? 9.531 5.808 -33.624 1.00 40.03 ? 60 ALA A N 1 ATOM 125 C CA . ALA A 1 17 ? 8.127 6.189 -33.756 1.00 40.42 ? 60 ALA A CA 1 ATOM 126 C C . ALA A 1 17 ? 7.403 5.468 -34.902 1.00 41.80 ? 60 ALA A C 1 ATOM 127 O O . ALA A 1 17 ? 6.176 5.361 -34.910 1.00 45.64 ? 60 ALA A O 1 ATOM 128 C CB . ALA A 1 17 ? 7.999 7.704 -33.900 1.00 44.20 ? 60 ALA A CB 1 ATOM 129 N N . HIS A 1 18 ? 8.166 4.962 -35.861 1.00 34.47 ? 61 HIS A N 1 ATOM 130 C CA . HIS A 1 18 ? 7.586 4.297 -37.025 1.00 37.80 ? 61 HIS A CA 1 ATOM 131 C C . HIS A 1 18 ? 7.400 2.792 -36.806 1.00 37.02 ? 61 HIS A C 1 ATOM 132 O O . HIS A 1 18 ? 6.813 2.090 -37.638 1.00 38.90 ? 61 HIS A O 1 ATOM 133 C CB . HIS A 1 18 ? 8.470 4.534 -38.251 1.00 38.87 ? 61 HIS A CB 1 ATOM 134 C CG . HIS A 1 18 ? 9.896 4.121 -38.055 1.00 46.86 ? 61 HIS A CG 1 ATOM 135 N ND1 . HIS A 1 18 ? 10.359 2.864 -38.381 1.00 52.64 ? 61 HIS A ND1 1 ATOM 136 C CD2 . HIS A 1 18 ? 10.958 4.795 -37.552 1.00 48.74 ? 61 HIS A CD2 1 ATOM 137 C CE1 . HIS A 1 18 ? 11.645 2.782 -38.091 1.00 52.17 ? 61 HIS A CE1 1 ATOM 138 N NE2 . HIS A 1 18 ? 12.032 3.940 -37.584 1.00 51.92 ? 61 HIS A NE2 1 ATOM 139 N N . GLU A 1 19 ? 7.906 2.304 -35.681 1.00 36.49 ? 62 GLU A N 1 ATOM 140 C CA . GLU A 1 19 ? 7.911 0.881 -35.385 1.00 35.77 ? 62 GLU A CA 1 ATOM 141 C C . GLU A 1 19 ? 6.525 0.469 -34.851 1.00 39.05 ? 62 GLU A C 1 ATOM 142 O O . GLU A 1 19 ? 5.895 1.224 -34.122 1.00 38.48 ? 62 GLU A O 1 ATOM 143 C CB . GLU A 1 19 ? 9.025 0.647 -34.352 1.00 40.76 ? 62 GLU A CB 1 ATOM 144 C CG . GLU A 1 19 ? 9.375 -0.756 -34.000 1.00 51.12 ? 62 GLU A CG 1 ATOM 145 C CD . GLU A 1 19 ? 9.484 -1.663 -35.190 1.00 49.57 ? 62 GLU A CD 1 ATOM 146 O OE1 . GLU A 1 19 ? 10.515 -1.636 -35.889 1.00 56.82 ? 62 GLU A OE1 1 ATOM 147 O OE2 . GLU A 1 19 ? 8.523 -2.412 -35.411 1.00 47.54 ? 62 GLU A OE2 1 ATOM 148 N N . THR A 1 20 ? 6.031 -0.706 -35.238 1.00 38.26 ? 63 THR A N 1 ATOM 149 C CA . THR A 1 20 ? 4.806 -1.237 -34.635 1.00 33.34 ? 63 THR A CA 1 ATOM 150 C C . THR A 1 20 ? 5.095 -2.195 -33.490 1.00 34.02 ? 63 THR A C 1 ATOM 151 O O . THR A 1 20 ? 4.177 -2.604 -32.770 1.00 30.66 ? 63 THR A O 1 ATOM 152 C CB . THR A 1 20 ? 3.923 -2.000 -35.646 1.00 38.69 ? 63 THR A CB 1 ATOM 153 O OG1 . THR A 1 20 ? 4.682 -3.066 -36.218 1.00 35.65 ? 63 THR A OG1 1 ATOM 154 C CG2 . THR A 1 20 ? 3.422 -1.071 -36.744 1.00 40.13 ? 63 THR A CG2 1 ATOM 155 N N . GLU A 1 21 ? 6.357 -2.588 -33.340 1.00 32.74 ? 64 GLU A N 1 ATOM 156 C CA . GLU A 1 21 ? 6.758 -3.427 -32.204 1.00 30.56 ? 64 GLU A CA 1 ATOM 157 C C . GLU A 1 21 ? 6.246 -2.785 -30.888 1.00 31.88 ? 64 GLU A C 1 ATOM 158 O O . GLU A 1 21 ? 6.383 -1.588 -30.692 1.00 36.37 ? 64 GLU A O 1 ATOM 159 C CB . GLU A 1 21 ? 8.282 -3.606 -32.209 1.00 29.61 ? 64 GLU A CB 1 ATOM 160 C CG . GLU A 1 21 ? 8.837 -4.599 -31.180 1.00 29.47 ? 64 GLU A CG 1 ATOM 161 C CD . GLU A 1 21 ? 8.660 -4.096 -29.767 1.00 32.22 ? 64 GLU A CD 1 ATOM 162 O OE1 . GLU A 1 21 ? 8.961 -2.915 -29.522 1.00 33.14 ? 64 GLU A OE1 1 ATOM 163 O OE2 . GLU A 1 21 ? 8.174 -4.866 -28.920 1.00 31.45 ? 64 GLU A OE2 1 ATOM 164 N N . VAL A 1 22 ? 5.634 -3.571 -29.999 1.00 27.28 ? 65 VAL A N 1 ATOM 165 C CA . VAL A 1 22 ? 4.830 -2.966 -28.931 1.00 30.53 ? 65 VAL A CA 1 ATOM 166 C C . VAL A 1 22 ? 5.609 -2.202 -27.841 1.00 29.83 ? 65 VAL A C 1 ATOM 167 O O . VAL A 1 22 ? 5.070 -1.285 -27.221 1.00 31.11 ? 65 VAL A O 1 ATOM 168 C CB . VAL A 1 22 ? 3.886 -3.995 -28.270 1.00 33.56 ? 65 VAL A CB 1 ATOM 169 C CG1 . VAL A 1 22 ? 2.932 -4.578 -29.303 1.00 28.26 ? 65 VAL A CG1 1 ATOM 170 C CG2 . VAL A 1 22 ? 4.686 -5.103 -27.585 1.00 31.11 ? 65 VAL A CG2 1 ATOM 171 N N . HIS A 1 23 ? 6.850 -2.584 -27.571 1.00 28.37 ? 66 HIS A N 1 ATOM 172 C CA . HIS A 1 23 ? 7.611 -1.850 -26.556 1.00 27.89 ? 66 HIS A CA 1 ATOM 173 C C . HIS A 1 23 ? 7.986 -0.488 -27.122 1.00 32.53 ? 66 HIS A C 1 ATOM 174 O O . HIS A 1 23 ? 8.006 0.515 -26.395 1.00 31.90 ? 66 HIS A O 1 ATOM 175 C CB . HIS A 1 23 ? 8.884 -2.576 -26.148 1.00 27.59 ? 66 HIS A CB 1 ATOM 176 C CG . HIS A 1 23 ? 8.653 -3.892 -25.469 1.00 31.32 ? 66 HIS A CG 1 ATOM 177 N ND1 . HIS A 1 23 ? 8.390 -5.051 -26.166 1.00 32.57 ? 66 HIS A ND1 1 ATOM 178 C CD2 . HIS A 1 23 ? 8.711 -4.242 -24.158 1.00 33.02 ? 66 HIS A CD2 1 ATOM 179 C CE1 . HIS A 1 23 ? 8.262 -6.055 -25.312 1.00 31.52 ? 66 HIS A CE1 1 ATOM 180 N NE2 . HIS A 1 23 ? 8.454 -5.591 -24.091 1.00 32.45 ? 66 HIS A NE2 1 ATOM 181 N N . ASN A 1 24 ? 8.334 -0.472 -28.407 1.00 30.56 ? 67 ASN A N 1 ATOM 182 C CA . ASN A 1 24 ? 8.554 0.794 -29.119 1.00 34.12 ? 67 ASN A CA 1 ATOM 183 C C . ASN A 1 24 ? 7.329 1.692 -29.059 1.00 36.52 ? 67 ASN A C 1 ATOM 184 O O . ASN A 1 24 ? 7.431 2.881 -28.761 1.00 34.12 ? 67 ASN A O 1 ATOM 185 C CB . ASN A 1 24 ? 8.938 0.561 -30.576 1.00 31.99 ? 67 ASN A CB 1 ATOM 186 C CG . ASN A 1 24 ? 10.394 0.173 -30.742 1.00 35.74 ? 67 ASN A CG 1 ATOM 187 O OD1 . ASN A 1 24 ? 11.239 1.021 -30.996 1.00 37.97 ? 67 ASN A OD1 1 ATOM 188 N ND2 . ASN A 1 24 ? 10.689 -1.116 -30.618 1.00 35.86 ? 67 ASN A ND2 1 ATOM 189 N N . VAL A 1 25 ? 6.169 1.122 -29.366 1.00 33.92 ? 68 VAL A N 1 ATOM 190 C CA . VAL A 1 25 ? 4.937 1.890 -29.347 1.00 33.38 ? 68 VAL A CA 1 ATOM 191 C C . VAL A 1 25 ? 4.682 2.446 -27.954 1.00 34.99 ? 68 VAL A C 1 ATOM 192 O O . VAL A 1 25 ? 4.395 3.645 -27.806 1.00 32.18 ? 68 VAL A O 1 ATOM 193 C CB . VAL A 1 25 ? 3.737 1.062 -29.847 1.00 35.48 ? 68 VAL A CB 1 ATOM 194 C CG1 . VAL A 1 25 ? 2.422 1.754 -29.504 1.00 39.43 ? 68 VAL A CG1 1 ATOM 195 C CG2 . VAL A 1 25 ? 3.854 0.830 -31.352 1.00 38.04 ? 68 VAL A CG2 1 ATOM 196 N N . TRP A 1 26 ? 4.816 1.599 -26.929 1.00 34.58 ? 69 TRP A N 1 ATOM 197 C CA . TRP A 1 26 ? 4.584 2.044 -25.553 1.00 33.07 ? 69 TRP A CA 1 ATOM 198 C C . TRP A 1 26 ? 5.548 3.153 -25.154 1.00 35.14 ? 69 TRP A C 1 ATOM 199 O O . TRP A 1 26 ? 5.136 4.178 -24.609 1.00 30.41 ? 69 TRP A O 1 ATOM 200 C CB . TRP A 1 26 ? 4.726 0.888 -24.553 1.00 26.80 ? 69 TRP A CB 1 ATOM 201 C CG . TRP A 1 26 ? 4.500 1.315 -23.132 1.00 28.40 ? 69 TRP A CG 1 ATOM 202 C CD1 . TRP A 1 26 ? 3.302 1.411 -22.482 1.00 31.91 ? 69 TRP A CD1 1 ATOM 203 C CD2 . TRP A 1 26 ? 5.501 1.718 -22.189 1.00 29.17 ? 69 TRP A CD2 1 ATOM 204 N NE1 . TRP A 1 26 ? 3.494 1.841 -21.192 1.00 34.87 ? 69 TRP A NE1 1 ATOM 205 C CE2 . TRP A 1 26 ? 4.836 2.028 -20.981 1.00 33.31 ? 69 TRP A CE2 1 ATOM 206 C CE3 . TRP A 1 26 ? 6.893 1.849 -22.250 1.00 28.01 ? 69 TRP A CE3 1 ATOM 207 C CZ2 . TRP A 1 26 ? 5.518 2.463 -19.837 1.00 33.16 ? 69 TRP A CZ2 1 ATOM 208 C CZ3 . TRP A 1 26 ? 7.574 2.264 -21.111 1.00 31.57 ? 69 TRP A CZ3 1 ATOM 209 C CH2 . TRP A 1 26 ? 6.883 2.566 -19.920 1.00 30.95 ? 69 TRP A CH2 1 ATOM 210 N N . ALA A 1 27 ? 6.833 2.946 -25.426 1.00 30.12 ? 70 ALA A N 1 ATOM 211 C CA . ALA A 1 27 ? 7.839 3.918 -24.998 1.00 29.65 ? 70 ALA A CA 1 ATOM 212 C C . ALA A 1 27 ? 7.747 5.213 -25.797 1.00 34.15 ? 70 ALA A C 1 ATOM 213 O O . ALA A 1 27 ? 8.049 6.278 -25.281 1.00 36.27 ? 70 ALA A O 1 ATOM 214 C CB . ALA A 1 27 ? 9.245 3.334 -25.082 1.00 33.47 ? 70 ALA A CB 1 ATOM 215 N N . THR A 1 28 ? 7.323 5.110 -27.050 1.00 31.26 ? 71 THR A N 1 ATOM 216 C CA . THR A 1 28 ? 7.104 6.287 -27.885 1.00 35.53 ? 71 THR A CA 1 ATOM 217 C C . THR A 1 28 ? 6.109 7.252 -27.236 1.00 34.09 ? 71 THR A C 1 ATOM 218 O O . THR A 1 28 ? 6.260 8.469 -27.332 1.00 34.26 ? 71 THR A O 1 ATOM 219 C CB . THR A 1 28 ? 6.615 5.889 -29.310 1.00 35.44 ? 71 THR A CB 1 ATOM 220 O OG1 . THR A 1 28 ? 7.721 5.351 -30.045 1.00 34.75 ? 71 THR A OG1 1 ATOM 221 C CG2 . THR A 1 28 ? 6.076 7.105 -30.059 1.00 38.41 ? 71 THR A CG2 1 ATOM 222 N N . HIS A 1 29 ? 5.100 6.697 -26.574 1.00 34.96 ? 72 HIS A N 1 ATOM 223 C CA . HIS A 1 29 ? 4.066 7.489 -25.910 1.00 43.03 ? 72 HIS A CA 1 ATOM 224 C C . HIS A 1 29 ? 4.278 7.714 -24.406 1.00 38.12 ? 72 HIS A C 1 ATOM 225 O O . HIS A 1 29 ? 3.791 8.702 -23.857 1.00 40.08 ? 72 HIS A O 1 ATOM 226 C CB . HIS A 1 29 ? 2.691 6.870 -26.164 1.00 58.65 ? 72 HIS A CB 1 ATOM 227 C CG . HIS A 1 29 ? 2.304 6.858 -27.611 1.00 81.95 ? 72 HIS A CG 1 ATOM 228 N ND1 . HIS A 1 29 ? 1.514 5.875 -28.170 1.00 87.78 ? 72 HIS A ND1 1 ATOM 229 C CD2 . HIS A 1 29 ? 2.608 7.712 -28.619 1.00 91.77 ? 72 HIS A CD2 1 ATOM 230 C CE1 . HIS A 1 29 ? 1.345 6.125 -29.456 1.00 90.23 ? 72 HIS A CE1 1 ATOM 231 N NE2 . HIS A 1 29 ? 1.999 7.233 -29.755 1.00 93.37 ? 72 HIS A NE2 1 ATOM 232 N N . ALA A 1 30 ? 5.012 6.825 -23.745 1.00 34.39 ? 73 ALA A N 1 ATOM 233 C CA . ALA A 1 30 ? 5.118 6.880 -22.287 1.00 33.30 ? 73 ALA A CA 1 ATOM 234 C C . ALA A 1 30 ? 6.460 7.392 -21.778 1.00 31.28 ? 73 ALA A C 1 ATOM 235 O O . ALA A 1 30 ? 6.636 7.587 -20.570 1.00 34.75 ? 73 ALA A O 1 ATOM 236 C CB . ALA A 1 30 ? 4.825 5.487 -21.682 1.00 29.35 ? 73 ALA A CB 1 ATOM 237 N N . CYS A 1 31 ? 7.407 7.593 -22.689 1.00 32.54 ? 74 CYS A N 1 ATOM 238 C CA . CYS A 1 31 ? 8.776 7.950 -22.325 1.00 34.89 ? 74 CYS A CA 1 ATOM 239 C C . CYS A 1 31 ? 9.265 9.095 -23.191 1.00 35.00 ? 74 CYS A C 1 ATOM 240 O O . CYS A 1 31 ? 8.689 9.377 -24.232 1.00 33.53 ? 74 CYS A O 1 ATOM 241 C CB . CYS A 1 31 ? 9.732 6.763 -22.517 1.00 30.02 ? 74 CYS A CB 1 ATOM 242 S SG . CYS A 1 31 ? 9.303 5.285 -21.613 1.00 34.49 ? 74 CYS A SG 1 ATOM 243 N N . VAL A 1 32 ? 10.332 9.747 -22.749 1.00 31.95 ? 75 VAL A N 1 ATOM 244 C CA . VAL A 1 32 ? 10.959 10.813 -23.520 1.00 33.84 ? 75 VAL A CA 1 ATOM 245 C C . VAL A 1 32 ? 12.229 10.273 -24.177 1.00 33.45 ? 75 VAL A C 1 ATOM 246 O O . VAL A 1 32 ? 12.669 9.171 -23.859 1.00 37.84 ? 75 VAL A O 1 ATOM 247 C CB . VAL A 1 32 ? 11.286 12.031 -22.630 1.00 36.15 ? 75 VAL A CB 1 ATOM 248 C CG1 . VAL A 1 32 ? 10.004 12.652 -22.085 1.00 42.91 ? 75 VAL A CG1 1 ATOM 249 C CG2 . VAL A 1 32 ? 12.240 11.648 -21.490 1.00 35.11 ? 75 VAL A CG2 1 ATOM 250 N N . PRO A 1 33 ? 12.822 11.040 -25.098 1.00 38.94 ? 76 PRO A N 1 ATOM 251 C CA . PRO A 1 33 ? 14.093 10.626 -25.699 1.00 42.04 ? 76 PRO A CA 1 ATOM 252 C C . PRO A 1 33 ? 15.217 10.532 -24.677 1.00 41.99 ? 76 PRO A C 1 ATOM 253 O O . PRO A 1 33 ? 15.202 11.225 -23.648 1.00 39.87 ? 76 PRO A O 1 ATOM 254 C CB . PRO A 1 33 ? 14.382 11.760 -26.701 1.00 43.29 ? 76 PRO A CB 1 ATOM 255 C CG . PRO A 1 33 ? 13.032 12.219 -27.101 1.00 42.21 ? 76 PRO A CG 1 ATOM 256 C CD . PRO A 1 33 ? 12.243 12.193 -25.807 1.00 40.35 ? 76 PRO A CD 1 ATOM 257 N N . THR A 1 34 ? 16.189 9.671 -24.954 1.00 40.83 ? 77 THR A N 1 ATOM 258 C CA . THR A 1 34 ? 17.364 9.571 -24.102 1.00 42.03 ? 77 THR A CA 1 ATOM 259 C C . THR A 1 34 ? 18.225 10.815 -24.252 1.00 45.93 ? 77 THR A C 1 ATOM 260 O O . THR A 1 34 ? 18.096 11.569 -25.225 1.00 46.70 ? 77 THR A O 1 ATOM 261 C CB . THR A 1 34 ? 18.247 8.364 -24.468 1.00 40.93 ? 77 THR A CB 1 ATOM 262 O OG1 . THR A 1 34 ? 18.700 8.503 -25.821 1.00 42.12 ? 77 THR A OG1 1 ATOM 263 C CG2 . THR A 1 34 ? 17.497 7.043 -24.284 1.00 39.02 ? 77 THR A CG2 1 ATOM 264 N N . ASP A 1 35 ? 19.118 10.998 -23.287 1.00 43.99 ? 78 ASP A N 1 ATOM 265 C CA . ASP A 1 35 ? 20.092 12.078 -23.296 1.00 45.60 ? 78 ASP A CA 1 ATOM 266 C C . ASP A 1 35 ? 21.325 11.557 -23.997 1.00 49.16 ? 78 ASP A C 1 ATOM 267 O O . ASP A 1 35 ? 21.885 10.550 -23.587 1.00 50.92 ? 78 ASP A O 1 ATOM 268 C CB . ASP A 1 35 ? 20.444 12.475 -21.856 1.00 51.09 ? 78 ASP A CB 1 ATOM 269 C CG . ASP A 1 35 ? 21.296 13.744 -21.775 1.00 54.78 ? 78 ASP A CG 1 ATOM 270 O OD1 . ASP A 1 35 ? 21.875 14.160 -22.799 1.00 52.73 ? 78 ASP A OD1 1 ATOM 271 O OD2 . ASP A 1 35 ? 21.391 14.318 -20.671 1.00 60.15 ? 78 ASP A OD2 1 ATOM 272 N N . PRO A 1 36 ? 21.743 12.229 -25.078 1.00 59.44 ? 79 PRO A N 1 ATOM 273 C CA . PRO A 1 36 ? 22.930 11.779 -25.811 1.00 64.13 ? 79 PRO A CA 1 ATOM 274 C C . PRO A 1 36 ? 24.216 12.075 -25.038 1.00 68.07 ? 79 PRO A C 1 ATOM 275 O O . PRO A 1 36 ? 25.217 11.394 -25.245 1.00 71.11 ? 79 PRO A O 1 ATOM 276 C CB . PRO A 1 36 ? 22.873 12.604 -27.100 1.00 64.74 ? 79 PRO A CB 1 ATOM 277 C CG . PRO A 1 36 ? 22.167 13.853 -26.703 1.00 66.88 ? 79 PRO A CG 1 ATOM 278 C CD . PRO A 1 36 ? 21.138 13.429 -25.680 1.00 61.11 ? 79 PRO A CD 1 ATOM 279 N N . ASN A 1 37 ? 24.181 13.067 -24.152 1.00 66.43 ? 80 ASN A N 1 ATOM 280 C CA . ASN A 1 37 ? 25.352 13.436 -23.356 1.00 68.90 ? 80 ASN A CA 1 ATOM 281 C C . ASN A 1 37 ? 25.059 13.409 -21.850 1.00 62.44 ? 80 ASN A C 1 ATOM 282 O O . ASN A 1 37 ? 25.026 14.451 -21.195 1.00 61.23 ? 80 ASN A O 1 ATOM 283 C CB . ASN A 1 37 ? 25.855 14.821 -23.775 1.00 80.16 ? 80 ASN A CB 1 ATOM 284 C CG . ASN A 1 37 ? 26.120 14.919 -25.275 1.00 87.38 ? 80 ASN A CG 1 ATOM 285 O OD1 . ASN A 1 37 ? 26.865 14.117 -25.840 1.00 89.70 ? 80 ASN A OD1 1 ATOM 286 N ND2 . ASN A 1 37 ? 25.497 15.900 -25.926 1.00 89.13 ? 80 ASN A ND2 1 ATOM 287 N N . PRO A 1 38 ? 24.838 12.206 -21.301 1.00 58.89 ? 81 PRO A N 1 ATOM 288 C CA . PRO A 1 38 ? 24.432 12.051 -19.899 1.00 58.69 ? 81 PRO A CA 1 ATOM 289 C C . PRO A 1 38 ? 25.558 12.311 -18.896 1.00 65.01 ? 81 PRO A C 1 ATOM 290 O O . PRO A 1 38 ? 26.707 11.914 -19.108 1.00 66.93 ? 81 PRO A O 1 ATOM 291 C CB . PRO A 1 38 ? 23.986 10.589 -19.830 1.00 53.67 ? 81 PRO A CB 1 ATOM 292 C CG . PRO A 1 38 ? 24.789 9.911 -20.883 1.00 56.39 ? 81 PRO A CG 1 ATOM 293 C CD . PRO A 1 38 ? 24.914 10.911 -22.001 1.00 53.62 ? 81 PRO A CD 1 ATOM 294 N N . GLN A 1 39 ? 25.212 12.972 -17.797 1.00 64.45 ? 82 GLN A N 1 ATOM 295 C CA . GLN A 1 39 ? 26.183 13.291 -16.763 1.00 69.96 ? 82 GLN A CA 1 ATOM 296 C C . GLN A 1 39 ? 26.274 12.169 -15.738 1.00 62.15 ? 82 GLN A C 1 ATOM 297 O O . GLN A 1 39 ? 25.259 11.608 -15.339 1.00 60.14 ? 82 GLN A O 1 ATOM 298 C CB . GLN A 1 39 ? 25.798 14.597 -16.066 1.00 81.52 ? 82 GLN A CB 1 ATOM 299 C CG . GLN A 1 39 ? 25.757 15.794 -16.995 1.00 90.09 ? 82 GLN A CG 1 ATOM 300 C CD . GLN A 1 39 ? 27.091 16.041 -17.674 1.00 95.11 ? 82 GLN A CD 1 ATOM 301 O OE1 . GLN A 1 39 ? 28.135 16.088 -17.018 1.00 98.09 ? 82 GLN A OE1 1 ATOM 302 N NE2 . GLN A 1 39 ? 27.066 16.194 -18.995 1.00 94.13 ? 82 GLN A NE2 1 ATOM 303 N N . GLU A 1 40 ? 27.497 11.834 -15.338 1.00 57.15 ? 83 GLU A N 1 ATOM 304 C CA . GLU A 1 40 ? 27.725 10.942 -14.206 1.00 54.65 ? 83 GLU A CA 1 ATOM 305 C C . GLU A 1 40 ? 28.901 11.448 -13.396 1.00 55.46 ? 83 GLU A C 1 ATOM 306 O O . GLU A 1 40 ? 30.031 11.503 -13.893 1.00 56.80 ? 83 GLU A O 1 ATOM 307 C CB . GLU A 1 40 ? 27.997 9.508 -14.648 1.00 54.86 ? 83 GLU A CB 1 ATOM 308 C CG . GLU A 1 40 ? 28.347 8.593 -13.473 1.00 53.35 ? 83 GLU A CG 1 ATOM 309 C CD . GLU A 1 40 ? 28.363 7.127 -13.848 1.00 55.25 ? 83 GLU A CD 1 ATOM 310 O OE1 . GLU A 1 40 ? 28.031 6.811 -15.013 1.00 58.33 ? 83 GLU A OE1 1 ATOM 311 O OE2 . GLU A 1 40 ? 28.699 6.288 -12.976 1.00 53.47 ? 83 GLU A OE2 1 ATOM 312 N N . ILE A 1 41 ? 28.624 11.814 -12.149 1.00 50.80 ? 84 ILE A N 1 ATOM 313 C CA . ILE A 1 41 ? 29.625 12.374 -11.248 1.00 51.97 ? 84 ILE A CA 1 ATOM 314 C C . ILE A 1 41 ? 30.034 11.377 -10.174 1.00 56.76 ? 84 ILE A C 1 ATOM 315 O O . ILE A 1 41 ? 29.184 10.865 -9.443 1.00 55.73 ? 84 ILE A O 1 ATOM 316 C CB . ILE A 1 41 ? 29.068 13.620 -10.531 1.00 52.12 ? 84 ILE A CB 1 ATOM 317 C CG1 . ILE A 1 41 ? 28.481 14.605 -11.543 1.00 58.24 ? 84 ILE A CG1 1 ATOM 318 C CG2 . ILE A 1 41 ? 30.137 14.269 -9.659 1.00 54.02 ? 84 ILE A CG2 1 ATOM 319 C CD1 . ILE A 1 41 ? 27.698 15.724 -10.904 1.00 64.75 ? 84 ILE A CD1 1 ATOM 320 N N . HIS A 1 42 ? 31.330 11.102 -10.064 1.00 56.21 ? 85 HIS A N 1 ATOM 321 C CA . HIS A 1 42 ? 31.810 10.306 -8.944 1.00 58.95 ? 85 HIS A CA 1 ATOM 322 C C . HIS A 1 42 ? 31.818 11.159 -7.683 1.00 56.21 ? 85 HIS A C 1 ATOM 323 O O . HIS A 1 42 ? 32.365 12.262 -7.678 1.00 58.74 ? 85 HIS A O 1 ATOM 324 C CB . HIS A 1 42 ? 33.213 9.751 -9.186 1.00 66.29 ? 85 HIS A CB 1 ATOM 325 C CG . HIS A 1 42 ? 33.800 9.078 -7.980 1.00 73.42 ? 85 HIS A CG 1 ATOM 326 N ND1 . HIS A 1 42 ? 34.924 9.547 -7.336 1.00 76.71 ? 85 HIS A ND1 1 ATOM 327 C CD2 . HIS A 1 42 ? 33.396 7.988 -7.284 1.00 75.21 ? 85 HIS A CD2 1 ATOM 328 C CE1 . HIS A 1 42 ? 35.198 8.765 -6.305 1.00 76.47 ? 85 HIS A CE1 1 ATOM 329 N NE2 . HIS A 1 42 ? 34.285 7.812 -6.252 1.00 75.73 ? 85 HIS A NE2 1 ATOM 330 N N . LEU A 1 43 ? 31.206 10.642 -6.623 1.00 43.90 ? 86 LEU A N 1 ATOM 331 C CA . LEU A 1 43 ? 31.131 11.347 -5.359 1.00 45.35 ? 86 LEU A CA 1 ATOM 332 C C . LEU A 1 43 ? 32.342 10.998 -4.502 1.00 60.14 ? 86 LEU A C 1 ATOM 333 O O . LEU A 1 43 ? 32.403 9.926 -3.906 1.00 59.48 ? 86 LEU A O 1 ATOM 334 C CB . LEU A 1 43 ? 29.831 11.006 -4.642 1.00 44.30 ? 86 LEU A CB 1 ATOM 335 C CG . LEU A 1 43 ? 28.595 11.208 -5.527 1.00 49.83 ? 86 LEU A CG 1 ATOM 336 C CD1 . LEU A 1 43 ? 27.315 10.787 -4.807 1.00 49.67 ? 86 LEU A CD1 1 ATOM 337 C CD2 . LEU A 1 43 ? 28.513 12.656 -5.999 1.00 50.91 ? 86 LEU A CD2 1 ATOM 338 N N . GLU A 1 44 ? 33.303 11.916 -4.448 1.00 62.19 ? 87 GLU A N 1 ATOM 339 C CA . GLU A 1 44 ? 34.591 11.649 -3.806 1.00 66.72 ? 87 GLU A CA 1 ATOM 340 C C . GLU A 1 44 ? 34.471 11.346 -2.321 1.00 70.87 ? 87 GLU A C 1 ATOM 341 O O . GLU A 1 44 ? 33.732 12.017 -1.603 1.00 63.04 ? 87 GLU A O 1 ATOM 342 C CB . GLU A 1 44 ? 35.563 12.803 -4.047 1.00 70.52 ? 87 GLU A CB 1 ATOM 343 C CG . GLU A 1 44 ? 36.085 12.857 -5.471 1.00 79.34 ? 87 GLU A CG 1 ATOM 344 C CD . GLU A 1 44 ? 37.046 14.009 -5.702 1.00 93.18 ? 87 GLU A CD 1 ATOM 345 O OE1 . GLU A 1 44 ? 37.282 14.795 -4.757 1.00 93.58 ? 87 GLU A OE1 1 ATOM 346 O OE2 . GLU A 1 44 ? 37.564 14.128 -6.835 1.00 100.55 ? 87 GLU A OE2 1 ATOM 347 N N . ASN A 1 45 ? 35.224 10.336 -1.883 1.00 90.43 ? 88 ASN A N 1 ATOM 348 C CA . ASN A 1 45 ? 35.164 9.764 -0.524 1.00 105.06 ? 88 ASN A CA 1 ATOM 349 C C . ASN A 1 45 ? 33.772 9.726 0.131 1.00 90.18 ? 88 ASN A C 1 ATOM 350 O O . ASN A 1 45 ? 33.621 9.957 1.332 1.00 89.67 ? 88 ASN A O 1 ATOM 351 C CB . ASN A 1 45 ? 36.258 10.333 0.413 1.00 135.75 ? 88 ASN A CB 1 ATOM 352 C CG . ASN A 1 45 ? 35.956 11.740 0.906 1.00 148.97 ? 88 ASN A CG 1 ATOM 353 O OD1 . ASN A 1 45 ? 34.894 12.291 0.626 1.00 149.17 ? 88 ASN A OD1 1 ATOM 354 N ND2 . ASN A 1 45 ? 36.880 12.316 1.680 1.00 162.34 ? 88 ASN A ND2 1 ATOM 355 N N . VAL A 1 46 ? 32.766 9.409 -0.677 1.00 79.58 ? 89 VAL A N 1 ATOM 356 C CA . VAL A 1 46 ? 31.393 9.285 -0.201 1.00 67.60 ? 89 VAL A CA 1 ATOM 357 C C . VAL A 1 46 ? 31.023 7.817 -0.054 1.00 63.73 ? 89 VAL A C 1 ATOM 358 O O . VAL A 1 46 ? 31.258 7.020 -0.966 1.00 58.40 ? 89 VAL A O 1 ATOM 359 C CB . VAL A 1 46 ? 30.392 9.951 -1.178 1.00 57.39 ? 89 VAL A CB 1 ATOM 360 C CG1 . VAL A 1 46 ? 28.975 9.448 -0.928 1.00 52.82 ? 89 VAL A CG1 1 ATOM 361 C CG2 . VAL A 1 46 ? 30.457 11.467 -1.058 1.00 59.59 ? 89 VAL A CG2 1 ATOM 362 N N . THR A 1 47 ? 30.456 7.465 1.097 1.00 57.58 ? 90 THR A N 1 ATOM 363 C CA . THR A 1 47 ? 29.908 6.128 1.308 1.00 52.25 ? 90 THR A CA 1 ATOM 364 C C . THR A 1 47 ? 28.398 6.208 1.523 1.00 51.55 ? 90 THR A C 1 ATOM 365 O O . THR A 1 47 ? 27.920 6.977 2.362 1.00 50.19 ? 90 THR A O 1 ATOM 366 C CB . THR A 1 47 ? 30.544 5.441 2.524 1.00 56.43 ? 90 THR A CB 1 ATOM 367 O OG1 . THR A 1 47 ? 31.957 5.326 2.316 1.00 61.99 ? 90 THR A OG1 1 ATOM 368 C CG2 . THR A 1 47 ? 29.949 4.054 2.724 1.00 50.63 ? 90 THR A CG2 1 ATOM 369 N N . GLU A 1 48 ? 27.654 5.410 0.761 1.00 47.63 ? 91 GLU A N 1 ATOM 370 C CA . GLU A 1 48 ? 26.200 5.405 0.847 1.00 45.93 ? 91 GLU A CA 1 ATOM 371 C C . GLU A 1 48 ? 25.688 3.995 1.100 1.00 45.41 ? 91 GLU A C 1 ATOM 372 O O . GLU A 1 48 ? 26.275 3.019 0.633 1.00 41.13 ? 91 GLU A O 1 ATOM 373 C CB . GLU A 1 48 ? 25.583 5.942 -0.449 1.00 42.06 ? 91 GLU A CB 1 ATOM 374 C CG . GLU A 1 48 ? 25.738 7.427 -0.652 1.00 47.32 ? 91 GLU A CG 1 ATOM 375 C CD . GLU A 1 48 ? 24.750 8.237 0.178 1.00 54.13 ? 91 GLU A CD 1 ATOM 376 O OE1 . GLU A 1 48 ? 23.604 7.772 0.388 1.00 45.40 ? 91 GLU A OE1 1 ATOM 377 O OE2 . GLU A 1 48 ? 25.130 9.340 0.622 1.00 62.78 ? 91 GLU A OE2 1 ATOM 378 N N . ASN A 1 49 ? 24.592 3.894 1.844 1.00 41.10 ? 92 ASN A N 1 ATOM 379 C CA . ASN A 1 49 ? 23.961 2.610 2.068 1.00 36.21 ? 92 ASN A CA 1 ATOM 380 C C . ASN A 1 49 ? 22.875 2.375 1.037 1.00 39.72 ? 92 ASN A C 1 ATOM 381 O O . ASN A 1 49 ? 22.131 3.292 0.690 1.00 38.43 ? 92 ASN A O 1 ATOM 382 C CB . ASN A 1 49 ? 23.381 2.546 3.477 1.00 36.00 ? 92 ASN A CB 1 ATOM 383 C CG . ASN A 1 49 ? 24.409 2.865 4.528 1.00 50.38 ? 92 ASN A CG 1 ATOM 384 O OD1 . ASN A 1 49 ? 25.607 2.665 4.320 1.00 55.42 ? 92 ASN A OD1 1 ATOM 385 N ND2 . ASN A 1 49 ? 23.954 3.381 5.662 1.00 56.12 ? 92 ASN A ND2 1 ATOM 386 N N . PHE A 1 50 ? 22.803 1.144 0.537 1.00 38.29 ? 93 PHE A N 1 ATOM 387 C CA . PHE A 1 50 ? 21.780 0.756 -0.422 1.00 35.70 ? 93 PHE A CA 1 ATOM 388 C C . PHE A 1 50 ? 21.041 -0.438 0.160 1.00 33.72 ? 93 PHE A C 1 ATOM 389 O O . PHE A 1 50 ? 21.564 -1.158 1.016 1.00 36.06 ? 93 PHE A O 1 ATOM 390 C CB . PHE A 1 50 ? 22.393 0.378 -1.781 1.00 35.75 ? 93 PHE A CB 1 ATOM 391 C CG . PHE A 1 50 ? 22.962 1.544 -2.557 1.00 35.98 ? 93 PHE A CG 1 ATOM 392 C CD1 . PHE A 1 50 ? 22.315 2.026 -3.688 1.00 34.61 ? 93 PHE A CD1 1 ATOM 393 C CD2 . PHE A 1 50 ? 24.150 2.142 -2.166 1.00 38.77 ? 93 PHE A CD2 1 ATOM 394 C CE1 . PHE A 1 50 ? 22.838 3.090 -4.411 1.00 33.64 ? 93 PHE A CE1 1 ATOM 395 C CE2 . PHE A 1 50 ? 24.676 3.202 -2.875 1.00 39.27 ? 93 PHE A CE2 1 ATOM 396 C CZ . PHE A 1 50 ? 24.018 3.683 -4.000 1.00 36.24 ? 93 PHE A CZ 1 ATOM 397 N N . ASN A 1 51 ? 19.813 -0.638 -0.289 1.00 31.36 ? 94 ASN A N 1 ATOM 398 C CA . ASN A 1 51 ? 19.058 -1.823 0.106 1.00 33.05 ? 94 ASN A CA 1 ATOM 399 C C . ASN A 1 51 ? 18.171 -2.153 -1.083 1.00 32.21 ? 94 ASN A C 1 ATOM 400 O O . ASN A 1 51 ? 17.100 -1.582 -1.231 1.00 31.46 ? 94 ASN A O 1 ATOM 401 C CB . ASN A 1 51 ? 18.236 -1.581 1.374 1.00 30.91 ? 94 ASN A CB 1 ATOM 402 C CG . ASN A 1 51 ? 17.497 -2.827 1.831 1.00 34.84 ? 94 ASN A CG 1 ATOM 403 O OD1 . ASN A 1 51 ? 17.590 -3.883 1.200 1.00 34.86 ? 94 ASN A OD1 1 ATOM 404 N ND2 . ASN A 1 51 ? 16.763 -2.714 2.929 1.00 41.05 ? 94 ASN A ND2 1 ATOM 405 N N . MET A 1 52 ? 18.653 -3.048 -1.943 1.00 26.48 ? 95 MET A N 1 ATOM 406 C CA . MET A 1 52 ? 17.946 -3.400 -3.174 1.00 29.74 ? 95 MET A CA 1 ATOM 407 C C . MET A 1 52 ? 16.577 -4.005 -2.885 1.00 33.44 ? 95 MET A C 1 ATOM 408 O O . MET A 1 52 ? 15.717 -4.053 -3.772 1.00 33.20 ? 95 MET A O 1 ATOM 409 C CB . MET A 1 52 ? 18.771 -4.393 -3.988 1.00 32.64 ? 95 MET A CB 1 ATOM 410 C CG . MET A 1 52 ? 19.034 -5.700 -3.236 1.00 30.47 ? 95 MET A CG 1 ATOM 411 S SD . MET A 1 52 ? 19.901 -6.937 -4.226 1.00 31.98 ? 95 MET A SD 1 ATOM 412 C CE . MET A 1 52 ? 18.612 -7.457 -5.377 1.00 25.57 ? 95 MET A CE 1 ATOM 413 N N . TRP A 1 53 ? 16.386 -4.473 -1.651 1.00 33.13 ? 96 TRP A N 1 ATOM 414 C CA . TRP A 1 53 ? 15.165 -5.189 -1.256 1.00 32.70 ? 96 TRP A CA 1 ATOM 415 C C . TRP A 1 53 ? 14.077 -4.249 -0.754 1.00 37.11 ? 96 TRP A C 1 ATOM 416 O O . TRP A 1 53 ? 12.934 -4.660 -0.530 1.00 39.02 ? 96 TRP A O 1 ATOM 417 C CB . TRP A 1 53 ? 15.487 -6.280 -0.218 1.00 33.34 ? 96 TRP A CB 1 ATOM 418 C CG . TRP A 1 53 ? 16.522 -7.229 -0.754 1.00 36.67 ? 96 TRP A CG 1 ATOM 419 C CD1 . TRP A 1 53 ? 17.844 -7.259 -0.434 1.00 35.09 ? 96 TRP A CD1 1 ATOM 420 C CD2 . TRP A 1 53 ? 16.323 -8.249 -1.743 1.00 35.15 ? 96 TRP A CD2 1 ATOM 421 N NE1 . TRP A 1 53 ? 18.482 -8.241 -1.157 1.00 38.63 ? 96 TRP A NE1 1 ATOM 422 C CE2 . TRP A 1 53 ? 17.570 -8.860 -1.969 1.00 35.06 ? 96 TRP A CE2 1 ATOM 423 C CE3 . TRP A 1 53 ? 15.207 -8.706 -2.459 1.00 36.47 ? 96 TRP A CE3 1 ATOM 424 C CZ2 . TRP A 1 53 ? 17.738 -9.901 -2.884 1.00 31.46 ? 96 TRP A CZ2 1 ATOM 425 C CZ3 . TRP A 1 53 ? 15.375 -9.747 -3.373 1.00 36.64 ? 96 TRP A CZ3 1 ATOM 426 C CH2 . TRP A 1 53 ? 16.632 -10.331 -3.577 1.00 35.86 ? 96 TRP A CH2 1 ATOM 427 N N . LYS A 1 54 ? 14.451 -2.985 -0.586 1.00 37.19 ? 97 LYS A N 1 ATOM 428 C CA . LYS A 1 54 ? 13.532 -1.924 -0.200 1.00 33.29 ? 97 LYS A CA 1 ATOM 429 C C . LYS A 1 54 ? 13.843 -0.730 -1.086 1.00 32.81 ? 97 LYS A C 1 ATOM 430 O O . LYS A 1 54 ? 14.523 0.215 -0.684 1.00 31.00 ? 97 LYS A O 1 ATOM 431 C CB . LYS A 1 54 ? 13.715 -1.564 1.277 1.00 39.29 ? 97 LYS A CB 1 ATOM 432 C CG . LYS A 1 54 ? 12.970 -2.479 2.233 1.00 50.97 ? 97 LYS A CG 1 ATOM 433 C CD . LYS A 1 54 ? 13.260 -2.128 3.690 1.00 64.97 ? 97 LYS A CD 1 ATOM 434 C CE . LYS A 1 54 ? 12.714 -0.754 4.062 1.00 73.92 ? 97 LYS A CE 1 ATOM 435 N NZ . LYS A 1 54 ? 11.228 -0.746 4.229 1.00 78.07 ? 97 LYS A NZ 1 ATOM 436 N N . ASN A 1 55 ? 13.350 -0.781 -2.314 1.00 34.38 ? 98 ASN A N 1 ATOM 437 C CA . ASN A 1 55 ? 13.767 0.177 -3.329 1.00 34.19 ? 98 ASN A CA 1 ATOM 438 C C . ASN A 1 55 ? 12.586 0.420 -4.241 1.00 31.10 ? 98 ASN A C 1 ATOM 439 O O . ASN A 1 55 ? 12.260 -0.408 -5.094 1.00 28.60 ? 98 ASN A O 1 ATOM 440 C CB . ASN A 1 55 ? 14.964 -0.369 -4.131 1.00 30.65 ? 98 ASN A CB 1 ATOM 441 C CG . ASN A 1 55 ? 15.438 0.596 -5.219 1.00 31.65 ? 98 ASN A CG 1 ATOM 442 O OD1 . ASN A 1 55 ? 14.958 1.728 -5.306 1.00 33.05 ? 98 ASN A OD1 1 ATOM 443 N ND2 . ASN A 1 55 ? 16.384 0.145 -6.060 1.00 27.81 ? 98 ASN A ND2 1 ATOM 444 N N . ASN A 1 56 ? 11.930 1.542 -4.016 1.00 33.00 ? 99 ASN A N 1 ATOM 445 C CA . ASN A 1 56 ? 10.711 1.880 -4.733 1.00 33.24 ? 99 ASN A CA 1 ATOM 446 C C . ASN A 1 56 ? 10.899 1.994 -6.251 1.00 29.79 ? 99 ASN A C 1 ATOM 447 O O . ASN A 1 56 ? 9.926 1.968 -7.003 1.00 28.39 ? 99 ASN A O 1 ATOM 448 C CB . ASN A 1 56 ? 10.140 3.174 -4.137 1.00 36.55 ? 99 ASN A CB 1 ATOM 449 C CG . ASN A 1 56 ? 8.807 3.559 -4.732 1.00 40.19 ? 99 ASN A CG 1 ATOM 450 O OD1 . ASN A 1 56 ? 8.685 4.598 -5.379 1.00 40.87 ? 99 ASN A OD1 1 ATOM 451 N ND2 . ASN A 1 56 ? 7.795 2.728 -4.509 1.00 41.37 ? 99 ASN A ND2 1 ATOM 452 N N . MET A 1 57 ? 12.144 2.109 -6.712 1.00 30.47 ? 100 MET A N 1 ATOM 453 C CA . MET A 1 57 ? 12.402 2.052 -8.160 1.00 32.66 ? 100 MET A CA 1 ATOM 454 C C . MET A 1 57 ? 11.873 0.774 -8.776 1.00 32.93 ? 100 MET A C 1 ATOM 455 O O . MET A 1 57 ? 11.416 0.758 -9.926 1.00 27.90 ? 100 MET A O 1 ATOM 456 C CB . MET A 1 57 ? 13.894 2.161 -8.452 1.00 29.48 ? 100 MET A CB 1 ATOM 457 C CG . MET A 1 57 ? 14.516 3.452 -7.928 1.00 33.42 ? 100 MET A CG 1 ATOM 458 S SD . MET A 1 57 ? 16.253 3.513 -8.320 1.00 31.03 ? 100 MET A SD 1 ATOM 459 C CE . MET A 1 57 ? 16.226 3.945 -10.056 1.00 33.38 ? 100 MET A CE 1 ATOM 460 N N . VAL A 1 58 ? 11.949 -0.303 -8.003 1.00 28.80 ? 101 VAL A N 1 ATOM 461 C CA . VAL A 1 58 ? 11.466 -1.602 -8.439 1.00 30.21 ? 101 VAL A CA 1 ATOM 462 C C . VAL A 1 58 ? 9.959 -1.586 -8.625 1.00 31.17 ? 101 VAL A C 1 ATOM 463 O O . VAL A 1 58 ? 9.456 -2.014 -9.665 1.00 30.27 ? 101 VAL A O 1 ATOM 464 C CB . VAL A 1 58 ? 11.844 -2.676 -7.412 1.00 32.63 ? 101 VAL A CB 1 ATOM 465 C CG1 . VAL A 1 58 ? 11.170 -4.021 -7.746 1.00 31.21 ? 101 VAL A CG1 1 ATOM 466 C CG2 . VAL A 1 58 ? 13.351 -2.792 -7.362 1.00 27.99 ? 101 VAL A CG2 1 ATOM 467 N N . GLU A 1 59 ? 9.238 -1.087 -7.618 1.00 30.51 ? 102 GLU A N 1 ATOM 468 C CA . GLU A 1 59 ? 7.785 -1.058 -7.701 1.00 32.58 ? 102 GLU A CA 1 ATOM 469 C C . GLU A 1 59 ? 7.342 -0.217 -8.902 1.00 32.88 ? 102 GLU A C 1 ATOM 470 O O . GLU A 1 59 ? 6.376 -0.530 -9.575 1.00 33.15 ? 102 GLU A O 1 ATOM 471 C CB . GLU A 1 59 ? 7.163 -0.546 -6.397 1.00 33.53 ? 102 GLU A CB 1 ATOM 472 C CG . GLU A 1 59 ? 6.941 -1.641 -5.340 1.00 40.79 ? 102 GLU A CG 1 ATOM 473 C CD . GLU A 1 59 ? 8.246 -2.202 -4.781 1.00 44.06 ? 102 GLU A CD 1 ATOM 474 O OE1 . GLU A 1 59 ? 8.281 -3.394 -4.412 1.00 49.45 ? 102 GLU A OE1 1 ATOM 475 O OE2 . GLU A 1 59 ? 9.240 -1.448 -4.703 1.00 38.72 ? 102 GLU A OE2 1 ATOM 476 N N . GLN A 1 60 ? 8.096 0.828 -9.184 1.00 27.05 ? 103 GLN A N 1 ATOM 477 C CA . GLN A 1 60 ? 7.777 1.729 -10.296 1.00 29.18 ? 103 GLN A CA 1 ATOM 478 C C . GLN A 1 60 ? 8.021 1.086 -11.656 1.00 32.91 ? 103 GLN A C 1 ATOM 479 O O . GLN A 1 60 ? 7.218 1.219 -12.577 1.00 29.69 ? 103 GLN A O 1 ATOM 480 C CB . GLN A 1 60 ? 8.552 3.027 -10.160 1.00 29.32 ? 103 GLN A CB 1 ATOM 481 C CG . GLN A 1 60 ? 8.024 3.908 -9.033 1.00 31.73 ? 103 GLN A CG 1 ATOM 482 C CD . GLN A 1 60 ? 8.571 5.314 -9.116 1.00 37.30 ? 103 GLN A CD 1 ATOM 483 O OE1 . GLN A 1 60 ? 8.538 5.933 -10.166 1.00 32.28 ? 103 GLN A OE1 1 ATOM 484 N NE2 . GLN A 1 60 ? 9.093 5.820 -8.001 1.00 39.61 ? 103 GLN A NE2 1 ATOM 485 N N . MET A 1 61 ? 9.124 0.369 -11.784 1.00 28.18 ? 104 MET A N 1 ATOM 486 C CA . MET A 1 61 ? 9.347 -0.359 -13.023 1.00 26.70 ? 104 MET A CA 1 ATOM 487 C C . MET A 1 61 ? 8.259 -1.406 -13.248 1.00 29.24 ? 104 MET A C 1 ATOM 488 O O . MET A 1 61 ? 7.781 -1.587 -14.386 1.00 27.30 ? 104 MET A O 1 ATOM 489 C CB . MET A 1 61 ? 10.732 -0.998 -13.071 1.00 30.62 ? 104 MET A CB 1 ATOM 490 C CG . MET A 1 61 ? 10.956 -1.760 -14.377 1.00 37.32 ? 104 MET A CG 1 ATOM 491 S SD . MET A 1 61 ? 12.664 -2.181 -14.742 1.00 31.26 ? 104 MET A SD 1 ATOM 492 C CE . MET A 1 61 ? 12.427 -2.918 -16.357 1.00 39.59 ? 104 MET A CE 1 ATOM 493 N N . GLN A 1 62 ? 7.871 -2.083 -12.168 1.00 28.94 ? 105 GLN A N 1 ATOM 494 C CA . GLN A 1 62 ? 6.845 -3.118 -12.242 1.00 31.01 ? 105 GLN A CA 1 ATOM 495 C C . GLN A 1 62 ? 5.569 -2.494 -12.759 1.00 32.16 ? 105 GLN A C 1 ATOM 496 O O . GLN A 1 62 ? 4.901 -3.040 -13.641 1.00 28.74 ? 105 GLN A O 1 ATOM 497 C CB . GLN A 1 62 ? 6.606 -3.742 -10.862 1.00 29.88 ? 105 GLN A CB 1 ATOM 498 C CG . GLN A 1 62 ? 5.394 -4.672 -10.785 1.00 32.78 ? 105 GLN A CG 1 ATOM 499 C CD . GLN A 1 62 ? 5.717 -6.063 -11.277 1.00 36.78 ? 105 GLN A CD 1 ATOM 500 O OE1 . GLN A 1 62 ? 6.685 -6.255 -12.007 1.00 33.79 ? 105 GLN A OE1 1 ATOM 501 N NE2 . GLN A 1 62 ? 4.928 -7.056 -10.844 1.00 38.80 ? 105 GLN A NE2 1 ATOM 502 N N . GLU A 1 63 ? 5.246 -1.335 -12.198 1.00 32.12 ? 106 GLU A N 1 ATOM 503 C CA . GLU A 1 63 ? 4.076 -0.589 -12.614 1.00 32.12 ? 106 GLU A CA 1 ATOM 504 C C . GLU A 1 63 ? 4.099 -0.323 -14.131 1.00 28.44 ? 106 GLU A C 1 ATOM 505 O O . GLU A 1 63 ? 3.121 -0.582 -14.814 1.00 29.29 ? 106 GLU A O 1 ATOM 506 C CB . GLU A 1 63 ? 3.923 0.678 -11.758 1.00 35.31 ? 106 GLU A CB 1 ATOM 507 C CG . GLU A 1 63 ? 3.531 0.299 -10.314 1.00 34.69 ? 106 GLU A CG 1 ATOM 508 C CD . GLU A 1 63 ? 3.554 1.449 -9.306 1.00 48.37 ? 106 GLU A CD 1 ATOM 509 O OE1 . GLU A 1 63 ? 4.042 2.555 -9.635 1.00 45.24 ? 106 GLU A OE1 1 ATOM 510 O OE2 . GLU A 1 63 ? 3.083 1.229 -8.165 1.00 49.93 ? 106 GLU A OE2 1 ATOM 511 N N . ASP A 1 64 ? 5.227 0.145 -14.651 1.00 27.90 ? 107 ASP A N 1 ATOM 512 C CA . ASP A 1 64 ? 5.361 0.371 -16.094 1.00 32.23 ? 107 ASP A CA 1 ATOM 513 C C . ASP A 1 64 ? 5.184 -0.891 -16.929 1.00 32.05 ? 107 ASP A C 1 ATOM 514 O O . ASP A 1 64 ? 4.481 -0.892 -17.933 1.00 27.07 ? 107 ASP A O 1 ATOM 515 C CB . ASP A 1 64 ? 6.735 0.947 -16.430 1.00 29.67 ? 107 ASP A CB 1 ATOM 516 C CG . ASP A 1 64 ? 6.863 2.422 -16.099 1.00 31.79 ? 107 ASP A CG 1 ATOM 517 O OD1 . ASP A 1 64 ? 5.861 3.104 -15.798 1.00 30.15 ? 107 ASP A OD1 1 ATOM 518 O OD2 . ASP A 1 64 ? 7.992 2.915 -16.212 1.00 30.26 ? 107 ASP A OD2 1 ATOM 519 N N . VAL A 1 65 ? 5.835 -1.975 -16.531 1.00 31.94 ? 108 VAL A N 1 ATOM 520 C CA . VAL A 1 65 ? 5.774 -3.184 -17.350 1.00 29.17 ? 108 VAL A CA 1 ATOM 521 C C . VAL A 1 65 ? 4.366 -3.732 -17.366 1.00 28.74 ? 108 VAL A C 1 ATOM 522 O O . VAL A 1 65 ? 3.906 -4.218 -18.391 1.00 26.57 ? 108 VAL A O 1 ATOM 523 C CB . VAL A 1 65 ? 6.753 -4.244 -16.849 1.00 28.18 ? 108 VAL A CB 1 ATOM 524 C CG1 . VAL A 1 65 ? 6.680 -5.513 -17.735 1.00 28.19 ? 108 VAL A CG1 1 ATOM 525 C CG2 . VAL A 1 65 ? 8.169 -3.653 -16.845 1.00 30.98 ? 108 VAL A CG2 1 ATOM 526 N N . ILE A 1 66 ? 3.665 -3.622 -16.238 1.00 26.04 ? 109 ILE A N 1 ATOM 527 C CA . ILE A 1 66 ? 2.283 -4.068 -16.188 1.00 30.08 ? 109 ILE A CA 1 ATOM 528 C C . ILE A 1 66 ? 1.437 -3.263 -17.192 1.00 27.51 ? 109 ILE A C 1 ATOM 529 O O . ILE A 1 66 ? 0.641 -3.822 -17.956 1.00 29.11 ? 109 ILE A O 1 ATOM 530 C CB . ILE A 1 66 ? 1.713 -3.923 -14.753 1.00 34.58 ? 109 ILE A CB 1 ATOM 531 C CG1 . ILE A 1 66 ? 2.340 -4.976 -13.828 1.00 37.68 ? 109 ILE A CG1 1 ATOM 532 C CG2 . ILE A 1 66 ? 0.197 -4.062 -14.753 1.00 32.87 ? 109 ILE A CG2 1 ATOM 533 C CD1 . ILE A 1 66 ? 1.864 -4.888 -12.404 1.00 40.98 ? 109 ILE A CD1 1 ATOM 534 N N . SER A 1 67 ? 1.638 -1.949 -17.180 1.00 31.17 ? 110 SER A N 1 ATOM 535 C CA . SER A 1 67 ? 0.929 -1.042 -18.072 1.00 33.10 ? 110 SER A CA 1 ATOM 536 C C . SER A 1 67 ? 1.261 -1.340 -19.541 1.00 31.76 ? 110 SER A C 1 ATOM 537 O O . SER A 1 67 ? 0.378 -1.378 -20.402 1.00 33.41 ? 110 SER A O 1 ATOM 538 C CB . SER A 1 67 ? 1.286 0.402 -17.731 1.00 32.16 ? 110 SER A CB 1 ATOM 539 O OG . SER A 1 67 ? 0.775 1.293 -18.708 1.00 45.02 ? 110 SER A OG 1 ATOM 540 N N . LEU A 1 68 ? 2.544 -1.513 -19.831 1.00 27.66 ? 111 LEU A N 1 ATOM 541 C CA . LEU A 1 68 ? 2.965 -1.907 -21.175 1.00 27.74 ? 111 LEU A CA 1 ATOM 542 C C . LEU A 1 68 ? 2.255 -3.205 -21.610 1.00 31.02 ? 111 LEU A C 1 ATOM 543 O O . LEU A 1 68 ? 1.624 -3.272 -22.667 1.00 33.66 ? 111 LEU A O 1 ATOM 544 C CB . LEU A 1 68 ? 4.489 -2.081 -21.216 1.00 32.06 ? 111 LEU A CB 1 ATOM 545 C CG . LEU A 1 68 ? 5.153 -2.138 -22.595 1.00 38.59 ? 111 LEU A CG 1 ATOM 546 C CD1 . LEU A 1 68 ? 6.610 -1.718 -22.483 1.00 34.03 ? 111 LEU A CD1 1 ATOM 547 C CD2 . LEU A 1 68 ? 5.034 -3.530 -23.181 1.00 39.14 ? 111 LEU A CD2 1 ATOM 548 N N . TRP A 1 69 ? 2.339 -4.234 -20.787 1.00 29.69 ? 112 TRP A N 1 ATOM 549 C CA . TRP A 1 69 ? 1.710 -5.492 -21.154 1.00 33.14 ? 112 TRP A CA 1 ATOM 550 C C . TRP A 1 69 ? 0.191 -5.352 -21.301 1.00 35.69 ? 112 TRP A C 1 ATOM 551 O O . TRP A 1 69 ? -0.406 -5.935 -22.208 1.00 35.80 ? 112 TRP A O 1 ATOM 552 C CB . TRP A 1 69 ? 2.076 -6.582 -20.149 1.00 31.50 ? 112 TRP A CB 1 ATOM 553 C CG . TRP A 1 69 ? 3.379 -7.231 -20.455 1.00 30.65 ? 112 TRP A CG 1 ATOM 554 C CD1 . TRP A 1 69 ? 4.597 -6.630 -20.547 1.00 32.64 ? 112 TRP A CD1 1 ATOM 555 C CD2 . TRP A 1 69 ? 3.595 -8.622 -20.709 1.00 31.62 ? 112 TRP A CD2 1 ATOM 556 N NE1 . TRP A 1 69 ? 5.566 -7.563 -20.848 1.00 31.00 ? 112 TRP A NE1 1 ATOM 557 C CE2 . TRP A 1 69 ? 4.974 -8.793 -20.951 1.00 28.52 ? 112 TRP A CE2 1 ATOM 558 C CE3 . TRP A 1 69 ? 2.755 -9.738 -20.752 1.00 32.43 ? 112 TRP A CE3 1 ATOM 559 C CZ2 . TRP A 1 69 ? 5.536 -10.037 -21.220 1.00 29.63 ? 112 TRP A CZ2 1 ATOM 560 C CZ3 . TRP A 1 69 ? 3.316 -10.985 -21.025 1.00 35.39 ? 112 TRP A CZ3 1 ATOM 561 C CH2 . TRP A 1 69 ? 4.694 -11.121 -21.252 1.00 29.87 ? 112 TRP A CH2 1 ATOM 562 N N . ASP A 1 70 ? -0.426 -4.571 -20.420 1.00 32.42 ? 113 ASP A N 1 ATOM 563 C CA . ASP A 1 70 ? -1.874 -4.395 -20.438 1.00 40.71 ? 113 ASP A CA 1 ATOM 564 C C . ASP A 1 70 ? -2.361 -3.752 -21.726 1.00 39.45 ? 113 ASP A C 1 ATOM 565 O O . ASP A 1 70 ? -3.428 -4.085 -22.237 1.00 41.26 ? 113 ASP A O 1 ATOM 566 C CB . ASP A 1 70 ? -2.340 -3.560 -19.243 1.00 45.34 ? 113 ASP A CB 1 ATOM 567 C CG . ASP A 1 70 ? -2.437 -4.372 -17.964 1.00 52.74 ? 113 ASP A CG 1 ATOM 568 O OD1 . ASP A 1 70 ? -1.967 -5.537 -17.951 1.00 52.13 ? 113 ASP A OD1 1 ATOM 569 O OD2 . ASP A 1 70 ? -2.970 -3.837 -16.966 1.00 57.12 ? 113 ASP A OD2 1 ATOM 570 N N . GLN A 1 71 ? -1.593 -2.826 -22.265 1.00 37.43 ? 114 GLN A N 1 ATOM 571 C CA . GLN A 1 71 ? -2.042 -2.203 -23.498 1.00 42.92 ? 114 GLN A CA 1 ATOM 572 C C . GLN A 1 71 ? -1.483 -2.864 -24.763 1.00 42.57 ? 114 GLN A C 1 ATOM 573 O O . GLN A 1 71 ? -1.889 -2.515 -25.874 1.00 44.60 ? 114 GLN A O 1 ATOM 574 C CB . GLN A 1 71 ? -1.797 -0.685 -23.477 1.00 50.52 ? 114 GLN A CB 1 ATOM 575 C CG . GLN A 1 71 ? -0.418 -0.264 -23.042 1.00 48.48 ? 114 GLN A CG 1 ATOM 576 C CD . GLN A 1 71 ? -0.339 1.220 -22.714 1.00 53.44 ? 114 GLN A CD 1 ATOM 577 O OE1 . GLN A 1 71 ? -0.622 1.635 -21.589 1.00 57.77 ? 114 GLN A OE1 1 ATOM 578 N NE2 . GLN A 1 71 ? 0.056 2.024 -23.697 1.00 49.98 ? 114 GLN A NE2 1 ATOM 579 N N . SER A 1 72 ? -0.585 -3.837 -24.608 1.00 32.88 ? 115 SER A N 1 ATOM 580 C CA . SER A 1 72 ? 0.078 -4.418 -25.784 1.00 36.96 ? 115 SER A CA 1 ATOM 581 C C . SER A 1 72 ? -0.337 -5.854 -26.093 1.00 37.80 ? 115 SER A C 1 ATOM 582 O O . SER A 1 72 ? -0.411 -6.245 -27.255 1.00 36.38 ? 115 SER A O 1 ATOM 583 C CB . SER A 1 72 ? 1.602 -4.389 -25.626 1.00 36.24 ? 115 SER A CB 1 ATOM 584 O OG . SER A 1 72 ? 2.068 -3.109 -25.250 1.00 40.27 ? 115 SER A OG 1 ATOM 585 N N . LEU A 1 73 ? -0.570 -6.636 -25.041 1.00 36.46 ? 116 LEU A N 1 ATOM 586 C CA . LEU A 1 73 ? -0.843 -8.059 -25.170 1.00 43.58 ? 116 LEU A CA 1 ATOM 587 C C . LEU A 1 73 ? -2.255 -8.418 -24.785 1.00 55.59 ? 116 LEU A C 1 ATOM 588 O O . LEU A 1 73 ? -2.464 -9.136 -23.802 1.00 58.90 ? 116 LEU A O 1 ATOM 589 C CB . LEU A 1 73 ? 0.119 -8.866 -24.298 1.00 44.57 ? 116 LEU A CB 1 ATOM 590 C CG . LEU A 1 73 ? 1.493 -9.066 -24.932 1.00 54.55 ? 116 LEU A CG 1 ATOM 591 C CD1 . LEU A 1 73 ? 2.591 -9.090 -23.899 1.00 60.47 ? 116 LEU A CD1 1 ATOM 592 C CD2 . LEU A 1 73 ? 1.487 -10.339 -25.758 1.00 55.29 ? 116 LEU A CD2 1 ATOM 593 N N . GLN A 1 74 ? -3.219 -7.942 -25.562 1.00 59.63 ? 117 GLN A N 1 ATOM 594 C CA . GLN A 1 74 ? -4.604 -8.401 -25.434 1.00 66.58 ? 117 GLN A CA 1 ATOM 595 C C . GLN A 1 74 ? -4.760 -9.889 -25.788 1.00 53.24 ? 117 GLN A C 1 ATOM 596 O O . GLN A 1 74 ? -4.458 -10.300 -26.909 1.00 55.69 ? 117 GLN A O 1 ATOM 597 C CB . GLN A 1 74 ? -5.519 -7.592 -26.359 1.00 81.85 ? 117 GLN A CB 1 ATOM 598 C CG . GLN A 1 74 ? -5.483 -6.083 -26.152 1.00 95.49 ? 117 GLN A CG 1 ATOM 599 C CD . GLN A 1 74 ? -6.409 -5.341 -27.114 1.00 103.93 ? 117 GLN A CD 1 ATOM 600 O OE1 . GLN A 1 74 ? -6.800 -5.873 -28.159 1.00 104.03 ? 117 GLN A OE1 1 ATOM 601 N NE2 . GLN A 1 74 ? -6.771 -4.110 -26.757 1.00 107.11 ? 117 GLN A NE2 1 ATOM 602 N N . PRO A 1 75 ? -5.260 -10.704 -24.844 1.00 45.38 ? 118 PRO A N 1 ATOM 603 C CA . PRO A 1 75 ? -5.605 -12.067 -25.250 1.00 39.98 ? 118 PRO A CA 1 ATOM 604 C C . PRO A 1 75 ? -6.977 -12.073 -25.923 1.00 41.54 ? 118 PRO A C 1 ATOM 605 O O . PRO A 1 75 ? -7.699 -11.077 -25.840 1.00 41.09 ? 118 PRO A O 1 ATOM 606 C CB . PRO A 1 75 ? -5.674 -12.805 -23.915 1.00 42.19 ? 118 PRO A CB 1 ATOM 607 C CG . PRO A 1 75 ? -6.165 -11.768 -22.953 1.00 41.36 ? 118 PRO A CG 1 ATOM 608 C CD . PRO A 1 75 ? -5.567 -10.453 -23.426 1.00 42.04 ? 118 PRO A CD 1 ATOM 609 N N . CYS A 1 76 ? -7.334 -13.172 -26.577 1.00 41.11 ? 119 CYS A N 1 ATOM 610 C CA . CYS A 1 76 ? -8.667 -13.318 -27.156 1.00 41.39 ? 119 CYS A CA 1 ATOM 611 C C . CYS A 1 76 ? -9.690 -13.401 -26.033 1.00 44.46 ? 119 CYS A C 1 ATOM 612 O O . CYS A 1 76 ? -10.806 -12.895 -26.150 1.00 42.38 ? 119 CYS A O 1 ATOM 613 C CB . CYS A 1 76 ? -8.751 -14.587 -27.999 1.00 42.32 ? 119 CYS A CB 1 ATOM 614 S SG . CYS A 1 76 ? -7.323 -14.881 -29.058 1.00 54.87 ? 119 CYS A SG 1 ATOM 615 N N . VAL A 1 77 ? -9.298 -14.064 -24.950 1.00 41.14 ? 120 VAL A N 1 ATOM 616 C CA . VAL A 1 77 ? -10.166 -14.250 -23.803 1.00 42.01 ? 120 VAL A CA 1 ATOM 617 C C . VAL A 1 77 ? -9.353 -14.022 -22.544 1.00 43.69 ? 120 VAL A C 1 ATOM 618 O O . VAL A 1 77 ? -8.243 -14.536 -22.417 1.00 41.14 ? 120 VAL A O 1 ATOM 619 C CB . VAL A 1 77 ? -10.747 -15.667 -23.754 1.00 45.86 ? 120 VAL A CB 1 ATOM 620 C CG1 . VAL A 1 77 ? -11.547 -15.868 -22.466 1.00 50.46 ? 120 VAL A CG1 1 ATOM 621 C CG2 . VAL A 1 77 ? -11.623 -15.926 -24.968 1.00 48.89 ? 120 VAL A CG2 1 ATOM 622 N N . LYS A 1 78 ? -9.906 -13.241 -21.622 1.00 43.94 ? 121 LYS A N 1 ATOM 623 C CA . LYS A 1 78 ? -9.287 -13.031 -20.316 1.00 43.16 ? 121 LYS A CA 1 ATOM 624 C C . LYS A 1 78 ? -10.267 -13.420 -19.215 1.00 48.03 ? 121 LYS A C 1 ATOM 625 O O . LYS A 1 78 ? -11.435 -13.016 -19.226 1.00 48.35 ? 121 LYS A O 1 ATOM 626 C CB . LYS A 1 78 ? -8.833 -11.576 -20.156 1.00 49.11 ? 121 LYS A CB 1 ATOM 627 C CG . LYS A 1 78 ? -8.131 -11.280 -18.843 1.00 58.65 ? 121 LYS A CG 1 ATOM 628 C CD . LYS A 1 78 ? -7.223 -10.058 -18.970 1.00 65.96 ? 121 LYS A CD 1 ATOM 629 C CE . LYS A 1 78 ? -7.958 -8.840 -19.525 1.00 73.54 ? 121 LYS A CE 1 ATOM 630 N NZ . LYS A 1 78 ? -7.064 -7.637 -19.620 1.00 74.07 ? 121 LYS A NZ 1 ATOM 631 N N . LEU A 1 79 ? -9.786 -14.233 -18.281 1.00 49.10 ? 122 LEU A N 1 ATOM 632 C CA . LEU A 1 79 ? -10.600 -14.718 -17.180 1.00 52.19 ? 122 LEU A CA 1 ATOM 633 C C . LEU A 1 79 ? -10.011 -14.125 -15.916 1.00 54.98 ? 122 LEU A C 1 ATOM 634 O O . LEU A 1 79 ? -8.951 -14.550 -15.449 1.00 51.71 ? 122 LEU A O 1 ATOM 635 C CB . LEU A 1 79 ? -10.551 -16.242 -17.124 1.00 59.28 ? 122 LEU A CB 1 ATOM 636 C CG . LEU A 1 79 ? -10.750 -16.967 -18.465 1.00 63.94 ? 122 LEU A CG 1 ATOM 637 C CD1 . LEU A 1 79 ? -10.332 -18.436 -18.373 1.00 63.61 ? 122 LEU A CD1 1 ATOM 638 C CD2 . LEU A 1 79 ? -12.189 -16.831 -18.961 1.00 68.14 ? 122 LEU A CD2 1 ATOM 639 N N . THR A 1 80 ? -10.688 -13.121 -15.375 1.00 56.13 ? 123 THR A N 1 ATOM 640 C CA . THR A 1 80 ? -10.130 -12.360 -14.263 1.00 54.07 ? 123 THR A CA 1 ATOM 641 C C . THR A 1 80 ? -11.217 -11.985 -13.261 1.00 59.77 ? 123 THR A C 1 ATOM 642 O O . THR A 1 80 ? -12.311 -11.572 -13.646 1.00 63.01 ? 123 THR A O 1 ATOM 643 C CB . THR A 1 80 ? -9.417 -11.093 -14.773 1.00 53.03 ? 123 THR A CB 1 ATOM 644 O OG1 . THR A 1 80 ? -8.901 -10.351 -13.662 1.00 53.73 ? 123 THR A OG1 1 ATOM 645 C CG2 . THR A 1 80 ? -10.386 -10.222 -15.578 1.00 55.31 ? 123 THR A CG2 1 ATOM 646 N N . GLY A 1 81 ? -10.915 -12.148 -11.975 1.00 62.20 ? 124 GLY A N 1 ATOM 647 C CA . GLY A 1 81 ? -11.890 -11.908 -10.924 1.00 64.23 ? 124 GLY A CA 1 ATOM 648 C C . GLY A 1 81 ? -13.276 -12.448 -11.242 1.00 68.20 ? 124 GLY A C 1 ATOM 649 O O . GLY A 1 81 ? -14.285 -11.805 -10.945 1.00 73.06 ? 124 GLY A O 1 ATOM 650 N N . GLY A 1 82 ? -13.331 -13.628 -11.855 1.00 67.33 ? 198 GLY A N 1 ATOM 651 C CA . GLY A 1 82 ? -14.598 -14.286 -12.127 1.00 67.43 ? 198 GLY A CA 1 ATOM 652 C C . GLY A 1 82 ? -15.356 -13.795 -13.350 1.00 67.84 ? 198 GLY A C 1 ATOM 653 O O . GLY A 1 82 ? -16.434 -14.304 -13.664 1.00 65.51 ? 198 GLY A O 1 ATOM 654 N N . SER A 1 83 ? -14.806 -12.805 -14.047 1.00 67.18 ? 199 SER A N 1 ATOM 655 C CA . SER A 1 83 ? -15.447 -12.303 -15.260 1.00 68.96 ? 199 SER A CA 1 ATOM 656 C C . SER A 1 83 ? -14.706 -12.747 -16.527 1.00 59.74 ? 199 SER A C 1 ATOM 657 O O . SER A 1 83 ? -13.521 -13.092 -16.484 1.00 55.52 ? 199 SER A O 1 ATOM 658 C CB . SER A 1 83 ? -15.594 -10.778 -15.215 1.00 72.61 ? 199 SER A CB 1 ATOM 659 O OG . SER A 1 83 ? -14.339 -10.151 -15.028 1.00 71.39 ? 199 SER A OG 1 ATOM 660 N N . VAL A 1 84 ? -15.418 -12.740 -17.649 1.00 58.10 ? 200 VAL A N 1 ATOM 661 C CA . VAL A 1 84 ? -14.860 -13.192 -18.917 1.00 62.18 ? 200 VAL A CA 1 ATOM 662 C C . VAL A 1 84 ? -14.903 -12.061 -19.932 1.00 64.31 ? 200 VAL A C 1 ATOM 663 O O . VAL A 1 84 ? -15.973 -11.528 -20.242 1.00 64.65 ? 200 VAL A O 1 ATOM 664 C CB . VAL A 1 84 ? -15.634 -14.393 -19.492 1.00 63.96 ? 200 VAL A CB 1 ATOM 665 C CG1 . VAL A 1 84 ? -14.939 -14.915 -20.749 1.00 62.57 ? 200 VAL A CG1 1 ATOM 666 C CG2 . VAL A 1 84 ? -15.771 -15.496 -18.450 1.00 64.50 ? 200 VAL A CG2 1 ATOM 667 N N . ILE A 1 85 ? -13.735 -11.704 -20.451 1.00 57.27 ? 201 ILE A N 1 ATOM 668 C CA . ILE A 1 85 ? -13.626 -10.616 -21.409 1.00 58.61 ? 201 ILE A CA 1 ATOM 669 C C . ILE A 1 85 ? -13.140 -11.138 -22.755 1.00 55.16 ? 201 ILE A C 1 ATOM 670 O O . ILE A 1 85 ? -12.090 -11.776 -22.843 1.00 51.62 ? 201 ILE A O 1 ATOM 671 C CB . ILE A 1 85 ? -12.648 -9.533 -20.903 1.00 61.71 ? 201 ILE A CB 1 ATOM 672 C CG1 . ILE A 1 85 ? -13.080 -9.020 -19.522 1.00 66.32 ? 201 ILE A CG1 1 ATOM 673 C CG2 . ILE A 1 85 ? -12.532 -8.408 -21.920 1.00 58.13 ? 201 ILE A CG2 1 ATOM 674 C CD1 . ILE A 1 85 ? -12.021 -8.194 -18.817 1.00 66.86 ? 201 ILE A CD1 1 ATOM 675 N N . LYS A 1 86 ? -13.914 -10.873 -23.801 1.00 57.21 ? 202 LYS A N 1 ATOM 676 C CA . LYS A 1 86 ? -13.568 -11.330 -25.143 1.00 57.96 ? 202 LYS A CA 1 ATOM 677 C C . LYS A 1 86 ? -13.245 -10.143 -26.034 1.00 59.58 ? 202 LYS A C 1 ATOM 678 O O . LYS A 1 86 ? -13.903 -9.110 -25.968 1.00 57.20 ? 202 LYS A O 1 ATOM 679 C CB . LYS A 1 86 ? -14.721 -12.131 -25.756 1.00 59.22 ? 202 LYS A CB 1 ATOM 680 C CG . LYS A 1 86 ? -15.066 -13.414 -25.011 1.00 60.57 ? 202 LYS A CG 1 ATOM 681 C CD . LYS A 1 86 ? -16.333 -14.043 -25.565 1.00 65.60 ? 202 LYS A CD 1 ATOM 682 C CE . LYS A 1 86 ? -16.600 -15.398 -24.933 1.00 68.96 ? 202 LYS A CE 1 ATOM 683 N NZ . LYS A 1 86 ? -17.648 -16.179 -25.662 1.00 71.24 ? 202 LYS A NZ 1 ATOM 684 N N . GLN A 1 87 ? -12.240 -10.298 -26.882 1.00 61.27 ? 203 GLN A N 1 ATOM 685 C CA . GLN A 1 87 ? -11.873 -9.229 -27.792 1.00 62.63 ? 203 GLN A CA 1 ATOM 686 C C . GLN A 1 87 ? -10.926 -9.734 -28.853 1.00 57.93 ? 203 GLN A C 1 ATOM 687 O O . GLN A 1 87 ? -10.518 -10.894 -28.822 1.00 54.30 ? 203 GLN A O 1 ATOM 688 C CB . GLN A 1 87 ? -11.206 -8.111 -27.021 1.00 65.67 ? 203 GLN A CB 1 ATOM 689 C CG . GLN A 1 87 ? -9.997 -8.561 -26.261 1.00 68.11 ? 203 GLN A CG 1 ATOM 690 C CD . GLN A 1 87 ? -9.470 -7.466 -25.387 1.00 76.39 ? 203 GLN A CD 1 ATOM 691 O OE1 . GLN A 1 87 ? -9.762 -7.410 -24.194 1.00 78.17 ? 203 GLN A OE1 1 ATOM 692 N NE2 . GLN A 1 87 ? -8.704 -6.564 -25.980 1.00 82.87 ? 203 GLN A NE2 1 ATOM 693 N N . ALA A 1 88 ? -10.573 -8.854 -29.784 1.00 55.93 ? 204 ALA A N 1 ATOM 694 C CA . ALA A 1 88 ? -9.677 -9.217 -30.871 1.00 57.97 ? 204 ALA A CA 1 ATOM 695 C C . ALA A 1 88 ? -8.277 -9.473 -30.332 1.00 49.11 ? 204 ALA A C 1 ATOM 696 O O . ALA A 1 88 ? -7.826 -8.822 -29.387 1.00 48.84 ? 204 ALA A O 1 ATOM 697 C CB . ALA A 1 88 ? -9.659 -8.135 -31.938 1.00 61.86 ? 204 ALA A CB 1 ATOM 698 N N . CYS A 1 89 ? -7.593 -10.437 -30.930 1.00 45.99 ? 205 CYS A N 1 ATOM 699 C CA . CYS A 1 89 ? -6.283 -10.839 -30.443 1.00 48.36 ? 205 CYS A CA 1 ATOM 700 C C . CYS A 1 89 ? -5.329 -11.060 -31.613 1.00 51.27 ? 205 CYS A C 1 ATOM 701 O O . CYS A 1 89 ? -4.828 -12.167 -31.817 1.00 50.54 ? 205 CYS A O 1 ATOM 702 C CB . CYS A 1 89 ? -6.411 -12.114 -29.604 1.00 48.69 ? 205 CYS A CB 1 ATOM 703 S SG . CYS A 1 89 ? -7.418 -13.371 -30.413 1.00 53.29 ? 205 CYS A SG 1 ATOM 704 N N . PRO A 1 90 ? -5.074 -9.997 -32.386 1.00 50.36 ? 206 PRO A N 1 ATOM 705 C CA . PRO A 1 90 ? -4.163 -10.114 -33.522 1.00 50.07 ? 206 PRO A CA 1 ATOM 706 C C . PRO A 1 90 ? -2.756 -10.452 -33.046 1.00 45.12 ? 206 PRO A C 1 ATOM 707 O O . PRO A 1 90 ? -2.390 -10.124 -31.917 1.00 39.96 ? 206 PRO A O 1 ATOM 708 C CB . PRO A 1 90 ? -4.183 -8.704 -34.127 1.00 50.56 ? 206 PRO A CB 1 ATOM 709 C CG . PRO A 1 90 ? -4.529 -7.809 -32.983 1.00 48.52 ? 206 PRO A CG 1 ATOM 710 C CD . PRO A 1 90 ? -5.493 -8.603 -32.149 1.00 51.41 ? 206 PRO A CD 1 ATOM 711 N N . LYS A 1 91 ? -1.976 -11.099 -33.904 1.00 41.95 ? 207 LYS A N 1 ATOM 712 C CA . LYS A 1 91 ? -0.559 -11.271 -33.643 1.00 39.61 ? 207 LYS A CA 1 ATOM 713 C C . LYS A 1 91 ? 0.153 -9.932 -33.632 1.00 39.63 ? 207 LYS A C 1 ATOM 714 O O . LYS A 1 91 ? -0.160 -9.034 -34.413 1.00 38.90 ? 207 LYS A O 1 ATOM 715 C CB . LYS A 1 91 ? 0.073 -12.197 -34.679 1.00 42.09 ? 207 LYS A CB 1 ATOM 716 C CG . LYS A 1 91 ? -0.384 -13.642 -34.533 1.00 42.35 ? 207 LYS A CG 1 ATOM 717 C CD . LYS A 1 91 ? -0.112 -14.139 -33.114 1.00 42.16 ? 207 LYS A CD 1 ATOM 718 C CE . LYS A 1 91 ? -0.193 -15.629 -33.039 1.00 40.05 ? 207 LYS A CE 1 ATOM 719 N NZ . LYS A 1 91 ? -0.043 -16.171 -31.650 1.00 36.83 ? 207 LYS A NZ 1 ATOM 720 N N . ILE A 1 92 ? 1.116 -9.800 -32.730 1.00 38.14 ? 208 ILE A N 1 ATOM 721 C CA . ILE A 1 92 ? 1.852 -8.563 -32.583 1.00 32.80 ? 208 ILE A CA 1 ATOM 722 C C . ILE A 1 92 ? 3.336 -8.763 -32.825 1.00 35.57 ? 208 ILE A C 1 ATOM 723 O O . ILE A 1 92 ? 3.831 -9.890 -32.912 1.00 36.00 ? 208 ILE A O 1 ATOM 724 C CB . ILE A 1 92 ? 1.661 -7.977 -31.157 1.00 41.66 ? 208 ILE A CB 1 ATOM 725 C CG1 . ILE A 1 92 ? 2.169 -8.968 -30.091 1.00 37.11 ? 208 ILE A CG1 1 ATOM 726 C CG2 . ILE A 1 92 ? 0.199 -7.652 -30.925 1.00 42.82 ? 208 ILE A CG2 1 ATOM 727 C CD1 . ILE A 1 92 ? 2.789 -8.314 -28.854 1.00 37.72 ? 208 ILE A CD1 1 ATOM 728 N N . SER A 1 93 ? 4.041 -7.648 -32.907 1.00 36.67 ? 209 SER A N 1 ATOM 729 C CA . SER A 1 93 ? 5.478 -7.643 -33.031 1.00 36.14 ? 209 SER A CA 1 ATOM 730 C C . SER A 1 93 ? 5.990 -7.305 -31.632 1.00 37.17 ? 209 SER A C 1 ATOM 731 O O . SER A 1 93 ? 5.576 -6.305 -31.049 1.00 33.58 ? 209 SER A O 1 ATOM 732 C CB . SER A 1 93 ? 5.905 -6.590 -34.059 1.00 38.71 ? 209 SER A CB 1 ATOM 733 O OG . SER A 1 93 ? 7.295 -6.333 -33.999 1.00 38.92 ? 209 SER A OG 1 ATOM 734 N N . PHE A 1 94 ? 6.875 -8.144 -31.101 1.00 31.79 ? 210 PHE A N 1 ATOM 735 C CA . PHE A 1 94 ? 7.237 -8.090 -29.686 1.00 33.55 ? 210 PHE A CA 1 ATOM 736 C C . PHE A 1 94 ? 8.709 -8.429 -29.496 1.00 33.43 ? 210 PHE A C 1 ATOM 737 O O . PHE A 1 94 ? 9.151 -9.538 -29.821 1.00 34.64 ? 210 PHE A O 1 ATOM 738 C CB . PHE A 1 94 ? 6.361 -9.094 -28.897 1.00 35.47 ? 210 PHE A CB 1 ATOM 739 C CG . PHE A 1 94 ? 6.637 -9.131 -27.405 1.00 35.47 ? 210 PHE A CG 1 ATOM 740 C CD1 . PHE A 1 94 ? 5.744 -8.561 -26.503 1.00 33.55 ? 210 PHE A CD1 1 ATOM 741 C CD2 . PHE A 1 94 ? 7.769 -9.754 -26.907 1.00 31.11 ? 210 PHE A CD2 1 ATOM 742 C CE1 . PHE A 1 94 ? 5.986 -8.600 -25.126 1.00 33.81 ? 210 PHE A CE1 1 ATOM 743 C CE2 . PHE A 1 94 ? 8.015 -9.805 -25.529 1.00 33.75 ? 210 PHE A CE2 1 ATOM 744 C CZ . PHE A 1 94 ? 7.120 -9.230 -24.643 1.00 29.15 ? 210 PHE A CZ 1 ATOM 745 N N . ASP A 1 95 ? 9.445 -7.484 -28.922 1.00 31.46 ? 211 ASP A N 1 ATOM 746 C CA . ASP A 1 95 ? 10.875 -7.620 -28.690 1.00 32.31 ? 211 ASP A CA 1 ATOM 747 C C . ASP A 1 95 ? 11.260 -6.459 -27.775 1.00 28.96 ? 211 ASP A C 1 ATOM 748 O O . ASP A 1 95 ? 11.277 -5.301 -28.220 1.00 32.48 ? 211 ASP A O 1 ATOM 749 C CB . ASP A 1 95 ? 11.640 -7.514 -30.019 1.00 35.05 ? 211 ASP A CB 1 ATOM 750 C CG . ASP A 1 95 ? 13.124 -7.797 -29.870 1.00 41.45 ? 211 ASP A CG 1 ATOM 751 O OD1 . ASP A 1 95 ? 13.526 -8.424 -28.864 1.00 38.40 ? 211 ASP A OD1 1 ATOM 752 O OD2 . ASP A 1 95 ? 13.890 -7.418 -30.780 1.00 51.03 ? 211 ASP A OD2 1 ATOM 753 N N . PRO A 1 96 ? 11.549 -6.764 -26.500 1.00 30.86 ? 212 PRO A N 1 ATOM 754 C CA . PRO A 1 96 ? 11.777 -5.726 -25.485 1.00 33.25 ? 212 PRO A CA 1 ATOM 755 C C . PRO A 1 96 ? 12.861 -4.735 -25.878 1.00 32.31 ? 212 PRO A C 1 ATOM 756 O O . PRO A 1 96 ? 13.852 -5.108 -26.487 1.00 34.80 ? 212 PRO A O 1 ATOM 757 C CB . PRO A 1 96 ? 12.212 -6.542 -24.267 1.00 30.61 ? 212 PRO A CB 1 ATOM 758 C CG . PRO A 1 96 ? 11.440 -7.818 -24.405 1.00 29.65 ? 212 PRO A CG 1 ATOM 759 C CD . PRO A 1 96 ? 11.508 -8.114 -25.889 1.00 26.91 ? 212 PRO A CD 1 ATOM 760 N N . ILE A 1 97 ? 12.670 -3.467 -25.544 1.00 31.35 ? 213 ILE A N 1 ATOM 761 C CA . ILE A 1 97 ? 13.737 -2.514 -25.767 1.00 31.35 ? 213 ILE A CA 1 ATOM 762 C C . ILE A 1 97 ? 14.190 -1.947 -24.421 1.00 28.31 ? 213 ILE A C 1 ATOM 763 O O . ILE A 1 97 ? 13.453 -1.999 -23.418 1.00 29.54 ? 213 ILE A O 1 ATOM 764 C CB . ILE A 1 97 ? 13.323 -1.373 -26.728 1.00 35.41 ? 213 ILE A CB 1 ATOM 765 C CG1 . ILE A 1 97 ? 12.320 -0.438 -26.047 1.00 31.97 ? 213 ILE A CG1 1 ATOM 766 C CG2 . ILE A 1 97 ? 12.814 -1.938 -28.086 1.00 42.47 ? 213 ILE A CG2 1 ATOM 767 C CD1 . ILE A 1 97 ? 11.982 0.786 -26.896 1.00 32.74 ? 213 ILE A CD1 1 ATOM 768 N N . PRO A 1 98 ? 15.413 -1.415 -24.380 1.00 32.56 ? 214 PRO A N 1 ATOM 769 C CA . PRO A 1 98 ? 15.889 -0.886 -23.106 1.00 32.68 ? 214 PRO A CA 1 ATOM 770 C C . PRO A 1 98 ? 15.081 0.346 -22.702 1.00 34.61 ? 214 PRO A C 1 ATOM 771 O O . PRO A 1 98 ? 14.781 1.210 -23.533 1.00 33.08 ? 214 PRO A O 1 ATOM 772 C CB . PRO A 1 98 ? 17.333 -0.474 -23.418 1.00 36.01 ? 214 PRO A CB 1 ATOM 773 C CG . PRO A 1 98 ? 17.726 -1.282 -24.581 1.00 38.51 ? 214 PRO A CG 1 ATOM 774 C CD . PRO A 1 98 ? 16.473 -1.440 -25.399 1.00 36.49 ? 214 PRO A CD 1 ATOM 775 N N . ILE A 1 99 ? 14.736 0.408 -21.427 1.00 31.82 ? 215 ILE A N 1 ATOM 776 C CA . ILE A 1 99 ? 14.070 1.564 -20.856 1.00 30.84 ? 215 ILE A CA 1 ATOM 777 C C . ILE A 1 99 ? 14.952 2.109 -19.739 1.00 30.53 ? 215 ILE A C 1 ATOM 778 O O . ILE A 1 99 ? 15.369 1.347 -18.851 1.00 29.47 ? 215 ILE A O 1 ATOM 779 C CB . ILE A 1 99 ? 12.702 1.156 -20.261 1.00 35.06 ? 215 ILE A CB 1 ATOM 780 C CG1 . ILE A 1 99 ? 11.840 0.443 -21.325 1.00 33.17 ? 215 ILE A CG1 1 ATOM 781 C CG2 . ILE A 1 99 ? 11.989 2.367 -19.688 1.00 35.87 ? 215 ILE A CG2 1 ATOM 782 C CD1 . ILE A 1 99 ? 11.568 1.280 -22.575 1.00 36.97 ? 215 ILE A CD1 1 ATOM 783 N N . HIS A 1 100 ? 15.231 3.415 -19.770 1.00 31.82 ? 216 HIS A N 1 ATOM 784 C CA . HIS A 1 100 ? 15.987 4.058 -18.688 1.00 32.06 ? 216 HIS A CA 1 ATOM 785 C C . HIS A 1 100 ? 15.040 4.694 -17.678 1.00 31.00 ? 216 HIS A C 1 ATOM 786 O O . HIS A 1 100 ? 14.003 5.244 -18.056 1.00 33.29 ? 216 HIS A O 1 ATOM 787 C CB . HIS A 1 100 ? 16.905 5.144 -19.237 1.00 33.34 ? 216 HIS A CB 1 ATOM 788 C CG . HIS A 1 100 ? 17.778 4.692 -20.368 1.00 38.92 ? 216 HIS A CG 1 ATOM 789 N ND1 . HIS A 1 100 ? 19.149 4.603 -20.261 1.00 35.41 ? 216 HIS A ND1 1 ATOM 790 C CD2 . HIS A 1 100 ? 17.475 4.335 -21.642 1.00 41.52 ? 216 HIS A CD2 1 ATOM 791 C CE1 . HIS A 1 100 ? 19.654 4.205 -21.416 1.00 36.40 ? 216 HIS A CE1 1 ATOM 792 N NE2 . HIS A 1 100 ? 18.660 4.030 -22.270 1.00 34.70 ? 216 HIS A NE2 1 ATOM 793 N N . TYR A 1 101 ? 15.402 4.616 -16.403 1.00 30.55 ? 217 TYR A N 1 ATOM 794 C CA . TYR A 1 101 ? 14.594 5.207 -15.348 1.00 29.04 ? 217 TYR A CA 1 ATOM 795 C C . TYR A 1 101 ? 15.300 6.445 -14.825 1.00 34.32 ? 217 TYR A C 1 ATOM 796 O O . TYR A 1 101 ? 16.475 6.393 -14.503 1.00 31.84 ? 217 TYR A O 1 ATOM 797 C CB . TYR A 1 101 ? 14.257 4.164 -14.266 1.00 27.73 ? 217 TYR A CB 1 ATOM 798 C CG . TYR A 1 101 ? 13.118 3.318 -14.762 1.00 35.58 ? 217 TYR A CG 1 ATOM 799 C CD1 . TYR A 1 101 ? 11.801 3.704 -14.547 1.00 33.28 ? 217 TYR A CD1 1 ATOM 800 C CD2 . TYR A 1 101 ? 13.357 2.189 -15.546 1.00 35.75 ? 217 TYR A CD2 1 ATOM 801 C CE1 . TYR A 1 101 ? 10.748 2.967 -15.066 1.00 28.84 ? 217 TYR A CE1 1 ATOM 802 C CE2 . TYR A 1 101 ? 12.314 1.442 -16.054 1.00 37.54 ? 217 TYR A CE2 1 ATOM 803 C CZ . TYR A 1 101 ? 11.018 1.841 -15.815 1.00 30.70 ? 217 TYR A CZ 1 ATOM 804 O OH . TYR A 1 101 ? 9.985 1.117 -16.345 1.00 31.19 ? 217 TYR A OH 1 ATOM 805 N N . CYS A 1 102 ? 14.578 7.560 -14.792 1.00 31.98 ? 218 CYS A N 1 ATOM 806 C CA . CYS A 1 102 ? 15.184 8.864 -14.569 1.00 30.15 ? 218 CYS A CA 1 ATOM 807 C C . CYS A 1 102 ? 14.497 9.653 -13.445 1.00 31.57 ? 218 CYS A C 1 ATOM 808 O O . CYS A 1 102 ? 13.292 9.559 -13.239 1.00 33.26 ? 218 CYS A O 1 ATOM 809 C CB . CYS A 1 102 ? 15.149 9.680 -15.867 1.00 38.79 ? 218 CYS A CB 1 ATOM 810 S SG . CYS A 1 102 ? 15.786 8.819 -17.346 1.00 37.53 ? 218 CYS A SG 1 ATOM 811 N N . THR A 1 103 ? 15.276 10.459 -12.741 1.00 37.11 ? 219 THR A N 1 ATOM 812 C CA . THR A 1 103 ? 14.719 11.316 -11.711 1.00 36.80 ? 219 THR A CA 1 ATOM 813 C C . THR A 1 103 ? 14.282 12.671 -12.239 1.00 36.60 ? 219 THR A C 1 ATOM 814 O O . THR A 1 103 ? 14.933 13.260 -13.113 1.00 35.64 ? 219 THR A O 1 ATOM 815 C CB . THR A 1 103 ? 15.748 11.548 -10.574 1.00 37.39 ? 219 THR A CB 1 ATOM 816 O OG1 . THR A 1 103 ? 17.057 11.680 -11.143 1.00 38.18 ? 219 THR A OG1 1 ATOM 817 C CG2 . THR A 1 103 ? 15.730 10.378 -9.601 1.00 31.01 ? 219 THR A CG2 1 ATOM 818 N N . PRO A 1 104 ? 13.196 13.203 -11.665 1.00 39.01 ? 220 PRO A N 1 ATOM 819 C CA . PRO A 1 104 ? 12.800 14.575 -11.978 1.00 44.03 ? 220 PRO A CA 1 ATOM 820 C C . PRO A 1 104 ? 13.696 15.572 -11.237 1.00 43.64 ? 220 PRO A C 1 ATOM 821 O O . PRO A 1 104 ? 14.527 15.181 -10.405 1.00 42.79 ? 220 PRO A O 1 ATOM 822 C CB . PRO A 1 104 ? 11.368 14.643 -11.448 1.00 46.92 ? 220 PRO A CB 1 ATOM 823 C CG . PRO A 1 104 ? 11.369 13.711 -10.284 1.00 41.13 ? 220 PRO A CG 1 ATOM 824 C CD . PRO A 1 104 ? 12.327 12.592 -10.641 1.00 36.43 ? 220 PRO A CD 1 ATOM 825 N N . ALA A 1 105 ? 13.527 16.849 -11.544 1.00 41.12 ? 221 ALA A N 1 ATOM 826 C CA . ALA A 1 105 ? 14.320 17.901 -10.910 1.00 43.26 ? 221 ALA A CA 1 ATOM 827 C C . ALA A 1 105 ? 14.259 17.815 -9.380 1.00 46.77 ? 221 ALA A C 1 ATOM 828 O O . ALA A 1 105 ? 13.234 17.441 -8.809 1.00 45.57 ? 221 ALA A O 1 ATOM 829 C CB . ALA A 1 105 ? 13.847 19.280 -11.399 1.00 48.02 ? 221 ALA A CB 1 ATOM 830 N N . GLY A 1 106 ? 15.360 18.165 -8.719 1.00 49.94 ? 222 GLY A N 1 ATOM 831 C CA . GLY A 1 106 ? 15.405 18.101 -7.269 1.00 53.13 ? 222 GLY A CA 1 ATOM 832 C C . GLY A 1 106 ? 15.744 16.729 -6.721 1.00 46.99 ? 222 GLY A C 1 ATOM 833 O O . GLY A 1 106 ? 15.889 16.553 -5.511 1.00 41.73 ? 222 GLY A O 1 ATOM 834 N N . TYR A 1 107 ? 15.860 15.738 -7.600 1.00 45.34 ? 223 TYR A N 1 ATOM 835 C CA . TYR A 1 107 ? 16.300 14.411 -7.165 1.00 39.12 ? 223 TYR A CA 1 ATOM 836 C C . TYR A 1 107 ? 17.400 13.913 -8.071 1.00 41.13 ? 223 TYR A C 1 ATOM 837 O O . TYR A 1 107 ? 17.613 14.429 -9.174 1.00 44.43 ? 223 TYR A O 1 ATOM 838 C CB . TYR A 1 107 ? 15.164 13.389 -7.183 1.00 37.41 ? 223 TYR A CB 1 ATOM 839 C CG . TYR A 1 107 ? 13.990 13.741 -6.319 1.00 43.09 ? 223 TYR A CG 1 ATOM 840 C CD1 . TYR A 1 107 ? 13.740 13.057 -5.142 1.00 40.29 ? 223 TYR A CD1 1 ATOM 841 C CD2 . TYR A 1 107 ? 13.117 14.748 -6.688 1.00 43.24 ? 223 TYR A CD2 1 ATOM 842 C CE1 . TYR A 1 107 ? 12.656 13.380 -4.349 1.00 42.72 ? 223 TYR A CE1 1 ATOM 843 C CE2 . TYR A 1 107 ? 12.034 15.074 -5.909 1.00 47.59 ? 223 TYR A CE2 1 ATOM 844 C CZ . TYR A 1 107 ? 11.803 14.388 -4.742 1.00 50.50 ? 223 TYR A CZ 1 ATOM 845 O OH . TYR A 1 107 ? 10.713 14.724 -3.969 1.00 57.23 ? 223 TYR A OH 1 ATOM 846 N N . VAL A 1 108 ? 18.107 12.897 -7.603 1.00 36.67 ? 224 VAL A N 1 ATOM 847 C CA . VAL A 1 108 ? 19.137 12.302 -8.421 1.00 37.64 ? 224 VAL A CA 1 ATOM 848 C C . VAL A 1 108 ? 19.223 10.834 -8.072 1.00 36.86 ? 224 VAL A C 1 ATOM 849 O O . VAL A 1 108 ? 18.702 10.404 -7.046 1.00 36.77 ? 224 VAL A O 1 ATOM 850 C CB . VAL A 1 108 ? 20.491 12.994 -8.207 1.00 45.86 ? 224 VAL A CB 1 ATOM 851 C CG1 . VAL A 1 108 ? 21.107 12.580 -6.870 1.00 42.36 ? 224 VAL A CG1 1 ATOM 852 C CG2 . VAL A 1 108 ? 21.432 12.696 -9.378 1.00 54.32 ? 224 VAL A CG2 1 ATOM 853 N N . ILE A 1 109 ? 19.861 10.061 -8.933 1.00 33.87 ? 225 ILE A N 1 ATOM 854 C CA . ILE A 1 109 ? 20.022 8.643 -8.663 1.00 34.23 ? 225 ILE A CA 1 ATOM 855 C C . ILE A 1 109 ? 21.457 8.381 -8.236 1.00 32.47 ? 225 ILE A C 1 ATOM 856 O O . ILE A 1 109 ? 22.398 8.782 -8.919 1.00 36.91 ? 225 ILE A O 1 ATOM 857 C CB . ILE A 1 109 ? 19.670 7.819 -9.909 1.00 31.07 ? 225 ILE A CB 1 ATOM 858 C CG1 . ILE A 1 109 ? 18.200 8.056 -10.282 1.00 35.07 ? 225 ILE A CG1 1 ATOM 859 C CG2 . ILE A 1 109 ? 19.925 6.338 -9.666 1.00 31.76 ? 225 ILE A CG2 1 ATOM 860 C CD1 . ILE A 1 109 ? 17.762 7.354 -11.599 1.00 30.37 ? 225 ILE A CD1 1 ATOM 861 N N . LEU A 1 110 ? 21.630 7.750 -7.086 1.00 31.62 ? 226 LEU A N 1 ATOM 862 C CA . LEU A 1 110 ? 22.959 7.321 -6.688 1.00 36.39 ? 226 LEU A CA 1 ATOM 863 C C . LEU A 1 110 ? 23.182 5.917 -7.216 1.00 33.15 ? 226 LEU A C 1 ATOM 864 O O . LEU A 1 110 ? 22.276 5.086 -7.191 1.00 33.63 ? 226 LEU A O 1 ATOM 865 C CB . LEU A 1 110 ? 23.154 7.394 -5.174 1.00 32.68 ? 226 LEU A CB 1 ATOM 866 C CG . LEU A 1 110 ? 22.941 8.798 -4.597 1.00 36.34 ? 226 LEU A CG 1 ATOM 867 C CD1 . LEU A 1 110 ? 23.440 8.878 -3.153 1.00 36.42 ? 226 LEU A CD1 1 ATOM 868 C CD2 . LEU A 1 110 ? 23.616 9.864 -5.481 1.00 35.80 ? 226 LEU A CD2 1 ATOM 869 N N . LYS A 1 111 ? 24.382 5.669 -7.726 1.00 33.32 ? 227 LYS A N 1 ATOM 870 C CA . LYS A 1 111 ? 24.701 4.385 -8.330 1.00 30.86 ? 227 LYS A CA 1 ATOM 871 C C . LYS A 1 111 ? 25.875 3.790 -7.573 1.00 33.62 ? 227 LYS A C 1 ATOM 872 O O . LYS A 1 111 ? 26.884 4.455 -7.351 1.00 37.23 ? 227 LYS A O 1 ATOM 873 C CB . LYS A 1 111 ? 25.075 4.584 -9.805 1.00 35.20 ? 227 LYS A CB 1 ATOM 874 C CG . LYS A 1 111 ? 25.342 3.304 -10.563 1.00 36.19 ? 227 LYS A CG 1 ATOM 875 C CD . LYS A 1 111 ? 25.848 3.590 -11.969 1.00 41.41 ? 227 LYS A CD 1 ATOM 876 C CE . LYS A 1 111 ? 26.051 2.292 -12.750 1.00 43.52 ? 227 LYS A CE 1 ATOM 877 N NZ . LYS A 1 111 ? 26.749 2.529 -14.046 1.00 42.05 ? 227 LYS A NZ 1 ATOM 878 N N . CYS A 1 112 ? 25.744 2.541 -7.162 1.00 30.77 ? 228 CYS A N 1 ATOM 879 C CA . CYS A 1 112 ? 26.828 1.884 -6.457 1.00 34.03 ? 228 CYS A CA 1 ATOM 880 C C . CYS A 1 112 ? 27.744 1.219 -7.457 1.00 29.99 ? 228 CYS A C 1 ATOM 881 O O . CYS A 1 112 ? 27.331 0.306 -8.166 1.00 33.65 ? 228 CYS A O 1 ATOM 882 C CB . CYS A 1 112 ? 26.294 0.817 -5.496 1.00 34.09 ? 228 CYS A CB 1 ATOM 883 S SG . CYS A 1 112 ? 27.619 -0.063 -4.671 1.00 41.48 ? 228 CYS A SG 1 ATOM 884 N N . ASN A 1 113 ? 29.002 1.635 -7.473 1.00 36.31 ? 229 ASN A N 1 ATOM 885 C CA . ASN A 1 113 ? 29.938 1.073 -8.420 1.00 41.69 ? 229 ASN A CA 1 ATOM 886 C C . ASN A 1 113 ? 30.889 0.053 -7.814 1.00 40.38 ? 229 ASN A C 1 ATOM 887 O O . ASN A 1 113 ? 31.832 -0.377 -8.472 1.00 44.67 ? 229 ASN A O 1 ATOM 888 C CB . ASN A 1 113 ? 30.669 2.191 -9.159 1.00 43.22 ? 229 ASN A CB 1 ATOM 889 C CG . ASN A 1 113 ? 29.704 3.150 -9.823 1.00 41.44 ? 229 ASN A CG 1 ATOM 890 O OD1 . ASN A 1 113 ? 29.040 2.794 -10.791 1.00 44.92 ? 229 ASN A OD1 1 ATOM 891 N ND2 . ASN A 1 113 ? 29.592 4.361 -9.283 1.00 39.91 ? 229 ASN A ND2 1 ATOM 892 N N . ASP A 1 114 ? 30.632 -0.353 -6.570 1.00 38.99 ? 230 ASP A N 1 ATOM 893 C CA . ASP A 1 114 ? 31.412 -1.438 -5.966 1.00 42.78 ? 230 ASP A CA 1 ATOM 894 C C . ASP A 1 114 ? 31.098 -2.718 -6.740 1.00 46.26 ? 230 ASP A C 1 ATOM 895 O O . ASP A 1 114 ? 29.952 -3.152 -6.778 1.00 39.08 ? 230 ASP A O 1 ATOM 896 C CB . ASP A 1 114 ? 31.066 -1.612 -4.484 1.00 46.15 ? 230 ASP A CB 1 ATOM 897 C CG . ASP A 1 114 ? 31.584 -0.469 -3.614 1.00 50.26 ? 230 ASP A CG 1 ATOM 898 O OD1 . ASP A 1 114 ? 32.061 0.542 -4.166 1.00 49.56 ? 230 ASP A OD1 1 ATOM 899 O OD2 . ASP A 1 114 ? 31.496 -0.581 -2.367 1.00 52.50 ? 230 ASP A OD2 1 ATOM 900 N N . LYS A 1 115 ? 32.099 -3.316 -7.375 1.00 49.80 ? 231 LYS A N 1 ATOM 901 C CA . LYS A 1 115 ? 31.818 -4.403 -8.314 1.00 53.54 ? 231 LYS A CA 1 ATOM 902 C C . LYS A 1 115 ? 31.176 -5.618 -7.658 1.00 53.16 ? 231 LYS A C 1 ATOM 903 O O . LYS A 1 115 ? 30.345 -6.296 -8.271 1.00 56.85 ? 231 LYS A O 1 ATOM 904 C CB . LYS A 1 115 ? 33.067 -4.824 -9.095 1.00 55.96 ? 231 LYS A CB 1 ATOM 905 C CG . LYS A 1 115 ? 33.378 -3.944 -10.290 1.00 59.96 ? 231 LYS A CG 1 ATOM 906 C CD . LYS A 1 115 ? 34.520 -4.534 -11.112 1.00 68.84 ? 231 LYS A CD 1 ATOM 907 C CE . LYS A 1 115 ? 34.866 -3.649 -12.302 1.00 74.42 ? 231 LYS A CE 1 ATOM 908 N NZ . LYS A 1 115 ? 35.454 -2.348 -11.863 1.00 77.62 ? 231 LYS A NZ 1 ATOM 909 N N . ASN A 1 116 ? 31.551 -5.891 -6.414 1.00 44.20 ? 232 ASN A N 1 ATOM 910 C CA . ASN A 1 116 ? 31.005 -7.048 -5.705 1.00 43.66 ? 232 ASN A CA 1 ATOM 911 C C . ASN A 1 116 ? 29.916 -6.697 -4.693 1.00 40.81 ? 232 ASN A C 1 ATOM 912 O O . ASN A 1 116 ? 29.638 -7.473 -3.783 1.00 41.27 ? 232 ASN A O 1 ATOM 913 C CB . ASN A 1 116 ? 32.125 -7.854 -5.039 1.00 52.02 ? 232 ASN A CB 1 ATOM 914 C CG . ASN A 1 116 ? 32.974 -8.607 -6.047 1.00 55.69 ? 232 ASN A CG 1 ATOM 915 O OD1 . ASN A 1 116 ? 32.463 -9.129 -7.044 1.00 52.36 ? 232 ASN A OD1 1 ATOM 916 N ND2 . ASN A 1 116 ? 34.279 -8.657 -5.802 1.00 57.93 ? 232 ASN A ND2 1 ATOM 917 N N . PHE A 1 117 ? 29.294 -5.533 -4.862 1.00 41.33 ? 233 PHE A N 1 ATOM 918 C CA . PHE A 1 117 ? 28.205 -5.119 -3.979 1.00 43.84 ? 233 PHE A CA 1 ATOM 919 C C . PHE A 1 117 ? 27.062 -6.140 -3.995 1.00 42.66 ? 233 PHE A C 1 ATOM 920 O O . PHE A 1 117 ? 26.555 -6.493 -5.062 1.00 37.40 ? 233 PHE A O 1 ATOM 921 C CB . PHE A 1 117 ? 27.679 -3.728 -4.365 1.00 38.78 ? 233 PHE A CB 1 ATOM 922 C CG . PHE A 1 117 ? 26.630 -3.207 -3.427 1.00 43.35 ? 233 PHE A CG 1 ATOM 923 C CD1 . PHE A 1 117 ? 26.872 -3.160 -2.064 1.00 50.59 ? 233 PHE A CD1 1 ATOM 924 C CD2 . PHE A 1 117 ? 25.393 -2.786 -3.900 1.00 45.48 ? 233 PHE A CD2 1 ATOM 925 C CE1 . PHE A 1 117 ? 25.908 -2.694 -1.183 1.00 51.71 ? 233 PHE A CE1 1 ATOM 926 C CE2 . PHE A 1 117 ? 24.419 -2.313 -3.024 1.00 40.51 ? 233 PHE A CE2 1 ATOM 927 C CZ . PHE A 1 117 ? 24.683 -2.271 -1.665 1.00 48.89 ? 233 PHE A CZ 1 ATOM 928 N N . ASN A 1 118 ? 26.654 -6.617 -2.821 1.00 41.27 ? 234 ASN A N 1 ATOM 929 C CA . ASN A 1 118 ? 25.614 -7.645 -2.777 1.00 40.56 ? 234 ASN A CA 1 ATOM 930 C C . ASN A 1 118 ? 24.179 -7.107 -2.821 1.00 40.20 ? 234 ASN A C 1 ATOM 931 O O . ASN A 1 118 ? 23.224 -7.885 -2.879 1.00 39.11 ? 234 ASN A O 1 ATOM 932 C CB . ASN A 1 118 ? 25.832 -8.629 -1.608 1.00 43.41 ? 234 ASN A CB 1 ATOM 933 C CG . ASN A 1 118 ? 25.584 -8.009 -0.240 1.00 51.49 ? 234 ASN A CG 1 ATOM 934 O OD1 . ASN A 1 118 ? 24.825 -7.050 -0.096 1.00 44.63 ? 234 ASN A OD1 1 ATOM 935 N ND2 . ASN A 1 118 ? 26.219 -8.576 0.780 1.00 63.44 ? 234 ASN A ND2 1 ATOM 936 N N . GLY A 1 119 ? 24.031 -5.781 -2.801 1.00 34.03 ? 235 GLY A N 1 ATOM 937 C CA . GLY A 1 119 ? 22.710 -5.169 -2.860 1.00 34.62 ? 235 GLY A CA 1 ATOM 938 C C . GLY A 1 119 ? 22.192 -4.527 -1.567 1.00 38.26 ? 235 GLY A C 1 ATOM 939 O O . GLY A 1 119 ? 21.243 -3.750 -1.600 1.00 38.01 ? 235 GLY A O 1 ATOM 940 N N . THR A 1 120 ? 22.787 -4.848 -0.423 1.00 34.64 ? 236 THR A N 1 ATOM 941 C CA . THR A 1 120 ? 22.432 -4.155 0.816 1.00 37.22 ? 236 THR A CA 1 ATOM 942 C C . THR A 1 120 ? 23.665 -3.835 1.643 1.00 40.44 ? 236 THR A C 1 ATOM 943 O O . THR A 1 120 ? 24.545 -4.672 1.807 1.00 47.67 ? 236 THR A O 1 ATOM 944 C CB . THR A 1 120 ? 21.500 -4.995 1.695 1.00 44.04 ? 236 THR A CB 1 ATOM 945 O OG1 . THR A 1 120 ? 22.292 -5.907 2.453 1.00 52.52 ? 236 THR A OG1 1 ATOM 946 C CG2 . THR A 1 120 ? 20.515 -5.779 0.841 1.00 38.59 ? 236 THR A CG2 1 ATOM 947 N N . GLY A 1 121 ? 23.718 -2.634 2.199 1.00 39.91 ? 237 GLY A N 1 ATOM 948 C CA . GLY A 1 121 ? 24.870 -2.253 2.987 1.00 34.51 ? 237 GLY A CA 1 ATOM 949 C C . GLY A 1 121 ? 25.590 -1.085 2.349 1.00 41.19 ? 237 GLY A C 1 ATOM 950 O O . GLY A 1 121 ? 25.083 -0.463 1.408 1.00 37.23 ? 237 GLY A O 1 ATOM 951 N N . PRO A 1 122 ? 26.783 -0.770 2.862 1.00 40.34 ? 238 PRO A N 1 ATOM 952 C CA . PRO A 1 122 ? 27.500 0.415 2.394 1.00 35.98 ? 238 PRO A CA 1 ATOM 953 C C . PRO A 1 122 ? 28.221 0.173 1.071 1.00 43.74 ? 238 PRO A C 1 ATOM 954 O O . PRO A 1 122 ? 28.681 -0.930 0.781 1.00 43.01 ? 238 PRO A O 1 ATOM 955 C CB . PRO A 1 122 ? 28.498 0.684 3.533 1.00 38.07 ? 238 PRO A CB 1 ATOM 956 C CG . PRO A 1 122 ? 28.775 -0.651 4.098 1.00 42.76 ? 238 PRO A CG 1 ATOM 957 C CD . PRO A 1 122 ? 27.516 -1.482 3.922 1.00 44.33 ? 238 PRO A CD 1 ATOM 958 N N . CYS A 1 123 ? 28.288 1.227 0.271 1.00 42.94 ? 239 CYS A N 1 ATOM 959 C CA . CYS A 1 123 ? 28.966 1.215 -1.006 1.00 34.69 ? 239 CYS A CA 1 ATOM 960 C C . CYS A 1 123 ? 30.000 2.319 -0.942 1.00 40.47 ? 239 CYS A C 1 ATOM 961 O O . CYS A 1 123 ? 29.669 3.459 -0.611 1.00 43.40 ? 239 CYS A O 1 ATOM 962 C CB . CYS A 1 123 ? 27.963 1.516 -2.118 1.00 32.91 ? 239 CYS A CB 1 ATOM 963 S SG . CYS A 1 123 ? 28.672 1.499 -3.791 1.00 43.54 ? 239 CYS A SG 1 ATOM 964 N N . LYS A 1 124 ? 31.251 1.989 -1.243 1.00 43.20 ? 240 LYS A N 1 ATOM 965 C CA . LYS A 1 124 ? 32.336 2.961 -1.095 1.00 49.71 ? 240 LYS A CA 1 ATOM 966 C C . LYS A 1 124 ? 32.520 3.818 -2.356 1.00 48.55 ? 240 LYS A C 1 ATOM 967 O O . LYS A 1 124 ? 32.948 4.967 -2.267 1.00 50.72 ? 240 LYS A O 1 ATOM 968 C CB . LYS A 1 124 ? 33.655 2.271 -0.715 1.00 50.90 ? 240 LYS A CB 1 ATOM 969 C CG . LYS A 1 124 ? 33.577 1.365 0.515 1.00 57.25 ? 240 LYS A CG 1 ATOM 970 C CD . LYS A 1 124 ? 33.187 2.134 1.779 1.00 67.92 ? 240 LYS A CD 1 ATOM 971 C CE . LYS A 1 124 ? 34.356 2.943 2.346 1.00 74.47 ? 240 LYS A CE 1 ATOM 972 N NZ . LYS A 1 124 ? 34.060 3.525 3.696 1.00 74.21 ? 240 LYS A NZ 1 ATOM 973 N N . ASN A 1 125 ? 32.180 3.255 -3.515 1.00 41.51 ? 241 ASN A N 1 ATOM 974 C CA . ASN A 1 125 ? 32.394 3.913 -4.807 1.00 39.64 ? 241 ASN A CA 1 ATOM 975 C C . ASN A 1 125 ? 31.054 4.304 -5.437 1.00 35.41 ? 241 ASN A C 1 ATOM 976 O O . ASN A 1 125 ? 30.462 3.538 -6.193 1.00 39.68 ? 241 ASN A O 1 ATOM 977 C CB . ASN A 1 125 ? 33.195 2.974 -5.723 1.00 50.48 ? 241 ASN A CB 1 ATOM 978 C CG . ASN A 1 125 ? 33.546 3.594 -7.071 1.00 64.26 ? 241 ASN A CG 1 ATOM 979 O OD1 . ASN A 1 125 ? 33.248 4.757 -7.334 1.00 60.58 ? 241 ASN A OD1 1 ATOM 980 N ND2 . ASN A 1 125 ? 34.194 2.802 -7.932 1.00 83.23 ? 241 ASN A ND2 1 ATOM 981 N N . VAL A 1 126 ? 30.572 5.495 -5.101 1.00 45.60 ? 242 VAL A N 1 ATOM 982 C CA . VAL A 1 126 ? 29.230 5.914 -5.490 1.00 42.00 ? 242 VAL A CA 1 ATOM 983 C C . VAL A 1 126 ? 29.301 7.046 -6.495 1.00 40.31 ? 242 VAL A C 1 ATOM 984 O O . VAL A 1 126 ? 30.147 7.932 -6.375 1.00 43.65 ? 242 VAL A O 1 ATOM 985 C CB . VAL A 1 126 ? 28.439 6.464 -4.272 1.00 38.48 ? 242 VAL A CB 1 ATOM 986 C CG1 . VAL A 1 126 ? 26.993 6.721 -4.663 1.00 34.77 ? 242 VAL A CG1 1 ATOM 987 C CG2 . VAL A 1 126 ? 28.532 5.516 -3.092 1.00 45.89 ? 242 VAL A CG2 1 ATOM 988 N N . SER A 1 127 ? 28.398 7.030 -7.467 1.00 37.06 ? 243 SER A N 1 ATOM 989 C CA . SER A 1 127 ? 28.279 8.139 -8.401 1.00 41.09 ? 243 SER A CA 1 ATOM 990 C C . SER A 1 127 ? 26.815 8.575 -8.495 1.00 41.07 ? 243 SER A C 1 ATOM 991 O O . SER A 1 127 ? 25.915 7.873 -8.032 1.00 38.72 ? 243 SER A O 1 ATOM 992 C CB . SER A 1 127 ? 28.852 7.759 -9.785 1.00 38.79 ? 243 SER A CB 1 ATOM 993 O OG . SER A 1 127 ? 28.190 6.629 -10.330 1.00 42.41 ? 243 SER A OG 1 ATOM 994 N N . SER A 1 128 ? 26.578 9.753 -9.058 1.00 40.54 ? 244 SER A N 1 ATOM 995 C CA . SER A 1 128 ? 25.208 10.209 -9.277 1.00 38.54 ? 244 SER A CA 1 ATOM 996 C C . SER A 1 128 ? 24.932 10.306 -10.774 1.00 43.51 ? 244 SER A C 1 ATOM 997 O O . SER A 1 128 ? 25.816 10.649 -11.559 1.00 45.68 ? 244 SER A O 1 ATOM 998 C CB . SER A 1 128 ? 24.940 11.548 -8.581 1.00 41.01 ? 244 SER A CB 1 ATOM 999 O OG . SER A 1 128 ? 25.760 12.572 -9.115 1.00 49.13 ? 244 SER A OG 1 ATOM 1000 N N . VAL A 1 129 ? 23.703 9.981 -11.158 1.00 40.29 ? 245 VAL A N 1 ATOM 1001 C CA . VAL A 1 129 ? 23.292 9.981 -12.555 1.00 38.46 ? 245 VAL A CA 1 ATOM 1002 C C . VAL A 1 129 ? 21.846 10.436 -12.619 1.00 39.51 ? 245 VAL A C 1 ATOM 1003 O O . VAL A 1 129 ? 21.130 10.365 -11.623 1.00 40.87 ? 245 VAL A O 1 ATOM 1004 C CB . VAL A 1 129 ? 23.362 8.572 -13.146 1.00 41.87 ? 245 VAL A CB 1 ATOM 1005 C CG1 . VAL A 1 129 ? 24.780 8.048 -13.098 1.00 45.69 ? 245 VAL A CG1 1 ATOM 1006 C CG2 . VAL A 1 129 ? 22.424 7.636 -12.388 1.00 36.08 ? 245 VAL A CG2 1 ATOM 1007 N N . GLN A 1 130 ? 21.416 10.900 -13.787 1.00 37.80 ? 246 GLN A N 1 ATOM 1008 C CA . GLN A 1 130 ? 20.032 11.319 -13.983 1.00 42.11 ? 246 GLN A CA 1 ATOM 1009 C C . GLN A 1 130 ? 19.127 10.128 -14.305 1.00 39.28 ? 246 GLN A C 1 ATOM 1010 O O . GLN A 1 130 ? 17.941 10.126 -13.961 1.00 37.22 ? 246 GLN A O 1 ATOM 1011 C CB . GLN A 1 130 ? 19.943 12.366 -15.096 1.00 48.45 ? 246 GLN A CB 1 ATOM 1012 C CG . GLN A 1 130 ? 20.713 13.643 -14.774 1.00 71.81 ? 246 GLN A CG 1 ATOM 1013 C CD . GLN A 1 130 ? 20.828 14.588 -15.959 1.00 90.06 ? 246 GLN A CD 1 ATOM 1014 O OE1 . GLN A 1 130 ? 20.838 14.159 -17.118 1.00 97.22 ? 246 GLN A OE1 1 ATOM 1015 N NE2 . GLN A 1 130 ? 20.914 15.886 -15.671 1.00 93.93 ? 246 GLN A NE2 1 ATOM 1016 N N . CYS A 1 131 ? 19.700 9.120 -14.953 1.00 35.84 ? 247 CYS A N 1 ATOM 1017 C CA . CYS A 1 131 ? 18.944 7.952 -15.399 1.00 37.77 ? 247 CYS A CA 1 ATOM 1018 C C . CYS A 1 131 ? 19.721 6.675 -15.152 1.00 32.74 ? 247 CYS A C 1 ATOM 1019 O O . CYS A 1 131 ? 20.949 6.680 -15.161 1.00 36.82 ? 247 CYS A O 1 ATOM 1020 C CB . CYS A 1 131 ? 18.670 8.035 -16.910 1.00 33.83 ? 247 CYS A CB 1 ATOM 1021 S SG . CYS A 1 131 ? 17.714 9.489 -17.465 1.00 42.08 ? 247 CYS A SG 1 ATOM 1022 N N . THR A 1 132 ? 19.002 5.571 -14.990 1.00 28.08 ? 248 THR A N 1 ATOM 1023 C CA . THR A 1 132 ? 19.644 4.268 -14.927 1.00 33.63 ? 248 THR A CA 1 ATOM 1024 C C . THR A 1 132 ? 20.152 3.931 -16.317 1.00 35.83 ? 248 THR A C 1 ATOM 1025 O O . THR A 1 132 ? 19.857 4.642 -17.280 1.00 34.93 ? 248 THR A O 1 ATOM 1026 C CB . THR A 1 132 ? 18.657 3.152 -14.534 1.00 29.81 ? 248 THR A CB 1 ATOM 1027 O OG1 . THR A 1 132 ? 17.601 3.084 -15.511 1.00 31.68 ? 248 THR A OG1 1 ATOM 1028 C CG2 . THR A 1 132 ? 18.078 3.397 -13.149 1.00 32.84 ? 248 THR A CG2 1 ATOM 1029 N N . HIS A 1 133 ? 20.889 2.826 -16.419 1.00 35.24 ? 249 HIS A N 1 ATOM 1030 C CA . HIS A 1 133 ? 21.222 2.255 -17.717 1.00 37.16 ? 249 HIS A CA 1 ATOM 1031 C C . HIS A 1 133 ? 19.921 1.766 -18.318 1.00 32.27 ? 249 HIS A C 1 ATOM 1032 O O . HIS A 1 133 ? 18.900 1.734 -17.634 1.00 31.85 ? 249 HIS A O 1 ATOM 1033 C CB . HIS A 1 133 ? 22.220 1.102 -17.576 1.00 33.63 ? 249 HIS A CB 1 ATOM 1034 C CG . HIS A 1 133 ? 21.673 -0.094 -16.866 1.00 34.19 ? 249 HIS A CG 1 ATOM 1035 N ND1 . HIS A 1 133 ? 21.503 -0.136 -15.498 1.00 32.38 ? 249 HIS A ND1 1 ATOM 1036 C CD2 . HIS A 1 133 ? 21.256 -1.296 -17.335 1.00 30.92 ? 249 HIS A CD2 1 ATOM 1037 C CE1 . HIS A 1 133 ? 21.004 -1.310 -15.153 1.00 30.69 ? 249 HIS A CE1 1 ATOM 1038 N NE2 . HIS A 1 133 ? 20.851 -2.033 -16.249 1.00 31.99 ? 249 HIS A NE2 1 ATOM 1039 N N . GLY A 1 134 ? 19.941 1.434 -19.607 1.00 33.77 ? 250 GLY A N 1 ATOM 1040 C CA . GLY A 1 134 ? 18.736 0.982 -20.288 1.00 31.10 ? 250 GLY A CA 1 ATOM 1041 C C . GLY A 1 134 ? 18.438 -0.454 -19.910 1.00 30.17 ? 250 GLY A C 1 ATOM 1042 O O . GLY A 1 134 ? 19.226 -1.344 -20.190 1.00 32.91 ? 250 GLY A O 1 ATOM 1043 N N . ILE A 1 135 ? 17.300 -0.671 -19.266 1.00 26.44 ? 251 ILE A N 1 ATOM 1044 C CA . ILE A 1 135 ? 16.928 -1.986 -18.770 1.00 26.30 ? 251 ILE A CA 1 ATOM 1045 C C . ILE A 1 135 ? 15.815 -2.546 -19.655 1.00 31.85 ? 251 ILE A C 1 ATOM 1046 O O . ILE A 1 135 ? 14.770 -1.920 -19.809 1.00 26.77 ? 251 ILE A O 1 ATOM 1047 C CB . ILE A 1 135 ? 16.432 -1.891 -17.305 1.00 29.62 ? 251 ILE A CB 1 ATOM 1048 C CG1 . ILE A 1 135 ? 17.530 -1.320 -16.399 1.00 33.04 ? 251 ILE A CG1 1 ATOM 1049 C CG2 . ILE A 1 135 ? 15.938 -3.247 -16.785 1.00 27.12 ? 251 ILE A CG2 1 ATOM 1050 C CD1 . ILE A 1 135 ? 17.022 -0.868 -15.027 1.00 35.39 ? 251 ILE A CD1 1 ATOM 1051 N N . LYS A 1 136 ? 16.046 -3.714 -20.256 1.00 28.87 ? 252 LYS A N 1 ATOM 1052 C CA . LYS A 1 136 ? 15.002 -4.356 -21.051 1.00 27.40 ? 252 LYS A CA 1 ATOM 1053 C C . LYS A 1 136 ? 14.033 -5.005 -20.074 1.00 23.18 ? 252 LYS A C 1 ATOM 1054 O O . LYS A 1 136 ? 14.462 -5.677 -19.141 1.00 28.57 ? 252 LYS A O 1 ATOM 1055 C CB . LYS A 1 136 ? 15.604 -5.410 -21.984 1.00 26.33 ? 252 LYS A CB 1 ATOM 1056 C CG . LYS A 1 136 ? 16.396 -4.824 -23.175 1.00 32.62 ? 252 LYS A CG 1 ATOM 1057 C CD . LYS A 1 136 ? 17.028 -5.989 -23.974 1.00 38.42 ? 252 LYS A CD 1 ATOM 1058 C CE . LYS A 1 136 ? 17.083 -5.714 -25.472 1.00 47.50 ? 252 LYS A CE 1 ATOM 1059 N NZ . LYS A 1 136 ? 17.658 -6.862 -26.289 1.00 48.01 ? 252 LYS A NZ 1 ATOM 1060 N N . PRO A 1 137 ? 12.721 -4.777 -20.255 1.00 26.70 ? 253 PRO A N 1 ATOM 1061 C CA . PRO A 1 137 ? 11.778 -5.365 -19.293 1.00 24.65 ? 253 PRO A CA 1 ATOM 1062 C C . PRO A 1 137 ? 11.431 -6.813 -19.643 1.00 30.92 ? 253 PRO A C 1 ATOM 1063 O O . PRO A 1 137 ? 10.294 -7.128 -20.017 1.00 29.62 ? 253 PRO A O 1 ATOM 1064 C CB . PRO A 1 137 ? 10.550 -4.487 -19.443 1.00 28.05 ? 253 PRO A CB 1 ATOM 1065 C CG . PRO A 1 137 ? 10.584 -4.105 -20.935 1.00 30.07 ? 253 PRO A CG 1 ATOM 1066 C CD . PRO A 1 137 ? 12.047 -3.927 -21.254 1.00 28.07 ? 253 PRO A CD 1 ATOM 1067 N N . VAL A 1 138 ? 12.416 -7.689 -19.516 1.00 29.33 ? 254 VAL A N 1 ATOM 1068 C CA . VAL A 1 138 ? 12.233 -9.068 -19.922 1.00 28.24 ? 254 VAL A CA 1 ATOM 1069 C C . VAL A 1 138 ? 11.511 -9.798 -18.810 1.00 28.32 ? 254 VAL A C 1 ATOM 1070 O O . VAL A 1 138 ? 12.019 -9.902 -17.689 1.00 29.63 ? 254 VAL A O 1 ATOM 1071 C CB . VAL A 1 138 ? 13.568 -9.770 -20.242 1.00 29.72 ? 254 VAL A CB 1 ATOM 1072 C CG1 . VAL A 1 138 ? 13.297 -11.157 -20.855 1.00 33.89 ? 254 VAL A CG1 1 ATOM 1073 C CG2 . VAL A 1 138 ? 14.418 -8.891 -21.189 1.00 30.55 ? 254 VAL A CG2 1 ATOM 1074 N N . VAL A 1 139 ? 10.320 -10.280 -19.130 1.00 29.83 ? 255 VAL A N 1 ATOM 1075 C CA . VAL A 1 139 ? 9.527 -11.032 -18.175 1.00 30.09 ? 255 VAL A CA 1 ATOM 1076 C C . VAL A 1 139 ? 9.839 -12.513 -18.331 1.00 29.01 ? 255 VAL A C 1 ATOM 1077 O O . VAL A 1 139 ? 9.637 -13.096 -19.400 1.00 28.88 ? 255 VAL A O 1 ATOM 1078 C CB . VAL A 1 139 ? 8.019 -10.758 -18.338 1.00 29.47 ? 255 VAL A CB 1 ATOM 1079 C CG1 . VAL A 1 139 ? 7.224 -11.551 -17.308 1.00 29.53 ? 255 VAL A CG1 1 ATOM 1080 C CG2 . VAL A 1 139 ? 7.743 -9.258 -18.169 1.00 29.35 ? 255 VAL A CG2 1 ATOM 1081 N N . SER A 1 140 ? 10.363 -13.117 -17.268 1.00 27.85 ? 256 SER A N 1 ATOM 1082 C CA . SER A 1 140 ? 10.665 -14.546 -17.281 1.00 25.98 ? 256 SER A CA 1 ATOM 1083 C C . SER A 1 140 ? 10.667 -15.107 -15.871 1.00 30.04 ? 256 SER A C 1 ATOM 1084 O O . SER A 1 140 ? 10.741 -14.373 -14.888 1.00 28.19 ? 256 SER A O 1 ATOM 1085 C CB . SER A 1 140 ? 12.046 -14.814 -17.875 1.00 30.15 ? 256 SER A CB 1 ATOM 1086 O OG . SER A 1 140 ? 13.050 -14.238 -17.059 1.00 35.31 ? 256 SER A OG 1 ATOM 1087 N N . THR A 1 141 ? 10.627 -16.430 -15.783 1.00 32.53 ? 257 THR A N 1 ATOM 1088 C CA . THR A 1 141 ? 10.798 -17.081 -14.498 1.00 29.64 ? 257 THR A CA 1 ATOM 1089 C C . THR A 1 141 ? 12.018 -17.970 -14.544 1.00 28.89 ? 257 THR A C 1 ATOM 1090 O O . THR A 1 141 ? 12.484 -18.313 -15.614 1.00 32.87 ? 257 THR A O 1 ATOM 1091 C CB . THR A 1 141 ? 9.588 -17.915 -14.147 1.00 30.16 ? 257 THR A CB 1 ATOM 1092 O OG1 . THR A 1 141 ? 9.412 -18.925 -15.147 1.00 28.82 ? 257 THR A OG1 1 ATOM 1093 C CG2 . THR A 1 141 ? 8.339 -17.033 -14.072 1.00 32.99 ? 257 THR A CG2 1 ATOM 1094 N N . GLN A 1 142 ? 12.535 -18.316 -13.365 1.00 28.10 ? 258 GLN A N 1 ATOM 1095 C CA . GLN A 1 142 ? 13.682 -19.213 -13.212 1.00 28.12 ? 258 GLN A CA 1 ATOM 1096 C C . GLN A 1 142 ? 15.010 -18.636 -13.688 1.00 32.11 ? 258 GLN A C 1 ATOM 1097 O O . GLN A 1 142 ? 15.974 -18.556 -12.918 1.00 33.46 ? 258 GLN A O 1 ATOM 1098 C CB . GLN A 1 142 ? 13.429 -20.560 -13.895 1.00 29.63 ? 258 GLN A CB 1 ATOM 1099 C CG . GLN A 1 142 ? 12.197 -21.274 -13.363 1.00 33.45 ? 258 GLN A CG 1 ATOM 1100 C CD . GLN A 1 142 ? 12.218 -22.769 -13.665 1.00 35.70 ? 258 GLN A CD 1 ATOM 1101 O OE1 . GLN A 1 142 ? 13.154 -23.280 -14.274 1.00 35.74 ? 258 GLN A OE1 1 ATOM 1102 N NE2 . GLN A 1 142 ? 11.175 -23.471 -13.238 1.00 33.56 ? 258 GLN A NE2 1 ATOM 1103 N N . LEU A 1 143 ? 15.071 -18.276 -14.960 1.00 29.53 ? 259 LEU A N 1 ATOM 1104 C CA . LEU A 1 143 ? 16.274 -17.696 -15.541 1.00 31.52 ? 259 LEU A CA 1 ATOM 1105 C C . LEU A 1 143 ? 16.037 -16.246 -15.911 1.00 33.16 ? 259 LEU A C 1 ATOM 1106 O O . LEU A 1 143 ? 15.006 -15.908 -16.504 1.00 33.12 ? 259 LEU A O 1 ATOM 1107 C CB . LEU A 1 143 ? 16.690 -18.449 -16.809 1.00 31.41 ? 259 LEU A CB 1 ATOM 1108 C CG . LEU A 1 143 ? 16.863 -19.960 -16.692 1.00 32.34 ? 259 LEU A CG 1 ATOM 1109 C CD1 . LEU A 1 143 ? 17.148 -20.533 -18.071 1.00 33.34 ? 259 LEU A CD1 1 ATOM 1110 C CD2 . LEU A 1 143 ? 17.990 -20.275 -15.692 1.00 34.82 ? 259 LEU A CD2 1 ATOM 1111 N N . LEU A 1 144 ? 17.003 -15.396 -15.577 1.00 27.81 ? 260 LEU A N 1 ATOM 1112 C CA . LEU A 1 144 ? 16.967 -13.997 -15.975 1.00 28.94 ? 260 LEU A CA 1 ATOM 1113 C C . LEU A 1 144 ? 17.689 -13.860 -17.311 1.00 33.93 ? 260 LEU A C 1 ATOM 1114 O O . LEU A 1 144 ? 18.828 -14.316 -17.458 1.00 31.86 ? 260 LEU A O 1 ATOM 1115 C CB . LEU A 1 144 ? 17.635 -13.105 -14.908 1.00 27.34 ? 260 LEU A CB 1 ATOM 1116 C CG . LEU A 1 144 ? 17.077 -13.215 -13.478 1.00 30.34 ? 260 LEU A CG 1 ATOM 1117 C CD1 . LEU A 1 144 ? 17.879 -12.361 -12.485 1.00 30.05 ? 260 LEU A CD1 1 ATOM 1118 C CD2 . LEU A 1 144 ? 15.612 -12.816 -13.470 1.00 35.15 ? 260 LEU A CD2 1 ATOM 1119 N N . LEU A 1 145 ? 17.027 -13.224 -18.277 1.00 32.83 ? 261 LEU A N 1 ATOM 1120 C CA . LEU A 1 145 ? 17.503 -13.192 -19.664 1.00 33.22 ? 261 LEU A CA 1 ATOM 1121 C C . LEU A 1 145 ? 17.837 -11.786 -20.128 1.00 32.01 ? 261 LEU A C 1 ATOM 1122 O O . LEU A 1 145 ? 17.155 -10.826 -19.773 1.00 32.25 ? 261 LEU A O 1 ATOM 1123 C CB . LEU A 1 145 ? 16.432 -13.742 -20.603 1.00 30.16 ? 261 LEU A CB 1 ATOM 1124 C CG . LEU A 1 145 ? 15.887 -15.130 -20.291 1.00 31.45 ? 261 LEU A CG 1 ATOM 1125 C CD1 . LEU A 1 145 ? 14.848 -15.544 -21.337 1.00 29.41 ? 261 LEU A CD1 1 ATOM 1126 C CD2 . LEU A 1 145 ? 17.030 -16.133 -20.202 1.00 31.17 ? 261 LEU A CD2 1 ATOM 1127 N N . ASN A 1 146 ? 18.887 -11.686 -20.934 1.00 30.49 ? 262 ASN A N 1 ATOM 1128 C CA . ASN A 1 146 ? 19.269 -10.449 -21.597 1.00 32.78 ? 262 ASN A CA 1 ATOM 1129 C C . ASN A 1 146 ? 19.502 -9.321 -20.609 1.00 34.19 ? 262 ASN A C 1 ATOM 1130 O O . ASN A 1 146 ? 19.243 -8.161 -20.920 1.00 33.47 ? 262 ASN A O 1 ATOM 1131 C CB . ASN A 1 146 ? 18.202 -10.015 -22.613 1.00 31.43 ? 262 ASN A CB 1 ATOM 1132 C CG . ASN A 1 146 ? 18.150 -10.923 -23.855 1.00 36.54 ? 262 ASN A CG 1 ATOM 1133 O OD1 . ASN A 1 146 ? 19.049 -11.735 -24.092 1.00 33.54 ? 262 ASN A OD1 1 ATOM 1134 N ND2 . ASN A 1 146 ? 17.082 -10.777 -24.646 1.00 33.20 ? 262 ASN A ND2 1 ATOM 1135 N N . GLY A 1 147 ? 19.990 -9.665 -19.425 1.00 32.64 ? 263 GLY A N 1 ATOM 1136 C CA . GLY A 1 147 ? 20.218 -8.672 -18.390 1.00 32.35 ? 263 GLY A CA 1 ATOM 1137 C C . GLY A 1 147 ? 21.664 -8.231 -18.368 1.00 36.54 ? 263 GLY A C 1 ATOM 1138 O O . GLY A 1 147 ? 22.438 -8.568 -19.264 1.00 35.44 ? 263 GLY A O 1 ATOM 1139 N N . SER A 1 148 ? 22.030 -7.470 -17.339 1.00 34.20 ? 264 SER A N 1 ATOM 1140 C CA . SER A 1 148 ? 23.416 -7.067 -17.132 1.00 35.74 ? 264 SER A CA 1 ATOM 1141 C C . SER A 1 148 ? 24.119 -8.131 -16.319 1.00 36.28 ? 264 SER A C 1 ATOM 1142 O O . SER A 1 148 ? 23.489 -8.809 -15.511 1.00 39.27 ? 264 SER A O 1 ATOM 1143 C CB . SER A 1 148 ? 23.483 -5.732 -16.397 1.00 39.41 ? 264 SER A CB 1 ATOM 1144 O OG . SER A 1 148 ? 22.625 -4.806 -17.033 1.00 41.82 ? 264 SER A OG 1 ATOM 1145 N N . LEU A 1 149 ? 25.418 -8.281 -16.549 1.00 33.96 ? 265 LEU A N 1 ATOM 1146 C CA . LEU A 1 149 ? 26.227 -9.260 -15.833 1.00 40.81 ? 265 LEU A CA 1 ATOM 1147 C C . LEU A 1 149 ? 26.960 -8.597 -14.681 1.00 43.94 ? 265 LEU A C 1 ATOM 1148 O O . LEU A 1 149 ? 27.271 -7.402 -14.734 1.00 39.15 ? 265 LEU A O 1 ATOM 1149 C CB . LEU A 1 149 ? 27.268 -9.873 -16.771 1.00 40.75 ? 265 LEU A CB 1 ATOM 1150 C CG . LEU A 1 149 ? 26.703 -10.666 -17.949 1.00 42.43 ? 265 LEU A CG 1 ATOM 1151 C CD1 . LEU A 1 149 ? 27.752 -10.855 -19.032 1.00 46.56 ? 265 LEU A CD1 1 ATOM 1152 C CD2 . LEU A 1 149 ? 26.172 -12.003 -17.445 1.00 39.10 ? 265 LEU A CD2 1 ATOM 1153 N N . ALA A 1 150 ? 27.239 -9.391 -13.652 1.00 40.07 ? 266 ALA A N 1 ATOM 1154 C CA . ALA A 1 150 ? 28.109 -8.972 -12.568 1.00 38.08 ? 266 ALA A CA 1 ATOM 1155 C C . ALA A 1 150 ? 29.476 -8.750 -13.188 1.00 43.74 ? 266 ALA A C 1 ATOM 1156 O O . ALA A 1 150 ? 29.905 -9.515 -14.057 1.00 41.77 ? 266 ALA A O 1 ATOM 1157 C CB . ALA A 1 150 ? 28.170 -10.049 -11.501 1.00 39.85 ? 266 ALA A CB 1 ATOM 1158 N N . GLU A 1 151 ? 30.162 -7.703 -12.750 1.00 48.75 ? 267 GLU A N 1 ATOM 1159 C CA . GLU A 1 151 ? 31.386 -7.289 -13.419 1.00 54.25 ? 267 GLU A CA 1 ATOM 1160 C C . GLU A 1 151 ? 32.613 -8.030 -12.911 1.00 55.05 ? 267 GLU A C 1 ATOM 1161 O O . GLU A 1 151 ? 33.663 -7.992 -13.548 1.00 60.21 ? 267 GLU A O 1 ATOM 1162 C CB . GLU A 1 151 ? 31.574 -5.776 -13.304 1.00 60.05 ? 267 GLU A CB 1 ATOM 1163 C CG . GLU A 1 151 ? 30.436 -4.986 -13.927 1.00 67.23 ? 267 GLU A CG 1 ATOM 1164 C CD . GLU A 1 151 ? 30.691 -3.494 -13.947 1.00 77.14 ? 267 GLU A CD 1 ATOM 1165 O OE1 . GLU A 1 151 ? 31.813 -3.072 -13.600 1.00 79.93 ? 267 GLU A OE1 1 ATOM 1166 O OE2 . GLU A 1 151 ? 29.763 -2.743 -14.313 1.00 82.06 ? 267 GLU A OE2 1 ATOM 1167 N N . GLU A 1 152 ? 32.477 -8.712 -11.775 1.00 49.08 ? 268 GLU A N 1 ATOM 1168 C CA . GLU A 1 152 ? 33.596 -9.449 -11.200 1.00 45.13 ? 268 GLU A CA 1 ATOM 1169 C C . GLU A 1 152 ? 33.191 -10.867 -10.808 1.00 46.00 ? 268 GLU A C 1 ATOM 1170 O O . GLU A 1 152 ? 33.125 -11.745 -11.657 1.00 47.62 ? 268 GLU A O 1 ATOM 1171 C CB . GLU A 1 152 ? 34.187 -8.687 -10.012 1.00 50.00 ? 268 GLU A CB 1 ATOM 1172 C CG . GLU A 1 152 ? 35.623 -9.058 -9.692 1.00 59.71 ? 268 GLU A CG 1 ATOM 1173 C CD . GLU A 1 152 ? 36.236 -8.147 -8.645 1.00 69.06 ? 268 GLU A CD 1 ATOM 1174 O OE1 . GLU A 1 152 ? 36.605 -8.651 -7.561 1.00 69.51 ? 268 GLU A OE1 1 ATOM 1175 O OE2 . GLU A 1 152 ? 36.349 -6.926 -8.909 1.00 70.93 ? 268 GLU A OE2 1 ATOM 1176 N N . GLU A 1 153 ? 32.914 -11.090 -9.527 1.00 47.70 ? 269 GLU A N 1 ATOM 1177 C CA . GLU A 1 153 ? 32.458 -12.396 -9.056 1.00 51.29 ? 269 GLU A CA 1 ATOM 1178 C C . GLU A 1 153 ? 30.961 -12.624 -9.287 1.00 45.21 ? 269 GLU A C 1 ATOM 1179 O O . GLU A 1 153 ? 30.184 -11.675 -9.390 1.00 42.67 ? 269 GLU A O 1 ATOM 1180 C CB . GLU A 1 153 ? 32.758 -12.566 -7.566 1.00 55.58 ? 269 GLU A CB 1 ATOM 1181 C CG . GLU A 1 153 ? 34.225 -12.762 -7.232 1.00 70.55 ? 269 GLU A CG 1 ATOM 1182 C CD . GLU A 1 153 ? 34.445 -12.961 -5.749 1.00 84.16 ? 269 GLU A CD 1 ATOM 1183 O OE1 . GLU A 1 153 ? 33.520 -12.641 -4.969 1.00 89.51 ? 269 GLU A OE1 1 ATOM 1184 O OE2 . GLU A 1 153 ? 35.535 -13.436 -5.362 1.00 87.72 ? 269 GLU A OE2 1 ATOM 1185 N N . ILE A 1 154 ? 30.568 -13.894 -9.367 1.00 42.94 ? 270 ILE A N 1 ATOM 1186 C CA . ILE A 1 154 ? 29.161 -14.253 -9.246 1.00 43.03 ? 270 ILE A CA 1 ATOM 1187 C C . ILE A 1 154 ? 28.652 -13.747 -7.891 1.00 42.89 ? 270 ILE A C 1 ATOM 1188 O O . ILE A 1 154 ? 29.305 -13.936 -6.866 1.00 43.70 ? 270 ILE A O 1 ATOM 1189 C CB . ILE A 1 154 ? 28.961 -15.771 -9.340 1.00 43.10 ? 270 ILE A CB 1 ATOM 1190 C CG1 . ILE A 1 154 ? 29.194 -16.245 -10.779 1.00 39.68 ? 270 ILE A CG1 1 ATOM 1191 C CG2 . ILE A 1 154 ? 27.556 -16.159 -8.876 1.00 39.63 ? 270 ILE A CG2 1 ATOM 1192 C CD1 . ILE A 1 154 ? 29.275 -17.755 -10.925 1.00 40.38 ? 270 ILE A CD1 1 ATOM 1193 N N . ILE A 1 155 ? 27.506 -13.076 -7.890 1.00 39.61 ? 271 ILE A N 1 ATOM 1194 C CA . ILE A 1 155 ? 26.965 -12.532 -6.654 1.00 37.87 ? 271 ILE A CA 1 ATOM 1195 C C . ILE A 1 155 ? 25.670 -13.223 -6.238 1.00 36.94 ? 271 ILE A C 1 ATOM 1196 O O . ILE A 1 155 ? 24.746 -13.380 -7.039 1.00 38.47 ? 271 ILE A O 1 ATOM 1197 C CB . ILE A 1 155 ? 26.696 -11.017 -6.768 1.00 39.48 ? 271 ILE A CB 1 ATOM 1198 C CG1 . ILE A 1 155 ? 27.914 -10.289 -7.334 1.00 39.35 ? 271 ILE A CG1 1 ATOM 1199 C CG2 . ILE A 1 155 ? 26.255 -10.440 -5.403 1.00 37.98 ? 271 ILE A CG2 1 ATOM 1200 C CD1 . ILE A 1 155 ? 29.143 -10.391 -6.475 1.00 41.61 ? 271 ILE A CD1 1 ATOM 1201 N N . ILE A 1 156 ? 25.610 -13.621 -4.974 1.00 36.70 ? 272 ILE A N 1 ATOM 1202 C CA . ILE A 1 156 ? 24.388 -14.158 -4.392 1.00 37.41 ? 272 ILE A CA 1 ATOM 1203 C C . ILE A 1 156 ? 23.674 -13.044 -3.656 1.00 37.80 ? 272 ILE A C 1 ATOM 1204 O O . ILE A 1 156 ? 24.266 -12.390 -2.801 1.00 38.01 ? 272 ILE A O 1 ATOM 1205 C CB . ILE A 1 156 ? 24.705 -15.285 -3.398 1.00 41.54 ? 272 ILE A CB 1 ATOM 1206 C CG1 . ILE A 1 156 ? 25.527 -16.381 -4.086 1.00 40.12 ? 272 ILE A CG1 1 ATOM 1207 C CG2 . ILE A 1 156 ? 23.430 -15.827 -2.767 1.00 41.76 ? 272 ILE A CG2 1 ATOM 1208 C CD1 . ILE A 1 156 ? 24.961 -16.864 -5.392 1.00 35.43 ? 272 ILE A CD1 1 ATOM 1209 N N . ARG A 1 157 ? 22.405 -12.823 -3.993 1.00 30.97 ? 273 ARG A N 1 ATOM 1210 C CA . ARG A 1 157 ? 21.630 -11.727 -3.426 1.00 32.01 ? 273 ARG A CA 1 ATOM 1211 C C . ARG A 1 157 ? 20.375 -12.278 -2.764 1.00 36.18 ? 273 ARG A C 1 ATOM 1212 O O . ARG A 1 157 ? 19.660 -13.095 -3.343 1.00 36.95 ? 273 ARG A O 1 ATOM 1213 C CB . ARG A 1 157 ? 21.206 -10.736 -4.519 1.00 33.94 ? 273 ARG A CB 1 ATOM 1214 C CG . ARG A 1 157 ? 22.310 -10.285 -5.455 1.00 31.23 ? 273 ARG A CG 1 ATOM 1215 C CD . ARG A 1 157 ? 21.820 -9.183 -6.413 1.00 34.37 ? 273 ARG A CD 1 ATOM 1216 N NE . ARG A 1 157 ? 22.857 -8.808 -7.376 1.00 32.54 ? 273 ARG A NE 1 ATOM 1217 C CZ . ARG A 1 157 ? 23.920 -8.071 -7.068 1.00 34.45 ? 273 ARG A CZ 1 ATOM 1218 N NH1 . ARG A 1 157 ? 24.080 -7.628 -5.823 1.00 33.24 ? 273 ARG A NH1 1 ATOM 1219 N NH2 . ARG A 1 157 ? 24.831 -7.782 -7.992 1.00 35.39 ? 273 ARG A NH2 1 ATOM 1220 N N . SER A 1 158 ? 20.095 -11.807 -1.558 1.00 38.99 ? 274 SER A N 1 ATOM 1221 C CA . SER A 1 158 ? 18.885 -12.204 -0.854 1.00 37.49 ? 274 SER A CA 1 ATOM 1222 C C . SER A 1 158 ? 18.602 -11.205 0.241 1.00 35.77 ? 274 SER A C 1 ATOM 1223 O O . SER A 1 158 ? 19.523 -10.694 0.867 1.00 37.74 ? 274 SER A O 1 ATOM 1224 C CB . SER A 1 158 ? 19.037 -13.608 -0.256 1.00 36.59 ? 274 SER A CB 1 ATOM 1225 O OG . SER A 1 158 ? 17.998 -13.872 0.678 1.00 37.03 ? 274 SER A OG 1 ATOM 1226 N N . GLU A 1 159 ? 17.329 -10.915 0.464 1.00 38.41 ? 275 GLU A N 1 ATOM 1227 C CA . GLU A 1 159 ? 16.950 -10.076 1.593 1.00 37.53 ? 275 GLU A CA 1 ATOM 1228 C C . GLU A 1 159 ? 17.389 -10.679 2.930 1.00 36.31 ? 275 GLU A C 1 ATOM 1229 O O . GLU A 1 159 ? 17.619 -9.955 3.905 1.00 41.92 ? 275 GLU A O 1 ATOM 1230 C CB . GLU A 1 159 ? 15.443 -9.839 1.588 1.00 40.54 ? 275 GLU A CB 1 ATOM 1231 C CG . GLU A 1 159 ? 14.963 -8.884 2.664 1.00 45.17 ? 275 GLU A CG 1 ATOM 1232 C CD . GLU A 1 159 ? 13.531 -8.461 2.434 1.00 51.73 ? 275 GLU A CD 1 ATOM 1233 O OE1 . GLU A 1 159 ? 12.860 -9.109 1.597 1.00 49.80 ? 275 GLU A OE1 1 ATOM 1234 O OE2 . GLU A 1 159 ? 13.083 -7.481 3.075 1.00 59.54 ? 275 GLU A OE2 1 ATOM 1235 N N . ASN A 1 160 ? 17.513 -11.999 2.975 1.00 38.97 ? 276 ASN A N 1 ATOM 1236 C CA . ASN A 1 160 ? 17.882 -12.705 4.195 1.00 43.83 ? 276 ASN A CA 1 ATOM 1237 C C . ASN A 1 160 ? 18.109 -14.182 3.875 1.00 42.09 ? 276 ASN A C 1 ATOM 1238 O O . ASN A 1 160 ? 17.160 -14.960 3.847 1.00 40.81 ? 276 ASN A O 1 ATOM 1239 C CB . ASN A 1 160 ? 16.775 -12.516 5.257 1.00 45.88 ? 276 ASN A CB 1 ATOM 1240 C CG . ASN A 1 160 ? 17.024 -13.305 6.544 1.00 49.46 ? 276 ASN A CG 1 ATOM 1241 O OD1 . ASN A 1 160 ? 18.076 -13.936 6.726 1.00 43.10 ? 276 ASN A OD1 1 ATOM 1242 N ND2 . ASN A 1 160 ? 16.034 -13.258 7.456 1.00 61.49 ? 276 ASN A ND2 1 ATOM 1243 N N . LEU A 1 161 ? 19.365 -14.552 3.626 1.00 42.14 ? 277 LEU A N 1 ATOM 1244 C CA . LEU A 1 161 ? 19.723 -15.903 3.198 1.00 47.81 ? 277 LEU A CA 1 ATOM 1245 C C . LEU A 1 161 ? 19.251 -16.966 4.175 1.00 48.97 ? 277 LEU A C 1 ATOM 1246 O O . LEU A 1 161 ? 18.976 -18.094 3.783 1.00 47.23 ? 277 LEU A O 1 ATOM 1247 C CB . LEU A 1 161 ? 21.235 -16.044 3.028 1.00 49.30 ? 277 LEU A CB 1 ATOM 1248 C CG . LEU A 1 161 ? 21.812 -15.692 1.664 1.00 49.71 ? 277 LEU A CG 1 ATOM 1249 C CD1 . LEU A 1 161 ? 23.308 -15.952 1.657 1.00 54.08 ? 277 LEU A CD1 1 ATOM 1250 C CD2 . LEU A 1 161 ? 21.099 -16.477 0.548 1.00 40.22 ? 277 LEU A CD2 1 ATOM 1251 N N . THR A 1 162 ? 19.176 -16.590 5.447 1.00 49.00 ? 278 THR A N 1 ATOM 1252 C CA . THR A 1 162 ? 18.816 -17.508 6.520 1.00 49.68 ? 278 THR A CA 1 ATOM 1253 C C . THR A 1 162 ? 17.342 -17.883 6.437 1.00 47.86 ? 278 THR A C 1 ATOM 1254 O O . THR A 1 162 ? 16.940 -18.969 6.865 1.00 44.88 ? 278 THR A O 1 ATOM 1255 C CB . THR A 1 162 ? 19.117 -16.877 7.888 1.00 51.21 ? 278 THR A CB 1 ATOM 1256 O OG1 . THR A 1 162 ? 20.494 -16.483 7.924 1.00 54.71 ? 278 THR A OG1 1 ATOM 1257 C CG2 . THR A 1 162 ? 18.839 -17.865 9.021 1.00 49.53 ? 278 THR A CG2 1 ATOM 1258 N N . ASN A 1 163 ? 16.548 -16.972 5.884 1.00 47.02 ? 279 ASN A N 1 ATOM 1259 C CA . ASN A 1 163 ? 15.120 -17.179 5.694 1.00 47.28 ? 279 ASN A CA 1 ATOM 1260 C C . ASN A 1 163 ? 14.852 -17.874 4.356 1.00 41.71 ? 279 ASN A C 1 ATOM 1261 O O . ASN A 1 163 ? 15.028 -17.297 3.286 1.00 40.54 ? 279 ASN A O 1 ATOM 1262 C CB . ASN A 1 163 ? 14.382 -15.839 5.787 1.00 47.43 ? 279 ASN A CB 1 ATOM 1263 C CG . ASN A 1 163 ? 12.875 -15.986 5.662 1.00 51.01 ? 279 ASN A CG 1 ATOM 1264 O OD1 . ASN A 1 163 ? 12.370 -17.058 5.312 1.00 49.25 ? 279 ASN A OD1 1 ATOM 1265 N ND2 . ASN A 1 163 ? 12.146 -14.907 5.955 1.00 45.57 ? 279 ASN A ND2 1 ATOM 1266 N N . ASN A 1 164 ? 14.445 -19.134 4.424 1.00 41.19 ? 280 ASN A N 1 ATOM 1267 C CA . ASN A 1 164 ? 14.272 -19.930 3.217 1.00 40.21 ? 280 ASN A CA 1 ATOM 1268 C C . ASN A 1 164 ? 13.137 -19.429 2.334 1.00 41.10 ? 280 ASN A C 1 ATOM 1269 O O . ASN A 1 164 ? 13.089 -19.750 1.162 1.00 41.29 ? 280 ASN A O 1 ATOM 1270 C CB . ASN A 1 164 ? 14.033 -21.393 3.591 1.00 49.17 ? 280 ASN A CB 1 ATOM 1271 C CG . ASN A 1 164 ? 12.880 -21.554 4.548 1.00 54.52 ? 280 ASN A CG 1 ATOM 1272 O OD1 . ASN A 1 164 ? 13.023 -21.327 5.749 1.00 63.29 ? 280 ASN A OD1 1 ATOM 1273 N ND2 . ASN A 1 164 ? 11.719 -21.924 4.019 1.00 54.87 ? 280 ASN A ND2 1 ATOM 1274 N N . ALA A 1 165 ? 12.231 -18.635 2.896 1.00 50.83 ? 281 ALA A N 1 ATOM 1275 C CA . ALA A 1 165 ? 11.130 -18.072 2.112 1.00 45.56 ? 281 ALA A CA 1 ATOM 1276 C C . ALA A 1 165 ? 11.574 -16.931 1.197 1.00 48.36 ? 281 ALA A C 1 ATOM 1277 O O . ALA A 1 165 ? 10.827 -16.517 0.308 1.00 50.81 ? 281 ALA A O 1 ATOM 1278 C CB . ALA A 1 165 ? 10.000 -17.608 3.022 1.00 51.22 ? 281 ALA A CB 1 ATOM 1279 N N . LYS A 1 166 ? 12.786 -16.429 1.401 1.00 40.37 ? 282 LYS A N 1 ATOM 1280 C CA . LYS A 1 166 ? 13.273 -15.300 0.599 1.00 40.67 ? 282 LYS A CA 1 ATOM 1281 C C . LYS A 1 166 ? 14.011 -15.797 -0.633 1.00 44.80 ? 282 LYS A C 1 ATOM 1282 O O . LYS A 1 166 ? 14.911 -16.641 -0.537 1.00 39.99 ? 282 LYS A O 1 ATOM 1283 C CB . LYS A 1 166 ? 14.169 -14.385 1.438 1.00 35.72 ? 282 LYS A CB 1 ATOM 1284 C CG . LYS A 1 166 ? 13.453 -13.742 2.615 1.00 45.08 ? 282 LYS A CG 1 ATOM 1285 C CD . LYS A 1 166 ? 12.428 -12.710 2.128 1.00 50.72 ? 282 LYS A CD 1 ATOM 1286 C CE . LYS A 1 166 ? 11.810 -11.945 3.296 1.00 52.83 ? 282 LYS A CE 1 ATOM 1287 N NZ . LYS A 1 166 ? 10.631 -11.166 2.857 1.00 56.12 ? 282 LYS A NZ 1 ATOM 1288 N N . THR A 1 167 ? 13.601 -15.284 -1.793 1.00 36.00 ? 283 THR A N 1 ATOM 1289 C CA . THR A 1 167 ? 14.184 -15.660 -3.066 1.00 37.51 ? 283 THR A CA 1 ATOM 1290 C C . THR A 1 167 ? 15.643 -15.254 -3.138 1.00 30.43 ? 283 THR A C 1 ATOM 1291 O O . THR A 1 167 ? 16.049 -14.228 -2.591 1.00 38.80 ? 283 THR A O 1 ATOM 1292 C CB . THR A 1 167 ? 13.433 -14.978 -4.227 1.00 42.63 ? 283 THR A CB 1 ATOM 1293 O OG1 . THR A 1 167 ? 12.061 -15.385 -4.203 1.00 46.77 ? 283 THR A OG1 1 ATOM 1294 C CG2 . THR A 1 167 ? 14.059 -15.357 -5.568 1.00 40.53 ? 283 THR A CG2 1 ATOM 1295 N N . ILE A 1 168 ? 16.424 -16.083 -3.808 1.00 32.43 ? 284 ILE A N 1 ATOM 1296 C CA . ILE A 1 168 ? 17.831 -15.818 -4.024 1.00 35.38 ? 284 ILE A CA 1 ATOM 1297 C C . ILE A 1 168 ? 18.024 -15.471 -5.495 1.00 33.65 ? 284 ILE A C 1 ATOM 1298 O O . ILE A 1 168 ? 17.588 -16.213 -6.372 1.00 35.40 ? 284 ILE A O 1 ATOM 1299 C CB . ILE A 1 168 ? 18.690 -17.061 -3.732 1.00 34.13 ? 284 ILE A CB 1 ATOM 1300 C CG1 . ILE A 1 168 ? 18.696 -17.381 -2.233 1.00 33.96 ? 284 ILE A CG1 1 ATOM 1301 C CG2 . ILE A 1 168 ? 20.096 -16.828 -4.249 1.00 37.10 ? 284 ILE A CG2 1 ATOM 1302 C CD1 . ILE A 1 168 ? 19.122 -18.819 -1.911 1.00 36.22 ? 284 ILE A CD1 1 ATOM 1303 N N . ILE A 1 169 ? 18.637 -14.324 -5.755 1.00 30.03 ? 285 ILE A N 1 ATOM 1304 C CA . ILE A 1 169 ? 19.015 -13.955 -7.115 1.00 30.40 ? 285 ILE A CA 1 ATOM 1305 C C . ILE A 1 169 ? 20.497 -14.228 -7.256 1.00 33.75 ? 285 ILE A C 1 ATOM 1306 O O . ILE A 1 169 ? 21.325 -13.666 -6.509 1.00 34.78 ? 285 ILE A O 1 ATOM 1307 C CB . ILE A 1 169 ? 18.802 -12.458 -7.389 1.00 33.24 ? 285 ILE A CB 1 ATOM 1308 C CG1 . ILE A 1 169 ? 17.339 -12.062 -7.200 1.00 34.69 ? 285 ILE A CG1 1 ATOM 1309 C CG2 . ILE A 1 169 ? 19.308 -12.083 -8.793 1.00 28.78 ? 285 ILE A CG2 1 ATOM 1310 C CD1 . ILE A 1 169 ? 17.116 -10.547 -7.286 1.00 35.61 ? 285 ILE A CD1 1 ATOM 1311 N N . VAL A 1 170 ? 20.824 -15.113 -8.187 1.00 34.20 ? 286 VAL A N 1 ATOM 1312 C CA . VAL A 1 170 ? 22.197 -15.396 -8.538 1.00 35.51 ? 286 VAL A CA 1 ATOM 1313 C C . VAL A 1 170 ? 22.581 -14.490 -9.702 1.00 38.34 ? 286 VAL A C 1 ATOM 1314 O O . VAL A 1 170 ? 22.012 -14.580 -10.785 1.00 37.40 ? 286 VAL A O 1 ATOM 1315 C CB . VAL A 1 170 ? 22.381 -16.863 -8.951 1.00 30.92 ? 286 VAL A CB 1 ATOM 1316 C CG1 . VAL A 1 170 ? 23.841 -17.144 -9.286 1.00 33.26 ? 286 VAL A CG1 1 ATOM 1317 C CG2 . VAL A 1 170 ? 21.881 -17.784 -7.858 1.00 30.54 ? 286 VAL A CG2 1 ATOM 1318 N N . HIS A 1 171 ? 23.542 -13.607 -9.475 1.00 35.45 ? 287 HIS A N 1 ATOM 1319 C CA . HIS A 1 171 ? 23.964 -12.702 -10.531 1.00 36.13 ? 287 HIS A CA 1 ATOM 1320 C C . HIS A 1 171 ? 25.222 -13.237 -11.212 1.00 36.51 ? 287 HIS A C 1 ATOM 1321 O O . HIS A 1 171 ? 26.310 -13.226 -10.624 1.00 38.25 ? 287 HIS A O 1 ATOM 1322 C CB . HIS A 1 171 ? 24.214 -11.305 -9.968 1.00 29.90 ? 287 HIS A CB 1 ATOM 1323 C CG . HIS A 1 171 ? 24.221 -10.229 -11.014 1.00 34.97 ? 287 HIS A CG 1 ATOM 1324 N ND1 . HIS A 1 171 ? 24.546 -8.918 -10.736 1.00 39.29 ? 287 HIS A ND1 1 ATOM 1325 C CD2 . HIS A 1 171 ? 23.941 -10.275 -12.340 1.00 35.49 ? 287 HIS A CD2 1 ATOM 1326 C CE1 . HIS A 1 171 ? 24.462 -8.201 -11.843 1.00 39.55 ? 287 HIS A CE1 1 ATOM 1327 N NE2 . HIS A 1 171 ? 24.099 -9.001 -12.831 1.00 36.38 ? 287 HIS A NE2 1 ATOM 1328 N N . LEU A 1 172 ? 25.070 -13.688 -12.455 1.00 33.75 ? 288 LEU A N 1 ATOM 1329 C CA . LEU A 1 172 ? 26.170 -14.326 -13.181 1.00 37.13 ? 288 LEU A CA 1 ATOM 1330 C C . LEU A 1 172 ? 27.175 -13.300 -13.675 1.00 41.61 ? 288 LEU A C 1 ATOM 1331 O O . LEU A 1 172 ? 26.806 -12.161 -13.963 1.00 40.20 ? 288 LEU A O 1 ATOM 1332 C CB . LEU A 1 172 ? 25.632 -15.109 -14.382 1.00 39.63 ? 288 LEU A CB 1 ATOM 1333 C CG . LEU A 1 172 ? 24.620 -16.194 -14.038 1.00 35.67 ? 288 LEU A CG 1 ATOM 1334 C CD1 . LEU A 1 172 ? 24.158 -16.921 -15.316 1.00 32.29 ? 288 LEU A CD1 1 ATOM 1335 C CD2 . LEU A 1 172 ? 25.235 -17.163 -13.023 1.00 34.90 ? 288 LEU A CD2 1 ATOM 1336 N N . ASN A 1 173 ? 28.437 -13.711 -13.787 1.00 40.18 ? 289 ASN A N 1 ATOM 1337 C CA . ASN A 1 173 ? 29.472 -12.841 -14.339 1.00 39.38 ? 289 ASN A CA 1 ATOM 1338 C C . ASN A 1 173 ? 29.834 -13.212 -15.779 1.00 46.57 ? 289 ASN A C 1 ATOM 1339 O O . ASN A 1 173 ? 30.613 -12.524 -16.443 1.00 42.65 ? 289 ASN A O 1 ATOM 1340 C CB . ASN A 1 173 ? 30.719 -12.766 -13.434 1.00 43.24 ? 289 ASN A CB 1 ATOM 1341 C CG . ASN A 1 173 ? 31.411 -14.115 -13.233 1.00 49.02 ? 289 ASN A CG 1 ATOM 1342 O OD1 . ASN A 1 173 ? 30.936 -15.156 -13.694 1.00 47.36 ? 289 ASN A OD1 1 ATOM 1343 N ND2 . ASN A 1 173 ? 32.557 -14.083 -12.543 1.00 62.31 ? 289 ASN A ND2 1 ATOM 1344 N N . LYS A 1 174 ? 29.233 -14.290 -16.263 1.00 44.31 ? 290 LYS A N 1 ATOM 1345 C CA . LYS A 1 174 ? 29.432 -14.721 -17.636 1.00 49.06 ? 290 LYS A CA 1 ATOM 1346 C C . LYS A 1 174 ? 28.106 -15.226 -18.220 1.00 44.36 ? 290 LYS A C 1 ATOM 1347 O O . LYS A 1 174 ? 27.433 -16.068 -17.625 1.00 44.25 ? 290 LYS A O 1 ATOM 1348 C CB . LYS A 1 174 ? 30.519 -15.799 -17.706 1.00 55.56 ? 290 LYS A CB 1 ATOM 1349 C CG . LYS A 1 174 ? 30.885 -16.225 -19.125 1.00 68.26 ? 290 LYS A CG 1 ATOM 1350 C CD . LYS A 1 174 ? 31.989 -17.273 -19.134 1.00 76.74 ? 290 LYS A CD 1 ATOM 1351 C CE . LYS A 1 174 ? 32.205 -17.830 -20.534 1.00 85.38 ? 290 LYS A CE 1 ATOM 1352 N NZ . LYS A 1 174 ? 33.404 -18.716 -20.615 1.00 92.11 ? 290 LYS A NZ 1 ATOM 1353 N N . SER A 1 175 ? 27.722 -14.675 -19.368 1.00 39.77 ? 291 SER A N 1 ATOM 1354 C CA . SER A 1 175 ? 26.485 -15.074 -20.039 1.00 42.82 ? 291 SER A CA 1 ATOM 1355 C C . SER A 1 175 ? 26.559 -16.509 -20.524 1.00 46.29 ? 291 SER A C 1 ATOM 1356 O O . SER A 1 175 ? 27.620 -16.974 -20.940 1.00 42.47 ? 291 SER A O 1 ATOM 1357 C CB . SER A 1 175 ? 26.223 -14.171 -21.249 1.00 45.10 ? 291 SER A CB 1 ATOM 1358 O OG . SER A 1 175 ? 25.872 -12.856 -20.848 1.00 55.12 ? 291 SER A OG 1 ATOM 1359 N N . VAL A 1 176 ? 25.431 -17.210 -20.467 1.00 40.95 ? 292 VAL A N 1 ATOM 1360 C CA . VAL A 1 176 ? 25.290 -18.462 -21.201 1.00 43.59 ? 292 VAL A CA 1 ATOM 1361 C C . VAL A 1 176 ? 24.090 -18.346 -22.141 1.00 41.04 ? 292 VAL A C 1 ATOM 1362 O O . VAL A 1 176 ? 22.961 -18.078 -21.708 1.00 37.39 ? 292 VAL A O 1 ATOM 1363 C CB . VAL A 1 176 ? 25.119 -19.682 -20.273 1.00 45.02 ? 292 VAL A CB 1 ATOM 1364 C CG1 . VAL A 1 176 ? 25.058 -20.962 -21.091 1.00 45.20 ? 292 VAL A CG1 1 ATOM 1365 C CG2 . VAL A 1 176 ? 26.268 -19.747 -19.257 1.00 50.05 ? 292 VAL A CG2 1 ATOM 1366 N N . GLU A 1 177 ? 24.341 -18.524 -23.432 1.00 41.94 ? 293 GLU A N 1 ATOM 1367 C CA . GLU A 1 177 ? 23.279 -18.415 -24.415 1.00 43.61 ? 293 GLU A CA 1 ATOM 1368 C C . GLU A 1 177 ? 22.273 -19.538 -24.263 1.00 40.93 ? 293 GLU A C 1 ATOM 1369 O O . GLU A 1 177 ? 22.622 -20.681 -23.985 1.00 40.53 ? 293 GLU A O 1 ATOM 1370 C CB . GLU A 1 177 ? 23.833 -18.405 -25.845 1.00 48.10 ? 293 GLU A CB 1 ATOM 1371 C CG . GLU A 1 177 ? 24.526 -17.112 -26.230 1.00 51.98 ? 293 GLU A CG 1 ATOM 1372 C CD . GLU A 1 177 ? 24.622 -16.913 -27.736 1.00 56.04 ? 293 GLU A CD 1 ATOM 1373 O OE1 . GLU A 1 177 ? 24.496 -17.906 -28.492 1.00 50.40 ? 293 GLU A OE1 1 ATOM 1374 O OE2 . GLU A 1 177 ? 24.807 -15.752 -28.161 1.00 59.87 ? 293 GLU A OE2 1 ATOM 1375 N N . ILE A 1 178 ? 21.010 -19.187 -24.434 1.00 37.16 ? 294 ILE A N 1 ATOM 1376 C CA . ILE A 1 178 ? 19.957 -20.165 -24.545 1.00 35.31 ? 294 ILE A CA 1 ATOM 1377 C C . ILE A 1 178 ? 19.217 -19.834 -25.831 1.00 37.13 ? 294 ILE A C 1 ATOM 1378 O O . ILE A 1 178 ? 18.751 -18.708 -26.038 1.00 37.80 ? 294 ILE A O 1 ATOM 1379 C CB . ILE A 1 178 ? 19.037 -20.174 -23.301 1.00 34.36 ? 294 ILE A CB 1 ATOM 1380 C CG1 . ILE A 1 178 ? 17.919 -21.203 -23.472 1.00 31.45 ? 294 ILE A CG1 1 ATOM 1381 C CG2 . ILE A 1 178 ? 18.479 -18.762 -22.994 1.00 33.20 ? 294 ILE A CG2 1 ATOM 1382 C CD1 . ILE A 1 178 ? 17.104 -21.423 -22.200 1.00 37.12 ? 294 ILE A CD1 1 ATOM 1383 N N . ASN A 1 179 ? 19.167 -20.820 -26.718 1.00 39.51 ? 295 ASN A N 1 ATOM 1384 C CA . ASN A 1 179 ? 18.698 -20.635 -28.085 1.00 38.22 ? 295 ASN A CA 1 ATOM 1385 C C . ASN A 1 179 ? 17.399 -21.396 -28.270 1.00 38.74 ? 295 ASN A C 1 ATOM 1386 O O . ASN A 1 179 ? 17.401 -22.616 -28.394 1.00 40.81 ? 295 ASN A O 1 ATOM 1387 C CB . ASN A 1 179 ? 19.776 -21.156 -29.046 1.00 42.32 ? 295 ASN A CB 1 ATOM 1388 C CG . ASN A 1 179 ? 19.360 -21.096 -30.518 1.00 49.78 ? 295 ASN A CG 1 ATOM 1389 O OD1 . ASN A 1 179 ? 18.292 -20.583 -30.858 1.00 40.93 ? 295 ASN A OD1 1 ATOM 1390 N ND2 . ASN A 1 179 ? 20.238 -21.609 -31.396 1.00 64.20 ? 295 ASN A ND2 1 ATOM 1391 N N . CYS A 1 180 ? 16.288 -20.673 -28.261 1.00 36.30 ? 296 CYS A N 1 ATOM 1392 C CA . CYS A 1 180 ? 14.985 -21.312 -28.298 1.00 36.72 ? 296 CYS A CA 1 ATOM 1393 C C . CYS A 1 180 ? 14.328 -21.210 -29.665 1.00 36.32 ? 296 CYS A C 1 ATOM 1394 O O . CYS A 1 180 ? 14.327 -20.151 -30.295 1.00 38.10 ? 296 CYS A O 1 ATOM 1395 C CB . CYS A 1 180 ? 14.070 -20.745 -27.203 1.00 29.36 ? 296 CYS A CB 1 ATOM 1396 S SG . CYS A 1 180 ? 14.858 -20.786 -25.582 1.00 37.99 ? 296 CYS A SG 1 ATOM 1397 N N . THR A 1 181 ? 13.773 -22.332 -30.115 1.00 33.91 ? 297 THR A N 1 ATOM 1398 C CA . THR A 1 181 ? 13.231 -22.418 -31.459 1.00 34.74 ? 297 THR A CA 1 ATOM 1399 C C . THR A 1 181 ? 11.962 -23.255 -31.516 1.00 38.90 ? 297 THR A C 1 ATOM 1400 O O . THR A 1 181 ? 11.910 -24.358 -30.976 1.00 37.72 ? 297 THR A O 1 ATOM 1401 C CB . THR A 1 181 ? 14.260 -23.050 -32.442 1.00 45.78 ? 297 THR A CB 1 ATOM 1402 O OG1 . THR A 1 181 ? 15.480 -22.294 -32.431 1.00 44.32 ? 297 THR A OG1 1 ATOM 1403 C CG2 . THR A 1 181 ? 13.698 -23.074 -33.850 1.00 46.88 ? 297 THR A CG2 1 ATOM 1404 N N . ARG A 1 182 ? 10.935 -22.709 -32.159 1.00 38.70 ? 298 ARG A N 1 ATOM 1405 C CA . ARG A 1 182 ? 9.821 -23.507 -32.640 1.00 38.40 ? 298 ARG A CA 1 ATOM 1406 C C . ARG A 1 182 ? 10.095 -23.636 -34.126 1.00 35.95 ? 298 ARG A C 1 ATOM 1407 O O . ARG A 1 182 ? 9.904 -22.677 -34.879 1.00 39.92 ? 298 ARG A O 1 ATOM 1408 C CB . ARG A 1 182 ? 8.490 -22.785 -32.421 1.00 37.19 ? 298 ARG A CB 1 ATOM 1409 C CG . ARG A 1 182 ? 7.245 -23.667 -32.523 1.00 39.27 ? 298 ARG A CG 1 ATOM 1410 C CD . ARG A 1 182 ? 7.029 -24.274 -33.915 1.00 42.90 ? 298 ARG A CD 1 ATOM 1411 N NE . ARG A 1 182 ? 6.908 -23.270 -34.974 1.00 45.39 ? 298 ARG A NE 1 ATOM 1412 C CZ . ARG A 1 182 ? 5.776 -22.652 -35.302 1.00 39.98 ? 298 ARG A CZ 1 ATOM 1413 N NH1 . ARG A 1 182 ? 4.660 -22.915 -34.632 1.00 33.90 ? 298 ARG A NH1 1 ATOM 1414 N NH2 . ARG A 1 182 ? 5.761 -21.754 -36.284 1.00 34.32 ? 298 ARG A NH2 1 ATOM 1415 N N . PRO A 1 183 ? 10.555 -24.813 -34.559 1.00 41.66 ? 299 PRO A N 1 ATOM 1416 C CA . PRO A 1 183 ? 10.982 -24.936 -35.958 1.00 47.87 ? 299 PRO A CA 1 ATOM 1417 C C . PRO A 1 183 ? 9.843 -24.758 -36.971 1.00 52.85 ? 299 PRO A C 1 ATOM 1418 O O . PRO A 1 183 ? 8.686 -25.037 -36.664 1.00 49.08 ? 299 PRO A O 1 ATOM 1419 C CB . PRO A 1 183 ? 11.579 -26.349 -36.023 1.00 48.56 ? 299 PRO A CB 1 ATOM 1420 C CG . PRO A 1 183 ? 10.933 -27.100 -34.904 1.00 47.49 ? 299 PRO A CG 1 ATOM 1421 C CD . PRO A 1 183 ? 10.661 -26.087 -33.819 1.00 42.44 ? 299 PRO A CD 1 ATOM 1422 N N . SER A 1 184 ? 10.183 -24.286 -38.169 1.00 57.20 ? 300 SER A N 1 ATOM 1423 C CA . SER A 1 184 ? 9.199 -24.079 -39.231 1.00 63.85 ? 300 SER A CA 1 ATOM 1424 C C . SER A 1 184 ? 8.438 -25.351 -39.611 1.00 70.45 ? 300 SER A C 1 ATOM 1425 O O . SER A 1 184 ? 7.232 -25.308 -39.864 1.00 72.00 ? 300 SER A O 1 ATOM 1426 C CB . SER A 1 184 ? 9.873 -23.505 -40.478 1.00 65.00 ? 300 SER A CB 1 ATOM 1427 O OG . SER A 1 184 ? 8.902 -23.173 -41.453 1.00 66.95 ? 300 SER A OG 1 ATOM 1428 N N . ASN A 1 185 ? 9.145 -26.476 -39.658 1.00 73.20 ? 301 ASN A N 1 ATOM 1429 C CA . ASN A 1 185 ? 8.541 -27.741 -40.068 1.00 88.23 ? 301 ASN A CA 1 ATOM 1430 C C . ASN A 1 185 ? 9.352 -28.941 -39.572 1.00 94.05 ? 301 ASN A C 1 ATOM 1431 O O . ASN A 1 185 ? 9.548 -29.925 -40.290 1.00 97.14 ? 301 ASN A O 1 ATOM 1432 C CB . ASN A 1 185 ? 8.377 -27.781 -41.596 1.00 95.43 ? 301 ASN A CB 1 ATOM 1433 C CG . ASN A 1 185 ? 7.526 -28.952 -42.072 1.00 99.90 ? 301 ASN A CG 1 ATOM 1434 O OD1 . ASN A 1 185 ? 6.307 -28.963 -41.891 1.00 100.38 ? 301 ASN A OD1 1 ATOM 1435 N ND2 . ASN A 1 185 ? 8.167 -29.937 -42.698 1.00 101.75 ? 301 ASN A ND2 1 ATOM 1436 N N . GLY A 1 192 ? 4.193 -31.282 -37.965 1.00 97.02 ? 324 GLY A N 1 ATOM 1437 C CA . GLY A 1 192 ? 3.807 -31.951 -36.737 1.00 95.41 ? 324 GLY A CA 1 ATOM 1438 C C . GLY A 1 192 ? 3.152 -31.014 -35.739 1.00 91.17 ? 324 GLY A C 1 ATOM 1439 O O . GLY A 1 192 ? 2.134 -30.385 -36.037 1.00 92.23 ? 324 GLY A O 1 ATOM 1440 N N . ASP A 1 193 ? 3.747 -30.917 -34.551 1.00 79.31 ? 325 ASP A N 1 ATOM 1441 C CA . ASP A 1 193 ? 3.168 -30.148 -33.454 1.00 63.27 ? 325 ASP A CA 1 ATOM 1442 C C . ASP A 1 193 ? 3.618 -28.682 -33.478 1.00 49.93 ? 325 ASP A C 1 ATOM 1443 O O . ASP A 1 193 ? 4.779 -28.379 -33.221 1.00 48.71 ? 325 ASP A O 1 ATOM 1444 C CB . ASP A 1 193 ? 3.529 -30.791 -32.113 1.00 60.59 ? 325 ASP A CB 1 ATOM 1445 C CG . ASP A 1 193 ? 2.798 -30.151 -30.947 1.00 56.72 ? 325 ASP A CG 1 ATOM 1446 O OD1 . ASP A 1 193 ? 2.251 -29.045 -31.129 1.00 50.35 ? 325 ASP A OD1 1 ATOM 1447 O OD2 . ASP A 1 193 ? 2.765 -30.753 -29.852 1.00 61.55 ? 325 ASP A OD2 1 ATOM 1448 N N . ILE A 1 194 ? 2.695 -27.776 -33.787 1.00 41.78 ? 326 ILE A N 1 ATOM 1449 C CA . ILE A 1 194 ? 3.046 -26.363 -33.902 1.00 38.84 ? 326 ILE A CA 1 ATOM 1450 C C . ILE A 1 194 ? 3.397 -25.702 -32.564 1.00 39.60 ? 326 ILE A C 1 ATOM 1451 O O . ILE A 1 194 ? 3.976 -24.626 -32.552 1.00 38.87 ? 326 ILE A O 1 ATOM 1452 C CB . ILE A 1 194 ? 1.943 -25.528 -34.586 1.00 41.21 ? 326 ILE A CB 1 ATOM 1453 C CG1 . ILE A 1 194 ? 0.651 -25.563 -33.772 1.00 46.20 ? 326 ILE A CG1 1 ATOM 1454 C CG2 . ILE A 1 194 ? 1.708 -26.000 -36.014 1.00 46.23 ? 326 ILE A CG2 1 ATOM 1455 C CD1 . ILE A 1 194 ? -0.421 -24.608 -34.289 1.00 44.91 ? 326 ILE A CD1 1 ATOM 1456 N N . ARG A 1 195 ? 3.041 -26.328 -31.443 1.00 37.79 ? 327 ARG A N 1 ATOM 1457 C CA . ARG A 1 195 ? 3.394 -25.763 -30.141 1.00 38.60 ? 327 ARG A CA 1 ATOM 1458 C C . ARG A 1 195 ? 4.645 -26.407 -29.556 1.00 35.41 ? 327 ARG A C 1 ATOM 1459 O O . ARG A 1 195 ? 5.126 -26.003 -28.500 1.00 35.80 ? 327 ARG A O 1 ATOM 1460 C CB . ARG A 1 195 ? 2.229 -25.871 -29.155 1.00 38.80 ? 327 ARG A CB 1 ATOM 1461 C CG . ARG A 1 195 ? 1.080 -24.952 -29.485 1.00 35.90 ? 327 ARG A CG 1 ATOM 1462 C CD . ARG A 1 195 ? -0.187 -25.405 -28.776 1.00 35.42 ? 327 ARG A CD 1 ATOM 1463 N NE . ARG A 1 195 ? -1.352 -24.940 -29.513 1.00 39.55 ? 327 ARG A NE 1 ATOM 1464 C CZ . ARG A 1 195 ? -1.891 -25.586 -30.541 1.00 39.36 ? 327 ARG A CZ 1 ATOM 1465 N NH1 . ARG A 1 195 ? -1.372 -26.733 -30.963 1.00 40.51 ? 327 ARG A NH1 1 ATOM 1466 N NH2 . ARG A 1 195 ? -2.943 -25.072 -31.159 1.00 38.94 ? 327 ARG A NH2 1 ATOM 1467 N N . LYS A 1 196 ? 5.184 -27.406 -30.240 1.00 35.29 ? 328 LYS A N 1 ATOM 1468 C CA . LYS A 1 196 ? 6.394 -28.046 -29.752 1.00 37.61 ? 328 LYS A CA 1 ATOM 1469 C C . LYS A 1 196 ? 7.613 -27.190 -30.075 1.00 34.96 ? 328 LYS A C 1 ATOM 1470 O O . LYS A 1 196 ? 7.802 -26.759 -31.213 1.00 37.22 ? 328 LYS A O 1 ATOM 1471 C CB . LYS A 1 196 ? 6.557 -29.435 -30.362 1.00 42.59 ? 328 LYS A CB 1 ATOM 1472 C CG . LYS A 1 196 ? 7.651 -30.252 -29.719 1.00 51.46 ? 328 LYS A CG 1 ATOM 1473 C CD . LYS A 1 196 ? 7.584 -31.717 -30.175 1.00 61.97 ? 328 LYS A CD 1 ATOM 1474 C CE . LYS A 1 196 ? 6.313 -32.413 -29.678 1.00 71.24 ? 328 LYS A CE 1 ATOM 1475 N NZ . LYS A 1 196 ? 6.388 -32.829 -28.242 1.00 73.92 ? 328 LYS A NZ 1 ATOM 1476 N N . ALA A 1 197 ? 8.427 -26.925 -29.062 1.00 35.73 ? 329 ALA A N 1 ATOM 1477 C CA . ALA A 1 197 ? 9.620 -26.129 -29.254 1.00 38.16 ? 329 ALA A CA 1 ATOM 1478 C C . ALA A 1 197 ? 10.739 -26.664 -28.373 1.00 40.69 ? 329 ALA A C 1 ATOM 1479 O O . ALA A 1 197 ? 10.552 -27.642 -27.646 1.00 38.14 ? 329 ALA A O 1 ATOM 1480 C CB . ALA A 1 197 ? 9.335 -24.658 -28.952 1.00 36.02 ? 329 ALA A CB 1 ATOM 1481 N N . TYR A 1 198 ? 11.907 -26.037 -28.449 1.00 36.26 ? 330 TYR A N 1 ATOM 1482 C CA . TYR A 1 198 ? 13.037 -26.459 -27.638 1.00 41.04 ? 330 TYR A CA 1 ATOM 1483 C C . TYR A 1 198 ? 14.033 -25.325 -27.446 1.00 36.47 ? 330 TYR A C 1 ATOM 1484 O O . TYR A 1 198 ? 14.072 -24.381 -28.232 1.00 38.79 ? 330 TYR A O 1 ATOM 1485 C CB . TYR A 1 198 ? 13.719 -27.681 -28.262 1.00 48.26 ? 330 TYR A CB 1 ATOM 1486 C CG . TYR A 1 198 ? 14.154 -27.488 -29.698 1.00 55.23 ? 330 TYR A CG 1 ATOM 1487 C CD1 . TYR A 1 198 ? 15.412 -26.967 -30.002 1.00 63.20 ? 330 TYR A CD1 1 ATOM 1488 C CD2 . TYR A 1 198 ? 13.315 -27.834 -30.754 1.00 54.66 ? 330 TYR A CD2 1 ATOM 1489 C CE1 . TYR A 1 198 ? 15.818 -26.787 -31.318 1.00 63.02 ? 330 TYR A CE1 1 ATOM 1490 C CE2 . TYR A 1 198 ? 13.714 -27.655 -32.069 1.00 59.86 ? 330 TYR A CE2 1 ATOM 1491 C CZ . TYR A 1 198 ? 14.965 -27.133 -32.345 1.00 65.83 ? 330 TYR A CZ 1 ATOM 1492 O OH . TYR A 1 198 ? 15.360 -26.962 -33.657 1.00 71.87 ? 330 TYR A OH 1 ATOM 1493 N N . CYS A 1 199 ? 14.817 -25.422 -26.379 1.00 40.83 ? 331 CYS A N 1 ATOM 1494 C CA . CYS A 1 199 ? 15.904 -24.487 -26.133 1.00 40.78 ? 331 CYS A CA 1 ATOM 1495 C C . CYS A 1 199 ? 17.201 -25.256 -26.082 1.00 45.65 ? 331 CYS A C 1 ATOM 1496 O O . CYS A 1 199 ? 17.313 -26.263 -25.375 1.00 43.93 ? 331 CYS A O 1 ATOM 1497 C CB . CYS A 1 199 ? 15.707 -23.755 -24.808 1.00 40.41 ? 331 CYS A CB 1 ATOM 1498 S SG . CYS A 1 199 ? 14.338 -22.619 -24.835 1.00 42.99 ? 331 CYS A SG 1 ATOM 1499 N N . GLU A 1 200 ? 18.184 -24.775 -26.829 1.00 43.93 ? 332 GLU A N 1 ATOM 1500 C CA . GLU A 1 200 ? 19.490 -25.409 -26.838 1.00 42.57 ? 332 GLU A CA 1 ATOM 1501 C C . GLU A 1 200 ? 20.463 -24.609 -25.985 1.00 45.93 ? 332 GLU A C 1 ATOM 1502 O O . GLU A 1 200 ? 20.559 -23.393 -26.120 1.00 42.24 ? 332 GLU A O 1 ATOM 1503 C CB . GLU A 1 200 ? 19.989 -25.557 -28.278 1.00 42.99 ? 332 GLU A CB 1 ATOM 1504 C CG . GLU A 1 200 ? 19.141 -26.527 -29.090 1.00 45.72 ? 332 GLU A CG 1 ATOM 1505 C CD . GLU A 1 200 ? 19.610 -26.663 -30.527 1.00 52.60 ? 332 GLU A CD 1 ATOM 1506 O OE1 . GLU A 1 200 ? 20.132 -25.669 -31.081 1.00 56.99 ? 332 GLU A OE1 1 ATOM 1507 O OE2 . GLU A 1 200 ? 19.457 -27.765 -31.094 1.00 51.49 ? 332 GLU A OE2 1 ATOM 1508 N N . ILE A 1 201 ? 21.154 -25.289 -25.081 1.00 42.72 ? 333 ILE A N 1 ATOM 1509 C CA . ILE A 1 201 ? 22.181 -24.641 -24.278 1.00 41.97 ? 333 ILE A CA 1 ATOM 1510 C C . ILE A 1 201 ? 23.473 -25.427 -24.386 1.00 46.41 ? 333 ILE A C 1 ATOM 1511 O O . ILE A 1 201 ? 23.468 -26.652 -24.469 1.00 49.10 ? 333 ILE A O 1 ATOM 1512 C CB . ILE A 1 201 ? 21.798 -24.530 -22.782 1.00 45.80 ? 333 ILE A CB 1 ATOM 1513 C CG1 . ILE A 1 201 ? 20.442 -23.838 -22.603 1.00 44.81 ? 333 ILE A CG1 1 ATOM 1514 C CG2 . ILE A 1 201 ? 22.866 -23.771 -22.018 1.00 42.54 ? 333 ILE A CG2 1 ATOM 1515 C CD1 . ILE A 1 201 ? 19.277 -24.789 -22.532 1.00 48.84 ? 333 ILE A CD1 1 ATOM 1516 N N . ASN A 1 202 ? 24.587 -24.716 -24.385 1.00 46.91 ? 334 ASN A N 1 ATOM 1517 C CA . ASN A 1 202 ? 25.882 -25.370 -24.380 1.00 52.88 ? 334 ASN A CA 1 ATOM 1518 C C . ASN A 1 202 ? 26.176 -26.000 -23.016 1.00 47.13 ? 334 ASN A C 1 ATOM 1519 O O . ASN A 1 202 ? 26.463 -25.294 -22.050 1.00 48.91 ? 334 ASN A O 1 ATOM 1520 C CB . ASN A 1 202 ? 26.957 -24.356 -24.748 1.00 61.83 ? 334 ASN A CB 1 ATOM 1521 C CG . ASN A 1 202 ? 28.324 -24.965 -24.813 1.00 72.18 ? 334 ASN A CG 1 ATOM 1522 O OD1 . ASN A 1 202 ? 28.676 -25.814 -23.994 1.00 60.24 ? 334 ASN A OD1 1 ATOM 1523 N ND2 . ASN A 1 202 ? 29.109 -24.543 -25.792 1.00 96.98 ? 334 ASN A ND2 1 ATOM 1524 N N . GLY A 1 203 ? 26.101 -27.326 -22.946 1.00 50.65 ? 335 GLY A N 1 ATOM 1525 C CA . GLY A 1 203 ? 26.258 -28.050 -21.695 1.00 52.56 ? 335 GLY A CA 1 ATOM 1526 C C . GLY A 1 203 ? 27.578 -27.845 -20.972 1.00 52.14 ? 335 GLY A C 1 ATOM 1527 O O . GLY A 1 203 ? 27.605 -27.742 -19.745 1.00 48.19 ? 335 GLY A O 1 ATOM 1528 N N . THR A 1 204 ? 28.677 -27.811 -21.722 1.00 51.39 ? 336 THR A N 1 ATOM 1529 C CA . THR A 1 204 ? 29.989 -27.558 -21.139 1.00 54.17 ? 336 THR A CA 1 ATOM 1530 C C . THR A 1 204 ? 30.025 -26.190 -20.464 1.00 56.64 ? 336 THR A C 1 ATOM 1531 O O . THR A 1 204 ? 30.462 -26.064 -19.318 1.00 56.47 ? 336 THR A O 1 ATOM 1532 C CB . THR A 1 204 ? 31.106 -27.626 -22.199 1.00 64.53 ? 336 THR A CB 1 ATOM 1533 O OG1 . THR A 1 204 ? 31.062 -28.894 -22.856 1.00 66.62 ? 336 THR A OG1 1 ATOM 1534 C CG2 . THR A 1 204 ? 32.473 -27.455 -21.551 1.00 70.58 ? 336 THR A CG2 1 ATOM 1535 N N . LYS A 1 205 ? 29.562 -25.168 -21.179 1.00 53.90 ? 337 LYS A N 1 ATOM 1536 C CA . LYS A 1 205 ? 29.537 -23.813 -20.647 1.00 53.23 ? 337 LYS A CA 1 ATOM 1537 C C . LYS A 1 205 ? 28.593 -23.718 -19.455 1.00 50.97 ? 337 LYS A C 1 ATOM 1538 O O . LYS A 1 205 ? 28.950 -23.187 -18.400 1.00 52.58 ? 337 LYS A O 1 ATOM 1539 C CB . LYS A 1 205 ? 29.097 -22.818 -21.724 1.00 58.71 ? 337 LYS A CB 1 ATOM 1540 C CG . LYS A 1 205 ? 30.181 -22.406 -22.704 1.00 68.96 ? 337 LYS A CG 1 ATOM 1541 C CD . LYS A 1 205 ? 29.619 -21.452 -23.760 1.00 74.73 ? 337 LYS A CD 1 ATOM 1542 C CE . LYS A 1 205 ? 30.719 -20.710 -24.517 1.00 80.74 ? 337 LYS A CE 1 ATOM 1543 N NZ . LYS A 1 205 ? 31.636 -21.615 -25.272 1.00 83.15 ? 337 LYS A NZ 1 ATOM 1544 N N . TRP A 1 206 ? 27.383 -24.237 -19.627 1.00 44.39 ? 338 TRP A N 1 ATOM 1545 C CA . TRP A 1 206 ? 26.378 -24.117 -18.587 1.00 46.77 ? 338 TRP A CA 1 ATOM 1546 C C . TRP A 1 206 ? 26.795 -24.820 -17.294 1.00 45.42 ? 338 TRP A C 1 ATOM 1547 O O . TRP A 1 206 ? 26.669 -24.260 -16.201 1.00 46.00 ? 338 TRP A O 1 ATOM 1548 C CB . TRP A 1 206 ? 25.025 -24.644 -19.050 1.00 47.10 ? 338 TRP A CB 1 ATOM 1549 C CG . TRP A 1 206 ? 24.090 -24.765 -17.901 1.00 48.29 ? 338 TRP A CG 1 ATOM 1550 C CD1 . TRP A 1 206 ? 23.735 -25.904 -17.251 1.00 51.53 ? 338 TRP A CD1 1 ATOM 1551 C CD2 . TRP A 1 206 ? 23.413 -23.697 -17.241 1.00 45.75 ? 338 TRP A CD2 1 ATOM 1552 N NE1 . TRP A 1 206 ? 22.868 -25.611 -16.228 1.00 48.32 ? 338 TRP A NE1 1 ATOM 1553 C CE2 . TRP A 1 206 ? 22.653 -24.263 -16.201 1.00 45.97 ? 338 TRP A CE2 1 ATOM 1554 C CE3 . TRP A 1 206 ? 23.368 -22.313 -17.433 1.00 44.92 ? 338 TRP A CE3 1 ATOM 1555 C CZ2 . TRP A 1 206 ? 21.847 -23.495 -15.357 1.00 40.67 ? 338 TRP A CZ2 1 ATOM 1556 C CZ3 . TRP A 1 206 ? 22.576 -21.551 -16.589 1.00 46.52 ? 338 TRP A CZ3 1 ATOM 1557 C CH2 . TRP A 1 206 ? 21.826 -22.145 -15.567 1.00 43.85 ? 338 TRP A CH2 1 ATOM 1558 N N . ASN A 1 207 ? 27.288 -26.045 -17.413 1.00 44.13 ? 339 ASN A N 1 ATOM 1559 C CA . ASN A 1 207 ? 27.701 -26.784 -16.234 1.00 52.05 ? 339 ASN A CA 1 ATOM 1560 C C . ASN A 1 207 ? 28.899 -26.157 -15.531 1.00 50.53 ? 339 ASN A C 1 ATOM 1561 O O . ASN A 1 207 ? 29.044 -26.270 -14.315 1.00 48.53 ? 339 ASN A O 1 ATOM 1562 C CB . ASN A 1 207 ? 27.947 -28.249 -16.577 1.00 58.31 ? 339 ASN A CB 1 ATOM 1563 C CG . ASN A 1 207 ? 26.658 -28.987 -16.827 1.00 63.61 ? 339 ASN A CG 1 ATOM 1564 O OD1 . ASN A 1 207 ? 25.657 -28.748 -16.148 1.00 63.87 ? 339 ASN A OD1 1 ATOM 1565 N ND2 . ASN A 1 207 ? 26.656 -29.859 -17.825 1.00 66.28 ? 339 ASN A ND2 1 ATOM 1566 N N . LYS A 1 208 ? 29.747 -25.482 -16.294 1.00 49.34 ? 340 LYS A N 1 ATOM 1567 C CA . LYS A 1 208 ? 30.881 -24.788 -15.701 1.00 54.58 ? 340 LYS A CA 1 ATOM 1568 C C . LYS A 1 208 ? 30.384 -23.646 -14.824 1.00 51.14 ? 340 LYS A C 1 ATOM 1569 O O . LYS A 1 208 ? 30.864 -23.441 -13.709 1.00 52.20 ? 340 LYS A O 1 ATOM 1570 C CB . LYS A 1 208 ? 31.805 -24.245 -16.787 1.00 59.56 ? 340 LYS A CB 1 ATOM 1571 C CG . LYS A 1 208 ? 32.972 -23.464 -16.243 1.00 66.55 ? 340 LYS A CG 1 ATOM 1572 C CD . LYS A 1 208 ? 33.916 -23.057 -17.354 1.00 78.56 ? 340 LYS A CD 1 ATOM 1573 C CE . LYS A 1 208 ? 35.108 -22.298 -16.798 1.00 86.80 ? 340 LYS A CE 1 ATOM 1574 N NZ . LYS A 1 208 ? 36.021 -21.869 -17.883 1.00 90.96 ? 340 LYS A NZ 1 ATOM 1575 N N . VAL A 1 209 ? 29.413 -22.904 -15.339 1.00 45.09 ? 341 VAL A N 1 ATOM 1576 C CA . VAL A 1 209 ? 28.852 -21.787 -14.600 1.00 42.97 ? 341 VAL A CA 1 ATOM 1577 C C . VAL A 1 209 ? 28.096 -22.291 -13.380 1.00 46.77 ? 341 VAL A C 1 ATOM 1578 O O . VAL A 1 209 ? 28.233 -21.750 -12.283 1.00 46.52 ? 341 VAL A O 1 ATOM 1579 C CB . VAL A 1 209 ? 27.896 -20.968 -15.477 1.00 41.43 ? 341 VAL A CB 1 ATOM 1580 C CG1 . VAL A 1 209 ? 27.124 -19.967 -14.619 1.00 41.40 ? 341 VAL A CG1 1 ATOM 1581 C CG2 . VAL A 1 209 ? 28.681 -20.262 -16.586 1.00 44.54 ? 341 VAL A CG2 1 ATOM 1582 N N . LEU A 1 210 ? 27.300 -23.333 -13.578 1.00 44.52 ? 342 LEU A N 1 ATOM 1583 C CA . LEU A 1 210 ? 26.506 -23.891 -12.492 1.00 50.52 ? 342 LEU A CA 1 ATOM 1584 C C . LEU A 1 210 ? 27.407 -24.407 -11.365 1.00 51.02 ? 342 LEU A C 1 ATOM 1585 O O . LEU A 1 210 ? 27.098 -24.251 -10.182 1.00 47.34 ? 342 LEU A O 1 ATOM 1586 C CB . LEU A 1 210 ? 25.598 -25.008 -13.016 1.00 49.33 ? 342 LEU A CB 1 ATOM 1587 C CG . LEU A 1 210 ? 24.492 -25.401 -12.040 1.00 52.09 ? 342 LEU A CG 1 ATOM 1588 C CD1 . LEU A 1 210 ? 23.626 -24.182 -11.722 1.00 47.60 ? 342 LEU A CD1 1 ATOM 1589 C CD2 . LEU A 1 210 ? 23.658 -26.546 -12.580 1.00 58.10 ? 342 LEU A CD2 1 ATOM 1590 N N . LYS A 1 211 ? 28.518 -25.035 -11.744 1.00 49.46 ? 343 LYS A N 1 ATOM 1591 C CA . LYS A 1 211 ? 29.541 -25.435 -10.782 1.00 53.59 ? 343 LYS A CA 1 ATOM 1592 C C . LYS A 1 211 ? 30.011 -24.231 -9.970 1.00 50.75 ? 343 LYS A C 1 ATOM 1593 O O . LYS A 1 211 ? 30.079 -24.292 -8.744 1.00 49.64 ? 343 LYS A O 1 ATOM 1594 C CB . LYS A 1 211 ? 30.727 -26.089 -11.495 1.00 61.11 ? 343 LYS A CB 1 ATOM 1595 C CG . LYS A 1 211 ? 31.824 -26.563 -10.558 1.00 71.03 ? 343 LYS A CG 1 ATOM 1596 C CD . LYS A 1 211 ? 31.267 -27.483 -9.482 1.00 79.44 ? 343 LYS A CD 1 ATOM 1597 C CE . LYS A 1 211 ? 32.379 -28.117 -8.652 1.00 86.39 ? 343 LYS A CE 1 ATOM 1598 N NZ . LYS A 1 211 ? 31.848 -28.821 -7.450 1.00 87.89 ? 343 LYS A NZ 1 ATOM 1599 N N . GLN A 1 212 ? 30.320 -23.132 -10.653 1.00 46.90 ? 344 GLN A N 1 ATOM 1600 C CA . GLN A 1 212 ? 30.761 -21.918 -9.972 1.00 44.72 ? 344 GLN A CA 1 ATOM 1601 C C . GLN A 1 212 ? 29.684 -21.361 -9.044 1.00 43.65 ? 344 GLN A C 1 ATOM 1602 O O . GLN A 1 212 ? 29.969 -20.888 -7.944 1.00 45.23 ? 344 GLN A O 1 ATOM 1603 C CB . GLN A 1 212 ? 31.165 -20.857 -10.987 1.00 44.18 ? 344 GLN A CB 1 ATOM 1604 C CG . GLN A 1 212 ? 32.463 -21.146 -11.711 1.00 51.18 ? 344 GLN A CG 1 ATOM 1605 C CD . GLN A 1 212 ? 32.690 -20.188 -12.860 1.00 57.92 ? 344 GLN A CD 1 ATOM 1606 O OE1 . GLN A 1 212 ? 31.736 -19.703 -13.464 1.00 59.88 ? 344 GLN A OE1 1 ATOM 1607 N NE2 . GLN A 1 212 ? 33.952 -19.912 -13.171 1.00 61.75 ? 344 GLN A NE2 1 ATOM 1608 N N . VAL A 1 213 ? 28.440 -21.405 -9.491 1.00 41.58 ? 345 VAL A N 1 ATOM 1609 C CA . VAL A 1 213 ? 27.351 -20.933 -8.657 1.00 42.60 ? 345 VAL A CA 1 ATOM 1610 C C . VAL A 1 213 ? 27.286 -21.785 -7.399 1.00 44.03 ? 345 VAL A C 1 ATOM 1611 O O . VAL A 1 213 ? 27.063 -21.283 -6.297 1.00 46.86 ? 345 VAL A O 1 ATOM 1612 C CB . VAL A 1 213 ? 26.025 -21.006 -9.407 1.00 38.90 ? 345 VAL A CB 1 ATOM 1613 C CG1 . VAL A 1 213 ? 24.865 -20.604 -8.483 1.00 36.06 ? 345 VAL A CG1 1 ATOM 1614 C CG2 . VAL A 1 213 ? 26.100 -20.123 -10.637 1.00 34.64 ? 345 VAL A CG2 1 ATOM 1615 N N . THR A 1 214 ? 27.496 -23.082 -7.573 1.00 41.78 ? 346 THR A N 1 ATOM 1616 C CA . THR A 1 214 ? 27.540 -23.993 -6.444 1.00 44.91 ? 346 THR A CA 1 ATOM 1617 C C . THR A 1 214 ? 28.662 -23.609 -5.476 1.00 47.69 ? 346 THR A C 1 ATOM 1618 O O . THR A 1 214 ? 28.449 -23.561 -4.265 1.00 45.61 ? 346 THR A O 1 ATOM 1619 C CB . THR A 1 214 ? 27.680 -25.451 -6.913 1.00 50.73 ? 346 THR A CB 1 ATOM 1620 O OG1 . THR A 1 214 ? 26.504 -25.817 -7.645 1.00 55.98 ? 346 THR A OG1 1 ATOM 1621 C CG2 . THR A 1 214 ? 27.850 -26.396 -5.725 1.00 53.06 ? 346 THR A CG2 1 ATOM 1622 N N . GLU A 1 215 ? 29.846 -23.319 -6.010 1.00 46.66 ? 347 GLU A N 1 ATOM 1623 C CA . GLU A 1 215 ? 30.979 -22.945 -5.168 1.00 50.29 ? 347 GLU A CA 1 ATOM 1624 C C . GLU A 1 215 ? 30.642 -21.697 -4.369 1.00 50.70 ? 347 GLU A C 1 ATOM 1625 O O . GLU A 1 215 ? 30.891 -21.617 -3.160 1.00 52.58 ? 347 GLU A O 1 ATOM 1626 C CB . GLU A 1 215 ? 32.238 -22.706 -6.007 1.00 56.76 ? 347 GLU A CB 1 ATOM 1627 C CG . GLU A 1 215 ? 32.735 -23.948 -6.725 1.00 69.43 ? 347 GLU A CG 1 ATOM 1628 C CD . GLU A 1 215 ? 32.693 -25.187 -5.839 1.00 78.09 ? 347 GLU A CD 1 ATOM 1629 O OE1 . GLU A 1 215 ? 33.460 -25.248 -4.849 1.00 79.85 ? 347 GLU A OE1 1 ATOM 1630 O OE2 . GLU A 1 215 ? 31.882 -26.095 -6.129 1.00 80.15 ? 347 GLU A OE2 1 ATOM 1631 N N . LYS A 1 216 ? 30.080 -20.716 -5.059 1.00 43.17 ? 348 LYS A N 1 ATOM 1632 C CA . LYS A 1 216 ? 29.678 -19.480 -4.418 1.00 46.86 ? 348 LYS A CA 1 ATOM 1633 C C . LYS A 1 216 ? 28.633 -19.749 -3.320 1.00 46.75 ? 348 LYS A C 1 ATOM 1634 O O . LYS A 1 216 ? 28.740 -19.223 -2.218 1.00 50.18 ? 348 LYS A O 1 ATOM 1635 C CB . LYS A 1 216 ? 29.168 -18.484 -5.468 1.00 44.14 ? 348 LYS A CB 1 ATOM 1636 C CG . LYS A 1 216 ? 28.996 -17.100 -4.937 1.00 46.46 ? 348 LYS A CG 1 ATOM 1637 C CD . LYS A 1 216 ? 30.293 -16.578 -4.342 1.00 57.61 ? 348 LYS A CD 1 ATOM 1638 C CE . LYS A 1 216 ? 29.984 -15.513 -3.308 1.00 73.69 ? 348 LYS A CE 1 ATOM 1639 N NZ . LYS A 1 216 ? 31.195 -14.916 -2.667 1.00 85.42 ? 348 LYS A NZ 1 ATOM 1640 N N . LEU A 1 217 ? 27.639 -20.587 -3.608 1.00 41.46 ? 349 LEU A N 1 ATOM 1641 C CA . LEU A 1 217 ? 26.629 -20.907 -2.602 1.00 40.42 ? 349 LEU A CA 1 ATOM 1642 C C . LEU A 1 217 ? 27.256 -21.509 -1.341 1.00 46.07 ? 349 LEU A C 1 ATOM 1643 O O . LEU A 1 217 ? 26.795 -21.257 -0.228 1.00 45.85 ? 349 LEU A O 1 ATOM 1644 C CB . LEU A 1 217 ? 25.558 -21.844 -3.163 1.00 38.91 ? 349 LEU A CB 1 ATOM 1645 C CG . LEU A 1 217 ? 24.540 -21.160 -4.077 1.00 39.34 ? 349 LEU A CG 1 ATOM 1646 C CD1 . LEU A 1 217 ? 23.614 -22.169 -4.750 1.00 44.01 ? 349 LEU A CD1 1 ATOM 1647 C CD2 . LEU A 1 217 ? 23.758 -20.143 -3.269 1.00 41.07 ? 349 LEU A CD2 1 ATOM 1648 N N . LYS A 1 218 ? 28.305 -22.303 -1.519 1.00 49.76 ? 350 LYS A N 1 ATOM 1649 C CA . LYS A 1 218 ? 28.984 -22.932 -0.383 1.00 47.24 ? 350 LYS A CA 1 ATOM 1650 C C . LYS A 1 218 ? 29.595 -21.889 0.547 1.00 48.55 ? 350 LYS A C 1 ATOM 1651 O O . LYS A 1 218 ? 29.617 -22.059 1.771 1.00 49.27 ? 350 LYS A O 1 ATOM 1652 C CB . LYS A 1 218 ? 30.067 -23.892 -0.876 1.00 48.92 ? 350 LYS A CB 1 ATOM 1653 C CG . LYS A 1 218 ? 29.546 -25.239 -1.338 1.00 51.97 ? 350 LYS A CG 1 ATOM 1654 C CD . LYS A 1 218 ? 30.670 -26.066 -1.943 1.00 59.95 ? 350 LYS A CD 1 ATOM 1655 C CE . LYS A 1 218 ? 30.193 -27.452 -2.382 1.00 69.34 ? 350 LYS A CE 1 ATOM 1656 N NZ . LYS A 1 218 ? 29.755 -28.285 -1.223 1.00 71.90 ? 350 LYS A NZ 1 ATOM 1657 N N . GLU A 1 219 ? 30.100 -20.810 -0.039 1.00 50.22 ? 351 GLU A N 1 ATOM 1658 C CA . GLU A 1 219 ? 30.728 -19.752 0.739 1.00 52.45 ? 351 GLU A CA 1 ATOM 1659 C C . GLU A 1 219 ? 29.728 -19.164 1.717 1.00 54.00 ? 351 GLU A C 1 ATOM 1660 O O . GLU A 1 219 ? 30.096 -18.675 2.787 1.00 54.62 ? 351 GLU A O 1 ATOM 1661 C CB . GLU A 1 219 ? 31.253 -18.648 -0.174 1.00 53.35 ? 351 GLU A CB 1 ATOM 1662 C CG . GLU A 1 219 ? 32.268 -19.108 -1.200 1.00 63.53 ? 351 GLU A CG 1 ATOM 1663 C CD . GLU A 1 219 ? 32.791 -17.955 -2.038 1.00 72.31 ? 351 GLU A CD 1 ATOM 1664 O OE1 . GLU A 1 219 ? 32.750 -16.805 -1.545 1.00 73.11 ? 351 GLU A OE1 1 ATOM 1665 O OE2 . GLU A 1 219 ? 33.231 -18.198 -3.185 1.00 75.91 ? 351 GLU A OE2 1 ATOM 1666 N N . HIS A 1 220 ? 28.455 -19.231 1.344 1.00 47.71 ? 352 HIS A N 1 ATOM 1667 C CA . HIS A 1 220 ? 27.391 -18.593 2.113 1.00 43.95 ? 352 HIS A CA 1 ATOM 1668 C C . HIS A 1 220 ? 26.703 -19.557 3.061 1.00 44.63 ? 352 HIS A C 1 ATOM 1669 O O . HIS A 1 220 ? 26.029 -19.140 4.000 1.00 48.53 ? 352 HIS A O 1 ATOM 1670 C CB . HIS A 1 220 ? 26.350 -17.995 1.170 1.00 43.51 ? 352 HIS A CB 1 ATOM 1671 C CG . HIS A 1 220 ? 26.752 -16.680 0.592 1.00 52.09 ? 352 HIS A CG 1 ATOM 1672 N ND1 . HIS A 1 220 ? 27.325 -16.557 -0.657 1.00 54.54 ? 352 HIS A ND1 1 ATOM 1673 C CD2 . HIS A 1 220 ? 26.670 -15.426 1.095 1.00 50.15 ? 352 HIS A CD2 1 ATOM 1674 C CE1 . HIS A 1 220 ? 27.568 -15.281 -0.902 1.00 46.55 ? 352 HIS A CE1 1 ATOM 1675 N NE2 . HIS A 1 220 ? 27.183 -14.575 0.146 1.00 50.98 ? 352 HIS A NE2 1 ATOM 1676 N N . PHE A 1 221 ? 26.868 -20.847 2.804 1.00 42.80 ? 353 PHE A N 1 ATOM 1677 C CA . PHE A 1 221 ? 26.172 -21.862 3.576 1.00 46.66 ? 353 PHE A CA 1 ATOM 1678 C C . PHE A 1 221 ? 27.144 -22.814 4.255 1.00 50.64 ? 353 PHE A C 1 ATOM 1679 O O . PHE A 1 221 ? 26.979 -24.031 4.219 1.00 49.88 ? 353 PHE A O 1 ATOM 1680 C CB . PHE A 1 221 ? 25.144 -22.599 2.698 1.00 45.14 ? 353 PHE A CB 1 ATOM 1681 C CG . PHE A 1 221 ? 23.936 -21.762 2.378 1.00 41.84 ? 353 PHE A CG 1 ATOM 1682 C CD1 . PHE A 1 221 ? 22.917 -21.615 3.305 1.00 49.14 ? 353 PHE A CD1 1 ATOM 1683 C CD2 . PHE A 1 221 ? 23.847 -21.070 1.181 1.00 42.86 ? 353 PHE A CD2 1 ATOM 1684 C CE1 . PHE A 1 221 ? 21.818 -20.826 3.032 1.00 47.77 ? 353 PHE A CE1 1 ATOM 1685 C CE2 . PHE A 1 221 ? 22.743 -20.285 0.899 1.00 42.16 ? 353 PHE A CE2 1 ATOM 1686 C CZ . PHE A 1 221 ? 21.732 -20.169 1.831 1.00 46.19 ? 353 PHE A CZ 1 ATOM 1687 N N . ASN A 1 222 ? 28.161 -22.228 4.877 1.00 53.37 ? 354 ASN A N 1 ATOM 1688 C CA . ASN A 1 222 ? 29.113 -22.969 5.687 1.00 49.40 ? 354 ASN A CA 1 ATOM 1689 C C . ASN A 1 222 ? 29.624 -24.261 5.037 1.00 52.86 ? 354 ASN A C 1 ATOM 1690 O O . ASN A 1 222 ? 29.771 -25.282 5.709 1.00 51.97 ? 354 ASN A O 1 ATOM 1691 C CB . ASN A 1 222 ? 28.504 -23.279 7.051 1.00 51.95 ? 354 ASN A CB 1 ATOM 1692 C CG . ASN A 1 222 ? 29.557 -23.516 8.105 1.00 56.27 ? 354 ASN A CG 1 ATOM 1693 O OD1 . ASN A 1 222 ? 30.635 -22.930 8.046 1.00 60.47 ? 354 ASN A OD1 1 ATOM 1694 N ND2 . ASN A 1 222 ? 29.259 -24.381 9.070 1.00 55.73 ? 354 ASN A ND2 1 ATOM 1695 N N . ASN A 1 223 ? 29.881 -24.201 3.732 1.00 56.53 ? 355 ASN A N 1 ATOM 1696 C CA . ASN A 1 223 ? 30.430 -25.320 2.966 1.00 61.62 ? 355 ASN A CA 1 ATOM 1697 C C . ASN A 1 223 ? 29.558 -26.584 3.004 1.00 57.55 ? 355 ASN A C 1 ATOM 1698 O O . ASN A 1 223 ? 30.046 -27.696 2.792 1.00 58.37 ? 355 ASN A O 1 ATOM 1699 C CB . ASN A 1 223 ? 31.871 -25.623 3.407 1.00 71.82 ? 355 ASN A CB 1 ATOM 1700 C CG . ASN A 1 223 ? 32.647 -26.430 2.372 1.00 84.50 ? 355 ASN A CG 1 ATOM 1701 O OD1 . ASN A 1 223 ? 32.265 -26.489 1.202 1.00 85.75 ? 355 ASN A OD1 1 ATOM 1702 N ND2 . ASN A 1 223 ? 33.744 -27.055 2.803 1.00 92.06 ? 355 ASN A ND2 1 ATOM 1703 N N . LYS A 1 224 ? 28.268 -26.413 3.277 1.00 55.64 ? 357 LYS A N 1 ATOM 1704 C CA . LYS A 1 224 ? 27.350 -27.546 3.265 1.00 56.72 ? 357 LYS A CA 1 ATOM 1705 C C . LYS A 1 224 ? 27.240 -28.073 1.840 1.00 56.34 ? 357 LYS A C 1 ATOM 1706 O O . LYS A 1 224 ? 27.633 -27.395 0.894 1.00 53.19 ? 357 LYS A O 1 ATOM 1707 C CB . LYS A 1 224 ? 25.973 -27.150 3.806 1.00 56.61 ? 357 LYS A CB 1 ATOM 1708 C CG . LYS A 1 224 ? 25.966 -26.768 5.289 1.00 62.37 ? 357 LYS A CG 1 ATOM 1709 C CD . LYS A 1 224 ? 24.544 -26.606 5.845 1.00 66.87 ? 357 LYS A CD 1 ATOM 1710 C CE . LYS A 1 224 ? 23.736 -27.906 5.728 1.00 68.22 ? 357 LYS A CE 1 ATOM 1711 N NZ . LYS A 1 224 ? 22.366 -27.802 6.320 1.00 65.25 ? 357 LYS A NZ 1 ATOM 1712 N N . THR A 1 225 ? 26.727 -29.287 1.681 1.00 58.09 ? 358 THR A N 1 ATOM 1713 C CA . THR A 1 225 ? 26.561 -29.841 0.342 1.00 56.67 ? 358 THR A CA 1 ATOM 1714 C C . THR A 1 225 ? 25.421 -29.118 -0.382 1.00 55.50 ? 358 THR A C 1 ATOM 1715 O O . THR A 1 225 ? 24.353 -28.899 0.185 1.00 55.02 ? 358 THR A O 1 ATOM 1716 C CB . THR A 1 225 ? 26.306 -31.356 0.384 1.00 62.58 ? 358 THR A CB 1 ATOM 1717 O OG1 . THR A 1 225 ? 27.452 -32.018 0.939 1.00 65.79 ? 358 THR A OG1 1 ATOM 1718 C CG2 . THR A 1 225 ? 26.038 -31.897 -1.008 1.00 61.08 ? 358 THR A CG2 1 ATOM 1719 N N . ILE A 1 226 ? 25.659 -28.738 -1.631 1.00 51.13 ? 359 ILE A N 1 ATOM 1720 C CA . ILE A 1 226 ? 24.668 -27.985 -2.394 1.00 51.49 ? 359 ILE A CA 1 ATOM 1721 C C . ILE A 1 226 ? 23.962 -28.892 -3.383 1.00 54.11 ? 359 ILE A C 1 ATOM 1722 O O . ILE A 1 226 ? 24.598 -29.494 -4.256 1.00 56.04 ? 359 ILE A O 1 ATOM 1723 C CB . ILE A 1 226 ? 25.313 -26.848 -3.187 1.00 45.96 ? 359 ILE A CB 1 ATOM 1724 C CG1 . ILE A 1 226 ? 26.142 -25.955 -2.256 1.00 52.94 ? 359 ILE A CG1 1 ATOM 1725 C CG2 . ILE A 1 226 ? 24.244 -26.066 -3.991 1.00 41.41 ? 359 ILE A CG2 1 ATOM 1726 C CD1 . ILE A 1 226 ? 25.387 -25.453 -1.034 1.00 52.04 ? 359 ILE A CD1 1 ATOM 1727 N N . ILE A 1 227 ? 22.647 -28.993 -3.246 1.00 44.93 ? 360 ILE A N 1 ATOM 1728 C CA . ILE A 1 227 ? 21.878 -29.864 -4.130 1.00 50.12 ? 360 ILE A CA 1 ATOM 1729 C C . ILE A 1 227 ? 20.804 -29.083 -4.874 1.00 48.80 ? 360 ILE A C 1 ATOM 1730 O O . ILE A 1 227 ? 20.082 -28.295 -4.273 1.00 50.43 ? 360 ILE A O 1 ATOM 1731 C CB . ILE A 1 227 ? 21.212 -31.009 -3.356 1.00 54.26 ? 360 ILE A CB 1 ATOM 1732 C CG1 . ILE A 1 227 ? 22.231 -31.700 -2.438 1.00 59.06 ? 360 ILE A CG1 1 ATOM 1733 C CG2 . ILE A 1 227 ? 20.579 -32.004 -4.322 1.00 51.98 ? 360 ILE A CG2 1 ATOM 1734 C CD1 . ILE A 1 227 ? 21.618 -32.725 -1.512 1.00 61.23 ? 360 ILE A CD1 1 ATOM 1735 N N . PHE A 1 228 ? 20.713 -29.299 -6.183 1.00 47.69 ? 361 PHE A N 1 ATOM 1736 C CA . PHE A 1 228 ? 19.627 -28.729 -6.980 1.00 49.79 ? 361 PHE A CA 1 ATOM 1737 C C . PHE A 1 228 ? 18.516 -29.749 -7.196 1.00 50.87 ? 361 PHE A C 1 ATOM 1738 O O . PHE A 1 228 ? 18.776 -30.933 -7.416 1.00 49.02 ? 361 PHE A O 1 ATOM 1739 C CB . PHE A 1 228 ? 20.137 -28.212 -8.326 1.00 43.40 ? 361 PHE A CB 1 ATOM 1740 C CG . PHE A 1 228 ? 21.037 -27.020 -8.211 1.00 46.34 ? 361 PHE A CG 1 ATOM 1741 C CD1 . PHE A 1 228 ? 20.514 -25.762 -7.951 1.00 44.51 ? 361 PHE A CD1 1 ATOM 1742 C CD2 . PHE A 1 228 ? 22.408 -27.155 -8.337 1.00 54.87 ? 361 PHE A CD2 1 ATOM 1743 C CE1 . PHE A 1 228 ? 21.343 -24.662 -7.839 1.00 50.11 ? 361 PHE A CE1 1 ATOM 1744 C CE2 . PHE A 1 228 ? 23.241 -26.057 -8.220 1.00 54.34 ? 361 PHE A CE2 1 ATOM 1745 C CZ . PHE A 1 228 ? 22.709 -24.811 -7.968 1.00 52.14 ? 361 PHE A CZ 1 ATOM 1746 N N . GLN A 1 229 ? 17.276 -29.284 -7.114 1.00 49.19 ? 362 GLN A N 1 ATOM 1747 C CA . GLN A 1 229 ? 16.116 -30.130 -7.379 1.00 46.35 ? 362 GLN A CA 1 ATOM 1748 C C . GLN A 1 229 ? 15.142 -29.353 -8.248 1.00 49.44 ? 362 GLN A C 1 ATOM 1749 O O . GLN A 1 229 ? 15.195 -28.122 -8.287 1.00 47.13 ? 362 GLN A O 1 ATOM 1750 C CB . GLN A 1 229 ? 15.437 -30.520 -6.070 1.00 44.58 ? 362 GLN A CB 1 ATOM 1751 C CG . GLN A 1 229 ? 16.163 -31.622 -5.298 1.00 52.57 ? 362 GLN A CG 1 ATOM 1752 C CD . GLN A 1 229 ? 16.004 -32.977 -5.959 1.00 59.61 ? 362 GLN A CD 1 ATOM 1753 O OE1 . GLN A 1 229 ? 16.729 -33.317 -6.896 1.00 58.15 ? 362 GLN A OE1 1 ATOM 1754 N NE2 . GLN A 1 229 ? 15.036 -33.750 -5.486 1.00 63.30 ? 362 GLN A NE2 1 ATOM 1755 N N . PRO A 1 230 ? 14.252 -30.063 -8.953 1.00 55.41 ? 363 PRO A N 1 ATOM 1756 C CA . PRO A 1 230 ? 13.231 -29.363 -9.734 1.00 52.66 ? 363 PRO A CA 1 ATOM 1757 C C . PRO A 1 230 ? 12.240 -28.737 -8.775 1.00 50.45 ? 363 PRO A C 1 ATOM 1758 O O . PRO A 1 230 ? 12.069 -29.242 -7.669 1.00 49.87 ? 363 PRO A O 1 ATOM 1759 C CB . PRO A 1 230 ? 12.564 -30.489 -10.531 1.00 49.52 ? 363 PRO A CB 1 ATOM 1760 C CG . PRO A 1 230 ? 12.748 -31.700 -9.679 1.00 60.78 ? 363 PRO A CG 1 ATOM 1761 C CD . PRO A 1 230 ? 14.092 -31.527 -9.011 1.00 62.05 ? 363 PRO A CD 1 ATOM 1762 N N . PRO A 1 231 ? 11.609 -27.633 -9.183 1.00 45.48 ? 364 PRO A N 1 ATOM 1763 C CA . PRO A 1 231 ? 10.593 -26.975 -8.355 1.00 46.80 ? 364 PRO A CA 1 ATOM 1764 C C . PRO A 1 231 ? 9.647 -28.011 -7.742 1.00 57.75 ? 364 PRO A C 1 ATOM 1765 O O . PRO A 1 231 ? 9.301 -28.995 -8.403 1.00 59.30 ? 364 PRO A O 1 ATOM 1766 C CB . PRO A 1 231 ? 9.858 -26.099 -9.363 1.00 44.14 ? 364 PRO A CB 1 ATOM 1767 C CG . PRO A 1 231 ? 10.935 -25.764 -10.376 1.00 39.41 ? 364 PRO A CG 1 ATOM 1768 C CD . PRO A 1 231 ? 11.769 -26.986 -10.499 1.00 36.95 ? 364 PRO A CD 1 ATOM 1769 N N . SER A 1 232 ? 9.243 -27.792 -6.493 1.00 62.26 ? 365 SER A N 1 ATOM 1770 C CA . SER A 1 232 ? 8.450 -28.770 -5.747 1.00 69.81 ? 365 SER A CA 1 ATOM 1771 C C . SER A 1 232 ? 7.060 -28.985 -6.343 1.00 68.44 ? 365 SER A C 1 ATOM 1772 O O . SER A 1 232 ? 6.519 -30.089 -6.297 1.00 72.64 ? 365 SER A O 1 ATOM 1773 C CB . SER A 1 232 ? 8.332 -28.352 -4.276 1.00 72.29 ? 365 SER A CB 1 ATOM 1774 O OG . SER A 1 232 ? 7.825 -27.030 -4.155 1.00 74.30 ? 365 SER A OG 1 ATOM 1775 N N . GLY A 1 233 ? 6.493 -27.922 -6.902 1.00 60.54 ? 366 GLY A N 1 ATOM 1776 C CA . GLY A 1 233 ? 5.153 -27.952 -7.458 1.00 57.52 ? 366 GLY A CA 1 ATOM 1777 C C . GLY A 1 233 ? 4.738 -26.518 -7.720 1.00 58.16 ? 366 GLY A C 1 ATOM 1778 O O . GLY A 1 233 ? 5.529 -25.601 -7.504 1.00 55.17 ? 366 GLY A O 1 ATOM 1779 N N . GLY A 1 234 ? 3.508 -26.319 -8.186 1.00 56.67 ? 367 GLY A N 1 ATOM 1780 C CA . GLY A 1 234 ? 3.008 -24.986 -8.475 1.00 52.90 ? 367 GLY A CA 1 ATOM 1781 C C . GLY A 1 234 ? 2.515 -24.840 -9.906 1.00 47.09 ? 367 GLY A C 1 ATOM 1782 O O . GLY A 1 234 ? 2.416 -25.819 -10.648 1.00 45.50 ? 367 GLY A O 1 ATOM 1783 N N . ASP A 1 235 ? 2.189 -23.612 -10.295 1.00 41.59 ? 368 ASP A N 1 ATOM 1784 C CA . ASP A 1 235 ? 1.763 -23.346 -11.662 1.00 42.94 ? 368 ASP A CA 1 ATOM 1785 C C . ASP A 1 235 ? 2.934 -23.536 -12.616 1.00 39.60 ? 368 ASP A C 1 ATOM 1786 O O . ASP A 1 235 ? 4.098 -23.385 -12.222 1.00 32.43 ? 368 ASP A O 1 ATOM 1787 C CB . ASP A 1 235 ? 1.237 -21.918 -11.808 1.00 50.80 ? 368 ASP A CB 1 ATOM 1788 C CG . ASP A 1 235 ? -0.037 -21.666 -11.018 1.00 52.66 ? 368 ASP A CG 1 ATOM 1789 O OD1 . ASP A 1 235 ? -0.860 -22.597 -10.857 1.00 51.68 ? 368 ASP A OD1 1 ATOM 1790 O OD2 . ASP A 1 235 ? -0.213 -20.513 -10.590 1.00 52.11 ? 368 ASP A OD2 1 ATOM 1791 N N . LEU A 1 236 ? 2.611 -23.837 -13.874 1.00 32.33 ? 369 LEU A N 1 ATOM 1792 C CA . LEU A 1 236 ? 3.608 -24.073 -14.921 1.00 33.19 ? 369 LEU A CA 1 ATOM 1793 C C . LEU A 1 236 ? 4.525 -22.879 -15.171 1.00 34.88 ? 369 LEU A C 1 ATOM 1794 O O . LEU A 1 236 ? 5.671 -23.052 -15.592 1.00 33.82 ? 369 LEU A O 1 ATOM 1795 C CB . LEU A 1 236 ? 2.919 -24.455 -16.239 1.00 34.78 ? 369 LEU A CB 1 ATOM 1796 C CG . LEU A 1 236 ? 2.195 -25.804 -16.279 1.00 35.86 ? 369 LEU A CG 1 ATOM 1797 C CD1 . LEU A 1 236 ? 1.384 -25.964 -17.575 1.00 35.46 ? 369 LEU A CD1 1 ATOM 1798 C CD2 . LEU A 1 236 ? 3.195 -26.943 -16.103 1.00 41.35 ? 369 LEU A CD2 1 ATOM 1799 N N . GLU A 1 237 ? 4.009 -21.675 -14.933 1.00 32.61 ? 370 GLU A N 1 ATOM 1800 C CA . GLU A 1 237 ? 4.802 -20.461 -15.108 1.00 35.39 ? 370 GLU A CA 1 ATOM 1801 C C . GLU A 1 237 ? 5.984 -20.444 -14.128 1.00 33.67 ? 370 GLU A C 1 ATOM 1802 O O . GLU A 1 237 ? 7.000 -19.805 -14.379 1.00 33.99 ? 370 GLU A O 1 ATOM 1803 C CB . GLU A 1 237 ? 3.943 -19.207 -14.928 1.00 33.69 ? 370 GLU A CB 1 ATOM 1804 C CG . GLU A 1 237 ? 2.936 -18.971 -16.054 1.00 33.40 ? 370 GLU A CG 1 ATOM 1805 C CD . GLU A 1 237 ? 1.703 -19.852 -15.943 1.00 34.84 ? 370 GLU A CD 1 ATOM 1806 O OE1 . GLU A 1 237 ? 1.449 -20.380 -14.833 1.00 39.79 ? 370 GLU A OE1 1 ATOM 1807 O OE2 . GLU A 1 237 ? 0.990 -20.016 -16.967 1.00 32.19 ? 370 GLU A OE2 1 ATOM 1808 N N . ILE A 1 238 ? 5.864 -21.162 -13.021 1.00 34.12 ? 371 ILE A N 1 ATOM 1809 C CA . ILE A 1 238 ? 6.971 -21.184 -12.067 1.00 39.91 ? 371 ILE A CA 1 ATOM 1810 C C . ILE A 1 238 ? 7.758 -22.486 -12.099 1.00 38.69 ? 371 ILE A C 1 ATOM 1811 O O . ILE A 1 238 ? 8.971 -22.476 -11.896 1.00 41.96 ? 371 ILE A O 1 ATOM 1812 C CB . ILE A 1 238 ? 6.527 -20.810 -10.634 1.00 51.66 ? 371 ILE A CB 1 ATOM 1813 C CG1 . ILE A 1 238 ? 5.558 -21.840 -10.078 1.00 58.91 ? 371 ILE A CG1 1 ATOM 1814 C CG2 . ILE A 1 238 ? 5.892 -19.422 -10.623 1.00 57.13 ? 371 ILE A CG2 1 ATOM 1815 C CD1 . ILE A 1 238 ? 5.044 -21.495 -8.708 1.00 70.47 ? 371 ILE A CD1 1 ATOM 1816 N N . THR A 1 239 ? 7.089 -23.605 -12.370 1.00 37.94 ? 372 THR A N 1 ATOM 1817 C CA . THR A 1 239 ? 7.802 -24.886 -12.391 1.00 36.72 ? 372 THR A CA 1 ATOM 1818 C C . THR A 1 239 ? 8.625 -25.010 -13.668 1.00 32.79 ? 372 THR A C 1 ATOM 1819 O O . THR A 1 239 ? 9.552 -25.799 -13.732 1.00 32.83 ? 372 THR A O 1 ATOM 1820 C CB . THR A 1 239 ? 6.877 -26.106 -12.241 1.00 37.97 ? 372 THR A CB 1 ATOM 1821 O OG1 . THR A 1 239 ? 5.958 -26.162 -13.345 1.00 36.85 ? 372 THR A OG1 1 ATOM 1822 C CG2 . THR A 1 239 ? 6.106 -26.035 -10.912 1.00 38.93 ? 372 THR A CG2 1 ATOM 1823 N N . MET A 1 240 ? 8.284 -24.212 -14.677 1.00 33.80 ? 373 MET A N 1 ATOM 1824 C CA . MET A 1 240 ? 9.056 -24.175 -15.906 1.00 32.22 ? 373 MET A CA 1 ATOM 1825 C C . MET A 1 240 ? 9.649 -22.794 -16.122 1.00 32.53 ? 373 MET A C 1 ATOM 1826 O O . MET A 1 240 ? 9.165 -21.811 -15.571 1.00 30.41 ? 373 MET A O 1 ATOM 1827 C CB . MET A 1 240 ? 8.174 -24.560 -17.092 1.00 31.04 ? 373 MET A CB 1 ATOM 1828 C CG . MET A 1 240 ? 7.610 -25.966 -16.924 1.00 39.75 ? 373 MET A CG 1 ATOM 1829 S SD . MET A 1 240 ? 6.536 -26.463 -18.267 1.00 47.15 ? 373 MET A SD 1 ATOM 1830 C CE . MET A 1 240 ? 7.758 -26.933 -19.494 1.00 46.80 ? 373 MET A CE 1 ATOM 1831 N N . HIS A 1 241 ? 10.703 -22.740 -16.929 1.00 31.64 ? 374 HIS A N 1 ATOM 1832 C CA . HIS A 1 241 ? 11.250 -21.480 -17.386 1.00 29.22 ? 374 HIS A CA 1 ATOM 1833 C C . HIS A 1 241 ? 10.234 -20.882 -18.350 1.00 32.50 ? 374 HIS A C 1 ATOM 1834 O O . HIS A 1 241 ? 10.022 -21.410 -19.434 1.00 33.54 ? 374 HIS A O 1 ATOM 1835 C CB . HIS A 1 241 ? 12.582 -21.696 -18.117 1.00 30.77 ? 374 HIS A CB 1 ATOM 1836 C CG . HIS A 1 241 ? 13.130 -20.446 -18.733 1.00 27.87 ? 374 HIS A CG 1 ATOM 1837 N ND1 . HIS A 1 241 ? 13.776 -20.429 -19.956 1.00 33.79 ? 374 HIS A ND1 1 ATOM 1838 C CD2 . HIS A 1 241 ? 13.122 -19.165 -18.298 1.00 22.92 ? 374 HIS A CD2 1 ATOM 1839 C CE1 . HIS A 1 241 ? 14.146 -19.192 -20.240 1.00 25.72 ? 374 HIS A CE1 1 ATOM 1840 N NE2 . HIS A 1 241 ? 13.758 -18.406 -19.250 1.00 31.13 ? 374 HIS A NE2 1 ATOM 1841 N N . HIS A 1 242 ? 9.614 -19.779 -17.943 1.00 28.06 ? 375 HIS A N 1 ATOM 1842 C CA . HIS A 1 242 ? 8.527 -19.189 -18.700 1.00 27.05 ? 375 HIS A CA 1 ATOM 1843 C C . HIS A 1 242 ? 9.008 -17.851 -19.226 1.00 32.23 ? 375 HIS A C 1 ATOM 1844 O O . HIS A 1 242 ? 9.606 -17.063 -18.481 1.00 31.75 ? 375 HIS A O 1 ATOM 1845 C CB . HIS A 1 242 ? 7.323 -18.971 -17.790 1.00 27.15 ? 375 HIS A CB 1 ATOM 1846 C CG . HIS A 1 242 ? 6.142 -18.351 -18.475 1.00 31.19 ? 375 HIS A CG 1 ATOM 1847 N ND1 . HIS A 1 242 ? 5.519 -17.214 -18.002 1.00 35.56 ? 375 HIS A ND1 1 ATOM 1848 C CD2 . HIS A 1 242 ? 5.451 -18.732 -19.578 1.00 26.24 ? 375 HIS A CD2 1 ATOM 1849 C CE1 . HIS A 1 242 ? 4.498 -16.914 -18.792 1.00 30.04 ? 375 HIS A CE1 1 ATOM 1850 N NE2 . HIS A 1 242 ? 4.432 -17.823 -19.750 1.00 35.59 ? 375 HIS A NE2 1 ATOM 1851 N N . PHE A 1 243 ? 8.748 -17.597 -20.504 1.00 30.94 ? 376 PHE A N 1 ATOM 1852 C CA . PHE A 1 243 ? 9.142 -16.341 -21.131 1.00 30.34 ? 376 PHE A CA 1 ATOM 1853 C C . PHE A 1 243 ? 8.326 -16.115 -22.389 1.00 31.73 ? 376 PHE A C 1 ATOM 1854 O O . PHE A 1 243 ? 7.599 -16.997 -22.847 1.00 28.75 ? 376 PHE A O 1 ATOM 1855 C CB . PHE A 1 243 ? 10.632 -16.324 -21.475 1.00 28.74 ? 376 PHE A CB 1 ATOM 1856 C CG . PHE A 1 243 ? 11.056 -17.454 -22.349 1.00 28.31 ? 376 PHE A CG 1 ATOM 1857 C CD1 . PHE A 1 243 ? 11.255 -18.716 -21.812 1.00 30.49 ? 376 PHE A CD1 1 ATOM 1858 C CD2 . PHE A 1 243 ? 11.227 -17.270 -23.716 1.00 34.53 ? 376 PHE A CD2 1 ATOM 1859 C CE1 . PHE A 1 243 ? 11.642 -19.792 -22.631 1.00 33.49 ? 376 PHE A CE1 1 ATOM 1860 C CE2 . PHE A 1 243 ? 11.616 -18.333 -24.537 1.00 36.62 ? 376 PHE A CE2 1 ATOM 1861 C CZ . PHE A 1 243 ? 11.825 -19.585 -23.993 1.00 36.40 ? 376 PHE A CZ 1 ATOM 1862 N N . ASN A 1 244 ? 8.448 -14.915 -22.938 1.00 30.57 ? 377 ASN A N 1 ATOM 1863 C CA . ASN A 1 244 ? 7.761 -14.596 -24.169 1.00 25.92 ? 377 ASN A CA 1 ATOM 1864 C C . ASN A 1 244 ? 8.769 -14.358 -25.288 1.00 35.14 ? 377 ASN A C 1 ATOM 1865 O O . ASN A 1 244 ? 9.692 -13.559 -25.148 1.00 33.64 ? 377 ASN A O 1 ATOM 1866 C CB . ASN A 1 244 ? 6.855 -13.383 -23.973 1.00 30.02 ? 377 ASN A CB 1 ATOM 1867 C CG . ASN A 1 244 ? 5.931 -13.189 -25.130 1.00 30.35 ? 377 ASN A CG 1 ATOM 1868 O OD1 . ASN A 1 244 ? 6.388 -12.943 -26.233 1.00 30.87 ? 377 ASN A OD1 1 ATOM 1869 N ND2 . ASN A 1 244 ? 4.627 -13.345 -24.898 1.00 31.69 ? 377 ASN A ND2 1 ATOM 1870 N N . CYS A 1 245 ? 8.594 -15.083 -26.387 1.00 31.59 ? 378 CYS A N 1 ATOM 1871 C CA . CYS A 1 245 ? 9.471 -14.970 -27.549 1.00 31.84 ? 378 CYS A CA 1 ATOM 1872 C C . CYS A 1 245 ? 8.636 -14.618 -28.789 1.00 31.05 ? 378 CYS A C 1 ATOM 1873 O O . CYS A 1 245 ? 7.762 -15.390 -29.197 1.00 31.08 ? 378 CYS A O 1 ATOM 1874 C CB . CYS A 1 245 ? 10.216 -16.292 -27.756 1.00 31.32 ? 378 CYS A CB 1 ATOM 1875 S SG . CYS A 1 245 ? 11.217 -16.415 -29.270 1.00 39.16 ? 378 CYS A SG 1 ATOM 1876 N N . ARG A 1 246 ? 8.901 -13.449 -29.371 1.00 30.29 ? 379 ARG A N 1 ATOM 1877 C CA . ARG A 1 246 ? 8.175 -12.966 -30.552 1.00 29.94 ? 379 ARG A CA 1 ATOM 1878 C C . ARG A 1 246 ? 6.682 -12.998 -30.333 1.00 34.77 ? 379 ARG A C 1 ATOM 1879 O O . ARG A 1 246 ? 5.934 -13.252 -31.279 1.00 35.42 ? 379 ARG A O 1 ATOM 1880 C CB . ARG A 1 246 ? 8.485 -13.781 -31.821 1.00 35.75 ? 379 ARG A CB 1 ATOM 1881 C CG . ARG A 1 246 ? 9.946 -14.112 -32.041 1.00 47.45 ? 379 ARG A CG 1 ATOM 1882 C CD . ARG A 1 246 ? 10.811 -12.878 -32.159 1.00 55.11 ? 379 ARG A CD 1 ATOM 1883 N NE . ARG A 1 246 ? 12.230 -13.238 -32.166 1.00 62.71 ? 379 ARG A NE 1 ATOM 1884 C CZ . ARG A 1 246 ? 13.239 -12.369 -32.132 1.00 63.98 ? 379 ARG A CZ 1 ATOM 1885 N NH1 . ARG A 1 246 ? 13.010 -11.058 -32.094 1.00 58.66 ? 379 ARG A NH1 1 ATOM 1886 N NH2 . ARG A 1 246 ? 14.484 -12.821 -32.138 1.00 65.13 ? 379 ARG A NH2 1 ATOM 1887 N N . GLY A 1 247 ? 6.261 -12.759 -29.090 1.00 33.82 ? 380 GLY A N 1 ATOM 1888 C CA . GLY A 1 247 ? 4.857 -12.641 -28.754 1.00 34.78 ? 380 GLY A CA 1 ATOM 1889 C C . GLY A 1 247 ? 4.243 -13.935 -28.255 1.00 30.05 ? 380 GLY A C 1 ATOM 1890 O O . GLY A 1 247 ? 3.131 -13.935 -27.726 1.00 31.66 ? 380 GLY A O 1 ATOM 1891 N N . GLU A 1 248 ? 4.974 -15.030 -28.435 1.00 29.95 ? 381 GLU A N 1 ATOM 1892 C CA . GLU A 1 248 ? 4.510 -16.368 -28.070 1.00 29.91 ? 381 GLU A CA 1 ATOM 1893 C C . GLU A 1 248 ? 5.008 -16.747 -26.674 1.00 31.34 ? 381 GLU A C 1 ATOM 1894 O O . GLU A 1 248 ? 6.177 -16.524 -26.342 1.00 28.38 ? 381 GLU A O 1 ATOM 1895 C CB . GLU A 1 248 ? 5.005 -17.399 -29.097 1.00 27.53 ? 381 GLU A CB 1 ATOM 1896 C CG . GLU A 1 248 ? 4.743 -17.028 -30.587 1.00 32.65 ? 381 GLU A CG 1 ATOM 1897 C CD . GLU A 1 248 ? 3.266 -17.063 -30.955 1.00 35.96 ? 381 GLU A CD 1 ATOM 1898 O OE1 . GLU A 1 248 ? 2.484 -17.702 -30.217 1.00 38.52 ? 381 GLU A OE1 1 ATOM 1899 O OE2 . GLU A 1 248 ? 2.879 -16.469 -31.990 1.00 36.24 ? 381 GLU A OE2 1 ATOM 1900 N N . PHE A 1 249 ? 4.124 -17.338 -25.871 1.00 29.65 ? 382 PHE A N 1 ATOM 1901 C CA . PHE A 1 249 ? 4.448 -17.730 -24.491 1.00 31.10 ? 382 PHE A CA 1 ATOM 1902 C C . PHE A 1 249 ? 5.082 -19.121 -24.414 1.00 31.13 ? 382 PHE A C 1 ATOM 1903 O O . PHE A 1 249 ? 4.422 -20.123 -24.662 1.00 29.31 ? 382 PHE A O 1 ATOM 1904 C CB . PHE A 1 249 ? 3.177 -17.682 -23.642 1.00 29.55 ? 382 PHE A CB 1 ATOM 1905 C CG . PHE A 1 249 ? 2.674 -16.294 -23.424 1.00 30.20 ? 382 PHE A CG 1 ATOM 1906 C CD1 . PHE A 1 249 ? 3.175 -15.523 -22.388 1.00 31.51 ? 382 PHE A CD1 1 ATOM 1907 C CD2 . PHE A 1 249 ? 1.741 -15.736 -24.289 1.00 31.56 ? 382 PHE A CD2 1 ATOM 1908 C CE1 . PHE A 1 249 ? 2.731 -14.224 -22.191 1.00 30.13 ? 382 PHE A CE1 1 ATOM 1909 C CE2 . PHE A 1 249 ? 1.303 -14.444 -24.106 1.00 32.36 ? 382 PHE A CE2 1 ATOM 1910 C CZ . PHE A 1 249 ? 1.797 -13.685 -23.049 1.00 27.81 ? 382 PHE A CZ 1 ATOM 1911 N N . PHE A 1 250 ? 6.360 -19.168 -24.053 1.00 29.63 ? 383 PHE A N 1 ATOM 1912 C CA . PHE A 1 250 ? 7.110 -20.408 -24.014 1.00 28.08 ? 383 PHE A CA 1 ATOM 1913 C C . PHE A 1 250 ? 7.166 -20.907 -22.584 1.00 32.86 ? 383 PHE A C 1 ATOM 1914 O O . PHE A 1 250 ? 7.290 -20.124 -21.638 1.00 31.85 ? 383 PHE A O 1 ATOM 1915 C CB . PHE A 1 250 ? 8.563 -20.209 -24.501 1.00 29.04 ? 383 PHE A CB 1 ATOM 1916 C CG . PHE A 1 250 ? 8.737 -20.235 -25.993 1.00 36.98 ? 383 PHE A CG 1 ATOM 1917 C CD1 . PHE A 1 250 ? 9.538 -21.204 -26.590 1.00 40.60 ? 383 PHE A CD1 1 ATOM 1918 C CD2 . PHE A 1 250 ? 8.126 -19.288 -26.803 1.00 36.25 ? 383 PHE A CD2 1 ATOM 1919 C CE1 . PHE A 1 250 ? 9.730 -21.224 -27.975 1.00 40.40 ? 383 PHE A CE1 1 ATOM 1920 C CE2 . PHE A 1 250 ? 8.305 -19.319 -28.202 1.00 32.37 ? 383 PHE A CE2 1 ATOM 1921 C CZ . PHE A 1 250 ? 9.108 -20.280 -28.771 1.00 33.45 ? 383 PHE A CZ 1 ATOM 1922 N N . TYR A 1 251 ? 7.103 -22.225 -22.443 1.00 32.70 ? 384 TYR A N 1 ATOM 1923 C CA . TYR A 1 251 ? 7.267 -22.885 -21.162 1.00 32.74 ? 384 TYR A CA 1 ATOM 1924 C C . TYR A 1 251 ? 8.279 -23.993 -21.374 1.00 32.69 ? 384 TYR A C 1 ATOM 1925 O O . TYR A 1 251 ? 8.026 -24.926 -22.139 1.00 32.65 ? 384 TYR A O 1 ATOM 1926 C CB . TYR A 1 251 ? 5.945 -23.500 -20.722 1.00 31.01 ? 384 TYR A CB 1 ATOM 1927 C CG . TYR A 1 251 ? 4.881 -22.489 -20.344 1.00 33.06 ? 384 TYR A CG 1 ATOM 1928 C CD1 . TYR A 1 251 ? 4.443 -22.378 -19.020 1.00 32.11 ? 384 TYR A CD1 1 ATOM 1929 C CD2 . TYR A 1 251 ? 4.305 -21.658 -21.310 1.00 29.17 ? 384 TYR A CD2 1 ATOM 1930 C CE1 . TYR A 1 251 ? 3.467 -21.474 -18.671 1.00 33.65 ? 384 TYR A CE1 1 ATOM 1931 C CE2 . TYR A 1 251 ? 3.328 -20.757 -20.976 1.00 30.80 ? 384 TYR A CE2 1 ATOM 1932 C CZ . TYR A 1 251 ? 2.902 -20.671 -19.661 1.00 28.72 ? 384 TYR A CZ 1 ATOM 1933 O OH . TYR A 1 251 ? 1.936 -19.765 -19.313 1.00 32.15 ? 384 TYR A OH 1 ATOM 1934 N N . CYS A 1 252 ? 9.427 -23.896 -20.720 1.00 32.58 ? 385 CYS A N 1 ATOM 1935 C CA . CYS A 1 252 ? 10.497 -24.842 -20.995 1.00 33.31 ? 385 CYS A CA 1 ATOM 1936 C C . CYS A 1 252 ? 10.853 -25.583 -19.737 1.00 35.00 ? 385 CYS A C 1 ATOM 1937 O O . CYS A 1 252 ? 10.971 -24.989 -18.660 1.00 35.07 ? 385 CYS A O 1 ATOM 1938 C CB . CYS A 1 252 ? 11.732 -24.129 -21.552 1.00 32.55 ? 385 CYS A CB 1 ATOM 1939 S SG . CYS A 1 252 ? 11.427 -23.287 -23.142 1.00 39.13 ? 385 CYS A SG 1 ATOM 1940 N N . ASN A 1 253 ? 11.004 -26.891 -19.886 1.00 34.74 ? 386 ASN A N 1 ATOM 1941 C CA . ASN A 1 253 ? 11.362 -27.762 -18.786 1.00 38.99 ? 386 ASN A CA 1 ATOM 1942 C C . ASN A 1 253 ? 12.855 -27.641 -18.494 1.00 34.27 ? 386 ASN A C 1 ATOM 1943 O O . ASN A 1 253 ? 13.680 -27.949 -19.349 1.00 35.23 ? 386 ASN A O 1 ATOM 1944 C CB . ASN A 1 253 ? 11.014 -29.195 -19.154 1.00 40.99 ? 386 ASN A CB 1 ATOM 1945 C CG . ASN A 1 253 ? 11.170 -30.145 -17.990 1.00 46.63 ? 386 ASN A CG 1 ATOM 1946 O OD1 . ASN A 1 253 ? 12.151 -30.083 -17.237 1.00 40.59 ? 386 ASN A OD1 1 ATOM 1947 N ND2 . ASN A 1 253 ? 10.182 -31.001 -17.806 1.00 59.04 ? 386 ASN A ND2 1 ATOM 1948 N N . THR A 1 254 ? 13.194 -27.186 -17.291 1.00 36.89 ? 387 THR A N 1 ATOM 1949 C CA . THR A 1 254 ? 14.592 -26.938 -16.929 1.00 38.32 ? 387 THR A CA 1 ATOM 1950 C C . THR A 1 254 ? 15.262 -28.051 -16.104 1.00 42.13 ? 387 THR A C 1 ATOM 1951 O O . THR A 1 254 ? 16.356 -27.860 -15.567 1.00 42.79 ? 387 THR A O 1 ATOM 1952 C CB . THR A 1 254 ? 14.734 -25.609 -16.177 1.00 33.56 ? 387 THR A CB 1 ATOM 1953 O OG1 . THR A 1 254 ? 13.991 -25.675 -14.959 1.00 36.98 ? 387 THR A OG1 1 ATOM 1954 C CG2 . THR A 1 254 ? 14.190 -24.470 -17.033 1.00 31.23 ? 387 THR A CG2 1 ATOM 1955 N N . THR A 1 255 ? 14.612 -29.206 -16.003 1.00 39.35 ? 388 THR A N 1 ATOM 1956 C CA . THR A 1 255 ? 15.174 -30.324 -15.236 1.00 44.46 ? 388 THR A CA 1 ATOM 1957 C C . THR A 1 255 ? 16.634 -30.575 -15.607 1.00 46.96 ? 388 THR A C 1 ATOM 1958 O O . THR A 1 255 ? 17.495 -30.711 -14.738 1.00 49.36 ? 388 THR A O 1 ATOM 1959 C CB . THR A 1 255 ? 14.357 -31.610 -15.449 1.00 46.36 ? 388 THR A CB 1 ATOM 1960 O OG1 . THR A 1 255 ? 13.103 -31.492 -14.767 1.00 52.88 ? 388 THR A OG1 1 ATOM 1961 C CG2 . THR A 1 255 ? 15.096 -32.822 -14.906 1.00 57.50 ? 388 THR A CG2 1 ATOM 1962 N N . GLN A 1 256 ? 16.913 -30.605 -16.905 1.00 49.13 ? 389 GLN A N 1 ATOM 1963 C CA . GLN A 1 256 ? 18.260 -30.896 -17.387 1.00 52.02 ? 389 GLN A CA 1 ATOM 1964 C C . GLN A 1 256 ? 19.290 -29.842 -17.002 1.00 51.51 ? 389 GLN A C 1 ATOM 1965 O O . GLN A 1 256 ? 20.475 -30.142 -16.925 1.00 58.72 ? 389 GLN A O 1 ATOM 1966 C CB . GLN A 1 256 ? 18.263 -31.054 -18.901 1.00 51.57 ? 389 GLN A CB 1 ATOM 1967 C CG . GLN A 1 256 ? 17.576 -32.292 -19.408 1.00 52.83 ? 389 GLN A CG 1 ATOM 1968 C CD . GLN A 1 256 ? 17.590 -32.342 -20.917 1.00 55.17 ? 389 GLN A CD 1 ATOM 1969 O OE1 . GLN A 1 256 ? 18.450 -32.991 -21.521 1.00 55.17 ? 389 GLN A OE1 1 ATOM 1970 N NE2 . GLN A 1 256 ? 16.652 -31.631 -21.541 1.00 50.36 ? 389 GLN A NE2 1 ATOM 1971 N N . LEU A 1 257 ? 18.845 -28.613 -16.770 1.00 43.78 ? 390 LEU A N 1 ATOM 1972 C CA . LEU A 1 257 ? 19.773 -27.527 -16.454 1.00 46.99 ? 390 LEU A CA 1 ATOM 1973 C C . LEU A 1 257 ? 20.312 -27.639 -15.042 1.00 54.82 ? 390 LEU A C 1 ATOM 1974 O O . LEU A 1 257 ? 21.424 -27.212 -14.757 1.00 63.26 ? 390 LEU A O 1 ATOM 1975 C CB . LEU A 1 257 ? 19.099 -26.169 -16.595 1.00 47.53 ? 390 LEU A CB 1 ATOM 1976 C CG . LEU A 1 257 ? 18.953 -25.544 -17.981 1.00 49.28 ? 390 LEU A CG 1 ATOM 1977 C CD1 . LEU A 1 257 ? 18.431 -24.127 -17.801 1.00 44.90 ? 390 LEU A CD1 1 ATOM 1978 C CD2 . LEU A 1 257 ? 20.271 -25.551 -18.739 1.00 50.80 ? 390 LEU A CD2 1 ATOM 1979 N N . PHE A 1 258 ? 19.513 -28.190 -14.143 1.00 48.23 ? 391 PHE A N 1 ATOM 1980 C CA . PHE A 1 258 ? 19.947 -28.271 -12.763 1.00 52.15 ? 391 PHE A CA 1 ATOM 1981 C C . PHE A 1 258 ? 20.273 -29.716 -12.396 1.00 58.29 ? 391 PHE A C 1 ATOM 1982 O O . PHE A 1 258 ? 19.668 -30.310 -11.508 1.00 58.51 ? 391 PHE A O 1 ATOM 1983 C CB . PHE A 1 258 ? 18.919 -27.597 -11.857 1.00 47.75 ? 391 PHE A CB 1 ATOM 1984 C CG . PHE A 1 258 ? 18.715 -26.147 -12.191 1.00 48.73 ? 391 PHE A CG 1 ATOM 1985 C CD1 . PHE A 1 258 ? 17.722 -25.753 -13.074 1.00 45.47 ? 391 PHE A CD1 1 ATOM 1986 C CD2 . PHE A 1 258 ? 19.556 -25.180 -11.665 1.00 43.52 ? 391 PHE A CD2 1 ATOM 1987 C CE1 . PHE A 1 258 ? 17.547 -24.420 -13.391 1.00 42.98 ? 391 PHE A CE1 1 ATOM 1988 C CE2 . PHE A 1 258 ? 19.390 -23.847 -11.985 1.00 33.81 ? 391 PHE A CE2 1 ATOM 1989 C CZ . PHE A 1 258 ? 18.388 -23.468 -12.856 1.00 38.36 ? 391 PHE A CZ 1 ATOM 1990 N N . ASN A 1 259 ? 21.259 -30.246 -13.121 1.00 65.38 ? 392 ASN A N 1 ATOM 1991 C CA . ASN A 1 259 ? 21.674 -31.644 -13.072 1.00 73.10 ? 392 ASN A CA 1 ATOM 1992 C C . ASN A 1 259 ? 22.825 -31.815 -12.081 1.00 71.36 ? 392 ASN A C 1 ATOM 1993 O O . ASN A 1 259 ? 23.964 -31.423 -12.352 1.00 65.07 ? 392 ASN A O 1 ATOM 1994 C CB . ASN A 1 259 ? 22.104 -32.092 -14.479 1.00 83.20 ? 392 ASN A CB 1 ATOM 1995 C CG . ASN A 1 259 ? 22.209 -33.607 -14.627 1.00 98.66 ? 392 ASN A CG 1 ATOM 1996 O OD1 . ASN A 1 259 ? 22.502 -34.321 -13.669 1.00 96.45 ? 392 ASN A OD1 1 ATOM 1997 N ND2 . ASN A 1 259 ? 21.972 -34.097 -15.854 1.00 116.52 ? 392 ASN A ND2 1 ATOM 1998 N N . ASN A 1 260 ? 22.519 -32.405 -10.931 1.00 71.12 ? 393 ASN A N 1 ATOM 1999 C CA . ASN A 1 260 ? 23.495 -32.553 -9.860 1.00 72.01 ? 393 ASN A CA 1 ATOM 2000 C C . ASN A 1 260 ? 24.726 -33.358 -10.255 1.00 75.84 ? 393 ASN A C 1 ATOM 2001 O O . ASN A 1 260 ? 25.835 -33.089 -9.783 1.00 75.55 ? 393 ASN A O 1 ATOM 2002 C CB . ASN A 1 260 ? 22.830 -33.173 -8.636 1.00 72.89 ? 393 ASN A CB 1 ATOM 2003 C CG . ASN A 1 260 ? 21.761 -32.278 -8.048 1.00 71.96 ? 393 ASN A CG 1 ATOM 2004 O OD1 . ASN A 1 260 ? 22.029 -31.129 -7.690 1.00 61.63 ? 393 ASN A OD1 1 ATOM 2005 N ND2 . ASN A 1 260 ? 20.536 -32.791 -7.965 1.00 76.20 ? 393 ASN A ND2 1 ATOM 2006 N N . THR A 1 261 ? 24.529 -34.343 -11.124 1.00 77.78 ? 394 THR A N 1 ATOM 2007 C CA . THR A 1 261 ? 25.616 -35.245 -11.489 1.00 83.57 ? 394 THR A CA 1 ATOM 2008 C C . THR A 1 261 ? 26.639 -34.576 -12.414 1.00 77.61 ? 394 THR A C 1 ATOM 2009 O O . THR A 1 261 ? 27.793 -35.005 -12.489 1.00 73.24 ? 394 THR A O 1 ATOM 2010 C CB . THR A 1 261 ? 25.082 -36.565 -12.093 1.00 90.61 ? 394 THR A CB 1 ATOM 2011 O OG1 . THR A 1 261 ? 24.006 -36.279 -12.995 1.00 88.07 ? 394 THR A OG1 1 ATOM 2012 C CG2 . THR A 1 261 ? 24.565 -37.482 -10.994 1.00 94.79 ? 394 THR A CG2 1 ATOM 2013 N N . CYS A 1 262 ? 26.213 -33.511 -13.091 1.00 76.00 ? 395 CYS A N 1 ATOM 2014 C CA . CYS A 1 262 ? 27.095 -32.748 -13.975 1.00 79.62 ? 395 CYS A CA 1 ATOM 2015 C C . CYS A 1 262 ? 27.914 -31.698 -13.226 1.00 81.11 ? 395 CYS A C 1 ATOM 2016 O O . CYS A 1 262 ? 28.738 -30.999 -13.818 1.00 80.79 ? 395 CYS A O 1 ATOM 2017 C CB . CYS A 1 262 ? 26.291 -32.072 -15.088 1.00 78.76 ? 395 CYS A CB 1 ATOM 2018 S SG . CYS A 1 262 ? 26.308 -32.952 -16.654 1.00 85.59 ? 395 CYS A SG 1 ATOM 2019 N N . ILE A 1 263 ? 27.686 -31.586 -11.923 1.00 81.42 ? 396 ILE A N 1 ATOM 2020 C CA . ILE A 1 263 ? 28.404 -30.611 -11.112 1.00 83.51 ? 396 ILE A CA 1 ATOM 2021 C C . ILE A 1 263 ? 29.614 -31.237 -10.433 1.00 83.76 ? 396 ILE A C 1 ATOM 2022 O O . ILE A 1 263 ? 29.526 -32.332 -9.880 1.00 86.66 ? 396 ILE A O 1 ATOM 2023 C CB . ILE A 1 263 ? 27.485 -29.987 -10.053 1.00 84.86 ? 396 ILE A CB 1 ATOM 2024 C CG1 . ILE A 1 263 ? 26.401 -29.148 -10.727 1.00 82.47 ? 396 ILE A CG1 1 ATOM 2025 C CG2 . ILE A 1 263 ? 28.286 -29.138 -9.082 1.00 88.43 ? 396 ILE A CG2 1 ATOM 2026 C CD1 . ILE A 1 263 ? 25.320 -28.688 -9.783 1.00 84.71 ? 396 ILE A CD1 1 ATOM 2027 N N . LYS A 1 269 ? 30.492 -38.009 -15.360 1.00 150.95 ? 408 LYS A N 1 ATOM 2028 C CA . LYS A 1 269 ? 29.920 -38.625 -16.552 1.00 152.05 ? 408 LYS A CA 1 ATOM 2029 C C . LYS A 1 269 ? 30.237 -37.798 -17.793 1.00 146.23 ? 408 LYS A C 1 ATOM 2030 O O . LYS A 1 269 ? 30.754 -36.685 -17.689 1.00 144.49 ? 408 LYS A O 1 ATOM 2031 C CB . LYS A 1 269 ? 28.408 -38.771 -16.397 1.00 154.51 ? 408 LYS A CB 1 ATOM 2032 C CG . LYS A 1 269 ? 27.690 -37.447 -16.284 1.00 155.02 ? 408 LYS A CG 1 ATOM 2033 C CD . LYS A 1 269 ? 26.417 -37.575 -15.479 1.00 156.71 ? 408 LYS A CD 1 ATOM 2034 C CE . LYS A 1 269 ? 25.846 -36.208 -15.187 1.00 156.71 ? 408 LYS A CE 1 ATOM 2035 N NZ . LYS A 1 269 ? 25.529 -35.486 -16.430 1.00 157.19 ? 408 LYS A NZ 1 ATOM 2036 N N . GLY A 1 270 ? 29.925 -38.348 -18.963 1.00 141.84 ? 409 GLY A N 1 ATOM 2037 C CA . GLY A 1 270 ? 30.133 -37.653 -20.222 1.00 135.89 ? 409 GLY A CA 1 ATOM 2038 C C . GLY A 1 270 ? 28.904 -36.861 -20.628 1.00 127.58 ? 409 GLY A C 1 ATOM 2039 O O . GLY A 1 270 ? 28.042 -37.357 -21.353 1.00 124.66 ? 409 GLY A O 1 ATOM 2040 N N . CYS A 1 271 ? 28.832 -35.618 -20.161 1.00 123.86 ? 410 CYS A N 1 ATOM 2041 C CA . CYS A 1 271 ? 27.646 -34.782 -20.336 1.00 116.78 ? 410 CYS A CA 1 ATOM 2042 C C . CYS A 1 271 ? 28.014 -33.342 -20.677 1.00 107.91 ? 410 CYS A C 1 ATOM 2043 O O . CYS A 1 271 ? 27.458 -32.395 -20.115 1.00 101.16 ? 410 CYS A O 1 ATOM 2044 C CB . CYS A 1 271 ? 26.815 -34.789 -19.054 1.00 117.03 ? 410 CYS A CB 1 ATOM 2045 S SG . CYS A 1 271 ? 27.684 -34.114 -17.600 1.00 80.64 ? 410 CYS A SG 1 ATOM 2046 N N . ASN A 1 272 ? 28.953 -33.184 -21.602 1.00 105.88 ? 411 ASN A N 1 ATOM 2047 C CA . ASN A 1 272 ? 29.453 -31.869 -21.981 1.00 97.81 ? 411 ASN A CA 1 ATOM 2048 C C . ASN A 1 272 ? 28.811 -31.337 -23.264 1.00 83.05 ? 411 ASN A C 1 ATOM 2049 O O . ASN A 1 272 ? 29.186 -30.281 -23.768 1.00 80.57 ? 411 ASN A O 1 ATOM 2050 C CB . ASN A 1 272 ? 30.978 -31.916 -22.127 1.00 107.39 ? 411 ASN A CB 1 ATOM 2051 C CG . ASN A 1 272 ? 31.460 -33.154 -22.880 1.00 116.25 ? 411 ASN A CG 1 ATOM 2052 O OD1 . ASN A 1 272 ? 30.692 -33.802 -23.594 1.00 116.65 ? 411 ASN A OD1 1 ATOM 2053 N ND2 . ASN A 1 272 ? 32.737 -33.486 -22.717 1.00 120.92 ? 411 ASN A ND2 1 ATOM 2054 N N . GLY A 1 273 ? 27.831 -32.069 -23.779 1.00 72.63 ? 412 GLY A N 1 ATOM 2055 C CA . GLY A 1 273 ? 27.244 -31.747 -25.064 1.00 66.19 ? 412 GLY A CA 1 ATOM 2056 C C . GLY A 1 273 ? 26.128 -30.733 -24.983 1.00 61.62 ? 412 GLY A C 1 ATOM 2057 O O . GLY A 1 273 ? 25.929 -30.086 -23.959 1.00 55.22 ? 412 GLY A O 1 ATOM 2058 N N . THR A 1 274 ? 25.393 -30.595 -26.079 1.00 59.68 ? 413 THR A N 1 ATOM 2059 C CA . THR A 1 274 ? 24.260 -29.686 -26.123 1.00 58.36 ? 413 THR A CA 1 ATOM 2060 C C . THR A 1 274 ? 23.135 -30.145 -25.193 1.00 55.76 ? 413 THR A C 1 ATOM 2061 O O . THR A 1 274 ? 22.731 -31.302 -25.210 1.00 57.88 ? 413 THR A O 1 ATOM 2062 C CB . THR A 1 274 ? 23.730 -29.533 -27.562 1.00 58.99 ? 413 THR A CB 1 ATOM 2063 O OG1 . THR A 1 274 ? 24.736 -28.918 -28.375 1.00 60.06 ? 413 THR A OG1 1 ATOM 2064 C CG2 . THR A 1 274 ? 22.483 -28.669 -27.586 1.00 54.90 ? 413 THR A CG2 1 ATOM 2065 N N . ILE A 1 275 ? 22.648 -29.232 -24.363 1.00 52.15 ? 414 ILE A N 1 ATOM 2066 C CA . ILE A 1 275 ? 21.470 -29.497 -23.551 1.00 53.36 ? 414 ILE A CA 1 ATOM 2067 C C . ILE A 1 275 ? 20.252 -28.966 -24.299 1.00 51.37 ? 414 ILE A C 1 ATOM 2068 O O . ILE A 1 275 ? 20.183 -27.784 -24.630 1.00 53.57 ? 414 ILE A O 1 ATOM 2069 C CB . ILE A 1 275 ? 21.568 -28.823 -22.175 1.00 52.74 ? 414 ILE A CB 1 ATOM 2070 C CG1 . ILE A 1 275 ? 22.847 -29.257 -21.456 1.00 56.67 ? 414 ILE A CG1 1 ATOM 2071 C CG2 . ILE A 1 275 ? 20.326 -29.123 -21.332 1.00 50.07 ? 414 ILE A CG2 1 ATOM 2072 C CD1 . ILE A 1 275 ? 23.108 -28.483 -20.174 1.00 53.64 ? 414 ILE A CD1 1 ATOM 2073 N N . THR A 1 276 ? 19.308 -29.852 -24.587 1.00 50.02 ? 415 THR A N 1 ATOM 2074 C CA . THR A 1 276 ? 18.090 -29.484 -25.296 1.00 46.95 ? 415 THR A CA 1 ATOM 2075 C C . THR A 1 276 ? 16.906 -29.590 -24.347 1.00 46.60 ? 415 THR A C 1 ATOM 2076 O O . THR A 1 276 ? 16.493 -30.689 -23.983 1.00 46.23 ? 415 THR A O 1 ATOM 2077 C CB . THR A 1 276 ? 17.859 -30.403 -26.520 1.00 53.76 ? 415 THR A CB 1 ATOM 2078 O OG1 . THR A 1 276 ? 18.909 -30.209 -27.477 1.00 51.14 ? 415 THR A OG1 1 ATOM 2079 C CG2 . THR A 1 276 ? 16.529 -30.101 -27.188 1.00 55.65 ? 415 THR A CG2 1 ATOM 2080 N N . LEU A 1 277 ? 16.373 -28.444 -23.933 1.00 41.85 ? 416 LEU A N 1 ATOM 2081 C CA . LEU A 1 277 ? 15.208 -28.427 -23.059 1.00 42.37 ? 416 LEU A CA 1 ATOM 2082 C C . LEU A 1 277 ? 13.953 -28.557 -23.898 1.00 38.08 ? 416 LEU A C 1 ATOM 2083 O O . LEU A 1 277 ? 13.801 -27.862 -24.892 1.00 40.67 ? 416 LEU A O 1 ATOM 2084 C CB . LEU A 1 277 ? 15.126 -27.116 -22.268 1.00 39.80 ? 416 LEU A CB 1 ATOM 2085 C CG . LEU A 1 277 ? 16.386 -26.633 -21.546 1.00 40.92 ? 416 LEU A CG 1 ATOM 2086 C CD1 . LEU A 1 277 ? 16.066 -25.342 -20.826 1.00 34.80 ? 416 LEU A CD1 1 ATOM 2087 C CD2 . LEU A 1 277 ? 16.906 -27.681 -20.584 1.00 40.19 ? 416 LEU A CD2 1 ATOM 2088 N N . PRO A 1 278 ? 13.050 -29.458 -23.507 1.00 39.75 ? 417 PRO A N 1 ATOM 2089 C CA . PRO A 1 278 ? 11.781 -29.504 -24.233 1.00 42.12 ? 417 PRO A CA 1 ATOM 2090 C C . PRO A 1 278 ? 10.924 -28.320 -23.821 1.00 39.92 ? 417 PRO A C 1 ATOM 2091 O O . PRO A 1 278 ? 10.847 -27.979 -22.634 1.00 38.90 ? 417 PRO A O 1 ATOM 2092 C CB . PRO A 1 278 ? 11.151 -30.822 -23.765 1.00 41.11 ? 417 PRO A CB 1 ATOM 2093 C CG . PRO A 1 278 ? 11.721 -31.028 -22.395 1.00 46.50 ? 417 PRO A CG 1 ATOM 2094 C CD . PRO A 1 278 ? 13.119 -30.453 -22.424 1.00 43.84 ? 417 PRO A CD 1 ATOM 2095 N N . CYS A 1 279 ? 10.296 -27.690 -24.803 1.00 36.97 ? 418 CYS A N 1 ATOM 2096 C CA . CYS A 1 279 ? 9.456 -26.527 -24.550 1.00 40.25 ? 418 CYS A CA 1 ATOM 2097 C C . CYS A 1 279 ? 8.114 -26.713 -25.208 1.00 33.70 ? 418 CYS A C 1 ATOM 2098 O O . CYS A 1 279 ? 7.969 -27.521 -26.124 1.00 34.67 ? 418 CYS A O 1 ATOM 2099 C CB . CYS A 1 279 ? 10.087 -25.266 -25.135 1.00 35.98 ? 418 CYS A CB 1 ATOM 2100 S SG . CYS A 1 279 ? 11.681 -24.815 -24.463 1.00 42.48 ? 418 CYS A SG 1 ATOM 2101 N N . LYS A 1 280 ? 7.130 -25.964 -24.736 1.00 34.61 ? 419 LYS A N 1 ATOM 2102 C CA . LYS A 1 280 ? 5.882 -25.834 -25.466 1.00 37.08 ? 419 LYS A CA 1 ATOM 2103 C C . LYS A 1 280 ? 5.469 -24.372 -25.476 1.00 36.51 ? 419 LYS A C 1 ATOM 2104 O O . LYS A 1 280 ? 5.772 -23.610 -24.541 1.00 34.93 ? 419 LYS A O 1 ATOM 2105 C CB . LYS A 1 280 ? 4.779 -26.694 -24.843 1.00 46.38 ? 419 LYS A CB 1 ATOM 2106 C CG . LYS A 1 280 ? 4.274 -26.182 -23.510 1.00 57.13 ? 419 LYS A CG 1 ATOM 2107 C CD . LYS A 1 280 ? 3.377 -27.204 -22.790 1.00 70.22 ? 419 LYS A CD 1 ATOM 2108 C CE . LYS A 1 280 ? 2.053 -27.428 -23.523 1.00 74.61 ? 419 LYS A CE 1 ATOM 2109 N NZ . LYS A 1 280 ? 0.995 -27.951 -22.614 1.00 75.44 ? 419 LYS A NZ 1 ATOM 2110 N N . ILE A 1 281 ? 4.799 -23.975 -26.548 1.00 32.62 ? 420 ILE A N 1 ATOM 2111 C CA . ILE A 1 281 ? 4.160 -22.676 -26.577 1.00 30.72 ? 420 ILE A CA 1 ATOM 2112 C C . ILE A 1 281 ? 2.745 -22.887 -26.084 1.00 31.39 ? 420 ILE A C 1 ATOM 2113 O O . ILE A 1 281 ? 2.076 -23.817 -26.523 1.00 34.36 ? 420 ILE A O 1 ATOM 2114 C CB . ILE A 1 281 ? 4.135 -22.116 -27.997 1.00 28.47 ? 420 ILE A CB 1 ATOM 2115 C CG1 . ILE A 1 281 ? 5.571 -21.845 -28.463 1.00 33.24 ? 420 ILE A CG1 1 ATOM 2116 C CG2 . ILE A 1 281 ? 3.267 -20.874 -28.049 1.00 29.09 ? 420 ILE A CG2 1 ATOM 2117 C CD1 . ILE A 1 281 ? 5.679 -21.355 -29.902 1.00 37.05 ? 420 ILE A CD1 1 ATOM 2118 N N . LYS A 1 282 ? 2.290 -22.061 -25.157 1.00 28.82 ? 421 LYS A N 1 ATOM 2119 C CA . LYS A 1 282 ? 0.943 -22.235 -24.645 1.00 29.13 ? 421 LYS A CA 1 ATOM 2120 C C . LYS A 1 282 ? 0.109 -21.027 -24.989 1.00 28.86 ? 421 LYS A C 1 ATOM 2121 O O . LYS A 1 282 ? 0.565 -19.894 -24.850 1.00 27.69 ? 421 LYS A O 1 ATOM 2122 C CB . LYS A 1 282 ? 0.947 -22.455 -23.135 1.00 33.16 ? 421 LYS A CB 1 ATOM 2123 C CG . LYS A 1 282 ? 1.325 -23.883 -22.742 1.00 35.05 ? 421 LYS A CG 1 ATOM 2124 C CD . LYS A 1 282 ? 1.428 -24.053 -21.230 1.00 34.34 ? 421 LYS A CD 1 ATOM 2125 C CE . LYS A 1 282 ? 0.123 -23.671 -20.539 1.00 32.86 ? 421 LYS A CE 1 ATOM 2126 N NZ . LYS A 1 282 ? -1.053 -24.343 -21.147 1.00 35.34 ? 421 LYS A NZ 1 ATOM 2127 N N . GLN A 1 283 ? -1.109 -21.293 -25.444 1.00 28.97 ? 422 GLN A N 1 ATOM 2128 C CA . GLN A 1 283 ? -2.084 -20.258 -25.727 1.00 32.78 ? 422 GLN A CA 1 ATOM 2129 C C . GLN A 1 283 ? -2.802 -19.847 -24.453 1.00 35.57 ? 422 GLN A C 1 ATOM 2130 O O . GLN A 1 283 ? -3.210 -18.701 -24.315 1.00 34.61 ? 422 GLN A O 1 ATOM 2131 C CB . GLN A 1 283 ? -3.125 -20.777 -26.715 1.00 31.72 ? 422 GLN A CB 1 ATOM 2132 C CG . GLN A 1 283 ? -2.614 -20.939 -28.139 1.00 34.44 ? 422 GLN A CG 1 ATOM 2133 C CD . GLN A 1 283 ? -3.594 -21.708 -28.994 1.00 37.73 ? 422 GLN A CD 1 ATOM 2134 O OE1 . GLN A 1 283 ? -3.301 -22.819 -29.454 1.00 43.57 ? 422 GLN A OE1 1 ATOM 2135 N NE2 . GLN A 1 283 ? -4.778 -21.136 -29.194 1.00 35.78 ? 422 GLN A NE2 1 ATOM 2136 N N . ILE A 1 284 ? -2.984 -20.795 -23.540 1.00 36.14 ? 423 ILE A N 1 ATOM 2137 C CA . ILE A 1 284 ? -3.703 -20.506 -22.302 1.00 33.09 ? 423 ILE A CA 1 ATOM 2138 C C . ILE A 1 284 ? -2.717 -20.426 -21.145 1.00 34.95 ? 423 ILE A C 1 ATOM 2139 O O . ILE A 1 284 ? -1.999 -21.383 -20.863 1.00 37.03 ? 423 ILE A O 1 ATOM 2140 C CB . ILE A 1 284 ? -4.766 -21.561 -22.028 1.00 38.11 ? 423 ILE A CB 1 ATOM 2141 C CG1 . ILE A 1 284 ? -5.803 -21.536 -23.155 1.00 43.21 ? 423 ILE A CG1 1 ATOM 2142 C CG2 . ILE A 1 284 ? -5.416 -21.326 -20.661 1.00 38.01 ? 423 ILE A CG2 1 ATOM 2143 C CD1 . ILE A 1 284 ? -6.696 -22.742 -23.176 1.00 41.81 ? 423 ILE A CD1 1 ATOM 2144 N N . ILE A 1 285 ? -2.660 -19.267 -20.498 1.00 31.62 ? 424 ILE A N 1 ATOM 2145 C CA . ILE A 1 285 ? -1.624 -19.004 -19.507 1.00 31.08 ? 424 ILE A CA 1 ATOM 2146 C C . ILE A 1 285 ? -2.192 -18.370 -18.252 1.00 32.18 ? 424 ILE A C 1 ATOM 2147 O O . ILE A 1 285 ? -3.278 -17.815 -18.273 1.00 35.54 ? 424 ILE A O 1 ATOM 2148 C CB . ILE A 1 285 ? -0.563 -18.045 -20.065 1.00 33.32 ? 424 ILE A CB 1 ATOM 2149 C CG1 . ILE A 1 285 ? -1.095 -16.609 -20.092 1.00 36.32 ? 424 ILE A CG1 1 ATOM 2150 C CG2 . ILE A 1 285 ? -0.132 -18.488 -21.478 1.00 32.13 ? 424 ILE A CG2 1 ATOM 2151 C CD1 . ILE A 1 285 ? -0.094 -15.605 -20.614 1.00 35.94 ? 424 ILE A CD1 1 ATOM 2152 N N . ASN A 1 286 ? -1.439 -18.458 -17.160 1.00 28.49 ? 425 ASN A N 1 ATOM 2153 C CA . ASN A 1 286 ? -1.709 -17.645 -15.979 1.00 33.85 ? 425 ASN A CA 1 ATOM 2154 C C . ASN A 1 286 ? -0.923 -16.354 -16.123 1.00 32.77 ? 425 ASN A C 1 ATOM 2155 O O . ASN A 1 286 ? 0.295 -16.383 -16.294 1.00 35.09 ? 425 ASN A O 1 ATOM 2156 C CB . ASN A 1 286 ? -1.287 -18.387 -14.709 1.00 32.60 ? 425 ASN A CB 1 ATOM 2157 C CG . ASN A 1 286 ? -2.143 -19.607 -14.448 1.00 35.22 ? 425 ASN A CG 1 ATOM 2158 O OD1 . ASN A 1 286 ? -3.360 -19.498 -14.300 1.00 40.28 ? 425 ASN A OD1 1 ATOM 2159 N ND2 . ASN A 1 286 ? -1.514 -20.783 -14.406 1.00 34.67 ? 425 ASN A ND2 1 ATOM 2160 N N . MET A 1 287 ? -1.611 -15.219 -16.104 1.00 34.41 ? 426 MET A N 1 ATOM 2161 C CA . MET A 1 287 ? -0.927 -13.950 -16.313 1.00 34.13 ? 426 MET A CA 1 ATOM 2162 C C . MET A 1 287 ? 0.021 -13.659 -15.149 1.00 37.14 ? 426 MET A C 1 ATOM 2163 O O . MET A 1 287 ? -0.375 -13.749 -13.995 1.00 34.68 ? 426 MET A O 1 ATOM 2164 C CB . MET A 1 287 ? -1.947 -12.825 -16.487 1.00 34.91 ? 426 MET A CB 1 ATOM 2165 C CG . MET A 1 287 ? -2.726 -12.950 -17.786 1.00 35.31 ? 426 MET A CG 1 ATOM 2166 S SD . MET A 1 287 ? -4.086 -11.792 -17.880 1.00 41.80 ? 426 MET A SD 1 ATOM 2167 C CE . MET A 1 287 ? -3.305 -10.410 -18.705 1.00 130.70 ? 426 MET A CE 1 ATOM 2168 N N . TRP A 1 288 ? 1.275 -13.324 -15.453 1.00 37.90 ? 427 TRP A N 1 ATOM 2169 C CA . TRP A 1 288 ? 2.264 -13.049 -14.405 1.00 37.23 ? 427 TRP A CA 1 ATOM 2170 C C . TRP A 1 288 ? 1.854 -11.843 -13.569 1.00 37.58 ? 427 TRP A C 1 ATOM 2171 O O . TRP A 1 288 ? 2.329 -11.655 -12.444 1.00 38.32 ? 427 TRP A O 1 ATOM 2172 C CB . TRP A 1 288 ? 3.653 -12.814 -15.003 1.00 32.41 ? 427 TRP A CB 1 ATOM 2173 C CG . TRP A 1 288 ? 3.711 -11.610 -15.920 1.00 38.37 ? 427 TRP A CG 1 ATOM 2174 C CD1 . TRP A 1 288 ? 3.557 -11.608 -17.273 1.00 36.79 ? 427 TRP A CD1 1 ATOM 2175 C CD2 . TRP A 1 288 ? 3.949 -10.240 -15.541 1.00 38.19 ? 427 TRP A CD2 1 ATOM 2176 N NE1 . TRP A 1 288 ? 3.677 -10.331 -17.764 1.00 38.39 ? 427 TRP A NE1 1 ATOM 2177 C CE2 . TRP A 1 288 ? 3.915 -9.471 -16.723 1.00 39.00 ? 427 TRP A CE2 1 ATOM 2178 C CE3 . TRP A 1 288 ? 4.189 -9.596 -14.319 1.00 33.89 ? 427 TRP A CE3 1 ATOM 2179 C CZ2 . TRP A 1 288 ? 4.120 -8.098 -16.725 1.00 34.11 ? 427 TRP A CZ2 1 ATOM 2180 C CZ3 . TRP A 1 288 ? 4.384 -8.226 -14.317 1.00 41.63 ? 427 TRP A CZ3 1 ATOM 2181 C CH2 . TRP A 1 288 ? 4.343 -7.486 -15.518 1.00 39.27 ? 427 TRP A CH2 1 ATOM 2182 N N . GLN A 1 289 ? 0.978 -11.015 -14.128 1.00 33.03 ? 428 GLN A N 1 ATOM 2183 C CA . GLN A 1 289 ? 0.450 -9.876 -13.380 1.00 37.99 ? 428 GLN A CA 1 ATOM 2184 C C . GLN A 1 289 ? -0.388 -10.333 -12.168 1.00 42.23 ? 428 GLN A C 1 ATOM 2185 O O . GLN A 1 289 ? -0.742 -9.526 -11.301 1.00 44.98 ? 428 GLN A O 1 ATOM 2186 C CB . GLN A 1 289 ? -0.360 -8.953 -14.296 1.00 39.37 ? 428 GLN A CB 1 ATOM 2187 C CG . GLN A 1 289 ? 0.437 -8.420 -15.508 1.00 42.14 ? 428 GLN A CG 1 ATOM 2188 C CD . GLN A 1 289 ? 0.263 -9.271 -16.766 1.00 46.62 ? 428 GLN A CD 1 ATOM 2189 O OE1 . GLN A 1 289 ? 0.452 -10.489 -16.743 1.00 42.98 ? 428 GLN A OE1 1 ATOM 2190 N NE2 . GLN A 1 289 ? -0.102 -8.622 -17.875 1.00 45.08 ? 428 GLN A NE2 1 ATOM 2191 N N . GLY A 1 290 ? -0.690 -11.629 -12.107 1.00 42.79 ? 429 GLY A N 1 ATOM 2192 C CA . GLY A 1 290 ? -1.408 -12.204 -10.977 1.00 41.79 ? 429 GLY A CA 1 ATOM 2193 C C . GLY A 1 290 ? -2.907 -11.990 -11.057 1.00 44.98 ? 429 GLY A C 1 ATOM 2194 O O . GLY A 1 290 ? -3.645 -12.249 -10.091 1.00 44.93 ? 429 GLY A O 1 ATOM 2195 N N . THR A 1 291 ? -3.357 -11.539 -12.225 1.00 40.94 ? 430 THR A N 1 ATOM 2196 C CA . THR A 1 291 ? -4.741 -11.128 -12.439 1.00 45.60 ? 430 THR A CA 1 ATOM 2197 C C . THR A 1 291 ? -5.710 -12.207 -12.939 1.00 48.80 ? 430 THR A C 1 ATOM 2198 O O . THR A 1 291 ? -6.914 -11.956 -13.022 1.00 51.70 ? 430 THR A O 1 ATOM 2199 C CB . THR A 1 291 ? -4.805 -9.962 -13.443 1.00 49.55 ? 430 THR A CB 1 ATOM 2200 O OG1 . THR A 1 291 ? -3.971 -10.265 -14.567 1.00 47.53 ? 430 THR A OG1 1 ATOM 2201 C CG2 . THR A 1 291 ? -4.327 -8.663 -12.792 1.00 53.22 ? 430 THR A CG2 1 ATOM 2202 N N . GLY A 1 292 ? -5.202 -13.388 -13.284 1.00 41.21 ? 431 GLY A N 1 ATOM 2203 C CA . GLY A 1 292 ? -6.065 -14.442 -13.795 1.00 38.89 ? 431 GLY A CA 1 ATOM 2204 C C . GLY A 1 292 ? -5.490 -15.174 -14.998 1.00 39.66 ? 431 GLY A C 1 ATOM 2205 O O . GLY A 1 292 ? -4.274 -15.331 -15.123 1.00 37.07 ? 431 GLY A O 1 ATOM 2206 N N . GLN A 1 293 ? -6.375 -15.622 -15.887 1.00 36.94 ? 432 GLN A N 1 ATOM 2207 C CA . GLN A 1 293 ? -5.966 -16.454 -17.009 1.00 36.14 ? 432 GLN A CA 1 ATOM 2208 C C . GLN A 1 293 ? -6.233 -15.752 -18.327 1.00 37.12 ? 432 GLN A C 1 ATOM 2209 O O . GLN A 1 293 ? -7.198 -15.008 -18.444 1.00 40.07 ? 432 GLN A O 1 ATOM 2210 C CB . GLN A 1 293 ? -6.706 -17.796 -16.975 1.00 36.73 ? 432 GLN A CB 1 ATOM 2211 C CG . GLN A 1 293 ? -6.246 -18.746 -15.870 1.00 44.83 ? 432 GLN A CG 1 ATOM 2212 C CD . GLN A 1 293 ? -6.745 -18.353 -14.471 1.00 52.30 ? 432 GLN A CD 1 ATOM 2213 O OE1 . GLN A 1 293 ? -7.956 -18.252 -14.221 1.00 53.21 ? 432 GLN A OE1 1 ATOM 2214 N NE2 . GLN A 1 293 ? -5.803 -18.133 -13.552 1.00 48.96 ? 432 GLN A NE2 1 ATOM 2215 N N . ALA A 1 294 ? -5.366 -15.989 -19.310 1.00 36.81 ? 433 ALA A N 1 ATOM 2216 C CA . ALA A 1 294 ? -5.540 -15.430 -20.655 1.00 35.44 ? 433 ALA A CA 1 ATOM 2217 C C . ALA A 1 294 ? -5.426 -16.511 -21.734 1.00 40.35 ? 433 ALA A C 1 ATOM 2218 O O . ALA A 1 294 ? -4.635 -17.446 -21.596 1.00 39.00 ? 433 ALA A O 1 ATOM 2219 C CB . ALA A 1 294 ? -4.508 -14.348 -20.904 1.00 35.20 ? 433 ALA A CB 1 ATOM 2220 N N . MET A 1 295 ? -6.208 -16.383 -22.804 1.00 33.37 ? 434 MET A N 1 ATOM 2221 C CA . MET A 1 295 ? -6.056 -17.265 -23.962 1.00 36.93 ? 434 MET A CA 1 ATOM 2222 C C . MET A 1 295 ? -5.684 -16.506 -25.241 1.00 38.20 ? 434 MET A C 1 ATOM 2223 O O . MET A 1 295 ? -6.382 -15.571 -25.646 1.00 35.52 ? 434 MET A O 1 ATOM 2224 C CB . MET A 1 295 ? -7.331 -18.062 -24.218 1.00 37.09 ? 434 MET A CB 1 ATOM 2225 C CG . MET A 1 295 ? -7.295 -18.808 -25.543 1.00 38.60 ? 434 MET A CG 1 ATOM 2226 S SD . MET A 1 295 ? -8.541 -20.092 -25.678 1.00 43.87 ? 434 MET A SD 1 ATOM 2227 C CE . MET A 1 295 ? -10.071 -19.166 -25.760 1.00 43.73 ? 434 MET A CE 1 ATOM 2228 N N . TYR A 1 296 ? -4.605 -16.938 -25.886 1.00 35.19 ? 435 TYR A N 1 ATOM 2229 C CA . TYR A 1 296 ? -4.123 -16.305 -27.116 1.00 35.95 ? 435 TYR A CA 1 ATOM 2230 C C . TYR A 1 296 ? -4.354 -17.181 -28.332 1.00 41.65 ? 435 TYR A C 1 ATOM 2231 O O . TYR A 1 296 ? -4.644 -18.367 -28.204 1.00 35.15 ? 435 TYR A O 1 ATOM 2232 C CB . TYR A 1 296 ? -2.632 -15.991 -26.986 1.00 35.76 ? 435 TYR A CB 1 ATOM 2233 C CG . TYR A 1 296 ? -2.374 -14.931 -25.955 1.00 33.88 ? 435 TYR A CG 1 ATOM 2234 C CD1 . TYR A 1 296 ? -2.345 -13.588 -26.314 1.00 34.87 ? 435 TYR A CD1 1 ATOM 2235 C CD2 . TYR A 1 296 ? -2.196 -15.260 -24.613 1.00 31.53 ? 435 TYR A CD2 1 ATOM 2236 C CE1 . TYR A 1 296 ? -2.136 -12.601 -25.366 1.00 35.77 ? 435 TYR A CE1 1 ATOM 2237 C CE2 . TYR A 1 296 ? -1.987 -14.285 -23.654 1.00 32.08 ? 435 TYR A CE2 1 ATOM 2238 C CZ . TYR A 1 296 ? -1.957 -12.953 -24.043 1.00 36.02 ? 435 TYR A CZ 1 ATOM 2239 O OH . TYR A 1 296 ? -1.755 -11.963 -23.119 1.00 36.64 ? 435 TYR A OH 1 ATOM 2240 N N . ALA A 1 297 ? -4.222 -16.594 -29.517 1.00 36.47 ? 436 ALA A N 1 ATOM 2241 C CA . ALA A 1 297 ? -4.310 -17.362 -30.753 1.00 36.20 ? 436 ALA A CA 1 ATOM 2242 C C . ALA A 1 297 ? -3.102 -18.284 -30.855 1.00 33.34 ? 436 ALA A C 1 ATOM 2243 O O . ALA A 1 297 ? -2.104 -18.074 -30.179 1.00 32.84 ? 436 ALA A O 1 ATOM 2244 C CB . ALA A 1 297 ? -4.353 -16.424 -31.950 1.00 41.11 ? 436 ALA A CB 1 ATOM 2245 N N . PRO A 1 298 ? -3.187 -19.311 -31.707 1.00 35.93 ? 437 PRO A N 1 ATOM 2246 C CA . PRO A 1 298 ? -2.050 -20.219 -31.878 1.00 37.41 ? 437 PRO A CA 1 ATOM 2247 C C . PRO A 1 298 ? -0.845 -19.531 -32.524 1.00 38.19 ? 437 PRO A C 1 ATOM 2248 O O . PRO A 1 298 ? -0.974 -18.432 -33.081 1.00 39.95 ? 437 PRO A O 1 ATOM 2249 C CB . PRO A 1 298 ? -2.613 -21.337 -32.765 1.00 38.09 ? 437 PRO A CB 1 ATOM 2250 C CG . PRO A 1 298 ? -3.841 -20.786 -33.377 1.00 42.75 ? 437 PRO A CG 1 ATOM 2251 C CD . PRO A 1 298 ? -4.382 -19.760 -32.441 1.00 36.60 ? 437 PRO A CD 1 ATOM 2252 N N . PRO A 1 299 ? 0.327 -20.175 -32.456 1.00 38.87 ? 438 PRO A N 1 ATOM 2253 C CA . PRO A 1 299 ? 1.574 -19.514 -32.853 1.00 38.97 ? 438 PRO A CA 1 ATOM 2254 C C . PRO A 1 299 ? 1.596 -19.119 -34.325 1.00 38.19 ? 438 PRO A C 1 ATOM 2255 O O . PRO A 1 299 ? 0.959 -19.760 -35.169 1.00 36.99 ? 438 PRO A O 1 ATOM 2256 C CB . PRO A 1 299 ? 2.648 -20.583 -32.584 1.00 40.84 ? 438 PRO A CB 1 ATOM 2257 C CG . PRO A 1 299 ? 1.988 -21.624 -31.754 1.00 38.40 ? 438 PRO A CG 1 ATOM 2258 C CD . PRO A 1 299 ? 0.541 -21.579 -32.071 1.00 37.75 ? 438 PRO A CD 1 ATOM 2259 N N . ILE A 1 300 ? 2.331 -18.060 -34.629 1.00 41.86 ? 439 ILE A N 1 ATOM 2260 C CA . ILE A 1 300 ? 2.596 -17.699 -36.016 1.00 42.52 ? 439 ILE A CA 1 ATOM 2261 C C . ILE A 1 300 ? 3.316 -18.829 -36.745 1.00 39.08 ? 439 ILE A C 1 ATOM 2262 O O . ILE A 1 300 ? 3.962 -19.653 -36.120 1.00 39.75 ? 439 ILE A O 1 ATOM 2263 C CB . ILE A 1 300 ? 3.484 -16.453 -36.086 1.00 46.00 ? 439 ILE A CB 1 ATOM 2264 C CG1 . ILE A 1 300 ? 4.789 -16.692 -35.326 1.00 42.87 ? 439 ILE A CG1 1 ATOM 2265 C CG2 . ILE A 1 300 ? 2.764 -15.257 -35.502 1.00 41.72 ? 439 ILE A CG2 1 ATOM 2266 C CD1 . ILE A 1 300 ? 5.699 -15.486 -35.316 1.00 48.37 ? 439 ILE A CD1 1 ATOM 2267 N N . ASP A 1 301 ? 3.222 -18.848 -38.076 1.00 39.00 ? 440 ASP A N 1 ATOM 2268 C CA . ASP A 1 301 ? 3.973 -19.817 -38.878 1.00 43.85 ? 440 ASP A CA 1 ATOM 2269 C C . ASP A 1 301 ? 5.470 -19.516 -38.973 1.00 45.55 ? 440 ASP A C 1 ATOM 2270 O O . ASP A 1 301 ? 5.913 -18.389 -38.737 1.00 46.16 ? 440 ASP A O 1 ATOM 2271 C CB . ASP A 1 301 ? 3.402 -19.884 -40.292 1.00 53.46 ? 440 ASP A CB 1 ATOM 2272 C CG . ASP A 1 301 ? 2.010 -20.437 -40.315 1.00 59.46 ? 440 ASP A CG 1 ATOM 2273 O OD1 . ASP A 1 301 ? 1.171 -19.904 -41.077 1.00 64.96 ? 440 ASP A OD1 1 ATOM 2274 O OD2 . ASP A 1 301 ? 1.766 -21.403 -39.558 1.00 57.98 ? 440 ASP A OD2 1 ATOM 2275 N N . GLY A 1 302 ? 6.244 -20.535 -39.331 1.00 45.54 ? 441 GLY A N 1 ATOM 2276 C CA . GLY A 1 302 ? 7.656 -20.344 -39.598 1.00 50.89 ? 441 GLY A CA 1 ATOM 2277 C C . GLY A 1 302 ? 8.571 -20.576 -38.413 1.00 49.76 ? 441 GLY A C 1 ATOM 2278 O O . GLY A 1 302 ? 8.171 -21.140 -37.388 1.00 48.26 ? 441 GLY A O 1 ATOM 2279 N N . LYS A 1 303 ? 9.818 -20.151 -38.560 1.00 46.96 ? 442 LYS A N 1 ATOM 2280 C CA . LYS A 1 303 ? 10.801 -20.369 -37.514 1.00 48.12 ? 442 LYS A CA 1 ATOM 2281 C C . LYS A 1 303 ? 10.638 -19.280 -36.481 1.00 45.74 ? 442 LYS A C 1 ATOM 2282 O O . LYS A 1 303 ? 10.942 -18.121 -36.744 1.00 52.25 ? 442 LYS A O 1 ATOM 2283 C CB . LYS A 1 303 ? 12.227 -20.372 -38.073 1.00 57.55 ? 442 LYS A CB 1 ATOM 2284 C CG . LYS A 1 303 ? 12.529 -21.555 -38.979 1.00 75.04 ? 442 LYS A CG 1 ATOM 2285 C CD . LYS A 1 303 ? 13.862 -21.389 -39.710 1.00 88.41 ? 442 LYS A CD 1 ATOM 2286 C CE . LYS A 1 303 ? 14.039 -22.453 -40.791 1.00 90.78 ? 442 LYS A CE 1 ATOM 2287 N NZ . LYS A 1 303 ? 15.439 -22.490 -41.293 1.00 94.51 ? 442 LYS A NZ 1 ATOM 2288 N N . ILE A 1 304 ? 10.114 -19.658 -35.319 1.00 44.61 ? 443 ILE A N 1 ATOM 2289 C CA . ILE A 1 304 ? 10.055 -18.760 -34.179 1.00 43.63 ? 443 ILE A CA 1 ATOM 2290 C C . ILE A 1 304 ? 11.309 -18.990 -33.350 1.00 43.40 ? 443 ILE A C 1 ATOM 2291 O O . ILE A 1 304 ? 11.549 -20.099 -32.869 1.00 39.96 ? 443 ILE A O 1 ATOM 2292 C CB . ILE A 1 304 ? 8.805 -19.019 -33.303 1.00 35.85 ? 443 ILE A CB 1 ATOM 2293 C CG1 . ILE A 1 304 ? 7.528 -18.932 -34.157 1.00 37.08 ? 443 ILE A CG1 1 ATOM 2294 C CG2 . ILE A 1 304 ? 8.769 -18.023 -32.155 1.00 33.34 ? 443 ILE A CG2 1 ATOM 2295 C CD1 . ILE A 1 304 ? 6.301 -19.568 -33.521 1.00 37.85 ? 443 ILE A CD1 1 ATOM 2296 N N . ASN A 1 305 ? 12.108 -17.946 -33.179 1.00 38.79 ? 444 ASN A N 1 ATOM 2297 C CA . ASN A 1 305 ? 13.416 -18.121 -32.571 1.00 38.94 ? 444 ASN A CA 1 ATOM 2298 C C . ASN A 1 305 ? 13.884 -16.922 -31.753 1.00 40.74 ? 444 ASN A C 1 ATOM 2299 O O . ASN A 1 305 ? 13.833 -15.781 -32.224 1.00 40.37 ? 444 ASN A O 1 ATOM 2300 C CB . ASN A 1 305 ? 14.434 -18.455 -33.677 1.00 43.69 ? 444 ASN A CB 1 ATOM 2301 C CG . ASN A 1 305 ? 15.855 -18.499 -33.167 1.00 44.18 ? 444 ASN A CG 1 ATOM 2302 O OD1 . ASN A 1 305 ? 16.297 -19.492 -32.581 1.00 44.04 ? 444 ASN A OD1 1 ATOM 2303 N ND2 . ASN A 1 305 ? 16.583 -17.420 -33.390 1.00 46.56 ? 444 ASN A ND2 1 ATOM 2304 N N . CYS A 1 306 ? 14.329 -17.197 -30.522 1.00 37.37 ? 445 CYS A N 1 ATOM 2305 C CA . CYS A 1 306 ? 14.991 -16.211 -29.672 1.00 39.05 ? 445 CYS A CA 1 ATOM 2306 C C . CYS A 1 306 ? 16.267 -16.793 -29.080 1.00 38.13 ? 445 CYS A C 1 ATOM 2307 O O . CYS A 1 306 ? 16.238 -17.830 -28.419 1.00 38.48 ? 445 CYS A O 1 ATOM 2308 C CB . CYS A 1 306 ? 14.080 -15.772 -28.515 1.00 39.29 ? 445 CYS A CB 1 ATOM 2309 S SG . CYS A 1 306 ? 12.572 -14.927 -29.015 1.00 41.94 ? 445 CYS A SG 1 ATOM 2310 N N . VAL A 1 307 ? 17.388 -16.129 -29.314 1.00 38.41 ? 446 VAL A N 1 ATOM 2311 C CA . VAL A 1 307 ? 18.615 -16.490 -28.628 1.00 40.82 ? 446 VAL A CA 1 ATOM 2312 C C . VAL A 1 307 ? 18.792 -15.439 -27.563 1.00 38.84 ? 446 VAL A C 1 ATOM 2313 O O . VAL A 1 307 ? 18.791 -14.251 -27.872 1.00 35.24 ? 446 VAL A O 1 ATOM 2314 C CB . VAL A 1 307 ? 19.852 -16.463 -29.555 1.00 42.36 ? 446 VAL A CB 1 ATOM 2315 C CG1 . VAL A 1 307 ? 21.085 -16.938 -28.788 1.00 41.51 ? 446 VAL A CG1 1 ATOM 2316 C CG2 . VAL A 1 307 ? 19.631 -17.325 -30.774 1.00 43.42 ? 446 VAL A CG2 1 ATOM 2317 N N . SER A 1 308 ? 18.923 -15.879 -26.313 1.00 38.12 ? 447 SER A N 1 ATOM 2318 C CA . SER A 1 308 ? 19.020 -14.975 -25.175 1.00 38.42 ? 447 SER A CA 1 ATOM 2319 C C . SER A 1 308 ? 20.268 -15.298 -24.372 1.00 36.79 ? 447 SER A C 1 ATOM 2320 O O . SER A 1 308 ? 20.757 -16.427 -24.415 1.00 41.99 ? 447 SER A O 1 ATOM 2321 C CB . SER A 1 308 ? 17.789 -15.139 -24.283 1.00 35.97 ? 447 SER A CB 1 ATOM 2322 O OG . SER A 1 308 ? 16.597 -14.867 -25.000 1.00 34.07 ? 447 SER A OG 1 ATOM 2323 N N . ASN A 1 309 ? 20.797 -14.314 -23.653 1.00 35.96 ? 448 ASN A N 1 ATOM 2324 C CA . ASN A 1 309 ? 21.818 -14.604 -22.646 1.00 32.33 ? 448 ASN A CA 1 ATOM 2325 C C . ASN A 1 309 ? 21.154 -14.869 -21.320 1.00 32.89 ? 448 ASN A C 1 ATOM 2326 O O . ASN A 1 309 ? 20.340 -14.065 -20.867 1.00 32.39 ? 448 ASN A O 1 ATOM 2327 C CB . ASN A 1 309 ? 22.755 -13.423 -22.442 1.00 42.85 ? 448 ASN A CB 1 ATOM 2328 C CG . ASN A 1 309 ? 23.412 -12.979 -23.706 1.00 51.04 ? 448 ASN A CG 1 ATOM 2329 O OD1 . ASN A 1 309 ? 23.983 -13.780 -24.431 1.00 40.44 ? 448 ASN A OD1 1 ATOM 2330 N ND2 . ASN A 1 309 ? 23.339 -11.684 -23.978 1.00 74.13 ? 448 ASN A ND2 1 ATOM 2331 N N . ILE A 1 310 ? 21.499 -15.989 -20.694 1.00 35.07 ? 449 ILE A N 1 ATOM 2332 C CA . ILE A 1 310 ? 21.168 -16.177 -19.300 1.00 31.32 ? 449 ILE A CA 1 ATOM 2333 C C . ILE A 1 310 ? 22.202 -15.400 -18.497 1.00 37.89 ? 449 ILE A C 1 ATOM 2334 O O . ILE A 1 310 ? 23.402 -15.662 -18.599 1.00 38.83 ? 449 ILE A O 1 ATOM 2335 C CB . ILE A 1 310 ? 21.196 -17.637 -18.877 1.00 32.20 ? 449 ILE A CB 1 ATOM 2336 C CG1 . ILE A 1 310 ? 20.213 -18.448 -19.727 1.00 36.94 ? 449 ILE A CG1 1 ATOM 2337 C CG2 . ILE A 1 310 ? 20.822 -17.747 -17.395 1.00 33.26 ? 449 ILE A CG2 1 ATOM 2338 C CD1 . ILE A 1 310 ? 20.441 -19.964 -19.673 1.00 40.88 ? 449 ILE A CD1 1 ATOM 2339 N N . THR A 1 311 ? 21.726 -14.434 -17.719 1.00 30.98 ? 450 THR A N 1 ATOM 2340 C CA . THR A 1 311 ? 22.599 -13.538 -16.965 1.00 32.22 ? 450 THR A CA 1 ATOM 2341 C C . THR A 1 311 ? 22.336 -13.623 -15.461 1.00 33.00 ? 450 THR A C 1 ATOM 2342 O O . THR A 1 311 ? 23.076 -13.044 -14.647 1.00 33.08 ? 450 THR A O 1 ATOM 2343 C CB . THR A 1 311 ? 22.426 -12.074 -17.440 1.00 37.28 ? 450 THR A CB 1 ATOM 2344 O OG1 . THR A 1 311 ? 21.051 -11.695 -17.336 1.00 34.59 ? 450 THR A OG1 1 ATOM 2345 C CG2 . THR A 1 311 ? 22.883 -11.922 -18.896 1.00 35.26 ? 450 THR A CG2 1 ATOM 2346 N N . GLY A 1 312 ? 21.272 -14.333 -15.101 1.00 30.73 ? 451 GLY A N 1 ATOM 2347 C CA . GLY A 1 312 ? 20.895 -14.486 -13.709 1.00 38.08 ? 451 GLY A CA 1 ATOM 2348 C C . GLY A 1 312 ? 20.064 -15.735 -13.519 1.00 36.60 ? 451 GLY A C 1 ATOM 2349 O O . GLY A 1 312 ? 19.534 -16.287 -14.492 1.00 34.33 ? 451 GLY A O 1 ATOM 2350 N N . ILE A 1 313 ? 19.969 -16.191 -12.270 1.00 32.86 ? 452 ILE A N 1 ATOM 2351 C CA . ILE A 1 313 ? 19.139 -17.340 -11.923 1.00 31.58 ? 452 ILE A CA 1 ATOM 2352 C C . ILE A 1 313 ? 18.372 -17.004 -10.645 1.00 28.66 ? 452 ILE A C 1 ATOM 2353 O O . ILE A 1 313 ? 18.939 -16.433 -9.712 1.00 34.08 ? 452 ILE A O 1 ATOM 2354 C CB . ILE A 1 313 ? 19.987 -18.618 -11.703 1.00 33.12 ? 452 ILE A CB 1 ATOM 2355 C CG1 . ILE A 1 313 ? 20.897 -18.893 -12.901 1.00 32.45 ? 452 ILE A CG1 1 ATOM 2356 C CG2 . ILE A 1 313 ? 19.097 -19.845 -11.415 1.00 33.59 ? 452 ILE A CG2 1 ATOM 2357 C CD1 . ILE A 1 313 ? 21.897 -20.021 -12.664 1.00 34.27 ? 452 ILE A CD1 1 ATOM 2358 N N . LEU A 1 314 ? 17.089 -17.345 -10.602 1.00 31.67 ? 453 LEU A N 1 ATOM 2359 C CA . LEU A 1 314 ? 16.311 -17.182 -9.375 1.00 32.11 ? 453 LEU A CA 1 ATOM 2360 C C . LEU A 1 314 ? 16.213 -18.532 -8.673 1.00 34.00 ? 453 LEU A C 1 ATOM 2361 O O . LEU A 1 314 ? 15.864 -19.540 -9.297 1.00 33.38 ? 453 LEU A O 1 ATOM 2362 C CB . LEU A 1 314 ? 14.919 -16.640 -9.678 1.00 31.95 ? 453 LEU A CB 1 ATOM 2363 C CG . LEU A 1 314 ? 14.931 -15.303 -10.435 1.00 37.05 ? 453 LEU A CG 1 ATOM 2364 C CD1 . LEU A 1 314 ? 13.568 -14.993 -11.032 1.00 38.12 ? 453 LEU A CD1 1 ATOM 2365 C CD2 . LEU A 1 314 ? 15.386 -14.197 -9.515 1.00 33.21 ? 453 LEU A CD2 1 ATOM 2366 N N . LEU A 1 315 ? 16.532 -18.548 -7.385 1.00 33.55 ? 454 LEU A N 1 ATOM 2367 C CA . LEU A 1 315 ? 16.527 -19.802 -6.631 1.00 36.08 ? 454 LEU A CA 1 ATOM 2368 C C . LEU A 1 315 ? 15.721 -19.707 -5.349 1.00 38.74 ? 454 LEU A C 1 ATOM 2369 O O . LEU A 1 315 ? 15.713 -18.674 -4.688 1.00 38.60 ? 454 LEU A O 1 ATOM 2370 C CB . LEU A 1 315 ? 17.951 -20.227 -6.294 1.00 37.21 ? 454 LEU A CB 1 ATOM 2371 C CG . LEU A 1 315 ? 18.894 -20.594 -7.438 1.00 36.34 ? 454 LEU A CG 1 ATOM 2372 C CD1 . LEU A 1 315 ? 20.271 -20.887 -6.846 1.00 35.55 ? 454 LEU A CD1 1 ATOM 2373 C CD2 . LEU A 1 315 ? 18.365 -21.805 -8.231 1.00 34.89 ? 454 LEU A CD2 1 ATOM 2374 N N . THR A 1 316 ? 15.049 -20.799 -5.006 1.00 34.27 ? 455 THR A N 1 ATOM 2375 C CA . THR A 1 316 ? 14.427 -20.936 -3.704 1.00 37.09 ? 455 THR A CA 1 ATOM 2376 C C . THR A 1 316 ? 15.115 -22.074 -2.934 1.00 35.77 ? 455 THR A C 1 ATOM 2377 O O . THR A 1 316 ? 15.249 -23.185 -3.449 1.00 40.87 ? 455 THR A O 1 ATOM 2378 C CB . THR A 1 316 ? 12.908 -21.197 -3.841 1.00 40.98 ? 455 THR A CB 1 ATOM 2379 O OG1 . THR A 1 316 ? 12.305 -20.123 -4.584 1.00 38.46 ? 455 THR A OG1 1 ATOM 2380 C CG2 . THR A 1 316 ? 12.240 -21.300 -2.461 1.00 39.17 ? 455 THR A CG2 1 ATOM 2381 N N . ARG A 1 317 ? 15.583 -21.790 -1.723 1.00 36.20 ? 456 ARG A N 1 ATOM 2382 C CA . ARG A 1 317 ? 16.188 -22.846 -0.877 1.00 35.64 ? 456 ARG A CA 1 ATOM 2383 C C . ARG A 1 317 ? 15.138 -23.581 -0.044 1.00 41.51 ? 456 ARG A C 1 ATOM 2384 O O . ARG A 1 317 ? 14.239 -22.956 0.525 1.00 40.66 ? 456 ARG A O 1 ATOM 2385 C CB . ARG A 1 317 ? 17.258 -22.247 0.047 1.00 33.04 ? 456 ARG A CB 1 ATOM 2386 C CG . ARG A 1 317 ? 18.069 -23.241 0.883 1.00 37.53 ? 456 ARG A CG 1 ATOM 2387 C CD . ARG A 1 317 ? 19.146 -22.515 1.672 1.00 42.70 ? 456 ARG A CD 1 ATOM 2388 N NE . ARG A 1 317 ? 18.575 -21.492 2.547 1.00 43.42 ? 456 ARG A NE 1 ATOM 2389 C CZ . ARG A 1 317 ? 18.291 -21.668 3.835 1.00 48.29 ? 456 ARG A CZ 1 ATOM 2390 N NH1 . ARG A 1 317 ? 18.540 -22.826 4.426 1.00 49.79 ? 456 ARG A NH1 1 ATOM 2391 N NH2 . ARG A 1 317 ? 17.768 -20.675 4.545 1.00 48.30 ? 456 ARG A NH2 1 ATOM 2392 N N . ASP A 1 318 ? 15.258 -24.909 0.035 1.00 46.14 ? 457 ASP A N 1 ATOM 2393 C CA . ASP A 1 318 ? 14.391 -25.713 0.908 1.00 47.34 ? 457 ASP A CA 1 ATOM 2394 C C . ASP A 1 318 ? 14.546 -25.341 2.386 1.00 52.43 ? 457 ASP A C 1 ATOM 2395 O O . ASP A 1 318 ? 15.660 -25.247 2.900 1.00 49.96 ? 457 ASP A O 1 ATOM 2396 C CB . ASP A 1 318 ? 14.685 -27.209 0.744 1.00 51.87 ? 457 ASP A CB 1 ATOM 2397 C CG . ASP A 1 318 ? 14.050 -27.797 -0.498 1.00 50.75 ? 457 ASP A CG 1 ATOM 2398 O OD1 . ASP A 1 318 ? 13.572 -27.011 -1.343 1.00 47.16 ? 457 ASP A OD1 1 ATOM 2399 O OD2 . ASP A 1 318 ? 14.032 -29.043 -0.633 1.00 47.92 ? 457 ASP A OD2 1 ATOM 2400 N N . GLY A 1 319 ? 13.425 -25.145 3.069 1.00 54.97 ? 458 GLY A N 1 ATOM 2401 C CA . GLY A 1 319 ? 13.454 -24.920 4.503 1.00 63.97 ? 458 GLY A CA 1 ATOM 2402 C C . GLY A 1 319 ? 13.588 -26.228 5.264 1.00 70.82 ? 458 GLY A C 1 ATOM 2403 O O . GLY A 1 319 ? 13.426 -27.307 4.690 1.00 66.75 ? 458 GLY A O 1 ATOM 2404 N N . GLY A 1 320 ? 13.900 -26.128 6.554 1.00 81.03 ? 459 GLY A N 1 ATOM 2405 C CA . GLY A 1 320 ? 13.921 -27.282 7.439 1.00 92.63 ? 459 GLY A CA 1 ATOM 2406 C C . GLY A 1 320 ? 15.104 -28.228 7.313 1.00 101.89 ? 459 GLY A C 1 ATOM 2407 O O . GLY A 1 320 ? 15.152 -29.251 7.997 1.00 108.81 ? 459 GLY A O 1 ATOM 2408 N N . ALA A 1 321 ? 16.062 -27.896 6.454 1.00 103.26 ? 460 ALA A N 1 ATOM 2409 C CA . ALA A 1 321 ? 17.211 -28.772 6.224 1.00 106.74 ? 460 ALA A CA 1 ATOM 2410 C C . ALA A 1 321 ? 18.409 -28.439 7.120 1.00 108.12 ? 460 ALA A C 1 ATOM 2411 O O . ALA A 1 321 ? 19.544 -28.806 6.817 1.00 106.47 ? 460 ALA A O 1 ATOM 2412 C CB . ALA A 1 321 ? 17.618 -28.739 4.753 1.00 105.30 ? 460 ALA A CB 1 ATOM 2413 N N . ASN A 1 322 ? 18.151 -27.755 8.228 1.00 110.17 ? 461 ASN A N 1 ATOM 2414 C CA . ASN A 1 322 ? 19.224 -27.315 9.115 1.00 113.26 ? 461 ASN A CA 1 ATOM 2415 C C . ASN A 1 322 ? 19.958 -28.464 9.800 1.00 121.63 ? 461 ASN A C 1 ATOM 2416 O O . ASN A 1 322 ? 21.151 -28.360 10.088 1.00 123.17 ? 461 ASN A O 1 ATOM 2417 C CB . ASN A 1 322 ? 18.687 -26.326 10.153 1.00 110.74 ? 461 ASN A CB 1 ATOM 2418 C CG . ASN A 1 322 ? 18.127 -25.065 9.518 1.00 105.01 ? 461 ASN A CG 1 ATOM 2419 O OD1 . ASN A 1 322 ? 18.622 -24.599 8.490 1.00 103.76 ? 461 ASN A OD1 1 ATOM 2420 N ND2 . ASN A 1 322 ? 17.084 -24.510 10.125 1.00 102.26 ? 461 ASN A ND2 1 ATOM 2421 N N . ASN A 1 323 ? 19.244 -29.559 10.048 1.00 127.17 ? 462 ASN A N 1 ATOM 2422 C CA . ASN A 1 323 ? 19.815 -30.721 10.727 1.00 132.95 ? 462 ASN A CA 1 ATOM 2423 C C . ASN A 1 323 ? 20.641 -31.609 9.799 1.00 124.79 ? 462 ASN A C 1 ATOM 2424 O O . ASN A 1 323 ? 21.493 -32.376 10.253 1.00 126.06 ? 462 ASN A O 1 ATOM 2425 C CB . ASN A 1 323 ? 18.710 -31.551 11.385 1.00 143.26 ? 462 ASN A CB 1 ATOM 2426 C CG . ASN A 1 323 ? 17.878 -32.318 10.373 1.00 147.38 ? 462 ASN A CG 1 ATOM 2427 O OD1 . ASN A 1 323 ? 17.142 -31.727 9.579 1.00 145.01 ? 462 ASN A OD1 1 ATOM 2428 N ND2 . ASN A 1 323 ? 17.984 -33.644 10.402 1.00 150.74 ? 462 ASN A ND2 1 ATOM 2429 N N . THR A 1 324 ? 20.375 -31.511 8.501 1.00 113.18 ? 463 THR A N 1 ATOM 2430 C CA . THR A 1 324 ? 21.118 -32.281 7.513 1.00 104.95 ? 463 THR A CA 1 ATOM 2431 C C . THR A 1 324 ? 22.453 -31.614 7.205 1.00 94.50 ? 463 THR A C 1 ATOM 2432 O O . THR A 1 324 ? 22.780 -30.567 7.764 1.00 91.98 ? 463 THR A O 1 ATOM 2433 C CB . THR A 1 324 ? 20.323 -32.441 6.198 1.00 103.97 ? 463 THR A CB 1 ATOM 2434 O OG1 . THR A 1 324 ? 20.080 -31.151 5.617 1.00 100.03 ? 463 THR A OG1 1 ATOM 2435 C CG2 . THR A 1 324 ? 18.996 -33.146 6.453 1.00 103.57 ? 463 THR A CG2 1 ATOM 2436 N N . SER A 1 325 ? 23.223 -32.231 6.317 1.00 88.07 ? 464 SER A N 1 ATOM 2437 C CA . SER A 1 325 ? 24.477 -31.650 5.865 1.00 83.34 ? 464 SER A CA 1 ATOM 2438 C C . SER A 1 325 ? 24.306 -31.033 4.480 1.00 77.86 ? 464 SER A C 1 ATOM 2439 O O . SER A 1 325 ? 25.283 -30.647 3.838 1.00 76.11 ? 464 SER A O 1 ATOM 2440 C CB . SER A 1 325 ? 25.571 -32.716 5.833 1.00 90.83 ? 464 SER A CB 1 ATOM 2441 O OG . SER A 1 325 ? 25.208 -33.785 4.977 1.00 94.60 ? 464 SER A OG 1 ATOM 2442 N N . ASN A 1 326 ? 23.059 -30.936 4.023 1.00 70.94 ? 465 ASN A N 1 ATOM 2443 C CA . ASN A 1 326 ? 22.776 -30.437 2.682 1.00 64.82 ? 465 ASN A CA 1 ATOM 2444 C C . ASN A 1 326 ? 21.921 -29.182 2.683 1.00 57.66 ? 465 ASN A C 1 ATOM 2445 O O . ASN A 1 326 ? 21.154 -28.933 3.616 1.00 57.88 ? 465 ASN A O 1 ATOM 2446 C CB . ASN A 1 326 ? 22.059 -31.502 1.843 1.00 71.02 ? 465 ASN A CB 1 ATOM 2447 C CG . ASN A 1 326 ? 22.770 -32.838 1.863 1.00 78.87 ? 465 ASN A CG 1 ATOM 2448 O OD1 . ASN A 1 326 ? 22.160 -33.878 2.125 1.00 84.99 ? 465 ASN A OD1 1 ATOM 2449 N ND2 . ASN A 1 326 ? 24.068 -32.819 1.589 1.00 79.54 ? 465 ASN A ND2 1 ATOM 2450 N N . GLU A 1 327 ? 22.077 -28.394 1.626 1.00 49.76 ? 466 GLU A N 1 ATOM 2451 C CA . GLU A 1 327 ? 21.129 -27.336 1.280 1.00 48.06 ? 466 GLU A CA 1 ATOM 2452 C C . GLU A 1 327 ? 20.621 -27.628 -0.126 1.00 49.47 ? 466 GLU A C 1 ATOM 2453 O O . GLU A 1 327 ? 21.402 -27.856 -1.052 1.00 50.52 ? 466 GLU A O 1 ATOM 2454 C CB . GLU A 1 327 ? 21.776 -25.948 1.337 1.00 47.82 ? 466 GLU A CB 1 ATOM 2455 C CG . GLU A 1 327 ? 22.155 -25.458 2.745 1.00 51.58 ? 466 GLU A CG 1 ATOM 2456 C CD . GLU A 1 327 ? 20.956 -25.254 3.667 1.00 53.03 ? 466 GLU A CD 1 ATOM 2457 O OE1 . GLU A 1 327 ? 19.810 -25.196 3.172 1.00 51.28 ? 466 GLU A OE1 1 ATOM 2458 O OE2 . GLU A 1 327 ? 21.162 -25.157 4.898 1.00 56.81 ? 466 GLU A OE2 1 ATOM 2459 N N . THR A 1 328 ? 19.305 -27.639 -0.275 1.00 48.37 ? 467 THR A N 1 ATOM 2460 C CA . THR A 1 328 ? 18.688 -27.922 -1.563 1.00 47.03 ? 467 THR A CA 1 ATOM 2461 C C . THR A 1 328 ? 18.112 -26.648 -2.183 1.00 41.06 ? 467 THR A C 1 ATOM 2462 O O . THR A 1 328 ? 17.412 -25.893 -1.513 1.00 43.10 ? 467 THR A O 1 ATOM 2463 C CB . THR A 1 328 ? 17.570 -28.965 -1.415 1.00 48.88 ? 467 THR A CB 1 ATOM 2464 O OG1 . THR A 1 328 ? 18.114 -30.167 -0.867 1.00 55.01 ? 467 THR A OG1 1 ATOM 2465 C CG2 . THR A 1 328 ? 16.945 -29.274 -2.759 1.00 48.20 ? 467 THR A CG2 1 ATOM 2466 N N . PHE A 1 329 ? 18.415 -26.423 -3.462 1.00 42.57 ? 468 PHE A N 1 ATOM 2467 C CA . PHE A 1 329 ? 17.905 -25.262 -4.189 1.00 42.63 ? 468 PHE A CA 1 ATOM 2468 C C . PHE A 1 329 ? 17.060 -25.675 -5.391 1.00 43.01 ? 468 PHE A C 1 ATOM 2469 O O . PHE A 1 329 ? 17.327 -26.687 -6.027 1.00 41.77 ? 468 PHE A O 1 ATOM 2470 C CB . PHE A 1 329 ? 19.054 -24.347 -4.617 1.00 37.52 ? 468 PHE A CB 1 ATOM 2471 C CG . PHE A 1 329 ? 19.883 -23.868 -3.466 1.00 41.77 ? 468 PHE A CG 1 ATOM 2472 C CD1 . PHE A 1 329 ? 19.703 -22.599 -2.949 1.00 38.26 ? 468 PHE A CD1 1 ATOM 2473 C CD2 . PHE A 1 329 ? 20.809 -24.715 -2.863 1.00 44.75 ? 468 PHE A CD2 1 ATOM 2474 C CE1 . PHE A 1 329 ? 20.454 -22.161 -1.879 1.00 35.24 ? 468 PHE A CE1 1 ATOM 2475 C CE2 . PHE A 1 329 ? 21.572 -24.279 -1.783 1.00 46.11 ? 468 PHE A CE2 1 ATOM 2476 C CZ . PHE A 1 329 ? 21.387 -23.006 -1.288 1.00 34.43 ? 468 PHE A CZ 1 ATOM 2477 N N . ARG A 1 330 ? 16.027 -24.889 -5.677 1.00 40.70 ? 469 ARG A N 1 ATOM 2478 C CA . ARG A 1 330 ? 15.129 -25.193 -6.784 1.00 39.17 ? 469 ARG A CA 1 ATOM 2479 C C . ARG A 1 330 ? 14.984 -23.921 -7.611 1.00 37.41 ? 469 ARG A C 1 ATOM 2480 O O . ARG A 1 330 ? 14.905 -22.840 -7.056 1.00 36.85 ? 469 ARG A O 1 ATOM 2481 C CB . ARG A 1 330 ? 13.766 -25.665 -6.260 1.00 39.68 ? 469 ARG A CB 1 ATOM 2482 C CG . ARG A 1 330 ? 13.849 -26.862 -5.309 1.00 40.38 ? 469 ARG A CG 1 ATOM 2483 C CD . ARG A 1 330 ? 12.493 -27.287 -4.757 1.00 39.22 ? 469 ARG A CD 1 ATOM 2484 N NE . ARG A 1 330 ? 12.646 -28.281 -3.683 1.00 44.89 ? 469 ARG A NE 1 ATOM 2485 C CZ . ARG A 1 330 ? 12.535 -29.600 -3.836 1.00 47.42 ? 469 ARG A CZ 1 ATOM 2486 N NH1 . ARG A 1 330 ? 12.257 -30.125 -5.023 1.00 47.98 ? 469 ARG A NH1 1 ATOM 2487 N NH2 . ARG A 1 330 ? 12.696 -30.406 -2.788 1.00 46.53 ? 469 ARG A NH2 1 ATOM 2488 N N . PRO A 1 331 ? 14.976 -24.049 -8.940 1.00 37.34 ? 470 PRO A N 1 ATOM 2489 C CA . PRO A 1 331 ? 14.927 -22.808 -9.704 1.00 35.74 ? 470 PRO A CA 1 ATOM 2490 C C . PRO A 1 331 ? 13.573 -22.174 -9.514 1.00 37.70 ? 470 PRO A C 1 ATOM 2491 O O . PRO A 1 331 ? 12.601 -22.852 -9.177 1.00 41.53 ? 470 PRO A O 1 ATOM 2492 C CB . PRO A 1 331 ? 15.147 -23.261 -11.143 1.00 36.48 ? 470 PRO A CB 1 ATOM 2493 C CG . PRO A 1 331 ? 14.785 -24.715 -11.164 1.00 39.85 ? 470 PRO A CG 1 ATOM 2494 C CD . PRO A 1 331 ? 15.059 -25.250 -9.794 1.00 38.91 ? 470 PRO A CD 1 ATOM 2495 N N . GLY A 1 332 ? 13.531 -20.865 -9.672 1.00 42.80 ? 471 GLY A N 1 ATOM 2496 C CA . GLY A 1 332 ? 12.276 -20.156 -9.676 1.00 55.12 ? 471 GLY A CA 1 ATOM 2497 C C . GLY A 1 332 ? 12.278 -19.136 -8.577 1.00 67.06 ? 471 GLY A C 1 ATOM 2498 O O . GLY A 1 332 ? 12.555 -19.459 -7.421 1.00 59.81 ? 471 GLY A O 1 ATOM 2499 N N . GLY A 1 333 ? 12.018 -17.892 -8.958 1.00 80.55 ? 472 GLY A N 1 ATOM 2500 C CA . GLY A 1 333 ? 11.743 -16.838 -8.008 1.00 91.15 ? 472 GLY A CA 1 ATOM 2501 C C . GLY A 1 333 ? 10.239 -16.719 -7.966 1.00 101.32 ? 472 GLY A C 1 ATOM 2502 O O . GLY A 1 333 ? 9.552 -17.210 -8.864 1.00 105.93 ? 472 GLY A O 1 ATOM 2503 N N . GLY A 1 334 ? 9.713 -16.078 -6.933 1.00 101.20 ? 473 GLY A N 1 ATOM 2504 C CA . GLY A 1 334 ? 8.274 -15.991 -6.800 1.00 96.77 ? 473 GLY A CA 1 ATOM 2505 C C . GLY A 1 334 ? 7.714 -14.617 -7.085 1.00 85.65 ? 473 GLY A C 1 ATOM 2506 O O . GLY A 1 334 ? 6.729 -14.226 -6.454 1.00 86.93 ? 473 GLY A O 1 ATOM 2507 N N . ASN A 1 335 ? 8.304 -13.895 -8.040 1.00 72.32 ? 474 ASN A N 1 ATOM 2508 C CA . ASN A 1 335 ? 7.994 -12.474 -8.182 1.00 53.59 ? 474 ASN A CA 1 ATOM 2509 C C . ASN A 1 335 ? 8.703 -11.734 -9.325 1.00 39.82 ? 474 ASN A C 1 ATOM 2510 O O . ASN A 1 335 ? 9.914 -11.540 -9.268 1.00 31.57 ? 474 ASN A O 1 ATOM 2511 C CB . ASN A 1 335 ? 8.371 -11.797 -6.870 1.00 52.95 ? 474 ASN A CB 1 ATOM 2512 C CG . ASN A 1 335 ? 7.663 -10.494 -6.668 1.00 46.27 ? 474 ASN A CG 1 ATOM 2513 O OD1 . ASN A 1 335 ? 7.304 -9.813 -7.627 1.00 46.55 ? 474 ASN A OD1 1 ATOM 2514 N ND2 . ASN A 1 335 ? 7.434 -10.139 -5.406 1.00 53.46 ? 474 ASN A ND2 1 ATOM 2515 N N . ILE A 1 336 ? 7.958 -11.291 -10.338 1.00 31.65 ? 475 ILE A N 1 ATOM 2516 C CA . ILE A 1 336 ? 8.574 -10.538 -11.446 1.00 32.20 ? 475 ILE A CA 1 ATOM 2517 C C . ILE A 1 336 ? 9.306 -9.290 -10.969 1.00 30.53 ? 475 ILE A C 1 ATOM 2518 O O . ILE A 1 336 ? 10.227 -8.790 -11.634 1.00 31.13 ? 475 ILE A O 1 ATOM 2519 C CB . ILE A 1 336 ? 7.550 -10.165 -12.558 1.00 34.81 ? 475 ILE A CB 1 ATOM 2520 C CG1 . ILE A 1 336 ? 6.870 -11.424 -13.090 1.00 38.29 ? 475 ILE A CG1 1 ATOM 2521 C CG2 . ILE A 1 336 ? 8.239 -9.433 -13.704 1.00 34.25 ? 475 ILE A CG2 1 ATOM 2522 C CD1 . ILE A 1 336 ? 7.826 -12.421 -13.752 1.00 37.77 ? 475 ILE A CD1 1 ATOM 2523 N N . LYS A 1 337 ? 8.917 -8.766 -9.813 1.00 31.23 ? 476 LYS A N 1 ATOM 2524 C CA . LYS A 1 337 ? 9.623 -7.597 -9.312 1.00 35.42 ? 476 LYS A CA 1 ATOM 2525 C C . LYS A 1 337 ? 11.095 -7.927 -9.090 1.00 33.67 ? 476 LYS A C 1 ATOM 2526 O O . LYS A 1 337 ? 11.950 -7.048 -9.193 1.00 36.51 ? 476 LYS A O 1 ATOM 2527 C CB . LYS A 1 337 ? 8.985 -7.050 -8.028 1.00 36.02 ? 476 LYS A CB 1 ATOM 2528 C CG . LYS A 1 337 ? 7.708 -6.274 -8.284 1.00 37.84 ? 476 LYS A CG 1 ATOM 2529 C CD . LYS A 1 337 ? 7.291 -5.473 -7.061 1.00 42.19 ? 476 LYS A CD 1 ATOM 2530 C CE . LYS A 1 337 ? 7.014 -6.364 -5.857 1.00 48.36 ? 476 LYS A CE 1 ATOM 2531 N NZ . LYS A 1 337 ? 6.505 -5.522 -4.722 1.00 55.17 ? 476 LYS A NZ 1 ATOM 2532 N N . ASP A 1 338 ? 11.392 -9.189 -8.785 1.00 31.25 ? 477 ASP A N 1 ATOM 2533 C CA . ASP A 1 338 ? 12.774 -9.569 -8.550 1.00 28.47 ? 477 ASP A CA 1 ATOM 2534 C C . ASP A 1 338 ? 13.580 -9.417 -9.826 1.00 30.60 ? 477 ASP A C 1 ATOM 2535 O O . ASP A 1 338 ? 14.763 -9.084 -9.769 1.00 29.92 ? 477 ASP A O 1 ATOM 2536 C CB . ASP A 1 338 ? 12.901 -10.978 -8.001 1.00 30.54 ? 477 ASP A CB 1 ATOM 2537 C CG . ASP A 1 338 ? 12.356 -11.102 -6.587 1.00 40.96 ? 477 ASP A CG 1 ATOM 2538 O OD1 . ASP A 1 338 ? 12.549 -10.171 -5.786 1.00 37.99 ? 477 ASP A OD1 1 ATOM 2539 O OD2 . ASP A 1 338 ? 11.740 -12.131 -6.289 1.00 41.81 ? 477 ASP A OD2 1 ATOM 2540 N N . ASN A 1 339 ? 12.941 -9.643 -10.979 1.00 30.11 ? 478 ASN A N 1 ATOM 2541 C CA . ASN A 1 339 ? 13.616 -9.375 -12.266 1.00 28.51 ? 478 ASN A CA 1 ATOM 2542 C C . ASN A 1 339 ? 14.101 -7.939 -12.348 1.00 28.33 ? 478 ASN A C 1 ATOM 2543 O O . ASN A 1 339 ? 15.211 -7.674 -12.820 1.00 28.32 ? 478 ASN A O 1 ATOM 2544 C CB . ASN A 1 339 ? 12.711 -9.680 -13.468 1.00 27.37 ? 478 ASN A CB 1 ATOM 2545 C CG . ASN A 1 339 ? 12.380 -11.166 -13.596 1.00 26.84 ? 478 ASN A CG 1 ATOM 2546 O OD1 . ASN A 1 339 ? 12.084 -11.832 -12.612 1.00 31.63 ? 478 ASN A OD1 1 ATOM 2547 N ND2 . ASN A 1 339 ? 12.405 -11.676 -14.832 1.00 28.41 ? 478 ASN A ND2 1 ATOM 2548 N N . TRP A 1 340 ? 13.284 -6.985 -11.907 1.00 27.74 ? 479 TRP A N 1 ATOM 2549 C CA . TRP A 1 340 ? 13.737 -5.597 -12.002 1.00 29.06 ? 479 TRP A CA 1 ATOM 2550 C C . TRP A 1 340 ? 14.771 -5.320 -10.912 1.00 28.42 ? 479 TRP A C 1 ATOM 2551 O O . TRP A 1 340 ? 15.719 -4.549 -11.129 1.00 29.36 ? 479 TRP A O 1 ATOM 2552 C CB . TRP A 1 340 ? 12.570 -4.600 -11.939 1.00 28.89 ? 479 TRP A CB 1 ATOM 2553 C CG . TRP A 1 340 ? 11.331 -5.093 -12.640 1.00 32.18 ? 479 TRP A CG 1 ATOM 2554 C CD1 . TRP A 1 340 ? 10.047 -5.031 -12.171 1.00 32.05 ? 479 TRP A CD1 1 ATOM 2555 C CD2 . TRP A 1 340 ? 11.263 -5.754 -13.914 1.00 30.60 ? 479 TRP A CD2 1 ATOM 2556 N NE1 . TRP A 1 340 ? 9.189 -5.603 -13.077 1.00 29.19 ? 479 TRP A NE1 1 ATOM 2557 C CE2 . TRP A 1 340 ? 9.907 -6.052 -14.154 1.00 30.84 ? 479 TRP A CE2 1 ATOM 2558 C CE3 . TRP A 1 340 ? 12.214 -6.117 -14.875 1.00 28.99 ? 479 TRP A CE3 1 ATOM 2559 C CZ2 . TRP A 1 340 ? 9.480 -6.710 -15.310 1.00 32.84 ? 479 TRP A CZ2 1 ATOM 2560 C CZ3 . TRP A 1 340 ? 11.792 -6.773 -16.026 1.00 30.34 ? 479 TRP A CZ3 1 ATOM 2561 C CH2 . TRP A 1 340 ? 10.438 -7.063 -16.233 1.00 30.68 ? 479 TRP A CH2 1 ATOM 2562 N N . ARG A 1 341 ? 14.570 -5.942 -9.746 1.00 27.36 ? 480 ARG A N 1 ATOM 2563 C CA . ARG A 1 341 ? 15.487 -5.818 -8.616 1.00 29.19 ? 480 ARG A CA 1 ATOM 2564 C C . ARG A 1 341 ? 16.890 -6.173 -9.084 1.00 28.51 ? 480 ARG A C 1 ATOM 2565 O O . ARG A 1 341 ? 17.871 -5.554 -8.679 1.00 32.89 ? 480 ARG A O 1 ATOM 2566 C CB . ARG A 1 341 ? 15.056 -6.776 -7.494 1.00 31.79 ? 480 ARG A CB 1 ATOM 2567 C CG . ARG A 1 341 ? 14.983 -6.213 -6.082 1.00 41.24 ? 480 ARG A CG 1 ATOM 2568 C CD . ARG A 1 341 ? 14.125 -7.140 -5.120 1.00 27.42 ? 480 ARG A CD 1 ATOM 2569 N NE . ARG A 1 341 ? 12.943 -6.399 -4.683 1.00 43.26 ? 480 ARG A NE 1 ATOM 2570 C CZ . ARG A 1 341 ? 11.694 -6.857 -4.695 1.00 48.67 ? 480 ARG A CZ 1 ATOM 2571 N NH1 . ARG A 1 341 ? 11.422 -8.095 -5.093 1.00 56.85 ? 480 ARG A NH1 1 ATOM 2572 N NH2 . ARG A 1 341 ? 10.708 -6.073 -4.276 1.00 55.91 ? 480 ARG A NH2 1 ATOM 2573 N N . SER A 1 342 ? 16.979 -7.196 -9.925 1.00 28.66 ? 481 SER A N 1 ATOM 2574 C CA . SER A 1 342 ? 18.271 -7.701 -10.365 1.00 29.65 ? 481 SER A CA 1 ATOM 2575 C C . SER A 1 342 ? 19.009 -6.673 -11.198 1.00 33.11 ? 481 SER A C 1 ATOM 2576 O O . SER A 1 342 ? 20.234 -6.690 -11.240 1.00 37.63 ? 481 SER A O 1 ATOM 2577 C CB . SER A 1 342 ? 18.130 -9.025 -11.147 1.00 28.36 ? 481 SER A CB 1 ATOM 2578 O OG . SER A 1 342 ? 17.633 -8.772 -12.456 1.00 31.85 ? 481 SER A OG 1 ATOM 2579 N N . GLU A 1 343 ? 18.264 -5.786 -11.855 1.00 29.52 ? 482 GLU A N 1 ATOM 2580 C CA . GLU A 1 343 ? 18.870 -4.693 -12.620 1.00 33.98 ? 482 GLU A CA 1 ATOM 2581 C C . GLU A 1 343 ? 18.991 -3.379 -11.834 1.00 29.45 ? 482 GLU A C 1 ATOM 2582 O O . GLU A 1 343 ? 19.868 -2.561 -12.106 1.00 29.74 ? 482 GLU A O 1 ATOM 2583 C CB . GLU A 1 343 ? 18.111 -4.467 -13.954 1.00 29.83 ? 482 GLU A CB 1 ATOM 2584 C CG . GLU A 1 343 ? 18.195 -5.654 -14.881 1.00 30.31 ? 482 GLU A CG 1 ATOM 2585 C CD . GLU A 1 343 ? 19.605 -5.828 -15.453 1.00 36.52 ? 482 GLU A CD 1 ATOM 2586 O OE1 . GLU A 1 343 ? 20.251 -4.804 -15.768 1.00 36.09 ? 482 GLU A OE1 1 ATOM 2587 O OE2 . GLU A 1 343 ? 20.077 -6.979 -15.566 1.00 32.66 ? 482 GLU A OE2 1 ATOM 2588 N N . LEU A 1 344 ? 18.127 -3.168 -10.844 1.00 27.38 ? 483 LEU A N 1 ATOM 2589 C CA . LEU A 1 344 ? 18.090 -1.873 -10.174 1.00 25.19 ? 483 LEU A CA 1 ATOM 2590 C C . LEU A 1 344 ? 18.826 -1.850 -8.830 1.00 26.95 ? 483 LEU A C 1 ATOM 2591 O O . LEU A 1 344 ? 18.858 -0.834 -8.163 1.00 30.05 ? 483 LEU A O 1 ATOM 2592 C CB . LEU A 1 344 ? 16.646 -1.447 -9.955 1.00 30.15 ? 483 LEU A CB 1 ATOM 2593 C CG . LEU A 1 344 ? 15.840 -1.146 -11.214 1.00 28.09 ? 483 LEU A CG 1 ATOM 2594 C CD1 . LEU A 1 344 ? 14.379 -1.207 -10.871 1.00 32.46 ? 483 LEU A CD1 1 ATOM 2595 C CD2 . LEU A 1 344 ? 16.245 0.233 -11.756 1.00 31.08 ? 483 LEU A CD2 1 ATOM 2596 N N . TYR A 1 345 ? 19.432 -2.969 -8.466 1.00 28.41 ? 484 TYR A N 1 ATOM 2597 C CA . TYR A 1 345 ? 19.984 -3.139 -7.118 1.00 31.61 ? 484 TYR A CA 1 ATOM 2598 C C . TYR A 1 345 ? 21.034 -2.085 -6.767 1.00 31.84 ? 484 TYR A C 1 ATOM 2599 O O . TYR A 1 345 ? 21.237 -1.771 -5.585 1.00 32.39 ? 484 TYR A O 1 ATOM 2600 C CB . TYR A 1 345 ? 20.594 -4.542 -6.968 1.00 31.02 ? 484 TYR A CB 1 ATOM 2601 C CG . TYR A 1 345 ? 21.877 -4.692 -7.758 1.00 34.04 ? 484 TYR A CG 1 ATOM 2602 C CD1 . TYR A 1 345 ? 21.848 -5.048 -9.103 1.00 40.07 ? 484 TYR A CD1 1 ATOM 2603 C CD2 . TYR A 1 345 ? 23.111 -4.452 -7.171 1.00 34.65 ? 484 TYR A CD2 1 ATOM 2604 C CE1 . TYR A 1 345 ? 23.003 -5.169 -9.837 1.00 38.85 ? 484 TYR A CE1 1 ATOM 2605 C CE2 . TYR A 1 345 ? 24.274 -4.572 -7.898 1.00 37.93 ? 484 TYR A CE2 1 ATOM 2606 C CZ . TYR A 1 345 ? 24.212 -4.929 -9.234 1.00 44.58 ? 484 TYR A CZ 1 ATOM 2607 O OH . TYR A 1 345 ? 25.363 -5.056 -9.972 1.00 52.59 ? 484 TYR A OH 1 ATOM 2608 N N . LYS A 1 346 ? 21.702 -1.554 -7.789 1.00 33.82 ? 485 LYS A N 1 ATOM 2609 C CA . LYS A 1 346 ? 22.814 -0.634 -7.591 1.00 34.75 ? 485 LYS A CA 1 ATOM 2610 C C . LYS A 1 346 ? 22.373 0.816 -7.600 1.00 31.55 ? 485 LYS A C 1 ATOM 2611 O O . LYS A 1 346 ? 23.201 1.734 -7.532 1.00 36.34 ? 485 LYS A O 1 ATOM 2612 C CB . LYS A 1 346 ? 23.908 -0.859 -8.641 1.00 36.69 ? 485 LYS A CB 1 ATOM 2613 C CG . LYS A 1 346 ? 23.461 -0.672 -10.088 1.00 37.69 ? 485 LYS A CG 1 ATOM 2614 C CD . LYS A 1 346 ? 24.661 -0.649 -11.039 1.00 47.04 ? 485 LYS A CD 1 ATOM 2615 C CE . LYS A 1 346 ? 25.568 -1.863 -10.876 1.00 56.74 ? 485 LYS A CE 1 ATOM 2616 N NZ . LYS A 1 346 ? 26.590 -1.964 -11.992 1.00 58.92 ? 485 LYS A NZ 1 ATOM 2617 N N . TYR A 1 347 ? 21.066 1.026 -7.660 1.00 30.29 ? 486 TYR A N 1 ATOM 2618 C CA . TYR A 1 347 ? 20.529 2.379 -7.713 1.00 31.55 ? 486 TYR A CA 1 ATOM 2619 C C . TYR A 1 347 ? 19.635 2.716 -6.536 1.00 32.10 ? 486 TYR A C 1 ATOM 2620 O O . TYR A 1 347 ? 18.910 1.860 -6.015 1.00 30.58 ? 486 TYR A O 1 ATOM 2621 C CB . TYR A 1 347 ? 19.674 2.560 -8.963 1.00 24.41 ? 486 TYR A CB 1 ATOM 2622 C CG . TYR A 1 347 ? 20.395 2.352 -10.278 1.00 30.38 ? 486 TYR A CG 1 ATOM 2623 C CD1 . TYR A 1 347 ? 21.347 3.257 -10.726 1.00 29.09 ? 486 TYR A CD1 1 ATOM 2624 C CD2 . TYR A 1 347 ? 20.111 1.255 -11.072 1.00 28.83 ? 486 TYR A CD2 1 ATOM 2625 C CE1 . TYR A 1 347 ? 22.011 3.058 -11.939 1.00 33.03 ? 486 TYR A CE1 1 ATOM 2626 C CE2 . TYR A 1 347 ? 20.763 1.046 -12.274 1.00 31.57 ? 486 TYR A CE2 1 ATOM 2627 C CZ . TYR A 1 347 ? 21.704 1.957 -12.709 1.00 32.73 ? 486 TYR A CZ 1 ATOM 2628 O OH . TYR A 1 347 ? 22.336 1.751 -13.921 1.00 29.91 ? 486 TYR A OH 1 ATOM 2629 N N . LYS A 1 348 ? 19.647 3.987 -6.161 1.00 30.35 ? 487 LYS A N 1 ATOM 2630 C CA . LYS A 1 348 ? 18.638 4.511 -5.254 1.00 32.82 ? 487 LYS A CA 1 ATOM 2631 C C . LYS A 1 348 ? 18.395 5.979 -5.550 1.00 34.92 ? 487 LYS A C 1 ATOM 2632 O O . LYS A 1 348 ? 19.275 6.694 -6.043 1.00 34.19 ? 487 LYS A O 1 ATOM 2633 C CB . LYS A 1 348 ? 19.018 4.312 -3.783 1.00 31.05 ? 487 LYS A CB 1 ATOM 2634 C CG . LYS A 1 348 ? 20.036 5.286 -3.253 1.00 36.50 ? 487 LYS A CG 1 ATOM 2635 C CD . LYS A 1 348 ? 20.206 5.100 -1.739 1.00 42.59 ? 487 LYS A CD 1 ATOM 2636 C CE . LYS A 1 348 ? 21.420 5.844 -1.222 1.00 44.76 ? 487 LYS A CE 1 ATOM 2637 N NZ . LYS A 1 348 ? 21.501 5.880 0.264 1.00 42.22 ? 487 LYS A NZ 1 ATOM 2638 N N . VAL A 1 349 ? 17.177 6.409 -5.274 1.00 36.17 ? 488 VAL A N 1 ATOM 2639 C CA . VAL A 1 349 ? 16.808 7.791 -5.455 1.00 36.24 ? 488 VAL A CA 1 ATOM 2640 C C . VAL A 1 349 ? 17.097 8.564 -4.165 1.00 36.95 ? 488 VAL A C 1 ATOM 2641 O O . VAL A 1 349 ? 16.849 8.081 -3.048 1.00 36.67 ? 488 VAL A O 1 ATOM 2642 C CB . VAL A 1 349 ? 15.330 7.905 -5.829 1.00 33.50 ? 488 VAL A CB 1 ATOM 2643 C CG1 . VAL A 1 349 ? 14.910 9.383 -5.938 1.00 32.62 ? 488 VAL A CG1 1 ATOM 2644 C CG2 . VAL A 1 349 ? 15.064 7.144 -7.132 1.00 32.40 ? 488 VAL A CG2 1 ATOM 2645 N N . VAL A 1 350 ? 17.682 9.740 -4.325 1.00 35.70 ? 489 VAL A N 1 ATOM 2646 C CA . VAL A 1 350 ? 17.803 10.658 -3.204 1.00 37.22 ? 489 VAL A CA 1 ATOM 2647 C C . VAL A 1 350 ? 17.266 12.026 -3.598 1.00 36.80 ? 489 VAL A C 1 ATOM 2648 O O . VAL A 1 350 ? 17.241 12.379 -4.773 1.00 38.84 ? 489 VAL A O 1 ATOM 2649 C CB . VAL A 1 350 ? 19.256 10.781 -2.706 1.00 41.55 ? 489 VAL A CB 1 ATOM 2650 C CG1 . VAL A 1 350 ? 19.812 9.399 -2.363 1.00 44.75 ? 489 VAL A CG1 1 ATOM 2651 C CG2 . VAL A 1 350 ? 20.122 11.483 -3.741 1.00 40.05 ? 489 VAL A CG2 1 ATOM 2652 N N . GLN A 1 351 ? 16.804 12.776 -2.603 1.00 42.29 ? 490 GLN A N 1 ATOM 2653 C CA . GLN A 1 351 ? 16.393 14.155 -2.802 1.00 46.17 ? 490 GLN A CA 1 ATOM 2654 C C . GLN A 1 351 ? 17.565 15.072 -2.510 1.00 51.29 ? 490 GLN A C 1 ATOM 2655 O O . GLN A 1 351 ? 18.221 14.924 -1.482 1.00 50.01 ? 490 GLN A O 1 ATOM 2656 C CB . GLN A 1 351 ? 15.258 14.504 -1.852 1.00 44.56 ? 490 GLN A CB 1 ATOM 2657 C CG . GLN A 1 351 ? 14.558 15.787 -2.206 1.00 44.94 ? 490 GLN A CG 1 ATOM 2658 C CD . GLN A 1 351 ? 13.303 15.995 -1.386 1.00 58.95 ? 490 GLN A CD 1 ATOM 2659 O OE1 . GLN A 1 351 ? 13.113 15.358 -0.346 1.00 60.18 ? 490 GLN A OE1 1 ATOM 2660 N NE2 . GLN A 1 351 ? 12.434 16.889 -1.851 1.00 64.49 ? 490 GLN A NE2 1 ATOM 2661 N N . ILE A 1 352 ? 17.830 16.008 -3.416 1.00 51.89 ? 491 ILE A N 1 ATOM 2662 C CA . ILE A 1 352 ? 18.889 16.990 -3.219 1.00 58.00 ? 491 ILE A CA 1 ATOM 2663 C C . ILE A 1 352 ? 18.373 18.147 -2.364 1.00 70.39 ? 491 ILE A C 1 ATOM 2664 O O . ILE A 1 352 ? 17.248 18.617 -2.551 1.00 66.95 ? 491 ILE A O 1 ATOM 2665 C CB . ILE A 1 352 ? 19.396 17.561 -4.558 1.00 56.98 ? 491 ILE A CB 1 ATOM 2666 C CG1 . ILE A 1 352 ? 19.943 16.453 -5.455 1.00 57.59 ? 491 ILE A CG1 1 ATOM 2667 C CG2 . ILE A 1 352 ? 20.477 18.617 -4.320 1.00 55.99 ? 491 ILE A CG2 1 ATOM 2668 C CD1 . ILE A 1 352 ? 21.169 15.759 -4.893 1.00 57.62 ? 491 ILE A CD1 1 ATOM 2669 N N . GLU A 1 353 ? 19.194 18.602 -1.425 1.00 80.77 ? 492 GLU A N 1 ATOM 2670 C CA . GLU A 1 353 ? 18.828 19.743 -0.594 1.00 91.57 ? 492 GLU A CA 1 ATOM 2671 C C . GLU A 1 353 ? 18.998 21.043 -1.371 1.00 91.70 ? 492 GLU A C 1 ATOM 2672 O O . GLU A 1 353 ? 18.288 22.017 -1.129 1.00 92.32 ? 492 GLU A O 1 ATOM 2673 C CB . GLU A 1 353 ? 19.675 19.777 0.674 1.00 101.29 ? 492 GLU A CB 1 ATOM 2674 C CG . GLU A 1 353 ? 19.457 18.595 1.597 1.00 110.07 ? 492 GLU A CG 1 ATOM 2675 C CD . GLU A 1 353 ? 20.528 18.500 2.663 1.00 117.59 ? 492 GLU A CD 1 ATOM 2676 O OE1 . GLU A 1 353 ? 21.397 19.398 2.700 1.00 119.14 ? 492 GLU A OE1 1 ATOM 2677 O OE2 . GLU A 1 353 ? 20.507 17.530 3.454 1.00 121.06 ? 492 GLU A OE2 1 HETATM 2678 C C1 . NAG B 2 . ? 25.645 -8.559 1.956 1.00 49.06 ? 734 NAG A C1 1 HETATM 2679 C C2 . NAG B 2 . ? 25.207 -9.742 2.848 1.00 55.54 ? 734 NAG A C2 1 HETATM 2680 C C3 . NAG B 2 . ? 24.755 -9.279 4.253 1.00 58.55 ? 734 NAG A C3 1 HETATM 2681 C C4 . NAG B 2 . ? 25.887 -8.373 4.797 1.00 61.30 ? 734 NAG A C4 1 HETATM 2682 C C5 . NAG B 2 . ? 26.174 -7.229 3.789 1.00 62.91 ? 734 NAG A C5 1 HETATM 2683 C C6 . NAG B 2 . ? 27.285 -6.320 4.355 1.00 61.10 ? 734 NAG A C6 1 HETATM 2684 C C7 . NAG B 2 . ? 24.526 -11.561 1.351 1.00 68.64 ? 734 NAG A C7 1 HETATM 2685 C C8 . NAG B 2 . ? 23.414 -12.332 0.699 1.00 50.88 ? 734 NAG A C8 1 HETATM 2686 N N2 . NAG B 2 . ? 24.164 -10.520 2.193 1.00 70.38 ? 734 NAG A N2 1 HETATM 2687 O O3 . NAG B 2 . ? 24.584 -10.401 5.059 1.00 54.75 ? 734 NAG A O3 1 HETATM 2688 O O4 . NAG B 2 . ? 25.474 -7.799 5.997 1.00 53.48 ? 734 NAG A O4 1 HETATM 2689 O O5 . NAG B 2 . ? 26.650 -7.826 2.609 1.00 60.47 ? 734 NAG A O5 1 HETATM 2690 O O6 . NAG B 2 . ? 26.660 -5.260 5.012 1.00 66.07 ? 734 NAG A O6 1 HETATM 2691 O O7 . NAG B 2 . ? 25.707 -11.835 1.151 1.00 71.40 ? 734 NAG A O7 1 HETATM 2692 C C1 . NAG C 2 . ? 34.530 3.495 -9.156 1.00 66.04 ? 741 NAG A C1 1 HETATM 2693 C C2 . NAG C 2 . ? 36.025 3.363 -9.486 1.00 78.82 ? 741 NAG A C2 1 HETATM 2694 C C3 . NAG C 2 . ? 36.415 3.459 -10.971 1.00 83.27 ? 741 NAG A C3 1 HETATM 2695 C C4 . NAG C 2 . ? 35.289 3.143 -11.949 1.00 84.42 ? 741 NAG A C4 1 HETATM 2696 C C5 . NAG C 2 . ? 33.998 3.759 -11.437 1.00 80.62 ? 741 NAG A C5 1 HETATM 2697 C C6 . NAG C 2 . ? 32.848 3.588 -12.421 1.00 81.15 ? 741 NAG A C6 1 HETATM 2698 C C7 . NAG C 2 . ? 37.441 4.189 -7.670 1.00 89.38 ? 741 NAG A C7 1 HETATM 2699 C C8 . NAG C 2 . ? 37.727 5.388 -6.810 1.00 90.06 ? 741 NAG A C8 1 HETATM 2700 N N2 . NAG C 2 . ? 36.731 4.416 -8.774 1.00 84.43 ? 741 NAG A N2 1 HETATM 2701 O O3 . NAG C 2 . ? 37.499 2.594 -11.238 1.00 84.44 ? 741 NAG A O3 1 HETATM 2702 O O4 . NAG C 2 . ? 35.610 3.663 -13.224 1.00 86.11 ? 741 NAG A O4 1 HETATM 2703 O O5 . NAG C 2 . ? 33.687 3.113 -10.225 1.00 74.39 ? 741 NAG A O5 1 HETATM 2704 O O6 . NAG C 2 . ? 32.444 2.239 -12.419 1.00 84.98 ? 741 NAG A O6 1 HETATM 2705 O O7 . NAG C 2 . ? 37.847 3.071 -7.349 1.00 91.18 ? 741 NAG A O7 1 HETATM 2706 C C1 . NAG D 2 . ? 17.275 -11.317 -25.976 1.00 29.46 ? 762 NAG A C1 1 HETATM 2707 C C2 . NAG D 2 . ? 15.848 -11.608 -26.452 1.00 31.98 ? 762 NAG A C2 1 HETATM 2708 C C3 . NAG D 2 . ? 15.952 -12.165 -27.872 1.00 39.13 ? 762 NAG A C3 1 HETATM 2709 C C4 . NAG D 2 . ? 16.604 -11.137 -28.795 1.00 40.68 ? 762 NAG A C4 1 HETATM 2710 C C5 . NAG D 2 . ? 17.962 -10.780 -28.192 1.00 38.29 ? 762 NAG A C5 1 HETATM 2711 C C6 . NAG D 2 . ? 18.704 -9.698 -28.977 1.00 39.90 ? 762 NAG A C6 1 HETATM 2712 C C7 . NAG D 2 . ? 14.012 -12.319 -24.998 1.00 28.95 ? 762 NAG A C7 1 HETATM 2713 C C8 . NAG D 2 . ? 13.443 -13.449 -24.177 1.00 28.48 ? 762 NAG A C8 1 HETATM 2714 N N2 . NAG D 2 . ? 15.170 -12.564 -25.597 1.00 30.67 ? 762 NAG A N2 1 HETATM 2715 O O3 . NAG D 2 . ? 14.685 -12.549 -28.341 1.00 35.74 ? 762 NAG A O3 1 HETATM 2716 O O4 . NAG D 2 . ? 16.746 -11.681 -30.094 1.00 41.66 ? 762 NAG A O4 1 HETATM 2717 O O5 . NAG D 2 . ? 17.770 -10.321 -26.866 1.00 36.87 ? 762 NAG A O5 1 HETATM 2718 O O6 . NAG D 2 . ? 17.971 -8.489 -28.952 1.00 41.78 ? 762 NAG A O6 1 HETATM 2719 O O7 . NAG D 2 . ? 13.407 -11.255 -25.095 1.00 33.81 ? 762 NAG A O7 1 HETATM 2720 C C1 . NAG E 2 . ? 16.331 -13.846 8.794 1.00 39.79 ? 776 NAG A C1 1 HETATM 2721 C C2 . NAG E 2 . ? 15.774 -12.973 9.941 1.00 44.74 ? 776 NAG A C2 1 HETATM 2722 C C3 . NAG E 2 . ? 15.757 -13.723 11.293 1.00 51.54 ? 776 NAG A C3 1 HETATM 2723 C C4 . NAG E 2 . ? 15.049 -15.076 11.031 1.00 53.31 ? 776 NAG A C4 1 HETATM 2724 C C5 . NAG E 2 . ? 15.757 -15.825 9.873 1.00 48.95 ? 776 NAG A C5 1 HETATM 2725 C C6 . NAG E 2 . ? 15.058 -17.180 9.641 1.00 46.98 ? 776 NAG A C6 1 HETATM 2726 C C7 . NAG E 2 . ? 15.877 -10.529 9.759 1.00 52.61 ? 776 NAG A C7 1 HETATM 2727 C C8 . NAG E 2 . ? 16.688 -9.272 9.879 1.00 52.50 ? 776 NAG A C8 1 HETATM 2728 N N2 . NAG E 2 . ? 16.519 -11.725 10.044 1.00 47.11 ? 776 NAG A N2 1 HETATM 2729 O O3 . NAG E 2 . ? 15.050 -12.960 12.218 1.00 49.11 ? 776 NAG A O3 1 HETATM 2730 O O4 . NAG E 2 . ? 15.137 -15.864 12.176 1.00 54.77 ? 776 NAG A O4 1 HETATM 2731 O O5 . NAG E 2 . ? 15.600 -15.042 8.716 1.00 47.03 ? 776 NAG A O5 1 HETATM 2732 O O6 . NAG E 2 . ? 13.717 -16.915 9.365 1.00 50.01 ? 776 NAG A O6 1 HETATM 2733 O O7 . NAG E 2 . ? 14.694 -10.507 9.423 1.00 54.31 ? 776 NAG A O7 1 HETATM 2734 C C1 . NAG F 2 . ? 33.033 -15.368 -12.086 1.00 48.69 ? 789 NAG A C1 1 HETATM 2735 C C2 . NAG F 2 . ? 34.498 -15.164 -12.491 1.00 60.68 ? 789 NAG A C2 1 HETATM 2736 C C3 . NAG F 2 . ? 35.460 -16.177 -11.858 1.00 67.10 ? 789 NAG A C3 1 HETATM 2737 C C4 . NAG F 2 . ? 35.100 -16.554 -10.425 1.00 65.02 ? 789 NAG A C4 1 HETATM 2738 C C5 . NAG F 2 . ? 33.594 -16.687 -10.234 1.00 61.64 ? 789 NAG A C5 1 HETATM 2739 C C6 . NAG F 2 . ? 33.286 -17.002 -8.770 1.00 56.48 ? 789 NAG A C6 1 HETATM 2740 C C7 . NAG F 2 . ? 34.879 -14.183 -14.684 1.00 72.28 ? 789 NAG A C7 1 HETATM 2741 C C8 . NAG F 2 . ? 34.885 -14.402 -16.169 1.00 74.71 ? 789 NAG A C8 1 HETATM 2742 N N2 . NAG F 2 . ? 34.626 -15.254 -13.936 1.00 65.75 ? 789 NAG A N2 1 HETATM 2743 O O3 . NAG F 2 . ? 36.762 -15.633 -11.846 1.00 71.16 ? 789 NAG A O3 1 HETATM 2744 O O4 . NAG F 2 . ? 35.717 -17.781 -10.101 1.00 62.30 ? 789 NAG A O4 1 HETATM 2745 O O5 . NAG F 2 . ? 32.959 -15.504 -10.677 1.00 59.06 ? 789 NAG A O5 1 HETATM 2746 O O6 . NAG F 2 . ? 32.369 -16.094 -8.207 1.00 50.36 ? 789 NAG A O6 1 HETATM 2747 O O7 . NAG F 2 . ? 35.093 -13.063 -14.210 1.00 74.15 ? 789 NAG A O7 1 HETATM 2748 C C1 . NAG G 2 . ? 19.733 -21.799 -32.741 1.00 50.08 ? 795 NAG A C1 1 HETATM 2749 C C2 . NAG G 2 . ? 20.914 -21.454 -33.654 1.00 54.34 ? 795 NAG A C2 1 HETATM 2750 C C3 . NAG G 2 . ? 20.520 -21.634 -35.110 1.00 64.75 ? 795 NAG A C3 1 HETATM 2751 C C4 . NAG G 2 . ? 20.022 -23.047 -35.358 1.00 69.99 ? 795 NAG A C4 1 HETATM 2752 C C5 . NAG G 2 . ? 19.080 -23.590 -34.276 1.00 66.84 ? 795 NAG A C5 1 HETATM 2753 C C6 . NAG G 2 . ? 19.176 -25.114 -34.329 1.00 64.75 ? 795 NAG A C6 1 HETATM 2754 C C7 . NAG G 2 . ? 22.549 -19.866 -32.816 1.00 54.19 ? 795 NAG A C7 1 HETATM 2755 C C8 . NAG G 2 . ? 22.976 -18.428 -32.709 1.00 55.60 ? 795 NAG A C8 1 HETATM 2756 N N2 . NAG G 2 . ? 21.410 -20.103 -33.475 1.00 47.84 ? 795 NAG A N2 1 HETATM 2757 O O3 . NAG G 2 . ? 21.636 -21.404 -35.946 1.00 65.32 ? 795 NAG A O3 1 HETATM 2758 O O4 . NAG G 2 . ? 19.362 -23.042 -36.607 1.00 72.55 ? 795 NAG A O4 1 HETATM 2759 O O5 . NAG G 2 . ? 19.373 -23.158 -32.947 1.00 60.76 ? 795 NAG A O5 1 HETATM 2760 O O6 . NAG G 2 . ? 18.214 -25.740 -33.505 1.00 63.21 ? 795 NAG A O6 1 HETATM 2761 O O7 . NAG G 2 . ? 23.230 -20.759 -32.299 1.00 55.81 ? 795 NAG A O7 1 HETATM 2762 C C1 . NAG H 2 . ? 30.381 -25.186 -25.630 1.00 77.32 ? 834 NAG A C1 1 HETATM 2763 C C2 . NAG H 2 . ? 30.310 -26.059 -26.880 1.00 90.31 ? 834 NAG A C2 1 HETATM 2764 C C3 . NAG H 2 . ? 31.672 -26.638 -27.261 1.00 91.33 ? 834 NAG A C3 1 HETATM 2765 C C4 . NAG H 2 . ? 32.851 -25.707 -26.964 1.00 90.33 ? 834 NAG A C4 1 HETATM 2766 C C5 . NAG H 2 . ? 32.689 -24.936 -25.662 1.00 88.84 ? 834 NAG A C5 1 HETATM 2767 C C6 . NAG H 2 . ? 33.812 -23.921 -25.489 1.00 89.63 ? 834 NAG A C6 1 HETATM 2768 C C7 . NAG H 2 . ? 28.237 -27.328 -27.322 1.00 102.14 ? 834 NAG A C7 1 HETATM 2769 C C8 . NAG H 2 . ? 27.895 -28.749 -27.667 1.00 101.79 ? 834 NAG A C8 1 HETATM 2770 N N2 . NAG H 2 . ? 29.374 -27.150 -26.643 1.00 99.15 ? 834 NAG A N2 1 HETATM 2771 O O3 . NAG H 2 . ? 31.656 -26.942 -28.640 1.00 92.78 ? 834 NAG A O3 1 HETATM 2772 O O4 . NAG H 2 . ? 34.034 -26.468 -26.857 1.00 88.91 ? 834 NAG A O4 1 HETATM 2773 O O5 . NAG H 2 . ? 31.451 -24.270 -25.679 1.00 85.95 ? 834 NAG A O5 1 HETATM 2774 O O6 . NAG H 2 . ? 34.066 -23.739 -24.114 1.00 91.04 ? 834 NAG A O6 1 HETATM 2775 O O7 . NAG H 2 . ? 27.486 -26.407 -27.655 1.00 101.64 ? 834 NAG A O7 1 HETATM 2776 C C1 . NAG I 2 . ? 10.605 -31.946 -16.811 1.00 49.39 ? 886 NAG A C1 1 HETATM 2777 C C2 . NAG I 2 . ? 9.264 -32.251 -16.143 1.00 58.32 ? 886 NAG A C2 1 HETATM 2778 C C3 . NAG I 2 . ? 9.333 -33.500 -15.273 1.00 62.17 ? 886 NAG A C3 1 HETATM 2779 C C4 . NAG I 2 . ? 9.930 -34.623 -16.105 1.00 60.76 ? 886 NAG A C4 1 HETATM 2780 C C5 . NAG I 2 . ? 11.321 -34.197 -16.569 1.00 59.19 ? 886 NAG A C5 1 HETATM 2781 C C6 . NAG I 2 . ? 12.070 -35.317 -17.291 1.00 57.09 ? 886 NAG A C6 1 HETATM 2782 C C7 . NAG I 2 . ? 7.678 -30.488 -15.665 1.00 68.61 ? 886 NAG A C7 1 HETATM 2783 C C8 . NAG I 2 . ? 7.219 -29.427 -14.706 1.00 69.82 ? 886 NAG A C8 1 HETATM 2784 N N2 . NAG I 2 . ? 8.804 -31.123 -15.352 1.00 60.61 ? 886 NAG A N2 1 HETATM 2785 O O3 . NAG I 2 . ? 8.040 -33.831 -14.805 1.00 60.68 ? 886 NAG A O3 1 HETATM 2786 O O4 . NAG I 2 . ? 9.990 -35.820 -15.366 1.00 62.19 ? 886 NAG A O4 1 HETATM 2787 O O5 . NAG I 2 . ? 11.201 -33.073 -17.427 1.00 56.02 ? 886 NAG A O5 1 HETATM 2788 O O6 . NAG I 2 . ? 11.749 -35.327 -18.667 1.00 56.97 ? 886 NAG A O6 1 HETATM 2789 O O7 . NAG I 2 . ? 7.030 -30.735 -16.687 1.00 71.81 ? 886 NAG A O7 1 HETATM 2790 C C1 . NAG J 2 . ? 22.341 -35.489 -16.029 1.00 89.32 ? 892 NAG A C1 1 HETATM 2791 C C2 . NAG J 2 . ? 20.990 -35.986 -16.526 1.00 98.20 ? 892 NAG A C2 1 HETATM 2792 C C3 . NAG J 2 . ? 21.026 -37.486 -16.788 1.00 102.81 ? 892 NAG A C3 1 HETATM 2793 C C4 . NAG J 2 . ? 22.187 -37.867 -17.700 1.00 102.05 ? 892 NAG A C4 1 HETATM 2794 C C5 . NAG J 2 . ? 23.447 -37.017 -17.522 1.00 99.00 ? 892 NAG A C5 1 HETATM 2795 C C6 . NAG J 2 . ? 24.238 -36.997 -18.832 1.00 98.52 ? 892 NAG A C6 1 HETATM 2796 C C7 . NAG J 2 . ? 18.930 -34.870 -16.046 1.00 98.02 ? 892 NAG A C7 1 HETATM 2797 C C8 . NAG J 2 . ? 19.155 -34.237 -17.389 1.00 96.28 ? 892 NAG A C8 1 HETATM 2798 N N2 . NAG J 2 . ? 19.919 -35.643 -15.611 1.00 99.67 ? 892 NAG A N2 1 HETATM 2799 O O3 . NAG J 2 . ? 19.823 -37.864 -17.423 1.00 104.48 ? 892 NAG A O3 1 HETATM 2800 O O4 . NAG J 2 . ? 22.523 -39.219 -17.459 1.00 103.13 ? 892 NAG A O4 1 HETATM 2801 O O5 . NAG J 2 . ? 23.211 -35.671 -17.128 1.00 94.75 ? 892 NAG A O5 1 HETATM 2802 O O6 . NAG J 2 . ? 25.431 -37.743 -18.703 1.00 97.38 ? 892 NAG A O6 1 HETATM 2803 O O7 . NAG J 2 . ? 17.893 -34.676 -15.413 1.00 96.48 ? 892 NAG A O7 1 HETATM 2804 C C1 . NAG K 2 . ? 24.532 -11.249 -24.651 1.00 64.97 ? 948 NAG A C1 1 HETATM 2805 C C2 . NAG K 2 . ? 24.266 -9.778 -24.966 1.00 69.51 ? 948 NAG A C2 1 HETATM 2806 C C3 . NAG K 2 . ? 25.490 -9.099 -25.583 1.00 70.54 ? 948 NAG A C3 1 HETATM 2807 C C4 . NAG K 2 . ? 26.780 -9.490 -24.854 1.00 75.03 ? 948 NAG A C4 1 HETATM 2808 C C5 . NAG K 2 . ? 26.831 -11.000 -24.636 1.00 74.62 ? 948 NAG A C5 1 HETATM 2809 C C6 . NAG K 2 . ? 28.144 -11.488 -24.013 1.00 73.83 ? 948 NAG A C6 1 HETATM 2810 C C7 . NAG K 2 . ? 21.948 -9.135 -25.417 1.00 69.05 ? 948 NAG A C7 1 HETATM 2811 C C8 . NAG K 2 . ? 21.952 -8.416 -24.098 1.00 65.55 ? 948 NAG A C8 1 HETATM 2812 N N2 . NAG K 2 . ? 23.106 -9.655 -25.838 1.00 69.74 ? 948 NAG A N2 1 HETATM 2813 O O3 . NAG K 2 . ? 25.306 -7.700 -25.526 1.00 68.24 ? 948 NAG A O3 1 HETATM 2814 O O4 . NAG K 2 . ? 27.915 -9.095 -25.595 1.00 76.71 ? 948 NAG A O4 1 HETATM 2815 O O5 . NAG K 2 . ? 25.706 -11.379 -23.873 1.00 73.29 ? 948 NAG A O5 1 HETATM 2816 O O6 . NAG K 2 . ? 28.212 -11.247 -22.621 1.00 70.62 ? 948 NAG A O6 1 HETATM 2817 O O7 . NAG K 2 . ? 20.903 -9.222 -26.060 1.00 69.91 ? 948 NAG A O7 1 HETATM 2818 N N1 . EPE L 3 . ? 4.847 7.167 -16.712 1.00 37.10 ? 1 EPE A N1 1 HETATM 2819 C C2 . EPE L 3 . ? 5.776 6.320 -17.488 1.00 31.21 ? 1 EPE A C2 1 HETATM 2820 C C3 . EPE L 3 . ? 7.073 6.133 -16.701 1.00 31.82 ? 1 EPE A C3 1 HETATM 2821 N N4 . EPE L 3 . ? 6.864 5.700 -15.322 1.00 33.65 ? 1 EPE A N4 1 HETATM 2822 C C5 . EPE L 3 . ? 5.754 6.311 -14.602 1.00 37.94 ? 1 EPE A C5 1 HETATM 2823 C C6 . EPE L 3 . ? 4.497 6.488 -15.452 1.00 34.18 ? 1 EPE A C6 1 HETATM 2824 C C7 . EPE L 3 . ? 8.095 5.512 -14.555 1.00 29.55 ? 1 EPE A C7 1 HETATM 2825 C C8 . EPE L 3 . ? 7.959 4.608 -13.331 1.00 31.30 ? 1 EPE A C8 1 HETATM 2826 O O8 . EPE L 3 . ? 7.171 5.226 -12.335 1.00 34.97 ? 1 EPE A O8 1 HETATM 2827 C C9 . EPE L 3 . ? 3.608 7.331 -17.497 1.00 32.53 ? 1 EPE A C9 1 HETATM 2828 C C10 . EPE L 3 . ? 3.851 8.306 -18.638 1.00 31.80 ? 1 EPE A C10 1 HETATM 2829 S S . EPE L 3 . ? 2.245 8.811 -19.325 1.00 32.92 ? 1 EPE A S 1 HETATM 2830 O O1S . EPE L 3 . ? 2.523 9.712 -20.436 1.00 34.83 ? 1 EPE A O1S 1 HETATM 2831 O O2S . EPE L 3 . ? 1.559 7.616 -19.795 1.00 35.92 ? 1 EPE A O2S 1 HETATM 2832 O O3S . EPE L 3 . ? 1.466 9.380 -18.223 1.00 33.99 ? 1 EPE A O3S 1 HETATM 2833 O O . HOH M 4 . ? 15.529 -17.347 -25.416 1.00 31.54 ? 2 HOH A O 1 HETATM 2834 O O . HOH M 4 . ? 1.390 -18.029 -26.755 1.00 27.64 ? 3 HOH A O 1 HETATM 2835 O O . HOH M 4 . ? 14.579 -12.164 -17.683 1.00 33.93 ? 4 HOH A O 1 HETATM 2836 O O . HOH M 4 . ? 0.727 -15.309 -27.591 1.00 30.81 ? 5 HOH A O 1 HETATM 2837 O O . HOH M 4 . ? 11.055 7.249 -25.840 1.00 39.80 ? 6 HOH A O 1 HETATM 2838 O O . HOH M 4 . ? 11.258 -2.596 -3.049 1.00 32.64 ? 7 HOH A O 1 HETATM 2839 O O . HOH M 4 . ? 16.652 -9.185 -17.556 1.00 38.79 ? 8 HOH A O 1 HETATM 2840 O O . HOH M 4 . ? 15.235 -19.270 -0.422 1.00 33.49 ? 9 HOH A O 1 HETATM 2841 O O . HOH M 4 . ? 8.261 -7.270 -21.783 1.00 27.07 ? 10 HOH A O 1 HETATM 2842 O O . HOH M 4 . ? 21.271 -9.072 -9.845 1.00 35.09 ? 11 HOH A O 1 HETATM 2843 O O . HOH M 4 . ? 0.369 -19.041 -29.210 1.00 33.50 ? 12 HOH A O 1 HETATM 2844 O O . HOH M 4 . ? 19.132 -0.386 -4.512 1.00 30.28 ? 13 HOH A O 1 HETATM 2845 O O . HOH M 4 . ? -3.293 -13.860 -29.823 1.00 42.57 ? 14 HOH A O 1 HETATM 2846 O O . HOH M 4 . ? 8.083 8.753 -18.554 1.00 31.27 ? 15 HOH A O 1 HETATM 2847 O O . HOH M 4 . ? 17.104 -16.300 1.227 1.00 31.87 ? 16 HOH A O 1 HETATM 2848 O O . HOH M 4 . ? 2.298 -1.032 -27.000 1.00 30.99 ? 17 HOH A O 1 HETATM 2849 O O . HOH M 4 . ? 3.527 -13.984 -32.142 1.00 36.55 ? 18 HOH A O 1 HETATM 2850 O O . HOH M 4 . ? 2.692 -5.079 -32.908 1.00 33.30 ? 19 HOH A O 1 HETATM 2851 O O . HOH M 4 . ? 15.905 5.899 -1.797 1.00 43.64 ? 20 HOH A O 1 HETATM 2852 O O . HOH M 4 . ? 1.588 -12.174 -31.095 1.00 38.55 ? 21 HOH A O 1 HETATM 2853 O O . HOH M 4 . ? 11.278 8.273 -27.779 1.00 51.74 ? 22 HOH A O 1 HETATM 2854 O O . HOH M 4 . ? 17.635 -19.220 1.237 1.00 34.20 ? 23 HOH A O 1 HETATM 2855 O O . HOH M 4 . ? -0.347 -23.858 -14.554 1.00 37.70 ? 24 HOH A O 1 HETATM 2856 O O . HOH M 4 . ? 15.802 2.293 -25.899 1.00 34.10 ? 25 HOH A O 1 HETATM 2857 O O . HOH M 4 . ? 15.332 -12.074 -1.036 1.00 28.86 ? 26 HOH A O 1 HETATM 2858 O O . HOH M 4 . ? 0.998 -12.835 -18.754 1.00 39.85 ? 27 HOH A O 1 HETATM 2859 O O . HOH M 4 . ? 10.987 -27.372 -15.403 1.00 41.84 ? 28 HOH A O 1 HETATM 2860 O O . HOH M 4 . ? 30.841 -8.955 -9.563 1.00 42.50 ? 29 HOH A O 1 HETATM 2861 O O . HOH M 4 . ? -0.944 -4.666 -29.340 1.00 42.36 ? 30 HOH A O 1 HETATM 2862 O O . HOH M 4 . ? 27.692 -2.294 -7.920 1.00 41.08 ? 31 HOH A O 1 HETATM 2863 O O . HOH M 4 . ? 22.541 -3.708 -13.077 1.00 44.68 ? 32 HOH A O 1 HETATM 2864 O O . HOH M 4 . ? 15.287 4.418 -4.393 1.00 33.25 ? 33 HOH A O 1 HETATM 2865 O O . HOH M 4 . ? 10.972 -11.215 -23.996 1.00 31.24 ? 34 HOH A O 1 HETATM 2866 O O . HOH M 4 . ? -2.512 -17.481 -35.258 1.00 45.12 ? 35 HOH A O 1 HETATM 2867 O O . HOH M 4 . ? 29.141 3.728 -13.403 1.00 51.20 ? 36 HOH A O 1 HETATM 2868 O O . HOH M 4 . ? 32.327 7.456 -3.553 1.00 44.33 ? 37 HOH A O 1 HETATM 2869 O O . HOH M 4 . ? 24.883 -21.867 -24.780 1.00 51.11 ? 38 HOH A O 1 HETATM 2870 O O . HOH M 4 . ? 17.358 -14.000 -31.127 1.00 40.04 ? 39 HOH A O 1 HETATM 2871 O O . HOH M 4 . ? 16.762 -6.513 -18.162 1.00 36.47 ? 40 HOH A O 1 HETATM 2872 O O . HOH M 4 . ? 15.001 -7.590 -26.886 1.00 31.27 ? 41 HOH A O 1 HETATM 2873 O O . HOH M 4 . ? 14.997 -9.082 -24.478 1.00 30.01 ? 42 HOH A O 1 HETATM 2874 O O . HOH M 4 . ? -2.442 -22.452 -18.411 1.00 47.36 ? 43 HOH A O 1 HETATM 2875 O O . HOH M 4 . ? 0.504 -1.446 -29.311 1.00 47.64 ? 125 HOH A O 1 HETATM 2876 O O . HOH M 4 . ? 18.878 -30.198 -29.756 1.00 52.21 ? 126 HOH A O 1 HETATM 2877 O O . HOH M 4 . ? 7.710 -29.356 -21.892 1.00 57.21 ? 127 HOH A O 1 HETATM 2878 O O . HOH M 4 . ? 8.611 -31.259 -20.126 1.00 55.86 ? 128 HOH A O 1 HETATM 2879 O O . HOH M 4 . ? 10.405 17.333 -8.986 1.00 53.54 ? 129 HOH A O 1 HETATM 2880 O O . HOH M 4 . ? 19.103 3.035 1.478 1.00 50.24 ? 130 HOH A O 1 HETATM 2881 O O . HOH M 4 . ? 21.387 -8.865 -1.083 1.00 40.93 ? 131 HOH A O 1 HETATM 2882 O O . HOH M 4 . ? 9.783 -25.013 -5.815 1.00 57.39 ? 132 HOH A O 1 HETATM 2883 O O . HOH M 4 . ? 8.471 17.496 -10.942 1.00 51.88 ? 133 HOH A O 1 HETATM 2884 O O . HOH M 4 . ? 5.271 2.857 -5.987 1.00 57.24 ? 134 HOH A O 1 HETATM 2885 O O . HOH M 4 . ? 20.212 -4.502 -18.858 1.00 59.15 ? 135 HOH A O 1 HETATM 2886 O O . HOH M 4 . ? 22.363 1.638 -21.135 1.00 42.48 ? 136 HOH A O 1 HETATM 2887 O O . HOH M 4 . ? 11.330 -17.737 -3.188 1.00 53.12 ? 137 HOH A O 1 HETATM 2888 O O . HOH M 4 . ? 12.724 -4.221 -30.556 1.00 51.19 ? 138 HOH A O 1 HETATM 2889 O O . HOH M 4 . ? 5.760 -13.149 -38.671 1.00 53.52 ? 139 HOH A O 1 HETATM 2890 O O . HOH M 4 . ? 27.846 -13.457 -3.045 1.00 47.05 ? 140 HOH A O 1 HETATM 2891 O O . HOH M 4 . ? 1.114 -11.976 -28.293 1.00 45.29 ? 141 HOH A O 1 HETATM 2892 O O . HOH M 4 . ? -11.426 -12.731 -30.334 1.00 54.60 ? 142 HOH A O 1 HETATM 2893 O O . HOH M 4 . ? 0.841 -28.630 -26.867 1.00 47.34 ? 143 HOH A O 1 HETATM 2894 O O . HOH M 4 . ? 10.184 -9.889 -33.157 1.00 51.47 ? 144 HOH A O 1 HETATM 2895 O O . HOH M 4 . ? 10.324 -24.759 -2.818 1.00 51.29 ? 145 HOH A O 1 HETATM 2896 O O . HOH M 4 . ? 4.560 4.357 -7.543 1.00 56.73 ? 146 HOH A O 1 HETATM 2897 O O . HOH M 4 . ? 12.892 -33.459 -4.152 1.00 58.80 ? 147 HOH A O 1 HETATM 2898 O O . HOH M 4 . ? 4.681 -22.886 -39.757 1.00 58.34 ? 148 HOH A O 1 HETATM 2899 O O . HOH M 4 . ? 9.359 -9.893 -21.866 1.00 27.45 ? 493 HOH A O 1 HETATM 2900 O O . HOH M 4 . ? 21.024 -10.630 -14.667 1.00 35.99 ? 494 HOH A O 1 HETATM 2901 O O . HOH M 4 . ? 5.636 11.857 -7.042 1.00 51.35 ? 495 HOH A O 1 HETATM 2902 O O . HOH M 4 . ? 10.616 -14.223 -12.177 1.00 33.84 ? 496 HOH A O 1 HETATM 2903 O O . HOH M 4 . ? 6.313 3.252 -32.121 1.00 32.02 ? 497 HOH A O 1 HETATM 2904 O O . HOH M 4 . ? 1.562 -1.862 -32.196 1.00 41.55 ? 498 HOH A O 1 HETATM 2905 O O . HOH M 4 . ? 0.326 -28.714 -29.853 1.00 48.13 ? 499 HOH A O 1 HETATM 2906 O O . HOH M 4 . ? 10.812 -11.518 -28.892 1.00 48.25 ? 500 HOH A O 1 HETATM 2907 O O . HOH M 4 . ? 13.736 -27.838 -12.852 1.00 36.90 ? 501 HOH A O 1 HETATM 2908 O O . HOH M 4 . ? 17.760 -26.626 2.211 1.00 43.18 ? 502 HOH A O 1 HETATM 2909 O O . HOH M 4 . ? 23.271 6.239 3.055 1.00 49.33 ? 503 HOH A O 1 HETATM 2910 O O . HOH M 4 . ? 26.476 -11.808 -1.505 1.00 51.25 ? 504 HOH A O 1 HETATM 2911 O O . HOH M 4 . ? 19.008 -9.013 -14.693 1.00 43.63 ? 505 HOH A O 1 HETATM 2912 O O . HOH M 4 . ? 7.768 -4.803 -36.040 1.00 46.88 ? 506 HOH A O 1 HETATM 2913 O O . HOH M 4 . ? 15.898 -28.267 -11.050 1.00 50.88 ? 507 HOH A O 1 HETATM 2914 O O . HOH M 4 . ? -0.370 -22.486 -16.952 1.00 38.69 ? 508 HOH A O 1 HETATM 2915 O O . HOH M 4 . ? -13.155 -15.712 -14.964 1.00 54.51 ? 509 HOH A O 1 HETATM 2916 O O . HOH M 4 . ? 31.154 -17.654 -14.790 1.00 51.85 ? 510 HOH A O 1 HETATM 2917 O O . HOH M 4 . ? 30.080 -2.725 -1.320 1.00 47.54 ? 511 HOH A O 1 HETATM 2918 O O . HOH M 4 . ? 3.710 -12.188 -34.260 1.00 38.88 ? 512 HOH A O 1 HETATM 2919 O O . HOH M 4 . ? 21.710 9.294 1.198 1.00 43.48 ? 513 HOH A O 1 HETATM 2920 O O . HOH M 4 . ? 12.640 3.251 -1.774 1.00 42.59 ? 514 HOH A O 1 HETATM 2921 O O . HOH M 4 . ? 22.177 -8.056 6.388 1.00 52.37 ? 515 HOH A O 1 HETATM 2922 O O . HOH M 4 . ? 10.421 -13.235 -21.788 1.00 35.65 ? 516 HOH A O 1 HETATM 2923 O O . HOH M 4 . ? 8.291 -15.566 -10.437 1.00 50.59 ? 517 HOH A O 1 HETATM 2924 O O . HOH M 4 . ? -0.609 -14.409 -29.748 1.00 36.40 ? 518 HOH A O 1 HETATM 2925 O O . HOH M 4 . ? 4.454 4.211 -11.580 1.00 44.34 ? 519 HOH A O 1 HETATM 2926 O O . HOH M 4 . ? 11.670 -29.267 -13.839 1.00 44.06 ? 520 HOH A O 1 HETATM 2927 O O . HOH M 4 . ? 6.122 9.849 -16.552 1.00 40.45 ? 521 HOH A O 1 HETATM 2928 O O . HOH M 4 . ? 9.631 7.214 -30.596 1.00 40.29 ? 522 HOH A O 1 HETATM 2929 O O . HOH M 4 . ? -2.557 -14.705 -12.542 1.00 44.66 ? 523 HOH A O 1 HETATM 2930 O O . HOH M 4 . ? 12.905 -24.568 -2.386 1.00 44.82 ? 524 HOH A O 1 HETATM 2931 O O . HOH M 4 . ? 19.421 -18.395 -34.268 1.00 48.80 ? 525 HOH A O 1 HETATM 2932 O O . HOH M 4 . ? 0.434 -0.292 -13.777 1.00 45.17 ? 526 HOH A O 1 HETATM 2933 O O . HOH M 4 . ? 0.158 -4.350 -32.012 1.00 46.67 ? 527 HOH A O 1 HETATM 2934 O O . HOH M 4 . ? -16.359 -9.316 -23.575 1.00 55.52 ? 528 HOH A O 1 HETATM 2935 O O . HOH M 4 . ? 14.411 -9.763 -16.367 1.00 40.79 ? 529 HOH A O 1 HETATM 2936 O O . HOH M 4 . ? 10.929 -25.253 1.747 1.00 51.96 ? 530 HOH A O 1 HETATM 2937 O O . HOH M 4 . ? 30.129 9.293 3.096 1.00 49.88 ? 531 HOH A O 1 HETATM 2938 O O . HOH M 4 . ? 1.101 1.414 -25.979 1.00 42.92 ? 532 HOH A O 1 HETATM 2939 O O . HOH M 4 . ? 7.418 -27.716 -33.655 1.00 48.06 ? 533 HOH A O 1 HETATM 2940 O O . HOH M 4 . ? 16.247 8.568 -28.068 1.00 44.07 ? 534 HOH A O 1 HETATM 2941 O O . HOH M 4 . ? 12.967 -10.866 -27.939 1.00 45.09 ? 535 HOH A O 1 HETATM 2942 O O . HOH M 4 . ? 15.051 -30.504 -18.905 1.00 45.71 ? 536 HOH A O 1 HETATM 2943 O O . HOH M 4 . ? 6.417 -11.295 -34.849 1.00 53.14 ? 537 HOH A O 1 HETATM 2944 O O . HOH M 4 . ? 27.408 -6.276 -7.618 1.00 45.76 ? 538 HOH A O 1 HETATM 2945 O O . HOH M 4 . ? 17.953 10.972 -28.030 1.00 44.03 ? 539 HOH A O 1 HETATM 2946 O O . HOH M 4 . ? 13.537 -12.404 6.649 1.00 40.71 ? 540 HOH A O 1 HETATM 2947 O O . HOH M 4 . ? 10.639 -23.003 -6.570 1.00 59.74 ? 541 HOH A O 1 HETATM 2948 O O . HOH M 4 . ? 14.687 14.035 -23.385 1.00 53.65 ? 542 HOH A O 1 HETATM 2949 O O . HOH M 4 . ? 10.472 -12.859 -3.997 1.00 51.39 ? 543 HOH A O 1 HETATM 2950 O O . HOH M 4 . ? 32.772 -18.070 3.716 1.00 53.36 ? 544 HOH A O 1 HETATM 2951 O O . HOH M 4 . ? 7.429 -10.429 -32.640 1.00 39.38 ? 545 HOH A O 1 HETATM 2952 O O . HOH M 4 . ? 9.227 14.867 -7.957 1.00 50.81 ? 546 HOH A O 1 HETATM 2953 O O . HOH M 4 . ? 1.244 -16.762 -39.203 1.00 60.57 ? 547 HOH A O 1 HETATM 2954 O O . HOH M 4 . ? 11.847 7.736 -33.725 1.00 43.28 ? 548 HOH A O 1 HETATM 2955 O O . HOH M 4 . ? 16.372 -25.478 5.691 1.00 48.86 ? 549 HOH A O 1 HETATM 2956 O O . HOH M 4 . ? 32.352 -19.574 -7.962 1.00 54.58 ? 550 HOH A O 1 HETATM 2957 O O . HOH M 4 . ? 15.195 -30.408 1.465 1.00 49.86 ? 551 HOH A O 1 HETATM 2958 O O . HOH M 4 . ? 30.558 -13.113 -4.641 1.00 42.67 ? 552 HOH A O 1 HETATM 2959 O O . HOH M 4 . ? 15.532 1.284 1.694 1.00 51.27 ? 553 HOH A O 1 HETATM 2960 O O . HOH M 4 . ? 3.321 -11.840 -37.198 1.00 54.16 ? 554 HOH A O 1 HETATM 2961 O O . HOH M 4 . ? 20.930 -32.242 -26.691 1.00 56.42 ? 555 HOH A O 1 HETATM 2962 O O . HOH M 4 . ? 7.028 10.806 -14.231 1.00 41.77 ? 556 HOH A O 1 HETATM 2963 O O . HOH M 4 . ? 4.441 -28.081 -13.049 1.00 46.76 ? 557 HOH A O 1 HETATM 2964 O O . HOH M 4 . ? -0.749 -11.571 -20.742 1.00 52.74 ? 558 HOH A O 1 HETATM 2965 O O . HOH M 4 . ? 2.173 -22.338 -36.105 1.00 34.56 ? 559 HOH A O 1 HETATM 2966 O O . HOH M 4 . ? -3.413 -11.401 -36.548 1.00 55.74 ? 560 HOH A O 1 HETATM 2967 O O . HOH M 4 . ? 14.821 -18.639 -22.990 1.00 33.63 ? 561 HOH A O 1 HETATM 2968 O O . HOH M 4 . ? 11.417 -13.258 -1.818 1.00 43.58 ? 562 HOH A O 1 HETATM 2969 O O . HOH M 4 . ? 4.020 4.746 -32.205 1.00 43.63 ? 563 HOH A O 1 HETATM 2970 O O . HOH M 4 . ? 3.364 6.339 -10.906 1.00 42.33 ? 564 HOH A O 1 HETATM 2971 O O . HOH M 4 . ? 9.461 -30.156 -12.346 1.00 60.41 ? 565 HOH A O 1 HETATM 2972 O O . HOH M 4 . ? 8.454 -29.439 -10.875 1.00 55.81 ? 566 HOH A O 1 HETATM 2973 O O . HOH M 4 . ? 18.634 -5.133 -19.915 1.00 37.79 ? 567 HOH A O 1 HETATM 2974 O O . HOH M 4 . ? 2.451 -14.985 -17.732 1.00 44.57 ? 568 HOH A O 1 HETATM 2975 O O . HOH M 4 . ? 5.945 -30.602 -11.158 1.00 57.36 ? 569 HOH A O 1 HETATM 2976 O O . HOH M 4 . ? 24.668 -1.983 -14.351 1.00 62.52 ? 570 HOH A O 1 HETATM 2977 O O . HOH M 4 . ? 11.568 -12.567 8.993 1.00 56.18 ? 571 HOH A O 1 HETATM 2978 O O . HOH M 4 . ? 25.917 -0.234 -15.021 1.00 53.94 ? 572 HOH A O 1 HETATM 2979 O O . HOH M 4 . ? 19.597 -32.582 -23.820 1.00 58.31 ? 573 HOH A O 1 HETATM 2980 O O . HOH M 4 . ? 20.926 -4.958 -21.076 1.00 52.31 ? 574 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . VAL A 1 ? 0.9347 0.9662 0.7468 -0.2664 -0.0432 -0.1966 44 VAL A N 2 C CA . VAL A 1 ? 0.9389 1.0007 0.7467 -0.2521 -0.0471 -0.1964 44 VAL A CA 3 C C . VAL A 1 ? 0.9016 0.9381 0.7076 -0.2262 -0.0417 -0.1882 44 VAL A C 4 O O . VAL A 1 ? 0.9034 0.8934 0.7052 -0.2221 -0.0352 -0.1891 44 VAL A O 5 C CB . VAL A 1 ? 0.9547 1.0222 0.7456 -0.2657 -0.0500 -0.2177 44 VAL A CB 6 C CG1 . VAL A 1 ? 0.9749 1.0794 0.7619 -0.2509 -0.0543 -0.2157 44 VAL A CG1 7 C CG2 . VAL A 1 ? 0.9291 1.0195 0.7221 -0.2938 -0.0555 -0.2270 44 VAL A CG2 8 N N . TRP A 2 ? 0.8374 0.9057 0.6475 -0.2087 -0.0442 -0.1795 45 TRP A N 9 C CA . TRP A 2 ? 0.7550 0.8078 0.5691 -0.1836 -0.0398 -0.1674 45 TRP A CA 10 C C . TRP A 2 ? 0.7140 0.7938 0.5257 -0.1670 -0.0413 -0.1662 45 TRP A C 11 O O . TRP A 2 ? 0.6911 0.8077 0.4992 -0.1738 -0.0463 -0.1721 45 TRP A O 12 C CB . TRP A 2 ? 0.7263 0.7897 0.5578 -0.1767 -0.0392 -0.1482 45 TRP A CB 13 C CG . TRP A 2 ? 0.7468 0.8632 0.5905 -0.1810 -0.0441 -0.1398 45 TRP A CG 14 C CD1 . TRP A 2 ? 0.7284 0.8850 0.5788 -0.1676 -0.0458 -0.1317 45 TRP A CD1 15 C CD2 . TRP A 2 ? 0.8012 0.9368 0.6533 -0.1994 -0.0469 -0.1374 45 TRP A CD2 16 N NE1 . TRP A 2 ? 0.7069 0.9071 0.5695 -0.1763 -0.0494 -0.1239 45 TRP A NE1 17 C CE2 . TRP A 2 ? 0.7321 0.9208 0.5961 -0.1960 -0.0504 -0.1273 45 TRP A CE2 18 C CE3 . TRP A 2 ? 0.8861 0.9997 0.7380 -0.2182 -0.0461 -0.1420 45 TRP A CE3 19 C CZ2 . TRP A 2 ? 0.7311 0.9519 0.6069 -0.2107 -0.0535 -0.1215 45 TRP A CZ2 20 C CZ3 . TRP A 2 ? 0.8845 1.0295 0.7479 -0.2332 -0.0493 -0.1369 45 TRP A CZ3 21 C CH2 . TRP A 2 ? 0.8045 1.0029 0.6798 -0.2293 -0.0531 -0.1266 45 TRP A CH2 22 N N . LYS A 3 ? 0.6926 0.7546 0.5065 -0.1453 -0.0368 -0.1582 46 LYS A N 23 C CA . LYS A 3 ? 0.6581 0.7426 0.4724 -0.1265 -0.0366 -0.1543 46 LYS A CA 24 C C . LYS A 3 ? 0.6291 0.7084 0.4574 -0.1051 -0.0328 -0.1371 46 LYS A C 25 O O . LYS A 3 ? 0.5909 0.6347 0.4210 -0.1025 -0.0295 -0.1332 46 LYS A O 26 C CB . LYS A 3 ? 0.6761 0.7345 0.4728 -0.1230 -0.0337 -0.1690 46 LYS A CB 27 C CG . LYS A 3 ? 0.9752 1.0451 0.7561 -0.1429 -0.0375 -0.1874 46 LYS A CG 28 C CD . LYS A 3 ? 1.1394 1.1822 0.9011 -0.1392 -0.0331 -0.2027 46 LYS A CD 29 C CE . LYS A 3 ? 1.2109 1.2588 0.9549 -0.1626 -0.0363 -0.2235 46 LYS A CE 30 N NZ . LYS A 3 ? 1.2490 1.2655 0.9722 -0.1608 -0.0304 -0.2401 46 LYS A NZ 31 N N . ASP A 4 ? 0.6097 0.7249 0.4479 -0.0904 -0.0330 -0.1267 47 ASP A N 32 C CA . ASP A 4 ? 0.6244 0.7358 0.4758 -0.0703 -0.0287 -0.1117 47 ASP A CA 33 C C . ASP A 4 ? 0.6661 0.7334 0.5104 -0.0593 -0.0246 -0.1156 47 ASP A C 34 O O . ASP A 4 ? 0.6395 0.6969 0.4719 -0.0561 -0.0236 -0.1259 47 ASP A O 35 C CB . ASP A 4 ? 0.6347 0.7874 0.4959 -0.0545 -0.0276 -0.1026 47 ASP A CB 36 C CG . ASP A 4 ? 0.6481 0.8482 0.5197 -0.0621 -0.0304 -0.0952 47 ASP A CG 37 O OD1 . ASP A 4 ? 0.6348 0.8367 0.5084 -0.0786 -0.0331 -0.0953 47 ASP A OD1 38 O OD2 . ASP A 4 ? 0.6912 0.9280 0.5705 -0.0506 -0.0292 -0.0879 47 ASP A OD2 39 N N . ALA A 5 ? 0.6514 0.6934 0.5027 -0.0532 -0.0221 -0.1068 48 ALA A N 40 C CA . ALA A 5 ? 0.6145 0.6165 0.4614 -0.0424 -0.0185 -0.1080 48 ALA A CA 41 C C . ALA A 5 ? 0.5900 0.5858 0.4503 -0.0291 -0.0165 -0.0935 48 ALA A C 42 O O . ALA A 5 ? 0.5820 0.5935 0.4517 -0.0325 -0.0174 -0.0847 48 ALA A O 43 C CB . ALA A 5 ? 0.6661 0.6296 0.5013 -0.0567 -0.0178 -0.1177 48 ALA A CB 44 N N . ASP A 6 ? 0.6150 0.5880 0.4761 -0.0141 -0.0134 -0.0912 49 ASP A N 45 C CA . ASP A 6 ? 0.5771 0.5381 0.4489 -0.0036 -0.0121 -0.0791 49 ASP A CA 46 C C . ASP A 6 ? 0.6243 0.5429 0.4895 -0.0073 -0.0114 -0.0805 49 ASP A C 47 O O . ASP A 6 ? 0.7025 0.5973 0.5575 -0.0087 -0.0094 -0.0894 49 ASP A O 48 C CB . ASP A 6 ? 0.5735 0.5425 0.4544 0.0170 -0.0092 -0.0731 49 ASP A CB 49 C CG . ASP A 6 ? 0.6357 0.6472 0.5260 0.0229 -0.0084 -0.0688 49 ASP A CG 50 O OD1 . ASP A 6 ? 0.6332 0.6681 0.5272 0.0132 -0.0099 -0.0660 49 ASP A OD1 51 O OD2 . ASP A 6 ? 0.6440 0.6654 0.5389 0.0379 -0.0054 -0.0673 49 ASP A OD2 52 N N . THR A 7 ? 0.5815 0.4909 0.4522 -0.0090 -0.0124 -0.0714 50 THR A N 53 C CA . THR A 7 ? 0.5899 0.4622 0.4571 -0.0091 -0.0115 -0.0688 50 THR A CA 54 C C . THR A 7 ? 0.5505 0.4237 0.4272 -0.0031 -0.0128 -0.0557 50 THR A C 55 O O . THR A 7 ? 0.5206 0.4201 0.4048 -0.0026 -0.0137 -0.0505 50 THR A O 56 C CB . THR A 7 ? 0.6255 0.4789 0.4826 -0.0273 -0.0114 -0.0755 50 THR A CB 57 O OG1 . THR A 7 ? 0.6777 0.4930 0.5308 -0.0252 -0.0087 -0.0738 50 THR A OG1 58 C CG2 . THR A 7 ? 0.6478 0.5150 0.5083 -0.0386 -0.0139 -0.0698 50 THR A CG2 59 N N . THR A 8 ? 0.6009 0.4456 0.4771 0.0015 -0.0125 -0.0503 51 THR A N 60 C CA . THR A 8 ? 0.5606 0.4048 0.4436 0.0058 -0.0145 -0.0386 51 THR A CA 61 C C . THR A 8 ? 0.5699 0.4158 0.4492 -0.0087 -0.0159 -0.0359 51 THR A C 62 O O . THR A 8 ? 0.5837 0.4084 0.4553 -0.0188 -0.0153 -0.0379 51 THR A O 63 C CB . THR A 8 ? 0.6236 0.4385 0.5071 0.0144 -0.0143 -0.0323 51 THR A CB 64 O OG1 . THR A 8 ? 0.6686 0.4811 0.5564 0.0282 -0.0122 -0.0341 51 THR A OG1 65 C CG2 . THR A 8 ? 0.6565 0.4747 0.5464 0.0185 -0.0173 -0.0207 51 THR A CG2 66 N N . LEU A 9 ? 0.5072 0.3776 0.3925 -0.0094 -0.0166 -0.0311 52 LEU A N 67 C CA . LEU A 9 ? 0.5221 0.3950 0.4045 -0.0217 -0.0171 -0.0272 52 LEU A CA 68 C C . LEU A 9 ? 0.5609 0.4134 0.4412 -0.0201 -0.0186 -0.0181 52 LEU A C 69 O O . LEU A 9 ? 0.5450 0.3874 0.4284 -0.0088 -0.0198 -0.0138 52 LEU A O 70 C CB . LEU A 9 ? 0.4063 0.3115 0.2964 -0.0215 -0.0158 -0.0241 52 LEU A CB 71 C CG . LEU A 9 ? 0.4826 0.4136 0.3763 -0.0215 -0.0145 -0.0307 52 LEU A CG 72 C CD1 . LEU A 9 ? 0.5326 0.4956 0.4367 -0.0174 -0.0116 -0.0254 52 LEU A CD1 73 C CD2 . LEU A 9 ? 0.6128 0.5426 0.4991 -0.0372 -0.0154 -0.0384 52 LEU A CD2 74 N N . PHE A 10 ? 0.4437 0.2919 0.3190 -0.0314 -0.0186 -0.0146 53 PHE A N 75 C CA . PHE A 10 ? 0.4907 0.3275 0.3639 -0.0296 -0.0201 -0.0049 53 PHE A CA 76 C C . PHE A 10 ? 0.5287 0.3852 0.4029 -0.0347 -0.0189 -0.0008 53 PHE A C 77 O O . PHE A 10 ? 0.5089 0.3859 0.3863 -0.0402 -0.0166 -0.0047 53 PHE A O 78 C CB . PHE A 10 ? 0.5153 0.3231 0.3803 -0.0361 -0.0202 -0.0018 53 PHE A CB 79 C CG . PHE A 10 ? 0.5238 0.3297 0.3836 -0.0515 -0.0179 -0.0046 53 PHE A CG 80 C CD1 . PHE A 10 ? 0.5610 0.3617 0.4191 -0.0592 -0.0159 -0.0145 53 PHE A CD1 81 C CD2 . PHE A 10 ? 0.4949 0.3032 0.3513 -0.0587 -0.0174 0.0023 53 PHE A CD2 82 C CE1 . PHE A 10 ? 0.6198 0.4192 0.4745 -0.0744 -0.0138 -0.0173 53 PHE A CE1 83 C CE2 . PHE A 10 ? 0.5626 0.3689 0.4156 -0.0728 -0.0149 0.0006 53 PHE A CE2 84 C CZ . PHE A 10 ? 0.6246 0.4268 0.4775 -0.0809 -0.0132 -0.0092 53 PHE A CZ 85 N N . CYS A 11 ? 0.4712 0.3228 0.3429 -0.0327 -0.0202 0.0072 54 CYS A N 86 C CA . CYS A 11 ? 0.4554 0.3228 0.3266 -0.0377 -0.0177 0.0109 54 CYS A CA 87 C C . CYS A 11 ? 0.5339 0.3873 0.3951 -0.0477 -0.0176 0.0168 54 CYS A C 88 O O . CYS A 11 ? 0.5687 0.3999 0.4237 -0.0479 -0.0202 0.0207 54 CYS A O 89 C CB . CYS A 11 ? 0.4897 0.3687 0.3662 -0.0281 -0.0176 0.0140 54 CYS A CB 90 S SG . CYS A 11 ? 0.5405 0.4005 0.4133 -0.0204 -0.0233 0.0207 54 CYS A SG 91 N N . ALA A 12 ? 0.4880 0.3552 0.3483 -0.0551 -0.0137 0.0184 55 ALA A N 92 C CA . ALA A 12 ? 0.5138 0.3712 0.3647 -0.0642 -0.0123 0.0245 55 ALA A CA 93 C C . ALA A 12 ? 0.5371 0.4097 0.3872 -0.0639 -0.0086 0.0283 55 ALA A C 94 O O . ALA A 12 ? 0.5287 0.4219 0.3875 -0.0603 -0.0051 0.0254 55 ALA A O 95 C CB . ALA A 12 ? 0.5380 0.3943 0.3885 -0.0764 -0.0097 0.0220 55 ALA A CB 96 N N . SER A 13 ? 0.5367 0.3987 0.3762 -0.0674 -0.0085 0.0350 56 SER A N 97 C CA . SER A 13 ? 0.5491 0.4215 0.3847 -0.0682 -0.0041 0.0383 56 SER A CA 98 C C . SER A 13 ? 0.5667 0.4258 0.3881 -0.0757 -0.0032 0.0456 56 SER A C 99 O O . SER A 13 ? 0.5365 0.3778 0.3519 -0.0786 -0.0066 0.0492 56 SER A O 100 C CB . SER A 13 ? 0.5397 0.4153 0.3765 -0.0585 -0.0066 0.0377 56 SER A CB 101 O OG . SER A 13 ? 0.5581 0.4175 0.3840 -0.0578 -0.0123 0.0431 56 SER A OG 102 N N . ASP A 14 ? 0.6063 0.4737 0.4225 -0.0782 0.0024 0.0479 57 ASP A N 103 C CA . ASP A 14 ? 0.6401 0.4966 0.4411 -0.0842 0.0038 0.0549 57 ASP A CA 104 C C . ASP A 14 ? 0.6600 0.5132 0.4508 -0.0797 0.0005 0.0568 57 ASP A C 105 O O . ASP A 14 ? 0.6505 0.5021 0.4286 -0.0840 0.0041 0.0605 57 ASP A O 106 C CB . ASP A 14 ? 0.6592 0.5258 0.4593 -0.0916 0.0136 0.0566 57 ASP A CB 107 C CG . ASP A 14 ? 0.7006 0.5704 0.5095 -0.0985 0.0160 0.0561 57 ASP A CG 108 O OD1 . ASP A 14 ? 0.6496 0.5050 0.4573 -0.1013 0.0114 0.0570 57 ASP A OD1 109 O OD2 . ASP A 14 ? 0.7356 0.6228 0.5534 -0.1011 0.0230 0.0549 57 ASP A OD2 110 N N . ALA A 15 ? 0.5739 0.4266 0.3702 -0.0714 -0.0063 0.0542 58 ALA A N 111 C CA . ALA A 15 ? 0.5650 0.4161 0.3534 -0.0676 -0.0110 0.0558 58 ALA A CA 112 C C . ALA A 15 ? 0.6407 0.4788 0.4113 -0.0726 -0.0142 0.0643 58 ALA A C 113 O O . ALA A 15 ? 0.6180 0.4437 0.3860 -0.0750 -0.0160 0.0698 58 ALA A O 114 C CB . ALA A 15 ? 0.5579 0.4078 0.3559 -0.0583 -0.0188 0.0539 58 ALA A CB 115 N N . LYS A 16 ? 0.6241 0.4651 0.3824 -0.0742 -0.0142 0.0652 59 LYS A N 116 C CA . LYS A 16 ? 0.7381 0.5697 0.4779 -0.0783 -0.0176 0.0736 59 LYS A CA 117 C C . LYS A 16 ? 0.6911 0.5202 0.4293 -0.0724 -0.0288 0.0775 59 LYS A C 118 O O . LYS A 16 ? 0.5869 0.4250 0.3300 -0.0684 -0.0319 0.0723 59 LYS A O 119 C CB . LYS A 16 ? 0.7903 0.6272 0.5156 -0.0845 -0.0108 0.0719 59 LYS A CB 120 C CG . LYS A 16 ? 0.9713 0.8107 0.6984 -0.0901 0.0010 0.0705 59 LYS A CG 121 C CD . LYS A 16 ? 1.1010 0.9507 0.8260 -0.0920 0.0106 0.0639 59 LYS A CD 122 C CE . LYS A 16 ? 1.2295 1.0915 0.9737 -0.0854 0.0122 0.0555 59 LYS A CE 123 N NZ . LYS A 16 ? 1.1670 1.0357 0.9295 -0.0836 0.0165 0.0541 59 LYS A NZ 124 N N . ALA A 17 ? 0.6569 0.4743 0.3897 -0.0717 -0.0341 0.0873 60 ALA A N 125 C CA . ALA A 17 ? 0.6620 0.4778 0.3961 -0.0651 -0.0445 0.0933 60 ALA A CA 126 C C . ALA A 17 ? 0.6814 0.5057 0.4010 -0.0670 -0.0501 0.0954 60 ALA A C 127 O O . ALA A 17 ? 0.7271 0.5566 0.4506 -0.0617 -0.0589 0.0978 60 ALA A O 128 C CB . ALA A 17 ? 0.7151 0.5159 0.4483 -0.0634 -0.0469 0.1046 60 ALA A CB 129 N N . HIS A 18 ? 0.5933 0.4198 0.2964 -0.0749 -0.0448 0.0944 61 HIS A N 130 C CA . HIS A 18 ? 0.6388 0.4729 0.3247 -0.0786 -0.0495 0.0953 61 HIS A CA 131 C C . HIS A 18 ? 0.6239 0.4696 0.3130 -0.0800 -0.0466 0.0825 61 HIS A C 132 O O . HIS A 18 ? 0.6495 0.5024 0.3262 -0.0837 -0.0505 0.0803 61 HIS A O 133 C CB . HIS A 18 ? 0.6615 0.4904 0.3251 -0.0865 -0.0443 0.1009 61 HIS A CB 134 C CG . HIS A 18 ? 0.7634 0.5898 0.4271 -0.0917 -0.0312 0.0946 61 HIS A CG 135 N ND1 . HIS A 18 ? 0.8369 0.6700 0.4933 -0.0967 -0.0234 0.0853 61 HIS A ND1 136 C CD2 . HIS A 18 ? 0.7872 0.6060 0.4586 -0.0927 -0.0239 0.0965 61 HIS A CD2 137 C CE1 . HIS A 18 ? 0.8306 0.6609 0.4907 -0.0998 -0.0119 0.0831 61 HIS A CE1 138 N NE2 . HIS A 18 ? 0.8269 0.6495 0.4962 -0.0979 -0.0126 0.0896 61 HIS A NE2 139 N N . GLU A 19 ? 0.6109 0.4587 0.3170 -0.0773 -0.0393 0.0740 62 GLU A N 140 C CA . GLU A 19 ? 0.5966 0.4543 0.3082 -0.0780 -0.0334 0.0623 62 GLU A CA 141 C C . GLU A 19 ? 0.6311 0.4966 0.3560 -0.0714 -0.0421 0.0593 62 GLU A C 142 O O . GLU A 19 ? 0.6204 0.4835 0.3582 -0.0641 -0.0489 0.0639 62 GLU A O 143 C CB . GLU A 19 ? 0.6547 0.5132 0.3807 -0.0766 -0.0222 0.0571 62 GLU A CB 144 C CG . GLU A 19 ? 0.7805 0.6482 0.5136 -0.0770 -0.0120 0.0470 62 GLU A CG 145 C CD . GLU A 19 ? 0.7667 0.6353 0.4813 -0.0846 -0.0070 0.0432 62 GLU A CD 146 O OE1 . GLU A 19 ? 0.8646 0.7286 0.5656 -0.0910 0.0013 0.0451 62 GLU A OE1 147 O OE2 . GLU A 19 ? 0.7395 0.6133 0.4534 -0.0845 -0.0110 0.0379 62 GLU A OE2 148 N N . THR A 20 ? 0.6194 0.4932 0.3410 -0.0744 -0.0415 0.0517 63 THR A N 149 C CA . THR A 20 ? 0.5491 0.4314 0.2864 -0.0684 -0.0480 0.0477 63 THR A CA 150 C C . THR A 20 ? 0.5494 0.4369 0.3063 -0.0637 -0.0382 0.0380 63 THR A C 151 O O . THR A 20 ? 0.4991 0.3930 0.2727 -0.0572 -0.0419 0.0349 63 THR A O 152 C CB . THR A 20 ? 0.6183 0.5082 0.3435 -0.0745 -0.0540 0.0443 63 THR A CB 153 O OG1 . THR A 20 ? 0.5836 0.4739 0.2969 -0.0828 -0.0425 0.0349 63 THR A OG1 154 C CG2 . THR A 20 ? 0.6430 0.5318 0.3502 -0.0779 -0.0656 0.0554 63 THR A CG2 155 N N . GLU A 21 ? 0.5341 0.4201 0.2897 -0.0667 -0.0253 0.0340 64 GLU A N 156 C CA . GLU A 21 ? 0.4978 0.3903 0.2729 -0.0613 -0.0150 0.0270 64 GLU A CA 157 C C . GLU A 21 ? 0.5074 0.4013 0.3026 -0.0508 -0.0208 0.0296 64 GLU A C 158 O O . GLU A 21 ? 0.5671 0.4539 0.3609 -0.0493 -0.0263 0.0364 64 GLU A O 159 C CB . GLU A 21 ? 0.4875 0.3787 0.2589 -0.0653 -0.0015 0.0262 64 GLU A CB 160 C CG . GLU A 21 ? 0.4765 0.3769 0.2666 -0.0603 0.0111 0.0202 64 GLU A CG 161 C CD . GLU A 21 ? 0.5030 0.4080 0.3133 -0.0508 0.0076 0.0218 64 GLU A CD 162 O OE1 . GLU A 21 ? 0.5170 0.4165 0.3255 -0.0506 0.0019 0.0275 64 GLU A OE1 163 O OE2 . GLU A 21 ? 0.4847 0.3981 0.3121 -0.0437 0.0106 0.0173 64 GLU A OE2 164 N N . VAL A 22 ? 0.4403 0.3423 0.2539 -0.0437 -0.0190 0.0242 65 VAL A N 165 C CA . VAL A 22 ? 0.4758 0.3783 0.3058 -0.0337 -0.0264 0.0271 65 VAL A CA 166 C C . VAL A 22 ? 0.4649 0.3652 0.3035 -0.0291 -0.0232 0.0290 65 VAL A C 167 O O . VAL A 22 ? 0.4806 0.3760 0.3256 -0.0232 -0.0303 0.0330 65 VAL A O 168 C CB . VAL A 22 ? 0.5051 0.4170 0.3531 -0.0268 -0.0253 0.0214 65 VAL A CB 169 C CG1 . VAL A 22 ? 0.4397 0.3539 0.2801 -0.0321 -0.0311 0.0195 65 VAL A CG1 170 C CG2 . VAL A 22 ? 0.4674 0.3876 0.3269 -0.0246 -0.0107 0.0147 65 VAL A CG2 171 N N . HIS A 23 ? 0.4446 0.3492 0.2842 -0.0317 -0.0123 0.0262 66 HIS A N 172 C CA . HIS A 23 ? 0.4360 0.3407 0.2831 -0.0289 -0.0102 0.0276 66 HIS A CA 173 C C . HIS A 23 ? 0.5037 0.3955 0.3370 -0.0348 -0.0159 0.0339 66 HIS A C 174 O O . HIS A 23 ? 0.4961 0.3822 0.3340 -0.0320 -0.0196 0.0360 66 HIS A O 175 C CB . HIS A 23 ? 0.4268 0.3421 0.2794 -0.0306 0.0026 0.0246 66 HIS A CB 176 C CG . HIS A 23 ? 0.4644 0.3928 0.3329 -0.0237 0.0107 0.0195 66 HIS A CG 177 N ND1 . HIS A 23 ? 0.4800 0.4110 0.3465 -0.0258 0.0167 0.0158 66 HIS A ND1 178 C CD2 . HIS A 23 ? 0.4761 0.4159 0.3626 -0.0151 0.0149 0.0176 66 HIS A CD2 179 C CE1 . HIS A 23 ? 0.4571 0.3996 0.3412 -0.0183 0.0248 0.0123 66 HIS A CE1 180 N NE2 . HIS A 23 ? 0.4627 0.4115 0.3590 -0.0112 0.0236 0.0139 66 HIS A NE2 181 N N . ASN A 24 ? 0.4862 0.3728 0.3022 -0.0432 -0.0154 0.0367 67 ASN A N 182 C CA . ASN A 24 ? 0.5401 0.4138 0.3424 -0.0485 -0.0207 0.0441 67 ASN A CA 183 C C . ASN A 24 ? 0.5728 0.4383 0.3765 -0.0431 -0.0321 0.0494 67 ASN A C 184 O O . ASN A 24 ? 0.5457 0.4010 0.3497 -0.0424 -0.0351 0.0541 67 ASN A O 185 C CB . ASN A 24 ? 0.5207 0.3913 0.3032 -0.0573 -0.0187 0.0466 67 ASN A CB 186 C CG . ASN A 24 ? 0.5685 0.4422 0.3473 -0.0636 -0.0068 0.0449 67 ASN A CG 187 O OD1 . ASN A 24 ? 0.6011 0.4681 0.3735 -0.0685 -0.0051 0.0498 67 ASN A OD1 188 N ND2 . ASN A 24 ? 0.5650 0.4489 0.3488 -0.0633 0.0024 0.0386 67 ASN A ND2 189 N N . VAL A 25 ? 0.5380 0.4078 0.3430 -0.0397 -0.0379 0.0490 68 VAL A N 190 C CA . VAL A 25 ? 0.5320 0.3962 0.3400 -0.0339 -0.0485 0.0555 68 VAL A CA 191 C C . VAL A 25 ? 0.5479 0.4090 0.3726 -0.0252 -0.0487 0.0545 68 VAL A C 192 O O . VAL A 25 ? 0.5163 0.3656 0.3408 -0.0226 -0.0530 0.0610 68 VAL A O 193 C CB . VAL A 25 ? 0.5554 0.4283 0.3644 -0.0322 -0.0547 0.0547 68 VAL A CB 194 C CG1 . VAL A 25 ? 0.6031 0.4734 0.4218 -0.0238 -0.0646 0.0616 68 VAL A CG1 195 C CG2 . VAL A 25 ? 0.5944 0.4681 0.3828 -0.0417 -0.0567 0.0571 68 VAL A CG2 196 N N . TRP A 26 ? 0.5348 0.4056 0.3735 -0.0205 -0.0431 0.0466 69 TRP A N 197 C CA . TRP A 26 ? 0.5113 0.3804 0.3647 -0.0120 -0.0428 0.0448 69 TRP A CA 198 C C . TRP A 26 ? 0.5422 0.4014 0.3917 -0.0158 -0.0401 0.0457 69 TRP A C 199 O O . TRP A 26 ? 0.4848 0.3329 0.3377 -0.0116 -0.0433 0.0484 69 TRP A O 200 C CB . TRP A 26 ? 0.4223 0.3057 0.2903 -0.0067 -0.0360 0.0367 69 TRP A CB 201 C CG . TRP A 26 ? 0.4384 0.3210 0.3196 0.0020 -0.0356 0.0346 69 TRP A CG 202 C CD1 . TRP A 26 ? 0.4796 0.3607 0.3722 0.0120 -0.0399 0.0358 69 TRP A CD1 203 C CD2 . TRP A 26 ? 0.4468 0.3307 0.3306 0.0010 -0.0303 0.0309 69 TRP A CD2 204 N NE1 . TRP A 26 ? 0.5148 0.3947 0.4154 0.0177 -0.0371 0.0326 69 TRP A NE1 205 C CE2 . TRP A 26 ? 0.4960 0.3784 0.3911 0.0107 -0.0317 0.0292 69 TRP A CE2 206 C CE3 . TRP A 26 ? 0.4332 0.3202 0.3109 -0.0073 -0.0247 0.0291 69 TRP A CE3 207 C CZ2 . TRP A 26 ? 0.4923 0.3766 0.3912 0.0115 -0.0280 0.0247 69 TRP A CZ2 208 C CZ3 . TRP A 26 ? 0.4753 0.3657 0.3585 -0.0067 -0.0215 0.0253 69 TRP A CZ3 209 C CH2 . TRP A 26 ? 0.4646 0.3538 0.3575 0.0024 -0.0234 0.0227 69 TRP A CH2 210 N N . ALA A 27 ? 0.4795 0.3425 0.3224 -0.0239 -0.0335 0.0433 70 ALA A N 211 C CA . ALA A 27 ? 0.4766 0.3326 0.3175 -0.0287 -0.0305 0.0431 70 ALA A CA 212 C C . ALA A 27 ? 0.5433 0.3815 0.3727 -0.0331 -0.0348 0.0511 70 ALA A C 213 O O . ALA A 27 ? 0.5734 0.4006 0.4040 -0.0344 -0.0343 0.0515 70 ALA A O 214 C CB . ALA A 27 ? 0.5221 0.3888 0.3610 -0.0361 -0.0221 0.0398 70 ALA A CB 215 N N . THR A 28 ? 0.5113 0.3469 0.3296 -0.0355 -0.0385 0.0573 71 THR A N 216 C CA . THR A 28 ? 0.5740 0.3942 0.3818 -0.0380 -0.0426 0.0670 71 THR A CA 217 C C . THR A 28 ? 0.5568 0.3653 0.3730 -0.0300 -0.0472 0.0709 71 THR A C 218 O O . THR A 28 ? 0.5653 0.3583 0.3783 -0.0316 -0.0467 0.0765 71 THR A O 219 C CB . THR A 28 ? 0.5764 0.3995 0.3708 -0.0406 -0.0471 0.0734 71 THR A CB 220 O OG1 . THR A 28 ? 0.5698 0.3976 0.3530 -0.0495 -0.0410 0.0713 71 THR A OG1 221 C CG2 . THR A 28 ? 0.6212 0.4306 0.4078 -0.0400 -0.0525 0.0855 71 THR A CG2 222 N N . HIS A 29 ? 0.5618 0.3771 0.3894 -0.0210 -0.0506 0.0682 72 HIS A N 223 C CA . HIS A 29 ? 0.6645 0.4694 0.5012 -0.0120 -0.0540 0.0721 72 HIS A CA 224 C C . HIS A 29 ? 0.5994 0.4015 0.4475 -0.0078 -0.0496 0.0638 72 HIS A C 225 O O . HIS A 29 ? 0.6276 0.4153 0.4799 -0.0029 -0.0496 0.0664 72 HIS A O 226 C CB . HIS A 29 ? 0.8575 0.6707 0.7002 -0.0042 -0.0610 0.0762 72 HIS A CB 227 C CG . HIS A 29 ? 1.1557 0.9712 0.9866 -0.0081 -0.0670 0.0855 72 HIS A CG 228 N ND1 . HIS A 29 ? 1.2248 1.0544 1.0561 -0.0070 -0.0726 0.0859 72 HIS A ND1 229 C CD2 . HIS A 29 ? 1.2877 1.0938 1.1054 -0.0134 -0.0680 0.0947 72 HIS A CD2 230 C CE1 . HIS A 29 ? 1.2602 1.0900 1.0780 -0.0118 -0.0776 0.0947 72 HIS A CE1 231 N NE2 . HIS A 29 ? 1.3075 1.1233 1.1169 -0.0151 -0.0747 0.1007 72 HIS A NE2 232 N N . ALA A 30 ? 0.5460 0.3619 0.3986 -0.0095 -0.0451 0.0542 73 ALA A N 233 C CA . ALA A 30 ? 0.5283 0.3458 0.3913 -0.0047 -0.0416 0.0463 73 ALA A CA 234 C C . ALA A 30 ? 0.5043 0.3201 0.3640 -0.0132 -0.0361 0.0404 73 ALA A C 235 O O . ALA A 30 ? 0.5458 0.3626 0.4120 -0.0108 -0.0336 0.0335 73 ALA A O 236 C CB . ALA A 30 ? 0.4682 0.3050 0.3420 0.0018 -0.0404 0.0405 73 ALA A CB 237 N N . CYS A 31 ? 0.5241 0.3383 0.3738 -0.0234 -0.0343 0.0430 74 CYS A N 238 C CA . CYS A 31 ? 0.5539 0.3701 0.4016 -0.0329 -0.0292 0.0380 74 CYS A CA 239 C C . CYS A 31 ? 0.5645 0.3634 0.4020 -0.0416 -0.0285 0.0440 74 CYS A C 240 O O . CYS A 31 ? 0.5513 0.3409 0.3819 -0.0405 -0.0316 0.0528 74 CYS A O 241 C CB . CYS A 31 ? 0.4851 0.3222 0.3334 -0.0373 -0.0250 0.0349 74 CYS A CB 242 S SG . CYS A 31 ? 0.5301 0.3890 0.3914 -0.0274 -0.0235 0.0291 74 CYS A SG 243 N N . VAL A 32 ? 0.5270 0.3228 0.3642 -0.0502 -0.0244 0.0395 75 VAL A N 244 C CA . VAL A 32 ? 0.5589 0.3389 0.3879 -0.0594 -0.0221 0.0448 75 VAL A CA 245 C C . VAL A 32 ? 0.5512 0.3440 0.3759 -0.0689 -0.0184 0.0454 75 VAL A C 246 O O . VAL A 32 ? 0.5984 0.4117 0.4276 -0.0684 -0.0167 0.0410 75 VAL A O 247 C CB . VAL A 32 ? 0.5922 0.3573 0.4242 -0.0641 -0.0193 0.0392 75 VAL A CB 248 C CG1 . VAL A 32 ? 0.6821 0.4308 0.5175 -0.0544 -0.0213 0.0399 75 VAL A CG1 249 C CG2 . VAL A 32 ? 0.5712 0.3533 0.4096 -0.0693 -0.0169 0.0280 75 VAL A CG2 250 N N . PRO A 33 ? 0.6272 0.4081 0.4440 -0.0769 -0.0159 0.0518 76 PRO A N 251 C CA . PRO A 33 ? 0.6641 0.4559 0.4773 -0.0862 -0.0112 0.0529 76 PRO A CA 252 C C . PRO A 33 ? 0.6560 0.4613 0.4781 -0.0930 -0.0074 0.0444 76 PRO A C 253 O O . PRO A 33 ? 0.6289 0.4290 0.4570 -0.0944 -0.0080 0.0378 76 PRO A O 254 C CB . PRO A 33 ? 0.6894 0.4616 0.4939 -0.0926 -0.0091 0.0616 76 PRO A CB 255 C CG . PRO A 33 ? 0.6821 0.4393 0.4825 -0.0839 -0.0139 0.0684 76 PRO A CG 256 C CD . PRO A 33 ? 0.6550 0.4127 0.4655 -0.0763 -0.0169 0.0606 76 PRO A CD 257 N N . THR A 34 ? 0.6349 0.4584 0.4580 -0.0975 -0.0033 0.0447 77 THR A N 258 C CA . THR A 34 ? 0.6417 0.4815 0.4739 -0.1048 0.0003 0.0388 77 THR A CA 259 C C . THR A 34 ? 0.6956 0.5230 0.5267 -0.1168 0.0028 0.0397 77 THR A C 260 O O . THR A 34 ? 0.7146 0.5226 0.5373 -0.1194 0.0036 0.0467 77 THR A O 261 C CB . THR A 34 ? 0.6195 0.4816 0.4540 -0.1064 0.0058 0.0412 77 THR A CB 262 O OG1 . THR A 34 ? 0.6408 0.4942 0.4653 -0.1117 0.0095 0.0494 77 THR A OG1 263 C CG2 . THR A 34 ? 0.5901 0.4653 0.4273 -0.0953 0.0052 0.0396 77 THR A CG2 264 N N . ASP A 35 ? 0.6637 0.5039 0.5038 -0.1242 0.0041 0.0329 78 ASP A N 265 C CA . ASP A 35 ? 0.6861 0.5186 0.5278 -0.1375 0.0070 0.0321 78 ASP A CA 266 C C . ASP A 35 ? 0.7255 0.5735 0.5689 -0.1446 0.0125 0.0382 78 ASP A C 267 O O . ASP A 35 ? 0.7368 0.6104 0.5874 -0.1436 0.0141 0.0371 78 ASP A O 268 C CB . ASP A 35 ? 0.7498 0.5914 0.6002 -0.1429 0.0051 0.0208 78 ASP A CB 269 C CG . ASP A 35 ? 0.7997 0.6297 0.6519 -0.1578 0.0076 0.0179 78 ASP A CG 270 O OD1 . ASP A 35 ? 0.7779 0.5985 0.6272 -0.1645 0.0118 0.0255 78 ASP A OD1 271 O OD2 . ASP A 35 ? 0.8663 0.6966 0.7226 -0.1632 0.0058 0.0076 78 ASP A OD2 272 N N . PRO A 36 ? 0.8629 0.6953 0.7001 -0.1511 0.0162 0.0458 79 PRO A N 273 C CA . PRO A 36 ? 0.9176 0.7629 0.7561 -0.1578 0.0226 0.0525 79 PRO A CA 274 C C . PRO A 36 ? 0.9576 0.8198 0.8090 -0.1700 0.0248 0.0482 79 PRO A C 275 O O . PRO A 36 ? 0.9873 0.8699 0.8445 -0.1736 0.0297 0.0525 79 PRO A O 276 C CB . PRO A 36 ? 0.9371 0.7579 0.7649 -0.1607 0.0256 0.0616 79 PRO A CB 277 C CG . PRO A 36 ? 0.9723 0.7697 0.7993 -0.1615 0.0222 0.0579 79 PRO A CG 278 C CD . PRO A 36 ? 0.8968 0.6990 0.7261 -0.1519 0.0158 0.0496 79 PRO A CD 279 N N . ASN A 37 ? 0.9380 0.7924 0.7938 -0.1764 0.0215 0.0398 80 ASN A N 280 C CA . ASN A 37 ? 0.9597 0.8307 0.8274 -0.1896 0.0224 0.0343 80 ASN A CA 281 C C . ASN A 37 ? 0.8717 0.7553 0.7453 -0.1889 0.0165 0.0220 80 ASN A C 282 O O . ASN A 37 ? 0.8602 0.7315 0.7346 -0.1969 0.0145 0.0134 80 ASN A O 283 C CB . ASN A 37 ? 1.1097 0.9588 0.9772 -0.2024 0.0256 0.0351 80 ASN A CB 284 C CG . ASN A 37 ? 1.2079 1.0435 1.0686 -0.2025 0.0317 0.0480 80 ASN A CG 285 O OD1 . ASN A 37 ? 1.2309 1.0838 1.0937 -0.2028 0.0360 0.0554 80 ASN A OD1 286 N ND2 . ASN A 37 ? 1.2431 1.0479 1.0955 -0.2017 0.0330 0.0514 80 ASN A ND2 287 N N . PRO A 38 ? 0.8176 0.7251 0.6948 -0.1793 0.0146 0.0212 81 PRO A N 288 C CA . PRO A 38 ? 0.8094 0.7297 0.6908 -0.1760 0.0093 0.0107 81 PRO A CA 289 C C . PRO A 38 ? 0.8779 0.8225 0.7697 -0.1890 0.0079 0.0042 81 PRO A C 290 O O . PRO A 38 ? 0.8917 0.8591 0.7924 -0.1958 0.0112 0.0100 81 PRO A O 291 C CB . PRO A 38 ? 0.7388 0.6785 0.6221 -0.1616 0.0096 0.0148 81 PRO A CB 292 C CG . PRO A 38 ? 0.7692 0.7190 0.6545 -0.1629 0.0161 0.0257 81 PRO A CG 293 C CD . PRO A 38 ? 0.7460 0.6681 0.6231 -0.1704 0.0185 0.0303 81 PRO A CD 294 N N . GLN A 39 ? 0.8725 0.8129 0.7633 -0.1924 0.0033 -0.0078 82 GLN A N 295 C CA . GLN A 39 ? 0.9319 0.8955 0.8309 -0.2058 0.0007 -0.0158 82 GLN A CA 296 C C . GLN A 39 ? 0.8184 0.8188 0.7244 -0.1983 -0.0022 -0.0171 82 GLN A C 297 O O . GLN A 39 ? 0.7949 0.7932 0.6969 -0.1841 -0.0040 -0.0188 82 GLN A O 298 C CB . GLN A 39 ? 1.0881 1.0282 0.9810 -0.2146 -0.0019 -0.0293 82 GLN A CB 299 C CG . GLN A 39 ? 1.2105 1.1141 1.0982 -0.2226 0.0024 -0.0279 82 GLN A CG 300 C CD . GLN A 39 ? 1.2682 1.1814 1.1641 -0.2368 0.0062 -0.0215 82 GLN A CD 301 O OE1 . GLN A 39 ? 1.2943 1.2334 1.1995 -0.2496 0.0043 -0.0261 82 GLN A OE1 302 N NE2 . GLN A 39 ? 1.2632 1.1570 1.1561 -0.2345 0.0114 -0.0104 82 GLN A NE2 303 N N . GLU A 40 ? 0.7397 0.7746 0.6573 -0.2073 -0.0023 -0.0150 83 GLU A N 304 C CA . GLU A 40 ? 0.6926 0.7657 0.6181 -0.2024 -0.0053 -0.0164 83 GLU A CA 305 C C . GLU A 40 ? 0.6912 0.7910 0.6249 -0.2198 -0.0090 -0.0220 83 GLU A C 306 O O . GLU A 40 ? 0.7003 0.8144 0.6435 -0.2305 -0.0063 -0.0150 83 GLU A O 307 C CB . GLU A 40 ? 0.6841 0.7819 0.6185 -0.1904 0.0000 -0.0027 83 GLU A CB 308 C CG . GLU A 40 ? 0.6473 0.7876 0.5922 -0.1853 -0.0019 -0.0020 83 GLU A CG 309 C CD . GLU A 40 ? 0.6621 0.8219 0.6154 -0.1705 0.0051 0.0110 83 GLU A CD 310 O OE1 . GLU A 40 ? 0.7095 0.8483 0.6586 -0.1644 0.0109 0.0178 83 GLU A OE1 311 O OE2 . GLU A 40 ? 0.6239 0.8200 0.5879 -0.1648 0.0054 0.0143 83 GLU A OE2 312 N N . ILE A 41 ? 0.6312 0.7381 0.5611 -0.2229 -0.0150 -0.0347 84 ILE A N 313 C CA . ILE A 41 ? 0.6358 0.7678 0.5711 -0.2407 -0.0200 -0.0428 84 ILE A CA 314 C C . ILE A 41 ? 0.6774 0.8577 0.6217 -0.2356 -0.0235 -0.0402 84 ILE A C 315 O O . ILE A 41 ? 0.6648 0.8488 0.6038 -0.2222 -0.0254 -0.0436 84 ILE A O 316 C CB . ILE A 41 ? 0.6509 0.7561 0.5734 -0.2502 -0.0241 -0.0610 84 ILE A CB 317 C CG1 . ILE A 41 ? 0.7480 0.8031 0.6617 -0.2524 -0.0195 -0.0626 84 ILE A CG1 318 C CG2 . ILE A 41 ? 0.6652 0.7951 0.5922 -0.2714 -0.0294 -0.0710 84 ILE A CG2 319 C CD1 . ILE A 41 ? 0.8454 0.8685 0.7461 -0.2573 -0.0210 -0.0790 84 ILE A CD1 320 N N . HIS A 42 ? 0.6530 0.8713 0.6116 -0.2458 -0.0240 -0.0333 85 HIS A N 321 C CA . HIS A 42 ? 0.6682 0.9356 0.6359 -0.2430 -0.0280 -0.0307 85 HIS A CA 322 C C . HIS A 42 ? 0.6340 0.9083 0.5935 -0.2562 -0.0368 -0.0483 85 HIS A C 323 O O . HIS A 42 ? 0.6699 0.9347 0.6273 -0.2762 -0.0398 -0.0580 85 HIS A O 324 C CB . HIS A 42 ? 0.7409 1.0498 0.7280 -0.2497 -0.0257 -0.0165 85 HIS A CB 325 C CG . HIS A 42 ? 0.8099 1.1724 0.8073 -0.2490 -0.0304 -0.0135 85 HIS A CG 326 N ND1 . HIS A 42 ? 0.8372 1.2342 0.8431 -0.2679 -0.0369 -0.0164 85 HIS A ND1 327 C CD2 . HIS A 42 ? 0.8230 1.2112 0.8236 -0.2317 -0.0296 -0.0075 85 HIS A CD2 328 C CE1 . HIS A 42 ? 0.8162 1.2596 0.8297 -0.2619 -0.0403 -0.0116 85 HIS A CE1 329 N NE2 . HIS A 42 ? 0.8094 1.2478 0.8201 -0.2396 -0.0354 -0.0058 85 HIS A NE2 330 N N . LEU A 43 ? 0.4744 0.7648 0.4290 -0.2451 -0.0402 -0.0525 86 LEU A N 331 C CA . LEU A 43 ? 0.4936 0.7916 0.4379 -0.2558 -0.0480 -0.0695 86 LEU A CA 332 C C . LEU A 43 ? 0.6576 1.0132 0.6141 -0.2662 -0.0539 -0.0661 86 LEU A C 333 O O . LEU A 43 ? 0.6342 1.0276 0.5983 -0.2531 -0.0542 -0.0564 86 LEU A O 334 C CB . LEU A 43 ? 0.4887 0.7741 0.4206 -0.2382 -0.0484 -0.0757 86 LEU A CB 335 C CG . LEU A 43 ? 0.5794 0.8122 0.5019 -0.2258 -0.0426 -0.0762 86 LEU A CG 336 C CD1 . LEU A 43 ? 0.5837 0.8070 0.4964 -0.2075 -0.0425 -0.0806 86 LEU A CD1 337 C CD2 . LEU A 43 ? 0.6106 0.8007 0.5229 -0.2420 -0.0424 -0.0885 86 LEU A CD2 338 N N . GLU A 44 ? 0.6803 1.0433 0.6395 -0.2898 -0.0583 -0.0734 87 GLU A N 339 C CA . GLU A 44 ? 0.7139 1.1335 0.6874 -0.3023 -0.0642 -0.0683 87 GLU A CA 340 C C . GLU A 44 ? 0.7564 1.2123 0.7239 -0.3003 -0.0719 -0.0753 87 GLU A C 341 O O . GLU A 44 ? 0.6707 1.1048 0.6196 -0.3035 -0.0757 -0.0934 87 GLU A O 342 C CB . GLU A 44 ? 0.7621 1.1783 0.7390 -0.3297 -0.0676 -0.0768 87 GLU A CB 343 C CG . GLU A 44 ? 0.8754 1.2744 0.8647 -0.3320 -0.0599 -0.0639 87 GLU A CG 344 C CD . GLU A 44 ? 1.0503 1.4457 1.0445 -0.3591 -0.0626 -0.0720 87 GLU A CD 345 O OE1 . GLU A 44 ? 1.0546 1.4591 1.0419 -0.3772 -0.0705 -0.0891 87 GLU A OE1 346 O OE2 . GLU A 44 ? 1.1443 1.5271 1.1491 -0.3626 -0.0562 -0.0615 87 GLU A OE2 347 N N . ASN A 45 ? 0.9801 1.4919 0.9638 -0.2947 -0.0734 -0.0600 88 ASN A N 348 C CA . ASN A 45 ? 1.1519 1.7069 1.1331 -0.2883 -0.0795 -0.0608 88 ASN A CA 349 C C . ASN A 45 ? 0.9790 1.5071 0.9403 -0.2732 -0.0792 -0.0724 88 ASN A C 350 O O . ASN A 45 ? 0.9704 1.5166 0.9200 -0.2774 -0.0864 -0.0843 88 ASN A O 351 C CB . ASN A 45 ? 1.5250 2.1244 1.5085 -0.3123 -0.0907 -0.0689 88 ASN A CB 352 C CG . ASN A 45 ? 1.7100 2.2780 1.6721 -0.3329 -0.0973 -0.0959 88 ASN A CG 353 O OD1 . ASN A 45 ? 1.7362 2.2499 1.6817 -0.3279 -0.0931 -0.1081 88 ASN A OD1 354 N ND2 . ASN A 45 ? 1.8675 2.4706 1.8300 -0.3562 -0.1072 -0.1054 88 ASN A ND2 355 N N . VAL A 46 ? 0.8598 1.3460 0.8178 -0.2554 -0.0707 -0.0681 89 VAL A N 356 C CA . VAL A 46 ? 0.7225 1.1814 0.6646 -0.2388 -0.0690 -0.0762 89 VAL A CA 357 C C . VAL A 46 ? 0.6614 1.1455 0.6145 -0.2133 -0.0633 -0.0586 89 VAL A C 358 O O . VAL A 46 ? 0.5876 1.0753 0.5561 -0.2034 -0.0559 -0.0416 89 VAL A O 359 C CB . VAL A 46 ? 0.6186 1.0125 0.5495 -0.2356 -0.0634 -0.0835 89 VAL A CB 360 C CG1 . VAL A 46 ? 0.5716 0.9424 0.4931 -0.2128 -0.0594 -0.0844 89 VAL A CG1 361 C CG2 . VAL A 46 ? 0.6616 1.0248 0.5779 -0.2581 -0.0678 -0.1041 89 VAL A CG2 362 N N . THR A 47 ? 0.7107 0.8376 0.6396 -0.1241 -0.1262 -0.0821 90 THR A N 363 C CA . THR A 47 ? 0.6455 0.7718 0.5678 -0.1052 -0.1243 -0.0735 90 THR A CA 364 C C . THR A 47 ? 0.6586 0.7503 0.5499 -0.0986 -0.1120 -0.0691 90 THR A C 365 O O . THR A 47 ? 0.6580 0.7268 0.5221 -0.1019 -0.1137 -0.0745 90 THR A O 366 C CB . THR A 47 ? 0.6982 0.8340 0.6120 -0.0967 -0.1433 -0.0747 90 THR A CB 367 O OG1 . THR A 47 ? 0.7449 0.9175 0.6931 -0.1011 -0.1559 -0.0804 90 THR A OG1 368 C CG2 . THR A 47 ? 0.6306 0.7599 0.5332 -0.0788 -0.1417 -0.0645 90 THR A CG2 369 N N . GLU A 48 ? 0.6078 0.6973 0.5045 -0.0893 -0.0994 -0.0606 91 GLU A N 370 C CA . GLU A 48 ? 0.6029 0.6654 0.4768 -0.0829 -0.0867 -0.0571 91 GLU A CA 371 C C . GLU A 48 ? 0.5990 0.6613 0.4651 -0.0689 -0.0842 -0.0482 91 GLU A C 372 O O . GLU A 48 ? 0.5321 0.6131 0.4174 -0.0629 -0.0876 -0.0430 91 GLU A O 373 C CB . GLU A 48 ? 0.5525 0.6071 0.4386 -0.0874 -0.0731 -0.0555 91 GLU A CB 374 C CG . GLU A 48 ? 0.6240 0.6657 0.5081 -0.1014 -0.0742 -0.0632 91 GLU A CG 375 C CD . GLU A 48 ? 0.7296 0.7417 0.5856 -0.0997 -0.0724 -0.0697 91 GLU A CD 376 O OE1 . GLU A 48 ? 0.6269 0.6275 0.4707 -0.0887 -0.0635 -0.0672 91 GLU A OE1 377 O OE2 . GLU A 48 ? 0.8457 0.8470 0.6928 -0.1097 -0.0797 -0.0784 91 GLU A OE2 378 N N . ASN A 49 ? 0.5612 0.6018 0.3986 -0.0642 -0.0780 -0.0473 92 ASN A N 379 C CA . ASN A 49 ? 0.5047 0.5406 0.3307 -0.0538 -0.0736 -0.0382 92 ASN A CA 380 C C . ASN A 49 ? 0.5475 0.5781 0.3837 -0.0505 -0.0569 -0.0337 92 ASN A C 381 O O . ASN A 49 ? 0.5347 0.5547 0.3708 -0.0543 -0.0476 -0.0387 92 ASN A O 382 C CB . ASN A 49 ? 0.5211 0.5382 0.3086 -0.0528 -0.0748 -0.0398 92 ASN A CB 383 C CG . ASN A 49 ? 0.7070 0.7265 0.4806 -0.0567 -0.0929 -0.0449 92 ASN A CG 384 O OD1 . ASN A 49 ? 0.7577 0.7962 0.5518 -0.0566 -0.1070 -0.0446 92 ASN A OD1 385 N ND2 . ASN A 49 ? 0.7970 0.7987 0.5368 -0.0603 -0.0928 -0.0510 92 ASN A ND2 386 N N . PHE A 50 ? 0.5242 0.5611 0.3695 -0.0430 -0.0546 -0.0247 93 PHE A N 387 C CA . PHE A 50 ? 0.4899 0.5224 0.3442 -0.0397 -0.0402 -0.0199 93 PHE A CA 388 C C . PHE A 50 ? 0.4749 0.4969 0.3095 -0.0332 -0.0365 -0.0123 93 PHE A C 389 O O . PHE A 50 ? 0.5104 0.5303 0.3294 -0.0301 -0.0469 -0.0084 93 PHE A O 390 C CB . PHE A 50 ? 0.4748 0.5240 0.3596 -0.0386 -0.0397 -0.0166 93 PHE A CB 391 C CG . PHE A 50 ? 0.4692 0.5263 0.3716 -0.0482 -0.0398 -0.0228 93 PHE A CG 392 C CD1 . PHE A 50 ? 0.4507 0.5017 0.3625 -0.0516 -0.0296 -0.0223 93 PHE A CD1 393 C CD2 . PHE A 50 ? 0.4984 0.5679 0.4067 -0.0549 -0.0511 -0.0288 93 PHE A CD2 394 C CE1 . PHE A 50 ? 0.4339 0.4874 0.3567 -0.0624 -0.0301 -0.0266 93 PHE A CE1 395 C CE2 . PHE A 50 ? 0.4982 0.5733 0.4205 -0.0665 -0.0506 -0.0340 93 PHE A CE2 396 C CZ . PHE A 50 ? 0.4614 0.5266 0.3890 -0.0707 -0.0398 -0.0324 93 PHE A CZ 397 N N . ASN A 51 ? 0.4477 0.4618 0.2819 -0.0319 -0.0224 -0.0102 94 ASN A N 398 C CA . ASN A 51 ? 0.4778 0.4823 0.2954 -0.0283 -0.0169 -0.0024 94 ASN A CA 399 C C . ASN A 51 ? 0.4605 0.4666 0.2967 -0.0264 -0.0049 0.0005 94 ASN A C 400 O O . ASN A 51 ? 0.4520 0.4541 0.2891 -0.0285 0.0062 -0.0042 94 ASN A O 401 C CB . ASN A 51 ? 0.4658 0.4567 0.2518 -0.0323 -0.0108 -0.0061 94 ASN A CB 402 C CG . ASN A 51 ? 0.5263 0.5061 0.2915 -0.0320 -0.0046 0.0026 94 ASN A CG 403 O OD1 . ASN A 51 ? 0.5234 0.5033 0.2979 -0.0279 -0.0062 0.0116 94 ASN A OD1 404 N ND2 . ASN A 51 ? 0.6184 0.5875 0.3539 -0.0374 0.0030 -0.0005 94 ASN A ND2 405 N N . MET A 52 ? 0.3803 0.3930 0.2328 -0.0219 -0.0082 0.0071 95 MET A N 406 C CA . MET A 52 ? 0.4153 0.4295 0.2854 -0.0204 0.0012 0.0099 95 MET A CA 407 C C . MET A 52 ? 0.4701 0.4734 0.3272 -0.0211 0.0124 0.0131 95 MET A C 408 O O . MET A 52 ? 0.4623 0.4664 0.3327 -0.0211 0.0211 0.0131 95 MET A O 409 C CB . MET A 52 ? 0.4442 0.4663 0.3299 -0.0149 -0.0047 0.0153 95 MET A CB 410 C CG . MET A 52 ? 0.4251 0.4383 0.2943 -0.0095 -0.0121 0.0228 95 MET A CG 411 S SD . MET A 52 ? 0.4350 0.4556 0.3244 -0.0001 -0.0191 0.0270 95 MET A SD 412 C CE . MET A 52 ? 0.3540 0.3672 0.2505 -0.0015 -0.0045 0.0305 95 MET A CE 413 N N . TRP A 53 ? 0.4785 0.4716 0.3087 -0.0228 0.0119 0.0156 96 TRP A N 414 C CA . TRP A 53 ? 0.4814 0.4648 0.2962 -0.0263 0.0233 0.0192 96 TRP A CA 415 C C . TRP A 53 ? 0.5384 0.5233 0.3481 -0.0312 0.0358 0.0095 96 TRP A C 416 O O . TRP A 53 ? 0.5656 0.5482 0.3688 -0.0354 0.0482 0.0094 96 TRP A O 417 C CB . TRP A 53 ? 0.5047 0.4731 0.2889 -0.0274 0.0168 0.0281 96 TRP A CB 418 C CG . TRP A 53 ? 0.5445 0.5114 0.3373 -0.0198 0.0034 0.0359 96 TRP A CG 419 C CD1 . TRP A 53 ? 0.5239 0.4934 0.3160 -0.0143 -0.0132 0.0365 96 TRP A CD1 420 C CD2 . TRP A 53 ? 0.5215 0.4859 0.3282 -0.0160 0.0050 0.0420 96 TRP A CD2 421 N NE1 . TRP A 53 ? 0.5638 0.5338 0.3701 -0.0061 -0.0215 0.0419 96 TRP A NE1 422 C CE2 . TRP A 53 ? 0.5177 0.4831 0.3315 -0.0072 -0.0103 0.0454 96 TRP A CE2 423 C CE3 . TRP A 53 ? 0.5363 0.4984 0.3510 -0.0191 0.0174 0.0439 96 TRP A CE3 424 C CZ2 . TRP A 53 ? 0.4686 0.4312 0.2957 -0.0007 -0.0128 0.0501 96 TRP A CZ2 425 C CZ3 . TRP A 53 ? 0.5360 0.4940 0.3622 -0.0140 0.0143 0.0496 96 TRP A CZ3 426 C CH2 . TRP A 53 ? 0.5245 0.4819 0.3560 -0.0047 -0.0003 0.0523 96 TRP A CH2 427 N N . LYS A 54 ? 0.5367 0.5260 0.3506 -0.0310 0.0323 0.0003 97 LYS A N 428 C CA . LYS A 54 ? 0.4870 0.4777 0.3002 -0.0331 0.0421 -0.0117 97 LYS A CA 429 C C . LYS A 54 ? 0.4718 0.4668 0.3081 -0.0301 0.0371 -0.0184 97 LYS A C 430 O O . LYS A 54 ? 0.4513 0.4440 0.2825 -0.0313 0.0299 -0.0245 97 LYS A O 431 C CB . LYS A 54 ? 0.5755 0.5594 0.3578 -0.0374 0.0415 -0.0170 97 LYS A CB 432 C CG . LYS A 54 ? 0.7350 0.7122 0.4897 -0.0434 0.0516 -0.0134 97 LYS A CG 433 C CD . LYS A 54 ? 0.9272 0.8953 0.6461 -0.0486 0.0498 -0.0182 97 LYS A CD 434 C CE . LYS A 54 ? 1.0380 1.0109 0.7598 -0.0487 0.0577 -0.0355 97 LYS A CE 435 N NZ . LYS A 54 ? 1.0872 1.0673 0.8118 -0.0516 0.0780 -0.0442 97 LYS A NZ 436 N N . ASN A 55 ? 0.4826 0.4815 0.3423 -0.0273 0.0401 -0.0167 98 ASN A N 437 C CA . ASN A 55 ? 0.4740 0.4730 0.3521 -0.0260 0.0338 -0.0196 98 ASN A CA 438 C C . ASN A 55 ? 0.4288 0.4280 0.3249 -0.0229 0.0402 -0.0227 98 ASN A C 439 O O . ASN A 55 ? 0.3924 0.3949 0.2994 -0.0217 0.0425 -0.0160 98 ASN A O 440 C CB . ASN A 55 ? 0.4247 0.4284 0.3116 -0.0265 0.0252 -0.0108 98 ASN A CB 441 C CG . ASN A 55 ? 0.4324 0.4355 0.3347 -0.0286 0.0201 -0.0130 98 ASN A CG 442 O OD1 . ASN A 55 ? 0.4522 0.4474 0.3561 -0.0292 0.0202 -0.0203 98 ASN A OD1 443 N ND2 . ASN A 55 ? 0.3780 0.3883 0.2905 -0.0300 0.0155 -0.0071 98 ASN A ND2 444 N N . ASN A 56 ? 0.4534 0.4484 0.3522 -0.0208 0.0420 -0.0339 99 ASN A N 445 C CA . ASN A 56 ? 0.4503 0.4457 0.3671 -0.0159 0.0462 -0.0393 99 ASN A CA 446 C C . ASN A 56 ? 0.4029 0.3936 0.3352 -0.0151 0.0389 -0.0330 99 ASN A C 447 O O . ASN A 56 ? 0.3799 0.3714 0.3272 -0.0110 0.0405 -0.0345 99 ASN A O 448 C CB . ASN A 56 ? 0.4941 0.4839 0.4105 -0.0120 0.0468 -0.0543 99 ASN A CB 449 C CG . ASN A 56 ? 0.5325 0.5245 0.4700 -0.0046 0.0498 -0.0625 99 ASN A CG 450 O OD1 . ASN A 56 ? 0.5422 0.5221 0.4888 0.0000 0.0410 -0.0674 99 ASN A OD1 451 N ND2 . ASN A 56 ? 0.5400 0.5468 0.4852 -0.0038 0.0612 -0.0642 99 ASN A ND2 452 N N . MET A 57 ? 0.4141 0.4009 0.3426 -0.0196 0.0309 -0.0265 100 MET A N 453 C CA . MET A 57 ? 0.4396 0.4228 0.3785 -0.0211 0.0261 -0.0197 100 MET A CA 454 C C . MET A 57 ? 0.4378 0.4287 0.3847 -0.0192 0.0313 -0.0128 100 MET A C 455 O O . MET A 57 ? 0.3722 0.3592 0.3289 -0.0183 0.0294 -0.0104 100 MET A O 456 C CB . MET A 57 ? 0.4006 0.3845 0.3350 -0.0281 0.0200 -0.0147 100 MET A CB 457 C CG . MET A 57 ? 0.4563 0.4312 0.3824 -0.0325 0.0136 -0.0212 100 MET A CG 458 S SD . MET A 57 ? 0.4238 0.4056 0.3495 -0.0427 0.0076 -0.0165 100 MET A SD 459 C CE . MET A 57 ? 0.4550 0.4261 0.3870 -0.0484 0.0057 -0.0117 100 MET A CE 460 N N . VAL A 58 ? 0.3849 0.3843 0.3252 -0.0193 0.0369 -0.0094 101 VAL A N 461 C CA . VAL A 58 ? 0.3995 0.4037 0.3446 -0.0185 0.0418 -0.0029 101 VAL A CA 462 C C . VAL A 58 ? 0.4072 0.4137 0.3636 -0.0159 0.0476 -0.0078 101 VAL A C 463 O O . VAL A 58 ? 0.3920 0.3985 0.3596 -0.0151 0.0470 -0.0048 101 VAL A O 464 C CB . VAL A 58 ? 0.4339 0.4412 0.3647 -0.0199 0.0450 0.0019 101 VAL A CB 465 C CG1 . VAL A 58 ? 0.4148 0.4230 0.3481 -0.0202 0.0504 0.0080 101 VAL A CG1 466 C CG2 . VAL A 58 ? 0.3766 0.3849 0.3018 -0.0206 0.0369 0.0061 101 VAL A CG2 467 N N . GLU A 59 ? 0.3984 0.4082 0.3526 -0.0146 0.0533 -0.0168 102 GLU A N 468 C CA . GLU A 59 ? 0.4170 0.4344 0.3863 -0.0118 0.0598 -0.0242 102 GLU A CA 469 C C . GLU A 59 ? 0.4170 0.4287 0.4037 -0.0065 0.0512 -0.0275 102 GLU A C 470 O O . GLU A 59 ? 0.4132 0.4303 0.4160 -0.0042 0.0518 -0.0288 102 GLU A O 471 C CB . GLU A 59 ? 0.4284 0.4525 0.3931 -0.0112 0.0684 -0.0359 102 GLU A CB 472 C CG . GLU A 59 ? 0.5230 0.5543 0.4725 -0.0182 0.0803 -0.0330 102 GLU A CG 473 C CD . GLU A 59 ? 0.5758 0.5978 0.5004 -0.0226 0.0760 -0.0227 102 GLU A CD 474 O OE1 . GLU A 59 ? 0.6487 0.6696 0.5604 -0.0279 0.0804 -0.0144 102 GLU A OE1 475 O OE2 . GLU A 59 ? 0.5127 0.5277 0.4308 -0.0207 0.0671 -0.0232 102 GLU A OE2 476 N N . GLN A 60 ? 0.3491 0.3481 0.3305 -0.0055 0.0419 -0.0283 103 GLN A N 477 C CA . GLN A 60 ? 0.3769 0.3636 0.3681 -0.0016 0.0314 -0.0302 103 GLN A CA 478 C C . GLN A 60 ? 0.4249 0.4074 0.4180 -0.0047 0.0267 -0.0197 103 GLN A C 479 O O . GLN A 60 ? 0.3818 0.3601 0.3862 -0.0011 0.0211 -0.0205 103 GLN A O 480 C CB . GLN A 60 ? 0.3876 0.3582 0.3682 -0.0024 0.0231 -0.0333 103 GLN A CB 481 C CG . GLN A 60 ? 0.4179 0.3886 0.3991 0.0032 0.0254 -0.0471 103 GLN A CG 482 C CD . GLN A 60 ? 0.4986 0.4477 0.4711 0.0033 0.0144 -0.0512 103 GLN A CD 483 O OE1 . GLN A 60 ? 0.4402 0.3719 0.4144 0.0040 0.0036 -0.0484 103 GLN A OE1 484 N NE2 . GLN A 60 ? 0.5324 0.4799 0.4926 0.0014 0.0165 -0.0576 103 GLN A NE2 485 N N . MET A 61 ? 0.3681 0.3521 0.3506 -0.0108 0.0284 -0.0108 104 MET A N 486 C CA . MET A 61 ? 0.3497 0.3314 0.3334 -0.0137 0.0261 -0.0025 104 MET A CA 487 C C . MET A 61 ? 0.3751 0.3657 0.3701 -0.0114 0.0309 -0.0020 104 MET A C 488 O O . MET A 61 ? 0.3501 0.3359 0.3511 -0.0111 0.0261 0.0003 104 MET A O 489 C CB . MET A 61 ? 0.4015 0.3866 0.3753 -0.0192 0.0278 0.0045 104 MET A CB 490 C CG . MET A 61 ? 0.4867 0.4699 0.4613 -0.0218 0.0267 0.0109 104 MET A CG 491 S SD . MET A 61 ? 0.4106 0.3989 0.3782 -0.0274 0.0274 0.0157 104 MET A SD 492 C CE . MET A 61 ? 0.5174 0.5009 0.4858 -0.0293 0.0272 0.0199 104 MET A CE 493 N N . GLN A 62 ? 0.3673 0.3694 0.3630 -0.0113 0.0401 -0.0041 105 GLN A N 494 C CA . GLN A 62 ? 0.3872 0.3984 0.3927 -0.0119 0.0461 -0.0038 105 GLN A CA 495 C C . GLN A 62 ? 0.3943 0.4086 0.4189 -0.0071 0.0422 -0.0118 105 GLN A C 496 O O . GLN A 62 ? 0.3470 0.3630 0.3821 -0.0073 0.0397 -0.0102 105 GLN A O 497 C CB . GLN A 62 ? 0.3718 0.3925 0.3710 -0.0148 0.0572 -0.0054 105 GLN A CB 498 C CG . GLN A 62 ? 0.4014 0.4327 0.4113 -0.0181 0.0653 -0.0069 105 GLN A CG 499 C CD . GLN A 62 ? 0.4565 0.4820 0.4591 -0.0229 0.0657 0.0034 105 GLN A CD 500 O OE1 . GLN A 62 ? 0.4240 0.4398 0.4198 -0.0216 0.0589 0.0099 105 GLN A OE1 501 N NE2 . GLN A 62 ? 0.4799 0.5111 0.4832 -0.0292 0.0744 0.0042 105 GLN A NE2 502 N N . GLU A 63 ? 0.3921 0.4068 0.4216 -0.0019 0.0406 -0.0213 106 GLU A N 503 C CA . GLU A 63 ? 0.3845 0.4017 0.4344 0.0056 0.0345 -0.0310 106 GLU A CA 504 C C . GLU A 63 ? 0.3426 0.3443 0.3938 0.0072 0.0203 -0.0255 106 GLU A C 505 O O . GLU A 63 ? 0.3463 0.3531 0.4137 0.0101 0.0158 -0.0279 106 GLU A O 506 C CB . GLU A 63 ? 0.4246 0.4405 0.4766 0.0121 0.0337 -0.0428 106 GLU A CB 507 C CG . GLU A 63 ? 0.4101 0.4450 0.4629 0.0099 0.0496 -0.0505 106 GLU A CG 508 C CD . GLU A 63 ? 0.5851 0.6182 0.6346 0.0152 0.0510 -0.0628 106 GLU A CD 509 O OE1 . GLU A 63 ? 0.5533 0.5679 0.5976 0.0198 0.0392 -0.0642 106 GLU A OE1 510 O OE2 . GLU A 63 ? 0.5993 0.6485 0.6494 0.0134 0.0646 -0.0712 106 GLU A OE2 511 N N . ASP A 64 ? 0.3481 0.3314 0.3808 0.0038 0.0135 -0.0181 107 ASP A N 512 C CA . ASP A 64 ? 0.4107 0.3765 0.4375 0.0024 0.0012 -0.0118 107 ASP A CA 513 C C . ASP A 64 ? 0.4061 0.3771 0.4344 -0.0018 0.0032 -0.0052 107 ASP A C 514 O O . ASP A 64 ? 0.3432 0.3081 0.3774 0.0001 -0.0061 -0.0049 107 ASP A O 515 C CB . ASP A 64 ? 0.3913 0.3399 0.3961 -0.0043 -0.0024 -0.0049 107 ASP A CB 516 C CG . ASP A 64 ? 0.4251 0.3578 0.4248 -0.0013 -0.0105 -0.0103 107 ASP A CG 517 O OD1 . ASP A 64 ? 0.4004 0.3318 0.4135 0.0081 -0.0159 -0.0197 107 ASP A OD1 518 O OD2 . ASP A 64 ? 0.4155 0.3362 0.3980 -0.0088 -0.0120 -0.0056 107 ASP A OD2 519 N N . VAL A 65 ? 0.4040 0.3840 0.4256 -0.0073 0.0140 0.0000 108 VAL A N 520 C CA . VAL A 65 ? 0.3688 0.3501 0.3894 -0.0113 0.0154 0.0059 108 VAL A CA 521 C C . VAL A 65 ? 0.3530 0.3461 0.3931 -0.0090 0.0161 0.0009 108 VAL A C 522 O O . VAL A 65 ? 0.3256 0.3150 0.3687 -0.0103 0.0103 0.0029 108 VAL A O 523 C CB . VAL A 65 ? 0.3581 0.3444 0.3682 -0.0157 0.0251 0.0114 108 VAL A CB 524 C CG1 . VAL A 65 ? 0.3593 0.3439 0.3677 -0.0189 0.0258 0.0162 108 VAL A CG1 525 C CG2 . VAL A 65 ? 0.4007 0.3801 0.3962 -0.0182 0.0239 0.0146 108 VAL A CG2 526 N N . ILE A 66 ? 0.3091 0.3176 0.3627 -0.0064 0.0233 -0.0067 109 ILE A N 527 C CA . ILE A 66 ? 0.3474 0.3721 0.4235 -0.0055 0.0255 -0.0135 109 ILE A CA 528 C C . ILE A 66 ? 0.3113 0.3315 0.4025 0.0016 0.0102 -0.0188 109 ILE A C 529 O O . ILE A 66 ? 0.3260 0.3508 0.4294 0.0006 0.0050 -0.0195 109 ILE A O 530 C CB . ILE A 66 ? 0.3944 0.4380 0.4815 -0.0048 0.0377 -0.0227 109 ILE A CB 531 C CG1 . ILE A 66 ? 0.4386 0.4844 0.5087 -0.0133 0.0511 -0.0161 109 ILE A CG1 532 C CG2 . ILE A 66 ? 0.3558 0.4205 0.4724 -0.0031 0.0392 -0.0334 109 ILE A CG2 533 C CD1 . ILE A 66 ? 0.4740 0.5355 0.5474 -0.0152 0.0642 -0.0239 109 ILE A CD1 534 N N . SER A 67 ? 0.3622 0.3712 0.4509 0.0085 0.0014 -0.0224 110 SER A N 535 C CA . SER A 67 ? 0.3867 0.3853 0.4856 0.0167 -0.0162 -0.0269 110 SER A CA 536 C C . SER A 67 ? 0.3820 0.3605 0.4645 0.0121 -0.0279 -0.0168 110 SER A C 537 O O . SER A 67 ? 0.3994 0.3766 0.4934 0.0155 -0.0402 -0.0190 110 SER A O 538 C CB . SER A 67 ? 0.3821 0.3653 0.4745 0.0237 -0.0235 -0.0311 110 SER A CB 539 O OG . SER A 67 ? 0.5503 0.5148 0.6454 0.0312 -0.0437 -0.0328 110 SER A OG 540 N N . LEU A 68 ? 0.3439 0.3075 0.3995 0.0044 -0.0243 -0.0066 111 LEU A N 541 C CA . LEU A 68 ? 0.3569 0.3034 0.3938 -0.0019 -0.0315 0.0022 111 LEU A CA 542 C C . LEU A 68 ? 0.3907 0.3495 0.4386 -0.0047 -0.0291 0.0022 111 LEU A C 543 O O . LEU A 68 ? 0.4264 0.3771 0.4753 -0.0042 -0.0417 0.0025 111 LEU A O 544 C CB . LEU A 68 ? 0.4228 0.3605 0.4347 -0.0103 -0.0232 0.0103 111 LEU A CB 545 C CG . LEU A 68 ? 0.5203 0.4379 0.5079 -0.0179 -0.0295 0.0180 111 LEU A CG 546 C CD1 . LEU A 68 ? 0.4717 0.3820 0.4393 -0.0250 -0.0232 0.0226 111 LEU A CD1 547 C CD2 . LEU A 68 ? 0.5252 0.4494 0.5125 -0.0218 -0.0247 0.0203 111 LEU A CD2 548 N N . TRP A 69 ? 0.3658 0.3420 0.4203 -0.0082 -0.0141 0.0019 112 TRP A N 549 C CA . TRP A 69 ? 0.4038 0.3887 0.4666 -0.0127 -0.0115 0.0022 112 TRP A CA 550 C C . TRP A 69 ? 0.4221 0.4208 0.5131 -0.0082 -0.0198 -0.0067 112 TRP A C 551 O O . TRP A 69 ? 0.4227 0.4199 0.5178 -0.0108 -0.0275 -0.0065 112 TRP A O 552 C CB . TRP A 69 ? 0.3795 0.3761 0.4412 -0.0179 0.0051 0.0041 112 TRP A CB 553 C CG . TRP A 69 ? 0.3808 0.3648 0.4189 -0.0223 0.0097 0.0123 112 TRP A CG 554 C CD1 . TRP A 69 ? 0.4152 0.3890 0.4361 -0.0219 0.0095 0.0161 112 TRP A CD1 555 C CD2 . TRP A 69 ? 0.3962 0.3776 0.4275 -0.0276 0.0150 0.0162 112 TRP A CD2 556 N NE1 . TRP A 69 ? 0.4009 0.3694 0.4074 -0.0257 0.0149 0.0211 112 TRP A NE1 557 C CE2 . TRP A 69 ? 0.3669 0.3380 0.3785 -0.0283 0.0177 0.0213 112 TRP A CE2 558 C CE3 . TRP A 69 ? 0.4018 0.3883 0.4421 -0.0323 0.0174 0.0151 112 TRP A CE3 559 C CZ2 . TRP A 69 ? 0.3862 0.3515 0.3879 -0.0310 0.0222 0.0244 112 TRP A CZ2 560 C CZ3 . TRP A 69 ? 0.4470 0.4238 0.4740 -0.0364 0.0215 0.0197 112 TRP A CZ3 561 C CH2 . TRP A 69 ? 0.3868 0.3529 0.3951 -0.0346 0.0235 0.0239 112 TRP A CH2 562 N N . ASP A 70 ? 0.3690 0.3823 0.4803 -0.0012 -0.0184 -0.0158 113 ASP A N 563 C CA . ASP A 70 ? 0.4566 0.4892 0.6009 0.0044 -0.0251 -0.0271 113 ASP A CA 564 C C . ASP A 70 ? 0.4453 0.4625 0.5913 0.0108 -0.0479 -0.0277 113 ASP A C 565 O O . ASP A 70 ? 0.4568 0.4861 0.6248 0.0121 -0.0568 -0.0335 113 ASP A O 566 C CB . ASP A 70 ? 0.5024 0.5532 0.6673 0.0121 -0.0187 -0.0388 113 ASP A CB 567 C CG . ASP A 70 ? 0.5865 0.6600 0.7576 0.0044 0.0032 -0.0417 113 ASP A CG 568 O OD1 . ASP A 70 ? 0.5849 0.6551 0.7406 -0.0064 0.0124 -0.0327 113 ASP A OD1 569 O OD2 . ASP A 70 ? 0.6294 0.7220 0.8188 0.0090 0.0108 -0.0531 113 ASP A OD2 570 N N . GLN A 71 ? 0.4368 0.4265 0.5588 0.0140 -0.0586 -0.0217 114 GLN A N 571 C CA . GLN A 71 ? 0.5145 0.4841 0.6321 0.0191 -0.0820 -0.0208 114 GLN A CA 572 C C . GLN A 71 ? 0.5272 0.4752 0.6151 0.0093 -0.0874 -0.0096 114 GLN A C 573 O O . GLN A 71 ? 0.5616 0.4914 0.6415 0.0115 -0.1073 -0.0079 114 GLN A O 574 C CB . GLN A 71 ? 0.6210 0.5689 0.7297 0.0283 -0.0949 -0.0218 114 GLN A CB 575 C CG . GLN A 71 ? 0.6101 0.5420 0.6901 0.0225 -0.0845 -0.0142 114 GLN A CG 576 C CD . GLN A 71 ? 0.6795 0.5941 0.7568 0.0316 -0.0949 -0.0181 114 GLN A CD 577 O OE1 . GLN A 71 ? 0.7221 0.6532 0.8194 0.0389 -0.0876 -0.0281 114 GLN A OE1 578 N NE2 . GLN A 71 ? 0.6567 0.5356 0.7065 0.0301 -0.1121 -0.0104 114 GLN A NE2 579 N N . SER A 72 ? 0.4094 0.3590 0.4807 -0.0008 -0.0707 -0.0029 115 SER A N 580 C CA . SER A 72 ? 0.4779 0.4070 0.5193 -0.0097 -0.0737 0.0059 115 SER A CA 581 C C . SER A 72 ? 0.4827 0.4229 0.5307 -0.0161 -0.0685 0.0053 115 SER A C 582 O O . SER A 72 ? 0.4748 0.4003 0.5071 -0.0206 -0.0781 0.0083 115 SER A O 583 C CB . SER A 72 ? 0.4818 0.3995 0.4954 -0.0162 -0.0611 0.0135 115 SER A CB 584 O OG . SER A 72 ? 0.5389 0.4460 0.5453 -0.0125 -0.0644 0.0142 115 SER A OG 585 N N . LEU A 73 ? 0.4513 0.4149 0.5191 -0.0176 -0.0531 0.0015 116 LEU A N 586 C CA . LEU A 73 ? 0.5377 0.5089 0.6091 -0.0254 -0.0461 0.0017 116 LEU A CA 587 C C . LEU A 73 ? 0.6701 0.6658 0.7762 -0.0252 -0.0475 -0.0072 116 LEU A C 588 O O . LEU A 73 ? 0.7018 0.7153 0.8210 -0.0299 -0.0326 -0.0095 116 LEU A O 589 C CB . LEU A 73 ? 0.5529 0.5269 0.6138 -0.0302 -0.0268 0.0060 116 LEU A CB 590 C CG . LEU A 73 ? 0.6966 0.6503 0.7258 -0.0331 -0.0241 0.0133 116 LEU A CG 591 C CD1 . LEU A 73 ? 0.7728 0.7300 0.7948 -0.0324 -0.0100 0.0164 116 LEU A CD1 592 C CD2 . LEU A 73 ? 0.7123 0.6574 0.7311 -0.0396 -0.0241 0.0146 116 LEU A CD2 593 N N . GLN A 74 ? 0.7162 0.7130 0.8366 -0.0207 -0.0659 -0.0124 117 GLN A N 594 C CA . GLN A 74 ? 0.7837 0.8064 0.9398 -0.0220 -0.0693 -0.0222 117 GLN A CA 595 C C . GLN A 74 ? 0.6160 0.6390 0.7677 -0.0346 -0.0637 -0.0201 117 GLN A C 596 O O . GLN A 74 ? 0.6619 0.6633 0.7907 -0.0384 -0.0731 -0.0151 117 GLN A O 597 C CB . GLN A 74 ? 0.9730 0.9935 1.1434 -0.0133 -0.0945 -0.0280 117 GLN A CB 598 C CG . GLN A 74 ? 1.1464 1.1610 1.3206 0.0004 -0.1048 -0.0308 117 GLN A CG 599 C CD . GLN A 74 ? 1.2512 1.2596 1.4379 0.0101 -0.1332 -0.0361 117 GLN A CD 600 O OE1 . GLN A 74 ? 1.2573 1.2574 1.4380 0.0056 -0.1469 -0.0345 117 GLN A OE1 601 N NE2 . GLN A 74 ? 1.2851 1.2959 1.4886 0.0242 -0.1434 -0.0430 117 GLN A NE2 602 N N . PRO A 75 ? 0.5022 0.5479 0.6740 -0.0422 -0.0483 -0.0242 118 PRO A N 603 C CA . PRO A 75 ? 0.4349 0.4792 0.6052 -0.0548 -0.0463 -0.0234 118 PRO A CA 604 C C . PRO A 75 ? 0.4387 0.5003 0.6394 -0.0557 -0.0624 -0.0331 118 PRO A C 605 O O . PRO A 75 ? 0.4180 0.4974 0.6458 -0.0459 -0.0724 -0.0415 118 PRO A O 606 C CB . PRO A 75 ? 0.4544 0.5150 0.6335 -0.0638 -0.0246 -0.0239 118 PRO A CB 607 C CG . PRO A 75 ? 0.4265 0.5130 0.6322 -0.0562 -0.0198 -0.0320 118 PRO A CG 608 C CD . PRO A 75 ? 0.4439 0.5153 0.6379 -0.0415 -0.0326 -0.0301 118 PRO A CD 609 N N . CYS A 76 ? 0.4361 0.4923 0.6335 -0.0668 -0.0661 -0.0329 119 CYS A N 610 C CA . CYS A 76 ? 0.4226 0.4984 0.6516 -0.0698 -0.0812 -0.0429 119 CYS A CA 611 C C . CYS A 76 ? 0.4334 0.5502 0.7058 -0.0747 -0.0688 -0.0537 119 CYS A C 612 O O . CYS A 76 ? 0.3846 0.5297 0.6959 -0.0701 -0.0803 -0.0657 119 CYS A O 613 C CB . CYS A 76 ? 0.4451 0.5047 0.6583 -0.0829 -0.0855 -0.0404 119 CYS A CB 614 S SG . CYS A 76 ? 0.6386 0.6508 0.7952 -0.0816 -0.0895 -0.0284 119 CYS A SG 615 N N . VAL A 77 ? 0.3928 0.5127 0.6577 -0.0845 -0.0455 -0.0498 120 VAL A N 616 C CA . VAL A 77 ? 0.3803 0.5368 0.6792 -0.0930 -0.0294 -0.0590 120 VAL A CA 617 C C . VAL A 77 ? 0.4081 0.5616 0.6904 -0.0917 -0.0088 -0.0535 120 VAL A C 618 O O . VAL A 77 ? 0.3983 0.5220 0.6429 -0.0944 -0.0014 -0.0412 120 VAL A O 619 C CB . VAL A 77 ? 0.4256 0.5873 0.7294 -0.1143 -0.0214 -0.0596 120 VAL A CB 620 C CG1 . VAL A 77 ? 0.4616 0.6602 0.7953 -0.1263 -0.0008 -0.0682 120 VAL A CG1 621 C CG2 . VAL A 77 ? 0.4560 0.6231 0.7783 -0.1169 -0.0425 -0.0664 120 VAL A CG2 622 N N . LYS A 78 ? 0.3911 0.5759 0.7024 -0.0868 -0.0003 -0.0638 121 LYS A N 623 C CA . LYS A 78 ? 0.3856 0.5713 0.6831 -0.0873 0.0199 -0.0606 121 LYS A CA 624 C C . LYS A 78 ? 0.4256 0.6479 0.7513 -0.1014 0.0393 -0.0709 121 LYS A C 625 O O . LYS A 78 ? 0.4027 0.6622 0.7722 -0.1000 0.0365 -0.0866 121 LYS A O 626 C CB . LYS A 78 ? 0.4613 0.6455 0.7591 -0.0677 0.0137 -0.0632 121 LYS A CB 627 C CG . LYS A 78 ? 0.5880 0.7712 0.8693 -0.0674 0.0325 -0.0603 121 LYS A CG 628 C CD . LYS A 78 ? 0.6923 0.8567 0.9572 -0.0499 0.0233 -0.0570 121 LYS A CD 629 C CE . LYS A 78 ? 0.7737 0.9517 1.0689 -0.0340 0.0055 -0.0690 121 LYS A CE 630 N NZ . LYS A 78 ? 0.7944 0.9497 1.0702 -0.0192 -0.0034 -0.0651 121 LYS A NZ 631 N N . LEU A 79 ? 0.4515 0.6628 0.7513 -0.1157 0.0587 -0.0624 122 LEU A N 632 C CA . LEU A 79 ? 0.4753 0.7157 0.7918 -0.1334 0.0800 -0.0699 122 LEU A CA 633 C C . LEU A 79 ? 0.5159 0.7568 0.8161 -0.1293 0.0961 -0.0688 122 LEU A C 634 O O . LEU A 79 ? 0.4989 0.7082 0.7577 -0.1324 0.1023 -0.0547 122 LEU A O 635 C CB . LEU A 79 ? 0.5795 0.8001 0.8726 -0.1561 0.0881 -0.0595 122 LEU A CB 636 C CG . LEU A 79 ? 0.6435 0.8485 0.9375 -0.1596 0.0704 -0.0565 122 LEU A CG 637 C CD1 . LEU A 79 ? 0.6621 0.8338 0.9208 -0.1785 0.0770 -0.0434 122 LEU A CD1 638 C CD2 . LEU A 79 ? 0.6662 0.9121 1.0109 -0.1641 0.0635 -0.0731 122 LEU A CD2 639 N N . THR A 80 ? 0.5077 0.7843 0.8409 -0.1213 0.1014 -0.0848 123 THR A N 640 C CA . THR A 80 ? 0.4864 0.7632 0.8050 -0.1144 0.1139 -0.0859 123 THR A CA 641 C C . THR A 80 ? 0.5315 0.8546 0.8847 -0.1207 0.1325 -0.1050 123 THR A C 642 O O . THR A 80 ? 0.5445 0.9041 0.9453 -0.1159 0.1272 -0.1221 123 THR A O 643 C CB . THR A 80 ? 0.4795 0.7409 0.7943 -0.0894 0.0963 -0.0855 123 THR A CB 644 O OG1 . THR A 80 ? 0.4929 0.7547 0.7940 -0.0836 0.1082 -0.0877 123 THR A OG1 645 C CG2 . THR A 80 ? 0.4844 0.7719 0.8451 -0.0748 0.0795 -0.1014 123 THR A CG2 646 N N . GLY A 81 ? 0.5706 0.8929 0.8998 -0.1316 0.1541 -0.1028 124 GLY A N 647 C CA . GLY A 81 ? 0.5730 0.9386 0.9289 -0.1412 0.1762 -0.1209 124 GLY A CA 648 C C . GLY A 81 ? 0.5947 1.0010 0.9957 -0.1556 0.1811 -0.1347 124 GLY A C 649 O O . GLY A 81 ? 0.6251 1.0785 1.0722 -0.1518 0.1885 -0.1570 124 GLY A O 650 N N . GLY A 82 ? 0.5930 0.9823 0.9828 -0.1719 0.1766 -0.1228 198 GLY A N 651 C CA . GLY A 82 ? 0.5692 0.9947 0.9982 -0.1900 0.1819 -0.1344 198 GLY A CA 652 C C . GLY A 82 ? 0.5495 0.9994 1.0288 -0.1743 0.1588 -0.1474 198 GLY A C 653 O O . GLY A 82 ? 0.4964 0.9794 1.0132 -0.1881 0.1602 -0.1585 198 GLY A O 654 N N . SER A 83 ? 0.5467 0.9797 1.0260 -0.1464 0.1364 -0.1461 199 SER A N 655 C CA . SER A 83 ? 0.5505 0.9991 1.0707 -0.1302 0.1106 -0.1563 199 SER A CA 656 C C . SER A 83 ? 0.4593 0.8616 0.9487 -0.1256 0.0869 -0.1380 199 SER A C 657 O O . SER A 83 ? 0.4376 0.7955 0.8764 -0.1268 0.0880 -0.1190 199 SER A O 658 C CB . SER A 83 ? 0.5814 1.0477 1.1298 -0.1021 0.1003 -0.1716 199 SER A CB 659 O OG . SER A 83 ? 0.5939 1.0195 1.0992 -0.0881 0.0965 -0.1583 199 SER A OG 660 N N . VAL A 84 ? 0.4240 0.8385 0.9448 -0.1205 0.0655 -0.1450 200 VAL A N 661 C CA . VAL A 84 ? 0.4983 0.8724 0.9919 -0.1179 0.0433 -0.1303 200 VAL A CA 662 C C . VAL A 84 ? 0.5219 0.8911 1.0307 -0.0919 0.0144 -0.1352 200 VAL A C 663 O O . VAL A 84 ? 0.4976 0.9031 1.0556 -0.0833 0.0023 -0.1528 200 VAL A O 664 C CB . VAL A 84 ? 0.5127 0.8967 1.0207 -0.1389 0.0407 -0.1316 200 VAL A CB 665 C CG1 . VAL A 84 ? 0.5225 0.8601 0.9949 -0.1368 0.0199 -0.1161 200 VAL A CG1 666 C CG2 . VAL A 84 ? 0.5214 0.9119 1.0173 -0.1672 0.0692 -0.1282 200 VAL A CG2 667 N N . ILE A 85 ? 0.4620 0.7858 0.9280 -0.0799 0.0028 -0.1199 201 ILE A N 668 C CA . ILE A 85 ? 0.4826 0.7924 0.9519 -0.0572 -0.0245 -0.1213 201 ILE A CA 669 C C . ILE A 85 ? 0.4620 0.7336 0.9001 -0.0591 -0.0443 -0.1078 201 ILE A C 670 O O . ILE A 85 ? 0.4439 0.6804 0.8370 -0.0669 -0.0372 -0.0918 201 ILE A O 671 C CB . ILE A 85 ? 0.5372 0.8259 0.9818 -0.0413 -0.0220 -0.1162 201 ILE A CB 672 C CG1 . ILE A 85 ? 0.5747 0.8992 1.0461 -0.0396 -0.0011 -0.1303 201 ILE A CG1 673 C CG2 . ILE A 85 ? 0.4988 0.7676 0.9424 -0.0200 -0.0510 -0.1163 201 ILE A CG2 674 C CD1 . ILE A 85 ? 0.5992 0.9012 1.0402 -0.0293 0.0064 -0.1240 201 ILE A CD1 675 N N . LYS A 86 ? 0.4775 0.7565 0.9397 -0.0517 -0.0695 -0.1153 202 LYS A N 676 C CA . LYS A 86 ? 0.5084 0.7526 0.9412 -0.0539 -0.0896 -0.1046 202 LYS A CA 677 C C . LYS A 86 ? 0.5420 0.7606 0.9612 -0.0334 -0.1160 -0.1017 202 LYS A C 678 O O . LYS A 86 ? 0.4943 0.7326 0.9466 -0.0174 -0.1291 -0.1138 202 LYS A O 679 C CB . LYS A 86 ? 0.5058 0.7738 0.9705 -0.0655 -0.1002 -0.1140 202 LYS A CB 680 C CG . LYS A 86 ? 0.5133 0.8011 0.9868 -0.0899 -0.0757 -0.1154 202 LYS A CG 681 C CD . LYS A 86 ? 0.5537 0.8716 1.0670 -0.1013 -0.0870 -0.1277 202 LYS A CD 682 C CE . LYS A 86 ? 0.5922 0.9214 1.1064 -0.1288 -0.0637 -0.1268 202 LYS A CE 683 N NZ . LYS A 86 ? 0.6053 0.9536 1.1480 -0.1433 -0.0765 -0.1357 202 LYS A NZ 684 N N . GLN A 87 ? 0.5947 0.7685 0.9646 -0.0342 -0.1241 -0.0864 203 GLN A N 685 C CA . GLN A 87 ? 0.6288 0.7728 0.9779 -0.0185 -0.1485 -0.0817 203 GLN A CA 686 C C . GLN A 87 ? 0.6015 0.7015 0.8980 -0.0255 -0.1550 -0.0666 203 GLN A C 687 O O . GLN A 87 ? 0.5640 0.6570 0.8422 -0.0403 -0.1403 -0.0606 203 GLN A O 688 C CB . GLN A 87 ? 0.6723 0.8094 1.0133 -0.0057 -0.1409 -0.0799 203 GLN A CB 689 C CG . GLN A 87 ? 0.7193 0.8418 1.0268 -0.0147 -0.1147 -0.0685 203 GLN A CG 690 C CD . GLN A 87 ? 0.8253 0.9465 1.1306 -0.0031 -0.1070 -0.0692 203 GLN A CD 691 O OE1 . GLN A 87 ? 0.8304 0.9800 1.1598 -0.0035 -0.0890 -0.0775 203 GLN A OE1 692 N NE2 . GLN A 87 ? 0.9290 1.0162 1.2036 0.0060 -0.1206 -0.0610 203 GLN A NE2 693 N N . ALA A 88 ? 0.5951 0.6641 0.8659 -0.0151 -0.1770 -0.0609 204 ALA A N 694 C CA . ALA A 88 ? 0.6520 0.6795 0.8709 -0.0219 -0.1833 -0.0479 204 ALA A CA 695 C C . ALA A 88 ? 0.5576 0.5672 0.7413 -0.0275 -0.1587 -0.0369 204 ALA A C 696 O O . ALA A 88 ? 0.5507 0.5665 0.7386 -0.0212 -0.1461 -0.0364 204 ALA A O 697 C CB . ALA A 88 ? 0.7185 0.7161 0.9158 -0.0110 -0.2122 -0.0443 204 ALA A CB 698 N N . CYS A 89 ? 0.5365 0.5246 0.6864 -0.0389 -0.1526 -0.0294 205 CYS A N 699 C CA . CYS A 89 ? 0.5808 0.5551 0.7014 -0.0439 -0.1300 -0.0207 205 CYS A CA 700 C C . CYS A 89 ? 0.6459 0.5838 0.7183 -0.0485 -0.1350 -0.0122 205 CYS A C 701 O O . CYS A 89 ? 0.6456 0.5744 0.7001 -0.0577 -0.1241 -0.0098 205 CYS A O 702 C CB . CYS A 89 ? 0.5740 0.5665 0.7093 -0.0545 -0.1095 -0.0229 205 CYS A CB 703 S SG . CYS A 89 ? 0.6275 0.6241 0.7733 -0.0668 -0.1197 -0.0286 205 CYS A SG 704 N N . PRO A 90 ? 0.6493 0.5649 0.6993 -0.0426 -0.1514 -0.0081 206 PRO A N 705 C CA . PRO A 90 ? 0.6731 0.5548 0.6747 -0.0487 -0.1548 -0.0006 206 PRO A CA 706 C C . PRO A 90 ? 0.6198 0.4952 0.5992 -0.0527 -0.1304 0.0051 206 PRO A C 707 O O . PRO A 90 ? 0.5444 0.4347 0.5393 -0.0482 -0.1164 0.0056 206 PRO A O 708 C CB . PRO A 90 ? 0.6918 0.5525 0.6766 -0.0417 -0.1752 0.0033 206 PRO A CB 709 C CG . PRO A 90 ? 0.6475 0.5292 0.6667 -0.0305 -0.1729 -0.0003 206 PRO A CG 710 C CD . PRO A 90 ? 0.6564 0.5751 0.7218 -0.0302 -0.1652 -0.0100 206 PRO A CD 711 N N . LYS A 91 ? 0.5984 0.4529 0.5424 -0.0606 -0.1261 0.0081 207 LYS A N 712 C CA . LYS A 91 ? 0.5786 0.4263 0.5002 -0.0630 -0.1061 0.0123 207 LYS A CA 713 C C . LYS A 91 ? 0.5880 0.4249 0.4928 -0.0599 -0.1074 0.0181 207 LYS A C 714 O O . LYS A 91 ? 0.5901 0.4090 0.4787 -0.0596 -0.1255 0.0209 207 LYS A O 715 C CB . LYS A 91 ? 0.6275 0.4562 0.5156 -0.0713 -0.1021 0.0118 207 LYS A CB 716 C CG . LYS A 91 ? 0.6235 0.4600 0.5257 -0.0750 -0.0969 0.0062 207 LYS A CG 717 C CD . LYS A 91 ? 0.6058 0.4624 0.5336 -0.0718 -0.0787 0.0060 207 LYS A CD 718 C CE . LYS A 91 ? 0.5789 0.4340 0.5089 -0.0770 -0.0711 0.0022 207 LYS A CE 719 N NZ . LYS A 91 ? 0.5257 0.3963 0.4774 -0.0752 -0.0558 0.0031 207 LYS A NZ 720 N N . ILE A 92 ? 0.5652 0.4112 0.4727 -0.0581 -0.0894 0.0202 208 ILE A N 721 C CA . ILE A 92 ? 0.5051 0.3425 0.3988 -0.0567 -0.0887 0.0252 208 ILE A CA 722 C C . ILE A 92 ? 0.5518 0.3818 0.4179 -0.0634 -0.0723 0.0278 208 ILE A C 723 O O . ILE A 92 ? 0.5570 0.3915 0.4194 -0.0662 -0.0601 0.0248 208 ILE A O 724 C CB . ILE A 92 ? 0.5997 0.4580 0.5254 -0.0481 -0.0830 0.0239 208 ILE A CB 725 C CG1 . ILE A 92 ? 0.5301 0.4085 0.4714 -0.0479 -0.0623 0.0219 208 ILE A CG1 726 C CG2 . ILE A 92 ? 0.6005 0.4697 0.5566 -0.0409 -0.0984 0.0190 208 ILE A CG2 727 C CD1 . ILE A 92 ? 0.5302 0.4207 0.4823 -0.0432 -0.0512 0.0231 208 ILE A CD1 728 N N . SER A 93 ? 0.5753 0.3943 0.4236 -0.0657 -0.0725 0.0326 209 SER A N 729 C CA . SER A 93 ? 0.5764 0.3935 0.4034 -0.0726 -0.0563 0.0340 209 SER A CA 730 C C . SER A 93 ? 0.5747 0.4118 0.4257 -0.0665 -0.0447 0.0339 209 SER A C 731 O O . SER A 93 ? 0.5256 0.3625 0.3879 -0.0617 -0.0525 0.0359 209 SER A O 732 C CB . SER A 93 ? 0.6304 0.4208 0.4194 -0.0824 -0.0643 0.0397 209 SER A CB 733 O OG . SER A 93 ? 0.6372 0.4306 0.4110 -0.0901 -0.0478 0.0406 209 SER A OG 734 N N . PHE A 94 ? 0.4989 0.3519 0.3570 -0.0659 -0.0275 0.0310 210 PHE A N 735 C CA . PHE A 94 ? 0.5065 0.3794 0.3888 -0.0593 -0.0177 0.0303 210 PHE A CA 736 C C . PHE A 94 ? 0.5040 0.3863 0.3800 -0.0618 -0.0018 0.0286 210 PHE A C 737 O O . PHE A 94 ? 0.5191 0.4049 0.3920 -0.0620 0.0061 0.0246 210 PHE A O 738 C CB . PHE A 94 ? 0.5175 0.4041 0.4261 -0.0524 -0.0166 0.0273 210 PHE A CB 739 C CG . PHE A 94 ? 0.5045 0.4092 0.4341 -0.0465 -0.0071 0.0270 210 PHE A CG 740 C CD1 . PHE A 94 ? 0.4705 0.3840 0.4205 -0.0415 -0.0115 0.0265 210 PHE A CD1 741 C CD2 . PHE A 94 ? 0.4469 0.3599 0.3755 -0.0455 0.0056 0.0262 210 PHE A CD2 742 C CE1 . PHE A 94 ? 0.4637 0.3922 0.4286 -0.0373 -0.0024 0.0260 210 PHE A CE1 743 C CE2 . PHE A 94 ? 0.4704 0.3973 0.4145 -0.0404 0.0124 0.0266 210 PHE A CE2 744 C CZ . PHE A 94 ? 0.4046 0.3383 0.3648 -0.0372 0.0089 0.0268 210 PHE A CZ 745 N N . ASP A 95 ? 0.4772 0.3645 0.3537 -0.0631 0.0021 0.0305 211 ASP A N 746 C CA . ASP A 95 ? 0.4844 0.3844 0.3588 -0.0658 0.0159 0.0281 211 ASP A CA 747 C C . ASP A 95 ? 0.4379 0.3432 0.3192 -0.0658 0.0158 0.0306 211 ASP A C 748 O O . ASP A 95 ? 0.4926 0.3832 0.3580 -0.0731 0.0095 0.0343 211 ASP A O 749 C CB . ASP A 95 ? 0.5316 0.4220 0.3783 -0.0773 0.0203 0.0267 211 ASP A CB 750 C CG . ASP A 95 ? 0.6055 0.5146 0.4548 -0.0799 0.0358 0.0213 211 ASP A CG 751 O OD1 . ASP A 95 ? 0.5531 0.4808 0.4252 -0.0705 0.0417 0.0181 211 ASP A OD1 752 O OD2 . ASP A 95 ? 0.7350 0.6406 0.5633 -0.0917 0.0420 0.0197 211 ASP A OD2 753 N N . PRO A 96 ? 0.4492 0.3721 0.3514 -0.0581 0.0215 0.0290 212 PRO A N 754 C CA . PRO A 96 ? 0.4752 0.4030 0.3851 -0.0570 0.0205 0.0304 212 PRO A CA 755 C C . PRO A 96 ? 0.4692 0.3942 0.3643 -0.0677 0.0234 0.0312 212 PRO A C 756 O O . PRO A 96 ? 0.5010 0.4330 0.3883 -0.0741 0.0322 0.0284 212 PRO A O 757 C CB . PRO A 96 ? 0.4291 0.3763 0.3576 -0.0489 0.0280 0.0278 212 PRO A CB 758 C CG . PRO A 96 ? 0.4154 0.3615 0.3497 -0.0436 0.0278 0.0270 212 PRO A CG 759 C CD . PRO A 96 ? 0.3899 0.3250 0.3074 -0.0498 0.0271 0.0261 212 PRO A CD 760 N N . ILE A 97 ? 0.4619 0.3764 0.3531 -0.0704 0.0164 0.0340 213 ILE A N 761 C CA . ILE A 97 ? 0.4673 0.3789 0.3449 -0.0824 0.0197 0.0349 213 ILE A CA 762 C C . ILE A 97 ? 0.4197 0.3435 0.3122 -0.0789 0.0212 0.0331 213 ILE A C 763 O O . ILE A 97 ? 0.4290 0.3565 0.3369 -0.0680 0.0173 0.0322 213 ILE A O 764 C CB . ILE A 97 ? 0.5378 0.4187 0.3890 -0.0924 0.0088 0.0404 213 ILE A CB 765 C CG1 . ILE A 97 ? 0.4968 0.3633 0.3546 -0.0844 -0.0048 0.0422 213 ILE A CG1 766 C CG2 . ILE A 97 ? 0.6382 0.5045 0.4708 -0.0962 0.0054 0.0423 213 ILE A CG2 767 C CD1 . ILE A 97 ? 0.5271 0.3590 0.3580 -0.0929 -0.0186 0.0479 213 ILE A CD1 768 N N . PRO A 98 ? 0.4725 0.4040 0.3604 -0.0893 0.0275 0.0318 214 PRO A N 769 C CA . PRO A 98 ? 0.4659 0.4089 0.3669 -0.0867 0.0278 0.0296 214 PRO A CA 770 C C . PRO A 98 ? 0.4999 0.4204 0.3947 -0.0856 0.0162 0.0322 214 PRO A C 771 O O . PRO A 98 ? 0.4957 0.3906 0.3705 -0.0939 0.0087 0.0363 214 PRO A O 772 C CB . PRO A 98 ? 0.5062 0.4604 0.4018 -0.1014 0.0360 0.0273 214 PRO A CB 773 C CG . PRO A 98 ? 0.5381 0.4984 0.4266 -0.1068 0.0443 0.0257 214 PRO A CG 774 C CD . PRO A 98 ? 0.5258 0.4613 0.3995 -0.1037 0.0364 0.0306 214 PRO A CD 775 N N . ILE A 99 ? 0.4567 0.3854 0.3671 -0.0753 0.0144 0.0294 215 ILE A N 776 C CA . ILE A 99 ? 0.4508 0.3620 0.3589 -0.0723 0.0047 0.0288 215 ILE A CA 777 C C . ILE A 99 ? 0.4417 0.3636 0.3549 -0.0749 0.0075 0.0252 215 ILE A C 778 O O . ILE A 99 ? 0.4159 0.3608 0.3431 -0.0692 0.0140 0.0222 215 ILE A O 779 C CB . ILE A 99 ? 0.4988 0.4118 0.4215 -0.0573 0.0009 0.0264 215 ILE A CB 780 C CG1 . ILE A 99 ? 0.4775 0.3842 0.3985 -0.0547 -0.0020 0.0291 215 ILE A CG1 781 C CG2 . ILE A 99 ? 0.5145 0.4112 0.4374 -0.0524 -0.0088 0.0232 215 ILE A CG2 782 C CD1 . ILE A 99 ? 0.5420 0.4203 0.4424 -0.0621 -0.0129 0.0335 215 ILE A CD1 783 N N . HIS A 100 ? 0.4686 0.3714 0.3689 -0.0837 0.0012 0.0256 216 HIS A N 784 C CA . HIS A 100 ? 0.4681 0.3780 0.3720 -0.0868 0.0018 0.0214 216 HIS A CA 785 C C . HIS A 100 ? 0.4569 0.3558 0.3653 -0.0754 -0.0055 0.0169 216 HIS A C 786 O O . HIS A 100 ? 0.4950 0.3715 0.3984 -0.0701 -0.0144 0.0173 216 HIS A O 787 C CB . HIS A 100 ? 0.4952 0.3899 0.3816 -0.1053 -0.0003 0.0235 216 HIS A CB 788 C CG . HIS A 100 ? 0.5654 0.4690 0.4445 -0.1191 0.0080 0.0267 216 HIS A CG 789 N ND1 . HIS A 100 ? 0.5112 0.4382 0.3962 -0.1311 0.0168 0.0236 216 HIS A ND1 790 C CD2 . HIS A 100 ? 0.6060 0.4992 0.4723 -0.1235 0.0091 0.0316 216 HIS A CD2 791 C CE1 . HIS A 100 ? 0.5245 0.4568 0.4018 -0.1421 0.0246 0.0256 216 HIS A CE1 792 N NE2 . HIS A 100 ? 0.5147 0.4252 0.3784 -0.1381 0.0202 0.0308 216 HIS A NE2 793 N N . TYR A 101 ? 0.4426 0.3576 0.3605 -0.0712 -0.0023 0.0117 217 TYR A N 794 C CA . TYR A 101 ? 0.4249 0.3324 0.3462 -0.0611 -0.0069 0.0053 217 TYR A CA 795 C C . TYR A 101 ? 0.4993 0.3940 0.4106 -0.0696 -0.0122 0.0016 217 TYR A C 796 O O . TYR A 101 ? 0.4634 0.3719 0.3745 -0.0788 -0.0086 0.0015 217 TYR A O 797 C CB . TYR A 101 ? 0.3959 0.3271 0.3306 -0.0501 0.0005 0.0019 217 TYR A CB 798 C CG . TYR A 101 ? 0.4916 0.4255 0.4348 -0.0414 0.0025 0.0038 217 TYR A CG 799 C CD1 . TYR A 101 ? 0.4632 0.3885 0.4125 -0.0317 -0.0014 -0.0013 217 TYR A CD1 800 C CD2 . TYR A 101 ? 0.4892 0.4338 0.4352 -0.0432 0.0074 0.0096 217 TYR A CD2 801 C CE1 . TYR A 101 ? 0.4023 0.3318 0.3617 -0.0251 -0.0005 -0.0003 217 TYR A CE1 802 C CE2 . TYR A 101 ? 0.5095 0.4547 0.4623 -0.0368 0.0082 0.0111 217 TYR A CE2 803 C CZ . TYR A 101 ? 0.4226 0.3611 0.3826 -0.0284 0.0041 0.0064 217 TYR A CZ 804 O OH . TYR A 101 ? 0.4248 0.3663 0.3940 -0.0232 0.0041 0.0072 217 TYR A OH 805 N N . CYS A 102 ? 0.4811 0.3487 0.3850 -0.0663 -0.0218 -0.0018 218 CYS A N 806 C CA . CYS A 102 ? 0.4698 0.3158 0.3597 -0.0764 -0.0291 -0.0043 218 CYS A CA 807 C C . CYS A 102 ? 0.4911 0.3257 0.3826 -0.0653 -0.0346 -0.0149 218 CYS A C 808 O O . CYS A 102 ? 0.5101 0.3428 0.4108 -0.0503 -0.0362 -0.0199 218 CYS A O 809 C CB . CYS A 102 ? 0.5966 0.4093 0.4680 -0.0867 -0.0383 0.0024 218 CYS A CB 810 S SG . CYS A 102 ? 0.5795 0.4018 0.4447 -0.1002 -0.0311 0.0134 218 CYS A SG 811 N N . THR A 103 ? 0.5664 0.3942 0.4494 -0.0735 -0.0374 -0.0194 219 THR A N 812 C CA . THR A 103 ? 0.5678 0.3815 0.4490 -0.0643 -0.0429 -0.0308 219 THR A CA 813 C C . THR A 103 ? 0.5841 0.3551 0.4514 -0.0650 -0.0571 -0.0327 219 THR A C 814 O O . THR A 103 ? 0.5849 0.3335 0.4360 -0.0805 -0.0634 -0.0249 219 THR A O 815 C CB . THR A 103 ? 0.5729 0.3979 0.4499 -0.0722 -0.0405 -0.0363 219 THR A CB 816 O OG1 . THR A 103 ? 0.5846 0.4115 0.4546 -0.0915 -0.0409 -0.0292 219 THR A OG1 817 C CG2 . THR A 103 ? 0.4765 0.3363 0.3654 -0.0640 -0.0299 -0.0388 219 THR A CG2 818 N N . PRO A 104 ? 0.6171 0.3756 0.4896 -0.0486 -0.0625 -0.0438 220 PRO A N 819 C CA . PRO A 104 ? 0.6997 0.4142 0.5589 -0.0466 -0.0786 -0.0478 220 PRO A CA 820 C C . PRO A 104 ? 0.7059 0.4029 0.5492 -0.0579 -0.0829 -0.0535 220 PRO A C 821 O O . PRO A 104 ? 0.6862 0.4084 0.5313 -0.0653 -0.0738 -0.0555 220 PRO A O 822 C CB . PRO A 104 ? 0.7296 0.4466 0.6064 -0.0231 -0.0803 -0.0611 220 PRO A CB 823 C CG . PRO A 104 ? 0.6380 0.3959 0.5288 -0.0182 -0.0640 -0.0677 220 PRO A CG 824 C CD . PRO A 104 ? 0.5699 0.3541 0.4602 -0.0318 -0.0537 -0.0543 220 PRO A CD 825 N N . ALA A 105 ? 0.6945 0.3464 0.5214 -0.0594 -0.0985 -0.0560 221 ALA A N 826 C CA . ALA A 105 ? 0.7351 0.3639 0.5447 -0.0711 -0.1047 -0.0617 221 ALA A CA 827 C C . ALA A 105 ? 0.7690 0.4201 0.5879 -0.0615 -0.0972 -0.0771 221 ALA A C 828 O O . ALA A 105 ? 0.7431 0.4103 0.5782 -0.0416 -0.0922 -0.0873 221 ALA A O 829 C CB . ALA A 105 ? 0.8207 0.3922 0.6116 -0.0688 -0.1245 -0.0642 221 ALA A CB 830 N N . GLY A 106 ? 0.8124 0.4649 0.6202 -0.0770 -0.0963 -0.0793 222 GLY A N 831 C CA . GLY A 106 ? 0.8454 0.5165 0.6567 -0.0703 -0.0904 -0.0932 222 GLY A CA 832 C C . GLY A 106 ? 0.7466 0.4672 0.5717 -0.0697 -0.0751 -0.0899 222 GLY A C 833 O O . GLY A 106 ? 0.6747 0.4120 0.4989 -0.0665 -0.0699 -0.0994 222 GLY A O 834 N N . TYR A 107 ? 0.7150 0.4569 0.5507 -0.0727 -0.0686 -0.0765 223 TYR A N 835 C CA . TYR A 107 ? 0.6181 0.4030 0.4652 -0.0731 -0.0561 -0.0721 223 TYR A CA 836 C C . TYR A 107 ? 0.6385 0.4368 0.4875 -0.0899 -0.0542 -0.0587 223 TYR A C 837 O O . TYR A 107 ? 0.6897 0.4668 0.5318 -0.1005 -0.0597 -0.0513 223 TYR A O 838 C CB . TYR A 107 ? 0.5845 0.3897 0.4472 -0.0560 -0.0469 -0.0719 223 TYR A CB 839 C CG . TYR A 107 ? 0.6575 0.4571 0.5228 -0.0390 -0.0455 -0.0868 223 TYR A CG 840 C CD1 . TYR A 107 ? 0.6128 0.4375 0.4805 -0.0323 -0.0348 -0.0939 223 TYR A CD1 841 C CD2 . TYR A 107 ? 0.6697 0.4386 0.5347 -0.0296 -0.0549 -0.0943 223 TYR A CD2 842 C CE1 . TYR A 107 ? 0.6433 0.4660 0.5137 -0.0181 -0.0311 -0.1092 223 TYR A CE1 843 C CE2 . TYR A 107 ? 0.7230 0.4907 0.5944 -0.0130 -0.0528 -0.1104 223 TYR A CE2 844 C CZ . TYR A 107 ? 0.7492 0.5456 0.6238 -0.0079 -0.0395 -0.1184 223 TYR A CZ 845 O OH . TYR A 107 ? 0.8318 0.6295 0.7131 0.0075 -0.0351 -0.1362 223 TYR A OH 846 N N . VAL A 108 ? 0.5673 0.4008 0.4251 -0.0924 -0.0464 -0.0559 224 VAL A N 847 C CA . VAL A 108 ? 0.5710 0.4237 0.4355 -0.1059 -0.0430 -0.0457 224 VAL A CA 848 C C . VAL A 108 ? 0.5442 0.4334 0.4229 -0.0973 -0.0338 -0.0424 224 VAL A C 849 O O . VAL A 108 ? 0.5401 0.4381 0.4190 -0.0853 -0.0310 -0.0478 224 VAL A O 850 C CB . VAL A 108 ? 0.6770 0.5299 0.5356 -0.1254 -0.0482 -0.0475 224 VAL A CB 851 C CG1 . VAL A 108 ? 0.6230 0.5011 0.4856 -0.1232 -0.0480 -0.0543 224 VAL A CG1 852 C CG2 . VAL A 108 ? 0.7777 0.6437 0.6425 -0.1420 -0.0445 -0.0382 224 VAL A CG2 853 N N . ILE A 109 ? 0.4966 0.4051 0.3853 -0.1038 -0.0291 -0.0340 225 ILE A N 854 C CA . ILE A 109 ? 0.4864 0.4263 0.3880 -0.0955 -0.0221 -0.0308 225 ILE A CA 855 C C . ILE A 109 ? 0.4533 0.4183 0.3622 -0.1050 -0.0239 -0.0321 225 ILE A C 856 O O . ILE A 109 ? 0.5067 0.4762 0.4194 -0.1202 -0.0249 -0.0307 225 ILE A O 857 C CB . ILE A 109 ? 0.4417 0.3872 0.3516 -0.0930 -0.0158 -0.0222 225 ILE A CB 858 C CG1 . ILE A 109 ? 0.5015 0.4243 0.4068 -0.0825 -0.0161 -0.0219 225 ILE A CG1 859 C CG2 . ILE A 109 ? 0.4365 0.4113 0.3589 -0.0850 -0.0098 -0.0191 225 ILE A CG2 860 C CD1 . ILE A 109 ? 0.4399 0.3636 0.3505 -0.0809 -0.0119 -0.0137 225 ILE A CD1 861 N N . LEU A 110 ? 0.4367 0.4178 0.3468 -0.0970 -0.0251 -0.0352 226 LEU A N 862 C CA . LEU A 110 ? 0.4846 0.4928 0.4051 -0.1028 -0.0288 -0.0365 226 LEU A CA 863 C C . LEU A 110 ? 0.4304 0.4625 0.3665 -0.0955 -0.0234 -0.0303 226 LEU A C 864 O O . LEU A 110 ? 0.4383 0.4673 0.3722 -0.0829 -0.0185 -0.0262 226 LEU A O 865 C CB . LEU A 110 ? 0.4402 0.4506 0.3508 -0.0986 -0.0360 -0.0429 226 LEU A CB 866 C CG . LEU A 110 ? 0.5006 0.4857 0.3944 -0.1053 -0.0416 -0.0511 226 LEU A CG 867 C CD1 . LEU A 110 ? 0.5030 0.4939 0.3866 -0.1047 -0.0499 -0.0582 226 LEU A CD1 868 C CD2 . LEU A 110 ? 0.4957 0.4718 0.3926 -0.1232 -0.0445 -0.0517 226 LEU A CD2 869 N N . LYS A 111 ? 0.4189 0.4752 0.3718 -0.1039 -0.0238 -0.0306 227 LYS A N 870 C CA . LYS A 111 ? 0.3746 0.4538 0.3443 -0.0969 -0.0189 -0.0267 227 LYS A CA 871 C C . LYS A 111 ? 0.3950 0.5031 0.3793 -0.0942 -0.0266 -0.0311 227 LYS A C 872 O O . LYS A 111 ? 0.4336 0.5551 0.4259 -0.1058 -0.0323 -0.0372 227 LYS A O 873 C CB . LYS A 111 ? 0.4247 0.5091 0.4036 -0.1089 -0.0112 -0.0249 227 LYS A CB 874 C CG . LYS A 111 ? 0.4245 0.5306 0.4200 -0.1017 -0.0047 -0.0225 227 LYS A CG 875 C CD . LYS A 111 ? 0.4860 0.5992 0.4881 -0.1164 0.0039 -0.0226 227 LYS A CD 876 C CE . LYS A 111 ? 0.5008 0.6344 0.5183 -0.1080 0.0112 -0.0219 227 LYS A CE 877 N NZ . LYS A 111 ? 0.4755 0.6221 0.5001 -0.1240 0.0209 -0.0243 227 LYS A NZ 878 N N . CYS A 112 ? 0.3550 0.4717 0.3425 -0.0790 -0.0283 -0.0281 228 CYS A N 879 C CA . CYS A 112 ? 0.3833 0.5252 0.3846 -0.0736 -0.0385 -0.0318 228 CYS A CA 880 C C . CYS A 112 ? 0.3129 0.4842 0.3424 -0.0739 -0.0348 -0.0343 228 CYS A C 881 O O . CYS A 112 ? 0.3580 0.5289 0.3917 -0.0654 -0.0278 -0.0300 228 CYS A O 882 C CB . CYS A 112 ? 0.3916 0.5245 0.3794 -0.0572 -0.0440 -0.0269 228 CYS A CB 883 S SG . CYS A 112 ? 0.4712 0.6306 0.4741 -0.0481 -0.0606 -0.0307 228 CYS A SG 884 N N . ASN A 113 ? 0.3770 0.5757 0.4270 -0.0836 -0.0396 -0.0424 229 ASN A N 885 C CA . ASN A 113 ? 0.4241 0.6559 0.5042 -0.0848 -0.0345 -0.0477 229 ASN A CA 886 C C . ASN A 113 ? 0.3900 0.6511 0.4932 -0.0705 -0.0467 -0.0532 229 ASN A C 887 O O . ASN A 113 ? 0.4229 0.7177 0.5566 -0.0705 -0.0440 -0.0610 229 ASN A O 888 C CB . ASN A 113 ? 0.4350 0.6811 0.5262 -0.1078 -0.0277 -0.0539 229 ASN A CB 889 C CG . ASN A 113 ? 0.4324 0.6441 0.4981 -0.1204 -0.0181 -0.0474 229 ASN A CG 890 O OD1 . ASN A 113 ? 0.4823 0.6824 0.5420 -0.1184 -0.0077 -0.0420 229 ASN A OD1 891 N ND2 . ASN A 113 ? 0.4246 0.6175 0.4743 -0.1325 -0.0232 -0.0482 229 ASN A ND2 892 N N . ASP A 114 ? 0.3821 0.6295 0.4697 -0.0579 -0.0604 -0.0498 230 ASP A N 893 C CA . ASP A 114 ? 0.4178 0.6853 0.5223 -0.0413 -0.0752 -0.0531 230 ASP A CA 894 C C . ASP A 114 ? 0.4594 0.7265 0.5717 -0.0267 -0.0686 -0.0496 230 ASP A C 895 O O . ASP A 114 ? 0.3867 0.6234 0.4747 -0.0208 -0.0628 -0.0398 230 ASP A O 896 C CB . ASP A 114 ? 0.4771 0.7220 0.5542 -0.0324 -0.0910 -0.0480 230 ASP A CB 897 C CG . ASP A 114 ? 0.5297 0.7785 0.6014 -0.0449 -0.1011 -0.0539 230 ASP A CG 898 O OD1 . ASP A 114 ? 0.5109 0.7749 0.5972 -0.0619 -0.0946 -0.0606 230 ASP A OD1 899 O OD2 . ASP A 114 ? 0.5702 0.8044 0.6201 -0.0388 -0.1156 -0.0516 230 ASP A OD2 900 N N . LYS A 115 ? 0.4810 0.7828 0.6283 -0.0213 -0.0689 -0.0588 231 LYS A N 901 C CA . LYS A 115 ? 0.5257 0.8273 0.6812 -0.0099 -0.0599 -0.0575 231 LYS A CA 902 C C . LYS A 115 ? 0.5365 0.8107 0.6727 0.0101 -0.0702 -0.0485 231 LYS A C 903 O O . LYS A 115 ? 0.5935 0.8481 0.7184 0.0156 -0.0609 -0.0421 231 LYS A O 904 C CB . LYS A 115 ? 0.5269 0.8736 0.7257 -0.0068 -0.0578 -0.0719 231 LYS A CB 905 C CG . LYS A 115 ? 0.5661 0.9334 0.7786 -0.0281 -0.0386 -0.0786 231 LYS A CG 906 C CD . LYS A 115 ? 0.6490 1.0624 0.9041 -0.0239 -0.0334 -0.0941 231 LYS A CD 907 C CE . LYS A 115 ? 0.7097 1.1434 0.9746 -0.0484 -0.0128 -0.1008 231 LYS A CE 908 N NZ . LYS A 115 ? 0.7442 1.1917 1.0133 -0.0696 -0.0154 -0.1045 231 LYS A NZ 909 N N . ASN A 116 ? 0.4261 0.6971 0.5561 0.0197 -0.0900 -0.0475 232 ASN A N 910 C CA . ASN A 116 ? 0.4368 0.6783 0.5439 0.0368 -0.1014 -0.0379 232 ASN A CA 911 C C . ASN A 116 ? 0.4281 0.6313 0.4913 0.0315 -0.1028 -0.0260 232 ASN A C 912 O O . ASN A 116 ? 0.4497 0.6291 0.4894 0.0420 -0.1156 -0.0183 232 ASN A O 913 C CB . ASN A 116 ? 0.5306 0.7892 0.6568 0.0541 -0.1247 -0.0440 232 ASN A CB 914 C CG . ASN A 116 ? 0.5524 0.8433 0.7202 0.0655 -0.1227 -0.0557 232 ASN A CG 915 O OD1 . ASN A 116 ? 0.5121 0.7961 0.6814 0.0676 -0.1080 -0.0544 232 ASN A OD1 916 N ND2 . ASN A 116 ? 0.5568 0.8847 0.7597 0.0728 -0.1376 -0.0686 232 ASN A ND2 917 N N . PHE A 117 ? 0.4411 0.6372 0.4922 0.0149 -0.0896 -0.0249 233 PHE A N 918 C CA . PHE A 117 ? 0.4966 0.6598 0.5092 0.0096 -0.0880 -0.0164 233 PHE A CA 919 C C . PHE A 117 ? 0.4993 0.6328 0.4889 0.0175 -0.0824 -0.0056 233 PHE A C 920 O O . PHE A 117 ? 0.4304 0.5623 0.4284 0.0179 -0.0694 -0.0040 233 PHE A O 921 C CB . PHE A 117 ? 0.4351 0.5954 0.4429 -0.0074 -0.0741 -0.0186 233 PHE A CB 922 C CG . PHE A 117 ? 0.5145 0.6455 0.4870 -0.0120 -0.0723 -0.0133 233 PHE A CG 923 C CD1 . PHE A 117 ? 0.6158 0.7386 0.5680 -0.0101 -0.0864 -0.0131 233 PHE A CD1 924 C CD2 . PHE A 117 ? 0.5520 0.6644 0.5117 -0.0178 -0.0568 -0.0097 233 PHE A CD2 925 C CE1 . PHE A 117 ? 0.6496 0.7470 0.5683 -0.0147 -0.0829 -0.0100 233 PHE A CE1 926 C CE2 . PHE A 117 ? 0.5064 0.5956 0.4370 -0.0211 -0.0540 -0.0074 233 PHE A CE2 927 C CZ . PHE A 117 ? 0.6219 0.7041 0.5316 -0.0200 -0.0659 -0.0079 233 PHE A CZ 928 N N . ASN A 118 ? 0.5002 0.6092 0.4589 0.0223 -0.0921 0.0018 234 ASN A N 929 C CA . ASN A 118 ? 0.5081 0.5888 0.4440 0.0276 -0.0871 0.0122 234 ASN A CA 930 C C . ASN A 118 ? 0.5170 0.5786 0.4317 0.0169 -0.0695 0.0165 234 ASN A C 931 O O . ASN A 118 ? 0.5156 0.5565 0.4141 0.0186 -0.0627 0.0242 234 ASN A O 932 C CB . ASN A 118 ? 0.5596 0.6197 0.4701 0.0374 -0.1054 0.0193 234 ASN A CB 933 C CG . ASN A 118 ? 0.6784 0.7231 0.5549 0.0299 -0.1114 0.0216 234 ASN A CG 934 O OD1 . ASN A 118 ? 0.5968 0.6373 0.4615 0.0181 -0.0981 0.0200 234 ASN A OD1 935 N ND2 . ASN A 118 ? 0.8389 0.8733 0.6981 0.0374 -0.1324 0.0249 234 ASN A ND2 936 N N . GLY A 119 ? 0.4362 0.5048 0.3522 0.0059 -0.0627 0.0108 235 GLY A N 937 C CA . GLY A 119 ? 0.4537 0.5071 0.3545 -0.0023 -0.0474 0.0124 235 GLY A CA 938 C C . GLY A 119 ? 0.5148 0.5532 0.3856 -0.0082 -0.0481 0.0117 235 GLY A C 939 O O . GLY A 119 ? 0.5164 0.5476 0.3802 -0.0148 -0.0363 0.0091 235 GLY A O 940 N N . THR A 120 ? 0.4770 0.5100 0.3292 -0.0053 -0.0625 0.0133 236 THR A N 941 C CA . THR A 120 ? 0.5240 0.5441 0.3461 -0.0119 -0.0636 0.0109 236 THR A CA 942 C C . THR A 120 ? 0.5631 0.5913 0.3820 -0.0113 -0.0827 0.0066 236 THR A C 943 O O . THR A 120 ? 0.6516 0.6844 0.4753 -0.0028 -0.0984 0.0100 236 THR A O 944 C CB . THR A 120 ? 0.6310 0.6260 0.4165 -0.0121 -0.0599 0.0192 236 THR A CB 945 O OG1 . THR A 120 ? 0.7468 0.7331 0.5158 -0.0057 -0.0784 0.0254 236 THR A OG1 946 C CG2 . THR A 120 ? 0.5616 0.5505 0.3540 -0.0106 -0.0459 0.0253 236 THR A CG2 947 N N . GLY A 121 ? 0.5590 0.5879 0.3694 -0.0196 -0.0829 -0.0014 237 GLY A N 948 C CA . GLY A 121 ? 0.4888 0.5260 0.2964 -0.0205 -0.1017 -0.0065 237 GLY A CA 949 C C . GLY A 121 ? 0.5562 0.6153 0.3937 -0.0276 -0.1020 -0.0167 237 GLY A C 950 O O . GLY A 121 ? 0.4999 0.5619 0.3530 -0.0326 -0.0873 -0.0193 237 GLY A O 951 N N . PRO A 122 ? 0.5383 0.6117 0.3829 -0.0290 -0.1198 -0.0224 238 PRO A N 952 C CA . PRO A 122 ? 0.4683 0.5611 0.3377 -0.0393 -0.1205 -0.0326 238 PRO A CA 953 C C . PRO A 122 ? 0.5428 0.6639 0.4552 -0.0382 -0.1175 -0.0340 238 PRO A C 954 O O . PRO A 122 ? 0.5243 0.6576 0.4522 -0.0272 -0.1235 -0.0303 238 PRO A O 955 C CB . PRO A 122 ? 0.4960 0.5945 0.3558 -0.0412 -0.1421 -0.0382 238 PRO A CB 956 C CG . PRO A 122 ? 0.5601 0.6551 0.4095 -0.0278 -0.1563 -0.0304 238 PRO A CG 957 C CD . PRO A 122 ? 0.5949 0.6660 0.4235 -0.0220 -0.1413 -0.0198 238 PRO A CD 958 N N . CYS A 123 ? 0.5245 0.6535 0.4534 -0.0502 -0.1078 -0.0399 239 CYS A N 959 C CA . CYS A 123 ? 0.3989 0.5543 0.3649 -0.0538 -0.1023 -0.0427 239 CYS A CA 960 C C . CYS A 123 ? 0.4607 0.6348 0.4423 -0.0683 -0.1095 -0.0529 239 CYS A C 961 O O . CYS A 123 ? 0.5091 0.6663 0.4737 -0.0797 -0.1076 -0.0565 239 CYS A O 962 C CB . CYS A 123 ? 0.3809 0.5229 0.3466 -0.0581 -0.0828 -0.0388 239 CYS A CB 963 S SG . CYS A 123 ? 0.4936 0.6635 0.4973 -0.0648 -0.0729 -0.0415 239 CYS A SG 964 N N . LYS A 124 ? 0.4724 0.6817 0.4874 -0.0681 -0.1180 -0.0587 240 LYS A N 965 C CA . LYS A 124 ? 0.5415 0.7730 0.5742 -0.0832 -0.1263 -0.0694 240 LYS A CA 966 C C . LYS A 124 ? 0.5170 0.7590 0.5687 -0.1011 -0.1109 -0.0730 240 LYS A C 967 O O . LYS A 124 ? 0.5438 0.7872 0.5962 -0.1188 -0.1128 -0.0795 240 LYS A O 968 C CB . LYS A 124 ? 0.5345 0.8029 0.5967 -0.0754 -0.1446 -0.0761 240 LYS A CB 969 C CG . LYS A 124 ? 0.6264 0.8817 0.6671 -0.0578 -0.1632 -0.0715 240 LYS A CG 970 C CD . LYS A 124 ? 0.7840 1.0112 0.7856 -0.0641 -0.1722 -0.0715 240 LYS A CD 971 C CE . LYS A 124 ? 0.8543 1.1045 0.8707 -0.0757 -0.1891 -0.0833 240 LYS A CE 972 N NZ . LYS A 124 ? 0.8739 1.0963 0.8495 -0.0794 -0.2011 -0.0842 240 LYS A NZ 973 N N . ASN A 125 ? 0.4224 0.6685 0.4861 -0.0974 -0.0962 -0.0684 241 ASN A N 974 C CA . ASN A 125 ? 0.3903 0.6461 0.4696 -0.1144 -0.0813 -0.0709 241 ASN A CA 975 C C . ASN A 125 ? 0.3581 0.5763 0.4110 -0.1168 -0.0669 -0.0621 241 ASN A C 976 O O . ASN A 125 ? 0.4134 0.6272 0.4672 -0.1077 -0.0569 -0.0560 241 ASN A O 977 C CB . ASN A 125 ? 0.5026 0.7969 0.6185 -0.1093 -0.0762 -0.0748 241 ASN A CB 978 C CG . ASN A 125 ? 0.6675 0.9755 0.7986 -0.1292 -0.0598 -0.0782 241 ASN A CG 979 O OD1 . ASN A 125 ? 0.6335 0.9206 0.7475 -0.1477 -0.0540 -0.0767 241 ASN A OD1 980 N ND2 . ASN A 125 ? 0.8862 1.2282 1.0481 -0.1256 -0.0525 -0.0832 241 ASN A ND2 981 N N . VAL A 126 ? 0.5042 0.6945 0.5339 -0.1282 -0.0673 -0.0624 242 VAL A N 982 C CA . VAL A 126 ? 0.4796 0.6321 0.4839 -0.1273 -0.0575 -0.0554 242 VAL A CA 983 C C . VAL A 126 ? 0.4624 0.6039 0.4652 -0.1476 -0.0498 -0.0561 242 VAL A C 984 O O . VAL A 126 ? 0.5005 0.6495 0.5085 -0.1649 -0.0546 -0.0626 242 VAL A O 985 C CB . VAL A 126 ? 0.4551 0.5774 0.4298 -0.1226 -0.0645 -0.0562 242 VAL A CB 986 C CG1 . VAL A 126 ? 0.4260 0.5146 0.3803 -0.1176 -0.0546 -0.0506 242 VAL A CG1 987 C CG2 . VAL A 126 ? 0.5478 0.6782 0.5175 -0.1071 -0.0746 -0.0560 242 VAL A CG2 988 N N . SER A 127 ? 0.4311 0.5524 0.4246 -0.1464 -0.0389 -0.0491 243 SER A N 989 C CA . SER A 127 ? 0.4924 0.5929 0.4759 -0.1649 -0.0333 -0.0477 243 SER A CA 990 C C . SER A 127 ? 0.5147 0.5731 0.4725 -0.1573 -0.0316 -0.0422 243 SER A C 991 O O . SER A 127 ? 0.4890 0.5410 0.4413 -0.1389 -0.0310 -0.0395 243 SER A O 992 C CB . SER A 127 ? 0.4506 0.5722 0.4510 -0.1750 -0.0220 -0.0458 243 SER A CB 993 O OG . SER A 127 ? 0.4945 0.6187 0.4981 -0.1588 -0.0148 -0.0399 243 SER A OG 994 N N . SER A 128 ? 0.5230 0.5523 0.4652 -0.1718 -0.0315 -0.0412 244 SER A N 995 C CA . SER A 128 ? 0.5176 0.5077 0.4390 -0.1637 -0.0314 -0.0371 244 SER A CA 996 C C . SER A 128 ? 0.5864 0.5634 0.5032 -0.1720 -0.0243 -0.0295 244 SER A C 997 O O . SER A 128 ? 0.6104 0.5951 0.5301 -0.1917 -0.0209 -0.0286 244 SER A O 998 C CB . SER A 128 ? 0.5663 0.5236 0.4681 -0.1694 -0.0407 -0.0428 244 SER A CB 999 O OG . SER A 128 ? 0.6743 0.6217 0.5709 -0.1933 -0.0432 -0.0436 244 SER A OG 1000 N N . VAL A 129 ? 0.5544 0.5129 0.4636 -0.1578 -0.0221 -0.0244 245 VAL A N 1001 C CA . VAL A 129 ? 0.5387 0.4821 0.4405 -0.1631 -0.0173 -0.0167 245 VAL A CA 1002 C C . VAL A 129 ? 0.5693 0.4760 0.4558 -0.1507 -0.0227 -0.0146 245 VAL A C 1003 O O . VAL A 129 ? 0.5872 0.4908 0.4748 -0.1351 -0.0259 -0.0195 245 VAL A O 1004 C CB . VAL A 129 ? 0.5668 0.5394 0.4848 -0.1548 -0.0077 -0.0130 245 VAL A CB 1005 C CG1 . VAL A 129 ? 0.5952 0.6076 0.5332 -0.1639 -0.0029 -0.0171 245 VAL A CG1 1006 C CG2 . VAL A 129 ? 0.4895 0.4677 0.4137 -0.1315 -0.0078 -0.0133 245 VAL A CG2 1007 N N . GLN A 130 ? 0.5615 0.4412 0.4336 -0.1577 -0.0239 -0.0081 246 GLN A N 1008 C CA . GLN A 130 ? 0.6313 0.4771 0.4917 -0.1448 -0.0310 -0.0066 246 GLN A CA 1009 C C . GLN A 130 ? 0.5867 0.4469 0.4588 -0.1274 -0.0254 -0.0034 246 GLN A C 1010 O O . GLN A 130 ? 0.5639 0.4125 0.4377 -0.1108 -0.0292 -0.0061 246 GLN A O 1011 C CB . GLN A 130 ? 0.7328 0.5384 0.5694 -0.1597 -0.0381 -0.0004 246 GLN A CB 1012 C CG . GLN A 130 ? 1.0409 0.8248 0.8626 -0.1781 -0.0450 -0.0033 246 GLN A CG 1013 C CD . GLN A 130 ? 1.2948 1.0383 1.0887 -0.1977 -0.0511 0.0049 246 GLN A CD 1014 O OE1 . GLN A 130 ? 1.3878 1.1312 1.1747 -0.2049 -0.0460 0.0133 246 GLN A OE1 1015 N NE2 . GLN A 130 ? 1.3628 1.0686 1.1376 -0.2073 -0.0625 0.0026 246 GLN A NE2 1016 N N . CYS A 131 ? 0.5313 0.4177 0.4128 -0.1317 -0.0160 0.0009 247 CYS A N 1017 C CA . CYS A 131 ? 0.5487 0.4469 0.4394 -0.1181 -0.0107 0.0044 247 CYS A CA 1018 C C . CYS A 131 ? 0.4659 0.4032 0.3748 -0.1155 -0.0012 0.0035 247 CYS A C 1019 O O . CYS A 131 ? 0.5095 0.4658 0.4238 -0.1276 0.0024 0.0017 247 CYS A O 1020 C CB . CYS A 131 ? 0.5098 0.3890 0.3868 -0.1262 -0.0111 0.0121 247 CYS A CB 1021 S SG . CYS A 131 ? 0.6403 0.4664 0.4923 -0.1285 -0.0262 0.0152 247 CYS A SG 1022 N N . THR A 132 ? 0.3996 0.3487 0.3186 -0.1000 0.0024 0.0044 248 THR A N 1023 C CA . THR A 132 ? 0.4545 0.4348 0.3886 -0.0959 0.0099 0.0044 248 THR A CA 1024 C C . THR A 132 ? 0.4811 0.4664 0.4139 -0.1061 0.0160 0.0079 248 THR A C 1025 O O . THR A 132 ? 0.4826 0.4448 0.3998 -0.1157 0.0141 0.0118 248 THR A O 1026 C CB . THR A 132 ? 0.4019 0.3876 0.3431 -0.0788 0.0120 0.0055 248 THR A CB 1027 O OG1 . THR A 132 ? 0.4333 0.4016 0.3687 -0.0761 0.0117 0.0097 248 THR A OG1 1028 C CG2 . THR A 132 ? 0.4417 0.4238 0.3821 -0.0695 0.0084 0.0013 248 THR A CG2 1029 N N . HIS A 133 ? 0.4592 0.4729 0.4067 -0.1034 0.0228 0.0062 249 HIS A N 1030 C CA . HIS A 133 ? 0.4811 0.5021 0.4286 -0.1097 0.0305 0.0078 249 HIS A CA 1031 C C . HIS A 133 ? 0.4283 0.4304 0.3675 -0.1003 0.0295 0.0130 249 HIS A C 1032 O O . HIS A 133 ? 0.4266 0.4177 0.3659 -0.0885 0.0242 0.0141 249 HIS A O 1033 C CB . HIS A 133 ? 0.4178 0.4738 0.3862 -0.1047 0.0367 0.0026 249 HIS A CB 1034 C CG . HIS A 133 ? 0.4197 0.4819 0.3976 -0.0855 0.0349 0.0032 249 HIS A CG 1035 N ND1 . HIS A 133 ? 0.3952 0.4588 0.3765 -0.0761 0.0285 0.0024 249 HIS A ND1 1036 C CD2 . HIS A 133 ? 0.3761 0.4409 0.3577 -0.0755 0.0385 0.0046 249 HIS A CD2 1037 C CE1 . HIS A 133 ? 0.3714 0.4375 0.3571 -0.0621 0.0286 0.0041 249 HIS A CE1 1038 N NE2 . HIS A 133 ? 0.3874 0.4540 0.3743 -0.0613 0.0342 0.0054 249 HIS A NE2 1039 N N . GLY A 134 ? 0.4508 0.4497 0.3825 -0.1067 0.0346 0.0153 250 GLY A N 1040 C CA . GLY A 134 ? 0.4258 0.4068 0.3492 -0.0993 0.0323 0.0198 250 GLY A CA 1041 C C . GLY A 134 ? 0.4033 0.4009 0.3422 -0.0840 0.0356 0.0183 250 GLY A C 1042 O O . GLY A 134 ? 0.4280 0.4460 0.3763 -0.0834 0.0427 0.0149 250 GLY A O 1043 N N . ILE A 135 ? 0.3581 0.3467 0.2999 -0.0721 0.0306 0.0200 251 ILE A N 1044 C CA . ILE A 135 ? 0.3487 0.3486 0.3020 -0.0593 0.0330 0.0195 251 ILE A CA 1045 C C . ILE A 135 ? 0.4250 0.4118 0.3734 -0.0560 0.0321 0.0226 251 ILE A C 1046 O O . ILE A 135 ? 0.3682 0.3379 0.3112 -0.0552 0.0260 0.0245 251 ILE A O 1047 C CB . ILE A 135 ? 0.3885 0.3896 0.3474 -0.0506 0.0296 0.0185 251 ILE A CB 1048 C CG1 . ILE A 135 ? 0.4267 0.4397 0.3888 -0.0542 0.0287 0.0151 251 ILE A CG1 1049 C CG2 . ILE A 135 ? 0.3522 0.3600 0.3182 -0.0398 0.0320 0.0195 251 ILE A CG2 1050 C CD1 . ILE A 135 ? 0.4582 0.4672 0.4193 -0.0487 0.0248 0.0134 251 ILE A CD1 1051 N N . LYS A 136 ? 0.3836 0.3783 0.3351 -0.0535 0.0371 0.0220 252 LYS A N 1052 C CA . LYS A 136 ? 0.3703 0.3533 0.3175 -0.0506 0.0356 0.0242 252 LYS A CA 1053 C C . LYS A 136 ? 0.3134 0.2972 0.2703 -0.0402 0.0338 0.0250 252 LYS A C 1054 O O . LYS A 136 ? 0.3753 0.3705 0.3398 -0.0345 0.0366 0.0241 252 LYS A O 1055 C CB . LYS A 136 ? 0.3549 0.3448 0.3009 -0.0515 0.0419 0.0220 252 LYS A CB 1056 C CG . LYS A 136 ? 0.4394 0.4276 0.3722 -0.0645 0.0458 0.0206 252 LYS A CG 1057 C CD . LYS A 136 ? 0.5088 0.5079 0.4431 -0.0635 0.0539 0.0155 252 LYS A CD 1058 C CE . LYS A 136 ? 0.6345 0.6222 0.5481 -0.0758 0.0570 0.0153 252 LYS A CE 1059 N NZ . LYS A 136 ? 0.6372 0.6355 0.5514 -0.0745 0.0660 0.0082 252 LYS A NZ 1060 N N . PRO A 137 ? 0.3621 0.3339 0.3185 -0.0384 0.0288 0.0265 253 PRO A N 1061 C CA . PRO A 137 ? 0.3315 0.3071 0.2979 -0.0311 0.0293 0.0262 253 PRO A CA 1062 C C . PRO A 137 ? 0.4099 0.3863 0.3787 -0.0284 0.0322 0.0273 253 PRO A C 1063 O O . PRO A 137 ? 0.3942 0.3651 0.3663 -0.0278 0.0296 0.0275 253 PRO A O 1064 C CB . PRO A 137 ? 0.3770 0.3429 0.3459 -0.0303 0.0226 0.0252 253 PRO A CB 1065 C CG . PRO A 137 ? 0.4111 0.3630 0.3684 -0.0361 0.0170 0.0272 253 PRO A CG 1066 C CD . PRO A 137 ? 0.3881 0.3430 0.3353 -0.0430 0.0216 0.0280 253 PRO A CD 1067 N N . VAL A 138 ? 0.3877 0.3708 0.3559 -0.0266 0.0365 0.0272 254 VAL A N 1068 C CA . VAL A 138 ? 0.3750 0.3549 0.3432 -0.0239 0.0383 0.0276 254 VAL A CA 1069 C C . VAL A 138 ? 0.3748 0.3541 0.3470 -0.0203 0.0392 0.0298 254 VAL A C 1070 O O . VAL A 138 ? 0.3898 0.3741 0.3619 -0.0172 0.0404 0.0307 254 VAL A O 1071 C CB . VAL A 138 ? 0.3918 0.3782 0.3591 -0.0215 0.0416 0.0250 254 VAL A CB 1072 C CG1 . VAL A 138 ? 0.4480 0.4264 0.4133 -0.0184 0.0424 0.0242 254 VAL A CG1 1073 C CG2 . VAL A 138 ? 0.4023 0.3933 0.3651 -0.0281 0.0434 0.0220 254 VAL A CG2 1074 N N . VAL A 139 ? 0.3859 0.3675 0.3801 0.0026 0.0126 0.0013 255 VAL A N 1075 C CA . VAL A 139 ? 0.3854 0.3710 0.3870 0.0111 0.0164 -0.0016 255 VAL A CA 1076 C C . VAL A 139 ? 0.3663 0.3618 0.3740 0.0101 0.0227 -0.0032 255 VAL A C 1077 O O . VAL A 139 ? 0.3630 0.3627 0.3717 0.0069 0.0239 -0.0038 255 VAL A O 1078 C CB . VAL A 139 ? 0.3769 0.3614 0.3815 0.0164 0.0137 -0.0022 255 VAL A CB 1079 C CG1 . VAL A 139 ? 0.3722 0.3651 0.3846 0.0222 0.0197 -0.0047 255 VAL A CG1 1080 C CG2 . VAL A 139 ? 0.3821 0.3530 0.3801 0.0201 0.0050 -0.0021 255 VAL A CG2 1081 N N . SER A 140 ? 0.3506 0.3472 0.3604 0.0134 0.0253 -0.0044 256 SER A N 1082 C CA . SER A 140 ? 0.3242 0.3247 0.3384 0.0143 0.0287 -0.0060 256 SER A CA 1083 C C . SER A 140 ? 0.3776 0.3735 0.3901 0.0187 0.0294 -0.0050 256 SER A C 1084 O O . SER A 140 ? 0.3571 0.3494 0.3646 0.0210 0.0279 -0.0042 256 SER A O 1085 C CB . SER A 140 ? 0.3735 0.3813 0.3906 0.0122 0.0290 -0.0090 256 SER A CB 1086 O OG . SER A 140 ? 0.4385 0.4474 0.4558 0.0128 0.0265 -0.0089 256 SER A OG 1087 N N . THR A 141 ? 0.4096 0.4030 0.4236 0.0195 0.0307 -0.0051 257 THR A N 1088 C CA . THR A 141 ? 0.3774 0.3629 0.3859 0.0223 0.0298 -0.0027 257 THR A CA 1089 C C . THR A 141 ? 0.3680 0.3507 0.3791 0.0260 0.0257 -0.0052 257 THR A C 1090 O O . THR A 141 ? 0.4140 0.4026 0.4321 0.0263 0.0258 -0.0099 257 THR A O 1091 C CB . THR A 141 ? 0.3864 0.3673 0.3922 0.0192 0.0330 0.0010 257 THR A CB 1092 O OG1 . THR A 141 ? 0.3686 0.3471 0.3793 0.0167 0.0323 -0.0007 257 THR A OG1 1093 C CG2 . THR A 141 ? 0.4189 0.4082 0.4264 0.0175 0.0372 0.0015 257 THR A CG2 1094 N N . GLN A 142 ? 0.3629 0.3373 0.3675 0.0296 0.0216 -0.0029 258 GLN A N 1095 C CA . GLN A 142 ? 0.3634 0.3337 0.3712 0.0358 0.0150 -0.0057 258 GLN A CA 1096 C C . GLN A 142 ? 0.4046 0.3911 0.4245 0.0389 0.0127 -0.0120 258 GLN A C 1097 O O . GLN A 142 ? 0.4208 0.4085 0.4421 0.0434 0.0063 -0.0129 258 GLN A O 1098 C CB . GLN A 142 ? 0.3848 0.3463 0.3947 0.0370 0.0140 -0.0076 258 GLN A CB 1099 C CG . GLN A 142 ? 0.4423 0.3876 0.4408 0.0312 0.0152 -0.0002 258 GLN A CG 1100 C CD . GLN A 142 ? 0.4775 0.4049 0.4741 0.0329 0.0095 -0.0011 258 GLN A CD 1101 O OE1 . GLN A 142 ? 0.4754 0.4030 0.4798 0.0411 0.0045 -0.0089 258 GLN A OE1 1102 N NE2 . GLN A 142 ? 0.4589 0.3711 0.4452 0.0249 0.0100 0.0063 258 GLN A NE2 1103 N N . LEU A 143 ? 0.3646 0.3645 0.3929 0.0355 0.0177 -0.0164 259 LEU A N 1104 C CA . LEU A 143 ? 0.3794 0.3989 0.4193 0.0349 0.0179 -0.0220 259 LEU A CA 1105 C C . LEU A 143 ? 0.3991 0.4247 0.4360 0.0257 0.0212 -0.0190 259 LEU A C 1106 O O . LEU A 143 ? 0.4024 0.4229 0.4330 0.0211 0.0249 -0.0162 259 LEU A O 1107 C CB . LEU A 143 ? 0.3710 0.4024 0.4203 0.0372 0.0213 -0.0301 259 LEU A CB 1108 C CG . LEU A 143 ? 0.3852 0.4065 0.4370 0.0475 0.0166 -0.0349 259 LEU A CG 1109 C CD1 . LEU A 143 ? 0.3916 0.4250 0.4504 0.0498 0.0211 -0.0450 259 LEU A CD1 1110 C CD2 . LEU A 143 ? 0.4136 0.4367 0.4728 0.0568 0.0078 -0.0372 259 LEU A CD2 1111 N N . LEU A 144 ? 0.3267 0.3619 0.3681 0.0228 0.0182 -0.0196 260 LEU A N 1112 C CA . LEU A 144 ? 0.3415 0.3791 0.3790 0.0128 0.0191 -0.0166 260 LEU A CA 1113 C C . LEU A 144 ? 0.3952 0.4530 0.4409 0.0054 0.0243 -0.0200 260 LEU A C 1114 O O . LEU A 144 ? 0.3578 0.4355 0.4174 0.0072 0.0251 -0.0260 260 LEU A O 1115 C CB . LEU A 144 ? 0.3223 0.3578 0.3587 0.0109 0.0121 -0.0153 260 LEU A CB 1116 C CG . LEU A 144 ? 0.3701 0.3875 0.3952 0.0181 0.0073 -0.0129 260 LEU A CG 1117 C CD1 . LEU A 144 ? 0.3677 0.3833 0.3906 0.0162 -0.0010 -0.0133 260 LEU A CD1 1118 C CD2 . LEU A 144 ? 0.4401 0.4428 0.4528 0.0181 0.0107 -0.0095 260 LEU A CD2 1119 N N . LEU A 145 ? 0.3856 0.4393 0.4223 -0.0027 0.0276 -0.0165 261 LEU A N 1120 C CA . LEU A 145 ? 0.3843 0.4552 0.4228 -0.0110 0.0340 -0.0188 261 LEU A CA 1121 C C . LEU A 145 ? 0.3711 0.4428 0.4022 -0.0260 0.0330 -0.0129 261 LEU A C 1122 O O . LEU A 145 ? 0.3850 0.4359 0.4045 -0.0290 0.0269 -0.0064 261 LEU A O 1123 C CB . LEU A 145 ? 0.3509 0.4140 0.3808 -0.0095 0.0374 -0.0190 261 LEU A CB 1124 C CG . LEU A 145 ? 0.3683 0.4248 0.4020 0.0025 0.0373 -0.0235 261 LEU A CG 1125 C CD1 . LEU A 145 ? 0.3475 0.3975 0.3726 0.0010 0.0395 -0.0238 261 LEU A CD1 1126 C CD2 . LEU A 145 ? 0.3547 0.4274 0.4023 0.0100 0.0389 -0.0326 261 LEU A CD2 1127 N N . ASN A 146 ? 0.3417 0.4376 0.3790 -0.0357 0.0388 -0.0156 262 ASN A N 1128 C CA . ASN A 146 ? 0.3733 0.4711 0.4011 -0.0541 0.0390 -0.0087 262 ASN A CA 1129 C C . ASN A 146 ? 0.3966 0.4799 0.4223 -0.0598 0.0295 -0.0030 262 ASN A C 1130 O O . ASN A 146 ? 0.3986 0.4643 0.4088 -0.0721 0.0245 0.0053 262 ASN A O 1131 C CB . ASN A 146 ? 0.3696 0.4485 0.3760 -0.0601 0.0387 -0.0020 262 ASN A CB 1132 C CG . ASN A 146 ? 0.4298 0.5247 0.4337 -0.0597 0.0482 -0.0075 262 ASN A CG 1133 O OD1 . ASN A 146 ? 0.3778 0.5007 0.3959 -0.0569 0.0563 -0.0168 262 ASN A OD1 1134 N ND2 . ASN A 146 ? 0.3994 0.4766 0.3854 -0.0614 0.0460 -0.0029 262 ASN A ND2 1135 N N . GLY A 147 ? 0.3710 0.4589 0.4102 -0.0506 0.0254 -0.0076 263 GLY A N 1136 C CA . GLY A 147 ? 0.3733 0.4464 0.4094 -0.0545 0.0153 -0.0041 263 GLY A CA 1137 C C . GLY A 147 ? 0.4133 0.5114 0.4636 -0.0679 0.0148 -0.0053 263 GLY A C 1138 O O . GLY A 147 ? 0.3855 0.5141 0.4471 -0.0756 0.0239 -0.0084 263 GLY A O 1139 N N . SER A 148 ? 0.3875 0.4745 0.4374 -0.0710 0.0044 -0.0039 264 SER A N 1140 C CA . SER A 148 ? 0.3933 0.5051 0.4596 -0.0839 0.0016 -0.0057 264 SER A CA 1141 C C . SER A 148 ? 0.3850 0.5199 0.4736 -0.0689 0.0004 -0.0151 264 SER A C 1142 O O . SER A 148 ? 0.4300 0.5484 0.5138 -0.0512 -0.0032 -0.0174 264 SER A O 1143 C CB . SER A 148 ? 0.4527 0.5383 0.5067 -0.0947 -0.0116 -0.0003 264 SER A CB 1144 O OG . SER A 148 ? 0.5012 0.5562 0.5314 -0.1036 -0.0136 0.0081 264 SER A OG 1145 N N . LEU A 149 ? 0.3345 0.5083 0.4473 -0.0766 0.0030 -0.0202 265 LEU A N 1146 C CA . LEU A 149 ? 0.4051 0.6035 0.5421 -0.0618 -0.0007 -0.0299 265 LEU A CA 1147 C C . LEU A 149 ? 0.4429 0.6402 0.5864 -0.0666 -0.0150 -0.0300 265 LEU A C 1148 O O . LEU A 149 ? 0.3854 0.5784 0.5239 -0.0865 -0.0192 -0.0245 265 LEU A O 1149 C CB . LEU A 149 ? 0.3786 0.6267 0.5430 -0.0646 0.0103 -0.0385 265 LEU A CB 1150 C CG . LEU A 149 ? 0.3998 0.6533 0.5591 -0.0586 0.0243 -0.0414 265 LEU A CG 1151 C CD1 . LEU A 149 ? 0.4278 0.7319 0.6093 -0.0680 0.0372 -0.0492 265 LEU A CD1 1152 C CD2 . LEU A 149 ? 0.3620 0.6018 0.5219 -0.0328 0.0212 -0.0476 265 LEU A CD2 1153 N N . ALA A 150 ? 0.3902 0.5892 0.5431 -0.0490 -0.0239 -0.0360 266 ALA A N 1154 C CA . ALA A 150 ? 0.3597 0.5644 0.5227 -0.0515 -0.0387 -0.0382 266 ALA A CA 1155 C C . ALA A 150 ? 0.4039 0.6585 0.5995 -0.0661 -0.0356 -0.0433 266 ALA A C 1156 O O . ALA A 150 ? 0.3602 0.6502 0.5767 -0.0620 -0.0242 -0.0499 266 ALA A O 1157 C CB . ALA A 150 ? 0.3830 0.5820 0.5491 -0.0288 -0.0485 -0.0435 266 ALA A CB 1158 N N . GLU A 151 ? 0.4645 0.7233 0.6646 -0.0837 -0.0455 -0.0410 267 GLU A N 1159 C CA . GLU A 151 ? 0.5080 0.8153 0.7378 -0.1039 -0.0409 -0.0439 267 GLU A CA 1160 C C . GLU A 151 ? 0.4902 0.8429 0.7586 -0.0933 -0.0482 -0.0558 267 GLU A C 1161 O O . GLU A 151 ? 0.5273 0.9323 0.8281 -0.1053 -0.0414 -0.0615 267 GLU A O 1162 C CB . GLU A 151 ? 0.5911 0.8820 0.8085 -0.1316 -0.0486 -0.0352 267 GLU A CB 1163 C CG . GLU A 151 ? 0.7086 0.9561 0.8899 -0.1421 -0.0430 -0.0239 267 GLU A CG 1164 C CD . GLU A 151 ? 0.8442 1.0737 1.0130 -0.1708 -0.0516 -0.0151 267 GLU A CD 1165 O OE1 . GLU A 151 ? 0.8634 1.1197 1.0540 -0.1861 -0.0597 -0.0176 267 GLU A OE1 1166 O OE2 . GLU A 151 ? 0.9311 1.1184 1.0685 -0.1779 -0.0517 -0.0060 267 GLU A OE2 1167 N N . GLU A 152 ? 0.4218 0.7560 0.6869 -0.0707 -0.0621 -0.0596 268 GLU A N 1168 C CA . GLU A 152 ? 0.3477 0.7196 0.6476 -0.0574 -0.0731 -0.0708 268 GLU A CA 1169 C C . GLU A 152 ? 0.3641 0.7226 0.6609 -0.0263 -0.0764 -0.0761 268 GLU A C 1170 O O . GLU A 152 ? 0.3747 0.7517 0.6830 -0.0154 -0.0638 -0.0820 268 GLU A O 1171 C CB . GLU A 152 ? 0.4112 0.7761 0.7123 -0.0656 -0.0942 -0.0698 268 GLU A CB 1172 C CG . GLU A 152 ? 0.5013 0.9199 0.8474 -0.0619 -0.1051 -0.0812 268 GLU A CG 1173 C CD . GLU A 152 ? 0.6211 1.0345 0.9684 -0.0752 -0.1261 -0.0798 268 GLU A CD 1174 O OE1 . GLU A 152 ? 0.6266 1.0361 0.9786 -0.0581 -0.1455 -0.0848 268 GLU A OE1 1175 O OE2 . GLU A 152 ? 0.6477 1.0583 0.9891 -0.1033 -0.1246 -0.0736 268 GLU A OE2 1176 N N . GLU A 153 ? 0.4033 0.7275 0.6818 -0.0130 -0.0937 -0.0738 269 GLU A N 1177 C CA . GLU A 153 ? 0.4589 0.7619 0.7278 0.0137 -0.0988 -0.0760 269 GLU A CA 1178 C C . GLU A 153 ? 0.4096 0.6673 0.6410 0.0177 -0.0875 -0.0674 269 GLU A C 1179 O O . GLU A 153 ? 0.3941 0.6266 0.6007 0.0031 -0.0815 -0.0591 269 GLU A O 1180 C CB . GLU A 153 ? 0.5227 0.8062 0.7830 0.0248 -0.1224 -0.0757 269 GLU A CB 1181 C CG . GLU A 153 ? 0.6837 1.0122 0.9846 0.0293 -0.1376 -0.0862 269 GLU A CG 1182 C CD . GLU A 153 ? 0.8690 1.1729 1.1559 0.0409 -0.1628 -0.0849 269 GLU A CD 1183 O OE1 . GLU A 153 ? 0.9674 1.2219 1.2116 0.0393 -0.1666 -0.0755 269 GLU A OE1 1184 O OE2 . GLU A 153 ? 0.8933 1.2282 1.2113 0.0519 -0.1790 -0.0937 269 GLU A OE2 1185 N N . ILE A 154 ? 0.3851 0.6326 0.6136 0.0377 -0.0861 -0.0700 270 ILE A N 1186 C CA . ILE A 154 ? 0.4134 0.6156 0.6061 0.0432 -0.0802 -0.0616 270 ILE A CA 1187 C C . ILE A 154 ? 0.4348 0.5987 0.5963 0.0419 -0.0926 -0.0536 270 ILE A C 1188 O O . ILE A 154 ? 0.4446 0.6075 0.6084 0.0493 -0.1100 -0.0555 270 ILE A O 1189 C CB . ILE A 154 ? 0.4162 0.6106 0.6107 0.0645 -0.0815 -0.0655 270 ILE A CB 1190 C CG1 . ILE A 154 ? 0.3545 0.5806 0.5724 0.0660 -0.0663 -0.0742 270 ILE A CG1 1191 C CG2 . ILE A 154 ? 0.4011 0.5470 0.5575 0.0686 -0.0795 -0.0555 270 ILE A CG2 1192 C CD1 . ILE A 154 ? 0.3617 0.5847 0.5877 0.0886 -0.0704 -0.0818 270 ILE A CD1 1193 N N . ILE A 155 ? 0.4128 0.5468 0.5452 0.0331 -0.0843 -0.0458 271 ILE A N 1194 C CA . ILE A 155 ? 0.4125 0.5125 0.5139 0.0321 -0.0937 -0.0403 271 ILE A CA 1195 C C . ILE A 155 ? 0.4225 0.4875 0.4934 0.0416 -0.0888 -0.0340 271 ILE A C 1196 O O . ILE A 155 ? 0.4459 0.5047 0.5113 0.0401 -0.0744 -0.0313 271 ILE A O 1197 C CB . ILE A 155 ? 0.4392 0.5311 0.5298 0.0145 -0.0907 -0.0377 271 ILE A CB 1198 C CG1 . ILE A 155 ? 0.4159 0.5430 0.5363 0.0000 -0.0934 -0.0421 271 ILE A CG1 1199 C CG2 . ILE A 155 ? 0.4418 0.5004 0.5008 0.0155 -0.1019 -0.0352 271 ILE A CG2 1200 C CD1 . ILE A 155 ? 0.4326 0.5780 0.5703 0.0029 -0.1114 -0.0475 271 ILE A CD1 1201 N N . ILE A 156 ? 0.4336 0.4769 0.4841 0.0500 -0.1013 -0.0314 272 ILE A N 1202 C CA . ILE A 156 ? 0.4643 0.4749 0.4823 0.0554 -0.0968 -0.0244 272 ILE A CA 1203 C C . ILE A 156 ? 0.4855 0.4753 0.4754 0.0479 -0.0956 -0.0221 272 ILE A C 1204 O O . ILE A 156 ? 0.4917 0.4782 0.4744 0.0455 -0.1084 -0.0244 272 ILE A O 1205 C CB . ILE A 156 ? 0.5254 0.5212 0.5317 0.0680 -0.1114 -0.0218 272 ILE A CB 1206 C CG1 . ILE A 156 ? 0.4908 0.5065 0.5271 0.0787 -0.1158 -0.0266 272 ILE A CG1 1207 C CG2 . ILE A 156 ? 0.5511 0.5140 0.5215 0.0699 -0.1056 -0.0131 272 ILE A CG2 1208 C CD1 . ILE A 156 ? 0.4244 0.4482 0.4735 0.0786 -0.0992 -0.0279 272 ILE A CD1 1209 N N . ARG A 157 ? 0.4083 0.3851 0.3833 0.0450 -0.0812 -0.0188 273 ARG A N 1210 C CA . ARG A 157 ? 0.4353 0.3945 0.3863 0.0401 -0.0785 -0.0190 273 ARG A CA 1211 C C . ARG A 157 ? 0.5045 0.4432 0.4271 0.0451 -0.0707 -0.0142 273 ARG A C 1212 O O . ARG A 157 ? 0.5128 0.4523 0.4387 0.0470 -0.0602 -0.0102 273 ARG A O 1213 C CB . ARG A 157 ? 0.4540 0.4196 0.4157 0.0314 -0.0684 -0.0208 273 ARG A CB 1214 C CG . ARG A 157 ? 0.4023 0.3916 0.3929 0.0228 -0.0714 -0.0237 273 ARG A CG 1215 C CD . ARG A 157 ? 0.4419 0.4295 0.4345 0.0123 -0.0635 -0.0234 273 ARG A CD 1216 N NE . ARG A 157 ? 0.4021 0.4141 0.4202 0.0010 -0.0643 -0.0245 273 ARG A NE 1217 C CZ . ARG A 157 ? 0.4207 0.4410 0.4473 -0.0083 -0.0757 -0.0272 273 ARG A CZ 1218 N NH1 . ARG A 157 ? 0.4166 0.4197 0.4267 -0.0062 -0.0885 -0.0295 273 ARG A NH1 1219 N NH2 . ARG A 157 ? 0.4156 0.4626 0.4666 -0.0207 -0.0742 -0.0278 273 ARG A NH2 1220 N N . SER A 158 ? 0.5553 0.4769 0.4494 0.0461 -0.0756 -0.0151 274 SER A N 1221 C CA . SER A 158 ? 0.5509 0.4570 0.4164 0.0488 -0.0664 -0.0111 274 SER A CA 1222 C C . SER A 158 ? 0.5432 0.4355 0.3806 0.0488 -0.0697 -0.0164 274 SER A C 1223 O O . SER A 158 ? 0.5713 0.4593 0.4034 0.0484 -0.0844 -0.0203 274 SER A O 1224 C CB . SER A 158 ? 0.5464 0.4438 0.3999 0.0530 -0.0715 -0.0033 274 SER A CB 1225 O OG . SER A 158 ? 0.5683 0.4503 0.3882 0.0524 -0.0641 0.0011 274 SER A OG 1226 N N . GLU A 159 ? 0.5841 0.4710 0.4045 0.0497 -0.0563 -0.0178 275 GLU A N 1227 C CA . GLU A 159 ? 0.5873 0.4612 0.3773 0.0520 -0.0578 -0.0245 275 GLU A CA 1228 C C . GLU A 159 ? 0.5864 0.4474 0.3459 0.0533 -0.0677 -0.0209 275 GLU A C 1229 O O . GLU A 159 ? 0.6695 0.5187 0.4046 0.0548 -0.0760 -0.0276 275 GLU A O 1230 C CB . GLU A 159 ? 0.6280 0.5042 0.4081 0.0543 -0.0399 -0.0274 275 GLU A CB 1231 C CG . GLU A 159 ? 0.7001 0.5658 0.4504 0.0589 -0.0394 -0.0377 275 GLU A CG 1232 C CD . GLU A 159 ? 0.7802 0.6544 0.5307 0.0632 -0.0223 -0.0438 275 GLU A CD 1233 O OE1 . GLU A 159 ? 0.7448 0.6328 0.5146 0.0612 -0.0107 -0.0377 275 GLU A OE1 1234 O OE2 . GLU A 159 ? 0.8874 0.7550 0.6200 0.0695 -0.0215 -0.0558 275 GLU A OE2 1235 N N . ASN A 160 ? 0.6207 0.4810 0.3791 0.0529 -0.0683 -0.0104 276 ASN A N 1236 C CA . ASN A 160 ? 0.6980 0.5425 0.4247 0.0537 -0.0789 -0.0044 276 ASN A CA 1237 C C . ASN A 160 ? 0.6741 0.5161 0.4090 0.0537 -0.0818 0.0074 276 ASN A C 1238 O O . ASN A 160 ? 0.6626 0.5011 0.3869 0.0503 -0.0691 0.0150 276 ASN A O 1239 C CB . ASN A 160 ? 0.7406 0.5758 0.4267 0.0524 -0.0671 -0.0053 276 ASN A CB 1240 C CG . ASN A 160 ? 0.8056 0.6220 0.4515 0.0509 -0.0766 0.0031 276 ASN A CG 1241 O OD1 . ASN A 160 ? 0.7276 0.5349 0.3752 0.0526 -0.0952 0.0091 276 ASN A OD1 1242 N ND2 . ASN A 160 ? 0.9721 0.7834 0.5806 0.0479 -0.0639 0.0033 276 ASN A ND2 1243 N N . LEU A 161 ? 0.6673 0.5116 0.4221 0.0575 -0.0992 0.0080 277 LEU A N 1244 C CA . LEU A 161 ? 0.7358 0.5773 0.5034 0.0606 -0.1048 0.0164 277 LEU A CA 1245 C C . LEU A 161 ? 0.7718 0.5882 0.5008 0.0590 -0.1073 0.0284 277 LEU A C 1246 O O . LEU A 161 ? 0.7511 0.5598 0.4834 0.0587 -0.1053 0.0368 277 LEU A O 1247 C CB . LEU A 161 ? 0.7437 0.5933 0.5362 0.0673 -0.1257 0.0127 277 LEU A CB 1248 C CG . LEU A 161 ? 0.7240 0.6013 0.5635 0.0682 -0.1224 0.0050 277 LEU A CG 1249 C CD1 . LEU A 161 ? 0.7674 0.6567 0.6308 0.0751 -0.1430 0.0010 277 LEU A CD1 1250 C CD2 . LEU A 161 ? 0.5966 0.4790 0.4527 0.0680 -0.1072 0.0084 277 LEU A CD2 1251 N N . THR A 162 ? 0.7898 0.5918 0.4800 0.0570 -0.1125 0.0293 278 THR A N 1252 C CA . THR A 162 ? 0.8217 0.5978 0.4680 0.0533 -0.1165 0.0419 278 THR A CA 1253 C C . THR A 162 ? 0.8038 0.5797 0.4348 0.0437 -0.0929 0.0485 278 THR A C 1254 O O . THR A 162 ? 0.7811 0.5375 0.3865 0.0377 -0.0931 0.0620 278 THR A O 1255 C CB . THR A 162 ? 0.8588 0.6219 0.4651 0.0530 -0.1272 0.0394 278 THR A CB 1256 O OG1 . THR A 162 ? 0.8957 0.6625 0.5205 0.0607 -0.1500 0.0325 278 THR A OG1 1257 C CG2 . THR A 162 ? 0.8639 0.5979 0.4200 0.0477 -0.1332 0.0542 278 THR A CG2 1258 N N . ASN A 163 ? 0.7807 0.5779 0.4279 0.0419 -0.0737 0.0391 279 ASN A N 1259 C CA . ASN A 163 ? 0.7832 0.5886 0.4245 0.0336 -0.0505 0.0426 279 ASN A CA 1260 C C . ASN A 163 ? 0.6975 0.5120 0.3753 0.0326 -0.0442 0.0459 279 ASN A C 1261 O O . ASN A 163 ? 0.6646 0.4968 0.3788 0.0373 -0.0414 0.0370 279 ASN A O 1262 C CB . ASN A 163 ? 0.7791 0.6028 0.4203 0.0347 -0.0353 0.0292 279 ASN A CB 1263 C CG . ASN A 163 ? 0.8209 0.6589 0.4585 0.0274 -0.0113 0.0308 279 ASN A CG 1264 O OD1 . ASN A 163 ? 0.7981 0.6343 0.4389 0.0196 -0.0051 0.0421 279 ASN A OD1 1265 N ND2 . ASN A 163 ? 0.7489 0.6018 0.3808 0.0300 0.0016 0.0187 279 ASN A ND2 1266 N N . ASN A 164 ? 0.7002 0.4998 0.3652 0.0254 -0.0432 0.0591 280 ASN A N 1267 C CA . ASN A 164 ? 0.6766 0.4794 0.3720 0.0246 -0.0404 0.0622 280 ASN A CA 1268 C C . ASN A 164 ? 0.6716 0.4998 0.3903 0.0204 -0.0191 0.0561 280 ASN A C 1269 O O . ASN A 164 ? 0.6613 0.4972 0.4104 0.0217 -0.0171 0.0544 280 ASN A O 1270 C CB . ASN A 164 ? 0.8071 0.5825 0.4786 0.0164 -0.0458 0.0782 280 ASN A CB 1271 C CG . ASN A 164 ? 0.8889 0.6602 0.5224 0.0015 -0.0311 0.0873 280 ASN A CG 1272 O OD1 . ASN A 164 ? 1.0159 0.7764 0.6124 -0.0007 -0.0351 0.0906 280 ASN A OD1 1273 N ND2 . ASN A 164 ? 0.8865 0.6692 0.5290 -0.0095 -0.0137 0.0909 280 ASN A ND2 1274 N N . ALA A 165 ? 0.7953 0.6369 0.4993 0.0163 -0.0040 0.0518 281 ALA A N 1275 C CA . ALA A 165 ? 0.7122 0.5796 0.4394 0.0144 0.0144 0.0446 281 ALA A CA 1276 C C . ALA A 165 ? 0.7320 0.6144 0.4912 0.0247 0.0120 0.0313 281 ALA A C 1277 O O . ALA A 165 ? 0.7491 0.6496 0.5319 0.0248 0.0229 0.0258 281 ALA A O 1278 C CB . ALA A 165 ? 0.7876 0.6675 0.4909 0.0086 0.0313 0.0425 281 ALA A CB 1279 N N . LYS A 166 ? 0.6334 0.5077 0.3928 0.0321 -0.0034 0.0268 282 LYS A N 1280 C CA . LYS A 166 ? 0.6243 0.5106 0.4105 0.0388 -0.0065 0.0156 282 LYS A CA 1281 C C . LYS A 166 ? 0.6648 0.5549 0.4826 0.0405 -0.0133 0.0168 282 LYS A C 1282 O O . LYS A 166 ? 0.6072 0.4869 0.4251 0.0424 -0.0258 0.0218 282 LYS A O 1283 C CB . LYS A 166 ? 0.5690 0.4477 0.3406 0.0436 -0.0190 0.0089 282 LYS A CB 1284 C CG . LYS A 166 ? 0.6993 0.5751 0.4385 0.0436 -0.0119 0.0043 282 LYS A CG 1285 C CD . LYS A 166 ? 0.7612 0.6529 0.5130 0.0464 0.0021 -0.0062 282 LYS A CD 1286 C CE . LYS A 166 ? 0.7984 0.6892 0.5197 0.0494 0.0085 -0.0148 282 LYS A CE 1287 N NZ . LYS A 166 ? 0.8299 0.7380 0.5644 0.0539 0.0230 -0.0249 282 LYS A NZ 1288 N N . THR A 167 ? 0.5396 0.4449 0.3832 0.0406 -0.0055 0.0116 283 THR A N 1289 C CA . THR A 167 ? 0.5469 0.4593 0.4192 0.0416 -0.0089 0.0112 283 THR A CA 1290 C C . THR A 167 ? 0.4530 0.3670 0.3363 0.0456 -0.0230 0.0069 283 THR A C 1291 O O . THR A 167 ? 0.5615 0.4748 0.4380 0.0466 -0.0284 0.0018 283 THR A O 1292 C CB . THR A 167 ? 0.6000 0.5272 0.4925 0.0401 0.0015 0.0063 283 THR A CB 1293 O OG1 . THR A 167 ? 0.6532 0.5837 0.5403 0.0363 0.0141 0.0096 283 THR A OG1 1294 C CG2 . THR A 167 ? 0.5620 0.4973 0.4806 0.0402 -0.0012 0.0055 283 THR A CG2 1295 N N . ILE A 168 ? 0.4712 0.3884 0.3724 0.0481 -0.0292 0.0080 284 ILE A N 1296 C CA . ILE A 168 ? 0.4998 0.4262 0.4183 0.0516 -0.0413 0.0031 284 ILE A CA 1297 C C . ILE A 168 ? 0.4618 0.4077 0.4091 0.0493 -0.0351 -0.0019 284 ILE A C 1298 O O . ILE A 168 ? 0.4797 0.4286 0.4368 0.0494 -0.0282 -0.0007 284 ILE A O 1299 C CB . ILE A 168 ? 0.4857 0.4050 0.4060 0.0583 -0.0540 0.0060 284 ILE A CB 1300 C CG1 . ILE A 168 ? 0.5015 0.3991 0.3898 0.0598 -0.0636 0.0121 284 ILE A CG1 1301 C CG2 . ILE A 168 ? 0.5076 0.4464 0.4557 0.0624 -0.0638 -0.0013 284 ILE A CG2 1302 C CD1 . ILE A 168 ? 0.5378 0.4185 0.4197 0.0660 -0.0756 0.0183 284 ILE A CD1 1303 N N . ILE A 169 ? 0.4087 0.3658 0.3665 0.0459 -0.0378 -0.0071 285 ILE A N 1304 C CA . ILE A 169 ? 0.3988 0.3750 0.3812 0.0416 -0.0331 -0.0109 285 ILE A CA 1305 C C . ILE A 169 ? 0.4287 0.4220 0.4316 0.0439 -0.0430 -0.0151 285 ILE A C 1306 O O . ILE A 169 ? 0.4413 0.4367 0.4436 0.0430 -0.0539 -0.0173 285 ILE A O 1307 C CB . ILE A 169 ? 0.4350 0.4120 0.4159 0.0338 -0.0308 -0.0131 285 ILE A CB 1308 C CG1 . ILE A 169 ? 0.4639 0.4269 0.4274 0.0341 -0.0224 -0.0112 285 ILE A CG1 1309 C CG2 . ILE A 169 ? 0.3649 0.3608 0.3678 0.0267 -0.0268 -0.0152 285 ILE A CG2 1310 C CD1 . ILE A 169 ? 0.4791 0.4362 0.4376 0.0294 -0.0237 -0.0143 285 ILE A CD1 1311 N N . VAL A 170 ? 0.4237 0.4306 0.4452 0.0474 -0.0397 -0.0175 286 VAL A N 1312 C CA . VAL A 170 ? 0.4238 0.4547 0.4706 0.0508 -0.0465 -0.0240 286 VAL A CA 1313 C C . VAL A 170 ? 0.4455 0.5008 0.5104 0.0399 -0.0385 -0.0277 286 VAL A C 1314 O O . VAL A 170 ? 0.4313 0.4907 0.4989 0.0365 -0.0271 -0.0276 286 VAL A O 1315 C CB . VAL A 170 ? 0.3616 0.3945 0.4186 0.0622 -0.0475 -0.0268 286 VAL A CB 1316 C CG1 . VAL A 170 ? 0.3715 0.4341 0.4583 0.0684 -0.0547 -0.0361 286 VAL A CG1 1317 C CG2 . VAL A 170 ? 0.3744 0.3774 0.4087 0.0701 -0.0556 -0.0205 286 VAL A CG2 1318 N N . HIS A 171 ? 0.4002 0.4708 0.4758 0.0329 -0.0452 -0.0303 287 HIS A N 1319 C CA . HIS A 171 ? 0.3967 0.4892 0.4868 0.0192 -0.0382 -0.0321 287 HIS A CA 1320 C C . HIS A 171 ? 0.3783 0.5091 0.5000 0.0209 -0.0376 -0.0402 287 HIS A C 1321 O O . HIS A 171 ? 0.3890 0.5374 0.5271 0.0229 -0.0484 -0.0447 287 HIS A O 1322 C CB . HIS A 171 ? 0.3227 0.4083 0.4050 0.0070 -0.0453 -0.0299 287 HIS A CB 1323 C CG . HIS A 171 ? 0.3833 0.4768 0.4686 -0.0100 -0.0381 -0.0277 287 HIS A CG 1324 N ND1 . HIS A 171 ? 0.4420 0.5289 0.5220 -0.0239 -0.0452 -0.0257 287 HIS A ND1 1325 C CD2 . HIS A 171 ? 0.3846 0.4891 0.4748 -0.0161 -0.0257 -0.0267 287 HIS A CD2 1326 C CE1 . HIS A 171 ? 0.4433 0.5351 0.5241 -0.0385 -0.0377 -0.0223 287 HIS A CE1 1327 N NE2 . HIS A 171 ? 0.3974 0.5010 0.4839 -0.0340 -0.0255 -0.0227 287 HIS A NE2 1328 N N . LEU A 172 ? 0.3353 0.4810 0.4661 0.0204 -0.0252 -0.0432 288 LEU A N 1329 C CA . LEU A 172 ? 0.3551 0.5398 0.5158 0.0247 -0.0221 -0.0534 288 LEU A CA 1330 C C . LEU A 172 ? 0.3941 0.6132 0.5737 0.0074 -0.0192 -0.0555 288 LEU A C 1331 O O . LEU A 172 ? 0.3840 0.5933 0.5500 -0.0100 -0.0153 -0.0481 288 LEU A O 1332 C CB . LEU A 172 ? 0.3858 0.5739 0.5461 0.0292 -0.0092 -0.0569 288 LEU A CB 1333 C CG . LEU A 172 ? 0.3524 0.5076 0.4954 0.0436 -0.0116 -0.0546 288 LEU A CG 1334 C CD1 . LEU A 172 ? 0.3078 0.4676 0.4513 0.0464 0.0001 -0.0595 288 LEU A CD1 1335 C CD2 . LEU A 172 ? 0.3412 0.4924 0.4925 0.0607 -0.0260 -0.0589 288 LEU A CD2 1336 N N . ASN A 173 ? 0.3521 0.6114 0.5633 0.0118 -0.0216 -0.0657 289 ASN A N 1337 C CA . ASN A 173 ? 0.3209 0.6210 0.5543 -0.0067 -0.0170 -0.0685 289 ASN A CA 1338 C C . ASN A 173 ? 0.3938 0.7319 0.6439 -0.0101 0.0003 -0.0764 289 ASN A C 1339 O O . ASN A 173 ? 0.3263 0.7014 0.5927 -0.0284 0.0082 -0.0780 289 ASN A O 1340 C CB . ASN A 173 ? 0.3520 0.6786 0.6123 -0.0041 -0.0316 -0.0747 289 ASN A CB 1341 C CG . ASN A 173 ? 0.4088 0.7584 0.6953 0.0204 -0.0379 -0.0877 289 ASN A CG 1342 O OD1 . ASN A 173 ? 0.3920 0.7331 0.6745 0.0363 -0.0322 -0.0921 289 ASN A OD1 1343 N ND2 . ASN A 173 ? 0.5583 0.9366 0.8725 0.0237 -0.0515 -0.0944 289 ASN A ND2 1344 N N . LYS A 174 ? 0.3707 0.6984 0.6144 0.0062 0.0062 -0.0811 290 LYS A N 1345 C CA . LYS A 174 ? 0.4173 0.7757 0.6710 0.0051 0.0227 -0.0898 290 LYS A CA 1346 C C . LYS A 174 ? 0.3795 0.7017 0.6045 0.0106 0.0293 -0.0856 290 LYS A C 1347 O O . LYS A 174 ? 0.3925 0.6824 0.6065 0.0277 0.0212 -0.0851 290 LYS A O 1348 C CB . LYS A 174 ? 0.4741 0.8736 0.7632 0.0245 0.0212 -0.1077 290 LYS A CB 1349 C CG . LYS A 174 ? 0.6176 1.0564 0.9194 0.0241 0.0393 -0.1201 290 LYS A CG 1350 C CD . LYS A 174 ? 0.6983 1.1795 1.0380 0.0465 0.0366 -0.1406 290 LYS A CD 1351 C CE . LYS A 174 ? 0.7935 1.3093 1.1414 0.0499 0.0553 -0.1552 290 LYS A CE 1352 N NZ . LYS A 174 ? 0.8480 1.4140 1.2376 0.0715 0.0540 -0.1779 290 LYS A NZ 1353 N N . SER A 175 ? 0.3242 0.6510 0.5358 -0.0056 0.0431 -0.0816 291 SER A N 1354 C CA . SER A 175 ? 0.3816 0.6780 0.5672 -0.0025 0.0489 -0.0781 291 SER A CA 1355 C C . SER A 175 ? 0.4192 0.7250 0.6144 0.0179 0.0523 -0.0925 291 SER A C 1356 O O . SER A 175 ? 0.3486 0.6958 0.5692 0.0243 0.0575 -0.1067 291 SER A O 1357 C CB . SER A 175 ? 0.4136 0.7167 0.5832 -0.0247 0.0616 -0.0715 291 SER A CB 1358 O OG . SER A 175 ? 0.5533 0.8342 0.7070 -0.0423 0.0561 -0.0569 291 SER A OG 1359 N N . VAL A 176 ? 0.3709 0.6386 0.5464 0.0283 0.0490 -0.0897 292 VAL A N 1360 C CA . VAL A 176 ? 0.4032 0.6727 0.5802 0.0435 0.0531 -0.1024 292 VAL A CA 1361 C C . VAL A 176 ? 0.3876 0.6345 0.5373 0.0345 0.0606 -0.0962 292 VAL A C 1362 O O . VAL A 176 ? 0.3603 0.5706 0.4900 0.0306 0.0552 -0.0838 292 VAL A O 1363 C CB . VAL A 176 ? 0.4289 0.6724 0.6092 0.0659 0.0392 -0.1065 292 VAL A CB 1364 C CG1 . VAL A 176 ? 0.4305 0.6743 0.6126 0.0816 0.0420 -0.1212 292 VAL A CG1 1365 C CG2 . VAL A 176 ? 0.4779 0.7403 0.6833 0.0755 0.0283 -0.1113 292 VAL A CG2 1366 N N . GLU A 177 ? 0.3911 0.6622 0.5402 0.0310 0.0730 -0.1056 293 GLU A N 1367 C CA . GLU A 177 ? 0.4274 0.6795 0.5501 0.0221 0.0790 -0.1007 293 GLU A CA 1368 C C . GLU A 177 ? 0.4091 0.6253 0.5209 0.0368 0.0714 -0.1030 293 GLU A C 1369 O O . GLU A 177 ? 0.4003 0.6154 0.5243 0.0553 0.0662 -0.1149 293 GLU A O 1370 C CB . GLU A 177 ? 0.4731 0.7601 0.5944 0.0149 0.0942 -0.1112 293 GLU A CB 1371 C CG . GLU A 177 ? 0.5121 0.8286 0.6343 -0.0079 0.1034 -0.1041 293 GLU A CG 1372 C CD . GLU A 177 ? 0.5615 0.9000 0.6677 -0.0213 0.1186 -0.1081 293 GLU A CD 1373 O OE1 . GLU A 177 ? 0.4899 0.8331 0.5920 -0.0092 0.1238 -0.1223 293 GLU A OE1 1374 O OE2 . GLU A 177 ? 0.6105 0.9589 0.7054 -0.0448 0.1245 -0.0968 293 GLU A OE2 1375 N N . ILE A 178 ? 0.3788 0.5650 0.4679 0.0281 0.0695 -0.0912 294 ILE A N 1376 C CA . ILE A 178 ? 0.3695 0.5253 0.4466 0.0368 0.0642 -0.0928 294 ILE A CA 1377 C C . ILE A 178 ? 0.4003 0.5536 0.4568 0.0251 0.0708 -0.0909 294 ILE A C 1378 O O . ILE A 178 ? 0.4143 0.5636 0.4582 0.0100 0.0723 -0.0786 294 ILE A O 1379 C CB . ILE A 178 ? 0.3704 0.4924 0.4426 0.0388 0.0533 -0.0803 294 ILE A CB 1380 C CG1 . ILE A 178 ? 0.3472 0.4401 0.4078 0.0443 0.0483 -0.0813 294 ILE A CG1 1381 C CG2 . ILE A 178 ? 0.3611 0.4767 0.4235 0.0237 0.0535 -0.0650 294 ILE A CG2 1382 C CD1 . ILE A 178 ? 0.4297 0.4936 0.4869 0.0464 0.0390 -0.0705 294 ILE A CD1 1383 N N . ASN A 179 ? 0.4316 0.5862 0.4834 0.0328 0.0736 -0.1042 295 ASN A N 1384 C CA . ASN A 179 ? 0.4211 0.5785 0.4524 0.0230 0.0803 -0.1061 295 ASN A CA 1385 C C . ASN A 179 ? 0.4436 0.5674 0.4608 0.0266 0.0720 -0.1052 295 ASN A C 1386 O O . ASN A 179 ? 0.4721 0.5867 0.4918 0.0396 0.0684 -0.1179 295 ASN A O 1387 C CB . ASN A 179 ? 0.4603 0.6511 0.4966 0.0286 0.0913 -0.1249 295 ASN A CB 1388 C CG . ASN A 179 ? 0.5621 0.7562 0.5731 0.0192 0.0986 -0.1291 295 ASN A CG 1389 O OD1 . ASN A 179 ? 0.4644 0.6361 0.4546 0.0077 0.0944 -0.1167 295 ASN A OD1 1390 N ND2 . ASN A 179 ? 0.7341 0.9583 0.7469 0.0248 0.1096 -0.1475 295 ASN A ND2 1391 N N . CYS A 180 ? 0.4234 0.5286 0.4272 0.0153 0.0676 -0.0907 296 CYS A N 1392 C CA . CYS A 180 ? 0.4414 0.5178 0.4361 0.0168 0.0589 -0.0884 296 CYS A CA 1393 C C . CYS A 180 ? 0.4442 0.5182 0.4175 0.0084 0.0599 -0.0902 296 CYS A C 1394 O O . CYS A 180 ? 0.4679 0.5512 0.4285 -0.0038 0.0639 -0.0830 296 CYS A O 1395 C CB . CYS A 180 ? 0.3529 0.4112 0.3513 0.0129 0.0517 -0.0728 296 CYS A CB 1396 S SG . CYS A 180 ? 0.4551 0.5150 0.4732 0.0216 0.0496 -0.0699 296 CYS A SG 1397 N N . THR A 181 ? 0.4208 0.4793 0.3881 0.0143 0.0549 -0.0997 297 THR A N 1398 C CA . THR A 181 ? 0.4395 0.4954 0.3850 0.0079 0.0547 -0.1045 297 THR A CA 1399 C C . THR A 181 ? 0.5028 0.5314 0.4437 0.0087 0.0429 -0.1050 297 THR A C 1400 O O . THR A 181 ? 0.4898 0.5033 0.4401 0.0181 0.0376 -0.1117 297 THR A O 1401 C CB . THR A 181 ? 0.5755 0.6502 0.5140 0.0143 0.0638 -0.1239 297 THR A CB 1402 O OG1 . THR A 181 ? 0.5442 0.6503 0.4895 0.0116 0.0759 -0.1241 297 THR A OG1 1403 C CG2 . THR A 181 ? 0.5996 0.6709 0.5106 0.0065 0.0635 -0.1286 297 THR A CG2 1404 N N . ARG A 182 ? 0.5074 0.5289 0.4340 -0.0019 0.0376 -0.0971 298 ARG A N 1405 C CA . ARG A 182 ? 0.5129 0.5146 0.4316 -0.0034 0.0270 -0.1009 298 ARG A CA 1406 C C . ARG A 182 ? 0.4881 0.4960 0.3820 -0.0060 0.0300 -0.1125 298 ARG A C 1407 O O . ARG A 182 ? 0.5416 0.5568 0.4184 -0.0160 0.0310 -0.1055 298 ARG A O 1408 C CB . ARG A 182 ? 0.4996 0.4933 0.4201 -0.0126 0.0180 -0.0859 298 ARG A CB 1409 C CG . ARG A 182 ? 0.5314 0.5070 0.4537 -0.0150 0.0060 -0.0878 298 ARG A CG 1410 C CD . ARG A 182 ? 0.5870 0.5558 0.4872 -0.0174 0.0009 -0.1000 298 ARG A CD 1411 N NE . ARG A 182 ? 0.6225 0.6003 0.5017 -0.0250 0.0008 -0.0959 298 ARG A NE 1412 C CZ . ARG A 182 ? 0.5566 0.5307 0.4320 -0.0327 -0.0100 -0.0863 298 ARG A CZ 1413 N NH1 . ARG A 182 ? 0.4754 0.4424 0.3701 -0.0343 -0.0195 -0.0807 298 ARG A NH1 1414 N NH2 . ARG A 182 ? 0.4911 0.4695 0.3435 -0.0393 -0.0116 -0.0821 298 ARG A NH2 1415 N N . PRO A 183 ? 0.5634 0.5669 0.4528 0.0032 0.0308 -0.1307 299 PRO A N 1416 C CA . PRO A 183 ? 0.6472 0.6606 0.5112 0.0020 0.0363 -0.1444 299 PRO A CA 1417 C C . PRO A 183 ? 0.7225 0.7230 0.5627 -0.0090 0.0262 -0.1411 299 PRO A C 1418 O O . PRO A 183 ? 0.6791 0.6600 0.5256 -0.0123 0.0129 -0.1347 299 PRO A O 1419 C CB . PRO A 183 ? 0.6570 0.6634 0.5247 0.0174 0.0363 -0.1661 299 PRO A CB 1420 C CG . PRO A 183 ? 0.6458 0.6258 0.5330 0.0219 0.0243 -0.1611 299 PRO A CG 1421 C CD . PRO A 183 ? 0.5739 0.5601 0.4784 0.0150 0.0254 -0.1398 299 PRO A CD 1422 N N . SER A 184 ? 0.7825 0.7958 0.5950 -0.0156 0.0324 -0.1453 300 SER A N 1423 C CA . SER A 184 ? 0.8799 0.8811 0.6652 -0.0259 0.0217 -0.1426 300 SER A CA 1424 C C . SER A 184 ? 0.9729 0.9510 0.7529 -0.0214 0.0088 -0.1564 300 SER A C 1425 O O . SER A 184 ? 0.9995 0.9619 0.7744 -0.0289 -0.0063 -0.1496 300 SER A O 1426 C CB . SER A 184 ? 0.8999 0.9183 0.6514 -0.0336 0.0321 -0.1467 300 SER A CB 1427 O OG . SER A 184 ? 0.9388 0.9435 0.6617 -0.0443 0.0197 -0.1413 300 SER A OG 1428 N N . ASN A 185 ? 1.0079 0.9837 0.7897 -0.0090 0.0134 -0.1764 301 ASN A N 1429 C CA . ASN A 185 ? 1.2095 1.1595 0.9833 -0.0047 0.0004 -0.1917 301 ASN A CA 1430 C C . ASN A 185 ? 1.2811 1.2236 1.0689 0.0124 0.0034 -0.2099 301 ASN A C 1431 O O . ASN A 185 ? 1.3297 1.2601 1.1012 0.0205 0.0002 -0.2314 301 ASN A O 1432 C CB . ASN A 185 ? 1.3139 1.2633 1.0486 -0.0101 -0.0017 -0.2033 301 ASN A CB 1433 C CG . ASN A 185 ? 1.3841 1.3035 1.1082 -0.0091 -0.0190 -0.2168 301 ASN A CG 1434 O OD1 . ASN A 185 ? 1.3935 1.2961 1.1243 -0.0184 -0.0352 -0.2059 301 ASN A OD1 1435 N ND2 . ASN A 185 ? 1.4149 1.3283 1.1229 0.0023 -0.0161 -0.2419 301 ASN A ND2 1436 N N . GLY A 192 ? 1.3397 1.1782 1.1683 -0.0226 -0.0674 -0.1821 324 GLY A N 1437 C CA . GLY A 192 ? 1.3171 1.1382 1.1697 -0.0252 -0.0731 -0.1739 324 GLY A CA 1438 C C . GLY A 192 ? 1.2488 1.0890 1.1264 -0.0343 -0.0695 -0.1512 324 GLY A C 1439 O O . GLY A 192 ? 1.2570 1.1090 1.1381 -0.0456 -0.0756 -0.1419 324 GLY A O 1440 N N . ASP A 193 ? 1.0918 0.9353 0.9864 -0.0281 -0.0605 -0.1432 325 ASP A N 1441 C CA . ASP A 193 ? 0.8757 0.7348 0.7934 -0.0354 -0.0566 -0.1235 325 ASP A CA 1442 C C . ASP A 193 ? 0.6964 0.5852 0.6155 -0.0316 -0.0445 -0.1152 325 ASP A C 1443 O O . ASP A 193 ? 0.6787 0.5757 0.5963 -0.0212 -0.0332 -0.1176 325 ASP A O 1444 C CB . ASP A 193 ? 0.8418 0.6865 0.7737 -0.0321 -0.0545 -0.1182 325 ASP A CB 1445 C CG . ASP A 193 ? 0.7808 0.6400 0.7343 -0.0411 -0.0510 -0.0992 325 ASP A CG 1446 O OD1 . ASP A 193 ? 0.6898 0.5736 0.6497 -0.0454 -0.0480 -0.0913 325 ASP A OD1 1447 O OD2 . ASP A 193 ? 0.8436 0.6888 0.8063 -0.0436 -0.0517 -0.0925 325 ASP A OD2 1448 N N . ILE A 194 ? 0.5870 0.4910 0.5093 -0.0402 -0.0483 -0.1058 326 ILE A N 1449 C CA . ILE A 194 ? 0.5432 0.4692 0.4632 -0.0378 -0.0400 -0.0976 326 ILE A CA 1450 C C . ILE A 194 ? 0.5425 0.4798 0.4821 -0.0340 -0.0302 -0.0856 326 ILE A C 1451 O O . ILE A 194 ? 0.5297 0.4811 0.4662 -0.0308 -0.0224 -0.0804 326 ILE A O 1452 C CB . ILE A 194 ? 0.5708 0.5067 0.4883 -0.0460 -0.0497 -0.0907 326 ILE A CB 1453 C CG1 . ILE A 194 ? 0.6235 0.5644 0.5677 -0.0534 -0.0572 -0.0811 326 ILE A CG1 1454 C CG2 . ILE A 194 ? 0.6461 0.5719 0.5384 -0.0496 -0.0597 -0.1024 326 ILE A CG2 1455 C CD1 . ILE A 194 ? 0.6011 0.5561 0.5491 -0.0582 -0.0674 -0.0742 326 ILE A CD1 1456 N N . ARG A 195 ? 0.5163 0.4459 0.4738 -0.0358 -0.0310 -0.0809 327 ARG A N 1457 C CA . ARG A 195 ? 0.5184 0.4571 0.4911 -0.0321 -0.0220 -0.0706 327 ARG A CA 1458 C C . ARG A 195 ? 0.4822 0.4105 0.4529 -0.0225 -0.0156 -0.0760 327 ARG A C 1459 O O . ARG A 195 ? 0.4820 0.4160 0.4623 -0.0184 -0.0088 -0.0689 327 ARG A O 1460 C CB . ARG A 195 ? 0.5133 0.4549 0.5060 -0.0405 -0.0253 -0.0603 327 ARG A CB 1461 C CG . ARG A 195 ? 0.4676 0.4274 0.4692 -0.0464 -0.0303 -0.0542 327 ARG A CG 1462 C CD . ARG A 195 ? 0.4529 0.4180 0.4751 -0.0568 -0.0347 -0.0483 327 ARG A CD 1463 N NE . ARG A 195 ? 0.4975 0.4776 0.5275 -0.0625 -0.0444 -0.0479 327 ARG A NE 1464 C CZ . ARG A 195 ? 0.5000 0.4721 0.5232 -0.0694 -0.0563 -0.0548 327 ARG A CZ 1465 N NH1 . ARG A 195 ? 0.5280 0.4758 0.5354 -0.0711 -0.0593 -0.0636 327 ARG A NH1 1466 N NH2 . ARG A 195 ? 0.4867 0.4744 0.5185 -0.0736 -0.0666 -0.0539 327 ARG A NH2 1467 N N . LYS A 196 ? 0.4899 0.4027 0.4482 -0.0177 -0.0189 -0.0898 328 LYS A N 1468 C CA . LYS A 196 ? 0.5224 0.4260 0.4805 -0.0058 -0.0148 -0.0970 328 LYS A CA 1469 C C . LYS A 196 ? 0.4828 0.4083 0.4371 0.0030 -0.0035 -0.1011 328 LYS A C 1470 O O . LYS A 196 ? 0.5121 0.4492 0.4529 0.0020 -0.0006 -0.1076 328 LYS A O 1471 C CB . LYS A 196 ? 0.5977 0.4759 0.5445 -0.0014 -0.0235 -0.1126 328 LYS A CB 1472 C CG . LYS A 196 ? 0.7141 0.5778 0.6635 0.0124 -0.0233 -0.1200 328 LYS A CG 1473 C CD . LYS A 196 ? 0.8619 0.6921 0.8004 0.0162 -0.0357 -0.1344 328 LYS A CD 1474 C CE . LYS A 196 ? 0.9872 0.7914 0.9280 0.0008 -0.0478 -0.1243 328 LYS A CE 1475 N NZ . LYS A 196 ? 1.0237 0.8111 0.9737 0.0000 -0.0503 -0.1121 328 LYS A NZ 1476 N N . ALA A 197 ? 0.4868 0.4188 0.4522 0.0098 0.0026 -0.0965 329 ALA A N 1477 C CA . ALA A 197 ? 0.5099 0.4649 0.4752 0.0162 0.0132 -0.0997 329 ALA A CA 1478 C C . ALA A 197 ? 0.5390 0.4920 0.5151 0.0288 0.0150 -0.1045 329 ALA A C 1479 O O . ALA A 197 ? 0.5130 0.4429 0.4932 0.0325 0.0071 -0.1044 329 ALA A O 1480 C CB . ALA A 197 ? 0.4757 0.4481 0.4449 0.0083 0.0181 -0.0852 329 ALA A CB 1481 N N . TYR A 198 ? 0.4735 0.4503 0.4539 0.0346 0.0243 -0.1084 330 TYR A N 1482 C CA . TYR A 198 ? 0.5288 0.5084 0.5221 0.0476 0.0249 -0.1136 330 TYR A CA 1483 C C . TYR A 198 ? 0.4576 0.4682 0.4597 0.0474 0.0350 -0.1106 330 TYR A C 1484 O O . TYR A 198 ? 0.4831 0.5130 0.4779 0.0385 0.0427 -0.1086 330 TYR A O 1485 C CB . TYR A 198 ? 0.6232 0.5961 0.6142 0.0618 0.0219 -0.1340 330 TYR A CB 1486 C CG . TYR A 198 ? 0.7079 0.7026 0.6880 0.0622 0.0307 -0.1482 330 TYR A CG 1487 C CD1 . TYR A 198 ? 0.7948 0.8243 0.7823 0.0676 0.0426 -0.1565 330 TYR A CD1 1488 C CD2 . TYR A 198 ? 0.7110 0.6931 0.6726 0.0559 0.0273 -0.1535 330 TYR A CD2 1489 C CE1 . TYR A 198 ? 0.7891 0.8412 0.7641 0.0660 0.0525 -0.1692 330 TYR A CE1 1490 C CE2 . TYR A 198 ? 0.7751 0.7768 0.7224 0.0554 0.0357 -0.1664 330 TYR A CE2 1491 C CZ . TYR A 198 ? 0.8371 0.8740 0.7902 0.0602 0.0491 -0.1740 330 TYR A CZ 1492 O OH . TYR A 198 ? 0.9120 0.9704 0.8483 0.0580 0.0591 -0.1866 330 TYR A OH 1493 N N . CYS A 199 ? 0.5071 0.5204 0.5237 0.0560 0.0336 -0.1093 331 CYS A N 1494 C CA . CYS A 199 ? 0.4929 0.5360 0.5207 0.0564 0.0416 -0.1084 331 CYS A CA 1495 C C . CYS A 199 ? 0.5455 0.6017 0.5873 0.0731 0.0415 -0.1246 331 CYS A C 1496 O O . CYS A 199 ? 0.5290 0.5640 0.5762 0.0855 0.0313 -0.1282 331 CYS A O 1497 C CB . CYS A 199 ? 0.4878 0.5256 0.5221 0.0518 0.0386 -0.0924 331 CYS A CB 1498 S SG . CYS A 199 ? 0.5268 0.5573 0.5494 0.0350 0.0395 -0.0756 331 CYS A SG 1499 N N . GLU A 200 ? 0.5099 0.6016 0.5575 0.0733 0.0525 -0.1342 332 GLU A N 1500 C CA . GLU A 200 ? 0.4795 0.5929 0.5450 0.0902 0.0538 -0.1518 332 GLU A CA 1501 C C . GLU A 200 ? 0.5067 0.6463 0.5922 0.0895 0.0562 -0.1463 332 GLU A C 1502 O O . GLU A 200 ? 0.4539 0.6131 0.5378 0.0739 0.0645 -0.1364 332 GLU A O 1503 C CB . GLU A 200 ? 0.4774 0.6183 0.5378 0.0917 0.0656 -0.1695 332 GLU A CB 1504 C CG . GLU A 200 ? 0.5277 0.6406 0.5687 0.0955 0.0607 -0.1785 332 GLU A CG 1505 C CD . GLU A 200 ? 0.6092 0.7488 0.6408 0.0970 0.0728 -0.1971 332 GLU A CD 1506 O OE1 . GLU A 200 ? 0.6531 0.8286 0.6836 0.0850 0.0869 -0.1949 332 GLU A OE1 1507 O OE2 . GLU A 200 ? 0.6033 0.7264 0.6266 0.1093 0.0678 -0.2138 332 GLU A OE2 1508 N N . ILE A 201 ? 0.4614 0.5975 0.5642 0.1060 0.0467 -0.1521 333 ILE A N 1509 C CA . ILE A 201 ? 0.4360 0.5989 0.5600 0.1071 0.0468 -0.1495 333 ILE A CA 1510 C C . ILE A 201 ? 0.4751 0.6649 0.6234 0.1280 0.0453 -0.1707 333 ILE A C 1511 O O . ILE A 201 ? 0.5157 0.6858 0.6641 0.1462 0.0365 -0.1833 333 ILE A O 1512 C CB . ILE A 201 ? 0.4946 0.6283 0.6174 0.1069 0.0338 -0.1334 333 ILE A CB 1513 C CG1 . ILE A 201 ? 0.4979 0.6058 0.5989 0.0891 0.0349 -0.1146 333 ILE A CG1 1514 C CG2 . ILE A 201 ? 0.4370 0.5992 0.5801 0.1065 0.0333 -0.1312 333 ILE A CG2 1515 C CD1 . ILE A 201 ? 0.5680 0.6352 0.6524 0.0914 0.0269 -0.1113 333 ILE A CD1 1516 N N . ASN A 202 ? 0.4590 0.6942 0.6290 0.1255 0.0531 -0.1750 334 ASN A N 1517 C CA . ASN A 202 ? 0.5139 0.7821 0.7132 0.1462 0.0512 -0.1957 334 ASN A CA 1518 C C . ASN A 202 ? 0.4449 0.6894 0.6565 0.1635 0.0309 -0.1935 334 ASN A C 1519 O O . ASN A 202 ? 0.4632 0.7124 0.6829 0.1567 0.0258 -0.1813 334 ASN A O 1520 C CB . ASN A 202 ? 0.6004 0.9280 0.8210 0.1349 0.0658 -0.1996 334 ASN A CB 1521 C CG . ASN A 202 ? 0.7051 1.0766 0.9608 0.1560 0.0657 -0.2228 334 ASN A CG 1522 O OD1 . ASN A 202 ? 0.5539 0.9105 0.8244 0.1784 0.0488 -0.2296 334 ASN A OD1 1523 N ND2 . ASN A 202 ? 0.9961 1.4232 1.2655 0.1491 0.0843 -0.2354 334 ASN A ND2 1524 N N . GLY A 203 ? 0.4994 0.7155 0.7096 0.1854 0.0181 -0.2052 335 GLY A N 1525 C CA . GLY A 203 ? 0.5328 0.7165 0.7476 0.2016 -0.0037 -0.2015 335 GLY A CA 1526 C C . GLY A 203 ? 0.5049 0.7241 0.7522 0.2135 -0.0107 -0.2081 335 GLY A C 1527 O O . GLY A 203 ? 0.4621 0.6606 0.7084 0.2142 -0.0253 -0.1950 335 GLY A O 1528 N N . THR A 204 ? 0.4672 0.7417 0.7437 0.2230 -0.0006 -0.2291 336 THR A N 1529 C CA . THR A 204 ? 0.4757 0.7937 0.7886 0.2333 -0.0061 -0.2373 336 THR A CA 1530 C C . THR A 204 ? 0.5022 0.8345 0.8156 0.2087 -0.0021 -0.2171 336 THR A C 1531 O O . THR A 204 ? 0.4980 0.8255 0.8220 0.2134 -0.0177 -0.2104 336 THR A O 1532 C CB . THR A 204 ? 0.5738 0.9586 0.9193 0.2434 0.0089 -0.2637 336 THR A CB 1533 O OG1 . THR A 204 ? 0.6060 0.9759 0.9495 0.2680 0.0048 -0.2848 336 THR A OG1 1534 C CG2 . THR A 204 ? 0.6202 1.0529 1.0085 0.2556 0.0010 -0.2735 336 THR A CG2 1535 N N . LYS A 205 ? 0.4671 0.8140 0.7668 0.1827 0.0173 -0.2078 337 LYS A N 1536 C CA . LYS A 205 ? 0.4564 0.8127 0.7534 0.1583 0.0210 -0.1894 337 LYS A CA 1537 C C . LYS A 205 ? 0.4553 0.7551 0.7263 0.1539 0.0062 -0.1684 337 LYS A C 1538 O O . LYS A 205 ? 0.4735 0.7733 0.7510 0.1504 -0.0040 -0.1594 337 LYS A O 1539 C CB . LYS A 205 ? 0.5253 0.8985 0.8068 0.1323 0.0424 -0.1829 337 LYS A CB 1540 C CG . LYS A 205 ? 0.6246 1.0640 0.9316 0.1261 0.0599 -0.1977 337 LYS A CG 1541 C CD . LYS A 205 ? 0.7034 1.1493 0.9866 0.0986 0.0790 -0.1881 337 LYS A CD 1542 C CE . LYS A 205 ? 0.7502 1.2622 1.0555 0.0835 0.0966 -0.1961 337 LYS A CE 1543 N NZ . LYS A 205 ? 0.7560 1.3155 1.0876 0.1028 0.1055 -0.2234 337 LYS A NZ 1544 N N . TRP A 206 ? 0.3973 0.6508 0.6386 0.1533 0.0052 -0.1613 338 TRP A N 1545 C CA . TRP A 206 ? 0.4525 0.6567 0.6678 0.1464 -0.0053 -0.1416 338 TRP A CA 1546 C C . TRP A 206 ? 0.4410 0.6231 0.6614 0.1636 -0.0269 -0.1404 338 TRP A C 1547 O O . TRP A 206 ? 0.4561 0.6236 0.6680 0.1563 -0.0349 -0.1264 338 TRP A O 1548 C CB . TRP A 206 ? 0.4799 0.6432 0.6662 0.1424 -0.0026 -0.1356 338 TRP A CB 1549 C CG . TRP A 206 ? 0.5184 0.6347 0.6817 0.1386 -0.0141 -0.1181 338 TRP A CG 1550 C CD1 . TRP A 206 ? 0.5767 0.6526 0.7286 0.1510 -0.0292 -0.1161 338 TRP A CD1 1551 C CD2 . TRP A 206 ? 0.4949 0.6005 0.6428 0.1207 -0.0114 -0.1003 338 TRP A CD2 1552 N NE1 . TRP A 206 ? 0.5541 0.5979 0.6840 0.1402 -0.0342 -0.0976 338 TRP A NE1 1553 C CE2 . TRP A 206 ? 0.5187 0.5811 0.6467 0.1230 -0.0232 -0.0888 338 TRP A CE2 1554 C CE3 . TRP A 206 ? 0.4774 0.6042 0.6252 0.1028 -0.0006 -0.0933 338 TRP A CE3 1555 C CZ2 . TRP A 206 ? 0.4637 0.5083 0.5733 0.1093 -0.0227 -0.0725 338 TRP A CZ2 1556 C CZ3 . TRP A 206 ? 0.5110 0.6158 0.6407 0.0910 -0.0024 -0.0775 338 TRP A CZ3 1557 C CH2 . TRP A 206 ? 0.4959 0.5625 0.6076 0.0950 -0.0125 -0.0682 338 TRP A CH2 1558 N N . ASN A 207 ? 0.4224 0.5998 0.6544 0.1870 -0.0374 -0.1554 339 ASN A N 1559 C CA . ASN A 207 ? 0.5303 0.6826 0.7648 0.2047 -0.0605 -0.1541 339 ASN A CA 1560 C C . ASN A 207 ? 0.4894 0.6790 0.7514 0.2079 -0.0677 -0.1568 339 ASN A C 1561 O O . ASN A 207 ? 0.4738 0.6404 0.7296 0.2129 -0.0858 -0.1477 339 ASN A O 1562 C CB . ASN A 207 ? 0.6137 0.7481 0.8535 0.2305 -0.0724 -0.1705 339 ASN A CB 1563 C CG . ASN A 207 ? 0.7096 0.7910 0.9163 0.2262 -0.0733 -0.1628 339 ASN A CG 1564 O OD1 . ASN A 207 ? 0.7344 0.7792 0.9132 0.2106 -0.0752 -0.1425 339 ASN A OD1 1565 N ND2 . ASN A 207 ? 0.7432 0.8223 0.9529 0.2392 -0.0712 -0.1798 339 ASN A ND2 1566 N N . LYS A 208 ? 0.4453 0.6932 0.7364 0.2032 -0.0536 -0.1688 340 LYS A N 1567 C CA . LYS A 208 ? 0.4884 0.7771 0.8082 0.2023 -0.0592 -0.1714 340 LYS A CA 1568 C C . LYS A 208 ? 0.4576 0.7288 0.7569 0.1797 -0.0601 -0.1501 340 LYS A C 1569 O O . LYS A 208 ? 0.4707 0.7381 0.7746 0.1827 -0.0763 -0.1449 340 LYS A O 1570 C CB . LYS A 208 ? 0.5175 0.8745 0.8710 0.1969 -0.0409 -0.1873 340 LYS A CB 1571 C CG . LYS A 208 ? 0.5795 0.9835 0.9654 0.1922 -0.0456 -0.1898 340 LYS A CG 1572 C CD . LYS A 208 ? 0.6963 1.1716 1.1172 0.1864 -0.0265 -0.2066 340 LYS A CD 1573 C CE . LYS A 208 ? 0.7720 1.2974 1.2287 0.1799 -0.0321 -0.2094 340 LYS A CE 1574 N NZ . LYS A 208 ? 0.7887 1.3878 1.2796 0.1706 -0.0115 -0.2248 340 LYS A NZ 1575 N N . VAL A 209 ? 0.3927 0.6521 0.6683 0.1581 -0.0437 -0.1387 341 VAL A N 1576 C CA . VAL A 209 ? 0.3788 0.6201 0.6336 0.1378 -0.0435 -0.1204 341 VAL A CA 1577 C C . VAL A 209 ? 0.4546 0.6418 0.6808 0.1439 -0.0595 -0.1075 341 VAL A C 1578 O O . VAL A 209 ? 0.4571 0.6345 0.6761 0.1393 -0.0701 -0.0985 341 VAL A O 1579 C CB . VAL A 209 ? 0.3672 0.6044 0.6024 0.1164 -0.0242 -0.1121 341 VAL A CB 1580 C CG1 . VAL A 209 ? 0.3850 0.5934 0.5948 0.1000 -0.0266 -0.0942 341 VAL A CG1 1581 C CG2 . VAL A 209 ? 0.3811 0.6714 0.6397 0.1049 -0.0083 -0.1214 341 VAL A CG2 1582 N N . LEU A 210 ? 0.4439 0.5957 0.6519 0.1529 -0.0612 -0.1067 342 LEU A N 1583 C CA . LEU A 210 ? 0.5472 0.6472 0.7253 0.1559 -0.0747 -0.0934 342 LEU A CA 1584 C C . LEU A 210 ? 0.5531 0.6464 0.7389 0.1722 -0.0977 -0.0950 342 LEU A C 1585 O O . LEU A 210 ? 0.5238 0.5880 0.6869 0.1683 -0.1087 -0.0818 342 LEU A O 1586 C CB . LEU A 210 ? 0.5492 0.6150 0.7099 0.1617 -0.0734 -0.0936 342 LEU A CB 1587 C CG . LEU A 210 ? 0.6136 0.6271 0.7386 0.1562 -0.0813 -0.0763 342 LEU A CG 1588 C CD1 . LEU A 210 ? 0.5630 0.5752 0.6702 0.1347 -0.0692 -0.0626 342 LEU A CD1 1589 C CD2 . LEU A 210 ? 0.7055 0.6861 0.8157 0.1601 -0.0816 -0.0769 342 LEU A CD2 1590 N N . LYS A 211 ? 0.5137 0.6346 0.7310 0.1914 -0.1053 -0.1121 343 LYS A N 1591 C CA . LYS A 211 ? 0.5605 0.6837 0.7921 0.2086 -0.1286 -0.1162 343 LYS A CA 1592 C C . LYS A 211 ? 0.5162 0.6598 0.7524 0.1954 -0.1315 -0.1091 343 LYS A C 1593 O O . LYS A 211 ? 0.5164 0.6337 0.7361 0.1983 -0.1498 -0.0997 343 LYS A O 1594 C CB . LYS A 211 ? 0.6284 0.7921 0.9015 0.2309 -0.1329 -0.1392 343 LYS A CB 1595 C CG . LYS A 211 ? 0.7459 0.9146 1.0383 0.2519 -0.1595 -0.1454 343 LYS A CG 1596 C CD . LYS A 211 ? 0.8866 0.9888 1.1429 0.2615 -0.1824 -0.1320 343 LYS A CD 1597 C CE . LYS A 211 ? 0.9683 1.0712 1.2429 0.2863 -0.2123 -0.1395 343 LYS A CE 1598 N NZ . LYS A 211 ? 1.0236 1.0593 1.2564 0.2904 -0.2356 -0.1222 343 LYS A NZ 1599 N N . GLN A 212 ? 0.4464 0.6340 0.7018 0.1797 -0.1143 -0.1132 344 GLN A N 1600 C CA . GLN A 212 ? 0.4113 0.6171 0.6709 0.1649 -0.1170 -0.1072 344 GLN A CA 1601 C C . GLN A 212 ? 0.4270 0.5873 0.6442 0.1505 -0.1183 -0.0883 344 GLN A C 1602 O O . GLN A 212 ? 0.4527 0.6046 0.6613 0.1477 -0.1320 -0.0822 344 GLN A O 1603 C CB . GLN A 212 ? 0.3799 0.6354 0.6633 0.1474 -0.0973 -0.1133 344 GLN A CB 1604 C CG . GLN A 212 ? 0.4335 0.7472 0.7637 0.1584 -0.0959 -0.1328 344 GLN A CG 1605 C CD . GLN A 212 ? 0.4984 0.8573 0.8450 0.1378 -0.0729 -0.1368 344 GLN A CD 1606 O OE1 . GLN A 212 ? 0.5374 0.8785 0.8593 0.1217 -0.0569 -0.1278 344 GLN A OE1 1607 N NE2 . GLN A 212 ? 0.5132 0.9314 0.9015 0.1376 -0.0716 -0.1500 344 GLN A NE2 1608 N N . VAL A 213 ? 0.4187 0.5516 0.6097 0.1417 -0.1041 -0.0802 345 VAL A N 1609 C CA . VAL A 213 ? 0.4573 0.5511 0.6100 0.1295 -0.1034 -0.0643 345 VAL A CA 1610 C C . VAL A 213 ? 0.4957 0.5513 0.6261 0.1414 -0.1237 -0.0572 345 VAL A C 1611 O O . VAL A 213 ? 0.5457 0.5819 0.6528 0.1349 -0.1312 -0.0475 345 VAL A O 1612 C CB . VAL A 213 ? 0.4235 0.4980 0.5566 0.1204 -0.0859 -0.0584 345 VAL A CB 1613 C CG1 . VAL A 213 ? 0.4123 0.4498 0.5080 0.1098 -0.0850 -0.0434 345 VAL A CG1 1614 C CG2 . VAL A 213 ? 0.3522 0.4612 0.5028 0.1079 -0.0677 -0.0640 345 VAL A CG2 1615 N N . THR A 214 ? 0.4696 0.5127 0.6053 0.1589 -0.1334 -0.0624 346 THR A N 1616 C CA . THR A 214 ? 0.5293 0.5336 0.6435 0.1710 -0.1555 -0.0553 346 THR A CA 1617 C C . THR A 214 ? 0.5560 0.5748 0.6812 0.1772 -0.1751 -0.0576 346 THR A C 1618 O O . THR A 214 ? 0.5500 0.5382 0.6450 0.1747 -0.1881 -0.0460 346 THR A O 1619 C CB . THR A 214 ? 0.6065 0.5939 0.7273 0.1903 -0.1649 -0.0624 346 THR A CB 1620 O OG1 . THR A 214 ? 0.6857 0.6521 0.7894 0.1819 -0.1490 -0.0580 346 THR A OG1 1621 C CG2 . THR A 214 ? 0.6582 0.6023 0.7557 0.2031 -0.1916 -0.0543 346 THR A CG2 1622 N N . GLU A 215 ? 0.5124 0.5800 0.6805 0.1842 -0.1768 -0.0726 347 GLU A N 1623 C CA . GLU A 215 ? 0.5461 0.6337 0.7308 0.1898 -0.1964 -0.0764 347 GLU A CA 1624 C C . GLU A 215 ? 0.5613 0.6422 0.7230 0.1697 -0.1937 -0.0656 347 GLU A C 1625 O O . GLU A 215 ? 0.5978 0.6591 0.7408 0.1718 -0.2129 -0.0593 347 GLU A O 1626 C CB . GLU A 215 ? 0.5891 0.7394 0.8280 0.1963 -0.1939 -0.0951 347 GLU A CB 1627 C CG . GLU A 215 ? 0.7371 0.8985 1.0024 0.2204 -0.1990 -0.1098 347 GLU A CG 1628 C CD . GLU A 215 ? 0.8703 0.9828 1.1140 0.2413 -0.2255 -0.1050 347 GLU A CD 1629 O OE1 . GLU A 215 ? 0.8915 1.0029 1.1394 0.2511 -0.2500 -0.1047 347 GLU A OE1 1630 O OE2 . GLU A 215 ? 0.9172 0.9903 1.1380 0.2467 -0.2230 -0.1009 347 GLU A OE2 1631 N N . LYS A 216 ? 0.4612 0.5565 0.6225 0.1510 -0.1710 -0.0641 348 LYS A N 1632 C CA . LYS A 216 ? 0.5181 0.6049 0.6573 0.1326 -0.1673 -0.0557 348 LYS A CA 1633 C C . LYS A 216 ? 0.5509 0.5850 0.6402 0.1311 -0.1725 -0.0413 348 LYS A C 1634 O O . LYS A 216 ? 0.6059 0.6262 0.6745 0.1269 -0.1842 -0.0362 348 LYS A O 1635 C CB . LYS A 216 ? 0.4749 0.5811 0.6210 0.1146 -0.1430 -0.0564 348 LYS A CB 1636 C CG . LYS A 216 ? 0.5102 0.6134 0.6416 0.0972 -0.1414 -0.0513 348 LYS A CG 1637 C CD . LYS A 216 ? 0.6355 0.7649 0.7887 0.0966 -0.1589 -0.0576 348 LYS A CD 1638 C CE . LYS A 216 ? 0.8566 0.9631 0.9802 0.0844 -0.1653 -0.0509 348 LYS A CE 1639 N NZ . LYS A 216 ? 0.9916 1.1205 1.1336 0.0813 -0.1841 -0.0566 348 LYS A NZ 1640 N N . LEU A 217 ? 0.5000 0.5058 0.5695 0.1336 -0.1639 -0.0351 349 LEU A N 1641 C CA . LEU A 217 ? 0.5177 0.4774 0.5407 0.1300 -0.1668 -0.0211 349 LEU A CA 1642 C C . LEU A 217 ? 0.6025 0.5394 0.6083 0.1411 -0.1933 -0.0167 349 LEU A C 1643 O O . LEU A 217 ? 0.6215 0.5309 0.5895 0.1346 -0.1986 -0.0067 349 LEU A O 1644 C CB . LEU A 217 ? 0.5113 0.4468 0.5201 0.1303 -0.1554 -0.0154 349 LEU A CB 1645 C CG . LEU A 217 ? 0.5133 0.4588 0.5228 0.1162 -0.1301 -0.0150 349 LEU A CG 1646 C CD1 . LEU A 217 ? 0.5814 0.5075 0.5832 0.1171 -0.1210 -0.0115 349 LEU A CD1 1647 C CD2 . LEU A 217 ? 0.5490 0.4823 0.5292 0.1025 -0.1233 -0.0070 349 LEU A CD2 1648 N N . LYS A 218 ? 0.6363 0.5850 0.6693 0.1586 -0.2105 -0.0249 350 LYS A N 1649 C CA . LYS A 218 ? 0.6164 0.5431 0.6354 0.1715 -0.2393 -0.0213 350 LYS A CA 1650 C C . LYS A 218 ? 0.6304 0.5692 0.6452 0.1651 -0.2506 -0.0217 350 LYS A C 1651 O O . LYS A 218 ? 0.6613 0.5692 0.6417 0.1667 -0.2688 -0.0128 350 LYS A O 1652 C CB . LYS A 218 ? 0.6194 0.5632 0.6762 0.1940 -0.2560 -0.0335 350 LYS A CB 1653 C CG . LYS A 218 ? 0.6717 0.5838 0.7192 0.2049 -0.2569 -0.0310 350 LYS A CG 1654 C CD . LYS A 218 ? 0.7508 0.6860 0.8410 0.2295 -0.2719 -0.0474 350 LYS A CD 1655 C CE . LYS A 218 ? 0.8860 0.7837 0.9650 0.2420 -0.2762 -0.0463 350 LYS A CE 1656 N NZ . LYS A 218 ? 0.9556 0.7903 0.9860 0.2442 -0.2977 -0.0288 350 LYS A NZ 1657 N N . GLU A 219 ? 0.6261 0.6084 0.6739 0.1568 -0.2405 -0.0319 351 GLU A N 1658 C CA . GLU A 219 ? 0.6498 0.6456 0.6974 0.1491 -0.2515 -0.0339 351 GLU A CA 1659 C C . GLU A 219 ? 0.6993 0.6578 0.6945 0.1359 -0.2471 -0.0220 351 GLU A C 1660 O O . GLU A 219 ? 0.7168 0.6659 0.6927 0.1335 -0.2633 -0.0203 351 GLU A O 1661 C CB . GLU A 219 ? 0.6315 0.6761 0.7195 0.1377 -0.2379 -0.0448 351 GLU A CB 1662 C CG . GLU A 219 ? 0.7270 0.8176 0.8691 0.1487 -0.2385 -0.0584 351 GLU A CG 1663 C CD . GLU A 219 ? 0.8103 0.9491 0.9880 0.1331 -0.2245 -0.0671 351 GLU A CD 1664 O OE1 . GLU A 219 ? 0.8253 0.9621 0.9903 0.1168 -0.2251 -0.0640 351 GLU A OE1 1665 O OE2 . GLU A 219 ? 0.8304 1.0074 1.0466 0.1364 -0.2132 -0.0771 351 GLU A OE2 1666 N N . HIS A 220 ? 0.6338 0.5727 0.6064 0.1277 -0.2252 -0.0149 352 HIS A N 1667 C CA . HIS A 220 ? 0.6104 0.5216 0.5379 0.1149 -0.2157 -0.0061 352 HIS A CA 1668 C C . HIS A 220 ? 0.6491 0.5163 0.5302 0.1181 -0.2227 0.0071 352 HIS A C 1669 O O . HIS A 220 ? 0.7201 0.5644 0.5596 0.1096 -0.2202 0.0140 352 HIS A O 1670 C CB . HIS A 220 ? 0.6007 0.5203 0.5322 0.1033 -0.1875 -0.0066 352 HIS A CB 1671 C CG . HIS A 220 ? 0.6902 0.6409 0.6479 0.0937 -0.1801 -0.0157 352 HIS A CG 1672 N ND1 . HIS A 220 ? 0.6948 0.6811 0.6962 0.0933 -0.1727 -0.0240 352 HIS A ND1 1673 C CD2 . HIS A 220 ? 0.6705 0.6201 0.6148 0.0832 -0.1797 -0.0178 352 HIS A CD2 1674 C CE1 . HIS A 220 ? 0.5837 0.5884 0.5965 0.0811 -0.1680 -0.0289 352 HIS A CE1 1675 N NE2 . HIS A 220 ? 0.6588 0.6402 0.6381 0.0754 -0.1731 -0.0256 352 HIS A NE2 1676 N N . PHE A 221 ? 0.6282 0.4828 0.5151 0.1298 -0.2315 0.0104 353 PHE A N 1677 C CA . PHE A 221 ? 0.7070 0.5165 0.5493 0.1304 -0.2377 0.0249 353 PHE A CA 1678 C C . PHE A 221 ? 0.7655 0.5559 0.6029 0.1461 -0.2694 0.0275 353 PHE A C 1679 O O . PHE A 221 ? 0.7690 0.5308 0.5954 0.1537 -0.2781 0.0348 353 PHE A O 1680 C CB . PHE A 221 ? 0.6912 0.4902 0.5336 0.1268 -0.2187 0.0296 353 PHE A CB 1681 C CG . PHE A 221 ? 0.6502 0.4570 0.4827 0.1106 -0.1905 0.0311 353 PHE A CG 1682 C CD1 . PHE A 221 ? 0.7662 0.5482 0.5526 0.0989 -0.1827 0.0421 353 PHE A CD1 1683 C CD2 . PHE A 221 ? 0.6398 0.4803 0.5086 0.1074 -0.1726 0.0208 353 PHE A CD2 1684 C CE1 . PHE A 221 ? 0.7474 0.5396 0.5279 0.0865 -0.1580 0.0414 353 PHE A CE1 1685 C CE2 . PHE A 221 ? 0.6320 0.4780 0.4920 0.0945 -0.1496 0.0218 353 PHE A CE2 1686 C CZ . PHE A 221 ? 0.7048 0.5276 0.5225 0.0852 -0.1427 0.0313 353 PHE A CZ 1687 N N . ASN A 222 ? 0.7925 0.5974 0.6380 0.1507 -0.2883 0.0214 354 ASN A N 1688 C CA . ASN A 222 ? 0.7506 0.5377 0.5888 0.1658 -0.3218 0.0238 354 ASN A CA 1689 C C . ASN A 222 ? 0.7867 0.5697 0.6521 0.1850 -0.3351 0.0207 354 ASN A C 1690 O O . ASN A 222 ? 0.7974 0.5411 0.6360 0.1951 -0.3584 0.0301 354 ASN A O 1691 C CB . ASN A 222 ? 0.8215 0.5588 0.5935 0.1587 -0.3319 0.0408 354 ASN A CB 1692 C CG . ASN A 222 ? 0.8851 0.6087 0.6443 0.1703 -0.3678 0.0422 354 ASN A CG 1693 O OD1 . ASN A 222 ? 0.9146 0.6726 0.7103 0.1775 -0.3811 0.0293 354 ASN A OD1 1694 N ND2 . ASN A 222 ? 0.9124 0.5857 0.6193 0.1710 -0.3846 0.0584 354 ASN A ND2 1695 N N . ASN A 223 ? 0.8034 0.6250 0.7194 0.1899 -0.3207 0.0072 355 ASN A N 1696 C CA . ASN A 223 ? 0.8558 0.6813 0.8043 0.2101 -0.3310 -0.0006 355 ASN A CA 1697 C C . ASN A 223 ? 0.8335 0.6062 0.7468 0.2122 -0.3328 0.0124 355 ASN A C 1698 O O . ASN A 223 ? 0.8452 0.6023 0.7701 0.2315 -0.3518 0.0091 355 ASN A O 1699 C CB . ASN A 223 ? 0.9711 0.8114 0.9463 0.2310 -0.3641 -0.0099 355 ASN A CB 1700 C CG . ASN A 223 ? 1.1058 0.9725 1.1325 0.2535 -0.3702 -0.0260 355 ASN A CG 1701 O OD1 . ASN A 223 ? 1.1073 0.9936 1.1571 0.2512 -0.3466 -0.0334 355 ASN A OD1 1702 N ND2 . ASN A 223 ? 1.1951 1.0630 1.2397 0.2763 -0.4026 -0.0326 355 ASN A ND2 1703 N N . LYS A 224 ? 0.8326 0.5780 0.7036 0.1923 -0.3137 0.0266 357 LYS A N 1704 C CA . LYS A 224 ? 0.8730 0.5710 0.7112 0.1893 -0.3125 0.0400 357 LYS A CA 1705 C C . LYS A 224 ? 0.8502 0.5644 0.7261 0.1969 -0.2996 0.0287 357 LYS A C 1706 O O . LYS A 224 ? 0.7792 0.5423 0.6995 0.1992 -0.2850 0.0130 357 LYS A O 1707 C CB . LYS A 224 ? 0.8949 0.5707 0.6855 0.1646 -0.2915 0.0557 357 LYS A CB 1708 C CG . LYS A 224 ? 0.9912 0.6441 0.7345 0.1566 -0.3039 0.0677 357 LYS A CG 1709 C CD . LYS A 224 ? 1.0727 0.7018 0.7663 0.1334 -0.2830 0.0833 357 LYS A CD 1710 C CE . LYS A 224 ? 1.1129 0.6989 0.7803 0.1279 -0.2831 0.0978 357 LYS A CE 1711 N NZ . LYS A 224 ? 1.0972 0.6644 0.7174 0.1038 -0.2626 0.1133 357 LYS A NZ 1712 N N . THR A 225 ? 0.8928 0.5649 0.7495 0.2000 -0.3058 0.0366 358 THR A N 1713 C CA . THR A 225 ? 0.8608 0.5438 0.7487 0.2070 -0.2944 0.0254 358 THR A CA 1714 C C . THR A 225 ? 0.8390 0.5422 0.7277 0.1857 -0.2595 0.0265 358 THR A C 1715 O O . THR A 225 ? 0.8527 0.5345 0.7034 0.1657 -0.2476 0.0418 358 THR A O 1716 C CB . THR A 225 ? 0.9620 0.5889 0.8269 0.2156 -0.3130 0.0333 358 THR A CB 1717 O OG1 . THR A 225 ? 1.0066 0.6168 0.8764 0.2394 -0.3478 0.0297 358 THR A OG1 1718 C CG2 . THR A 225 ? 0.9304 0.5665 0.8237 0.2214 -0.3002 0.0208 358 THR A CG2 1719 N N . ILE A 226 ? 0.7549 0.5010 0.6868 0.1901 -0.2435 0.0099 359 ILE A N 1720 C CA . ILE A 226 ? 0.7511 0.5187 0.6867 0.1718 -0.2127 0.0098 359 ILE A CA 1721 C C . ILE A 226 ? 0.7891 0.5401 0.7268 0.1717 -0.2044 0.0082 359 ILE A C 1722 O O . ILE A 226 ? 0.8002 0.5618 0.7673 0.1885 -0.2102 -0.0062 359 ILE A O 1723 C CB . ILE A 226 ? 0.6477 0.4732 0.6255 0.1727 -0.1988 -0.0059 359 ILE A CB 1724 C CG1 . ILE A 226 ? 0.7294 0.5727 0.7094 0.1732 -0.2098 -0.0064 359 ILE A CG1 1725 C CG2 . ILE A 226 ? 0.5839 0.4267 0.5626 0.1543 -0.1694 -0.0050 359 ILE A CG2 1726 C CD1 . ILE A 226 ? 0.7419 0.5585 0.6768 0.1575 -0.2087 0.0098 359 ILE A CD1 1727 N N . ILE A 227 ? 0.6912 0.4177 0.5983 0.1527 -0.1909 0.0220 360 ILE A N 1728 C CA . ILE A 227 ? 0.7636 0.4712 0.6696 0.1496 -0.1842 0.0217 360 ILE A CA 1729 C C . ILE A 227 ? 0.7369 0.4691 0.6481 0.1315 -0.1557 0.0217 360 ILE A C 1730 O O . ILE A 227 ? 0.7623 0.4991 0.6549 0.1153 -0.1433 0.0316 360 ILE A O 1731 C CB . ILE A 227 ? 0.8497 0.4984 0.7135 0.1426 -0.1980 0.0394 360 ILE A CB 1732 C CG1 . ILE A 227 ? 0.9246 0.5433 0.7762 0.1597 -0.2292 0.0424 360 ILE A CG1 1733 C CG2 . ILE A 227 ? 0.8274 0.4544 0.6934 0.1413 -0.1954 0.0370 360 ILE A CG2 1734 C CD1 . ILE A 227 ? 0.9889 0.5456 0.7918 0.1498 -0.2446 0.0632 360 ILE A CD1 1735 N N . PHE A 228 ? 0.7092 0.4574 0.6454 0.1356 -0.1462 0.0095 361 PHE A N 1736 C CA . PHE A 228 ? 0.7287 0.4946 0.6683 0.1193 -0.1224 0.0099 361 PHE A CA 1737 C C . PHE A 228 ? 0.7614 0.4911 0.6803 0.1090 -0.1215 0.0186 361 PHE A C 1738 O O . PHE A 228 ? 0.7489 0.4484 0.6650 0.1190 -0.1369 0.0160 361 PHE A O 1739 C CB . PHE A 228 ? 0.6216 0.4294 0.5979 0.1267 -0.1111 -0.0080 361 PHE A CB 1740 C CG . PHE A 228 ? 0.6386 0.4865 0.6355 0.1301 -0.1075 -0.0149 361 PHE A CG 1741 C CD1 . PHE A 228 ? 0.6113 0.4771 0.6026 0.1153 -0.0932 -0.0091 361 PHE A CD1 1742 C CD2 . PHE A 228 ? 0.7317 0.5991 0.7541 0.1480 -0.1196 -0.0277 361 PHE A CD2 1743 C CE1 . PHE A 228 ? 0.6657 0.5640 0.6741 0.1165 -0.0917 -0.0150 361 PHE A CE1 1744 C CE2 . PHE A 228 ? 0.7057 0.6111 0.7480 0.1482 -0.1169 -0.0335 361 PHE A CE2 1745 C CZ . PHE A 228 ? 0.6763 0.5948 0.7102 0.1316 -0.1034 -0.0265 361 PHE A CZ 1746 N N . GLN A 229 ? 0.7437 0.4763 0.6489 0.0890 -0.1047 0.0284 362 GLN A N 1747 C CA . GLN A 229 ? 0.7222 0.4277 0.6114 0.0752 -0.1014 0.0367 362 GLN A CA 1748 C C . GLN A 229 ? 0.7464 0.4827 0.6492 0.0627 -0.0792 0.0332 362 GLN A C 1749 O O . GLN A 229 ? 0.7018 0.4724 0.6164 0.0614 -0.0669 0.0295 362 GLN A O 1750 C CB . GLN A 229 ? 0.7233 0.3959 0.5747 0.0600 -0.1058 0.0565 362 GLN A CB 1751 C CG . GLN A 229 ? 0.8465 0.4740 0.6768 0.0696 -0.1315 0.0632 362 GLN A CG 1752 C CD . GLN A 229 ? 0.9489 0.5393 0.7766 0.0724 -0.1440 0.0618 362 GLN A CD 1753 O OE1 . GLN A 229 ? 0.9203 0.5163 0.7729 0.0908 -0.1511 0.0452 362 GLN A OE1 1754 N NE2 . GLN A 229 ? 1.0184 0.5713 0.8153 0.0530 -0.1463 0.0785 362 GLN A NE2 1755 N N . PRO A 230 ? 0.8274 0.5498 0.7282 0.0534 -0.0759 0.0343 363 PRO A N 1756 C CA . PRO A 230 ? 0.7793 0.5295 0.6918 0.0411 -0.0569 0.0321 363 PRO A CA 1757 C C . PRO A 230 ? 0.7547 0.5116 0.6507 0.0240 -0.0454 0.0455 363 PRO A C 1758 O O . PRO A 230 ? 0.7644 0.4956 0.6349 0.0168 -0.0519 0.0585 363 PRO A O 1759 C CB . PRO A 230 ? 0.7483 0.4747 0.6586 0.0349 -0.0608 0.0313 363 PRO A CB 1760 C CG . PRO A 230 ? 0.9149 0.5941 0.8005 0.0343 -0.0788 0.0417 363 PRO A CG 1761 C CD . PRO A 230 ? 0.9312 0.6091 0.8173 0.0528 -0.0910 0.0384 363 PRO A CD 1762 N N . PRO A 231 ? 0.6759 0.4669 0.5852 0.0183 -0.0290 0.0420 364 PRO A N 1763 C CA . PRO A 231 ? 0.6926 0.4955 0.5899 0.0041 -0.0165 0.0515 364 PRO A CA 1764 C C . PRO A 231 ? 0.8475 0.6243 0.7225 -0.0130 -0.0176 0.0654 364 PRO A C 1765 O O . PRO A 231 ? 0.8727 0.6312 0.7494 -0.0183 -0.0229 0.0660 364 PRO A O 1766 C CB . PRO A 231 ? 0.6409 0.4763 0.5600 0.0010 -0.0026 0.0437 364 PRO A CB 1767 C CG . PRO A 231 ? 0.5705 0.4173 0.5095 0.0162 -0.0069 0.0305 364 PRO A CG 1768 C CD . PRO A 231 ? 0.5498 0.3690 0.4851 0.0247 -0.0219 0.0286 364 PRO A CD 1769 N N . SER A 232 ? 0.9128 0.6875 0.7654 -0.0228 -0.0128 0.0764 365 SER A N 1770 C CA . SER A 232 ? 1.0257 0.7748 0.8521 -0.0417 -0.0139 0.0920 365 SER A CA 1771 C C . SER A 232 ? 0.9999 0.7636 0.8370 -0.0595 -0.0015 0.0940 365 SER A C 1772 O O . SER A 232 ? 1.0660 0.8039 0.8902 -0.0748 -0.0065 0.1040 365 SER A O 1773 C CB . SER A 232 ? 1.0662 0.8158 0.8648 -0.0486 -0.0089 0.1022 365 SER A CB 1774 O OG . SER A 232 ? 1.0742 0.8644 0.8845 -0.0479 0.0084 0.0953 365 SER A OG 1775 N N . GLY A 233 ? 0.8785 0.6824 0.7393 -0.0577 0.0129 0.0847 366 GLY A N 1776 C CA . GLY A 233 ? 0.8283 0.6536 0.7036 -0.0728 0.0245 0.0850 366 GLY A CA 1777 C C . GLY A 233 ? 0.8150 0.6836 0.7114 -0.0657 0.0384 0.0748 366 GLY A C 1778 O O . GLY A 233 ? 0.7741 0.6506 0.6715 -0.0508 0.0379 0.0684 366 GLY A O 1779 N N . GLY A 234 ? 0.7814 0.6768 0.6949 -0.0763 0.0491 0.0731 367 GLY A N 1780 C CA . GLY A 234 ? 0.7139 0.6481 0.6480 -0.0687 0.0602 0.0631 367 GLY A CA 1781 C C . GLY A 234 ? 0.6261 0.5757 0.5873 -0.0669 0.0591 0.0545 367 GLY A C 1782 O O . GLY A 234 ? 0.6106 0.5434 0.5747 -0.0738 0.0515 0.0560 367 GLY A O 1783 N N . ASP A 235 ? 0.5407 0.5197 0.5197 -0.0575 0.0652 0.0453 368 ASP A N 1784 C CA . ASP A 235 ? 0.5457 0.5382 0.5475 -0.0546 0.0626 0.0374 368 ASP A CA 1785 C C . ASP A 235 ? 0.5109 0.4820 0.5117 -0.0439 0.0513 0.0324 368 ASP A C 1786 O O . ASP A 235 ? 0.4289 0.3851 0.4180 -0.0342 0.0471 0.0320 368 ASP A O 1787 C CB . ASP A 235 ? 0.6295 0.6535 0.6474 -0.0451 0.0691 0.0291 368 ASP A CB 1788 C CG . ASP A 235 ? 0.6406 0.6944 0.6658 -0.0534 0.0814 0.0303 368 ASP A CG 1789 O OD1 . ASP A 235 ? 0.6258 0.6846 0.6532 -0.0703 0.0851 0.0367 368 ASP A OD1 1790 O OD2 . ASP A 235 ? 0.6258 0.6988 0.6552 -0.0429 0.0871 0.0240 368 ASP A OD2 1791 N N . LEU A 236 ? 0.4142 0.3866 0.4276 -0.0457 0.0465 0.0276 369 LEU A N 1792 C CA . LEU A 236 ? 0.4305 0.3870 0.4434 -0.0366 0.0375 0.0211 369 LEU A CA 1793 C C . LEU A 236 ? 0.4484 0.4135 0.4634 -0.0222 0.0379 0.0149 369 LEU A C 1794 O O . LEU A 236 ? 0.4403 0.3933 0.4513 -0.0141 0.0325 0.0107 369 LEU A O 1795 C CB . LEU A 236 ? 0.4455 0.4059 0.4701 -0.0420 0.0334 0.0162 369 LEU A CB 1796 C CG . LEU A 236 ? 0.4649 0.4104 0.4871 -0.0573 0.0292 0.0209 369 LEU A CG 1797 C CD1 . LEU A 236 ? 0.4524 0.4070 0.4879 -0.0628 0.0248 0.0150 369 LEU A CD1 1798 C CD2 . LEU A 236 ? 0.5523 0.4614 0.5576 -0.0551 0.0204 0.0223 369 LEU A CD2 1799 N N . GLU A 237 ? 0.4100 0.3967 0.4322 -0.0194 0.0439 0.0137 370 GLU A N 1800 C CA . GLU A 237 ? 0.4433 0.4354 0.4658 -0.0082 0.0432 0.0090 370 GLU A CA 1801 C C . GLU A 237 ? 0.4301 0.4095 0.4397 -0.0025 0.0420 0.0110 370 GLU A C 1802 O O . GLU A 237 ? 0.4345 0.4132 0.4437 0.0050 0.0391 0.0073 370 GLU A O 1803 C CB . GLU A 237 ? 0.4122 0.4248 0.4431 -0.0054 0.0478 0.0070 370 GLU A CB 1804 C CG . GLU A 237 ? 0.3991 0.4255 0.4446 -0.0076 0.0457 0.0036 370 GLU A CG 1805 C CD . GLU A 237 ? 0.4109 0.4474 0.4655 -0.0186 0.0487 0.0062 370 GLU A CD 1806 O OE1 . GLU A 237 ? 0.4752 0.5120 0.5245 -0.0250 0.0548 0.0113 370 GLU A OE1 1807 O OE2 . GLU A 237 ? 0.3710 0.4152 0.4370 -0.0224 0.0445 0.0037 370 GLU A OE2 1808 N N . ILE A 238 ? 0.4427 0.4123 0.4413 -0.0074 0.0434 0.0175 371 ILE A N 1809 C CA . ILE A 238 ? 0.5251 0.4813 0.5101 -0.0017 0.0399 0.0197 371 ILE A CA 1810 C C . ILE A 238 ? 0.5200 0.4526 0.4976 -0.0013 0.0313 0.0219 371 ILE A C 1811 O O . ILE A 238 ? 0.5652 0.4896 0.5394 0.0075 0.0249 0.0196 371 ILE A O 1812 C CB . ILE A 238 ? 0.6769 0.6367 0.6491 -0.0045 0.0459 0.0248 371 ILE A CB 1813 C CG1 . ILE A 238 ? 0.7729 0.7281 0.7372 -0.0177 0.0501 0.0330 371 ILE A CG1 1814 C CG2 . ILE A 238 ? 0.7359 0.7180 0.7166 -0.0006 0.0526 0.0193 371 ILE A CG2 1815 C CD1 . ILE A 238 ? 0.9217 0.8843 0.8716 -0.0221 0.0584 0.0376 371 ILE A CD1 1816 N N . THR A 239 ? 0.5148 0.4360 0.4909 -0.0103 0.0298 0.0256 372 THR A N 1817 C CA . THR A 239 ? 0.5116 0.4047 0.4788 -0.0085 0.0193 0.0270 372 THR A CA 1818 C C . THR A 239 ? 0.4577 0.3513 0.4368 0.0015 0.0139 0.0161 372 THR A C 1819 O O . THR A 239 ? 0.4655 0.3409 0.4410 0.0093 0.0047 0.0130 372 THR A O 1820 C CB . THR A 239 ? 0.5364 0.4111 0.4953 -0.0229 0.0173 0.0349 372 THR A CB 1821 O OG1 . THR A 239 ? 0.5133 0.4003 0.4865 -0.0296 0.0204 0.0306 372 THR A OG1 1822 C CG2 . THR A 239 ? 0.5525 0.4294 0.4973 -0.0349 0.0244 0.0464 372 THR A CG2 1823 N N . MET A 240 ? 0.4591 0.3740 0.4513 0.0018 0.0195 0.0098 373 MET A N 1824 C CA . MET A 240 ? 0.4345 0.3544 0.4353 0.0099 0.0168 -0.0006 373 MET A CA 1825 C C . MET A 240 ? 0.4291 0.3705 0.4366 0.0154 0.0214 -0.0044 373 MET A C 1826 O O . MET A 240 ? 0.3987 0.3509 0.4060 0.0127 0.0263 -0.0002 373 MET A O 1827 C CB . MET A 240 ? 0.4174 0.3388 0.4232 0.0033 0.0171 -0.0044 373 MET A CB 1828 C CG . MET A 240 ? 0.5383 0.4352 0.5369 -0.0042 0.0109 -0.0008 373 MET A CG 1829 S SD . MET A 240 ? 0.6299 0.5276 0.6341 -0.0134 0.0092 -0.0056 373 MET A SD 1830 C CE . MET A 240 ? 0.6283 0.5182 0.6317 0.0001 0.0033 -0.0205 373 MET A CE 1831 N N . HIS A 241 ? 0.4139 0.3613 0.4271 0.0228 0.0196 -0.0128 374 HIS A N 1832 C CA . HIS A 241 ? 0.3747 0.3419 0.3936 0.0245 0.0237 -0.0160 374 HIS A CA 1833 C C . HIS A 241 ? 0.4128 0.3889 0.4333 0.0176 0.0276 -0.0159 374 HIS A C 1834 O O . HIS A 241 ? 0.4261 0.4015 0.4470 0.0161 0.0269 -0.0209 374 HIS A O 1835 C CB . HIS A 241 ? 0.3894 0.3650 0.4148 0.0319 0.0223 -0.0256 374 HIS A CB 1836 C CG . HIS A 241 ? 0.3443 0.3405 0.3741 0.0297 0.0271 -0.0278 374 HIS A CG 1837 N ND1 . HIS A 241 ? 0.4134 0.4236 0.4470 0.0302 0.0303 -0.0361 374 HIS A ND1 1838 C CD2 . HIS A 241 ? 0.2795 0.2829 0.3085 0.0258 0.0289 -0.0226 374 HIS A CD2 1839 C CE1 . HIS A 241 ? 0.3060 0.3310 0.3404 0.0247 0.0339 -0.0342 374 HIS A CE1 1840 N NE2 . HIS A 241 ? 0.3773 0.3964 0.4091 0.0224 0.0322 -0.0262 374 HIS A NE2 1841 N N . HIS A 242 ? 0.3541 0.3374 0.3744 0.0145 0.0304 -0.0109 375 HIS A N 1842 C CA . HIS A 242 ? 0.3383 0.3286 0.3607 0.0096 0.0316 -0.0101 375 HIS A CA 1843 C C . HIS A 242 ? 0.4013 0.4004 0.4229 0.0101 0.0318 -0.0109 375 HIS A C 1844 O O . HIS A 242 ? 0.3953 0.3955 0.4155 0.0125 0.0320 -0.0092 375 HIS A O 1845 C CB . HIS A 242 ? 0.3384 0.3305 0.3626 0.0069 0.0337 -0.0048 375 HIS A CB 1846 C CG . HIS A 242 ? 0.3842 0.3863 0.4145 0.0039 0.0333 -0.0050 375 HIS A CG 1847 N ND1 . HIS A 242 ? 0.4358 0.4462 0.4691 0.0065 0.0343 -0.0037 375 HIS A ND1 1848 C CD2 . HIS A 242 ? 0.3196 0.3240 0.3535 -0.0003 0.0305 -0.0071 375 HIS A CD2 1849 C CE1 . HIS A 242 ? 0.3608 0.3793 0.4012 0.0049 0.0316 -0.0048 375 HIS A CE1 1850 N NE2 . HIS A 242 ? 0.4322 0.4474 0.4727 0.0000 0.0291 -0.0064 375 HIS A NE2 1851 N N . PHE A 243 ? 0.3841 0.3871 0.4042 0.0067 0.0307 -0.0130 376 PHE A N 1852 C CA . PHE A 243 ? 0.3767 0.3842 0.3920 0.0045 0.0297 -0.0120 376 PHE A CA 1853 C C . PHE A 243 ? 0.3956 0.4035 0.4065 0.0002 0.0265 -0.0120 376 PHE A C 1854 O O . PHE A 243 ? 0.3575 0.3644 0.3703 -0.0010 0.0252 -0.0143 376 PHE A O 1855 C CB . PHE A 243 ? 0.3549 0.3686 0.3684 0.0039 0.0324 -0.0155 376 PHE A CB 1856 C CG . PHE A 243 ? 0.3484 0.3656 0.3617 0.0046 0.0345 -0.0227 376 PHE A CG 1857 C CD1 . PHE A 243 ? 0.3761 0.3880 0.3946 0.0106 0.0342 -0.0267 376 PHE A CD1 1858 C CD2 . PHE A 243 ? 0.4277 0.4512 0.4332 -0.0005 0.0359 -0.0257 376 PHE A CD2 1859 C CE1 . PHE A 243 ? 0.4141 0.4263 0.4320 0.0134 0.0347 -0.0355 376 PHE A CE1 1860 C CE2 . PHE A 243 ? 0.4534 0.4806 0.4574 0.0015 0.0383 -0.0348 376 PHE A CE2 1861 C CZ . PHE A 243 ? 0.4502 0.4715 0.4614 0.0094 0.0374 -0.0405 376 PHE A CZ 1862 N N . ASN A 244 ? 0.3836 0.3908 0.3870 -0.0030 0.0235 -0.0088 377 ASN A N 1863 C CA . ASN A 244 ? 0.3281 0.3333 0.3235 -0.0072 0.0182 -0.0078 377 ASN A CA 1864 C C . ASN A 244 ? 0.4486 0.4562 0.4302 -0.0143 0.0202 -0.0084 377 ASN A C 1865 O O . ASN A 244 ? 0.4309 0.4394 0.4078 -0.0180 0.0220 -0.0056 377 ASN A O 1866 C CB . ASN A 244 ? 0.3821 0.3812 0.3774 -0.0050 0.0105 -0.0028 377 ASN A CB 1867 C CG . ASN A 244 ? 0.3893 0.3854 0.3784 -0.0074 0.0023 -0.0017 377 ASN A CG 1868 O OD1 . ASN A 244 ? 0.4024 0.3946 0.3759 -0.0141 0.0002 -0.0001 377 ASN A OD1 1869 N ND2 . ASN A 244 ? 0.4008 0.4010 0.4023 -0.0027 -0.0024 -0.0027 377 ASN A ND2 1870 N N . CYS A 245 ? 0.4054 0.4150 0.3799 -0.0173 0.0203 -0.0127 378 CYS A N 1871 C CA . CYS A 245 ? 0.4119 0.4270 0.3708 -0.0247 0.0240 -0.0146 378 CYS A CA 1872 C C . CYS A 245 ? 0.4101 0.4177 0.3520 -0.0305 0.0162 -0.0117 378 CYS A C 1873 O O . CYS A 245 ? 0.4109 0.4161 0.3540 -0.0283 0.0120 -0.0157 378 CYS A O 1874 C CB . CYS A 245 ? 0.4008 0.4256 0.3637 -0.0213 0.0317 -0.0255 378 CYS A CB 1875 S SG . CYS A 245 ? 0.5018 0.5398 0.4462 -0.0289 0.0391 -0.0322 378 CYS A SG 1876 N N . ARG A 246 ? 0.4079 0.4101 0.3329 -0.0388 0.0129 -0.0041 379 ARG A N 1877 C CA . ARG A 246 ? 0.4138 0.4054 0.3183 -0.0448 0.0031 0.0007 379 ARG A CA 1878 C C . ARG A 246 ? 0.4743 0.4577 0.3892 -0.0372 -0.0088 0.0017 379 ARG A C 1879 O O . ARG A 246 ? 0.4872 0.4667 0.3919 -0.0391 -0.0167 0.0008 379 ARG A O 1880 C CB . ARG A 246 ? 0.4908 0.4894 0.3782 -0.0506 0.0078 -0.0062 379 ARG A CB 1881 C CG . ARG A 246 ? 0.6346 0.6502 0.5179 -0.0555 0.0225 -0.0122 379 ARG A CG 1882 C CD . ARG A 246 ? 0.7357 0.7521 0.6061 -0.0674 0.0252 -0.0026 379 ARG A CD 1883 N NE . ARG A 246 ? 0.8225 0.8627 0.6976 -0.0710 0.0404 -0.0097 379 ARG A NE 1884 C CZ . ARG A 246 ? 0.8373 0.8862 0.7075 -0.0826 0.0461 -0.0036 379 ARG A CZ 1885 N NH1 . ARG A 246 ? 0.7805 0.8108 0.6376 -0.0924 0.0369 0.0105 379 ARG A NH1 1886 N NH2 . ARG A 246 ? 0.8396 0.9160 0.7191 -0.0845 0.0600 -0.0124 379 ARG A NH2 1887 N N . GLY A 247 ? 0.4554 0.4388 0.3908 -0.0288 -0.0099 0.0027 380 GLY A N 1888 C CA . GLY A 247 ? 0.4637 0.4451 0.4129 -0.0212 -0.0199 0.0031 380 GLY A CA 1889 C C . GLY A 247 ? 0.3932 0.3862 0.3622 -0.0170 -0.0156 -0.0039 380 GLY A C 1890 O O . GLY A 247 ? 0.4062 0.4042 0.3923 -0.0114 -0.0205 -0.0044 380 GLY A O 1891 N N . GLU A 248 ? 0.3914 0.3887 0.3579 -0.0199 -0.0067 -0.0097 381 GLU A N 1892 C CA . GLU A 248 ? 0.3845 0.3868 0.3651 -0.0181 -0.0039 -0.0159 381 GLU A CA 1893 C C . GLU A 248 ? 0.3970 0.4023 0.3915 -0.0136 0.0049 -0.0163 381 GLU A C 1894 O O . GLU A 248 ? 0.3608 0.3663 0.3510 -0.0127 0.0114 -0.0162 381 GLU A O 1895 C CB . GLU A 248 ? 0.3594 0.3598 0.3269 -0.0222 -0.0018 -0.0235 381 GLU A CB 1896 C CG . GLU A 248 ? 0.4328 0.4290 0.3789 -0.0281 -0.0096 -0.0234 381 GLU A CG 1897 C CD . GLU A 248 ? 0.4731 0.4679 0.4252 -0.0287 -0.0227 -0.0223 381 GLU A CD 1898 O OE1 . GLU A 248 ? 0.4968 0.4966 0.4701 -0.0264 -0.0236 -0.0240 381 GLU A OE1 1899 O OE2 . GLU A 248 ? 0.4839 0.4736 0.4196 -0.0322 -0.0327 -0.0195 381 GLU A OE2 1900 N N . PHE A 249 ? 0.3691 0.3780 0.3797 -0.0119 0.0047 -0.0165 382 PHE A N 1901 C CA . PHE A 249 ? 0.3838 0.3936 0.4042 -0.0087 0.0119 -0.0156 382 PHE A CA 1902 C C . PHE A 249 ? 0.3871 0.3902 0.4057 -0.0097 0.0156 -0.0203 382 PHE A C 1903 O O . PHE A 249 ? 0.3642 0.3637 0.3859 -0.0136 0.0126 -0.0229 382 PHE A O 1904 C CB . PHE A 249 ? 0.3561 0.3743 0.3925 -0.0081 0.0109 -0.0130 382 PHE A CB 1905 C CG . PHE A 249 ? 0.3611 0.3851 0.4014 -0.0030 0.0073 -0.0102 382 PHE A CG 1906 C CD1 . PHE A 249 ? 0.3781 0.4011 0.4181 0.0024 0.0116 -0.0082 382 PHE A CD1 1907 C CD2 . PHE A 249 ? 0.3761 0.4042 0.4190 -0.0025 -0.0022 -0.0103 382 PHE A CD2 1908 C CE1 . PHE A 249 ? 0.3594 0.3838 0.4016 0.0087 0.0067 -0.0071 382 PHE A CE1 1909 C CE2 . PHE A 249 ? 0.3847 0.4144 0.4306 0.0044 -0.0079 -0.0087 382 PHE A CE2 1910 C CZ . PHE A 249 ? 0.3281 0.3551 0.3736 0.0103 -0.0032 -0.0075 382 PHE A CZ 1911 N N . PHE A 250 ? 0.3702 0.3710 0.3845 -0.0060 0.0207 -0.0219 383 PHE A N 1912 C CA . PHE A 250 ? 0.3537 0.3470 0.3662 -0.0037 0.0224 -0.0279 383 PHE A CA 1913 C C . PHE A 250 ? 0.4140 0.4012 0.4332 -0.0012 0.0241 -0.0240 383 PHE A C 1914 O O . PHE A 250 ? 0.3988 0.3904 0.4209 0.0008 0.0268 -0.0188 383 PHE A O 1915 C CB . PHE A 250 ? 0.3662 0.3648 0.3724 0.0001 0.0266 -0.0333 383 PHE A CB 1916 C CG . PHE A 250 ? 0.4692 0.4716 0.4641 -0.0029 0.0264 -0.0397 383 PHE A CG 1917 C CD1 . PHE A 250 ? 0.5166 0.5186 0.5073 0.0012 0.0284 -0.0508 383 PHE A CD1 1918 C CD2 . PHE A 250 ? 0.4617 0.4674 0.4482 -0.0089 0.0234 -0.0355 383 PHE A CD2 1919 C CE1 . PHE A 250 ? 0.5169 0.5241 0.4941 -0.0017 0.0296 -0.0579 383 PHE A CE1 1920 C CE2 . PHE A 250 ? 0.4169 0.4249 0.3880 -0.0129 0.0230 -0.0408 383 PHE A CE2 1921 C CZ . PHE A 250 ? 0.4317 0.4416 0.3977 -0.0097 0.0272 -0.0521 383 PHE A CZ 1922 N N . TYR A 251 ? 0.4165 0.3907 0.4352 -0.0016 0.0215 -0.0268 384 TYR A N 1923 C CA . TYR A 251 ? 0.4202 0.3834 0.4402 -0.0002 0.0215 -0.0225 384 TYR A CA 1924 C C . TYR A 251 ? 0.4259 0.3748 0.4415 0.0064 0.0178 -0.0301 384 TYR A C 1925 O O . TYR A 251 ? 0.4303 0.3678 0.4424 0.0049 0.0132 -0.0362 384 TYR A O 1926 C CB . TYR A 251 ? 0.3993 0.3567 0.4224 -0.0096 0.0196 -0.0168 384 TYR A CB 1927 C CG . TYR A 251 ? 0.4167 0.3917 0.4478 -0.0141 0.0234 -0.0109 384 TYR A CG 1928 C CD1 . TYR A 251 ? 0.4029 0.3810 0.4361 -0.0168 0.0278 -0.0038 384 TYR A CD1 1929 C CD2 . TYR A 251 ? 0.3615 0.3500 0.3970 -0.0148 0.0219 -0.0132 384 TYR A CD2 1930 C CE1 . TYR A 251 ? 0.4131 0.4100 0.4554 -0.0186 0.0317 -0.0011 384 TYR A CE1 1931 C CE2 . TYR A 251 ? 0.3737 0.3780 0.4186 -0.0160 0.0235 -0.0096 384 TYR A CE2 1932 C CZ . TYR A 251 ? 0.3438 0.3538 0.3935 -0.0172 0.0289 -0.0046 384 TYR A CZ 1933 O OH . TYR A 251 ? 0.3774 0.4061 0.4380 -0.0162 0.0312 -0.0035 384 TYR A OH 1934 N N . CYS A 252 ? 0.4242 0.3734 0.4403 0.0147 0.0187 -0.0310 385 CYS A N 1935 C CA . CYS A 252 ? 0.4368 0.3767 0.4520 0.0244 0.0145 -0.0406 385 CYS A CA 1936 C C . CYS A 252 ? 0.4652 0.3863 0.4782 0.0288 0.0087 -0.0360 385 CYS A C 1937 O O . CYS A 252 ? 0.4650 0.3896 0.4780 0.0283 0.0104 -0.0278 385 CYS A O 1938 C CB . CYS A 252 ? 0.4185 0.3798 0.4386 0.0316 0.0194 -0.0484 385 CYS A CB 1939 S SG . CYS A 252 ? 0.4968 0.4769 0.5131 0.0248 0.0255 -0.0529 385 CYS A SG 1940 N N . ASN A 253 ? 0.4711 0.3692 0.4797 0.0332 0.0004 -0.0414 386 ASN A N 1941 C CA . ASN A 253 ? 0.5352 0.4083 0.5380 0.0377 -0.0085 -0.0367 386 ASN A CA 1942 C C . ASN A 253 ? 0.4702 0.3518 0.4800 0.0534 -0.0111 -0.0439 386 ASN A C 1943 O O . ASN A 253 ? 0.4775 0.3667 0.4942 0.0645 -0.0122 -0.0580 386 ASN A O 1944 C CB . ASN A 253 ? 0.5738 0.4151 0.5684 0.0372 -0.0189 -0.0408 386 ASN A CB 1945 C CG . ASN A 253 ? 0.6600 0.4679 0.6438 0.0385 -0.0303 -0.0328 386 ASN A CG 1946 O OD1 . ASN A 253 ? 0.5836 0.3903 0.5682 0.0496 -0.0345 -0.0324 386 ASN A OD1 1947 N ND2 . ASN A 253 ? 0.8300 0.6105 0.8026 0.0257 -0.0361 -0.0251 386 ASN A ND2 1948 N N . THR A 254 ? 0.5035 0.3862 0.5120 0.0542 -0.0121 -0.0351 387 THR A N 1949 C CA . THR A 254 ? 0.5143 0.4094 0.5322 0.0678 -0.0154 -0.0411 387 THR A CA 1950 C C . THR A 254 ? 0.5736 0.4409 0.5863 0.0793 -0.0305 -0.0412 387 THR A C 1951 O O . THR A 254 ? 0.5762 0.4528 0.5969 0.0904 -0.0356 -0.0444 387 THR A O 1952 C CB . THR A 254 ? 0.4466 0.3618 0.4667 0.0629 -0.0090 -0.0333 387 THR A CB 1953 O OG1 . THR A 254 ? 0.5010 0.3974 0.5066 0.0551 -0.0114 -0.0196 387 THR A OG1 1954 C CG2 . THR A 254 ? 0.4074 0.3468 0.4322 0.0536 0.0032 -0.0337 387 THR A CG2 1955 N N . THR A 255 ? 0.5545 0.3868 0.5538 0.0763 -0.0392 -0.0376 388 THR A N 1956 C CA . THR A 255 ? 0.6335 0.4317 0.6239 0.0868 -0.0564 -0.0363 388 THR A CA 1957 C C . THR A 255 ? 0.6554 0.4659 0.6629 0.1092 -0.0637 -0.0531 388 THR A C 1958 O O . THR A 255 ? 0.6871 0.4921 0.6961 0.1203 -0.0745 -0.0519 388 THR A O 1959 C CB . THR A 255 ? 0.6765 0.4338 0.6514 0.0806 -0.0658 -0.0336 388 THR A CB 1960 O OG1 . THR A 255 ? 0.7682 0.5137 0.7274 0.0594 -0.0611 -0.0159 388 THR A OG1 1961 C CG2 . THR A 255 ? 0.8334 0.5518 0.7996 0.0951 -0.0865 -0.0356 388 THR A CG2 1962 N N . GLN A 256 ? 0.6718 0.5022 0.6927 0.1159 -0.0574 -0.0695 389 GLN A N 1963 C CA . GLN A 256 ? 0.6962 0.5443 0.7360 0.1375 -0.0621 -0.0884 389 GLN A CA 1964 C C . GLN A 256 ? 0.6703 0.5584 0.7286 0.1423 -0.0566 -0.0901 389 GLN A C 1965 O O . GLN A 256 ? 0.7520 0.6525 0.8268 0.1607 -0.0645 -0.1023 389 GLN A O 1966 C CB . GLN A 256 ? 0.6822 0.5475 0.7295 0.1411 -0.0534 -0.1057 389 GLN A CB 1967 C CG . GLN A 256 ? 0.7164 0.5419 0.7490 0.1420 -0.0628 -0.1104 389 GLN A CG 1968 C CD . GLN A 256 ? 0.7380 0.5830 0.7754 0.1451 -0.0534 -0.1284 389 GLN A CD 1969 O OE1 . GLN A 256 ? 0.7332 0.5829 0.7800 0.1647 -0.0580 -0.1487 389 GLN A OE1 1970 N NE2 . GLN A 256 ? 0.6747 0.5330 0.7057 0.1267 -0.0404 -0.1219 389 GLN A NE2 1971 N N . LEU A 257 ? 0.5662 0.4745 0.6227 0.1262 -0.0442 -0.0788 390 LEU A N 1972 C CA . LEU A 257 ? 0.5893 0.5340 0.6621 0.1277 -0.0392 -0.0799 390 LEU A CA 1973 C C . LEU A 257 ? 0.6940 0.6248 0.7640 0.1341 -0.0532 -0.0721 390 LEU A C 1974 O O . LEU A 257 ? 0.7864 0.7430 0.8742 0.1427 -0.0563 -0.0781 390 LEU A O 1975 C CB . LEU A 257 ? 0.5910 0.5549 0.6598 0.1090 -0.0243 -0.0702 390 LEU A CB 1976 C CG . LEU A 257 ? 0.6018 0.5933 0.6771 0.1018 -0.0095 -0.0777 390 LEU A CG 1977 C CD1 . LEU A 257 ? 0.5435 0.5482 0.6141 0.0856 0.0001 -0.0662 390 LEU A CD1 1978 C CD2 . LEU A 257 ? 0.6023 0.6285 0.6993 0.1132 -0.0063 -0.0948 390 LEU A CD2 1979 N N . PHE A 258 ? 0.6316 0.5226 0.6783 0.1285 -0.0619 -0.0582 391 PHE A N 1980 C CA . PHE A 258 ? 0.6896 0.5643 0.7276 0.1327 -0.0755 -0.0490 391 PHE A CA 1981 C C . PHE A 258 ? 0.7830 0.6189 0.8128 0.1476 -0.0960 -0.0510 391 PHE A C 1982 O O . PHE A 258 ? 0.8077 0.6035 0.8117 0.1414 -0.1059 -0.0367 391 PHE A O 1983 C CB . PHE A 258 ? 0.6452 0.5083 0.6608 0.1142 -0.0693 -0.0308 391 PHE A CB 1984 C CG . PHE A 258 ? 0.6429 0.5412 0.6675 0.1031 -0.0526 -0.0306 391 PHE A CG 1985 C CD1 . PHE A 258 ? 0.5992 0.5056 0.6228 0.0911 -0.0382 -0.0299 391 PHE A CD1 1986 C CD2 . PHE A 258 ? 0.5659 0.4876 0.6001 0.1050 -0.0533 -0.0316 391 PHE A CD2 1987 C CE1 . PHE A 258 ? 0.5564 0.4902 0.5864 0.0819 -0.0256 -0.0293 391 PHE A CE1 1988 C CE2 . PHE A 258 ? 0.4318 0.3804 0.4724 0.0944 -0.0401 -0.0312 391 PHE A CE2 1989 C CZ . PHE A 258 ? 0.4888 0.4422 0.5266 0.0834 -0.0266 -0.0299 391 PHE A CZ 1990 N N . ASN A 259 ? 0.8608 0.7105 0.9127 0.1671 -0.1021 -0.0695 392 ASN A N 1991 C CA . ASN A 259 ? 0.9711 0.7861 1.0202 0.1859 -0.1224 -0.0769 392 ASN A CA 1992 C C . ASN A 259 ? 0.9469 0.7604 1.0039 0.2032 -0.1418 -0.0782 392 ASN A C 1993 O O . ASN A 259 ? 0.8434 0.6983 0.9307 0.2173 -0.1415 -0.0930 392 ASN A O 1994 C CB . ASN A 259 ? 1.0853 0.9202 1.1557 0.1999 -0.1174 -0.0997 392 ASN A CB 1995 C CG . ASN A 259 ? 1.2986 1.0891 1.3611 0.2174 -0.1374 -0.1084 392 ASN A CG 1996 O OD1 . ASN A 259 ? 1.2867 1.0404 1.3378 0.2272 -0.1591 -0.1019 392 ASN A OD1 1997 N ND2 . ASN A 259 ? 1.5230 1.3146 1.5897 0.2216 -0.1312 -0.1236 392 ASN A ND2 1998 N N . ASN A 260 ? 0.9688 0.7355 0.9981 0.2009 -0.1591 -0.0622 393 ASN A N 1999 C CA . ASN A 260 ? 0.9821 0.7414 1.0127 0.2154 -0.1801 -0.0601 393 ASN A CA 2000 C C . ASN A 260 ? 1.0195 0.7850 1.0770 0.2460 -0.1979 -0.0810 393 ASN A C 2001 O O . ASN A 260 ? 1.0009 0.7907 1.0788 0.2608 -0.2089 -0.0878 393 ASN A O 2002 C CB . ASN A 260 ? 1.0264 0.7277 1.0155 0.2057 -0.1958 -0.0379 393 ASN A CB 2003 C CG . ASN A 260 ? 1.0218 0.7250 0.9873 0.1781 -0.1785 -0.0189 393 ASN A CG 2004 O OD1 . ASN A 260 ? 0.8765 0.6145 0.8506 0.1725 -0.1689 -0.0176 393 ASN A OD1 2005 N ND2 . ASN A 260 ? 1.0971 0.7642 1.0338 0.1604 -0.1746 -0.0051 393 ASN A ND2 2006 N N . THR A 261 ? 1.0508 0.7953 1.1091 0.2560 -0.2014 -0.0926 394 THR A N 2007 C CA . THR A 261 ? 1.1165 0.8609 1.1980 0.2878 -0.2202 -0.1142 394 THR A CA 2008 C C . THR A 261 ? 1.0019 0.8181 1.1290 0.3008 -0.2054 -0.1384 394 THR A C 2009 O O . THR A 261 ? 0.9310 0.7655 1.0862 0.3282 -0.2197 -0.1571 394 THR A O 2010 C CB . THR A 261 ? 1.2281 0.9217 1.2931 0.2954 -0.2309 -0.1203 394 THR A CB 2011 O OG1 . THR A 261 ? 1.1969 0.8964 1.2529 0.2741 -0.2075 -0.1182 394 THR A OG1 2012 C CG2 . THR A 261 ? 1.3190 0.9387 1.3439 0.2910 -0.2559 -0.0994 394 THR A CG2 2013 N N . CYS A 262 ? 0.9654 0.8227 1.0995 0.2807 -0.1773 -0.1374 395 CYS A N 2014 C CA . CYS A 262 ? 0.9753 0.9019 1.1482 0.2864 -0.1602 -0.1568 395 CYS A CA 2015 C C . CYS A 262 ? 0.9741 0.9413 1.1663 0.2830 -0.1600 -0.1525 395 CYS A C 2016 O O . CYS A 262 ? 0.9390 0.9660 1.1647 0.2852 -0.1471 -0.1666 395 CYS A O 2017 C CB . CYS A 262 ? 0.9582 0.9073 1.1271 0.2655 -0.1322 -0.1570 395 CYS A CB 2018 S SG . CYS A 262 ? 1.0396 0.9945 1.2179 0.2803 -0.1252 -0.1823 395 CYS A SG 2019 N N . ILE A 263 ? 0.9963 0.9311 1.1661 0.2761 -0.1743 -0.1330 396 ILE A N 2020 C CA . ILE A 263 ? 1.0076 0.9743 1.1910 0.2720 -0.1769 -0.1281 396 ILE A CA 2021 C C . ILE A 263 ? 1.0037 0.9717 1.2070 0.2989 -0.2044 -0.1378 396 ILE A C 2022 O O . ILE A 263 ? 1.0638 0.9806 1.2481 0.3132 -0.2278 -0.1339 396 ILE A O 2023 C CB . ILE A 263 ? 1.0474 0.9829 1.1940 0.2485 -0.1756 -0.1024 396 ILE A CB 2024 C CG1 . ILE A 263 ? 1.0178 0.9632 1.1524 0.2232 -0.1483 -0.0949 396 ILE A CG1 2025 C CG2 . ILE A 263 ? 1.0813 1.0407 1.2380 0.2473 -0.1841 -0.0983 396 ILE A CG2 2026 C CD1 . ILE A 263 ? 1.0696 0.9821 1.1669 0.2021 -0.1456 -0.0719 396 ILE A CD1 2027 N N . LYS A 269 ? 1.8712 1.7469 2.1175 0.4372 -0.2480 -0.2596 408 LYS A N 2028 C CA . LYS A 269 ? 1.8937 1.7541 2.1297 0.4394 -0.2379 -0.2744 408 LYS A CA 2029 C C . LYS A 269 ? 1.7847 1.7223 2.0490 0.4337 -0.2046 -0.2932 408 LYS A C 2030 O O . LYS A 269 ? 1.7346 1.7327 2.0227 0.4227 -0.1883 -0.2904 408 LYS A O 2031 C CB . LYS A 269 ? 1.9615 1.7598 2.1492 0.4096 -0.2352 -0.2484 408 LYS A CB 2032 C CG . LYS A 269 ? 1.9616 1.7886 2.1398 0.3731 -0.2087 -0.2263 408 LYS A CG 2033 C CD . LYS A 269 ? 2.0185 1.7832 2.1525 0.3470 -0.2150 -0.1954 408 LYS A CD 2034 C CE . LYS A 269 ? 2.0100 1.8058 2.1384 0.3157 -0.1918 -0.1751 408 LYS A CE 2035 N NZ . LYS A 269 ? 1.9974 1.8385 2.1368 0.3029 -0.1629 -0.1846 408 LYS A NZ 2036 N N . GLY A 270 ? 1.7323 1.6656 1.9915 0.4400 -0.1954 -0.3119 409 GLY A N 2037 C CA . GLY A 270 ? 1.6282 1.6285 1.9066 0.4331 -0.1638 -0.3292 409 GLY A CA 2038 C C . GLY A 270 ? 1.5350 1.5289 1.7836 0.3951 -0.1409 -0.3080 409 GLY A C 2039 O O . GLY A 270 ? 1.5176 1.4781 1.7409 0.3888 -0.1373 -0.3103 409 GLY A O 2040 N N . CYS A 271 ? 1.4760 1.5017 1.7284 0.3704 -0.1267 -0.2880 410 CYS A N 2041 C CA . CYS A 271 ? 1.3986 1.4152 1.6234 0.3351 -0.1085 -0.2650 410 CYS A CA 2042 C C . CYS A 271 ? 1.2577 1.3415 1.5009 0.3161 -0.0829 -0.2618 410 CYS A C 2043 O O . CYS A 271 ? 1.1771 1.2586 1.4078 0.2912 -0.0763 -0.2381 410 CYS A O 2044 C CB . CYS A 271 ? 1.4299 1.3906 1.6263 0.3198 -0.1236 -0.2350 410 CYS A CB 2045 S SG . CYS A 271 ? 0.9566 0.9365 1.1709 0.3219 -0.1354 -0.2219 410 CYS A SG 2046 N N . ASN A 272 ? 1.2024 1.3458 1.4747 0.3277 -0.0689 -0.2862 411 ASN A N 2047 C CA . ASN A 272 ? 1.0717 1.2814 1.3633 0.3096 -0.0454 -0.2848 411 ASN A CA 2048 C C . ASN A 272 ? 0.8847 1.1117 1.1592 0.2890 -0.0203 -0.2859 411 ASN A C 2049 O O . ASN A 272 ? 0.8319 1.1115 1.1179 0.2723 0.0002 -0.2852 411 ASN A O 2050 C CB . ASN A 272 ? 1.1566 1.4298 1.4938 0.3319 -0.0444 -0.3095 411 ASN A CB 2051 C CG . ASN A 272 ? 1.2642 1.5393 1.6134 0.3643 -0.0502 -0.3412 411 ASN A CG 2052 O OD1 . ASN A 272 ? 1.2901 1.5293 1.6129 0.3658 -0.0487 -0.3467 411 ASN A OD1 2053 N ND2 . ASN A 272 ? 1.2956 1.6132 1.6856 0.3914 -0.0580 -0.3633 411 ASN A ND2 2054 N N . GLY A 273 ? 0.7780 0.9583 1.0231 0.2889 -0.0234 -0.2866 412 GLY A N 2055 C CA . GLY A 273 ? 0.6981 0.8913 0.9255 0.2734 -0.0030 -0.2908 412 GLY A CA 2056 C C . GLY A 273 ? 0.6541 0.8317 0.8557 0.2406 0.0064 -0.2632 412 GLY A C 2057 O O . GLY A 273 ? 0.5764 0.7442 0.7775 0.2284 0.0013 -0.2418 412 GLY A O 2058 N N . THR A 274 ? 0.6375 0.8128 0.8172 0.2273 0.0194 -0.2647 413 THR A N 2059 C CA . THR A 274 ? 0.6343 0.7937 0.7895 0.1985 0.0269 -0.2406 413 THR A CA 2060 C C . THR A 274 ? 0.6284 0.7264 0.7638 0.1939 0.0097 -0.2217 413 THR A C 2061 O O . THR A 274 ? 0.6724 0.7297 0.7969 0.2060 -0.0039 -0.2286 413 THR A O 2062 C CB . THR A 274 ? 0.6459 0.8148 0.7808 0.1873 0.0420 -0.2480 413 THR A CB 2063 O OG1 . THR A 274 ? 0.6342 0.8637 0.7842 0.1857 0.0609 -0.2615 413 THR A OG1 2064 C CG2 . THR A 274 ? 0.6092 0.7573 0.7195 0.1602 0.0460 -0.2235 413 THR A CG2 2065 N N . ILE A 275 ? 0.5863 0.6782 0.7169 0.1759 0.0101 -0.1981 414 ILE A N 2066 C CA . ILE A 275 ? 0.6252 0.6665 0.7356 0.1667 -0.0017 -0.1788 414 ILE A CA 2067 C C . ILE A 275 ? 0.6098 0.6434 0.6987 0.1455 0.0082 -0.1689 414 ILE A C 2068 O O . ILE A 275 ? 0.6284 0.6898 0.7171 0.1300 0.0214 -0.1612 414 ILE A O 2069 C CB . ILE A 275 ? 0.6166 0.6551 0.7321 0.1604 -0.0072 -0.1602 414 ILE A CB 2070 C CG1 . ILE A 275 ? 0.6548 0.7051 0.7932 0.1814 -0.0183 -0.1701 414 ILE A CG1 2071 C CG2 . ILE A 275 ? 0.6064 0.5962 0.6999 0.1500 -0.0172 -0.1410 414 ILE A CG2 2072 C CD1 . ILE A 275 ? 0.6134 0.6675 0.7573 0.1750 -0.0231 -0.1540 414 ILE A CD1 2073 N N . THR A 276 ? 0.6116 0.6065 0.6826 0.1449 0.0003 -0.1695 415 THR A N 2074 C CA . THR A 276 ? 0.5820 0.5678 0.6340 0.1263 0.0065 -0.1612 415 THR A CA 2075 C C . THR A 276 ? 0.5938 0.5426 0.6342 0.1140 -0.0027 -0.1409 415 THR A C 2076 O O . THR A 276 ? 0.6046 0.5149 0.6370 0.1187 -0.0161 -0.1410 415 THR A O 2077 C CB . THR A 276 ? 0.6761 0.6504 0.7163 0.1327 0.0052 -0.1794 415 THR A CB 2078 O OG1 . THR A 276 ? 0.6263 0.6411 0.6755 0.1422 0.0171 -0.1989 415 THR A OG1 2079 C CG2 . THR A 276 ? 0.7108 0.6724 0.7313 0.1135 0.0081 -0.1701 415 THR A CG2 2080 N N . LEU A 277 ? 0.5302 0.4905 0.5693 0.0980 0.0044 -0.1238 416 LEU A N 2081 C CA . LEU A 277 ? 0.5491 0.4823 0.5786 0.0855 -0.0013 -0.1055 416 LEU A CA 2082 C C . LEU A 277 ? 0.5030 0.4244 0.5194 0.0728 -0.0003 -0.1035 416 LEU A C 2083 O O . LEU A 277 ? 0.5296 0.4724 0.5433 0.0666 0.0086 -0.1068 416 LEU A O 2084 C CB . LEU A 277 ? 0.5091 0.4603 0.5430 0.0756 0.0055 -0.0903 416 LEU A CB 2085 C CG . LEU A 277 ? 0.5118 0.4832 0.5598 0.0846 0.0061 -0.0915 416 LEU A CG 2086 C CD1 . LEU A 277 ? 0.4307 0.4131 0.4784 0.0727 0.0114 -0.0765 416 LEU A CD1 2087 C CD2 . LEU A 277 ? 0.5097 0.4573 0.5600 0.0983 -0.0076 -0.0932 416 LEU A CD2 2088 N N . PRO A 278 ? 0.5387 0.4257 0.5461 0.0679 -0.0104 -0.0977 417 PRO A N 2089 C CA . PRO A 278 ? 0.5744 0.4537 0.5723 0.0538 -0.0103 -0.0948 417 PRO A CA 2090 C C . PRO A 278 ? 0.5403 0.4359 0.5407 0.0391 -0.0030 -0.0787 417 PRO A C 2091 O O . PRO A 278 ? 0.5266 0.4207 0.5306 0.0365 -0.0026 -0.0664 417 PRO A O 2092 C CB . PRO A 278 ? 0.5781 0.4162 0.5677 0.0511 -0.0239 -0.0920 417 PRO A CB 2093 C CG . PRO A 278 ? 0.6495 0.4753 0.6420 0.0572 -0.0290 -0.0836 417 PRO A CG 2094 C CD . PRO A 278 ? 0.6026 0.4561 0.6070 0.0729 -0.0232 -0.0928 417 PRO A CD 2095 N N . CYS A 279 ? 0.4991 0.4095 0.4963 0.0308 0.0019 -0.0795 418 CYS A N 2096 C CA . CYS A 279 ? 0.5344 0.4602 0.5346 0.0194 0.0072 -0.0665 418 CYS A CA 2097 C C . CYS A 279 ? 0.4550 0.3746 0.4509 0.0078 0.0030 -0.0645 418 CYS A C 2098 O O . CYS A 279 ? 0.4738 0.3817 0.4620 0.0080 -0.0024 -0.0746 418 CYS A O 2099 C CB . CYS A 279 ? 0.4709 0.4242 0.4720 0.0206 0.0161 -0.0680 418 CYS A CB 2100 S SG . CYS A 279 ? 0.5451 0.5141 0.5549 0.0314 0.0216 -0.0704 418 CYS A SG 2101 N N . LYS A 280 ? 0.4615 0.3902 0.4631 -0.0016 0.0048 -0.0527 419 LYS A N 2102 C CA . LYS A 280 ? 0.4917 0.4240 0.4933 -0.0119 0.0011 -0.0512 419 LYS A CA 2103 C C . LYS A 280 ? 0.4754 0.4299 0.4821 -0.0143 0.0057 -0.0439 419 LYS A C 2104 O O . LYS A 280 ? 0.4507 0.4136 0.4630 -0.0114 0.0112 -0.0371 419 LYS A O 2105 C CB . LYS A 280 ? 0.6125 0.5308 0.6191 -0.0223 -0.0047 -0.0451 419 LYS A CB 2106 C CG . LYS A 280 ? 0.7422 0.6697 0.7588 -0.0269 0.0003 -0.0324 419 LYS A CG 2107 C CD . LYS A 280 ? 0.9120 0.8249 0.9312 -0.0391 -0.0039 -0.0258 419 LYS A CD 2108 C CE . LYS A 280 ? 0.9632 0.8824 0.9893 -0.0518 -0.0094 -0.0264 419 LYS A CE 2109 N NZ . LYS A 280 ? 0.9709 0.8902 1.0053 -0.0670 -0.0093 -0.0166 419 LYS A NZ 2110 N N . ILE A 281 ? 0.4249 0.3864 0.4280 -0.0190 0.0020 -0.0459 420 ILE A N 2111 C CA . ILE A 281 ? 0.3938 0.3715 0.4020 -0.0213 0.0024 -0.0387 420 ILE A CA 2112 C C . ILE A 281 ? 0.3961 0.3780 0.4186 -0.0288 -0.0018 -0.0333 420 ILE A C 2113 O O . ILE A 281 ? 0.4359 0.4104 0.4591 -0.0356 -0.0083 -0.0367 420 ILE A O 2114 C CB . ILE A 281 ? 0.3682 0.3502 0.3633 -0.0226 -0.0015 -0.0427 420 ILE A CB 2115 C CG1 . ILE A 281 ? 0.4326 0.4162 0.4143 -0.0173 0.0053 -0.0478 420 ILE A CG1 2116 C CG2 . ILE A 281 ? 0.3703 0.3639 0.3709 -0.0244 -0.0054 -0.0350 420 ILE A CG2 2117 C CD1 . ILE A 281 ? 0.4860 0.4729 0.4490 -0.0206 0.0030 -0.0514 420 ILE A CD1 2118 N N . LYS A 282 ? 0.3553 0.3500 0.3895 -0.0279 0.0019 -0.0259 421 LYS A N 2119 C CA . LYS A 282 ? 0.3501 0.3557 0.4008 -0.0351 -0.0001 -0.0219 421 LYS A CA 2120 C C . LYS A 282 ? 0.3374 0.3616 0.3974 -0.0326 -0.0039 -0.0203 421 LYS A C 2121 O O . LYS A 282 ? 0.3227 0.3503 0.3791 -0.0248 -0.0017 -0.0184 421 LYS A O 2122 C CB . LYS A 282 ? 0.3983 0.4054 0.4561 -0.0362 0.0078 -0.0159 421 LYS A CB 2123 C CG . LYS A 282 ? 0.4316 0.4178 0.4825 -0.0417 0.0075 -0.0158 421 LYS A CG 2124 C CD . LYS A 282 ? 0.4227 0.4073 0.4747 -0.0433 0.0146 -0.0082 421 LYS A CD 2125 C CE . LYS A 282 ? 0.3908 0.3988 0.4589 -0.0510 0.0191 -0.0029 421 LYS A CE 2126 N NZ . LYS A 282 ? 0.4163 0.4309 0.4956 -0.0638 0.0133 -0.0038 421 LYS A NZ 2127 N N . GLN A 283 ? 0.3312 0.3660 0.4036 -0.0393 -0.0113 -0.0215 422 GLN A N 2128 C CA . GLN A 283 ? 0.3686 0.4227 0.4542 -0.0359 -0.0175 -0.0208 422 GLN A CA 2129 C C . GLN A 283 ? 0.3897 0.4652 0.4965 -0.0342 -0.0104 -0.0177 422 GLN A C 2130 O O . GLN A 283 ? 0.3701 0.4592 0.4858 -0.0253 -0.0124 -0.0178 422 GLN A O 2131 C CB . GLN A 283 ? 0.3506 0.4108 0.4437 -0.0438 -0.0295 -0.0244 422 GLN A CB 2132 C CG . GLN A 283 ? 0.3986 0.4410 0.4688 -0.0442 -0.0383 -0.0288 422 GLN A CG 2133 C CD . GLN A 283 ? 0.4376 0.4827 0.5133 -0.0538 -0.0506 -0.0332 422 GLN A CD 2134 O OE1 . GLN A 283 ? 0.5211 0.5493 0.5850 -0.0607 -0.0527 -0.0380 422 GLN A OE1 2135 N NE2 . GLN A 283 ? 0.3993 0.4657 0.4944 -0.0537 -0.0600 -0.0326 422 GLN A NE2 2136 N N . ILE A 284 ? 0.3940 0.4716 0.5074 -0.0428 -0.0028 -0.0153 423 ILE A N 2137 C CA . ILE A 284 ? 0.3415 0.4424 0.4731 -0.0433 0.0060 -0.0127 423 ILE A CA 2138 C C . ILE A 284 ? 0.3735 0.4626 0.4920 -0.0392 0.0171 -0.0089 423 ILE A C 2139 O O . ILE A 284 ? 0.4111 0.4798 0.5160 -0.0449 0.0197 -0.0061 423 ILE A O 2140 C CB . ILE A 284 ? 0.3947 0.5103 0.5430 -0.0593 0.0071 -0.0113 423 ILE A CB 2141 C CG1 . ILE A 284 ? 0.4488 0.5799 0.6132 -0.0628 -0.0056 -0.0159 423 ILE A CG1 2142 C CG2 . ILE A 284 ? 0.3793 0.5215 0.5435 -0.0614 0.0195 -0.0085 423 ILE A CG2 2143 C CD1 . ILE A 284 ? 0.4237 0.5633 0.6016 -0.0818 -0.0078 -0.0148 423 ILE A CD1 2144 N N . ILE A 285 ? 0.3267 0.4266 0.4483 -0.0281 0.0215 -0.0094 424 ILE A N 2145 C CA . ILE A 285 ? 0.3290 0.4162 0.4359 -0.0226 0.0295 -0.0067 424 ILE A CA 2146 C C . ILE A 285 ? 0.3328 0.4407 0.4493 -0.0184 0.0385 -0.0070 424 ILE A C 2147 O O . ILE A 285 ? 0.3604 0.4939 0.4962 -0.0152 0.0379 -0.0110 424 ILE A O 2148 C CB . ILE A 285 ? 0.3674 0.4388 0.4600 -0.0117 0.0247 -0.0083 424 ILE A CB 2149 C CG1 . ILE A 285 ? 0.3982 0.4824 0.4993 -0.0008 0.0209 -0.0114 424 ILE A CG1 2150 C CG2 . ILE A 285 ? 0.3603 0.4172 0.4434 -0.0150 0.0163 -0.0099 424 ILE A CG2 2151 C CD1 . ILE A 285 ? 0.4046 0.4710 0.4899 0.0068 0.0154 -0.0112 424 ILE A CD1 2152 N N . ASN A 286 ? 0.2940 0.3916 0.3967 -0.0175 0.0463 -0.0036 425 ASN A N 2153 C CA . ASN A 286 ? 0.3562 0.4689 0.4611 -0.0105 0.0546 -0.0055 425 ASN A CA 2154 C C . ASN A 286 ? 0.3493 0.4504 0.4455 0.0040 0.0495 -0.0092 425 ASN A C 2155 O O . ASN A 286 ? 0.3919 0.4698 0.4717 0.0052 0.0464 -0.0067 425 ASN A O 2156 C CB . ASN A 286 ? 0.3477 0.4527 0.4381 -0.0180 0.0640 0.0005 425 ASN A CB 2157 C CG . ASN A 286 ? 0.3753 0.4906 0.4724 -0.0351 0.0693 0.0057 425 ASN A CG 2158 O OD1 . ASN A 286 ? 0.4227 0.5688 0.5391 -0.0394 0.0745 0.0031 425 ASN A OD1 2159 N ND2 . ASN A 286 ? 0.3819 0.4716 0.4637 -0.0451 0.0670 0.0127 425 ASN A ND2 2160 N N . MET A 287 ? 0.3610 0.4777 0.4688 0.0149 0.0473 -0.0155 426 MET A N 2161 C CA . MET A 287 ? 0.3658 0.4669 0.4640 0.0272 0.0400 -0.0183 426 MET A CA 2162 C C . MET A 287 ? 0.4140 0.5023 0.4949 0.0304 0.0458 -0.0175 426 MET A C 2163 O O . MET A 287 ? 0.3783 0.4797 0.4598 0.0310 0.0553 -0.0193 426 MET A O 2164 C CB . MET A 287 ? 0.3650 0.4824 0.4792 0.0398 0.0342 -0.0261 426 MET A CB 2165 C CG . MET A 287 ? 0.3625 0.4880 0.4912 0.0381 0.0239 -0.0266 426 MET A CG 2166 S SD . MET A 287 ? 0.4285 0.5782 0.5814 0.0546 0.0158 -0.0368 426 MET A SD 2167 C CE . MET A 287 ? 1.5728 1.6870 1.7063 0.0656 -0.0014 -0.0358 426 MET A CE 2168 N N . TRP A 288 ? 0.4368 0.5014 0.5020 0.0315 0.0403 -0.0149 427 TRP A N 2169 C CA . TRP A 288 ? 0.4377 0.4897 0.4871 0.0339 0.0435 -0.0143 427 TRP A CA 2170 C C . TRP A 288 ? 0.4407 0.4974 0.4896 0.0456 0.0438 -0.0214 427 TRP A C 2171 O O . TRP A 288 ? 0.4559 0.5077 0.4925 0.0479 0.0480 -0.0226 427 TRP A O 2172 C CB . TRP A 288 ? 0.3878 0.4187 0.4250 0.0323 0.0367 -0.0112 427 TRP A CB 2173 C CG . TRP A 288 ? 0.4662 0.4887 0.5029 0.0371 0.0267 -0.0129 427 TRP A CG 2174 C CD1 . TRP A 288 ? 0.4459 0.4663 0.4855 0.0337 0.0202 -0.0111 427 TRP A CD1 2175 C CD2 . TRP A 288 ? 0.4701 0.4814 0.4997 0.0451 0.0206 -0.0163 427 TRP A CD2 2176 N NE1 . TRP A 288 ? 0.4724 0.4803 0.5060 0.0383 0.0104 -0.0116 427 TRP A NE1 2177 C CE2 . TRP A 288 ? 0.4842 0.4852 0.5123 0.0453 0.0100 -0.0149 427 TRP A CE2 2178 C CE3 . TRP A 288 ? 0.4198 0.4262 0.4416 0.0516 0.0220 -0.0204 427 TRP A CE3 2179 C CZ2 . TRP A 288 ? 0.4309 0.4145 0.4505 0.0512 0.0000 -0.0166 427 TRP A CZ2 2180 C CZ3 . TRP A 288 ? 0.5256 0.5159 0.5402 0.0585 0.0124 -0.0238 427 TRP A CZ3 2181 C CH2 . TRP A 288 ? 0.5001 0.4780 0.5139 0.0580 0.0010 -0.0215 427 TRP A CH2 2182 N N . GLN A 289 ? 0.3764 0.4412 0.4376 0.0539 0.0377 -0.0269 428 GLN A N 2183 C CA . GLN A 289 ? 0.4368 0.5068 0.4999 0.0678 0.0369 -0.0363 428 GLN A CA 2184 C C . GLN A 289 ? 0.4794 0.5762 0.5489 0.0686 0.0511 -0.0411 428 GLN A C 2185 O O . GLN A 289 ? 0.5126 0.6160 0.5805 0.0803 0.0537 -0.0506 428 GLN A O 2186 C CB . GLN A 289 ? 0.4492 0.5213 0.5255 0.0782 0.0251 -0.0416 428 GLN A CB 2187 C CG . GLN A 289 ? 0.4972 0.5413 0.5625 0.0754 0.0109 -0.0355 428 GLN A CG 2188 C CD . GLN A 289 ? 0.5503 0.5989 0.6221 0.0650 0.0084 -0.0289 428 GLN A CD 2189 O OE1 . GLN A 289 ? 0.5011 0.5579 0.5742 0.0540 0.0171 -0.0245 428 GLN A OE1 2190 N NE2 . GLN A 289 ? 0.5329 0.5732 0.6066 0.0688 -0.0052 -0.0285 428 GLN A NE2 2191 N N . GLY A 290 ? 0.4800 0.5910 0.5547 0.0555 0.0603 -0.0349 429 GLY A N 2192 C CA . GLY A 290 ? 0.4584 0.5940 0.5355 0.0512 0.0750 -0.0365 429 GLY A CA 2193 C C . GLY A 290 ? 0.4776 0.6502 0.5814 0.0563 0.0796 -0.0451 429 GLY A C 2194 O O . GLY A 290 ? 0.4662 0.6664 0.5747 0.0540 0.0934 -0.0490 429 GLY A O 2195 N N . THR A 291 ? 0.4199 0.5946 0.5411 0.0626 0.0679 -0.0481 430 THR A N 2196 C CA . THR A 291 ? 0.4577 0.6671 0.6079 0.0718 0.0677 -0.0582 430 THR A CA 2197 C C . THR A 291 ? 0.4806 0.7195 0.6540 0.0578 0.0721 -0.0546 430 THR A C 2198 O O . THR A 291 ? 0.4960 0.7709 0.6975 0.0641 0.0732 -0.0635 430 THR A O 2199 C CB . THR A 291 ? 0.5105 0.7053 0.6670 0.0877 0.0491 -0.0637 430 THR A CB 2200 O OG1 . THR A 291 ? 0.4991 0.6636 0.6432 0.0787 0.0382 -0.0530 430 THR A OG1 2201 C CG2 . THR A 291 ? 0.5683 0.7438 0.7099 0.1048 0.0445 -0.0721 430 THR A CG2 2202 N N . GLY A 292 ? 0.3928 0.6169 0.5562 0.0395 0.0734 -0.0426 431 GLY A N 2203 C CA . GLY A 292 ? 0.3494 0.5960 0.5324 0.0243 0.0755 -0.0388 431 GLY A CA 2204 C C . GLY A 292 ? 0.3707 0.5902 0.5459 0.0142 0.0643 -0.0303 431 GLY A C 2205 O O . GLY A 292 ? 0.3574 0.5426 0.5084 0.0127 0.0610 -0.0243 431 GLY A O 2206 N N . GLN A 293 ? 0.3233 0.5604 0.5200 0.0076 0.0582 -0.0310 432 GLN A N 2207 C CA . GLN A 293 ? 0.3233 0.5376 0.5123 -0.0033 0.0485 -0.0244 432 GLN A CA 2208 C C . GLN A 293 ? 0.3339 0.5452 0.5314 0.0065 0.0319 -0.0287 432 GLN A C 2209 O O . GLN A 293 ? 0.3550 0.5924 0.5752 0.0169 0.0272 -0.0364 432 GLN A O 2210 C CB . GLN A 293 ? 0.3212 0.5520 0.5224 -0.0238 0.0537 -0.0200 432 GLN A CB 2211 C CG . GLN A 293 ? 0.4330 0.6536 0.6168 -0.0378 0.0667 -0.0118 432 GLN A CG 2212 C CD . GLN A 293 ? 0.5163 0.7654 0.7053 -0.0360 0.0824 -0.0144 432 GLN A CD 2213 O OE1 . GLN A 293 ? 0.5051 0.7959 0.7205 -0.0389 0.0889 -0.0196 432 GLN A OE1 2214 N NE2 . GLN A 293 ? 0.4893 0.7178 0.6530 -0.0313 0.0887 -0.0115 432 GLN A NE2 2215 N N . ALA A 294 ? 0.3468 0.5267 0.5252 0.0036 0.0226 -0.0242 433 ALA A N 2216 C CA . ALA A 294 ? 0.3315 0.5039 0.5110 0.0098 0.0061 -0.0263 433 ALA A CA 2217 C C . ALA A 294 ? 0.4001 0.5601 0.5729 -0.0038 -0.0004 -0.0229 433 ALA A C 2218 O O . ALA A 294 ? 0.3945 0.5360 0.5514 -0.0137 0.0056 -0.0185 433 ALA A O 2219 C CB . ALA A 294 ? 0.3453 0.4896 0.5026 0.0213 0.0002 -0.0253 433 ALA A CB 2220 N N . MET A 295 ? 0.3050 0.4737 0.4892 -0.0033 -0.0141 -0.0258 434 MET A N 2221 C CA . MET A 295 ? 0.3589 0.5122 0.5323 -0.0144 -0.0227 -0.0242 434 MET A CA 2222 C C . MET A 295 ? 0.3874 0.5208 0.5430 -0.0072 -0.0377 -0.0242 434 MET A C 2223 O O . MET A 295 ? 0.3468 0.4901 0.5128 0.0028 -0.0495 -0.0268 434 MET A O 2224 C CB . MET A 295 ? 0.3436 0.5231 0.5426 -0.0254 -0.0272 -0.0269 434 MET A CB 2225 C CG . MET A 295 ? 0.3722 0.5350 0.5595 -0.0348 -0.0399 -0.0272 434 MET A CG 2226 S SD . MET A 295 ? 0.4225 0.6088 0.6355 -0.0539 -0.0435 -0.0292 434 MET A SD 2227 C CE . MET A 295 ? 0.3923 0.6243 0.6448 -0.0451 -0.0532 -0.0351 434 MET A CE 2228 N N . TYR A 296 ? 0.3677 0.4735 0.4960 -0.0125 -0.0375 -0.0217 435 TYR A N 2229 C CA . TYR A 296 ? 0.3915 0.4774 0.4970 -0.0091 -0.0493 -0.0206 435 TYR A CA 2230 C C . TYR A 296 ? 0.4688 0.5483 0.5655 -0.0189 -0.0587 -0.0229 435 TYR A C 2231 O O . TYR A 296 ? 0.3820 0.4664 0.4870 -0.0288 -0.0553 -0.0252 435 TYR A O 2232 C CB . TYR A 296 ? 0.4054 0.4683 0.4850 -0.0075 -0.0411 -0.0171 435 TYR A CB 2233 C CG . TYR A 296 ? 0.3797 0.4442 0.4635 0.0026 -0.0358 -0.0152 435 TYR A CG 2234 C CD1 . TYR A 296 ? 0.3982 0.4532 0.4736 0.0113 -0.0458 -0.0132 435 TYR A CD1 2235 C CD2 . TYR A 296 ? 0.3436 0.4166 0.4377 0.0031 -0.0222 -0.0155 435 TYR A CD2 2236 C CE1 . TYR A 296 ? 0.4091 0.4625 0.4874 0.0210 -0.0427 -0.0128 435 TYR A CE1 2237 C CE2 . TYR A 296 ? 0.3496 0.4235 0.4457 0.0127 -0.0180 -0.0152 435 TYR A CE2 2238 C CZ . TYR A 296 ? 0.4053 0.4692 0.4942 0.0220 -0.0285 -0.0145 435 TYR A CZ 2239 O OH . TYR A 296 ? 0.4138 0.4749 0.5032 0.0319 -0.0262 -0.0154 435 TYR A OH 2240 N N . ALA A 297 ? 0.4142 0.4802 0.4913 -0.0169 -0.0715 -0.0220 436 ALA A N 2241 C CA . ALA A 297 ? 0.4189 0.4755 0.4808 -0.0257 -0.0807 -0.0250 436 ALA A CA 2242 C C . ALA A 297 ? 0.3958 0.4349 0.4362 -0.0321 -0.0689 -0.0270 436 ALA A C 2243 O O . ALA A 297 ? 0.3938 0.4265 0.4276 -0.0288 -0.0564 -0.0247 436 ALA A O 2244 C CB . ALA A 297 ? 0.4926 0.5367 0.5328 -0.0222 -0.0965 -0.0224 436 ALA A CB 2245 N N . PRO A 298 ? 0.4346 0.4660 0.4645 -0.0404 -0.0741 -0.0325 437 PRO A N 2246 C CA . PRO A 298 ? 0.4656 0.4802 0.4756 -0.0439 -0.0644 -0.0370 437 PRO A CA 2247 C C . PRO A 298 ? 0.4894 0.4917 0.4699 -0.0404 -0.0602 -0.0359 437 PRO A C 2248 O O . PRO A 298 ? 0.5158 0.5169 0.4853 -0.0381 -0.0678 -0.0308 437 PRO A O 2249 C CB . PRO A 298 ? 0.4779 0.4865 0.4830 -0.0525 -0.0746 -0.0446 437 PRO A CB 2250 C CG . PRO A 298 ? 0.5299 0.5502 0.5442 -0.0537 -0.0912 -0.0431 437 PRO A CG 2251 C CD . PRO A 298 ? 0.4373 0.4765 0.4767 -0.0464 -0.0896 -0.0363 437 PRO A CD 2252 N N . PRO A 299 ? 0.5054 0.4986 0.4731 -0.0403 -0.0486 -0.0406 438 PRO A N 2253 C CA . PRO A 299 ? 0.5158 0.5042 0.4608 -0.0382 -0.0410 -0.0394 438 PRO A CA 2254 C C . PRO A 299 ? 0.5179 0.4997 0.4336 -0.0427 -0.0493 -0.0404 438 PRO A C 2255 O O . PRO A 299 ? 0.5068 0.4842 0.4146 -0.0468 -0.0593 -0.0463 438 PRO A O 2256 C CB . PRO A 299 ? 0.5420 0.5258 0.4839 -0.0365 -0.0292 -0.0478 438 PRO A CB 2257 C CG . PRO A 299 ? 0.5046 0.4867 0.4679 -0.0373 -0.0305 -0.0500 438 PRO A CG 2258 C CD . PRO A 299 ? 0.4912 0.4781 0.4648 -0.0426 -0.0436 -0.0478 438 PRO A CD 2259 N N . ILE A 300 ? 0.5709 0.5509 0.4687 -0.0433 -0.0459 -0.0342 439 ILE A N 2260 C CA . ILE A 300 ? 0.5932 0.5658 0.4566 -0.0497 -0.0509 -0.0341 439 ILE A CA 2261 C C . ILE A 300 ? 0.5557 0.5276 0.4016 -0.0521 -0.0430 -0.0472 439 ILE A C 2262 O O . ILE A 300 ? 0.5586 0.5346 0.4173 -0.0476 -0.0318 -0.0549 439 ILE A O 2263 C CB . ILE A 300 ? 0.6436 0.6143 0.4900 -0.0528 -0.0454 -0.0244 439 ILE A CB 2264 C CG1 . ILE A 300 ? 0.5980 0.5780 0.4527 -0.0507 -0.0268 -0.0279 439 ILE A CG1 2265 C CG2 . ILE A 300 ? 0.5867 0.5529 0.4455 -0.0491 -0.0560 -0.0127 439 ILE A CG2 2266 C CD1 . ILE A 300 ? 0.6724 0.6521 0.5134 -0.0561 -0.0211 -0.0183 439 ILE A CD1 2267 N N . ASP A 301 ? 0.5672 0.5327 0.3820 -0.0582 -0.0498 -0.0505 440 ASP A N 2268 C CA . ASP A 301 ? 0.6357 0.6012 0.4293 -0.0595 -0.0417 -0.0649 440 ASP A CA 2269 C C . ASP A 301 ? 0.6581 0.6345 0.4380 -0.0606 -0.0231 -0.0669 440 ASP A C 2270 O O . ASP A 301 ? 0.6655 0.6460 0.4422 -0.0645 -0.0189 -0.0548 440 ASP A O 2271 C CB . ASP A 301 ? 0.7714 0.7274 0.5323 -0.0664 -0.0547 -0.0682 440 ASP A CB 2272 C CG . ASP A 301 ? 0.8450 0.7936 0.6206 -0.0659 -0.0729 -0.0703 440 ASP A CG 2273 O OD1 . ASP A 301 ? 0.9218 0.8639 0.6823 -0.0707 -0.0896 -0.0645 440 ASP A OD1 2274 O OD2 . ASP A 301 ? 0.8170 0.7665 0.6195 -0.0616 -0.0712 -0.0772 440 ASP A OD2 2275 N N . GLY A 302 ? 0.6588 0.6403 0.4312 -0.0570 -0.0128 -0.0830 441 GLY A N 2276 C CA . GLY A 302 ? 0.7253 0.7233 0.4850 -0.0582 0.0051 -0.0880 441 GLY A CA 2277 C C . GLY A 302 ? 0.6968 0.7075 0.4864 -0.0495 0.0180 -0.0907 441 GLY A C 2278 O O . GLY A 302 ? 0.6707 0.6746 0.4884 -0.0414 0.0139 -0.0912 441 GLY A O 2279 N N . LYS A 303 ? 0.6570 0.6873 0.4400 -0.0522 0.0334 -0.0923 442 LYS A N 2280 C CA . LYS A 303 ? 0.6575 0.7026 0.4683 -0.0436 0.0449 -0.0961 442 LYS A CA 2281 C C . LYS A 303 ? 0.6224 0.6652 0.4504 -0.0472 0.0420 -0.0780 442 LYS A C 2282 O O . LYS A 303 ? 0.7075 0.7553 0.5222 -0.0583 0.0445 -0.0663 442 LYS A O 2283 C CB . LYS A 303 ? 0.7709 0.8436 0.5721 -0.0451 0.0628 -0.1068 442 LYS A CB 2284 C CG . LYS A 303 ? 0.9955 1.0732 0.7827 -0.0375 0.0674 -0.1292 442 LYS A CG 2285 C CD . LYS A 303 ? 1.1579 1.2689 0.9321 -0.0411 0.0866 -0.1397 442 LYS A CD 2286 C CE . LYS A 303 ? 1.1937 1.3086 0.9469 -0.0340 0.0907 -0.1631 442 LYS A CE 2287 N NZ . LYS A 303 ? 1.2288 1.3832 0.9788 -0.0330 0.1119 -0.1778 442 LYS A NZ 2288 N N . ILE A 304 ? 0.6024 0.6354 0.4574 -0.0385 0.0359 -0.0756 443 ILE A N 2289 C CA . ILE A 304 ? 0.5841 0.6163 0.4575 -0.0389 0.0345 -0.0619 443 ILE A CA 2290 C C . ILE A 304 ? 0.5695 0.6178 0.4616 -0.0324 0.0461 -0.0672 443 ILE A C 2291 O O . ILE A 304 ? 0.5211 0.5691 0.4281 -0.0215 0.0476 -0.0780 443 ILE A O 2292 C CB . ILE A 304 ? 0.4845 0.5009 0.3766 -0.0338 0.0229 -0.0565 443 ILE A CB 2293 C CG1 . ILE A 304 ? 0.5090 0.5129 0.3869 -0.0389 0.0097 -0.0536 443 ILE A CG1 2294 C CG2 . ILE A 304 ? 0.4475 0.4640 0.3553 -0.0334 0.0223 -0.0440 443 ILE A CG2 2295 C CD1 . ILE A 304 ? 0.5154 0.5098 0.4128 -0.0348 -0.0003 -0.0532 443 ILE A CD1 2296 N N . ASN A 305 ? 0.5072 0.5681 0.3984 -0.0395 0.0527 -0.0595 444 ASN A N 2297 C CA . ASN A 305 ? 0.4965 0.5781 0.4049 -0.0347 0.0637 -0.0658 444 ASN A CA 2298 C C . ASN A 305 ? 0.5148 0.6010 0.4321 -0.0411 0.0647 -0.0531 444 ASN A C 2299 O O . ASN A 305 ? 0.5166 0.6002 0.4171 -0.0545 0.0635 -0.0418 444 ASN A O 2300 C CB . ASN A 305 ? 0.5530 0.6587 0.4485 -0.0377 0.0763 -0.0787 444 ASN A CB 2301 C CG . ASN A 305 ? 0.5429 0.6772 0.4584 -0.0338 0.0879 -0.0857 444 ASN A CG 2302 O OD1 . ASN A 305 ? 0.5326 0.6722 0.4686 -0.0186 0.0889 -0.0980 444 ASN A OD1 2303 N ND2 . ASN A 305 ? 0.5690 0.7213 0.4787 -0.0482 0.0954 -0.0777 444 ASN A ND2 2304 N N . CYS A 306 ? 0.4627 0.5526 0.4044 -0.0318 0.0654 -0.0548 445 CYS A N 2305 C CA . CYS A 306 ? 0.4782 0.5750 0.4303 -0.0365 0.0667 -0.0461 445 CYS A CA 2306 C C . CYS A 306 ? 0.4517 0.5716 0.4254 -0.0284 0.0742 -0.0566 445 CYS A C 2307 O O . CYS A 306 ? 0.4529 0.5682 0.4412 -0.0142 0.0715 -0.0644 445 CYS A O 2308 C CB . CYS A 306 ? 0.4859 0.5606 0.4461 -0.0326 0.0564 -0.0358 445 CYS A CB 2309 S SG . CYS A 306 ? 0.5338 0.5842 0.4755 -0.0392 0.0451 -0.0240 445 CYS A SG 2310 N N . VAL A 307 ? 0.4464 0.5909 0.4221 -0.0380 0.0826 -0.0564 446 VAL A N 2311 C CA . VAL A 307 ? 0.4604 0.6299 0.4608 -0.0306 0.0877 -0.0651 446 VAL A CA 2312 C C . VAL A 307 ? 0.4347 0.5981 0.4431 -0.0369 0.0821 -0.0528 446 VAL A C 2313 O O . VAL A 307 ? 0.3943 0.5552 0.3895 -0.0533 0.0821 -0.0416 446 VAL A O 2314 C CB . VAL A 307 ? 0.4661 0.6750 0.4683 -0.0379 0.1019 -0.0750 446 VAL A CB 2315 C CG1 . VAL A 307 ? 0.4355 0.6730 0.4688 -0.0270 0.1052 -0.0861 446 VAL A CG1 2316 C CG2 . VAL A 307 ? 0.4827 0.6967 0.4702 -0.0339 0.1081 -0.0874 446 VAL A CG2 2317 N N . SER A 308 ? 0.4211 0.5790 0.4482 -0.0241 0.0761 -0.0548 447 SER A N 2318 C CA . SER A 308 ? 0.4259 0.5748 0.4591 -0.0278 0.0693 -0.0447 447 SER A CA 2319 C C . SER A 308 ? 0.3894 0.5615 0.4469 -0.0207 0.0701 -0.0523 447 SER A C 2320 O O . SER A 308 ? 0.4462 0.6321 0.5173 -0.0072 0.0724 -0.0651 447 SER A O 2321 C CB . SER A 308 ? 0.4072 0.5234 0.4360 -0.0191 0.0595 -0.0384 447 SER A CB 2322 O OG . SER A 308 ? 0.3956 0.4932 0.4058 -0.0241 0.0573 -0.0325 447 SER A OG 2323 N N . ASN A 309 ? 0.3758 0.5514 0.4391 -0.0291 0.0665 -0.0453 448 ASN A N 2324 C CA . ASN A 309 ? 0.3165 0.5089 0.4032 -0.0209 0.0629 -0.0513 448 ASN A CA 2325 C C . ASN A 309 ? 0.3337 0.4967 0.4192 -0.0090 0.0517 -0.0469 448 ASN A C 2326 O O . ASN A 309 ? 0.3406 0.4785 0.4118 -0.0146 0.0464 -0.0365 448 ASN A O 2327 C CB . ASN A 309 ? 0.4412 0.6518 0.5350 -0.0370 0.0631 -0.0462 448 ASN A CB 2328 C CG . ASN A 309 ? 0.5356 0.7761 0.6277 -0.0539 0.0751 -0.0477 448 ASN A CG 2329 O OD1 . ASN A 309 ? 0.3879 0.6581 0.4907 -0.0486 0.0848 -0.0599 448 ASN A OD1 2330 N ND2 . ASN A 309 ? 0.8359 1.0678 0.9127 -0.0748 0.0743 -0.0353 448 ASN A ND2 2331 N N . ILE A 310 ? 0.3560 0.5213 0.4552 0.0076 0.0476 -0.0552 449 ILE A N 2332 C CA . ILE A 310 ? 0.3166 0.4588 0.4146 0.0165 0.0369 -0.0506 449 ILE A CA 2333 C C . ILE A 310 ? 0.3908 0.5478 0.5010 0.0118 0.0317 -0.0494 449 ILE A C 2334 O O . ILE A 310 ? 0.3854 0.5731 0.5168 0.0147 0.0325 -0.0583 449 ILE A O 2335 C CB . ILE A 310 ? 0.3282 0.4625 0.4327 0.0345 0.0318 -0.0580 449 ILE A CB 2336 C CG1 . ILE A 310 ? 0.3972 0.5165 0.4900 0.0376 0.0360 -0.0601 449 ILE A CG1 2337 C CG2 . ILE A 310 ? 0.3524 0.4610 0.4502 0.0406 0.0209 -0.0509 449 ILE A CG2 2338 C CD1 . ILE A 310 ? 0.4465 0.5603 0.5465 0.0545 0.0313 -0.0704 449 ILE A CD1 2339 N N . THR A 311 ? 0.3142 0.4509 0.4121 0.0049 0.0259 -0.0397 450 THR A N 2340 C CA . THR A 311 ? 0.3242 0.4700 0.4298 -0.0021 0.0194 -0.0379 450 THR A CA 2341 C C . THR A 311 ? 0.3442 0.4668 0.4429 0.0070 0.0079 -0.0347 450 THR A C 2342 O O . THR A 311 ? 0.3416 0.4691 0.4461 0.0039 -0.0002 -0.0345 450 THR A O 2343 C CB . THR A 311 ? 0.3938 0.5350 0.4878 -0.0214 0.0214 -0.0298 450 THR A CB 2344 O OG1 . THR A 311 ? 0.3782 0.4861 0.4498 -0.0209 0.0199 -0.0224 450 THR A OG1 2345 C CG2 . THR A 311 ? 0.3580 0.5252 0.4565 -0.0337 0.0326 -0.0319 450 THR A CG2 2346 N N . GLY A 312 ? 0.3283 0.4260 0.4134 0.0167 0.0073 -0.0322 451 GLY A N 2347 C CA . GLY A 312 ? 0.4328 0.5078 0.5064 0.0241 -0.0015 -0.0284 451 GLY A CA 2348 C C . GLY A 312 ? 0.4226 0.4800 0.4880 0.0349 -0.0009 -0.0277 451 GLY A C 2349 O O . GLY A 312 ? 0.3935 0.4517 0.4594 0.0352 0.0063 -0.0293 451 GLY A O 2350 N N . ILE A 313 ? 0.3840 0.4244 0.4400 0.0422 -0.0092 -0.0249 452 ILE A N 2351 C CA . ILE A 313 ? 0.3787 0.3982 0.4230 0.0493 -0.0097 -0.0217 452 ILE A CA 2352 C C . ILE A 313 ? 0.3562 0.3540 0.3786 0.0479 -0.0126 -0.0142 452 ILE A C 2353 O O . ILE A 313 ? 0.4267 0.4234 0.4447 0.0482 -0.0201 -0.0137 452 ILE A O 2354 C CB . ILE A 313 ? 0.3950 0.4148 0.4487 0.0616 -0.0186 -0.0266 452 ILE A CB 2355 C CG1 . ILE A 313 ? 0.3694 0.4165 0.4470 0.0649 -0.0152 -0.0371 452 ILE A CG1 2356 C CG2 . ILE A 313 ? 0.4150 0.4077 0.4537 0.0663 -0.0204 -0.0219 452 ILE A CG2 2357 C CD1 . ILE A 313 ? 0.3864 0.4378 0.4778 0.0801 -0.0259 -0.0449 452 ILE A CD1 2358 N N . LEU A 314 ? 0.4038 0.3868 0.4129 0.0459 -0.0066 -0.0092 453 LEU A N 2359 C CA . LEU A 314 ? 0.4220 0.3880 0.4099 0.0447 -0.0072 -0.0030 453 LEU A CA 2360 C C . LEU A 314 ? 0.4557 0.4039 0.4322 0.0491 -0.0126 0.0018 453 LEU A C 2361 O O . LEU A 314 ? 0.4484 0.3912 0.4285 0.0498 -0.0108 0.0023 453 LEU A O 2362 C CB . LEU A 314 ? 0.4226 0.3873 0.4041 0.0389 0.0032 -0.0007 453 LEU A CB 2363 C CG . LEU A 314 ? 0.4806 0.4569 0.4704 0.0347 0.0063 -0.0043 453 LEU A CG 2364 C CD1 . LEU A 314 ? 0.4946 0.4709 0.4830 0.0314 0.0146 -0.0031 453 LEU A CD1 2365 C CD2 . LEU A 314 ? 0.4358 0.4088 0.4172 0.0346 0.0007 -0.0055 453 LEU A CD2 2366 N N . LEU A 315 ? 0.4594 0.3956 0.4196 0.0513 -0.0206 0.0054 454 LEU A N 2367 C CA . LEU A 315 ? 0.5038 0.4183 0.4486 0.0545 -0.0285 0.0118 454 LEU A CA 2368 C C . LEU A 315 ? 0.5527 0.4514 0.4680 0.0490 -0.0264 0.0201 454 LEU A C 2369 O O . LEU A 315 ? 0.5523 0.4556 0.4586 0.0476 -0.0252 0.0185 454 LEU A O 2370 C CB . LEU A 315 ? 0.5160 0.4295 0.4681 0.0645 -0.0443 0.0085 454 LEU A CB 2371 C CG . LEU A 315 ? 0.4893 0.4205 0.4708 0.0721 -0.0473 -0.0009 454 LEU A CG 2372 C CD1 . LEU A 315 ? 0.4760 0.4095 0.4653 0.0829 -0.0642 -0.0047 454 LEU A CD1 2373 C CD2 . LEU A 315 ? 0.4741 0.3938 0.4579 0.0740 -0.0447 -0.0008 454 LEU A CD2 2374 N N . THR A 316 ? 0.5078 0.3873 0.4069 0.0451 -0.0261 0.0285 455 THR A N 2375 C CA . THR A 316 ? 0.5593 0.4229 0.4269 0.0388 -0.0251 0.0376 455 THR A CA 2376 C C . THR A 316 ? 0.5580 0.3941 0.4072 0.0424 -0.0415 0.0452 455 THR A C 2377 O O . THR A 316 ? 0.6254 0.4474 0.4802 0.0446 -0.0479 0.0475 455 THR A O 2378 C CB . THR A 316 ? 0.6106 0.4755 0.4710 0.0272 -0.0098 0.0430 455 THR A CB 2379 O OG1 . THR A 316 ? 0.5643 0.4538 0.4431 0.0264 0.0025 0.0352 455 THR A OG1 2380 C CG2 . THR A 316 ? 0.6028 0.4563 0.4294 0.0188 -0.0059 0.0521 455 THR A CG2 2381 N N . ARG A 317 ? 0.5742 0.4004 0.4007 0.0440 -0.0502 0.0485 456 ARG A N 2382 C CA . ARG A 317 ? 0.5848 0.3808 0.3886 0.0473 -0.0682 0.0574 456 ARG A CA 2383 C C . ARG A 317 ? 0.6794 0.4513 0.4465 0.0338 -0.0633 0.0719 456 ARG A C 2384 O O . ARG A 317 ? 0.6713 0.4523 0.4212 0.0239 -0.0488 0.0742 456 ARG A O 2385 C CB . ARG A 317 ? 0.5551 0.3504 0.3497 0.0550 -0.0827 0.0546 456 ARG A CB 2386 C CG . ARG A 317 ? 0.6291 0.3941 0.4029 0.0615 -0.1057 0.0625 456 ARG A CG 2387 C CD . ARG A 317 ? 0.6940 0.4642 0.4641 0.0692 -0.1205 0.0575 456 ARG A CD 2388 N NE . ARG A 317 ? 0.7102 0.4848 0.4546 0.0605 -0.1105 0.0582 456 ARG A NE 2389 C CZ . ARG A 317 ? 0.7942 0.5459 0.4946 0.0545 -0.1152 0.0680 456 ARG A CZ 2390 N NH1 . ARG A 317 ? 0.8323 0.5518 0.5077 0.0553 -0.1313 0.0801 456 ARG A NH1 2391 N NH2 . ARG A 317 ? 0.7989 0.5583 0.4780 0.0482 -0.1045 0.0654 456 ARG A NH2 2392 N N . ASP A 318 ? 0.7523 0.4936 0.5071 0.0331 -0.0756 0.0814 457 ASP A N 2393 C CA . ASP A 318 ? 0.7899 0.5034 0.5055 0.0177 -0.0739 0.0978 457 ASP A CA 2394 C C . ASP A 318 ? 0.8711 0.5734 0.5474 0.0140 -0.0786 0.1050 457 ASP A C 2395 O O . ASP A 318 ? 0.8451 0.5374 0.5158 0.0258 -0.0972 0.1031 457 ASP A O 2396 C CB . ASP A 318 ? 0.8629 0.5379 0.5701 0.0190 -0.0916 0.1067 457 ASP A CB 2397 C CG . ASP A 318 ? 0.8396 0.5177 0.5708 0.0149 -0.0835 0.1038 457 ASP A CG 2398 O OD1 . ASP A 318 ? 0.7735 0.4861 0.5324 0.0141 -0.0663 0.0936 457 ASP A OD1 2399 O OD2 . ASP A 318 ? 0.8188 0.4623 0.5396 0.0127 -0.0960 0.1117 457 ASP A OD2 2400 N N . GLY A 319 ? 0.9112 0.6171 0.5604 -0.0024 -0.0618 0.1127 458 GLY A N 2401 C CA . GLY A 319 ? 1.0441 0.7370 0.6493 -0.0081 -0.0648 0.1205 458 GLY A CA 2402 C C . GLY A 319 ? 1.1594 0.8070 0.7246 -0.0164 -0.0814 0.1393 458 GLY A C 2403 O O . GLY A 319 ? 1.1130 0.7393 0.6839 -0.0203 -0.0874 0.1467 458 GLY A O 2404 N N . GLY A 320 ? 1.3089 0.9385 0.8314 -0.0189 -0.0905 0.1470 459 GLY A N 2405 C CA . GLY A 320 ? 1.4870 1.0705 0.9619 -0.0298 -0.1058 0.1673 459 GLY A CA 2406 C C . GLY A 320 ? 1.6164 1.1617 1.0933 -0.0152 -0.1383 0.1717 459 GLY A C 2407 O O . GLY A 320 ? 1.7324 1.2329 1.1688 -0.0233 -0.1547 0.1896 459 GLY A O 2408 N N . ALA A 321 ? 1.6127 1.1753 1.1355 0.0064 -0.1484 0.1554 460 ALA A N 2409 C CA . ALA A 321 ? 1.6631 1.1966 1.1960 0.0238 -0.1787 0.1557 460 ALA A CA 2410 C C . ALA A 321 ? 1.6881 1.2130 1.2070 0.0381 -0.2028 0.1536 460 ALA A C 2411 O O . ALA A 321 ? 1.6619 1.1795 1.2038 0.0580 -0.2268 0.1469 460 ALA A O 2412 C CB . ALA A 321 ? 1.6169 1.1757 1.2082 0.0391 -0.1766 0.1387 460 ALA A CB 2413 N N . ASN A 322 ? 1.7259 1.2530 1.2072 0.0283 -0.1970 0.1585 461 ASN A N 2414 C CA . ASN A 322 ? 1.7718 1.2933 1.2382 0.0402 -0.2192 0.1555 461 ASN A CA 2415 C C . ASN A 322 ? 1.9055 1.3761 1.3399 0.0467 -0.2535 0.1699 461 ASN A C 2416 O O . ASN A 322 ? 1.9230 1.3906 1.3661 0.0645 -0.2795 0.1637 461 ASN A O 2417 C CB . ASN A 322 ? 1.7483 1.2819 1.1773 0.0275 -0.2042 0.1565 461 ASN A CB 2418 C CG . ASN A 322 ? 1.6483 1.2307 1.1111 0.0258 -0.1754 0.1396 461 ASN A CG 2419 O OD1 . ASN A 322 ? 1.6057 1.2163 1.1204 0.0384 -0.1741 0.1245 461 ASN A OD1 2420 N ND2 . ASN A 322 ? 1.6200 1.2127 1.0526 0.0103 -0.1525 0.1421 461 ASN A ND2 2421 N N . ASN A 323 ? 2.0015 1.4314 1.3992 0.0318 -0.2549 0.1892 462 ASN A N 2422 C CA . ASN A 323 ? 2.1063 1.4791 1.4663 0.0358 -0.2887 0.2057 462 ASN A CA 2423 C C . ASN A 323 ? 1.9945 1.3522 1.3947 0.0577 -0.3120 0.1989 462 ASN A C 2424 O O . ASN A 323 ? 2.0293 1.3473 1.4131 0.0713 -0.3464 0.2055 462 ASN A O 2425 C CB . ASN A 323 ? 2.2702 1.6018 1.5712 0.0082 -0.2815 0.2307 462 ASN A CB 2426 C CG . ASN A 323 ? 2.3175 1.6432 1.6389 -0.0020 -0.2676 0.2342 462 ASN A CG 2427 O OD1 . ASN A 323 ? 2.2619 1.6304 1.6175 -0.0083 -0.2377 0.2232 462 ASN A OD1 2428 N ND2 . ASN A 323 ? 2.3861 1.6561 1.6851 -0.0036 -0.2912 0.2497 462 ASN A ND2 2429 N N . THR A 324 ? 1.8200 1.2089 1.2714 0.0621 -0.2939 0.1850 463 THR A N 2430 C CA . THR A 324 ? 1.7046 1.0858 1.1973 0.0839 -0.3121 0.1747 463 THR A CA 2431 C C . THR A 324 ? 1.5441 0.9627 1.0838 0.1103 -0.3254 0.1536 463 THR A C 2432 O O . THR A 324 ? 1.5033 0.9496 1.0418 0.1101 -0.3217 0.1482 463 THR A O 2433 C CB . THR A 324 ? 1.6738 1.0749 1.2017 0.0778 -0.2876 0.1670 463 THR A CB 2434 O OG1 . THR A 324 ? 1.5919 1.0528 1.1559 0.0759 -0.2590 0.1512 463 THR A OG1 2435 C CG2 . THR A 324 ? 1.6940 1.0612 1.1800 0.0500 -0.2751 0.1876 463 THR A CG2 2436 N N . SER A 325 ? 1.4485 0.8683 1.0295 0.1326 -0.3409 0.1410 464 SER A N 2437 C CA . SER A 325 ? 1.3570 0.8197 0.9900 0.1567 -0.3508 0.1194 464 SER A CA 2438 C C . SER A 325 ? 1.2517 0.7673 0.9394 0.1583 -0.3230 0.1005 464 SER A C 2439 O O . SER A 325 ? 1.2000 0.7552 0.9367 0.1766 -0.3272 0.0814 464 SER A O 2440 C CB . SER A 325 ? 1.4572 0.8915 1.1023 0.1834 -0.3880 0.1153 464 SER A CB 2441 O OG . SER A 325 ? 1.5107 0.9192 1.1644 0.1877 -0.3889 0.1149 464 SER A OG 2442 N N . ASN A 326 ? 1.1664 0.6839 0.8450 0.1381 -0.2948 0.1062 465 ASN A N 2443 C CA . ASN A 326 ? 1.0591 0.6204 0.7835 0.1381 -0.2695 0.0905 465 ASN A CA 2444 C C . ASN A 326 ? 0.9576 0.5531 0.6800 0.1189 -0.2387 0.0903 465 ASN A C 2445 O O . ASN A 326 ? 0.9795 0.5595 0.6603 0.1014 -0.2312 0.1043 465 ASN A O 2446 C CB . ASN A 326 ? 1.1460 0.6816 0.8710 0.1346 -0.2649 0.0935 465 ASN A CB 2447 C CG . ASN A 326 ? 1.2609 0.7533 0.9824 0.1535 -0.2968 0.0943 465 ASN A CG 2448 O OD1 . ASN A 326 ? 1.3673 0.8080 1.0540 0.1447 -0.3059 0.1095 465 ASN A OD1 2449 N ND2 . ASN A 326 ? 1.2504 0.7636 1.0083 0.1796 -0.3146 0.0776 465 ASN A ND2 2450 N N . GLU A 327 ? 0.8270 0.4693 0.5942 0.1229 -0.2216 0.0737 466 GLU A N 2451 C CA . GLU A 327 ? 0.7941 0.4664 0.5655 0.1064 -0.1917 0.0718 466 GLU A CA 2452 C C . GLU A 327 ? 0.7974 0.4838 0.5985 0.1057 -0.1759 0.0641 466 GLU A C 2453 O O . GLU A 327 ? 0.7927 0.4962 0.6305 0.1210 -0.1815 0.0504 466 GLU A O 2454 C CB . GLU A 327 ? 0.7701 0.4834 0.5635 0.1096 -0.1869 0.0600 466 GLU A CB 2455 C CG . GLU A 327 ? 0.8321 0.5343 0.5936 0.1079 -0.2000 0.0663 466 GLU A CG 2456 C CD . GLU A 327 ? 0.8729 0.5554 0.5865 0.0889 -0.1867 0.0803 466 GLU A CD 2457 O OE1 . GLU A 327 ? 0.8494 0.5374 0.5616 0.0763 -0.1639 0.0830 466 GLU A OE1 2458 O OE2 . GLU A 327 ? 0.9395 0.6026 0.6164 0.0866 -0.1992 0.0882 466 GLU A OE2 2459 N N . THR A 328 ? 0.7907 0.4716 0.5756 0.0879 -0.1564 0.0723 467 THR A N 2460 C CA . THR A 328 ? 0.7622 0.4539 0.5708 0.0850 -0.1420 0.0663 467 THR A CA 2461 C C . THR A 328 ? 0.6661 0.3994 0.4946 0.0766 -0.1172 0.0585 467 THR A C 2462 O O . THR A 328 ? 0.6963 0.4359 0.5056 0.0643 -0.1052 0.0644 467 THR A O 2463 C CB . THR A 328 ? 0.8078 0.4625 0.5871 0.0700 -0.1398 0.0809 467 THR A CB 2464 O OG1 . THR A 328 ? 0.9074 0.5172 0.6656 0.0777 -0.1653 0.0891 467 THR A OG1 2465 C CG2 . THR A 328 ? 0.7876 0.4527 0.5912 0.0670 -0.1270 0.0738 467 THR A CG2 2466 N N . PHE A 329 ? 0.6640 0.4243 0.5293 0.0839 -0.1104 0.0447 468 PHE A N 2467 C CA . PHE A 329 ? 0.6465 0.4424 0.5307 0.0767 -0.0895 0.0376 468 PHE A CA 2468 C C . PHE A 329 ? 0.6460 0.4454 0.5429 0.0712 -0.0770 0.0350 468 PHE A C 2469 O O . PHE A 329 ? 0.6319 0.4179 0.5375 0.0786 -0.0851 0.0312 468 PHE A O 2470 C CB . PHE A 329 ? 0.5607 0.3901 0.4749 0.0871 -0.0915 0.0243 468 PHE A CB 2471 C CG . PHE A 329 ? 0.6184 0.4465 0.5220 0.0915 -0.1048 0.0259 468 PHE A CG 2472 C CD1 . PHE A 329 ? 0.5713 0.4144 0.4679 0.0839 -0.0969 0.0259 468 PHE A CD1 2473 C CD2 . PHE A 329 ? 0.6644 0.4731 0.5628 0.1039 -0.1272 0.0272 468 PHE A CD2 2474 C CE1 . PHE A 329 ? 0.5380 0.3782 0.4227 0.0874 -0.1103 0.0267 468 PHE A CE1 2475 C CE2 . PHE A 329 ? 0.6858 0.4930 0.5733 0.1079 -0.1414 0.0287 468 PHE A CE2 2476 C CZ . PHE A 329 ? 0.5350 0.3580 0.4150 0.0989 -0.1327 0.0285 468 PHE A CZ 2477 N N . ARG A 330 ? 0.6107 0.4273 0.5082 0.0589 -0.0586 0.0361 469 ARG A N 2478 C CA . ARG A 330 ? 0.5860 0.4075 0.4947 0.0523 -0.0473 0.0339 469 ARG A CA 2479 C C . ARG A 330 ? 0.5449 0.4014 0.4750 0.0510 -0.0333 0.0250 469 ARG A C 2480 O O . ARG A 330 ? 0.5349 0.4045 0.4608 0.0481 -0.0280 0.0256 469 ARG A O 2481 C CB . ARG A 330 ? 0.6063 0.4102 0.4912 0.0362 -0.0400 0.0467 469 ARG A CB 2482 C CG . ARG A 330 ? 0.6378 0.4021 0.4943 0.0337 -0.0543 0.0588 469 ARG A CG 2483 C CD . ARG A 330 ? 0.6358 0.3863 0.4679 0.0138 -0.0453 0.0726 469 ARG A CD 2484 N NE . ARG A 330 ? 0.7321 0.4428 0.5307 0.0092 -0.0595 0.0866 469 ARG A NE 2485 C CZ . ARG A 330 ? 0.7800 0.4545 0.5673 0.0054 -0.0715 0.0936 469 ARG A CZ 2486 N NH1 . ARG A 330 ? 0.7805 0.4546 0.5881 0.0059 -0.0705 0.0867 469 ARG A NH1 2487 N NH2 . ARG A 330 ? 0.7932 0.4287 0.5462 0.0004 -0.0858 0.1079 469 ARG A NH2 2488 N N . PRO A 331 ? 0.5329 0.4019 0.4838 0.0533 -0.0288 0.0166 470 PRO A N 2489 C CA . PRO A 331 ? 0.4971 0.3960 0.4649 0.0514 -0.0178 0.0096 470 PRO A CA 2490 C C . PRO A 331 ? 0.5236 0.4267 0.4822 0.0397 -0.0056 0.0155 470 PRO A C 2491 O O . PRO A 331 ? 0.5812 0.4699 0.5268 0.0318 -0.0030 0.0230 470 PRO A O 2492 C CB . PRO A 331 ? 0.4974 0.4050 0.4837 0.0554 -0.0161 0.0003 470 PRO A CB 2493 C CG . PRO A 331 ? 0.5523 0.4324 0.5294 0.0559 -0.0231 0.0034 470 PRO A CG 2494 C CD . PRO A 331 ? 0.5551 0.4106 0.5128 0.0578 -0.0344 0.0123 470 PRO A CD 2495 N N . GLY A 332 ? 0.5793 0.5021 0.5448 0.0385 0.0010 0.0119 471 GLY A N 2496 C CA . GLY A 332 ? 0.7338 0.6647 0.6960 0.0307 0.0119 0.0142 471 GLY A CA 2497 C C . GLY A 332 ? 0.8881 0.8215 0.8384 0.0310 0.0130 0.0154 471 GLY A C 2498 O O . GLY A 332 ? 0.8064 0.7269 0.7394 0.0317 0.0079 0.0202 471 GLY A O 2499 N N . GLY A 333 ? 1.0516 0.9994 1.0094 0.0308 0.0180 0.0107 472 GLY A N 2500 C CA . GLY A 333 ? 1.1893 1.1386 1.1353 0.0314 0.0201 0.0099 472 GLY A CA 2501 C C . GLY A 333 ? 1.3165 1.2727 1.2604 0.0271 0.0308 0.0111 472 GLY A C 2502 O O . GLY A 333 ? 1.3693 1.3310 1.3246 0.0234 0.0350 0.0119 472 GLY A O 2503 N N . GLY A 334 ? 1.3192 1.2769 1.2492 0.0278 0.0350 0.0101 473 GLY A N 2504 C CA . GLY A 334 ? 1.2588 1.2288 1.1893 0.0245 0.0461 0.0098 473 GLY A CA 2505 C C . GLY A 334 ? 1.1111 1.0930 1.0502 0.0305 0.0489 0.0013 473 GLY A C 2506 O O . GLY A 334 ? 1.1251 1.1180 1.0597 0.0319 0.0571 -0.0021 473 GLY A O 2507 N N . ASN A 335 ? 0.9389 0.9191 0.8900 0.0340 0.0421 -0.0025 474 ASN A N 2508 C CA . ASN A 335 ? 0.6997 0.6826 0.6539 0.0404 0.0405 -0.0100 474 ASN A CA 2509 C C . ASN A 335 ? 0.5236 0.5013 0.4880 0.0406 0.0321 -0.0115 474 ASN A C 2510 O O . ASN A 335 ? 0.4231 0.3924 0.3839 0.0392 0.0251 -0.0108 474 ASN A O 2511 C CB . ASN A 335 ? 0.7005 0.6754 0.6358 0.0451 0.0382 -0.0142 474 ASN A CB 2512 C CG . ASN A 335 ? 0.6156 0.5927 0.5499 0.0535 0.0387 -0.0236 474 ASN A CG 2513 O OD1 . ASN A 335 ? 0.6142 0.5928 0.5618 0.0564 0.0355 -0.0266 474 ASN A OD1 2514 N ND2 . ASN A 335 ? 0.7128 0.6890 0.6296 0.0582 0.0418 -0.0290 474 ASN A ND2 2515 N N . ILE A 336 ? 0.3864 0.3894 0.4269 -0.0307 0.0185 0.0840 475 ILE A N 2516 C CA . ILE A 336 ? 0.3965 0.3941 0.4327 -0.0364 0.0116 0.0738 475 ILE A CA 2517 C C . ILE A 336 ? 0.3762 0.3830 0.4009 -0.0354 0.0123 0.0643 475 ILE A C 2518 O O . ILE A 336 ? 0.3862 0.3919 0.4047 -0.0382 0.0075 0.0562 475 ILE A O 2519 C CB . ILE A 336 ? 0.4293 0.4149 0.4784 -0.0433 0.0073 0.0736 475 ILE A CB 2520 C CG1 . ILE A 336 ? 0.4731 0.4479 0.5340 -0.0447 0.0046 0.0825 475 ILE A CG1 2521 C CG2 . ILE A 336 ? 0.4264 0.4058 0.4693 -0.0484 0.0008 0.0637 475 ILE A CG2 2522 C CD1 . ILE A 336 ? 0.4714 0.4394 0.5245 -0.0443 -0.0002 0.0818 475 ILE A CD1 2523 N N . LYS A 337 ? 0.3834 0.3984 0.4049 -0.0311 0.0182 0.0653 476 LYS A N 2524 C CA . LYS A 337 ? 0.4379 0.4603 0.4477 -0.0299 0.0177 0.0559 476 LYS A CA 2525 C C . LYS A 337 ? 0.4176 0.4460 0.4156 -0.0273 0.0143 0.0522 476 LYS A C 2526 O O . LYS A 337 ? 0.4546 0.4865 0.4461 -0.0287 0.0104 0.0433 476 LYS A O 2527 C CB . LYS A 337 ? 0.4449 0.4735 0.4501 -0.0244 0.0249 0.0576 476 LYS A CB 2528 C CG . LYS A 337 ? 0.4656 0.4897 0.4824 -0.0276 0.0280 0.0583 476 LYS A CG 2529 C CD . LYS A 337 ? 0.5216 0.5512 0.5302 -0.0217 0.0351 0.0574 476 LYS A CD 2530 C CE . LYS A 337 ? 0.6001 0.6339 0.6033 -0.0131 0.0431 0.0671 476 LYS A CE 2531 N NZ . LYS A 337 ? 0.6887 0.7253 0.6823 -0.0067 0.0509 0.0662 476 LYS A NZ 2532 N N . ASP A 338 ? 0.3871 0.4166 0.3836 -0.0234 0.0156 0.0594 477 ASP A N 2533 C CA . ASP A 338 ? 0.3532 0.3886 0.3401 -0.0206 0.0125 0.0570 477 ASP A CA 2534 C C . ASP A 338 ? 0.3809 0.4112 0.3704 -0.0259 0.0065 0.0512 477 ASP A C 2535 O O . ASP A 338 ? 0.3726 0.4085 0.3560 -0.0253 0.0032 0.0458 477 ASP A O 2536 C CB . ASP A 338 ? 0.3791 0.4164 0.3649 -0.0153 0.0153 0.0664 477 ASP A CB 2537 C CG . ASP A 338 ? 0.5110 0.5547 0.4908 -0.0083 0.0219 0.0721 477 ASP A CG 2538 O OD1 . ASP A 338 ? 0.4749 0.5244 0.4443 -0.0056 0.0225 0.0667 477 ASP A OD1 2539 O OD2 . ASP A 338 ? 0.5204 0.5625 0.5056 -0.0053 0.0265 0.0821 477 ASP A OD2 2540 N N . ASN A 339 ? 0.3755 0.3945 0.3740 -0.0309 0.0050 0.0527 478 ASN A N 2541 C CA . ASN A 339 ? 0.3573 0.3693 0.3564 -0.0356 0.0002 0.0470 478 ASN A CA 2542 C C . ASN A 339 ? 0.3543 0.3711 0.3508 -0.0382 -0.0020 0.0376 478 ASN A C 2543 O O . ASN A 339 ? 0.3546 0.3729 0.3485 -0.0390 -0.0049 0.0329 478 ASN A O 2544 C CB . ASN A 339 ? 0.3452 0.3423 0.3522 -0.0405 -0.0019 0.0493 478 ASN A CB 2545 C CG . ASN A 339 ? 0.3398 0.3299 0.3502 -0.0385 -0.0015 0.0581 478 ASN A CG 2546 O OD1 . ASN A 339 ? 0.3980 0.3941 0.4097 -0.0342 0.0024 0.0648 478 ASN A OD1 2547 N ND2 . ASN A 339 ? 0.3641 0.3401 0.3753 -0.0414 -0.0055 0.0582 478 ASN A ND2 2548 N N . TRP A 340 ? 0.3455 0.3645 0.3439 -0.0394 -0.0004 0.0350 479 TRP A N 2549 C CA . TRP A 340 ? 0.3616 0.3845 0.3582 -0.0421 -0.0030 0.0258 479 TRP A CA 2550 C C . TRP A 340 ? 0.3524 0.3871 0.3402 -0.0375 -0.0039 0.0224 479 TRP A C 2551 O O . TRP A 340 ? 0.3634 0.4019 0.3503 -0.0392 -0.0078 0.0156 479 TRP A O 2552 C CB . TRP A 340 ? 0.3585 0.3791 0.3600 -0.0448 -0.0012 0.0236 479 TRP A CB 2553 C CG . TRP A 340 ? 0.4004 0.4105 0.4117 -0.0479 -0.0001 0.0296 479 TRP A CG 2554 C CD1 . TRP A 340 ? 0.3970 0.4059 0.4148 -0.0473 0.0040 0.0344 479 TRP A CD1 2555 C CD2 . TRP A 340 ? 0.3829 0.3812 0.3987 -0.0516 -0.0035 0.0320 479 TRP A CD2 2556 N NE1 . TRP A 340 ? 0.3610 0.3590 0.3893 -0.0511 0.0024 0.0397 479 TRP A NE1 2557 C CE2 . TRP A 340 ? 0.3852 0.3757 0.4110 -0.0537 -0.0027 0.0379 479 TRP A CE2 2558 C CE3 . TRP A 340 ? 0.3655 0.3583 0.3775 -0.0529 -0.0072 0.0299 479 TRP A CE3 2559 C CZ2 . TRP A 340 ? 0.4133 0.3900 0.4445 -0.0573 -0.0069 0.0411 479 TRP A CZ2 2560 C CZ3 . TRP A 340 ? 0.3864 0.3648 0.4015 -0.0559 -0.0101 0.0329 479 TRP A CZ3 2561 C CH2 . TRP A 340 ? 0.3905 0.3607 0.4147 -0.0582 -0.0107 0.0381 479 TRP A CH2 2562 N N . ARG A 341 ? 0.3392 0.3792 0.3210 -0.0316 -0.0006 0.0275 480 ARG A N 2563 C CA . ARG A 341 ? 0.3625 0.4125 0.3340 -0.0265 -0.0023 0.0252 480 ARG A CA 2564 C C . ARG A 341 ? 0.3527 0.4057 0.3250 -0.0270 -0.0070 0.0237 480 ARG A C 2565 O O . ARG A 341 ? 0.4070 0.4669 0.3757 -0.0262 -0.0116 0.0181 480 ARG A O 2566 C CB . ARG A 341 ? 0.3968 0.4497 0.3616 -0.0196 0.0026 0.0333 480 ARG A CB 2567 C CG . ARG A 341 ? 0.5187 0.5776 0.4707 -0.0138 0.0040 0.0311 480 ARG A CG 2568 C CD . ARG A 341 ? 0.3451 0.4042 0.2924 -0.0070 0.0117 0.0411 480 ARG A CD 2569 N NE . ARG A 341 ? 0.5470 0.6033 0.4933 -0.0058 0.0175 0.0410 480 ARG A NE 2570 C CZ . ARG A 341 ? 0.6142 0.6663 0.5687 -0.0050 0.0249 0.0493 480 ARG A CZ 2571 N NH1 . ARG A 341 ? 0.7155 0.7652 0.6795 -0.0054 0.0269 0.0584 480 ARG A NH1 2572 N NH2 . ARG A 341 ? 0.7068 0.7568 0.6608 -0.0036 0.0303 0.0488 480 ARG A NH2 2573 N N . SER A 342 ? 0.3548 0.4021 0.3322 -0.0281 -0.0060 0.0290 481 SER A N 2574 C CA . SER A 342 ? 0.3662 0.4156 0.3446 -0.0275 -0.0088 0.0293 481 SER A CA 2575 C C . SER A 342 ? 0.4085 0.4578 0.3918 -0.0320 -0.0125 0.0219 481 SER A C 2576 O O . SER A 342 ? 0.4633 0.5182 0.4481 -0.0309 -0.0153 0.0207 481 SER A O 2577 C CB . SER A 342 ? 0.3517 0.3926 0.3333 -0.0272 -0.0064 0.0364 481 SER A CB 2578 O OG . SER A 342 ? 0.3980 0.4272 0.3848 -0.0324 -0.0066 0.0346 481 SER A OG 2579 N N . GLU A 343 ? 0.3638 0.4070 0.3509 -0.0368 -0.0123 0.0177 482 GLU A N 2580 C CA . GLU A 343 ? 0.4186 0.4616 0.4109 -0.0411 -0.0154 0.0109 482 GLU A CA 2581 C C . GLU A 343 ? 0.3589 0.4097 0.3502 -0.0418 -0.0186 0.0035 482 GLU A C 2582 O O . GLU A 343 ? 0.3597 0.4144 0.3557 -0.0439 -0.0223 -0.0017 482 GLU A O 2583 C CB . GLU A 343 ? 0.3687 0.3991 0.3656 -0.0462 -0.0140 0.0104 482 GLU A CB 2584 C CG . GLU A 343 ? 0.3782 0.3986 0.3746 -0.0455 -0.0123 0.0161 482 GLU A CG 2585 C CD . GLU A 343 ? 0.4560 0.4780 0.4537 -0.0443 -0.0129 0.0157 482 GLU A CD 2586 O OE1 . GLU A 343 ? 0.4478 0.4735 0.4500 -0.0466 -0.0145 0.0106 482 GLU A OE1 2587 O OE2 . GLU A 343 ? 0.4085 0.4284 0.4040 -0.0409 -0.0113 0.0211 482 GLU A OE2 2588 N N . LEU A 344 ? 0.3341 0.3868 0.3193 -0.0396 -0.0171 0.0033 483 LEU A N 2589 C CA . LEU A 344 ? 0.3058 0.3630 0.2885 -0.0402 -0.0200 -0.0042 483 LEU A CA 2590 C C . LEU A 344 ? 0.3282 0.3943 0.3015 -0.0348 -0.0238 -0.0059 483 LEU A C 2591 O O . LEU A 344 ? 0.3681 0.4369 0.3369 -0.0344 -0.0271 -0.0125 483 LEU A O 2592 C CB . LEU A 344 ? 0.3708 0.4229 0.3519 -0.0408 -0.0157 -0.0042 483 LEU A CB 2593 C CG . LEU A 344 ? 0.3445 0.3875 0.3351 -0.0467 -0.0139 -0.0041 483 LEU A CG 2594 C CD1 . LEU A 344 ? 0.4014 0.4399 0.3920 -0.0460 -0.0088 -0.0004 483 LEU A CD1 2595 C CD2 . LEU A 344 ? 0.3805 0.4239 0.3766 -0.0515 -0.0178 -0.0125 483 LEU A CD2 2596 N N . TYR A 345 ? 0.3465 0.4163 0.3166 -0.0307 -0.0238 -0.0002 484 TYR A N 2597 C CA . TYR A 345 ? 0.3883 0.4652 0.3474 -0.0247 -0.0272 -0.0003 484 TYR A CA 2598 C C . TYR A 345 ? 0.3890 0.4718 0.3488 -0.0257 -0.0360 -0.0085 484 TYR A C 2599 O O . TYR A 345 ? 0.3988 0.4850 0.3470 -0.0214 -0.0402 -0.0115 484 TYR A O 2600 C CB . TYR A 345 ? 0.3801 0.4601 0.3383 -0.0208 -0.0263 0.0076 484 TYR A CB 2601 C CG . TYR A 345 ? 0.4137 0.4969 0.3827 -0.0232 -0.0303 0.0074 484 TYR A CG 2602 C CD1 . TYR A 345 ? 0.4888 0.5660 0.4677 -0.0271 -0.0268 0.0100 484 TYR A CD1 2603 C CD2 . TYR A 345 ? 0.4185 0.5102 0.3880 -0.0214 -0.0376 0.0049 484 TYR A CD2 2604 C CE1 . TYR A 345 ? 0.4695 0.5488 0.4578 -0.0285 -0.0288 0.0104 484 TYR A CE1 2605 C CE2 . TYR A 345 ? 0.4549 0.5499 0.4366 -0.0234 -0.0404 0.0058 484 TYR A CE2 2606 C CZ . TYR A 345 ? 0.5380 0.6269 0.5289 -0.0267 -0.0351 0.0087 484 TYR A CZ 2607 O OH . TYR A 345 ? 0.6346 0.7261 0.6373 -0.0277 -0.0363 0.0103 484 TYR A OH 2608 N N . LYS A 346 ? 0.4095 0.4928 0.3827 -0.0311 -0.0388 -0.0116 485 LYS A N 2609 C CA . LYS A 346 ? 0.4175 0.5067 0.3960 -0.0326 -0.0476 -0.0181 485 LYS A CA 2610 C C . LYS A 346 ? 0.3775 0.4642 0.3570 -0.0363 -0.0501 -0.0268 485 LYS A C 2611 O O . LYS A 346 ? 0.4346 0.5253 0.4208 -0.0385 -0.0578 -0.0328 485 LYS A O 2612 C CB . LYS A 346 ? 0.4359 0.5279 0.4303 -0.0357 -0.0487 -0.0157 485 LYS A CB 2613 C CG . LYS A 346 ? 0.4478 0.5326 0.4517 -0.0408 -0.0429 -0.0150 485 LYS A CG 2614 C CD . LYS A 346 ? 0.5604 0.6478 0.5791 -0.0430 -0.0440 -0.0135 485 LYS A CD 2615 C CE . LYS A 346 ? 0.6813 0.7732 0.7013 -0.0388 -0.0438 -0.0064 485 LYS A CE 2616 N NZ . LYS A 346 ? 0.7039 0.7962 0.7385 -0.0403 -0.0419 -0.0033 485 LYS A NZ 2617 N N . TYR A 347 ? 0.3656 0.4457 0.3396 -0.0368 -0.0440 -0.0271 486 TYR A N 2618 C CA . TYR A 347 ? 0.3822 0.4591 0.3574 -0.0401 -0.0453 -0.0348 486 TYR A CA 2619 C C . TYR A 347 ? 0.3954 0.4696 0.3547 -0.0355 -0.0437 -0.0375 486 TYR A C 2620 O O . TYR A 347 ? 0.3800 0.4523 0.3295 -0.0308 -0.0375 -0.0314 486 TYR A O 2621 C CB . TYR A 347 ? 0.2908 0.3610 0.2756 -0.0454 -0.0391 -0.0334 486 TYR A CB 2622 C CG . TYR A 347 ? 0.3619 0.4318 0.3607 -0.0498 -0.0392 -0.0311 486 TYR A CG 2623 C CD1 . TYR A 347 ? 0.3407 0.4141 0.3505 -0.0534 -0.0446 -0.0360 486 TYR A CD1 2624 C CD2 . TYR A 347 ? 0.3432 0.4084 0.3438 -0.0499 -0.0336 -0.0237 486 TYR A CD2 2625 C CE1 . TYR A 347 ? 0.3868 0.4593 0.4087 -0.0564 -0.0432 -0.0330 486 TYR A CE1 2626 C CE2 . TYR A 347 ? 0.3753 0.4383 0.3857 -0.0528 -0.0329 -0.0215 486 TYR A CE2 2627 C CZ . TYR A 347 ? 0.3854 0.4521 0.4061 -0.0558 -0.0371 -0.0259 486 TYR A CZ 2628 O OH . TYR A 347 ? 0.3476 0.4114 0.3774 -0.0578 -0.0349 -0.0230 486 TYR A OH 2629 N N . LYS A 348 ? 0.3743 0.4475 0.3313 -0.0366 -0.0486 -0.0462 487 LYS A N 2630 C CA . LYS A 348 ? 0.4121 0.4803 0.3547 -0.0326 -0.0454 -0.0494 487 LYS A CA 2631 C C . LYS A 348 ? 0.4379 0.5027 0.3861 -0.0371 -0.0481 -0.0582 487 LYS A C 2632 O O . LYS A 348 ? 0.4240 0.4916 0.3836 -0.0418 -0.0556 -0.0634 487 LYS A O 2633 C CB . LYS A 348 ? 0.3959 0.4652 0.3187 -0.0247 -0.0498 -0.0510 487 LYS A CB 2634 C CG . LYS A 348 ? 0.4653 0.5363 0.3854 -0.0250 -0.0621 -0.0604 487 LYS A CG 2635 C CD . LYS A 348 ? 0.5510 0.6202 0.4472 -0.0163 -0.0663 -0.0621 487 LYS A CD 2636 C CE . LYS A 348 ? 0.5784 0.6494 0.4730 -0.0166 -0.0812 -0.0705 487 LYS A CE 2637 N NZ . LYS A 348 ? 0.5567 0.6228 0.4247 -0.0079 -0.0866 -0.0740 487 LYS A NZ 2638 N N . VAL A 349 ? 0.4580 0.5168 0.3996 -0.0354 -0.0415 -0.0591 488 VAL A N 2639 C CA . VAL A 349 ? 0.4589 0.5137 0.4044 -0.0389 -0.0431 -0.0672 488 VAL A CA 2640 C C . VAL A 349 ? 0.4744 0.5269 0.4026 -0.0336 -0.0495 -0.0755 488 VAL A C 2641 O O . VAL A 349 ? 0.4780 0.5284 0.3870 -0.0257 -0.0472 -0.0737 488 VAL A O 2642 C CB . VAL A 349 ? 0.4251 0.4742 0.3737 -0.0398 -0.0327 -0.0637 488 VAL A CB 2643 C CG1 . VAL A 349 ? 0.4143 0.4589 0.3662 -0.0428 -0.0340 -0.0722 488 VAL A CG1 2644 C CG2 . VAL A 349 ? 0.4058 0.4552 0.3702 -0.0451 -0.0283 -0.0560 488 VAL A CG2 2645 N N . VAL A 350 ? 0.4565 0.5087 0.3911 -0.0376 -0.0580 -0.0846 489 VAL A N 2646 C CA . VAL A 350 ? 0.4829 0.5301 0.4013 -0.0331 -0.0645 -0.0938 489 VAL A CA 2647 C C . VAL A 350 ? 0.4768 0.5189 0.4026 -0.0374 -0.0643 -0.1012 489 VAL A C 2648 O O . VAL A 350 ? 0.4950 0.5394 0.4412 -0.0450 -0.0631 -0.1005 489 VAL A O 2649 C CB . VAL A 350 ? 0.5370 0.5881 0.4536 -0.0327 -0.0788 -0.0988 489 VAL A CB 2650 C CG1 . VAL A 350 ? 0.5776 0.6343 0.4885 -0.0286 -0.0789 -0.0909 489 VAL A CG1 2651 C CG2 . VAL A 350 ? 0.5080 0.5642 0.4494 -0.0415 -0.0862 -0.1022 489 VAL A CG2 2652 N N . GLN A 351 ? 0.5549 0.5890 0.4627 -0.0320 -0.0649 -0.1081 490 GLN A N 2653 C CA . GLN A 351 ? 0.6043 0.6327 0.5170 -0.0352 -0.0661 -0.1164 490 GLN A CA 2654 C C . GLN A 351 ? 0.6688 0.6970 0.5831 -0.0373 -0.0815 -0.1266 490 GLN A C 2655 O O . GLN A 351 ? 0.6589 0.6850 0.5561 -0.0318 -0.0899 -0.1302 490 GLN A O 2656 C CB . GLN A 351 ? 0.5943 0.6128 0.4860 -0.0274 -0.0581 -0.1185 490 GLN A CB 2657 C CG . GLN A 351 ? 0.5987 0.6112 0.4976 -0.0307 -0.0557 -0.1248 490 GLN A CG 2658 C CD . GLN A 351 ? 0.7854 0.7884 0.6659 -0.0226 -0.0447 -0.1244 490 GLN A CD 2659 O OE1 . GLN A 351 ? 0.8097 0.8091 0.6678 -0.0134 -0.0409 -0.1217 490 GLN A OE1 2660 N NE2 . GLN A 351 ? 0.8537 0.8525 0.7440 -0.0256 -0.0388 -0.1266 490 GLN A NE2 2661 N N . ILE A 352 ? 0.6688 0.6987 0.6041 -0.0453 -0.0855 -0.1308 491 ILE A N 2662 C CA . ILE A 352 ? 0.7443 0.7739 0.6854 -0.0482 -0.1002 -0.1403 491 ILE A CA 2663 C C . ILE A 352 ? 0.9106 0.9286 0.8355 -0.0443 -0.1031 -0.1508 491 ILE A C 2664 O O . ILE A 352 ? 0.8693 0.8818 0.7927 -0.0440 -0.0932 -0.1512 491 ILE A O 2665 C CB . ILE A 352 ? 0.7191 0.7551 0.6907 -0.0582 -0.1028 -0.1399 491 ILE A CB 2666 C CG1 . ILE A 352 ? 0.7186 0.7645 0.7052 -0.0615 -0.0995 -0.1297 491 ILE A CG1 2667 C CG2 . ILE A 352 ? 0.7038 0.7395 0.6841 -0.0612 -0.1183 -0.1492 491 ILE A CG2 2668 C CD1 . ILE A 352 ? 0.7180 0.7696 0.7018 -0.0589 -0.1092 -0.1284 491 ILE A CD1 2669 N N . GLU A 353 ? 1.0477 1.0611 0.9603 -0.0411 -0.1169 -0.1592 492 GLU A N 2670 C CA . GLU A 353 ? 1.1944 1.1949 1.0900 -0.0370 -0.1214 -0.1704 492 GLU A CA 2671 C C . GLU A 353 ? 1.1885 1.1887 1.1070 -0.0453 -0.1267 -0.1769 492 GLU A C 2672 O O . GLU A 353 ? 1.2019 1.1924 1.1133 -0.0438 -0.1245 -0.1839 492 GLU A O 2673 C CB . GLU A 353 ? 1.3271 1.3210 1.2003 -0.0306 -0.1361 -0.1775 492 GLU A CB 2674 C CG . GLU A 353 ? 1.4479 1.4399 1.2942 -0.0211 -0.1311 -0.1718 492 GLU A CG 2675 C CD . GLU A 353 ? 1.5504 1.5382 1.3792 -0.0162 -0.1479 -0.1775 492 GLU A CD 2676 O OE1 . GLU A 353 ? 1.5678 1.5534 1.4057 -0.0204 -0.1639 -0.1863 492 GLU A OE1 2677 O OE2 . GLU A 353 ? 1.6023 1.5886 1.4089 -0.0083 -0.1456 -0.1729 492 GLU A OE2 # 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 VAL 1 44 44 VAL VAL A . n A 1 2 TRP 2 45 45 TRP TRP A . n A 1 3 LYS 3 46 46 LYS LYS A . n A 1 4 ASP 4 47 47 ASP ASP A . n A 1 5 ALA 5 48 48 ALA ALA A . n A 1 6 ASP 6 49 49 ASP ASP A . n A 1 7 THR 7 50 50 THR THR A . n A 1 8 THR 8 51 51 THR THR A . n A 1 9 LEU 9 52 52 LEU LEU A . n A 1 10 PHE 10 53 53 PHE PHE A . n A 1 11 CYS 11 54 54 CYS CYS A . n A 1 12 ALA 12 55 55 ALA ALA A . n A 1 13 SER 13 56 56 SER SER A . n A 1 14 ASP 14 57 57 ASP ASP A . n A 1 15 ALA 15 58 58 ALA ALA A . n A 1 16 LYS 16 59 59 LYS LYS A . n A 1 17 ALA 17 60 60 ALA ALA A . n A 1 18 HIS 18 61 61 HIS HIS A . n A 1 19 GLU 19 62 62 GLU GLU A . n A 1 20 THR 20 63 63 THR THR A . n A 1 21 GLU 21 64 64 GLU GLU A . n A 1 22 VAL 22 65 65 VAL VAL A . n A 1 23 HIS 23 66 66 HIS HIS A . n A 1 24 ASN 24 67 67 ASN ASN A . n A 1 25 VAL 25 68 68 VAL VAL A . n A 1 26 TRP 26 69 69 TRP TRP A . n A 1 27 ALA 27 70 70 ALA ALA A . n A 1 28 THR 28 71 71 THR THR A . n A 1 29 HIS 29 72 72 HIS HIS A . n A 1 30 ALA 30 73 73 ALA ALA A . n A 1 31 CYS 31 74 74 CYS CYS A . n A 1 32 VAL 32 75 75 VAL VAL A . n A 1 33 PRO 33 76 76 PRO PRO A . n A 1 34 THR 34 77 77 THR THR A . n A 1 35 ASP 35 78 78 ASP ASP A . n A 1 36 PRO 36 79 79 PRO PRO A . n A 1 37 ASN 37 80 80 ASN ASN A . n A 1 38 PRO 38 81 81 PRO PRO A . n A 1 39 GLN 39 82 82 GLN GLN A . n A 1 40 GLU 40 83 83 GLU GLU A . n A 1 41 ILE 41 84 84 ILE ILE A . n A 1 42 HIS 42 85 85 HIS HIS A . n A 1 43 LEU 43 86 86 LEU LEU A . n A 1 44 GLU 44 87 87 GLU GLU A . n A 1 45 ASN 45 88 88 ASN ASN A . n A 1 46 VAL 46 89 89 VAL VAL A . n A 1 47 THR 47 90 90 THR THR A . n A 1 48 GLU 48 91 91 GLU GLU A . n A 1 49 ASN 49 92 92 ASN ASN A . n A 1 50 PHE 50 93 93 PHE PHE A . n A 1 51 ASN 51 94 94 ASN ASN A . n A 1 52 MET 52 95 95 MET MET A . n A 1 53 TRP 53 96 96 TRP TRP A . n A 1 54 LYS 54 97 97 LYS LYS A . n A 1 55 ASN 55 98 98 ASN ASN A . n A 1 56 ASN 56 99 99 ASN ASN A . n A 1 57 MET 57 100 100 MET MET A . n A 1 58 VAL 58 101 101 VAL VAL A . n A 1 59 GLU 59 102 102 GLU GLU A . n A 1 60 GLN 60 103 103 GLN GLN A . n A 1 61 MET 61 104 104 MET MET A . n A 1 62 GLN 62 105 105 GLN GLN A . n A 1 63 GLU 63 106 106 GLU GLU A . n A 1 64 ASP 64 107 107 ASP ASP A . n A 1 65 VAL 65 108 108 VAL VAL A . n A 1 66 ILE 66 109 109 ILE ILE A . n A 1 67 SER 67 110 110 SER SER A . n A 1 68 LEU 68 111 111 LEU LEU A . n A 1 69 TRP 69 112 112 TRP TRP A . n A 1 70 ASP 70 113 113 ASP ASP A . n A 1 71 GLN 71 114 114 GLN GLN A . n A 1 72 SER 72 115 115 SER SER A . n A 1 73 LEU 73 116 116 LEU LEU A . n A 1 74 GLN 74 117 117 GLN GLN A . n A 1 75 PRO 75 118 118 PRO PRO A . n A 1 76 CYS 76 119 119 CYS CYS A . n A 1 77 VAL 77 120 120 VAL VAL A . n A 1 78 LYS 78 121 121 LYS LYS A . n A 1 79 LEU 79 122 122 LEU LEU A . n A 1 80 THR 80 123 123 THR THR A . n A 1 81 GLY 81 124 124 GLY GLY A . n A 1 82 GLY 82 198 198 GLY GLY A . n A 1 83 SER 83 199 199 SER SER A . n A 1 84 VAL 84 200 200 VAL VAL A . n A 1 85 ILE 85 201 201 ILE ILE A . n A 1 86 LYS 86 202 202 LYS LYS A . n A 1 87 GLN 87 203 203 GLN GLN A . n A 1 88 ALA 88 204 204 ALA ALA A . n A 1 89 CYS 89 205 205 CYS CYS A . n A 1 90 PRO 90 206 206 PRO PRO A . n A 1 91 LYS 91 207 207 LYS LYS A . n A 1 92 ILE 92 208 208 ILE ILE A . n A 1 93 SER 93 209 209 SER SER A . n A 1 94 PHE 94 210 210 PHE PHE A . n A 1 95 ASP 95 211 211 ASP ASP A . n A 1 96 PRO 96 212 212 PRO PRO A . n A 1 97 ILE 97 213 213 ILE ILE A . n A 1 98 PRO 98 214 214 PRO PRO A . n A 1 99 ILE 99 215 215 ILE ILE A . n A 1 100 HIS 100 216 216 HIS HIS A . n A 1 101 TYR 101 217 217 TYR TYR A . n A 1 102 CYS 102 218 218 CYS CYS A . n A 1 103 THR 103 219 219 THR THR A . n A 1 104 PRO 104 220 220 PRO PRO A . n A 1 105 ALA 105 221 221 ALA ALA A . n A 1 106 GLY 106 222 222 GLY GLY A . n A 1 107 TYR 107 223 223 TYR TYR A . n A 1 108 VAL 108 224 224 VAL VAL A . n A 1 109 ILE 109 225 225 ILE ILE A . n A 1 110 LEU 110 226 226 LEU LEU A . n A 1 111 LYS 111 227 227 LYS LYS A . n A 1 112 CYS 112 228 228 CYS CYS A . n A 1 113 ASN 113 229 229 ASN ASN A . n A 1 114 ASP 114 230 230 ASP ASP A . n A 1 115 LYS 115 231 231 LYS LYS A . n A 1 116 ASN 116 232 232 ASN ASN A . n A 1 117 PHE 117 233 233 PHE PHE A . n A 1 118 ASN 118 234 234 ASN ASN A . n A 1 119 GLY 119 235 235 GLY GLY A . n A 1 120 THR 120 236 236 THR THR A . n A 1 121 GLY 121 237 237 GLY GLY A . n A 1 122 PRO 122 238 238 PRO PRO A . n A 1 123 CYS 123 239 239 CYS CYS A . n A 1 124 LYS 124 240 240 LYS LYS A . n A 1 125 ASN 125 241 241 ASN ASN A . n A 1 126 VAL 126 242 242 VAL VAL A . n A 1 127 SER 127 243 243 SER SER A . n A 1 128 SER 128 244 244 SER SER A . n A 1 129 VAL 129 245 245 VAL VAL A . n A 1 130 GLN 130 246 246 GLN GLN A . n A 1 131 CYS 131 247 247 CYS CYS A . n A 1 132 THR 132 248 248 THR THR A . n A 1 133 HIS 133 249 249 HIS HIS A . n A 1 134 GLY 134 250 250 GLY GLY A . n A 1 135 ILE 135 251 251 ILE ILE A . n A 1 136 LYS 136 252 252 LYS LYS A . n A 1 137 PRO 137 253 253 PRO PRO A . n A 1 138 VAL 138 254 254 VAL VAL A . n A 1 139 VAL 139 255 255 VAL VAL A . n A 1 140 SER 140 256 256 SER SER A . n A 1 141 THR 141 257 257 THR THR A . n A 1 142 GLN 142 258 258 GLN GLN A . n A 1 143 LEU 143 259 259 LEU LEU A . n A 1 144 LEU 144 260 260 LEU LEU A . n A 1 145 LEU 145 261 261 LEU LEU A . n A 1 146 ASN 146 262 262 ASN ASN A . n A 1 147 GLY 147 263 263 GLY GLY A . n A 1 148 SER 148 264 264 SER SER A . n A 1 149 LEU 149 265 265 LEU LEU A . n A 1 150 ALA 150 266 266 ALA ALA A . n A 1 151 GLU 151 267 267 GLU GLU A . n A 1 152 GLU 152 268 268 GLU GLU A . n A 1 153 GLU 153 269 269 GLU GLU A . n A 1 154 ILE 154 270 270 ILE ILE A . n A 1 155 ILE 155 271 271 ILE ILE A . n A 1 156 ILE 156 272 272 ILE ILE A . n A 1 157 ARG 157 273 273 ARG ARG A . n A 1 158 SER 158 274 274 SER SER A . n A 1 159 GLU 159 275 275 GLU GLU A . n A 1 160 ASN 160 276 276 ASN ASN A . n A 1 161 LEU 161 277 277 LEU LEU A . n A 1 162 THR 162 278 278 THR THR A . n A 1 163 ASN 163 279 279 ASN ASN A . n A 1 164 ASN 164 280 280 ASN ASN A . n A 1 165 ALA 165 281 281 ALA ALA A . n A 1 166 LYS 166 282 282 LYS LYS A . n A 1 167 THR 167 283 283 THR THR A . n A 1 168 ILE 168 284 284 ILE ILE A . n A 1 169 ILE 169 285 285 ILE ILE A . n A 1 170 VAL 170 286 286 VAL VAL A . n A 1 171 HIS 171 287 287 HIS HIS A . n A 1 172 LEU 172 288 288 LEU LEU A . n A 1 173 ASN 173 289 289 ASN ASN A . n A 1 174 LYS 174 290 290 LYS LYS A . n A 1 175 SER 175 291 291 SER SER A . n A 1 176 VAL 176 292 292 VAL VAL A . n A 1 177 GLU 177 293 293 GLU GLU A . n A 1 178 ILE 178 294 294 ILE ILE A . n A 1 179 ASN 179 295 295 ASN ASN A . n A 1 180 CYS 180 296 296 CYS CYS A . n A 1 181 THR 181 297 297 THR THR A . n A 1 182 ARG 182 298 298 ARG ARG A . n A 1 183 PRO 183 299 299 PRO PRO A . n A 1 184 SER 184 300 300 SER SER A . n A 1 185 ASN 185 301 301 ASN ASN A . n A 1 186 GLY 186 318 ? ? ? A . n A 1 187 GLY 187 319 ? ? ? A . n A 1 188 SER 188 320 ? ? ? A . n A 1 189 GLY 189 321 ? ? ? A . n A 1 190 SER 190 322 ? ? ? A . n A 1 191 GLY 191 323 ? ? ? A . n A 1 192 GLY 192 324 324 GLY GLY A . n A 1 193 ASP 193 325 325 ASP ASP A . n A 1 194 ILE 194 326 326 ILE ILE A . n A 1 195 ARG 195 327 327 ARG ARG A . n A 1 196 LYS 196 328 328 LYS LYS A . n A 1 197 ALA 197 329 329 ALA ALA A . n A 1 198 TYR 198 330 330 TYR TYR A . n A 1 199 CYS 199 331 331 CYS CYS A . n A 1 200 GLU 200 332 332 GLU GLU A . n A 1 201 ILE 201 333 333 ILE ILE A . n A 1 202 ASN 202 334 334 ASN ASN A . n A 1 203 GLY 203 335 335 GLY GLY A . n A 1 204 THR 204 336 336 THR THR A . n A 1 205 LYS 205 337 337 LYS LYS A . n A 1 206 TRP 206 338 338 TRP TRP A . n A 1 207 ASN 207 339 339 ASN ASN A . n A 1 208 LYS 208 340 340 LYS LYS A . n A 1 209 VAL 209 341 341 VAL VAL A . n A 1 210 LEU 210 342 342 LEU LEU A . n A 1 211 LYS 211 343 343 LYS LYS A . n A 1 212 GLN 212 344 344 GLN GLN A . n A 1 213 VAL 213 345 345 VAL VAL A . n A 1 214 THR 214 346 346 THR THR A . n A 1 215 GLU 215 347 347 GLU GLU A . n A 1 216 LYS 216 348 348 LYS LYS A . n A 1 217 LEU 217 349 349 LEU LEU A . n A 1 218 LYS 218 350 350 LYS LYS A . n A 1 219 GLU 219 351 351 GLU GLU A . n A 1 220 HIS 220 352 352 HIS HIS A . n A 1 221 PHE 221 353 353 PHE PHE A . n A 1 222 ASN 222 354 354 ASN ASN A . n A 1 223 ASN 223 355 355 ASN ASN A . n A 1 224 LYS 224 357 357 LYS LYS A . n A 1 225 THR 225 358 358 THR THR A . n A 1 226 ILE 226 359 359 ILE ILE A . n A 1 227 ILE 227 360 360 ILE ILE A . n A 1 228 PHE 228 361 361 PHE PHE A . n A 1 229 GLN 229 362 362 GLN GLN A . n A 1 230 PRO 230 363 363 PRO PRO A . n A 1 231 PRO 231 364 364 PRO PRO A . n A 1 232 SER 232 365 365 SER SER A . n A 1 233 GLY 233 366 366 GLY GLY A . n A 1 234 GLY 234 367 367 GLY GLY A . n A 1 235 ASP 235 368 368 ASP ASP A . n A 1 236 LEU 236 369 369 LEU LEU A . n A 1 237 GLU 237 370 370 GLU GLU A . n A 1 238 ILE 238 371 371 ILE ILE A . n A 1 239 THR 239 372 372 THR THR A . n A 1 240 MET 240 373 373 MET MET A . n A 1 241 HIS 241 374 374 HIS HIS A . n A 1 242 HIS 242 375 375 HIS HIS A . n A 1 243 PHE 243 376 376 PHE PHE A . n A 1 244 ASN 244 377 377 ASN ASN A . n A 1 245 CYS 245 378 378 CYS CYS A . n A 1 246 ARG 246 379 379 ARG ARG A . n A 1 247 GLY 247 380 380 GLY GLY A . n A 1 248 GLU 248 381 381 GLU GLU A . n A 1 249 PHE 249 382 382 PHE PHE A . n A 1 250 PHE 250 383 383 PHE PHE A . n A 1 251 TYR 251 384 384 TYR TYR A . n A 1 252 CYS 252 385 385 CYS CYS A . n A 1 253 ASN 253 386 386 ASN ASN A . n A 1 254 THR 254 387 387 THR THR A . n A 1 255 THR 255 388 388 THR THR A . n A 1 256 GLN 256 389 389 GLN GLN A . n A 1 257 LEU 257 390 390 LEU LEU A . n A 1 258 PHE 258 391 391 PHE PHE A . n A 1 259 ASN 259 392 392 ASN ASN A . n A 1 260 ASN 260 393 393 ASN ASN A . n A 1 261 THR 261 394 394 THR THR A . n A 1 262 CYS 262 395 395 CYS CYS A . n A 1 263 ILE 263 396 396 ILE ILE A . n A 1 264 GLY 264 403 ? ? ? A . n A 1 265 ASN 265 404 ? ? ? A . n A 1 266 GLU 266 405 ? ? ? A . n A 1 267 THR 267 406 ? ? ? A . n A 1 268 MET 268 407 ? ? ? A . n A 1 269 LYS 269 408 408 LYS LYS A . n A 1 270 GLY 270 409 409 GLY GLY A . n A 1 271 CYS 271 410 410 CYS CYS A . n A 1 272 ASN 272 411 411 ASN ASN A . n A 1 273 GLY 273 412 412 GLY GLY A . n A 1 274 THR 274 413 413 THR THR A . n A 1 275 ILE 275 414 414 ILE ILE A . n A 1 276 THR 276 415 415 THR THR A . n A 1 277 LEU 277 416 416 LEU LEU A . n A 1 278 PRO 278 417 417 PRO PRO A . n A 1 279 CYS 279 418 418 CYS CYS A . n A 1 280 LYS 280 419 419 LYS LYS A . n A 1 281 ILE 281 420 420 ILE ILE A . n A 1 282 LYS 282 421 421 LYS LYS A . n A 1 283 GLN 283 422 422 GLN GLN A . n A 1 284 ILE 284 423 423 ILE ILE A . n A 1 285 ILE 285 424 424 ILE ILE A . n A 1 286 ASN 286 425 425 ASN ASN A . n A 1 287 MET 287 426 426 MET MET A . n A 1 288 TRP 288 427 427 TRP TRP A . n A 1 289 GLN 289 428 428 GLN GLN A . n A 1 290 GLY 290 429 429 GLY GLY A . n A 1 291 THR 291 430 430 THR THR A . n A 1 292 GLY 292 431 431 GLY GLY A . n A 1 293 GLN 293 432 432 GLN GLN A . n A 1 294 ALA 294 433 433 ALA ALA A . n A 1 295 MET 295 434 434 MET MET A . n A 1 296 TYR 296 435 435 TYR TYR A . n A 1 297 ALA 297 436 436 ALA ALA A . n A 1 298 PRO 298 437 437 PRO PRO A . n A 1 299 PRO 299 438 438 PRO PRO A . n A 1 300 ILE 300 439 439 ILE ILE A . n A 1 301 ASP 301 440 440 ASP ASP A . n A 1 302 GLY 302 441 441 GLY GLY A . n A 1 303 LYS 303 442 442 LYS LYS A . n A 1 304 ILE 304 443 443 ILE ILE A . n A 1 305 ASN 305 444 444 ASN ASN A . n A 1 306 CYS 306 445 445 CYS CYS A . n A 1 307 VAL 307 446 446 VAL VAL A . n A 1 308 SER 308 447 447 SER SER A . n A 1 309 ASN 309 448 448 ASN ASN A . n A 1 310 ILE 310 449 449 ILE ILE A . n A 1 311 THR 311 450 450 THR THR A . n A 1 312 GLY 312 451 451 GLY GLY A . n A 1 313 ILE 313 452 452 ILE ILE A . n A 1 314 LEU 314 453 453 LEU LEU A . n A 1 315 LEU 315 454 454 LEU LEU A . n A 1 316 THR 316 455 455 THR THR A . n A 1 317 ARG 317 456 456 ARG ARG A . n A 1 318 ASP 318 457 457 ASP ASP A . n A 1 319 GLY 319 458 458 GLY GLY A . n A 1 320 GLY 320 459 459 GLY GLY A . n A 1 321 ALA 321 460 460 ALA ALA A . n A 1 322 ASN 322 461 461 ASN ASN A . n A 1 323 ASN 323 462 462 ASN ASN A . n A 1 324 THR 324 463 463 THR THR A . n A 1 325 SER 325 464 464 SER SER A . n A 1 326 ASN 326 465 465 ASN ASN A . n A 1 327 GLU 327 466 466 GLU GLU A . n A 1 328 THR 328 467 467 THR THR A . n A 1 329 PHE 329 468 468 PHE PHE A . n A 1 330 ARG 330 469 469 ARG ARG A . n A 1 331 PRO 331 470 470 PRO PRO A . n A 1 332 GLY 332 471 471 GLY GLY A . n A 1 333 GLY 333 472 472 GLY GLY A . n A 1 334 GLY 334 473 473 GLY GLY A . n A 1 335 ASN 335 474 474 ASN ASN A . n A 1 336 ILE 336 475 475 ILE ILE A . n A 1 337 LYS 337 476 476 LYS LYS A . n A 1 338 ASP 338 477 477 ASP ASP A . n A 1 339 ASN 339 478 478 ASN ASN A . n A 1 340 TRP 340 479 479 TRP TRP A . n A 1 341 ARG 341 480 480 ARG ARG A . n A 1 342 SER 342 481 481 SER SER A . n A 1 343 GLU 343 482 482 GLU GLU A . n A 1 344 LEU 344 483 483 LEU LEU A . n A 1 345 TYR 345 484 484 TYR TYR A . n A 1 346 LYS 346 485 485 LYS LYS A . n A 1 347 TYR 347 486 486 TYR TYR A . n A 1 348 LYS 348 487 487 LYS LYS A . n A 1 349 VAL 349 488 488 VAL VAL A . n A 1 350 VAL 350 489 489 VAL VAL A . n A 1 351 GLN 351 490 490 GLN GLN A . n A 1 352 ILE 352 491 491 ILE ILE A . n A 1 353 GLU 353 492 492 GLU GLU A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 734 734 NAG NAG A . C 2 NAG 1 741 741 NAG NAG A . D 2 NAG 1 762 762 NAG NAG A . E 2 NAG 1 776 776 NAG NAG A . F 2 NAG 1 789 789 NAG NAG A . G 2 NAG 1 795 795 NAG NAG A . H 2 NAG 1 834 834 NAG NAG A . I 2 NAG 1 886 886 NAG NAG A . J 2 NAG 1 892 892 NAG NAG A . K 2 NAG 1 948 948 NAG NAG A . L 3 EPE 1 1 1 EPE EPE A . M 4 HOH 1 2 2 HOH HOH A . M 4 HOH 2 3 3 HOH HOH A . M 4 HOH 3 4 4 HOH HOH A . M 4 HOH 4 5 5 HOH HOH A . M 4 HOH 5 6 6 HOH HOH A . M 4 HOH 6 7 7 HOH HOH A . M 4 HOH 7 8 8 HOH HOH A . M 4 HOH 8 9 9 HOH HOH A . M 4 HOH 9 10 10 HOH HOH A . M 4 HOH 10 11 11 HOH HOH A . M 4 HOH 11 12 12 HOH HOH A . M 4 HOH 12 13 13 HOH HOH A . M 4 HOH 13 14 14 HOH HOH A . M 4 HOH 14 15 15 HOH HOH A . M 4 HOH 15 16 16 HOH HOH A . M 4 HOH 16 17 17 HOH HOH A . M 4 HOH 17 18 18 HOH HOH A . M 4 HOH 18 19 19 HOH HOH A . M 4 HOH 19 20 20 HOH HOH A . M 4 HOH 20 21 21 HOH HOH A . M 4 HOH 21 22 22 HOH HOH A . M 4 HOH 22 23 23 HOH HOH A . M 4 HOH 23 24 24 HOH HOH A . M 4 HOH 24 25 25 HOH HOH A . M 4 HOH 25 26 26 HOH HOH A . M 4 HOH 26 27 27 HOH HOH A . M 4 HOH 27 28 28 HOH HOH A . M 4 HOH 28 29 29 HOH HOH A . M 4 HOH 29 30 30 HOH HOH A . M 4 HOH 30 31 31 HOH HOH A . M 4 HOH 31 32 32 HOH HOH A . M 4 HOH 32 33 33 HOH HOH A . M 4 HOH 33 34 34 HOH HOH A . M 4 HOH 34 35 35 HOH HOH A . M 4 HOH 35 36 36 HOH HOH A . M 4 HOH 36 37 37 HOH HOH A . M 4 HOH 37 38 38 HOH HOH A . M 4 HOH 38 39 39 HOH HOH A . M 4 HOH 39 40 40 HOH HOH A . M 4 HOH 40 41 41 HOH HOH A . M 4 HOH 41 42 42 HOH HOH A . M 4 HOH 42 43 43 HOH HOH A . M 4 HOH 43 125 125 HOH HOH A . M 4 HOH 44 126 126 HOH HOH A . M 4 HOH 45 127 127 HOH HOH A . M 4 HOH 46 128 128 HOH HOH A . M 4 HOH 47 129 129 HOH HOH A . M 4 HOH 48 130 130 HOH HOH A . M 4 HOH 49 131 131 HOH HOH A . M 4 HOH 50 132 132 HOH HOH A . M 4 HOH 51 133 133 HOH HOH A . M 4 HOH 52 134 134 HOH HOH A . M 4 HOH 53 135 135 HOH HOH A . M 4 HOH 54 136 136 HOH HOH A . M 4 HOH 55 137 137 HOH HOH A . M 4 HOH 56 138 138 HOH HOH A . M 4 HOH 57 139 139 HOH HOH A . M 4 HOH 58 140 140 HOH HOH A . M 4 HOH 59 141 141 HOH HOH A . M 4 HOH 60 142 142 HOH HOH A . M 4 HOH 61 143 143 HOH HOH A . M 4 HOH 62 144 144 HOH HOH A . M 4 HOH 63 145 145 HOH HOH A . M 4 HOH 64 146 146 HOH HOH A . M 4 HOH 65 147 147 HOH HOH A . M 4 HOH 66 148 148 HOH HOH A . M 4 HOH 67 493 1 HOH HOH A . M 4 HOH 68 494 44 HOH HOH A . M 4 HOH 69 495 45 HOH HOH A . M 4 HOH 70 496 46 HOH HOH A . M 4 HOH 71 497 47 HOH HOH A . M 4 HOH 72 498 48 HOH HOH A . M 4 HOH 73 499 49 HOH HOH A . M 4 HOH 74 500 50 HOH HOH A . M 4 HOH 75 501 51 HOH HOH A . M 4 HOH 76 502 52 HOH HOH A . M 4 HOH 77 503 53 HOH HOH A . M 4 HOH 78 504 54 HOH HOH A . M 4 HOH 79 505 55 HOH HOH A . M 4 HOH 80 506 56 HOH HOH A . M 4 HOH 81 507 57 HOH HOH A . M 4 HOH 82 508 58 HOH HOH A . M 4 HOH 83 509 59 HOH HOH A . M 4 HOH 84 510 60 HOH HOH A . M 4 HOH 85 511 61 HOH HOH A . M 4 HOH 86 512 62 HOH HOH A . M 4 HOH 87 513 63 HOH HOH A . M 4 HOH 88 514 64 HOH HOH A . M 4 HOH 89 515 65 HOH HOH A . M 4 HOH 90 516 66 HOH HOH A . M 4 HOH 91 517 67 HOH HOH A . M 4 HOH 92 518 68 HOH HOH A . M 4 HOH 93 519 69 HOH HOH A . M 4 HOH 94 520 70 HOH HOH A . M 4 HOH 95 521 71 HOH HOH A . M 4 HOH 96 522 72 HOH HOH A . M 4 HOH 97 523 73 HOH HOH A . M 4 HOH 98 524 74 HOH HOH A . M 4 HOH 99 525 75 HOH HOH A . M 4 HOH 100 526 76 HOH HOH A . M 4 HOH 101 527 77 HOH HOH A . M 4 HOH 102 528 78 HOH HOH A . M 4 HOH 103 529 79 HOH HOH A . M 4 HOH 104 530 80 HOH HOH A . M 4 HOH 105 531 81 HOH HOH A . M 4 HOH 106 532 82 HOH HOH A . M 4 HOH 107 533 83 HOH HOH A . M 4 HOH 108 534 84 HOH HOH A . M 4 HOH 109 535 85 HOH HOH A . M 4 HOH 110 536 86 HOH HOH A . M 4 HOH 111 537 87 HOH HOH A . M 4 HOH 112 538 88 HOH HOH A . M 4 HOH 113 539 89 HOH HOH A . M 4 HOH 114 540 90 HOH HOH A . M 4 HOH 115 541 91 HOH HOH A . M 4 HOH 116 542 92 HOH HOH A . M 4 HOH 117 543 93 HOH HOH A . M 4 HOH 118 544 94 HOH HOH A . M 4 HOH 119 545 95 HOH HOH A . M 4 HOH 120 546 96 HOH HOH A . M 4 HOH 121 547 97 HOH HOH A . M 4 HOH 122 548 98 HOH HOH A . M 4 HOH 123 549 99 HOH HOH A . M 4 HOH 124 550 100 HOH HOH A . M 4 HOH 125 551 101 HOH HOH A . M 4 HOH 126 552 102 HOH HOH A . M 4 HOH 127 553 103 HOH HOH A . M 4 HOH 128 554 104 HOH HOH A . M 4 HOH 129 555 105 HOH HOH A . M 4 HOH 130 556 106 HOH HOH A . M 4 HOH 131 557 107 HOH HOH A . M 4 HOH 132 558 108 HOH HOH A . M 4 HOH 133 559 109 HOH HOH A . M 4 HOH 134 560 110 HOH HOH A . M 4 HOH 135 561 111 HOH HOH A . M 4 HOH 136 562 112 HOH HOH A . M 4 HOH 137 563 113 HOH HOH A . M 4 HOH 138 564 114 HOH HOH A . M 4 HOH 139 565 115 HOH HOH A . M 4 HOH 140 566 116 HOH HOH A . M 4 HOH 141 567 117 HOH HOH A . M 4 HOH 142 568 118 HOH HOH A . M 4 HOH 143 569 119 HOH HOH A . M 4 HOH 144 570 120 HOH HOH A . M 4 HOH 145 571 121 HOH HOH A . M 4 HOH 146 572 122 HOH HOH A . M 4 HOH 147 573 123 HOH HOH A . M 4 HOH 148 574 124 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 118 A ASN 234 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 202 A ASN 334 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 253 A ASN 386 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 309 A ASN 448 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 173 A ASN 289 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 125 A ASN 241 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 146 A ASN 262 ? ASN 'GLYCOSYLATION SITE' 8 A ASN 179 A ASN 295 ? ASN 'GLYCOSYLATION SITE' 9 A ASN 259 A ASN 392 ? ASN 'GLYCOSYLATION SITE' 10 A ASN 160 A ASN 276 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2012-04-04 2 'Structure model' 1 1 2012-05-23 3 'Structure model' 1 2 2017-11-08 # _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 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 # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 15.7912 7.5291 -18.3549 0.4241 0.3251 0.2948 -0.0748 -0.0077 0.0066 1.3719 0.8971 0.8850 0.0160 -0.9221 -0.5505 -0.0685 -0.1073 0.3159 -0.1386 0.0355 -0.0473 -0.4479 0.3098 0.0401 'X-RAY DIFFRACTION' 2 ? refined 11.6296 -1.6387 -13.8940 0.2575 0.2436 0.2280 -0.0231 0.0274 0.0108 1.3780 2.4082 2.4516 0.6429 0.7281 0.9575 -0.1086 -0.1682 0.1367 0.0236 -0.0019 0.1441 -0.1841 0.0563 0.0820 'X-RAY DIFFRACTION' 3 ? refined 15.9172 -21.2629 -15.1480 0.2850 0.2674 0.3199 0.0524 0.0071 -0.0256 1.8624 2.1698 2.9239 0.3582 1.2056 0.5581 0.0584 0.1011 -0.2977 0.1776 0.1187 -0.2488 0.3329 0.2811 -0.1788 'X-RAY DIFFRACTION' 4 ? refined 16.6589 0.2471 -7.9503 0.2943 0.3541 0.2599 -0.0358 -0.0195 -0.0152 0.5689 1.4921 0.2340 -0.4296 0.0995 -0.4937 -0.1333 -0.3578 0.0285 0.2787 0.1294 -0.0060 -0.0038 0.1200 -0.0069 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? 'chain A and resi 44:89' 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? 'chain A and resi 90:254' 'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? 'chain A and resi 255:474' 'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? 'chain A and resi 475:492' # loop_ _software.pdbx_ordinal _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id 1 PHENIX 1.6.1_357 ? package 'Paul D. Adams' PDAdams@lbl.gov refinement http://www.phenix-online.org/ C++ ? 2 PDB_EXTRACT 3.10 'June 10, 2010' package PDB deposit@deposit.rcsb.org 'data extraction' http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++ ? 3 DENZO . ? ? ? ? 'data reduction' ? ? ? 4 SCALEPACK . ? ? ? ? 'data scaling' ? ? ? # 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 565 ? ? O A HOH 566 ? ? 1.92 2 1 O A HOH 135 ? ? O A HOH 567 ? ? 2.00 3 1 ND2 A ASN 234 ? ? O5 A NAG 734 ? ? 2.02 # 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 88 ? ? 35.01 39.43 2 1 LEU A 116 ? ? -112.54 66.07 3 1 ASP A 211 ? ? -168.87 107.73 4 1 GLN A 258 ? ? 69.17 -59.25 5 1 GLU A 268 ? ? -131.94 -99.50 6 1 ASN A 276 ? ? -173.00 94.68 7 1 PHE A 391 ? ? -108.48 61.19 8 1 ASN A 474 ? ? -178.92 112.89 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A GLY 318 ? A GLY 186 2 1 Y 1 A GLY 319 ? A GLY 187 3 1 Y 1 A SER 320 ? A SER 188 4 1 Y 1 A GLY 321 ? A GLY 189 5 1 Y 1 A SER 322 ? A SER 190 6 1 Y 1 A GLY 323 ? A GLY 191 7 1 Y 1 A GLY 403 ? A GLY 264 8 1 Y 1 A ASN 404 ? A ASN 265 9 1 Y 1 A GLU 405 ? A GLU 266 10 1 Y 1 A THR 406 ? A THR 267 11 1 Y 1 A MET 407 ? A MET 268 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 4 water HOH #