data_4DKQ # _entry.id 4DKQ # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4DKQ RCSB RCSB070451 WWPDB D_1000070451 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 4DKO . unspecified PDB 4DKP . unspecified PDB 4DKR . unspecified # _pdbx_database_status.entry_id 4DKQ _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.recvd_initial_deposition_date 2012-02-03 _pdbx_database_status.status_code REL _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 'LaLonde, J.M.' 2 'Jones, D.M.' 3 'Sun, A.W.' 4 'Courter, J.R.' 5 'Soeta, T.' 6 'Kobayashi, T.' 7 'Princiotto, A.M.' 8 'Wu, X.' 9 'Mascola, J.' 10 'Schon, A.' 11 'Freire, E.' 12 'Sodroski, J.' 13 'Madani, N.' 14 'Smith III, A.B.' 15 'Kwong, P.D.' 16 # _citation.id primary _citation.title 'Structure-Based Design, Synthesis, and Characterization of Dual Hotspot Small-Molecule HIV-1 Entry Inhibitors.' _citation.journal_abbrev J.Med.Chem. _citation.journal_volume 55 _citation.page_first 4382 _citation.page_last 4396 _citation.year 2012 _citation.journal_id_ASTM JMCMAR _citation.country US _citation.journal_id_ISSN 0022-2623 _citation.journal_id_CSD 0151 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 22497421 _citation.pdbx_database_id_DOI 10.1021/jm300265j # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Lalonde, J.M.' 1 primary 'Kwon, Y.D.' 2 primary 'Jones, D.M.' 3 primary 'Sun, A.W.' 4 primary 'Courter, J.R.' 5 primary 'Soeta, T.' 6 primary 'Kobayashi, T.' 7 primary 'Princiotto, A.M.' 8 primary 'Wu, X.' 9 primary 'Schon, A.' 10 primary 'Freire, E.' 11 primary 'Kwong, P.D.' 12 primary 'Mascola, J.R.' 13 primary 'Sodroski, J.' 14 primary 'Madani, N.' 15 primary 'Smith, A.B.' 16 # _cell.entry_id 4DKQ _cell.length_a 63.741 _cell.length_b 67.523 _cell.length_c 89.255 _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 4DKQ _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 'clade A/E 93TH057 HIV-1 gp120 core' 39160.367 1 ? ? ? ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 11 ? ? ? ? 3 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305 1 ? ? ? ? 4 non-polymer syn "N-[(1S,2S)-2-carbamimidamido-2,3-dihydro-1H-inden-1-yl]-N'-(4-chloro-3-fluorophenyl)ethanediamide" 389.811 1 ? ? ? ? 5 water nat water 18.015 198 ? ? ? ? # _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 HSFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRDGG ANNTSNETFRPGGGNIKDNWRSELYKYKVVQIE ; _entity_poly.pdbx_seq_one_letter_code_can ;VWKDADTTLFCASDAKAHETEVHNVWATHACVPTDPNPQEIHLENVTENFNMWKNNMVEQMQEDVISLWDQSLQPCVKLT GGSVIKQACPKISFDPIPIHYCTPAGYVILKCNDKNFNGTGPCKNVSSVQCTHGIKPVVSTQLLLNGSLAEEEIIIRSEN LTNNAKTIIVHLNKSVEINCTRPSNGGSGSGGDIRKAYCEINGTKWNKVLKQVTEKLKEHFNNKTIIFQPPSGGDLEITM HSFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRDGG 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 SER 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 'clade A/E 93TH057' _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 TYPE 1' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 11686 _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 293F _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type plasmid _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name pVRC8400 _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name PDB _struct_ref.db_code 4DKQ _struct_ref.pdbx_db_accession 4DKQ _struct_ref.entity_id 1 _struct_ref.pdbx_align_begin 1 _struct_ref.pdbx_seq_one_letter_code ;VWKDADTTLFCASDAKAHETEVHNVWATHACVPTDPNPQEIHLENVTENFNMWKNNMVEQMQEDVISLWDQSLQPCVKLT GGSVIKQACPKISFDPIPIHYCTPAGYVILKCNDKNFNGTGPCKNVSSVQCTHGIKPVVSTQLLLNGSLAEEEIIIRSEN LTNNAKTIIVHLNKSVEINCTRPSNGGSGSGGDIRKAYCEINGTKWNKVLKQVTEKLKEHFNNKTIIFQPPSGGDLEITM HSFNCRGEFFYCNTTQLFNNTCIGNETMKGCNGTITLPCKIKQIINMWQGTGQAMYAPPIDGKINCVSNITGILLTRDGG ANNTSNETFRPGGGNIKDNWRSELYKYKVVQIE ; _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 4DKQ _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 4DKQ _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 0LK non-polymer . "N-[(1S,2S)-2-carbamimidamido-2,3-dihydro-1H-inden-1-yl]-N'-(4-chloro-3-fluorophenyl)ethanediamide" ? 'C18 H17 Cl F N5 O2' 389.811 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.crystals_number 1 _exptl.entry_id 4DKQ _exptl.method 'X-RAY DIFFRACTION' # _exptl_crystal.id 1 _exptl_crystal.density_Matthews 2.45 _exptl_crystal.density_meas ? _exptl_crystal.density_percent_sol 49.85 _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.pH 7.5 _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pdbx_details '10% PEG 8000, 5% iso-propanol, 0.1M HEPES 7.5 , VAPOR DIFFUSION, HANGING DROP, temperature 293K' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type 'MAR scanner 300 mm plate' _diffrn_detector.pdbx_collection_date 2011-01-01 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _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-ID' _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1 _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 22-ID # _reflns.entry_id 4DKQ _reflns.observed_criterion_sigma_F 0.0 _reflns.observed_criterion_sigma_I 0.0 _reflns.d_resolution_high 1.8880 _reflns.d_resolution_low 50 _reflns.number_all 31547 _reflns.number_obs 30727 _reflns.percent_possible_obs 97.4 _reflns.pdbx_Rmerge_I_obs 0.080 _reflns.pdbx_Rsym_value 0.090 _reflns.pdbx_netI_over_sigmaI 34.7 _reflns.B_iso_Wilson_estimate 28.1 _reflns.pdbx_redundancy 5.2 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.89 _reflns_shell.d_res_low 1.92 _reflns_shell.percent_possible_obs ? _reflns_shell.percent_possible_all 72.1 _reflns_shell.Rmerge_I_obs 0.368 _reflns_shell.meanI_over_sigI_obs 2.5 _reflns_shell.pdbx_Rsym_value 0.379 _reflns_shell.pdbx_redundancy 1.9 _reflns_shell.number_unique_all 1107 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 4DKQ _refine.ls_d_res_high 1.8880 _refine.ls_d_res_low 46.3510 _refine.pdbx_ls_sigma_F 0.000 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_percent_reflns_obs 94.3900 _refine.ls_number_reflns_obs 29830 _refine.ls_number_reflns_all ? _refine.pdbx_ls_cross_valid_method ? _refine.pdbx_R_Free_selection_details Random _refine.details ? _refine.ls_R_factor_all 0.1937 _refine.ls_R_factor_obs 0.1937 _refine.ls_R_factor_R_work 0.1916 _refine.ls_wR_factor_R_work ? _refine.ls_R_factor_R_free 0.2330 _refine.ls_wR_factor_R_free ? _refine.ls_percent_reflns_R_free 4.9800 _refine.ls_number_reflns_R_free 1485 _refine.ls_R_factor_R_free_error ? _refine.B_iso_mean 34.0177 _refine.solvent_model_param_bsol 29.6790 _refine.solvent_model_param_ksol 0.3430 _refine.pdbx_isotropic_thermal_model ? _refine.aniso_B[1][1] 5.7261 _refine.aniso_B[2][2] -4.5338 _refine.aniso_B[3][3] -1.1923 _refine.aniso_B[1][2] -0.0000 _refine.aniso_B[1][3] -0.0000 _refine.aniso_B[2][3] -0.0000 _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.2200 _refine.overall_SU_B ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.pdbx_solvent_vdw_probe_radii 1.2000 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.9500 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.pdbx_starting_model 3TGT _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.overall_FOM_work_R_set ? _refine.B_iso_max 94.930 _refine.B_iso_min 13.770 _refine.pdbx_overall_phase_error 20.8600 _refine.occupancy_max 1.000 _refine.occupancy_min 1.000 _refine.pdbx_ls_sigma_I ? _refine.ls_redundancy_reflns_obs ? _refine.ls_R_factor_R_free_error_details ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.overall_FOM_free_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2654 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 196 _refine_hist.number_atoms_solvent 198 _refine_hist.number_atoms_total 3048 _refine_hist.d_res_high 1.8880 _refine_hist.d_res_low 46.3510 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.number _refine_ls_restr.weight _refine_ls_restr.pdbx_restraint_function _refine_ls_restr.pdbx_refine_id f_bond_d 0.007 ? ? ? ? 'X-RAY DIFFRACTION' f_angle_d 0.869 ? ? ? ? 'X-RAY DIFFRACTION' f_chiral_restr 0.054 ? ? ? ? 'X-RAY DIFFRACTION' f_plane_restr 0.012 ? ? ? ? 'X-RAY DIFFRACTION' f_dihedral_angle_d 12.849 ? ? ? ? 'X-RAY DIFFRACTION' # loop_ _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_obs _refine_ls_shell.number_reflns_R_free _refine_ls_shell.R_factor_R_work _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_obs _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.number_reflns_R_work _refine_ls_shell.redundancy_reflns_obs _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all _refine_ls_shell.pdbx_refine_id 1.8882 1.9492 1829 108 0.2379 0.2622 . 72.1 . . . . . . 'X-RAY DIFFRACTION' 1.9492 2.0188 2438 1470 0.1964 0.2118 . 90.7 . . . . . . 'X-RAY DIFFRACTION' # _struct.entry_id 4DKQ _struct.title 'Crystal structure of clade A/E 93TH057 HIV-1 gp120 core in complex with DMJ-I-228' _struct.pdbx_descriptor 'clade A/E 93TH057 HIV-1 gp120 core' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4DKQ _struct_keywords.pdbx_keywords 'VIRAL PROTEIN/INHIBITOR' _struct_keywords.text 'HIV-1 gp120, clade A/E, CD4 mimic, DMJ-I-228, VIRAL PROTEIN-INHIBITOR complex' # 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 2 ? M N N 3 ? N N N 4 ? O N N 5 ? # _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 ILE A 336 ? TYR A 345 ? ILE A 475 TYR A 484 1 ? 10 # _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 ? ? ? ? ? ? ? 2.041 ? disulf2 disulf ? ? A CYS 102 SG ? ? ? 1_555 A CYS 131 SG ? ? A CYS 218 A CYS 247 1_555 ? ? ? ? ? ? ? 2.043 ? disulf3 disulf ? ? A CYS 112 SG ? ? ? 1_555 A CYS 123 SG ? ? A CYS 228 A CYS 239 1_555 ? ? ? ? ? ? ? 2.053 ? disulf4 disulf ? ? A CYS 180 SG ? ? ? 1_555 A CYS 199 SG ? ? A CYS 296 A CYS 331 1_555 ? ? ? ? ? ? ? 1.875 ? disulf5 disulf ? ? A CYS 245 SG ? ? ? 1_555 A CYS 306 SG ? ? A CYS 378 A CYS 445 1_555 ? ? ? ? ? ? ? 2.032 ? disulf6 disulf ? ? A CYS 252 SG ? ? ? 1_555 A CYS 279 SG ? ? A CYS 385 A CYS 418 1_555 ? ? ? ? ? ? ? 2.039 ? covale1 covale ? ? A CYS 76 SG ? ? ? 1_555 A CYS 89 SG ? ? A CYS 119 A CYS 205 1_555 ? ? ? ? ? ? ? 1.524 ? covale2 covale ? ? A ASN 179 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 295 A NAG 606 1_555 ? ? ? ? ? ? ? 1.297 ? covale3 covale ? ? A ASN 160 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 276 A NAG 604 1_555 ? ? ? ? ? ? ? 1.365 ? covale4 covale ? ? A ASN 223 ND2 ? ? ? 1_555 I NAG . C1 ? ? A ASN 355 A NAG 608 1_555 ? ? ? ? ? ? ? 1.409 ? covale5 covale ? ? A ASN 309 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 448 A NAG 611 1_555 ? ? ? ? ? ? ? 1.437 ? covale6 covale ? ? A ASN 259 ND2 ? ? ? 1_555 K NAG . C1 ? ? A ASN 392 A NAG 610 1_555 ? ? ? ? ? ? ? 1.438 ? covale7 covale ? ? A ASN 125 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 241 A NAG 602 1_555 ? ? ? ? ? ? ? 1.439 ? covale8 covale ? ? A ASN 253 ND2 ? ? ? 1_555 J NAG . C1 ? ? A ASN 386 A NAG 609 1_555 ? ? ? ? ? ? ? 1.439 ? covale9 covale ? ? A ASN 202 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 334 A NAG 607 1_555 ? ? ? ? ? ? ? 1.440 ? covale10 covale ? ? A ASN 118 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 234 A NAG 601 1_555 ? ? ? ? ? ? ? 1.442 ? covale11 covale ? ? A ASN 146 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 262 A NAG 603 1_555 ? ? ? ? ? ? ? 1.443 ? covale12 covale ? ? A ASN 173 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 289 A NAG 605 1_555 ? ? ? ? ? ? ? 1.445 ? # 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 ? LYS A 282 ? THR A 413 LYS A 421 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 ILE A 85 ? O ILE A 201 N LYS A 78 ? N LYS A 121 D 2 3 N VAL A 77 ? N VAL A 120 O MET A 295 ? O MET A 434 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 282 ? O LYS A 421 N PHE A 249 ? N PHE A 382 F 6 7 O CYS A 252 ? O CYS A 385 N HIS A 241 ? N HIS A 374 # 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 ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 601' AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 602' AC3 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE NAG A 603' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 604' AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 605' AC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 606' AC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 607' AC8 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 608' AC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 609' BC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 610' BC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 611' BC3 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE EPE A 612' BC4 Software ? ? ? ? 14 'BINDING SITE FOR RESIDUE 0LK A 613' # 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 5 ASN A 118 ? ASN A 234 . ? 1_555 ? 2 AC1 5 THR A 120 ? THR A 236 . ? 1_555 ? 3 AC1 5 ILE A 156 ? ILE A 272 . ? 1_555 ? 4 AC1 5 HOH O . ? HOH A 750 . ? 1_555 ? 5 AC1 5 HOH O . ? HOH A 830 . ? 1_555 ? 6 AC2 2 ASN A 113 ? ASN A 229 . ? 1_555 ? 7 AC2 2 ASN A 125 ? ASN A 241 . ? 1_555 ? 8 AC3 11 ASN A 146 ? ASN A 262 . ? 1_555 ? 9 AC3 11 ARG A 246 ? ARG A 379 . ? 1_555 ? 10 AC3 11 CYS A 306 ? CYS A 445 . ? 1_555 ? 11 AC3 11 VAL A 307 ? VAL A 446 . ? 1_555 ? 12 AC3 11 SER A 308 ? SER A 447 . ? 1_555 ? 13 AC3 11 NAG L . ? NAG A 611 . ? 1_555 ? 14 AC3 11 HOH O . ? HOH A 716 . ? 1_555 ? 15 AC3 11 HOH O . ? HOH A 727 . ? 1_555 ? 16 AC3 11 HOH O . ? HOH A 749 . ? 1_555 ? 17 AC3 11 HOH O . ? HOH A 768 . ? 1_555 ? 18 AC3 11 HOH O . ? HOH A 790 . ? 1_555 ? 19 AC4 5 ASN A 160 ? ASN A 276 . ? 1_555 ? 20 AC4 5 ASN A 163 ? ASN A 279 . ? 1_555 ? 21 AC4 5 HOH O . ? HOH A 776 . ? 1_555 ? 22 AC4 5 HOH O . ? HOH A 861 . ? 1_555 ? 23 AC4 5 HOH O . ? HOH A 869 . ? 1_555 ? 24 AC5 6 GLU A 153 ? GLU A 269 . ? 1_555 ? 25 AC5 6 ILE A 154 ? ILE A 270 . ? 1_555 ? 26 AC5 6 ASN A 173 ? ASN A 289 . ? 1_555 ? 27 AC5 6 LYS A 216 ? LYS A 348 . ? 1_555 ? 28 AC5 6 HOH O . ? HOH A 855 . ? 1_555 ? 29 AC5 6 HOH O . ? HOH A 872 . ? 1_555 ? 30 AC6 5 ASN A 179 ? ASN A 295 . ? 1_555 ? 31 AC6 5 THR A 181 ? THR A 297 . ? 1_555 ? 32 AC6 5 TYR A 198 ? TYR A 330 . ? 1_555 ? 33 AC6 5 GLU A 200 ? GLU A 332 . ? 1_555 ? 34 AC6 5 HOH O . ? HOH A 765 . ? 1_555 ? 35 AC7 6 PRO A 38 ? PRO A 81 . ? 3_445 ? 36 AC7 6 GLU A 40 ? GLU A 83 . ? 3_445 ? 37 AC7 6 ASN A 202 ? ASN A 334 . ? 1_555 ? 38 AC7 6 LYS A 205 ? LYS A 337 . ? 1_555 ? 39 AC7 6 GLY A 273 ? GLY A 412 . ? 1_555 ? 40 AC7 6 THR A 274 ? THR A 413 . ? 1_555 ? 41 AC8 7 GLU A 215 ? GLU A 347 . ? 1_555 ? 42 AC8 7 ASN A 223 ? ASN A 355 . ? 1_555 ? 43 AC8 7 ASN A 335 ? ASN A 474 . ? 4_445 ? 44 AC8 7 LYS A 337 ? LYS A 476 . ? 4_445 ? 45 AC8 7 HOH O . ? HOH A 737 . ? 4_445 ? 46 AC8 7 HOH O . ? HOH A 802 . ? 4_445 ? 47 AC8 7 HOH O . ? HOH A 809 . ? 1_555 ? 48 AC9 3 ASN A 253 ? ASN A 386 . ? 1_555 ? 49 AC9 3 THR A 255 ? THR A 388 . ? 1_555 ? 50 AC9 3 HOH O . ? HOH A 819 . ? 1_555 ? 51 BC1 4 THR A 255 ? THR A 388 . ? 1_555 ? 52 BC1 4 GLN A 256 ? GLN A 389 . ? 1_555 ? 53 BC1 4 ASN A 259 ? ASN A 392 . ? 1_555 ? 54 BC1 4 CYS A 262 ? CYS A 395 . ? 1_555 ? 55 BC2 3 SER A 175 ? SER A 291 . ? 1_555 ? 56 BC2 3 ASN A 309 ? ASN A 448 . ? 1_555 ? 57 BC2 3 NAG D . ? NAG A 603 . ? 1_555 ? 58 BC3 12 LEU A 9 ? LEU A 52 . ? 1_555 ? 59 BC3 12 CYS A 11 ? CYS A 54 . ? 1_555 ? 60 BC3 12 ALA A 30 ? ALA A 73 . ? 1_555 ? 61 BC3 12 GLN A 60 ? GLN A 103 . ? 1_555 ? 62 BC3 12 ASP A 64 ? ASP A 107 . ? 1_555 ? 63 BC3 12 TYR A 101 ? TYR A 217 . ? 1_555 ? 64 BC3 12 ARG A 195 ? ARG A 327 . ? 3_555 ? 65 BC3 12 LYS A 280 ? LYS A 419 . ? 3_555 ? 66 BC3 12 LYS A 282 ? LYS A 421 . ? 3_555 ? 67 BC3 12 GLN A 283 ? GLN A 422 . ? 3_555 ? 68 BC3 12 ILE A 284 ? ILE A 423 . ? 3_555 ? 69 BC3 12 HOH O . ? HOH A 797 . ? 1_555 ? 70 BC4 14 VAL A 139 ? VAL A 255 . ? 1_555 ? 71 BC4 14 SER A 140 ? SER A 256 . ? 1_555 ? 72 BC4 14 ASP A 235 ? ASP A 368 . ? 1_555 ? 73 BC4 14 GLU A 237 ? GLU A 370 . ? 1_555 ? 74 BC4 14 SER A 242 ? SER A 375 . ? 1_555 ? 75 BC4 14 PHE A 243 ? PHE A 376 . ? 1_555 ? 76 BC4 14 PHE A 249 ? PHE A 382 . ? 1_555 ? 77 BC4 14 ILE A 285 ? ILE A 424 . ? 1_555 ? 78 BC4 14 ASN A 286 ? ASN A 425 . ? 1_555 ? 79 BC4 14 MET A 287 ? MET A 426 . ? 1_555 ? 80 BC4 14 TRP A 288 ? TRP A 427 . ? 1_555 ? 81 BC4 14 GLY A 334 ? GLY A 473 . ? 1_555 ? 82 BC4 14 ASN A 335 ? ASN A 474 . ? 1_555 ? 83 BC4 14 HOH O . ? HOH A 895 . ? 4_545 ? # _atom_sites.entry_id 4DKQ _atom_sites.fract_transf_matrix[1][1] 0.015688 _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] 0.014810 _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] 0.011204 _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 CL F 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 ? -24.451 18.250 0.894 1.00 42.84 ? 44 VAL A N 1 ATOM 2 C CA . VAL A 1 1 ? -23.937 17.279 -0.065 1.00 42.86 ? 44 VAL A CA 1 ATOM 3 C C . VAL A 1 1 ? -22.534 16.829 0.335 1.00 40.78 ? 44 VAL A C 1 ATOM 4 O O . VAL A 1 1 ? -21.816 17.548 1.033 1.00 44.79 ? 44 VAL A O 1 ATOM 5 C CB . VAL A 1 1 ? -23.920 17.849 -1.493 1.00 52.74 ? 44 VAL A CB 1 ATOM 6 C CG1 . VAL A 1 1 ? -22.983 19.032 -1.570 1.00 56.82 ? 44 VAL A CG1 1 ATOM 7 C CG2 . VAL A 1 1 ? -23.516 16.777 -2.494 1.00 54.02 ? 44 VAL A CG2 1 ATOM 8 N N . TRP A 1 2 ? -22.149 15.639 -0.114 1.00 33.85 ? 45 TRP A N 1 ATOM 9 C CA . TRP A 1 2 ? -20.934 14.993 0.364 1.00 35.84 ? 45 TRP A CA 1 ATOM 10 C C . TRP A 1 2 ? -20.354 14.063 -0.701 1.00 37.41 ? 45 TRP A C 1 ATOM 11 O O . TRP A 1 2 ? -20.968 13.845 -1.742 1.00 41.78 ? 45 TRP A O 1 ATOM 12 C CB . TRP A 1 2 ? -21.267 14.179 1.610 1.00 35.16 ? 45 TRP A CB 1 ATOM 13 C CG . TRP A 1 2 ? -22.316 13.152 1.331 1.00 40.56 ? 45 TRP A CG 1 ATOM 14 C CD1 . TRP A 1 2 ? -22.134 11.938 0.734 1.00 41.08 ? 45 TRP A CD1 1 ATOM 15 C CD2 . TRP A 1 2 ? -23.717 13.254 1.612 1.00 46.50 ? 45 TRP A CD2 1 ATOM 16 N NE1 . TRP A 1 2 ? -23.331 11.276 0.632 1.00 40.72 ? 45 TRP A NE1 1 ATOM 17 C CE2 . TRP A 1 2 ? -24.319 12.061 1.165 1.00 44.74 ? 45 TRP A CE2 1 ATOM 18 C CE3 . TRP A 1 2 ? -24.519 14.234 2.202 1.00 52.26 ? 45 TRP A CE3 1 ATOM 19 C CZ2 . TRP A 1 2 ? -25.685 11.822 1.290 1.00 52.24 ? 45 TRP A CZ2 1 ATOM 20 C CZ3 . TRP A 1 2 ? -25.877 13.996 2.323 1.00 57.94 ? 45 TRP A CZ3 1 ATOM 21 C CH2 . TRP A 1 2 ? -26.445 12.799 1.872 1.00 54.46 ? 45 TRP A CH2 1 ATOM 22 N N . LYS A 1 3 ? -19.173 13.511 -0.430 1.00 34.56 ? 46 LYS A N 1 ATOM 23 C CA . LYS A 1 3 ? -18.540 12.541 -1.324 1.00 36.76 ? 46 LYS A CA 1 ATOM 24 C C . LYS A 1 3 ? -17.732 11.533 -0.510 1.00 35.14 ? 46 LYS A C 1 ATOM 25 O O . LYS A 1 3 ? -17.253 11.856 0.579 1.00 37.09 ? 46 LYS A O 1 ATOM 26 C CB . LYS A 1 3 ? -17.621 13.246 -2.321 1.00 37.81 ? 46 LYS A CB 1 ATOM 27 C CG . LYS A 1 3 ? -16.281 13.660 -1.736 1.00 47.64 ? 46 LYS A CG 1 ATOM 28 C CD . LYS A 1 3 ? -15.455 14.459 -2.731 1.00 60.04 ? 46 LYS A CD 1 ATOM 29 C CE . LYS A 1 3 ? -14.158 14.946 -2.098 1.00 65.67 ? 46 LYS A CE 1 ATOM 30 N NZ . LYS A 1 3 ? -13.555 16.082 -2.857 1.00 66.66 ? 46 LYS A NZ 1 ATOM 31 N N . ASP A 1 4 ? -17.585 10.313 -1.024 1.00 33.88 ? 47 ASP A N 1 ATOM 32 C CA . ASP A 1 4 ? -16.804 9.296 -0.320 1.00 34.98 ? 47 ASP A CA 1 ATOM 33 C C . ASP A 1 4 ? -15.383 9.800 -0.112 1.00 32.67 ? 47 ASP A C 1 ATOM 34 O O . ASP A 1 4 ? -14.788 10.379 -1.019 1.00 33.85 ? 47 ASP A O 1 ATOM 35 C CB . ASP A 1 4 ? -16.766 7.981 -1.103 1.00 40.46 ? 47 ASP A CB 1 ATOM 36 C CG . ASP A 1 4 ? -18.132 7.349 -1.258 1.00 40.72 ? 47 ASP A CG 1 ATOM 37 O OD1 . ASP A 1 4 ? -19.048 7.702 -0.492 1.00 35.08 ? 47 ASP A OD1 1 ATOM 38 O OD2 . ASP A 1 4 ? -18.288 6.489 -2.149 1.00 51.55 ? 47 ASP A OD2 1 ATOM 39 N N . ALA A 1 5 ? -14.831 9.576 1.076 1.00 29.66 ? 48 ALA A N 1 ATOM 40 C CA . ALA A 1 5 ? -13.488 10.057 1.368 1.00 32.22 ? 48 ALA A CA 1 ATOM 41 C C . ALA A 1 5 ? -12.825 9.263 2.478 1.00 35.37 ? 48 ALA A C 1 ATOM 42 O O . ALA A 1 5 ? -13.497 8.667 3.315 1.00 31.07 ? 48 ALA A O 1 ATOM 43 C CB . ALA A 1 5 ? -13.524 11.523 1.736 1.00 32.84 ? 48 ALA A CB 1 ATOM 44 N N . ASP A 1 6 ? -11.498 9.263 2.473 1.00 34.97 ? 49 ASP A N 1 ATOM 45 C CA . ASP A 1 6 ? -10.729 8.694 3.565 1.00 32.65 ? 49 ASP A CA 1 ATOM 46 C C . ASP A 1 6 ? -10.112 9.816 4.381 1.00 30.25 ? 49 ASP A C 1 ATOM 47 O O . ASP A 1 6 ? -9.711 10.848 3.838 1.00 31.25 ? 49 ASP A O 1 ATOM 48 C CB . ASP A 1 6 ? -9.620 7.785 3.036 1.00 36.31 ? 49 ASP A CB 1 ATOM 49 C CG . ASP A 1 6 ? -10.155 6.513 2.413 1.00 41.68 ? 49 ASP A CG 1 ATOM 50 O OD1 . ASP A 1 6 ? -11.328 6.167 2.671 1.00 39.70 ? 49 ASP A OD1 1 ATOM 51 O OD2 . ASP A 1 6 ? -9.395 5.855 1.671 1.00 42.78 ? 49 ASP A OD2 1 ATOM 52 N N . THR A 1 7 ? -10.047 9.614 5.688 1.00 25.07 ? 50 THR A N 1 ATOM 53 C CA . THR A 1 7 ? -9.374 10.553 6.572 1.00 28.58 ? 50 THR A CA 1 ATOM 54 C C . THR A 1 7 ? -9.079 9.828 7.872 1.00 27.73 ? 50 THR A C 1 ATOM 55 O O . THR A 1 7 ? -9.637 8.761 8.135 1.00 25.64 ? 50 THR A O 1 ATOM 56 C CB . THR A 1 7 ? -10.223 11.819 6.844 1.00 34.58 ? 50 THR A CB 1 ATOM 57 O OG1 . THR A 1 7 ? -9.405 12.836 7.443 1.00 31.56 ? 50 THR A OG1 1 ATOM 58 C CG2 . THR A 1 7 ? -11.398 11.499 7.763 1.00 34.75 ? 50 THR A CG2 1 ATOM 59 N N . THR A 1 8 ? -8.190 10.393 8.677 1.00 26.70 ? 51 THR A N 1 ATOM 60 C CA . THR A 1 8 ? -7.843 9.779 9.951 1.00 25.62 ? 51 THR A CA 1 ATOM 61 C C . THR A 1 8 ? -8.957 9.986 10.968 1.00 25.26 ? 51 THR A C 1 ATOM 62 O O . THR A 1 8 ? -9.369 11.109 11.243 1.00 25.32 ? 51 THR A O 1 ATOM 63 C CB . THR A 1 8 ? -6.497 10.308 10.494 1.00 28.66 ? 51 THR A CB 1 ATOM 64 O OG1 . THR A 1 8 ? -5.462 10.027 9.541 1.00 31.13 ? 51 THR A OG1 1 ATOM 65 C CG2 . THR A 1 8 ? -6.147 9.628 11.813 1.00 29.77 ? 51 THR A CG2 1 ATOM 66 N N . LEU A 1 9 ? -9.451 8.879 11.508 1.00 20.54 ? 52 LEU A N 1 ATOM 67 C CA . LEU A 1 9 ? -10.501 8.902 12.511 1.00 21.21 ? 52 LEU A CA 1 ATOM 68 C C . LEU A 1 9 ? -9.886 9.087 13.892 1.00 23.18 ? 52 LEU A C 1 ATOM 69 O O . LEU A 1 9 ? -8.679 8.937 14.068 1.00 21.87 ? 52 LEU A O 1 ATOM 70 C CB . LEU A 1 9 ? -11.265 7.575 12.473 1.00 19.11 ? 52 LEU A CB 1 ATOM 71 C CG . LEU A 1 9 ? -11.785 7.209 11.081 1.00 20.76 ? 52 LEU A CG 1 ATOM 72 C CD1 . LEU A 1 9 ? -12.363 5.802 11.066 1.00 26.21 ? 52 LEU A CD1 1 ATOM 73 C CD2 . LEU A 1 9 ? -12.821 8.235 10.638 1.00 27.41 ? 52 LEU A CD2 1 ATOM 74 N N . PHE A 1 10 ? -10.712 9.426 14.872 1.00 20.59 ? 53 PHE A N 1 ATOM 75 C CA . PHE A 1 10 ? -10.273 9.334 16.251 1.00 22.73 ? 53 PHE A CA 1 ATOM 76 C C . PHE A 1 10 ? -11.184 8.357 16.980 1.00 25.19 ? 53 PHE A C 1 ATOM 77 O O . PHE A 1 10 ? -12.198 7.918 16.435 1.00 22.69 ? 53 PHE A O 1 ATOM 78 C CB . PHE A 1 10 ? -10.202 10.705 16.943 1.00 20.47 ? 53 PHE A CB 1 ATOM 79 C CG . PHE A 1 10 ? -11.534 11.395 17.111 1.00 26.12 ? 53 PHE A CG 1 ATOM 80 C CD1 . PHE A 1 10 ? -12.032 12.227 16.118 1.00 27.57 ? 53 PHE A CD1 1 ATOM 81 C CD2 . PHE A 1 10 ? -12.265 11.245 18.281 1.00 24.10 ? 53 PHE A CD2 1 ATOM 82 C CE1 . PHE A 1 10 ? -13.245 12.875 16.277 1.00 33.33 ? 53 PHE A CE1 1 ATOM 83 C CE2 . PHE A 1 10 ? -13.479 11.889 18.447 1.00 29.60 ? 53 PHE A CE2 1 ATOM 84 C CZ . PHE A 1 10 ? -13.970 12.705 17.443 1.00 32.40 ? 53 PHE A CZ 1 ATOM 85 N N . CYS A 1 11 ? -10.809 7.989 18.194 1.00 17.08 ? 54 CYS A N 1 ATOM 86 C CA . CYS A 1 11 ? -11.623 7.040 18.940 1.00 19.30 ? 54 CYS A CA 1 ATOM 87 C C . CYS A 1 11 ? -12.180 7.672 20.207 1.00 24.89 ? 54 CYS A C 1 ATOM 88 O O . CYS A 1 11 ? -11.610 8.624 20.751 1.00 23.24 ? 54 CYS A O 1 ATOM 89 C CB . CYS A 1 11 ? -10.843 5.755 19.241 1.00 23.74 ? 54 CYS A CB 1 ATOM 90 S SG . CYS A 1 11 ? -9.334 5.975 20.213 1.00 29.73 ? 54 CYS A SG 1 ATOM 91 N N . ALA A 1 12 ? -13.318 7.151 20.651 1.00 18.87 ? 55 ALA A N 1 ATOM 92 C CA . ALA A 1 12 ? -13.949 7.602 21.877 1.00 24.05 ? 55 ALA A CA 1 ATOM 93 C C . ALA A 1 12 ? -14.371 6.378 22.670 1.00 23.87 ? 55 ALA A C 1 ATOM 94 O O . ALA A 1 12 ? -14.678 5.333 22.091 1.00 26.15 ? 55 ALA A O 1 ATOM 95 C CB . ALA A 1 12 ? -15.150 8.482 21.566 1.00 19.51 ? 55 ALA A CB 1 ATOM 96 N N . SER A 1 13 ? -14.376 6.499 23.992 1.00 24.06 ? 56 SER A N 1 ATOM 97 C CA . SER A 1 13 ? -14.700 5.361 24.845 1.00 24.32 ? 56 SER A CA 1 ATOM 98 C C . SER A 1 13 ? -15.067 5.825 26.243 1.00 23.74 ? 56 SER A C 1 ATOM 99 O O . SER A 1 13 ? -14.894 6.998 26.582 1.00 21.99 ? 56 SER A O 1 ATOM 100 C CB . SER A 1 13 ? -13.516 4.391 24.926 1.00 27.78 ? 56 SER A CB 1 ATOM 101 O OG . SER A 1 13 ? -12.616 4.775 25.958 1.00 27.93 ? 56 SER A OG 1 ATOM 102 N N . ASP A 1 14 ? -15.571 4.896 27.052 1.00 23.37 ? 57 ASP A N 1 ATOM 103 C CA . ASP A 1 14 ? -15.901 5.187 28.440 1.00 26.95 ? 57 ASP A CA 1 ATOM 104 C C . ASP A 1 14 ? -14.867 4.546 29.357 1.00 28.91 ? 57 ASP A C 1 ATOM 105 O O . ASP A 1 14 ? -15.170 4.163 30.487 1.00 29.20 ? 57 ASP A O 1 ATOM 106 C CB . ASP A 1 14 ? -17.311 4.691 28.778 1.00 31.04 ? 57 ASP A CB 1 ATOM 107 C CG . ASP A 1 14 ? -18.397 5.470 28.049 1.00 38.70 ? 57 ASP A CG 1 ATOM 108 O OD1 . ASP A 1 14 ? -18.327 6.717 28.029 1.00 39.72 ? 57 ASP A OD1 1 ATOM 109 O OD2 . ASP A 1 14 ? -19.317 4.836 27.486 1.00 40.61 ? 57 ASP A OD2 1 ATOM 110 N N . ALA A 1 15 ? -13.638 4.441 28.860 1.00 28.21 ? 58 ALA A N 1 ATOM 111 C CA . ALA A 1 15 ? -12.543 3.844 29.622 1.00 25.71 ? 58 ALA A CA 1 ATOM 112 C C . ALA A 1 15 ? -12.378 4.494 30.994 1.00 29.30 ? 58 ALA A C 1 ATOM 113 O O . ALA A 1 15 ? -12.559 5.705 31.143 1.00 31.88 ? 58 ALA A O 1 ATOM 114 C CB . ALA A 1 15 ? -11.249 3.941 28.843 1.00 24.14 ? 58 ALA A CB 1 ATOM 115 N N . LYS A 1 16 ? -12.025 3.679 31.985 1.00 29.36 ? 59 LYS A N 1 ATOM 116 C CA . LYS A 1 16 ? -11.807 4.143 33.354 1.00 31.67 ? 59 LYS A CA 1 ATOM 117 C C . LYS A 1 16 ? -10.331 4.426 33.606 1.00 28.11 ? 59 LYS A C 1 ATOM 118 O O . LYS A 1 16 ? -9.488 3.553 33.416 1.00 26.64 ? 59 LYS A O 1 ATOM 119 C CB . LYS A 1 16 ? -12.291 3.092 34.352 1.00 36.28 ? 59 LYS A CB 1 ATOM 120 C CG . LYS A 1 16 ? -13.791 3.079 34.586 1.00 49.97 ? 59 LYS A CG 1 ATOM 121 C CD . LYS A 1 16 ? -14.568 2.905 33.297 1.00 61.31 ? 59 LYS A CD 1 ATOM 122 C CE . LYS A 1 16 ? -16.065 2.862 33.564 1.00 67.05 ? 59 LYS A CE 1 ATOM 123 N NZ . LYS A 1 16 ? -16.862 2.967 32.309 1.00 65.66 ? 59 LYS A NZ 1 ATOM 124 N N . ALA A 1 17 ? -10.026 5.645 34.040 1.00 28.12 ? 60 ALA A N 1 ATOM 125 C CA . ALA A 1 17 ? -8.643 6.068 34.242 1.00 35.43 ? 60 ALA A CA 1 ATOM 126 C C . ALA A 1 17 ? -7.955 5.361 35.415 1.00 36.71 ? 60 ALA A C 1 ATOM 127 O O . ALA A 1 17 ? -6.726 5.316 35.481 1.00 37.31 ? 60 ALA A O 1 ATOM 128 C CB . ALA A 1 17 ? -8.571 7.581 34.413 1.00 39.35 ? 60 ALA A CB 1 ATOM 129 N N . HIS A 1 18 ? -8.746 4.810 36.332 1.00 31.74 ? 61 HIS A N 1 ATOM 130 C CA . HIS A 1 18 ? -8.203 4.121 37.502 1.00 31.45 ? 61 HIS A CA 1 ATOM 131 C C . HIS A 1 18 ? -8.034 2.617 37.281 1.00 28.22 ? 61 HIS A C 1 ATOM 132 O O . HIS A 1 18 ? -7.528 1.908 38.153 1.00 29.60 ? 61 HIS A O 1 ATOM 133 C CB . HIS A 1 18 ? -9.096 4.358 38.719 1.00 31.61 ? 61 HIS A CB 1 ATOM 134 C CG . HIS A 1 18 ? -10.514 3.939 38.512 1.00 40.26 ? 61 HIS A CG 1 ATOM 135 N ND1 . HIS A 1 18 ? -10.964 2.660 38.786 1.00 47.01 ? 61 HIS A ND1 1 ATOM 136 C CD2 . HIS A 1 18 ? -11.588 4.615 38.041 1.00 41.11 ? 61 HIS A CD2 1 ATOM 137 C CE1 . HIS A 1 18 ? -12.246 2.576 38.502 1.00 45.70 ? 61 HIS A CE1 1 ATOM 138 N NE2 . HIS A 1 18 ? -12.653 3.750 38.044 1.00 47.65 ? 61 HIS A NE2 1 ATOM 139 N N . GLU A 1 19 ? -8.475 2.134 36.125 1.00 29.46 ? 62 GLU A N 1 ATOM 140 C CA . GLU A 1 19 ? -8.370 0.717 35.794 1.00 32.33 ? 62 GLU A CA 1 ATOM 141 C C . GLU A 1 19 ? -6.976 0.339 35.312 1.00 30.75 ? 62 GLU A C 1 ATOM 142 O O . GLU A 1 19 ? -6.315 1.120 34.629 1.00 29.62 ? 62 GLU A O 1 ATOM 143 C CB . GLU A 1 19 ? -9.391 0.336 34.719 1.00 31.37 ? 62 GLU A CB 1 ATOM 144 C CG . GLU A 1 19 ? -10.661 -0.291 35.259 1.00 38.16 ? 62 GLU A CG 1 ATOM 145 C CD . GLU A 1 19 ? -10.410 -1.628 35.932 1.00 43.13 ? 62 GLU A CD 1 ATOM 146 O OE1 . GLU A 1 19 ? -11.291 -2.085 36.690 1.00 46.82 ? 62 GLU A OE1 1 ATOM 147 O OE2 . GLU A 1 19 ? -9.334 -2.224 35.702 1.00 35.82 ? 62 GLU A OE2 1 ATOM 148 N N . THR A 1 20 ? -6.537 -0.865 35.672 1.00 27.95 ? 63 THR A N 1 ATOM 149 C CA . THR A 1 20 ? -5.287 -1.408 35.153 1.00 29.52 ? 63 THR A CA 1 ATOM 150 C C . THR A 1 20 ? -5.543 -2.301 33.946 1.00 25.37 ? 63 THR A C 1 ATOM 151 O O . THR A 1 20 ? -4.612 -2.663 33.230 1.00 25.10 ? 63 THR A O 1 ATOM 152 C CB . THR A 1 20 ? -4.514 -2.213 36.217 1.00 32.82 ? 63 THR A CB 1 ATOM 153 O OG1 . THR A 1 20 ? -5.351 -3.252 36.735 1.00 30.07 ? 63 THR A OG1 1 ATOM 154 C CG2 . THR A 1 20 ? -4.074 -1.305 37.352 1.00 32.91 ? 63 THR A CG2 1 ATOM 155 N N . GLU A 1 21 ? -6.804 -2.665 33.727 1.00 21.05 ? 64 GLU A N 1 ATOM 156 C CA . GLU A 1 21 ? -7.168 -3.490 32.574 1.00 22.70 ? 64 GLU A CA 1 ATOM 157 C C . GLU A 1 21 ? -6.631 -2.817 31.307 1.00 20.16 ? 64 GLU A C 1 ATOM 158 O O . GLU A 1 21 ? -6.714 -1.599 31.173 1.00 25.02 ? 64 GLU A O 1 ATOM 159 C CB . GLU A 1 21 ? -8.687 -3.673 32.517 1.00 25.51 ? 64 GLU A CB 1 ATOM 160 C CG . GLU A 1 21 ? -9.165 -4.749 31.555 1.00 21.60 ? 64 GLU A CG 1 ATOM 161 C CD . GLU A 1 21 ? -9.089 -4.305 30.111 1.00 22.25 ? 64 GLU A CD 1 ATOM 162 O OE1 . GLU A 1 21 ? -9.514 -3.168 29.817 1.00 26.33 ? 64 GLU A OE1 1 ATOM 163 O OE2 . GLU A 1 21 ? -8.603 -5.088 29.271 1.00 25.51 ? 64 GLU A OE2 1 ATOM 164 N N . VAL A 1 22 ? -6.069 -3.602 30.389 1.00 19.63 ? 65 VAL A N 1 ATOM 165 C CA . VAL A 1 22 ? -5.242 -3.043 29.316 1.00 24.98 ? 65 VAL A CA 1 ATOM 166 C C . VAL A 1 22 ? -5.993 -2.253 28.233 1.00 24.40 ? 65 VAL A C 1 ATOM 167 O O . VAL A 1 22 ? -5.459 -1.288 27.690 1.00 22.76 ? 65 VAL A O 1 ATOM 168 C CB . VAL A 1 22 ? -4.331 -4.117 28.669 1.00 24.23 ? 65 VAL A CB 1 ATOM 169 C CG1 . VAL A 1 22 ? -3.354 -4.675 29.705 1.00 25.82 ? 65 VAL A CG1 1 ATOM 170 C CG2 . VAL A 1 22 ? -5.161 -5.233 28.067 1.00 22.48 ? 65 VAL A CG2 1 ATOM 171 N N . HIS A 1 23 ? -7.221 -2.652 27.920 1.00 21.77 ? 66 HIS A N 1 ATOM 172 C CA . HIS A 1 23 ? -8.028 -1.894 26.966 1.00 19.44 ? 66 HIS A CA 1 ATOM 173 C C . HIS A 1 23 ? -8.398 -0.538 27.554 1.00 19.51 ? 66 HIS A C 1 ATOM 174 O O . HIS A 1 23 ? -8.424 0.471 26.850 1.00 20.68 ? 66 HIS A O 1 ATOM 175 C CB . HIS A 1 23 ? -9.302 -2.652 26.597 1.00 17.75 ? 66 HIS A CB 1 ATOM 176 C CG . HIS A 1 23 ? -9.055 -3.932 25.858 1.00 21.79 ? 66 HIS A CG 1 ATOM 177 N ND1 . HIS A 1 23 ? -8.672 -5.093 26.490 1.00 21.42 ? 66 HIS A ND1 1 ATOM 178 C CD2 . HIS A 1 23 ? -9.155 -4.233 24.540 1.00 22.33 ? 66 HIS A CD2 1 ATOM 179 C CE1 . HIS A 1 23 ? -8.533 -6.056 25.593 1.00 20.26 ? 66 HIS A CE1 1 ATOM 180 N NE2 . HIS A 1 23 ? -8.824 -5.560 24.404 1.00 23.15 ? 66 HIS A NE2 1 ATOM 181 N N . ASN A 1 24 ? -8.705 -0.529 28.848 1.00 21.67 ? 67 ASN A N 1 ATOM 182 C CA . ASN A 1 24 ? -8.995 0.711 29.554 1.00 26.83 ? 67 ASN A CA 1 ATOM 183 C C . ASN A 1 24 ? -7.796 1.646 29.541 1.00 24.97 ? 67 ASN A C 1 ATOM 184 O O . ASN A 1 24 ? -7.929 2.837 29.276 1.00 23.12 ? 67 ASN A O 1 ATOM 185 C CB . ASN A 1 24 ? -9.412 0.430 30.999 1.00 23.18 ? 67 ASN A CB 1 ATOM 186 C CG . ASN A 1 24 ? -10.872 0.043 31.120 1.00 28.62 ? 67 ASN A CG 1 ATOM 187 O OD1 . ASN A 1 24 ? -11.739 0.900 31.299 1.00 26.63 ? 67 ASN A OD1 1 ATOM 188 N ND2 . ASN A 1 24 ? -11.153 -1.250 31.028 1.00 26.94 ? 67 ASN A ND2 1 ATOM 189 N N . VAL A 1 25 ? -6.627 1.096 29.847 1.00 26.53 ? 68 VAL A N 1 ATOM 190 C CA . VAL A 1 25 ? -5.400 1.877 29.872 1.00 25.02 ? 68 VAL A CA 1 ATOM 191 C C . VAL A 1 25 ? -5.081 2.461 28.503 1.00 22.17 ? 68 VAL A C 1 ATOM 192 O O . VAL A 1 25 ? -4.773 3.647 28.389 1.00 23.76 ? 68 VAL A O 1 ATOM 193 C CB . VAL A 1 25 ? -4.206 1.041 30.371 1.00 23.08 ? 68 VAL A CB 1 ATOM 194 C CG1 . VAL A 1 25 ? -2.897 1.765 30.093 1.00 31.21 ? 68 VAL A CG1 1 ATOM 195 C CG2 . VAL A 1 25 ? -4.351 0.760 31.859 1.00 24.42 ? 68 VAL A CG2 1 ATOM 196 N N . TRP A 1 26 ? -5.156 1.631 27.467 1.00 24.89 ? 69 TRP A N 1 ATOM 197 C CA . TRP A 1 26 ? -4.901 2.095 26.104 1.00 22.50 ? 69 TRP A CA 1 ATOM 198 C C . TRP A 1 26 ? -5.837 3.233 25.713 1.00 24.84 ? 69 TRP A C 1 ATOM 199 O O . TRP A 1 26 ? -5.393 4.269 25.214 1.00 23.68 ? 69 TRP A O 1 ATOM 200 C CB . TRP A 1 26 ? -5.032 0.945 25.100 1.00 22.27 ? 69 TRP A CB 1 ATOM 201 C CG . TRP A 1 26 ? -4.769 1.354 23.674 1.00 24.51 ? 69 TRP A CG 1 ATOM 202 C CD1 . TRP A 1 26 ? -3.559 1.387 23.041 1.00 25.54 ? 69 TRP A CD1 1 ATOM 203 C CD2 . TRP A 1 26 ? -5.738 1.795 22.710 1.00 19.45 ? 69 TRP A CD2 1 ATOM 204 N NE1 . TRP A 1 26 ? -3.715 1.820 21.746 1.00 29.35 ? 69 TRP A NE1 1 ATOM 205 C CE2 . TRP A 1 26 ? -5.040 2.077 21.518 1.00 26.33 ? 69 TRP A CE2 1 ATOM 206 C CE3 . TRP A 1 26 ? -7.124 1.977 22.741 1.00 22.93 ? 69 TRP A CE3 1 ATOM 207 C CZ2 . TRP A 1 26 ? -5.686 2.528 20.361 1.00 28.98 ? 69 TRP A CZ2 1 ATOM 208 C CZ3 . TRP A 1 26 ? -7.764 2.421 21.589 1.00 24.11 ? 69 TRP A CZ3 1 ATOM 209 C CH2 . TRP A 1 26 ? -7.043 2.695 20.420 1.00 25.61 ? 69 TRP A CH2 1 ATOM 210 N N . ALA A 1 27 ? -7.132 3.035 25.940 1.00 21.76 ? 70 ALA A N 1 ATOM 211 C CA . ALA A 1 27 ? -8.136 4.022 25.549 1.00 21.76 ? 70 ALA A CA 1 ATOM 212 C C . ALA A 1 27 ? -8.021 5.313 26.355 1.00 25.60 ? 70 ALA A C 1 ATOM 213 O O . ALA A 1 27 ? -8.303 6.397 25.850 1.00 26.81 ? 70 ALA A O 1 ATOM 214 C CB . ALA A 1 27 ? -9.533 3.437 25.680 1.00 20.99 ? 70 ALA A CB 1 ATOM 215 N N . THR A 1 28 ? -7.606 5.195 27.610 1.00 24.17 ? 71 THR A N 1 ATOM 216 C CA . THR A 1 28 ? -7.417 6.369 28.450 1.00 26.27 ? 71 THR A CA 1 ATOM 217 C C . THR A 1 28 ? -6.390 7.314 27.837 1.00 25.42 ? 71 THR A C 1 ATOM 218 O O . THR A 1 28 ? -6.481 8.535 27.995 1.00 26.63 ? 71 THR A O 1 ATOM 219 C CB . THR A 1 28 ? -6.977 5.980 29.876 1.00 28.93 ? 71 THR A CB 1 ATOM 220 O OG1 . THR A 1 28 ? -8.071 5.353 30.555 1.00 28.93 ? 71 THR A OG1 1 ATOM 221 C CG2 . THR A 1 28 ? -6.558 7.214 30.657 1.00 30.45 ? 71 THR A CG2 1 ATOM 222 N N . HIS A 1 29 ? -5.428 6.741 27.122 1.00 27.38 ? 72 HIS A N 1 ATOM 223 C CA . HIS A 1 29 ? -4.343 7.512 26.524 1.00 31.75 ? 72 HIS A CA 1 ATOM 224 C C . HIS A 1 29 ? -4.542 7.791 25.027 1.00 31.96 ? 72 HIS A C 1 ATOM 225 O O . HIS A 1 29 ? -3.982 8.749 24.495 1.00 33.99 ? 72 HIS A O 1 ATOM 226 C CB . HIS A 1 29 ? -3.007 6.794 26.751 1.00 42.45 ? 72 HIS A CB 1 ATOM 227 C CG . HIS A 1 29 ? -2.678 6.567 28.196 1.00 52.47 ? 72 HIS A CG 1 ATOM 228 N ND1 . HIS A 1 29 ? -3.418 5.732 29.007 1.00 52.75 ? 72 HIS A ND1 1 ATOM 229 C CD2 . HIS A 1 29 ? -1.693 7.070 28.975 1.00 60.79 ? 72 HIS A CD2 1 ATOM 230 C CE1 . HIS A 1 29 ? -2.898 5.726 30.220 1.00 54.68 ? 72 HIS A CE1 1 ATOM 231 N NE2 . HIS A 1 29 ? -1.849 6.528 30.230 1.00 61.19 ? 72 HIS A NE2 1 ATOM 232 N N . ALA A 1 30 ? -5.341 6.969 24.351 1.00 23.62 ? 73 ALA A N 1 ATOM 233 C CA . ALA A 1 30 ? -5.477 7.070 22.894 1.00 25.32 ? 73 ALA A CA 1 ATOM 234 C C . ALA A 1 30 ? -6.831 7.593 22.407 1.00 27.90 ? 73 ALA A C 1 ATOM 235 O O . ALA A 1 30 ? -6.988 7.913 21.226 1.00 25.81 ? 73 ALA A O 1 ATOM 236 C CB . ALA A 1 30 ? -5.162 5.723 22.240 1.00 21.19 ? 73 ALA A CB 1 ATOM 237 N N . CYS A 1 31 ? -7.807 7.674 23.305 1.00 29.15 ? 74 CYS A N 1 ATOM 238 C CA . CYS A 1 31 ? -9.164 8.051 22.914 1.00 29.84 ? 74 CYS A CA 1 ATOM 239 C C . CYS A 1 31 ? -9.687 9.224 23.731 1.00 28.34 ? 74 CYS A C 1 ATOM 240 O O . CYS A 1 31 ? -9.107 9.588 24.751 1.00 24.37 ? 74 CYS A O 1 ATOM 241 C CB . CYS A 1 31 ? -10.109 6.859 23.083 1.00 29.41 ? 74 CYS A CB 1 ATOM 242 S SG . CYS A 1 31 ? -9.659 5.394 22.142 1.00 26.34 ? 74 CYS A SG 1 ATOM 243 N N . VAL A 1 32 ? -10.789 9.815 23.275 1.00 22.49 ? 75 VAL A N 1 ATOM 244 C CA . VAL A 1 32 ? -11.444 10.884 24.019 1.00 24.63 ? 75 VAL A CA 1 ATOM 245 C C . VAL A 1 32 ? -12.767 10.378 24.601 1.00 26.35 ? 75 VAL A C 1 ATOM 246 O O . VAL A 1 32 ? -13.207 9.276 24.276 1.00 27.80 ? 75 VAL A O 1 ATOM 247 C CB . VAL A 1 32 ? -11.691 12.135 23.131 1.00 35.24 ? 75 VAL A CB 1 ATOM 248 C CG1 . VAL A 1 32 ? -10.376 12.680 22.593 1.00 35.44 ? 75 VAL A CG1 1 ATOM 249 C CG2 . VAL A 1 32 ? -12.646 11.816 21.995 1.00 32.64 ? 75 VAL A CG2 1 ATOM 250 N N . PRO A 1 33 ? -13.397 11.172 25.478 1.00 28.84 ? 76 PRO A N 1 ATOM 251 C CA . PRO A 1 33 ? -14.688 10.776 26.054 1.00 30.67 ? 76 PRO A CA 1 ATOM 252 C C . PRO A 1 33 ? -15.803 10.698 25.012 1.00 31.29 ? 76 PRO A C 1 ATOM 253 O O . PRO A 1 33 ? -15.755 11.382 23.988 1.00 28.74 ? 76 PRO A O 1 ATOM 254 C CB . PRO A 1 33 ? -14.975 11.896 27.063 1.00 36.38 ? 76 PRO A CB 1 ATOM 255 C CG . PRO A 1 33 ? -13.623 12.422 27.426 1.00 33.18 ? 76 PRO A CG 1 ATOM 256 C CD . PRO A 1 33 ? -12.846 12.367 26.141 1.00 32.21 ? 76 PRO A CD 1 ATOM 257 N N . THR A 1 34 ? -16.800 9.859 25.275 1.00 29.20 ? 77 THR A N 1 ATOM 258 C CA . THR A 1 34 ? -17.939 9.728 24.377 1.00 32.32 ? 77 THR A CA 1 ATOM 259 C C . THR A 1 34 ? -18.896 10.898 24.543 1.00 35.09 ? 77 THR A C 1 ATOM 260 O O . THR A 1 34 ? -18.830 11.639 25.525 1.00 36.54 ? 77 THR A O 1 ATOM 261 C CB . THR A 1 34 ? -18.726 8.435 24.652 1.00 32.18 ? 77 THR A CB 1 ATOM 262 O OG1 . THR A 1 34 ? -19.225 8.471 25.994 1.00 30.51 ? 77 THR A OG1 1 ATOM 263 C CG2 . THR A 1 34 ? -17.839 7.206 24.467 1.00 28.90 ? 77 THR A CG2 1 ATOM 264 N N . ASP A 1 35 ? -19.789 11.053 23.573 1.00 31.47 ? 78 ASP A N 1 ATOM 265 C CA . ASP A 1 35 ? -20.831 12.066 23.624 1.00 34.21 ? 78 ASP A CA 1 ATOM 266 C C . ASP A 1 35 ? -22.072 11.451 24.254 1.00 37.60 ? 78 ASP A C 1 ATOM 267 O O . ASP A 1 35 ? -22.617 10.480 23.730 1.00 33.16 ? 78 ASP A O 1 ATOM 268 C CB . ASP A 1 35 ? -21.148 12.557 22.210 1.00 34.13 ? 78 ASP A CB 1 ATOM 269 C CG . ASP A 1 35 ? -22.122 13.726 22.193 1.00 42.30 ? 78 ASP A CG 1 ATOM 270 O OD1 . ASP A 1 35 ? -22.862 13.915 23.181 1.00 40.00 ? 78 ASP A OD1 1 ATOM 271 O OD2 . ASP A 1 35 ? -22.152 14.453 21.179 1.00 47.76 ? 78 ASP A OD2 1 ATOM 272 N N . PRO A 1 36 ? -22.521 12.009 25.388 1.00 44.00 ? 79 PRO A N 1 ATOM 273 C CA . PRO A 1 36 ? -23.696 11.473 26.082 1.00 50.82 ? 79 PRO A CA 1 ATOM 274 C C . PRO A 1 36 ? -24.994 11.742 25.321 1.00 55.45 ? 79 PRO A C 1 ATOM 275 O O . PRO A 1 36 ? -26.010 11.112 25.610 1.00 56.61 ? 79 PRO A O 1 ATOM 276 C CB . PRO A 1 36 ? -23.691 12.236 27.410 1.00 48.89 ? 79 PRO A CB 1 ATOM 277 C CG . PRO A 1 36 ? -23.008 13.521 27.097 1.00 48.76 ? 79 PRO A CG 1 ATOM 278 C CD . PRO A 1 36 ? -21.955 13.182 26.077 1.00 44.58 ? 79 PRO A CD 1 ATOM 279 N N . ASN A 1 37 ? -24.955 12.664 24.362 1.00 54.60 ? 80 ASN A N 1 ATOM 280 C CA . ASN A 1 37 ? -26.136 12.998 23.570 1.00 54.24 ? 80 ASN A CA 1 ATOM 281 C C . ASN A 1 37 ? -25.857 12.995 22.066 1.00 44.97 ? 80 ASN A C 1 ATOM 282 O O . ASN A 1 37 ? -25.991 14.025 21.407 1.00 45.88 ? 80 ASN A O 1 ATOM 283 C CB . ASN A 1 37 ? -26.692 14.362 23.988 1.00 61.69 ? 80 ASN A CB 1 ATOM 284 C CG . ASN A 1 37 ? -26.945 14.460 25.482 1.00 71.64 ? 80 ASN A CG 1 ATOM 285 O OD1 . ASN A 1 37 ? -27.155 13.452 26.157 1.00 75.28 ? 80 ASN A OD1 1 ATOM 286 N ND2 . ASN A 1 37 ? -26.930 15.681 26.005 1.00 75.25 ? 80 ASN A ND2 1 ATOM 287 N N . PRO A 1 38 ? -25.478 11.830 21.519 1.00 44.55 ? 81 PRO A N 1 ATOM 288 C CA . PRO A 1 38 ? -25.112 11.715 20.103 1.00 45.00 ? 81 PRO A CA 1 ATOM 289 C C . PRO A 1 38 ? -26.269 12.040 19.166 1.00 43.77 ? 81 PRO A C 1 ATOM 290 O O . PRO A 1 38 ? -27.411 11.659 19.424 1.00 46.64 ? 81 PRO A O 1 ATOM 291 C CB . PRO A 1 38 ? -24.717 10.242 19.962 1.00 44.04 ? 81 PRO A CB 1 ATOM 292 C CG . PRO A 1 38 ? -25.423 9.550 21.078 1.00 42.61 ? 81 PRO A CG 1 ATOM 293 C CD . PRO A 1 38 ? -25.418 10.530 22.209 1.00 41.16 ? 81 PRO A CD 1 ATOM 294 N N . GLN A 1 39 ? -25.961 12.743 18.083 1.00 43.13 ? 82 GLN A N 1 ATOM 295 C CA . GLN A 1 39 ? -26.957 13.109 17.089 1.00 44.06 ? 82 GLN A CA 1 ATOM 296 C C . GLN A 1 39 ? -26.920 12.126 15.927 1.00 41.27 ? 82 GLN A C 1 ATOM 297 O O . GLN A 1 39 ? -25.850 11.771 15.443 1.00 37.58 ? 82 GLN A O 1 ATOM 298 C CB . GLN A 1 39 ? -26.700 14.528 16.578 1.00 53.26 ? 82 GLN A CB 1 ATOM 299 C CG . GLN A 1 39 ? -26.914 15.627 17.621 1.00 61.98 ? 82 GLN A CG 1 ATOM 300 C CD . GLN A 1 39 ? -26.581 17.020 17.104 1.00 67.18 ? 82 GLN A CD 1 ATOM 301 O OE1 . GLN A 1 39 ? -25.786 17.184 16.178 1.00 60.77 ? 82 GLN A OE1 1 ATOM 302 N NE2 . GLN A 1 39 ? -27.198 18.032 17.704 1.00 72.72 ? 82 GLN A NE2 1 ATOM 303 N N . GLU A 1 40 ? -28.091 11.677 15.491 1.00 37.74 ? 83 GLU A N 1 ATOM 304 C CA . GLU A 1 40 ? -28.187 10.827 14.310 1.00 36.08 ? 83 GLU A CA 1 ATOM 305 C C . GLU A 1 40 ? -29.288 11.366 13.415 1.00 38.79 ? 83 GLU A C 1 ATOM 306 O O . GLU A 1 40 ? -30.440 11.489 13.839 1.00 35.24 ? 83 GLU A O 1 ATOM 307 C CB . GLU A 1 40 ? -28.468 9.373 14.696 1.00 41.66 ? 83 GLU A CB 1 ATOM 308 C CG . GLU A 1 40 ? -28.624 8.444 13.498 1.00 41.05 ? 83 GLU A CG 1 ATOM 309 C CD . GLU A 1 40 ? -28.590 6.976 13.875 1.00 46.25 ? 83 GLU A CD 1 ATOM 310 O OE1 . GLU A 1 40 ? -28.314 6.659 15.053 1.00 39.79 ? 83 GLU A OE1 1 ATOM 311 O OE2 . GLU A 1 40 ? -28.833 6.133 12.984 1.00 47.48 ? 83 GLU A OE2 1 ATOM 312 N N . ILE A 1 41 ? -28.923 11.702 12.182 1.00 29.35 ? 84 ILE A N 1 ATOM 313 C CA . ILE A 1 41 ? -29.854 12.318 11.249 1.00 34.72 ? 84 ILE A CA 1 ATOM 314 C C . ILE A 1 41 ? -30.221 11.358 10.127 1.00 40.57 ? 84 ILE A C 1 ATOM 315 O O . ILE A 1 41 ? -29.350 10.890 9.395 1.00 37.83 ? 84 ILE A O 1 ATOM 316 C CB . ILE A 1 41 ? -29.243 13.587 10.628 1.00 37.12 ? 84 ILE A CB 1 ATOM 317 C CG1 . ILE A 1 41 ? -28.807 14.560 11.726 1.00 40.52 ? 84 ILE A CG1 1 ATOM 318 C CG2 . ILE A 1 41 ? -30.229 14.247 9.666 1.00 38.82 ? 84 ILE A CG2 1 ATOM 319 C CD1 . ILE A 1 41 ? -28.022 15.744 11.209 1.00 46.93 ? 84 ILE A CD1 1 ATOM 320 N N . HIS A 1 42 ? -31.509 11.058 9.994 1.00 40.39 ? 85 HIS A N 1 ATOM 321 C CA . HIS A 1 42 ? -31.961 10.246 8.875 1.00 44.51 ? 85 HIS A CA 1 ATOM 322 C C . HIS A 1 42 ? -32.009 11.093 7.613 1.00 40.55 ? 85 HIS A C 1 ATOM 323 O O . HIS A 1 42 ? -32.587 12.175 7.610 1.00 38.95 ? 85 HIS A O 1 ATOM 324 C CB . HIS A 1 42 ? -33.340 9.643 9.131 1.00 51.66 ? 85 HIS A CB 1 ATOM 325 C CG . HIS A 1 42 ? -33.961 9.045 7.906 1.00 55.89 ? 85 HIS A CG 1 ATOM 326 N ND1 . HIS A 1 42 ? -35.017 9.635 7.241 1.00 61.98 ? 85 HIS A ND1 1 ATOM 327 C CD2 . HIS A 1 42 ? -33.657 7.926 7.207 1.00 55.83 ? 85 HIS A CD2 1 ATOM 328 C CE1 . HIS A 1 42 ? -35.343 8.897 6.197 1.00 60.66 ? 85 HIS A CE1 1 ATOM 329 N NE2 . HIS A 1 42 ? -34.534 7.854 6.152 1.00 57.64 ? 85 HIS A NE2 1 ATOM 330 N N . LEU A 1 43 ? -31.404 10.594 6.542 1.00 34.85 ? 86 LEU A N 1 ATOM 331 C CA . LEU A 1 43 ? -31.370 11.320 5.284 1.00 34.56 ? 86 LEU A CA 1 ATOM 332 C C . LEU A 1 43 ? -32.565 10.925 4.427 1.00 37.27 ? 86 LEU A C 1 ATOM 333 O O . LEU A 1 43 ? -32.605 9.828 3.881 1.00 40.95 ? 86 LEU A O 1 ATOM 334 C CB . LEU A 1 43 ? -30.061 11.032 4.546 1.00 36.13 ? 86 LEU A CB 1 ATOM 335 C CG . LEU A 1 43 ? -28.798 11.097 5.412 1.00 40.46 ? 86 LEU A CG 1 ATOM 336 C CD1 . LEU A 1 43 ? -27.556 10.800 4.589 1.00 41.82 ? 86 LEU A CD1 1 ATOM 337 C CD2 . LEU A 1 43 ? -28.678 12.452 6.093 1.00 43.72 ? 86 LEU A CD2 1 ATOM 338 N N . GLU A 1 44 ? -33.544 11.817 4.315 1.00 38.63 ? 87 GLU A N 1 ATOM 339 C CA . GLU A 1 44 ? -34.753 11.516 3.552 1.00 41.78 ? 87 GLU A CA 1 ATOM 340 C C . GLU A 1 44 ? -34.467 11.327 2.060 1.00 40.47 ? 87 GLU A C 1 ATOM 341 O O . GLU A 1 44 ? -33.735 12.109 1.450 1.00 45.48 ? 87 GLU A O 1 ATOM 342 C CB . GLU A 1 44 ? -35.815 12.596 3.774 1.00 54.44 ? 87 GLU A CB 1 ATOM 343 C CG . GLU A 1 44 ? -36.359 12.636 5.202 1.00 63.28 ? 87 GLU A CG 1 ATOM 344 C CD . GLU A 1 44 ? -37.551 13.570 5.357 1.00 74.16 ? 87 GLU A CD 1 ATOM 345 O OE1 . GLU A 1 44 ? -37.864 14.309 4.399 1.00 75.50 ? 87 GLU A OE1 1 ATOM 346 O OE2 . GLU A 1 44 ? -38.177 13.563 6.439 1.00 79.06 ? 87 GLU A OE2 1 ATOM 347 N N . ASN A 1 45 ? -35.050 10.277 1.487 1.00 38.96 ? 88 ASN A N 1 ATOM 348 C CA . ASN A 1 45 ? -34.864 9.923 0.071 1.00 44.99 ? 88 ASN A CA 1 ATOM 349 C C . ASN A 1 45 ? -33.431 9.896 -0.417 1.00 46.21 ? 88 ASN A C 1 ATOM 350 O O . ASN A 1 45 ? -33.149 10.312 -1.545 1.00 50.54 ? 88 ASN A O 1 ATOM 351 C CB . ASN A 1 45 ? -35.616 10.866 -0.870 1.00 57.39 ? 88 ASN A CB 1 ATOM 352 C CG . ASN A 1 45 ? -37.102 10.680 -0.819 1.00 69.47 ? 88 ASN A CG 1 ATOM 353 O OD1 . ASN A 1 45 ? -37.597 9.611 -0.432 1.00 75.29 ? 88 ASN A OD1 1 ATOM 354 N ND2 . ASN A 1 45 ? -37.835 11.721 -1.192 1.00 75.35 ? 88 ASN A ND2 1 ATOM 355 N N . VAL A 1 46 ? -32.518 9.429 0.415 1.00 41.24 ? 89 VAL A N 1 ATOM 356 C CA . VAL A 1 46 ? -31.143 9.330 -0.028 1.00 37.74 ? 89 VAL A CA 1 ATOM 357 C C . VAL A 1 46 ? -30.772 7.867 -0.144 1.00 40.14 ? 89 VAL A C 1 ATOM 358 O O . VAL A 1 46 ? -30.995 7.093 0.786 1.00 38.66 ? 89 VAL A O 1 ATOM 359 C CB . VAL A 1 46 ? -30.179 10.068 0.924 1.00 35.62 ? 89 VAL A CB 1 ATOM 360 C CG1 . VAL A 1 46 ? -28.738 9.610 0.707 1.00 35.73 ? 89 VAL A CG1 1 ATOM 361 C CG2 . VAL A 1 46 ? -30.301 11.574 0.735 1.00 36.22 ? 89 VAL A CG2 1 ATOM 362 N N . THR A 1 47 ? -30.235 7.489 -1.299 1.00 31.61 ? 90 THR A N 1 ATOM 363 C CA . THR A 1 47 ? -29.689 6.154 -1.493 1.00 29.18 ? 90 THR A CA 1 ATOM 364 C C . THR A 1 47 ? -28.174 6.274 -1.620 1.00 32.25 ? 90 THR A C 1 ATOM 365 O O . THR A 1 47 ? -27.676 7.071 -2.412 1.00 36.89 ? 90 THR A O 1 ATOM 366 C CB . THR A 1 47 ? -30.263 5.491 -2.762 1.00 36.01 ? 90 THR A CB 1 ATOM 367 O OG1 . THR A 1 47 ? -31.686 5.368 -2.639 1.00 40.15 ? 90 THR A OG1 1 ATOM 368 C CG2 . THR A 1 47 ? -29.658 4.111 -2.969 1.00 33.29 ? 90 THR A CG2 1 ATOM 369 N N . GLU A 1 48 ? -27.446 5.498 -0.823 1.00 26.94 ? 91 GLU A N 1 ATOM 370 C CA . GLU A 1 48 ? -25.985 5.521 -0.852 1.00 30.15 ? 91 GLU A CA 1 ATOM 371 C C . GLU A 1 48 ? -25.427 4.119 -1.074 1.00 29.06 ? 91 GLU A C 1 ATOM 372 O O . GLU A 1 48 ? -25.980 3.136 -0.573 1.00 24.43 ? 91 GLU A O 1 ATOM 373 C CB . GLU A 1 48 ? -25.426 6.096 0.457 1.00 27.98 ? 91 GLU A CB 1 ATOM 374 C CG . GLU A 1 48 ? -25.658 7.584 0.649 1.00 35.20 ? 91 GLU A CG 1 ATOM 375 C CD . GLU A 1 48 ? -24.672 8.434 -0.132 1.00 35.68 ? 91 GLU A CD 1 ATOM 376 O OE1 . GLU A 1 48 ? -23.528 7.983 -0.342 1.00 33.05 ? 91 GLU A OE1 1 ATOM 377 O OE2 . GLU A 1 48 ? -25.046 9.552 -0.540 1.00 42.84 ? 91 GLU A OE2 1 ATOM 378 N N . ASN A 1 49 ? -24.337 4.029 -1.831 1.00 26.80 ? 92 ASN A N 1 ATOM 379 C CA . ASN A 1 49 ? -23.651 2.755 -2.029 1.00 22.17 ? 92 ASN A CA 1 ATOM 380 C C . ASN A 1 49 ? -22.589 2.527 -0.961 1.00 25.83 ? 92 ASN A C 1 ATOM 381 O O . ASN A 1 49 ? -21.853 3.446 -0.602 1.00 25.37 ? 92 ASN A O 1 ATOM 382 C CB . ASN A 1 49 ? -23.009 2.701 -3.418 1.00 26.69 ? 92 ASN A CB 1 ATOM 383 C CG . ASN A 1 49 ? -24.012 2.892 -4.530 1.00 35.63 ? 92 ASN A CG 1 ATOM 384 O OD1 . ASN A 1 49 ? -25.184 2.546 -4.388 1.00 35.34 ? 92 ASN A OD1 1 ATOM 385 N ND2 . ASN A 1 49 ? -23.558 3.447 -5.651 1.00 46.10 ? 92 ASN A ND2 1 ATOM 386 N N . PHE A 1 50 ? -22.524 1.300 -0.450 1.00 24.32 ? 93 PHE A N 1 ATOM 387 C CA . PHE A 1 50 ? -21.489 0.898 0.495 1.00 21.21 ? 93 PHE A CA 1 ATOM 388 C C . PHE A 1 50 ? -20.714 -0.286 -0.075 1.00 23.45 ? 93 PHE A C 1 ATOM 389 O O . PHE A 1 50 ? -21.233 -1.041 -0.903 1.00 25.88 ? 93 PHE A O 1 ATOM 390 C CB . PHE A 1 50 ? -22.110 0.502 1.842 1.00 23.08 ? 93 PHE A CB 1 ATOM 391 C CG . PHE A 1 50 ? -22.788 1.634 2.557 1.00 25.36 ? 93 PHE A CG 1 ATOM 392 C CD1 . PHE A 1 50 ? -23.987 2.151 2.089 1.00 26.17 ? 93 PHE A CD1 1 ATOM 393 C CD2 . PHE A 1 50 ? -22.226 2.185 3.700 1.00 23.29 ? 93 PHE A CD2 1 ATOM 394 C CE1 . PHE A 1 50 ? -24.610 3.195 2.743 1.00 26.31 ? 93 PHE A CE1 1 ATOM 395 C CE2 . PHE A 1 50 ? -22.850 3.226 4.362 1.00 23.43 ? 93 PHE A CE2 1 ATOM 396 C CZ . PHE A 1 50 ? -24.041 3.735 3.882 1.00 25.79 ? 93 PHE A CZ 1 ATOM 397 N N . ASN A 1 51 ? -19.466 -0.439 0.352 1.00 20.42 ? 94 ASN A N 1 ATOM 398 C CA . ASN A 1 51 ? -18.696 -1.636 0.029 1.00 21.38 ? 94 ASN A CA 1 ATOM 399 C C . ASN A 1 51 ? -17.821 -2.016 1.211 1.00 21.08 ? 94 ASN A C 1 ATOM 400 O O . ASN A 1 51 ? -16.736 -1.463 1.400 1.00 21.70 ? 94 ASN A O 1 ATOM 401 C CB . ASN A 1 51 ? -17.858 -1.446 -1.244 1.00 20.08 ? 94 ASN A CB 1 ATOM 402 C CG . ASN A 1 51 ? -17.106 -2.709 -1.642 1.00 22.30 ? 94 ASN A CG 1 ATOM 403 O OD1 . ASN A 1 51 ? -17.179 -3.724 -0.958 1.00 22.72 ? 94 ASN A OD1 1 ATOM 404 N ND2 . ASN A 1 51 ? -16.384 -2.649 -2.757 1.00 23.76 ? 94 ASN A ND2 1 ATOM 405 N N . MET A 1 52 ? -18.305 -2.957 2.015 1.00 18.49 ? 95 MET A N 1 ATOM 406 C CA . MET A 1 52 ? -17.632 -3.323 3.255 1.00 21.75 ? 95 MET A CA 1 ATOM 407 C C . MET A 1 52 ? -16.228 -3.879 3.015 1.00 23.32 ? 95 MET A C 1 ATOM 408 O O . MET A 1 52 ? -15.394 -3.885 3.923 1.00 20.43 ? 95 MET A O 1 ATOM 409 C CB . MET A 1 52 ? -18.464 -4.355 4.023 1.00 21.70 ? 95 MET A CB 1 ATOM 410 C CG . MET A 1 52 ? -18.611 -5.688 3.299 1.00 18.27 ? 95 MET A CG 1 ATOM 411 S SD . MET A 1 52 ? -19.524 -6.917 4.252 1.00 19.25 ? 95 MET A SD 1 ATOM 412 C CE . MET A 1 52 ? -18.316 -7.344 5.505 1.00 18.06 ? 95 MET A CE 1 ATOM 413 N N . TRP A 1 53 ? -15.977 -4.348 1.797 1.00 22.46 ? 96 TRP A N 1 ATOM 414 C CA . TRP A 1 53 ? -14.715 -5.016 1.468 1.00 19.45 ? 96 TRP A CA 1 ATOM 415 C C . TRP A 1 53 ? -13.638 -4.029 1.026 1.00 25.65 ? 96 TRP A C 1 ATOM 416 O O . TRP A 1 53 ? -12.477 -4.400 0.834 1.00 25.54 ? 96 TRP A O 1 ATOM 417 C CB . TRP A 1 53 ? -14.955 -6.102 0.412 1.00 19.94 ? 96 TRP A CB 1 ATOM 418 C CG . TRP A 1 53 ? -16.001 -7.052 0.882 1.00 23.77 ? 96 TRP A CG 1 ATOM 419 C CD1 . TRP A 1 53 ? -17.311 -7.082 0.507 1.00 25.09 ? 96 TRP A CD1 1 ATOM 420 C CD2 . TRP A 1 53 ? -15.841 -8.078 1.870 1.00 23.82 ? 96 TRP A CD2 1 ATOM 421 N NE1 . TRP A 1 53 ? -17.971 -8.077 1.185 1.00 20.45 ? 96 TRP A NE1 1 ATOM 422 C CE2 . TRP A 1 53 ? -17.090 -8.705 2.029 1.00 20.39 ? 96 TRP A CE2 1 ATOM 423 C CE3 . TRP A 1 53 ? -14.757 -8.535 2.629 1.00 24.12 ? 96 TRP A CE3 1 ATOM 424 C CZ2 . TRP A 1 53 ? -17.292 -9.763 2.916 1.00 19.20 ? 96 TRP A CZ2 1 ATOM 425 C CZ3 . TRP A 1 53 ? -14.955 -9.584 3.508 1.00 23.00 ? 96 TRP A CZ3 1 ATOM 426 C CH2 . TRP A 1 53 ? -16.213 -10.190 3.641 1.00 24.83 ? 96 TRP A CH2 1 ATOM 427 N N . LYS A 1 54 ? -14.037 -2.769 0.875 1.00 23.20 ? 97 LYS A N 1 ATOM 428 C CA . LYS A 1 54 ? -13.110 -1.690 0.563 1.00 23.30 ? 97 LYS A CA 1 ATOM 429 C C . LYS A 1 54 ? -13.480 -0.509 1.436 1.00 24.36 ? 97 LYS A C 1 ATOM 430 O O . LYS A 1 54 ? -14.079 0.470 0.984 1.00 22.47 ? 97 LYS A O 1 ATOM 431 C CB . LYS A 1 54 ? -13.164 -1.312 -0.922 1.00 31.03 ? 97 LYS A CB 1 ATOM 432 C CG . LYS A 1 54 ? -12.588 -2.371 -1.849 1.00 42.36 ? 97 LYS A CG 1 ATOM 433 C CD . LYS A 1 54 ? -12.583 -1.899 -3.300 1.00 52.80 ? 97 LYS A CD 1 ATOM 434 C CE . LYS A 1 54 ? -11.862 -2.889 -4.206 1.00 56.94 ? 97 LYS A CE 1 ATOM 435 N NZ . LYS A 1 54 ? -12.488 -4.237 -4.172 1.00 59.27 ? 97 LYS A NZ 1 ATOM 436 N N . ASN A 1 55 ? -13.123 -0.625 2.707 1.00 24.16 ? 98 ASN A N 1 ATOM 437 C CA . ASN A 1 55 ? -13.506 0.347 3.707 1.00 22.05 ? 98 ASN A CA 1 ATOM 438 C C . ASN A 1 55 ? -12.312 0.622 4.600 1.00 21.44 ? 98 ASN A C 1 ATOM 439 O O . ASN A 1 55 ? -11.942 -0.215 5.432 1.00 18.44 ? 98 ASN A O 1 ATOM 440 C CB . ASN A 1 55 ? -14.669 -0.197 4.539 1.00 21.87 ? 98 ASN A CB 1 ATOM 441 C CG . ASN A 1 55 ? -15.175 0.805 5.550 1.00 20.74 ? 98 ASN A CG 1 ATOM 442 O OD1 . ASN A 1 55 ? -14.706 1.941 5.596 1.00 22.65 ? 98 ASN A OD1 1 ATOM 443 N ND2 . ASN A 1 55 ? -16.139 0.394 6.367 1.00 23.51 ? 98 ASN A ND2 1 ATOM 444 N N . ASN A 1 56 ? -11.715 1.797 4.428 1.00 23.26 ? 99 ASN A N 1 ATOM 445 C CA . ASN A 1 56 ? -10.500 2.155 5.145 1.00 23.82 ? 99 ASN A CA 1 ATOM 446 C C . ASN A 1 56 ? -10.675 2.259 6.658 1.00 21.48 ? 99 ASN A C 1 ATOM 447 O O . ASN A 1 56 ? -9.686 2.286 7.385 1.00 17.88 ? 99 ASN A O 1 ATOM 448 C CB . ASN A 1 56 ? -9.895 3.448 4.583 1.00 29.58 ? 99 ASN A CB 1 ATOM 449 C CG . ASN A 1 56 ? -8.587 3.829 5.262 1.00 31.60 ? 99 ASN A CG 1 ATOM 450 O OD1 . ASN A 1 56 ? -8.525 4.805 6.011 1.00 32.36 ? 99 ASN A OD1 1 ATOM 451 N ND2 . ASN A 1 56 ? -7.536 3.049 5.010 1.00 25.21 ? 99 ASN A ND2 1 ATOM 452 N N . MET A 1 57 ? -11.921 2.310 7.134 1.00 20.87 ? 100 MET A N 1 ATOM 453 C CA . MET A 1 57 ? -12.187 2.266 8.575 1.00 23.13 ? 100 MET A CA 1 ATOM 454 C C . MET A 1 57 ? -11.679 0.961 9.187 1.00 20.43 ? 100 MET A C 1 ATOM 455 O O . MET A 1 57 ? -11.241 0.926 10.338 1.00 19.11 ? 100 MET A O 1 ATOM 456 C CB . MET A 1 57 ? -13.686 2.405 8.871 1.00 19.82 ? 100 MET A CB 1 ATOM 457 C CG . MET A 1 57 ? -14.337 3.671 8.336 1.00 19.85 ? 100 MET A CG 1 ATOM 458 S SD . MET A 1 57 ? -16.128 3.658 8.597 1.00 20.42 ? 100 MET A SD 1 ATOM 459 C CE . MET A 1 57 ? -16.230 4.072 10.335 1.00 21.20 ? 100 MET A CE 1 ATOM 460 N N . VAL A 1 58 ? -11.764 -0.113 8.413 1.00 19.65 ? 101 VAL A N 1 ATOM 461 C CA . VAL A 1 58 ? -11.287 -1.423 8.841 1.00 17.31 ? 101 VAL A CA 1 ATOM 462 C C . VAL A 1 58 ? -9.773 -1.424 9.072 1.00 18.68 ? 101 VAL A C 1 ATOM 463 O O . VAL A 1 58 ? -9.290 -1.935 10.083 1.00 19.50 ? 101 VAL A O 1 ATOM 464 C CB . VAL A 1 58 ? -11.640 -2.501 7.800 1.00 19.82 ? 101 VAL A CB 1 ATOM 465 C CG1 . VAL A 1 58 ? -10.975 -3.841 8.152 1.00 19.33 ? 101 VAL A CG1 1 ATOM 466 C CG2 . VAL A 1 58 ? -13.160 -2.657 7.689 1.00 18.27 ? 101 VAL A CG2 1 ATOM 467 N N . GLU A 1 59 ? -9.027 -0.864 8.124 1.00 17.74 ? 102 GLU A N 1 ATOM 468 C CA . GLU A 1 59 ? -7.575 -0.776 8.262 1.00 20.77 ? 102 GLU A CA 1 ATOM 469 C C . GLU A 1 59 ? -7.192 0.053 9.481 1.00 25.87 ? 102 GLU A C 1 ATOM 470 O O . GLU A 1 59 ? -6.231 -0.268 10.186 1.00 25.43 ? 102 GLU A O 1 ATOM 471 C CB . GLU A 1 59 ? -6.941 -0.167 7.011 1.00 26.28 ? 102 GLU A CB 1 ATOM 472 C CG . GLU A 1 59 ? -6.572 -1.175 5.936 1.00 31.68 ? 102 GLU A CG 1 ATOM 473 C CD . GLU A 1 59 ? -7.784 -1.829 5.303 1.00 36.32 ? 102 GLU A CD 1 ATOM 474 O OE1 . GLU A 1 59 ? -7.694 -3.023 4.946 1.00 35.75 ? 102 GLU A OE1 1 ATOM 475 O OE2 . GLU A 1 59 ? -8.821 -1.148 5.156 1.00 32.85 ? 102 GLU A OE2 1 ATOM 476 N N . GLN A 1 60 ? -7.944 1.121 9.728 1.00 20.48 ? 103 GLN A N 1 ATOM 477 C CA . GLN A 1 60 ? -7.657 2.000 10.861 1.00 20.14 ? 103 GLN A CA 1 ATOM 478 C C . GLN A 1 60 ? -7.937 1.313 12.194 1.00 21.03 ? 103 GLN A C 1 ATOM 479 O O . GLN A 1 60 ? -7.167 1.458 13.145 1.00 19.58 ? 103 GLN A O 1 ATOM 480 C CB . GLN A 1 60 ? -8.435 3.316 10.754 1.00 22.49 ? 103 GLN A CB 1 ATOM 481 C CG . GLN A 1 60 ? -7.958 4.210 9.619 1.00 23.07 ? 103 GLN A CG 1 ATOM 482 C CD . GLN A 1 60 ? -8.482 5.626 9.726 1.00 25.14 ? 103 GLN A CD 1 ATOM 483 O OE1 . GLN A 1 60 ? -8.480 6.222 10.803 1.00 21.76 ? 103 GLN A OE1 1 ATOM 484 N NE2 . GLN A 1 60 ? -8.925 6.180 8.603 1.00 26.20 ? 103 GLN A NE2 1 ATOM 485 N N . MET A 1 61 ? -9.033 0.561 12.271 1.00 21.44 ? 104 MET A N 1 ATOM 486 C CA . MET A 1 61 ? -9.310 -0.185 13.491 1.00 22.12 ? 104 MET A CA 1 ATOM 487 C C . MET A 1 61 ? -8.224 -1.229 13.713 1.00 21.08 ? 104 MET A C 1 ATOM 488 O O . MET A 1 61 ? -7.767 -1.431 14.838 1.00 19.71 ? 104 MET A O 1 ATOM 489 C CB . MET A 1 61 ? -10.680 -0.860 13.454 1.00 20.10 ? 104 MET A CB 1 ATOM 490 C CG . MET A 1 61 ? -10.960 -1.671 14.710 1.00 21.32 ? 104 MET A CG 1 ATOM 491 S SD . MET A 1 61 ? -12.664 -2.233 14.892 1.00 21.97 ? 104 MET A SD 1 ATOM 492 C CE . MET A 1 61 ? -12.601 -2.891 16.554 1.00 32.44 ? 104 MET A CE 1 ATOM 493 N N . GLN A 1 62 ? -7.809 -1.887 12.633 1.00 13.77 ? 105 GLN A N 1 ATOM 494 C CA . GLN A 1 62 ? -6.727 -2.869 12.713 1.00 19.30 ? 105 GLN A CA 1 ATOM 495 C C . GLN A 1 62 ? -5.458 -2.232 13.271 1.00 19.56 ? 105 GLN A C 1 ATOM 496 O O . GLN A 1 62 ? -4.811 -2.792 14.152 1.00 17.76 ? 105 GLN A O 1 ATOM 497 C CB . GLN A 1 62 ? -6.437 -3.483 11.341 1.00 24.18 ? 105 GLN A CB 1 ATOM 498 C CG . GLN A 1 62 ? -5.251 -4.450 11.314 1.00 23.59 ? 105 GLN A CG 1 ATOM 499 C CD . GLN A 1 62 ? -5.640 -5.874 11.661 1.00 24.76 ? 105 GLN A CD 1 ATOM 500 O OE1 . GLN A 1 62 ? -6.671 -6.113 12.291 1.00 23.73 ? 105 GLN A OE1 1 ATOM 501 N NE2 . GLN A 1 62 ? -4.813 -6.836 11.246 1.00 27.97 ? 105 GLN A NE2 1 ATOM 502 N N . GLU A 1 63 ? -5.099 -1.066 12.745 1.00 19.53 ? 106 GLU A N 1 ATOM 503 C CA . GLU A 1 63 ? -3.927 -0.344 13.237 1.00 24.70 ? 106 GLU A CA 1 ATOM 504 C C . GLU A 1 63 ? -4.021 -0.090 14.750 1.00 23.76 ? 106 GLU A C 1 ATOM 505 O O . GLU A 1 63 ? -3.040 -0.274 15.479 1.00 21.21 ? 106 GLU A O 1 ATOM 506 C CB . GLU A 1 63 ? -3.716 0.950 12.436 1.00 27.31 ? 106 GLU A CB 1 ATOM 507 C CG . GLU A 1 63 ? -3.300 0.681 10.984 1.00 36.66 ? 106 GLU A CG 1 ATOM 508 C CD . GLU A 1 63 ? -3.528 1.856 10.040 1.00 49.21 ? 106 GLU A CD 1 ATOM 509 O OE1 . GLU A 1 63 ? -4.226 2.822 10.420 1.00 42.25 ? 106 GLU A OE1 1 ATOM 510 O OE2 . GLU A 1 63 ? -3.011 1.805 8.902 1.00 54.97 ? 106 GLU A OE2 1 ATOM 511 N N . ASP A 1 64 ? -5.204 0.300 15.224 1.00 18.63 ? 107 ASP A N 1 ATOM 512 C CA . ASP A 1 64 ? -5.414 0.544 16.661 1.00 21.57 ? 107 ASP A CA 1 ATOM 513 C C . ASP A 1 64 ? -5.216 -0.704 17.520 1.00 19.47 ? 107 ASP A C 1 ATOM 514 O O . ASP A 1 64 ? -4.545 -0.670 18.562 1.00 17.86 ? 107 ASP A O 1 ATOM 515 C CB . ASP A 1 64 ? -6.825 1.084 16.924 1.00 20.75 ? 107 ASP A CB 1 ATOM 516 C CG . ASP A 1 64 ? -6.956 2.565 16.654 1.00 26.49 ? 107 ASP A CG 1 ATOM 517 O OD1 . ASP A 1 64 ? -5.927 3.245 16.433 1.00 22.93 ? 107 ASP A OD1 1 ATOM 518 O OD2 . ASP A 1 64 ? -8.106 3.051 16.682 1.00 23.71 ? 107 ASP A OD2 1 ATOM 519 N N . VAL A 1 65 ? -5.823 -1.810 17.106 1.00 20.22 ? 108 VAL A N 1 ATOM 520 C CA . VAL A 1 65 ? -5.739 -3.034 17.899 1.00 19.61 ? 108 VAL A CA 1 ATOM 521 C C . VAL A 1 65 ? -4.319 -3.592 17.898 1.00 21.55 ? 108 VAL A C 1 ATOM 522 O O . VAL A 1 65 ? -3.863 -4.136 18.899 1.00 21.29 ? 108 VAL A O 1 ATOM 523 C CB . VAL A 1 65 ? -6.740 -4.096 17.422 1.00 20.13 ? 108 VAL A CB 1 ATOM 524 C CG1 . VAL A 1 65 ? -6.635 -5.348 18.289 1.00 19.77 ? 108 VAL A CG1 1 ATOM 525 C CG2 . VAL A 1 65 ? -8.154 -3.529 17.462 1.00 19.79 ? 108 VAL A CG2 1 ATOM 526 N N . ILE A 1 66 ? -3.616 -3.449 16.778 1.00 19.04 ? 109 ILE A N 1 ATOM 527 C CA . ILE A 1 66 ? -2.214 -3.852 16.726 1.00 21.48 ? 109 ILE A CA 1 ATOM 528 C C . ILE A 1 66 ? -1.406 -3.037 17.736 1.00 22.94 ? 109 ILE A C 1 ATOM 529 O O . ILE A 1 66 ? -0.592 -3.578 18.480 1.00 26.34 ? 109 ILE A O 1 ATOM 530 C CB . ILE A 1 66 ? -1.613 -3.682 15.308 1.00 18.06 ? 109 ILE A CB 1 ATOM 531 C CG1 . ILE A 1 66 ? -2.242 -4.686 14.339 1.00 20.86 ? 109 ILE A CG1 1 ATOM 532 C CG2 . ILE A 1 66 ? -0.102 -3.874 15.341 1.00 20.30 ? 109 ILE A CG2 1 ATOM 533 C CD1 . ILE A 1 66 ? -1.734 -4.556 12.908 1.00 27.17 ? 109 ILE A CD1 1 ATOM 534 N N . SER A 1 67 ? -1.648 -1.731 17.761 1.00 23.82 ? 110 SER A N 1 ATOM 535 C CA . SER A 1 67 ? -0.970 -0.853 18.701 1.00 26.90 ? 110 SER A CA 1 ATOM 536 C C . SER A 1 67 ? -1.294 -1.245 20.140 1.00 24.34 ? 110 SER A C 1 ATOM 537 O O . SER A 1 67 ? -0.409 -1.307 20.997 1.00 22.31 ? 110 SER A O 1 ATOM 538 C CB . SER A 1 67 ? -1.359 0.602 18.446 1.00 28.95 ? 110 SER A CB 1 ATOM 539 O OG . SER A 1 67 ? -0.654 1.468 19.316 1.00 34.62 ? 110 SER A OG 1 ATOM 540 N N . LEU A 1 68 ? -2.567 -1.509 20.404 1.00 18.10 ? 111 LEU A N 1 ATOM 541 C CA . LEU A 1 68 ? -2.987 -1.942 21.733 1.00 20.98 ? 111 LEU A CA 1 ATOM 542 C C . LEU A 1 68 ? -2.293 -3.246 22.154 1.00 23.68 ? 111 LEU A C 1 ATOM 543 O O . LEU A 1 68 ? -1.739 -3.340 23.255 1.00 26.18 ? 111 LEU A O 1 ATOM 544 C CB . LEU A 1 68 ? -4.514 -2.073 21.786 1.00 25.69 ? 111 LEU A CB 1 ATOM 545 C CG . LEU A 1 68 ? -5.182 -2.197 23.159 1.00 29.98 ? 111 LEU A CG 1 ATOM 546 C CD1 . LEU A 1 68 ? -6.629 -1.709 23.104 1.00 31.31 ? 111 LEU A CD1 1 ATOM 547 C CD2 . LEU A 1 68 ? -5.115 -3.627 23.652 1.00 26.98 ? 111 LEU A CD2 1 ATOM 548 N N . TRP A 1 69 ? -2.296 -4.243 21.277 1.00 19.73 ? 112 TRP A N 1 ATOM 549 C CA . TRP A 1 69 ? -1.670 -5.530 21.595 1.00 23.59 ? 112 TRP A CA 1 ATOM 550 C C . TRP A 1 69 ? -0.145 -5.419 21.698 1.00 27.14 ? 112 TRP A C 1 ATOM 551 O O . TRP A 1 69 ? 0.483 -6.126 22.482 1.00 26.21 ? 112 TRP A O 1 ATOM 552 C CB . TRP A 1 69 ? -2.064 -6.597 20.569 1.00 24.06 ? 112 TRP A CB 1 ATOM 553 C CG . TRP A 1 69 ? -3.404 -7.226 20.841 1.00 20.13 ? 112 TRP A CG 1 ATOM 554 C CD1 . TRP A 1 69 ? -4.602 -6.581 20.951 1.00 24.86 ? 112 TRP A CD1 1 ATOM 555 C CD2 . TRP A 1 69 ? -3.681 -8.619 21.023 1.00 20.25 ? 112 TRP A CD2 1 ATOM 556 N NE1 . TRP A 1 69 ? -5.607 -7.486 21.198 1.00 24.47 ? 112 TRP A NE1 1 ATOM 557 C CE2 . TRP A 1 69 ? -5.066 -8.748 21.244 1.00 21.55 ? 112 TRP A CE2 1 ATOM 558 C CE3 . TRP A 1 69 ? -2.891 -9.775 21.017 1.00 23.64 ? 112 TRP A CE3 1 ATOM 559 C CZ2 . TRP A 1 69 ? -5.681 -9.977 21.463 1.00 24.28 ? 112 TRP A CZ2 1 ATOM 560 C CZ3 . TRP A 1 69 ? -3.500 -10.999 21.235 1.00 24.74 ? 112 TRP A CZ3 1 ATOM 561 C CH2 . TRP A 1 69 ? -4.881 -11.093 21.452 1.00 24.89 ? 112 TRP A CH2 1 ATOM 562 N N . ASP A 1 70 ? 0.450 -4.529 20.914 1.00 26.51 ? 113 ASP A N 1 ATOM 563 C CA . ASP A 1 70 ? 1.898 -4.356 20.953 1.00 31.48 ? 113 ASP A CA 1 ATOM 564 C C . ASP A 1 70 ? 2.360 -3.726 22.273 1.00 33.67 ? 113 ASP A C 1 ATOM 565 O O . ASP A 1 70 ? 3.440 -4.033 22.774 1.00 37.92 ? 113 ASP A O 1 ATOM 566 C CB . ASP A 1 70 ? 2.367 -3.523 19.760 1.00 35.04 ? 113 ASP A CB 1 ATOM 567 C CG . ASP A 1 70 ? 2.459 -4.331 18.482 1.00 42.66 ? 113 ASP A CG 1 ATOM 568 O OD1 . ASP A 1 70 ? 1.893 -5.439 18.427 1.00 48.05 ? 113 ASP A OD1 1 ATOM 569 O OD2 . ASP A 1 70 ? 3.084 -3.848 17.518 1.00 46.38 ? 113 ASP A OD2 1 ATOM 570 N N . GLN A 1 71 ? 1.534 -2.859 22.845 1.00 31.93 ? 114 GLN A N 1 ATOM 571 C CA . GLN A 1 71 ? 1.886 -2.197 24.096 1.00 32.39 ? 114 GLN A CA 1 ATOM 572 C C . GLN A 1 71 ? 1.503 -3.050 25.308 1.00 34.25 ? 114 GLN A C 1 ATOM 573 O O . GLN A 1 71 ? 2.150 -2.975 26.355 1.00 39.06 ? 114 GLN A O 1 ATOM 574 C CB . GLN A 1 71 ? 1.193 -0.832 24.189 1.00 38.65 ? 114 GLN A CB 1 ATOM 575 C CG . GLN A 1 71 ? 1.521 0.141 23.045 1.00 50.93 ? 114 GLN A CG 1 ATOM 576 C CD . GLN A 1 71 ? 0.582 1.334 22.996 1.00 58.73 ? 114 GLN A CD 1 ATOM 577 O OE1 . GLN A 1 71 ? -0.184 1.578 23.925 1.00 60.44 ? 114 GLN A OE1 1 ATOM 578 N NE2 . GLN A 1 71 ? 0.642 2.084 21.908 1.00 60.45 ? 114 GLN A NE2 1 ATOM 579 N N . SER A 1 72 ? 0.467 -3.871 25.157 1.00 28.62 ? 115 SER A N 1 ATOM 580 C CA . SER A 1 72 ? -0.179 -4.510 26.300 1.00 34.22 ? 115 SER A CA 1 ATOM 581 C C . SER A 1 72 ? 0.129 -5.995 26.455 1.00 30.71 ? 115 SER A C 1 ATOM 582 O O . SER A 1 72 ? 0.038 -6.529 27.559 1.00 31.88 ? 115 SER A O 1 ATOM 583 C CB . SER A 1 72 ? -1.693 -4.324 26.195 1.00 38.58 ? 115 SER A CB 1 ATOM 584 O OG . SER A 1 72 ? -2.014 -2.993 25.826 1.00 49.38 ? 115 SER A OG 1 ATOM 585 N N . LEU A 1 73 ? 0.479 -6.661 25.357 1.00 26.24 ? 116 LEU A N 1 ATOM 586 C CA . LEU A 1 73 ? 0.678 -8.109 25.379 1.00 31.53 ? 116 LEU A CA 1 ATOM 587 C C . LEU A 1 73 ? 2.013 -8.539 24.781 1.00 31.79 ? 116 LEU A C 1 ATOM 588 O O . LEU A 1 73 ? 2.060 -9.434 23.944 1.00 32.81 ? 116 LEU A O 1 ATOM 589 C CB . LEU A 1 73 ? -0.467 -8.830 24.652 1.00 31.35 ? 116 LEU A CB 1 ATOM 590 C CG . LEU A 1 73 ? -1.835 -8.926 25.338 1.00 35.50 ? 116 LEU A CG 1 ATOM 591 C CD1 . LEU A 1 73 ? -2.603 -7.619 25.227 1.00 37.23 ? 116 LEU A CD1 1 ATOM 592 C CD2 . LEU A 1 73 ? -2.652 -10.066 24.747 1.00 33.30 ? 116 LEU A CD2 1 ATOM 593 N N . GLN A 1 74 ? 3.102 -7.916 25.215 1.00 33.17 ? 117 GLN A N 1 ATOM 594 C CA . GLN A 1 74 ? 4.424 -8.373 24.805 1.00 38.61 ? 117 GLN A CA 1 ATOM 595 C C . GLN A 1 74 ? 4.748 -9.697 25.490 1.00 35.60 ? 117 GLN A C 1 ATOM 596 O O . GLN A 1 74 ? 4.473 -9.878 26.676 1.00 36.19 ? 117 GLN A O 1 ATOM 597 C CB . GLN A 1 74 ? 5.494 -7.322 25.106 1.00 45.58 ? 117 GLN A CB 1 ATOM 598 C CG . GLN A 1 74 ? 5.426 -6.084 24.201 1.00 49.05 ? 117 GLN A CG 1 ATOM 599 C CD . GLN A 1 74 ? 5.934 -6.341 22.791 1.00 50.94 ? 117 GLN A CD 1 ATOM 600 O OE1 . GLN A 1 74 ? 6.856 -7.122 22.585 1.00 48.02 ? 117 GLN A OE1 1 ATOM 601 N NE2 . GLN A 1 74 ? 5.337 -5.674 21.817 1.00 48.83 ? 117 GLN A NE2 1 ATOM 602 N N . PRO A 1 75 ? 5.315 -10.640 24.731 1.00 31.92 ? 118 PRO A N 1 ATOM 603 C CA . PRO A 1 75 ? 5.617 -11.992 25.204 1.00 28.65 ? 118 PRO A CA 1 ATOM 604 C C . PRO A 1 75 ? 6.981 -12.061 25.866 1.00 28.68 ? 118 PRO A C 1 ATOM 605 O O . PRO A 1 75 ? 7.758 -11.111 25.760 1.00 30.45 ? 118 PRO A O 1 ATOM 606 C CB . PRO A 1 75 ? 5.672 -12.787 23.905 1.00 27.03 ? 118 PRO A CB 1 ATOM 607 C CG . PRO A 1 75 ? 6.264 -11.818 22.941 1.00 27.44 ? 118 PRO A CG 1 ATOM 608 C CD . PRO A 1 75 ? 5.663 -10.473 23.309 1.00 30.65 ? 118 PRO A CD 1 ATOM 609 N N . CYS A 1 76 ? 7.272 -13.171 26.531 1.00 25.65 ? 119 CYS A N 1 ATOM 610 C CA . CYS A 1 76 ? 8.584 -13.375 27.122 1.00 29.20 ? 119 CYS A CA 1 ATOM 611 C C . CYS A 1 76 ? 9.615 -13.538 26.014 1.00 33.47 ? 119 CYS A C 1 ATOM 612 O O . CYS A 1 76 ? 10.742 -13.063 26.125 1.00 33.53 ? 119 CYS A O 1 ATOM 613 C CB . CYS A 1 76 ? 8.571 -14.600 28.033 1.00 33.72 ? 119 CYS A CB 1 ATOM 614 S SG . CYS A 1 76 ? 7.263 -14.555 29.278 1.00 61.42 ? 119 CYS A SG 1 ATOM 615 N N . VAL A 1 77 ? 9.212 -14.205 24.939 1.00 27.83 ? 120 VAL A N 1 ATOM 616 C CA . VAL A 1 77 ? 10.076 -14.405 23.786 1.00 30.74 ? 120 VAL A CA 1 ATOM 617 C C . VAL A 1 77 ? 9.315 -14.121 22.501 1.00 32.83 ? 120 VAL A C 1 ATOM 618 O O . VAL A 1 77 ? 8.165 -14.521 22.352 1.00 28.52 ? 120 VAL A O 1 ATOM 619 C CB . VAL A 1 77 ? 10.612 -15.844 23.726 1.00 43.69 ? 120 VAL A CB 1 ATOM 620 C CG1 . VAL A 1 77 ? 11.428 -16.052 22.460 1.00 51.32 ? 120 VAL A CG1 1 ATOM 621 C CG2 . VAL A 1 77 ? 11.438 -16.157 24.962 1.00 43.46 ? 120 VAL A CG2 1 ATOM 622 N N . LYS A 1 78 ? 9.964 -13.430 21.573 1.00 32.58 ? 121 LYS A N 1 ATOM 623 C CA . LYS A 1 78 ? 9.352 -13.127 20.289 1.00 31.59 ? 121 LYS A CA 1 ATOM 624 C C . LYS A 1 78 ? 10.272 -13.524 19.144 1.00 32.84 ? 121 LYS A C 1 ATOM 625 O O . LYS A 1 78 ? 11.362 -12.982 18.997 1.00 33.67 ? 121 LYS A O 1 ATOM 626 C CB . LYS A 1 78 ? 9.006 -11.641 20.194 1.00 41.25 ? 121 LYS A CB 1 ATOM 627 C CG . LYS A 1 78 ? 8.112 -11.289 19.019 1.00 52.48 ? 121 LYS A CG 1 ATOM 628 C CD . LYS A 1 78 ? 8.278 -9.833 18.619 1.00 62.71 ? 121 LYS A CD 1 ATOM 629 C CE . LYS A 1 78 ? 7.354 -8.931 19.419 1.00 71.73 ? 121 LYS A CE 1 ATOM 630 N NZ . LYS A 1 78 ? 7.832 -7.521 19.436 1.00 76.35 ? 121 LYS A NZ 1 ATOM 631 N N . LEU A 1 79 ? 9.823 -14.478 18.337 1.00 28.82 ? 122 LEU A N 1 ATOM 632 C CA . LEU A 1 79 ? 10.582 -14.927 17.182 1.00 30.66 ? 122 LEU A CA 1 ATOM 633 C C . LEU A 1 79 ? 10.020 -14.284 15.923 1.00 35.14 ? 122 LEU A C 1 ATOM 634 O O . LEU A 1 79 ? 8.946 -14.653 15.453 1.00 31.27 ? 122 LEU A O 1 ATOM 635 C CB . LEU A 1 79 ? 10.531 -16.450 17.068 1.00 36.06 ? 122 LEU A CB 1 ATOM 636 C CG . LEU A 1 79 ? 10.771 -17.224 18.366 1.00 40.72 ? 122 LEU A CG 1 ATOM 637 C CD1 . LEU A 1 79 ? 10.092 -18.583 18.324 1.00 38.62 ? 122 LEU A CD1 1 ATOM 638 C CD2 . LEU A 1 79 ? 12.259 -17.370 18.635 1.00 43.77 ? 122 LEU A CD2 1 ATOM 639 N N . THR A 1 80 ? 10.747 -13.312 15.386 1.00 33.87 ? 123 THR A N 1 ATOM 640 C CA . THR A 1 80 ? 10.271 -12.559 14.235 1.00 32.57 ? 123 THR A CA 1 ATOM 641 C C . THR A 1 80 ? 11.390 -12.226 13.254 1.00 37.79 ? 123 THR A C 1 ATOM 642 O O . THR A 1 80 ? 12.405 -11.646 13.626 1.00 40.75 ? 123 THR A O 1 ATOM 643 C CB . THR A 1 80 ? 9.576 -11.257 14.676 1.00 35.40 ? 123 THR A CB 1 ATOM 644 O OG1 . THR A 1 80 ? 9.248 -10.470 13.525 1.00 42.68 ? 123 THR A OG1 1 ATOM 645 C CG2 . THR A 1 80 ? 10.483 -10.455 15.588 1.00 36.07 ? 123 THR A CG2 1 ATOM 646 N N . GLY A 1 81 ? 11.187 -12.601 11.996 1.00 44.14 ? 124 GLY A N 1 ATOM 647 C CA . GLY A 1 81 ? 12.128 -12.305 10.928 1.00 44.25 ? 124 GLY A CA 1 ATOM 648 C C . GLY A 1 81 ? 13.546 -12.775 11.189 1.00 47.51 ? 124 GLY A C 1 ATOM 649 O O . GLY A 1 81 ? 14.511 -12.124 10.787 1.00 52.55 ? 124 GLY A O 1 ATOM 650 N N . GLY A 1 82 ? 13.675 -13.909 11.868 1.00 44.15 ? 198 GLY A N 1 ATOM 651 C CA . GLY A 1 82 ? 14.976 -14.500 12.116 1.00 42.47 ? 198 GLY A CA 1 ATOM 652 C C . GLY A 1 82 ? 15.646 -14.024 13.390 1.00 43.98 ? 198 GLY A C 1 ATOM 653 O O . GLY A 1 82 ? 16.688 -14.548 13.778 1.00 50.32 ? 198 GLY A O 1 ATOM 654 N N . SER A 1 83 ? 15.056 -13.029 14.045 1.00 43.82 ? 199 SER A N 1 ATOM 655 C CA . SER A 1 83 ? 15.627 -12.504 15.282 1.00 44.72 ? 199 SER A CA 1 ATOM 656 C C . SER A 1 83 ? 14.871 -12.972 16.526 1.00 41.25 ? 199 SER A C 1 ATOM 657 O O . SER A 1 83 ? 13.697 -13.336 16.458 1.00 35.26 ? 199 SER A O 1 ATOM 658 C CB . SER A 1 83 ? 15.708 -10.975 15.239 1.00 48.03 ? 199 SER A CB 1 ATOM 659 O OG . SER A 1 83 ? 14.445 -10.402 14.952 1.00 54.84 ? 199 SER A OG 1 ATOM 660 N N . VAL A 1 84 ? 15.561 -12.969 17.661 1.00 41.97 ? 200 VAL A N 1 ATOM 661 C CA . VAL A 1 84 ? 14.962 -13.379 18.924 1.00 41.67 ? 200 VAL A CA 1 ATOM 662 C C . VAL A 1 84 ? 14.948 -12.218 19.910 1.00 42.91 ? 200 VAL A C 1 ATOM 663 O O . VAL A 1 84 ? 15.999 -11.714 20.306 1.00 44.06 ? 200 VAL A O 1 ATOM 664 C CB . VAL A 1 84 ? 15.721 -14.562 19.553 1.00 46.75 ? 200 VAL A CB 1 ATOM 665 C CG1 . VAL A 1 84 ? 15.077 -14.964 20.873 1.00 46.76 ? 200 VAL A CG1 1 ATOM 666 C CG2 . VAL A 1 84 ? 15.762 -15.741 18.591 1.00 44.70 ? 200 VAL A CG2 1 ATOM 667 N N . ILE A 1 85 ? 13.750 -11.798 20.302 1.00 40.36 ? 201 ILE A N 1 ATOM 668 C CA . ILE A 1 85 ? 13.583 -10.683 21.224 1.00 42.54 ? 201 ILE A CA 1 ATOM 669 C C . ILE A 1 85 ? 13.053 -11.191 22.560 1.00 42.19 ? 201 ILE A C 1 ATOM 670 O O . ILE A 1 85 ? 11.991 -11.808 22.614 1.00 39.78 ? 201 ILE A O 1 ATOM 671 C CB . ILE A 1 85 ? 12.598 -9.641 20.658 1.00 46.58 ? 201 ILE A CB 1 ATOM 672 C CG1 . ILE A 1 85 ? 12.945 -9.308 19.204 1.00 50.12 ? 201 ILE A CG1 1 ATOM 673 C CG2 . ILE A 1 85 ? 12.588 -8.384 21.518 1.00 47.28 ? 201 ILE A CG2 1 ATOM 674 C CD1 . ILE A 1 85 ? 14.304 -8.664 19.032 1.00 54.47 ? 201 ILE A CD1 1 ATOM 675 N N . LYS A 1 86 ? 13.793 -10.937 23.635 1.00 35.18 ? 202 LYS A N 1 ATOM 676 C CA . LYS A 1 86 ? 13.383 -11.391 24.963 1.00 40.37 ? 202 LYS A CA 1 ATOM 677 C C . LYS A 1 86 ? 13.039 -10.214 25.863 1.00 41.31 ? 202 LYS A C 1 ATOM 678 O O . LYS A 1 86 ? 13.753 -9.211 25.876 1.00 41.94 ? 202 LYS A O 1 ATOM 679 C CB . LYS A 1 86 ? 14.491 -12.218 25.619 1.00 42.27 ? 202 LYS A CB 1 ATOM 680 C CG . LYS A 1 86 ? 14.903 -13.466 24.849 1.00 45.73 ? 202 LYS A CG 1 ATOM 681 C CD . LYS A 1 86 ? 16.037 -14.185 25.570 1.00 50.12 ? 202 LYS A CD 1 ATOM 682 C CE . LYS A 1 86 ? 16.580 -15.349 24.753 1.00 54.43 ? 202 LYS A CE 1 ATOM 683 N NZ . LYS A 1 86 ? 15.613 -16.478 24.640 1.00 58.56 ? 202 LYS A NZ 1 ATOM 684 N N . GLN A 1 87 ? 11.947 -10.334 26.613 1.00 41.64 ? 203 GLN A N 1 ATOM 685 C CA . GLN A 1 87 ? 11.572 -9.293 27.566 1.00 45.15 ? 203 GLN A CA 1 ATOM 686 C C . GLN A 1 87 ? 10.630 -9.803 28.652 1.00 42.49 ? 203 GLN A C 1 ATOM 687 O O . GLN A 1 87 ? 10.185 -10.949 28.612 1.00 34.58 ? 203 GLN A O 1 ATOM 688 C CB . GLN A 1 87 ? 10.967 -8.089 26.843 1.00 49.02 ? 203 GLN A CB 1 ATOM 689 C CG . GLN A 1 87 ? 9.797 -8.435 25.931 1.00 48.14 ? 203 GLN A CG 1 ATOM 690 C CD . GLN A 1 87 ? 9.611 -7.422 24.812 1.00 51.15 ? 203 GLN A CD 1 ATOM 691 O OE1 . GLN A 1 87 ? 10.030 -6.273 24.920 1.00 55.21 ? 203 GLN A OE1 1 ATOM 692 N NE2 . GLN A 1 87 ? 8.980 -7.848 23.731 1.00 49.38 ? 203 GLN A NE2 1 ATOM 693 N N . ALA A 1 88 ? 10.355 -8.950 29.634 1.00 41.31 ? 204 ALA A N 1 ATOM 694 C CA . ALA A 1 88 ? 9.452 -9.286 30.729 1.00 43.79 ? 204 ALA A CA 1 ATOM 695 C C . ALA A 1 88 ? 8.030 -9.497 30.219 1.00 39.51 ? 204 ALA A C 1 ATOM 696 O O . ALA A 1 88 ? 7.568 -8.781 29.331 1.00 34.90 ? 204 ALA A O 1 ATOM 697 C CB . ALA A 1 88 ? 9.479 -8.191 31.779 1.00 42.37 ? 204 ALA A CB 1 ATOM 698 N N . CYS A 1 89 ? 7.333 -10.467 30.802 1.00 35.13 ? 205 CYS A N 1 ATOM 699 C CA . CYS A 1 89 ? 5.991 -10.821 30.353 1.00 34.37 ? 205 CYS A CA 1 ATOM 700 C C . CYS A 1 89 ? 5.036 -11.036 31.525 1.00 31.51 ? 205 CYS A C 1 ATOM 701 O O . CYS A 1 89 ? 4.514 -12.131 31.710 1.00 30.22 ? 205 CYS A O 1 ATOM 702 C CB . CYS A 1 89 ? 6.049 -12.087 29.495 1.00 35.35 ? 205 CYS A CB 1 ATOM 703 S SG . CYS A 1 89 ? 6.966 -13.446 30.281 1.00 48.01 ? 205 CYS A SG 1 ATOM 704 N N . PRO A 1 90 ? 4.785 -9.978 32.305 1.00 37.11 ? 206 PRO A N 1 ATOM 705 C CA . PRO A 1 90 ? 3.913 -10.094 33.477 1.00 41.02 ? 206 PRO A CA 1 ATOM 706 C C . PRO A 1 90 ? 2.478 -10.428 33.084 1.00 36.85 ? 206 PRO A C 1 ATOM 707 O O . PRO A 1 90 ? 2.055 -10.116 31.972 1.00 31.91 ? 206 PRO A O 1 ATOM 708 C CB . PRO A 1 90 ? 3.969 -8.691 34.089 1.00 43.29 ? 206 PRO A CB 1 ATOM 709 C CG . PRO A 1 90 ? 4.290 -7.793 32.940 1.00 42.00 ? 206 PRO A CG 1 ATOM 710 C CD . PRO A 1 90 ? 5.227 -8.591 32.078 1.00 40.16 ? 206 PRO A CD 1 ATOM 711 N N . LYS A 1 91 ? 1.743 -11.063 33.989 1.00 31.07 ? 207 LYS A N 1 ATOM 712 C CA . LYS A 1 91 ? 0.325 -11.304 33.769 1.00 33.53 ? 207 LYS A CA 1 ATOM 713 C C . LYS A 1 91 ? -0.422 -9.983 33.802 1.00 31.50 ? 207 LYS A C 1 ATOM 714 O O . LYS A 1 91 ? -0.045 -9.071 34.537 1.00 33.51 ? 207 LYS A O 1 ATOM 715 C CB . LYS A 1 91 ? -0.229 -12.251 34.831 1.00 35.41 ? 207 LYS A CB 1 ATOM 716 C CG . LYS A 1 91 ? 0.259 -13.669 34.676 1.00 35.82 ? 207 LYS A CG 1 ATOM 717 C CD . LYS A 1 91 ? -0.140 -14.209 33.312 1.00 37.81 ? 207 LYS A CD 1 ATOM 718 C CE . LYS A 1 91 ? 0.322 -15.633 33.126 1.00 37.68 ? 207 LYS A CE 1 ATOM 719 N NZ . LYS A 1 91 ? -0.141 -16.185 31.825 1.00 33.07 ? 207 LYS A NZ 1 ATOM 720 N N . ILE A 1 92 ? -1.478 -9.880 33.002 1.00 27.02 ? 208 ILE A N 1 ATOM 721 C CA . ILE A 1 92 ? -2.238 -8.643 32.909 1.00 24.30 ? 208 ILE A CA 1 ATOM 722 C C . ILE A 1 92 ? -3.720 -8.866 33.179 1.00 26.55 ? 208 ILE A C 1 ATOM 723 O O . ILE A 1 92 ? -4.192 -10.007 33.265 1.00 26.38 ? 208 ILE A O 1 ATOM 724 C CB . ILE A 1 92 ? -2.114 -8.016 31.500 1.00 28.58 ? 208 ILE A CB 1 ATOM 725 C CG1 . ILE A 1 92 ? -2.667 -8.972 30.440 1.00 25.53 ? 208 ILE A CG1 1 ATOM 726 C CG2 . ILE A 1 92 ? -0.670 -7.654 31.195 1.00 33.39 ? 208 ILE A CG2 1 ATOM 727 C CD1 . ILE A 1 92 ? -2.835 -8.323 29.065 1.00 26.10 ? 208 ILE A CD1 1 ATOM 728 N N . SER A 1 93 ? -4.441 -7.756 33.305 1.00 26.01 ? 209 SER A N 1 ATOM 729 C CA . SER A 1 93 ? -5.893 -7.762 33.358 1.00 29.33 ? 209 SER A CA 1 ATOM 730 C C . SER A 1 93 ? -6.398 -7.462 31.949 1.00 26.61 ? 209 SER A C 1 ATOM 731 O O . SER A 1 93 ? -6.018 -6.457 31.351 1.00 22.62 ? 209 SER A O 1 ATOM 732 C CB . SER A 1 93 ? -6.386 -6.702 34.342 1.00 32.09 ? 209 SER A CB 1 ATOM 733 O OG . SER A 1 93 ? -7.793 -6.560 34.289 1.00 32.34 ? 209 SER A OG 1 ATOM 734 N N . PHE A 1 94 ? -7.248 -8.333 31.419 1.00 27.48 ? 210 PHE A N 1 ATOM 735 C CA . PHE A 1 94 ? -7.619 -8.270 30.010 1.00 23.75 ? 210 PHE A CA 1 ATOM 736 C C . PHE A 1 94 ? -9.107 -8.551 29.803 1.00 23.86 ? 210 PHE A C 1 ATOM 737 O O . PHE A 1 94 ? -9.596 -9.635 30.134 1.00 24.34 ? 210 PHE A O 1 ATOM 738 C CB . PHE A 1 94 ? -6.776 -9.284 29.231 1.00 23.12 ? 210 PHE A CB 1 ATOM 739 C CG . PHE A 1 94 ? -7.029 -9.293 27.744 1.00 23.49 ? 210 PHE A CG 1 ATOM 740 C CD1 . PHE A 1 94 ? -8.110 -9.979 27.210 1.00 24.22 ? 210 PHE A CD1 1 ATOM 741 C CD2 . PHE A 1 94 ? -6.163 -8.645 26.880 1.00 24.08 ? 210 PHE A CD2 1 ATOM 742 C CE1 . PHE A 1 94 ? -8.330 -10.002 25.842 1.00 21.85 ? 210 PHE A CE1 1 ATOM 743 C CE2 . PHE A 1 94 ? -6.375 -8.667 25.513 1.00 24.02 ? 210 PHE A CE2 1 ATOM 744 C CZ . PHE A 1 94 ? -7.461 -9.347 24.996 1.00 21.90 ? 210 PHE A CZ 1 ATOM 745 N N . ASP A 1 95 ? -9.807 -7.572 29.238 1.00 23.69 ? 211 ASP A N 1 ATOM 746 C CA . ASP A 1 95 ? -11.240 -7.669 28.965 1.00 23.08 ? 211 ASP A CA 1 ATOM 747 C C . ASP A 1 95 ? -11.638 -6.507 28.051 1.00 20.54 ? 211 ASP A C 1 ATOM 748 O O . ASP A 1 95 ? -11.710 -5.358 28.491 1.00 23.62 ? 211 ASP A O 1 ATOM 749 C CB . ASP A 1 95 ? -12.034 -7.627 30.277 1.00 26.94 ? 211 ASP A CB 1 ATOM 750 C CG . ASP A 1 95 ? -13.501 -7.987 30.091 1.00 35.19 ? 211 ASP A CG 1 ATOM 751 O OD1 . ASP A 1 95 ? -13.848 -8.640 29.081 1.00 30.21 ? 211 ASP A OD1 1 ATOM 752 O OD2 . ASP A 1 95 ? -14.310 -7.626 30.969 1.00 40.96 ? 211 ASP A OD2 1 ATOM 753 N N . PRO A 1 96 ? -11.881 -6.803 26.766 1.00 21.86 ? 212 PRO A N 1 ATOM 754 C CA . PRO A 1 96 ? -12.144 -5.770 25.753 1.00 20.87 ? 212 PRO A CA 1 ATOM 755 C C . PRO A 1 96 ? -13.268 -4.807 26.145 1.00 22.51 ? 212 PRO A C 1 ATOM 756 O O . PRO A 1 96 ? -14.253 -5.222 26.749 1.00 22.74 ? 212 PRO A O 1 ATOM 757 C CB . PRO A 1 96 ? -12.553 -6.591 24.525 1.00 21.93 ? 212 PRO A CB 1 ATOM 758 C CG . PRO A 1 96 ? -11.830 -7.898 24.702 1.00 21.98 ? 212 PRO A CG 1 ATOM 759 C CD . PRO A 1 96 ? -11.862 -8.158 26.187 1.00 20.70 ? 212 PRO A CD 1 ATOM 760 N N . ILE A 1 97 ? -13.105 -3.529 25.814 1.00 21.82 ? 213 ILE A N 1 ATOM 761 C CA . ILE A 1 97 ? -14.158 -2.547 26.021 1.00 19.87 ? 213 ILE A CA 1 ATOM 762 C C . ILE A 1 97 ? -14.586 -1.967 24.679 1.00 19.22 ? 213 ILE A C 1 ATOM 763 O O . ILE A 1 97 ? -13.829 -2.011 23.708 1.00 20.87 ? 213 ILE A O 1 ATOM 764 C CB . ILE A 1 97 ? -13.715 -1.401 26.959 1.00 27.23 ? 213 ILE A CB 1 ATOM 765 C CG1 . ILE A 1 97 ? -12.627 -0.544 26.302 1.00 23.85 ? 213 ILE A CG1 1 ATOM 766 C CG2 . ILE A 1 97 ? -13.257 -1.958 28.305 1.00 33.77 ? 213 ILE A CG2 1 ATOM 767 C CD1 . ILE A 1 97 ? -12.231 0.689 27.142 1.00 25.40 ? 213 ILE A CD1 1 ATOM 768 N N . PRO A 1 98 ? -15.813 -1.435 24.613 1.00 19.98 ? 214 PRO A N 1 ATOM 769 C CA . PRO A 1 98 ? -16.284 -0.882 23.341 1.00 21.60 ? 214 PRO A CA 1 ATOM 770 C C . PRO A 1 98 ? -15.518 0.380 22.955 1.00 20.21 ? 214 PRO A C 1 ATOM 771 O O . PRO A 1 98 ? -15.313 1.271 23.774 1.00 23.65 ? 214 PRO A O 1 ATOM 772 C CB . PRO A 1 98 ? -17.753 -0.543 23.624 1.00 27.59 ? 214 PRO A CB 1 ATOM 773 C CG . PRO A 1 98 ? -18.124 -1.398 24.804 1.00 30.78 ? 214 PRO A CG 1 ATOM 774 C CD . PRO A 1 98 ? -16.877 -1.474 25.630 1.00 26.47 ? 214 PRO A CD 1 ATOM 775 N N . ILE A 1 99 ? -15.083 0.436 21.706 1.00 15.86 ? 215 ILE A N 1 ATOM 776 C CA . ILE A 1 99 ? -14.408 1.614 21.187 1.00 14.54 ? 215 ILE A CA 1 ATOM 777 C C . ILE A 1 99 ? -15.239 2.172 20.046 1.00 15.81 ? 215 ILE A C 1 ATOM 778 O O . ILE A 1 99 ? -15.630 1.428 19.151 1.00 19.62 ? 215 ILE A O 1 ATOM 779 C CB . ILE A 1 99 ? -13.015 1.260 20.642 1.00 23.05 ? 215 ILE A CB 1 ATOM 780 C CG1 . ILE A 1 99 ? -12.186 0.534 21.707 1.00 23.96 ? 215 ILE A CG1 1 ATOM 781 C CG2 . ILE A 1 99 ? -12.310 2.511 20.148 1.00 23.89 ? 215 ILE A CG2 1 ATOM 782 C CD1 . ILE A 1 99 ? -11.970 1.356 22.984 1.00 28.30 ? 215 ILE A CD1 1 ATOM 783 N N . HIS A 1 100 ? -15.508 3.477 20.085 1.00 19.33 ? 216 HIS A N 1 ATOM 784 C CA . HIS A 1 100 ? -16.251 4.160 19.036 1.00 23.78 ? 216 HIS A CA 1 ATOM 785 C C . HIS A 1 100 ? -15.278 4.811 18.064 1.00 25.44 ? 216 HIS A C 1 ATOM 786 O O . HIS A 1 100 ? -14.313 5.438 18.486 1.00 25.08 ? 216 HIS A O 1 ATOM 787 C CB . HIS A 1 100 ? -17.123 5.269 19.633 1.00 21.53 ? 216 HIS A CB 1 ATOM 788 C CG . HIS A 1 100 ? -18.128 4.786 20.637 1.00 26.85 ? 216 HIS A CG 1 ATOM 789 N ND1 . HIS A 1 100 ? -19.454 4.618 20.333 1.00 25.85 ? 216 HIS A ND1 1 ATOM 790 C CD2 . HIS A 1 100 ? -17.985 4.453 21.943 1.00 30.09 ? 216 HIS A CD2 1 ATOM 791 C CE1 . HIS A 1 100 ? -20.099 4.188 21.412 1.00 28.61 ? 216 HIS A CE1 1 ATOM 792 N NE2 . HIS A 1 100 ? -19.231 4.082 22.394 1.00 27.24 ? 216 HIS A NE2 1 ATOM 793 N N . TYR A 1 101 ? -15.542 4.673 16.771 1.00 20.76 ? 217 TYR A N 1 ATOM 794 C CA . TYR A 1 101 ? -14.748 5.355 15.750 1.00 19.10 ? 217 TYR A CA 1 ATOM 795 C C . TYR A 1 101 ? -15.479 6.579 15.211 1.00 19.33 ? 217 TYR A C 1 ATOM 796 O O . TYR A 1 101 ? -16.654 6.503 14.851 1.00 19.33 ? 217 TYR A O 1 ATOM 797 C CB . TYR A 1 101 ? -14.322 4.374 14.648 1.00 22.62 ? 217 TYR A CB 1 ATOM 798 C CG . TYR A 1 101 ? -13.199 3.504 15.150 1.00 21.81 ? 217 TYR A CG 1 ATOM 799 C CD1 . TYR A 1 101 ? -11.883 3.916 15.029 1.00 26.40 ? 217 TYR A CD1 1 ATOM 800 C CD2 . TYR A 1 101 ? -13.458 2.315 15.822 1.00 28.18 ? 217 TYR A CD2 1 ATOM 801 C CE1 . TYR A 1 101 ? -10.850 3.151 15.523 1.00 23.20 ? 217 TYR A CE1 1 ATOM 802 C CE2 . TYR A 1 101 ? -12.427 1.541 16.321 1.00 27.21 ? 217 TYR A CE2 1 ATOM 803 C CZ . TYR A 1 101 ? -11.123 1.972 16.169 1.00 22.31 ? 217 TYR A CZ 1 ATOM 804 O OH . TYR A 1 101 ? -10.080 1.225 16.664 1.00 23.00 ? 217 TYR A OH 1 ATOM 805 N N . CYS A 1 102 ? -14.774 7.709 15.180 1.00 18.34 ? 218 CYS A N 1 ATOM 806 C CA . CYS A 1 102 ? -15.392 9.006 14.942 1.00 18.08 ? 218 CYS A CA 1 ATOM 807 C C . CYS A 1 102 ? -14.666 9.834 13.887 1.00 23.65 ? 218 CYS A C 1 ATOM 808 O O . CYS A 1 102 ? -13.444 9.771 13.758 1.00 21.67 ? 218 CYS A O 1 ATOM 809 C CB . CYS A 1 102 ? -15.433 9.809 16.243 1.00 22.76 ? 218 CYS A CB 1 ATOM 810 S SG . CYS A 1 102 ? -16.095 8.904 17.656 1.00 30.46 ? 218 CYS A SG 1 ATOM 811 N N . THR A 1 103 ? -15.429 10.640 13.160 1.00 24.05 ? 219 THR A N 1 ATOM 812 C CA . THR A 1 103 ? -14.864 11.503 12.132 1.00 22.64 ? 219 THR A CA 1 ATOM 813 C C . THR A 1 103 ? -14.501 12.884 12.672 1.00 26.99 ? 219 THR A C 1 ATOM 814 O O . THR A 1 103 ? -15.181 13.418 13.545 1.00 28.39 ? 219 THR A O 1 ATOM 815 C CB . THR A 1 103 ? -15.843 11.667 10.961 1.00 25.82 ? 219 THR A CB 1 ATOM 816 O OG1 . THR A 1 103 ? -17.177 11.779 11.475 1.00 23.79 ? 219 THR A OG1 1 ATOM 817 C CG2 . THR A 1 103 ? -15.764 10.458 10.038 1.00 23.82 ? 219 THR A CG2 1 ATOM 818 N N . PRO A 1 104 ? -13.423 13.472 12.139 1.00 26.84 ? 220 PRO A N 1 ATOM 819 C CA . PRO A 1 104 ? -13.046 14.845 12.475 1.00 30.91 ? 220 PRO A CA 1 ATOM 820 C C . PRO A 1 104 ? -13.959 15.848 11.776 1.00 29.67 ? 220 PRO A C 1 ATOM 821 O O . PRO A 1 104 ? -14.828 15.459 10.990 1.00 31.22 ? 220 PRO A O 1 ATOM 822 C CB . PRO A 1 104 ? -11.631 14.954 11.910 1.00 33.99 ? 220 PRO A CB 1 ATOM 823 C CG . PRO A 1 104 ? -11.653 14.048 10.721 1.00 29.43 ? 220 PRO A CG 1 ATOM 824 C CD . PRO A 1 104 ? -12.533 12.888 11.120 1.00 24.96 ? 220 PRO A CD 1 ATOM 825 N N . ALA A 1 105 ? -13.764 17.130 12.066 1.00 32.79 ? 221 ALA A N 1 ATOM 826 C CA . ALA A 1 105 ? -14.560 18.184 11.449 1.00 35.55 ? 221 ALA A CA 1 ATOM 827 C C . ALA A 1 105 ? -14.514 18.087 9.927 1.00 32.89 ? 221 ALA A C 1 ATOM 828 O O . ALA A 1 105 ? -13.477 17.761 9.350 1.00 31.50 ? 221 ALA A O 1 ATOM 829 C CB . ALA A 1 105 ? -14.068 19.547 11.903 1.00 38.38 ? 221 ALA A CB 1 ATOM 830 N N . GLY A 1 106 ? -15.642 18.368 9.283 1.00 31.35 ? 222 GLY A N 1 ATOM 831 C CA . GLY A 1 106 ? -15.706 18.387 7.835 1.00 32.60 ? 222 GLY A CA 1 ATOM 832 C C . GLY A 1 106 ? -16.022 17.024 7.259 1.00 31.52 ? 222 GLY A C 1 ATOM 833 O O . GLY A 1 106 ? -16.154 16.866 6.046 1.00 32.06 ? 222 GLY A O 1 ATOM 834 N N . TYR A 1 107 ? -16.143 16.033 8.137 1.00 26.82 ? 223 TYR A N 1 ATOM 835 C CA . TYR A 1 107 ? -16.488 14.683 7.724 1.00 24.74 ? 223 TYR A CA 1 ATOM 836 C C . TYR A 1 107 ? -17.632 14.150 8.565 1.00 27.61 ? 223 TYR A C 1 ATOM 837 O O . TYR A 1 107 ? -17.929 14.680 9.633 1.00 30.03 ? 223 TYR A O 1 ATOM 838 C CB . TYR A 1 107 ? -15.285 13.751 7.868 1.00 26.58 ? 223 TYR A CB 1 ATOM 839 C CG . TYR A 1 107 ? -14.126 14.115 6.976 1.00 28.77 ? 223 TYR A CG 1 ATOM 840 C CD1 . TYR A 1 107 ? -13.221 15.100 7.348 1.00 31.48 ? 223 TYR A CD1 1 ATOM 841 C CD2 . TYR A 1 107 ? -13.939 13.477 5.758 1.00 28.55 ? 223 TYR A CD2 1 ATOM 842 C CE1 . TYR A 1 107 ? -12.158 15.440 6.529 1.00 33.63 ? 223 TYR A CE1 1 ATOM 843 C CE2 . TYR A 1 107 ? -12.881 13.808 4.936 1.00 32.26 ? 223 TYR A CE2 1 ATOM 844 C CZ . TYR A 1 107 ? -11.995 14.791 5.324 1.00 33.57 ? 223 TYR A CZ 1 ATOM 845 O OH . TYR A 1 107 ? -10.937 15.118 4.506 1.00 36.06 ? 223 TYR A OH 1 ATOM 846 N N . VAL A 1 108 ? -18.263 13.090 8.078 1.00 20.45 ? 224 VAL A N 1 ATOM 847 C CA . VAL A 1 108 ? -19.314 12.421 8.823 1.00 27.07 ? 224 VAL A CA 1 ATOM 848 C C . VAL A 1 108 ? -19.335 10.950 8.425 1.00 26.11 ? 224 VAL A C 1 ATOM 849 O O . VAL A 1 108 ? -18.760 10.565 7.409 1.00 26.23 ? 224 VAL A O 1 ATOM 850 C CB . VAL A 1 108 ? -20.690 13.071 8.559 1.00 37.12 ? 224 VAL A CB 1 ATOM 851 C CG1 . VAL A 1 108 ? -21.198 12.700 7.180 1.00 32.82 ? 224 VAL A CG1 1 ATOM 852 C CG2 . VAL A 1 108 ? -21.691 12.658 9.624 1.00 44.65 ? 224 VAL A CG2 1 ATOM 853 N N . ILE A 1 109 ? -19.981 10.126 9.238 1.00 18.67 ? 225 ILE A N 1 ATOM 854 C CA . ILE A 1 109 ? -20.121 8.715 8.926 1.00 16.71 ? 225 ILE A CA 1 ATOM 855 C C . ILE A 1 109 ? -21.550 8.454 8.478 1.00 24.73 ? 225 ILE A C 1 ATOM 856 O O . ILE A 1 109 ? -22.495 8.763 9.200 1.00 27.58 ? 225 ILE A O 1 ATOM 857 C CB . ILE A 1 109 ? -19.801 7.838 10.149 1.00 20.79 ? 225 ILE A CB 1 ATOM 858 C CG1 . ILE A 1 109 ? -18.357 8.076 10.609 1.00 24.22 ? 225 ILE A CG1 1 ATOM 859 C CG2 . ILE A 1 109 ? -20.040 6.362 9.832 1.00 22.41 ? 225 ILE A CG2 1 ATOM 860 C CD1 . ILE A 1 109 ? -17.997 7.360 11.894 1.00 24.37 ? 225 ILE A CD1 1 ATOM 861 N N . LEU A 1 110 ? -21.705 7.914 7.275 1.00 24.09 ? 226 LEU A N 1 ATOM 862 C CA . LEU A 1 110 ? -23.008 7.445 6.820 1.00 22.53 ? 226 LEU A CA 1 ATOM 863 C C . LEU A 1 110 ? -23.210 6.012 7.285 1.00 19.75 ? 226 LEU A C 1 ATOM 864 O O . LEU A 1 110 ? -22.283 5.206 7.247 1.00 21.15 ? 226 LEU A O 1 ATOM 865 C CB . LEU A 1 110 ? -23.121 7.527 5.296 1.00 24.89 ? 226 LEU A CB 1 ATOM 866 C CG . LEU A 1 110 ? -22.988 8.933 4.713 1.00 28.24 ? 226 LEU A CG 1 ATOM 867 C CD1 . LEU A 1 110 ? -23.421 8.950 3.254 1.00 27.89 ? 226 LEU A CD1 1 ATOM 868 C CD2 . LEU A 1 110 ? -23.810 9.923 5.537 1.00 35.54 ? 226 LEU A CD2 1 ATOM 869 N N . LYS A 1 111 ? -24.422 5.702 7.733 1.00 19.82 ? 227 LYS A N 1 ATOM 870 C CA . LYS A 1 111 ? -24.732 4.391 8.291 1.00 18.29 ? 227 LYS A CA 1 ATOM 871 C C . LYS A 1 111 ? -25.890 3.760 7.532 1.00 21.93 ? 227 LYS A C 1 ATOM 872 O O . LYS A 1 111 ? -26.932 4.384 7.348 1.00 22.99 ? 227 LYS A O 1 ATOM 873 C CB . LYS A 1 111 ? -25.108 4.524 9.776 1.00 26.10 ? 227 LYS A CB 1 ATOM 874 C CG . LYS A 1 111 ? -25.487 3.208 10.443 1.00 21.36 ? 227 LYS A CG 1 ATOM 875 C CD . LYS A 1 111 ? -26.001 3.414 11.874 1.00 25.59 ? 227 LYS A CD 1 ATOM 876 C CE . LYS A 1 111 ? -26.329 2.070 12.533 1.00 32.96 ? 227 LYS A CE 1 ATOM 877 N NZ . LYS A 1 111 ? -26.828 2.212 13.940 1.00 32.03 ? 227 LYS A NZ 1 ATOM 878 N N . CYS A 1 112 ? -25.709 2.527 7.083 1.00 23.81 ? 228 CYS A N 1 ATOM 879 C CA . CYS A 1 112 ? -26.782 1.828 6.392 1.00 26.28 ? 228 CYS A CA 1 ATOM 880 C C . CYS A 1 112 ? -27.696 1.157 7.403 1.00 22.46 ? 228 CYS A C 1 ATOM 881 O O . CYS A 1 112 ? -27.250 0.339 8.197 1.00 25.13 ? 228 CYS A O 1 ATOM 882 C CB . CYS A 1 112 ? -26.225 0.783 5.426 1.00 32.54 ? 228 CYS A CB 1 ATOM 883 S SG . CYS A 1 112 ? -27.515 -0.211 4.645 1.00 33.76 ? 228 CYS A SG 1 ATOM 884 N N . ASN A 1 113 ? -28.980 1.501 7.361 1.00 25.35 ? 229 ASN A N 1 ATOM 885 C CA . ASN A 1 113 ? -29.948 0.918 8.276 1.00 26.04 ? 229 ASN A CA 1 ATOM 886 C C . ASN A 1 113 ? -30.865 -0.115 7.623 1.00 30.11 ? 229 ASN A C 1 ATOM 887 O O . ASN A 1 113 ? -31.806 -0.597 8.254 1.00 31.67 ? 229 ASN A O 1 ATOM 888 C CB . ASN A 1 113 ? -30.757 2.015 8.969 1.00 28.39 ? 229 ASN A CB 1 ATOM 889 C CG . ASN A 1 113 ? -29.871 3.003 9.697 1.00 24.91 ? 229 ASN A CG 1 ATOM 890 O OD1 . ASN A 1 113 ? -29.218 2.655 10.676 1.00 29.78 ? 229 ASN A OD1 1 ATOM 891 N ND2 . ASN A 1 113 ? -29.825 4.236 9.209 1.00 29.45 ? 229 ASN A ND2 1 ATOM 892 N N . ASP A 1 114 ? -30.586 -0.457 6.366 1.00 26.52 ? 230 ASP A N 1 ATOM 893 C CA . ASP A 1 114 ? -31.302 -1.551 5.707 1.00 30.42 ? 230 ASP A CA 1 ATOM 894 C C . ASP A 1 114 ? -31.000 -2.860 6.445 1.00 29.26 ? 230 ASP A C 1 ATOM 895 O O . ASP A 1 114 ? -29.853 -3.291 6.507 1.00 28.73 ? 230 ASP A O 1 ATOM 896 C CB . ASP A 1 114 ? -30.903 -1.656 4.229 1.00 31.42 ? 230 ASP A CB 1 ATOM 897 C CG . ASP A 1 114 ? -31.499 -0.545 3.377 1.00 39.60 ? 230 ASP A CG 1 ATOM 898 O OD1 . ASP A 1 114 ? -32.034 0.429 3.942 1.00 34.21 ? 230 ASP A OD1 1 ATOM 899 O OD2 . ASP A 1 114 ? -31.425 -0.643 2.132 1.00 40.81 ? 230 ASP A OD2 1 ATOM 900 N N . LYS A 1 115 ? -32.028 -3.491 7.004 1.00 30.94 ? 231 LYS A N 1 ATOM 901 C CA . LYS A 1 115 ? -31.813 -4.624 7.906 1.00 40.63 ? 231 LYS A CA 1 ATOM 902 C C . LYS A 1 115 ? -31.126 -5.834 7.271 1.00 41.10 ? 231 LYS A C 1 ATOM 903 O O . LYS A 1 115 ? -30.339 -6.518 7.930 1.00 48.69 ? 231 LYS A O 1 ATOM 904 C CB . LYS A 1 115 ? -33.119 -5.039 8.588 1.00 47.78 ? 231 LYS A CB 1 ATOM 905 C CG . LYS A 1 115 ? -33.536 -4.101 9.719 1.00 51.63 ? 231 LYS A CG 1 ATOM 906 C CD . LYS A 1 115 ? -34.781 -4.591 10.442 1.00 56.00 ? 231 LYS A CD 1 ATOM 907 C CE . LYS A 1 115 ? -35.212 -3.601 11.510 1.00 59.12 ? 231 LYS A CE 1 ATOM 908 N NZ . LYS A 1 115 ? -34.107 -3.272 12.444 1.00 58.72 ? 231 LYS A NZ 1 ATOM 909 N N . ASN A 1 116 ? -31.406 -6.092 5.999 1.00 33.84 ? 232 ASN A N 1 ATOM 910 C CA . ASN A 1 116 ? -30.830 -7.257 5.332 1.00 33.33 ? 232 ASN A CA 1 ATOM 911 C C . ASN A 1 116 ? -29.710 -6.904 4.352 1.00 33.37 ? 232 ASN A C 1 ATOM 912 O O . ASN A 1 116 ? -29.389 -7.683 3.456 1.00 30.73 ? 232 ASN A O 1 ATOM 913 C CB . ASN A 1 116 ? -31.930 -8.066 4.641 1.00 39.95 ? 232 ASN A CB 1 ATOM 914 C CG . ASN A 1 116 ? -32.863 -8.746 5.635 1.00 41.61 ? 232 ASN A CG 1 ATOM 915 O OD1 . ASN A 1 116 ? -32.417 -9.313 6.635 1.00 31.60 ? 232 ASN A OD1 1 ATOM 916 N ND2 . ASN A 1 116 ? -34.163 -8.679 5.372 1.00 40.95 ? 232 ASN A ND2 1 ATOM 917 N N . PHE A 1 117 ? -29.108 -5.733 4.544 1.00 29.91 ? 233 PHE A N 1 ATOM 918 C CA . PHE A 1 117 ? -28.006 -5.275 3.696 1.00 31.11 ? 233 PHE A CA 1 ATOM 919 C C . PHE A 1 117 ? -26.828 -6.240 3.772 1.00 24.15 ? 233 PHE A C 1 ATOM 920 O O . PHE A 1 117 ? -26.356 -6.564 4.864 1.00 25.14 ? 233 PHE A O 1 ATOM 921 C CB . PHE A 1 117 ? -27.569 -3.873 4.125 1.00 27.22 ? 233 PHE A CB 1 ATOM 922 C CG . PHE A 1 117 ? -26.404 -3.328 3.345 1.00 29.22 ? 233 PHE A CG 1 ATOM 923 C CD1 . PHE A 1 117 ? -26.465 -3.213 1.966 1.00 38.39 ? 233 PHE A CD1 1 ATOM 924 C CD2 . PHE A 1 117 ? -25.252 -2.914 3.997 1.00 30.38 ? 233 PHE A CD2 1 ATOM 925 C CE1 . PHE A 1 117 ? -25.398 -2.702 1.250 1.00 39.87 ? 233 PHE A CE1 1 ATOM 926 C CE2 . PHE A 1 117 ? -24.184 -2.400 3.286 1.00 27.63 ? 233 PHE A CE2 1 ATOM 927 C CZ . PHE A 1 117 ? -24.257 -2.296 1.911 1.00 32.63 ? 233 PHE A CZ 1 ATOM 928 N N . ASN A 1 118 ? -26.343 -6.691 2.618 1.00 24.18 ? 234 ASN A N 1 ATOM 929 C CA . ASN A 1 118 ? -25.281 -7.699 2.601 1.00 25.46 ? 234 ASN A CA 1 ATOM 930 C C . ASN A 1 118 ? -23.860 -7.135 2.679 1.00 24.98 ? 234 ASN A C 1 ATOM 931 O O . ASN A 1 118 ? -22.888 -7.887 2.787 1.00 25.42 ? 234 ASN A O 1 ATOM 932 C CB . ASN A 1 118 ? -25.437 -8.670 1.420 1.00 27.73 ? 234 ASN A CB 1 ATOM 933 C CG . ASN A 1 118 ? -25.134 -8.035 0.071 1.00 35.75 ? 234 ASN A CG 1 ATOM 934 O OD1 . ASN A 1 118 ? -24.507 -6.977 -0.015 1.00 34.06 ? 234 ASN A OD1 1 ATOM 935 N ND2 . ASN A 1 118 ? -25.580 -8.701 -0.996 1.00 38.34 ? 234 ASN A ND2 1 ATOM 936 N N . GLY A 1 119 ? -23.740 -5.814 2.624 1.00 23.16 ? 235 GLY A N 1 ATOM 937 C CA . GLY A 1 119 ? -22.443 -5.179 2.782 1.00 26.26 ? 235 GLY A CA 1 ATOM 938 C C . GLY A 1 119 ? -21.906 -4.509 1.533 1.00 24.66 ? 235 GLY A C 1 ATOM 939 O O . GLY A 1 119 ? -20.995 -3.686 1.617 1.00 24.28 ? 235 GLY A O 1 ATOM 940 N N . THR A 1 120 ? -22.465 -4.856 0.376 1.00 23.93 ? 236 THR A N 1 ATOM 941 C CA . THR A 1 120 ? -22.064 -4.234 -0.881 1.00 28.71 ? 236 THR A CA 1 ATOM 942 C C . THR A 1 120 ? -23.270 -3.856 -1.737 1.00 30.90 ? 236 THR A C 1 ATOM 943 O O . THR A 1 120 ? -24.124 -4.692 -2.031 1.00 40.54 ? 236 THR A O 1 ATOM 944 C CB . THR A 1 120 ? -21.147 -5.158 -1.705 1.00 33.79 ? 236 THR A CB 1 ATOM 945 O OG1 . THR A 1 120 ? -20.117 -5.687 -0.864 1.00 38.22 ? 236 THR A OG1 1 ATOM 946 C CG2 . THR A 1 120 ? -20.508 -4.387 -2.845 1.00 39.36 ? 236 THR A CG2 1 ATOM 947 N N . GLY A 1 121 ? -23.329 -2.595 -2.146 1.00 27.84 ? 237 GLY A N 1 ATOM 948 C CA . GLY A 1 121 ? -24.414 -2.135 -2.995 1.00 25.95 ? 237 GLY A CA 1 ATOM 949 C C . GLY A 1 121 ? -25.172 -0.987 -2.360 1.00 23.66 ? 237 GLY A C 1 ATOM 950 O O . GLY A 1 121 ? -24.716 -0.421 -1.369 1.00 23.86 ? 237 GLY A O 1 ATOM 951 N N . PRO A 1 122 ? -26.334 -0.638 -2.938 1.00 27.85 ? 238 PRO A N 1 ATOM 952 C CA . PRO A 1 122 ? -27.161 0.487 -2.491 1.00 23.91 ? 238 PRO A CA 1 ATOM 953 C C . PRO A 1 122 ? -27.889 0.222 -1.178 1.00 22.69 ? 238 PRO A C 1 ATOM 954 O O . PRO A 1 122 ? -28.287 -0.905 -0.894 1.00 27.76 ? 238 PRO A O 1 ATOM 955 C CB . PRO A 1 122 ? -28.178 0.647 -3.623 1.00 23.32 ? 238 PRO A CB 1 ATOM 956 C CG . PRO A 1 122 ? -28.252 -0.691 -4.269 1.00 27.14 ? 238 PRO A CG 1 ATOM 957 C CD . PRO A 1 122 ? -26.876 -1.281 -4.148 1.00 28.28 ? 238 PRO A CD 1 ATOM 958 N N . CYS A 1 123 ? -28.045 1.276 -0.387 1.00 26.53 ? 239 CYS A N 1 ATOM 959 C CA . CYS A 1 123 ? -28.782 1.219 0.867 1.00 24.22 ? 239 CYS A CA 1 ATOM 960 C C . CYS A 1 123 ? -29.819 2.330 0.802 1.00 25.11 ? 239 CYS A C 1 ATOM 961 O O . CYS A 1 123 ? -29.494 3.462 0.443 1.00 25.87 ? 239 CYS A O 1 ATOM 962 C CB . CYS A 1 123 ? -27.835 1.439 2.048 1.00 32.94 ? 239 CYS A CB 1 ATOM 963 S SG . CYS A 1 123 ? -28.590 1.255 3.691 1.00 41.43 ? 239 CYS A SG 1 ATOM 964 N N . LYS A 1 124 ? -31.064 2.009 1.135 1.00 28.34 ? 240 LYS A N 1 ATOM 965 C CA . LYS A 1 124 ? -32.167 2.954 0.956 1.00 32.71 ? 240 LYS A CA 1 ATOM 966 C C . LYS A 1 124 ? -32.488 3.759 2.215 1.00 34.10 ? 240 LYS A C 1 ATOM 967 O O . LYS A 1 124 ? -33.054 4.850 2.136 1.00 35.34 ? 240 LYS A O 1 ATOM 968 C CB . LYS A 1 124 ? -33.420 2.217 0.479 1.00 40.54 ? 240 LYS A CB 1 ATOM 969 C CG . LYS A 1 124 ? -33.183 1.298 -0.710 1.00 52.19 ? 240 LYS A CG 1 ATOM 970 C CD . LYS A 1 124 ? -32.761 2.074 -1.949 1.00 59.15 ? 240 LYS A CD 1 ATOM 971 C CE . LYS A 1 124 ? -33.893 2.945 -2.473 1.00 63.49 ? 240 LYS A CE 1 ATOM 972 N NZ . LYS A 1 124 ? -33.553 3.568 -3.783 1.00 63.36 ? 240 LYS A NZ 1 ATOM 973 N N . ASN A 1 125 ? -32.130 3.212 3.370 1.00 25.77 ? 241 ASN A N 1 ATOM 974 C CA . ASN A 1 125 ? -32.383 3.858 4.651 1.00 24.52 ? 241 ASN A CA 1 ATOM 975 C C . ASN A 1 125 ? -31.059 4.249 5.306 1.00 24.18 ? 241 ASN A C 1 ATOM 976 O O . ASN A 1 125 ? -30.467 3.471 6.050 1.00 25.73 ? 241 ASN A O 1 ATOM 977 C CB . ASN A 1 125 ? -33.161 2.912 5.561 1.00 34.57 ? 241 ASN A CB 1 ATOM 978 C CG . ASN A 1 125 ? -33.743 3.608 6.773 1.00 48.61 ? 241 ASN A CG 1 ATOM 979 O OD1 . ASN A 1 125 ? -33.459 4.778 7.031 1.00 48.69 ? 241 ASN A OD1 1 ATOM 980 N ND2 . ASN A 1 125 ? -34.568 2.883 7.527 1.00 65.19 ? 241 ASN A ND2 1 ATOM 981 N N . VAL A 1 126 ? -30.598 5.458 5.013 1.00 25.18 ? 242 VAL A N 1 ATOM 982 C CA . VAL A 1 126 ? -29.270 5.901 5.416 1.00 26.97 ? 242 VAL A CA 1 ATOM 983 C C . VAL A 1 126 ? -29.369 7.012 6.447 1.00 26.94 ? 242 VAL A C 1 ATOM 984 O O . VAL A 1 126 ? -30.216 7.890 6.332 1.00 27.83 ? 242 VAL A O 1 ATOM 985 C CB . VAL A 1 126 ? -28.491 6.471 4.209 1.00 29.86 ? 242 VAL A CB 1 ATOM 986 C CG1 . VAL A 1 126 ? -27.082 6.863 4.627 1.00 25.57 ? 242 VAL A CG1 1 ATOM 987 C CG2 . VAL A 1 126 ? -28.466 5.470 3.060 1.00 31.50 ? 242 VAL A CG2 1 ATOM 988 N N . SER A 1 127 ? -28.503 6.973 7.454 1.00 26.60 ? 243 SER A N 1 ATOM 989 C CA . SER A 1 127 ? -28.426 8.062 8.420 1.00 31.57 ? 243 SER A CA 1 ATOM 990 C C . SER A 1 127 ? -26.988 8.554 8.536 1.00 30.43 ? 243 SER A C 1 ATOM 991 O O . SER A 1 127 ? -26.059 7.885 8.085 1.00 30.44 ? 243 SER A O 1 ATOM 992 C CB . SER A 1 127 ? -28.969 7.630 9.787 1.00 26.75 ? 243 SER A CB 1 ATOM 993 O OG . SER A 1 127 ? -28.206 6.571 10.341 1.00 27.55 ? 243 SER A OG 1 ATOM 994 N N . SER A 1 128 ? -26.805 9.739 9.108 1.00 26.10 ? 244 SER A N 1 ATOM 995 C CA . SER A 1 128 ? -25.460 10.253 9.332 1.00 28.42 ? 244 SER A CA 1 ATOM 996 C C . SER A 1 128 ? -25.193 10.395 10.822 1.00 27.80 ? 244 SER A C 1 ATOM 997 O O . SER A 1 128 ? -26.061 10.822 11.581 1.00 27.77 ? 244 SER A O 1 ATOM 998 C CB . SER A 1 128 ? -25.231 11.584 8.612 1.00 33.38 ? 244 SER A CB 1 ATOM 999 O OG . SER A 1 128 ? -25.976 12.632 9.200 1.00 35.40 ? 244 SER A OG 1 ATOM 1000 N N . VAL A 1 129 ? -23.984 10.023 11.225 1.00 26.21 ? 245 VAL A N 1 ATOM 1001 C CA . VAL A 1 129 ? -23.575 10.039 12.623 1.00 27.71 ? 245 VAL A CA 1 ATOM 1002 C C . VAL A 1 129 ? -22.130 10.513 12.705 1.00 27.21 ? 245 VAL A C 1 ATOM 1003 O O . VAL A 1 129 ? -21.406 10.459 11.711 1.00 25.27 ? 245 VAL A O 1 ATOM 1004 C CB . VAL A 1 129 ? -23.674 8.631 13.247 1.00 24.81 ? 245 VAL A CB 1 ATOM 1005 C CG1 . VAL A 1 129 ? -25.114 8.149 13.245 1.00 28.60 ? 245 VAL A CG1 1 ATOM 1006 C CG2 . VAL A 1 129 ? -22.783 7.640 12.494 1.00 17.96 ? 245 VAL A CG2 1 ATOM 1007 N N . GLN A 1 130 ? -21.706 10.979 13.877 1.00 26.42 ? 246 GLN A N 1 ATOM 1008 C CA . GLN A 1 130 ? -20.305 11.360 14.055 1.00 26.95 ? 246 GLN A CA 1 ATOM 1009 C C . GLN A 1 130 ? -19.437 10.160 14.428 1.00 26.68 ? 246 GLN A C 1 ATOM 1010 O O . GLN A 1 130 ? -18.247 10.130 14.112 1.00 24.11 ? 246 GLN A O 1 ATOM 1011 C CB . GLN A 1 130 ? -20.135 12.462 15.104 1.00 34.13 ? 246 GLN A CB 1 ATOM 1012 C CG . GLN A 1 130 ? -18.678 12.907 15.260 1.00 42.78 ? 246 GLN A CG 1 ATOM 1013 C CD . GLN A 1 130 ? -18.479 13.971 16.326 1.00 57.05 ? 246 GLN A CD 1 ATOM 1014 O OE1 . GLN A 1 130 ? -19.249 14.064 17.281 1.00 62.74 ? 246 GLN A OE1 1 ATOM 1015 N NE2 . GLN A 1 130 ? -17.438 14.781 16.165 1.00 59.44 ? 246 GLN A NE2 1 ATOM 1016 N N . CYS A 1 131 ? -20.042 9.175 15.091 1.00 19.81 ? 247 CYS A N 1 ATOM 1017 C CA . CYS A 1 131 ? -19.317 8.018 15.599 1.00 19.92 ? 247 CYS A CA 1 ATOM 1018 C C . CYS A 1 131 ? -20.052 6.712 15.316 1.00 22.68 ? 247 CYS A C 1 ATOM 1019 O O . CYS A 1 131 ? -21.282 6.686 15.225 1.00 24.89 ? 247 CYS A O 1 ATOM 1020 C CB . CYS A 1 131 ? -19.104 8.145 17.113 1.00 23.86 ? 247 CYS A CB 1 ATOM 1021 S SG . CYS A 1 131 ? -18.042 9.521 17.637 1.00 38.85 ? 247 CYS A SG 1 ATOM 1022 N N . THR A 1 132 ? -19.293 5.629 15.201 1.00 21.95 ? 248 THR A N 1 ATOM 1023 C CA . THR A 1 132 ? -19.877 4.296 15.105 1.00 22.04 ? 248 THR A CA 1 ATOM 1024 C C . THR A 1 132 ? -20.417 3.899 16.469 1.00 24.96 ? 248 THR A C 1 ATOM 1025 O O . THR A 1 132 ? -20.194 4.599 17.461 1.00 24.72 ? 248 THR A O 1 ATOM 1026 C CB . THR A 1 132 ? -18.828 3.236 14.696 1.00 18.94 ? 248 THR A CB 1 ATOM 1027 O OG1 . THR A 1 132 ? -17.842 3.108 15.732 1.00 19.97 ? 248 THR A OG1 1 ATOM 1028 C CG2 . THR A 1 132 ? -18.140 3.624 13.391 1.00 19.64 ? 248 THR A CG2 1 ATOM 1029 N N . HIS A 1 133 ? -21.121 2.772 16.520 1.00 25.01 ? 249 HIS A N 1 ATOM 1030 C CA . HIS A 1 133 ? -21.463 2.165 17.795 1.00 24.85 ? 249 HIS A CA 1 ATOM 1031 C C . HIS A 1 133 ? -20.165 1.742 18.470 1.00 22.77 ? 249 HIS A C 1 ATOM 1032 O O . HIS A 1 133 ? -19.100 1.792 17.852 1.00 20.05 ? 249 HIS A O 1 ATOM 1033 C CB . HIS A 1 133 ? -22.421 0.976 17.614 1.00 24.68 ? 249 HIS A CB 1 ATOM 1034 C CG . HIS A 1 133 ? -21.816 -0.211 16.936 1.00 27.32 ? 249 HIS A CG 1 ATOM 1035 N ND1 . HIS A 1 133 ? -21.716 -0.320 15.556 1.00 25.16 ? 249 HIS A ND1 1 ATOM 1036 C CD2 . HIS A 1 133 ? -21.305 -1.364 17.428 1.00 24.05 ? 249 HIS A CD2 1 ATOM 1037 C CE1 . HIS A 1 133 ? -21.160 -1.467 15.244 1.00 29.41 ? 249 HIS A CE1 1 ATOM 1038 N NE2 . HIS A 1 133 ? -20.900 -2.129 16.366 1.00 29.32 ? 249 HIS A NE2 1 ATOM 1039 N N . GLY A 1 134 ? -20.243 1.366 19.744 1.00 20.01 ? 250 GLY A N 1 ATOM 1040 C CA . GLY A 1 134 ? -19.074 0.899 20.470 1.00 23.01 ? 250 GLY A CA 1 ATOM 1041 C C . GLY A 1 134 ? -18.700 -0.511 20.054 1.00 20.32 ? 250 GLY A C 1 ATOM 1042 O O . GLY A 1 134 ? -19.440 -1.456 20.316 1.00 22.34 ? 250 GLY A O 1 ATOM 1043 N N . ILE A 1 135 ? -17.553 -0.655 19.397 1.00 16.16 ? 251 ILE A N 1 ATOM 1044 C CA . ILE A 1 135 ? -17.105 -1.955 18.917 1.00 17.44 ? 251 ILE A CA 1 ATOM 1045 C C . ILE A 1 135 ? -16.010 -2.536 19.816 1.00 18.38 ? 251 ILE A C 1 ATOM 1046 O O . ILE A 1 135 ? -14.954 -1.929 19.993 1.00 18.52 ? 251 ILE A O 1 ATOM 1047 C CB . ILE A 1 135 ? -16.565 -1.849 17.482 1.00 18.60 ? 251 ILE A CB 1 ATOM 1048 C CG1 . ILE A 1 135 ? -17.627 -1.233 16.565 1.00 22.68 ? 251 ILE A CG1 1 ATOM 1049 C CG2 . ILE A 1 135 ? -16.148 -3.218 16.973 1.00 21.28 ? 251 ILE A CG2 1 ATOM 1050 C CD1 . ILE A 1 135 ? -17.103 -0.809 15.204 1.00 25.83 ? 251 ILE A CD1 1 ATOM 1051 N N . LYS A 1 136 ? -16.258 -3.711 20.386 1.00 21.69 ? 252 LYS A N 1 ATOM 1052 C CA . LYS A 1 136 ? -15.229 -4.384 21.175 1.00 18.23 ? 252 LYS A CA 1 ATOM 1053 C C . LYS A 1 136 ? -14.235 -5.061 20.239 1.00 16.46 ? 252 LYS A C 1 ATOM 1054 O O . LYS A 1 136 ? -14.633 -5.783 19.329 1.00 19.43 ? 252 LYS A O 1 ATOM 1055 C CB . LYS A 1 136 ? -15.852 -5.412 22.119 1.00 19.64 ? 252 LYS A CB 1 ATOM 1056 C CG . LYS A 1 136 ? -16.735 -4.788 23.200 1.00 21.41 ? 252 LYS A CG 1 ATOM 1057 C CD . LYS A 1 136 ? -17.269 -5.855 24.137 1.00 27.43 ? 252 LYS A CD 1 ATOM 1058 C CE . LYS A 1 136 ? -18.305 -5.282 25.081 1.00 45.03 ? 252 LYS A CE 1 ATOM 1059 N NZ . LYS A 1 136 ? -19.600 -5.001 24.394 1.00 56.17 ? 252 LYS A NZ 1 ATOM 1060 N N . PRO A 1 137 ? -12.934 -4.832 20.460 1.00 15.34 ? 253 PRO A N 1 ATOM 1061 C CA . PRO A 1 137 ? -11.918 -5.394 19.560 1.00 15.82 ? 253 PRO A CA 1 ATOM 1062 C C . PRO A 1 137 ? -11.583 -6.838 19.913 1.00 19.31 ? 253 PRO A C 1 ATOM 1063 O O . PRO A 1 137 ? -10.458 -7.143 20.301 1.00 19.45 ? 253 PRO A O 1 ATOM 1064 C CB . PRO A 1 137 ? -10.712 -4.494 19.806 1.00 20.69 ? 253 PRO A CB 1 ATOM 1065 C CG . PRO A 1 137 ? -10.859 -4.097 21.258 1.00 21.12 ? 253 PRO A CG 1 ATOM 1066 C CD . PRO A 1 137 ? -12.346 -3.935 21.472 1.00 14.56 ? 253 PRO A CD 1 ATOM 1067 N N . VAL A 1 138 ? -12.560 -7.722 19.758 1.00 17.07 ? 254 VAL A N 1 ATOM 1068 C CA . VAL A 1 138 ? -12.384 -9.118 20.114 1.00 17.11 ? 254 VAL A CA 1 ATOM 1069 C C . VAL A 1 138 ? -11.653 -9.854 19.006 1.00 17.78 ? 254 VAL A C 1 ATOM 1070 O O . VAL A 1 138 ? -12.139 -9.943 17.878 1.00 20.87 ? 254 VAL A O 1 ATOM 1071 C CB . VAL A 1 138 ? -13.733 -9.811 20.378 1.00 17.88 ? 254 VAL A CB 1 ATOM 1072 C CG1 . VAL A 1 138 ? -13.502 -11.191 20.982 1.00 22.03 ? 254 VAL A CG1 1 ATOM 1073 C CG2 . VAL A 1 138 ? -14.612 -8.948 21.302 1.00 18.51 ? 254 VAL A CG2 1 ATOM 1074 N N . VAL A 1 139 ? -10.478 -10.373 19.338 1.00 16.94 ? 255 VAL A N 1 ATOM 1075 C CA . VAL A 1 139 ? -9.679 -11.142 18.398 1.00 16.51 ? 255 VAL A CA 1 ATOM 1076 C C . VAL A 1 139 ? -10.006 -12.623 18.546 1.00 16.54 ? 255 VAL A C 1 ATOM 1077 O O . VAL A 1 139 ? -9.868 -13.196 19.628 1.00 18.20 ? 255 VAL A O 1 ATOM 1078 C CB . VAL A 1 139 ? -8.175 -10.922 18.641 1.00 21.83 ? 255 VAL A CB 1 ATOM 1079 C CG1 . VAL A 1 139 ? -7.345 -11.768 17.679 1.00 19.49 ? 255 VAL A CG1 1 ATOM 1080 C CG2 . VAL A 1 139 ? -7.830 -9.458 18.490 1.00 23.72 ? 255 VAL A CG2 1 ATOM 1081 N N . SER A 1 140 ? -10.450 -13.242 17.458 1.00 15.45 ? 256 SER A N 1 ATOM 1082 C CA . SER A 1 140 ? -10.747 -14.670 17.473 1.00 18.54 ? 256 SER A CA 1 ATOM 1083 C C . SER A 1 140 ? -10.690 -15.239 16.067 1.00 18.64 ? 256 SER A C 1 ATOM 1084 O O . SER A 1 140 ? -10.681 -14.493 15.083 1.00 18.48 ? 256 SER A O 1 ATOM 1085 C CB . SER A 1 140 ? -12.144 -14.913 18.039 1.00 22.08 ? 256 SER A CB 1 ATOM 1086 O OG . SER A 1 140 ? -13.130 -14.449 17.125 1.00 23.55 ? 256 SER A OG 1 ATOM 1087 N N . THR A 1 141 ? -10.650 -16.565 15.978 1.00 15.78 ? 257 THR A N 1 ATOM 1088 C CA . THR A 1 141 ? -10.837 -17.248 14.701 1.00 19.19 ? 257 THR A CA 1 ATOM 1089 C C . THR A 1 141 ? -12.060 -18.166 14.756 1.00 21.75 ? 257 THR A C 1 ATOM 1090 O O . THR A 1 141 ? -12.535 -18.511 15.839 1.00 22.01 ? 257 THR A O 1 ATOM 1091 C CB . THR A 1 141 ? -9.614 -18.089 14.317 1.00 21.39 ? 257 THR A CB 1 ATOM 1092 O OG1 . THR A 1 141 ? -9.489 -19.183 15.232 1.00 19.90 ? 257 THR A OG1 1 ATOM 1093 C CG2 . THR A 1 141 ? -8.351 -17.244 14.353 1.00 20.30 ? 257 THR A CG2 1 ATOM 1094 N N . GLN A 1 142 ? -12.560 -18.536 13.577 1.00 17.07 ? 258 GLN A N 1 ATOM 1095 C CA . GLN A 1 142 ? -13.688 -19.459 13.420 1.00 21.06 ? 258 GLN A CA 1 ATOM 1096 C C . GLN A 1 142 ? -15.026 -18.880 13.859 1.00 21.45 ? 258 GLN A C 1 ATOM 1097 O O . GLN A 1 142 ? -15.971 -18.820 13.072 1.00 21.19 ? 258 GLN A O 1 ATOM 1098 C CB . GLN A 1 142 ? -13.428 -20.798 14.126 1.00 19.63 ? 258 GLN A CB 1 ATOM 1099 C CG . GLN A 1 142 ? -12.216 -21.546 13.593 1.00 24.22 ? 258 GLN A CG 1 ATOM 1100 C CD . GLN A 1 142 ? -12.250 -23.023 13.927 1.00 22.69 ? 258 GLN A CD 1 ATOM 1101 O OE1 . GLN A 1 142 ? -13.196 -23.511 14.544 1.00 22.78 ? 258 GLN A OE1 1 ATOM 1102 N NE2 . GLN A 1 142 ? -11.218 -23.747 13.508 1.00 23.55 ? 258 GLN A NE2 1 ATOM 1103 N N . LEU A 1 143 ? -15.105 -18.476 15.120 1.00 20.27 ? 259 LEU A N 1 ATOM 1104 C CA . LEU A 1 143 ? -16.330 -17.928 15.680 1.00 18.43 ? 259 LEU A CA 1 ATOM 1105 C C . LEU A 1 143 ? -16.135 -16.466 16.062 1.00 21.35 ? 259 LEU A C 1 ATOM 1106 O O . LEU A 1 143 ? -15.148 -16.116 16.704 1.00 24.25 ? 259 LEU A O 1 ATOM 1107 C CB . LEU A 1 143 ? -16.739 -18.728 16.921 1.00 21.63 ? 259 LEU A CB 1 ATOM 1108 C CG . LEU A 1 143 ? -16.945 -20.224 16.703 1.00 24.75 ? 259 LEU A CG 1 ATOM 1109 C CD1 . LEU A 1 143 ? -17.212 -20.930 18.031 1.00 24.95 ? 259 LEU A CD1 1 ATOM 1110 C CD2 . LEU A 1 143 ? -18.087 -20.461 15.716 1.00 25.53 ? 259 LEU A CD2 1 ATOM 1111 N N . LEU A 1 144 ? -17.074 -15.616 15.661 1.00 18.45 ? 260 LEU A N 1 ATOM 1112 C CA . LEU A 1 144 ? -17.059 -14.219 16.073 1.00 19.11 ? 260 LEU A CA 1 ATOM 1113 C C . LEU A 1 144 ? -17.775 -14.085 17.411 1.00 20.89 ? 260 LEU A C 1 ATOM 1114 O O . LEU A 1 144 ? -18.904 -14.547 17.564 1.00 21.09 ? 260 LEU A O 1 ATOM 1115 C CB . LEU A 1 144 ? -17.725 -13.336 15.016 1.00 17.10 ? 260 LEU A CB 1 ATOM 1116 C CG . LEU A 1 144 ? -17.054 -13.358 13.643 1.00 15.13 ? 260 LEU A CG 1 ATOM 1117 C CD1 . LEU A 1 144 ? -17.808 -12.451 12.680 1.00 17.50 ? 260 LEU A CD1 1 ATOM 1118 C CD2 . LEU A 1 144 ? -15.592 -12.926 13.752 1.00 22.83 ? 260 LEU A CD2 1 ATOM 1119 N N . LEU A 1 145 ? -17.117 -13.452 18.376 1.00 19.49 ? 261 LEU A N 1 ATOM 1120 C CA . LEU A 1 145 ? -17.625 -13.413 19.743 1.00 22.02 ? 261 LEU A CA 1 ATOM 1121 C C . LEU A 1 145 ? -17.982 -12.002 20.193 1.00 21.87 ? 261 LEU A C 1 ATOM 1122 O O . LEU A 1 145 ? -17.278 -11.043 19.880 1.00 20.77 ? 261 LEU A O 1 ATOM 1123 C CB . LEU A 1 145 ? -16.595 -14.001 20.708 1.00 18.45 ? 261 LEU A CB 1 ATOM 1124 C CG . LEU A 1 145 ? -16.092 -15.404 20.359 1.00 22.22 ? 261 LEU A CG 1 ATOM 1125 C CD1 . LEU A 1 145 ? -14.968 -15.824 21.304 1.00 21.80 ? 261 LEU A CD1 1 ATOM 1126 C CD2 . LEU A 1 145 ? -17.236 -16.400 20.390 1.00 19.37 ? 261 LEU A CD2 1 ATOM 1127 N N . ASN A 1 146 ? -19.080 -11.894 20.935 1.00 19.63 ? 262 ASN A N 1 ATOM 1128 C CA . ASN A 1 146 ? -19.484 -10.640 21.562 1.00 21.29 ? 262 ASN A CA 1 ATOM 1129 C C . ASN A 1 146 ? -19.695 -9.496 20.577 1.00 23.76 ? 262 ASN A C 1 ATOM 1130 O O . ASN A 1 146 ? -19.534 -8.332 20.937 1.00 22.29 ? 262 ASN A O 1 ATOM 1131 C CB . ASN A 1 146 ? -18.462 -10.203 22.616 1.00 22.66 ? 262 ASN A CB 1 ATOM 1132 C CG . ASN A 1 146 ? -18.469 -11.086 23.856 1.00 22.82 ? 262 ASN A CG 1 ATOM 1133 O OD1 . ASN A 1 146 ? -19.348 -11.936 24.031 1.00 20.04 ? 262 ASN A OD1 1 ATOM 1134 N ND2 . ASN A 1 146 ? -17.471 -10.877 24.727 1.00 21.91 ? 262 ASN A ND2 1 ATOM 1135 N N . GLY A 1 147 ? -20.046 -9.824 19.339 1.00 24.04 ? 263 GLY A N 1 ATOM 1136 C CA . GLY A 1 147 ? -20.310 -8.802 18.343 1.00 17.94 ? 263 GLY A CA 1 ATOM 1137 C C . GLY A 1 147 ? -21.768 -8.380 18.327 1.00 23.27 ? 263 GLY A C 1 ATOM 1138 O O . GLY A 1 147 ? -22.541 -8.732 19.224 1.00 22.67 ? 263 GLY A O 1 ATOM 1139 N N . SER A 1 148 ? -22.146 -7.619 17.305 1.00 21.72 ? 264 SER A N 1 ATOM 1140 C CA . SER A 1 148 ? -23.535 -7.213 17.121 1.00 25.64 ? 264 SER A CA 1 ATOM 1141 C C . SER A 1 148 ? -24.260 -8.232 16.255 1.00 27.60 ? 264 SER A C 1 ATOM 1142 O O . SER A 1 148 ? -23.664 -8.832 15.365 1.00 29.91 ? 264 SER A O 1 ATOM 1143 C CB . SER A 1 148 ? -23.595 -5.839 16.457 1.00 33.96 ? 264 SER A CB 1 ATOM 1144 O OG . SER A 1 148 ? -22.756 -4.924 17.135 1.00 36.74 ? 264 SER A OG 1 ATOM 1145 N N . LEU A 1 149 ? -25.546 -8.431 16.514 1.00 25.01 ? 265 LEU A N 1 ATOM 1146 C CA . LEU A 1 149 ? -26.324 -9.412 15.759 1.00 26.23 ? 265 LEU A CA 1 ATOM 1147 C C . LEU A 1 149 ? -27.045 -8.778 14.577 1.00 30.43 ? 265 LEU A C 1 ATOM 1148 O O . LEU A 1 149 ? -27.364 -7.588 14.598 1.00 28.10 ? 265 LEU A O 1 ATOM 1149 C CB . LEU A 1 149 ? -27.350 -10.091 16.668 1.00 31.19 ? 265 LEU A CB 1 ATOM 1150 C CG . LEU A 1 149 ? -26.824 -11.027 17.754 1.00 29.22 ? 265 LEU A CG 1 ATOM 1151 C CD1 . LEU A 1 149 ? -27.911 -11.311 18.776 1.00 36.17 ? 265 LEU A CD1 1 ATOM 1152 C CD2 . LEU A 1 149 ? -26.295 -12.320 17.150 1.00 26.92 ? 265 LEU A CD2 1 ATOM 1153 N N . ALA A 1 150 ? -27.324 -9.583 13.558 1.00 29.25 ? 266 ALA A N 1 ATOM 1154 C CA . ALA A 1 150 ? -28.156 -9.142 12.450 1.00 32.41 ? 266 ALA A CA 1 ATOM 1155 C C . ALA A 1 150 ? -29.560 -8.899 12.987 1.00 31.78 ? 266 ALA A C 1 ATOM 1156 O O . ALA A 1 150 ? -30.039 -9.642 13.840 1.00 32.61 ? 266 ALA A O 1 ATOM 1157 C CB . ALA A 1 150 ? -28.175 -10.183 11.346 1.00 29.85 ? 266 ALA A CB 1 ATOM 1158 N N . GLU A 1 151 ? -30.211 -7.852 12.497 1.00 31.19 ? 267 GLU A N 1 ATOM 1159 C CA . GLU A 1 151 ? -31.496 -7.430 13.045 1.00 35.69 ? 267 GLU A CA 1 ATOM 1160 C C . GLU A 1 151 ? -32.690 -8.204 12.492 1.00 35.35 ? 267 GLU A C 1 ATOM 1161 O O . GLU A 1 151 ? -33.753 -8.227 13.105 1.00 35.48 ? 267 GLU A O 1 ATOM 1162 C CB . GLU A 1 151 ? -31.696 -5.928 12.838 1.00 38.99 ? 267 GLU A CB 1 ATOM 1163 C CG . GLU A 1 151 ? -30.879 -5.068 13.788 1.00 49.07 ? 267 GLU A CG 1 ATOM 1164 C CD . GLU A 1 151 ? -31.134 -3.586 13.605 1.00 60.35 ? 267 GLU A CD 1 ATOM 1165 O OE1 . GLU A 1 151 ? -32.134 -3.224 12.950 1.00 64.77 ? 267 GLU A OE1 1 ATOM 1166 O OE2 . GLU A 1 151 ? -30.333 -2.781 14.120 1.00 63.17 ? 267 GLU A OE2 1 ATOM 1167 N N . GLU A 1 152 ? -32.514 -8.834 11.336 1.00 33.56 ? 268 GLU A N 1 ATOM 1168 C CA . GLU A 1 152 ? -33.592 -9.607 10.732 1.00 36.00 ? 268 GLU A CA 1 ATOM 1169 C C . GLU A 1 152 ? -33.161 -11.037 10.417 1.00 34.23 ? 268 GLU A C 1 ATOM 1170 O O . GLU A 1 152 ? -33.111 -11.887 11.301 1.00 32.65 ? 268 GLU A O 1 ATOM 1171 C CB . GLU A 1 152 ? -34.118 -8.914 9.474 1.00 42.77 ? 268 GLU A CB 1 ATOM 1172 C CG . GLU A 1 152 ? -35.594 -9.156 9.215 1.00 52.05 ? 268 GLU A CG 1 ATOM 1173 C CD . GLU A 1 152 ? -36.182 -8.180 8.218 1.00 61.19 ? 268 GLU A CD 1 ATOM 1174 O OE1 . GLU A 1 152 ? -36.444 -8.588 7.069 1.00 64.93 ? 268 GLU A OE1 1 ATOM 1175 O OE2 . GLU A 1 152 ? -36.387 -7.006 8.585 1.00 65.55 ? 268 GLU A OE2 1 ATOM 1176 N N . GLU A 1 153 ? -32.850 -11.298 9.154 1.00 31.60 ? 269 GLU A N 1 ATOM 1177 C CA . GLU A 1 153 ? -32.430 -12.628 8.738 1.00 34.37 ? 269 GLU A CA 1 ATOM 1178 C C . GLU A 1 153 ? -30.923 -12.803 8.873 1.00 26.05 ? 269 GLU A C 1 ATOM 1179 O O . GLU A 1 153 ? -30.177 -11.829 8.891 1.00 27.58 ? 269 GLU A O 1 ATOM 1180 C CB . GLU A 1 153 ? -32.853 -12.892 7.292 1.00 37.52 ? 269 GLU A CB 1 ATOM 1181 C CG . GLU A 1 153 ? -34.340 -12.708 7.034 1.00 48.89 ? 269 GLU A CG 1 ATOM 1182 C CD . GLU A 1 153 ? -34.873 -13.652 5.975 1.00 61.97 ? 269 GLU A CD 1 ATOM 1183 O OE1 . GLU A 1 153 ? -34.128 -14.556 5.548 1.00 62.17 ? 269 GLU A OE1 1 ATOM 1184 O OE2 . GLU A 1 153 ? -36.041 -13.488 5.567 1.00 70.34 ? 269 GLU A OE2 1 ATOM 1185 N N . ILE A 1 154 ? -30.483 -14.052 8.966 1.00 25.74 ? 270 ILE A N 1 ATOM 1186 C CA . ILE A 1 154 ? -29.062 -14.359 8.921 1.00 24.41 ? 270 ILE A CA 1 ATOM 1187 C C . ILE A 1 154 ? -28.515 -13.853 7.596 1.00 24.83 ? 270 ILE A C 1 ATOM 1188 O O . ILE A 1 154 ? -29.166 -13.987 6.558 1.00 27.64 ? 270 ILE A O 1 ATOM 1189 C CB . ILE A 1 154 ? -28.800 -15.870 9.052 1.00 23.54 ? 270 ILE A CB 1 ATOM 1190 C CG1 . ILE A 1 154 ? -29.170 -16.349 10.455 1.00 30.12 ? 270 ILE A CG1 1 ATOM 1191 C CG2 . ILE A 1 154 ? -27.338 -16.186 8.771 1.00 20.71 ? 270 ILE A CG2 1 ATOM 1192 C CD1 . ILE A 1 154 ? -29.213 -17.850 10.591 1.00 30.98 ? 270 ILE A CD1 1 ATOM 1193 N N . ILE A 1 155 ? -27.334 -13.248 7.632 1.00 24.99 ? 271 ILE A N 1 ATOM 1194 C CA . ILE A 1 155 ? -26.758 -12.669 6.427 1.00 26.39 ? 271 ILE A CA 1 ATOM 1195 C C . ILE A 1 155 ? -25.429 -13.323 6.066 1.00 26.38 ? 271 ILE A C 1 ATOM 1196 O O . ILE A 1 155 ? -24.549 -13.475 6.913 1.00 24.15 ? 271 ILE A O 1 ATOM 1197 C CB . ILE A 1 155 ? -26.537 -11.147 6.578 1.00 26.97 ? 271 ILE A CB 1 ATOM 1198 C CG1 . ILE A 1 155 ? -27.808 -10.457 7.085 1.00 27.73 ? 271 ILE A CG1 1 ATOM 1199 C CG2 . ILE A 1 155 ? -26.072 -10.539 5.256 1.00 26.74 ? 271 ILE A CG2 1 ATOM 1200 C CD1 . ILE A 1 155 ? -28.958 -10.475 6.102 1.00 29.13 ? 271 ILE A CD1 1 ATOM 1201 N N . ILE A 1 156 ? -25.292 -13.700 4.800 1.00 22.60 ? 272 ILE A N 1 ATOM 1202 C CA . ILE A 1 156 ? -24.035 -14.218 4.277 1.00 22.09 ? 272 ILE A CA 1 ATOM 1203 C C . ILE A 1 156 ? -23.262 -13.097 3.592 1.00 25.48 ? 272 ILE A C 1 ATOM 1204 O O . ILE A 1 156 ? -23.770 -12.467 2.661 1.00 28.02 ? 272 ILE A O 1 ATOM 1205 C CB . ILE A 1 156 ? -24.287 -15.343 3.257 1.00 26.85 ? 272 ILE A CB 1 ATOM 1206 C CG1 . ILE A 1 156 ? -25.249 -16.384 3.833 1.00 29.28 ? 272 ILE A CG1 1 ATOM 1207 C CG2 . ILE A 1 156 ? -22.971 -15.988 2.827 1.00 25.13 ? 272 ILE A CG2 1 ATOM 1208 C CD1 . ILE A 1 156 ? -24.780 -17.001 5.130 1.00 26.32 ? 272 ILE A CD1 1 ATOM 1209 N N . ARG A 1 157 ? -22.037 -12.842 4.050 1.00 19.44 ? 273 ARG A N 1 ATOM 1210 C CA . ARG A 1 157 ? -21.222 -11.772 3.481 1.00 19.66 ? 273 ARG A CA 1 ATOM 1211 C C . ARG A 1 157 ? -19.954 -12.349 2.874 1.00 24.03 ? 273 ARG A C 1 ATOM 1212 O O . ARG A 1 157 ? -19.286 -13.169 3.497 1.00 20.17 ? 273 ARG A O 1 ATOM 1213 C CB . ARG A 1 157 ? -20.829 -10.751 4.557 1.00 21.27 ? 273 ARG A CB 1 ATOM 1214 C CG . ARG A 1 157 ? -21.993 -10.230 5.384 1.00 22.05 ? 273 ARG A CG 1 ATOM 1215 C CD . ARG A 1 157 ? -21.555 -9.174 6.396 1.00 26.00 ? 273 ARG A CD 1 ATOM 1216 N NE . ARG A 1 157 ? -22.643 -8.846 7.316 1.00 24.61 ? 273 ARG A NE 1 ATOM 1217 C CZ . ARG A 1 157 ? -23.718 -8.139 6.986 1.00 26.95 ? 273 ARG A CZ 1 ATOM 1218 N NH1 . ARG A 1 157 ? -23.852 -7.663 5.750 1.00 23.82 ? 273 ARG A NH1 1 ATOM 1219 N NH2 . ARG A 1 157 ? -24.660 -7.904 7.894 1.00 23.27 ? 273 ARG A NH2 1 ATOM 1220 N N . SER A 1 158 ? -19.625 -11.912 1.663 1.00 21.83 ? 274 SER A N 1 ATOM 1221 C CA . SER A 1 158 ? -18.380 -12.309 1.012 1.00 20.54 ? 274 SER A CA 1 ATOM 1222 C C . SER A 1 158 ? -17.968 -11.283 -0.039 1.00 25.65 ? 274 SER A C 1 ATOM 1223 O O . SER A 1 158 ? -18.817 -10.711 -0.717 1.00 24.04 ? 274 SER A O 1 ATOM 1224 C CB . SER A 1 158 ? -18.527 -13.683 0.357 1.00 22.66 ? 274 SER A CB 1 ATOM 1225 O OG . SER A 1 158 ? -17.359 -14.006 -0.377 1.00 23.52 ? 274 SER A OG 1 ATOM 1226 N N . GLU A 1 159 ? -16.665 -11.054 -0.177 1.00 21.65 ? 275 GLU A N 1 ATOM 1227 C CA . GLU A 1 159 ? -16.173 -10.155 -1.219 1.00 26.00 ? 275 GLU A CA 1 ATOM 1228 C C . GLU A 1 159 ? -16.581 -10.694 -2.593 1.00 25.29 ? 275 GLU A C 1 ATOM 1229 O O . GLU A 1 159 ? -16.812 -9.935 -3.538 1.00 27.03 ? 275 GLU A O 1 ATOM 1230 C CB . GLU A 1 159 ? -14.652 -9.997 -1.122 1.00 28.23 ? 275 GLU A CB 1 ATOM 1231 C CG . GLU A 1 159 ? -14.068 -9.007 -2.120 1.00 33.89 ? 275 GLU A CG 1 ATOM 1232 C CD . GLU A 1 159 ? -12.598 -8.716 -1.868 1.00 44.41 ? 275 GLU A CD 1 ATOM 1233 O OE1 . GLU A 1 159 ? -12.051 -9.207 -0.858 1.00 40.76 ? 275 GLU A OE1 1 ATOM 1234 O OE2 . GLU A 1 159 ? -11.987 -7.991 -2.682 1.00 54.05 ? 275 GLU A OE2 1 ATOM 1235 N N . ASN A 1 160 ? -16.672 -12.015 -2.680 1.00 23.84 ? 276 ASN A N 1 ATOM 1236 C CA . ASN A 1 160 ? -17.086 -12.697 -3.898 1.00 27.10 ? 276 ASN A CA 1 ATOM 1237 C C . ASN A 1 160 ? -17.440 -14.151 -3.598 1.00 22.77 ? 276 ASN A C 1 ATOM 1238 O O . ASN A 1 160 ? -16.574 -15.019 -3.578 1.00 26.12 ? 276 ASN A O 1 ATOM 1239 C CB . ASN A 1 160 ? -15.990 -12.618 -4.960 1.00 28.95 ? 276 ASN A CB 1 ATOM 1240 C CG . ASN A 1 160 ? -16.392 -13.279 -6.263 1.00 27.84 ? 276 ASN A CG 1 ATOM 1241 O OD1 . ASN A 1 160 ? -17.474 -13.848 -6.372 1.00 24.84 ? 276 ASN A OD1 1 ATOM 1242 N ND2 . ASN A 1 160 ? -15.520 -13.205 -7.260 1.00 29.96 ? 276 ASN A ND2 1 ATOM 1243 N N . LEU A 1 161 ? -18.721 -14.399 -3.351 1.00 24.09 ? 277 LEU A N 1 ATOM 1244 C CA . LEU A 1 161 ? -19.205 -15.721 -2.969 1.00 29.66 ? 277 LEU A CA 1 ATOM 1245 C C . LEU A 1 161 ? -18.791 -16.818 -3.949 1.00 29.73 ? 277 LEU A C 1 ATOM 1246 O O . LEU A 1 161 ? -18.549 -17.953 -3.551 1.00 30.27 ? 277 LEU A O 1 ATOM 1247 C CB . LEU A 1 161 ? -20.727 -15.702 -2.823 1.00 35.23 ? 277 LEU A CB 1 ATOM 1248 C CG . LEU A 1 161 ? -21.352 -16.697 -1.846 1.00 38.18 ? 277 LEU A CG 1 ATOM 1249 C CD1 . LEU A 1 161 ? -20.505 -16.839 -0.593 1.00 32.83 ? 277 LEU A CD1 1 ATOM 1250 C CD2 . LEU A 1 161 ? -22.773 -16.284 -1.494 1.00 32.23 ? 277 LEU A CD2 1 ATOM 1251 N N . THR A 1 162 ? -18.716 -16.473 -5.229 1.00 29.98 ? 278 THR A N 1 ATOM 1252 C CA . THR A 1 162 ? -18.371 -17.440 -6.264 1.00 28.34 ? 278 THR A CA 1 ATOM 1253 C C . THR A 1 162 ? -16.919 -17.888 -6.159 1.00 27.59 ? 278 THR A C 1 ATOM 1254 O O . THR A 1 162 ? -16.564 -18.981 -6.593 1.00 28.54 ? 278 THR A O 1 ATOM 1255 C CB . THR A 1 162 ? -18.618 -16.868 -7.670 1.00 31.67 ? 278 THR A CB 1 ATOM 1256 O OG1 . THR A 1 162 ? -19.927 -16.292 -7.729 1.00 32.75 ? 278 THR A OG1 1 ATOM 1257 C CG2 . THR A 1 162 ? -18.504 -17.962 -8.714 1.00 34.08 ? 278 THR A CG2 1 ATOM 1258 N N . ASN A 1 163 ? -16.087 -17.030 -5.584 1.00 23.16 ? 279 ASN A N 1 ATOM 1259 C CA . ASN A 1 163 ? -14.667 -17.310 -5.418 1.00 28.43 ? 279 ASN A CA 1 ATOM 1260 C C . ASN A 1 163 ? -14.424 -18.018 -4.090 1.00 27.97 ? 279 ASN A C 1 ATOM 1261 O O . ASN A 1 163 ? -14.470 -17.395 -3.037 1.00 27.86 ? 279 ASN A O 1 ATOM 1262 C CB . ASN A 1 163 ? -13.875 -15.999 -5.478 1.00 27.09 ? 279 ASN A CB 1 ATOM 1263 C CG . ASN A 1 163 ? -12.372 -16.206 -5.350 1.00 29.37 ? 279 ASN A CG 1 ATOM 1264 O OD1 . ASN A 1 163 ? -11.900 -17.306 -5.065 1.00 31.36 ? 279 ASN A OD1 1 ATOM 1265 N ND2 . ASN A 1 163 ? -11.615 -15.133 -5.549 1.00 29.75 ? 279 ASN A ND2 1 ATOM 1266 N N . ASN A 1 164 ? -14.168 -19.320 -4.147 1.00 26.12 ? 280 ASN A N 1 ATOM 1267 C CA . ASN A 1 164 ? -13.985 -20.128 -2.942 1.00 27.11 ? 280 ASN A CA 1 ATOM 1268 C C . ASN A 1 164 ? -12.827 -19.677 -2.051 1.00 29.95 ? 280 ASN A C 1 ATOM 1269 O O . ASN A 1 164 ? -12.734 -20.084 -0.894 1.00 32.14 ? 280 ASN A O 1 ATOM 1270 C CB . ASN A 1 164 ? -13.805 -21.600 -3.317 1.00 37.11 ? 280 ASN A CB 1 ATOM 1271 C CG . ASN A 1 164 ? -12.622 -21.824 -4.232 1.00 41.34 ? 280 ASN A CG 1 ATOM 1272 O OD1 . ASN A 1 164 ? -11.497 -22.016 -3.774 1.00 44.23 ? 280 ASN A OD1 1 ATOM 1273 N ND2 . ASN A 1 164 ? -12.870 -21.804 -5.533 1.00 47.57 ? 280 ASN A ND2 1 ATOM 1274 N N . ALA A 1 165 ? -11.945 -18.837 -2.583 1.00 28.55 ? 281 ALA A N 1 ATOM 1275 C CA . ALA A 1 165 ? -10.794 -18.374 -1.816 1.00 32.85 ? 281 ALA A CA 1 ATOM 1276 C C . ALA A 1 165 ? -11.139 -17.197 -0.905 1.00 32.49 ? 281 ALA A C 1 ATOM 1277 O O . ALA A 1 165 ? -10.351 -16.828 -0.035 1.00 31.56 ? 281 ALA A O 1 ATOM 1278 C CB . ALA A 1 165 ? -9.644 -18.008 -2.742 1.00 39.87 ? 281 ALA A CB 1 ATOM 1279 N N . LYS A 1 166 ? -12.311 -16.603 -1.109 1.00 25.60 ? 282 LYS A N 1 ATOM 1280 C CA . LYS A 1 166 ? -12.730 -15.474 -0.279 1.00 21.00 ? 282 LYS A CA 1 ATOM 1281 C C . LYS A 1 166 ? -13.504 -15.976 0.931 1.00 24.60 ? 282 LYS A C 1 ATOM 1282 O O . LYS A 1 166 ? -14.394 -16.816 0.811 1.00 23.64 ? 282 LYS A O 1 ATOM 1283 C CB . LYS A 1 166 ? -13.578 -14.492 -1.086 1.00 23.66 ? 282 LYS A CB 1 ATOM 1284 C CG . LYS A 1 166 ? -12.839 -13.853 -2.257 1.00 26.02 ? 282 LYS A CG 1 ATOM 1285 C CD . LYS A 1 166 ? -11.638 -13.044 -1.786 1.00 32.71 ? 282 LYS A CD 1 ATOM 1286 C CE . LYS A 1 166 ? -11.004 -12.274 -2.939 1.00 38.08 ? 282 LYS A CE 1 ATOM 1287 N NZ . LYS A 1 166 ? -9.804 -11.507 -2.498 1.00 42.50 ? 282 LYS A NZ 1 ATOM 1288 N N . THR A 1 167 ? -13.151 -15.463 2.103 1.00 25.88 ? 283 THR A N 1 ATOM 1289 C CA . THR A 1 167 ? -13.773 -15.904 3.338 1.00 22.27 ? 283 THR A CA 1 ATOM 1290 C C . THR A 1 167 ? -15.229 -15.456 3.425 1.00 17.89 ? 283 THR A C 1 ATOM 1291 O O . THR A 1 167 ? -15.590 -14.362 2.985 1.00 26.24 ? 283 THR A O 1 ATOM 1292 C CB . THR A 1 167 ? -12.985 -15.398 4.565 1.00 31.48 ? 283 THR A CB 1 ATOM 1293 O OG1 . THR A 1 167 ? -11.670 -15.966 4.546 1.00 31.52 ? 283 THR A OG1 1 ATOM 1294 C CG2 . THR A 1 167 ? -13.682 -15.793 5.859 1.00 32.35 ? 283 THR A CG2 1 ATOM 1295 N N . ILE A 1 168 ? -16.066 -16.323 3.976 1.00 18.28 ? 284 ILE A N 1 ATOM 1296 C CA . ILE A 1 168 ? -17.468 -16.006 4.169 1.00 19.14 ? 284 ILE A CA 1 ATOM 1297 C C . ILE A 1 168 ? -17.711 -15.616 5.623 1.00 22.48 ? 284 ILE A C 1 ATOM 1298 O O . ILE A 1 168 ? -17.316 -16.333 6.537 1.00 24.16 ? 284 ILE A O 1 ATOM 1299 C CB . ILE A 1 168 ? -18.357 -17.206 3.840 1.00 20.86 ? 284 ILE A CB 1 ATOM 1300 C CG1 . ILE A 1 168 ? -18.165 -17.634 2.379 1.00 19.97 ? 284 ILE A CG1 1 ATOM 1301 C CG2 . ILE A 1 168 ? -19.811 -16.880 4.137 1.00 22.90 ? 284 ILE A CG2 1 ATOM 1302 C CD1 . ILE A 1 168 ? -18.775 -18.987 2.065 1.00 23.59 ? 284 ILE A CD1 1 ATOM 1303 N N . ILE A 1 169 ? -18.353 -14.472 5.828 1.00 20.84 ? 285 ILE A N 1 ATOM 1304 C CA . ILE A 1 169 ? -18.783 -14.074 7.160 1.00 20.21 ? 285 ILE A CA 1 ATOM 1305 C C . ILE A 1 169 ? -20.270 -14.364 7.274 1.00 22.08 ? 285 ILE A C 1 ATOM 1306 O O . ILE A 1 169 ? -21.073 -13.825 6.514 1.00 21.72 ? 285 ILE A O 1 ATOM 1307 C CB . ILE A 1 169 ? -18.551 -12.585 7.409 1.00 21.48 ? 285 ILE A CB 1 ATOM 1308 C CG1 . ILE A 1 169 ? -17.069 -12.243 7.244 1.00 24.39 ? 285 ILE A CG1 1 ATOM 1309 C CG2 . ILE A 1 169 ? -19.069 -12.184 8.800 1.00 25.05 ? 285 ILE A CG2 1 ATOM 1310 C CD1 . ILE A 1 169 ? -16.768 -10.765 7.319 1.00 24.14 ? 285 ILE A CD1 1 ATOM 1311 N N . VAL A 1 170 ? -20.626 -15.243 8.199 1.00 21.72 ? 286 VAL A N 1 ATOM 1312 C CA . VAL A 1 170 ? -22.023 -15.528 8.481 1.00 24.64 ? 286 VAL A CA 1 ATOM 1313 C C . VAL A 1 170 ? -22.436 -14.641 9.641 1.00 25.88 ? 286 VAL A C 1 ATOM 1314 O O . VAL A 1 170 ? -21.868 -14.721 10.727 1.00 22.25 ? 286 VAL A O 1 ATOM 1315 C CB . VAL A 1 170 ? -22.245 -17.002 8.867 1.00 28.09 ? 286 VAL A CB 1 ATOM 1316 C CG1 . VAL A 1 170 ? -23.715 -17.252 9.207 1.00 24.49 ? 286 VAL A CG1 1 ATOM 1317 C CG2 . VAL A 1 170 ? -21.787 -17.926 7.743 1.00 26.04 ? 286 VAL A CG2 1 ATOM 1318 N N . HIS A 1 171 ? -23.414 -13.780 9.407 1.00 20.49 ? 287 HIS A N 1 ATOM 1319 C CA . HIS A 1 171 ? -23.868 -12.880 10.452 1.00 20.63 ? 287 HIS A CA 1 ATOM 1320 C C . HIS A 1 171 ? -25.148 -13.426 11.081 1.00 24.78 ? 287 HIS A C 1 ATOM 1321 O O . HIS A 1 171 ? -26.208 -13.437 10.455 1.00 25.33 ? 287 HIS A O 1 ATOM 1322 C CB . HIS A 1 171 ? -24.096 -11.485 9.875 1.00 21.87 ? 287 HIS A CB 1 ATOM 1323 C CG . HIS A 1 171 ? -24.148 -10.406 10.909 1.00 20.42 ? 287 HIS A CG 1 ATOM 1324 N ND1 . HIS A 1 171 ? -24.406 -9.089 10.594 1.00 26.50 ? 287 HIS A ND1 1 ATOM 1325 C CD2 . HIS A 1 171 ? -23.976 -10.445 12.252 1.00 22.86 ? 287 HIS A CD2 1 ATOM 1326 C CE1 . HIS A 1 171 ? -24.389 -8.362 11.698 1.00 27.58 ? 287 HIS A CE1 1 ATOM 1327 N NE2 . HIS A 1 171 ? -24.133 -9.162 12.719 1.00 27.02 ? 287 HIS A NE2 1 ATOM 1328 N N . LEU A 1 172 ? -25.042 -13.894 12.318 1.00 22.36 ? 288 LEU A N 1 ATOM 1329 C CA . LEU A 1 172 ? -26.170 -14.541 12.978 1.00 21.99 ? 288 LEU A CA 1 ATOM 1330 C C . LEU A 1 172 ? -27.188 -13.513 13.449 1.00 25.44 ? 288 LEU A C 1 ATOM 1331 O O . LEU A 1 172 ? -26.841 -12.356 13.702 1.00 25.76 ? 288 LEU A O 1 ATOM 1332 C CB . LEU A 1 172 ? -25.683 -15.375 14.164 1.00 22.97 ? 288 LEU A CB 1 ATOM 1333 C CG . LEU A 1 172 ? -24.663 -16.470 13.860 1.00 26.72 ? 288 LEU A CG 1 ATOM 1334 C CD1 . LEU A 1 172 ? -24.220 -17.144 15.151 1.00 25.84 ? 288 LEU A CD1 1 ATOM 1335 C CD2 . LEU A 1 172 ? -25.252 -17.486 12.894 1.00 26.06 ? 288 LEU A CD2 1 ATOM 1336 N N . ASN A 1 173 ? -28.445 -13.935 13.563 1.00 25.75 ? 289 ASN A N 1 ATOM 1337 C CA . ASN A 1 173 ? -29.488 -13.052 14.071 1.00 25.60 ? 289 ASN A CA 1 ATOM 1338 C C . ASN A 1 173 ? -29.893 -13.399 15.505 1.00 30.62 ? 289 ASN A C 1 ATOM 1339 O O . ASN A 1 173 ? -30.691 -12.699 16.122 1.00 27.86 ? 289 ASN A O 1 ATOM 1340 C CB . ASN A 1 173 ? -30.704 -13.012 13.127 1.00 27.05 ? 289 ASN A CB 1 ATOM 1341 C CG . ASN A 1 173 ? -31.413 -14.355 12.999 1.00 32.92 ? 289 ASN A CG 1 ATOM 1342 O OD1 . ASN A 1 173 ? -30.889 -15.396 13.392 1.00 29.61 ? 289 ASN A OD1 1 ATOM 1343 N ND2 . ASN A 1 173 ? -32.628 -14.326 12.440 1.00 33.46 ? 289 ASN A ND2 1 ATOM 1344 N N . LYS A 1 174 ? -29.321 -14.478 16.029 1.00 28.35 ? 290 LYS A N 1 ATOM 1345 C CA . LYS A 1 174 ? -29.579 -14.903 17.403 1.00 29.85 ? 290 LYS A CA 1 ATOM 1346 C C . LYS A 1 174 ? -28.300 -15.438 18.039 1.00 30.63 ? 290 LYS A C 1 ATOM 1347 O O . LYS A 1 174 ? -27.640 -16.313 17.477 1.00 30.53 ? 290 LYS A O 1 ATOM 1348 C CB . LYS A 1 174 ? -30.674 -15.971 17.435 1.00 36.32 ? 290 LYS A CB 1 ATOM 1349 C CG . LYS A 1 174 ? -30.977 -16.530 18.819 1.00 49.28 ? 290 LYS A CG 1 ATOM 1350 C CD . LYS A 1 174 ? -31.498 -15.453 19.759 1.00 59.91 ? 290 LYS A CD 1 ATOM 1351 C CE . LYS A 1 174 ? -31.858 -16.036 21.120 1.00 66.56 ? 290 LYS A CE 1 ATOM 1352 N NZ . LYS A 1 174 ? -32.302 -14.989 22.085 1.00 67.97 ? 290 LYS A NZ 1 ATOM 1353 N N . SER A 1 175 ? -27.958 -14.911 19.213 1.00 32.04 ? 291 SER A N 1 ATOM 1354 C CA . SER A 1 175 ? -26.745 -15.320 19.919 1.00 32.08 ? 291 SER A CA 1 ATOM 1355 C C . SER A 1 175 ? -26.830 -16.755 20.422 1.00 30.65 ? 291 SER A C 1 ATOM 1356 O O . SER A 1 175 ? -27.889 -17.216 20.838 1.00 28.47 ? 291 SER A O 1 ATOM 1357 C CB . SER A 1 175 ? -26.479 -14.399 21.115 1.00 32.45 ? 291 SER A CB 1 ATOM 1358 O OG . SER A 1 175 ? -26.117 -13.098 20.701 1.00 42.48 ? 291 SER A OG 1 ATOM 1359 N N . VAL A 1 176 ? -25.702 -17.453 20.387 1.00 29.06 ? 292 VAL A N 1 ATOM 1360 C CA . VAL A 1 176 ? -25.578 -18.736 21.055 1.00 30.48 ? 292 VAL A CA 1 ATOM 1361 C C . VAL A 1 176 ? -24.398 -18.658 22.015 1.00 26.86 ? 292 VAL A C 1 ATOM 1362 O O . VAL A 1 176 ? -23.267 -18.415 21.600 1.00 25.33 ? 292 VAL A O 1 ATOM 1363 C CB . VAL A 1 176 ? -25.349 -19.883 20.055 1.00 32.97 ? 292 VAL A CB 1 ATOM 1364 C CG1 . VAL A 1 176 ? -25.121 -21.186 20.797 1.00 31.69 ? 292 VAL A CG1 1 ATOM 1365 C CG2 . VAL A 1 176 ? -26.533 -20.008 19.109 1.00 37.78 ? 292 VAL A CG2 1 ATOM 1366 N N . GLU A 1 177 ? -24.659 -18.850 23.303 1.00 24.36 ? 293 GLU A N 1 ATOM 1367 C CA . GLU A 1 177 ? -23.600 -18.720 24.298 1.00 20.33 ? 293 GLU A CA 1 ATOM 1368 C C . GLU A 1 177 ? -22.580 -19.840 24.201 1.00 24.51 ? 293 GLU A C 1 ATOM 1369 O O . GLU A 1 177 ? -22.924 -20.993 23.955 1.00 29.67 ? 293 GLU A O 1 ATOM 1370 C CB . GLU A 1 177 ? -24.177 -18.691 25.716 1.00 30.11 ? 293 GLU A CB 1 ATOM 1371 C CG . GLU A 1 177 ? -24.932 -17.425 26.059 1.00 38.34 ? 293 GLU A CG 1 ATOM 1372 C CD . GLU A 1 177 ? -25.171 -17.285 27.551 1.00 41.90 ? 293 GLU A CD 1 ATOM 1373 O OE1 . GLU A 1 177 ? -24.820 -18.221 28.304 1.00 39.78 ? 293 GLU A OE1 1 ATOM 1374 O OE2 . GLU A 1 177 ? -25.703 -16.236 27.969 1.00 46.31 ? 293 GLU A OE2 1 ATOM 1375 N N . ILE A 1 178 ? -21.319 -19.486 24.400 1.00 24.13 ? 294 ILE A N 1 ATOM 1376 C CA . ILE A 1 178 ? -20.259 -20.471 24.511 1.00 22.93 ? 294 ILE A CA 1 ATOM 1377 C C . ILE A 1 178 ? -19.549 -20.189 25.829 1.00 24.51 ? 294 ILE A C 1 ATOM 1378 O O . ILE A 1 178 ? -19.126 -19.065 26.089 1.00 27.45 ? 294 ILE A O 1 ATOM 1379 C CB . ILE A 1 178 ? -19.293 -20.422 23.302 1.00 21.81 ? 294 ILE A CB 1 ATOM 1380 C CG1 . ILE A 1 178 ? -18.259 -21.547 23.399 1.00 22.89 ? 294 ILE A CG1 1 ATOM 1381 C CG2 . ILE A 1 178 ? -18.626 -19.049 23.191 1.00 23.11 ? 294 ILE A CG2 1 ATOM 1382 C CD1 . ILE A 1 178 ? -17.465 -21.766 22.129 1.00 27.73 ? 294 ILE A CD1 1 ATOM 1383 N N . ASN A 1 179 ? -19.490 -21.202 26.686 1.00 24.42 ? 295 ASN A N 1 ATOM 1384 C CA . ASN A 1 179 ? -18.987 -21.045 28.045 1.00 29.55 ? 295 ASN A CA 1 ATOM 1385 C C . ASN A 1 179 ? -17.698 -21.820 28.250 1.00 25.78 ? 295 ASN A C 1 ATOM 1386 O O . ASN A 1 179 ? -17.715 -23.038 28.400 1.00 27.48 ? 295 ASN A O 1 ATOM 1387 C CB . ASN A 1 179 ? -20.048 -21.501 29.053 1.00 29.90 ? 295 ASN A CB 1 ATOM 1388 C CG . ASN A 1 179 ? -19.552 -21.469 30.487 1.00 36.71 ? 295 ASN A CG 1 ATOM 1389 O OD1 . ASN A 1 179 ? -18.463 -20.982 30.771 1.00 30.57 ? 295 ASN A OD1 1 ATOM 1390 N ND2 . ASN A 1 179 ? -20.360 -21.993 31.400 1.00 41.62 ? 295 ASN A ND2 1 ATOM 1391 N N . CYS A 1 180 ? -16.581 -21.103 28.248 1.00 25.00 ? 296 CYS A N 1 ATOM 1392 C CA . CYS A 1 180 ? -15.269 -21.729 28.315 1.00 26.30 ? 296 CYS A CA 1 ATOM 1393 C C . CYS A 1 180 ? -14.635 -21.598 29.694 1.00 26.05 ? 296 CYS A C 1 ATOM 1394 O O . CYS A 1 180 ? -14.705 -20.548 30.326 1.00 29.44 ? 296 CYS A O 1 ATOM 1395 C CB . CYS A 1 180 ? -14.354 -21.148 27.238 1.00 33.40 ? 296 CYS A CB 1 ATOM 1396 S SG . CYS A 1 180 ? -15.046 -21.263 25.573 1.00 36.10 ? 296 CYS A SG 1 ATOM 1397 N N . THR A 1 181 ? -14.019 -22.682 30.153 1.00 31.31 ? 297 THR A N 1 ATOM 1398 C CA . THR A 1 181 ? -13.442 -22.723 31.487 1.00 28.53 ? 297 THR A CA 1 ATOM 1399 C C . THR A 1 181 ? -12.193 -23.592 31.561 1.00 27.69 ? 297 THR A C 1 ATOM 1400 O O . THR A 1 181 ? -12.145 -24.684 31.002 1.00 27.46 ? 297 THR A O 1 ATOM 1401 C CB . THR A 1 181 ? -14.457 -23.272 32.511 1.00 40.17 ? 297 THR A CB 1 ATOM 1402 O OG1 . THR A 1 181 ? -15.710 -22.597 32.364 1.00 43.10 ? 297 THR A OG1 1 ATOM 1403 C CG2 . THR A 1 181 ? -13.945 -23.087 33.928 1.00 32.30 ? 297 THR A CG2 1 ATOM 1404 N N . ARG A 1 182 ? -11.188 -23.090 32.267 1.00 27.88 ? 298 ARG A N 1 ATOM 1405 C CA . ARG A 1 182 ? -10.043 -23.882 32.678 1.00 28.36 ? 298 ARG A CA 1 ATOM 1406 C C . ARG A 1 182 ? -10.254 -24.097 34.166 1.00 31.86 ? 298 ARG A C 1 ATOM 1407 O O . ARG A 1 182 ? -10.026 -23.188 34.959 1.00 27.75 ? 298 ARG A O 1 ATOM 1408 C CB . ARG A 1 182 ? -8.746 -23.115 32.435 1.00 24.69 ? 298 ARG A CB 1 ATOM 1409 C CG . ARG A 1 182 ? -7.480 -23.938 32.609 1.00 23.38 ? 298 ARG A CG 1 ATOM 1410 C CD . ARG A 1 182 ? -7.360 -24.497 34.017 1.00 27.65 ? 298 ARG A CD 1 ATOM 1411 N NE . ARG A 1 182 ? -7.150 -23.456 35.018 1.00 30.00 ? 298 ARG A NE 1 ATOM 1412 C CZ . ARG A 1 182 ? -5.968 -22.923 35.309 1.00 31.38 ? 298 ARG A CZ 1 ATOM 1413 N NH1 . ARG A 1 182 ? -4.881 -23.324 34.670 1.00 28.46 ? 298 ARG A NH1 1 ATOM 1414 N NH2 . ARG A 1 182 ? -5.874 -21.983 36.237 1.00 29.52 ? 298 ARG A NH2 1 ATOM 1415 N N . PRO A 1 183 ? -10.721 -25.283 34.546 1.00 29.29 ? 299 PRO A N 1 ATOM 1416 C CA . PRO A 1 183 ? -11.181 -25.494 35.924 1.00 37.46 ? 299 PRO A CA 1 ATOM 1417 C C . PRO A 1 183 ? -10.082 -25.253 36.954 1.00 41.01 ? 299 PRO A C 1 ATOM 1418 O O . PRO A 1 183 ? -8.900 -25.447 36.667 1.00 36.06 ? 299 PRO A O 1 ATOM 1419 C CB . PRO A 1 183 ? -11.627 -26.961 35.926 1.00 40.71 ? 299 PRO A CB 1 ATOM 1420 C CG . PRO A 1 183 ? -10.861 -27.593 34.823 1.00 41.55 ? 299 PRO A CG 1 ATOM 1421 C CD . PRO A 1 183 ? -10.714 -26.533 33.767 1.00 33.96 ? 299 PRO A CD 1 ATOM 1422 N N . SER A 1 184 ? -10.487 -24.834 38.147 1.00 49.03 ? 300 SER A N 1 ATOM 1423 C CA . SER A 1 184 ? -9.555 -24.425 39.191 1.00 58.31 ? 300 SER A CA 1 ATOM 1424 C C . SER A 1 184 ? -8.593 -25.531 39.627 1.00 63.70 ? 300 SER A C 1 ATOM 1425 O O . SER A 1 184 ? -7.379 -25.322 39.659 1.00 64.12 ? 300 SER A O 1 ATOM 1426 C CB . SER A 1 184 ? -10.324 -23.886 40.397 1.00 62.64 ? 300 SER A CB 1 ATOM 1427 O OG . SER A 1 184 ? -9.440 -23.510 41.433 1.00 62.37 ? 300 SER A OG 1 ATOM 1428 N N . ASN A 1 185 ? -9.131 -26.703 39.955 1.00 68.53 ? 301 ASN A N 1 ATOM 1429 C CA . ASN A 1 185 ? -8.300 -27.821 40.401 1.00 78.17 ? 301 ASN A CA 1 ATOM 1430 C C . ASN A 1 185 ? -8.362 -29.026 39.466 1.00 83.06 ? 301 ASN A C 1 ATOM 1431 O O . ASN A 1 185 ? -8.508 -30.162 39.915 1.00 87.85 ? 301 ASN A O 1 ATOM 1432 C CB . ASN A 1 185 ? -8.683 -28.243 41.822 1.00 83.63 ? 301 ASN A CB 1 ATOM 1433 C CG . ASN A 1 185 ? -8.264 -27.225 42.870 1.00 86.84 ? 301 ASN A CG 1 ATOM 1434 O OD1 . ASN A 1 185 ? -7.351 -26.428 42.653 1.00 87.18 ? 301 ASN A OD1 1 ATOM 1435 N ND2 . ASN A 1 185 ? -8.943 -27.243 44.012 1.00 88.42 ? 301 ASN A ND2 1 ATOM 1436 N N . GLY A 1 192 ? -3.365 -31.790 38.287 1.00 75.31 ? 324 GLY A N 1 ATOM 1437 C CA . GLY A 1 192 ? -4.022 -31.895 36.996 1.00 73.76 ? 324 GLY A CA 1 ATOM 1438 C C . GLY A 1 192 ? -3.347 -31.062 35.921 1.00 70.57 ? 324 GLY A C 1 ATOM 1439 O O . GLY A 1 192 ? -2.488 -30.231 36.215 1.00 70.28 ? 324 GLY A O 1 ATOM 1440 N N . ASP A 1 193 ? -3.742 -31.291 34.671 1.00 63.67 ? 325 ASP A N 1 ATOM 1441 C CA . ASP A 1 193 ? -3.187 -30.563 33.533 1.00 53.35 ? 325 ASP A CA 1 ATOM 1442 C C . ASP A 1 193 ? -3.721 -29.130 33.486 1.00 42.53 ? 325 ASP A C 1 ATOM 1443 O O . ASP A 1 193 ? -4.887 -28.903 33.165 1.00 42.71 ? 325 ASP A O 1 ATOM 1444 C CB . ASP A 1 193 ? -3.516 -31.300 32.233 1.00 53.40 ? 325 ASP A CB 1 ATOM 1445 C CG . ASP A 1 193 ? -2.930 -30.621 31.012 1.00 52.68 ? 325 ASP A CG 1 ATOM 1446 O OD1 . ASP A 1 193 ? -2.600 -29.424 31.102 1.00 49.06 ? 325 ASP A OD1 1 ATOM 1447 O OD2 . ASP A 1 193 ? -2.808 -31.281 29.959 1.00 55.51 ? 325 ASP A OD2 1 ATOM 1448 N N . ILE A 1 194 ? -2.857 -28.166 33.794 1.00 33.87 ? 326 ILE A N 1 ATOM 1449 C CA . ILE A 1 194 ? -3.271 -26.770 33.925 1.00 29.17 ? 326 ILE A CA 1 ATOM 1450 C C . ILE A 1 194 ? -3.629 -26.096 32.596 1.00 24.59 ? 326 ILE A C 1 ATOM 1451 O O . ILE A 1 194 ? -4.243 -25.031 32.586 1.00 25.30 ? 326 ILE A O 1 ATOM 1452 C CB . ILE A 1 194 ? -2.193 -25.923 34.639 1.00 33.97 ? 326 ILE A CB 1 ATOM 1453 C CG1 . ILE A 1 194 ? -0.932 -25.818 33.777 1.00 39.77 ? 326 ILE A CG1 1 ATOM 1454 C CG2 . ILE A 1 194 ? -1.865 -26.514 36.007 1.00 39.03 ? 326 ILE A CG2 1 ATOM 1455 C CD1 . ILE A 1 194 ? 0.149 -24.932 34.373 1.00 32.67 ? 326 ILE A CD1 1 ATOM 1456 N N . ARG A 1 195 ? -3.242 -26.703 31.480 1.00 26.59 ? 327 ARG A N 1 ATOM 1457 C CA . ARG A 1 195 ? -3.546 -26.119 30.172 1.00 25.68 ? 327 ARG A CA 1 ATOM 1458 C C . ARG A 1 195 ? -4.800 -26.732 29.564 1.00 31.16 ? 327 ARG A C 1 ATOM 1459 O O . ARG A 1 195 ? -5.251 -26.314 28.498 1.00 26.97 ? 327 ARG A O 1 ATOM 1460 C CB . ARG A 1 195 ? -2.358 -26.274 29.217 1.00 24.44 ? 327 ARG A CB 1 ATOM 1461 C CG . ARG A 1 195 ? -1.158 -25.444 29.634 1.00 28.14 ? 327 ARG A CG 1 ATOM 1462 C CD . ARG A 1 195 ? 0.087 -25.796 28.845 1.00 29.80 ? 327 ARG A CD 1 ATOM 1463 N NE . ARG A 1 195 ? 1.259 -25.206 29.479 1.00 30.82 ? 327 ARG A NE 1 ATOM 1464 C CZ . ARG A 1 195 ? 1.879 -25.739 30.527 1.00 32.44 ? 327 ARG A CZ 1 ATOM 1465 N NH1 . ARG A 1 195 ? 1.442 -26.877 31.047 1.00 30.04 ? 327 ARG A NH1 1 ATOM 1466 N NH2 . ARG A 1 195 ? 2.933 -25.134 31.058 1.00 32.51 ? 327 ARG A NH2 1 ATOM 1467 N N . LYS A 1 196 ? -5.359 -27.725 30.247 1.00 28.84 ? 328 LYS A N 1 ATOM 1468 C CA . LYS A 1 196 ? -6.572 -28.383 29.774 1.00 30.22 ? 328 LYS A CA 1 ATOM 1469 C C . LYS A 1 196 ? -7.803 -27.540 30.078 1.00 26.94 ? 328 LYS A C 1 ATOM 1470 O O . LYS A 1 196 ? -8.023 -27.137 31.221 1.00 26.38 ? 328 LYS A O 1 ATOM 1471 C CB . LYS A 1 196 ? -6.725 -29.761 30.421 1.00 30.41 ? 328 LYS A CB 1 ATOM 1472 C CG . LYS A 1 196 ? -8.029 -30.458 30.064 1.00 42.46 ? 328 LYS A CG 1 ATOM 1473 C CD . LYS A 1 196 ? -8.066 -31.883 30.599 1.00 50.16 ? 328 LYS A CD 1 ATOM 1474 C CE . LYS A 1 196 ? -6.823 -32.651 30.184 1.00 55.92 ? 328 LYS A CE 1 ATOM 1475 N NZ . LYS A 1 196 ? -6.576 -32.554 28.719 1.00 60.26 ? 328 LYS A NZ 1 ATOM 1476 N N . ALA A 1 197 ? -8.609 -27.279 29.054 1.00 24.38 ? 329 ALA A N 1 ATOM 1477 C CA . ALA A 1 197 ? -9.827 -26.497 29.232 1.00 24.43 ? 329 ALA A CA 1 ATOM 1478 C C . ALA A 1 197 ? -10.957 -27.072 28.390 1.00 26.83 ? 329 ALA A C 1 ATOM 1479 O O . ALA A 1 197 ? -10.780 -28.082 27.711 1.00 28.25 ? 329 ALA A O 1 ATOM 1480 C CB . ALA A 1 197 ? -9.580 -25.039 28.872 1.00 23.86 ? 329 ALA A CB 1 ATOM 1481 N N . TYR A 1 198 ? -12.116 -26.425 28.432 1.00 24.61 ? 330 TYR A N 1 ATOM 1482 C CA . TYR A 1 198 ? -13.267 -26.890 27.667 1.00 31.40 ? 330 TYR A CA 1 ATOM 1483 C C . TYR A 1 198 ? -14.321 -25.798 27.521 1.00 32.64 ? 330 TYR A C 1 ATOM 1484 O O . TYR A 1 198 ? -14.443 -24.922 28.374 1.00 32.25 ? 330 TYR A O 1 ATOM 1485 C CB . TYR A 1 198 ? -13.876 -28.140 28.308 1.00 36.48 ? 330 TYR A CB 1 ATOM 1486 C CG . TYR A 1 198 ? -14.207 -27.976 29.774 1.00 42.58 ? 330 TYR A CG 1 ATOM 1487 C CD1 . TYR A 1 198 ? -15.446 -27.495 30.177 1.00 45.94 ? 330 TYR A CD1 1 ATOM 1488 C CD2 . TYR A 1 198 ? -13.280 -28.303 30.755 1.00 45.26 ? 330 TYR A CD2 1 ATOM 1489 C CE1 . TYR A 1 198 ? -15.752 -27.341 31.517 1.00 49.90 ? 330 TYR A CE1 1 ATOM 1490 C CE2 . TYR A 1 198 ? -13.577 -28.153 32.097 1.00 48.65 ? 330 TYR A CE2 1 ATOM 1491 C CZ . TYR A 1 198 ? -14.814 -27.672 32.472 1.00 53.04 ? 330 TYR A CZ 1 ATOM 1492 O OH . TYR A 1 198 ? -15.115 -27.522 33.806 1.00 57.72 ? 330 TYR A OH 1 ATOM 1493 N N . CYS A 1 199 ? -15.070 -25.849 26.425 1.00 29.89 ? 331 CYS A N 1 ATOM 1494 C CA . CYS A 1 199 ? -16.144 -24.897 26.187 1.00 28.77 ? 331 CYS A CA 1 ATOM 1495 C C . CYS A 1 199 ? -17.464 -25.644 26.130 1.00 32.34 ? 331 CYS A C 1 ATOM 1496 O O . CYS A 1 199 ? -17.556 -26.710 25.522 1.00 32.67 ? 331 CYS A O 1 ATOM 1497 C CB . CYS A 1 199 ? -15.916 -24.130 24.883 1.00 32.15 ? 331 CYS A CB 1 ATOM 1498 S SG . CYS A 1 199 ? -14.542 -22.950 24.928 1.00 36.49 ? 331 CYS A SG 1 ATOM 1499 N N . GLU A 1 200 ? -18.484 -25.096 26.776 1.00 30.26 ? 332 GLU A N 1 ATOM 1500 C CA . GLU A 1 200 ? -19.788 -25.741 26.776 1.00 26.35 ? 332 GLU A CA 1 ATOM 1501 C C . GLU A 1 200 ? -20.770 -24.929 25.947 1.00 31.94 ? 332 GLU A C 1 ATOM 1502 O O . GLU A 1 200 ? -20.828 -23.707 26.059 1.00 28.22 ? 332 GLU A O 1 ATOM 1503 C CB . GLU A 1 200 ? -20.302 -25.930 28.206 1.00 30.65 ? 332 GLU A CB 1 ATOM 1504 C CG . GLU A 1 200 ? -19.447 -26.875 29.040 1.00 39.78 ? 332 GLU A CG 1 ATOM 1505 C CD . GLU A 1 200 ? -19.952 -27.020 30.463 1.00 51.83 ? 332 GLU A CD 1 ATOM 1506 O OE1 . GLU A 1 200 ? -20.409 -26.009 31.038 1.00 59.12 ? 332 GLU A OE1 1 ATOM 1507 O OE2 . GLU A 1 200 ? -19.898 -28.146 31.003 1.00 50.11 ? 332 GLU A OE2 1 ATOM 1508 N N . ILE A 1 201 ? -21.524 -25.621 25.101 1.00 33.29 ? 333 ILE A N 1 ATOM 1509 C CA . ILE A 1 201 ? -22.511 -24.982 24.244 1.00 33.36 ? 333 ILE A CA 1 ATOM 1510 C C . ILE A 1 201 ? -23.802 -25.786 24.279 1.00 32.99 ? 333 ILE A C 1 ATOM 1511 O O . ILE A 1 201 ? -23.786 -27.008 24.161 1.00 34.68 ? 333 ILE A O 1 ATOM 1512 C CB . ILE A 1 201 ? -22.030 -24.897 22.779 1.00 35.21 ? 333 ILE A CB 1 ATOM 1513 C CG1 . ILE A 1 201 ? -20.681 -24.180 22.684 1.00 36.96 ? 333 ILE A CG1 1 ATOM 1514 C CG2 . ILE A 1 201 ? -23.068 -24.197 21.910 1.00 37.17 ? 333 ILE A CG2 1 ATOM 1515 C CD1 . ILE A 1 201 ? -19.502 -25.120 22.536 1.00 38.76 ? 333 ILE A CD1 1 ATOM 1516 N N . ASN A 1 202 ? -24.921 -25.094 24.441 1.00 32.99 ? 334 ASN A N 1 ATOM 1517 C CA . ASN A 1 202 ? -26.218 -25.742 24.379 1.00 34.01 ? 334 ASN A CA 1 ATOM 1518 C C . ASN A 1 202 ? -26.434 -26.318 22.983 1.00 32.45 ? 334 ASN A C 1 ATOM 1519 O O . ASN A 1 202 ? -26.568 -25.576 22.011 1.00 34.07 ? 334 ASN A O 1 ATOM 1520 C CB . ASN A 1 202 ? -27.317 -24.746 24.732 1.00 36.79 ? 334 ASN A CB 1 ATOM 1521 C CG . ASN A 1 202 ? -28.678 -25.388 24.815 1.00 44.58 ? 334 ASN A CG 1 ATOM 1522 O OD1 . ASN A 1 202 ? -29.064 -26.165 23.942 1.00 41.57 ? 334 ASN A OD1 1 ATOM 1523 N ND2 . ASN A 1 202 ? -29.415 -25.071 25.875 1.00 59.38 ? 334 ASN A ND2 1 ATOM 1524 N N . GLY A 1 203 ? -26.454 -27.645 22.894 1.00 34.93 ? 335 GLY A N 1 ATOM 1525 C CA . GLY A 1 203 ? -26.543 -28.331 21.618 1.00 38.22 ? 335 GLY A CA 1 ATOM 1526 C C . GLY A 1 203 ? -27.867 -28.146 20.904 1.00 38.59 ? 335 GLY A C 1 ATOM 1527 O O . GLY A 1 203 ? -27.913 -28.097 19.678 1.00 35.63 ? 335 GLY A O 1 ATOM 1528 N N . THR A 1 204 ? -28.950 -28.055 21.668 1.00 34.10 ? 336 THR A N 1 ATOM 1529 C CA . THR A 1 204 ? -30.259 -27.815 21.080 1.00 39.29 ? 336 THR A CA 1 ATOM 1530 C C . THR A 1 204 ? -30.279 -26.465 20.372 1.00 39.26 ? 336 THR A C 1 ATOM 1531 O O . THR A 1 204 ? -30.765 -26.353 19.245 1.00 34.69 ? 336 THR A O 1 ATOM 1532 C CB . THR A 1 204 ? -31.371 -27.852 22.137 1.00 38.46 ? 336 THR A CB 1 ATOM 1533 O OG1 . THR A 1 204 ? -31.466 -29.173 22.685 1.00 42.09 ? 336 THR A OG1 1 ATOM 1534 C CG2 . THR A 1 204 ? -32.708 -27.469 21.516 1.00 43.80 ? 336 THR A CG2 1 ATOM 1535 N N . LYS A 1 205 ? -29.744 -25.445 21.039 1.00 35.65 ? 337 LYS A N 1 ATOM 1536 C CA . LYS A 1 205 ? -29.732 -24.091 20.497 1.00 37.31 ? 337 LYS A CA 1 ATOM 1537 C C . LYS A 1 205 ? -28.811 -23.980 19.290 1.00 36.87 ? 337 LYS A C 1 ATOM 1538 O O . LYS A 1 205 ? -29.175 -23.393 18.270 1.00 33.81 ? 337 LYS A O 1 ATOM 1539 C CB . LYS A 1 205 ? -29.292 -23.084 21.565 1.00 38.96 ? 337 LYS A CB 1 ATOM 1540 C CG . LYS A 1 205 ? -30.349 -22.765 22.615 1.00 47.75 ? 337 LYS A CG 1 ATOM 1541 C CD . LYS A 1 205 ? -29.822 -21.759 23.630 1.00 52.50 ? 337 LYS A CD 1 ATOM 1542 C CE . LYS A 1 205 ? -30.945 -21.157 24.461 1.00 57.73 ? 337 LYS A CE 1 ATOM 1543 N NZ . LYS A 1 205 ? -31.690 -22.184 25.234 1.00 61.57 ? 337 LYS A NZ 1 ATOM 1544 N N . TRP A 1 206 ? -27.615 -24.542 19.413 1.00 32.56 ? 338 TRP A N 1 ATOM 1545 C CA . TRP A 1 206 ? -26.611 -24.407 18.366 1.00 35.54 ? 338 TRP A CA 1 ATOM 1546 C C . TRP A 1 206 ? -27.005 -25.115 17.070 1.00 34.57 ? 338 TRP A C 1 ATOM 1547 O O . TRP A 1 206 ? -26.866 -24.553 15.982 1.00 35.84 ? 338 TRP A O 1 ATOM 1548 C CB . TRP A 1 206 ? -25.256 -24.919 18.845 1.00 35.90 ? 338 TRP A CB 1 ATOM 1549 C CG . TRP A 1 206 ? -24.272 -25.029 17.732 1.00 34.59 ? 338 TRP A CG 1 ATOM 1550 C CD1 . TRP A 1 206 ? -23.904 -26.164 17.074 1.00 35.90 ? 338 TRP A CD1 1 ATOM 1551 C CD2 . TRP A 1 206 ? -23.545 -23.958 17.124 1.00 36.91 ? 338 TRP A CD2 1 ATOM 1552 N NE1 . TRP A 1 206 ? -22.986 -25.865 16.096 1.00 35.43 ? 338 TRP A NE1 1 ATOM 1553 C CE2 . TRP A 1 206 ? -22.747 -24.517 16.109 1.00 34.11 ? 338 TRP A CE2 1 ATOM 1554 C CE3 . TRP A 1 206 ? -23.488 -22.578 17.343 1.00 36.51 ? 338 TRP A CE3 1 ATOM 1555 C CZ2 . TRP A 1 206 ? -21.901 -23.747 15.313 1.00 37.01 ? 338 TRP A CZ2 1 ATOM 1556 C CZ3 . TRP A 1 206 ? -22.649 -21.816 16.551 1.00 40.09 ? 338 TRP A CZ3 1 ATOM 1557 C CH2 . TRP A 1 206 ? -21.867 -22.402 15.550 1.00 38.23 ? 338 TRP A CH2 1 ATOM 1558 N N . ASN A 1 207 ? -27.485 -26.349 17.185 1.00 30.56 ? 339 ASN A N 1 ATOM 1559 C CA . ASN A 1 207 ? -27.881 -27.110 16.007 1.00 38.00 ? 339 ASN A CA 1 ATOM 1560 C C . ASN A 1 207 ? -29.074 -26.480 15.295 1.00 37.44 ? 339 ASN A C 1 ATOM 1561 O O . ASN A 1 207 ? -29.221 -26.602 14.078 1.00 36.70 ? 339 ASN A O 1 ATOM 1562 C CB . ASN A 1 207 ? -28.161 -28.571 16.371 1.00 43.03 ? 339 ASN A CB 1 ATOM 1563 C CG . ASN A 1 207 ? -26.894 -29.336 16.715 1.00 42.83 ? 339 ASN A CG 1 ATOM 1564 O OD1 . ASN A 1 207 ? -25.871 -29.195 16.047 1.00 47.48 ? 339 ASN A OD1 1 ATOM 1565 N ND2 . ASN A 1 207 ? -26.955 -30.142 17.767 1.00 43.33 ? 339 ASN A ND2 1 ATOM 1566 N N . LYS A 1 208 ? -29.920 -25.801 16.062 1.00 32.98 ? 340 LYS A N 1 ATOM 1567 C CA . LYS A 1 208 ? -31.027 -25.039 15.493 1.00 39.49 ? 340 LYS A CA 1 ATOM 1568 C C . LYS A 1 208 ? -30.489 -23.922 14.607 1.00 35.07 ? 340 LYS A C 1 ATOM 1569 O O . LYS A 1 208 ? -30.955 -23.719 13.480 1.00 33.98 ? 340 LYS A O 1 ATOM 1570 C CB . LYS A 1 208 ? -31.879 -24.443 16.613 1.00 46.84 ? 340 LYS A CB 1 ATOM 1571 C CG . LYS A 1 208 ? -33.087 -23.656 16.139 1.00 56.42 ? 340 LYS A CG 1 ATOM 1572 C CD . LYS A 1 208 ? -33.620 -22.743 17.239 1.00 65.31 ? 340 LYS A CD 1 ATOM 1573 C CE . LYS A 1 208 ? -33.719 -23.459 18.576 1.00 70.88 ? 340 LYS A CE 1 ATOM 1574 N NZ . LYS A 1 208 ? -34.168 -22.556 19.683 1.00 73.62 ? 340 LYS A NZ 1 ATOM 1575 N N . VAL A 1 209 ? -29.501 -23.201 15.126 1.00 27.30 ? 341 VAL A N 1 ATOM 1576 C CA . VAL A 1 209 ? -28.899 -22.090 14.404 1.00 28.09 ? 341 VAL A CA 1 ATOM 1577 C C . VAL A 1 209 ? -28.097 -22.556 13.192 1.00 22.13 ? 341 VAL A C 1 ATOM 1578 O O . VAL A 1 209 ? -28.160 -21.940 12.130 1.00 31.69 ? 341 VAL A O 1 ATOM 1579 C CB . VAL A 1 209 ? -27.999 -21.249 15.323 1.00 28.62 ? 341 VAL A CB 1 ATOM 1580 C CG1 . VAL A 1 209 ? -27.200 -20.241 14.510 1.00 31.37 ? 341 VAL A CG1 1 ATOM 1581 C CG2 . VAL A 1 209 ? -28.844 -20.539 16.378 1.00 29.32 ? 341 VAL A CG2 1 ATOM 1582 N N . LEU A 1 210 ? -27.343 -23.636 13.349 1.00 26.02 ? 342 LEU A N 1 ATOM 1583 C CA . LEU A 1 210 ? -26.551 -24.164 12.243 1.00 33.14 ? 342 LEU A CA 1 ATOM 1584 C C . LEU A 1 210 ? -27.471 -24.636 11.121 1.00 32.32 ? 342 LEU A C 1 ATOM 1585 O O . LEU A 1 210 ? -27.174 -24.455 9.941 1.00 28.04 ? 342 LEU A O 1 ATOM 1586 C CB . LEU A 1 210 ? -25.647 -25.304 12.719 1.00 31.49 ? 342 LEU A CB 1 ATOM 1587 C CG . LEU A 1 210 ? -24.462 -25.663 11.823 1.00 36.33 ? 342 LEU A CG 1 ATOM 1588 C CD1 . LEU A 1 210 ? -23.619 -24.428 11.522 1.00 35.44 ? 342 LEU A CD1 1 ATOM 1589 C CD2 . LEU A 1 210 ? -23.617 -26.753 12.469 1.00 41.99 ? 342 LEU A CD2 1 ATOM 1590 N N . LYS A 1 211 ? -28.596 -25.238 11.491 1.00 32.89 ? 343 LYS A N 1 ATOM 1591 C CA . LYS A 1 211 ? -29.576 -25.654 10.497 1.00 30.22 ? 343 LYS A CA 1 ATOM 1592 C C . LYS A 1 211 ? -30.087 -24.444 9.721 1.00 32.92 ? 343 LYS A C 1 ATOM 1593 O O . LYS A 1 211 ? -30.236 -24.499 8.499 1.00 34.39 ? 343 LYS A O 1 ATOM 1594 C CB . LYS A 1 211 ? -30.731 -26.416 11.152 1.00 36.61 ? 343 LYS A CB 1 ATOM 1595 C CG . LYS A 1 211 ? -31.739 -26.986 10.168 1.00 46.26 ? 343 LYS A CG 1 ATOM 1596 C CD . LYS A 1 211 ? -32.741 -27.889 10.876 1.00 57.60 ? 343 LYS A CD 1 ATOM 1597 C CE . LYS A 1 211 ? -33.767 -28.460 9.906 1.00 65.46 ? 343 LYS A CE 1 ATOM 1598 N NZ . LYS A 1 211 ? -34.609 -27.395 9.290 1.00 66.91 ? 343 LYS A NZ 1 ATOM 1599 N N . GLN A 1 212 ? -30.338 -23.347 10.431 1.00 29.80 ? 344 GLN A N 1 ATOM 1600 C CA . GLN A 1 212 ? -30.765 -22.105 9.796 1.00 28.78 ? 344 GLN A CA 1 ATOM 1601 C C . GLN A 1 212 ? -29.673 -21.528 8.898 1.00 26.95 ? 344 GLN A C 1 ATOM 1602 O O . GLN A 1 212 ? -29.956 -20.988 7.828 1.00 26.08 ? 344 GLN A O 1 ATOM 1603 C CB . GLN A 1 212 ? -31.173 -21.076 10.852 1.00 32.09 ? 344 GLN A CB 1 ATOM 1604 C CG . GLN A 1 212 ? -32.476 -21.405 11.561 1.00 39.29 ? 344 GLN A CG 1 ATOM 1605 C CD . GLN A 1 212 ? -32.767 -20.452 12.699 1.00 46.59 ? 344 GLN A CD 1 ATOM 1606 O OE1 . GLN A 1 212 ? -31.881 -20.121 13.484 1.00 44.78 ? 344 GLN A OE1 1 ATOM 1607 N NE2 . GLN A 1 212 ? -34.011 -19.999 12.790 1.00 51.42 ? 344 GLN A NE2 1 ATOM 1608 N N . VAL A 1 213 ? -28.422 -21.634 9.333 1.00 25.01 ? 345 VAL A N 1 ATOM 1609 C CA . VAL A 1 213 ? -27.313 -21.163 8.511 1.00 28.49 ? 345 VAL A CA 1 ATOM 1610 C C . VAL A 1 213 ? -27.250 -21.988 7.229 1.00 27.96 ? 345 VAL A C 1 ATOM 1611 O O . VAL A 1 213 ? -27.035 -21.458 6.140 1.00 28.41 ? 345 VAL A O 1 ATOM 1612 C CB . VAL A 1 213 ? -25.973 -21.263 9.259 1.00 30.43 ? 345 VAL A CB 1 ATOM 1613 C CG1 . VAL A 1 213 ? -24.816 -20.976 8.314 1.00 25.19 ? 345 VAL A CG1 1 ATOM 1614 C CG2 . VAL A 1 213 ? -25.960 -20.308 10.440 1.00 26.22 ? 345 VAL A CG2 1 ATOM 1615 N N . THR A 1 214 ? -27.452 -23.292 7.374 1.00 25.10 ? 346 THR A N 1 ATOM 1616 C CA . THR A 1 214 ? -27.494 -24.206 6.241 1.00 33.25 ? 346 THR A CA 1 ATOM 1617 C C . THR A 1 214 ? -28.592 -23.820 5.256 1.00 33.96 ? 346 THR A C 1 ATOM 1618 O O . THR A 1 214 ? -28.389 -23.860 4.039 1.00 30.65 ? 346 THR A O 1 ATOM 1619 C CB . THR A 1 214 ? -27.720 -25.656 6.713 1.00 38.41 ? 346 THR A CB 1 ATOM 1620 O OG1 . THR A 1 214 ? -26.586 -26.088 7.476 1.00 39.37 ? 346 THR A OG1 1 ATOM 1621 C CG2 . THR A 1 214 ? -27.916 -26.586 5.527 1.00 43.32 ? 346 THR A CG2 1 ATOM 1622 N N . GLU A 1 215 ? -29.753 -23.445 5.785 1.00 29.74 ? 347 GLU A N 1 ATOM 1623 C CA . GLU A 1 215 ? -30.881 -23.059 4.942 1.00 34.73 ? 347 GLU A CA 1 ATOM 1624 C C . GLU A 1 215 ? -30.576 -21.771 4.190 1.00 30.81 ? 347 GLU A C 1 ATOM 1625 O O . GLU A 1 215 ? -30.990 -21.599 3.044 1.00 31.43 ? 347 GLU A O 1 ATOM 1626 C CB . GLU A 1 215 ? -32.156 -22.895 5.772 1.00 37.83 ? 347 GLU A CB 1 ATOM 1627 C CG . GLU A 1 215 ? -32.573 -24.146 6.522 1.00 51.64 ? 347 GLU A CG 1 ATOM 1628 C CD . GLU A 1 215 ? -32.703 -25.351 5.615 1.00 60.68 ? 347 GLU A CD 1 ATOM 1629 O OE1 . GLU A 1 215 ? -33.541 -25.313 4.689 1.00 65.37 ? 347 GLU A OE1 1 ATOM 1630 O OE2 . GLU A 1 215 ? -31.961 -26.335 5.823 1.00 63.52 ? 347 GLU A OE2 1 ATOM 1631 N N . LYS A 1 216 ? -29.848 -20.864 4.836 1.00 26.54 ? 348 LYS A N 1 ATOM 1632 C CA . LYS A 1 216 ? -29.460 -19.620 4.187 1.00 27.11 ? 348 LYS A CA 1 ATOM 1633 C C . LYS A 1 216 ? -28.457 -19.889 3.074 1.00 30.13 ? 348 LYS A C 1 ATOM 1634 O O . LYS A 1 216 ? -28.564 -19.330 1.980 1.00 31.43 ? 348 LYS A O 1 ATOM 1635 C CB . LYS A 1 216 ? -28.873 -18.633 5.197 1.00 32.27 ? 348 LYS A CB 1 ATOM 1636 C CG . LYS A 1 216 ? -29.882 -18.108 6.193 1.00 41.10 ? 348 LYS A CG 1 ATOM 1637 C CD . LYS A 1 216 ? -31.071 -17.465 5.485 1.00 44.21 ? 348 LYS A CD 1 ATOM 1638 C CE . LYS A 1 216 ? -30.649 -16.255 4.676 1.00 32.50 ? 348 LYS A CE 1 ATOM 1639 N NZ . LYS A 1 216 ? -31.826 -15.557 4.097 1.00 35.89 ? 348 LYS A NZ 1 ATOM 1640 N N . LEU A 1 217 ? -27.477 -20.738 3.359 1.00 25.72 ? 349 LEU A N 1 ATOM 1641 C CA . LEU A 1 217 ? -26.470 -21.083 2.365 1.00 26.08 ? 349 LEU A CA 1 ATOM 1642 C C . LEU A 1 217 ? -27.119 -21.746 1.146 1.00 30.37 ? 349 LEU A C 1 ATOM 1643 O O . LEU A 1 217 ? -26.697 -21.527 0.010 1.00 32.77 ? 349 LEU A O 1 ATOM 1644 C CB . LEU A 1 217 ? -25.397 -21.989 2.975 1.00 24.74 ? 349 LEU A CB 1 ATOM 1645 C CG . LEU A 1 217 ? -24.462 -21.297 3.972 1.00 24.77 ? 349 LEU A CG 1 ATOM 1646 C CD1 . LEU A 1 217 ? -23.607 -22.315 4.712 1.00 26.13 ? 349 LEU A CD1 1 ATOM 1647 C CD2 . LEU A 1 217 ? -23.595 -20.263 3.267 1.00 24.99 ? 349 LEU A CD2 1 ATOM 1648 N N . LYS A 1 218 ? -28.156 -22.541 1.379 1.00 29.31 ? 350 LYS A N 1 ATOM 1649 C CA . LYS A 1 218 ? -28.882 -23.164 0.272 1.00 28.38 ? 350 LYS A CA 1 ATOM 1650 C C . LYS A 1 218 ? -29.475 -22.112 -0.660 1.00 29.71 ? 350 LYS A C 1 ATOM 1651 O O . LYS A 1 218 ? -29.565 -22.317 -1.872 1.00 31.76 ? 350 LYS A O 1 ATOM 1652 C CB . LYS A 1 218 ? -29.994 -24.080 0.785 1.00 37.06 ? 350 LYS A CB 1 ATOM 1653 C CG . LYS A 1 218 ? -29.515 -25.397 1.361 1.00 40.78 ? 350 LYS A CG 1 ATOM 1654 C CD . LYS A 1 218 ? -30.700 -26.277 1.740 1.00 47.25 ? 350 LYS A CD 1 ATOM 1655 C CE . LYS A 1 218 ? -30.248 -27.597 2.344 1.00 56.04 ? 350 LYS A CE 1 ATOM 1656 N NZ . LYS A 1 218 ? -29.461 -28.413 1.378 1.00 59.88 ? 350 LYS A NZ 1 ATOM 1657 N N . GLU A 1 219 ? -29.883 -20.982 -0.095 1.00 31.43 ? 351 GLU A N 1 ATOM 1658 C CA . GLU A 1 219 ? -30.472 -19.923 -0.899 1.00 36.12 ? 351 GLU A CA 1 ATOM 1659 C C . GLU A 1 219 ? -29.436 -19.334 -1.851 1.00 35.22 ? 351 GLU A C 1 ATOM 1660 O O . GLU A 1 219 ? -29.780 -18.833 -2.920 1.00 31.53 ? 351 GLU A O 1 ATOM 1661 C CB . GLU A 1 219 ? -31.065 -18.831 -0.007 1.00 37.16 ? 351 GLU A CB 1 ATOM 1662 C CG . GLU A 1 219 ? -32.140 -19.337 0.943 1.00 45.44 ? 351 GLU A CG 1 ATOM 1663 C CD . GLU A 1 219 ? -32.705 -18.244 1.828 1.00 53.39 ? 351 GLU A CD 1 ATOM 1664 O OE1 . GLU A 1 219 ? -32.520 -17.053 1.500 1.00 52.16 ? 351 GLU A OE1 1 ATOM 1665 O OE2 . GLU A 1 219 ? -33.332 -18.578 2.857 1.00 61.72 ? 351 GLU A OE2 1 ATOM 1666 N N . HIS A 1 220 ? -28.166 -19.406 -1.461 1.00 32.58 ? 352 HIS A N 1 ATOM 1667 C CA . HIS A 1 220 ? -27.085 -18.831 -2.258 1.00 29.98 ? 352 HIS A CA 1 ATOM 1668 C C . HIS A 1 220 ? -26.445 -19.842 -3.198 1.00 28.65 ? 352 HIS A C 1 ATOM 1669 O O . HIS A 1 220 ? -25.843 -19.470 -4.206 1.00 33.74 ? 352 HIS A O 1 ATOM 1670 C CB . HIS A 1 220 ? -26.010 -18.237 -1.352 1.00 25.13 ? 352 HIS A CB 1 ATOM 1671 C CG . HIS A 1 220 ? -26.424 -16.956 -0.693 1.00 32.69 ? 352 HIS A CG 1 ATOM 1672 N ND1 . HIS A 1 220 ? -27.011 -16.919 0.545 1.00 35.24 ? 352 HIS A ND1 1 ATOM 1673 C CD2 . HIS A 1 220 ? -26.345 -15.677 -1.127 1.00 29.06 ? 352 HIS A CD2 1 ATOM 1674 C CE1 . HIS A 1 220 ? -27.276 -15.656 0.862 1.00 29.32 ? 352 HIS A CE1 1 ATOM 1675 N NE2 . HIS A 1 220 ? -26.882 -14.891 -0.132 1.00 33.27 ? 352 HIS A NE2 1 ATOM 1676 N N . PHE A 1 221 ? -26.570 -21.119 -2.861 1.00 24.14 ? 353 PHE A N 1 ATOM 1677 C CA . PHE A 1 221 ? -25.920 -22.170 -3.626 1.00 26.90 ? 353 PHE A CA 1 ATOM 1678 C C . PHE A 1 221 ? -26.917 -23.135 -4.268 1.00 29.04 ? 353 PHE A C 1 ATOM 1679 O O . PHE A 1 221 ? -26.702 -24.342 -4.303 1.00 31.27 ? 353 PHE A O 1 ATOM 1680 C CB . PHE A 1 221 ? -24.897 -22.901 -2.755 1.00 29.90 ? 353 PHE A CB 1 ATOM 1681 C CG . PHE A 1 221 ? -23.707 -22.054 -2.394 1.00 28.11 ? 353 PHE A CG 1 ATOM 1682 C CD1 . PHE A 1 221 ? -22.621 -21.964 -3.250 1.00 27.82 ? 353 PHE A CD1 1 ATOM 1683 C CD2 . PHE A 1 221 ? -23.680 -21.336 -1.209 1.00 25.04 ? 353 PHE A CD2 1 ATOM 1684 C CE1 . PHE A 1 221 ? -21.531 -21.183 -2.929 1.00 28.14 ? 353 PHE A CE1 1 ATOM 1685 C CE2 . PHE A 1 221 ? -22.591 -20.551 -0.882 1.00 26.17 ? 353 PHE A CE2 1 ATOM 1686 C CZ . PHE A 1 221 ? -21.513 -20.477 -1.746 1.00 28.04 ? 353 PHE A CZ 1 ATOM 1687 N N . ASN A 1 222 ? -28.016 -22.576 -4.765 1.00 34.23 ? 354 ASN A N 1 ATOM 1688 C CA . ASN A 1 222 ? -28.972 -23.303 -5.595 1.00 35.75 ? 354 ASN A CA 1 ATOM 1689 C C . ASN A 1 222 ? -29.498 -24.601 -4.987 1.00 30.31 ? 354 ASN A C 1 ATOM 1690 O O . ASN A 1 222 ? -29.726 -25.575 -5.702 1.00 29.05 ? 354 ASN A O 1 ATOM 1691 C CB . ASN A 1 222 ? -28.372 -23.587 -6.973 1.00 37.34 ? 354 ASN A CB 1 ATOM 1692 C CG . ASN A 1 222 ? -29.428 -23.909 -8.010 1.00 36.77 ? 354 ASN A CG 1 ATOM 1693 O OD1 . ASN A 1 222 ? -30.529 -23.359 -7.980 1.00 38.77 ? 354 ASN A OD1 1 ATOM 1694 N ND2 . ASN A 1 222 ? -29.102 -24.808 -8.930 1.00 33.23 ? 354 ASN A ND2 1 ATOM 1695 N N . ASN A 1 223 ? -29.691 -24.604 -3.672 1.00 33.20 ? 355 ASN A N 1 ATOM 1696 C CA . ASN A 1 223 ? -30.222 -25.769 -2.967 1.00 34.79 ? 355 ASN A CA 1 ATOM 1697 C C . ASN A 1 223 ? -29.344 -27.014 -3.026 1.00 34.12 ? 355 ASN A C 1 ATOM 1698 O O . ASN A 1 223 ? -29.833 -28.128 -2.861 1.00 33.28 ? 355 ASN A O 1 ATOM 1699 C CB . ASN A 1 223 ? -31.634 -26.109 -3.461 1.00 43.10 ? 355 ASN A CB 1 ATOM 1700 C CG . ASN A 1 223 ? -32.713 -25.544 -2.564 1.00 49.56 ? 355 ASN A CG 1 ATOM 1701 O OD1 . ASN A 1 223 ? -32.492 -24.564 -1.852 1.00 47.11 ? 355 ASN A OD1 1 ATOM 1702 N ND2 . ASN A 1 223 ? -33.887 -26.166 -2.584 1.00 53.59 ? 355 ASN A ND2 1 ATOM 1703 N N . LYS A 1 224 ? -28.052 -26.833 -3.268 1.00 33.46 ? 357 LYS A N 1 ATOM 1704 C CA . LYS A 1 224 ? -27.132 -27.956 -3.200 1.00 34.39 ? 357 LYS A CA 1 ATOM 1705 C C . LYS A 1 224 ? -27.056 -28.434 -1.755 1.00 34.66 ? 357 LYS A C 1 ATOM 1706 O O . LYS A 1 224 ? -27.393 -27.695 -0.832 1.00 33.10 ? 357 LYS A O 1 ATOM 1707 C CB . LYS A 1 224 ? -25.744 -27.562 -3.709 1.00 33.42 ? 357 LYS A CB 1 ATOM 1708 C CG . LYS A 1 224 ? -25.712 -27.184 -5.181 1.00 40.49 ? 357 LYS A CG 1 ATOM 1709 C CD . LYS A 1 224 ? -24.299 -26.860 -5.650 1.00 47.69 ? 357 LYS A CD 1 ATOM 1710 C CE . LYS A 1 224 ? -23.419 -28.099 -5.638 1.00 51.03 ? 357 LYS A CE 1 ATOM 1711 N NZ . LYS A 1 224 ? -22.087 -27.864 -6.260 1.00 53.48 ? 357 LYS A NZ 1 ATOM 1712 N N . THR A 1 225 ? -26.631 -29.675 -1.558 1.00 36.30 ? 358 THR A N 1 ATOM 1713 C CA . THR A 1 225 ? -26.470 -30.198 -0.209 1.00 38.22 ? 358 THR A CA 1 ATOM 1714 C C . THR A 1 225 ? -25.326 -29.458 0.478 1.00 34.86 ? 358 THR A C 1 ATOM 1715 O O . THR A 1 225 ? -24.246 -29.303 -0.088 1.00 33.93 ? 358 THR A O 1 ATOM 1716 C CB . THR A 1 225 ? -26.195 -31.711 -0.223 1.00 41.47 ? 358 THR A CB 1 ATOM 1717 O OG1 . THR A 1 225 ? -27.224 -32.377 -0.967 1.00 44.11 ? 358 THR A OG1 1 ATOM 1718 C CG2 . THR A 1 225 ? -26.154 -32.272 1.193 1.00 43.16 ? 358 THR A CG2 1 ATOM 1719 N N . ILE A 1 226 ? -25.569 -28.991 1.696 1.00 34.22 ? 359 ILE A N 1 ATOM 1720 C CA . ILE A 1 226 ? -24.558 -28.241 2.431 1.00 36.62 ? 359 ILE A CA 1 ATOM 1721 C C . ILE A 1 226 ? -23.893 -29.143 3.464 1.00 37.30 ? 359 ILE A C 1 ATOM 1722 O O . ILE A 1 226 ? -24.563 -29.705 4.329 1.00 37.50 ? 359 ILE A O 1 ATOM 1723 C CB . ILE A 1 226 ? -25.169 -27.003 3.119 1.00 31.71 ? 359 ILE A CB 1 ATOM 1724 C CG1 . ILE A 1 226 ? -25.899 -26.134 2.092 1.00 41.25 ? 359 ILE A CG1 1 ATOM 1725 C CG2 . ILE A 1 226 ? -24.096 -26.196 3.842 1.00 31.10 ? 359 ILE A CG2 1 ATOM 1726 C CD1 . ILE A 1 226 ? -25.035 -25.723 0.917 1.00 38.78 ? 359 ILE A CD1 1 ATOM 1727 N N . ILE A 1 227 ? -22.575 -29.287 3.357 1.00 32.49 ? 360 ILE A N 1 ATOM 1728 C CA . ILE A 1 227 ? -21.821 -30.154 4.253 1.00 35.43 ? 360 ILE A CA 1 ATOM 1729 C C . ILE A 1 227 ? -20.745 -29.373 4.993 1.00 34.58 ? 360 ILE A C 1 ATOM 1730 O O . ILE A 1 227 ? -20.035 -28.557 4.400 1.00 33.26 ? 360 ILE A O 1 ATOM 1731 C CB . ILE A 1 227 ? -21.147 -31.315 3.487 1.00 38.73 ? 360 ILE A CB 1 ATOM 1732 C CG1 . ILE A 1 227 ? -22.128 -31.945 2.496 1.00 43.00 ? 360 ILE A CG1 1 ATOM 1733 C CG2 . ILE A 1 227 ? -20.606 -32.354 4.461 1.00 42.72 ? 360 ILE A CG2 1 ATOM 1734 C CD1 . ILE A 1 227 ? -21.494 -32.973 1.583 1.00 52.20 ? 360 ILE A CD1 1 ATOM 1735 N N . PHE A 1 228 ? -20.635 -29.618 6.294 1.00 31.87 ? 361 PHE A N 1 ATOM 1736 C CA . PHE A 1 228 ? -19.566 -29.019 7.086 1.00 34.04 ? 361 PHE A CA 1 ATOM 1737 C C . PHE A 1 228 ? -18.450 -30.040 7.316 1.00 35.87 ? 361 PHE A C 1 ATOM 1738 O O . PHE A 1 228 ? -18.711 -31.226 7.512 1.00 36.70 ? 361 PHE A O 1 ATOM 1739 C CB . PHE A 1 228 ? -20.099 -28.487 8.421 1.00 34.90 ? 361 PHE A CB 1 ATOM 1740 C CG . PHE A 1 228 ? -20.994 -27.285 8.283 1.00 37.40 ? 361 PHE A CG 1 ATOM 1741 C CD1 . PHE A 1 228 ? -20.463 -26.031 8.016 1.00 36.08 ? 361 PHE A CD1 1 ATOM 1742 C CD2 . PHE A 1 228 ? -22.365 -27.408 8.418 1.00 38.04 ? 361 PHE A CD2 1 ATOM 1743 C CE1 . PHE A 1 228 ? -21.287 -24.924 7.883 1.00 35.16 ? 361 PHE A CE1 1 ATOM 1744 C CE2 . PHE A 1 228 ? -23.192 -26.305 8.289 1.00 37.99 ? 361 PHE A CE2 1 ATOM 1745 C CZ . PHE A 1 228 ? -22.653 -25.063 8.022 1.00 34.76 ? 361 PHE A CZ 1 ATOM 1746 N N . GLN A 1 229 ? -17.210 -29.568 7.272 1.00 33.56 ? 362 GLN A N 1 ATOM 1747 C CA . GLN A 1 229 ? -16.051 -30.422 7.466 1.00 36.23 ? 362 GLN A CA 1 ATOM 1748 C C . GLN A 1 229 ? -15.024 -29.687 8.319 1.00 35.42 ? 362 GLN A C 1 ATOM 1749 O O . GLN A 1 229 ? -15.049 -28.454 8.383 1.00 32.86 ? 362 GLN A O 1 ATOM 1750 C CB . GLN A 1 229 ? -15.449 -30.809 6.113 1.00 39.40 ? 362 GLN A CB 1 ATOM 1751 C CG . GLN A 1 229 ? -16.170 -31.951 5.419 1.00 46.45 ? 362 GLN A CG 1 ATOM 1752 C CD . GLN A 1 229 ? -16.083 -33.238 6.212 1.00 50.63 ? 362 GLN A CD 1 ATOM 1753 O OE1 . GLN A 1 229 ? -16.990 -33.572 6.974 1.00 50.93 ? 362 GLN A OE1 1 ATOM 1754 N NE2 . GLN A 1 229 ? -14.987 -33.969 6.037 1.00 50.53 ? 362 GLN A NE2 1 ATOM 1755 N N . PRO A 1 230 ? -14.109 -30.427 8.969 1.00 43.15 ? 363 PRO A N 1 ATOM 1756 C CA . PRO A 1 230 ? -13.137 -29.718 9.793 1.00 40.83 ? 363 PRO A CA 1 ATOM 1757 C C . PRO A 1 230 ? -12.137 -29.008 8.891 1.00 36.82 ? 363 PRO A C 1 ATOM 1758 O O . PRO A 1 230 ? -12.047 -29.346 7.709 1.00 37.76 ? 363 PRO A O 1 ATOM 1759 C CB . PRO A 1 230 ? -12.444 -30.849 10.537 1.00 44.84 ? 363 PRO A CB 1 ATOM 1760 C CG . PRO A 1 230 ? -12.482 -31.987 9.574 1.00 51.29 ? 363 PRO A CG 1 ATOM 1761 C CD . PRO A 1 230 ? -13.791 -31.861 8.864 1.00 48.58 ? 363 PRO A CD 1 ATOM 1762 N N . PRO A 1 231 ? -11.416 -28.016 9.422 1.00 32.21 ? 364 PRO A N 1 ATOM 1763 C CA . PRO A 1 231 ? -10.394 -27.396 8.582 1.00 37.16 ? 364 PRO A CA 1 ATOM 1764 C C . PRO A 1 231 ? -9.444 -28.473 8.059 1.00 44.00 ? 364 PRO A C 1 ATOM 1765 O O . PRO A 1 231 ? -9.147 -29.431 8.775 1.00 45.00 ? 364 PRO A O 1 ATOM 1766 C CB . PRO A 1 231 ? -9.690 -26.451 9.550 1.00 31.41 ? 364 PRO A CB 1 ATOM 1767 C CG . PRO A 1 231 ? -10.756 -26.097 10.549 1.00 31.20 ? 364 PRO A CG 1 ATOM 1768 C CD . PRO A 1 231 ? -11.549 -27.351 10.729 1.00 31.60 ? 364 PRO A CD 1 ATOM 1769 N N . SER A 1 232 ? -8.990 -28.326 6.819 1.00 48.78 ? 365 SER A N 1 ATOM 1770 C CA . SER A 1 232 ? -8.185 -29.362 6.175 1.00 49.27 ? 365 SER A CA 1 ATOM 1771 C C . SER A 1 232 ? -6.705 -29.270 6.539 1.00 55.14 ? 365 SER A C 1 ATOM 1772 O O . SER A 1 232 ? -5.947 -30.213 6.315 1.00 58.84 ? 365 SER A O 1 ATOM 1773 C CB . SER A 1 232 ? -8.364 -29.315 4.655 1.00 48.65 ? 365 SER A CB 1 ATOM 1774 O OG . SER A 1 232 ? -8.040 -28.034 4.141 1.00 52.84 ? 365 SER A OG 1 ATOM 1775 N N . GLY A 1 233 ? -6.299 -28.137 7.100 1.00 52.50 ? 366 GLY A N 1 ATOM 1776 C CA . GLY A 1 233 ? -4.916 -27.940 7.496 1.00 51.69 ? 366 GLY A CA 1 ATOM 1777 C C . GLY A 1 233 ? -4.614 -26.497 7.849 1.00 47.33 ? 366 GLY A C 1 ATOM 1778 O O . GLY A 1 233 ? -5.503 -25.647 7.838 1.00 43.35 ? 366 GLY A O 1 ATOM 1779 N N . GLY A 1 234 ? -3.352 -26.217 8.158 1.00 45.45 ? 367 GLY A N 1 ATOM 1780 C CA . GLY A 1 234 ? -2.938 -24.871 8.511 1.00 40.11 ? 367 GLY A CA 1 ATOM 1781 C C . GLY A 1 234 ? -2.478 -24.775 9.953 1.00 38.18 ? 367 GLY A C 1 ATOM 1782 O O . GLY A 1 234 ? -2.370 -25.785 10.653 1.00 40.54 ? 367 GLY A O 1 ATOM 1783 N N . ASP A 1 235 ? -2.201 -23.554 10.397 1.00 33.78 ? 368 ASP A N 1 ATOM 1784 C CA . ASP A 1 235 ? -1.747 -23.319 11.760 1.00 30.64 ? 368 ASP A CA 1 ATOM 1785 C C . ASP A 1 235 ? -2.859 -23.619 12.756 1.00 25.34 ? 368 ASP A C 1 ATOM 1786 O O . ASP A 1 235 ? -4.042 -23.535 12.423 1.00 21.64 ? 368 ASP A O 1 ATOM 1787 C CB . ASP A 1 235 ? -1.284 -21.870 11.932 1.00 38.55 ? 368 ASP A CB 1 ATOM 1788 C CG . ASP A 1 235 ? 0.050 -21.598 11.263 1.00 48.58 ? 368 ASP A CG 1 ATOM 1789 O OD1 . ASP A 1 235 ? 0.836 -22.553 11.078 1.00 50.50 ? 368 ASP A OD1 1 ATOM 1790 O OD2 . ASP A 1 235 ? 0.314 -20.423 10.933 1.00 49.21 ? 368 ASP A OD2 1 ATOM 1791 N N . LEU A 1 236 ? -2.471 -23.949 13.982 1.00 22.25 ? 369 LEU A N 1 ATOM 1792 C CA . LEU A 1 236 ? -3.432 -24.277 15.030 1.00 26.05 ? 369 LEU A CA 1 ATOM 1793 C C . LEU A 1 236 ? -4.406 -23.139 15.299 1.00 22.94 ? 369 LEU A C 1 ATOM 1794 O O . LEU A 1 236 ? -5.556 -23.374 15.663 1.00 24.96 ? 369 LEU A O 1 ATOM 1795 C CB . LEU A 1 236 ? -2.709 -24.648 16.324 1.00 25.51 ? 369 LEU A CB 1 ATOM 1796 C CG . LEU A 1 236 ? -2.036 -26.019 16.346 1.00 29.52 ? 369 LEU A CG 1 ATOM 1797 C CD1 . LEU A 1 236 ? -1.173 -26.150 17.583 1.00 33.43 ? 369 LEU A CD1 1 ATOM 1798 C CD2 . LEU A 1 236 ? -3.083 -27.126 16.296 1.00 32.22 ? 369 LEU A CD2 1 ATOM 1799 N N . GLU A 1 237 ? -3.941 -21.905 15.121 1.00 19.28 ? 370 GLU A N 1 ATOM 1800 C CA . GLU A 1 237 ? -4.783 -20.743 15.364 1.00 22.35 ? 370 GLU A CA 1 ATOM 1801 C C . GLU A 1 237 ? -5.993 -20.726 14.430 1.00 21.67 ? 370 GLU A C 1 ATOM 1802 O O . GLU A 1 237 ? -7.024 -20.139 14.750 1.00 23.10 ? 370 GLU A O 1 ATOM 1803 C CB . GLU A 1 237 ? -3.970 -19.453 15.225 1.00 26.24 ? 370 GLU A CB 1 ATOM 1804 C CG . GLU A 1 237 ? -2.915 -19.255 16.326 1.00 28.25 ? 370 GLU A CG 1 ATOM 1805 C CD . GLU A 1 237 ? -1.680 -20.132 16.152 1.00 26.22 ? 370 GLU A CD 1 ATOM 1806 O OE1 . GLU A 1 237 ? -1.465 -20.665 15.045 1.00 23.69 ? 370 GLU A OE1 1 ATOM 1807 O OE2 . GLU A 1 237 ? -0.914 -20.284 17.130 1.00 25.62 ? 370 GLU A OE2 1 ATOM 1808 N N . ILE A 1 238 ? -5.860 -21.388 13.284 1.00 21.31 ? 371 ILE A N 1 ATOM 1809 C CA . ILE A 1 238 ? -6.915 -21.419 12.270 1.00 27.22 ? 371 ILE A CA 1 ATOM 1810 C C . ILE A 1 238 ? -7.734 -22.704 12.313 1.00 24.10 ? 371 ILE A C 1 ATOM 1811 O O . ILE A 1 238 ? -8.953 -22.686 12.128 1.00 25.38 ? 371 ILE A O 1 ATOM 1812 C CB . ILE A 1 238 ? -6.326 -21.302 10.849 1.00 35.22 ? 371 ILE A CB 1 ATOM 1813 C CG1 . ILE A 1 238 ? -5.317 -20.155 10.779 1.00 40.53 ? 371 ILE A CG1 1 ATOM 1814 C CG2 . ILE A 1 238 ? -7.436 -21.140 9.821 1.00 37.47 ? 371 ILE A CG2 1 ATOM 1815 C CD1 . ILE A 1 238 ? -5.849 -18.861 11.317 1.00 31.55 ? 371 ILE A CD1 1 ATOM 1816 N N . THR A 1 239 ? -7.062 -23.828 12.532 1.00 22.16 ? 372 THR A N 1 ATOM 1817 C CA . THR A 1 239 ? -7.757 -25.108 12.572 1.00 24.13 ? 372 THR A CA 1 ATOM 1818 C C . THR A 1 239 ? -8.564 -25.258 13.856 1.00 24.39 ? 372 THR A C 1 ATOM 1819 O O . THR A 1 239 ? -9.493 -26.059 13.922 1.00 24.96 ? 372 THR A O 1 ATOM 1820 C CB . THR A 1 239 ? -6.795 -26.300 12.388 1.00 28.02 ? 372 THR A CB 1 ATOM 1821 O OG1 . THR A 1 239 ? -5.855 -26.343 13.471 1.00 23.28 ? 372 THR A OG1 1 ATOM 1822 C CG2 . THR A 1 239 ? -6.039 -26.159 11.073 1.00 28.74 ? 372 THR A CG2 1 ATOM 1823 N N . MET A 1 240 ? -8.220 -24.466 14.866 1.00 21.21 ? 373 MET A N 1 ATOM 1824 C CA . MET A 1 240 ? -8.969 -24.456 16.115 1.00 23.03 ? 373 MET A CA 1 ATOM 1825 C C . MET A 1 240 ? -9.609 -23.081 16.296 1.00 23.52 ? 373 MET A C 1 ATOM 1826 O O . MET A 1 240 ? -9.160 -22.100 15.698 1.00 21.09 ? 373 MET A O 1 ATOM 1827 C CB . MET A 1 240 ? -8.047 -24.763 17.300 1.00 23.27 ? 373 MET A CB 1 ATOM 1828 C CG . MET A 1 240 ? -7.189 -26.002 17.111 1.00 31.46 ? 373 MET A CG 1 ATOM 1829 S SD . MET A 1 240 ? -6.357 -26.585 18.602 1.00 45.56 ? 373 MET A SD 1 ATOM 1830 C CE . MET A 1 240 ? -7.654 -27.581 19.331 1.00 69.89 ? 373 MET A CE 1 ATOM 1831 N N . HIS A 1 241 ? -10.675 -23.012 17.089 1.00 20.55 ? 374 HIS A N 1 ATOM 1832 C CA . HIS A 1 241 ? -11.241 -21.723 17.483 1.00 18.79 ? 374 HIS A CA 1 ATOM 1833 C C . HIS A 1 241 ? -10.306 -21.107 18.507 1.00 20.59 ? 374 HIS A C 1 ATOM 1834 O O . HIS A 1 241 ? -10.238 -21.576 19.645 1.00 24.16 ? 374 HIS A O 1 ATOM 1835 C CB . HIS A 1 241 ? -12.637 -21.905 18.103 1.00 19.41 ? 374 HIS A CB 1 ATOM 1836 C CG . HIS A 1 241 ? -13.179 -20.672 18.773 1.00 20.43 ? 374 HIS A CG 1 ATOM 1837 N ND1 . HIS A 1 241 ? -13.824 -20.706 19.988 1.00 31.74 ? 374 HIS A ND1 1 ATOM 1838 C CD2 . HIS A 1 241 ? -13.175 -19.373 18.384 1.00 15.06 ? 374 HIS A CD2 1 ATOM 1839 C CE1 . HIS A 1 241 ? -14.188 -19.479 20.329 1.00 21.41 ? 374 HIS A CE1 1 ATOM 1840 N NE2 . HIS A 1 241 ? -13.806 -18.654 19.370 1.00 25.50 ? 374 HIS A NE2 1 ATOM 1841 N N . SER A 1 242 ? -9.579 -20.065 18.114 1.00 20.17 ? 375 SER A N 1 ATOM 1842 C CA . SER A 1 242 ? -8.670 -19.421 19.048 1.00 19.44 ? 375 SER A CA 1 ATOM 1843 C C . SER A 1 242 ? -9.188 -18.056 19.483 1.00 19.22 ? 375 SER A C 1 ATOM 1844 O O . SER A 1 242 ? -9.800 -17.326 18.703 1.00 19.23 ? 375 SER A O 1 ATOM 1845 C CB . SER A 1 242 ? -7.253 -19.321 18.473 1.00 27.46 ? 375 SER A CB 1 ATOM 1846 O OG . SER A 1 242 ? -7.242 -18.659 17.224 1.00 32.10 ? 375 SER A OG 1 ATOM 1847 N N . PHE A 1 243 ? -8.950 -17.730 20.745 1.00 19.23 ? 376 PHE A N 1 ATOM 1848 C CA . PHE A 1 243 ? -9.379 -16.460 21.304 1.00 19.95 ? 376 PHE A CA 1 ATOM 1849 C C . PHE A 1 243 ? -8.589 -16.225 22.572 1.00 21.61 ? 376 PHE A C 1 ATOM 1850 O O . PHE A 1 243 ? -7.856 -17.102 23.023 1.00 19.44 ? 376 PHE A O 1 ATOM 1851 C CB . PHE A 1 243 ? -10.877 -16.484 21.614 1.00 22.28 ? 376 PHE A CB 1 ATOM 1852 C CG . PHE A 1 243 ? -11.289 -17.604 22.524 1.00 23.79 ? 376 PHE A CG 1 ATOM 1853 C CD1 . PHE A 1 243 ? -11.449 -18.887 22.032 1.00 28.74 ? 376 PHE A CD1 1 ATOM 1854 C CD2 . PHE A 1 243 ? -11.524 -17.373 23.870 1.00 28.16 ? 376 PHE A CD2 1 ATOM 1855 C CE1 . PHE A 1 243 ? -11.831 -19.922 22.871 1.00 33.87 ? 376 PHE A CE1 1 ATOM 1856 C CE2 . PHE A 1 243 ? -11.907 -18.406 24.714 1.00 28.52 ? 376 PHE A CE2 1 ATOM 1857 C CZ . PHE A 1 243 ? -12.058 -19.677 24.214 1.00 32.27 ? 376 PHE A CZ 1 ATOM 1858 N N . ASN A 1 244 ? -8.735 -15.040 23.145 1.00 23.09 ? 377 ASN A N 1 ATOM 1859 C CA . ASN A 1 244 ? -8.059 -14.729 24.392 1.00 22.32 ? 377 ASN A CA 1 ATOM 1860 C C . ASN A 1 244 ? -9.068 -14.524 25.515 1.00 25.10 ? 377 ASN A C 1 ATOM 1861 O O . ASN A 1 244 ? -9.995 -13.727 25.389 1.00 24.52 ? 377 ASN A O 1 ATOM 1862 C CB . ASN A 1 244 ? -7.172 -13.493 24.237 1.00 19.90 ? 377 ASN A CB 1 ATOM 1863 C CG . ASN A 1 244 ? -6.270 -13.284 25.427 1.00 26.90 ? 377 ASN A CG 1 ATOM 1864 O OD1 . ASN A 1 244 ? -6.741 -12.991 26.524 1.00 23.94 ? 377 ASN A OD1 1 ATOM 1865 N ND2 . ASN A 1 244 ? -4.963 -13.452 25.225 1.00 29.19 ? 377 ASN A ND2 1 ATOM 1866 N N . CYS A 1 245 ? -8.884 -15.263 26.606 1.00 21.56 ? 378 CYS A N 1 ATOM 1867 C CA . CYS A 1 245 ? -9.766 -15.179 27.765 1.00 25.26 ? 378 CYS A CA 1 ATOM 1868 C C . CYS A 1 245 ? -8.946 -14.789 28.992 1.00 24.48 ? 378 CYS A C 1 ATOM 1869 O O . CYS A 1 245 ? -8.090 -15.552 29.427 1.00 25.56 ? 378 CYS A O 1 ATOM 1870 C CB . CYS A 1 245 ? -10.442 -16.536 27.992 1.00 28.76 ? 378 CYS A CB 1 ATOM 1871 S SG . CYS A 1 245 ? -11.510 -16.653 29.448 1.00 36.50 ? 378 CYS A SG 1 ATOM 1872 N N . ARG A 1 246 ? -9.202 -13.598 29.534 1.00 25.98 ? 379 ARG A N 1 ATOM 1873 C CA . ARG A 1 246 ? -8.486 -13.101 30.713 1.00 23.54 ? 379 ARG A CA 1 ATOM 1874 C C . ARG A 1 246 ? -6.978 -13.072 30.499 1.00 26.65 ? 379 ARG A C 1 ATOM 1875 O O . ARG A 1 246 ? -6.214 -13.274 31.446 1.00 31.51 ? 379 ARG A O 1 ATOM 1876 C CB . ARG A 1 246 ? -8.787 -13.960 31.945 1.00 25.84 ? 379 ARG A CB 1 ATOM 1877 C CG . ARG A 1 246 ? -10.257 -14.214 32.193 1.00 36.91 ? 379 ARG A CG 1 ATOM 1878 C CD . ARG A 1 246 ? -11.023 -12.915 32.283 1.00 47.05 ? 379 ARG A CD 1 ATOM 1879 N NE . ARG A 1 246 ? -12.455 -13.144 32.452 1.00 61.00 ? 379 ARG A NE 1 ATOM 1880 C CZ . ARG A 1 246 ? -13.372 -12.183 32.416 1.00 63.76 ? 379 ARG A CZ 1 ATOM 1881 N NH1 . ARG A 1 246 ? -13.009 -10.924 32.214 1.00 59.18 ? 379 ARG A NH1 1 ATOM 1882 N NH2 . ARG A 1 246 ? -14.653 -12.483 32.579 1.00 70.03 ? 379 ARG A NH2 1 ATOM 1883 N N . GLY A 1 247 ? -6.551 -12.855 29.258 1.00 25.49 ? 380 GLY A N 1 ATOM 1884 C CA . GLY A 1 247 ? -5.135 -12.779 28.948 1.00 25.03 ? 380 GLY A CA 1 ATOM 1885 C C . GLY A 1 247 ? -4.515 -14.080 28.468 1.00 26.09 ? 380 GLY A C 1 ATOM 1886 O O . GLY A 1 247 ? -3.395 -14.083 27.953 1.00 26.03 ? 380 GLY A O 1 ATOM 1887 N N . GLU A 1 248 ? -5.241 -15.184 28.630 1.00 22.05 ? 381 GLU A N 1 ATOM 1888 C CA . GLU A 1 248 ? -4.743 -16.506 28.259 1.00 23.45 ? 381 GLU A CA 1 ATOM 1889 C C . GLU A 1 248 ? -5.257 -16.897 26.880 1.00 24.74 ? 381 GLU A C 1 ATOM 1890 O O . GLU A 1 248 ? -6.410 -16.624 26.541 1.00 21.02 ? 381 GLU A O 1 ATOM 1891 C CB . GLU A 1 248 ? -5.180 -17.545 29.295 1.00 26.99 ? 381 GLU A CB 1 ATOM 1892 C CG . GLU A 1 248 ? -4.857 -17.163 30.741 1.00 25.61 ? 381 GLU A CG 1 ATOM 1893 C CD . GLU A 1 248 ? -3.375 -17.273 31.050 1.00 28.99 ? 381 GLU A CD 1 ATOM 1894 O OE1 . GLU A 1 248 ? -2.670 -17.957 30.284 1.00 31.19 ? 381 GLU A OE1 1 ATOM 1895 O OE2 . GLU A 1 248 ? -2.917 -16.686 32.058 1.00 28.45 ? 381 GLU A OE2 1 ATOM 1896 N N . PHE A 1 249 ? -4.400 -17.531 26.084 1.00 21.55 ? 382 PHE A N 1 ATOM 1897 C CA . PHE A 1 249 ? -4.778 -17.930 24.729 1.00 23.60 ? 382 PHE A CA 1 ATOM 1898 C C . PHE A 1 249 ? -5.399 -19.320 24.688 1.00 22.97 ? 382 PHE A C 1 ATOM 1899 O O . PHE A 1 249 ? -4.713 -20.321 24.905 1.00 22.54 ? 382 PHE A O 1 ATOM 1900 C CB . PHE A 1 249 ? -3.575 -17.854 23.782 1.00 21.42 ? 382 PHE A CB 1 ATOM 1901 C CG . PHE A 1 249 ? -3.073 -16.451 23.555 1.00 17.92 ? 382 PHE A CG 1 ATOM 1902 C CD1 . PHE A 1 249 ? -3.636 -15.650 22.574 1.00 19.63 ? 382 PHE A CD1 1 ATOM 1903 C CD2 . PHE A 1 249 ? -2.040 -15.938 24.321 1.00 23.56 ? 382 PHE A CD2 1 ATOM 1904 C CE1 . PHE A 1 249 ? -3.176 -14.354 22.359 1.00 19.97 ? 382 PHE A CE1 1 ATOM 1905 C CE2 . PHE A 1 249 ? -1.581 -14.645 24.119 1.00 25.44 ? 382 PHE A CE2 1 ATOM 1906 C CZ . PHE A 1 249 ? -2.152 -13.852 23.134 1.00 24.37 ? 382 PHE A CZ 1 ATOM 1907 N N . PHE A 1 250 ? -6.701 -19.366 24.401 1.00 22.77 ? 383 PHE A N 1 ATOM 1908 C CA . PHE A 1 250 ? -7.444 -20.618 24.308 1.00 22.86 ? 383 PHE A CA 1 ATOM 1909 C C . PHE A 1 250 ? -7.482 -21.132 22.874 1.00 23.19 ? 383 PHE A C 1 ATOM 1910 O O . PHE A 1 250 ? -7.706 -20.366 21.938 1.00 23.38 ? 383 PHE A O 1 ATOM 1911 C CB . PHE A 1 250 ? -8.890 -20.426 24.788 1.00 22.88 ? 383 PHE A CB 1 ATOM 1912 C CG . PHE A 1 250 ? -9.057 -20.484 26.280 1.00 26.30 ? 383 PHE A CG 1 ATOM 1913 C CD1 . PHE A 1 250 ? -8.504 -19.510 27.093 1.00 27.17 ? 383 PHE A CD1 1 ATOM 1914 C CD2 . PHE A 1 250 ? -9.776 -21.511 26.868 1.00 30.88 ? 383 PHE A CD2 1 ATOM 1915 C CE1 . PHE A 1 250 ? -8.659 -19.563 28.474 1.00 28.17 ? 383 PHE A CE1 1 ATOM 1916 C CE2 . PHE A 1 250 ? -9.938 -21.567 28.247 1.00 33.92 ? 383 PHE A CE2 1 ATOM 1917 C CZ . PHE A 1 250 ? -9.378 -20.589 29.047 1.00 30.38 ? 383 PHE A CZ 1 ATOM 1918 N N . TYR A 1 251 ? -7.268 -22.434 22.716 1.00 21.24 ? 384 TYR A N 1 ATOM 1919 C CA . TYR A 1 251 ? -7.435 -23.107 21.431 1.00 22.17 ? 384 TYR A CA 1 ATOM 1920 C C . TYR A 1 251 ? -8.454 -24.223 21.608 1.00 23.87 ? 384 TYR A C 1 ATOM 1921 O O . TYR A 1 251 ? -8.207 -25.173 22.353 1.00 26.55 ? 384 TYR A O 1 ATOM 1922 C CB . TYR A 1 251 ? -6.112 -23.709 20.959 1.00 22.06 ? 384 TYR A CB 1 ATOM 1923 C CG . TYR A 1 251 ? -5.072 -22.697 20.529 1.00 20.79 ? 384 TYR A CG 1 ATOM 1924 C CD1 . TYR A 1 251 ? -4.558 -21.775 21.435 1.00 22.62 ? 384 TYR A CD1 1 ATOM 1925 C CD2 . TYR A 1 251 ? -4.596 -22.671 19.223 1.00 23.51 ? 384 TYR A CD2 1 ATOM 1926 C CE1 . TYR A 1 251 ? -3.602 -20.853 21.054 1.00 23.93 ? 384 TYR A CE1 1 ATOM 1927 C CE2 . TYR A 1 251 ? -3.634 -21.748 18.829 1.00 25.19 ? 384 TYR A CE2 1 ATOM 1928 C CZ . TYR A 1 251 ? -3.142 -20.844 19.753 1.00 26.59 ? 384 TYR A CZ 1 ATOM 1929 O OH . TYR A 1 251 ? -2.189 -19.919 19.383 1.00 27.49 ? 384 TYR A OH 1 ATOM 1930 N N . CYS A 1 252 ? -9.588 -24.117 20.922 1.00 24.45 ? 385 CYS A N 1 ATOM 1931 C CA . CYS A 1 252 ? -10.680 -25.072 21.111 1.00 24.18 ? 385 CYS A CA 1 ATOM 1932 C C . CYS A 1 252 ? -11.027 -25.833 19.844 1.00 27.22 ? 385 CYS A C 1 ATOM 1933 O O . CYS A 1 252 ? -11.172 -25.250 18.769 1.00 23.69 ? 385 CYS A O 1 ATOM 1934 C CB . CYS A 1 252 ? -11.927 -24.362 21.633 1.00 28.43 ? 385 CYS A CB 1 ATOM 1935 S SG . CYS A 1 252 ? -11.689 -23.550 23.219 1.00 33.89 ? 385 CYS A SG 1 ATOM 1936 N N . ASN A 1 253 ? -11.171 -27.145 19.990 1.00 22.38 ? 386 ASN A N 1 ATOM 1937 C CA . ASN A 1 253 ? -11.506 -28.022 18.881 1.00 25.56 ? 386 ASN A CA 1 ATOM 1938 C C . ASN A 1 253 ? -12.999 -27.960 18.568 1.00 22.00 ? 386 ASN A C 1 ATOM 1939 O O . ASN A 1 253 ? -13.825 -28.351 19.390 1.00 23.73 ? 386 ASN A O 1 ATOM 1940 C CB . ASN A 1 253 ? -11.087 -29.449 19.229 1.00 27.65 ? 386 ASN A CB 1 ATOM 1941 C CG . ASN A 1 253 ? -11.170 -30.385 18.047 1.00 30.17 ? 386 ASN A CG 1 ATOM 1942 O OD1 . ASN A 1 253 ? -12.150 -30.376 17.300 1.00 30.28 ? 386 ASN A OD1 1 ATOM 1943 N ND2 . ASN A 1 253 ? -10.127 -31.191 17.860 1.00 37.91 ? 386 ASN A ND2 1 ATOM 1944 N N . THR A 1 254 ? -13.342 -27.478 17.378 1.00 24.71 ? 387 THR A N 1 ATOM 1945 C CA . THR A 1 254 ? -14.741 -27.247 17.020 1.00 25.17 ? 387 THR A CA 1 ATOM 1946 C C . THR A 1 254 ? -15.368 -28.359 16.170 1.00 26.63 ? 387 THR A C 1 ATOM 1947 O O . THR A 1 254 ? -16.445 -28.179 15.609 1.00 27.26 ? 387 THR A O 1 ATOM 1948 C CB . THR A 1 254 ? -14.908 -25.903 16.287 1.00 26.71 ? 387 THR A CB 1 ATOM 1949 O OG1 . THR A 1 254 ? -14.104 -25.899 15.101 1.00 28.10 ? 387 THR A OG1 1 ATOM 1950 C CG2 . THR A 1 254 ? -14.473 -24.755 17.189 1.00 26.01 ? 387 THR A CG2 1 ATOM 1951 N N . THR A 1 255 ? -14.702 -29.503 16.080 1.00 26.39 ? 388 THR A N 1 ATOM 1952 C CA . THR A 1 255 ? -15.234 -30.626 15.305 1.00 35.97 ? 388 THR A CA 1 ATOM 1953 C C . THR A 1 255 ? -16.707 -30.895 15.628 1.00 36.89 ? 388 THR A C 1 ATOM 1954 O O . THR A 1 255 ? -17.529 -31.046 14.723 1.00 34.67 ? 388 THR A O 1 ATOM 1955 C CB . THR A 1 255 ? -14.415 -31.912 15.536 1.00 38.46 ? 388 THR A CB 1 ATOM 1956 O OG1 . THR A 1 255 ? -13.164 -31.815 14.844 1.00 41.65 ? 388 THR A OG1 1 ATOM 1957 C CG2 . THR A 1 255 ? -15.167 -33.128 15.019 1.00 43.58 ? 388 THR A CG2 1 ATOM 1958 N N . GLN A 1 256 ? -17.035 -30.940 16.918 1.00 35.12 ? 389 GLN A N 1 ATOM 1959 C CA . GLN A 1 256 ? -18.388 -31.258 17.369 1.00 36.34 ? 389 GLN A CA 1 ATOM 1960 C C . GLN A 1 256 ? -19.408 -30.176 17.039 1.00 36.89 ? 389 GLN A C 1 ATOM 1961 O O . GLN A 1 256 ? -20.609 -30.446 17.003 1.00 39.41 ? 389 GLN A O 1 ATOM 1962 C CB . GLN A 1 256 ? -18.409 -31.504 18.879 1.00 37.11 ? 389 GLN A CB 1 ATOM 1963 C CG . GLN A 1 256 ? -17.604 -32.703 19.346 1.00 47.79 ? 389 GLN A CG 1 ATOM 1964 C CD . GLN A 1 256 ? -17.561 -32.816 20.858 1.00 53.21 ? 389 GLN A CD 1 ATOM 1965 O OE1 . GLN A 1 256 ? -18.479 -33.348 21.479 1.00 52.04 ? 389 GLN A OE1 1 ATOM 1966 N NE2 . GLN A 1 256 ? -16.492 -32.309 21.457 1.00 50.96 ? 389 GLN A NE2 1 ATOM 1967 N N . LEU A 1 257 ? -18.941 -28.952 16.814 1.00 27.85 ? 390 LEU A N 1 ATOM 1968 C CA . LEU A 1 257 ? -19.855 -27.850 16.534 1.00 30.79 ? 390 LEU A CA 1 ATOM 1969 C C . LEU A 1 257 ? -20.439 -27.956 15.134 1.00 36.57 ? 390 LEU A C 1 ATOM 1970 O O . LEU A 1 257 ? -21.583 -27.577 14.900 1.00 47.55 ? 390 LEU A O 1 ATOM 1971 C CB . LEU A 1 257 ? -19.158 -26.500 16.705 1.00 36.30 ? 390 LEU A CB 1 ATOM 1972 C CG . LEU A 1 257 ? -18.996 -25.959 18.123 1.00 40.97 ? 390 LEU A CG 1 ATOM 1973 C CD1 . LEU A 1 257 ? -18.523 -24.513 18.080 1.00 34.52 ? 390 LEU A CD1 1 ATOM 1974 C CD2 . LEU A 1 257 ? -20.308 -26.062 18.884 1.00 43.77 ? 390 LEU A CD2 1 ATOM 1975 N N . PHE A 1 258 ? -19.647 -28.480 14.208 1.00 26.91 ? 391 PHE A N 1 ATOM 1976 C CA . PHE A 1 258 ? -20.061 -28.545 12.818 1.00 35.66 ? 391 PHE A CA 1 ATOM 1977 C C . PHE A 1 258 ? -20.369 -29.983 12.427 1.00 38.09 ? 391 PHE A C 1 ATOM 1978 O O . PHE A 1 258 ? -19.745 -30.558 11.535 1.00 40.76 ? 391 PHE A O 1 ATOM 1979 C CB . PHE A 1 258 ? -19.000 -27.891 11.933 1.00 35.48 ? 391 PHE A CB 1 ATOM 1980 C CG . PHE A 1 258 ? -18.723 -26.455 12.310 1.00 33.38 ? 391 PHE A CG 1 ATOM 1981 C CD1 . PHE A 1 258 ? -19.555 -25.438 11.872 1.00 32.87 ? 391 PHE A CD1 1 ATOM 1982 C CD2 . PHE A 1 258 ? -17.657 -26.129 13.133 1.00 29.29 ? 391 PHE A CD2 1 ATOM 1983 C CE1 . PHE A 1 258 ? -19.319 -24.118 12.232 1.00 25.30 ? 391 PHE A CE1 1 ATOM 1984 C CE2 . PHE A 1 258 ? -17.418 -24.810 13.497 1.00 27.18 ? 391 PHE A CE2 1 ATOM 1985 C CZ . PHE A 1 258 ? -18.250 -23.808 13.047 1.00 25.09 ? 391 PHE A CZ 1 ATOM 1986 N N . ASN A 1 259 ? -21.351 -30.543 13.125 1.00 41.45 ? 392 ASN A N 1 ATOM 1987 C CA . ASN A 1 259 ? -21.744 -31.935 12.965 1.00 48.70 ? 392 ASN A CA 1 ATOM 1988 C C . ASN A 1 259 ? -22.932 -32.065 12.019 1.00 46.66 ? 392 ASN A C 1 ATOM 1989 O O . ASN A 1 259 ? -24.042 -31.638 12.340 1.00 42.09 ? 392 ASN A O 1 ATOM 1990 C CB . ASN A 1 259 ? -22.091 -32.526 14.333 1.00 56.24 ? 392 ASN A CB 1 ATOM 1991 C CG . ASN A 1 259 ? -22.069 -34.043 14.343 1.00 67.00 ? 392 ASN A CG 1 ATOM 1992 O OD1 . ASN A 1 259 ? -22.568 -34.693 13.424 1.00 65.52 ? 392 ASN A OD1 1 ATOM 1993 N ND2 . ASN A 1 259 ? -21.475 -34.615 15.386 1.00 77.39 ? 392 ASN A ND2 1 ATOM 1994 N N . ASN A 1 260 ? -22.693 -32.658 10.852 1.00 44.99 ? 393 ASN A N 1 ATOM 1995 C CA . ASN A 1 260 ? -23.733 -32.815 9.840 1.00 48.76 ? 393 ASN A CA 1 ATOM 1996 C C . ASN A 1 260 ? -24.906 -33.671 10.311 1.00 51.66 ? 393 ASN A C 1 ATOM 1997 O O . ASN A 1 260 ? -26.043 -33.479 9.875 1.00 49.95 ? 393 ASN A O 1 ATOM 1998 C CB . ASN A 1 260 ? -23.145 -33.404 8.557 1.00 47.53 ? 393 ASN A CB 1 ATOM 1999 C CG . ASN A 1 260 ? -22.001 -32.577 8.011 1.00 41.70 ? 393 ASN A CG 1 ATOM 2000 O OD1 . ASN A 1 260 ? -22.210 -31.487 7.485 1.00 37.10 ? 393 ASN A OD1 1 ATOM 2001 N ND2 . ASN A 1 260 ? -20.784 -33.094 8.129 1.00 40.29 ? 393 ASN A ND2 1 ATOM 2002 N N . THR A 1 261 ? -24.622 -34.616 11.201 1.00 51.66 ? 394 THR A N 1 ATOM 2003 C CA . THR A 1 261 ? -25.641 -35.533 11.701 1.00 52.65 ? 394 THR A CA 1 ATOM 2004 C C . THR A 1 261 ? -26.778 -34.792 12.396 1.00 50.90 ? 394 THR A C 1 ATOM 2005 O O . THR A 1 261 ? -27.953 -35.098 12.184 1.00 49.46 ? 394 THR A O 1 ATOM 2006 C CB . THR A 1 261 ? -25.038 -36.560 12.681 1.00 58.50 ? 394 THR A CB 1 ATOM 2007 O OG1 . THR A 1 261 ? -23.929 -37.223 12.061 1.00 58.01 ? 394 THR A OG1 1 ATOM 2008 C CG2 . THR A 1 261 ? -26.083 -37.591 13.084 1.00 60.54 ? 394 THR A CG2 1 ATOM 2009 N N . CYS A 1 262 ? -26.420 -33.816 13.225 1.00 49.22 ? 395 CYS A N 1 ATOM 2010 C CA . CYS A 1 262 ? -27.400 -33.063 14.004 1.00 57.20 ? 395 CYS A CA 1 ATOM 2011 C C . CYS A 1 262 ? -28.215 -32.090 13.143 1.00 61.21 ? 395 CYS A C 1 ATOM 2012 O O . CYS A 1 262 ? -29.089 -31.385 13.650 1.00 62.43 ? 395 CYS A O 1 ATOM 2013 C CB . CYS A 1 262 ? -26.707 -32.306 15.143 1.00 57.28 ? 395 CYS A CB 1 ATOM 2014 S SG . CYS A 1 262 ? -25.514 -33.304 16.085 1.00 77.83 ? 395 CYS A SG 1 ATOM 2015 N N . ILE A 1 263 ? -27.921 -32.046 11.847 1.00 60.76 ? 396 ILE A N 1 ATOM 2016 C CA . ILE A 1 263 ? -28.683 -31.215 10.917 1.00 62.30 ? 396 ILE A CA 1 ATOM 2017 C C . ILE A 1 263 ? -29.811 -32.009 10.258 1.00 67.15 ? 396 ILE A C 1 ATOM 2018 O O . ILE A 1 263 ? -29.597 -32.713 9.270 1.00 67.95 ? 396 ILE A O 1 ATOM 2019 C CB . ILE A 1 263 ? -27.781 -30.602 9.821 1.00 66.62 ? 396 ILE A CB 1 ATOM 2020 C CG1 . ILE A 1 263 ? -26.704 -29.715 10.449 1.00 63.76 ? 396 ILE A CG1 1 ATOM 2021 C CG2 . ILE A 1 263 ? -28.615 -29.798 8.828 1.00 69.85 ? 396 ILE A CG2 1 ATOM 2022 C CD1 . ILE A 1 263 ? -25.593 -29.319 9.492 1.00 64.46 ? 396 ILE A CD1 1 ATOM 2023 N N . ASN A 1 272 ? -28.841 -32.659 20.941 1.00 62.47 ? 411 ASN A N 1 ATOM 2024 C CA . ASN A 1 272 ? -29.668 -31.779 21.757 1.00 65.27 ? 411 ASN A CA 1 ATOM 2025 C C . ASN A 1 272 ? -29.162 -31.650 23.191 1.00 60.68 ? 411 ASN A C 1 ATOM 2026 O O . ASN A 1 272 ? -29.765 -30.951 24.009 1.00 65.13 ? 411 ASN A O 1 ATOM 2027 C CB . ASN A 1 272 ? -31.129 -32.243 21.743 1.00 73.99 ? 411 ASN A CB 1 ATOM 2028 C CG . ASN A 1 272 ? -31.922 -31.646 20.593 1.00 80.19 ? 411 ASN A CG 1 ATOM 2029 O OD1 . ASN A 1 272 ? -32.916 -30.951 20.804 1.00 82.69 ? 411 ASN A OD1 1 ATOM 2030 N ND2 . ASN A 1 272 ? -31.480 -31.911 19.370 1.00 81.46 ? 411 ASN A ND2 1 ATOM 2031 N N . GLY A 1 273 ? -28.052 -32.320 23.490 1.00 51.41 ? 412 GLY A N 1 ATOM 2032 C CA . GLY A 1 273 ? -27.471 -32.249 24.817 1.00 48.85 ? 412 GLY A CA 1 ATOM 2033 C C . GLY A 1 273 ? -26.445 -31.138 24.896 1.00 47.99 ? 412 GLY A C 1 ATOM 2034 O O . GLY A 1 273 ? -26.404 -30.264 24.033 1.00 45.97 ? 412 GLY A O 1 ATOM 2035 N N . THR A 1 274 ? -25.620 -31.158 25.937 1.00 42.12 ? 413 THR A N 1 ATOM 2036 C CA . THR A 1 274 ? -24.530 -30.200 26.034 1.00 37.99 ? 413 THR A CA 1 ATOM 2037 C C . THR A 1 274 ? -23.373 -30.648 25.152 1.00 39.42 ? 413 THR A C 1 ATOM 2038 O O . THR A 1 274 ? -22.944 -31.800 25.209 1.00 44.08 ? 413 THR A O 1 ATOM 2039 C CB . THR A 1 274 ? -24.027 -30.041 27.477 1.00 42.86 ? 413 THR A CB 1 ATOM 2040 O OG1 . THR A 1 274 ? -25.078 -29.516 28.295 1.00 44.26 ? 413 THR A OG1 1 ATOM 2041 C CG2 . THR A 1 274 ? -22.840 -29.087 27.522 1.00 43.80 ? 413 THR A CG2 1 ATOM 2042 N N . ILE A 1 275 ? -22.884 -29.734 24.326 1.00 40.08 ? 414 ILE A N 1 ATOM 2043 C CA . ILE A 1 275 ? -21.697 -29.985 23.528 1.00 39.43 ? 414 ILE A CA 1 ATOM 2044 C C . ILE A 1 275 ? -20.498 -29.412 24.265 1.00 33.49 ? 414 ILE A C 1 ATOM 2045 O O . ILE A 1 275 ? -20.454 -28.220 24.548 1.00 35.22 ? 414 ILE A O 1 ATOM 2046 C CB . ILE A 1 275 ? -21.811 -29.328 22.145 1.00 35.68 ? 414 ILE A CB 1 ATOM 2047 C CG1 . ILE A 1 275 ? -23.011 -29.902 21.389 1.00 35.91 ? 414 ILE A CG1 1 ATOM 2048 C CG2 . ILE A 1 275 ? -20.520 -29.516 21.351 1.00 38.41 ? 414 ILE A CG2 1 ATOM 2049 C CD1 . ILE A 1 275 ? -23.335 -29.162 20.111 1.00 35.37 ? 414 ILE A CD1 1 ATOM 2050 N N . THR A 1 276 ? -19.535 -30.266 24.596 1.00 35.52 ? 415 THR A N 1 ATOM 2051 C CA . THR A 1 276 ? -18.327 -29.814 25.278 1.00 36.73 ? 415 THR A CA 1 ATOM 2052 C C . THR A 1 276 ? -17.114 -29.955 24.365 1.00 33.79 ? 415 THR A C 1 ATOM 2053 O O . THR A 1 276 ? -16.724 -31.066 24.016 1.00 37.59 ? 415 THR A O 1 ATOM 2054 C CB . THR A 1 276 ? -18.072 -30.611 26.574 1.00 41.01 ? 415 THR A CB 1 ATOM 2055 O OG1 . THR A 1 276 ? -19.154 -30.412 27.492 1.00 42.04 ? 415 THR A OG1 1 ATOM 2056 C CG2 . THR A 1 276 ? -16.775 -30.154 27.222 1.00 44.03 ? 415 THR A CG2 1 ATOM 2057 N N . LEU A 1 277 ? -16.529 -28.828 23.974 1.00 33.31 ? 416 LEU A N 1 ATOM 2058 C CA . LEU A 1 277 ? -15.343 -28.837 23.125 1.00 29.62 ? 416 LEU A CA 1 ATOM 2059 C C . LEU A 1 277 ? -14.088 -28.917 23.980 1.00 31.03 ? 416 LEU A C 1 ATOM 2060 O O . LEU A 1 277 ? -13.956 -28.184 24.956 1.00 28.88 ? 416 LEU A O 1 ATOM 2061 C CB . LEU A 1 277 ? -15.283 -27.568 22.274 1.00 28.15 ? 416 LEU A CB 1 ATOM 2062 C CG . LEU A 1 277 ? -16.577 -27.139 21.584 1.00 29.78 ? 416 LEU A CG 1 ATOM 2063 C CD1 . LEU A 1 277 ? -16.373 -25.808 20.892 1.00 25.35 ? 416 LEU A CD1 1 ATOM 2064 C CD2 . LEU A 1 277 ? -17.042 -28.201 20.596 1.00 29.96 ? 416 LEU A CD2 1 ATOM 2065 N N . PRO A 1 278 ? -13.159 -29.811 23.617 1.00 29.56 ? 417 PRO A N 1 ATOM 2066 C CA . PRO A 1 278 ? -11.883 -29.843 24.335 1.00 31.22 ? 417 PRO A CA 1 ATOM 2067 C C . PRO A 1 278 ? -11.015 -28.664 23.909 1.00 29.10 ? 417 PRO A C 1 ATOM 2068 O O . PRO A 1 278 ? -10.914 -28.358 22.715 1.00 26.75 ? 417 PRO A O 1 ATOM 2069 C CB . PRO A 1 278 ? -11.264 -31.166 23.886 1.00 32.24 ? 417 PRO A CB 1 ATOM 2070 C CG . PRO A 1 278 ? -11.832 -31.401 22.533 1.00 33.89 ? 417 PRO A CG 1 ATOM 2071 C CD . PRO A 1 278 ? -13.227 -30.828 22.554 1.00 32.44 ? 417 PRO A CD 1 ATOM 2072 N N . CYS A 1 279 ? -10.415 -27.996 24.886 1.00 29.10 ? 418 CYS A N 1 ATOM 2073 C CA . CYS A 1 279 ? -9.588 -26.830 24.618 1.00 28.54 ? 418 CYS A CA 1 ATOM 2074 C C . CYS A 1 279 ? -8.234 -26.973 25.283 1.00 26.72 ? 418 CYS A C 1 ATOM 2075 O O . CYS A 1 279 ? -8.040 -27.815 26.155 1.00 24.50 ? 418 CYS A O 1 ATOM 2076 C CB . CYS A 1 279 ? -10.258 -25.557 25.139 1.00 33.44 ? 418 CYS A CB 1 ATOM 2077 S SG . CYS A 1 279 ? -11.862 -25.187 24.423 1.00 34.51 ? 418 CYS A SG 1 ATOM 2078 N N . LYS A 1 280 ? -7.299 -26.137 24.857 1.00 25.37 ? 419 LYS A N 1 ATOM 2079 C CA . LYS A 1 280 ? -6.001 -26.054 25.493 1.00 26.58 ? 419 LYS A CA 1 ATOM 2080 C C . LYS A 1 280 ? -5.531 -24.609 25.517 1.00 29.45 ? 419 LYS A C 1 ATOM 2081 O O . LYS A 1 280 ? -5.706 -23.872 24.544 1.00 26.16 ? 419 LYS A O 1 ATOM 2082 C CB . LYS A 1 280 ? -4.994 -26.916 24.738 1.00 34.91 ? 419 LYS A CB 1 ATOM 2083 C CG . LYS A 1 280 ? -3.552 -26.578 25.037 1.00 42.86 ? 419 LYS A CG 1 ATOM 2084 C CD . LYS A 1 280 ? -2.605 -27.626 24.477 1.00 47.76 ? 419 LYS A CD 1 ATOM 2085 C CE . LYS A 1 280 ? -1.207 -27.058 24.340 1.00 44.82 ? 419 LYS A CE 1 ATOM 2086 N NZ . LYS A 1 280 ? -0.853 -26.194 25.498 1.00 29.42 ? 419 LYS A NZ 1 ATOM 2087 N N . ILE A 1 281 ? -4.952 -24.198 26.638 1.00 25.15 ? 420 ILE A N 1 ATOM 2088 C CA . ILE A 1 281 ? -4.299 -22.903 26.709 1.00 20.56 ? 420 ILE A CA 1 ATOM 2089 C C . ILE A 1 281 ? -2.887 -23.072 26.172 1.00 26.37 ? 420 ILE A C 1 ATOM 2090 O O . ILE A 1 281 ? -2.144 -23.933 26.639 1.00 31.51 ? 420 ILE A O 1 ATOM 2091 C CB . ILE A 1 281 ? -4.239 -22.378 28.152 1.00 26.08 ? 420 ILE A CB 1 ATOM 2092 C CG1 . ILE A 1 281 ? -5.654 -22.173 28.702 1.00 27.63 ? 420 ILE A CG1 1 ATOM 2093 C CG2 . ILE A 1 281 ? -3.428 -21.090 28.212 1.00 22.84 ? 420 ILE A CG2 1 ATOM 2094 C CD1 . ILE A 1 281 ? -5.705 -21.815 30.169 1.00 30.38 ? 420 ILE A CD1 1 ATOM 2095 N N . LYS A 1 282 ? -2.522 -22.271 25.177 1.00 26.41 ? 421 LYS A N 1 ATOM 2096 C CA . LYS A 1 282 ? -1.189 -22.354 24.591 1.00 28.38 ? 421 LYS A CA 1 ATOM 2097 C C . LYS A 1 282 ? -0.327 -21.173 25.010 1.00 24.90 ? 421 LYS A C 1 ATOM 2098 O O . LYS A 1 282 ? -0.805 -20.047 25.091 1.00 24.89 ? 421 LYS A O 1 ATOM 2099 C CB . LYS A 1 282 ? -1.262 -22.426 23.064 1.00 29.63 ? 421 LYS A CB 1 ATOM 2100 C CG . LYS A 1 282 ? -1.513 -23.827 22.520 1.00 30.63 ? 421 LYS A CG 1 ATOM 2101 C CD . LYS A 1 282 ? -1.495 -23.839 20.997 1.00 31.32 ? 421 LYS A CD 1 ATOM 2102 C CE . LYS A 1 282 ? -0.236 -24.492 20.447 1.00 37.07 ? 421 LYS A CE 1 ATOM 2103 N NZ . LYS A 1 282 ? 1.020 -23.864 20.927 1.00 38.50 ? 421 LYS A NZ 1 ATOM 2104 N N . GLN A 1 283 ? 0.950 -21.444 25.257 1.00 23.87 ? 422 GLN A N 1 ATOM 2105 C CA . GLN A 1 283 ? 1.914 -20.408 25.598 1.00 24.04 ? 422 GLN A CA 1 ATOM 2106 C C . GLN A 1 283 ? 2.620 -19.890 24.350 1.00 22.86 ? 422 GLN A C 1 ATOM 2107 O O . GLN A 1 283 ? 2.972 -18.718 24.268 1.00 28.92 ? 422 GLN A O 1 ATOM 2108 C CB . GLN A 1 283 ? 2.949 -20.942 26.589 1.00 22.66 ? 422 GLN A CB 1 ATOM 2109 C CG . GLN A 1 283 ? 2.396 -21.245 27.970 1.00 24.82 ? 422 GLN A CG 1 ATOM 2110 C CD . GLN A 1 283 ? 3.397 -21.970 28.848 1.00 32.81 ? 422 GLN A CD 1 ATOM 2111 O OE1 . GLN A 1 283 ? 3.132 -23.068 29.330 1.00 38.64 ? 422 GLN A OE1 1 ATOM 2112 N NE2 . GLN A 1 283 ? 4.556 -21.359 29.054 1.00 29.08 ? 422 GLN A NE2 1 ATOM 2113 N N . ILE A 1 284 ? 2.829 -20.777 23.384 1.00 22.26 ? 423 ILE A N 1 ATOM 2114 C CA . ILE A 1 284 ? 3.487 -20.417 22.135 1.00 20.62 ? 423 ILE A CA 1 ATOM 2115 C C . ILE A 1 284 ? 2.449 -20.187 21.043 1.00 27.10 ? 423 ILE A C 1 ATOM 2116 O O . ILE A 1 284 ? 1.650 -21.068 20.742 1.00 27.07 ? 423 ILE A O 1 ATOM 2117 C CB . ILE A 1 284 ? 4.484 -21.500 21.691 1.00 24.61 ? 423 ILE A CB 1 ATOM 2118 C CG1 . ILE A 1 284 ? 5.510 -21.753 22.795 1.00 26.28 ? 423 ILE A CG1 1 ATOM 2119 C CG2 . ILE A 1 284 ? 5.173 -21.094 20.400 1.00 29.89 ? 423 ILE A CG2 1 ATOM 2120 C CD1 . ILE A 1 284 ? 6.438 -22.912 22.512 1.00 30.42 ? 423 ILE A CD1 1 ATOM 2121 N N . ILE A 1 285 ? 2.465 -18.995 20.460 1.00 26.12 ? 424 ILE A N 1 ATOM 2122 C CA . ILE A 1 285 ? 1.423 -18.578 19.535 1.00 29.24 ? 424 ILE A CA 1 ATOM 2123 C C . ILE A 1 285 ? 1.954 -18.031 18.216 1.00 25.78 ? 424 ILE A C 1 ATOM 2124 O O . ILE A 1 285 ? 2.999 -17.390 18.174 1.00 28.46 ? 424 ILE A O 1 ATOM 2125 C CB . ILE A 1 285 ? 0.553 -17.477 20.171 1.00 35.53 ? 424 ILE A CB 1 ATOM 2126 C CG1 . ILE A 1 285 ? 0.166 -17.859 21.600 1.00 40.81 ? 424 ILE A CG1 1 ATOM 2127 C CG2 . ILE A 1 285 ? -0.678 -17.207 19.322 1.00 43.15 ? 424 ILE A CG2 1 ATOM 2128 C CD1 . ILE A 1 285 ? -0.741 -19.062 21.684 1.00 44.08 ? 424 ILE A CD1 1 ATOM 2129 N N . ASN A 1 286 ? 1.210 -18.276 17.144 1.00 20.76 ? 425 ASN A N 1 ATOM 2130 C CA . ASN A 1 286 ? 1.450 -17.618 15.871 1.00 22.41 ? 425 ASN A CA 1 ATOM 2131 C C . ASN A 1 286 ? 0.678 -16.311 15.890 1.00 22.39 ? 425 ASN A C 1 ATOM 2132 O O . ASN A 1 286 ? -0.547 -16.311 15.973 1.00 21.55 ? 425 ASN A O 1 ATOM 2133 C CB . ASN A 1 286 ? 0.977 -18.486 14.708 1.00 23.84 ? 425 ASN A CB 1 ATOM 2134 C CG . ASN A 1 286 ? 1.912 -19.640 14.425 1.00 31.08 ? 425 ASN A CG 1 ATOM 2135 O OD1 . ASN A 1 286 ? 3.115 -19.453 14.264 1.00 27.52 ? 425 ASN A OD1 1 ATOM 2136 N ND2 . ASN A 1 286 ? 1.361 -20.842 14.364 1.00 27.04 ? 425 ASN A ND2 1 ATOM 2137 N N . MET A 1 287 ? 1.393 -15.197 15.835 1.00 20.32 ? 426 MET A N 1 ATOM 2138 C CA . MET A 1 287 ? 0.759 -13.899 16.029 1.00 20.43 ? 426 MET A CA 1 ATOM 2139 C C . MET A 1 287 ? -0.161 -13.506 14.879 1.00 22.42 ? 426 MET A C 1 ATOM 2140 O O . MET A 1 287 ? 0.209 -13.626 13.719 1.00 22.39 ? 426 MET A O 1 ATOM 2141 C CB . MET A 1 287 ? 1.813 -12.825 16.279 1.00 19.61 ? 426 MET A CB 1 ATOM 2142 C CG . MET A 1 287 ? 2.514 -12.957 17.634 1.00 23.40 ? 426 MET A CG 1 ATOM 2143 S SD . MET A 1 287 ? 3.697 -11.636 17.769 1.00 31.70 ? 426 MET A SD 1 ATOM 2144 C CE . MET A 1 287 ? 2.573 -10.263 17.875 1.00 77.45 ? 426 MET A CE 1 ATOM 2145 N N . TRP A 1 288 ? -1.368 -13.048 15.214 1.00 20.77 ? 427 TRP A N 1 ATOM 2146 C CA . TRP A 1 288 ? -2.334 -12.634 14.196 1.00 19.49 ? 427 TRP A CA 1 ATOM 2147 C C . TRP A 1 288 ? -1.861 -11.404 13.429 1.00 17.80 ? 427 TRP A C 1 ATOM 2148 O O . TRP A 1 288 ? -2.375 -11.088 12.350 1.00 20.40 ? 427 TRP A O 1 ATOM 2149 C CB . TRP A 1 288 ? -3.720 -12.388 14.804 1.00 17.18 ? 427 TRP A CB 1 ATOM 2150 C CG . TRP A 1 288 ? -3.758 -11.351 15.899 1.00 20.38 ? 427 TRP A CG 1 ATOM 2151 C CD1 . TRP A 1 288 ? -3.650 -11.574 17.243 1.00 20.41 ? 427 TRP A CD1 1 ATOM 2152 C CD2 . TRP A 1 288 ? -3.936 -9.939 15.740 1.00 20.71 ? 427 TRP A CD2 1 ATOM 2153 N NE1 . TRP A 1 288 ? -3.741 -10.389 17.928 1.00 18.22 ? 427 TRP A NE1 1 ATOM 2154 C CE2 . TRP A 1 288 ? -3.911 -9.369 17.030 1.00 21.26 ? 427 TRP A CE2 1 ATOM 2155 C CE3 . TRP A 1 288 ? -4.102 -9.101 14.633 1.00 21.46 ? 427 TRP A CE3 1 ATOM 2156 C CZ2 . TRP A 1 288 ? -4.056 -7.998 17.242 1.00 22.56 ? 427 TRP A CZ2 1 ATOM 2157 C CZ3 . TRP A 1 288 ? -4.243 -7.739 14.845 1.00 25.09 ? 427 TRP A CZ3 1 ATOM 2158 C CH2 . TRP A 1 288 ? -4.214 -7.200 16.140 1.00 24.00 ? 427 TRP A CH2 1 ATOM 2159 N N . GLN A 1 289 ? -0.885 -10.707 13.992 1.00 17.54 ? 428 GLN A N 1 ATOM 2160 C CA . GLN A 1 289 ? -0.292 -9.564 13.316 1.00 18.55 ? 428 GLN A CA 1 ATOM 2161 C C . GLN A 1 289 ? 0.558 -10.021 12.127 1.00 22.64 ? 428 GLN A C 1 ATOM 2162 O O . GLN A 1 289 ? 0.964 -9.209 11.291 1.00 24.42 ? 428 GLN A O 1 ATOM 2163 C CB . GLN A 1 289 ? 0.538 -8.716 14.289 1.00 21.30 ? 428 GLN A CB 1 ATOM 2164 C CG . GLN A 1 289 ? -0.249 -8.141 15.468 1.00 24.22 ? 428 GLN A CG 1 ATOM 2165 C CD . GLN A 1 289 ? -0.190 -9.021 16.710 1.00 26.19 ? 428 GLN A CD 1 ATOM 2166 O OE1 . GLN A 1 289 ? -0.330 -10.237 16.630 1.00 22.20 ? 428 GLN A OE1 1 ATOM 2167 N NE2 . GLN A 1 289 ? 0.028 -8.402 17.866 1.00 26.01 ? 428 GLN A NE2 1 ATOM 2168 N N . GLY A 1 290 ? 0.814 -11.322 12.053 1.00 22.40 ? 429 GLY A N 1 ATOM 2169 C CA . GLY A 1 290 ? 1.539 -11.906 10.937 1.00 26.28 ? 429 GLY A CA 1 ATOM 2170 C C . GLY A 1 290 ? 3.044 -11.774 11.063 1.00 29.30 ? 429 GLY A C 1 ATOM 2171 O O . GLY A 1 290 ? 3.779 -12.023 10.110 1.00 31.32 ? 429 GLY A O 1 ATOM 2172 N N . THR A 1 291 ? 3.503 -11.409 12.254 1.00 23.94 ? 430 THR A N 1 ATOM 2173 C CA . THR A 1 291 ? 4.908 -11.070 12.471 1.00 25.50 ? 430 THR A CA 1 ATOM 2174 C C . THR A 1 291 ? 5.795 -12.204 12.993 1.00 30.33 ? 430 THR A C 1 ATOM 2175 O O . THR A 1 291 ? 7.005 -12.025 13.122 1.00 32.74 ? 430 THR A O 1 ATOM 2176 C CB . THR A 1 291 ? 5.034 -9.884 13.435 1.00 29.53 ? 430 THR A CB 1 ATOM 2177 O OG1 . THR A 1 291 ? 4.194 -10.115 14.572 1.00 33.47 ? 430 THR A OG1 1 ATOM 2178 C CG2 . THR A 1 291 ? 4.599 -8.596 12.747 1.00 33.13 ? 430 THR A CG2 1 ATOM 2179 N N . GLY A 1 292 ? 5.208 -13.355 13.303 1.00 24.32 ? 431 GLY A N 1 ATOM 2180 C CA . GLY A 1 292 ? 5.989 -14.488 13.784 1.00 26.80 ? 431 GLY A CA 1 ATOM 2181 C C . GLY A 1 292 ? 5.401 -15.183 14.998 1.00 26.39 ? 431 GLY A C 1 ATOM 2182 O O . GLY A 1 292 ? 4.180 -15.286 15.125 1.00 24.79 ? 431 GLY A O 1 ATOM 2183 N N . GLN A 1 293 ? 6.265 -15.662 15.891 1.00 25.81 ? 432 GLN A N 1 ATOM 2184 C CA . GLN A 1 293 ? 5.806 -16.398 17.071 1.00 28.81 ? 432 GLN A CA 1 ATOM 2185 C C . GLN A 1 293 ? 6.030 -15.636 18.369 1.00 29.81 ? 432 GLN A C 1 ATOM 2186 O O . GLN A 1 293 ? 6.979 -14.868 18.488 1.00 33.88 ? 432 GLN A O 1 ATOM 2187 C CB . GLN A 1 293 ? 6.475 -17.774 17.166 1.00 25.45 ? 432 GLN A CB 1 ATOM 2188 C CG . GLN A 1 293 ? 6.030 -18.765 16.098 1.00 29.22 ? 432 GLN A CG 1 ATOM 2189 C CD . GLN A 1 293 ? 6.603 -18.451 14.739 1.00 42.40 ? 432 GLN A CD 1 ATOM 2190 O OE1 . GLN A 1 293 ? 7.813 -18.310 14.582 1.00 48.20 ? 432 GLN A OE1 1 ATOM 2191 N NE2 . GLN A 1 293 ? 5.736 -18.343 13.743 1.00 42.56 ? 432 GLN A NE2 1 ATOM 2192 N N . ALA A 1 294 ? 5.144 -15.853 19.335 1.00 28.12 ? 433 ALA A N 1 ATOM 2193 C CA . ALA A 1 294 ? 5.254 -15.223 20.641 1.00 27.17 ? 433 ALA A CA 1 ATOM 2194 C C . ALA A 1 294 ? 5.059 -16.284 21.723 1.00 29.81 ? 433 ALA A C 1 ATOM 2195 O O . ALA A 1 294 ? 4.151 -17.119 21.637 1.00 30.94 ? 433 ALA A O 1 ATOM 2196 C CB . ALA A 1 294 ? 4.221 -14.115 20.778 1.00 26.66 ? 433 ALA A CB 1 ATOM 2197 N N . MET A 1 295 ? 5.905 -16.250 22.746 1.00 24.37 ? 434 MET A N 1 ATOM 2198 C CA . MET A 1 295 ? 5.794 -17.209 23.837 1.00 25.64 ? 434 MET A CA 1 ATOM 2199 C C . MET A 1 295 ? 5.463 -16.496 25.138 1.00 28.90 ? 434 MET A C 1 ATOM 2200 O O . MET A 1 295 ? 6.169 -15.573 25.541 1.00 33.55 ? 434 MET A O 1 ATOM 2201 C CB . MET A 1 295 ? 7.087 -18.016 23.985 1.00 27.31 ? 434 MET A CB 1 ATOM 2202 C CG . MET A 1 295 ? 7.051 -19.032 25.125 1.00 31.23 ? 434 MET A CG 1 ATOM 2203 S SD . MET A 1 295 ? 8.527 -20.066 25.226 1.00 40.09 ? 434 MET A SD 1 ATOM 2204 C CE . MET A 1 295 ? 9.489 -19.168 26.441 1.00 66.26 ? 434 MET A CE 1 ATOM 2205 N N . TYR A 1 296 ? 4.393 -16.937 25.797 1.00 24.70 ? 435 TYR A N 1 ATOM 2206 C CA . TYR A 1 296 ? 3.945 -16.328 27.046 1.00 28.08 ? 435 TYR A CA 1 ATOM 2207 C C . TYR A 1 296 ? 4.134 -17.259 28.240 1.00 26.48 ? 435 TYR A C 1 ATOM 2208 O O . TYR A 1 296 ? 4.473 -18.424 28.074 1.00 25.12 ? 435 TYR A O 1 ATOM 2209 C CB . TYR A 1 296 ? 2.476 -15.926 26.933 1.00 28.06 ? 435 TYR A CB 1 ATOM 2210 C CG . TYR A 1 296 ? 2.239 -14.849 25.912 1.00 26.25 ? 435 TYR A CG 1 ATOM 2211 C CD1 . TYR A 1 296 ? 2.007 -15.166 24.579 1.00 27.21 ? 435 TYR A CD1 1 ATOM 2212 C CD2 . TYR A 1 296 ? 2.262 -13.508 26.276 1.00 23.97 ? 435 TYR A CD2 1 ATOM 2213 C CE1 . TYR A 1 296 ? 1.801 -14.180 23.642 1.00 25.73 ? 435 TYR A CE1 1 ATOM 2214 C CE2 . TYR A 1 296 ? 2.052 -12.518 25.347 1.00 24.36 ? 435 TYR A CE2 1 ATOM 2215 C CZ . TYR A 1 296 ? 1.824 -12.857 24.031 1.00 25.02 ? 435 TYR A CZ 1 ATOM 2216 O OH . TYR A 1 296 ? 1.618 -11.865 23.102 1.00 27.52 ? 435 TYR A OH 1 ATOM 2217 N N . ALA A 1 297 ? 3.915 -16.731 29.443 1.00 27.28 ? 436 ALA A N 1 ATOM 2218 C CA . ALA A 1 297 ? 4.049 -17.516 30.670 1.00 28.06 ? 436 ALA A CA 1 ATOM 2219 C C . ALA A 1 297 ? 2.846 -18.437 30.876 1.00 28.72 ? 436 ALA A C 1 ATOM 2220 O O . ALA A 1 297 ? 1.805 -18.249 30.248 1.00 28.62 ? 436 ALA A O 1 ATOM 2221 C CB . ALA A 1 297 ? 4.226 -16.590 31.867 1.00 37.55 ? 436 ALA A CB 1 ATOM 2222 N N . PRO A 1 298 ? 2.991 -19.447 31.752 1.00 29.68 ? 437 PRO A N 1 ATOM 2223 C CA . PRO A 1 298 ? 1.909 -20.392 32.062 1.00 31.83 ? 437 PRO A CA 1 ATOM 2224 C C . PRO A 1 298 ? 0.671 -19.681 32.597 1.00 23.04 ? 437 PRO A C 1 ATOM 2225 O O . PRO A 1 298 ? 0.776 -18.551 33.062 1.00 29.16 ? 437 PRO A O 1 ATOM 2226 C CB . PRO A 1 298 ? 2.517 -21.267 33.161 1.00 33.10 ? 437 PRO A CB 1 ATOM 2227 C CG . PRO A 1 298 ? 3.979 -21.197 32.927 1.00 37.52 ? 437 PRO A CG 1 ATOM 2228 C CD . PRO A 1 298 ? 4.247 -19.808 32.434 1.00 31.79 ? 437 PRO A CD 1 ATOM 2229 N N . PRO A 1 299 ? -0.493 -20.346 32.541 1.00 26.00 ? 438 PRO A N 1 ATOM 2230 C CA . PRO A 1 299 ? -1.770 -19.739 32.931 1.00 27.26 ? 438 PRO A CA 1 ATOM 2231 C C . PRO A 1 299 ? -1.787 -19.359 34.403 1.00 29.82 ? 438 PRO A C 1 ATOM 2232 O O . PRO A 1 299 ? -1.109 -19.998 35.205 1.00 32.61 ? 438 PRO A O 1 ATOM 2233 C CB . PRO A 1 299 ? -2.782 -20.866 32.696 1.00 28.03 ? 438 PRO A CB 1 ATOM 2234 C CG . PRO A 1 299 ? -2.105 -21.831 31.797 1.00 34.47 ? 438 PRO A CG 1 ATOM 2235 C CD . PRO A 1 299 ? -0.653 -21.749 32.129 1.00 29.55 ? 438 PRO A CD 1 ATOM 2236 N N . ILE A 1 300 ? -2.561 -18.335 34.743 1.00 33.29 ? 439 ILE A N 1 ATOM 2237 C CA . ILE A 1 300 ? -2.791 -17.956 36.132 1.00 36.74 ? 439 ILE A CA 1 ATOM 2238 C C . ILE A 1 300 ? -3.511 -19.076 36.868 1.00 35.10 ? 439 ILE A C 1 ATOM 2239 O O . ILE A 1 300 ? -4.063 -19.980 36.245 1.00 31.72 ? 439 ILE A O 1 ATOM 2240 C CB . ILE A 1 300 ? -3.672 -16.695 36.223 1.00 37.92 ? 439 ILE A CB 1 ATOM 2241 C CG1 . ILE A 1 300 ? -4.991 -16.926 35.478 1.00 32.48 ? 439 ILE A CG1 1 ATOM 2242 C CG2 . ILE A 1 300 ? -2.944 -15.485 35.655 1.00 39.54 ? 439 ILE A CG2 1 ATOM 2243 C CD1 . ILE A 1 300 ? -5.955 -15.762 35.542 1.00 35.92 ? 439 ILE A CD1 1 ATOM 2244 N N . ASP A 1 301 ? -3.516 -19.000 38.197 1.00 34.32 ? 440 ASP A N 1 ATOM 2245 C CA . ASP A 1 301 ? -4.207 -19.979 39.028 1.00 39.69 ? 440 ASP A CA 1 ATOM 2246 C C . ASP A 1 301 ? -5.705 -19.713 39.108 1.00 36.92 ? 440 ASP A C 1 ATOM 2247 O O . ASP A 1 301 ? -6.171 -18.613 38.814 1.00 38.63 ? 440 ASP A O 1 ATOM 2248 C CB . ASP A 1 301 ? -3.623 -19.986 40.441 1.00 48.41 ? 440 ASP A CB 1 ATOM 2249 C CG . ASP A 1 301 ? -2.245 -20.607 40.499 1.00 59.26 ? 440 ASP A CG 1 ATOM 2250 O OD1 . ASP A 1 301 ? -1.981 -21.543 39.715 1.00 56.98 ? 440 ASP A OD1 1 ATOM 2251 O OD2 . ASP A 1 301 ? -1.429 -20.163 41.336 1.00 66.24 ? 440 ASP A OD2 1 ATOM 2252 N N . GLY A 1 302 ? -6.456 -20.735 39.507 1.00 42.08 ? 441 GLY A N 1 ATOM 2253 C CA . GLY A 1 302 ? -7.879 -20.582 39.744 1.00 44.75 ? 441 GLY A CA 1 ATOM 2254 C C . GLY A 1 302 ? -8.748 -20.906 38.547 1.00 43.83 ? 441 GLY A C 1 ATOM 2255 O O . GLY A 1 302 ? -8.289 -21.480 37.560 1.00 35.09 ? 441 GLY A O 1 ATOM 2256 N N . LYS A 1 303 ? -10.018 -20.531 38.641 1.00 48.62 ? 442 LYS A N 1 ATOM 2257 C CA . LYS A 1 303 ? -10.974 -20.806 37.582 1.00 46.67 ? 442 LYS A CA 1 ATOM 2258 C C . LYS A 1 303 ? -10.905 -19.715 36.525 1.00 37.52 ? 442 LYS A C 1 ATOM 2259 O O . LYS A 1 303 ? -11.251 -18.567 36.785 1.00 38.35 ? 442 LYS A O 1 ATOM 2260 C CB . LYS A 1 303 ? -12.392 -20.899 38.154 1.00 47.79 ? 442 LYS A CB 1 ATOM 2261 C CG . LYS A 1 303 ? -13.441 -21.359 37.152 1.00 47.44 ? 442 LYS A CG 1 ATOM 2262 C CD . LYS A 1 303 ? -14.843 -21.013 37.624 1.00 51.89 ? 442 LYS A CD 1 ATOM 2263 C CE . LYS A 1 303 ? -15.027 -19.504 37.724 1.00 57.81 ? 442 LYS A CE 1 ATOM 2264 N NZ . LYS A 1 303 ? -16.409 -19.123 38.135 1.00 63.18 ? 442 LYS A NZ 1 ATOM 2265 N N . ILE A 1 304 ? -10.442 -20.073 35.333 1.00 35.72 ? 443 ILE A N 1 ATOM 2266 C CA . ILE A 1 304 ? -10.421 -19.125 34.226 1.00 31.05 ? 443 ILE A CA 1 ATOM 2267 C C . ILE A 1 304 ? -11.675 -19.351 33.392 1.00 33.30 ? 443 ILE A C 1 ATOM 2268 O O . ILE A 1 304 ? -11.843 -20.412 32.797 1.00 38.15 ? 443 ILE A O 1 ATOM 2269 C CB . ILE A 1 304 ? -9.168 -19.311 33.346 1.00 25.95 ? 443 ILE A CB 1 ATOM 2270 C CG1 . ILE A 1 304 ? -7.910 -19.352 34.219 1.00 30.07 ? 443 ILE A CG1 1 ATOM 2271 C CG2 . ILE A 1 304 ? -9.068 -18.190 32.329 1.00 24.70 ? 443 ILE A CG2 1 ATOM 2272 C CD1 . ILE A 1 304 ? -6.658 -19.787 33.468 1.00 28.59 ? 443 ILE A CD1 1 ATOM 2273 N N . ASN A 1 305 ? -12.557 -18.358 33.358 1.00 28.67 ? 444 ASN A N 1 ATOM 2274 C CA . ASN A 1 305 ? -13.851 -18.515 32.700 1.00 32.04 ? 444 ASN A CA 1 ATOM 2275 C C . ASN A 1 305 ? -14.248 -17.319 31.833 1.00 32.52 ? 444 ASN A C 1 ATOM 2276 O O . ASN A 1 305 ? -14.159 -16.167 32.259 1.00 35.20 ? 444 ASN A O 1 ATOM 2277 C CB . ASN A 1 305 ? -14.934 -18.804 33.746 1.00 34.01 ? 444 ASN A CB 1 ATOM 2278 C CG . ASN A 1 305 ? -16.318 -18.930 33.141 1.00 39.31 ? 444 ASN A CG 1 ATOM 2279 O OD1 . ASN A 1 305 ? -16.637 -19.922 32.489 1.00 43.24 ? 444 ASN A OD1 1 ATOM 2280 N ND2 . ASN A 1 305 ? -17.153 -17.926 33.367 1.00 38.47 ? 444 ASN A ND2 1 ATOM 2281 N N . CYS A 1 306 ? -14.680 -17.608 30.610 1.00 31.70 ? 445 CYS A N 1 ATOM 2282 C CA . CYS A 1 306 ? -15.226 -16.591 29.721 1.00 31.37 ? 445 CYS A CA 1 ATOM 2283 C C . CYS A 1 306 ? -16.515 -17.102 29.101 1.00 29.00 ? 445 CYS A C 1 ATOM 2284 O O . CYS A 1 306 ? -16.512 -18.120 28.414 1.00 28.49 ? 445 CYS A O 1 ATOM 2285 C CB . CYS A 1 306 ? -14.233 -16.241 28.613 1.00 33.76 ? 445 CYS A CB 1 ATOM 2286 S SG . CYS A 1 306 ? -12.868 -15.176 29.127 1.00 42.31 ? 445 CYS A SG 1 ATOM 2287 N N . VAL A 1 307 ? -17.616 -16.407 29.359 1.00 26.15 ? 446 VAL A N 1 ATOM 2288 C CA . VAL A 1 307 ? -18.876 -16.714 28.696 1.00 25.37 ? 446 VAL A CA 1 ATOM 2289 C C . VAL A 1 307 ? -19.106 -15.659 27.619 1.00 23.43 ? 446 VAL A C 1 ATOM 2290 O O . VAL A 1 307 ? -19.191 -14.469 27.923 1.00 26.97 ? 446 VAL A O 1 ATOM 2291 C CB . VAL A 1 307 ? -20.058 -16.706 29.683 1.00 27.65 ? 446 VAL A CB 1 ATOM 2292 C CG1 . VAL A 1 307 ? -21.350 -17.087 28.967 1.00 29.57 ? 446 VAL A CG1 1 ATOM 2293 C CG2 . VAL A 1 307 ? -19.792 -17.653 30.851 1.00 28.75 ? 446 VAL A CG2 1 ATOM 2294 N N . SER A 1 308 ? -19.187 -16.094 26.362 1.00 25.38 ? 447 SER A N 1 ATOM 2295 C CA . SER A 1 308 ? -19.322 -15.172 25.238 1.00 23.91 ? 447 SER A CA 1 ATOM 2296 C C . SER A 1 308 ? -20.539 -15.519 24.390 1.00 24.99 ? 447 SER A C 1 ATOM 2297 O O . SER A 1 308 ? -21.030 -16.643 24.437 1.00 27.45 ? 447 SER A O 1 ATOM 2298 C CB . SER A 1 308 ? -18.072 -15.223 24.352 1.00 24.74 ? 447 SER A CB 1 ATOM 2299 O OG . SER A 1 308 ? -16.891 -15.101 25.118 1.00 28.13 ? 447 SER A OG 1 ATOM 2300 N N . ASN A 1 309 ? -21.019 -14.550 23.613 1.00 23.48 ? 448 ASN A N 1 ATOM 2301 C CA . ASN A 1 309 ? -22.046 -14.813 22.610 1.00 23.88 ? 448 ASN A CA 1 ATOM 2302 C C . ASN A 1 309 ? -21.390 -15.114 21.282 1.00 23.13 ? 448 ASN A C 1 ATOM 2303 O O . ASN A 1 309 ? -20.596 -14.319 20.803 1.00 22.06 ? 448 ASN A O 1 ATOM 2304 C CB . ASN A 1 309 ? -22.931 -13.587 22.391 1.00 24.29 ? 448 ASN A CB 1 ATOM 2305 C CG . ASN A 1 309 ? -23.622 -13.126 23.643 1.00 38.13 ? 448 ASN A CG 1 ATOM 2306 O OD1 . ASN A 1 309 ? -24.162 -13.929 24.399 1.00 30.72 ? 448 ASN A OD1 1 ATOM 2307 N ND2 . ASN A 1 309 ? -23.603 -11.816 23.874 1.00 50.29 ? 448 ASN A ND2 1 ATOM 2308 N N . ILE A 1 310 ? -21.718 -16.247 20.674 1.00 23.26 ? 449 ILE A N 1 ATOM 2309 C CA . ILE A 1 310 ? -21.355 -16.435 19.280 1.00 22.05 ? 449 ILE A CA 1 ATOM 2310 C C . ILE A 1 310 ? -22.327 -15.583 18.468 1.00 21.19 ? 449 ILE A C 1 ATOM 2311 O O . ILE A 1 310 ? -23.541 -15.738 18.588 1.00 23.68 ? 449 ILE A O 1 ATOM 2312 C CB . ILE A 1 310 ? -21.466 -17.899 18.845 1.00 24.10 ? 449 ILE A CB 1 ATOM 2313 C CG1 . ILE A 1 310 ? -20.601 -18.793 19.739 1.00 25.83 ? 449 ILE A CG1 1 ATOM 2314 C CG2 . ILE A 1 310 ? -21.050 -18.053 17.384 1.00 25.98 ? 449 ILE A CG2 1 ATOM 2315 C CD1 . ILE A 1 310 ? -20.822 -20.269 19.501 1.00 27.08 ? 449 ILE A CD1 1 ATOM 2316 N N . THR A 1 311 ? -21.799 -14.676 17.657 1.00 16.24 ? 450 THR A N 1 ATOM 2317 C CA . THR A 1 311 ? -22.644 -13.760 16.899 1.00 14.64 ? 450 THR A CA 1 ATOM 2318 C C . THR A 1 311 ? -22.344 -13.855 15.406 1.00 19.28 ? 450 THR A C 1 ATOM 2319 O O . THR A 1 311 ? -23.029 -13.243 14.586 1.00 24.12 ? 450 THR A O 1 ATOM 2320 C CB . THR A 1 311 ? -22.483 -12.293 17.376 1.00 24.07 ? 450 THR A CB 1 ATOM 2321 O OG1 . THR A 1 311 ? -21.103 -11.907 17.313 1.00 23.63 ? 450 THR A OG1 1 ATOM 2322 C CG2 . THR A 1 311 ? -22.991 -12.128 18.815 1.00 27.30 ? 450 THR A CG2 1 ATOM 2323 N N . GLY A 1 312 ? -21.312 -14.624 15.069 1.00 21.10 ? 451 GLY A N 1 ATOM 2324 C CA . GLY A 1 312 ? -20.909 -14.813 13.687 1.00 21.26 ? 451 GLY A CA 1 ATOM 2325 C C . GLY A 1 312 ? -20.052 -16.051 13.513 1.00 22.70 ? 451 GLY A C 1 ATOM 2326 O O . GLY A 1 312 ? -19.536 -16.604 14.485 1.00 20.86 ? 451 GLY A O 1 ATOM 2327 N N . ILE A 1 313 ? -19.919 -16.497 12.267 1.00 19.45 ? 452 ILE A N 1 ATOM 2328 C CA . ILE A 1 313 ? -19.070 -17.631 11.932 1.00 20.36 ? 452 ILE A CA 1 ATOM 2329 C C . ILE A 1 313 ? -18.253 -17.271 10.700 1.00 20.37 ? 452 ILE A C 1 ATOM 2330 O O . ILE A 1 313 ? -18.764 -16.659 9.766 1.00 22.44 ? 452 ILE A O 1 ATOM 2331 C CB . ILE A 1 313 ? -19.890 -18.897 11.611 1.00 23.83 ? 452 ILE A CB 1 ATOM 2332 C CG1 . ILE A 1 313 ? -20.928 -19.172 12.702 1.00 23.92 ? 452 ILE A CG1 1 ATOM 2333 C CG2 . ILE A 1 313 ? -18.966 -20.104 11.434 1.00 26.57 ? 452 ILE A CG2 1 ATOM 2334 C CD1 . ILE A 1 313 ? -21.879 -20.316 12.364 1.00 26.43 ? 452 ILE A CD1 1 ATOM 2335 N N . LEU A 1 314 ? -16.980 -17.644 10.700 1.00 20.00 ? 453 LEU A N 1 ATOM 2336 C CA . LEU A 1 314 ? -16.134 -17.429 9.535 1.00 17.84 ? 453 LEU A CA 1 ATOM 2337 C C . LEU A 1 314 ? -15.933 -18.769 8.836 1.00 21.62 ? 453 LEU A C 1 ATOM 2338 O O . LEU A 1 314 ? -15.481 -19.731 9.453 1.00 21.13 ? 453 LEU A O 1 ATOM 2339 C CB . LEU A 1 314 ? -14.791 -16.843 9.961 1.00 18.24 ? 453 LEU A CB 1 ATOM 2340 C CG . LEU A 1 314 ? -14.844 -15.540 10.767 1.00 23.12 ? 453 LEU A CG 1 ATOM 2341 C CD1 . LEU A 1 314 ? -13.445 -15.141 11.203 1.00 23.37 ? 453 LEU A CD1 1 ATOM 2342 C CD2 . LEU A 1 314 ? -15.489 -14.429 9.953 1.00 23.26 ? 453 LEU A CD2 1 ATOM 2343 N N . LEU A 1 315 ? -16.280 -18.833 7.554 1.00 20.80 ? 454 LEU A N 1 ATOM 2344 C CA . LEU A 1 315 ? -16.212 -20.080 6.800 1.00 19.58 ? 454 LEU A CA 1 ATOM 2345 C C . LEU A 1 315 ? -15.387 -19.949 5.524 1.00 19.43 ? 454 LEU A C 1 ATOM 2346 O O . LEU A 1 315 ? -15.270 -18.867 4.959 1.00 25.14 ? 454 LEU A O 1 ATOM 2347 C CB . LEU A 1 315 ? -17.620 -20.542 6.409 1.00 19.75 ? 454 LEU A CB 1 ATOM 2348 C CG . LEU A 1 315 ? -18.598 -20.856 7.538 1.00 23.85 ? 454 LEU A CG 1 ATOM 2349 C CD1 . LEU A 1 315 ? -19.984 -21.121 6.969 1.00 23.54 ? 454 LEU A CD1 1 ATOM 2350 C CD2 . LEU A 1 315 ? -18.105 -22.045 8.348 1.00 24.43 ? 454 LEU A CD2 1 ATOM 2351 N N . THR A 1 316 ? -14.833 -21.066 5.068 1.00 20.49 ? 455 THR A N 1 ATOM 2352 C CA . THR A 1 316 ? -14.239 -21.136 3.743 1.00 20.05 ? 455 THR A CA 1 ATOM 2353 C C . THR A 1 316 ? -14.879 -22.303 3.013 1.00 27.46 ? 455 THR A C 1 ATOM 2354 O O . THR A 1 316 ? -15.098 -23.362 3.597 1.00 28.58 ? 455 THR A O 1 ATOM 2355 C CB . THR A 1 316 ? -12.715 -21.343 3.798 1.00 27.49 ? 455 THR A CB 1 ATOM 2356 O OG1 . THR A 1 316 ? -12.426 -22.593 4.431 1.00 36.41 ? 455 THR A OG1 1 ATOM 2357 C CG2 . THR A 1 316 ? -12.051 -20.220 4.577 1.00 25.54 ? 455 THR A CG2 1 ATOM 2358 N N . ARG A 1 317 ? -15.184 -22.101 1.737 1.00 24.96 ? 456 ARG A N 1 ATOM 2359 C CA . ARG A 1 317 ? -15.847 -23.121 0.937 1.00 24.96 ? 456 ARG A CA 1 ATOM 2360 C C . ARG A 1 317 ? -14.842 -23.883 0.084 1.00 29.59 ? 456 ARG A C 1 ATOM 2361 O O . ARG A 1 317 ? -13.938 -23.285 -0.505 1.00 32.42 ? 456 ARG A O 1 ATOM 2362 C CB . ARG A 1 317 ? -16.912 -22.474 0.052 1.00 24.26 ? 456 ARG A CB 1 ATOM 2363 C CG . ARG A 1 317 ? -17.654 -23.437 -0.847 1.00 27.69 ? 456 ARG A CG 1 ATOM 2364 C CD . ARG A 1 317 ? -18.773 -22.732 -1.587 1.00 28.83 ? 456 ARG A CD 1 ATOM 2365 N NE . ARG A 1 317 ? -18.289 -21.642 -2.433 1.00 26.93 ? 456 ARG A NE 1 ATOM 2366 C CZ . ARG A 1 317 ? -18.020 -21.762 -3.730 1.00 30.95 ? 456 ARG A CZ 1 ATOM 2367 N NH1 . ARG A 1 317 ? -18.181 -22.931 -4.338 1.00 27.67 ? 456 ARG A NH1 1 ATOM 2368 N NH2 . ARG A 1 317 ? -17.588 -20.715 -4.420 1.00 29.06 ? 456 ARG A NH2 1 ATOM 2369 N N . ASP A 1 318 ? -15.002 -25.204 0.024 1.00 29.14 ? 457 ASP A N 1 ATOM 2370 C CA . ASP A 1 318 ? -14.137 -26.052 -0.793 1.00 33.61 ? 457 ASP A CA 1 ATOM 2371 C C . ASP A 1 318 ? -14.269 -25.722 -2.271 1.00 35.61 ? 457 ASP A C 1 ATOM 2372 O O . ASP A 1 318 ? -15.377 -25.545 -2.780 1.00 32.18 ? 457 ASP A O 1 ATOM 2373 C CB . ASP A 1 318 ? -14.480 -27.527 -0.581 1.00 37.49 ? 457 ASP A CB 1 ATOM 2374 C CG . ASP A 1 318 ? -13.907 -28.080 0.706 1.00 39.95 ? 457 ASP A CG 1 ATOM 2375 O OD1 . ASP A 1 318 ? -13.494 -27.275 1.565 1.00 35.84 ? 457 ASP A OD1 1 ATOM 2376 O OD2 . ASP A 1 318 ? -13.872 -29.320 0.857 1.00 40.30 ? 457 ASP A OD2 1 ATOM 2377 N N . GLY A 1 319 ? -13.137 -25.644 -2.962 1.00 35.84 ? 458 GLY A N 1 ATOM 2378 C CA . GLY A 1 319 ? -13.145 -25.447 -4.400 1.00 44.18 ? 458 GLY A CA 1 ATOM 2379 C C . GLY A 1 319 ? -13.336 -26.761 -5.136 1.00 49.90 ? 458 GLY A C 1 ATOM 2380 O O . GLY A 1 319 ? -13.096 -27.831 -4.579 1.00 52.57 ? 458 GLY A O 1 ATOM 2381 N N . GLY A 1 320 ? -13.779 -26.681 -6.387 1.00 56.91 ? 459 GLY A N 1 ATOM 2382 C CA . GLY A 1 320 ? -13.877 -27.853 -7.241 1.00 63.88 ? 459 GLY A CA 1 ATOM 2383 C C . GLY A 1 320 ? -15.052 -28.779 -6.973 1.00 70.40 ? 459 GLY A C 1 ATOM 2384 O O . GLY A 1 320 ? -15.010 -29.957 -7.329 1.00 73.83 ? 459 GLY A O 1 ATOM 2385 N N . ALA A 1 321 ? -16.104 -28.255 -6.352 1.00 72.63 ? 460 ALA A N 1 ATOM 2386 C CA . ALA A 1 321 ? -17.303 -29.046 -6.085 1.00 74.44 ? 460 ALA A CA 1 ATOM 2387 C C . ALA A 1 321 ? -18.426 -28.687 -7.058 1.00 76.49 ? 460 ALA A C 1 ATOM 2388 O O . ALA A 1 321 ? -19.576 -29.084 -6.869 1.00 74.77 ? 460 ALA A O 1 ATOM 2389 C CB . ALA A 1 321 ? -17.757 -28.859 -4.643 1.00 72.03 ? 460 ALA A CB 1 ATOM 2390 N N . ASN A 1 322 ? -18.078 -27.945 -8.106 1.00 79.81 ? 461 ASN A N 1 ATOM 2391 C CA . ASN A 1 322 ? -19.048 -27.507 -9.103 1.00 84.86 ? 461 ASN A CA 1 ATOM 2392 C C . ASN A 1 322 ? -19.722 -28.682 -9.817 1.00 85.22 ? 461 ASN A C 1 ATOM 2393 O O . ASN A 1 322 ? -20.890 -28.605 -10.197 1.00 84.31 ? 461 ASN A O 1 ATOM 2394 C CB . ASN A 1 322 ? -18.385 -26.580 -10.130 1.00 88.16 ? 461 ASN A CB 1 ATOM 2395 C CG . ASN A 1 322 ? -17.642 -25.425 -9.488 1.00 90.28 ? 461 ASN A CG 1 ATOM 2396 O OD1 . ASN A 1 322 ? -16.460 -25.207 -9.758 1.00 91.15 ? 461 ASN A OD1 1 ATOM 2397 N ND2 . ASN A 1 322 ? -18.330 -24.676 -8.639 1.00 90.26 ? 461 ASN A ND2 1 ATOM 2398 N N . ASN A 1 323 ? -18.973 -29.765 -9.995 1.00 85.50 ? 462 ASN A N 1 ATOM 2399 C CA . ASN A 1 323 ? -19.471 -30.972 -10.645 1.00 85.70 ? 462 ASN A CA 1 ATOM 2400 C C . ASN A 1 323 ? -20.412 -31.788 -9.769 1.00 80.79 ? 462 ASN A C 1 ATOM 2401 O O . ASN A 1 323 ? -21.162 -32.627 -10.267 1.00 83.95 ? 462 ASN A O 1 ATOM 2402 C CB . ASN A 1 323 ? -18.292 -31.843 -11.082 1.00 90.56 ? 462 ASN A CB 1 ATOM 2403 C CG . ASN A 1 323 ? -17.205 -31.934 -10.015 1.00 92.74 ? 462 ASN A CG 1 ATOM 2404 O OD1 . ASN A 1 323 ? -16.827 -30.928 -9.415 1.00 90.54 ? 462 ASN A OD1 1 ATOM 2405 N ND2 . ASN A 1 323 ? -16.703 -33.143 -9.774 1.00 94.93 ? 462 ASN A ND2 1 ATOM 2406 N N . THR A 1 324 ? -20.379 -31.520 -8.467 1.00 71.53 ? 463 THR A N 1 ATOM 2407 C CA . THR A 1 324 ? -21.154 -32.289 -7.503 1.00 68.26 ? 463 THR A CA 1 ATOM 2408 C C . THR A 1 324 ? -22.451 -31.589 -7.116 1.00 64.92 ? 463 THR A C 1 ATOM 2409 O O . THR A 1 324 ? -22.736 -30.488 -7.580 1.00 65.17 ? 463 THR A O 1 ATOM 2410 C CB . THR A 1 324 ? -20.341 -32.560 -6.223 1.00 67.76 ? 463 THR A CB 1 ATOM 2411 O OG1 . THR A 1 324 ? -20.325 -31.385 -5.404 1.00 64.15 ? 463 THR A OG1 1 ATOM 2412 C CG2 . THR A 1 324 ? -18.909 -32.957 -6.562 1.00 66.38 ? 463 THR A CG2 1 ATOM 2413 N N . SER A 1 325 ? -23.243 -32.251 -6.277 1.00 63.68 ? 464 SER A N 1 ATOM 2414 C CA . SER A 1 325 ? -24.479 -31.672 -5.767 1.00 61.29 ? 464 SER A CA 1 ATOM 2415 C C . SER A 1 325 ? -24.253 -31.166 -4.352 1.00 52.32 ? 464 SER A C 1 ATOM 2416 O O . SER A 1 325 ? -25.202 -30.850 -3.635 1.00 47.89 ? 464 SER A O 1 ATOM 2417 C CB . SER A 1 325 ? -25.604 -32.708 -5.779 1.00 69.90 ? 464 SER A CB 1 ATOM 2418 O OG . SER A 1 325 ? -26.824 -32.146 -5.330 1.00 72.58 ? 464 SER A OG 1 ATOM 2419 N N . ASN A 1 326 ? -22.986 -31.091 -3.956 1.00 47.61 ? 465 ASN A N 1 ATOM 2420 C CA . ASN A 1 326 ? -22.631 -30.651 -2.610 1.00 44.93 ? 465 ASN A CA 1 ATOM 2421 C C . ASN A 1 326 ? -21.729 -29.420 -2.611 1.00 37.57 ? 465 ASN A C 1 ATOM 2422 O O . ASN A 1 326 ? -20.959 -29.202 -3.549 1.00 38.08 ? 465 ASN A O 1 ATOM 2423 C CB . ASN A 1 326 ? -21.931 -31.778 -1.842 1.00 47.92 ? 465 ASN A CB 1 ATOM 2424 C CG . ASN A 1 326 ? -22.689 -33.084 -1.897 1.00 56.28 ? 465 ASN A CG 1 ATOM 2425 O OD1 . ASN A 1 326 ? -22.097 -34.153 -2.039 1.00 57.12 ? 465 ASN A OD1 1 ATOM 2426 N ND2 . ASN A 1 326 ? -24.004 -33.008 -1.782 1.00 61.80 ? 465 ASN A ND2 1 ATOM 2427 N N . GLU A 1 327 ? -21.852 -28.614 -1.563 1.00 33.37 ? 466 GLU A N 1 ATOM 2428 C CA . GLU A 1 327 ? -20.885 -27.571 -1.261 1.00 30.12 ? 466 GLU A CA 1 ATOM 2429 C C . GLU A 1 327 ? -20.365 -27.838 0.145 1.00 32.55 ? 466 GLU A C 1 ATOM 2430 O O . GLU A 1 327 ? -21.143 -28.086 1.073 1.00 34.68 ? 466 GLU A O 1 ATOM 2431 C CB . GLU A 1 327 ? -21.520 -26.180 -1.333 1.00 29.80 ? 466 GLU A CB 1 ATOM 2432 C CG . GLU A 1 327 ? -21.941 -25.740 -2.732 1.00 34.45 ? 466 GLU A CG 1 ATOM 2433 C CD . GLU A 1 327 ? -20.769 -25.593 -3.692 1.00 39.72 ? 466 GLU A CD 1 ATOM 2434 O OE1 . GLU A 1 327 ? -19.609 -25.535 -3.225 1.00 33.87 ? 466 GLU A OE1 1 ATOM 2435 O OE2 . GLU A 1 327 ? -21.011 -25.530 -4.918 1.00 41.95 ? 466 GLU A OE2 1 ATOM 2436 N N . THR A 1 328 ? -19.048 -27.788 0.303 1.00 30.72 ? 467 THR A N 1 ATOM 2437 C CA . THR A 1 328 ? -18.427 -28.099 1.583 1.00 29.53 ? 467 THR A CA 1 ATOM 2438 C C . THR A 1 328 ? -17.864 -26.843 2.233 1.00 28.07 ? 467 THR A C 1 ATOM 2439 O O . THR A 1 328 ? -17.203 -26.039 1.575 1.00 29.89 ? 467 THR A O 1 ATOM 2440 C CB . THR A 1 328 ? -17.316 -29.148 1.408 1.00 31.58 ? 467 THR A CB 1 ATOM 2441 O OG1 . THR A 1 328 ? -17.902 -30.375 0.961 1.00 37.55 ? 467 THR A OG1 1 ATOM 2442 C CG2 . THR A 1 328 ? -16.597 -29.398 2.720 1.00 32.87 ? 467 THR A CG2 1 ATOM 2443 N N . PHE A 1 329 ? -18.143 -26.674 3.522 1.00 24.01 ? 468 PHE A N 1 ATOM 2444 C CA . PHE A 1 329 ? -17.698 -25.498 4.258 1.00 23.40 ? 468 PHE A CA 1 ATOM 2445 C C . PHE A 1 329 ? -16.886 -25.924 5.475 1.00 26.00 ? 468 PHE A C 1 ATOM 2446 O O . PHE A 1 329 ? -17.197 -26.930 6.120 1.00 26.92 ? 468 PHE A O 1 ATOM 2447 C CB . PHE A 1 329 ? -18.894 -24.643 4.683 1.00 22.34 ? 468 PHE A CB 1 ATOM 2448 C CG . PHE A 1 329 ? -19.700 -24.118 3.526 1.00 22.04 ? 468 PHE A CG 1 ATOM 2449 C CD1 . PHE A 1 329 ? -20.695 -24.894 2.948 1.00 24.13 ? 468 PHE A CD1 1 ATOM 2450 C CD2 . PHE A 1 329 ? -19.446 -22.863 3.003 1.00 23.83 ? 468 PHE A CD2 1 ATOM 2451 C CE1 . PHE A 1 329 ? -21.436 -24.415 1.876 1.00 23.75 ? 468 PHE A CE1 1 ATOM 2452 C CE2 . PHE A 1 329 ? -20.176 -22.381 1.929 1.00 22.69 ? 468 PHE A CE2 1 ATOM 2453 C CZ . PHE A 1 329 ? -21.171 -23.167 1.361 1.00 21.21 ? 468 PHE A CZ 1 ATOM 2454 N N . ARG A 1 330 ? -15.844 -25.154 5.777 1.00 22.02 ? 469 ARG A N 1 ATOM 2455 C CA . ARG A 1 330 ? -14.971 -25.444 6.909 1.00 19.79 ? 469 ARG A CA 1 ATOM 2456 C C . ARG A 1 330 ? -14.744 -24.147 7.669 1.00 24.99 ? 469 ARG A C 1 ATOM 2457 O O . ARG A 1 330 ? -14.619 -23.085 7.061 1.00 26.21 ? 469 ARG A O 1 ATOM 2458 C CB . ARG A 1 330 ? -13.630 -26.001 6.419 1.00 26.25 ? 469 ARG A CB 1 ATOM 2459 C CG . ARG A 1 330 ? -13.751 -27.183 5.454 1.00 24.90 ? 469 ARG A CG 1 ATOM 2460 C CD . ARG A 1 330 ? -12.390 -27.615 4.902 1.00 26.49 ? 469 ARG A CD 1 ATOM 2461 N NE . ARG A 1 330 ? -12.526 -28.584 3.812 1.00 31.67 ? 469 ARG A NE 1 ATOM 2462 C CZ . ARG A 1 330 ? -12.373 -29.899 3.944 1.00 39.04 ? 469 ARG A CZ 1 ATOM 2463 N NH1 . ARG A 1 330 ? -12.069 -30.423 5.125 1.00 38.08 ? 469 ARG A NH1 1 ATOM 2464 N NH2 . ARG A 1 330 ? -12.521 -30.693 2.889 1.00 34.55 ? 469 ARG A NH2 1 ATOM 2465 N N . PRO A 1 331 ? -14.712 -24.222 9.006 1.00 23.73 ? 470 PRO A N 1 ATOM 2466 C CA . PRO A 1 331 ? -14.479 -22.992 9.761 1.00 22.82 ? 470 PRO A CA 1 ATOM 2467 C C . PRO A 1 331 ? -13.107 -22.445 9.418 1.00 23.54 ? 470 PRO A C 1 ATOM 2468 O O . PRO A 1 331 ? -12.191 -23.215 9.129 1.00 26.40 ? 470 PRO A O 1 ATOM 2469 C CB . PRO A 1 331 ? -14.537 -23.453 11.221 1.00 26.79 ? 470 PRO A CB 1 ATOM 2470 C CG . PRO A 1 331 ? -14.266 -24.924 11.177 1.00 31.45 ? 470 PRO A CG 1 ATOM 2471 C CD . PRO A 1 331 ? -14.837 -25.405 9.876 1.00 25.32 ? 470 PRO A CD 1 ATOM 2472 N N . GLY A 1 332 ? -12.970 -21.126 9.429 1.00 26.78 ? 471 GLY A N 1 ATOM 2473 C CA . GLY A 1 332 ? -11.712 -20.509 9.068 1.00 29.29 ? 471 GLY A CA 1 ATOM 2474 C C . GLY A 1 332 ? -11.481 -19.206 9.794 1.00 28.13 ? 471 GLY A C 1 ATOM 2475 O O . GLY A 1 332 ? -11.852 -19.055 10.954 1.00 25.10 ? 471 GLY A O 1 ATOM 2476 N N . GLY A 1 333 ? -10.872 -18.256 9.098 1.00 27.77 ? 472 GLY A N 1 ATOM 2477 C CA . GLY A 1 333 ? -10.524 -16.982 9.694 1.00 24.94 ? 472 GLY A CA 1 ATOM 2478 C C . GLY A 1 333 ? -9.020 -16.848 9.775 1.00 23.84 ? 472 GLY A C 1 ATOM 2479 O O . GLY A 1 333 ? -8.291 -17.545 9.069 1.00 23.16 ? 472 GLY A O 1 ATOM 2480 N N . GLY A 1 334 ? -8.548 -15.943 10.624 1.00 22.12 ? 473 GLY A N 1 ATOM 2481 C CA . GLY A 1 334 ? -7.122 -15.724 10.774 1.00 19.07 ? 473 GLY A CA 1 ATOM 2482 C C . GLY A 1 334 ? -6.687 -14.363 10.270 1.00 19.16 ? 473 GLY A C 1 ATOM 2483 O O . GLY A 1 334 ? -5.636 -13.858 10.668 1.00 20.40 ? 473 GLY A O 1 ATOM 2484 N N . ASN A 1 335 ? -7.474 -13.787 9.360 1.00 17.22 ? 474 ASN A N 1 ATOM 2485 C CA . ASN A 1 335 ? -7.288 -12.400 8.961 1.00 20.85 ? 474 ASN A CA 1 ATOM 2486 C C . ASN A 1 335 ? -8.199 -11.563 9.835 1.00 19.95 ? 474 ASN A C 1 ATOM 2487 O O . ASN A 1 335 ? -9.393 -11.455 9.561 1.00 16.86 ? 474 ASN A O 1 ATOM 2488 C CB . ASN A 1 335 ? -7.638 -12.192 7.484 1.00 22.10 ? 474 ASN A CB 1 ATOM 2489 C CG . ASN A 1 335 ? -7.485 -10.747 7.046 1.00 22.03 ? 474 ASN A CG 1 ATOM 2490 O OD1 . ASN A 1 335 ? -7.088 -9.887 7.832 1.00 27.10 ? 474 ASN A OD1 1 ATOM 2491 N ND2 . ASN A 1 335 ? -7.801 -10.473 5.787 1.00 25.16 ? 474 ASN A ND2 1 ATOM 2492 N N . ILE A 1 336 ? -7.641 -11.001 10.902 1.00 18.22 ? 475 ILE A N 1 ATOM 2493 C CA . ILE A 1 336 ? -8.448 -10.317 11.913 1.00 18.48 ? 475 ILE A CA 1 ATOM 2494 C C . ILE A 1 336 ? -9.163 -9.082 11.352 1.00 16.75 ? 475 ILE A C 1 ATOM 2495 O O . ILE A 1 336 ? -10.131 -8.590 11.936 1.00 15.36 ? 475 ILE A O 1 ATOM 2496 C CB . ILE A 1 336 ? -7.600 -9.956 13.149 1.00 20.83 ? 475 ILE A CB 1 ATOM 2497 C CG1 . ILE A 1 336 ? -6.897 -11.211 13.670 1.00 18.49 ? 475 ILE A CG1 1 ATOM 2498 C CG2 . ILE A 1 336 ? -8.464 -9.357 14.248 1.00 19.67 ? 475 ILE A CG2 1 ATOM 2499 C CD1 . ILE A 1 336 ? -7.854 -12.362 13.984 1.00 20.91 ? 475 ILE A CD1 1 ATOM 2500 N N . LYS A 1 337 ? -8.728 -8.613 10.191 1.00 17.93 ? 476 LYS A N 1 ATOM 2501 C CA . LYS A 1 337 ? -9.427 -7.519 9.531 1.00 18.10 ? 476 LYS A CA 1 ATOM 2502 C C . LYS A 1 337 ? -10.876 -7.904 9.245 1.00 22.88 ? 476 LYS A C 1 ATOM 2503 O O . LYS A 1 337 ? -11.768 -7.062 9.282 1.00 24.53 ? 476 LYS A O 1 ATOM 2504 C CB . LYS A 1 337 ? -8.713 -7.109 8.245 1.00 19.57 ? 476 LYS A CB 1 ATOM 2505 C CG . LYS A 1 337 ? -7.609 -6.090 8.463 1.00 23.32 ? 476 LYS A CG 1 ATOM 2506 C CD . LYS A 1 337 ? -6.950 -5.694 7.154 1.00 32.50 ? 476 LYS A CD 1 ATOM 2507 C CE . LYS A 1 337 ? -5.625 -4.995 7.399 1.00 39.53 ? 476 LYS A CE 1 ATOM 2508 N NZ . LYS A 1 337 ? -4.997 -4.533 6.133 1.00 37.26 ? 476 LYS A NZ 1 ATOM 2509 N N . ASP A 1 338 ? -11.103 -9.184 8.970 1.00 22.36 ? 477 ASP A N 1 ATOM 2510 C CA . ASP A 1 338 ? -12.449 -9.682 8.718 1.00 22.87 ? 477 ASP A CA 1 ATOM 2511 C C . ASP A 1 338 ? -13.330 -9.494 9.950 1.00 21.24 ? 477 ASP A C 1 ATOM 2512 O O . ASP A 1 338 ? -14.522 -9.226 9.836 1.00 19.42 ? 477 ASP A O 1 ATOM 2513 C CB . ASP A 1 338 ? -12.415 -11.156 8.317 1.00 21.28 ? 477 ASP A CB 1 ATOM 2514 C CG . ASP A 1 338 ? -11.896 -11.365 6.909 1.00 29.23 ? 477 ASP A CG 1 ATOM 2515 O OD1 . ASP A 1 338 ? -12.091 -10.472 6.063 1.00 31.39 ? 477 ASP A OD1 1 ATOM 2516 O OD2 . ASP A 1 338 ? -11.294 -12.425 6.651 1.00 33.53 ? 477 ASP A OD2 1 ATOM 2517 N N . ASN A 1 339 ? -12.731 -9.637 11.126 1.00 22.32 ? 478 ASN A N 1 ATOM 2518 C CA . ASN A 1 339 ? -13.452 -9.440 12.375 1.00 19.21 ? 478 ASN A CA 1 ATOM 2519 C C . ASN A 1 339 ? -14.006 -8.023 12.468 1.00 17.20 ? 478 ASN A C 1 ATOM 2520 O O . ASN A 1 339 ? -15.160 -7.822 12.832 1.00 18.18 ? 478 ASN A O 1 ATOM 2521 C CB . ASN A 1 339 ? -12.546 -9.734 13.573 1.00 17.98 ? 478 ASN A CB 1 ATOM 2522 C CG . ASN A 1 339 ? -12.252 -11.213 13.735 1.00 19.53 ? 478 ASN A CG 1 ATOM 2523 O OD1 . ASN A 1 339 ? -12.398 -11.771 14.820 1.00 20.65 ? 478 ASN A OD1 1 ATOM 2524 N ND2 . ASN A 1 339 ? -11.829 -11.852 12.655 1.00 18.58 ? 478 ASN A ND2 1 ATOM 2525 N N . TRP A 1 340 ? -13.173 -7.046 12.129 1.00 16.59 ? 479 TRP A N 1 ATOM 2526 C CA . TRP A 1 340 ? -13.590 -5.659 12.139 1.00 18.06 ? 479 TRP A CA 1 ATOM 2527 C C . TRP A 1 340 ? -14.598 -5.407 11.059 1.00 20.76 ? 479 TRP A C 1 ATOM 2528 O O . TRP A 1 340 ? -15.552 -4.629 11.246 1.00 18.28 ? 479 TRP A O 1 ATOM 2529 C CB . TRP A 1 340 ? -12.393 -4.735 11.961 1.00 17.97 ? 479 TRP A CB 1 ATOM 2530 C CG . TRP A 1 340 ? -11.195 -5.125 12.790 1.00 17.73 ? 479 TRP A CG 1 ATOM 2531 C CD1 . TRP A 1 340 ? -9.852 -4.983 12.461 1.00 20.27 ? 479 TRP A CD1 1 ATOM 2532 C CD2 . TRP A 1 340 ? -11.196 -5.741 14.122 1.00 18.59 ? 479 TRP A CD2 1 ATOM 2533 N NE1 . TRP A 1 340 ? -9.051 -5.454 13.467 1.00 19.48 ? 479 TRP A NE1 1 ATOM 2534 C CE2 . TRP A 1 340 ? -9.792 -5.921 14.490 1.00 18.52 ? 479 TRP A CE2 1 ATOM 2535 C CE3 . TRP A 1 340 ? -12.180 -6.144 15.008 1.00 16.44 ? 479 TRP A CE3 1 ATOM 2536 C CZ2 . TRP A 1 340 ? -9.419 -6.482 15.695 1.00 16.43 ? 479 TRP A CZ2 1 ATOM 2537 C CZ3 . TRP A 1 340 ? -11.789 -6.709 16.221 1.00 23.38 ? 479 TRP A CZ3 1 ATOM 2538 C CH2 . TRP A 1 340 ? -10.441 -6.872 16.553 1.00 25.45 ? 479 TRP A CH2 1 ATOM 2539 N N . ARG A 1 341 ? -14.406 -6.057 9.917 1.00 17.29 ? 480 ARG A N 1 ATOM 2540 C CA . ARG A 1 341 ? -15.326 -5.926 8.796 1.00 18.72 ? 480 ARG A CA 1 ATOM 2541 C C . ARG A 1 341 ? -16.740 -6.312 9.211 1.00 19.76 ? 480 ARG A C 1 ATOM 2542 O O . ARG A 1 341 ? -17.714 -5.704 8.777 1.00 19.17 ? 480 ARG A O 1 ATOM 2543 C CB . ARG A 1 341 ? -14.873 -6.805 7.629 1.00 19.82 ? 480 ARG A CB 1 ATOM 2544 C CG . ARG A 1 341 ? -14.353 -6.034 6.428 1.00 25.73 ? 480 ARG A CG 1 ATOM 2545 C CD . ARG A 1 341 ? -13.508 -6.913 5.520 1.00 28.99 ? 480 ARG A CD 1 ATOM 2546 N NE . ARG A 1 341 ? -12.375 -6.180 4.969 1.00 36.05 ? 480 ARG A NE 1 ATOM 2547 C CZ . ARG A 1 341 ? -11.135 -6.650 4.901 1.00 36.51 ? 480 ARG A CZ 1 ATOM 2548 N NH1 . ARG A 1 341 ? -10.855 -7.868 5.346 1.00 39.52 ? 480 ARG A NH1 1 ATOM 2549 N NH2 . ARG A 1 341 ? -10.172 -5.902 4.383 1.00 45.41 ? 480 ARG A NH2 1 ATOM 2550 N N . SER A 1 342 ? -16.839 -7.332 10.055 1.00 19.02 ? 481 SER A N 1 ATOM 2551 C CA . SER A 1 342 ? -18.124 -7.855 10.488 1.00 22.45 ? 481 SER A CA 1 ATOM 2552 C C . SER A 1 342 ? -18.901 -6.821 11.289 1.00 24.21 ? 481 SER A C 1 ATOM 2553 O O . SER A 1 342 ? -20.122 -6.906 11.380 1.00 23.99 ? 481 SER A O 1 ATOM 2554 C CB . SER A 1 342 ? -17.942 -9.143 11.299 1.00 24.55 ? 481 SER A CB 1 ATOM 2555 O OG . SER A 1 342 ? -17.440 -8.874 12.600 1.00 25.49 ? 481 SER A OG 1 ATOM 2556 N N . GLU A 1 343 ? -18.194 -5.842 11.858 1.00 21.66 ? 482 GLU A N 1 ATOM 2557 C CA . GLU A 1 343 ? -18.824 -4.803 12.674 1.00 19.59 ? 482 GLU A CA 1 ATOM 2558 C C . GLU A 1 343 ? -18.949 -3.468 11.940 1.00 23.24 ? 482 GLU A C 1 ATOM 2559 O O . GLU A 1 343 ? -19.862 -2.688 12.207 1.00 24.05 ? 482 GLU A O 1 ATOM 2560 C CB . GLU A 1 343 ? -18.059 -4.601 13.994 1.00 24.36 ? 482 GLU A CB 1 ATOM 2561 C CG . GLU A 1 343 ? -18.204 -5.750 14.993 1.00 26.16 ? 482 GLU A CG 1 ATOM 2562 C CD . GLU A 1 343 ? -19.621 -5.884 15.527 1.00 30.50 ? 482 GLU A CD 1 ATOM 2563 O OE1 . GLU A 1 343 ? -20.208 -4.855 15.926 1.00 30.18 ? 482 GLU A OE1 1 ATOM 2564 O OE2 . GLU A 1 343 ? -20.152 -7.016 15.541 1.00 30.53 ? 482 GLU A OE2 1 ATOM 2565 N N . LEU A 1 344 ? -18.036 -3.207 11.012 1.00 18.53 ? 483 LEU A N 1 ATOM 2566 C CA . LEU A 1 344 ? -17.980 -1.904 10.347 1.00 15.96 ? 483 LEU A CA 1 ATOM 2567 C C . LEU A 1 344 ? -18.685 -1.866 8.987 1.00 17.15 ? 483 LEU A C 1 ATOM 2568 O O . LEU A 1 344 ? -18.728 -0.821 8.337 1.00 21.63 ? 483 LEU A O 1 ATOM 2569 C CB . LEU A 1 344 ? -16.519 -1.477 10.176 1.00 17.15 ? 483 LEU A CB 1 ATOM 2570 C CG . LEU A 1 344 ? -15.770 -1.090 11.452 1.00 21.37 ? 483 LEU A CG 1 ATOM 2571 C CD1 . LEU A 1 344 ? -14.268 -1.046 11.185 1.00 20.58 ? 483 LEU A CD1 1 ATOM 2572 C CD2 . LEU A 1 344 ? -16.272 0.249 11.974 1.00 23.40 ? 483 LEU A CD2 1 ATOM 2573 N N . TYR A 1 345 ? -19.234 -3.001 8.569 1.00 18.21 ? 484 TYR A N 1 ATOM 2574 C CA . TYR A 1 345 ? -19.798 -3.154 7.228 1.00 19.59 ? 484 TYR A CA 1 ATOM 2575 C C . TYR A 1 345 ? -20.864 -2.107 6.878 1.00 18.00 ? 484 TYR A C 1 ATOM 2576 O O . TYR A 1 345 ? -21.080 -1.801 5.707 1.00 21.22 ? 484 TYR A O 1 ATOM 2577 C CB . TYR A 1 345 ? -20.393 -4.557 7.061 1.00 18.48 ? 484 TYR A CB 1 ATOM 2578 C CG . TYR A 1 345 ? -21.713 -4.720 7.777 1.00 22.96 ? 484 TYR A CG 1 ATOM 2579 C CD1 . TYR A 1 345 ? -21.757 -5.149 9.097 1.00 27.35 ? 484 TYR A CD1 1 ATOM 2580 C CD2 . TYR A 1 345 ? -22.913 -4.419 7.143 1.00 25.39 ? 484 TYR A CD2 1 ATOM 2581 C CE1 . TYR A 1 345 ? -22.957 -5.285 9.764 1.00 31.64 ? 484 TYR A CE1 1 ATOM 2582 C CE2 . TYR A 1 345 ? -24.121 -4.551 7.804 1.00 32.57 ? 484 TYR A CE2 1 ATOM 2583 C CZ . TYR A 1 345 ? -24.134 -4.985 9.115 1.00 35.61 ? 484 TYR A CZ 1 ATOM 2584 O OH . TYR A 1 345 ? -25.327 -5.125 9.782 1.00 40.46 ? 484 TYR A OH 1 ATOM 2585 N N . LYS A 1 346 ? -21.540 -1.574 7.887 1.00 22.10 ? 485 LYS A N 1 ATOM 2586 C CA . LYS A 1 346 ? -22.650 -0.660 7.642 1.00 23.60 ? 485 LYS A CA 1 ATOM 2587 C C . LYS A 1 346 ? -22.233 0.805 7.645 1.00 21.05 ? 485 LYS A C 1 ATOM 2588 O O . LYS A 1 346 ? -23.081 1.689 7.521 1.00 27.53 ? 485 LYS A O 1 ATOM 2589 C CB . LYS A 1 346 ? -23.755 -0.875 8.681 1.00 27.48 ? 485 LYS A CB 1 ATOM 2590 C CG . LYS A 1 346 ? -23.341 -0.521 10.097 1.00 28.64 ? 485 LYS A CG 1 ATOM 2591 C CD . LYS A 1 346 ? -24.531 -0.592 11.048 1.00 36.30 ? 485 LYS A CD 1 ATOM 2592 C CE . LYS A 1 346 ? -25.235 -1.936 10.958 1.00 43.65 ? 485 LYS A CE 1 ATOM 2593 N NZ . LYS A 1 346 ? -26.349 -2.049 11.947 1.00 48.20 ? 485 LYS A NZ 1 ATOM 2594 N N . TYR A 1 347 ? -20.934 1.066 7.783 1.00 15.87 ? 486 TYR A N 1 ATOM 2595 C CA . TYR A 1 347 ? -20.442 2.440 7.872 1.00 17.04 ? 486 TYR A CA 1 ATOM 2596 C C . TYR A 1 347 ? -19.543 2.827 6.712 1.00 17.90 ? 486 TYR A C 1 ATOM 2597 O O . TYR A 1 347 ? -18.814 1.997 6.171 1.00 20.77 ? 486 TYR A O 1 ATOM 2598 C CB . TYR A 1 347 ? -19.647 2.645 9.163 1.00 16.65 ? 486 TYR A CB 1 ATOM 2599 C CG . TYR A 1 347 ? -20.421 2.387 10.432 1.00 20.67 ? 486 TYR A CG 1 ATOM 2600 C CD1 . TYR A 1 347 ? -21.420 3.256 10.848 1.00 19.28 ? 486 TYR A CD1 1 ATOM 2601 C CD2 . TYR A 1 347 ? -20.135 1.282 11.227 1.00 22.11 ? 486 TYR A CD2 1 ATOM 2602 C CE1 . TYR A 1 347 ? -22.126 3.027 12.017 1.00 23.13 ? 486 TYR A CE1 1 ATOM 2603 C CE2 . TYR A 1 347 ? -20.830 1.050 12.404 1.00 20.38 ? 486 TYR A CE2 1 ATOM 2604 C CZ . TYR A 1 347 ? -21.822 1.924 12.790 1.00 22.78 ? 486 TYR A CZ 1 ATOM 2605 O OH . TYR A 1 347 ? -22.516 1.693 13.955 1.00 24.30 ? 486 TYR A OH 1 ATOM 2606 N N . LYS A 1 348 ? -19.592 4.105 6.347 1.00 18.07 ? 487 LYS A N 1 ATOM 2607 C CA . LYS A 1 348 ? -18.594 4.668 5.457 1.00 21.76 ? 487 LYS A CA 1 ATOM 2608 C C . LYS A 1 348 ? -18.402 6.147 5.765 1.00 23.68 ? 487 LYS A C 1 ATOM 2609 O O . LYS A 1 348 ? -19.324 6.826 6.212 1.00 24.82 ? 487 LYS A O 1 ATOM 2610 C CB . LYS A 1 348 ? -18.978 4.460 3.990 1.00 24.48 ? 487 LYS A CB 1 ATOM 2611 C CG . LYS A 1 348 ? -20.110 5.332 3.497 1.00 24.99 ? 487 LYS A CG 1 ATOM 2612 C CD . LYS A 1 348 ? -20.236 5.194 1.980 1.00 27.55 ? 487 LYS A CD 1 ATOM 2613 C CE . LYS A 1 348 ? -21.269 6.138 1.397 1.00 29.50 ? 487 LYS A CE 1 ATOM 2614 N NZ . LYS A 1 348 ? -21.291 6.027 -0.098 1.00 27.69 ? 487 LYS A NZ 1 ATOM 2615 N N . VAL A 1 349 ? -17.194 6.639 5.528 1.00 23.98 ? 488 VAL A N 1 ATOM 2616 C CA . VAL A 1 349 ? -16.893 8.043 5.765 1.00 20.46 ? 488 VAL A CA 1 ATOM 2617 C C . VAL A 1 349 ? -17.115 8.863 4.501 1.00 22.12 ? 488 VAL A C 1 ATOM 2618 O O . VAL A 1 349 ? -16.752 8.441 3.401 1.00 24.60 ? 488 VAL A O 1 ATOM 2619 C CB . VAL A 1 349 ? -15.435 8.220 6.232 1.00 25.60 ? 488 VAL A CB 1 ATOM 2620 C CG1 . VAL A 1 349 ? -15.065 9.699 6.309 1.00 25.31 ? 488 VAL A CG1 1 ATOM 2621 C CG2 . VAL A 1 349 ? -15.223 7.527 7.570 1.00 28.49 ? 488 VAL A CG2 1 ATOM 2622 N N . VAL A 1 350 ? -17.728 10.031 4.659 1.00 23.97 ? 489 VAL A N 1 ATOM 2623 C CA . VAL A 1 350 ? -17.862 10.965 3.554 1.00 24.80 ? 489 VAL A CA 1 ATOM 2624 C C . VAL A 1 350 ? -17.350 12.338 3.977 1.00 23.31 ? 489 VAL A C 1 ATOM 2625 O O . VAL A 1 350 ? -17.360 12.676 5.165 1.00 27.15 ? 489 VAL A O 1 ATOM 2626 C CB . VAL A 1 350 ? -19.323 11.075 3.053 1.00 24.66 ? 489 VAL A CB 1 ATOM 2627 C CG1 . VAL A 1 350 ? -19.847 9.707 2.622 1.00 22.23 ? 489 VAL A CG1 1 ATOM 2628 C CG2 . VAL A 1 350 ? -20.215 11.683 4.123 1.00 23.42 ? 489 VAL A CG2 1 ATOM 2629 N N . GLN A 1 351 ? -16.871 13.112 3.009 1.00 26.92 ? 490 GLN A N 1 ATOM 2630 C CA . GLN A 1 351 ? -16.465 14.485 3.270 1.00 29.45 ? 490 GLN A CA 1 ATOM 2631 C C . GLN A 1 351 ? -17.590 15.438 2.884 1.00 33.92 ? 490 GLN A C 1 ATOM 2632 O O . GLN A 1 351 ? -18.104 15.377 1.771 1.00 32.62 ? 490 GLN A O 1 ATOM 2633 C CB . GLN A 1 351 ? -15.196 14.840 2.490 1.00 35.43 ? 490 GLN A CB 1 ATOM 2634 C CG . GLN A 1 351 ? -14.682 16.236 2.791 1.00 42.29 ? 490 GLN A CG 1 ATOM 2635 C CD . GLN A 1 351 ? -13.337 16.530 2.159 1.00 51.82 ? 490 GLN A CD 1 ATOM 2636 O OE1 . GLN A 1 351 ? -12.927 15.877 1.199 1.00 51.28 ? 490 GLN A OE1 1 ATOM 2637 N NE2 . GLN A 1 351 ? -12.640 17.523 2.698 1.00 56.55 ? 490 GLN A NE2 1 ATOM 2638 N N . ILE A 1 352 ? -17.972 16.315 3.806 1.00 31.89 ? 491 ILE A N 1 ATOM 2639 C CA . ILE A 1 352 ? -19.009 17.307 3.534 1.00 33.36 ? 491 ILE A CA 1 ATOM 2640 C C . ILE A 1 352 ? -18.449 18.429 2.664 1.00 38.50 ? 491 ILE A C 1 ATOM 2641 O O . ILE A 1 352 ? -17.405 19.005 2.979 1.00 40.81 ? 491 ILE A O 1 ATOM 2642 C CB . ILE A 1 352 ? -19.575 17.905 4.840 1.00 36.86 ? 491 ILE A CB 1 ATOM 2643 C CG1 . ILE A 1 352 ? -20.247 16.819 5.682 1.00 40.15 ? 491 ILE A CG1 1 ATOM 2644 C CG2 . ILE A 1 352 ? -20.555 19.039 4.537 1.00 43.18 ? 491 ILE A CG2 1 ATOM 2645 C CD1 . ILE A 1 352 ? -20.675 17.293 7.053 1.00 44.05 ? 491 ILE A CD1 1 ATOM 2646 N N . GLU A 1 353 ? -19.135 18.736 1.567 1.00 40.03 ? 492 GLU A N 1 ATOM 2647 C CA . GLU A 1 353 ? -18.672 19.790 0.674 1.00 50.13 ? 492 GLU A CA 1 ATOM 2648 C C . GLU A 1 353 ? -19.323 21.128 1.009 1.00 58.00 ? 492 GLU A C 1 ATOM 2649 O O . GLU A 1 353 ? -18.724 21.970 1.680 1.00 62.95 ? 492 GLU A O 1 ATOM 2650 C CB . GLU A 1 353 ? -18.951 19.418 -0.780 1.00 55.78 ? 492 GLU A CB 1 ATOM 2651 C CG . GLU A 1 353 ? -18.434 20.431 -1.777 1.00 61.36 ? 492 GLU A CG 1 ATOM 2652 C CD . GLU A 1 353 ? -18.682 20.012 -3.206 1.00 65.87 ? 492 GLU A CD 1 ATOM 2653 O OE1 . GLU A 1 353 ? -19.294 18.944 -3.414 1.00 67.97 ? 492 GLU A OE1 1 ATOM 2654 O OE2 . GLU A 1 353 ? -18.270 20.756 -4.117 1.00 64.50 ? 492 GLU A OE2 1 HETATM 2655 C C1 . NAG B 2 . ? -24.979 -8.281 -2.238 1.00 34.84 ? 601 NAG A C1 1 HETATM 2656 C C2 . NAG B 2 . ? -24.776 -9.564 -3.045 1.00 43.50 ? 601 NAG A C2 1 HETATM 2657 C C3 . NAG B 2 . ? -24.294 -9.260 -4.462 1.00 45.86 ? 601 NAG A C3 1 HETATM 2658 C C4 . NAG B 2 . ? -25.174 -8.206 -5.123 1.00 46.64 ? 601 NAG A C4 1 HETATM 2659 C C5 . NAG B 2 . ? -25.310 -7.001 -4.204 1.00 42.25 ? 601 NAG A C5 1 HETATM 2660 C C6 . NAG B 2 . ? -26.187 -5.912 -4.812 1.00 42.29 ? 601 NAG A C6 1 HETATM 2661 C C7 . NAG B 2 . ? -24.212 -11.424 -1.568 1.00 44.57 ? 601 NAG A C7 1 HETATM 2662 C C8 . NAG B 2 . ? -23.100 -12.168 -0.888 1.00 42.19 ? 601 NAG A C8 1 HETATM 2663 N N2 . NAG B 2 . ? -23.826 -10.450 -2.394 1.00 43.00 ? 601 NAG A N2 1 HETATM 2664 O O3 . NAG B 2 . ? -24.318 -10.463 -5.239 1.00 44.01 ? 601 NAG A O3 1 HETATM 2665 O O4 . NAG B 2 . ? -24.597 -7.798 -6.370 1.00 46.59 ? 601 NAG A O4 1 HETATM 2666 O O5 . NAG B 2 . ? -25.871 -7.436 -2.967 1.00 39.43 ? 601 NAG A O5 1 HETATM 2667 O O6 . NAG B 2 . ? -27.566 -6.220 -4.590 1.00 45.45 ? 601 NAG A O6 1 HETATM 2668 O O7 . NAG B 2 . ? -25.388 -11.694 -1.374 1.00 43.52 ? 601 NAG A O7 1 HETATM 2669 C C1 . NAG C 2 . ? -34.807 3.513 8.798 1.00 57.70 ? 602 NAG A C1 1 HETATM 2670 C C2 . NAG C 2 . ? -36.154 2.902 9.176 1.00 67.31 ? 602 NAG A C2 1 HETATM 2671 C C3 . NAG C 2 . ? -36.578 3.423 10.544 1.00 69.08 ? 602 NAG A C3 1 HETATM 2672 C C4 . NAG C 2 . ? -35.486 3.142 11.569 1.00 68.85 ? 602 NAG A C4 1 HETATM 2673 C C5 . NAG C 2 . ? -34.138 3.662 11.083 1.00 66.61 ? 602 NAG A C5 1 HETATM 2674 C C6 . NAG C 2 . ? -33.028 3.267 12.053 1.00 64.58 ? 602 NAG A C6 1 HETATM 2675 C C7 . NAG C 2 . ? -37.795 2.242 7.485 1.00 76.81 ? 602 NAG A C7 1 HETATM 2676 C C8 . NAG C 2 . ? -38.862 2.723 6.545 1.00 76.07 ? 602 NAG A C8 1 HETATM 2677 N N2 . NAG C 2 . ? -37.164 3.196 8.173 1.00 72.92 ? 602 NAG A N2 1 HETATM 2678 O O3 . NAG C 2 . ? -37.798 2.796 10.958 1.00 68.72 ? 602 NAG A O3 1 HETATM 2679 O O4 . NAG C 2 . ? -35.818 3.771 12.812 1.00 68.95 ? 602 NAG A O4 1 HETATM 2680 O O5 . NAG C 2 . ? -33.846 3.137 9.785 1.00 63.24 ? 602 NAG A O5 1 HETATM 2681 O O6 . NAG C 2 . ? -32.974 1.841 12.166 1.00 62.47 ? 602 NAG A O6 1 HETATM 2682 O O7 . NAG C 2 . ? -37.533 1.054 7.605 1.00 77.51 ? 602 NAG A O7 1 HETATM 2683 C C1 . NAG D 2 . ? -17.646 -11.494 26.020 1.00 21.23 ? 603 NAG A C1 1 HETATM 2684 C C2 . NAG D 2 . ? -16.244 -11.828 26.542 1.00 20.59 ? 603 NAG A C2 1 HETATM 2685 C C3 . NAG D 2 . ? -16.344 -12.403 27.957 1.00 27.86 ? 603 NAG A C3 1 HETATM 2686 C C4 . NAG D 2 . ? -17.040 -11.391 28.849 1.00 31.70 ? 603 NAG A C4 1 HETATM 2687 C C5 . NAG D 2 . ? -18.419 -11.140 28.260 1.00 30.77 ? 603 NAG A C5 1 HETATM 2688 C C6 . NAG D 2 . ? -19.239 -10.195 29.132 1.00 26.84 ? 603 NAG A C6 1 HETATM 2689 C C7 . NAG D 2 . ? -14.353 -12.525 25.154 1.00 23.08 ? 603 NAG A C7 1 HETATM 2690 C C8 . NAG D 2 . ? -13.705 -13.663 24.415 1.00 22.38 ? 603 NAG A C8 1 HETATM 2691 N N2 . NAG D 2 . ? -15.553 -12.779 25.681 1.00 22.02 ? 603 NAG A N2 1 HETATM 2692 O O3 . NAG D 2 . ? -15.049 -12.709 28.484 1.00 28.47 ? 603 NAG A O3 1 HETATM 2693 O O4 . NAG D 2 . ? -17.136 -11.882 30.191 1.00 37.82 ? 603 NAG A O4 1 HETATM 2694 O O5 . NAG D 2 . ? -18.255 -10.587 26.948 1.00 29.83 ? 603 NAG A O5 1 HETATM 2695 O O6 . NAG D 2 . ? -18.637 -8.898 29.128 1.00 26.90 ? 603 NAG A O6 1 HETATM 2696 O O7 . NAG D 2 . ? -13.805 -11.440 25.258 1.00 22.35 ? 603 NAG A O7 1 HETATM 2697 C C1 . NAG E 2 . ? -15.795 -13.817 -8.449 1.00 24.70 ? 604 NAG A C1 1 HETATM 2698 C C2 . NAG E 2 . ? -15.221 -12.969 -9.589 1.00 28.46 ? 604 NAG A C2 1 HETATM 2699 C C3 . NAG E 2 . ? -15.289 -13.693 -10.932 1.00 33.88 ? 604 NAG A C3 1 HETATM 2700 C C4 . NAG E 2 . ? -14.751 -15.112 -10.826 1.00 37.93 ? 604 NAG A C4 1 HETATM 2701 C C5 . NAG E 2 . ? -15.390 -15.837 -9.650 1.00 32.51 ? 604 NAG A C5 1 HETATM 2702 C C6 . NAG E 2 . ? -14.778 -17.222 -9.500 1.00 31.67 ? 604 NAG A C6 1 HETATM 2703 C C7 . NAG E 2 . ? -15.285 -10.529 -9.565 1.00 35.15 ? 604 NAG A C7 1 HETATM 2704 C C8 . NAG E 2 . ? -16.130 -9.312 -9.801 1.00 39.33 ? 604 NAG A C8 1 HETATM 2705 N N2 . NAG E 2 . ? -15.911 -11.697 -9.710 1.00 33.15 ? 604 NAG A N2 1 HETATM 2706 O O3 . NAG E 2 . ? -14.513 -12.967 -11.895 1.00 32.52 ? 604 NAG A O3 1 HETATM 2707 O O4 . NAG E 2 . ? -15.047 -15.828 -12.031 1.00 42.55 ? 604 NAG A O4 1 HETATM 2708 O O5 . NAG E 2 . ? -15.155 -15.094 -8.458 1.00 30.84 ? 604 NAG A O5 1 HETATM 2709 O O6 . NAG E 2 . ? -13.370 -17.078 -9.287 1.00 34.70 ? 604 NAG A O6 1 HETATM 2710 O O7 . NAG E 2 . ? -14.105 -10.447 -9.261 1.00 38.07 ? 604 NAG A O7 1 HETATM 2711 C C1 . NAG F 2 . ? -33.007 -15.604 11.883 1.00 27.25 ? 605 NAG A C1 1 HETATM 2712 C C2 . NAG F 2 . ? -34.487 -15.480 12.241 1.00 37.28 ? 605 NAG A C2 1 HETATM 2713 C C3 . NAG F 2 . ? -35.326 -16.566 11.581 1.00 47.16 ? 605 NAG A C3 1 HETATM 2714 C C4 . NAG F 2 . ? -35.053 -16.623 10.088 1.00 45.73 ? 605 NAG A C4 1 HETATM 2715 C C5 . NAG F 2 . ? -33.556 -16.684 9.819 1.00 39.80 ? 605 NAG A C5 1 HETATM 2716 C C6 . NAG F 2 . ? -33.303 -16.607 8.320 1.00 39.68 ? 605 NAG A C6 1 HETATM 2717 C C7 . NAG F 2 . ? -35.020 -14.434 14.336 1.00 53.57 ? 605 NAG A C7 1 HETATM 2718 C C8 . NAG F 2 . ? -34.896 -14.490 15.830 1.00 56.46 ? 605 NAG A C8 1 HETATM 2719 N N2 . NAG F 2 . ? -34.675 -15.534 13.678 1.00 45.44 ? 605 NAG A N2 1 HETATM 2720 O O3 . NAG F 2 . ? -36.712 -16.274 11.780 1.00 55.20 ? 605 NAG A O3 1 HETATM 2721 O O4 . NAG F 2 . ? -35.683 -17.787 9.539 1.00 48.63 ? 605 NAG A O4 1 HETATM 2722 O O5 . NAG F 2 . ? -32.894 -15.595 10.460 1.00 33.07 ? 605 NAG A O5 1 HETATM 2723 O O6 . NAG F 2 . ? -31.894 -16.620 8.079 1.00 36.77 ? 605 NAG A O6 1 HETATM 2724 O O7 . NAG F 2 . ? -35.413 -13.441 13.747 1.00 56.26 ? 605 NAG A O7 1 HETATM 2725 C C1 . NAG G 2 . ? -20.010 -22.163 32.637 1.00 37.47 ? 606 NAG A C1 1 HETATM 2726 C C2 . NAG G 2 . ? -21.242 -21.918 33.510 1.00 43.12 ? 606 NAG A C2 1 HETATM 2727 C C3 . NAG G 2 . ? -20.930 -22.248 34.962 1.00 51.06 ? 606 NAG A C3 1 HETATM 2728 C C4 . NAG G 2 . ? -20.419 -23.677 35.057 1.00 56.92 ? 606 NAG A C4 1 HETATM 2729 C C5 . NAG G 2 . ? -19.228 -23.880 34.130 1.00 54.24 ? 606 NAG A C5 1 HETATM 2730 C C6 . NAG G 2 . ? -18.796 -25.342 34.160 1.00 57.13 ? 606 NAG A C6 1 HETATM 2731 C C7 . NAG G 2 . ? -22.818 -20.225 32.771 1.00 49.39 ? 606 NAG A C7 1 HETATM 2732 C C8 . NAG G 2 . ? -23.231 -18.785 32.854 1.00 49.17 ? 606 NAG A C8 1 HETATM 2733 N N2 . NAG G 2 . ? -21.702 -20.544 33.423 1.00 45.96 ? 606 NAG A N2 1 HETATM 2734 O O3 . NAG G 2 . ? -22.109 -22.091 35.760 1.00 49.93 ? 606 NAG A O3 1 HETATM 2735 O O4 . NAG G 2 . ? -20.020 -23.947 36.405 1.00 63.05 ? 606 NAG A O4 1 HETATM 2736 O O5 . NAG G 2 . ? -19.580 -23.520 32.791 1.00 46.26 ? 606 NAG A O5 1 HETATM 2737 O O6 . NAG G 2 . ? -17.415 -25.448 33.796 1.00 60.58 ? 606 NAG A O6 1 HETATM 2738 O O7 . NAG G 2 . ? -23.460 -21.053 32.147 1.00 52.90 ? 606 NAG A O7 1 HETATM 2739 C C1 . NAG H 2 . ? -30.683 -25.751 25.827 1.00 47.67 ? 607 NAG A C1 1 HETATM 2740 C C2 . NAG H 2 . ? -30.674 -26.433 27.192 1.00 61.05 ? 607 NAG A C2 1 HETATM 2741 C C3 . NAG H 2 . ? -32.038 -27.017 27.543 1.00 60.52 ? 607 NAG A C3 1 HETATM 2742 C C4 . NAG H 2 . ? -33.177 -26.052 27.242 1.00 58.52 ? 607 NAG A C4 1 HETATM 2743 C C5 . NAG H 2 . ? -33.029 -25.437 25.860 1.00 59.89 ? 607 NAG A C5 1 HETATM 2744 C C6 . NAG H 2 . ? -34.116 -24.399 25.616 1.00 60.35 ? 607 NAG A C6 1 HETATM 2745 C C7 . NAG H 2 . ? -28.413 -27.339 27.411 1.00 83.45 ? 607 NAG A C7 1 HETATM 2746 C C8 . NAG H 2 . ? -27.554 -28.535 27.136 1.00 84.73 ? 607 NAG A C8 1 HETATM 2747 N N2 . NAG H 2 . ? -29.712 -27.518 27.186 1.00 73.86 ? 607 NAG A N2 1 HETATM 2748 O O3 . NAG H 2 . ? -32.064 -27.348 28.937 1.00 61.74 ? 607 NAG A O3 1 HETATM 2749 O O4 . NAG H 2 . ? -34.415 -26.768 27.279 1.00 52.39 ? 607 NAG A O4 1 HETATM 2750 O O5 . NAG H 2 . ? -31.754 -24.814 25.760 1.00 54.87 ? 607 NAG A O5 1 HETATM 2751 O O6 . NAG H 2 . ? -34.117 -24.039 24.231 1.00 66.14 ? 607 NAG A O6 1 HETATM 2752 O O7 . NAG H 2 . ? -27.950 -26.282 27.809 1.00 88.18 ? 607 NAG A O7 1 HETATM 2753 C C1 . NAG I 2 . ? -34.909 -25.209 -2.422 1.00 40.12 ? 608 NAG A C1 1 HETATM 2754 C C2 . NAG I 2 . ? -36.123 -25.858 -3.093 1.00 43.94 ? 608 NAG A C2 1 HETATM 2755 C C3 . NAG I 2 . ? -37.400 -25.730 -2.267 1.00 49.25 ? 608 NAG A C3 1 HETATM 2756 C C4 . NAG I 2 . ? -37.151 -25.991 -0.789 1.00 53.38 ? 608 NAG A C4 1 HETATM 2757 C C5 . NAG I 2 . ? -35.958 -25.183 -0.303 1.00 61.69 ? 608 NAG A C5 1 HETATM 2758 C C6 . NAG I 2 . ? -35.702 -25.428 1.180 1.00 67.91 ? 608 NAG A C6 1 HETATM 2759 C C7 . NAG I 2 . ? -36.032 -25.877 -5.528 1.00 38.75 ? 608 NAG A C7 1 HETATM 2760 C C8 . NAG I 2 . ? -36.476 -25.213 -6.799 1.00 34.99 ? 608 NAG A C8 1 HETATM 2761 N N2 . NAG I 2 . ? -36.341 -25.251 -4.393 1.00 40.92 ? 608 NAG A N2 1 HETATM 2762 O O3 . NAG I 2 . ? -38.365 -26.644 -2.741 1.00 39.90 ? 608 NAG A O3 1 HETATM 2763 O O4 . NAG I 2 . ? -38.297 -25.623 -0.054 1.00 53.36 ? 608 NAG A O4 1 HETATM 2764 O O5 . NAG I 2 . ? -34.816 -25.543 -1.051 1.00 48.39 ? 608 NAG A O5 1 HETATM 2765 O O6 . NAG I 2 . ? -35.424 -24.201 1.817 1.00 76.59 ? 608 NAG A O6 1 HETATM 2766 O O7 . NAG I 2 . ? -35.408 -26.936 -5.560 1.00 27.99 ? 608 NAG A O7 1 HETATM 2767 C C1 . NAG J 2 . ? -10.458 -32.226 16.916 1.00 37.37 ? 609 NAG A C1 1 HETATM 2768 C C2 . NAG J 2 . ? -9.059 -32.614 16.438 1.00 47.47 ? 609 NAG A C2 1 HETATM 2769 C C3 . NAG J 2 . ? -9.095 -33.862 15.566 1.00 52.65 ? 609 NAG A C3 1 HETATM 2770 C C4 . NAG J 2 . ? -9.888 -34.966 16.249 1.00 51.98 ? 609 NAG A C4 1 HETATM 2771 C C5 . NAG J 2 . ? -11.256 -34.436 16.660 1.00 49.36 ? 609 NAG A C5 1 HETATM 2772 C C6 . NAG J 2 . ? -12.095 -35.518 17.329 1.00 55.22 ? 609 NAG A C6 1 HETATM 2773 C C7 . NAG J 2 . ? -7.230 -31.087 16.005 1.00 60.17 ? 609 NAG A C7 1 HETATM 2774 C C8 . NAG J 2 . ? -6.633 -30.100 15.046 1.00 64.36 ? 609 NAG A C8 1 HETATM 2775 N N2 . NAG J 2 . ? -8.445 -31.530 15.695 1.00 52.00 ? 609 NAG A N2 1 HETATM 2776 O O3 . NAG J 2 . ? -7.755 -34.309 15.330 1.00 59.30 ? 609 NAG A O3 1 HETATM 2777 O O4 . NAG J 2 . ? -10.044 -36.068 15.348 1.00 54.40 ? 609 NAG A O4 1 HETATM 2778 O O5 . NAG J 2 . ? -11.078 -33.341 17.558 1.00 42.36 ? 609 NAG A O5 1 HETATM 2779 O O6 . NAG J 2 . ? -11.382 -36.045 18.456 1.00 59.53 ? 609 NAG A O6 1 HETATM 2780 O O7 . NAG J 2 . ? -6.639 -31.461 17.005 1.00 60.60 ? 609 NAG A O7 1 HETATM 2781 C C1 . NAG K 2 . ? -22.016 -35.932 15.589 1.00 64.15 ? 610 NAG A C1 1 HETATM 2782 C C2 . NAG K 2 . ? -20.778 -36.556 16.222 1.00 70.97 ? 610 NAG A C2 1 HETATM 2783 C C3 . NAG K 2 . ? -21.077 -37.993 16.621 1.00 74.15 ? 610 NAG A C3 1 HETATM 2784 C C4 . NAG K 2 . ? -22.269 -38.007 17.568 1.00 72.19 ? 610 NAG A C4 1 HETATM 2785 C C5 . NAG K 2 . ? -23.454 -37.262 16.955 1.00 70.50 ? 610 NAG A C5 1 HETATM 2786 C C6 . NAG K 2 . ? -24.605 -37.159 17.950 1.00 71.36 ? 610 NAG A C6 1 HETATM 2787 C C7 . NAG K 2 . ? -18.590 -35.709 15.623 1.00 75.16 ? 610 NAG A C7 1 HETATM 2788 C C8 . NAG K 2 . ? -18.636 -35.031 16.961 1.00 74.86 ? 610 NAG A C8 1 HETATM 2789 N N2 . NAG K 2 . ? -19.631 -36.488 15.335 1.00 72.89 ? 610 NAG A N2 1 HETATM 2790 O O3 . NAG K 2 . ? -19.935 -38.568 17.267 1.00 76.98 ? 610 NAG A O3 1 HETATM 2791 O O4 . NAG K 2 . ? -22.639 -39.362 17.850 1.00 71.79 ? 610 NAG A O4 1 HETATM 2792 O O5 . NAG K 2 . ? -23.071 -35.944 16.553 1.00 67.55 ? 610 NAG A O5 1 HETATM 2793 O O6 . NAG K 2 . ? -25.186 -38.452 18.156 1.00 72.66 ? 610 NAG A O6 1 HETATM 2794 O O7 . NAG K 2 . ? -17.656 -35.556 14.853 1.00 74.96 ? 610 NAG A O7 1 HETATM 2795 C C1 . NAG L 2 . ? -24.853 -11.380 24.434 1.00 45.38 ? 611 NAG A C1 1 HETATM 2796 C C2 . NAG L 2 . ? -24.609 -9.929 24.827 1.00 52.83 ? 611 NAG A C2 1 HETATM 2797 C C3 . NAG L 2 . ? -25.851 -9.391 25.524 1.00 55.35 ? 611 NAG A C3 1 HETATM 2798 C C4 . NAG L 2 . ? -27.077 -9.593 24.640 1.00 60.51 ? 611 NAG A C4 1 HETATM 2799 C C5 . NAG L 2 . ? -27.172 -11.022 24.109 1.00 59.93 ? 611 NAG A C5 1 HETATM 2800 C C6 . NAG L 2 . ? -28.296 -11.133 23.083 1.00 60.76 ? 611 NAG A C6 1 HETATM 2801 C C7 . NAG L 2 . ? -22.303 -9.249 25.272 1.00 54.07 ? 611 NAG A C7 1 HETATM 2802 C C8 . NAG L 2 . ? -22.321 -8.627 23.908 1.00 50.01 ? 611 NAG A C8 1 HETATM 2803 N N2 . NAG L 2 . ? -23.442 -9.807 25.683 1.00 53.92 ? 611 NAG A N2 1 HETATM 2804 O O3 . NAG L 2 . ? -25.681 -7.997 25.799 1.00 55.54 ? 611 NAG A O3 1 HETATM 2805 O O4 . NAG L 2 . ? -28.258 -9.300 25.396 1.00 64.56 ? 611 NAG A O4 1 HETATM 2806 O O5 . NAG L 2 . ? -25.936 -11.418 23.507 1.00 53.87 ? 611 NAG A O5 1 HETATM 2807 O O6 . NAG L 2 . ? -28.507 -12.506 22.730 1.00 59.27 ? 611 NAG A O6 1 HETATM 2808 O O7 . NAG L 2 . ? -21.299 -9.239 25.966 1.00 56.36 ? 611 NAG A O7 1 HETATM 2809 N N1 . EPE M 3 . ? -4.940 7.380 17.479 1.00 25.42 ? 612 EPE A N1 1 HETATM 2810 C C2 . EPE M 3 . ? -5.947 6.572 18.219 1.00 24.57 ? 612 EPE A C2 1 HETATM 2811 C C3 . EPE M 3 . ? -7.223 6.376 17.376 1.00 22.04 ? 612 EPE A C3 1 HETATM 2812 N N4 . EPE M 3 . ? -6.901 5.888 15.996 1.00 21.15 ? 612 EPE A N4 1 HETATM 2813 C C5 . EPE M 3 . ? -5.923 6.769 15.316 1.00 22.30 ? 612 EPE A C5 1 HETATM 2814 C C6 . EPE M 3 . ? -4.636 6.801 16.146 1.00 28.12 ? 612 EPE A C6 1 HETATM 2815 C C7 . EPE M 3 . ? -8.155 5.628 15.223 1.00 24.42 ? 612 EPE A C7 1 HETATM 2816 C C8 . EPE M 3 . ? -7.965 5.028 13.837 1.00 30.95 ? 612 EPE A C8 1 HETATM 2817 O O8 . EPE M 3 . ? -7.162 5.495 13.052 1.00 34.44 ? 612 EPE A O8 1 HETATM 2818 C C9 . EPE M 3 . ? -3.686 7.603 18.263 1.00 29.39 ? 612 EPE A C9 1 HETATM 2819 C C10 . EPE M 3 . ? -3.939 8.668 19.319 1.00 34.97 ? 612 EPE A C10 1 HETATM 2820 S S . EPE M 3 . ? -2.421 8.965 20.177 1.00 29.77 ? 612 EPE A S 1 HETATM 2821 O O1S . EPE M 3 . ? -1.445 9.482 19.003 1.00 22.89 ? 612 EPE A O1S 1 HETATM 2822 O O2S . EPE M 3 . ? -1.562 7.697 20.579 1.00 28.75 ? 612 EPE A O2S 1 HETATM 2823 O O3S . EPE M 3 . ? -2.352 10.145 21.238 1.00 31.42 ? 612 EPE A O3S 1 HETATM 2824 C C13 . 0LK N 4 . ? -3.826 -15.860 13.835 1.00 24.04 ? 613 0LK A C13 1 HETATM 2825 C C15 . 0LK N 4 . ? -4.055 -15.773 16.236 1.00 21.55 ? 613 0LK A C15 1 HETATM 2826 C C20 . 0LK N 4 . ? -5.428 -15.251 18.717 1.00 23.78 ? 613 0LK A C20 1 HETATM 2827 C C21 . 0LK N 4 . ? -6.143 -15.369 17.540 1.00 22.03 ? 613 0LK A C21 1 HETATM 2828 C C22 . 0LK N 4 . ? -5.486 -15.623 16.293 1.00 19.62 ? 613 0LK A C22 1 HETATM 2829 C C01 . 0LK N 4 . ? -4.784 -15.091 7.193 1.00 25.62 ? 613 0LK A C01 1 HETATM 2830 C C02 . 0LK N 4 . ? -4.190 -15.827 8.264 1.00 28.41 ? 613 0LK A C02 1 HETATM 2831 C C03 . 0LK N 4 . ? -3.257 -15.232 9.049 1.00 24.48 ? 613 0LK A C03 1 HETATM 2832 C C04 . 0LK N 4 . ? -2.902 -13.917 8.784 1.00 24.04 ? 613 0LK A C04 1 HETATM 2833 C C05 . 0LK N 4 . ? -3.483 -13.185 7.737 1.00 25.40 ? 613 0LK A C05 1 HETATM 2834 C C06 . 0LK N 4 . ? -4.426 -13.794 6.949 1.00 26.56 ? 613 0LK A C06 1 HETATM 2835 C C07 . 0LK N 4 . ? -2.512 -15.785 10.184 1.00 24.93 ? 613 0LK A C07 1 HETATM 2836 C C08 . 0LK N 4 . ? -1.364 -14.651 10.415 1.00 28.58 ? 613 0LK A C08 1 HETATM 2837 C C09 . 0LK N 4 . ? -1.866 -13.442 9.745 1.00 25.32 ? 613 0LK A C09 1 HETATM 2838 N N10 . 0LK N 4 . ? -0.038 -15.085 9.775 1.00 30.39 ? 613 0LK A N10 1 HETATM 2839 N N11 . 0LK N 4 . ? -3.359 -15.978 11.459 1.00 29.85 ? 613 0LK A N11 1 HETATM 2840 C C12 . 0LK N 4 . ? -2.895 -16.130 12.693 1.00 27.09 ? 613 0LK A C12 1 HETATM 2841 N N14 . 0LK N 4 . ? -3.381 -15.995 15.067 1.00 20.20 ? 613 0LK A N14 1 HETATM 2842 O O16 . 0LK N 4 . ? -5.064 -15.502 13.519 1.00 21.74 ? 613 0LK A O16 1 HETATM 2843 O O17 . 0LK N 4 . ? -1.719 -16.487 12.907 1.00 24.63 ? 613 0LK A O17 1 HETATM 2844 C C18 . 0LK N 4 . ? -3.356 -15.637 17.417 1.00 18.50 ? 613 0LK A C18 1 HETATM 2845 C C19 . 0LK N 4 . ? -4.060 -15.374 18.687 1.00 22.06 ? 613 0LK A C19 1 HETATM 2846 CL CL . 0LK N 4 . ? -6.280 -14.934 20.209 1.00 25.94 ? 613 0LK A CL 1 HETATM 2847 F F24 . 0LK N 4 . ? -7.452 -15.254 17.561 1.00 21.42 ? 613 0LK A F24 1 HETATM 2848 C C25 . 0LK N 4 . ? 0.597 -16.134 10.042 1.00 36.95 ? 613 0LK A C25 1 HETATM 2849 N N26 . 0LK N 4 . ? 0.180 -17.047 10.999 1.00 28.45 ? 613 0LK A N26 1 HETATM 2850 N N27 . 0LK N 4 . ? 1.793 -16.412 9.367 1.00 43.92 ? 613 0LK A N27 1 HETATM 2851 O O . HOH O 5 . ? 2.986 -19.308 10.665 1.00 50.73 ? 501 HOH A O 1 HETATM 2852 O O . HOH O 5 . ? 3.786 -17.117 12.131 1.00 49.03 ? 502 HOH A O 1 HETATM 2853 O O . HOH O 5 . ? 4.725 -15.554 10.521 1.00 52.08 ? 503 HOH A O 1 HETATM 2854 O O . HOH O 5 . ? 2.501 -14.469 12.552 1.00 22.53 ? 504 HOH A O 1 HETATM 2855 O O . HOH O 5 . ? -4.733 -10.942 10.934 1.00 31.50 ? 505 HOH A O 1 HETATM 2856 O O . HOH O 5 . ? -9.595 -9.994 22.175 1.00 19.61 ? 701 HOH A O 1 HETATM 2857 O O . HOH O 5 . ? -0.970 -12.456 18.440 1.00 24.39 ? 702 HOH A O 1 HETATM 2858 O O . HOH O 5 . ? -14.694 -12.286 1.514 1.00 22.02 ? 703 HOH A O 1 HETATM 2859 O O . HOH O 5 . ? -18.575 1.248 2.436 1.00 25.89 ? 704 HOH A O 1 HETATM 2860 O O . HOH O 5 . ? -15.144 4.659 4.617 1.00 24.94 ? 705 HOH A O 1 HETATM 2861 O O . HOH O 5 . ? -18.887 -0.266 4.705 1.00 22.51 ? 706 HOH A O 1 HETATM 2862 O O . HOH O 5 . ? -1.599 -18.185 26.930 1.00 23.19 ? 707 HOH A O 1 HETATM 2863 O O . HOH O 5 . ? -8.460 -7.181 22.209 1.00 20.89 ? 708 HOH A O 1 HETATM 2864 O O . HOH O 5 . ? -7.049 3.132 32.750 1.00 23.15 ? 709 HOH A O 1 HETATM 2865 O O . HOH O 5 . ? -16.760 -9.354 17.573 1.00 30.01 ? 710 HOH A O 1 HETATM 2866 O O . HOH O 5 . ? -16.586 -16.581 -0.934 1.00 23.56 ? 711 HOH A O 1 HETATM 2867 O O . HOH O 5 . ? -16.942 -6.649 18.349 1.00 27.09 ? 712 HOH A O 1 HETATM 2868 O O . HOH O 5 . ? -21.194 -9.169 9.919 1.00 25.34 ? 714 HOH A O 1 HETATM 2869 O O . HOH O 5 . ? -14.656 -12.339 17.770 1.00 22.67 ? 715 HOH A O 1 HETATM 2870 O O . HOH O 5 . ? -15.397 -9.148 24.648 1.00 23.09 ? 716 HOH A O 1 HETATM 2871 O O . HOH O 5 . ? -17.359 -19.263 -1.137 1.00 28.38 ? 717 HOH A O 1 HETATM 2872 O O . HOH O 5 . ? -8.403 9.074 19.085 1.00 25.76 ? 718 HOH A O 1 HETATM 2873 O O . HOH O 5 . ? -15.411 -7.725 26.956 1.00 24.13 ? 719 HOH A O 1 HETATM 2874 O O . HOH O 5 . ? -0.884 -15.398 27.690 1.00 25.89 ? 720 HOH A O 1 HETATM 2875 O O . HOH O 5 . ? -10.672 -2.286 3.499 1.00 29.99 ? 721 HOH A O 1 HETATM 2876 O O . HOH O 5 . ? -19.640 9.196 21.360 1.00 36.67 ? 722 HOH A O 1 HETATM 2877 O O . HOH O 5 . ? -0.556 -19.203 29.261 1.00 30.23 ? 723 HOH A O 1 HETATM 2878 O O . HOH O 5 . ? -12.305 3.537 2.193 1.00 27.84 ? 724 HOH A O 1 HETATM 2879 O O . HOH O 5 . ? -22.761 1.651 21.332 1.00 33.16 ? 725 HOH A O 1 HETATM 2880 O O . HOH O 5 . ? -20.824 -8.787 1.018 1.00 29.91 ? 726 HOH A O 1 HETATM 2881 O O . HOH O 5 . ? -17.697 -14.291 31.122 1.00 30.48 ? 727 HOH A O 1 HETATM 2882 O O . HOH O 5 . ? -16.284 2.329 26.099 1.00 27.63 ? 728 HOH A O 1 HETATM 2883 O O . HOH O 5 . ? -12.792 5.512 5.308 1.00 35.56 ? 729 HOH A O 1 HETATM 2884 O O . HOH O 5 . ? -3.735 -14.014 32.229 1.00 29.78 ? 730 HOH A O 1 HETATM 2885 O O . HOH O 5 . ? -3.042 -5.087 33.391 1.00 23.93 ? 731 HOH A O 1 HETATM 2886 O O . HOH O 5 . ? -30.617 -9.023 9.285 1.00 30.86 ? 733 HOH A O 1 HETATM 2887 O O . HOH O 5 . ? -20.920 -10.733 14.670 1.00 29.27 ? 734 HOH A O 1 HETATM 2888 O O . HOH O 5 . ? -10.994 -13.545 2.271 1.00 27.57 ? 735 HOH A O 1 HETATM 2889 O O . HOH O 5 . ? -25.059 -22.306 24.769 1.00 28.37 ? 736 HOH A O 1 HETATM 2890 O O . HOH O 5 . ? -7.876 -7.797 4.339 1.00 36.52 ? 737 HOH A O 1 HETATM 2891 O O . HOH O 5 . ? -10.888 -27.629 15.614 1.00 28.96 ? 738 HOH A O 1 HETATM 2892 O O . HOH O 5 . ? -12.881 -12.459 -6.436 1.00 32.71 ? 739 HOH A O 1 HETATM 2893 O O . HOH O 5 . ? -32.330 7.302 3.284 1.00 32.28 ? 740 HOH A O 1 HETATM 2894 O O . HOH O 5 . ? 9.605 -10.316 23.557 1.00 39.21 ? 741 HOH A O 1 HETATM 2895 O O . HOH O 5 . ? -14.979 -19.505 0.511 1.00 28.27 ? 742 HOH A O 1 HETATM 2896 O O . HOH O 5 . ? -18.792 -9.254 14.787 1.00 33.08 ? 743 HOH A O 1 HETATM 2897 O O . HOH O 5 . ? -15.943 -17.814 25.342 1.00 29.54 ? 744 HOH A O 1 HETATM 2898 O O . HOH O 5 . ? 0.383 -23.862 14.556 1.00 37.58 ? 745 HOH A O 1 HETATM 2899 O O . HOH O 5 . ? -17.524 -26.828 -2.038 1.00 29.36 ? 746 HOH A O 1 HETATM 2900 O O . HOH O 5 . ? -6.368 10.209 17.404 1.00 34.34 ? 747 HOH A O 1 HETATM 2901 O O . HOH O 5 . ? -11.143 -11.502 29.081 1.00 33.85 ? 748 HOH A O 1 HETATM 2902 O O . HOH O 5 . ? -11.075 -11.279 24.143 1.00 26.54 ? 749 HOH A O 1 HETATM 2903 O O . HOH O 5 . ? -26.185 -11.860 1.415 1.00 31.86 ? 750 HOH A O 1 HETATM 2904 O O . HOH O 5 . ? -13.806 -27.972 13.227 1.00 29.50 ? 751 HOH A O 1 HETATM 2905 O O . HOH O 5 . ? 3.012 -8.791 29.284 1.00 40.74 ? 752 HOH A O 1 HETATM 2906 O O . HOH O 5 . ? -16.408 -2.732 6.432 1.00 28.56 ? 753 HOH A O 1 HETATM 2907 O O . HOH O 5 . ? -9.853 -14.578 7.977 1.00 32.28 ? 754 HOH A O 1 HETATM 2908 O O . HOH O 5 . ? 3.236 -13.864 29.873 1.00 34.20 ? 755 HOH A O 1 HETATM 2909 O O . HOH O 5 . ? -13.812 -1.993 31.674 1.00 34.56 ? 756 HOH A O 1 HETATM 2910 O O . HOH O 5 . ? -14.399 -9.880 16.511 1.00 32.89 ? 757 HOH A O 1 HETATM 2911 O O . HOH O 5 . ? -12.488 7.493 34.552 1.00 30.73 ? 758 HOH A O 1 HETATM 2912 O O . HOH O 5 . ? -0.497 -29.007 30.155 1.00 40.06 ? 759 HOH A O 1 HETATM 2913 O O . HOH O 5 . ? -30.149 -13.038 4.214 1.00 29.95 ? 760 HOH A O 1 HETATM 2914 O O . HOH O 5 . ? -27.893 -6.000 0.103 1.00 41.05 ? 761 HOH A O 1 HETATM 2915 O O . HOH O 5 . ? -2.287 -22.640 36.076 1.00 31.29 ? 762 HOH A O 1 HETATM 2916 O O . HOH O 5 . ? -7.545 -28.070 33.760 1.00 34.15 ? 763 HOH A O 1 HETATM 2917 O O . HOH O 5 . ? -12.585 -3.929 4.443 1.00 26.65 ? 764 HOH A O 1 HETATM 2918 O O . HOH O 5 . ? -19.735 -18.627 34.179 1.00 42.18 ? 765 HOH A O 1 HETATM 2919 O O . HOH O 5 . ? -27.403 -6.351 7.405 1.00 42.05 ? 766 HOH A O 1 HETATM 2920 O O . HOH O 5 . ? -16.764 8.846 28.214 1.00 32.44 ? 767 HOH A O 1 HETATM 2921 O O . HOH O 5 . ? -13.211 -11.201 28.189 1.00 39.96 ? 768 HOH A O 1 HETATM 2922 O O . HOH O 5 . ? -12.950 -4.116 30.776 1.00 37.31 ? 769 HOH A O 1 HETATM 2923 O O . HOH O 5 . ? -27.526 -13.620 2.851 1.00 30.96 ? 770 HOH A O 1 HETATM 2924 O O . HOH O 5 . ? -16.271 -25.741 -5.296 1.00 41.07 ? 771 HOH A O 1 HETATM 2925 O O . HOH O 5 . ? -31.271 -17.875 14.532 1.00 35.59 ? 772 HOH A O 1 HETATM 2926 O O . HOH O 5 . ? 6.914 -22.708 29.701 1.00 36.51 ? 773 HOH A O 1 HETATM 2927 O O . HOH O 5 . ? -30.050 -2.725 1.179 1.00 35.09 ? 774 HOH A O 1 HETATM 2928 O O . HOH O 5 . ? -1.956 -2.064 32.996 1.00 45.60 ? 775 HOH A O 1 HETATM 2929 O O . HOH O 5 . ? -15.432 -12.907 -14.552 1.00 53.18 ? 776 HOH A O 1 HETATM 2930 O O . HOH O 5 . ? 0.190 -11.588 20.679 1.00 36.73 ? 777 HOH A O 1 HETATM 2931 O O . HOH O 5 . ? -9.698 -25.690 5.992 1.00 39.62 ? 778 HOH A O 1 HETATM 2932 O O . HOH O 5 . ? -10.674 -13.331 22.213 1.00 33.88 ? 779 HOH A O 1 HETATM 2933 O O . HOH O 5 . ? -4.076 -12.481 34.484 1.00 26.93 ? 780 HOH A O 1 HETATM 2934 O O . HOH O 5 . ? 0.572 -22.748 17.102 1.00 37.29 ? 781 HOH A O 1 HETATM 2935 O O . HOH O 5 . ? -23.482 11.304 16.147 1.00 37.53 ? 782 HOH A O 1 HETATM 2936 O O . HOH O 5 . ? -15.119 -30.849 19.053 1.00 34.17 ? 783 HOH A O 1 HETATM 2937 O O . HOH O 5 . ? -18.880 3.099 24.892 1.00 45.07 ? 784 HOH A O 1 HETATM 2938 O O . HOH O 5 . ? -7.973 -10.528 33.077 1.00 31.53 ? 785 HOH A O 1 HETATM 2939 O O . HOH O 5 . ? -18.429 11.238 28.403 1.00 42.85 ? 786 HOH A O 1 HETATM 2940 O O . HOH O 5 . ? -5.665 12.070 7.629 1.00 46.70 ? 787 HOH A O 1 HETATM 2941 O O . HOH O 5 . ? 2.423 -17.793 35.233 1.00 39.23 ? 788 HOH A O 1 HETATM 2942 O O . HOH O 5 . ? -10.055 7.179 31.072 1.00 32.31 ? 789 HOH A O 1 HETATM 2943 O O . HOH O 5 . ? -16.705 -8.421 31.212 1.00 46.09 ? 790 HOH A O 1 HETATM 2944 O O . HOH O 5 . ? -2.666 -1.047 27.505 1.00 26.18 ? 791 HOH A O 1 HETATM 2945 O O . HOH O 5 . ? -9.812 -18.767 -6.469 1.00 45.77 ? 792 HOH A O 1 HETATM 2946 O O . HOH O 5 . ? -17.019 2.195 0.487 1.00 39.41 ? 793 HOH A O 1 HETATM 2947 O O . HOH O 5 . ? 3.120 -11.468 36.634 1.00 49.89 ? 794 HOH A O 1 HETATM 2948 O O . HOH O 5 . ? -8.750 -14.713 -5.309 1.00 47.39 ? 795 HOH A O 1 HETATM 2949 O O . HOH O 5 . ? -21.235 13.356 18.528 1.00 44.46 ? 796 HOH A O 1 HETATM 2950 O O . HOH O 5 . ? -4.529 4.456 12.206 1.00 38.41 ? 797 HOH A O 1 HETATM 2951 O O . HOH O 5 . ? 0.268 -14.436 29.851 1.00 33.70 ? 798 HOH A O 1 HETATM 2952 O O . HOH O 5 . ? -8.394 -16.994 38.160 1.00 40.87 ? 799 HOH A O 1 HETATM 2953 O O . HOH O 5 . ? -23.045 6.535 -3.016 1.00 43.44 ? 800 HOH A O 1 HETATM 2954 O O . HOH O 5 . ? -22.395 -3.692 13.275 1.00 39.69 ? 801 HOH A O 1 HETATM 2955 O O . HOH O 5 . ? -4.824 -9.325 9.306 1.00 35.50 ? 802 HOH A O 1 HETATM 2956 O O . HOH O 5 . ? -5.381 -23.937 39.579 1.00 47.14 ? 803 HOH A O 1 HETATM 2957 O O . HOH O 5 . ? -12.055 -11.294 2.618 1.00 45.23 ? 804 HOH A O 1 HETATM 2958 O O . HOH O 5 . ? -14.557 9.254 30.211 1.00 42.85 ? 805 HOH A O 1 HETATM 2959 O O . HOH O 5 . ? -12.567 -24.994 2.468 1.00 38.93 ? 806 HOH A O 1 HETATM 2960 O O . HOH O 5 . ? 16.466 -9.581 23.579 1.00 44.36 ? 807 HOH A O 1 HETATM 2961 O O . HOH O 5 . ? -19.546 -33.169 23.690 1.00 43.98 ? 808 HOH A O 1 HETATM 2962 O O . HOH O 5 . ? -33.217 -22.644 2.107 1.00 39.41 ? 809 HOH A O 1 HETATM 2963 O O . HOH O 5 . ? -18.725 3.077 -1.659 1.00 47.59 ? 810 HOH A O 1 HETATM 2964 O O . HOH O 5 . ? -4.620 4.661 32.723 1.00 39.46 ? 811 HOH A O 1 HETATM 2965 O O . HOH O 5 . ? -15.527 14.346 23.525 1.00 45.78 ? 812 HOH A O 1 HETATM 2966 O O . HOH O 5 . ? -28.939 -20.016 -5.376 1.00 38.02 ? 813 HOH A O 1 HETATM 2967 O O . HOH O 5 . ? -23.353 -29.878 15.257 1.00 41.08 ? 814 HOH A O 1 HETATM 2968 O O . HOH O 5 . ? -17.163 16.717 -0.663 1.00 51.53 ? 815 HOH A O 1 HETATM 2969 O O . HOH O 5 . ? -0.402 0.089 14.772 1.00 38.73 ? 816 HOH A O 1 HETATM 2970 O O . HOH O 5 . ? -28.077 -3.913 -1.421 1.00 39.85 ? 817 HOH A O 1 HETATM 2971 O O . HOH O 5 . ? -27.244 -19.639 24.164 1.00 38.75 ? 818 HOH A O 1 HETATM 2972 O O . HOH O 5 . ? -13.234 -32.871 19.484 1.00 39.38 ? 819 HOH A O 1 HETATM 2973 O O . HOH O 5 . ? -14.870 -31.002 -1.134 1.00 44.98 ? 820 HOH A O 1 HETATM 2974 O O . HOH O 5 . ? -3.728 3.606 15.059 1.00 32.14 ? 821 HOH A O 1 HETATM 2975 O O . HOH O 5 . ? 11.555 -15.610 12.130 1.00 46.43 ? 822 HOH A O 1 HETATM 2976 O O . HOH O 5 . ? -15.904 -0.039 -3.616 1.00 42.00 ? 823 HOH A O 1 HETATM 2977 O O . HOH O 5 . ? -4.303 -28.587 13.318 1.00 46.80 ? 824 HOH A O 1 HETATM 2978 O O . HOH O 5 . ? -29.998 9.398 -3.452 1.00 41.77 ? 825 HOH A O 1 HETATM 2979 O O . HOH O 5 . ? -11.273 2.855 -0.065 1.00 53.18 ? 826 HOH A O 1 HETATM 2980 O O . HOH O 5 . ? -27.754 -2.541 7.870 1.00 32.17 ? 827 HOH A O 1 HETATM 2981 O O . HOH O 5 . ? -32.486 -5.082 3.689 1.00 46.20 ? 828 HOH A O 1 HETATM 2982 O O . HOH O 5 . ? -18.111 -33.181 12.643 1.00 45.60 ? 829 HOH A O 1 HETATM 2983 O O . HOH O 5 . ? -22.018 -7.890 -6.417 1.00 42.58 ? 830 HOH A O 1 HETATM 2984 O O . HOH O 5 . ? -14.725 0.299 31.164 1.00 47.94 ? 831 HOH A O 1 HETATM 2985 O O . HOH O 5 . ? 2.849 -5.839 15.411 1.00 47.34 ? 833 HOH A O 1 HETATM 2986 O O . HOH O 5 . ? -14.922 -18.916 23.039 1.00 24.37 ? 834 HOH A O 1 HETATM 2987 O O . HOH O 5 . ? -26.134 -0.438 15.139 1.00 44.73 ? 835 HOH A O 1 HETATM 2988 O O . HOH O 5 . ? -10.971 6.695 6.246 1.00 43.88 ? 836 HOH A O 1 HETATM 2989 O O . HOH O 5 . ? 2.784 -22.994 17.639 1.00 50.04 ? 837 HOH A O 1 HETATM 2990 O O . HOH O 5 . ? -29.249 3.549 13.264 1.00 38.29 ? 838 HOH A O 1 HETATM 2991 O O . HOH O 5 . ? -21.034 10.744 19.242 1.00 48.71 ? 839 HOH A O 1 HETATM 2992 O O . HOH O 5 . ? -2.597 -6.422 9.577 1.00 39.80 ? 840 HOH A O 1 HETATM 2993 O O . HOH O 5 . ? -15.447 6.080 2.397 1.00 36.54 ? 841 HOH A O 1 HETATM 2994 O O . HOH O 5 . ? -22.533 9.052 17.105 1.00 46.67 ? 842 HOH A O 1 HETATM 2995 O O . HOH O 5 . ? 12.569 -13.678 28.825 1.00 47.09 ? 843 HOH A O 1 HETATM 2996 O O . HOH O 5 . ? -17.476 -12.156 -14.048 1.00 45.76 ? 844 HOH A O 1 HETATM 2997 O O . HOH O 5 . ? -22.028 -6.519 13.235 1.00 33.59 ? 845 HOH A O 1 HETATM 2998 O O . HOH O 5 . ? -9.679 -13.010 4.542 1.00 40.61 ? 846 HOH A O 1 HETATM 2999 O O . HOH O 5 . ? -20.958 -11.344 11.900 1.00 39.56 ? 847 HOH A O 1 HETATM 3000 O O . HOH O 5 . ? 0.732 -4.858 29.989 1.00 45.97 ? 848 HOH A O 1 HETATM 3001 O O . HOH O 5 . ? -7.601 10.705 31.923 1.00 44.31 ? 849 HOH A O 1 HETATM 3002 O O . HOH O 5 . ? -8.286 -4.988 36.410 1.00 44.07 ? 850 HOH A O 1 HETATM 3003 O O . HOH O 5 . ? -21.283 9.357 -1.254 1.00 43.45 ? 851 HOH A O 1 HETATM 3004 O O . HOH O 5 . ? -9.726 9.774 31.486 1.00 36.29 ? 852 HOH A O 1 HETATM 3005 O O . HOH O 5 . ? -16.308 0.831 28.836 1.00 41.55 ? 853 HOH A O 1 HETATM 3006 O O . HOH O 5 . ? -3.307 -12.153 37.190 1.00 47.21 ? 854 HOH A O 1 HETATM 3007 O O . HOH O 5 . ? -32.227 -19.600 7.379 1.00 39.03 ? 855 HOH A O 1 HETATM 3008 O O . HOH O 5 . ? 3.652 -5.501 26.684 1.00 37.79 ? 856 HOH A O 1 HETATM 3009 O O . HOH O 5 . ? -26.315 -14.367 25.875 1.00 48.50 ? 857 HOH A O 1 HETATM 3010 O O . HOH O 5 . ? -0.605 -4.625 32.290 1.00 43.08 ? 858 HOH A O 1 HETATM 3011 O O . HOH O 5 . ? 11.001 -12.735 30.628 1.00 47.04 ? 859 HOH A O 1 HETATM 3012 O O . HOH O 5 . ? -17.162 -33.002 1.557 1.00 41.85 ? 860 HOH A O 1 HETATM 3013 O O . HOH O 5 . ? -11.507 -15.261 -9.277 1.00 51.27 ? 861 HOH A O 1 HETATM 3014 O O . HOH O 5 . ? -1.848 -12.365 31.222 1.00 30.88 ? 862 HOH A O 1 HETATM 3015 O O . HOH O 5 . ? 4.240 -7.918 16.353 1.00 47.65 ? 864 HOH A O 1 HETATM 3016 O O . HOH O 5 . ? -1.112 -12.126 28.561 1.00 45.64 ? 865 HOH A O 1 HETATM 3017 O O . HOH O 5 . ? -8.857 -13.431 36.265 1.00 52.98 ? 866 HOH A O 1 HETATM 3018 O O . HOH O 5 . ? -8.629 -30.098 11.135 1.00 57.55 ? 867 HOH A O 1 HETATM 3019 O O . HOH O 5 . ? 0.625 -11.494 29.418 1.00 53.51 ? 868 HOH A O 1 HETATM 3020 O O . HOH O 5 . ? -18.588 -11.874 -10.872 1.00 49.32 ? 869 HOH A O 1 HETATM 3021 O O . HOH O 5 . ? -12.437 -16.020 35.364 1.00 42.26 ? 870 HOH A O 1 HETATM 3022 O O . HOH O 5 . ? -23.495 -22.618 27.438 1.00 51.86 ? 871 HOH A O 1 HETATM 3023 O O . HOH O 5 . ? -34.370 -11.501 14.662 1.00 51.47 ? 872 HOH A O 1 HETATM 3024 O O . HOH O 5 . ? -18.258 -35.188 2.602 1.00 57.31 ? 874 HOH A O 1 HETATM 3025 O O . HOH O 5 . ? -9.709 -15.711 36.089 1.00 48.73 ? 875 HOH A O 1 HETATM 3026 O O . HOH O 5 . ? -10.214 -25.601 -1.903 1.00 51.29 ? 876 HOH A O 1 HETATM 3027 O O . HOH O 5 . ? -23.825 -24.277 28.532 1.00 51.75 ? 877 HOH A O 1 HETATM 3028 O O . HOH O 5 . ? -9.515 -21.705 43.034 1.00 51.46 ? 878 HOH A O 1 HETATM 3029 O O . HOH O 5 . ? -18.825 -5.251 20.031 1.00 29.96 ? 879 HOH A O 1 HETATM 3030 O O . HOH O 5 . ? -29.494 -9.881 1.834 1.00 48.61 ? 880 HOH A O 1 HETATM 3031 O O . HOH O 5 . ? -12.856 -33.808 5.434 1.00 55.75 ? 881 HOH A O 1 HETATM 3032 O O . HOH O 5 . ? -8.971 -19.292 6.733 1.00 49.81 ? 882 HOH A O 1 HETATM 3033 O O . HOH O 5 . ? -2.290 -5.356 36.211 1.00 52.75 ? 883 HOH A O 1 HETATM 3034 O O . HOH O 5 . ? -14.413 10.178 -3.948 1.00 50.09 ? 884 HOH A O 1 HETATM 3035 O O . HOH O 5 . ? -10.257 -14.551 12.338 1.00 20.41 ? 885 HOH A O 1 HETATM 3036 O O . HOH O 5 . ? -11.518 -29.439 13.778 1.00 40.54 ? 886 HOH A O 1 HETATM 3037 O O . HOH O 5 . ? -29.023 -6.169 10.459 1.00 32.20 ? 887 HOH A O 1 HETATM 3038 O O . HOH O 5 . ? -28.434 -17.091 14.612 1.00 34.82 ? 888 HOH A O 1 HETATM 3039 O O . HOH O 5 . ? -11.432 7.306 26.356 1.00 35.44 ? 889 HOH A O 1 HETATM 3040 O O . HOH O 5 . ? -27.603 -34.662 16.937 1.00 54.40 ? 890 HOH A O 1 HETATM 3041 O O . HOH O 5 . ? -8.215 0.792 2.767 1.00 42.86 ? 891 HOH A O 1 HETATM 3042 O O . HOH O 5 . ? -31.869 5.643 8.281 1.00 58.99 ? 892 HOH A O 1 HETATM 3043 O O . HOH O 5 . ? -11.915 17.950 14.083 1.00 46.77 ? 893 HOH A O 1 HETATM 3044 O O . HOH O 5 . ? -14.003 -20.644 -7.082 1.00 49.20 ? 894 HOH A O 1 HETATM 3045 O O . HOH O 5 . ? -30.953 -19.853 -7.316 1.00 42.71 ? 895 HOH A O 1 HETATM 3046 O O . HOH O 5 . ? -21.171 -2.045 21.923 1.00 50.43 ? 896 HOH A O 1 HETATM 3047 O O . HOH O 5 . ? -10.516 13.741 2.423 1.00 50.51 ? 897 HOH A O 1 HETATM 3048 O O . HOH O 5 . ? -1.519 1.478 26.567 1.00 43.34 ? 898 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 ? 0.6262 0.5524 0.4491 0.2186 -0.1004 0.0841 44 VAL A N 2 C CA . VAL A 1 ? 0.6207 0.5650 0.4428 0.2066 -0.0992 0.0868 44 VAL A CA 3 C C . VAL A 1 ? 0.5983 0.5317 0.4195 0.1863 -0.0910 0.0872 44 VAL A C 4 O O . VAL A 1 ? 0.6610 0.5653 0.4754 0.1822 -0.0879 0.0891 44 VAL A O 5 C CB . VAL A 1 ? 0.7557 0.6898 0.5584 0.2126 -0.1057 0.0992 44 VAL A CB 6 C CG1 . VAL A 1 ? 0.8282 0.7199 0.6106 0.2100 -0.1042 0.1103 44 VAL A CG1 7 C CG2 . VAL A 1 ? 0.7643 0.7210 0.5672 0.2013 -0.1046 0.1004 44 VAL A CG2 8 N N . TRP A 2 ? 0.5000 0.4571 0.3289 0.1737 -0.0878 0.0847 45 TRP A N 9 C CA . TRP A 2 ? 0.5250 0.4785 0.3583 0.1545 -0.0802 0.0826 45 TRP A CA 10 C C . TRP A 2 ? 0.5393 0.5097 0.3725 0.1422 -0.0784 0.0853 45 TRP A C 11 O O . TRP A 2 ? 0.5899 0.5772 0.4202 0.1488 -0.0832 0.0876 45 TRP A O 12 C CB . TRP A 2 ? 0.5033 0.4759 0.3566 0.1517 -0.0758 0.0703 45 TRP A CB 13 C CG . TRP A 2 ? 0.5531 0.5647 0.4234 0.1565 -0.0773 0.0630 45 TRP A CG 14 C CD1 . TRP A 2 ? 0.5472 0.5858 0.4278 0.1463 -0.0752 0.0603 45 TRP A CD1 15 C CD2 . TRP A 2 ? 0.6192 0.6476 0.4999 0.1728 -0.0810 0.0569 45 TRP A CD2 16 N NE1 . TRP A 2 ? 0.5264 0.5974 0.4234 0.1550 -0.0775 0.0527 45 TRP A NE1 17 C CE2 . TRP A 2 ? 0.5788 0.6445 0.4765 0.1712 -0.0810 0.0505 45 TRP A CE2 18 C CE3 . TRP A 2 ? 0.6971 0.7129 0.5756 0.1884 -0.0841 0.0556 45 TRP A CE3 19 C CZ2 . TRP A 2 ? 0.6603 0.7511 0.5737 0.1845 -0.0839 0.0428 45 TRP A CZ2 20 C CZ3 . TRP A 2 ? 0.7557 0.7965 0.6493 0.2018 -0.0869 0.0481 45 TRP A CZ3 21 C CH2 . TRP A 2 ? 0.6934 0.7714 0.6046 0.1996 -0.0867 0.0418 45 TRP A CH2 22 N N . LYS A 3 ? 0.5036 0.4695 0.3401 0.1245 -0.0719 0.0844 46 LYS A N 23 C CA . LYS A 3 ? 0.5250 0.5076 0.3640 0.1112 -0.0690 0.0854 46 LYS A CA 24 C C . LYS A 3 ? 0.4961 0.4879 0.3512 0.0949 -0.0621 0.0779 46 LYS A C 25 O O . LYS A 3 ? 0.5260 0.5002 0.3830 0.0913 -0.0594 0.0755 46 LYS A O 26 C CB . LYS A 3 ? 0.5537 0.5108 0.3720 0.1060 -0.0683 0.0974 46 LYS A CB 27 C CG . LYS A 3 ? 0.6891 0.6170 0.5038 0.0928 -0.0624 0.0999 46 LYS A CG 28 C CD . LYS A 3 ? 0.8619 0.7630 0.6564 0.0887 -0.0610 0.1122 46 LYS A CD 29 C CE . LYS A 3 ? 0.9435 0.8148 0.7368 0.0762 -0.0553 0.1138 46 LYS A CE 30 N NZ . LYS A 3 ? 0.9739 0.8122 0.7469 0.0763 -0.0541 0.1263 46 LYS A NZ 31 N N . ASP A 4 ? 0.4671 0.4863 0.3339 0.0853 -0.0597 0.0740 47 ASP A N 32 C CA . ASP A 4 ? 0.4726 0.5012 0.3552 0.0697 -0.0534 0.0673 47 ASP A CA 33 C C . ASP A 4 ? 0.4564 0.4547 0.3301 0.0573 -0.0496 0.0723 47 ASP A C 34 O O . ASP A 4 ? 0.4820 0.4634 0.3408 0.0544 -0.0495 0.0809 47 ASP A O 35 C CB . ASP A 4 ? 0.5273 0.5876 0.4226 0.0608 -0.0515 0.0634 47 ASP A CB 36 C CG . ASP A 4 ? 0.5152 0.6082 0.4236 0.0716 -0.0549 0.0566 47 ASP A CG 37 O OD1 . ASP A 4 ? 0.4421 0.5362 0.3547 0.0836 -0.0571 0.0530 47 ASP A OD1 38 O OD2 . ASP A 4 ? 0.6418 0.7597 0.5573 0.0678 -0.0552 0.0542 47 ASP A OD2 39 N N . ALA A 5 ? 0.4175 0.4090 0.3004 0.0500 -0.0463 0.0670 48 ALA A N 40 C CA . ALA A 5 ? 0.4613 0.4246 0.3383 0.0384 -0.0433 0.0703 48 ALA A CA 41 C C . ALA A 5 ? 0.4946 0.4624 0.3867 0.0271 -0.0398 0.0625 48 ALA A C 42 O O . ALA A 5 ? 0.4308 0.4156 0.3341 0.0312 -0.0397 0.0552 48 ALA A O 43 C CB . ALA A 5 ? 0.4854 0.4155 0.3468 0.0479 -0.0462 0.0754 48 ALA A CB 44 N N . ASP A 6 ? 0.4948 0.4469 0.3870 0.0129 -0.0367 0.0641 49 ASP A N 45 C CA . ASP A 6 ? 0.4619 0.4125 0.3662 0.0026 -0.0345 0.0575 49 ASP A CA 46 C C . ASP A 6 ? 0.4459 0.3626 0.3410 0.0033 -0.0360 0.0585 49 ASP A C 47 O O . ASP A 6 ? 0.4708 0.3633 0.3531 0.0042 -0.0365 0.0654 49 ASP A O 48 C CB . ASP A 6 ? 0.5018 0.4612 0.4166 -0.0147 -0.0303 0.0569 49 ASP A CB 49 C CG . ASP A 6 ? 0.5538 0.5485 0.4814 -0.0170 -0.0286 0.0536 49 ASP A CG 50 O OD1 . ASP A 6 ? 0.5207 0.5348 0.4529 -0.0067 -0.0303 0.0500 49 ASP A OD1 51 O OD2 . ASP A 6 ? 0.5626 0.5658 0.4968 -0.0294 -0.0252 0.0541 49 ASP A OD2 52 N N . THR A 7 ? 0.3789 0.2935 0.2802 0.0032 -0.0367 0.0515 50 THR A N 53 C CA . THR A 7 ? 0.4357 0.3199 0.3303 0.0027 -0.0385 0.0504 50 THR A CA 54 C C . THR A 7 ? 0.4196 0.3097 0.3243 -0.0021 -0.0385 0.0418 50 THR A C 55 O O . THR A 7 ? 0.3811 0.2973 0.2960 -0.0018 -0.0369 0.0376 50 THR A O 56 C CB . THR A 7 ? 0.5224 0.3885 0.4029 0.0188 -0.0419 0.0526 50 THR A CB 57 O OG1 . THR A 7 ? 0.4972 0.3308 0.3709 0.0167 -0.0435 0.0525 50 THR A OG1 58 C CG2 . THR A 7 ? 0.5182 0.4003 0.4019 0.0305 -0.0430 0.0462 50 THR A CG2 59 N N . THR A 8 ? 0.4155 0.2813 0.3176 -0.0066 -0.0403 0.0392 51 THR A N 60 C CA . THR A 8 ? 0.3985 0.2671 0.3077 -0.0106 -0.0412 0.0313 51 THR A CA 61 C C . THR A 8 ? 0.3952 0.2665 0.2983 0.0035 -0.0426 0.0268 51 THR A C 62 O O . THR A 8 ? 0.4061 0.2585 0.2974 0.0140 -0.0450 0.0275 51 THR A O 63 C CB . THR A 8 ? 0.4460 0.2881 0.3550 -0.0199 -0.0436 0.0289 51 THR A CB 64 O OG1 . THR A 8 ? 0.4747 0.3164 0.3915 -0.0337 -0.0412 0.0325 51 THR A OG1 65 C CG2 . THR A 8 ? 0.4568 0.3026 0.3717 -0.0234 -0.0455 0.0207 51 THR A CG2 66 N N . LEU A 9 ? 0.3245 0.2196 0.2364 0.0037 -0.0405 0.0223 52 LEU A N 67 C CA . LEU A 9 ? 0.3326 0.2331 0.2403 0.0159 -0.0402 0.0176 52 LEU A CA 68 C C . LEU A 9 ? 0.3650 0.2480 0.2677 0.0143 -0.0427 0.0116 52 LEU A C 69 O O . LEU A 9 ? 0.3509 0.2233 0.2569 0.0028 -0.0446 0.0104 52 LEU A O 70 C CB . LEU A 9 ? 0.2908 0.2245 0.2110 0.0158 -0.0359 0.0156 52 LEU A CB 71 C CG . LEU A 9 ? 0.3025 0.2567 0.2297 0.0158 -0.0341 0.0204 52 LEU A CG 72 C CD1 . LEU A 9 ? 0.3553 0.3423 0.2982 0.0133 -0.0297 0.0174 52 LEU A CD1 73 C CD2 . LEU A 9 ? 0.3918 0.3407 0.3089 0.0306 -0.0359 0.0234 52 LEU A CD2 74 N N . PHE A 10 ? 0.3358 0.2159 0.2305 0.0261 -0.0427 0.0072 53 PHE A N 75 C CA . PHE A 10 ? 0.3681 0.2375 0.2579 0.0251 -0.0444 0.0007 53 PHE A CA 76 C C . PHE A 10 ? 0.3906 0.2826 0.2839 0.0301 -0.0397 -0.0029 53 PHE A C 77 O O . PHE A 10 ? 0.3494 0.2633 0.2494 0.0353 -0.0354 -0.0009 53 PHE A O 78 C CB . PHE A 10 ? 0.3543 0.1942 0.2293 0.0335 -0.0486 -0.0024 53 PHE A CB 79 C CG . PHE A 10 ? 0.4283 0.2687 0.2953 0.0496 -0.0470 -0.0031 53 PHE A CG 80 C CD1 . PHE A 10 ? 0.4491 0.2846 0.3138 0.0563 -0.0476 0.0023 53 PHE A CD1 81 C CD2 . PHE A 10 ? 0.4034 0.2478 0.2645 0.0585 -0.0449 -0.0093 53 PHE A CD2 82 C CE1 . PHE A 10 ? 0.5239 0.3598 0.3827 0.0716 -0.0467 0.0013 53 PHE A CE1 83 C CE2 . PHE A 10 ? 0.4748 0.3198 0.3300 0.0733 -0.0430 -0.0107 53 PHE A CE2 84 C CZ . PHE A 10 ? 0.5117 0.3527 0.3666 0.0800 -0.0443 -0.0056 53 PHE A CZ 85 N N . CYS A 11 ? 0.2909 0.1778 0.1801 0.0283 -0.0403 -0.0081 54 CYS A N 86 C CA . CYS A 11 ? 0.3116 0.2183 0.2033 0.0324 -0.0349 -0.0109 54 CYS A CA 87 C C . CYS A 11 ? 0.3920 0.2855 0.2682 0.0441 -0.0347 -0.0164 54 CYS A C 88 O O . CYS A 11 ? 0.3836 0.2516 0.2476 0.0460 -0.0401 -0.0195 54 CYS A O 89 C CB . CYS A 11 ? 0.3608 0.2788 0.2622 0.0201 -0.0340 -0.0114 54 CYS A CB 90 S SG . CYS A 11 ? 0.4480 0.3404 0.3412 0.0120 -0.0416 -0.0155 54 CYS A SG 91 N N . ALA A 12 ? 0.3095 0.2207 0.1869 0.0521 -0.0280 -0.0182 55 ALA A N 92 C CA . ALA A 12 ? 0.3829 0.2849 0.2461 0.0633 -0.0260 -0.0237 55 ALA A CA 93 C C . ALA A 12 ? 0.3734 0.2938 0.2397 0.0625 -0.0190 -0.0254 55 ALA A C 94 O O . ALA A 12 ? 0.3890 0.3336 0.2711 0.0574 -0.0141 -0.0222 55 ALA A O 95 C CB . ALA A 12 ? 0.3259 0.2288 0.1866 0.0771 -0.0238 -0.0242 55 ALA A CB 96 N N . SER A 13 ? 0.3849 0.2934 0.2359 0.0673 -0.0182 -0.0303 56 SER A N 97 C CA . SER A 13 ? 0.3834 0.3060 0.2346 0.0664 -0.0112 -0.0313 56 SER A CA 98 C C . SER A 13 ? 0.3876 0.2960 0.2183 0.0764 -0.0092 -0.0372 56 SER A C 99 O O . SER A 13 ? 0.3774 0.2637 0.1942 0.0826 -0.0146 -0.0412 56 SER A O 100 C CB . SER A 13 ? 0.4251 0.3489 0.2816 0.0527 -0.0146 -0.0290 56 SER A CB 101 O OG . SER A 13 ? 0.4405 0.3410 0.2797 0.0518 -0.0212 -0.0330 56 SER A OG 102 N N . ASP A 14 ? 0.3795 0.3002 0.2082 0.0779 -0.0010 -0.0378 57 ASP A N 103 C CA . ASP A 14 ? 0.4360 0.3443 0.2436 0.0868 0.0022 -0.0431 57 ASP A CA 104 C C . ASP A 14 ? 0.4681 0.3662 0.2640 0.0796 -0.0017 -0.0434 57 ASP A C 105 O O . ASP A 14 ? 0.4771 0.3735 0.2588 0.0842 0.0038 -0.0455 57 ASP A O 106 C CB . ASP A 14 ? 0.4801 0.4078 0.2916 0.0952 0.0154 -0.0438 57 ASP A CB 107 C CG . ASP A 14 ? 0.5715 0.5069 0.3921 0.1048 0.0183 -0.0451 57 ASP A CG 108 O OD1 . ASP A 14 ? 0.5939 0.5106 0.4046 0.1113 0.0121 -0.0485 57 ASP A OD1 109 O OD2 . ASP A 14 ? 0.5815 0.5414 0.4200 0.1059 0.0263 -0.0430 57 ASP A OD2 110 N N . ALA A 15 ? 0.4595 0.3507 0.2616 0.0686 -0.0111 -0.0412 58 ALA A N 111 C CA . ALA A 15 ? 0.4339 0.3155 0.2275 0.0613 -0.0168 -0.0416 58 ALA A CA 112 C C . ALA A 15 ? 0.4959 0.3550 0.2623 0.0693 -0.0203 -0.0482 58 ALA A C 113 O O . ALA A 15 ? 0.5374 0.3806 0.2932 0.0771 -0.0236 -0.0534 58 ALA A O 114 C CB . ALA A 15 ? 0.4128 0.2871 0.2173 0.0496 -0.0273 -0.0400 58 ALA A CB 115 N N . LYS A 16 ? 0.5011 0.3585 0.2561 0.0675 -0.0197 -0.0481 59 LYS A N 116 C CA . LYS A 16 ? 0.5464 0.3832 0.2736 0.0747 -0.0234 -0.0544 59 LYS A CA 117 C C . LYS A 16 ? 0.5099 0.3271 0.2311 0.0679 -0.0382 -0.0577 59 LYS A C 118 O O . LYS A 16 ? 0.4862 0.3085 0.2174 0.0576 -0.0424 -0.0539 59 LYS A O 119 C CB . LYS A 16 ? 0.6059 0.4511 0.3214 0.0776 -0.0141 -0.0521 59 LYS A CB 120 C CG . LYS A 16 ? 0.7760 0.6336 0.4888 0.0878 0.0007 -0.0521 59 LYS A CG 121 C CD . LYS A 16 ? 0.9031 0.7832 0.6434 0.0857 0.0076 -0.0479 59 LYS A CD 122 C CE . LYS A 16 ? 0.9715 0.8649 0.7114 0.0960 0.0223 -0.0488 59 LYS A CE 123 N NZ . LYS A 16 ? 0.9389 0.8518 0.7041 0.0963 0.0268 -0.0466 59 LYS A NZ 124 N N . ALA A 17 ? 0.5224 0.3173 0.2287 0.0737 -0.0460 -0.0654 60 ALA A N 125 C CA . ALA A 17 ? 0.6228 0.3982 0.3254 0.0676 -0.0607 -0.0700 60 ALA A CA 126 C C . ALA A 17 ? 0.6470 0.4152 0.3327 0.0664 -0.0660 -0.0719 60 ALA A C 127 O O . ALA A 17 ? 0.6571 0.4151 0.3454 0.0590 -0.0780 -0.0741 60 ALA A O 128 C CB . ALA A 17 ? 0.6832 0.4367 0.3753 0.0746 -0.0671 -0.0784 60 ALA A CB 129 N N . HIS A 18 ? 0.5881 0.3615 0.2564 0.0740 -0.0571 -0.0709 61 HIS A N 130 C CA . HIS A 18 ? 0.5933 0.3595 0.2419 0.0744 -0.0613 -0.0718 61 HIS A CA 131 C C . HIS A 18 ? 0.5421 0.3264 0.2039 0.0659 -0.0567 -0.0625 61 HIS A C 132 O O . HIS A 18 ? 0.5657 0.3452 0.2136 0.0652 -0.0604 -0.0615 61 HIS A O 133 C CB . HIS A 18 ? 0.6075 0.3668 0.2266 0.0876 -0.0538 -0.0758 61 HIS A CB 134 C CG . HIS A 18 ? 0.7090 0.4875 0.3332 0.0927 -0.0362 -0.0705 61 HIS A CG 135 N ND1 . HIS A 18 ? 0.7890 0.5832 0.4138 0.0911 -0.0255 -0.0629 61 HIS A ND1 136 C CD2 . HIS A 18 ? 0.7155 0.5004 0.3461 0.0994 -0.0273 -0.0719 61 HIS A CD2 137 C CE1 . HIS A 18 ? 0.7649 0.5745 0.3969 0.0963 -0.0107 -0.0604 61 HIS A CE1 138 N NE2 . HIS A 18 ? 0.7900 0.5948 0.4257 0.1016 -0.0118 -0.0659 61 HIS A NE2 139 N N . GLU A 19 ? 0.5421 0.3470 0.2304 0.0598 -0.0489 -0.0558 62 GLU A N 140 C CA . GLU A 19 ? 0.5668 0.3903 0.2713 0.0513 -0.0438 -0.0473 62 GLU A CA 141 C C . GLU A 19 ? 0.5424 0.3634 0.2627 0.0390 -0.0563 -0.0464 62 GLU A C 142 O O . GLU A 19 ? 0.5270 0.3403 0.2580 0.0345 -0.0650 -0.0500 62 GLU A O 143 C CB . GLU A 19 ? 0.5388 0.3864 0.2667 0.0495 -0.0310 -0.0416 62 GLU A CB 144 C CG . GLU A 19 ? 0.6229 0.4835 0.3436 0.0568 -0.0153 -0.0382 62 GLU A CG 145 C CD . GLU A 19 ? 0.6854 0.5513 0.4020 0.0530 -0.0119 -0.0324 62 GLU A CD 146 O OE1 . GLU A 19 ? 0.7349 0.6054 0.4388 0.0598 0.0000 -0.0303 62 GLU A OE1 147 O OE2 . GLU A 19 ? 0.5897 0.4549 0.3164 0.0433 -0.0208 -0.0300 62 GLU A OE2 148 N N . THR A 20 ? 0.5042 0.3313 0.2264 0.0337 -0.0565 -0.0414 63 THR A N 149 C CA . THR A 20 ? 0.5172 0.3457 0.2585 0.0216 -0.0667 -0.0399 63 THR A CA 150 C C . THR A 20 ? 0.4463 0.2992 0.2184 0.0123 -0.0584 -0.0327 63 THR A C 151 O O . THR A 20 ? 0.4346 0.2915 0.2275 0.0015 -0.0651 -0.0316 63 THR A O 152 C CB . THR A 20 ? 0.5666 0.3867 0.2938 0.0208 -0.0740 -0.0390 63 THR A CB 153 O OG1 . THR A 20 ? 0.5302 0.3619 0.2503 0.0244 -0.0614 -0.0320 63 THR A OG1 154 C CG2 . THR A 20 ? 0.5858 0.3812 0.2835 0.0291 -0.0849 -0.0475 63 THR A CG2 155 N N . GLU A 21 ? 0.3848 0.2543 0.1605 0.0166 -0.0438 -0.0283 64 GLU A N 156 C CA . GLU A 21 ? 0.3879 0.2818 0.1929 0.0087 -0.0355 -0.0224 64 GLU A CA 157 C C . GLU A 21 ? 0.3488 0.2436 0.1734 0.0016 -0.0419 -0.0245 64 GLU A C 158 O O . GLU A 21 ? 0.4173 0.2998 0.2336 0.0065 -0.0457 -0.0292 64 GLU A O 159 C CB . GLU A 21 ? 0.4181 0.3278 0.2235 0.0160 -0.0197 -0.0197 64 GLU A CB 160 C CG . GLU A 21 ? 0.3502 0.2865 0.1841 0.0088 -0.0100 -0.0138 64 GLU A CG 161 C CD . GLU A 21 ? 0.3475 0.2937 0.2041 0.0030 -0.0122 -0.0145 64 GLU A CD 162 O OE1 . GLU A 21 ? 0.4034 0.3432 0.2538 0.0093 -0.0131 -0.0182 64 GLU A OE1 163 O OE2 . GLU A 21 ? 0.3766 0.3363 0.2565 -0.0075 -0.0129 -0.0115 64 GLU A OE2 164 N N . VAL A 22 ? 0.3291 0.2377 0.1792 -0.0100 -0.0427 -0.0209 65 VAL A N 165 C CA . VAL A 22 ? 0.3922 0.2981 0.2588 -0.0183 -0.0504 -0.0230 65 VAL A CA 166 C C . VAL A 22 ? 0.3796 0.2928 0.2546 -0.0160 -0.0452 -0.0230 65 VAL A C 167 O O . VAL A 22 ? 0.3622 0.2638 0.2389 -0.0180 -0.0520 -0.0260 65 VAL A O 168 C CB . VAL A 22 ? 0.3706 0.2884 0.2619 -0.0316 -0.0531 -0.0199 65 VAL A CB 169 C CG1 . VAL A 22 ? 0.3974 0.3035 0.2801 -0.0338 -0.0620 -0.0209 65 VAL A CG1 170 C CG2 . VAL A 22 ? 0.3335 0.2775 0.2430 -0.0345 -0.0409 -0.0141 65 VAL A CG2 171 N N . HIS A 23 ? 0.3382 0.2701 0.2189 -0.0116 -0.0333 -0.0196 66 HIS A N 172 C CA . HIS A 23 ? 0.3043 0.2431 0.1911 -0.0077 -0.0289 -0.0197 66 HIS A CA 173 C C . HIS A 23 ? 0.3193 0.2384 0.1837 0.0036 -0.0316 -0.0244 66 HIS A C 174 O O . HIS A 23 ? 0.3358 0.2483 0.2016 0.0052 -0.0346 -0.0259 66 HIS A O 175 C CB . HIS A 23 ? 0.2707 0.2346 0.1692 -0.0047 -0.0160 -0.0161 66 HIS A CB 176 C CG . HIS A 23 ? 0.3065 0.2917 0.2298 -0.0156 -0.0125 -0.0121 66 HIS A CG 177 N ND1 . HIS A 23 ? 0.2993 0.2889 0.2258 -0.0205 -0.0111 -0.0097 66 HIS A ND1 178 C CD2 . HIS A 23 ? 0.2998 0.3029 0.2457 -0.0222 -0.0102 -0.0102 66 HIS A CD2 179 C CE1 . HIS A 23 ? 0.2696 0.2790 0.2211 -0.0300 -0.0079 -0.0069 66 HIS A CE1 180 N NE2 . HIS A 23 ? 0.2993 0.3175 0.2625 -0.0312 -0.0073 -0.0074 66 HIS A NE2 181 N N . ASN A 24 ? 0.3569 0.2664 0.2001 0.0117 -0.0302 -0.0267 67 ASN A N 182 C CA . ASN A 24 ? 0.4364 0.3261 0.2570 0.0226 -0.0331 -0.0322 67 ASN A CA 183 C C . ASN A 24 ? 0.4222 0.2891 0.2376 0.0190 -0.0464 -0.0369 67 ASN A C 184 O O . ASN A 24 ? 0.4045 0.2592 0.2148 0.0239 -0.0493 -0.0403 67 ASN A O 185 C CB . ASN A 24 ? 0.3998 0.2832 0.1976 0.0309 -0.0293 -0.0340 67 ASN A CB 186 C CG . ASN A 24 ? 0.4629 0.3634 0.2610 0.0388 -0.0148 -0.0316 67 ASN A CG 187 O OD1 . ASN A 24 ? 0.4425 0.3389 0.2306 0.0491 -0.0107 -0.0350 67 ASN A OD1 188 N ND2 . ASN A 24 ? 0.4309 0.3508 0.2419 0.0339 -0.0067 -0.0262 67 ASN A ND2 189 N N . VAL A 25 ? 0.4431 0.3041 0.2609 0.0105 -0.0545 -0.0372 68 VAL A N 190 C CA . VAL A 25 ? 0.4314 0.2718 0.2473 0.0060 -0.0674 -0.0423 68 VAL A CA 191 C C . VAL A 25 ? 0.3886 0.2305 0.2233 -0.0007 -0.0690 -0.0410 68 VAL A C 192 O O . VAL A 25 ? 0.4165 0.2406 0.2458 0.0015 -0.0748 -0.0453 68 VAL A O 193 C CB . VAL A 25 ? 0.4070 0.2440 0.2259 -0.0024 -0.0757 -0.0428 68 VAL A CB 194 C CG1 . VAL A 25 ? 0.5135 0.3335 0.3388 -0.0095 -0.0884 -0.0479 68 VAL A CG1 195 C CG2 . VAL A 25 ? 0.4352 0.2633 0.2293 0.0056 -0.0770 -0.0452 68 VAL A CG2 196 N N . TRP A 26 ? 0.4089 0.2715 0.2653 -0.0088 -0.0636 -0.0352 69 TRP A N 197 C CA . TRP A 26 ? 0.3720 0.2376 0.2453 -0.0152 -0.0639 -0.0331 69 TRP A CA 198 C C . TRP A 26 ? 0.4059 0.2666 0.2715 -0.0056 -0.0603 -0.0334 69 TRP A C 199 O O . TRP A 26 ? 0.3961 0.2418 0.2619 -0.0066 -0.0652 -0.0350 69 TRP A O 200 C CB . TRP A 26 ? 0.3530 0.2441 0.2491 -0.0240 -0.0574 -0.0271 69 TRP A CB 201 C CG . TRP A 26 ? 0.3748 0.2698 0.2867 -0.0306 -0.0572 -0.0247 69 TRP A CG 202 C CD1 . TRP A 26 ? 0.3853 0.2747 0.3104 -0.0421 -0.0631 -0.0250 69 TRP A CD1 203 C CD2 . TRP A 26 ? 0.3063 0.2111 0.2216 -0.0259 -0.0508 -0.0214 69 TRP A CD2 204 N NE1 . TRP A 26 ? 0.4286 0.3230 0.3634 -0.0450 -0.0600 -0.0218 69 TRP A NE1 205 C CE2 . TRP A 26 ? 0.3893 0.2931 0.3180 -0.0349 -0.0531 -0.0194 69 TRP A CE2 206 C CE3 . TRP A 26 ? 0.3494 0.2638 0.2581 -0.0147 -0.0435 -0.0202 69 TRP A CE3 207 C CZ2 . TRP A 26 ? 0.4188 0.3303 0.3522 -0.0327 -0.0487 -0.0157 69 TRP A CZ2 208 C CZ3 . TRP A 26 ? 0.3592 0.2820 0.2747 -0.0125 -0.0399 -0.0171 69 TRP A CZ3 209 C CH2 . TRP A 26 ? 0.3752 0.2961 0.3018 -0.0212 -0.0427 -0.0146 69 TRP A CH2 210 N N . ALA A 27 ? 0.3647 0.2378 0.2244 0.0038 -0.0514 -0.0318 70 ALA A N 211 C CA . ALA A 27 ? 0.3671 0.2383 0.2214 0.0138 -0.0475 -0.0320 70 ALA A CA 212 C C . ALA A 27 ? 0.4312 0.2761 0.2654 0.0224 -0.0534 -0.0382 70 ALA A C 213 O O . ALA A 27 ? 0.4505 0.2857 0.2826 0.0273 -0.0544 -0.0388 70 ALA A O 214 C CB . ALA A 27 ? 0.3504 0.2420 0.2052 0.0218 -0.0365 -0.0298 70 ALA A CB 215 N N . THR A 28 ? 0.4222 0.2551 0.2412 0.0244 -0.0576 -0.0430 71 THR A N 216 C CA . THR A 28 ? 0.4636 0.2714 0.2633 0.0321 -0.0640 -0.0502 71 THR A CA 217 C C . THR A 28 ? 0.4566 0.2463 0.2628 0.0259 -0.0730 -0.0524 71 THR A C 218 O O . THR A 28 ? 0.4814 0.2525 0.2779 0.0326 -0.0763 -0.0568 71 THR A O 219 C CB . THR A 28 ? 0.5062 0.3046 0.2885 0.0341 -0.0684 -0.0552 71 THR A CB 220 O OG1 . THR A 28 ? 0.5053 0.3163 0.2775 0.0422 -0.0586 -0.0537 71 THR A OG1 221 C CG2 . THR A 28 ? 0.5404 0.3117 0.3048 0.0402 -0.0770 -0.0639 71 THR A CG2 222 N N . HIS A 29 ? 0.4738 0.2690 0.2974 0.0130 -0.0763 -0.0492 72 HIS A N 223 C CA . HIS A 29 ? 0.5318 0.3106 0.3639 0.0053 -0.0840 -0.0510 72 HIS A CA 224 C C . HIS A 29 ? 0.5267 0.3132 0.3743 0.0011 -0.0795 -0.0444 72 HIS A C 225 O O . HIS A 29 ? 0.5568 0.3271 0.4077 -0.0017 -0.0835 -0.0453 72 HIS A O 226 C CB . HIS A 29 ? 0.6648 0.4419 0.5062 -0.0065 -0.0915 -0.0529 72 HIS A CB 227 C CG . HIS A 29 ? 0.8003 0.5679 0.6255 -0.0026 -0.0978 -0.0593 72 HIS A CG 228 N ND1 . HIS A 29 ? 0.8038 0.5831 0.6175 0.0036 -0.0927 -0.0579 72 HIS A ND1 229 C CD2 . HIS A 29 ? 0.9149 0.6620 0.7329 -0.0037 -0.1089 -0.0672 72 HIS A CD2 230 C CE1 . HIS A 29 ? 0.8379 0.6037 0.6360 0.0064 -0.1004 -0.0642 72 HIS A CE1 231 N NE2 . HIS A 29 ? 0.9259 0.6726 0.7266 0.0022 -0.1108 -0.0703 72 HIS A NE2 232 N N . ALA A 30 ? 0.4100 0.2208 0.2668 0.0008 -0.0711 -0.0381 73 ALA A N 233 C CA . ALA A 30 ? 0.4235 0.2439 0.2948 -0.0038 -0.0672 -0.0317 73 ALA A CA 234 C C . ALA A 30 ? 0.4553 0.2827 0.3220 0.0074 -0.0607 -0.0286 73 ALA A C 235 O O . ALA A 30 ? 0.4249 0.2562 0.2997 0.0057 -0.0586 -0.0236 73 ALA A O 236 C CB . ALA A 30 ? 0.3574 0.2008 0.2469 -0.0149 -0.0638 -0.0272 73 ALA A CB 237 N N . CYS A 31 ? 0.4750 0.3040 0.3287 0.0191 -0.0575 -0.0315 74 CYS A N 238 C CA . CYS A 31 ? 0.4813 0.3198 0.3327 0.0303 -0.0511 -0.0293 74 CYS A CA 239 C C . CYS A 31 ? 0.4746 0.2937 0.3084 0.0432 -0.0527 -0.0347 74 CYS A C 240 O O . CYS A 31 ? 0.4345 0.2354 0.2562 0.0441 -0.0580 -0.0408 74 CYS A O 241 C CB . CYS A 31 ? 0.4649 0.3305 0.3221 0.0327 -0.0428 -0.0274 74 CYS A CB 242 S SG . CYS A 31 ? 0.4101 0.3012 0.2895 0.0185 -0.0398 -0.0218 74 CYS A SG 243 N N . VAL A 32 ? 0.3996 0.2229 0.2322 0.0535 -0.0485 -0.0330 75 VAL A N 244 C CA . VAL A 32 ? 0.4370 0.2445 0.2545 0.0668 -0.0489 -0.0383 75 VAL A CA 245 C C . VAL A 32 ? 0.4539 0.2794 0.2680 0.0770 -0.0405 -0.0399 75 VAL A C 246 O O . VAL A 32 ? 0.4603 0.3105 0.2856 0.0738 -0.0344 -0.0363 75 VAL A O 247 C CB . VAL A 32 ? 0.5755 0.3700 0.3936 0.0723 -0.0511 -0.0358 75 VAL A CB 248 C CG1 . VAL A 32 ? 0.5833 0.3584 0.4047 0.0620 -0.0582 -0.0342 75 VAL A CG1 249 C CG2 . VAL A 32 ? 0.5312 0.3479 0.3609 0.0753 -0.0456 -0.0291 75 VAL A CG2 250 N N . PRO A 33 ? 0.4943 0.3076 0.2940 0.0892 -0.0395 -0.0460 76 PRO A N 251 C CA . PRO A 33 ? 0.5131 0.3425 0.3099 0.0995 -0.0305 -0.0481 76 PRO A CA 252 C C . PRO A 33 ? 0.5093 0.3593 0.3204 0.1047 -0.0249 -0.0435 76 PRO A C 253 O O . PRO A 33 ? 0.4766 0.3217 0.2938 0.1051 -0.0287 -0.0397 76 PRO A O 254 C CB . PRO A 33 ? 0.5987 0.4064 0.3773 0.1111 -0.0321 -0.0561 76 PRO A CB 255 C CG . PRO A 33 ? 0.5694 0.3519 0.3393 0.1043 -0.0420 -0.0593 76 PRO A CG 256 C CD . PRO A 33 ? 0.5516 0.3354 0.3367 0.0932 -0.0465 -0.0523 76 PRO A CD 257 N N . THR A 34 ? 0.4734 0.3461 0.2900 0.1089 -0.0158 -0.0437 77 THR A N 258 C CA . THR A 34 ? 0.5008 0.3951 0.3322 0.1147 -0.0106 -0.0407 77 THR A CA 259 C C . THR A 34 ? 0.5409 0.4262 0.3660 0.1298 -0.0098 -0.0448 77 THR A C 260 O O . THR A 34 ? 0.5713 0.4369 0.3803 0.1362 -0.0110 -0.0508 77 THR A O 261 C CB . THR A 34 ? 0.4862 0.4084 0.3279 0.1142 -0.0004 -0.0406 77 THR A CB 262 O OG1 . THR A 34 ? 0.4714 0.3885 0.2994 0.1221 0.0055 -0.0466 77 THR A OG1 263 C CG2 . THR A 34 ? 0.4386 0.3711 0.2885 0.0996 -0.0007 -0.0364 77 THR A CG2 264 N N . ASP A 35 ? 0.4858 0.3860 0.3239 0.1357 -0.0081 -0.0419 78 ASP A N 265 C CA . ASP A 35 ? 0.5229 0.4183 0.3585 0.1507 -0.0070 -0.0455 78 ASP A CA 266 C C . ASP A 35 ? 0.5567 0.4736 0.3982 0.1587 0.0036 -0.0500 78 ASP A C 267 O O . ASP A 35 ? 0.4862 0.4297 0.3441 0.1559 0.0089 -0.0475 78 ASP A O 268 C CB . ASP A 35 ? 0.5166 0.4169 0.3633 0.1535 -0.0116 -0.0398 78 ASP A CB 269 C CG . ASP A 35 ? 0.6236 0.5159 0.4678 0.1693 -0.0123 -0.0429 78 ASP A CG 270 O OD1 . ASP A 35 ? 0.5961 0.4882 0.4354 0.1788 -0.0066 -0.0500 78 ASP A OD1 271 O OD2 . ASP A 35 ? 0.6939 0.5798 0.5411 0.1725 -0.0182 -0.0382 78 ASP A OD2 272 N N . PRO A 36 ? 0.6460 0.5513 0.4745 0.1684 0.0074 -0.0573 79 PRO A N 273 C CA . PRO A 36 ? 0.7246 0.6485 0.5576 0.1761 0.0189 -0.0621 79 PRO A CA 274 C C . PRO A 36 ? 0.7717 0.7136 0.6218 0.1868 0.0218 -0.0626 79 PRO A C 275 O O . PRO A 36 ? 0.7755 0.7390 0.6363 0.1915 0.0318 -0.0657 79 PRO A O 276 C CB . PRO A 36 ? 0.7147 0.6164 0.5266 0.1839 0.0204 -0.0700 79 PRO A CB 277 C CG . PRO A 36 ? 0.7252 0.5997 0.5277 0.1857 0.0093 -0.0700 79 PRO A CG 278 C CD . PRO A 36 ? 0.6702 0.5442 0.4795 0.1726 0.0014 -0.0619 79 PRO A CD 279 N N . ASN A 37 ? 0.7629 0.6958 0.6159 0.1908 0.0132 -0.0596 80 ASN A N 280 C CA . ASN A 37 ? 0.7479 0.6964 0.6166 0.2017 0.0139 -0.0598 80 ASN A CA 281 C C . ASN A 37 ? 0.6247 0.5797 0.5042 0.1971 0.0058 -0.0517 80 ASN A C 282 O O . ASN A 37 ? 0.6407 0.5836 0.5187 0.2044 -0.0013 -0.0496 80 ASN A O 283 C CB . ASN A 37 ? 0.8513 0.7811 0.7114 0.2164 0.0121 -0.0654 80 ASN A CB 284 C CG . ASN A 37 ? 0.9845 0.9060 0.8316 0.2216 0.0200 -0.0740 80 ASN A CG 285 O OD1 . ASN A 37 ? 1.0251 0.9616 0.8738 0.2176 0.0293 -0.0762 80 ASN A OD1 286 N ND2 . ASN A 37 ? 1.0429 0.9398 0.8766 0.2306 0.0167 -0.0790 80 ASN A ND2 287 N N . PRO A 38 ? 0.6096 0.5834 0.4996 0.1852 0.0071 -0.0471 81 PRO A N 288 C CA . PRO A 38 ? 0.6102 0.5907 0.5089 0.1793 -0.0001 -0.0395 81 PRO A CA 289 C C . PRO A 38 ? 0.5845 0.5814 0.4973 0.1907 -0.0018 -0.0392 81 PRO A C 290 O O . PRO A 38 ? 0.6094 0.6273 0.5353 0.1985 0.0050 -0.0444 81 PRO A O 291 C CB . PRO A 38 ? 0.5873 0.5892 0.4968 0.1657 0.0044 -0.0373 81 PRO A CB 292 C CG . PRO A 38 ? 0.5635 0.5788 0.4768 0.1686 0.0153 -0.0437 81 PRO A CG 293 C CD . PRO A 38 ? 0.5596 0.5500 0.4542 0.1769 0.0159 -0.0488 81 PRO A CD 294 N N . GLN A 39 ? 0.5806 0.5673 0.4908 0.1918 -0.0109 -0.0330 82 GLN A N 295 C CA . GLN A 39 ? 0.5842 0.5843 0.5057 0.2028 -0.0146 -0.0316 82 GLN A CA 296 C C . GLN A 39 ? 0.5358 0.5610 0.4714 0.1948 -0.0161 -0.0269 82 GLN A C 297 O O . GLN A 39 ? 0.4924 0.5120 0.4232 0.1820 -0.0191 -0.0212 82 GLN A O 298 C CB . GLN A 39 ? 0.7142 0.6868 0.6227 0.2102 -0.0237 -0.0270 82 GLN A CB 299 C CG . GLN A 39 ? 0.8341 0.7889 0.7320 0.1982 -0.0302 -0.0183 82 GLN A CG 300 C CD . GLN A 39 ? 0.9122 0.8442 0.7963 0.1877 -0.0290 -0.0195 82 GLN A CD 301 O OE1 . GLN A 39 ? 0.8266 0.7689 0.7135 0.1774 -0.0239 -0.0218 82 GLN A OE1 302 N NE2 . GLN A 39 ? 0.9976 0.8981 0.8674 0.1904 -0.0341 -0.0179 82 GLN A NE2 303 N N . GLU A 40 ? 0.4756 0.5288 0.4296 0.2024 -0.0140 -0.0302 83 GLU A N 304 C CA . GLU A 40 ? 0.4415 0.5196 0.4098 0.1968 -0.0165 -0.0268 83 GLU A CA 305 C C . GLU A 40 ? 0.4689 0.5587 0.4464 0.2111 -0.0223 -0.0271 83 GLU A C 306 O O . GLU A 40 ? 0.4159 0.5181 0.4049 0.2230 -0.0187 -0.0340 83 GLU A O 307 C CB . GLU A 40 ? 0.4967 0.6034 0.4827 0.1888 -0.0072 -0.0316 83 GLU A CB 308 C CG . GLU A 40 ? 0.4742 0.6085 0.4770 0.1831 -0.0094 -0.0297 83 GLU A CG 309 C CD . GLU A 40 ? 0.5269 0.6849 0.5457 0.1720 -0.0004 -0.0332 83 GLU A CD 310 O OE1 . GLU A 40 ? 0.4489 0.5998 0.4632 0.1676 0.0074 -0.0358 83 GLU A OE1 311 O OE2 . GLU A 40 ? 0.5284 0.7117 0.5639 0.1677 -0.0011 -0.0334 83 GLU A OE2 312 N N . ILE A 41 ? 0.3525 0.4379 0.3248 0.2103 -0.0313 -0.0196 84 ILE A N 313 C CA . ILE A 41 ? 0.4163 0.5092 0.3937 0.2244 -0.0389 -0.0185 84 ILE A CA 314 C C . ILE A 41 ? 0.4746 0.5988 0.4681 0.2212 -0.0414 -0.0181 84 ILE A C 315 O O . ILE A 41 ? 0.4415 0.5659 0.4301 0.2093 -0.0438 -0.0123 84 ILE A O 316 C CB . ILE A 41 ? 0.4641 0.5256 0.4207 0.2281 -0.0481 -0.0095 84 ILE A CB 317 C CG1 . ILE A 41 ? 0.5231 0.5523 0.4642 0.2306 -0.0461 -0.0106 84 ILE A CG1 318 C CG2 . ILE A 41 ? 0.4821 0.5502 0.4427 0.2439 -0.0566 -0.0077 84 ILE A CG2 319 C CD1 . ILE A 41 ? 0.6220 0.6178 0.5431 0.2316 -0.0537 -0.0016 84 ILE A CD1 320 N N . HIS A 42 ? 0.4567 0.6077 0.4703 0.2318 -0.0407 -0.0251 85 HIS A N 321 C CA . HIS A 42 ? 0.4934 0.6747 0.5232 0.2308 -0.0445 -0.0259 85 HIS A CA 322 C C . HIS A 42 ? 0.4500 0.6224 0.4685 0.2393 -0.0570 -0.0185 85 HIS A C 323 O O . HIS A 42 ? 0.4359 0.5953 0.4487 0.2539 -0.0624 -0.0178 85 HIS A O 324 C CB . HIS A 42 ? 0.5639 0.7778 0.6212 0.2394 -0.0400 -0.0366 85 HIS A CB 325 C CG . HIS A 42 ? 0.6019 0.8457 0.6760 0.2420 -0.0463 -0.0383 85 HIS A CG 326 N ND1 . HIS A 42 ? 0.6731 0.9268 0.7549 0.2584 -0.0550 -0.0406 85 HIS A ND1 327 C CD2 . HIS A 42 ? 0.5905 0.8561 0.6749 0.2306 -0.0461 -0.0385 85 HIS A CD2 328 C CE1 . HIS A 42 ? 0.6428 0.9236 0.7385 0.2571 -0.0600 -0.0424 85 HIS A CE1 329 N NE2 . HIS A 42 ? 0.6013 0.8899 0.6989 0.2402 -0.0545 -0.0413 85 HIS A NE2 330 N N . LEU A 43 ? 0.3767 0.5559 0.3916 0.2302 -0.0615 -0.0129 86 LEU A N 331 C CA . LEU A 43 ? 0.3803 0.5507 0.3819 0.2372 -0.0729 -0.0049 86 LEU A CA 332 C C . LEU A 43 ? 0.3976 0.6005 0.4179 0.2479 -0.0790 -0.0102 86 LEU A C 333 O O . LEU A 43 ? 0.4307 0.6605 0.4648 0.2401 -0.0781 -0.0135 86 LEU A O 334 C CB . LEU A 43 ? 0.4089 0.5686 0.3952 0.2220 -0.0742 0.0039 86 LEU A CB 335 C CG . LEU A 43 ? 0.4767 0.6106 0.4501 0.2082 -0.0672 0.0072 86 LEU A CG 336 C CD1 . LEU A 43 ? 0.5008 0.6263 0.4618 0.1936 -0.0686 0.0153 86 LEU A CD1 337 C CD2 . LEU A 43 ? 0.5347 0.6347 0.4917 0.2168 -0.0686 0.0104 86 LEU A CD2 338 N N . GLU A 44 ? 0.4150 0.6157 0.4369 0.2659 -0.0856 -0.0115 87 GLU A N 339 C CA . GLU A 44 ? 0.4383 0.6698 0.4793 0.2777 -0.0926 -0.0176 87 GLU A CA 340 C C . GLU A 44 ? 0.4224 0.6611 0.4543 0.2760 -0.1025 -0.0110 87 GLU A C 341 O O . GLU A 44 ? 0.5032 0.7154 0.5095 0.2758 -0.1084 0.0003 87 GLU A O 342 C CB . GLU A 44 ? 0.5999 0.8250 0.6438 0.2980 -0.0981 -0.0202 87 GLU A CB 343 C CG . GLU A 44 ? 0.7068 0.9328 0.7648 0.3014 -0.0878 -0.0294 87 GLU A CG 344 C CD . GLU A 44 ? 0.8419 1.0675 0.9082 0.3220 -0.0931 -0.0341 87 GLU A CD 345 O OE1 . GLU A 44 ? 0.8635 1.0836 0.9217 0.3340 -0.1056 -0.0287 87 GLU A OE1 346 O OE2 . GLU A 44 ? 0.8974 1.1283 0.9782 0.3264 -0.0846 -0.0431 87 GLU A OE2 347 N N . ASN A 45 ? 0.3842 0.6588 0.4373 0.2746 -0.1039 -0.0185 88 ASN A N 348 C CA . ASN A 45 ? 0.4585 0.7454 0.5055 0.2727 -0.1130 -0.0145 88 ASN A CA 349 C C . ASN A 45 ? 0.4893 0.7548 0.5115 0.2577 -0.1118 -0.0035 88 ASN A C 350 O O . ASN A 45 ? 0.5532 0.8104 0.5567 0.2607 -0.1208 0.0049 88 ASN A O 351 C CB . ASN A 45 ? 0.6196 0.9034 0.6576 0.2916 -0.1273 -0.0107 88 ASN A CB 352 C CG . ASN A 45 ? 0.7661 1.0541 0.8194 0.3089 -0.1292 -0.0178 88 ASN A CG 353 O OD1 . ASN A 45 ? 0.8521 1.1132 0.8954 0.3138 -0.1261 -0.0145 88 ASN A OD1 354 N ND2 . ASN A 45 ? 0.8208 1.1428 0.8995 0.3187 -0.1344 -0.0281 88 ASN A ND2 355 N N . VAL A 46 ? 0.4298 0.6858 0.4513 0.2420 -0.1008 -0.0033 89 VAL A N 356 C CA . VAL A 46 ? 0.3983 0.6361 0.3996 0.2270 -0.0991 0.0060 89 VAL A CA 357 C C . VAL A 46 ? 0.4142 0.6784 0.4324 0.2113 -0.0928 0.0000 89 VAL A C 358 O O . VAL A 46 ? 0.3837 0.6629 0.4223 0.2057 -0.0840 -0.0084 89 VAL A O 359 C CB . VAL A 46 ? 0.3894 0.5906 0.3734 0.2208 -0.0930 0.0124 89 VAL A CB 360 C CG1 . VAL A 46 ? 0.3988 0.5881 0.3708 0.2018 -0.0882 0.0185 89 VAL A CG1 361 C CG2 . VAL A 46 ? 0.4143 0.5850 0.3771 0.2346 -0.1004 0.0208 89 VAL A CG2 362 N N . THR A 47 ? 0.4076 0.4567 0.3368 0.0816 -0.0800 0.0213 90 THR A N 363 C CA . THR A 47 ? 0.3742 0.4287 0.3057 0.0707 -0.0769 0.0170 90 THR A CA 364 C C . THR A 47 ? 0.4255 0.4614 0.3385 0.0644 -0.0685 0.0172 90 THR A C 365 O O . THR A 47 ? 0.4965 0.5161 0.3890 0.0655 -0.0698 0.0211 90 THR A O 366 C CB . THR A 47 ? 0.4606 0.5201 0.3877 0.0683 -0.0877 0.0155 90 THR A CB 367 O OG1 . THR A 47 ? 0.4995 0.5786 0.4475 0.0734 -0.0965 0.0158 90 THR A OG1 368 C CG2 . THR A 47 ? 0.4254 0.4871 0.3525 0.0580 -0.0850 0.0101 90 THR A CG2 369 N N . GLU A 48 ? 0.3545 0.3936 0.2756 0.0578 -0.0598 0.0138 91 GLU A N 370 C CA . GLU A 48 ? 0.4041 0.4293 0.3122 0.0517 -0.0515 0.0139 91 GLU A CA 371 C C . GLU A 48 ? 0.3877 0.4184 0.2979 0.0434 -0.0482 0.0088 91 GLU A C 372 O O . GLU A 48 ? 0.3191 0.3635 0.2458 0.0413 -0.0493 0.0050 91 GLU A O 373 C CB . GLU A 48 ? 0.3764 0.3964 0.2904 0.0527 -0.0441 0.0148 91 GLU A CB 374 C CG . GLU A 48 ? 0.4744 0.4820 0.3812 0.0606 -0.0468 0.0194 91 GLU A CG 375 C CD . GLU A 48 ? 0.4938 0.4817 0.3803 0.0578 -0.0460 0.0245 91 GLU A CD 376 O OE1 . GLU A 48 ? 0.4634 0.4474 0.3448 0.0496 -0.0398 0.0242 91 GLU A OE1 377 O OE2 . GLU A 48 ? 0.5917 0.5682 0.4678 0.0639 -0.0516 0.0292 91 GLU A OE2 378 N N . ASN A 49 ? 0.3683 0.3883 0.2618 0.0391 -0.0442 0.0092 92 ASN A N 379 C CA . ASN A 49 ? 0.3087 0.3316 0.2020 0.0327 -0.0401 0.0040 92 ASN A CA 380 C C . ASN A 49 ? 0.3525 0.3746 0.2544 0.0285 -0.0302 0.0030 92 ASN A C 381 O O . ASN A 49 ? 0.3508 0.3643 0.2487 0.0286 -0.0252 0.0071 92 ASN A O 382 C CB . ASN A 49 ? 0.3767 0.3902 0.2471 0.0316 -0.0398 0.0046 92 ASN A CB 383 C CG . ASN A 49 ? 0.4942 0.5066 0.3530 0.0360 -0.0509 0.0054 92 ASN A CG 384 O OD1 . ASN A 49 ? 0.4831 0.5055 0.3544 0.0379 -0.0597 0.0029 92 ASN A OD1 385 N ND2 . ASN A 49 ? 0.6385 0.6394 0.4737 0.0375 -0.0506 0.0093 92 ASN A ND2 386 N N . PHE A 50 ? 0.3267 0.3570 0.2405 0.0247 -0.0284 -0.0024 93 PHE A N 387 C CA . PHE A 50 ? 0.2850 0.3147 0.2063 0.0208 -0.0199 -0.0039 93 PHE A CA 388 C C . PHE A 50 ? 0.3151 0.3444 0.2314 0.0166 -0.0171 -0.0088 93 PHE A C 389 O O . PHE A 50 ? 0.3470 0.3781 0.2583 0.0165 -0.0227 -0.0125 93 PHE A O 390 C CB . PHE A 50 ? 0.2991 0.3382 0.2397 0.0211 -0.0198 -0.0054 93 PHE A CB 391 C CG . PHE A 50 ? 0.3262 0.3658 0.2714 0.0269 -0.0211 -0.0014 93 PHE A CG 392 C CD1 . PHE A 50 ? 0.3349 0.3790 0.2804 0.0322 -0.0283 0.0006 93 PHE A CD1 393 C CD2 . PHE A 50 ? 0.3005 0.3353 0.2490 0.0280 -0.0159 -0.0002 93 PHE A CD2 394 C CE1 . PHE A 50 ? 0.3355 0.3795 0.2847 0.0392 -0.0293 0.0038 93 PHE A CE1 395 C CE2 . PHE A 50 ? 0.3023 0.3354 0.2526 0.0347 -0.0174 0.0025 93 PHE A CE2 396 C CZ . PHE A 50 ? 0.3304 0.3683 0.2811 0.0408 -0.0237 0.0045 93 PHE A CZ 397 N N . ASN A 51 ? 0.2775 0.3038 0.1947 0.0138 -0.0090 -0.0091 94 ASN A N 398 C CA . ASN A 51 ? 0.2901 0.3169 0.2053 0.0111 -0.0055 -0.0143 94 ASN A CA 399 C C . ASN A 51 ? 0.2815 0.3100 0.2095 0.0084 0.0008 -0.0153 94 ASN A C 400 O O . ASN A 51 ? 0.2906 0.3162 0.2176 0.0073 0.0070 -0.0123 94 ASN A O 401 C CB . ASN A 51 ? 0.2819 0.3028 0.1784 0.0119 -0.0015 -0.0132 94 ASN A CB 402 C CG . ASN A 51 ? 0.3111 0.3324 0.2039 0.0113 0.0022 -0.0195 94 ASN A CG 403 O OD1 . ASN A 51 ? 0.3115 0.3358 0.2159 0.0096 0.0010 -0.0245 94 ASN A OD1 404 N ND2 . ASN A 51 ? 0.3365 0.3541 0.2122 0.0132 0.0069 -0.0189 94 ASN A ND2 405 N N . MET A 52 ? 0.2428 0.2763 0.1835 0.0071 -0.0015 -0.0190 95 MET A N 406 C CA . MET A 52 ? 0.2798 0.3144 0.2323 0.0052 0.0030 -0.0197 95 MET A CA 407 C C . MET A 52 ? 0.3014 0.3336 0.2510 0.0038 0.0091 -0.0221 95 MET A C 408 O O . MET A 52 ? 0.2622 0.2944 0.2198 0.0026 0.0132 -0.0214 95 MET A O 409 C CB . MET A 52 ? 0.2731 0.3132 0.2381 0.0037 -0.0006 -0.0224 95 MET A CB 410 C CG . MET A 52 ? 0.2308 0.2701 0.1935 0.0017 -0.0042 -0.0281 95 MET A CG 411 S SD . MET A 52 ? 0.2359 0.2804 0.2152 -0.0020 -0.0086 -0.0296 95 MET A SD 412 C CE . MET A 52 ? 0.2197 0.2612 0.2055 -0.0028 -0.0014 -0.0298 95 MET A CE 413 N N . TRP A 53 ? 0.2951 0.3254 0.2330 0.0048 0.0095 -0.0250 96 TRP A N 414 C CA . TRP A 53 ? 0.2581 0.2877 0.1931 0.0051 0.0157 -0.0280 96 TRP A CA 415 C C . TRP A 53 ? 0.3384 0.3683 0.2679 0.0052 0.0231 -0.0225 96 TRP A C 416 O O . TRP A 53 ? 0.3360 0.3683 0.2661 0.0058 0.0299 -0.0234 96 TRP A O 417 C CB . TRP A 53 ? 0.2692 0.2957 0.1928 0.0073 0.0127 -0.0346 96 TRP A CB 418 C CG . TRP A 53 ? 0.3152 0.3412 0.2468 0.0054 0.0045 -0.0388 96 TRP A CG 419 C CD1 . TRP A 53 ? 0.3325 0.3586 0.2623 0.0047 -0.0042 -0.0394 96 TRP A CD1 420 C CD2 . TRP A 53 ? 0.3115 0.3375 0.2560 0.0034 0.0041 -0.0419 96 TRP A CD2 421 N NE1 . TRP A 53 ? 0.2692 0.2963 0.2114 0.0016 -0.0097 -0.0423 96 TRP A NE1 422 C CE2 . TRP A 53 ? 0.2662 0.2923 0.2164 0.0008 -0.0045 -0.0437 96 TRP A CE2 423 C CE3 . TRP A 53 ? 0.3128 0.3388 0.2649 0.0034 0.0097 -0.0429 96 TRP A CE3 424 C CZ2 . TRP A 53 ? 0.2473 0.2726 0.2096 -0.0023 -0.0071 -0.0457 96 TRP A CZ2 425 C CZ3 . TRP A 53 ? 0.2957 0.3199 0.2583 0.0014 0.0066 -0.0455 96 TRP A CZ3 426 C CH2 . TRP A 53 ? 0.3177 0.3410 0.2848 -0.0017 -0.0014 -0.0466 96 TRP A CH2 427 N N . LYS A 54 ? 0.3096 0.3373 0.2348 0.0048 0.0218 -0.0164 97 LYS A N 428 C CA . LYS A 54 ? 0.3122 0.3390 0.2340 0.0034 0.0277 -0.0095 97 LYS A CA 429 C C . LYS A 54 ? 0.3249 0.3477 0.2530 0.0018 0.0243 -0.0043 97 LYS A C 430 O O . LYS A 54 ? 0.3055 0.3232 0.2249 0.0028 0.0211 0.0002 97 LYS A O 431 C CB . LYS A 54 ? 0.4175 0.4416 0.3201 0.0055 0.0295 -0.0067 97 LYS A CB 432 C CG . LYS A 54 ? 0.5633 0.5900 0.4563 0.0085 0.0344 -0.0117 97 LYS A CG 433 C CD . LYS A 54 ? 0.7038 0.7273 0.5750 0.0113 0.0370 -0.0081 97 LYS A CD 434 C CE . LYS A 54 ? 0.7594 0.7851 0.6188 0.0157 0.0435 -0.0131 97 LYS A CE 435 N NZ . LYS A 54 ? 0.7903 0.8131 0.6483 0.0186 0.0366 -0.0239 97 LYS A NZ 436 N N . ASN A 55 ? 0.3173 0.3412 0.2593 0.0001 0.0243 -0.0053 98 ASN A N 437 C CA . ASN A 55 ? 0.2907 0.3094 0.2377 -0.0001 0.0203 -0.0023 98 ASN A CA 438 C C . ASN A 55 ? 0.2799 0.2977 0.2372 -0.0035 0.0230 -0.0005 98 ASN A C 439 O O . ASN A 55 ? 0.2375 0.2588 0.2044 -0.0038 0.0236 -0.0045 98 ASN A O 440 C CB . ASN A 55 ? 0.2859 0.3067 0.2385 0.0026 0.0154 -0.0065 98 ASN A CB 441 C CG . ASN A 55 ? 0.2726 0.2879 0.2276 0.0047 0.0118 -0.0040 98 ASN A CG 442 O OD1 . ASN A 55 ? 0.3005 0.3082 0.2521 0.0039 0.0115 0.0004 98 ASN A OD1 443 N ND2 . ASN A 55 ? 0.3046 0.3235 0.2653 0.0076 0.0091 -0.0065 98 ASN A ND2 444 N N . ASN A 56 ? 0.3054 0.3175 0.2608 -0.0063 0.0237 0.0059 99 ASN A N 445 C CA . ASN A 56 ? 0.3092 0.3205 0.2754 -0.0108 0.0250 0.0084 99 ASN A CA 446 C C . ASN A 56 ? 0.2790 0.2850 0.2522 -0.0097 0.0195 0.0054 99 ASN A C 447 O O . ASN A 56 ? 0.2301 0.2360 0.2131 -0.0129 0.0193 0.0058 99 ASN A O 448 C CB . ASN A 56 ? 0.3852 0.3904 0.3481 -0.0152 0.0259 0.0169 99 ASN A CB 449 C CG . ASN A 56 ? 0.4062 0.4116 0.3828 -0.0212 0.0262 0.0202 99 ASN A CG 450 O OD1 . ASN A 56 ? 0.4190 0.4132 0.3974 -0.0233 0.0200 0.0226 99 ASN A OD1 451 N ND2 . ASN A 56 ? 0.3178 0.3357 0.3044 -0.0234 0.0328 0.0200 99 ASN A ND2 452 N N . MET A 57 ? 0.2742 0.2764 0.2425 -0.0048 0.0152 0.0027 100 MET A N 453 C CA . MET A 57 ? 0.3028 0.3009 0.2752 -0.0022 0.0113 -0.0004 100 MET A CA 454 C C . MET A 57 ? 0.2630 0.2686 0.2446 -0.0030 0.0136 -0.0048 100 MET A C 455 O O . MET A 57 ? 0.2459 0.2480 0.2322 -0.0029 0.0112 -0.0062 100 MET A O 456 C CB . MET A 57 ? 0.2633 0.2600 0.2298 0.0040 0.0083 -0.0021 100 MET A CB 457 C CG . MET A 57 ? 0.2696 0.2580 0.2266 0.0067 0.0050 0.0018 100 MET A CG 458 S SD . MET A 57 ? 0.2767 0.2688 0.2306 0.0151 0.0023 -0.0002 100 MET A SD 459 C CE . MET A 57 ? 0.2889 0.2732 0.2434 0.0202 -0.0001 -0.0024 100 MET A CE 460 N N . VAL A 58 ? 0.2499 0.2644 0.2325 -0.0032 0.0174 -0.0072 101 VAL A N 461 C CA . VAL A 58 ? 0.2157 0.2360 0.2060 -0.0035 0.0193 -0.0113 101 VAL A CA 462 C C . VAL A 58 ? 0.2295 0.2516 0.2287 -0.0068 0.0212 -0.0103 101 VAL A C 463 O O . VAL A 58 ? 0.2376 0.2594 0.2439 -0.0066 0.0195 -0.0124 101 VAL A O 464 C CB . VAL A 58 ? 0.2463 0.2730 0.2338 -0.0027 0.0220 -0.0145 101 VAL A CB 465 C CG1 . VAL A 58 ? 0.2363 0.2668 0.2313 -0.0027 0.0237 -0.0188 101 VAL A CG1 466 C CG2 . VAL A 58 ? 0.2283 0.2551 0.2109 -0.0002 0.0186 -0.0157 101 VAL A CG2 467 N N . GLU A 59 ? 0.2166 0.2414 0.2159 -0.0097 0.0247 -0.0063 102 GLU A N 468 C CA . GLU A 59 ? 0.2497 0.2791 0.2604 -0.0134 0.0269 -0.0040 102 GLU A CA 469 C C . GLU A 59 ? 0.3151 0.3365 0.3314 -0.0157 0.0204 -0.0022 102 GLU A C 470 O O . GLU A 59 ? 0.3048 0.3291 0.3324 -0.0173 0.0190 -0.0030 102 GLU A O 471 C CB . GLU A 59 ? 0.3182 0.3526 0.3279 -0.0166 0.0327 0.0018 102 GLU A CB 472 C CG . GLU A 59 ? 0.3834 0.4285 0.3919 -0.0142 0.0405 -0.0003 102 GLU A CG 473 C CD . GLU A 59 ? 0.4476 0.4902 0.4422 -0.0096 0.0400 -0.0050 102 GLU A CD 474 O OE1 . GLU A 59 ? 0.4391 0.4864 0.4328 -0.0062 0.0428 -0.0104 102 GLU A OE1 475 O OE2 . GLU A 59 ? 0.4093 0.4446 0.3941 -0.0092 0.0361 -0.0035 102 GLU A OE2 476 N N . GLN A 60 ? 0.2535 0.2638 0.2610 -0.0152 0.0158 -0.0002 103 GLN A N 477 C CA . GLN A 60 ? 0.2524 0.2515 0.2614 -0.0165 0.0084 0.0006 103 GLN A CA 478 C C . GLN A 60 ? 0.2646 0.2608 0.2737 -0.0123 0.0046 -0.0048 103 GLN A C 479 O O . GLN A 60 ? 0.2459 0.2375 0.2605 -0.0137 -0.0005 -0.0054 103 GLN A O 480 C CB . GLN A 60 ? 0.2903 0.2763 0.2878 -0.0155 0.0042 0.0035 103 GLN A CB 481 C CG . GLN A 60 ? 0.2979 0.2832 0.2953 -0.0210 0.0064 0.0106 103 GLN A CG 482 C CD . GLN A 60 ? 0.3333 0.3017 0.3204 -0.0206 0.0000 0.0138 103 GLN A CD 483 O OE1 . GLN A 60 ? 0.2954 0.2509 0.2806 -0.0193 -0.0077 0.0119 103 GLN A OE1 484 N NE2 . GLN A 60 ? 0.3498 0.3167 0.3288 -0.0209 0.0025 0.0185 103 GLN A NE2 485 N N . MET A 61 ? 0.2711 0.2697 0.2739 -0.0073 0.0067 -0.0081 104 MET A N 486 C CA . MET A 61 ? 0.2804 0.2772 0.2829 -0.0035 0.0045 -0.0120 104 MET A CA 487 C C . MET A 61 ? 0.2612 0.2649 0.2748 -0.0055 0.0056 -0.0136 104 MET A C 488 O O . MET A 61 ? 0.2447 0.2440 0.2604 -0.0045 0.0012 -0.0152 104 MET A O 489 C CB . MET A 61 ? 0.2556 0.2559 0.2522 0.0009 0.0071 -0.0139 104 MET A CB 490 C CG . MET A 61 ? 0.2716 0.2706 0.2679 0.0042 0.0059 -0.0163 104 MET A CG 491 S SD . MET A 61 ? 0.2799 0.2834 0.2714 0.0087 0.0086 -0.0165 104 MET A SD 492 C CE . MET A 61 ? 0.4146 0.4138 0.4042 0.0119 0.0073 -0.0174 104 MET A CE 493 N N . GLN A 62 ? 0.1632 0.1772 0.1828 -0.0075 0.0111 -0.0136 105 GLN A N 494 C CA . GLN A 62 ? 0.2270 0.2485 0.2578 -0.0082 0.0127 -0.0153 105 GLN A CA 495 C C . GLN A 62 ? 0.2270 0.2479 0.2682 -0.0116 0.0085 -0.0129 105 GLN A C 496 O O . GLN A 62 ? 0.2019 0.2229 0.2500 -0.0107 0.0049 -0.0148 105 GLN A O 497 C CB . GLN A 62 ? 0.2845 0.3164 0.3180 -0.0085 0.0199 -0.0156 105 GLN A CB 498 C CG . GLN A 62 ? 0.2700 0.3107 0.3157 -0.0077 0.0223 -0.0174 105 GLN A CG 499 C CD . GLN A 62 ? 0.2858 0.3252 0.3297 -0.0036 0.0220 -0.0226 105 GLN A CD 500 O OE1 . GLN A 62 ? 0.2778 0.3098 0.3141 -0.0023 0.0188 -0.0239 105 GLN A OE1 501 N NE2 . GLN A 62 ? 0.3216 0.3681 0.3728 -0.0012 0.0253 -0.0251 105 GLN A NE2 502 N N . GLU A 63 ? 0.2265 0.2463 0.2693 -0.0160 0.0082 -0.0083 106 GLU A N 503 C CA . GLU A 63 ? 0.2883 0.3072 0.3428 -0.0209 0.0029 -0.0052 106 GLU A CA 504 C C . GLU A 63 ? 0.2824 0.2881 0.3324 -0.0190 -0.0070 -0.0080 106 GLU A C 505 O O . GLU A 63 ? 0.2462 0.2530 0.3067 -0.0205 -0.0124 -0.0085 106 GLU A O 506 C CB . GLU A 63 ? 0.3219 0.3389 0.3768 -0.0268 0.0035 0.0011 106 GLU A CB 507 C CG . GLU A 63 ? 0.4336 0.4653 0.4941 -0.0288 0.0138 0.0049 106 GLU A CG 508 C CD . GLU A 63 ? 0.5959 0.6236 0.6502 -0.0330 0.0159 0.0114 106 GLU A CD 509 O OE1 . GLU A 63 ? 0.5164 0.5289 0.5602 -0.0333 0.0095 0.0122 106 GLU A OE1 510 O OE2 . GLU A 63 ? 0.6635 0.7029 0.7223 -0.0354 0.0242 0.0160 106 GLU A OE2 511 N N . ASP A 64 ? 0.2268 0.2204 0.2606 -0.0148 -0.0094 -0.0099 107 ASP A N 512 C CA . ASP A 64 ? 0.2715 0.2514 0.2966 -0.0112 -0.0178 -0.0128 107 ASP A CA 513 C C . ASP A 64 ? 0.2432 0.2262 0.2704 -0.0075 -0.0184 -0.0163 107 ASP A C 514 O O . ASP A 64 ? 0.2245 0.2010 0.2530 -0.0071 -0.0263 -0.0176 107 ASP A O 515 C CB . ASP A 64 ? 0.2706 0.2400 0.2779 -0.0055 -0.0178 -0.0141 107 ASP A CB 516 C CG . ASP A 64 ? 0.3491 0.3070 0.3503 -0.0074 -0.0221 -0.0116 107 ASP A CG 517 O OD1 . ASP A 64 ? 0.3018 0.2575 0.3121 -0.0141 -0.0265 -0.0085 107 ASP A OD1 518 O OD2 . ASP A 64 ? 0.3207 0.2716 0.3087 -0.0021 -0.0214 -0.0123 107 ASP A OD2 519 N N . VAL A 65 ? 0.2502 0.2415 0.2766 -0.0048 -0.0113 -0.0176 108 VAL A N 520 C CA . VAL A 65 ? 0.2420 0.2342 0.2689 -0.0013 -0.0119 -0.0202 108 VAL A CA 521 C C . VAL A 65 ? 0.2588 0.2586 0.3017 -0.0036 -0.0139 -0.0203 108 VAL A C 522 O O . VAL A 65 ? 0.2564 0.2524 0.3001 -0.0013 -0.0192 -0.0218 108 VAL A O 523 C CB . VAL A 65 ? 0.2480 0.2457 0.2712 0.0012 -0.0048 -0.0212 108 VAL A CB 524 C CG1 . VAL A 65 ? 0.2438 0.2401 0.2671 0.0042 -0.0060 -0.0229 108 VAL A CG1 525 C CG2 . VAL A 65 ? 0.2495 0.2425 0.2599 0.0038 -0.0030 -0.0205 108 VAL A CG2 526 N N . ILE A 66 ? 0.2189 0.2301 0.2743 -0.0077 -0.0096 -0.0183 109 ILE A N 527 C CA . ILE A 66 ? 0.2405 0.2618 0.3139 -0.0095 -0.0109 -0.0177 109 ILE A CA 528 C C . ILE A 66 ? 0.2596 0.2740 0.3381 -0.0123 -0.0218 -0.0165 109 ILE A C 529 O O . ILE A 66 ? 0.2994 0.3153 0.3863 -0.0109 -0.0275 -0.0178 109 ILE A O 530 C CB . ILE A 66 ? 0.1882 0.2242 0.2737 -0.0131 -0.0030 -0.0146 109 ILE A CB 531 C CG1 . ILE A 66 ? 0.2236 0.2656 0.3035 -0.0093 0.0062 -0.0171 109 ILE A CG1 532 C CG2 . ILE A 66 ? 0.2053 0.2539 0.3122 -0.0152 -0.0046 -0.0128 109 ILE A CG2 533 C CD1 . ILE A 66 ? 0.2966 0.3519 0.3838 -0.0112 0.0150 -0.0144 109 ILE A CD1 534 N N . SER A 67 ? 0.2756 0.2811 0.3483 -0.0159 -0.0256 -0.0144 110 SER A N 535 C CA . SER A 67 ? 0.3172 0.3126 0.3924 -0.0189 -0.0377 -0.0139 110 SER A CA 536 C C . SER A 67 ? 0.2939 0.2756 0.3552 -0.0127 -0.0455 -0.0182 110 SER A C 537 O O . SER A 67 ? 0.2671 0.2459 0.3348 -0.0131 -0.0552 -0.0191 110 SER A O 538 C CB . SER A 67 ? 0.3494 0.3336 0.4169 -0.0229 -0.0407 -0.0113 110 SER A CB 539 O OG . SER A 67 ? 0.4243 0.3968 0.4943 -0.0265 -0.0538 -0.0112 110 SER A OG 540 N N . LEU A 68 ? 0.2238 0.1978 0.2662 -0.0068 -0.0414 -0.0204 111 LEU A N 541 C CA . LEU A 68 ? 0.2694 0.2313 0.2964 -0.0003 -0.0465 -0.0235 111 LEU A CA 542 C C . LEU A 68 ? 0.2983 0.2671 0.3342 0.0017 -0.0475 -0.0244 111 LEU A C 543 O O . LEU A 68 ? 0.3339 0.2942 0.3665 0.0040 -0.0571 -0.0258 111 LEU A O 544 C CB . LEU A 68 ? 0.3367 0.2939 0.3456 0.0052 -0.0393 -0.0242 111 LEU A CB 545 C CG . LEU A 68 ? 0.4022 0.3457 0.3911 0.0126 -0.0430 -0.0262 111 LEU A CG 546 C CD1 . LEU A 68 ? 0.4258 0.3649 0.3990 0.0172 -0.0370 -0.0260 111 LEU A CD1 547 C CD2 . LEU A 68 ? 0.3626 0.3102 0.3524 0.0154 -0.0408 -0.0261 111 LEU A CD2 548 N N . TRP A 69 ? 0.2404 0.2228 0.2863 0.0015 -0.0385 -0.0238 112 TRP A N 549 C CA . TRP A 69 ? 0.2849 0.2725 0.3388 0.0043 -0.0393 -0.0248 112 TRP A CA 550 C C . TRP A 69 ? 0.3207 0.3160 0.3945 0.0015 -0.0467 -0.0242 112 TRP A C 551 O O . TRP A 69 ? 0.3083 0.3020 0.3855 0.0047 -0.0530 -0.0253 112 TRP A O 552 C CB . TRP A 69 ? 0.2857 0.2839 0.3443 0.0052 -0.0287 -0.0252 112 TRP A CB 553 C CG . TRP A 69 ? 0.2438 0.2348 0.2862 0.0087 -0.0242 -0.0256 112 TRP A CG 554 C CD1 . TRP A 69 ? 0.3107 0.2953 0.3387 0.0091 -0.0217 -0.0248 112 TRP A CD1 555 C CD2 . TRP A 69 ? 0.2462 0.2364 0.2867 0.0119 -0.0218 -0.0263 112 TRP A CD2 556 N NE1 . TRP A 69 ? 0.3095 0.2916 0.3286 0.0119 -0.0175 -0.0244 112 TRP A NE1 557 C CE2 . TRP A 69 ? 0.2695 0.2538 0.2956 0.0130 -0.0177 -0.0251 112 TRP A CE2 558 C CE3 . TRP A 69 ? 0.2849 0.2785 0.3349 0.0142 -0.0230 -0.0275 112 TRP A CE3 559 C CZ2 . TRP A 69 ? 0.3063 0.2879 0.3282 0.0148 -0.0151 -0.0244 112 TRP A CZ2 560 C CZ3 . TRP A 69 ? 0.3027 0.2910 0.3464 0.0168 -0.0208 -0.0275 112 TRP A CZ3 561 C CH2 . TRP A 69 ? 0.3111 0.2934 0.3411 0.0163 -0.0170 -0.0257 112 TRP A CH2 562 N N . ASP A 70 ? 0.3052 0.3091 0.3928 -0.0046 -0.0460 -0.0218 113 ASP A N 563 C CA . ASP A 70 ? 0.3572 0.3714 0.4674 -0.0083 -0.0525 -0.0201 113 ASP A CA 564 C C . ASP A 70 ? 0.3910 0.3914 0.4971 -0.0090 -0.0681 -0.0211 113 ASP A C 565 O O . ASP A 70 ? 0.4380 0.4437 0.5590 -0.0091 -0.0764 -0.0210 113 ASP A O 566 C CB . ASP A 70 ? 0.3926 0.4200 0.5188 -0.0157 -0.0470 -0.0157 113 ASP A CB 567 C CG . ASP A 70 ? 0.4798 0.5251 0.6159 -0.0141 -0.0335 -0.0149 113 ASP A CG 568 O OD1 . ASP A 70 ? 0.5515 0.5956 0.6787 -0.0079 -0.0282 -0.0183 113 ASP A OD1 569 O OD2 . ASP A 70 ? 0.5169 0.5764 0.6687 -0.0192 -0.0281 -0.0107 113 ASP A OD2 570 N N . GLN A 71 ? 0.3819 0.3641 0.4671 -0.0085 -0.0725 -0.0224 114 GLN A N 571 C CA . GLN A 71 ? 0.3963 0.3618 0.4727 -0.0081 -0.0879 -0.0243 114 GLN A CA 572 C C . GLN A 71 ? 0.4301 0.3835 0.4876 0.0005 -0.0921 -0.0276 114 GLN A C 573 O O . GLN A 71 ? 0.4951 0.4391 0.5499 0.0021 -0.1055 -0.0293 114 GLN A O 574 C CB . GLN A 71 ? 0.4864 0.4354 0.5465 -0.0101 -0.0913 -0.0248 114 GLN A CB 575 C CG . GLN A 71 ? 0.6339 0.5912 0.7099 -0.0192 -0.0882 -0.0205 114 GLN A CG 576 C CD . GLN A 71 ? 0.7449 0.6850 0.8017 -0.0193 -0.0891 -0.0210 114 GLN A CD 577 O OE1 . GLN A 71 ? 0.7808 0.7023 0.8134 -0.0125 -0.0938 -0.0251 114 GLN A OE1 578 N NE2 . GLN A 71 ? 0.7612 0.7074 0.8281 -0.0263 -0.0842 -0.0166 114 GLN A NE2 579 N N . SER A 72 ? 0.3630 0.3167 0.4077 0.0057 -0.0811 -0.0280 115 SER A N 580 C CA . SER A 72 ? 0.4460 0.3860 0.4683 0.0135 -0.0831 -0.0297 115 SER A CA 581 C C . SER A 72 ? 0.3973 0.3440 0.4256 0.0172 -0.0807 -0.0291 115 SER A C 582 O O . SER A 72 ? 0.4209 0.3561 0.4344 0.0228 -0.0861 -0.0296 115 SER A O 583 C CB . SER A 72 ? 0.5100 0.4437 0.5120 0.0168 -0.0732 -0.0295 115 SER A CB 584 O OG . SER A 72 ? 0.6498 0.5785 0.6480 0.0139 -0.0740 -0.0299 115 SER A OG 585 N N . LEU A 73 ? 0.3283 0.2921 0.3765 0.0146 -0.0726 -0.0279 116 LEU A N 586 C CA . LEU A 73 ? 0.3921 0.3608 0.4452 0.0187 -0.0696 -0.0278 116 LEU A CA 587 C C . LEU A 73 ? 0.3808 0.3660 0.4611 0.0174 -0.0714 -0.0278 116 LEU A C 588 O O . LEU A 73 ? 0.3870 0.3827 0.4770 0.0187 -0.0629 -0.0280 116 LEU A O 589 C CB . LEU A 73 ? 0.3913 0.3625 0.4375 0.0196 -0.0566 -0.0272 116 LEU A CB 590 C CG . LEU A 73 ? 0.4563 0.4143 0.4781 0.0227 -0.0532 -0.0262 116 LEU A CG 591 C CD1 . LEU A 73 ? 0.4830 0.4370 0.4945 0.0207 -0.0513 -0.0262 116 LEU A CD1 592 C CD2 . LEU A 73 ? 0.4275 0.3892 0.4486 0.0233 -0.0433 -0.0251 116 LEU A CD2 593 N N . GLN A 74 ? 0.3934 0.3808 0.4861 0.0151 -0.0826 -0.0276 117 GLN A N 594 C CA . GLN A 74 ? 0.4471 0.4521 0.5677 0.0148 -0.0850 -0.0270 117 GLN A CA 595 C C . GLN A 74 ? 0.4108 0.4121 0.5297 0.0225 -0.0893 -0.0280 117 GLN A C 596 O O . GLN A 74 ? 0.4303 0.4144 0.5304 0.0264 -0.0978 -0.0286 117 GLN A O 597 C CB . GLN A 74 ? 0.5283 0.5379 0.6655 0.0092 -0.0970 -0.0257 117 GLN A CB 598 C CG . GLN A 74 ? 0.5672 0.5838 0.7127 0.0005 -0.0922 -0.0233 117 GLN A CG 599 C CD . GLN A 74 ? 0.5749 0.6158 0.7446 -0.0020 -0.0798 -0.0206 117 GLN A CD 600 O OE1 . GLN A 74 ? 0.5260 0.5825 0.7160 0.0011 -0.0792 -0.0202 117 GLN A OE1 601 N NE2 . GLN A 74 ? 0.5483 0.5921 0.7148 -0.0067 -0.0698 -0.0188 117 GLN A NE2 602 N N . PRO A 75 ? 0.3532 0.3694 0.4901 0.0256 -0.0831 -0.0283 118 PRO A N 603 C CA . PRO A 75 ? 0.3132 0.3257 0.4495 0.0336 -0.0862 -0.0293 118 PRO A CA 604 C C . PRO A 75 ? 0.3053 0.3244 0.4601 0.0361 -0.0996 -0.0290 118 PRO A C 605 O O . PRO A 75 ? 0.3178 0.3484 0.4907 0.0307 -0.1051 -0.0277 118 PRO A O 606 C CB . PRO A 75 ? 0.2838 0.3105 0.4326 0.0360 -0.0734 -0.0305 118 PRO A CB 607 C CG . PRO A 75 ? 0.2755 0.3220 0.4452 0.0300 -0.0685 -0.0291 118 PRO A CG 608 C CD . PRO A 75 ? 0.3236 0.3604 0.4807 0.0224 -0.0720 -0.0276 118 PRO A CD 609 N N . CYS A 76 ? 0.2703 0.2825 0.4219 0.0440 -0.1055 -0.0296 119 CYS A N 610 C CA . CYS A 76 ? 0.3064 0.3260 0.4771 0.0479 -0.1187 -0.0293 119 CYS A CA 611 C C . CYS A 76 ? 0.3395 0.3874 0.5449 0.0478 -0.1127 -0.0291 119 CYS A C 612 O O . CYS A 76 ? 0.3271 0.3900 0.5570 0.0455 -0.1213 -0.0276 119 CYS A O 613 C CB . CYS A 76 ? 0.3721 0.3780 0.5312 0.0573 -0.1243 -0.0297 119 CYS A CB 614 S SG . CYS A 76 ? 0.7475 0.7220 0.8641 0.0585 -0.1253 -0.0285 119 CYS A SG 615 N N . VAL A 77 ? 0.2650 0.3201 0.4723 0.0507 -0.0980 -0.0305 120 VAL A N 616 C CA . VAL A 77 ? 0.2831 0.3650 0.5197 0.0520 -0.0893 -0.0303 120 VAL A CA 617 C C . VAL A 77 ? 0.3103 0.3968 0.5404 0.0489 -0.0725 -0.0311 120 VAL A C 618 O O . VAL A 77 ? 0.2688 0.3392 0.4755 0.0504 -0.0664 -0.0332 120 VAL A O 619 C CB . VAL A 77 ? 0.4403 0.5292 0.6904 0.0638 -0.0907 -0.0323 120 VAL A CB 620 C CG1 . VAL A 77 ? 0.5544 0.6179 0.7776 0.0703 -0.0926 -0.0346 120 VAL A CG1 621 C CG2 . VAL A 77 ? 0.4232 0.5352 0.6929 0.0676 -0.0759 -0.0335 120 VAL A CG2 622 N N . LYS A 78 ? 0.2926 0.4013 0.5439 0.0440 -0.0654 -0.0287 121 LYS A N 623 C CA . LYS A 78 ? 0.2798 0.3946 0.5259 0.0409 -0.0499 -0.0288 121 LYS A CA 624 C C . LYS A 78 ? 0.2791 0.4194 0.5493 0.0469 -0.0394 -0.0289 121 LYS A C 625 O O . LYS A 78 ? 0.2727 0.4352 0.5713 0.0452 -0.0412 -0.0251 121 LYS A O 626 C CB . LYS A 78 ? 0.4021 0.5179 0.6474 0.0292 -0.0500 -0.0249 121 LYS A CB 627 C CG . LYS A 78 ? 0.5434 0.6663 0.7842 0.0253 -0.0350 -0.0239 121 LYS A CG 628 C CD . LYS A 78 ? 0.6878 0.7935 0.9012 0.0291 -0.0281 -0.0281 121 LYS A CD 629 C CE . LYS A 78 ? 0.8008 0.9145 1.0103 0.0263 -0.0140 -0.0275 121 LYS A CE 630 N NZ . LYS A 78 ? 0.8654 0.9739 1.0616 0.0339 -0.0054 -0.0326 121 LYS A NZ 631 N N . LEU A 79 ? 0.2330 0.3701 0.4920 0.0541 -0.0288 -0.0331 122 LEU A N 632 C CA . LEU A 79 ? 0.2430 0.4023 0.5197 0.0618 -0.0172 -0.0342 122 LEU A CA 633 C C . LEU A 79 ? 0.2996 0.4660 0.5696 0.0568 -0.0030 -0.0329 122 LEU A C 634 O O . LEU A 79 ? 0.2641 0.4146 0.5096 0.0576 0.0026 -0.0367 122 LEU A O 635 C CB . LEU A 79 ? 0.3181 0.4668 0.5850 0.0748 -0.0159 -0.0407 122 LEU A CB 636 C CG . LEU A 79 ? 0.3813 0.5173 0.6486 0.0808 -0.0303 -0.0421 122 LEU A CG 637 C CD1 . LEU A 79 ? 0.3676 0.4838 0.6161 0.0908 -0.0296 -0.0481 122 LEU A CD1 638 C CD2 . LEU A 79 ? 0.4010 0.5609 0.7013 0.0858 -0.0354 -0.0396 122 LEU A CD2 639 N N . THR A 80 ? 0.2683 0.4583 0.5602 0.0512 0.0025 -0.0270 123 THR A N 640 C CA . THR A 80 ? 0.2524 0.4481 0.5370 0.0450 0.0149 -0.0241 123 THR A CA 641 C C . THR A 80 ? 0.2989 0.5265 0.6102 0.0463 0.0267 -0.0189 123 THR A C 642 O O . THR A 80 ? 0.3207 0.5673 0.6604 0.0416 0.0223 -0.0127 123 THR A O 643 C CB . THR A 80 ? 0.2953 0.4790 0.5708 0.0313 0.0082 -0.0196 123 THR A CB 644 O OG1 . THR A 80 ? 0.3878 0.5771 0.6569 0.0256 0.0198 -0.0162 123 THR A OG1 645 C CG2 . THR A 80 ? 0.2919 0.4862 0.5922 0.0241 -0.0030 -0.0139 123 THR A CG2 646 N N . GLY A 81 ? 0.3806 0.6142 0.6824 0.0527 0.0416 -0.0211 124 GLY A N 647 C CA . GLY A 81 ? 0.3649 0.6287 0.6876 0.0549 0.0558 -0.0157 124 GLY A CA 648 C C . GLY A 81 ? 0.3864 0.6760 0.7428 0.0626 0.0553 -0.0139 124 GLY A C 649 O O . GLY A 81 ? 0.4312 0.7497 0.8159 0.0588 0.0619 -0.0056 124 GLY A O 650 N N . GLY A 82 ? 0.3477 0.6275 0.7024 0.0733 0.0472 -0.0211 198 GLY A N 651 C CA . GLY A 82 ? 0.3084 0.6114 0.6938 0.0831 0.0460 -0.0205 198 GLY A CA 652 C C . GLY A 82 ? 0.3176 0.6258 0.7275 0.0756 0.0293 -0.0157 198 GLY A C 653 O O . GLY A 82 ? 0.3835 0.7090 0.8194 0.0837 0.0250 -0.0154 198 GLY A O 654 N N . SER A 83 ? 0.3238 0.6165 0.7247 0.0610 0.0192 -0.0122 199 SER A N 655 C CA . SER A 83 ? 0.3284 0.6222 0.7484 0.0534 0.0016 -0.0084 199 SER A CA 656 C C . SER A 83 ? 0.3039 0.5645 0.6989 0.0546 -0.0144 -0.0145 199 SER A C 657 O O . SER A 83 ? 0.2475 0.4827 0.6096 0.0560 -0.0122 -0.0197 199 SER A O 658 C CB . SER A 83 ? 0.3642 0.6654 0.7955 0.0363 -0.0003 0.0005 199 SER A CB 659 O OG . SER A 83 ? 0.4688 0.7468 0.8682 0.0290 0.0031 -0.0006 199 SER A OG 660 N N . VAL A 84 ? 0.3071 0.5689 0.7185 0.0540 -0.0308 -0.0133 200 VAL A N 661 C CA . VAL A 84 ? 0.3211 0.5527 0.7096 0.0554 -0.0464 -0.0179 200 VAL A CA 662 C C . VAL A 84 ? 0.3394 0.5620 0.7289 0.0425 -0.0618 -0.0139 200 VAL A C 663 O O . VAL A 84 ? 0.3382 0.5785 0.7573 0.0383 -0.0713 -0.0093 200 VAL A O 664 C CB . VAL A 84 ? 0.3806 0.6150 0.7806 0.0687 -0.0549 -0.0213 200 VAL A CB 665 C CG1 . VAL A 84 ? 0.4002 0.6023 0.7741 0.0698 -0.0706 -0.0248 200 VAL A CG1 666 C CG2 . VAL A 84 ? 0.3533 0.5941 0.7510 0.0830 -0.0406 -0.0261 200 VAL A CG2 667 N N . ILE A 85 ? 0.3273 0.5220 0.6844 0.0366 -0.0647 -0.0159 201 ILE A N 668 C CA . ILE A 85 ? 0.3611 0.5424 0.7127 0.0257 -0.0790 -0.0135 201 ILE A CA 669 C C . ILE A 85 ? 0.3748 0.5275 0.7008 0.0303 -0.0931 -0.0180 201 ILE A C 670 O O . ILE A 85 ? 0.3606 0.4933 0.6574 0.0348 -0.0881 -0.0219 201 ILE A O 671 C CB . ILE A 85 ? 0.4217 0.5930 0.7550 0.0157 -0.0711 -0.0117 201 ILE A CB 672 C CG1 . ILE A 85 ? 0.4519 0.6487 0.8038 0.0127 -0.0542 -0.0072 201 ILE A CG1 673 C CG2 . ILE A 85 ? 0.4354 0.5946 0.7664 0.0047 -0.0860 -0.0092 201 ILE A CG2 674 C CD1 . ILE A 85 ? 0.4841 0.7098 0.8759 0.0065 -0.0571 0.0000 201 ILE A CD1 675 N N . LYS A 86 ? 0.2827 0.4340 0.6198 0.0289 -0.1110 -0.0169 202 LYS A N 676 C CA . LYS A 86 ? 0.3658 0.4902 0.6777 0.0338 -0.1252 -0.0204 202 LYS A CA 677 C C . LYS A 86 ? 0.3891 0.4947 0.6856 0.0248 -0.1387 -0.0198 202 LYS A C 678 O O . LYS A 86 ? 0.3863 0.5032 0.7042 0.0160 -0.1466 -0.0165 202 LYS A O 679 C CB . LYS A 86 ? 0.3804 0.5138 0.7120 0.0425 -0.1374 -0.0207 202 LYS A CB 680 C CG . LYS A 86 ? 0.4141 0.5637 0.7599 0.0539 -0.1260 -0.0222 202 LYS A CG 681 C CD . LYS A 86 ? 0.4598 0.6181 0.8263 0.0628 -0.1399 -0.0222 202 LYS A CD 682 C CE . LYS A 86 ? 0.5023 0.6791 0.8866 0.0753 -0.1287 -0.0238 202 LYS A CE 683 N NZ . LYS A 86 ? 0.5728 0.7264 0.9258 0.0841 -0.1210 -0.0285 202 LYS A NZ 684 N N . GLN A 87 ? 0.4153 0.4921 0.6749 0.0271 -0.1414 -0.0229 203 GLN A N 685 C CA . GLN A 87 ? 0.4732 0.5290 0.7133 0.0213 -0.1545 -0.0235 203 GLN A CA 686 C C . GLN A 87 ? 0.4623 0.4886 0.6638 0.0281 -0.1594 -0.0265 203 GLN A C 687 O O . GLN A 87 ? 0.3673 0.3890 0.5575 0.0359 -0.1519 -0.0275 203 GLN A O 688 C CB . GLN A 87 ? 0.5235 0.5791 0.7598 0.0113 -0.1463 -0.0220 203 GLN A CB 689 C CG . GLN A 87 ? 0.5189 0.5720 0.7380 0.0130 -0.1268 -0.0227 203 GLN A CG 690 C CD . GLN A 87 ? 0.5502 0.6144 0.7788 0.0038 -0.1164 -0.0198 203 GLN A CD 691 O OE1 . GLN A 87 ? 0.5980 0.6632 0.8366 -0.0048 -0.1246 -0.0174 203 GLN A OE1 692 N NE2 . GLN A 87 ? 0.5267 0.5979 0.7515 0.0055 -0.0992 -0.0198 203 GLN A NE2 693 N N . ALA A 88 ? 0.4608 0.4668 0.6420 0.0254 -0.1723 -0.0278 204 ALA A N 694 C CA . ALA A 88 ? 0.5144 0.4925 0.6570 0.0319 -0.1765 -0.0300 204 ALA A CA 695 C C . ALA A 88 ? 0.4705 0.4406 0.5900 0.0328 -0.1586 -0.0301 204 ALA A C 696 O O . ALA A 88 ? 0.4085 0.3854 0.5320 0.0265 -0.1482 -0.0296 204 ALA A O 697 C CB . ALA A 88 ? 0.5085 0.4672 0.6340 0.0291 -0.1933 -0.0319 204 ALA A CB 698 N N . CYS A 89 ? 0.4279 0.3833 0.5235 0.0403 -0.1556 -0.0301 205 CYS A N 699 C CA . CYS A 89 ? 0.4267 0.3761 0.5032 0.0411 -0.1394 -0.0294 205 CYS A CA 700 C C . CYS A 89 ? 0.4109 0.3357 0.4508 0.0464 -0.1418 -0.0289 205 CYS A C 701 O O . CYS A 89 ? 0.4004 0.3190 0.4287 0.0513 -0.1359 -0.0269 205 CYS A O 702 C CB . CYS A 89 ? 0.4303 0.3921 0.5208 0.0442 -0.1283 -0.0286 205 CYS A CB 703 S SG . CYS A 89 ? 0.5902 0.5485 0.6856 0.0536 -0.1392 -0.0280 205 CYS A SG 704 N N . PRO A 90 ? 0.4929 0.4033 0.5138 0.0456 -0.1500 -0.0304 206 PRO A N 705 C CA . PRO A 90 ? 0.5623 0.4499 0.5466 0.0519 -0.1519 -0.0297 206 PRO A CA 706 C C . PRO A 90 ? 0.5152 0.4009 0.4839 0.0523 -0.1342 -0.0273 206 PRO A C 707 O O . PRO A 90 ? 0.4442 0.3425 0.4258 0.0470 -0.1228 -0.0275 206 PRO A O 708 C CB . PRO A 90 ? 0.5997 0.4748 0.5705 0.0505 -0.1631 -0.0331 206 PRO A CB 709 C CG . PRO A 90 ? 0.5691 0.4605 0.5661 0.0415 -0.1596 -0.0343 206 PRO A CG 710 C CD . PRO A 90 ? 0.5269 0.4407 0.5583 0.0389 -0.1570 -0.0326 206 PRO A CD 711 N N . LYS A 91 ? 0.4560 0.3266 0.3978 0.0585 -0.1321 -0.0244 207 LYS A N 712 C CA . LYS A 91 ? 0.4929 0.3616 0.4196 0.0586 -0.1163 -0.0212 207 LYS A CA 713 C C . LYS A 91 ? 0.4732 0.3376 0.3861 0.0576 -0.1133 -0.0235 207 LYS A C 714 O O . LYS A 91 ? 0.5066 0.3595 0.4071 0.0599 -0.1249 -0.0268 207 LYS A O 715 C CB . LYS A 91 ? 0.5300 0.3838 0.4314 0.0652 -0.1152 -0.0161 207 LYS A CB 716 C CG . LYS A 91 ? 0.5303 0.3868 0.4439 0.0662 -0.1157 -0.0130 207 LYS A CG 717 C CD . LYS A 91 ? 0.5430 0.4152 0.4782 0.0605 -0.1027 -0.0126 207 LYS A CD 718 C CE . LYS A 91 ? 0.5377 0.4102 0.4837 0.0624 -0.1035 -0.0104 207 LYS A CE 719 N NZ . LYS A 91 ? 0.4696 0.3542 0.4326 0.0577 -0.0915 -0.0107 207 LYS A NZ 720 N N . ILE A 92 ? 0.4131 0.2857 0.3277 0.0546 -0.0987 -0.0220 208 ILE A N 721 C CA . ILE A 92 ? 0.3835 0.2531 0.2869 0.0543 -0.0950 -0.0241 208 ILE A CA 722 C C . ILE A 92 ? 0.4196 0.2862 0.3029 0.0580 -0.0818 -0.0201 208 ILE A C 723 O O . ILE A 92 ? 0.4174 0.2860 0.2991 0.0586 -0.0745 -0.0151 208 ILE A O 724 C CB . ILE A 92 ? 0.4241 0.3096 0.3522 0.0465 -0.0900 -0.0263 208 ILE A CB 725 C CG1 . ILE A 92 ? 0.3757 0.2758 0.3184 0.0429 -0.0764 -0.0233 208 ILE A CG1 726 C CG2 . ILE A 92 ? 0.4756 0.3670 0.4259 0.0421 -0.1018 -0.0292 208 ILE A CG2 727 C CD1 . ILE A 92 ? 0.3724 0.2865 0.3327 0.0365 -0.0693 -0.0247 208 ILE A CD1 728 N N . SER A 93 ? 0.4191 0.2808 0.2883 0.0603 -0.0791 -0.0221 209 SER A N 729 C CA . SER A 93 ? 0.4652 0.3288 0.3205 0.0635 -0.0653 -0.0185 209 SER A CA 730 C C . SER A 93 ? 0.4183 0.2982 0.2944 0.0567 -0.0560 -0.0189 209 SER A C 731 O O . SER A 93 ? 0.3643 0.2459 0.2493 0.0536 -0.0603 -0.0232 209 SER A O 732 C CB . SER A 93 ? 0.5148 0.3631 0.3412 0.0721 -0.0681 -0.0210 209 SER A CB 733 O OG . SER A 93 ? 0.5196 0.3731 0.3360 0.0757 -0.0540 -0.0176 209 SER A OG 734 N N . PHE A 94 ? 0.4232 0.3143 0.3068 0.0541 -0.0441 -0.0141 210 PHE A N 735 C CA . PHE A 94 ? 0.3639 0.2704 0.2682 0.0474 -0.0367 -0.0145 210 PHE A CA 736 C C . PHE A 94 ? 0.3639 0.2782 0.2646 0.0479 -0.0237 -0.0097 210 PHE A C 737 O O . PHE A 94 ? 0.3702 0.2858 0.2687 0.0477 -0.0184 -0.0042 210 PHE A O 738 C CB . PHE A 94 ? 0.3459 0.2604 0.2720 0.0415 -0.0383 -0.0146 210 PHE A CB 739 C CG . PHE A 94 ? 0.3393 0.2684 0.2848 0.0352 -0.0315 -0.0156 210 PHE A CG 740 C CD1 . PHE A 94 ? 0.3449 0.2816 0.2936 0.0329 -0.0217 -0.0121 210 PHE A CD1 741 C CD2 . PHE A 94 ? 0.3396 0.2748 0.3003 0.0312 -0.0354 -0.0195 210 PHE A CD2 742 C CE1 . PHE A 94 ? 0.3058 0.2543 0.2700 0.0277 -0.0168 -0.0136 210 PHE A CE1 743 C CE2 . PHE A 94 ? 0.3298 0.2775 0.3055 0.0262 -0.0289 -0.0202 210 PHE A CE2 744 C CZ . PHE A 94 ? 0.3008 0.2543 0.2771 0.0248 -0.0201 -0.0177 210 PHE A CZ 745 N N . ASP A 95 ? 0.3597 0.2794 0.2610 0.0480 -0.0192 -0.0113 211 ASP A N 746 C CA . ASP A 95 ? 0.3489 0.2785 0.2496 0.0487 -0.0076 -0.0070 211 ASP A CA 747 C C . ASP A 95 ? 0.3128 0.2483 0.2193 0.0479 -0.0060 -0.0103 211 ASP A C 748 O O . ASP A 95 ? 0.3592 0.2861 0.2522 0.0537 -0.0091 -0.0134 211 ASP A O 749 C CB . ASP A 95 ? 0.4075 0.3305 0.2855 0.0573 -0.0032 -0.0029 211 ASP A CB 750 C CG . ASP A 95 ? 0.5065 0.4431 0.3876 0.0573 0.0096 0.0035 211 ASP A CG 751 O OD1 . ASP A 95 ? 0.4326 0.3817 0.3334 0.0495 0.0136 0.0056 211 ASP A OD1 752 O OD2 . ASP A 95 ? 0.5857 0.5208 0.4499 0.0654 0.0154 0.0066 211 ASP A OD2 753 N N . PRO A 96 ? 0.3191 0.2674 0.2442 0.0410 -0.0020 -0.0100 212 PRO A N 754 C CA . PRO A 96 ? 0.3027 0.2562 0.2342 0.0395 -0.0012 -0.0128 212 PRO A CA 755 C C . PRO A 96 ? 0.3280 0.2809 0.2466 0.0468 0.0031 -0.0120 212 PRO A C 756 O O . PRO A 96 ? 0.3315 0.2889 0.2436 0.0510 0.0102 -0.0076 212 PRO A O 757 C CB . PRO A 96 ? 0.3055 0.2730 0.2547 0.0325 0.0041 -0.0110 212 PRO A CB 758 C CG . PRO A 96 ? 0.3045 0.2707 0.2599 0.0290 0.0021 -0.0101 212 PRO A CG 759 C CD . PRO A 96 ? 0.2969 0.2533 0.2364 0.0347 0.0010 -0.0074 212 PRO A CD 760 N N . ILE A 97 ? 0.3223 0.2695 0.2374 0.0487 -0.0010 -0.0159 213 ILE A N 761 C CA . ILE A 97 ? 0.3016 0.2478 0.2054 0.0566 0.0027 -0.0159 213 ILE A CA 762 C C . ILE A 97 ? 0.2864 0.2414 0.2025 0.0529 0.0045 -0.0163 213 ILE A C 763 O O . ILE A 97 ? 0.3024 0.2596 0.2311 0.0451 0.0010 -0.0176 213 ILE A O 764 C CB . ILE A 97 ? 0.4081 0.3349 0.2916 0.0645 -0.0051 -0.0205 213 ILE A CB 765 C CG1 . ILE A 97 ? 0.3662 0.2841 0.2559 0.0588 -0.0151 -0.0247 213 ILE A CG1 766 C CG2 . ILE A 97 ? 0.4994 0.4159 0.3680 0.0688 -0.0080 -0.0203 213 ILE A CG2 767 C CD1 . ILE A 97 ? 0.3995 0.2959 0.2697 0.0656 -0.0248 -0.0297 213 ILE A CD1 768 N N . PRO A 98 ? 0.2953 0.2563 0.2075 0.0592 0.0102 -0.0147 214 PRO A N 769 C CA . PRO A 98 ? 0.3097 0.2786 0.2324 0.0564 0.0112 -0.0147 214 PRO A CA 770 C C . PRO A 98 ? 0.2985 0.2532 0.2162 0.0560 0.0030 -0.0188 214 PRO A C 771 O O . PRO A 98 ? 0.3525 0.2916 0.2544 0.0629 -0.0020 -0.0218 214 PRO A O 772 C CB . PRO A 98 ? 0.3843 0.3617 0.3024 0.0654 0.0184 -0.0121 214 PRO A CB 773 C CG . PRO A 98 ? 0.4256 0.4064 0.3374 0.0694 0.0242 -0.0087 214 PRO A CG 774 C CD . PRO A 98 ? 0.3806 0.3443 0.2807 0.0690 0.0172 -0.0119 214 PRO A CD 775 N N . ILE A 99 ? 0.2376 0.1969 0.1680 0.0479 0.0013 -0.0187 215 ILE A N 776 C CA . ILE A 99 ? 0.2255 0.1732 0.1538 0.0458 -0.0056 -0.0207 215 ILE A CA 777 C C . ILE A 99 ? 0.2378 0.1924 0.1704 0.0460 -0.0029 -0.0189 215 ILE A C 778 O O . ILE A 99 ? 0.2773 0.2465 0.2215 0.0414 0.0019 -0.0167 215 ILE A O 779 C CB . ILE A 99 ? 0.3294 0.2770 0.2692 0.0357 -0.0097 -0.0210 215 ILE A CB 780 C CG1 . ILE A 99 ? 0.3431 0.2862 0.2811 0.0354 -0.0129 -0.0224 215 ILE A CG1 781 C CG2 . ILE A 99 ? 0.3443 0.2803 0.2830 0.0325 -0.0166 -0.0215 215 ILE A CG2 782 C CD1 . ILE A 99 ? 0.4100 0.3346 0.3305 0.0423 -0.0201 -0.0255 215 ILE A CD1 783 N N . HIS A 100 ? 0.2901 0.2323 0.2121 0.0518 -0.0069 -0.0201 216 HIS A N 784 C CA . HIS A 100 ? 0.3445 0.2903 0.2687 0.0530 -0.0059 -0.0183 216 HIS A CA 785 C C . HIS A 100 ? 0.3669 0.3049 0.2950 0.0446 -0.0113 -0.0174 216 HIS A C 786 O O . HIS A 100 ? 0.3690 0.2916 0.2922 0.0424 -0.0183 -0.0189 216 HIS A O 787 C CB . HIS A 100 ? 0.3244 0.2596 0.2339 0.0653 -0.0075 -0.0200 216 HIS A CB 788 C CG . HIS A 100 ? 0.3906 0.3343 0.2951 0.0751 -0.0010 -0.0201 216 HIS A CG 789 N ND1 . HIS A 100 ? 0.3707 0.3306 0.2809 0.0807 0.0057 -0.0174 216 HIS A ND1 790 C CD2 . HIS A 100 ? 0.4368 0.3752 0.3311 0.0804 0.0000 -0.0219 216 HIS A CD2 791 C CE1 . HIS A 100 ? 0.4053 0.3713 0.3104 0.0887 0.0117 -0.0169 216 HIS A CE1 792 N NE2 . HIS A 100 ? 0.3962 0.3486 0.2902 0.0889 0.0086 -0.0196 216 HIS A NE2 793 N N . TYR A 101 ? 0.3012 0.2496 0.2378 0.0399 -0.0085 -0.0145 217 TYR A N 794 C CA . TYR A 101 ? 0.2815 0.2237 0.2205 0.0327 -0.0120 -0.0121 217 TYR A CA 795 C C . TYR A 101 ? 0.2902 0.2235 0.2207 0.0377 -0.0149 -0.0104 217 TYR A C 796 O O . TYR A 101 ? 0.2873 0.2295 0.2175 0.0435 -0.0117 -0.0097 217 TYR A O 797 C CB . TYR A 101 ? 0.3169 0.2742 0.2683 0.0241 -0.0072 -0.0100 217 TYR A CB 798 C CG . TYR A 101 ? 0.3031 0.2633 0.2622 0.0186 -0.0069 -0.0115 217 TYR A CG 799 C CD1 . TYR A 101 ? 0.3620 0.3158 0.3255 0.0119 -0.0106 -0.0103 217 TYR A CD1 800 C CD2 . TYR A 101 ? 0.3798 0.3487 0.3424 0.0204 -0.0034 -0.0136 217 TYR A CD2 801 C CE1 . TYR A 101 ? 0.3173 0.2747 0.2893 0.0078 -0.0111 -0.0116 217 TYR A CE1 802 C CE2 . TYR A 101 ? 0.3650 0.3351 0.3338 0.0164 -0.0040 -0.0149 217 TYR A CE2 803 C CZ . TYR A 101 ? 0.3030 0.2678 0.2768 0.0106 -0.0080 -0.0142 217 TYR A CZ 804 O OH . TYR A 101 ? 0.3083 0.2756 0.2900 0.0073 -0.0093 -0.0154 217 TYR A OH 805 N N . CYS A 102 ? 0.2858 0.2009 0.2103 0.0354 -0.0218 -0.0094 218 CYS A N 806 C CA . CYS A 102 ? 0.2910 0.1916 0.2044 0.0417 -0.0266 -0.0084 218 CYS A CA 807 C C . CYS A 102 ? 0.3644 0.2556 0.2787 0.0332 -0.0305 -0.0032 218 CYS A C 808 O O . CYS A 102 ? 0.3376 0.2267 0.2590 0.0232 -0.0321 -0.0011 218 CYS A O 809 C CB . CYS A 102 ? 0.3615 0.2421 0.2612 0.0501 -0.0332 -0.0129 218 CYS A CB 810 S SG . CYS A 102 ? 0.4573 0.3468 0.3531 0.0601 -0.0282 -0.0180 218 CYS A SG 811 N N . THR A 103 ? 0.3736 0.2591 0.2810 0.0376 -0.0321 -0.0004 219 THR A N 812 C CA . THR A 103 ? 0.3598 0.2347 0.2656 0.0303 -0.0356 0.0058 219 THR A CA 813 C C . THR A 103 ? 0.4278 0.2747 0.3229 0.0317 -0.0458 0.0060 219 THR A C 814 O O . THR A 103 ? 0.4536 0.2879 0.3374 0.0428 -0.0503 0.0011 219 THR A O 815 C CB . THR A 103 ? 0.3990 0.2805 0.3016 0.0340 -0.0331 0.0095 219 THR A CB 816 O OG1 . THR A 103 ? 0.3747 0.2579 0.2714 0.0473 -0.0335 0.0055 219 THR A OG1 817 C CG2 . THR A 103 ? 0.3625 0.2670 0.2754 0.0278 -0.0250 0.0111 219 THR A CG2 818 N N . PRO A 104 ? 0.4282 0.2650 0.3267 0.0203 -0.0496 0.0118 220 PRO A N 819 C CA . PRO A 104 ? 0.4924 0.3004 0.3815 0.0195 -0.0608 0.0132 220 PRO A CA 820 C C . PRO A 104 ? 0.4855 0.2801 0.3619 0.0264 -0.0641 0.0166 220 PRO A C 821 O O . PRO A 104 ? 0.5002 0.3096 0.3765 0.0311 -0.0577 0.0182 220 PRO A O 822 C CB . PRO A 104 ? 0.5272 0.3356 0.4287 0.0033 -0.0616 0.0206 220 PRO A CB 823 C CG . PRO A 104 ? 0.4579 0.2916 0.3687 -0.0014 -0.0500 0.0253 220 PRO A CG 824 C CD . PRO A 104 ? 0.3948 0.2473 0.3064 0.0078 -0.0433 0.0180 220 PRO A CD 825 N N . ALA A 105 ? 0.5383 0.3037 0.4039 0.0272 -0.0750 0.0176 221 ALA A N 826 C CA . ALA A 105 ? 0.5832 0.3317 0.4357 0.0342 -0.0798 0.0211 221 ALA A CA 827 C C . ALA A 105 ? 0.5440 0.3043 0.4013 0.0263 -0.0738 0.0309 221 ALA A C 828 O O . ALA A 105 ? 0.5198 0.2890 0.3883 0.0123 -0.0699 0.0373 221 ALA A O 829 C CB . ALA A 105 ? 0.6346 0.3474 0.4762 0.0327 -0.0935 0.0219 221 ALA A CB 830 N N . GLY A 106 ? 0.5274 0.2881 0.3758 0.0361 -0.0732 0.0322 222 GLY A N 831 C CA . GLY A 106 ? 0.5407 0.3089 0.3890 0.0306 -0.0691 0.0413 222 GLY A CA 832 C C . GLY A 106 ? 0.5130 0.3134 0.3710 0.0299 -0.0580 0.0401 222 GLY A C 833 O O . GLY A 106 ? 0.5176 0.3267 0.3741 0.0266 -0.0540 0.0464 222 GLY A O 834 N N . TYR A 107 ? 0.4452 0.2619 0.3118 0.0330 -0.0536 0.0320 223 TYR A N 835 C CA . TYR A 107 ? 0.4063 0.2516 0.2823 0.0327 -0.0443 0.0299 223 TYR A CA 836 C C . TYR A 107 ? 0.4385 0.2947 0.3159 0.0452 -0.0430 0.0218 223 TYR A C 837 O O . TYR A 107 ? 0.4752 0.3187 0.3471 0.0536 -0.0476 0.0171 223 TYR A O 838 C CB . TYR A 107 ? 0.4210 0.2792 0.3099 0.0211 -0.0383 0.0297 223 TYR A CB 839 C CG . TYR A 107 ? 0.4494 0.3033 0.3405 0.0083 -0.0370 0.0386 223 TYR A CG 840 C CD1 . TYR A 107 ? 0.4905 0.3242 0.3813 0.0014 -0.0436 0.0426 223 TYR A CD1 841 C CD2 . TYR A 107 ? 0.4405 0.3104 0.3339 0.0031 -0.0293 0.0432 223 TYR A CD2 842 C CE1 . TYR A 107 ? 0.5168 0.3488 0.4120 -0.0111 -0.0416 0.0522 223 TYR A CE1 843 C CE2 . TYR A 107 ? 0.4875 0.3554 0.3827 -0.0080 -0.0264 0.0523 223 TYR A CE2 844 C CZ . TYR A 107 ? 0.5094 0.3594 0.4068 -0.0154 -0.0321 0.0574 223 TYR A CZ 845 O OH . TYR A 107 ? 0.5394 0.3897 0.4411 -0.0272 -0.0284 0.0678 223 TYR A OH 846 N N . VAL A 108 ? 0.3377 0.2172 0.2221 0.0465 -0.0368 0.0205 224 VAL A N 847 C CA . VAL A 108 ? 0.4149 0.3091 0.3044 0.0563 -0.0342 0.0144 224 VAL A CA 848 C C . VAL A 108 ? 0.3905 0.3094 0.2920 0.0506 -0.0269 0.0132 224 VAL A C 849 O O . VAL A 108 ? 0.3899 0.3138 0.2928 0.0420 -0.0245 0.0167 224 VAL A O 850 C CB . VAL A 108 ? 0.5447 0.4377 0.4282 0.0691 -0.0380 0.0148 224 VAL A CB 851 C CG1 . VAL A 108 ? 0.4853 0.3912 0.3706 0.0668 -0.0372 0.0189 224 VAL A CG1 852 C CG2 . VAL A 108 ? 0.6342 0.5394 0.5231 0.0804 -0.0354 0.0091 224 VAL A CG2 853 N N . ILE A 109 ? 0.2890 0.2223 0.1982 0.0557 -0.0235 0.0083 225 ILE A N 854 C CA . ILE A 109 ? 0.2531 0.2079 0.1737 0.0508 -0.0179 0.0069 225 ILE A CA 855 C C . ILE A 109 ? 0.3484 0.3179 0.2732 0.0579 -0.0184 0.0070 225 ILE A C 856 O O . ILE A 109 ? 0.3831 0.3555 0.3092 0.0680 -0.0191 0.0055 225 ILE A O 857 C CB . ILE A 109 ? 0.3000 0.2616 0.2281 0.0498 -0.0137 0.0026 225 ILE A CB 858 C CG1 . ILE A 109 ? 0.3489 0.2969 0.2745 0.0428 -0.0145 0.0023 225 ILE A CG1 859 C CG2 . ILE A 109 ? 0.3099 0.2919 0.2496 0.0451 -0.0088 0.0013 225 ILE A CG2 860 C CD1 . ILE A 109 ? 0.3482 0.2993 0.2784 0.0429 -0.0120 -0.0018 225 ILE A CD1 861 N N . LEU A 110 ? 0.3366 0.3154 0.2633 0.0531 -0.0185 0.0089 226 LEU A N 862 C CA . LEU A 110 ? 0.3091 0.3043 0.2428 0.0578 -0.0201 0.0087 226 LEU A CA 863 C C . LEU A 110 ? 0.2632 0.2765 0.2108 0.0539 -0.0156 0.0055 226 LEU A C 864 O O . LEU A 110 ? 0.2803 0.2939 0.2295 0.0456 -0.0122 0.0039 226 LEU A O 865 C CB . LEU A 110 ? 0.3413 0.3361 0.2682 0.0549 -0.0240 0.0118 226 LEU A CB 866 C CG . LEU A 110 ? 0.3948 0.3712 0.3071 0.0583 -0.0289 0.0165 226 LEU A CG 867 C CD1 . LEU A 110 ? 0.3920 0.3705 0.2971 0.0578 -0.0333 0.0198 226 LEU A CD1 868 C CD2 . LEU A 110 ? 0.4894 0.4598 0.4011 0.0702 -0.0323 0.0163 226 LEU A CD2 869 N N . LYS A 111 ? 0.2555 0.2837 0.2139 0.0601 -0.0156 0.0050 227 LYS A N 870 C CA . LYS A 111 ? 0.2258 0.2707 0.1985 0.0565 -0.0115 0.0032 227 LYS A CA 871 C C . LYS A 111 ? 0.2621 0.3248 0.2463 0.0562 -0.0153 0.0042 227 LYS A C 872 O O . LYS A 111 ? 0.2724 0.3414 0.2597 0.0641 -0.0189 0.0063 227 LYS A O 873 C CB . LYS A 111 ? 0.3219 0.3704 0.2993 0.0636 -0.0069 0.0026 227 LYS A CB 874 C CG . LYS A 111 ? 0.2513 0.3168 0.2434 0.0599 -0.0021 0.0024 227 LYS A CG 875 C CD . LYS A 111 ? 0.3024 0.3728 0.2972 0.0687 0.0034 0.0029 227 LYS A CD 876 C CE . LYS A 111 ? 0.3855 0.4722 0.3947 0.0638 0.0087 0.0042 227 LYS A CE 877 N NZ . LYS A 111 ? 0.3714 0.4639 0.3818 0.0726 0.0155 0.0056 227 LYS A NZ 878 N N . CYS A 112 ? 0.2814 0.3514 0.2718 0.0474 -0.0153 0.0026 228 CYS A N 879 C CA . CYS A 112 ? 0.3036 0.3894 0.3057 0.0457 -0.0205 0.0031 228 CYS A CA 880 C C . CYS A 112 ? 0.2425 0.3467 0.2640 0.0469 -0.0172 0.0046 228 CYS A C 881 O O . CYS A 112 ? 0.2744 0.3798 0.3007 0.0421 -0.0118 0.0037 228 CYS A O 882 C CB . CYS A 112 ? 0.3848 0.4681 0.3836 0.0362 -0.0232 0.0002 228 CYS A CB 883 S SG . CYS A 112 ? 0.3896 0.4902 0.4031 0.0327 -0.0318 0.0000 228 CYS A SG 884 N N . ASN A 113 ? 0.2703 0.3895 0.3035 0.0533 -0.0203 0.0076 229 ASN A N 885 C CA . ASN A 113 ? 0.2653 0.4052 0.3191 0.0547 -0.0164 0.0105 229 ASN A CA 886 C C . ASN A 113 ? 0.3045 0.4625 0.3770 0.0477 -0.0228 0.0120 229 ASN A C 887 O O . ASN A 113 ? 0.3106 0.4890 0.4038 0.0479 -0.0203 0.0160 229 ASN A O 888 C CB . ASN A 113 ? 0.2916 0.4387 0.3484 0.0683 -0.0134 0.0134 229 ASN A CB 889 C CG . ASN A 113 ? 0.2606 0.3875 0.2983 0.0750 -0.0085 0.0114 229 ASN A CG 890 O OD1 . ASN A 113 ? 0.3252 0.4469 0.3595 0.0731 -0.0018 0.0103 229 ASN A OD1 891 N ND2 . ASN A 113 ? 0.3268 0.4408 0.3513 0.0826 -0.0130 0.0110 229 ASN A ND2 892 N N . ASP A 114 ? 0.2641 0.4144 0.3292 0.0414 -0.0311 0.0091 230 ASP A N 893 C CA . ASP A 114 ? 0.3043 0.4672 0.3845 0.0332 -0.0391 0.0091 230 ASP A CA 894 C C . ASP A 114 ? 0.2851 0.4511 0.3754 0.0239 -0.0343 0.0089 230 ASP A C 895 O O . ASP A 114 ? 0.2880 0.4382 0.3652 0.0193 -0.0310 0.0051 230 ASP A O 896 C CB . ASP A 114 ? 0.3267 0.4762 0.3909 0.0294 -0.0488 0.0048 230 ASP A CB 897 C CG . ASP A 114 ? 0.4325 0.5821 0.4901 0.0375 -0.0562 0.0063 230 ASP A CG 898 O OD1 . ASP A 114 ? 0.3603 0.5167 0.4229 0.0471 -0.0532 0.0099 230 ASP A OD1 899 O OD2 . ASP A 114 ? 0.4545 0.5960 0.5002 0.0352 -0.0653 0.0038 230 ASP A OD2 900 N N . LYS A 115 ? 0.2913 0.4783 0.4060 0.0211 -0.0339 0.0136 231 LYS A N 901 C CA . LYS A 115 ? 0.4095 0.5997 0.5344 0.0132 -0.0280 0.0153 231 LYS A CA 902 C C . LYS A 115 ? 0.4219 0.5986 0.5410 0.0020 -0.0339 0.0104 231 LYS A C 903 O O . LYS A 115 ? 0.5224 0.6902 0.6375 -0.0024 -0.0281 0.0094 231 LYS A O 904 C CB . LYS A 115 ? 0.4816 0.6986 0.6353 0.0120 -0.0261 0.0230 231 LYS A CB 905 C CG . LYS A 115 ? 0.5251 0.7538 0.6827 0.0238 -0.0150 0.0280 231 LYS A CG 906 C CD . LYS A 115 ? 0.5609 0.8187 0.7482 0.0225 -0.0109 0.0367 231 LYS A CD 907 C CE . LYS A 115 ? 0.5962 0.8654 0.7846 0.0367 0.0007 0.0409 231 LYS A CE 908 N NZ . LYS A 115 ? 0.6056 0.8550 0.7707 0.0416 0.0104 0.0379 231 LYS A NZ 909 N N . ASN A 116 ? 0.3316 0.5056 0.4486 -0.0018 -0.0458 0.0069 232 ASN A N 910 C CA . ASN A 116 ? 0.3320 0.4923 0.4421 -0.0112 -0.0523 0.0013 232 ASN A CA 911 C C . ASN A 116 ? 0.3491 0.4878 0.4312 -0.0084 -0.0541 -0.0058 232 ASN A C 912 O O . ASN A 116 ? 0.3223 0.4498 0.3954 -0.0136 -0.0618 -0.0114 232 ASN A O 913 C CB . ASN A 116 ? 0.4062 0.5775 0.5340 -0.0188 -0.0655 0.0021 232 ASN A CB 914 C CG . ASN A 116 ? 0.4106 0.6024 0.5681 -0.0248 -0.0630 0.0099 232 ASN A CG 915 O OD1 . ASN A 116 ? 0.2836 0.4730 0.4441 -0.0282 -0.0542 0.0122 232 ASN A OD1 916 N ND2 . ASN A 116 ? 0.3877 0.6004 0.5676 -0.0262 -0.0706 0.0147 232 ASN A ND2 917 N N . PHE A 117 ? 0.3119 0.4444 0.3801 -0.0002 -0.0469 -0.0054 233 PHE A N 918 C CA . PHE A 117 ? 0.3416 0.4557 0.3848 0.0023 -0.0466 -0.0102 233 PHE A CA 919 C C . PHE A 117 ? 0.2608 0.3614 0.2951 -0.0030 -0.0430 -0.0150 233 PHE A C 920 O O . PHE A 117 ? 0.2716 0.3721 0.3117 -0.0044 -0.0352 -0.0137 233 PHE A O 921 C CB . PHE A 117 ? 0.2969 0.4070 0.3304 0.0107 -0.0391 -0.0075 233 PHE A CB 922 C CG . PHE A 117 ? 0.3358 0.4285 0.3458 0.0124 -0.0374 -0.0105 233 PHE A CG 923 C CD1 . PHE A 117 ? 0.4586 0.5452 0.4551 0.0128 -0.0450 -0.0127 233 PHE A CD1 924 C CD2 . PHE A 117 ? 0.3564 0.4394 0.3583 0.0137 -0.0284 -0.0105 233 PHE A CD2 925 C CE1 . PHE A 117 ? 0.4892 0.5613 0.4643 0.0144 -0.0420 -0.0141 233 PHE A CE1 926 C CE2 . PHE A 117 ? 0.3323 0.4018 0.3156 0.0145 -0.0263 -0.0119 233 PHE A CE2 927 C CZ . PHE A 117 ? 0.4018 0.4663 0.3718 0.0149 -0.0323 -0.0133 233 PHE A CZ 928 N N . ASN A 118 ? 0.2702 0.3591 0.2893 -0.0049 -0.0485 -0.0207 234 ASN A N 929 C CA . ASN A 118 ? 0.2932 0.3698 0.3045 -0.0088 -0.0458 -0.0260 234 ASN A CA 930 C C . ASN A 118 ? 0.2959 0.3618 0.2915 -0.0049 -0.0362 -0.0272 234 ASN A C 931 O O . ASN A 118 ? 0.3059 0.3633 0.2966 -0.0068 -0.0326 -0.0310 234 ASN A O 932 C CB . ASN A 118 ? 0.3273 0.3958 0.3304 -0.0123 -0.0565 -0.0324 234 ASN A CB 933 C CG . ASN A 118 ? 0.4395 0.4992 0.4197 -0.0073 -0.0598 -0.0355 234 ASN A CG 934 O OD1 . ASN A 118 ? 0.4228 0.4798 0.3917 -0.0021 -0.0526 -0.0330 234 ASN A OD1 935 N ND2 . ASN A 118 ? 0.4768 0.5308 0.4492 -0.0091 -0.0713 -0.0406 234 ASN A ND2 936 N N . GLY A 119 ? 0.2750 0.3413 0.2637 0.0004 -0.0326 -0.0236 235 GLY A N 937 C CA . GLY A 119 ? 0.3209 0.3786 0.2983 0.0029 -0.0239 -0.0233 235 GLY A CA 938 C C . GLY A 119 ? 0.3100 0.3594 0.2677 0.0058 -0.0242 -0.0239 235 GLY A C 939 O O . GLY A 119 ? 0.3095 0.3536 0.2595 0.0077 -0.0176 -0.0214 235 GLY A O 940 N N . THR A 120 ? 0.3041 0.3519 0.2532 0.0059 -0.0323 -0.0267 236 THR A N 941 C CA . THR A 120 ? 0.3744 0.4141 0.3022 0.0093 -0.0328 -0.0266 236 THR A CA 942 C C . THR A 120 ? 0.4029 0.4450 0.3262 0.0116 -0.0436 -0.0256 236 THR A C 943 O O . THR A 120 ? 0.5219 0.5675 0.4510 0.0093 -0.0530 -0.0291 236 THR A O 944 C CB . THR A 120 ? 0.4466 0.4775 0.3596 0.0087 -0.0310 -0.0328 236 THR A CB 945 O OG1 . THR A 120 ? 0.5005 0.5309 0.4209 0.0067 -0.0225 -0.0342 236 THR A OG1 946 C CG2 . THR A 120 ? 0.5272 0.5507 0.4175 0.0126 -0.0277 -0.0309 236 THR A CG2 947 N N . GLY A 121 ? 0.3684 0.4078 0.2817 0.0160 -0.0431 -0.0204 237 GLY A N 948 C CA . GLY A 121 ? 0.3458 0.3867 0.2535 0.0193 -0.0537 -0.0189 237 GLY A CA 949 C C . GLY A 121 ? 0.3109 0.3585 0.2296 0.0233 -0.0547 -0.0126 237 GLY A C 950 O O . GLY A 121 ? 0.3110 0.3588 0.2368 0.0240 -0.0465 -0.0095 237 GLY A O 951 N N . PRO A 122 ? 0.3620 0.4144 0.2816 0.0268 -0.0653 -0.0111 238 PRO A N 952 C CA . PRO A 122 ? 0.3070 0.3657 0.2357 0.0327 -0.0675 -0.0054 238 PRO A CA 953 C C . PRO A 122 ? 0.2773 0.3519 0.2331 0.0324 -0.0657 -0.0046 238 PRO A C 954 O O . PRO A 122 ? 0.3333 0.4176 0.3040 0.0271 -0.0681 -0.0076 238 PRO A O 955 C CB . PRO A 122 ? 0.3012 0.3616 0.2234 0.0362 -0.0810 -0.0050 238 PRO A CB 956 C CG . PRO A 122 ? 0.3501 0.4108 0.2702 0.0304 -0.0876 -0.0115 238 PRO A CG 957 C CD . PRO A 122 ? 0.3716 0.4221 0.2810 0.0261 -0.0769 -0.0151 238 PRO A CD 958 N N . CYS A 123 ? 0.3236 0.3997 0.2846 0.0383 -0.0612 -0.0001 239 CYS A N 959 C CA . CYS A 123 ? 0.2816 0.3730 0.2656 0.0404 -0.0582 0.0015 239 CYS A CA 960 C C . CYS A 123 ? 0.2896 0.3869 0.2776 0.0501 -0.0636 0.0058 239 CYS A C 961 O O . CYS A 123 ? 0.3090 0.3929 0.2808 0.0557 -0.0638 0.0083 239 CYS A O 962 C CB . CYS A 123 ? 0.3943 0.4793 0.3780 0.0401 -0.0466 0.0017 239 CYS A CB 963 S SG . CYS A 123 ? 0.4880 0.5902 0.4959 0.0431 -0.0408 0.0036 239 CYS A SG 964 N N . LYS A 124 ? 0.3162 0.4338 0.3266 0.0520 -0.0681 0.0072 240 LYS A N 965 C CA . LYS A 124 ? 0.3665 0.4929 0.3833 0.0620 -0.0745 0.0110 240 LYS A CA 966 C C . LYS A 124 ? 0.3787 0.5114 0.4054 0.0713 -0.0667 0.0140 240 LYS A C 967 O O . LYS A 124 ? 0.3953 0.5275 0.4199 0.0820 -0.0699 0.0168 240 LYS A O 968 C CB . LYS A 124 ? 0.4521 0.5991 0.4892 0.0598 -0.0853 0.0114 240 LYS A CB 969 C CG . LYS A 124 ? 0.6054 0.7454 0.6322 0.0510 -0.0945 0.0073 240 LYS A CG 970 C CD . LYS A 124 ? 0.7095 0.8303 0.7078 0.0549 -0.1007 0.0071 240 LYS A CD 971 C CE . LYS A 124 ? 0.7604 0.8889 0.7630 0.0642 -0.1115 0.0109 240 LYS A CE 972 N NZ . LYS A 124 ? 0.7748 0.8841 0.7483 0.0672 -0.1190 0.0112 240 LYS A NZ 973 N N . ASN A 125 ? 0.2687 0.4060 0.3046 0.0680 -0.0567 0.0132 241 ASN A N 974 C CA . ASN A 125 ? 0.2487 0.3913 0.2917 0.0770 -0.0484 0.0152 241 ASN A CA 975 C C . ASN A 125 ? 0.2576 0.3788 0.2825 0.0761 -0.0400 0.0131 241 ASN A C 976 O O . ASN A 125 ? 0.2759 0.3975 0.3042 0.0698 -0.0330 0.0114 241 ASN A O 977 C CB . ASN A 125 ? 0.3590 0.5262 0.4282 0.0746 -0.0436 0.0170 241 ASN A CB 978 C CG . ASN A 125 ? 0.5306 0.7080 0.6085 0.0867 -0.0357 0.0198 241 ASN A CG 979 O OD1 . ASN A 125 ? 0.5415 0.7044 0.6042 0.0968 -0.0339 0.0192 241 ASN A OD1 980 N ND2 . ASN A 125 ? 0.7243 0.9263 0.8263 0.0859 -0.0310 0.0231 241 ASN A ND2 981 N N . VAL A 126 ? 0.2828 0.3848 0.2890 0.0823 -0.0417 0.0136 242 VAL A N 982 C CA . VAL A 126 ? 0.3186 0.3987 0.3075 0.0799 -0.0362 0.0120 242 VAL A CA 983 C C . VAL A 126 ? 0.3223 0.3944 0.3068 0.0913 -0.0327 0.0125 242 VAL A C 984 O O . VAL A 126 ? 0.3329 0.4067 0.3177 0.1022 -0.0369 0.0144 242 VAL A O 985 C CB . VAL A 126 ? 0.3686 0.4290 0.3371 0.0764 -0.0411 0.0129 242 VAL A CB 986 C CG1 . VAL A 126 ? 0.3255 0.3659 0.2801 0.0723 -0.0356 0.0121 242 VAL A CG1 987 C CG2 . VAL A 126 ? 0.3873 0.4536 0.3560 0.0676 -0.0456 0.0117 242 VAL A CG2 988 N N . SER A 127 ? 0.3229 0.3855 0.3024 0.0894 -0.0259 0.0104 243 SER A N 989 C CA . SER A 127 ? 0.3932 0.4428 0.3636 0.1000 -0.0238 0.0098 243 SER A CA 990 C C . SER A 127 ? 0.3929 0.4171 0.3461 0.0944 -0.0234 0.0084 243 SER A C 991 O O . SER A 127 ? 0.3946 0.4158 0.3461 0.0826 -0.0222 0.0080 243 SER A O 992 C CB . SER A 127 ? 0.3234 0.3877 0.3054 0.1059 -0.0162 0.0087 243 SER A CB 993 O OG . SER A 127 ? 0.3316 0.3982 0.3170 0.0958 -0.0105 0.0071 243 SER A OG 994 N N . SER A 128 ? 0.3484 0.3541 0.2892 0.1029 -0.0249 0.0078 244 SER A N 995 C CA . SER A 128 ? 0.3905 0.3722 0.3172 0.0972 -0.0256 0.0069 244 SER A CA 996 C C . SER A 128 ? 0.3860 0.3610 0.3094 0.1026 -0.0218 0.0031 244 SER A C 997 O O . SER A 128 ? 0.3846 0.3627 0.3079 0.1156 -0.0207 0.0017 244 SER A O 998 C CB . SER A 128 ? 0.4658 0.4250 0.3773 0.1000 -0.0329 0.0098 244 SER A CB 999 O OG . SER A 128 ? 0.4966 0.4467 0.4019 0.1148 -0.0361 0.0088 244 SER A OG 1000 N N . VAL A 129 ? 0.3698 0.3360 0.2902 0.0931 -0.0198 0.0015 245 VAL A N 1001 C CA . VAL A 129 ? 0.3928 0.3514 0.3086 0.0967 -0.0172 -0.0023 245 VAL A CA 1002 C C . VAL A 129 ? 0.3974 0.3332 0.3032 0.0883 -0.0211 -0.0029 245 VAL A C 1003 O O . VAL A 129 ? 0.3735 0.3064 0.2804 0.0778 -0.0229 0.0002 245 VAL A O 1004 C CB . VAL A 129 ? 0.3451 0.3241 0.2735 0.0926 -0.0096 -0.0035 245 VAL A CB 1005 C CG1 . VAL A 129 ? 0.3809 0.3839 0.3220 0.0998 -0.0057 -0.0019 245 VAL A CG1 1006 C CG2 . VAL A 129 ? 0.2541 0.2387 0.1897 0.0776 -0.0085 -0.0024 245 VAL A CG2 1007 N N . GLN A 130 ? 0.3958 0.3161 0.2920 0.0931 -0.0228 -0.0066 246 GLN A N 1008 C CA . GLN A 130 ? 0.4113 0.3116 0.3010 0.0841 -0.0276 -0.0072 246 GLN A CA 1009 C C . GLN A 130 ? 0.4012 0.3122 0.3003 0.0740 -0.0230 -0.0082 246 GLN A C 1010 O O . GLN A 130 ? 0.3703 0.2744 0.2715 0.0629 -0.0253 -0.0068 246 GLN A O 1011 C CB . GLN A 130 ? 0.5161 0.3910 0.3897 0.0932 -0.0340 -0.0112 246 GLN A CB 1012 C CG . GLN A 130 ? 0.6341 0.4880 0.5031 0.0826 -0.0409 -0.0112 246 GLN A CG 1013 C CD . GLN A 130 ? 0.8300 0.6559 0.6818 0.0910 -0.0494 -0.0161 246 GLN A CD 1014 O OE1 . GLN A 130 ? 0.9056 0.7301 0.7481 0.1050 -0.0478 -0.0210 246 GLN A OE1 1015 N NE2 . GLN A 130 ? 0.8693 0.6725 0.7165 0.0827 -0.0585 -0.0146 246 GLN A NE2 1016 N N . CYS A 131 ? 0.3063 0.2347 0.2118 0.0778 -0.0164 -0.0101 247 CYS A N 1017 C CA . CYS A 131 ? 0.3023 0.2393 0.2152 0.0701 -0.0125 -0.0114 247 CYS A CA 1018 C C . CYS A 131 ? 0.3243 0.2865 0.2510 0.0682 -0.0052 -0.0099 247 CYS A C 1019 O O . CYS A 131 ? 0.3471 0.3215 0.2773 0.0756 -0.0024 -0.0087 247 CYS A O 1020 C CB . CYS A 131 ? 0.3593 0.2855 0.2620 0.0770 -0.0134 -0.0156 247 CYS A CB 1021 S SG . CYS A 131 ? 0.5652 0.4588 0.4519 0.0774 -0.0244 -0.0185 247 CYS A SG 1022 N N . THR A 132 ? 0.3097 0.2794 0.2449 0.0583 -0.0027 -0.0098 248 THR A N 1023 C CA . THR A 132 ? 0.2999 0.2901 0.2474 0.0556 0.0031 -0.0089 248 THR A CA 1024 C C . THR A 132 ? 0.3359 0.3306 0.2819 0.0628 0.0074 -0.0098 248 THR A C 1025 O O . THR A 132 ? 0.3415 0.3224 0.2753 0.0697 0.0056 -0.0120 248 THR A O 1026 C CB . THR A 132 ? 0.2569 0.2508 0.2120 0.0443 0.0042 -0.0092 248 THR A CB 1027 O OG1 . THR A 132 ? 0.2744 0.2587 0.2257 0.0430 0.0033 -0.0113 248 THR A OG1 1028 C CG2 . THR A 132 ? 0.2672 0.2567 0.2223 0.0375 0.0014 -0.0078 248 THR A CG2 1029 N N . HIS A 133 ? 0.3265 0.3395 0.2840 0.0610 0.0127 -0.0078 249 HIS A N 1030 C CA . HIS A 133 ? 0.3229 0.3413 0.2799 0.0654 0.0179 -0.0072 249 HIS A CA 1031 C C . HIS A 133 ? 0.3025 0.3089 0.2538 0.0604 0.0163 -0.0095 249 HIS A C 1032 O O . HIS A 133 ? 0.2705 0.2688 0.2225 0.0528 0.0119 -0.0111 249 HIS A O 1033 C CB . HIS A 133 ? 0.3081 0.3486 0.2811 0.0621 0.0233 -0.0033 249 HIS A CB 1034 C CG . HIS A 133 ? 0.3368 0.3814 0.3197 0.0500 0.0223 -0.0033 249 HIS A CG 1035 N ND1 . HIS A 133 ? 0.3067 0.3539 0.2954 0.0436 0.0186 -0.0039 249 HIS A ND1 1036 C CD2 . HIS A 133 ? 0.2939 0.3395 0.2805 0.0441 0.0243 -0.0029 249 HIS A CD2 1037 C CE1 . HIS A 133 ? 0.3576 0.4070 0.3527 0.0349 0.0185 -0.0045 249 HIS A CE1 1038 N NE2 . HIS A 133 ? 0.3570 0.4053 0.3517 0.0349 0.0218 -0.0039 249 HIS A NE2 1039 N N . GLY A 134 ? 0.2698 0.2753 0.2153 0.0651 0.0198 -0.0094 250 GLY A N 1040 C CA . GLY A 134 ? 0.3132 0.3079 0.2533 0.0612 0.0175 -0.0113 250 GLY A CA 1041 C C . GLY A 134 ? 0.2712 0.2760 0.2248 0.0509 0.0193 -0.0096 250 GLY A C 1042 O O . GLY A 134 ? 0.2902 0.3077 0.2510 0.0503 0.0247 -0.0061 250 GLY A O 1043 N N . ILE A 135 ? 0.2193 0.2181 0.1766 0.0430 0.0148 -0.0117 251 ILE A N 1044 C CA . ILE A 135 ? 0.2292 0.2355 0.1980 0.0345 0.0159 -0.0111 251 ILE A CA 1045 C C . ILE A 135 ? 0.2450 0.2428 0.2105 0.0328 0.0138 -0.0125 251 ILE A C 1046 O O . ILE A 135 ? 0.2521 0.2386 0.2129 0.0322 0.0086 -0.0150 251 ILE A O 1047 C CB . ILE A 135 ? 0.2411 0.2488 0.2167 0.0278 0.0135 -0.0124 251 ILE A CB 1048 C CG1 . ILE A 135 ? 0.2900 0.3047 0.2672 0.0299 0.0142 -0.0110 251 ILE A CG1 1049 C CG2 . ILE A 135 ? 0.2696 0.2838 0.2551 0.0208 0.0146 -0.0128 251 ILE A CG2 1050 C CD1 . ILE A 135 ? 0.3299 0.3429 0.3086 0.0251 0.0116 -0.0117 251 ILE A CD1 1051 N N . LYS A 136 ? 0.2841 0.2871 0.2529 0.0316 0.0171 -0.0103 252 LYS A N 1052 C CA . LYS A 136 ? 0.2437 0.2389 0.2099 0.0301 0.0145 -0.0112 252 LYS A CA 1053 C C . LYS A 136 ? 0.2172 0.2139 0.1945 0.0225 0.0120 -0.0132 252 LYS A C 1054 O O . LYS A 136 ? 0.2487 0.2543 0.2354 0.0182 0.0143 -0.0126 252 LYS A O 1055 C CB . LYS A 136 ? 0.2609 0.2597 0.2256 0.0316 0.0190 -0.0071 252 LYS A CB 1056 C CG . LYS A 136 ? 0.2880 0.2857 0.2399 0.0407 0.0228 -0.0047 252 LYS A CG 1057 C CD . LYS A 136 ? 0.3633 0.3652 0.3137 0.0415 0.0282 0.0009 252 LYS A CD 1058 C CE . LYS A 136 ? 0.5891 0.5939 0.5280 0.0512 0.0345 0.0042 252 LYS A CE 1059 N NZ . LYS A 136 ? 0.7210 0.7424 0.6708 0.0521 0.0401 0.0071 252 LYS A NZ 1060 N N . PRO A 137 ? 0.2061 0.1945 0.1824 0.0214 0.0068 -0.0158 253 PRO A N 1061 C CA . PRO A 137 ? 0.2073 0.1990 0.1948 0.0156 0.0054 -0.0177 253 PRO A CA 1062 C C . PRO A 137 ? 0.2496 0.2421 0.2418 0.0141 0.0057 -0.0174 253 PRO A C 1063 O O . PRO A 137 ? 0.2521 0.2401 0.2466 0.0137 0.0018 -0.0189 253 PRO A O 1064 C CB . PRO A 137 ? 0.2720 0.2558 0.2583 0.0154 -0.0005 -0.0196 253 PRO A CB 1065 C CG . PRO A 137 ? 0.2854 0.2585 0.2586 0.0211 -0.0039 -0.0195 253 PRO A CG 1066 C CD . PRO A 137 ? 0.2040 0.1800 0.1693 0.0258 0.0015 -0.0173 253 PRO A CD 1067 N N . VAL A 138 ? 0.2187 0.2166 0.2132 0.0129 0.0097 -0.0153 254 VAL A N 1068 C CA . VAL A 138 ? 0.2185 0.2149 0.2165 0.0113 0.0096 -0.0143 254 VAL A CA 1069 C C . VAL A 138 ? 0.2230 0.2220 0.2306 0.0076 0.0086 -0.0178 254 VAL A C 1070 O O . VAL A 138 ? 0.2588 0.2637 0.2706 0.0050 0.0105 -0.0190 254 VAL A O 1071 C CB . VAL A 138 ? 0.2268 0.2277 0.2249 0.0103 0.0137 -0.0098 254 VAL A CB 1072 C CG1 . VAL A 138 ? 0.2806 0.2763 0.2800 0.0086 0.0127 -0.0076 254 VAL A CG1 1073 C CG2 . VAL A 138 ? 0.2377 0.2394 0.2264 0.0154 0.0167 -0.0063 254 VAL A CG2 1074 N N . VAL A 139 ? 0.2040 0.2121 0.2274 0.0239 0.0070 0.0035 255 VAL A N 1075 C CA . VAL A 139 ? 0.1967 0.2059 0.2247 0.0188 0.0077 0.0027 255 VAL A CA 1076 C C . VAL A 139 ? 0.1968 0.2053 0.2264 0.0178 0.0130 0.0039 255 VAL A C 1077 O O . VAL A 139 ? 0.2206 0.2249 0.2461 0.0215 0.0149 0.0054 255 VAL A O 1078 C CB . VAL A 139 ? 0.2654 0.2718 0.2921 0.0199 0.0040 0.0017 255 VAL A CB 1079 C CG1 . VAL A 139 ? 0.2332 0.2427 0.2646 0.0160 0.0057 0.0006 255 VAL A CG1 1080 C CG2 . VAL A 139 ? 0.2900 0.2957 0.3157 0.0196 -0.0022 0.0013 255 VAL A CG2 1081 N N . SER A 140 ? 0.1803 0.1916 0.2151 0.0129 0.0144 0.0033 256 SER A N 1082 C CA . SER A 140 ? 0.2197 0.2284 0.2563 0.0111 0.0177 0.0043 256 SER A CA 1083 C C . SER A 140 ? 0.2194 0.2290 0.2598 0.0067 0.0167 0.0019 256 SER A C 1084 O O . SER A 140 ? 0.2157 0.2291 0.2572 0.0047 0.0146 0.0001 256 SER A O 1085 C CB . SER A 140 ? 0.2629 0.2739 0.3021 0.0106 0.0212 0.0077 256 SER A CB 1086 O OG . SER A 140 ? 0.2775 0.2945 0.3227 0.0072 0.0202 0.0070 256 SER A OG 1087 N N . THR A 141 ? 0.1846 0.1894 0.2255 0.0055 0.0178 0.0018 257 THR A N 1088 C CA . THR A 141 ? 0.2274 0.2311 0.2706 0.0021 0.0162 -0.0009 257 THR A CA 1089 C C . THR A 141 ? 0.2592 0.2601 0.3071 -0.0016 0.0168 0.0014 257 THR A C 1090 O O . THR A 141 ? 0.2628 0.2622 0.3115 -0.0015 0.0194 0.0056 257 THR A O 1091 C CB . THR A 141 ? 0.2579 0.2573 0.2977 0.0044 0.0152 -0.0041 257 THR A CB 1092 O OG1 . THR A 141 ? 0.2422 0.2337 0.2801 0.0060 0.0158 -0.0025 257 THR A OG1 1093 C CG2 . THR A 141 ? 0.2431 0.2474 0.2810 0.0074 0.0149 -0.0055 257 THR A CG2 1094 N N . GLN A 142 ? 0.1992 0.1995 0.2500 -0.0050 0.0140 -0.0010 258 GLN A N 1095 C CA . GLN A 142 ? 0.2487 0.2457 0.3056 -0.0096 0.0127 0.0008 258 GLN A CA 1096 C C . GLN A 142 ? 0.2483 0.2535 0.3133 -0.0124 0.0147 0.0048 258 GLN A C 1097 O O . GLN A 142 ? 0.2418 0.2501 0.3133 -0.0160 0.0119 0.0040 258 GLN A O 1098 C CB . GLN A 142 ? 0.2344 0.2217 0.2896 -0.0098 0.0130 0.0029 258 GLN A CB 1099 C CG . GLN A 142 ? 0.2978 0.2767 0.3457 -0.0063 0.0101 -0.0019 258 GLN A CG 1100 C CD . GLN A 142 ? 0.2831 0.2494 0.3298 -0.0076 0.0076 -0.0007 258 GLN A CD 1101 O OE1 . GLN A 142 ? 0.2832 0.2472 0.3351 -0.0123 0.0084 0.0047 258 GLN A OE1 1102 N NE2 . GLN A 142 ? 0.2988 0.2572 0.3386 -0.0032 0.0045 -0.0055 258 GLN A NE2 1103 N N . LEU A 143 ? 0.2323 0.2411 0.2967 -0.0099 0.0192 0.0089 259 LEU A N 1104 C CA . LEU A 143 ? 0.2034 0.2218 0.2750 -0.0108 0.0221 0.0128 259 LEU A CA 1105 C C . LEU A 143 ? 0.2399 0.2644 0.3071 -0.0055 0.0230 0.0117 259 LEU A C 1106 O O . LEU A 143 ? 0.2805 0.3013 0.3394 -0.0009 0.0238 0.0112 259 LEU A O 1107 C CB . LEU A 143 ? 0.2436 0.2613 0.3170 -0.0118 0.0270 0.0192 259 LEU A CB 1108 C CG . LEU A 143 ? 0.2846 0.2939 0.3619 -0.0177 0.0253 0.0214 259 LEU A CG 1109 C CD1 . LEU A 143 ? 0.2878 0.2954 0.3646 -0.0185 0.0306 0.0289 259 LEU A CD1 1110 C CD2 . LEU A 143 ? 0.2889 0.3027 0.3785 -0.0241 0.0217 0.0211 259 LEU A CD2 1111 N N . LEU A 144 ? 0.1984 0.2312 0.2713 -0.0058 0.0218 0.0110 260 LEU A N 1112 C CA . LEU A 144 ? 0.2068 0.2441 0.2754 -0.0003 0.0216 0.0100 260 LEU A CA 1113 C C . LEU A 144 ? 0.2266 0.2706 0.2966 0.0035 0.0270 0.0143 260 LEU A C 1114 O O . LEU A 144 ? 0.2233 0.2752 0.3030 0.0009 0.0301 0.0176 260 LEU A O 1115 C CB . LEU A 144 ? 0.1785 0.2204 0.2510 -0.0013 0.0170 0.0069 260 LEU A CB 1116 C CG . LEU A 144 ? 0.1567 0.1925 0.2257 -0.0044 0.0121 0.0030 260 LEU A CG 1117 C CD1 . LEU A 144 ? 0.1847 0.2240 0.2561 -0.0050 0.0073 0.0005 260 LEU A CD1 1118 C CD2 . LEU A 144 ? 0.2595 0.2894 0.3186 -0.0019 0.0115 0.0017 260 LEU A CD2 1119 N N . LEU A 145 ? 0.2130 0.2542 0.2733 0.0100 0.0281 0.0143 261 LEU A N 1120 C CA . LEU A 145 ? 0.2442 0.2901 0.3022 0.0151 0.0338 0.0183 261 LEU A CA 1121 C C . LEU A 145 ? 0.2422 0.2929 0.2957 0.0230 0.0323 0.0162 261 LEU A C 1122 O O . LEU A 145 ? 0.2324 0.2774 0.2794 0.0256 0.0264 0.0121 261 LEU A O 1123 C CB . LEU A 145 ? 0.2056 0.2420 0.2535 0.0178 0.0358 0.0202 261 LEU A CB 1124 C CG . LEU A 145 ? 0.2551 0.2841 0.3050 0.0116 0.0361 0.0217 261 LEU A CG 1125 C CD1 . LEU A 145 ? 0.2569 0.2756 0.2956 0.0157 0.0367 0.0225 261 LEU A CD1 1126 C CD2 . LEU A 145 ? 0.2138 0.2483 0.2739 0.0058 0.0405 0.0269 261 LEU A CD2 1127 N N . ASN A 146 ? 0.2091 0.2705 0.2662 0.0267 0.0376 0.0193 262 ASN A N 1128 C CA . ASN A 146 ? 0.2305 0.2966 0.2817 0.0363 0.0368 0.0171 262 ASN A CA 1129 C C . ASN A 146 ? 0.2611 0.3276 0.3143 0.0371 0.0291 0.0118 262 ASN A C 1130 O O . ASN A 146 ? 0.2465 0.3096 0.2908 0.0449 0.0247 0.0084 262 ASN A O 1131 C CB . ASN A 146 ? 0.2568 0.3123 0.2919 0.0441 0.0355 0.0161 262 ASN A CB 1132 C CG . ASN A 146 ? 0.2605 0.3163 0.2903 0.0466 0.0434 0.0216 262 ASN A CG 1133 O OD1 . ASN A 146 ? 0.2192 0.2847 0.2577 0.0428 0.0507 0.0270 262 ASN A OD1 1134 N ND2 . ASN A 146 ? 0.2576 0.3021 0.2728 0.0528 0.0414 0.0205 262 ASN A ND2 1135 N N . GLY A 147 ? 0.2603 0.3292 0.3240 0.0293 0.0266 0.0109 263 GLY A N 1136 C CA . GLY A 147 ? 0.1827 0.2513 0.2476 0.0296 0.0191 0.0064 263 GLY A CA 1137 C C . GLY A 147 ? 0.2423 0.3250 0.3169 0.0330 0.0201 0.0060 263 GLY A C 1138 O O . GLY A 147 ? 0.2291 0.3233 0.3089 0.0363 0.0273 0.0095 263 GLY A O 1139 N N . SER A 148 ? 0.2219 0.3043 0.2991 0.0325 0.0129 0.0021 264 SER A N 1140 C CA . SER A 148 ? 0.2634 0.3595 0.3514 0.0357 0.0124 0.0010 264 SER A CA 1141 C C . SER A 148 ? 0.2803 0.3841 0.3843 0.0265 0.0135 0.0028 264 SER A C 1142 O O . SER A 148 ? 0.3129 0.4074 0.4162 0.0188 0.0106 0.0025 264 SER A O 1143 C CB . SER A 148 ? 0.3730 0.4629 0.4545 0.0403 0.0026 -0.0044 264 SER A CB 1144 O OG . SER A 148 ? 0.4170 0.4959 0.4830 0.0472 -0.0006 -0.0062 264 SER A OG 1145 N N . LEU A 149 ? 0.2369 0.3579 0.3555 0.0278 0.0173 0.0047 265 LEU A N 1146 C CA . LEU A 149 ? 0.2439 0.3728 0.3799 0.0187 0.0173 0.0068 265 LEU A CA 1147 C C . LEU A 149 ? 0.2942 0.4252 0.4367 0.0186 0.0083 0.0018 265 LEU A C 1148 O O . LEU A 149 ? 0.2655 0.3984 0.4037 0.0268 0.0041 -0.0021 265 LEU A O 1149 C CB . LEU A 149 ? 0.2951 0.4433 0.4465 0.0184 0.0266 0.0128 265 LEU A CB 1150 C CG . LEU A 149 ? 0.2722 0.4188 0.4195 0.0163 0.0358 0.0193 265 LEU A CG 1151 C CD1 . LEU A 149 ? 0.3488 0.5167 0.5088 0.0187 0.0456 0.0254 265 LEU A CD1 1152 C CD2 . LEU A 149 ? 0.2457 0.3814 0.3958 0.0049 0.0345 0.0217 265 LEU A CD2 1153 N N . ALA A 150 ? 0.2768 0.4060 0.4287 0.0097 0.0045 0.0018 266 ALA A N 1154 C CA . ALA A 150 ? 0.3129 0.4454 0.4732 0.0090 -0.0041 -0.0024 266 ALA A CA 1155 C C . ALA A 150 ? 0.2912 0.4463 0.4699 0.0130 -0.0010 -0.0010 266 ALA A C 1156 O O . ALA A 150 ? 0.2932 0.4618 0.4839 0.0108 0.0077 0.0048 266 ALA A O 1157 C CB . ALA A 150 ? 0.2808 0.4064 0.4471 -0.0010 -0.0087 -0.0025 266 ALA A CB 1158 N N . GLU A 151 ? 0.2814 0.4412 0.4625 0.0191 -0.0081 -0.0060 267 GLU A N 1159 C CA . GLU A 151 ? 0.3255 0.5081 0.5223 0.0260 -0.0052 -0.0057 267 GLU A CA 1160 C C . GLU A 151 ? 0.3075 0.5061 0.5297 0.0194 -0.0073 -0.0043 267 GLU A C 1161 O O . GLU A 151 ? 0.2951 0.5172 0.5356 0.0226 -0.0022 -0.0019 267 GLU A O 1162 C CB . GLU A 151 ? 0.3719 0.5515 0.5582 0.0377 -0.0123 -0.0122 267 GLU A CB 1163 C CG . GLU A 151 ? 0.5107 0.6785 0.6753 0.0457 -0.0099 -0.0130 267 GLU A CG 1164 C CD . GLU A 151 ? 0.6592 0.8213 0.8126 0.0570 -0.0188 -0.0195 267 GLU A CD 1165 O OE1 . GLU A 151 ? 0.7122 0.8764 0.8723 0.0581 -0.0275 -0.0236 267 GLU A OE1 1166 O OE2 . GLU A 151 ? 0.7030 0.8570 0.8403 0.0650 -0.0180 -0.0206 267 GLU A OE2 1167 N N . GLU A 152 ? 0.2883 0.4748 0.5118 0.0104 -0.0150 -0.0058 268 GLU A N 1168 C CA . GLU A 152 ? 0.3073 0.5060 0.5545 0.0033 -0.0193 -0.0049 268 GLU A CA 1169 C C . GLU A 152 ? 0.2872 0.4760 0.5376 -0.0091 -0.0188 -0.0009 268 GLU A C 1170 O O . GLU A 152 ? 0.2622 0.4583 0.5202 -0.0139 -0.0096 0.0060 268 GLU A O 1171 C CB . GLU A 152 ? 0.3945 0.5886 0.6419 0.0062 -0.0326 -0.0123 268 GLU A CB 1172 C CG . GLU A 152 ? 0.4964 0.7092 0.7719 0.0023 -0.0376 -0.0122 268 GLU A CG 1173 C CD . GLU A 152 ? 0.6121 0.8247 0.8880 0.0091 -0.0498 -0.0198 268 GLU A CD 1174 O OE1 . GLU A 152 ? 0.6570 0.8670 0.9429 0.0037 -0.0601 -0.0224 268 GLU A OE1 1175 O OE2 . GLU A 152 ? 0.6703 0.8842 0.9360 0.0202 -0.0501 -0.0233 268 GLU A OE2 1176 N N . GLU A 153 ? 0.2621 0.4334 0.5051 -0.0137 -0.0291 -0.0053 269 GLU A N 1177 C CA . GLU A 153 ? 0.3008 0.4604 0.5447 -0.0239 -0.0303 -0.0028 269 GLU A CA 1178 C C . GLU A 153 ? 0.2099 0.3500 0.4300 -0.0237 -0.0262 -0.0025 269 GLU A C 1179 O O . GLU A 153 ? 0.2379 0.3703 0.4398 -0.0167 -0.0254 -0.0053 269 GLU A O 1180 C CB . GLU A 153 ? 0.3430 0.4928 0.5898 -0.0281 -0.0438 -0.0081 269 GLU A CB 1181 C CG . GLU A 153 ? 0.4722 0.6410 0.7442 -0.0287 -0.0498 -0.0090 269 GLU A CG 1182 C CD . GLU A 153 ? 0.6357 0.7988 0.9202 -0.0378 -0.0604 -0.0101 269 GLU A CD 1183 O OE1 . GLU A 153 ? 0.6515 0.7920 0.9188 -0.0402 -0.0667 -0.0137 269 GLU A OE1 1184 O OE2 . GLU A 153 ? 0.7265 0.9079 1.0381 -0.0423 -0.0625 -0.0075 269 GLU A OE2 1185 N N . ILE A 154 ? 0.2083 0.3406 0.4293 -0.0315 -0.0242 0.0011 270 ILE A N 1186 C CA . ILE A 154 ? 0.2048 0.3180 0.4046 -0.0315 -0.0222 0.0004 270 ILE A CA 1187 C C . ILE A 154 ? 0.2208 0.3181 0.4045 -0.0292 -0.0314 -0.0067 270 ILE A C 1188 O O . ILE A 154 ? 0.2550 0.3502 0.4448 -0.0316 -0.0409 -0.0103 270 ILE A O 1189 C CB . ILE A 154 ? 0.1946 0.3007 0.3989 -0.0400 -0.0209 0.0044 270 ILE A CB 1190 C CG1 . ILE A 154 ? 0.2693 0.3892 0.4858 -0.0423 -0.0103 0.0128 270 ILE A CG1 1191 C CG2 . ILE A 154 ? 0.1729 0.2589 0.3553 -0.0390 -0.0208 0.0020 270 ILE A CG2 1192 C CD1 . ILE A 154 ? 0.2793 0.3936 0.5043 -0.0518 -0.0104 0.0179 270 ILE A CD1 1193 N N . ILE A 155 ? 0.2333 0.3198 0.3966 -0.0247 -0.0290 -0.0084 271 ILE A N 1194 C CA . ILE A 155 ? 0.2610 0.3337 0.4078 -0.0224 -0.0363 -0.0139 271 ILE A CA 1195 C C . ILE A 155 ? 0.2713 0.3286 0.4022 -0.0242 -0.0350 -0.0146 271 ILE A C 1196 O O . ILE A 155 ? 0.2456 0.3015 0.3705 -0.0233 -0.0275 -0.0117 271 ILE A O 1197 C CB . ILE A 155 ? 0.2717 0.3452 0.4079 -0.0152 -0.0364 -0.0155 271 ILE A CB 1198 C CG1 . ILE A 155 ? 0.2708 0.3608 0.4222 -0.0114 -0.0370 -0.0153 271 ILE A CG1 1199 C CG2 . ILE A 155 ? 0.2788 0.3385 0.3988 -0.0139 -0.0444 -0.0200 271 ILE A CG2 1200 C CD1 . ILE A 155 ? 0.2834 0.3772 0.4463 -0.0128 -0.0466 -0.0187 271 ILE A CD1 1201 N N . ILE A 156 ? 0.2296 0.2755 0.3533 -0.0258 -0.0426 -0.0187 272 ILE A N 1202 C CA . ILE A 156 ? 0.2334 0.2655 0.3405 -0.0259 -0.0418 -0.0204 272 ILE A CA 1203 C C . ILE A 156 ? 0.2845 0.3102 0.3734 -0.0215 -0.0431 -0.0227 272 ILE A C 1204 O O . ILE A 156 ? 0.3189 0.3418 0.4039 -0.0201 -0.0503 -0.0257 272 ILE A O 1205 C CB . ILE A 156 ? 0.2968 0.3192 0.4043 -0.0292 -0.0496 -0.0239 272 ILE A CB 1206 C CG1 . ILE A 156 ? 0.3187 0.3473 0.4467 -0.0350 -0.0505 -0.0209 272 ILE A CG1 1207 C CG2 . ILE A 156 ? 0.2849 0.2944 0.3755 -0.0279 -0.0479 -0.0258 272 ILE A CG2 1208 C CD1 . ILE A 156 ? 0.2784 0.3107 0.4110 -0.0369 -0.0412 -0.0154 272 ILE A CD1 1209 N N . ARG A 157 ? 0.2124 0.2356 0.2905 -0.0197 -0.0365 -0.0209 273 ARG A N 1210 C CA . ARG A 157 ? 0.2223 0.2401 0.2844 -0.0168 -0.0371 -0.0216 273 ARG A CA 1211 C C . ARG A 157 ? 0.2849 0.2945 0.3335 -0.0168 -0.0348 -0.0226 273 ARG A C 1212 O O . ARG A 157 ? 0.2354 0.2452 0.2857 -0.0174 -0.0295 -0.0214 273 ARG A O 1213 C CB . ARG A 157 ? 0.2411 0.2644 0.3028 -0.0144 -0.0321 -0.0183 273 ARG A CB 1214 C CG . ARG A 157 ? 0.2432 0.2765 0.3180 -0.0127 -0.0326 -0.0172 273 ARG A CG 1215 C CD . ARG A 157 ? 0.2934 0.3296 0.3646 -0.0088 -0.0290 -0.0149 273 ARG A CD 1216 N NE . ARG A 157 ? 0.2681 0.3153 0.3516 -0.0057 -0.0281 -0.0141 273 ARG A NE 1217 C CZ . ARG A 157 ? 0.2945 0.3461 0.3832 -0.0032 -0.0339 -0.0163 273 ARG A CZ 1218 N NH1 . ARG A 157 ? 0.2599 0.3038 0.3412 -0.0036 -0.0417 -0.0192 273 ARG A NH1 1219 N NH2 . ARG A 157 ? 0.2398 0.3039 0.3405 0.0005 -0.0318 -0.0155 273 ARG A NH2 1220 N N . SER A 158 ? 0.2639 0.2666 0.2988 -0.0156 -0.0387 -0.0247 274 SER A N 1221 C CA . SER A 158 ? 0.2541 0.2512 0.2750 -0.0145 -0.0356 -0.0256 274 SER A CA 1222 C C . SER A 158 ? 0.3256 0.3182 0.3309 -0.0133 -0.0378 -0.0253 274 SER A C 1223 O O . SER A 158 ? 0.3072 0.2963 0.3099 -0.0130 -0.0447 -0.0267 274 SER A O 1224 C CB . SER A 158 ? 0.2836 0.2741 0.3033 -0.0143 -0.0389 -0.0298 274 SER A CB 1225 O OG . SER A 158 ? 0.3011 0.2870 0.3058 -0.0115 -0.0362 -0.0313 274 SER A OG 1226 N N . GLU A 159 ? 0.2781 0.2712 0.2733 -0.0127 -0.0321 -0.0230 275 GLU A N 1227 C CA . GLU A 159 ? 0.3397 0.3290 0.3193 -0.0123 -0.0332 -0.0215 275 GLU A CA 1228 C C . GLU A 159 ? 0.3372 0.3184 0.3055 -0.0101 -0.0386 -0.0259 275 GLU A C 1229 O O . GLU A 159 ? 0.3651 0.3406 0.3214 -0.0096 -0.0431 -0.0255 275 GLU A O 1230 C CB . GLU A 159 ? 0.3684 0.3622 0.3419 -0.0126 -0.0252 -0.0179 275 GLU A CB 1231 C CG . GLU A 159 ? 0.4459 0.4374 0.4043 -0.0134 -0.0251 -0.0143 275 GLU A CG 1232 C CD . GLU A 159 ? 0.5773 0.5762 0.5338 -0.0149 -0.0171 -0.0095 275 GLU A CD 1233 O OE1 . GLU A 159 ? 0.5255 0.5307 0.4925 -0.0148 -0.0126 -0.0094 275 GLU A OE1 1234 O OE2 . GLU A 159 ? 0.7034 0.7021 0.6483 -0.0165 -0.0157 -0.0054 275 GLU A OE2 1235 N N . ASN A 160 ? 0.3185 0.2975 0.2897 -0.0084 -0.0393 -0.0303 276 ASN A N 1236 C CA . ASN A 160 ? 0.3665 0.3361 0.3269 -0.0054 -0.0457 -0.0356 276 ASN A CA 1237 C C . ASN A 160 ? 0.3095 0.2763 0.2794 -0.0049 -0.0482 -0.0399 276 ASN A C 1238 O O . ASN A 160 ? 0.3532 0.3197 0.3194 -0.0025 -0.0437 -0.0413 276 ASN A O 1239 C CB . ASN A 160 ? 0.3974 0.3648 0.3377 -0.0018 -0.0415 -0.0354 276 ASN A CB 1240 C CG . ASN A 160 ? 0.3921 0.3484 0.3172 0.0029 -0.0486 -0.0413 276 ASN A CG 1241 O OD1 . ASN A 160 ? 0.3545 0.3039 0.2855 0.0030 -0.0574 -0.0460 276 ASN A OD1 1242 N ND2 . ASN A 160 ? 0.4261 0.3809 0.3315 0.0068 -0.0447 -0.0409 276 ASN A ND2 1243 N N . LEU A 161 ? 0.3226 0.2876 0.3052 -0.0073 -0.0556 -0.0418 277 LEU A N 1244 C CA . LEU A 161 ? 0.3901 0.3525 0.3845 -0.0087 -0.0587 -0.0445 277 LEU A CA 1245 C C . LEU A 161 ? 0.3994 0.3502 0.3801 -0.0043 -0.0627 -0.0503 277 LEU A C 1246 O O . LEU A 161 ? 0.4057 0.3533 0.3910 -0.0041 -0.0625 -0.0520 277 LEU A O 1247 C CB . LEU A 161 ? 0.4548 0.4181 0.4656 -0.0124 -0.0670 -0.0452 277 LEU A CB 1248 C CG . LEU A 161 ? 0.4814 0.4549 0.5143 -0.0172 -0.0634 -0.0411 277 LEU A CG 1249 C CD1 . LEU A 161 ? 0.4079 0.3819 0.4574 -0.0209 -0.0726 -0.0426 277 LEU A CD1 1250 C CD2 . LEU A 161 ? 0.4056 0.3785 0.4407 -0.0178 -0.0571 -0.0397 277 LEU A CD2 1251 N N . THR A 162 ? 0.4109 0.3546 0.3736 -0.0001 -0.0669 -0.0534 278 THR A N 1252 C CA . THR A 162 ? 0.3994 0.3311 0.3462 0.0058 -0.0719 -0.0599 278 THR A CA 1253 C C . THR A 162 ? 0.3925 0.3269 0.3289 0.0105 -0.0625 -0.0599 278 THR A C 1254 O O . THR A 162 ? 0.4105 0.3361 0.3379 0.0158 -0.0655 -0.0654 278 THR A O 1255 C CB . THR A 162 ? 0.4507 0.3742 0.3783 0.0100 -0.0783 -0.0629 278 THR A CB 1256 O OG1 . THR A 162 ? 0.4612 0.3838 0.3994 0.0059 -0.0869 -0.0626 278 THR A OG1 1257 C CG2 . THR A 162 ? 0.4915 0.4006 0.4027 0.0170 -0.0858 -0.0707 278 THR A CG2 1258 N N . ASN A 163 ? 0.3319 0.2783 0.2698 0.0089 -0.0520 -0.0539 279 ASN A N 1259 C CA . ASN A 163 ? 0.3990 0.3513 0.3300 0.0129 -0.0424 -0.0531 279 ASN A CA 1260 C C . ASN A 163 ? 0.3864 0.3427 0.3337 0.0104 -0.0388 -0.0518 279 ASN A C 1261 O O . ASN A 163 ? 0.3776 0.3427 0.3383 0.0053 -0.0343 -0.0463 279 ASN A O 1262 C CB . ASN A 163 ? 0.3802 0.3432 0.3057 0.0116 -0.0338 -0.0468 279 ASN A CB 1263 C CG . ASN A 163 ? 0.4078 0.3798 0.3283 0.0153 -0.0237 -0.0454 279 ASN A CG 1264 O OD1 . ASN A 163 ? 0.4329 0.4037 0.3550 0.0193 -0.0226 -0.0493 279 ASN A OD1 1265 N ND2 . ASN A 163 ? 0.4113 0.3926 0.3264 0.0139 -0.0167 -0.0397 279 ASN A ND2 1266 N N . ASN A 164 ? 0.3663 0.3150 0.3111 0.0146 -0.0416 -0.0569 280 ASN A N 1267 C CA . ASN A 164 ? 0.3741 0.3236 0.3324 0.0125 -0.0396 -0.0558 280 ASN A CA 1268 C C . ASN A 164 ? 0.4044 0.3667 0.3668 0.0126 -0.0286 -0.0510 280 ASN A C 1269 O O . ASN A 164 ? 0.4275 0.3916 0.4018 0.0100 -0.0264 -0.0487 280 ASN A O 1270 C CB . ASN A 164 ? 0.5074 0.4439 0.4587 0.0182 -0.0457 -0.0627 280 ASN A CB 1271 C CG . ASN A 164 ? 0.5673 0.5041 0.4994 0.0280 -0.0420 -0.0672 280 ASN A CG 1272 O OD1 . ASN A 164 ? 0.6016 0.5458 0.5332 0.0316 -0.0343 -0.0665 280 ASN A OD1 1273 N ND2 . ASN A 164 ? 0.6541 0.5833 0.5700 0.0330 -0.0474 -0.0720 280 ASN A ND2 1274 N N . ALA A 165 ? 0.3872 0.3580 0.3398 0.0152 -0.0221 -0.0492 281 ALA A N 1275 C CA . ALA A 165 ? 0.4359 0.4193 0.3932 0.0150 -0.0126 -0.0447 281 ALA A CA 1276 C C . ALA A 165 ? 0.4247 0.4155 0.3940 0.0078 -0.0101 -0.0379 281 ALA A C 1277 O O . ALA A 165 ? 0.4079 0.4074 0.3838 0.0067 -0.0041 -0.0341 281 ALA A O 1278 C CB . ALA A 165 ? 0.5267 0.5179 0.4703 0.0202 -0.0064 -0.0448 281 ALA A CB 1279 N N . LYS A 166 ? 0.3380 0.3250 0.3097 0.0037 -0.0155 -0.0369 282 LYS A N 1280 C CA . LYS A 166 ? 0.2744 0.2673 0.2561 -0.0017 -0.0143 -0.0313 282 LYS A CA 1281 C C . LYS A 166 ? 0.3153 0.3072 0.3122 -0.0047 -0.0159 -0.0305 282 LYS A C 1282 O O . LYS A 166 ? 0.3040 0.2891 0.3049 -0.0053 -0.0216 -0.0335 282 LYS A O 1283 C CB . LYS A 166 ? 0.3108 0.3009 0.2872 -0.0036 -0.0193 -0.0306 282 LYS A CB 1284 C CG . LYS A 166 ? 0.3458 0.3369 0.3060 -0.0015 -0.0171 -0.0297 282 LYS A CG 1285 C CD . LYS A 166 ? 0.4268 0.4281 0.3879 -0.0030 -0.0092 -0.0240 282 LYS A CD 1286 C CE . LYS A 166 ? 0.4992 0.5024 0.4452 -0.0025 -0.0067 -0.0213 282 LYS A CE 1287 N NZ . LYS A 166 ? 0.5505 0.5646 0.4996 -0.0052 0.0005 -0.0150 282 LYS A NZ 1288 N N . THR A 167 ? 0.3265 0.3253 0.3316 -0.0065 -0.0111 -0.0262 283 THR A N 1289 C CA . THR A 167 ? 0.2764 0.2755 0.2944 -0.0087 -0.0111 -0.0245 283 THR A CA 1290 C C . THR A 167 ? 0.2181 0.2174 0.2441 -0.0121 -0.0158 -0.0236 283 THR A C 1291 O O . THR A 167 ? 0.3241 0.3254 0.3474 -0.0127 -0.0178 -0.0227 283 THR A O 1292 C CB . THR A 167 ? 0.3894 0.3951 0.4118 -0.0086 -0.0052 -0.0205 283 THR A CB 1293 O OG1 . THR A 167 ? 0.3912 0.3978 0.4087 -0.0053 -0.0014 -0.0217 283 THR A OG1 1294 C CG2 . THR A 167 ? 0.3965 0.4026 0.4301 -0.0104 -0.0045 -0.0181 283 THR A CG2 1295 N N . ILE A 168 ? 0.2202 0.2177 0.2565 -0.0142 -0.0178 -0.0236 284 ILE A N 1296 C CA . ILE A 168 ? 0.2265 0.2271 0.2738 -0.0173 -0.0216 -0.0223 284 ILE A CA 1297 C C . ILE A 168 ? 0.2627 0.2713 0.3201 -0.0182 -0.0164 -0.0176 284 ILE A C 1298 O O . ILE A 168 ? 0.2830 0.2914 0.3436 -0.0184 -0.0123 -0.0155 284 ILE A O 1299 C CB . ILE A 168 ? 0.2478 0.2426 0.3021 -0.0200 -0.0275 -0.0245 284 ILE A CB 1300 C CG1 . ILE A 168 ? 0.2439 0.2287 0.2861 -0.0178 -0.0338 -0.0302 284 ILE A CG1 1301 C CG2 . ILE A 168 ? 0.2666 0.2680 0.3356 -0.0236 -0.0307 -0.0225 284 ILE A CG2 1302 C CD1 . ILE A 168 ? 0.2913 0.2670 0.3382 -0.0198 -0.0408 -0.0330 284 ILE A CD1 1303 N N . ILE A 169 ? 0.2386 0.2536 0.2996 -0.0180 -0.0171 -0.0160 285 ILE A N 1304 C CA . ILE A 169 ? 0.2249 0.2480 0.2949 -0.0176 -0.0129 -0.0121 285 ILE A CA 1305 C C . ILE A 169 ? 0.2419 0.2708 0.3261 -0.0203 -0.0156 -0.0114 285 ILE A C 1306 O O . ILE A 169 ? 0.2361 0.2666 0.3226 -0.0204 -0.0212 -0.0135 285 ILE A O 1307 C CB . ILE A 169 ? 0.2416 0.2680 0.3065 -0.0146 -0.0124 -0.0112 285 ILE A CB 1308 C CG1 . ILE A 169 ? 0.2839 0.3059 0.3369 -0.0131 -0.0101 -0.0112 285 ILE A CG1 1309 C CG2 . ILE A 169 ? 0.2816 0.3159 0.3543 -0.0125 -0.0085 -0.0080 285 ILE A CG2 1310 C CD1 . ILE A 169 ? 0.2824 0.3052 0.3296 -0.0113 -0.0115 -0.0101 285 ILE A CD1 1311 N N . VAL A 170 ? 0.2330 0.2653 0.3271 -0.0226 -0.0119 -0.0080 286 VAL A N 1312 C CA . VAL A 170 ? 0.2616 0.3026 0.3720 -0.0258 -0.0131 -0.0058 286 VAL A CA 1313 C C . VAL A 170 ? 0.2716 0.3245 0.3870 -0.0223 -0.0075 -0.0023 286 VAL A C 1314 O O . VAL A 170 ? 0.2265 0.2803 0.3387 -0.0204 -0.0010 0.0009 286 VAL A O 1315 C CB . VAL A 170 ? 0.3034 0.3416 0.4223 -0.0310 -0.0121 -0.0028 286 VAL A CB 1316 C CG1 . VAL A 170 ? 0.2474 0.2974 0.3858 -0.0354 -0.0127 0.0009 286 VAL A CG1 1317 C CG2 . VAL A 170 ? 0.2843 0.3088 0.3964 -0.0330 -0.0187 -0.0071 286 VAL A CG2 1318 N N . HIS A 171 ? 0.1982 0.2598 0.3204 -0.0206 -0.0106 -0.0035 287 HIS A N 1319 C CA . HIS A 171 ? 0.1949 0.2679 0.3209 -0.0157 -0.0060 -0.0012 287 HIS A CA 1320 C C . HIS A 171 ? 0.2363 0.3240 0.3814 -0.0183 -0.0028 0.0029 287 HIS A C 1321 O O . HIS A 171 ? 0.2367 0.3313 0.3943 -0.0206 -0.0078 0.0016 287 HIS A O 1322 C CB . HIS A 171 ? 0.2123 0.2857 0.3328 -0.0108 -0.0116 -0.0052 287 HIS A CB 1323 C CG . HIS A 171 ? 0.1929 0.2727 0.3104 -0.0036 -0.0081 -0.0043 287 HIS A CG 1324 N ND1 . HIS A 171 ? 0.2716 0.3513 0.3840 0.0018 -0.0135 -0.0075 287 HIS A ND1 1325 C CD2 . HIS A 171 ? 0.2220 0.3072 0.3393 -0.0002 -0.0006 -0.0007 287 HIS A CD2 1326 C CE1 . HIS A 171 ? 0.2848 0.3691 0.3942 0.0085 -0.0099 -0.0065 287 HIS A CE1 1327 N NE2 . HIS A 171 ? 0.2755 0.3636 0.3875 0.0076 -0.0018 -0.0024 287 HIS A NE2 1328 N N . LEU A 172 ? 0.2032 0.2958 0.3506 -0.0181 0.0055 0.0082 288 LEU A N 1329 C CA . LEU A 172 ? 0.1876 0.2949 0.3532 -0.0217 0.0101 0.0138 288 LEU A CA 1330 C C . LEU A 172 ? 0.2225 0.3475 0.3968 -0.0155 0.0122 0.0140 288 LEU A C 1331 O O . LEU A 172 ? 0.2306 0.3546 0.3936 -0.0073 0.0122 0.0108 288 LEU A O 1332 C CB . LEU A 172 ? 0.2014 0.3072 0.3643 -0.0231 0.0186 0.0202 288 LEU A CB 1333 C CG . LEU A 172 ? 0.2575 0.3459 0.4118 -0.0281 0.0167 0.0202 288 LEU A CG 1334 C CD1 . LEU A 172 ? 0.2483 0.3351 0.3985 -0.0281 0.0249 0.0265 288 LEU A CD1 1335 C CD2 . LEU A 172 ? 0.2463 0.3313 0.4125 -0.0367 0.0100 0.0199 288 LEU A CD2 1336 N N . ASN A 173 ? 0.2140 0.3553 0.4090 -0.0194 0.0137 0.0176 289 ASN A N 1337 C CA . ASN A 173 ? 0.2019 0.3633 0.4074 -0.0128 0.0166 0.0179 289 ASN A CA 1338 C C . ASN A 173 ? 0.2580 0.4350 0.4705 -0.0113 0.0287 0.0258 289 ASN A C 1339 O O . ASN A 173 ? 0.2145 0.4097 0.4341 -0.0043 0.0332 0.0265 289 ASN A O 1340 C CB . ASN A 173 ? 0.2101 0.3826 0.4350 -0.0161 0.0091 0.0156 289 ASN A CB 1341 C CG . ASN A 173 ? 0.2753 0.4546 0.5209 -0.0275 0.0094 0.0213 289 ASN A CG 1342 O OD1 . ASN A 173 ? 0.2368 0.4081 0.4800 -0.0339 0.0134 0.0264 289 ASN A OD1 1343 N ND2 . ASN A 173 ? 0.2703 0.4642 0.5370 -0.0302 0.0042 0.0206 289 ASN A ND2 1344 N N . LYS A 174 ? 0.2329 0.4021 0.4420 -0.0174 0.0338 0.0315 290 LYS A N 1345 C CA . LYS A 174 ? 0.2469 0.4279 0.4593 -0.0166 0.0456 0.0400 290 LYS A CA 1346 C C . LYS A 174 ? 0.2692 0.4322 0.4626 -0.0166 0.0492 0.0422 290 LYS A C 1347 O O . LYS A 174 ? 0.2746 0.4212 0.4643 -0.0239 0.0445 0.0419 290 LYS A O 1348 C CB . LYS A 174 ? 0.3157 0.5115 0.5527 -0.0271 0.0484 0.0479 290 LYS A CB 1349 C CG . LYS A 174 ? 0.4743 0.6827 0.7153 -0.0279 0.0613 0.0584 290 LYS A CG 1350 C CD . LYS A 174 ? 0.6029 0.8310 0.8424 -0.0155 0.0698 0.0587 290 LYS A CD 1351 C CE . LYS A 174 ? 0.6814 0.9234 0.9242 -0.0160 0.0836 0.0699 290 LYS A CE 1352 N NZ . LYS A 174 ? 0.6947 0.9551 0.9327 -0.0019 0.0922 0.0695 290 LYS A NZ 1353 N N . SER A 175 ? 0.2903 0.4559 0.4711 -0.0077 0.0568 0.0440 291 SER A N 1354 C CA . SER A 175 ? 0.3026 0.4516 0.4647 -0.0063 0.0598 0.0458 291 SER A CA 1355 C C . SER A 175 ? 0.2831 0.4305 0.4511 -0.0154 0.0652 0.0549 291 SER A C 1356 O O . SER A 175 ? 0.2444 0.4087 0.4286 -0.0198 0.0714 0.0624 291 SER A O 1357 C CB . SER A 175 ? 0.3110 0.4636 0.4583 0.0063 0.0659 0.0455 291 SER A CB 1358 O OG . SER A 175 ? 0.4429 0.5907 0.5804 0.0147 0.0592 0.0369 291 SER A OG 1359 N N . VAL A 176 ? 0.2739 0.4011 0.4292 -0.0183 0.0626 0.0545 292 VAL A N 1360 C CA . VAL A 176 ? 0.2938 0.4152 0.4491 -0.0251 0.0673 0.0631 292 VAL A CA 1361 C C . VAL A 176 ? 0.2598 0.3678 0.3930 -0.0177 0.0706 0.0631 292 VAL A C 1362 O O . VAL A 176 ? 0.2500 0.3423 0.3700 -0.0146 0.0644 0.0562 292 VAL A O 1363 C CB . VAL A 176 ? 0.3280 0.4353 0.4895 -0.0360 0.0592 0.0625 292 VAL A CB 1364 C CG1 . VAL A 176 ? 0.3158 0.4136 0.4748 -0.0423 0.0630 0.0713 292 VAL A CG1 1365 C CG2 . VAL A 176 ? 0.3775 0.4969 0.5612 -0.0435 0.0546 0.0624 292 VAL A CG2 1366 N N . GLU A 177 ? 0.2273 0.3419 0.3563 -0.0148 0.0802 0.0710 293 GLU A N 1367 C CA . GLU A 177 ? 0.1879 0.2898 0.2949 -0.0067 0.0828 0.0709 293 GLU A CA 1368 C C . GLU A 177 ? 0.2507 0.3312 0.3493 -0.0122 0.0786 0.0718 293 GLU A C 1369 O O . GLU A 177 ? 0.3140 0.3912 0.4222 -0.0224 0.0781 0.0775 293 GLU A O 1370 C CB . GLU A 177 ? 0.3091 0.4231 0.4118 -0.0015 0.0945 0.0795 293 GLU A CB 1371 C CG . GLU A 177 ? 0.4063 0.5394 0.5109 0.0086 0.0989 0.0770 293 GLU A CG 1372 C CD . GLU A 177 ? 0.4528 0.5938 0.5455 0.0174 0.1099 0.0836 293 GLU A CD 1373 O OE1 . GLU A 177 ? 0.4317 0.5637 0.5159 0.0143 0.1146 0.0913 293 GLU A OE1 1374 O OE2 . GLU A 177 ? 0.5045 0.6598 0.5952 0.0281 0.1136 0.0811 293 GLU A OE2 1375 N N . ILE A 178 ? 0.2566 0.3225 0.3376 -0.0051 0.0749 0.0660 294 ILE A N 1376 C CA . ILE A 178 ? 0.2515 0.2976 0.3221 -0.0075 0.0714 0.0666 294 ILE A CA 1377 C C . ILE A 178 ? 0.2800 0.3196 0.3315 0.0021 0.0754 0.0681 294 ILE A C 1378 O O . ILE A 178 ? 0.3198 0.3609 0.3622 0.0115 0.0743 0.0625 294 ILE A O 1379 C CB . ILE A 178 ? 0.2416 0.2759 0.3109 -0.0086 0.0614 0.0572 294 ILE A CB 1380 C CG1 . ILE A 178 ? 0.2648 0.2799 0.3249 -0.0106 0.0577 0.0576 294 ILE A CG1 1381 C CG2 . ILE A 178 ? 0.2606 0.2962 0.3214 0.0005 0.0585 0.0492 294 ILE A CG2 1382 C CD1 . ILE A 178 ? 0.3291 0.3345 0.3901 -0.0127 0.0489 0.0495 294 ILE A CD1 1383 N N . ASN A 179 ? 0.2838 0.3154 0.3288 -0.0004 0.0795 0.0762 295 ASN A N 1384 C CA . ASN A 179 ? 0.3567 0.3830 0.3831 0.0086 0.0845 0.0795 295 ASN A CA 1385 C C . ASN A 179 ? 0.3209 0.3251 0.3335 0.0096 0.0787 0.0778 295 ASN A C 1386 O O . ASN A 179 ? 0.3457 0.3400 0.3585 0.0026 0.0787 0.0839 295 ASN A O 1387 C CB . ASN A 179 ? 0.3568 0.3936 0.3856 0.0057 0.0954 0.0918 295 ASN A CB 1388 C CG . ASN A 179 ? 0.4523 0.4828 0.4595 0.0154 0.1011 0.0962 295 ASN A CG 1389 O OD1 . ASN A 179 ? 0.3842 0.4021 0.3751 0.0245 0.0960 0.0896 295 ASN A OD1 1390 N ND2 . ASN A 179 ? 0.5113 0.5514 0.5186 0.0136 0.1117 0.1077 295 ASN A ND2 1391 N N . CYS A 180 ? 0.3174 0.3139 0.3188 0.0182 0.0730 0.0694 296 CYS A N 1392 C CA . CYS A 180 ? 0.3436 0.3211 0.3346 0.0198 0.0662 0.0658 296 CYS A CA 1393 C C . CYS A 180 ? 0.3504 0.3183 0.3213 0.0296 0.0675 0.0675 296 CYS A C 1394 O O . CYS A 180 ? 0.3940 0.3676 0.3571 0.0384 0.0693 0.0653 296 CYS A O 1395 C CB . CYS A 180 ? 0.4326 0.4087 0.4278 0.0211 0.0577 0.0552 296 CYS A CB 1396 S SG . CYS A 180 ? 0.4567 0.4426 0.4724 0.0110 0.0552 0.0523 296 CYS A SG 1397 N N . THR A 181 ? 0.4254 0.3773 0.3868 0.0286 0.0659 0.0713 297 THR A N 1398 C CA . THR A 181 ? 0.4009 0.3413 0.3419 0.0382 0.0659 0.0725 297 THR A CA 1399 C C . THR A 181 ? 0.4000 0.3200 0.3320 0.0388 0.0585 0.0708 297 THR A C 1400 O O . THR A 181 ? 0.3976 0.3101 0.3357 0.0308 0.0564 0.0734 297 THR A O 1401 C CB . THR A 181 ? 0.5498 0.4950 0.4813 0.0404 0.0765 0.0833 297 THR A CB 1402 O OG1 . THR A 181 ? 0.5988 0.5262 0.5127 0.0431 0.0762 0.0887 297 THR A OG1 1403 C CG2 . THR A 181 ? 0.4400 0.3992 0.3882 0.0294 0.0841 0.0915 297 THR A CG2 1404 N N . ARG A 182 ? 0.4099 0.3211 0.3281 0.0489 0.0535 0.0656 298 ARG A N 1405 C CA . ARG A 182 ? 0.4266 0.3185 0.3326 0.0524 0.0470 0.0647 298 ARG A CA 1406 C C . ARG A 182 ? 0.4801 0.3643 0.3662 0.0585 0.0524 0.0727 298 ARG A C 1407 O O . ARG A 182 ? 0.4310 0.3174 0.3060 0.0681 0.0530 0.0706 298 ARG A O 1408 C CB . ARG A 182 ? 0.3816 0.2705 0.2861 0.0600 0.0377 0.0539 298 ARG A CB 1409 C CG . ARG A 182 ? 0.3732 0.2448 0.2702 0.0634 0.0294 0.0507 298 ARG A CG 1410 C CD . ARG A 182 ? 0.4398 0.2955 0.3152 0.0700 0.0300 0.0567 298 ARG A CD 1411 N NE . ARG A 182 ? 0.4736 0.3303 0.3360 0.0802 0.0300 0.0551 298 ARG A NE 1412 C CZ . ARG A 182 ? 0.4949 0.3457 0.3517 0.0888 0.0209 0.0473 298 ARG A CZ 1413 N NH1 . ARG A 182 ? 0.4568 0.3030 0.3214 0.0884 0.0124 0.0406 298 ARG A NH1 1414 N NH2 . ARG A 182 ? 0.4760 0.3260 0.3198 0.0982 0.0201 0.0460 298 ARG A NH2 1415 N N . PRO A 183 ? 0.4527 0.3269 0.3332 0.0531 0.0559 0.0823 299 PRO A N 1416 C CA . PRO A 183 ? 0.5644 0.4330 0.4259 0.0576 0.0631 0.0922 299 PRO A CA 1417 C C . PRO A 183 ? 0.6221 0.4749 0.4613 0.0705 0.0570 0.0883 299 PRO A C 1418 O O . PRO A 183 ? 0.5636 0.4047 0.4019 0.0737 0.0465 0.0803 299 PRO A O 1419 C CB . PRO A 183 ? 0.6089 0.4669 0.4711 0.0473 0.0653 0.1025 299 PRO A CB 1420 C CG . PRO A 183 ? 0.6187 0.4678 0.4921 0.0424 0.0550 0.0951 299 PRO A CG 1421 C CD . PRO A 183 ? 0.5116 0.3771 0.4015 0.0430 0.0524 0.0843 299 PRO A CD 1422 N N . SER A 184 ? 0.7295 0.5826 0.5508 0.0785 0.0635 0.0937 300 SER A N 1423 C CA . SER A 184 ? 0.8594 0.6982 0.6580 0.0922 0.0575 0.0895 300 SER A CA 1424 C C . SER A 184 ? 0.9402 0.7548 0.7251 0.0939 0.0497 0.0907 300 SER A C 1425 O O . SER A 184 ? 0.9504 0.7547 0.7310 0.1011 0.0384 0.0814 300 SER A O 1426 C CB . SER A 184 ? 0.9189 0.7623 0.6988 0.1007 0.0671 0.0964 300 SER A CB 1427 O OG . SER A 184 ? 0.9287 0.7564 0.6847 0.1146 0.0603 0.0921 300 SER A OG 1428 N N . ASN A 185 ? 1.0064 0.8122 0.7853 0.0870 0.0551 0.1022 301 ASN A N 1429 C CA . ASN A 185 ? 1.1417 0.9224 0.9060 0.0885 0.0474 0.1041 301 ASN A CA 1430 C C . ASN A 185 ? 1.2008 0.9754 0.9798 0.0760 0.0443 0.1066 301 ASN A C 1431 O O . ASN A 185 ? 1.2707 1.0286 1.0388 0.0718 0.0447 0.1159 301 ASN A O 1432 C CB . ASN A 185 ? 1.2241 0.9922 0.9612 0.0935 0.0539 0.1160 301 ASN A CB 1433 C CG . ASN A 185 ? 1.2789 1.0292 0.9913 0.1087 0.0452 0.1104 301 ASN A CG 1434 O OD1 . ASN A 185 ? 1.2867 1.0251 1.0004 0.1128 0.0322 0.1007 301 ASN A OD1 1435 N ND2 . ASN A 185 ? 1.3069 1.0559 0.9967 0.1178 0.0520 0.1162 301 ASN A ND2 1436 N N . GLY A 192 ? 1.1271 0.8341 0.9001 0.0921 -0.0086 0.0745 324 GLY A N 1437 C CA . GLY A 192 ? 1.0950 0.8167 0.8907 0.0808 -0.0047 0.0738 324 GLY A CA 1438 C C . GLY A 192 ? 1.0419 0.7819 0.8577 0.0830 -0.0086 0.0607 324 GLY A C 1439 O O . GLY A 192 ? 1.0372 0.7818 0.8513 0.0922 -0.0130 0.0531 324 GLY A O 1440 N N . ASP A 193 ? 0.9449 0.6948 0.7793 0.0743 -0.0075 0.0584 325 ASP A N 1441 C CA . ASP A 193 ? 0.8020 0.5698 0.6554 0.0752 -0.0101 0.0472 325 ASP A CA 1442 C C . ASP A 193 ? 0.6550 0.4444 0.5164 0.0743 -0.0025 0.0468 325 ASP A C 1443 O O . ASP A 193 ? 0.6513 0.4514 0.5201 0.0660 0.0058 0.0525 325 ASP A O 1444 C CB . ASP A 193 ? 0.7971 0.5667 0.6650 0.0668 -0.0114 0.0453 325 ASP A CB 1445 C CG . ASP A 193 ? 0.7761 0.5637 0.6619 0.0679 -0.0136 0.0343 325 ASP A CG 1446 O OD1 . ASP A 193 ? 0.7239 0.5261 0.6141 0.0719 -0.0118 0.0303 325 ASP A OD1 1447 O OD2 . ASP A 193 ? 0.8094 0.5959 0.7040 0.0650 -0.0174 0.0299 325 ASP A OD2 1448 N N . ILE A 194 ? 0.5437 0.3390 0.4041 0.0828 -0.0064 0.0398 326 ILE A N 1449 C CA . ILE A 194 ? 0.4773 0.2891 0.3418 0.0837 -0.0012 0.0392 326 ILE A CA 1450 C C . ILE A 194 ? 0.4055 0.2376 0.2912 0.0768 0.0019 0.0349 326 ILE A C 1451 O O . ILE A 194 ? 0.4087 0.2541 0.2984 0.0757 0.0070 0.0356 326 ILE A O 1452 C CB . ILE A 194 ? 0.5410 0.3512 0.3984 0.0947 -0.0083 0.0328 326 ILE A CB 1453 C CG1 . ILE A 194 ? 0.6077 0.4239 0.4796 0.0969 -0.0170 0.0224 326 ILE A CG1 1454 C CG2 . ILE A 194 ? 0.6199 0.4091 0.4540 0.1027 -0.0118 0.0369 326 ILE A CG2 1455 C CD1 . ILE A 194 ? 0.5185 0.3352 0.3878 0.1063 -0.0250 0.0160 326 ILE A CD1 1456 N N . ARG A 195 ? 0.4263 0.2600 0.3242 0.0729 -0.0017 0.0301 327 ARG A N 1457 C CA . ARG A 195 ? 0.4027 0.2542 0.3189 0.0667 0.0008 0.0260 327 ARG A CA 1458 C C . ARG A 195 ? 0.4696 0.3226 0.3916 0.0567 0.0067 0.0320 327 ARG A C 1459 O O . ARG A 195 ? 0.4075 0.2740 0.3433 0.0510 0.0091 0.0296 327 ARG A O 1460 C CB . ARG A 195 ? 0.3823 0.2376 0.3087 0.0693 -0.0062 0.0166 327 ARG A CB 1461 C CG . ARG A 195 ? 0.4277 0.2872 0.3542 0.0776 -0.0119 0.0105 327 ARG A CG 1462 C CD . ARG A 195 ? 0.4443 0.3075 0.3803 0.0811 -0.0185 0.0022 327 ARG A CD 1463 N NE . ARG A 195 ? 0.4571 0.3215 0.3923 0.0892 -0.0251 -0.0024 327 ARG A NE 1464 C CZ . ARG A 195 ? 0.4869 0.3360 0.4095 0.0969 -0.0312 -0.0025 327 ARG A CZ 1465 N NH1 . ARG A 195 ? 0.4672 0.2981 0.3760 0.0972 -0.0310 0.0023 327 ARG A NH1 1466 N NH2 . ARG A 195 ? 0.4868 0.3381 0.4104 0.1039 -0.0381 -0.0070 327 ARG A NH2 1467 N N . LYS A 196 ? 0.4485 0.2871 0.3601 0.0542 0.0085 0.0400 328 LYS A N 1468 C CA . LYS A 196 ? 0.4637 0.3027 0.3817 0.0438 0.0132 0.0469 328 LYS A CA 1469 C C . LYS A 196 ? 0.4161 0.2697 0.3377 0.0396 0.0229 0.0534 328 LYS A C 1470 O O . LYS A 196 ? 0.4132 0.2659 0.3230 0.0440 0.0273 0.0585 328 LYS A O 1471 C CB . LYS A 196 ? 0.4772 0.2950 0.3831 0.0416 0.0112 0.0544 328 LYS A CB 1472 C CG . LYS A 196 ? 0.6275 0.4450 0.5406 0.0297 0.0157 0.0631 328 LYS A CG 1473 C CD . LYS A 196 ? 0.7367 0.5308 0.6383 0.0268 0.0117 0.0703 328 LYS A CD 1474 C CE . LYS A 196 ? 0.8165 0.5945 0.7135 0.0330 0.0002 0.0615 328 LYS A CE 1475 N NZ . LYS A 196 ? 0.8633 0.6505 0.7756 0.0317 -0.0040 0.0515 328 LYS A NZ 1476 N N . ALA A 197 ? 0.3741 0.2411 0.3112 0.0319 0.0259 0.0529 329 ALA A N 1477 C CA . ALA A 197 ? 0.3677 0.2503 0.3105 0.0281 0.0347 0.0584 329 ALA A CA 1478 C C . ALA A 197 ? 0.3915 0.2794 0.3484 0.0167 0.0371 0.0628 329 ALA A C 1479 O O . ALA A 197 ? 0.4119 0.2893 0.3724 0.0121 0.0315 0.0615 329 ALA A O 1480 C CB . ALA A 197 ? 0.3533 0.2514 0.3018 0.0328 0.0349 0.0511 329 ALA A CB 1481 N N . TYR A 198 ? 0.3555 0.2593 0.3204 0.0128 0.0448 0.0675 330 TYR A N 1482 C CA . TYR A 198 ? 0.4340 0.3448 0.4143 0.0018 0.0468 0.0719 330 TYR A CA 1483 C C . TYR A 198 ? 0.4388 0.3715 0.4301 0.0005 0.0538 0.0732 330 TYR A C 1484 O O . TYR A 198 ? 0.4336 0.3742 0.4177 0.0072 0.0594 0.0747 330 TYR A O 1485 C CB . TYR A 198 ? 0.5032 0.4029 0.4802 -0.0053 0.0491 0.0834 330 TYR A CB 1486 C CG . TYR A 198 ? 0.5843 0.4850 0.5485 -0.0015 0.0577 0.0927 330 TYR A CG 1487 C CD1 . TYR A 198 ? 0.6186 0.5373 0.5898 -0.0047 0.0678 0.1006 330 TYR A CD1 1488 C CD2 . TYR A 198 ? 0.6304 0.5144 0.5749 0.0062 0.0555 0.0935 330 TYR A CD2 1489 C CE1 . TYR A 198 ? 0.6726 0.5931 0.6305 -0.0001 0.0764 0.1092 330 TYR A CE1 1490 C CE2 . TYR A 198 ? 0.6781 0.5620 0.6084 0.0106 0.0632 0.1019 330 TYR A CE2 1491 C CZ . TYR A 198 ? 0.7254 0.6278 0.6620 0.0076 0.0740 0.1099 330 TYR A CZ 1492 O OH . TYR A 198 ? 0.7897 0.6928 0.7106 0.0131 0.0825 0.1184 330 TYR A OH 1493 N N . CYS A 199 ? 0.3954 0.3370 0.4033 -0.0075 0.0527 0.0720 331 CYS A N 1494 C CA . CYS A 199 ? 0.3703 0.3326 0.3902 -0.0091 0.0583 0.0730 331 CYS A CA 1495 C C . CYS A 199 ? 0.4089 0.3775 0.4422 -0.0200 0.0624 0.0827 331 CYS A C 1496 O O . CYS A 199 ? 0.4145 0.3729 0.4540 -0.0282 0.0570 0.0841 331 CYS A O 1497 C CB . CYS A 199 ? 0.4078 0.3770 0.4367 -0.0086 0.0528 0.0629 331 CYS A CB 1498 S SG . CYS A 199 ? 0.4672 0.4347 0.4845 0.0030 0.0491 0.0528 331 CYS A SG 1499 N N . GLU A 200 ? 0.3753 0.3610 0.4135 -0.0199 0.0715 0.0893 332 GLU A N 1500 C CA . GLU A 200 ? 0.3173 0.3128 0.3709 -0.0307 0.0763 0.0994 332 GLU A CA 1501 C C . GLU A 200 ? 0.3749 0.3913 0.4472 -0.0332 0.0773 0.0963 332 GLU A C 1502 O O . GLU A 200 ? 0.3243 0.3533 0.3947 -0.0248 0.0803 0.0914 332 GLU A O 1503 C CB . GLU A 200 ? 0.3727 0.3732 0.4187 -0.0295 0.0872 0.1115 332 GLU A CB 1504 C CG . GLU A 200 ? 0.5020 0.4800 0.5293 -0.0282 0.0857 0.1161 332 GLU A CG 1505 C CD . GLU A 200 ? 0.6563 0.6391 0.6737 -0.0265 0.0971 0.1285 332 GLU A CD 1506 O OE1 . GLU A 200 ? 0.7435 0.7439 0.7589 -0.0188 0.1055 0.1290 332 GLU A OE1 1507 O OE2 . GLU A 200 ? 0.6417 0.6100 0.6524 -0.0323 0.0974 0.1378 332 GLU A OE2 1508 N N . ILE A 201 ? 0.3854 0.4041 0.4755 -0.0445 0.0735 0.0988 333 ILE A N 1509 C CA . ILE A 201 ? 0.3735 0.4110 0.4828 -0.0477 0.0730 0.0960 333 ILE A CA 1510 C C . ILE A 201 ? 0.3588 0.4067 0.4878 -0.0601 0.0761 0.1070 333 ILE A C 1511 O O . ILE A 201 ? 0.3842 0.4179 0.5157 -0.0695 0.0716 0.1122 333 ILE A O 1512 C CB . ILE A 201 ? 0.3987 0.4277 0.5114 -0.0488 0.0615 0.0846 333 ILE A CB 1513 C CG1 . ILE A 201 ? 0.4301 0.4491 0.5250 -0.0379 0.0582 0.0746 333 ILE A CG1 1514 C CG2 . ILE A 201 ? 0.4112 0.4586 0.5423 -0.0515 0.0603 0.0817 333 ILE A CG2 1515 C CD1 . ILE A 201 ? 0.4647 0.4607 0.5474 -0.0378 0.0514 0.0717 333 ILE A CD1 1516 N N . ASN A 202 ? 0.3458 0.4186 0.4893 -0.0602 0.0833 0.1105 334 ASN A N 1517 C CA . ASN A 202 ? 0.3463 0.4333 0.5128 -0.0724 0.0861 0.1206 334 ASN A CA 1518 C C . ASN A 202 ? 0.3242 0.4032 0.5055 -0.0820 0.0734 0.1157 334 ASN A C 1519 O O . ASN A 202 ? 0.3405 0.4256 0.5283 -0.0791 0.0677 0.1061 334 ASN A O 1520 C CB . ASN A 202 ? 0.3668 0.4844 0.5465 -0.0684 0.0957 0.1233 334 ASN A CB 1521 C CG . ASN A 202 ? 0.4507 0.5871 0.6561 -0.0809 0.1003 0.1352 334 ASN A CG 1522 O OD1 . ASN A 202 ? 0.4089 0.5400 0.6306 -0.0928 0.0915 0.1361 334 ASN A OD1 1523 N ND2 . ASN A 202 ? 0.6294 0.7881 0.8387 -0.0780 0.1140 0.1446 334 ASN A ND2 1524 N N . GLY A 203 ? 0.3595 0.4230 0.5446 -0.0932 0.0682 0.1222 335 GLY A N 1525 C CA . GLY A 203 ? 0.4019 0.4528 0.5974 -0.1016 0.0545 0.1171 335 GLY A CA 1526 C C . GLY A 203 ? 0.3908 0.4618 0.6136 -0.1095 0.0522 0.1185 335 GLY A C 1527 O O . GLY A 203 ? 0.3530 0.4186 0.5820 -0.1109 0.0411 0.1095 335 GLY A O 1528 N N . THR A 204 ? 0.3205 0.4153 0.5597 -0.1143 0.0627 0.1299 336 THR A N 1529 C CA . THR A 204 ? 0.3691 0.4869 0.6367 -0.1213 0.0613 0.1317 336 THR A CA 1530 C C . THR A 204 ? 0.3649 0.4946 0.6323 -0.1103 0.0594 0.1189 336 THR A C 1531 O O . THR A 204 ? 0.3015 0.4336 0.5829 -0.1138 0.0495 0.1126 336 THR A O 1532 C CB . THR A 204 ? 0.3437 0.4889 0.6287 -0.1266 0.0751 0.1465 336 THR A CB 1533 O OG1 . THR A 204 ? 0.3925 0.5262 0.6803 -0.1393 0.0756 0.1597 336 THR A OG1 1534 C CG2 . THR A 204 ? 0.3920 0.5643 0.7079 -0.1321 0.0737 0.1471 336 THR A CG2 1535 N N . LYS A 205 ? 0.3230 0.4584 0.5732 -0.0969 0.0680 0.1152 337 LYS A N 1536 C CA . LYS A 205 ? 0.3414 0.4869 0.5892 -0.0860 0.0666 0.1040 337 LYS A CA 1537 C C . LYS A 205 ? 0.3471 0.4708 0.5828 -0.0832 0.0538 0.0912 337 LYS A C 1538 O O . LYS A 205 ? 0.3040 0.4328 0.5479 -0.0819 0.0466 0.0834 337 LYS A O 1539 C CB . LYS A 205 ? 0.3656 0.5188 0.5959 -0.0723 0.0776 0.1034 337 LYS A CB 1540 C CG . LYS A 205 ? 0.4635 0.6449 0.7058 -0.0709 0.0911 0.1132 337 LYS A CG 1541 C CD . LYS A 205 ? 0.5295 0.7146 0.7507 -0.0556 0.1001 0.1109 337 LYS A CD 1542 C CE . LYS A 205 ? 0.5815 0.7977 0.8145 -0.0507 0.1126 0.1174 337 LYS A CE 1543 N NZ . LYS A 205 ? 0.6216 0.8499 0.8679 -0.0611 0.1221 0.1330 337 LYS A NZ 1544 N N . TRP A 206 ? 0.3073 0.4069 0.5230 -0.0816 0.0509 0.0892 338 TRP A N 1545 C CA . TRP A 206 ? 0.3560 0.4364 0.5580 -0.0773 0.0406 0.0774 338 TRP A CA 1546 C C . TRP A 206 ? 0.3427 0.4143 0.5567 -0.0860 0.0279 0.0737 338 TRP A C 1547 O O . TRP A 206 ? 0.3601 0.4293 0.5724 -0.0824 0.0204 0.0640 338 TRP A O 1548 C CB . TRP A 206 ? 0.3753 0.4339 0.5549 -0.0733 0.0407 0.0764 338 TRP A CB 1549 C CG . TRP A 206 ? 0.3688 0.4085 0.5369 -0.0705 0.0302 0.0656 338 TRP A CG 1550 C CD1 . TRP A 206 ? 0.3927 0.4127 0.5586 -0.0759 0.0207 0.0638 338 TRP A CD1 1551 C CD2 . TRP A 206 ? 0.4021 0.4413 0.5591 -0.0611 0.0280 0.0553 338 TRP A CD2 1552 N NE1 . TRP A 206 ? 0.3945 0.4033 0.5483 -0.0697 0.0138 0.0527 338 TRP A NE1 1553 C CE2 . TRP A 206 ? 0.3757 0.3963 0.5243 -0.0613 0.0184 0.0480 338 TRP A CE2 1554 C CE3 . TRP A 206 ? 0.3942 0.4461 0.5469 -0.0526 0.0329 0.0518 338 TRP A CE3 1555 C CZ2 . TRP A 206 ? 0.4175 0.4340 0.5546 -0.0539 0.0148 0.0382 338 TRP A CZ2 1556 C CZ3 . TRP A 206 ? 0.4453 0.4911 0.5869 -0.0460 0.0281 0.0423 338 TRP A CZ3 1557 C CH2 . TRP A 206 ? 0.4297 0.4590 0.5640 -0.0471 0.0198 0.0360 338 TRP A CH2 1558 N N . ASN A 207 ? 0.2901 0.3557 0.5153 -0.0974 0.0250 0.0817 339 ASN A N 1559 C CA . ASN A 207 ? 0.3841 0.4392 0.6204 -0.1058 0.0115 0.0784 339 ASN A CA 1560 C C . ASN A 207 ? 0.3632 0.4382 0.6210 -0.1085 0.0083 0.0764 339 ASN A C 1561 O O . ASN A 207 ? 0.3553 0.4222 0.6169 -0.1103 -0.0039 0.0688 339 ASN A O 1562 C CB . ASN A 207 ? 0.4492 0.4924 0.6932 -0.1181 0.0081 0.0884 339 ASN A CB 1563 C CG . ASN A 207 ? 0.4631 0.4801 0.6842 -0.1151 0.0062 0.0874 339 ASN A CG 1564 O OD1 . ASN A 207 ? 0.5330 0.5344 0.7367 -0.1071 0.0002 0.0766 339 ASN A OD1 1565 N ND2 . ASN A 207 ? 0.4708 0.4837 0.6918 -0.1212 0.0116 0.0990 339 ASN A ND2 1566 N N . LYS A 208 ? 0.2935 0.3948 0.5648 -0.1077 0.0189 0.0828 340 LYS A N 1567 C CA . LYS A 208 ? 0.3620 0.4851 0.6533 -0.1079 0.0169 0.0803 340 LYS A CA 1568 C C . LYS A 208 ? 0.3121 0.4308 0.5894 -0.0968 0.0119 0.0671 340 LYS A C 1569 O O . LYS A 208 ? 0.2955 0.4142 0.5812 -0.0981 0.0016 0.0605 340 LYS A O 1570 C CB . LYS A 208 ? 0.4409 0.5934 0.7455 -0.1062 0.0310 0.0891 340 LYS A CB 1571 C CG . LYS A 208 ? 0.5463 0.7241 0.8734 -0.1056 0.0296 0.0870 340 LYS A CG 1572 C CD . LYS A 208 ? 0.6481 0.8536 0.9799 -0.0979 0.0444 0.0920 340 LYS A CD 1573 C CE . LYS A 208 ? 0.7158 0.9281 1.0493 -0.1028 0.0570 0.1059 340 LYS A CE 1574 N NZ . LYS A 208 ? 0.7414 0.9800 1.0758 -0.0933 0.0719 0.1102 340 LYS A NZ 1575 N N . VAL A 209 ? 0.2225 0.3368 0.4781 -0.0862 0.0187 0.0637 341 VAL A N 1576 C CA . VAL A 209 ? 0.2387 0.3486 0.4798 -0.0761 0.0149 0.0526 341 VAL A CA 1577 C C . VAL A 209 ? 0.1753 0.2616 0.4041 -0.0768 0.0031 0.0442 341 VAL A C 1578 O O . VAL A 209 ? 0.2975 0.3822 0.5244 -0.0735 -0.0044 0.0361 341 VAL A O 1579 C CB . VAL A 209 ? 0.2519 0.3620 0.4735 -0.0654 0.0243 0.0518 341 VAL A CB 1580 C CG1 . VAL A 209 ? 0.2949 0.3964 0.5004 -0.0568 0.0191 0.0411 341 VAL A CG1 1581 C CG2 . VAL A 209 ? 0.2493 0.3840 0.4809 -0.0616 0.0352 0.0578 341 VAL A CG2 1582 N N . LEU A 210 ? 0.2339 0.3016 0.4531 -0.0802 0.0013 0.0461 342 LEU A N 1583 C CA . LEU A 210 ? 0.3357 0.3812 0.5423 -0.0797 -0.0095 0.0380 342 LEU A CA 1584 C C . LEU A 210 ? 0.3210 0.3645 0.5425 -0.0867 -0.0216 0.0353 342 LEU A C 1585 O O . LEU A 210 ? 0.2731 0.3062 0.4861 -0.0834 -0.0306 0.0263 342 LEU A O 1586 C CB . LEU A 210 ? 0.3252 0.3516 0.5199 -0.0816 -0.0095 0.0407 342 LEU A CB 1587 C CG . LEU A 210 ? 0.4002 0.4047 0.5756 -0.0765 -0.0174 0.0315 342 LEU A CG 1588 C CD1 . LEU A 210 ? 0.3927 0.4006 0.5532 -0.0660 -0.0139 0.0242 342 LEU A CD1 1589 C CD2 . LEU A 210 ? 0.4811 0.4685 0.6458 -0.0774 -0.0168 0.0347 342 LEU A CD2 1590 N N . LYS A 211 ? 0.3174 0.3711 0.5612 -0.0966 -0.0218 0.0436 343 LYS A N 1591 C CA . LYS A 211 ? 0.2777 0.3315 0.5390 -0.1040 -0.0341 0.0416 343 LYS A CA 1592 C C . LYS A 211 ? 0.3064 0.3730 0.5715 -0.0981 -0.0369 0.0345 343 LYS A C 1593 O O . LYS A 211 ? 0.3286 0.3854 0.5925 -0.0980 -0.0492 0.0268 343 LYS A O 1594 C CB . LYS A 211 ? 0.3456 0.4122 0.6334 -0.1164 -0.0326 0.0532 343 LYS A CB 1595 C CG . LYS A 211 ? 0.4616 0.5267 0.7695 -0.1255 -0.0469 0.0519 343 LYS A CG 1596 C CD . LYS A 211 ? 0.5928 0.6686 0.9270 -0.1394 -0.0455 0.0649 343 LYS A CD 1597 C CE . LYS A 211 ? 0.6854 0.7600 1.0419 -0.1493 -0.0612 0.0638 343 LYS A CE 1598 N NZ . LYS A 211 ? 0.6923 0.7875 1.0626 -0.1451 -0.0635 0.0582 343 LYS A NZ 1599 N N . GLN A 212 ? 0.2589 0.3461 0.5271 -0.0925 -0.0262 0.0367 344 GLN A N 1600 C CA . GLN A 212 ? 0.2418 0.3402 0.5115 -0.0857 -0.0286 0.0300 344 GLN A CA 1601 C C . GLN A 212 ? 0.2329 0.3139 0.4771 -0.0770 -0.0334 0.0198 344 GLN A C 1602 O O . GLN A 212 ? 0.2229 0.3020 0.4659 -0.0743 -0.0420 0.0127 344 GLN A O 1603 C CB . GLN A 212 ? 0.2738 0.3960 0.5495 -0.0802 -0.0161 0.0344 344 GLN A CB 1604 C CG . GLN A 212 ? 0.3477 0.4935 0.6518 -0.0875 -0.0112 0.0439 344 GLN A CG 1605 C CD . GLN A 212 ? 0.4319 0.6002 0.7383 -0.0802 0.0022 0.0480 344 GLN A CD 1606 O OE1 . GLN A 212 ? 0.4169 0.5801 0.7046 -0.0735 0.0108 0.0488 344 GLN A OE1 1607 N NE2 . GLN A 212 ? 0.4769 0.6703 0.8063 -0.0806 0.0036 0.0503 344 GLN A NE2 1608 N N . VAL A 213 ? 0.2191 0.2878 0.4432 -0.0727 -0.0278 0.0194 345 VAL A N 1609 C CA . VAL A 213 ? 0.2759 0.3295 0.4769 -0.0653 -0.0313 0.0109 345 VAL A CA 1610 C C . VAL A 213 ? 0.2765 0.3123 0.4736 -0.0682 -0.0443 0.0050 345 VAL A C 1611 O O . VAL A 213 ? 0.2879 0.3172 0.4743 -0.0635 -0.0508 -0.0026 345 VAL A O 1612 C CB . VAL A 213 ? 0.3096 0.3543 0.4924 -0.0608 -0.0233 0.0121 345 VAL A CB 1613 C CG1 . VAL A 213 ? 0.2553 0.2851 0.4167 -0.0545 -0.0275 0.0039 345 VAL A CG1 1614 C CG2 . VAL A 213 ? 0.2511 0.3111 0.4341 -0.0560 -0.0120 0.0164 345 VAL A CG2 1615 N N . THR A 214 ? 0.2405 0.2678 0.4454 -0.0758 -0.0483 0.0086 346 THR A N 1616 C CA . THR A 214 ? 0.3508 0.3598 0.5530 -0.0788 -0.0620 0.0031 346 THR A CA 1617 C C . THR A 214 ? 0.3536 0.3685 0.5683 -0.0806 -0.0722 -0.0009 346 THR A C 1618 O O . THR A 214 ? 0.3202 0.3212 0.5232 -0.0772 -0.0825 -0.0091 346 THR A O 1619 C CB . THR A 214 ? 0.4159 0.4155 0.6280 -0.0881 -0.0655 0.0092 346 THR A CB 1620 O OG1 . THR A 214 ? 0.4363 0.4263 0.6333 -0.0852 -0.0582 0.0115 346 THR A OG1 1621 C CG2 . THR A 214 ? 0.4850 0.4652 0.6957 -0.0911 -0.0817 0.0032 346 THR A CG2 1622 N N . GLU A 215 ? 0.2854 0.3213 0.5234 -0.0854 -0.0692 0.0049 347 GLU A N 1623 C CA . GLU A 215 ? 0.3409 0.3848 0.5938 -0.0871 -0.0791 0.0014 347 GLU A CA 1624 C C . GLU A 215 ? 0.2964 0.3406 0.5335 -0.0771 -0.0800 -0.0064 347 GLU A C 1625 O O . GLU A 215 ? 0.3067 0.3448 0.5426 -0.0757 -0.0917 -0.0131 347 GLU A O 1626 C CB . GLU A 215 ? 0.3616 0.4315 0.6443 -0.0935 -0.0741 0.0097 347 GLU A CB 1627 C CG . GLU A 215 ? 0.5301 0.6014 0.8306 -0.1050 -0.0729 0.0193 347 GLU A CG 1628 C CD . GLU A 215 ? 0.6509 0.7011 0.9535 -0.1120 -0.0888 0.0163 347 GLU A CD 1629 O OE1 . GLU A 215 ? 0.7059 0.7571 1.0206 -0.1144 -0.1013 0.0119 347 GLU A OE1 1630 O OE2 . GLU A 215 ? 0.6969 0.7283 0.9883 -0.1146 -0.0897 0.0179 347 GLU A OE2 1631 N N . LYS A 216 ? 0.2445 0.2948 0.4690 -0.0702 -0.0684 -0.0055 348 LYS A N 1632 C CA . LYS A 216 ? 0.2576 0.3067 0.4659 -0.0613 -0.0691 -0.0119 348 LYS A CA 1633 C C . LYS A 216 ? 0.3113 0.3381 0.4954 -0.0574 -0.0757 -0.0191 348 LYS A C 1634 O O . LYS A 216 ? 0.3328 0.3537 0.5077 -0.0533 -0.0836 -0.0254 348 LYS A O 1635 C CB . LYS A 216 ? 0.3221 0.3813 0.5228 -0.0555 -0.0561 -0.0088 348 LYS A CB 1636 C CG . LYS A 216 ? 0.4194 0.5019 0.6405 -0.0562 -0.0495 -0.0031 348 LYS A CG 1637 C CD . LYS A 216 ? 0.4506 0.5436 0.6855 -0.0555 -0.0579 -0.0065 348 LYS A CD 1638 C CE . LYS A 216 ? 0.3110 0.3968 0.5270 -0.0471 -0.0619 -0.0135 348 LYS A CE 1639 N NZ . LYS A 216 ? 0.3461 0.4425 0.5752 -0.0452 -0.0701 -0.0168 348 LYS A NZ 1640 N N . LEU A 217 ? 0.2632 0.2778 0.4363 -0.0579 -0.0724 -0.0182 349 LEU A N 1641 C CA . LEU A 217 ? 0.2819 0.2768 0.4321 -0.0532 -0.0775 -0.0249 349 LEU A CA 1642 C C . LEU A 217 ? 0.3398 0.3224 0.4916 -0.0552 -0.0927 -0.0306 349 LEU A C 1643 O O . LEU A 217 ? 0.3803 0.3511 0.5139 -0.0495 -0.0989 -0.0376 349 LEU A O 1644 C CB . LEU A 217 ? 0.2712 0.2564 0.4122 -0.0531 -0.0720 -0.0229 349 LEU A CB 1645 C CG . LEU A 217 ? 0.2717 0.2647 0.4048 -0.0490 -0.0586 -0.0193 349 LEU A CG 1646 C CD1 . LEU A 217 ? 0.2933 0.2779 0.4216 -0.0499 -0.0542 -0.0165 349 LEU A CD1 1647 C CD2 . LEU A 217 ? 0.2817 0.2724 0.3953 -0.0412 -0.0568 -0.0242 349 LEU A CD2 1648 N N . LYS A 218 ? 0.3182 0.3038 0.4918 -0.0635 -0.0989 -0.0273 350 LYS A N 1649 C CA . LYS A 218 ? 0.3089 0.2829 0.4866 -0.0661 -0.1150 -0.0327 350 LYS A CA 1650 C C . LYS A 218 ? 0.3249 0.3033 0.5005 -0.0617 -0.1214 -0.0380 350 LYS A C 1651 O O . LYS A 218 ? 0.3594 0.3230 0.5241 -0.0587 -0.1339 -0.0453 350 LYS A O 1652 C CB . LYS A 218 ? 0.4074 0.3873 0.6134 -0.0773 -0.1203 -0.0267 350 LYS A CB 1653 C CG . LYS A 218 ? 0.4586 0.4262 0.6645 -0.0826 -0.1199 -0.0228 350 LYS A CG 1654 C CD . LYS A 218 ? 0.5292 0.5019 0.7640 -0.0950 -0.1268 -0.0162 350 LYS A CD 1655 C CE . LYS A 218 ? 0.6455 0.6039 0.8796 -0.1009 -0.1272 -0.0115 350 LYS A CE 1656 N NZ . LYS A 218 ? 0.7114 0.6410 0.9227 -0.0958 -0.1389 -0.0204 350 LYS A NZ 1657 N N . GLU A 219 ? 0.3371 0.3350 0.5221 -0.0604 -0.1135 -0.0345 351 GLU A N 1658 C CA . GLU A 219 ? 0.3957 0.3978 0.5788 -0.0559 -0.1198 -0.0392 351 GLU A CA 1659 C C . GLU A 219 ? 0.3997 0.3867 0.5516 -0.0471 -0.1204 -0.0454 351 GLU A C 1660 O O . GLU A 219 ? 0.3580 0.3387 0.5014 -0.0431 -0.1300 -0.0510 351 GLU A O 1661 C CB . GLU A 219 ? 0.3961 0.4215 0.5944 -0.0553 -0.1110 -0.0343 351 GLU A CB 1662 C CG . GLU A 219 ? 0.4842 0.5282 0.7142 -0.0635 -0.1088 -0.0273 351 GLU A CG 1663 C CD . GLU A 219 ? 0.5725 0.6403 0.8157 -0.0609 -0.0996 -0.0232 351 GLU A CD 1664 O OE1 . GLU A 219 ? 0.5610 0.6294 0.7913 -0.0531 -0.0991 -0.0271 351 GLU A OE1 1665 O OE2 . GLU A 219 ? 0.6646 0.7500 0.9304 -0.0664 -0.0929 -0.0160 351 GLU A OE2 1666 N N . HIS A 220 ? 0.3737 0.3555 0.5088 -0.0440 -0.1103 -0.0440 352 HIS A N 1667 C CA . HIS A 220 ? 0.3538 0.3246 0.4608 -0.0362 -0.1087 -0.0484 352 HIS A CA 1668 C C . HIS A 220 ? 0.3496 0.3003 0.4387 -0.0335 -0.1157 -0.0542 352 HIS A C 1669 O O . HIS A 220 ? 0.4251 0.3656 0.4914 -0.0268 -0.1180 -0.0591 352 HIS A O 1670 C CB . HIS A 220 ? 0.2927 0.2706 0.3917 -0.0337 -0.0940 -0.0440 352 HIS A CB 1671 C CG . HIS A 220 ? 0.3803 0.3740 0.4877 -0.0330 -0.0881 -0.0402 352 HIS A CG 1672 N ND1 . HIS A 220 ? 0.4005 0.4099 0.5285 -0.0368 -0.0819 -0.0345 352 HIS A ND1 1673 C CD2 . HIS A 220 ? 0.3375 0.3326 0.4341 -0.0283 -0.0883 -0.0415 352 HIS A CD2 1674 C CE1 . HIS A 220 ? 0.3215 0.3416 0.4510 -0.0336 -0.0786 -0.0332 352 HIS A CE1 1675 N NE2 . HIS A 220 ? 0.3808 0.3917 0.4918 -0.0288 -0.0828 -0.0373 352 HIS A NE2 1676 N N . PHE A 221 ? 0.2913 0.2360 0.3900 -0.0382 -0.1191 -0.0535 353 PHE A N 1677 C CA . PHE A 221 ? 0.3386 0.2632 0.4202 -0.0347 -0.1260 -0.0594 353 PHE A CA 1678 C C . PHE A 221 ? 0.3663 0.2792 0.4578 -0.0388 -0.1427 -0.0634 353 PHE A C 1679 O O . PHE A 221 ? 0.3998 0.2988 0.4896 -0.0401 -0.1485 -0.0652 353 PHE A O 1680 C CB . PHE A 221 ? 0.3784 0.3009 0.4566 -0.0349 -0.1167 -0.0563 353 PHE A CB 1681 C CG . PHE A 221 ? 0.3581 0.2879 0.4220 -0.0293 -0.1029 -0.0543 353 PHE A CG 1682 C CD1 . PHE A 221 ? 0.3660 0.2864 0.4048 -0.0210 -0.1017 -0.0595 353 PHE A CD1 1683 C CD2 . PHE A 221 ? 0.3097 0.2562 0.3854 -0.0323 -0.0914 -0.0472 353 PHE A CD2 1684 C CE1 . PHE A 221 ? 0.3709 0.2992 0.3989 -0.0169 -0.0894 -0.0570 353 PHE A CE1 1685 C CE2 . PHE A 221 ? 0.3262 0.2783 0.3897 -0.0277 -0.0802 -0.0455 353 PHE A CE2 1686 C CZ . PHE A 221 ? 0.3604 0.3039 0.4011 -0.0206 -0.0793 -0.0501 353 PHE A CZ 1687 N N . ASN A 222 ? 0.4269 0.3449 0.5288 -0.0405 -0.1512 -0.0648 354 ASN A N 1688 C CA . ASN A 222 ? 0.4477 0.3538 0.5570 -0.0432 -0.1691 -0.0698 354 ASN A CA 1689 C C . ASN A 222 ? 0.3726 0.2755 0.5034 -0.0527 -0.1751 -0.0663 354 ASN A C 1690 O O . ASN A 222 ? 0.3641 0.2483 0.4915 -0.0533 -0.1899 -0.0717 354 ASN A O 1691 C CB . ASN A 222 ? 0.4854 0.3688 0.5645 -0.0338 -0.1788 -0.0794 354 ASN A CB 1692 C CG . ASN A 222 ? 0.4809 0.3526 0.5638 -0.0343 -0.1984 -0.0858 354 ASN A CG 1693 O OD1 . ASN A 222 ? 0.4956 0.3791 0.5983 -0.0388 -0.2034 -0.0841 354 ASN A OD1 1694 N ND2 . ASN A 222 ? 0.4501 0.2984 0.5140 -0.0290 -0.2103 -0.0936 354 ASN A ND2 1695 N N . ASN A 223 ? 0.3965 0.3167 0.5484 -0.0602 -0.1639 -0.0572 355 ASN A N 1696 C CA . ASN A 223 ? 0.4096 0.3289 0.5835 -0.0707 -0.1679 -0.0516 355 ASN A CA 1697 C C . ASN A 223 ? 0.4136 0.3105 0.5723 -0.0695 -0.1716 -0.0540 355 ASN A C 1698 O O . ASN A 223 ? 0.4015 0.2892 0.5738 -0.0775 -0.1812 -0.0519 355 ASN A O 1699 C CB . ASN A 223 ? 0.5067 0.4270 0.7039 -0.0781 -0.1840 -0.0525 355 ASN A CB 1700 C CG . ASN A 223 ? 0.5684 0.5168 0.7978 -0.0862 -0.1775 -0.0439 355 ASN A CG 1701 O OD1 . ASN A 223 ? 0.5312 0.4978 0.7610 -0.0832 -0.1625 -0.0398 355 ASN A OD1 1702 N ND2 . ASN A 223 ? 0.6090 0.5615 0.8659 -0.0962 -0.1889 -0.0412 355 ASN A ND2 1703 N N . LYS A 224 ? 0.4173 0.3055 0.5483 -0.0595 -0.1645 -0.0583 357 LYS A N 1704 C CA . LYS A 224 ? 0.4404 0.3096 0.5568 -0.0569 -0.1662 -0.0606 357 LYS A CA 1705 C C . LYS A 224 ? 0.4354 0.3133 0.5684 -0.0652 -0.1563 -0.0506 357 LYS A C 1706 O O . LYS A 224 ? 0.4031 0.3028 0.5518 -0.0696 -0.1444 -0.0428 357 LYS A O 1707 C CB . LYS A 224 ? 0.4406 0.3033 0.5259 -0.0441 -0.1589 -0.0667 357 LYS A CB 1708 C CG . LYS A 224 ? 0.5406 0.3925 0.6053 -0.0350 -0.1683 -0.0763 357 LYS A CG 1709 C CD . LYS A 224 ? 0.6432 0.4907 0.6781 -0.0228 -0.1597 -0.0812 357 LYS A CD 1710 C CE . LYS A 224 ? 0.6959 0.5257 0.7175 -0.0181 -0.1627 -0.0851 357 LYS A CE 1711 N NZ . LYS A 224 ? 0.7378 0.5638 0.7305 -0.0051 -0.1557 -0.0909 357 LYS A NZ 1712 N N . THR A 225 ? 0.4637 0.3236 0.5921 -0.0667 -0.1617 -0.0508 358 THR A N 1713 C CA . THR A 225 ? 0.4822 0.3472 0.6227 -0.0739 -0.1528 -0.0413 358 THR A CA 1714 C C . THR A 225 ? 0.4405 0.3165 0.5676 -0.0666 -0.1351 -0.0394 358 THR A C 1715 O O . THR A 225 ? 0.4393 0.3071 0.5426 -0.0558 -0.1331 -0.0465 358 THR A O 1716 C CB . THR A 225 ? 0.5335 0.3732 0.6689 -0.0761 -0.1642 -0.0427 358 THR A CB 1717 O OG1 . THR A 225 ? 0.5674 0.3947 0.7140 -0.0825 -0.1828 -0.0454 358 THR A OG1 1718 C CG2 . THR A 225 ? 0.5490 0.3932 0.6978 -0.0848 -0.1559 -0.0315 358 THR A CG2 1719 N N . ILE A 226 ? 0.4207 0.3161 0.5635 -0.0724 -0.1223 -0.0297 359 ILE A N 1720 C CA . ILE A 226 ? 0.4511 0.3572 0.5831 -0.0662 -0.1064 -0.0275 359 ILE A CA 1721 C C . ILE A 226 ? 0.4630 0.3613 0.5929 -0.0681 -0.1016 -0.0224 359 ILE A C 1722 O O . ILE A 226 ? 0.4588 0.3601 0.6061 -0.0778 -0.1010 -0.0137 359 ILE A O 1723 C CB . ILE A 226 ? 0.3754 0.3071 0.5222 -0.0688 -0.0953 -0.0212 359 ILE A CB 1724 C CG1 . ILE A 226 ? 0.4933 0.4314 0.6426 -0.0669 -0.1015 -0.0263 359 ILE A CG1 1725 C CG2 . ILE A 226 ? 0.3688 0.3095 0.5034 -0.0620 -0.0807 -0.0196 359 ILE A CG2 1726 C CD1 . ILE A 226 ? 0.4740 0.4012 0.5981 -0.0564 -0.1047 -0.0359 359 ILE A CD1 1727 N N . ILE A 227 ? 0.4124 0.3010 0.5209 -0.0588 -0.0983 -0.0274 360 ILE A N 1728 C CA . ILE A 227 ? 0.4547 0.3335 0.5582 -0.0587 -0.0950 -0.0239 360 ILE A CA 1729 C C . ILE A 227 ? 0.4432 0.3335 0.5371 -0.0520 -0.0804 -0.0224 360 ILE A C 1730 O O . ILE A 227 ? 0.4290 0.3245 0.5100 -0.0435 -0.0764 -0.0283 360 ILE A O 1731 C CB . ILE A 227 ? 0.5106 0.3638 0.5972 -0.0529 -0.1070 -0.0322 360 ILE A CB 1732 C CG1 . ILE A 227 ? 0.5672 0.4070 0.6595 -0.0575 -0.1236 -0.0363 360 ILE A CG1 1733 C CG2 . ILE A 227 ? 0.5659 0.4068 0.6504 -0.0547 -0.1062 -0.0277 360 ILE A CG2 1734 C CD1 . ILE A 227 ? 0.6989 0.5126 0.7717 -0.0495 -0.1367 -0.0463 360 ILE A CD1 1735 N N . PHE A 228 ? 0.4054 0.2996 0.5057 -0.0560 -0.0727 -0.0141 361 PHE A N 1736 C CA . PHE A 228 ? 0.4334 0.3356 0.5244 -0.0496 -0.0606 -0.0128 361 PHE A CA 1737 C C . PHE A 228 ? 0.4672 0.3519 0.5440 -0.0442 -0.0630 -0.0156 361 PHE A C 1738 O O . PHE A 228 ? 0.4823 0.3510 0.5614 -0.0489 -0.0708 -0.0134 361 PHE A O 1739 C CB . PHE A 228 ? 0.4343 0.3529 0.5388 -0.0554 -0.0499 -0.0024 361 PHE A CB 1740 C CG . PHE A 228 ? 0.4555 0.3938 0.5718 -0.0576 -0.0458 -0.0007 361 PHE A CG 1741 C CD1 . PHE A 228 ? 0.4379 0.3870 0.5461 -0.0505 -0.0399 -0.0046 361 PHE A CD1 1742 C CD2 . PHE A 228 ? 0.4545 0.4006 0.5904 -0.0669 -0.0484 0.0050 361 PHE A CD2 1743 C CE1 . PHE A 228 ? 0.4176 0.3828 0.5354 -0.0518 -0.0373 -0.0035 361 PHE A CE1 1744 C CE2 . PHE A 228 ? 0.4440 0.4085 0.5908 -0.0677 -0.0452 0.0059 361 PHE A CE2 1745 C CZ . PHE A 228 ? 0.4036 0.3767 0.5405 -0.0598 -0.0400 0.0014 361 PHE A CZ 1746 N N . GLN A 229 ? 0.4416 0.3292 0.5044 -0.0345 -0.0570 -0.0203 362 GLN A N 1747 C CA . GLN A 229 ? 0.4846 0.3581 0.5338 -0.0275 -0.0588 -0.0239 362 GLN A CA 1748 C C . GLN A 229 ? 0.4720 0.3573 0.5164 -0.0220 -0.0472 -0.0220 362 GLN A C 1749 O O . GLN A 229 ? 0.4327 0.3353 0.4804 -0.0215 -0.0394 -0.0206 362 GLN A O 1750 C CB . GLN A 229 ? 0.5333 0.3956 0.5679 -0.0187 -0.0670 -0.0350 362 GLN A CB 1751 C CG . GLN A 229 ? 0.6293 0.4715 0.6641 -0.0221 -0.0816 -0.0381 362 GLN A CG 1752 C CD . GLN A 229 ? 0.6882 0.5123 0.7233 -0.0253 -0.0873 -0.0345 362 GLN A CD 1753 O OE1 . GLN A 229 ? 0.6876 0.5106 0.7368 -0.0363 -0.0881 -0.0255 362 GLN A OE1 1754 N NE2 . GLN A 229 ? 0.6969 0.5070 0.7161 -0.0153 -0.0911 -0.0413 362 GLN A NE2 1755 N N . PRO A 230 ? 0.5760 0.4512 0.6125 -0.0175 -0.0471 -0.0222 363 PRO A N 1756 C CA . PRO A 230 ? 0.5440 0.4304 0.5769 -0.0123 -0.0372 -0.0206 363 PRO A CA 1757 C C . PRO A 230 ? 0.4934 0.3884 0.5172 -0.0031 -0.0346 -0.0285 363 PRO A C 1758 O O . PRO A 230 ? 0.5097 0.3984 0.5267 0.0008 -0.0409 -0.0357 363 PRO A O 1759 C CB . PRO A 230 ? 0.6025 0.4730 0.6283 -0.0092 -0.0403 -0.0200 363 PRO A CB 1760 C CG . PRO A 230 ? 0.6926 0.5443 0.7118 -0.0071 -0.0522 -0.0266 363 PRO A CG 1761 C CD . PRO A 230 ? 0.6548 0.5076 0.6835 -0.0153 -0.0569 -0.0254 363 PRO A CD 1762 N N . PRO A 231 ? 0.4303 0.3397 0.4539 0.0001 -0.0258 -0.0269 364 PRO A N 1763 C CA . PRO A 231 ? 0.4925 0.4107 0.5086 0.0080 -0.0232 -0.0333 364 PRO A CA 1764 C C . PRO A 231 ? 0.5867 0.4932 0.5917 0.0168 -0.0286 -0.0408 364 PRO A C 1765 O O . PRO A 231 ? 0.6043 0.4986 0.6071 0.0183 -0.0317 -0.0402 364 PRO A O 1766 C CB . PRO A 231 ? 0.4145 0.3459 0.4332 0.0094 -0.0146 -0.0294 364 PRO A CB 1767 C CG . PRO A 231 ? 0.4077 0.3418 0.4359 0.0013 -0.0119 -0.0213 364 PRO A CG 1768 C CD . PRO A 231 ? 0.4172 0.3359 0.4475 -0.0033 -0.0182 -0.0192 364 PRO A CD 1769 N N . SER A 232 ? 0.6489 0.5584 0.6461 0.0230 -0.0298 -0.0478 365 SER A N 1770 C CA . SER A 232 ? 0.6627 0.5613 0.6482 0.0328 -0.0355 -0.0561 365 SER A CA 1771 C C . SER A 232 ? 0.7352 0.6427 0.7171 0.0418 -0.0299 -0.0586 365 SER A C 1772 O O . SER A 232 ? 0.7879 0.6866 0.7613 0.0508 -0.0343 -0.0649 365 SER A O 1773 C CB . SER A 232 ? 0.6581 0.5557 0.6349 0.0369 -0.0393 -0.0629 365 SER A CB 1774 O OG . SER A 232 ? 0.7046 0.6212 0.6817 0.0375 -0.0312 -0.0621 365 SER A OG 1775 N N . GLY A 233 ? 0.6938 0.6186 0.6825 0.0396 -0.0211 -0.0538 366 GLY A N 1776 C CA . GLY A 233 ? 0.6801 0.6155 0.6684 0.0469 -0.0161 -0.0554 366 GLY A CA 1777 C C . GLY A 233 ? 0.6157 0.5706 0.6119 0.0431 -0.0076 -0.0502 366 GLY A C 1778 O O . GLY A 233 ? 0.5623 0.5214 0.5634 0.0353 -0.0056 -0.0454 366 GLY A O 1779 N N . GLY A 234 ? 0.5875 0.5539 0.5854 0.0488 -0.0034 -0.0512 367 GLY A N 1780 C CA . GLY A 234 ? 0.5116 0.4951 0.5172 0.0454 0.0033 -0.0464 367 GLY A CA 1781 C C . GLY A 234 ? 0.4854 0.4688 0.4966 0.0451 0.0040 -0.0427 367 GLY A C 1782 O O . GLY A 234 ? 0.5203 0.4911 0.5288 0.0483 0.0000 -0.0440 367 GLY A O 1783 N N . ASP A 235 ? 0.4231 0.4193 0.4412 0.0415 0.0083 -0.0382 368 ASP A N 1784 C CA . ASP A 235 ? 0.3818 0.3780 0.4044 0.0417 0.0085 -0.0350 368 ASP A CA 1785 C C . ASP A 235 ? 0.3199 0.3020 0.3410 0.0369 0.0063 -0.0305 368 ASP A C 1786 O O . ASP A 235 ? 0.2746 0.2524 0.2952 0.0311 0.0061 -0.0284 368 ASP A O 1787 C CB . ASP A 235 ? 0.4744 0.4860 0.5042 0.0384 0.0122 -0.0312 368 ASP A CB 1788 C CG . ASP A 235 ? 0.5947 0.6224 0.6286 0.0431 0.0148 -0.0341 368 ASP A CG 1789 O OD1 . ASP A 235 ? 0.6198 0.6473 0.6518 0.0508 0.0137 -0.0392 368 ASP A OD1 1790 O OD2 . ASP A 235 ? 0.5966 0.6373 0.6358 0.0390 0.0179 -0.0310 368 ASP A OD2 1791 N N . LEU A 236 ? 0.2829 0.2589 0.3035 0.0394 0.0049 -0.0288 369 LEU A N 1792 C CA . LEU A 236 ? 0.3360 0.2994 0.3542 0.0355 0.0039 -0.0237 369 LEU A CA 1793 C C . LEU A 236 ? 0.2934 0.2627 0.3155 0.0287 0.0072 -0.0183 369 LEU A C 1794 O O . LEU A 236 ? 0.3215 0.2839 0.3431 0.0239 0.0075 -0.0143 369 LEU A O 1795 C CB . LEU A 236 ? 0.3324 0.2892 0.3477 0.0402 0.0021 -0.0227 369 LEU A CB 1796 C CG . LEU A 236 ? 0.3889 0.3340 0.3986 0.0469 -0.0027 -0.0271 369 LEU A CG 1797 C CD1 . LEU A 236 ? 0.4407 0.3816 0.4480 0.0524 -0.0047 -0.0265 369 LEU A CD1 1798 C CD2 . LEU A 236 ? 0.4306 0.3585 0.4350 0.0433 -0.0059 -0.0253 369 LEU A CD2 1799 N N . GLU A 237 ? 0.2412 0.2236 0.2675 0.0283 0.0095 -0.0181 370 GLU A N 1800 C CA . GLU A 237 ? 0.2776 0.2651 0.3067 0.0232 0.0117 -0.0138 370 GLU A CA 1801 C C . GLU A 237 ? 0.2686 0.2559 0.2988 0.0179 0.0121 -0.0134 370 GLU A C 1802 O O . GLU A 237 ? 0.2857 0.2740 0.3179 0.0138 0.0133 -0.0097 370 GLU A O 1803 C CB . GLU A 237 ? 0.3214 0.3212 0.3545 0.0235 0.0124 -0.0139 370 GLU A CB 1804 C CG . GLU A 237 ? 0.3466 0.3466 0.3802 0.0280 0.0108 -0.0136 370 GLU A CG 1805 C CD . GLU A 237 ? 0.3204 0.3214 0.3546 0.0338 0.0094 -0.0180 370 GLU A CD 1806 O OE1 . GLU A 237 ? 0.2871 0.2914 0.3215 0.0348 0.0102 -0.0215 370 GLU A OE1 1807 O OE2 . GLU A 237 ? 0.3138 0.3120 0.3476 0.0383 0.0070 -0.0182 370 GLU A OE2 1808 N N . ILE A 238 ? 0.2650 0.2512 0.2936 0.0187 0.0106 -0.0176 371 ILE A N 1809 C CA . ILE A 238 ? 0.3400 0.3253 0.3690 0.0144 0.0096 -0.0182 371 ILE A CA 1810 C C . ILE A 238 ? 0.3053 0.2775 0.3330 0.0126 0.0063 -0.0182 371 ILE A C 1811 O O . ILE A 238 ? 0.3210 0.2912 0.3520 0.0072 0.0054 -0.0159 371 ILE A O 1812 C CB . ILE A 238 ? 0.4402 0.4315 0.4665 0.0167 0.0094 -0.0231 371 ILE A CB 1813 C CG1 . ILE A 238 ? 0.5023 0.5068 0.5308 0.0179 0.0126 -0.0224 371 ILE A CG1 1814 C CG2 . ILE A 238 ? 0.4694 0.4594 0.4951 0.0124 0.0077 -0.0236 371 ILE A CG2 1815 C CD1 . ILE A 238 ? 0.3858 0.3950 0.4181 0.0133 0.0138 -0.0176 371 ILE A CD1 1816 N N . THR A 239 ? 0.2853 0.2482 0.3086 0.0171 0.0037 -0.0209 372 THR A N 1817 C CA . THR A 239 ? 0.3157 0.2638 0.3372 0.0151 -0.0008 -0.0206 372 THR A CA 1818 C C . THR A 239 ? 0.3198 0.2628 0.3443 0.0103 0.0006 -0.0133 372 THR A C 1819 O O . THR A 239 ? 0.3296 0.2630 0.3558 0.0054 -0.0022 -0.0105 372 THR A O 1820 C CB . THR A 239 ? 0.3709 0.3085 0.3852 0.0222 -0.0052 -0.0261 372 THR A CB 1821 O OG1 . THR A 239 ? 0.3115 0.2490 0.3243 0.0268 -0.0037 -0.0250 372 THR A OG1 1822 C CG2 . THR A 239 ? 0.3788 0.3235 0.3896 0.0278 -0.0056 -0.0333 372 THR A CG2 1823 N N . MET A 240 ? 0.2770 0.2267 0.3021 0.0116 0.0050 -0.0099 373 MET A N 1824 C CA . MET A 240 ? 0.3006 0.2475 0.3270 0.0083 0.0077 -0.0027 373 MET A CA 1825 C C . MET A 240 ? 0.3007 0.2607 0.3322 0.0057 0.0121 0.0003 373 MET A C 1826 O O . MET A 240 ? 0.2664 0.2358 0.2989 0.0074 0.0126 -0.0029 373 MET A O 1827 C CB . MET A 240 ? 0.3078 0.2485 0.3278 0.0137 0.0080 -0.0014 373 MET A CB 1828 C CG . MET A 240 ? 0.4177 0.3459 0.4317 0.0183 0.0028 -0.0057 373 MET A CG 1829 S SD . MET A 240 ? 0.6028 0.5198 0.6084 0.0240 0.0018 -0.0032 373 MET A SD 1830 C CE . MET A 240 ? 0.9164 0.8191 0.9200 0.0167 0.0016 0.0054 373 MET A CE 1831 N N . HIS A 241 ? 0.2619 0.2226 0.2964 0.0018 0.0150 0.0066 374 HIS A N 1832 C CA . HIS A 241 ? 0.2346 0.2069 0.2724 0.0014 0.0190 0.0092 374 HIS A CA 1833 C C . HIS A 241 ? 0.2595 0.2322 0.2907 0.0076 0.0206 0.0094 374 HIS A C 1834 O O . HIS A 241 ? 0.3085 0.2749 0.3346 0.0096 0.0222 0.0133 374 HIS A O 1835 C CB . HIS A 241 ? 0.2399 0.2144 0.2831 -0.0035 0.0224 0.0160 374 HIS A CB 1836 C CG . HIS A 241 ? 0.2488 0.2343 0.2933 -0.0016 0.0268 0.0187 374 HIS A CG 1837 N ND1 . HIS A 241 ? 0.3918 0.3790 0.4352 -0.0011 0.0318 0.0251 374 HIS A ND1 1838 C CD2 . HIS A 241 ? 0.1773 0.1718 0.2230 0.0004 0.0265 0.0157 374 HIS A CD2 1839 C CE1 . HIS A 241 ? 0.2576 0.2548 0.3012 0.0022 0.0343 0.0252 374 HIS A CE1 1840 N NE2 . HIS A 241 ? 0.3076 0.3084 0.3528 0.0029 0.0306 0.0195 374 HIS A NE2 1841 N N . SER A 242 ? 0.2519 0.2315 0.2829 0.0104 0.0195 0.0056 375 SER A N 1842 C CA . SER A 242 ? 0.2443 0.2241 0.2702 0.0159 0.0194 0.0055 375 SER A CA 1843 C C . SER A 242 ? 0.2390 0.2260 0.2652 0.0167 0.0208 0.0072 375 SER A C 1844 O O . SER A 242 ? 0.2352 0.2293 0.2663 0.0137 0.0207 0.0064 375 SER A O 1845 C CB . SER A 242 ? 0.3453 0.3267 0.3711 0.0189 0.0163 0.0004 375 SER A CB 1846 O OG . SER A 242 ? 0.3998 0.3895 0.4303 0.0162 0.0157 -0.0023 375 SER A OG 1847 N N . PHE A 243 ? 0.2423 0.2263 0.2622 0.0216 0.0213 0.0093 376 PHE A N 1848 C CA . PHE A 243 ? 0.2505 0.2392 0.2684 0.0243 0.0217 0.0103 376 PHE A CA 1849 C C . PHE A 243 ? 0.2766 0.2590 0.2854 0.0311 0.0199 0.0105 376 PHE A C 1850 O O . PHE A 243 ? 0.2530 0.2279 0.2577 0.0332 0.0190 0.0106 376 PHE A O 1851 C CB . PHE A 243 ? 0.2780 0.2708 0.2977 0.0225 0.0264 0.0145 376 PHE A CB 1852 C CG . PHE A 243 ? 0.3003 0.2875 0.3162 0.0226 0.0306 0.0196 376 PHE A CG 1853 C CD1 . PHE A 243 ? 0.3632 0.3459 0.3831 0.0173 0.0311 0.0210 376 PHE A CD1 1854 C CD2 . PHE A 243 ? 0.3591 0.3445 0.3664 0.0282 0.0336 0.0232 376 PHE A CD2 1855 C CE1 . PHE A 243 ? 0.4315 0.4077 0.4477 0.0164 0.0344 0.0267 376 PHE A CE1 1856 C CE2 . PHE A 243 ? 0.3670 0.3470 0.3697 0.0279 0.0380 0.0291 376 PHE A CE2 1857 C CZ . PHE A 243 ? 0.4145 0.3897 0.4221 0.0214 0.0383 0.0312 376 PHE A CZ 1858 N N . ASN A 244 ? 0.2961 0.2803 0.3010 0.0352 0.0183 0.0103 377 ASN A N 1859 C CA . ASN A 244 ? 0.2921 0.2691 0.2869 0.0425 0.0154 0.0101 377 ASN A CA 1860 C C . ASN A 244 ? 0.3306 0.3065 0.3167 0.0476 0.0196 0.0138 377 ASN A C 1861 O O . ASN A 244 ? 0.3205 0.3030 0.3082 0.0479 0.0211 0.0142 377 ASN A O 1862 C CB . ASN A 244 ? 0.2610 0.2386 0.2566 0.0444 0.0083 0.0063 377 ASN A CB 1863 C CG . ASN A 244 ? 0.3556 0.3244 0.3420 0.0518 0.0033 0.0052 377 ASN A CG 1864 O OD1 . ASN A 244 ? 0.3234 0.2872 0.2990 0.0582 0.0038 0.0067 377 ASN A OD1 1865 N ND2 . ASN A 244 ? 0.3838 0.3512 0.3742 0.0514 -0.0017 0.0026 377 ASN A ND2 1866 N N . CYS A 245 ? 0.2918 0.2595 0.2680 0.0520 0.0214 0.0166 378 CYS A N 1867 C CA . CYS A 245 ? 0.3423 0.3092 0.3082 0.0576 0.0265 0.0209 378 CYS A CA 1868 C C . CYS A 245 ? 0.3409 0.2973 0.2919 0.0672 0.0217 0.0193 378 CYS A C 1869 O O . CYS A 245 ? 0.3596 0.3064 0.3052 0.0689 0.0194 0.0195 378 CYS A O 1870 C CB . CYS A 245 ? 0.3870 0.3528 0.3529 0.0535 0.0338 0.0273 378 CYS A CB 1871 S SG . CYS A 245 ? 0.4890 0.4555 0.4423 0.0596 0.0423 0.0346 378 CYS A SG 1872 N N . ARG A 246 ? 0.3621 0.3191 0.3059 0.0742 0.0193 0.0174 379 ARG A N 1873 C CA . ARG A 246 ? 0.3401 0.2859 0.2685 0.0844 0.0132 0.0152 379 ARG A CA 1874 C C . ARG A 246 ? 0.3809 0.3194 0.3123 0.0837 0.0036 0.0107 379 ARG A C 1875 O O . ARG A 246 ? 0.4499 0.3773 0.3701 0.0904 -0.0009 0.0098 379 ARG A O 1876 C CB . ARG A 246 ? 0.3766 0.3153 0.2899 0.0902 0.0191 0.0204 379 ARG A CB 1877 C CG . ARG A 246 ? 0.5140 0.4623 0.4263 0.0898 0.0303 0.0266 379 ARG A CG 1878 C CD . ARG A 246 ? 0.6404 0.5965 0.5508 0.0956 0.0302 0.0241 379 ARG A CD 1879 N NE . ARG A 246 ? 0.8123 0.7810 0.7246 0.0952 0.0414 0.0299 379 ARG A NE 1880 C CZ . ARG A 246 ? 0.8434 0.8225 0.7569 0.0997 0.0433 0.0284 379 ARG A CZ 1881 N NH1 . ARG A 246 ? 0.7871 0.7629 0.6985 0.1047 0.0340 0.0213 379 ARG A NH1 1882 N NH2 . ARG A 246 ? 0.9169 0.9096 0.8343 0.0990 0.0540 0.0342 379 ARG A NH2 1883 N N . GLY A 247 ? 0.3588 0.3042 0.3055 0.0759 0.0007 0.0080 380 GLY A N 1884 C CA . GLY A 247 ? 0.3521 0.2944 0.3047 0.0746 -0.0075 0.0041 380 GLY A CA 1885 C C . GLY A 247 ? 0.3632 0.3057 0.3225 0.0701 -0.0053 0.0047 380 GLY A C 1886 O O . GLY A 247 ? 0.3589 0.3033 0.3268 0.0679 -0.0107 0.0015 380 GLY A O 1887 N N . GLU A 248 ? 0.3137 0.2546 0.2694 0.0687 0.0022 0.0088 381 GLU A N 1888 C CA . GLU A 248 ? 0.3311 0.2692 0.2907 0.0655 0.0035 0.0093 381 GLU A CA 1889 C C . GLU A 248 ? 0.3399 0.2874 0.3126 0.0566 0.0078 0.0095 381 GLU A C 1890 O O . GLU A 248 ? 0.2898 0.2436 0.2653 0.0530 0.0129 0.0120 381 GLU A O 1891 C CB . GLU A 248 ? 0.3838 0.3113 0.3303 0.0689 0.0077 0.0142 381 GLU A CB 1892 C CG . GLU A 248 ? 0.3754 0.2924 0.3053 0.0788 0.0042 0.0145 381 GLU A CG 1893 C CD . GLU A 248 ? 0.4213 0.3305 0.3497 0.0835 -0.0052 0.0098 381 GLU A CD 1894 O OE1 . GLU A 248 ? 0.4452 0.3563 0.3837 0.0797 -0.0071 0.0075 381 GLU A OE1 1895 O OE2 . GLU A 248 ? 0.4208 0.3220 0.3379 0.0917 -0.0111 0.0082 381 GLU A OE2 1896 N N . PHE A 249 ? 0.2966 0.2453 0.2771 0.0539 0.0055 0.0065 382 PHE A N 1897 C CA . PHE A 249 ? 0.3165 0.2728 0.3076 0.0466 0.0085 0.0058 382 PHE A CA 1898 C C . PHE A 249 ? 0.3113 0.2612 0.3003 0.0440 0.0125 0.0090 382 PHE A C 1899 O O . PHE A 249 ? 0.3098 0.2512 0.2953 0.0463 0.0102 0.0081 382 PHE A O 1900 C CB . PHE A 249 ? 0.2836 0.2461 0.2840 0.0456 0.0045 0.0009 382 PHE A CB 1901 C CG . PHE A 249 ? 0.2350 0.2053 0.2406 0.0454 0.0007 -0.0011 382 PHE A CG 1902 C CD1 . PHE A 249 ? 0.2516 0.2308 0.2637 0.0399 0.0023 -0.0010 382 PHE A CD1 1903 C CD2 . PHE A 249 ? 0.3078 0.2754 0.3117 0.0503 -0.0055 -0.0029 382 PHE A CD2 1904 C CE1 . PHE A 249 ? 0.2525 0.2372 0.2689 0.0390 -0.0020 -0.0021 382 PHE A CE1 1905 C CE2 . PHE A 249 ? 0.3280 0.3015 0.3373 0.0491 -0.0102 -0.0042 382 PHE A CE2 1906 C CZ . PHE A 249 ? 0.3095 0.2913 0.3249 0.0432 -0.0083 -0.0035 382 PHE A CZ 1907 N N . PHE A 250 ? 0.3066 0.2603 0.2981 0.0390 0.0176 0.0127 383 PHE A N 1908 C CA . PHE A 250 ? 0.3097 0.2577 0.3011 0.0346 0.0209 0.0167 383 PHE A CA 1909 C C . PHE A 250 ? 0.3095 0.2609 0.3106 0.0290 0.0197 0.0134 383 PHE A C 1910 O O . PHE A 250 ? 0.3062 0.2675 0.3147 0.0261 0.0197 0.0109 383 PHE A O 1911 C CB . PHE A 250 ? 0.3088 0.2608 0.2998 0.0319 0.0271 0.0230 383 PHE A CB 1912 C CG . PHE A 250 ? 0.3584 0.3039 0.3370 0.0372 0.0299 0.0280 383 PHE A CG 1913 C CD1 . PHE A 250 ? 0.3723 0.3172 0.3426 0.0449 0.0276 0.0259 383 PHE A CD1 1914 C CD2 . PHE A 250 ? 0.4198 0.3591 0.3943 0.0345 0.0343 0.0352 383 PHE A CD2 1915 C CE1 . PHE A 250 ? 0.3920 0.3300 0.3485 0.0511 0.0300 0.0303 383 PHE A CE1 1916 C CE2 . PHE A 250 ? 0.4647 0.3982 0.4259 0.0397 0.0376 0.0405 383 PHE A CE2 1917 C CZ . PHE A 250 ? 0.4234 0.3561 0.3747 0.0487 0.0356 0.0377 383 PHE A CZ 1918 N N . TYR A 251 ? 0.2888 0.2303 0.2880 0.0280 0.0179 0.0135 384 TYR A N 1919 C CA . TYR A 251 ? 0.2982 0.2399 0.3041 0.0235 0.0161 0.0105 384 TYR A CA 1920 C C . TYR A 251 ? 0.3230 0.2557 0.3284 0.0181 0.0173 0.0160 384 TYR A C 1921 O O . TYR A 251 ? 0.3638 0.2835 0.3617 0.0198 0.0158 0.0188 384 TYR A O 1922 C CB . TYR A 251 ? 0.2990 0.2361 0.3033 0.0282 0.0112 0.0043 384 TYR A CB 1923 C CG . TYR A 251 ? 0.2777 0.2261 0.2859 0.0319 0.0099 -0.0009 384 TYR A CG 1924 C CD1 . TYR A 251 ? 0.3007 0.2522 0.3066 0.0358 0.0097 -0.0001 384 TYR A CD1 1925 C CD2 . TYR A 251 ? 0.3080 0.2635 0.3218 0.0315 0.0087 -0.0062 384 TYR A CD2 1926 C CE1 . TYR A 251 ? 0.3123 0.2738 0.3232 0.0379 0.0078 -0.0040 384 TYR A CE1 1927 C CE2 . TYR A 251 ? 0.3238 0.2910 0.3422 0.0338 0.0082 -0.0096 384 TYR A CE2 1928 C CZ . TYR A 251 ? 0.3408 0.3109 0.3587 0.0364 0.0075 -0.0082 384 TYR A CZ 1929 O OH . TYR A 251 ? 0.3463 0.3277 0.3703 0.0375 0.0062 -0.0107 384 TYR A OH 1930 N N . CYS A 252 ? 0.3255 0.2644 0.3391 0.0114 0.0192 0.0179 385 CYS A N 1931 C CA . CYS A 252 ? 0.3234 0.2559 0.3394 0.0047 0.0203 0.0243 385 CYS A CA 1932 C C . CYS A 252 ? 0.3610 0.2896 0.3834 -0.0004 0.0156 0.0212 385 CYS A C 1933 O O . CYS A 252 ? 0.3114 0.2488 0.3399 -0.0016 0.0145 0.0166 385 CYS A O 1934 C CB . CYS A 252 ? 0.3718 0.3156 0.3930 0.0011 0.0268 0.0308 385 CYS A CB 1935 S SG . CYS A 252 ? 0.4434 0.3898 0.4544 0.0082 0.0321 0.0348 385 CYS A SG 1936 N N . ASN A 253 ? 0.3055 0.2194 0.3253 -0.0034 0.0120 0.0241 386 ASN A N 1937 C CA . ASN A 253 ? 0.3470 0.2532 0.3711 -0.0079 0.0057 0.0211 386 ASN A CA 1938 C C . ASN A 253 ? 0.2955 0.2086 0.3316 -0.0173 0.0073 0.0264 386 ASN A C 1939 O O . ASN A 253 ? 0.3169 0.2286 0.3561 -0.0230 0.0105 0.0353 386 ASN A O 1940 C CB . ASN A 253 ? 0.3830 0.2685 0.3991 -0.0074 -0.0002 0.0223 386 ASN A CB 1941 C CG . ASN A 253 ? 0.4181 0.2926 0.4357 -0.0094 -0.0088 0.0170 386 ASN A CG 1942 O OD1 . ASN A 253 ? 0.4151 0.2934 0.4419 -0.0162 -0.0104 0.0177 386 ASN A OD1 1943 N ND2 . ASN A 253 ? 0.5240 0.3845 0.5321 -0.0026 -0.0153 0.0111 386 ASN A ND2 1944 N N . THR A 254 ? 0.3248 0.2461 0.3679 -0.0189 0.0051 0.0212 387 THR A N 1945 C CA . THR A 254 ? 0.3233 0.2536 0.3793 -0.0270 0.0062 0.0252 387 THR A CA 1946 C C . THR A 254 ? 0.3437 0.2627 0.4052 -0.0337 -0.0021 0.0247 387 THR A C 1947 O O . THR A 254 ? 0.3454 0.2718 0.4187 -0.0400 -0.0034 0.0261 387 THR A O 1948 C CB . THR A 254 ? 0.3359 0.2823 0.3964 -0.0249 0.0083 0.0205 387 THR A CB 1949 O OG1 . THR A 254 ? 0.3567 0.2991 0.4120 -0.0206 0.0029 0.0115 387 THR A OG1 1950 C CG2 . THR A 254 ? 0.3250 0.2819 0.3813 -0.0193 0.0154 0.0219 387 THR A CG2 1951 N N . THR A 255 ? 0.3497 0.2502 0.4029 -0.0320 -0.0087 0.0223 388 THR A N 1952 C CA . THR A 255 ? 0.4746 0.3608 0.5313 -0.0377 -0.0185 0.0214 388 THR A CA 1953 C C . THR A 255 ? 0.4799 0.3702 0.5516 -0.0496 -0.0177 0.0311 388 THR A C 1954 O O . THR A 255 ? 0.4483 0.3393 0.5298 -0.0553 -0.0236 0.0295 388 THR A O 1955 C CB . THR A 255 ? 0.5176 0.3810 0.5627 -0.0346 -0.0255 0.0198 388 THR A CB 1956 O OG1 . THR A 255 ? 0.5628 0.4229 0.5967 -0.0237 -0.0285 0.0090 388 THR A OG1 1957 C CG2 . THR A 255 ? 0.5866 0.4331 0.6362 -0.0424 -0.0361 0.0214 388 THR A CG2 1958 N N . GLN A 256 ? 0.4557 0.3496 0.5292 -0.0531 -0.0104 0.0412 389 GLN A N 1959 C CA . GLN A 256 ? 0.4642 0.3639 0.5526 -0.0646 -0.0081 0.0521 389 GLN A CA 1960 C C . GLN A 256 ? 0.4583 0.3815 0.5618 -0.0676 -0.0030 0.0529 389 GLN A C 1961 O O . GLN A 256 ? 0.4827 0.4125 0.6023 -0.0774 -0.0035 0.0596 389 GLN A O 1962 C CB . GLN A 256 ? 0.4756 0.3746 0.5597 -0.0662 0.0000 0.0630 389 GLN A CB 1963 C CG . GLN A 256 ? 0.6237 0.4980 0.6940 -0.0650 -0.0057 0.0645 389 GLN A CG 1964 C CD . GLN A 256 ? 0.6948 0.5686 0.7581 -0.0652 0.0029 0.0752 389 GLN A CD 1965 O OE1 . GLN A 256 ? 0.6773 0.5516 0.7483 -0.0750 0.0059 0.0871 389 GLN A OE1 1966 N NE2 . GLN A 256 ? 0.6716 0.5447 0.7201 -0.0544 0.0069 0.0713 389 GLN A NE2 1967 N N . LEU A 257 ? 0.3412 0.2769 0.4402 -0.0592 0.0016 0.0464 390 LEU A N 1968 C CA . LEU A 257 ? 0.3672 0.3239 0.4787 -0.0606 0.0059 0.0465 390 LEU A CA 1969 C C . LEU A 257 ? 0.4376 0.3936 0.5584 -0.0646 -0.0033 0.0407 390 LEU A C 1970 O O . LEU A 257 ? 0.5667 0.5366 0.7032 -0.0701 -0.0027 0.0435 390 LEU A O 1971 C CB . LEU A 257 ? 0.4363 0.4040 0.5391 -0.0507 0.0120 0.0414 390 LEU A CB 1972 C CG . LEU A 257 ? 0.4946 0.4701 0.5920 -0.0466 0.0221 0.0475 390 LEU A CG 1973 C CD1 . LEU A 257 ? 0.4109 0.3976 0.5029 -0.0380 0.0257 0.0418 390 LEU A CD1 1974 C CD2 . LEU A 257 ? 0.5214 0.5095 0.6321 -0.0535 0.0285 0.0580 390 LEU A CD2 1975 N N . PHE A 258 ? 0.3240 0.2639 0.4347 -0.0611 -0.0120 0.0323 391 PHE A N 1976 C CA . PHE A 258 ? 0.4341 0.3711 0.5495 -0.0628 -0.0215 0.0254 391 PHE A CA 1977 C C . PHE A 258 ? 0.4704 0.3882 0.5885 -0.0695 -0.0325 0.0263 391 PHE A C 1978 O O . PHE A 258 ? 0.5132 0.4148 0.6208 -0.0653 -0.0416 0.0181 391 PHE A O 1979 C CB . PHE A 258 ? 0.4371 0.3725 0.5383 -0.0528 -0.0229 0.0148 391 PHE A CB 1980 C CG . PHE A 258 ? 0.4055 0.3581 0.5047 -0.0473 -0.0135 0.0145 391 PHE A CG 1981 C CD1 . PHE A 258 ? 0.3910 0.3586 0.4994 -0.0486 -0.0123 0.0139 391 PHE A CD1 1982 C CD2 . PHE A 258 ? 0.3573 0.3101 0.4456 -0.0407 -0.0070 0.0148 391 PHE A CD2 1983 C CE1 . PHE A 258 ? 0.2914 0.2727 0.3972 -0.0434 -0.0050 0.0136 391 PHE A CE1 1984 C CE2 . PHE A 258 ? 0.3265 0.2933 0.4130 -0.0360 0.0001 0.0145 391 PHE A CE2 1985 C CZ . PHE A 258 ? 0.2927 0.2732 0.3876 -0.0373 0.0009 0.0140 391 PHE A CZ 1986 N N . ASN A 259 ? 0.5074 0.4276 0.6398 -0.0798 -0.0316 0.0366 392 ASN A N 1987 C CA . ASN A 259 ? 0.6039 0.5054 0.7409 -0.0883 -0.0421 0.0400 392 ASN A CA 1988 C C . ASN A 259 ? 0.5713 0.4762 0.7255 -0.0964 -0.0513 0.0392 392 ASN A C 1989 O O . ASN A 259 ? 0.5008 0.4246 0.6740 -0.1038 -0.0465 0.0464 392 ASN A O 1990 C CB . ASN A 259 ? 0.6976 0.5991 0.8401 -0.0959 -0.0357 0.0533 392 ASN A CB 1991 C CG . ASN A 259 ? 0.8431 0.7191 0.9835 -0.1027 -0.0468 0.0567 392 ASN A CG 1992 O OD1 . ASN A 259 ? 0.8258 0.6906 0.9731 -0.1082 -0.0595 0.0536 392 ASN A OD1 1993 N ND2 . ASN A 259 ? 0.9818 0.8469 1.1117 -0.1020 -0.0430 0.0628 392 ASN A ND2 1994 N N . ASN A 260 ? 0.5584 0.4451 0.7058 -0.0943 -0.0648 0.0300 393 ASN A N 1995 C CA . ASN A 260 ? 0.6015 0.4882 0.7630 -0.1009 -0.0759 0.0276 393 ASN A CA 1996 C C . ASN A 260 ? 0.6313 0.5173 0.8142 -0.1159 -0.0804 0.0389 393 ASN A C 1997 O O . ASN A 260 ? 0.5994 0.4967 0.8019 -0.1234 -0.0847 0.0409 393 ASN A O 1998 C CB . ASN A 260 ? 0.5987 0.4625 0.7448 -0.0944 -0.0902 0.0153 393 ASN A CB 1999 C CG . ASN A 260 ? 0.5306 0.3970 0.6568 -0.0801 -0.0854 0.0048 393 ASN A CG 2000 O OD1 . ASN A 260 ? 0.4665 0.3484 0.5946 -0.0767 -0.0816 0.0011 393 ASN A OD1 2001 N ND2 . ASN A 260 ? 0.5241 0.3753 0.6316 -0.0719 -0.0859 0.0004 393 ASN A ND2 2002 N N . THR A 261 ? 0.6369 0.5095 0.8163 -0.1205 -0.0798 0.0467 394 THR A N 2003 C CA . THR A 261 ? 0.6441 0.5138 0.8428 -0.1358 -0.0842 0.0589 394 THR A CA 2004 C C . THR A 261 ? 0.6036 0.5045 0.8260 -0.1439 -0.0721 0.0699 394 THR A C 2005 O O . THR A 261 ? 0.5751 0.4834 0.8208 -0.1558 -0.0778 0.0759 394 THR A O 2006 C CB . THR A 261 ? 0.7281 0.5787 0.9161 -0.1384 -0.0835 0.0665 394 THR A CB 2007 O OG1 . THR A 261 ? 0.7387 0.5612 0.9040 -0.1292 -0.0945 0.0555 394 THR A OG1 2008 C CG2 . THR A 261 ? 0.7493 0.5940 0.9568 -0.1556 -0.0899 0.0797 394 THR A CG2 2009 N N . CYS A 262 ? 0.5780 0.4976 0.7946 -0.1368 -0.0560 0.0721 395 CYS A N 2010 C CA . CYS A 262 ? 0.6624 0.6124 0.8985 -0.1417 -0.0430 0.0820 395 CYS A CA 2011 C C . CYS A 262 ? 0.7015 0.6717 0.9526 -0.1405 -0.0447 0.0761 395 CYS A C 2012 O O . CYS A 262 ? 0.7023 0.6993 0.9706 -0.1433 -0.0350 0.0826 395 CYS A O 2013 C CB . CYS A 262 ? 0.6644 0.6253 0.8866 -0.1327 -0.0266 0.0849 395 CYS A CB 2014 S SG . CYS A 262 ? 0.9410 0.8760 1.1403 -0.1305 -0.0254 0.0891 395 CYS A SG 2015 N N . ILE A 263 ? 0.7026 0.6598 0.9461 -0.1356 -0.0571 0.0636 396 ILE A N 2016 C CA . ILE A 263 ? 0.7131 0.6853 0.9689 -0.1344 -0.0612 0.0574 396 ILE A CA 2017 C C . ILE A 263 ? 0.7681 0.7368 1.0464 -0.1469 -0.0753 0.0599 396 ILE A C 2018 O O . ILE A 263 ? 0.7884 0.7339 1.0595 -0.1471 -0.0908 0.0523 396 ILE A O 2019 C CB . ILE A 263 ? 0.7784 0.7400 1.0128 -0.1216 -0.0665 0.0425 396 ILE A CB 2020 C CG1 . ILE A 263 ? 0.7468 0.7141 0.9619 -0.1101 -0.0531 0.0403 396 ILE A CG1 2021 C CG2 . ILE A 263 ? 0.8111 0.7857 1.0571 -0.1208 -0.0722 0.0365 396 ILE A CG2 2022 C CD1 . ILE A 263 ? 0.7675 0.7219 0.9596 -0.0983 -0.0573 0.0275 396 ILE A CD1 2023 N N . ASN A 272 ? 0.7003 0.7236 0.9497 -0.1544 0.0312 0.1484 411 ASN A N 2024 C CA . ASN A 272 ? 0.7208 0.7773 0.9819 -0.1525 0.0471 0.1561 411 ASN A CA 2025 C C . ASN A 272 ? 0.6688 0.7262 0.9107 -0.1459 0.0612 0.1640 411 ASN A C 2026 O O . ASN A 272 ? 0.7145 0.7982 0.9621 -0.1426 0.0754 0.1707 411 ASN A O 2027 C CB . ASN A 272 ? 0.8137 0.8903 1.1072 -0.1682 0.0481 0.1685 411 ASN A CB 2028 C CG . ASN A 272 ? 0.8795 0.9725 1.1951 -0.1694 0.0408 0.1602 411 ASN A CG 2029 O OD1 . ASN A 272 ? 0.8939 1.0185 1.2295 -0.1697 0.0495 0.1643 411 ASN A OD1 2030 N ND2 . ASN A 272 ? 0.9040 0.9756 1.2154 -0.1690 0.0246 0.1481 411 ASN A ND2 2031 N N . GLY A 273 ? 0.5688 0.5974 0.7873 -0.1431 0.0568 0.1628 412 GLY A N 2032 C CA . GLY A 273 ? 0.5444 0.5698 0.7418 -0.1361 0.0683 0.1693 412 GLY A CA 2033 C C . GLY A 273 ? 0.5409 0.5654 0.7171 -0.1185 0.0709 0.1563 412 GLY A C 2034 O O . GLY A 273 ? 0.5110 0.5440 0.6918 -0.1123 0.0671 0.1444 412 GLY A O 2035 N N . THR A 274 ? 0.4780 0.4917 0.6308 -0.1105 0.0769 0.1589 413 THR A N 2036 C CA . THR A 274 ? 0.4338 0.4433 0.5661 -0.0946 0.0775 0.1467 413 THR A CA 2037 C C . THR A 274 ? 0.4647 0.4476 0.5856 -0.0918 0.0635 0.1349 413 THR A C 2038 O O . THR A 274 ? 0.5338 0.4935 0.6475 -0.0971 0.0566 0.1383 413 THR A O 2039 C CB . THR A 274 ? 0.5036 0.5104 0.6143 -0.0861 0.0879 0.1530 413 THR A CB 2040 O OG1 . THR A 274 ? 0.5095 0.5431 0.6290 -0.0863 0.1020 0.1630 413 THR A OG1 2041 C CG2 . THR A 274 ? 0.5243 0.5248 0.6150 -0.0703 0.0862 0.1399 413 THR A CG2 2042 N N . ILE A 275 ? 0.4724 0.4590 0.5915 -0.0833 0.0593 0.1213 414 ILE A N 2043 C CA . ILE A 275 ? 0.4754 0.4406 0.5823 -0.0783 0.0480 0.1095 414 ILE A CA 2044 C C . ILE A 275 ? 0.4096 0.3684 0.4943 -0.0652 0.0515 0.1046 414 ILE A C 2045 O O . ILE A 275 ? 0.4274 0.4015 0.5094 -0.0568 0.0578 0.1011 414 ILE A O 2046 C CB . ILE A 275 ? 0.4220 0.3947 0.5391 -0.0769 0.0412 0.0979 414 ILE A CB 2047 C CG1 . ILE A 275 ? 0.4156 0.3936 0.5550 -0.0897 0.0361 0.1020 414 ILE A CG1 2048 C CG2 . ILE A 275 ? 0.4677 0.4208 0.5710 -0.0703 0.0312 0.0858 414 ILE A CG2 2049 C CD1 . ILE A 275 ? 0.4018 0.3899 0.5520 -0.0884 0.0304 0.0919 414 ILE A CD1 2050 N N . THR A 276 ? 0.4482 0.3839 0.5173 -0.0631 0.0464 0.1044 415 THR A N 2051 C CA . THR A 276 ? 0.4729 0.4011 0.5217 -0.0508 0.0480 0.0995 415 THR A CA 2052 C C . THR A 276 ? 0.4430 0.3565 0.4845 -0.0450 0.0374 0.0867 415 THR A C 2053 O O . THR A 276 ? 0.4988 0.3928 0.5368 -0.0482 0.0289 0.0859 415 THR A O 2054 C CB . THR A 276 ? 0.5368 0.4507 0.5707 -0.0508 0.0514 0.1096 415 THR A CB 2055 O OG1 . THR A 276 ? 0.5428 0.4726 0.5820 -0.0550 0.0630 0.1220 415 THR A OG1 2056 C CG2 . THR A 276 ? 0.5848 0.4899 0.5982 -0.0376 0.0512 0.1033 415 THR A CG2 2057 N N . LEU A 277 ? 0.4344 0.3575 0.4736 -0.0364 0.0377 0.0770 416 LEU A N 2058 C CA . LEU A 277 ? 0.3931 0.3062 0.4260 -0.0302 0.0294 0.0653 416 LEU A CA 2059 C C . LEU A 277 ? 0.4208 0.3219 0.4361 -0.0208 0.0287 0.0633 416 LEU A C 2060 O O . LEU A 277 ? 0.3938 0.3015 0.4019 -0.0152 0.0351 0.0659 416 LEU A O 2061 C CB . LEU A 277 ? 0.3670 0.2962 0.4063 -0.0262 0.0299 0.0567 416 LEU A CB 2062 C CG . LEU A 277 ? 0.3768 0.3217 0.4330 -0.0333 0.0317 0.0584 416 LEU A CG 2063 C CD1 . LEU A 277 ? 0.3155 0.2737 0.3741 -0.0279 0.0320 0.0502 416 LEU A CD1 2064 C CD2 . LEU A 277 ? 0.3793 0.3147 0.4445 -0.0419 0.0237 0.0580 416 LEU A CD2 2065 N N . PRO A 278 ? 0.4107 0.2938 0.4187 -0.0184 0.0203 0.0583 417 PRO A N 2066 C CA . PRO A 278 ? 0.4402 0.3130 0.4329 -0.0087 0.0185 0.0549 417 PRO A CA 2067 C C . PRO A 278 ? 0.4093 0.2941 0.4021 -0.0003 0.0185 0.0451 417 PRO A C 2068 O O . PRO A 278 ? 0.3746 0.2662 0.3755 -0.0009 0.0155 0.0379 417 PRO A O 2069 C CB . PRO A 278 ? 0.4619 0.3136 0.4493 -0.0087 0.0087 0.0517 417 PRO A CB 2070 C CG . PRO A 278 ? 0.4778 0.3323 0.4776 -0.0150 0.0042 0.0477 417 PRO A CG 2071 C CD . PRO A 278 ? 0.4495 0.3205 0.4624 -0.0236 0.0113 0.0549 417 PRO A CD 2072 N N . CYS A 279 ? 0.4118 0.2987 0.3953 0.0072 0.0216 0.0453 418 CYS A N 2073 C CA . CYS A 279 ? 0.4009 0.2986 0.3849 0.0144 0.0212 0.0373 418 CYS A CA 2074 C C . CYS A 279 ? 0.3852 0.2727 0.3574 0.0235 0.0169 0.0335 418 CYS A C 2075 O O . CYS A 279 ? 0.3655 0.2382 0.3271 0.0252 0.0155 0.0379 418 CYS A O 2076 C CB . CYS A 279 ? 0.4572 0.3701 0.4432 0.0152 0.0282 0.0404 418 CYS A CB 2077 S SG . CYS A 279 ? 0.4605 0.3887 0.4618 0.0059 0.0333 0.0442 418 CYS A SG 2078 N N . LYS A 280 ? 0.3644 0.2603 0.3392 0.0291 0.0146 0.0257 419 LYS A N 2079 C CA . LYS A 280 ? 0.3845 0.2745 0.3510 0.0379 0.0103 0.0217 419 LYS A CA 2080 C C . LYS A 280 ? 0.4151 0.3188 0.3850 0.0419 0.0111 0.0177 419 LYS A C 2081 O O . LYS A 280 ? 0.3656 0.2824 0.3458 0.0388 0.0122 0.0144 419 LYS A O 2082 C CB . LYS A 280 ? 0.4920 0.3749 0.4595 0.0409 0.0034 0.0148 419 LYS A CB 2083 C CG . LYS A 280 ? 0.5931 0.4771 0.5581 0.0500 -0.0012 0.0085 419 LYS A CG 2084 C CD . LYS A 280 ? 0.6581 0.5339 0.6226 0.0544 -0.0078 0.0023 419 LYS A CD 2085 C CE . LYS A 280 ? 0.6162 0.5015 0.5851 0.0620 -0.0114 -0.0051 419 LYS A CE 2086 N NZ . LYS A 280 ? 0.4222 0.3089 0.3866 0.0660 -0.0115 -0.0031 419 LYS A NZ 2087 N N . ILE A 281 ? 0.3651 0.2647 0.3257 0.0487 0.0097 0.0182 420 ILE A N 2088 C CA . ILE A 281 ? 0.3028 0.2123 0.2662 0.0530 0.0078 0.0138 420 ILE A CA 2089 C C . ILE A 281 ? 0.3743 0.2849 0.3428 0.0570 0.0014 0.0065 420 ILE A C 2090 O O . ILE A 281 ? 0.4453 0.3447 0.4073 0.0619 -0.0030 0.0052 420 ILE A O 2091 C CB . ILE A 281 ? 0.3790 0.2825 0.3296 0.0595 0.0077 0.0168 420 ILE A CB 2092 C CG1 . ILE A 281 ? 0.3997 0.3049 0.3454 0.0566 0.0153 0.0242 420 ILE A CG1 2093 C CG2 . ILE A 281 ? 0.3342 0.2455 0.2880 0.0640 0.0032 0.0115 420 ILE A CG2 2094 C CD1 . ILE A 281 ? 0.4422 0.3401 0.3720 0.0640 0.0161 0.0277 420 ILE A CD1 2095 N N . LYS A 282 ? 0.3662 0.2909 0.3463 0.0551 0.0009 0.0020 421 LYS A N 2096 C CA . LYS A 282 ? 0.3871 0.3169 0.3741 0.0586 -0.0040 -0.0045 421 LYS A CA 2097 C C . LYS A 282 ? 0.3395 0.2768 0.3299 0.0621 -0.0077 -0.0068 421 LYS A C 2098 O O . LYS A 282 ? 0.3368 0.2802 0.3288 0.0597 -0.0062 -0.0050 421 LYS A O 2099 C CB . LYS A 282 ? 0.3957 0.3364 0.3935 0.0538 -0.0019 -0.0077 421 LYS A CB 2100 C CG . LYS A 282 ? 0.4122 0.3439 0.4076 0.0530 -0.0022 -0.0086 421 LYS A CG 2101 C CD . LYS A 282 ? 0.4146 0.3567 0.4187 0.0499 -0.0010 -0.0127 421 LYS A CD 2102 C CE . LYS A 282 ? 0.4858 0.4301 0.4924 0.0563 -0.0048 -0.0193 421 LYS A CE 2103 N NZ . LYS A 282 ? 0.4998 0.4524 0.5108 0.0617 -0.0074 -0.0218 421 LYS A NZ 2104 N N . GLN A 283 ? 0.3262 0.2625 0.3183 0.0681 -0.0135 -0.0109 422 GLN A N 2105 C CA . GLN A 283 ? 0.3240 0.2677 0.3219 0.0710 -0.0186 -0.0133 422 GLN A CA 2106 C C . GLN A 283 ? 0.2976 0.2594 0.3117 0.0675 -0.0182 -0.0168 422 GLN A C 2107 O O . GLN A 283 ? 0.3686 0.3400 0.3902 0.0653 -0.0202 -0.0168 422 GLN A O 2108 C CB . GLN A 283 ? 0.3114 0.2458 0.3040 0.0794 -0.0257 -0.0159 422 GLN A CB 2109 C CG . GLN A 283 ? 0.3507 0.2671 0.3254 0.0838 -0.0269 -0.0120 422 GLN A CG 2110 C CD . GLN A 283 ? 0.4580 0.3629 0.4258 0.0924 -0.0344 -0.0146 422 GLN A CD 2111 O OE1 . GLN A 283 ? 0.5402 0.4309 0.4969 0.0950 -0.0342 -0.0129 422 GLN A OE1 2112 N NE2 . GLN A 283 ? 0.4066 0.3171 0.3813 0.0967 -0.0418 -0.0186 422 GLN A NE2 2113 N N . ILE A 284 ? 0.2872 0.2530 0.3057 0.0672 -0.0159 -0.0194 423 ILE A N 2114 C CA . ILE A 284 ? 0.2559 0.2396 0.2881 0.0648 -0.0144 -0.0225 423 ILE A CA 2115 C C . ILE A 284 ? 0.3357 0.3246 0.3693 0.0577 -0.0081 -0.0206 423 ILE A C 2116 O O . ILE A 284 ? 0.3402 0.3209 0.3675 0.0567 -0.0055 -0.0203 423 ILE A O 2117 C CB . ILE A 284 ? 0.3041 0.2908 0.3402 0.0710 -0.0163 -0.0277 423 ILE A CB 2118 C CG1 . ILE A 284 ? 0.3267 0.3090 0.3627 0.0785 -0.0235 -0.0299 423 ILE A CG1 2119 C CG2 . ILE A 284 ? 0.3595 0.3668 0.4092 0.0690 -0.0132 -0.0304 423 ILE A CG2 2120 C CD1 . ILE A 284 ? 0.3777 0.3614 0.4165 0.0862 -0.0264 -0.0356 423 ILE A CD1 2121 N N . ILE A 285 ? 0.3164 0.3181 0.3581 0.0526 -0.0067 -0.0194 424 ILE A N 2122 C CA . ILE A 285 ? 0.3548 0.3599 0.3964 0.0458 -0.0019 -0.0171 424 ILE A CA 2123 C C . ILE A 285 ? 0.3020 0.3239 0.3537 0.0422 0.0005 -0.0181 424 ILE A C 2124 O O . ILE A 285 ? 0.3293 0.3621 0.3901 0.0420 -0.0017 -0.0182 424 ILE A O 2125 C CB . ILE A 285 ? 0.4375 0.4378 0.4749 0.0427 -0.0026 -0.0130 424 ILE A CB 2126 C CG1 . ILE A 285 ? 0.5131 0.4986 0.5390 0.0445 -0.0014 -0.0107 424 ILE A CG1 2127 C CG2 . ILE A 285 ? 0.5301 0.5384 0.5712 0.0360 0.0003 -0.0112 424 ILE A CG2 2128 C CD1 . ILE A 285 ? 0.5601 0.5358 0.5790 0.0505 -0.0057 -0.0102 424 ILE A CD1 2129 N N . ASN A 286 ? 0.2384 0.2621 0.2884 0.0391 0.0047 -0.0186 425 ASN A N 2130 C CA . ASN A 286 ? 0.2525 0.2903 0.3088 0.0347 0.0078 -0.0182 425 ASN A CA 2131 C C . ASN A 286 ? 0.2523 0.2901 0.3084 0.0282 0.0076 -0.0139 425 ASN A C 2132 O O . ASN A 286 ? 0.2465 0.2759 0.2964 0.0258 0.0085 -0.0124 425 ASN A O 2133 C CB . ASN A 286 ? 0.2719 0.3096 0.3242 0.0350 0.0113 -0.0209 425 ASN A CB 2134 C CG . ASN A 286 ? 0.3629 0.4025 0.4155 0.0424 0.0111 -0.0261 425 ASN A CG 2135 O OD1 . ASN A 286 ? 0.3110 0.3632 0.3715 0.0456 0.0111 -0.0276 425 ASN A OD1 2136 N ND2 . ASN A 286 ? 0.3187 0.3456 0.3632 0.0453 0.0103 -0.0288 425 ASN A ND2 2137 N N . MET A 287 ? 0.2204 0.2675 0.2839 0.0253 0.0057 -0.0117 426 MET A N 2138 C CA . MET A 287 ? 0.2230 0.2676 0.2855 0.0202 0.0034 -0.0079 426 MET A CA 2139 C C . MET A 287 ? 0.2485 0.2951 0.3082 0.0150 0.0067 -0.0065 426 MET A C 2140 O O . MET A 287 ? 0.2440 0.3001 0.3065 0.0132 0.0101 -0.0069 426 MET A O 2141 C CB . MET A 287 ? 0.2070 0.2596 0.2786 0.0179 -0.0010 -0.0058 426 MET A CB 2142 C CG . MET A 287 ? 0.2564 0.3036 0.3293 0.0231 -0.0067 -0.0071 426 MET A CG 2143 S SD . MET A 287 ? 0.3540 0.4108 0.4396 0.0188 -0.0132 -0.0042 426 MET A SD 2144 C CE . MET A 287 ? 0.9392 0.9860 1.0175 0.0138 -0.0168 -0.0008 426 MET A CE 2145 N N . TRP A 288 ? 0.2325 0.2704 0.2864 0.0133 0.0056 -0.0049 427 TRP A N 2146 C CA . TRP A 288 ? 0.2170 0.2555 0.2680 0.0088 0.0075 -0.0038 427 TRP A CA 2147 C C . TRP A 288 ? 0.1918 0.2381 0.2467 0.0035 0.0061 -0.0009 427 TRP A C 2148 O O . TRP A 288 ? 0.2248 0.2732 0.2772 -0.0002 0.0078 0.0001 427 TRP A O 2149 C CB . TRP A 288 ? 0.1928 0.2219 0.2382 0.0089 0.0064 -0.0029 427 TRP A CB 2150 C CG . TRP A 288 ? 0.2352 0.2597 0.2793 0.0102 0.0017 -0.0012 427 TRP A CG 2151 C CD1 . TRP A 288 ? 0.2388 0.2567 0.2799 0.0152 -0.0002 -0.0015 427 TRP A CD1 2152 C CD2 . TRP A 288 ? 0.2396 0.2639 0.2835 0.0070 -0.0026 0.0009 427 TRP A CD2 2153 N NE1 . TRP A 288 ? 0.2132 0.2272 0.2520 0.0160 -0.0054 -0.0003 427 TRP A NE1 2154 C CE2 . TRP A 288 ? 0.2499 0.2672 0.2908 0.0110 -0.0074 0.0012 427 TRP A CE2 2155 C CE3 . TRP A 288 ? 0.2475 0.2755 0.2924 0.0017 -0.0035 0.0027 427 TRP A CE3 2156 C CZ2 . TRP A 288 ? 0.2683 0.2817 0.3072 0.0099 -0.0137 0.0025 427 TRP A CZ2 2157 C CZ3 . TRP A 288 ? 0.2953 0.3193 0.3386 -0.0001 -0.0095 0.0047 427 TRP A CZ3 2158 C CH2 . TRP A 288 ? 0.2849 0.3015 0.3256 0.0041 -0.0149 0.0044 427 TRP A CH2 2159 N N . GLN A 289 ? 0.1853 0.2350 0.2460 0.0028 0.0023 0.0009 428 GLN A N 2160 C CA . GLN A 289 ? 0.1939 0.2511 0.2598 -0.0033 0.0005 0.0048 428 GLN A CA 2161 C C . GLN A 289 ? 0.2393 0.3107 0.3102 -0.0049 0.0062 0.0052 428 GLN A C 2162 O O . GLN A 289 ? 0.2581 0.3374 0.3322 -0.0107 0.0068 0.0093 428 GLN A O 2163 C CB . GLN A 289 ? 0.2270 0.2833 0.2990 -0.0040 -0.0064 0.0068 428 GLN A CB 2164 C CG . GLN A 289 ? 0.2710 0.3131 0.3361 -0.0011 -0.0126 0.0062 428 GLN A CG 2165 C CD . GLN A 289 ? 0.2991 0.3348 0.3612 0.0064 -0.0132 0.0028 428 GLN A CD 2166 O OE1 . GLN A 289 ? 0.2489 0.2855 0.3093 0.0098 -0.0078 0.0003 428 GLN A OE1 2167 N NE2 . GLN A 289 ? 0.3000 0.3278 0.3605 0.0092 -0.0204 0.0027 428 GLN A NE2 2168 N N . GLY A 290 ? 0.2355 0.3096 0.3060 0.0006 0.0104 0.0010 429 GLY A N 2169 C CA . GLY A 290 ? 0.2794 0.3665 0.3525 0.0015 0.0163 0.0001 429 GLY A CA 2170 C C . GLY A 290 ? 0.3085 0.4106 0.3940 0.0017 0.0167 0.0014 429 GLY A C 2171 O O . GLY A 290 ? 0.3280 0.4447 0.4174 0.0020 0.0220 0.0017 429 GLY A O 2172 N N . THR A 291 ? 0.2397 0.3387 0.3314 0.0021 0.0108 0.0021 430 THR A N 2173 C CA . THR A 291 ? 0.2499 0.3631 0.3559 0.0009 0.0093 0.0041 430 THR A CA 2174 C C . THR A 291 ? 0.3073 0.4260 0.4190 0.0091 0.0098 -0.0008 430 THR A C 2175 O O . THR A 291 ? 0.3285 0.4614 0.4538 0.0088 0.0087 0.0003 430 THR A O 2176 C CB . THR A 291 ? 0.3016 0.4082 0.4123 -0.0035 0.0006 0.0077 430 THR A CB 2177 O OG1 . THR A 291 ? 0.3609 0.4492 0.4617 0.0012 -0.0041 0.0045 430 THR A OG1 2178 C CG2 . THR A 291 ? 0.3480 0.4538 0.4571 -0.0125 -0.0007 0.0137 430 THR A CG2 2179 N N . GLY A 292 ? 0.2383 0.3458 0.3401 0.0161 0.0108 -0.0061 431 GLY A N 2180 C CA . GLY A 292 ? 0.2677 0.3777 0.3728 0.0245 0.0105 -0.0112 431 GLY A CA 2181 C C . GLY A 292 ? 0.2720 0.3628 0.3678 0.0298 0.0060 -0.0143 431 GLY A C 2182 O O . GLY A 292 ? 0.2602 0.3369 0.3448 0.0286 0.0063 -0.0140 431 GLY A O 2183 N N . GLN A 293 ? 0.2631 0.3538 0.3637 0.0357 0.0018 -0.0170 432 GLN A N 2184 C CA . GLN A 293 ? 0.3107 0.3828 0.4012 0.0414 -0.0024 -0.0195 432 GLN A CA 2185 C C . GLN A 293 ? 0.3253 0.3902 0.4171 0.0412 -0.0099 -0.0177 432 GLN A C 2186 O O . GLN A 293 ? 0.3691 0.4449 0.4732 0.0391 -0.0136 -0.0163 432 GLN A O 2187 C CB . GLN A 293 ? 0.2683 0.3404 0.3584 0.0503 -0.0025 -0.0250 432 GLN A CB 2188 C CG . GLN A 293 ? 0.3183 0.3901 0.4019 0.0527 0.0031 -0.0281 432 GLN A CG 2189 C CD . GLN A 293 ? 0.4756 0.5679 0.5676 0.0507 0.0088 -0.0281 432 GLN A CD 2190 O OE1 . GLN A 293 ? 0.5391 0.6487 0.6437 0.0531 0.0091 -0.0289 432 GLN A OE1 2191 N NE2 . GLN A 293 ? 0.4802 0.5715 0.5656 0.0467 0.0134 -0.0269 432 GLN A NE2 2192 N N . ALA A 294 ? 0.3142 0.3608 0.3932 0.0435 -0.0122 -0.0175 433 ALA A N 2193 C CA . ALA A 294 ? 0.3064 0.3432 0.3826 0.0453 -0.0195 -0.0164 433 ALA A CA 2194 C C . ALA A 294 ? 0.3491 0.3700 0.4134 0.0531 -0.0216 -0.0187 433 ALA A C 2195 O O . ALA A 294 ? 0.3699 0.3815 0.4240 0.0540 -0.0172 -0.0187 433 ALA A O 2196 C CB . ALA A 294 ? 0.3042 0.3344 0.3742 0.0402 -0.0201 -0.0128 433 ALA A CB 2197 N N . MET A 295 ? 0.2812 0.2981 0.3467 0.0584 -0.0289 -0.0203 434 MET A N 2198 C CA . MET A 295 ? 0.3070 0.3074 0.3597 0.0661 -0.0317 -0.0220 434 MET A CA 2199 C C . MET A 295 ? 0.3564 0.3430 0.3986 0.0685 -0.0376 -0.0202 434 MET A C 2200 O O . MET A 295 ? 0.4120 0.4019 0.4609 0.0685 -0.0448 -0.0206 434 MET A O 2201 C CB . MET A 295 ? 0.3243 0.3292 0.3842 0.0727 -0.0359 -0.0264 434 MET A CB 2202 C CG . MET A 295 ? 0.3850 0.3711 0.4304 0.0811 -0.0399 -0.0279 434 MET A CG 2203 S SD . MET A 295 ? 0.4931 0.4838 0.5465 0.0901 -0.0456 -0.0340 434 MET A SD 2204 C CE . MET A 295 ? 0.8236 0.8126 0.8815 0.0939 -0.0572 -0.0349 434 MET A CE 2205 N N . TYR A 296 ? 0.3137 0.2852 0.3396 0.0707 -0.0347 -0.0181 435 TYR A N 2206 C CA . TYR A 296 ? 0.3654 0.3234 0.3781 0.0745 -0.0390 -0.0164 435 TYR A CA 2207 C C . TYR A 296 ? 0.3552 0.2971 0.3538 0.0830 -0.0423 -0.0170 435 TYR A C 2208 O O . TYR A 296 ? 0.3387 0.2786 0.3372 0.0854 -0.0411 -0.0185 435 TYR A O 2209 C CB . TYR A 296 ? 0.3690 0.3238 0.3733 0.0706 -0.0324 -0.0125 435 TYR A CB 2210 C CG . TYR A 296 ? 0.3383 0.3056 0.3535 0.0630 -0.0308 -0.0117 435 TYR A CG 2211 C CD1 . TYR A 296 ? 0.3436 0.3222 0.3680 0.0567 -0.0243 -0.0114 435 TYR A CD1 2212 C CD2 . TYR A 296 ? 0.3097 0.2761 0.3249 0.0626 -0.0367 -0.0113 435 TYR A CD2 2213 C CE1 . TYR A 296 ? 0.3187 0.3076 0.3514 0.0500 -0.0232 -0.0103 435 TYR A CE1 2214 C CE2 . TYR A 296 ? 0.3085 0.2845 0.3326 0.0555 -0.0361 -0.0101 435 TYR A CE2 2215 C CZ . TYR A 296 ? 0.3102 0.2976 0.3429 0.0491 -0.0290 -0.0093 435 TYR A CZ 2216 O OH . TYR A 296 ? 0.3366 0.3325 0.3766 0.0421 -0.0286 -0.0077 435 TYR A OH 2217 N N . ALA A 297 ? 0.3739 0.3034 0.3592 0.0881 -0.0470 -0.0161 436 ALA A N 2218 C CA . ALA A 297 ? 0.3949 0.3074 0.3638 0.0967 -0.0504 -0.0160 436 ALA A CA 2219 C C . ALA A 297 ? 0.4112 0.3142 0.3658 0.0963 -0.0415 -0.0113 436 ALA A C 2220 O O . ALA A 297 ? 0.4073 0.3163 0.3640 0.0900 -0.0335 -0.0082 436 ALA A O 2221 C CB . ALA A 297 ? 0.5222 0.4244 0.4801 0.1032 -0.0588 -0.0167 436 ALA A CB 2222 N N . PRO A 298 ? 0.4331 0.3209 0.3737 0.1026 -0.0432 -0.0104 437 PRO A N 2223 C CA . PRO A 298 ? 0.4684 0.3458 0.3952 0.1017 -0.0354 -0.0047 437 PRO A CA 2224 C C . PRO A 298 ? 0.3612 0.2370 0.2772 0.1010 -0.0294 0.0004 437 PRO A C 2225 O O . PRO A 298 ? 0.4393 0.3160 0.3527 0.1044 -0.0336 -0.0013 437 PRO A O 2226 C CB . PRO A 298 ? 0.4955 0.3550 0.4070 0.1103 -0.0413 -0.0047 437 PRO A CB 2227 C CG . PRO A 298 ? 0.5456 0.4103 0.4695 0.1140 -0.0510 -0.0117 437 PRO A CG 2228 C CD . PRO A 298 ? 0.4631 0.3432 0.4015 0.1106 -0.0532 -0.0145 437 PRO A CD 2229 N N . PRO A 299 ? 0.4015 0.2748 0.3116 0.0968 -0.0202 0.0064 438 PRO A N 2230 C CA . PRO A 299 ? 0.4192 0.2947 0.3216 0.0959 -0.0129 0.0115 438 PRO A CA 2231 C C . PRO A 299 ? 0.4627 0.3259 0.3445 0.1057 -0.0156 0.0131 438 PRO A C 2232 O O . PRO A 299 ? 0.5066 0.3558 0.3765 0.1120 -0.0207 0.0129 438 PRO A O 2233 C CB . PRO A 299 ? 0.4303 0.3038 0.3310 0.0897 -0.0040 0.0181 438 PRO A CB 2234 C CG . PRO A 299 ? 0.5084 0.3816 0.4198 0.0858 -0.0069 0.0151 438 PRO A CG 2235 C CD . PRO A 299 ? 0.4480 0.3161 0.3588 0.0931 -0.0169 0.0088 438 PRO A CD 2236 N N . ILE A 300 ? 0.5068 0.3745 0.3835 0.1078 -0.0126 0.0143 439 ILE A N 2237 C CA . ILE A 300 ? 0.5616 0.4181 0.4162 0.1181 -0.0135 0.0162 439 ILE A CA 2238 C C . ILE A 300 ? 0.5490 0.3965 0.3882 0.1190 -0.0052 0.0245 439 ILE A C 2239 O O . ILE A 300 ? 0.5021 0.3537 0.3494 0.1105 0.0019 0.0291 439 ILE A O 2240 C CB . ILE A 300 ? 0.5743 0.4393 0.4270 0.1202 -0.0105 0.0161 439 ILE A CB 2241 C CG1 . ILE A 300 ? 0.4977 0.3762 0.3601 0.1115 0.0017 0.0215 439 ILE A CG1 2242 C CG2 . ILE A 300 ? 0.5889 0.4595 0.4539 0.1199 -0.0202 0.0086 439 ILE A CG2 2243 C CD1 . ILE A 300 ? 0.5387 0.4265 0.3995 0.1142 0.0052 0.0213 439 ILE A CD1 2244 N N . ASP A 301 ? 0.5511 0.3856 0.3673 0.1294 -0.0064 0.0266 440 ASP A N 2245 C CA . ASP A 301 ? 0.6280 0.4532 0.4267 0.1308 0.0019 0.0357 440 ASP A CA 2246 C C . ASP A 301 ? 0.5895 0.4267 0.3866 0.1282 0.0151 0.0428 440 ASP A C 2247 O O . ASP A 301 ? 0.6050 0.4544 0.4085 0.1292 0.0163 0.0396 440 ASP A O 2248 C CB . ASP A 301 ? 0.7535 0.5598 0.5260 0.1438 -0.0044 0.0354 440 ASP A CB 2249 C CG . ASP A 301 ? 0.8954 0.6882 0.6679 0.1463 -0.0163 0.0304 440 ASP A CG 2250 O OD1 . ASP A 301 ? 0.8617 0.6557 0.6476 0.1382 -0.0160 0.0310 440 ASP A OD1 2251 O OD2 . ASP A 301 ? 0.9924 0.7731 0.7513 0.1570 -0.0265 0.0256 440 ASP A OD2 2252 N N . GLY A 302 ? 0.6587 0.4924 0.4476 0.1248 0.0246 0.0527 441 GLY A N 2253 C CA . GLY A 302 ? 0.6891 0.5352 0.4758 0.1230 0.0378 0.0607 441 GLY A CA 2254 C C . GLY A 302 ? 0.6640 0.5267 0.4747 0.1093 0.0451 0.0640 441 GLY A C 2255 O O . GLY A 302 ? 0.5482 0.4103 0.3747 0.1007 0.0407 0.0612 441 GLY A O 2256 N N . LYS A 303 ? 0.7188 0.5966 0.5318 0.1080 0.0560 0.0696 442 LYS A N 2257 C CA . LYS A 303 ? 0.6811 0.5754 0.5167 0.0954 0.0629 0.0731 442 LYS A CA 2258 C C . LYS A 303 ? 0.5551 0.4622 0.4081 0.0939 0.0581 0.0638 442 LYS A C 2259 O O . LYS A 303 ? 0.5641 0.4793 0.4136 0.1012 0.0588 0.0604 442 LYS A O 2260 C CB . LYS A 303 ? 0.6922 0.5992 0.5245 0.0945 0.0769 0.0837 442 LYS A CB 2261 C CG . LYS A 303 ? 0.6744 0.5976 0.5304 0.0807 0.0838 0.0889 442 LYS A CG 2262 C CD . LYS A 303 ? 0.7242 0.6663 0.5812 0.0818 0.0970 0.0968 442 LYS A CD 2263 C CE . LYS A 303 ? 0.7961 0.7495 0.6508 0.0928 0.0960 0.0888 442 LYS A CE 2264 N NZ . LYS A 303 ? 0.8565 0.8308 0.7133 0.0953 0.1089 0.0955 442 LYS A NZ 2265 N N . ILE A 304 ? 0.5262 0.4341 0.3968 0.0849 0.0528 0.0596 443 ILE A N 2266 C CA . ILE A 304 ? 0.4575 0.3775 0.3449 0.0819 0.0488 0.0520 443 ILE A CA 2267 C C . ILE A 304 ? 0.4749 0.4107 0.3795 0.0719 0.0568 0.0566 443 ILE A C 2268 O O . ILE A 304 ? 0.5336 0.4679 0.4478 0.0623 0.0582 0.0602 443 ILE A O 2269 C CB . ILE A 304 ? 0.3919 0.3055 0.2885 0.0787 0.0387 0.0445 443 ILE A CB 2270 C CG1 . ILE A 304 ? 0.4547 0.3521 0.3358 0.0877 0.0305 0.0409 443 ILE A CG1 2271 C CG2 . ILE A 304 ? 0.3676 0.2927 0.2783 0.0767 0.0345 0.0372 443 ILE A CG2 2272 C CD1 . ILE A 304 ? 0.4347 0.3266 0.3249 0.0848 0.0216 0.0348 443 ILE A CD1 2273 N N . ASN A 305 ? 0.4102 0.3604 0.3186 0.0745 0.0611 0.0561 444 ASN A N 2274 C CA . ASN A 305 ? 0.4420 0.4087 0.3667 0.0661 0.0689 0.0608 444 ASN A CA 2275 C C . ASN A 305 ? 0.4395 0.4197 0.3765 0.0662 0.0665 0.0542 444 ASN A C 2276 O O . ASN A 305 ? 0.4757 0.4573 0.4044 0.0757 0.0639 0.0496 444 ASN A O 2277 C CB . ASN A 305 ? 0.4671 0.4410 0.3840 0.0687 0.0804 0.0707 444 ASN A CB 2278 C CG . ASN A 305 ? 0.5215 0.5148 0.4571 0.0602 0.0885 0.0760 444 ASN A CG 2279 O OD1 . ASN A 305 ? 0.5666 0.5607 0.5156 0.0485 0.0897 0.0805 444 ASN A OD1 2280 N ND2 . ASN A 305 ? 0.5052 0.5142 0.4421 0.0666 0.0933 0.0751 444 ASN A ND2 2281 N N . CYS A 306 ? 0.4201 0.4084 0.3759 0.0558 0.0663 0.0538 445 CYS A N 2282 C CA . CYS A 306 ? 0.4076 0.4088 0.3756 0.0548 0.0646 0.0488 445 CYS A CA 2283 C C . CYS A 306 ? 0.3672 0.3827 0.3521 0.0457 0.0711 0.0542 445 CYS A C 2284 O O . CYS A 306 ? 0.3584 0.3709 0.3531 0.0358 0.0704 0.0565 445 CYS A O 2285 C CB . CYS A 306 ? 0.4377 0.4333 0.4119 0.0516 0.0548 0.0407 445 CYS A CB 2286 S SG . CYS A 306 ? 0.5544 0.5385 0.5145 0.0618 0.0455 0.0332 445 CYS A SG 2287 N N . VAL A 307 ? 0.3246 0.3556 0.3132 0.0494 0.0768 0.0560 446 VAL A N 2288 C CA . VAL A 307 ? 0.3031 0.3502 0.3107 0.0411 0.0818 0.0601 446 VAL A CA 2289 C C . VAL A 307 ? 0.2726 0.3273 0.2904 0.0412 0.0759 0.0523 446 VAL A C 2290 O O . VAL A 307 ? 0.3183 0.3769 0.3295 0.0507 0.0744 0.0478 446 VAL A O 2291 C CB . VAL A 307 ? 0.3269 0.3896 0.3342 0.0449 0.0932 0.0681 446 VAL A CB 2292 C CG1 . VAL A 307 ? 0.3375 0.4183 0.3676 0.0352 0.0977 0.0728 446 VAL A CG1 2293 C CG2 . VAL A 307 ? 0.3484 0.4021 0.3419 0.0459 0.0993 0.0765 446 VAL A CG2 2294 N N . SER A 308 ? 0.2923 0.3475 0.3246 0.0311 0.0717 0.0506 447 SER A N 2295 C CA . SER A 308 ? 0.2693 0.3293 0.3099 0.0305 0.0653 0.0434 447 SER A CA 2296 C C . SER A 308 ? 0.2719 0.3456 0.3320 0.0222 0.0672 0.0458 447 SER A C 2297 O O . SER A 308 ? 0.2994 0.3755 0.3680 0.0144 0.0714 0.0525 447 SER A O 2298 C CB . SER A 308 ? 0.2855 0.3314 0.3232 0.0273 0.0566 0.0373 447 SER A CB 2299 O OG . SER A 308 ? 0.3377 0.3710 0.3600 0.0336 0.0543 0.0356 447 SER A OG 2300 N N . ASN A 309 ? 0.2477 0.3295 0.3149 0.0237 0.0631 0.0406 448 ASN A N 2301 C CA . ASN A 309 ? 0.2429 0.3358 0.3288 0.0158 0.0622 0.0412 448 ASN A CA 2302 C C . ASN A 309 ? 0.2363 0.3179 0.3247 0.0088 0.0538 0.0362 448 ASN A C 2303 O O . ASN A 309 ? 0.2280 0.3018 0.3083 0.0123 0.0477 0.0299 448 ASN A O 2304 C CB . ASN A 309 ? 0.2415 0.3483 0.3330 0.0218 0.0611 0.0375 448 ASN A CB 2305 C CG . ASN A 309 ? 0.4136 0.5334 0.5017 0.0311 0.0692 0.0410 448 ASN A CG 2306 O OD1 . ASN A 309 ? 0.3156 0.4437 0.4081 0.0288 0.0780 0.0490 448 ASN A OD1 2307 N ND2 . ASN A 309 ? 0.5702 0.6912 0.6494 0.0419 0.0662 0.0354 448 ASN A ND2 2308 N N . ILE A 310 ? 0.2346 0.3151 0.3341 -0.0009 0.0531 0.0392 449 ILE A N 2309 C CA . ILE A 310 ? 0.2208 0.2934 0.3236 -0.0064 0.0450 0.0338 449 ILE A CA 2310 C C . ILE A 310 ? 0.2024 0.2868 0.3159 -0.0063 0.0416 0.0304 449 ILE A C 2311 O O . ILE A 310 ? 0.2246 0.3230 0.3522 -0.0088 0.0448 0.0342 449 ILE A O 2312 C CB . ILE A 310 ? 0.2464 0.3126 0.3569 -0.0160 0.0437 0.0371 449 ILE A CB 2313 C CG1 . ILE A 310 ? 0.2759 0.3300 0.3756 -0.0157 0.0468 0.0411 449 ILE A CG1 2314 C CG2 . ILE A 310 ? 0.2729 0.3301 0.3840 -0.0198 0.0350 0.0306 449 ILE A CG2 2315 C CD1 . ILE A 310 ? 0.2918 0.3386 0.3986 -0.0249 0.0453 0.0455 449 ILE A CD1 2316 N N . THR A 311 ? 0.1436 0.2227 0.2507 -0.0033 0.0352 0.0236 450 THR A N 2317 C CA . THR A 311 ? 0.1179 0.2058 0.2324 -0.0020 0.0309 0.0200 450 THR A CA 2318 C C . THR A 311 ? 0.1795 0.2588 0.2942 -0.0069 0.0228 0.0150 450 THR A C 2319 O O . THR A 311 ? 0.2372 0.3215 0.3577 -0.0069 0.0178 0.0118 450 THR A O 2320 C CB . THR A 311 ? 0.2400 0.3299 0.3448 0.0078 0.0302 0.0167 450 THR A CB 2321 O OG1 . THR A 311 ? 0.2441 0.3198 0.3339 0.0101 0.0268 0.0136 450 THR A OG1 2322 C CG2 . THR A 311 ? 0.2776 0.3778 0.3818 0.0144 0.0381 0.0210 450 THR A CG2 2323 N N . GLY A 312 ? 0.2092 0.2757 0.3167 -0.0102 0.0213 0.0142 451 GLY A N 2324 C CA . GLY A 312 ? 0.2149 0.2728 0.3202 -0.0138 0.0145 0.0095 451 GLY A CA 2325 C C . GLY A 312 ? 0.2385 0.2849 0.3393 -0.0175 0.0143 0.0098 451 GLY A C 2326 O O . GLY A 312 ? 0.2174 0.2606 0.3145 -0.0166 0.0189 0.0132 451 GLY A O 2327 N N . ILE A 313 ? 0.1997 0.2393 0.2999 -0.0209 0.0084 0.0060 452 ILE A N 2328 C CA . ILE A 313 ? 0.2170 0.2448 0.3116 -0.0228 0.0069 0.0047 452 ILE A CA 2329 C C . ILE A 313 ? 0.2226 0.2440 0.3072 -0.0210 0.0022 -0.0011 452 ILE A C 2330 O O . ILE A 313 ? 0.2478 0.2713 0.3333 -0.0214 -0.0021 -0.0039 452 ILE A O 2331 C CB . ILE A 313 ? 0.2587 0.2833 0.3635 -0.0293 0.0036 0.0063 452 ILE A CB 2332 C CG1 . ILE A 313 ? 0.2523 0.2866 0.3698 -0.0326 0.0085 0.0134 452 ILE A CG1 2333 C CG2 . ILE A 313 ? 0.3005 0.3111 0.3978 -0.0300 0.0016 0.0049 452 ILE A CG2 2334 C CD1 . ILE A 313 ? 0.2802 0.3130 0.4110 -0.0406 0.0044 0.0160 452 ILE A CD1 2335 N N . LEU A 314 ? 0.2237 0.2377 0.2985 -0.0185 0.0033 -0.0028 453 LEU A N 2336 C CA . LEU A 314 ? 0.2010 0.2104 0.2663 -0.0166 0.0002 -0.0077 453 LEU A CA 2337 C C . LEU A 314 ? 0.2529 0.2526 0.3159 -0.0178 -0.0035 -0.0107 453 LEU A C 2338 O O . LEU A 314 ? 0.2488 0.2428 0.3112 -0.0175 -0.0022 -0.0096 453 LEU A O 2339 C CB . LEU A 314 ? 0.2086 0.2188 0.2657 -0.0125 0.0038 -0.0077 453 LEU A CB 2340 C CG . LEU A 314 ? 0.2679 0.2849 0.3255 -0.0106 0.0062 -0.0051 453 LEU A CG 2341 C CD1 . LEU A 314 ? 0.2736 0.2899 0.3244 -0.0072 0.0084 -0.0051 453 LEU A CD1 2342 C CD2 . LEU A 314 ? 0.2684 0.2891 0.3261 -0.0113 0.0027 -0.0064 453 LEU A CD2 2343 N N . LEU A 315 ? 0.2445 0.2409 0.3051 -0.0186 -0.0091 -0.0148 454 LEU A N 2344 C CA . LEU A 315 ? 0.2337 0.2192 0.2911 -0.0188 -0.0144 -0.0186 454 LEU A CA 2345 C C . LEU A 315 ? 0.2375 0.2191 0.2816 -0.0144 -0.0167 -0.0242 454 LEU A C 2346 O O . LEU A 315 ? 0.3095 0.2965 0.3490 -0.0132 -0.0159 -0.0248 454 LEU A O 2347 C CB . LEU A 315 ? 0.2332 0.2166 0.3007 -0.0241 -0.0209 -0.0184 454 LEU A CB 2348 C CG . LEU A 315 ? 0.2784 0.2669 0.3609 -0.0294 -0.0188 -0.0122 454 LEU A CG 2349 C CD1 . LEU A 315 ? 0.2701 0.2596 0.3647 -0.0348 -0.0257 -0.0122 454 LEU A CD1 2350 C CD2 . LEU A 315 ? 0.2886 0.2689 0.3705 -0.0303 -0.0171 -0.0097 454 LEU A CD2 2351 N N . THR A 316 ? 0.2566 0.2282 0.2938 -0.0116 -0.0197 -0.0283 455 THR A N 2352 C CA . THR A 316 ? 0.2568 0.2242 0.2809 -0.0066 -0.0225 -0.0342 455 THR A CA 2353 C C . THR A 316 ? 0.3557 0.3097 0.3781 -0.0069 -0.0317 -0.0387 455 THR A C 2354 O O . THR A 316 ? 0.3706 0.3167 0.3984 -0.0090 -0.0346 -0.0379 455 THR A O 2355 C CB . THR A 316 ? 0.3536 0.3223 0.3684 -0.0003 -0.0175 -0.0361 455 THR A CB 2356 O OG1 . THR A 316 ? 0.4691 0.4291 0.4852 0.0010 -0.0190 -0.0370 455 THR A OG1 2357 C CG2 . THR A 316 ? 0.3239 0.3048 0.3417 -0.0006 -0.0098 -0.0315 455 THR A CG2 2358 N N . ARG A 317 ? 0.3279 0.2783 0.3422 -0.0050 -0.0370 -0.0432 456 ARG A N 2359 C CA . ARG A 317 ? 0.3334 0.2698 0.3451 -0.0048 -0.0476 -0.0482 456 ARG A CA 2360 C C . ARG A 317 ? 0.4011 0.3279 0.3955 0.0039 -0.0499 -0.0552 456 ARG A C 2361 O O . ARG A 317 ? 0.4389 0.3719 0.4212 0.0098 -0.0445 -0.0571 456 ARG A O 2362 C CB . ARG A 317 ? 0.3240 0.2608 0.3368 -0.0073 -0.0538 -0.0495 456 ARG A CB 2363 C CG . ARG A 317 ? 0.3734 0.2952 0.3836 -0.0072 -0.0664 -0.0551 456 ARG A CG 2364 C CD . ARG A 317 ? 0.3862 0.3095 0.3998 -0.0100 -0.0728 -0.0559 456 ARG A CD 2365 N NE . ARG A 317 ? 0.3654 0.2934 0.3642 -0.0049 -0.0693 -0.0575 456 ARG A NE 2366 C CZ . ARG A 317 ? 0.4257 0.3444 0.4060 0.0016 -0.0746 -0.0637 456 ARG A CZ 2367 N NH1 . ARG A 317 ? 0.3914 0.2947 0.3653 0.0047 -0.0844 -0.0700 456 ARG A NH1 2368 N NH2 . ARG A 317 ? 0.4043 0.3282 0.3715 0.0053 -0.0704 -0.0635 456 ARG A NH2 2369 N N . ASP A 318 ? 0.4006 0.3125 0.3939 0.0049 -0.0579 -0.0589 457 ASP A N 2370 C CA . ASP A 318 ? 0.4667 0.3675 0.4427 0.0147 -0.0617 -0.0668 457 ASP A CA 2371 C C . ASP A 318 ? 0.4982 0.3955 0.4593 0.0202 -0.0664 -0.0728 457 ASP A C 2372 O O . ASP A 318 ? 0.4551 0.3478 0.4197 0.0158 -0.0741 -0.0733 457 ASP A O 2373 C CB . ASP A 318 ? 0.5214 0.4037 0.4993 0.0140 -0.0720 -0.0696 457 ASP A CB 2374 C CG . ASP A 318 ? 0.5502 0.4326 0.5350 0.0126 -0.0673 -0.0655 457 ASP A CG 2375 O OD1 . ASP A 318 ? 0.4910 0.3884 0.4825 0.0104 -0.0566 -0.0597 457 ASP A OD1 2376 O OD2 . ASP A 318 ? 0.5609 0.4268 0.5435 0.0140 -0.0752 -0.0683 457 ASP A OD2 2377 N N . GLY A 319 ? 0.5057 0.4059 0.4500 0.0300 -0.0617 -0.0772 458 GLY A N 2378 C CA . GLY A 319 ? 0.6189 0.5145 0.5452 0.0369 -0.0657 -0.0831 458 GLY A CA 2379 C C . GLY A 319 ? 0.7022 0.5770 0.6166 0.0438 -0.0784 -0.0921 458 GLY A C 2380 O O . GLY A 319 ? 0.7384 0.6034 0.6555 0.0452 -0.0823 -0.0942 458 GLY A O 2381 N N . GLY A 320 ? 0.7988 0.6649 0.6988 0.0482 -0.0860 -0.0976 459 GLY A N 2382 C CA . GLY A 320 ? 0.8991 0.7442 0.7838 0.0568 -0.0989 -0.1074 459 GLY A CA 2383 C C . GLY A 320 ? 0.9838 0.8107 0.8804 0.0496 -0.1142 -0.1087 459 GLY A C 2384 O O . GLY A 320 ? 1.0368 0.8443 0.9240 0.0557 -0.1255 -0.1161 459 GLY A O 2385 N N . ALA A 321 ? 1.0029 0.8361 0.9206 0.0368 -0.1149 -0.1015 460 ALA A N 2386 C CA . ALA A 321 ? 1.0255 0.8447 0.9581 0.0282 -0.1287 -0.1012 460 ALA A CA 2387 C C . ALA A 321 ? 1.0539 0.8670 0.9855 0.0261 -0.1399 -0.1041 460 ALA A C 2388 O O . ALA A 321 ? 1.0289 0.8350 0.9770 0.0171 -0.1508 -0.1025 460 ALA A O 2389 C CB . ALA A 321 ? 0.9824 0.8134 0.9411 0.0155 -0.1222 -0.0909 460 ALA A CB 2390 N N . ASN A 322 ? 1.1013 0.9174 1.0136 0.0344 -0.1372 -0.1080 461 ASN A N 2391 C CA . ASN A 322 ? 1.1688 0.9789 1.0768 0.0339 -0.1476 -0.1112 461 ASN A CA 2392 C C . ASN A 322 ? 1.1835 0.9686 1.0859 0.0364 -0.1675 -0.1196 461 ASN A C 2393 O O . ASN A 322 ? 1.1711 0.9501 1.0824 0.0309 -0.1797 -0.1205 461 ASN A O 2394 C CB . ASN A 322 ? 1.2166 1.0324 1.1005 0.0437 -0.1406 -0.1138 461 ASN A CB 2395 C CG . ASN A 322 ? 1.2343 1.0731 1.1228 0.0412 -0.1221 -0.1055 461 ASN A CG 2396 O OD1 . ASN A 322 ? 1.2486 1.0940 1.1209 0.0494 -0.1118 -0.1062 461 ASN A OD1 2397 N ND2 . ASN A 322 ? 1.2224 1.0740 1.1332 0.0301 -0.1183 -0.0976 461 ASN A ND2 2398 N N . ASN A 323 ? 1.1970 0.9672 1.0847 0.0453 -0.1717 -0.1262 462 ASN A N 2399 C CA . ASN A 323 ? 1.2109 0.9543 1.0908 0.0490 -0.1918 -0.1350 462 ASN A CA 2400 C C . ASN A 323 ? 1.1426 0.8780 1.0492 0.0355 -0.2022 -0.1306 462 ASN A C 2401 O O . ASN A 323 ? 1.1894 0.9038 1.0964 0.0343 -0.2211 -0.1360 462 ASN A O 2402 C CB . ASN A 323 ? 1.2854 1.0157 1.1398 0.0642 -0.1925 -0.1437 462 ASN A CB 2403 C CG . ASN A 323 ? 1.3067 1.0504 1.1667 0.0645 -0.1770 -0.1387 462 ASN A CG 2404 O OD1 . ASN A 323 ? 1.2680 1.0351 1.1372 0.0600 -0.1604 -0.1307 462 ASN A OD1 2405 N ND2 . ASN A 323 ? 1.3417 1.0694 1.1959 0.0700 -0.1836 -0.1436 462 ASN A ND2 2406 N N . THR A 324 ? 1.0121 0.7646 0.9411 0.0251 -0.1900 -0.1203 463 THR A N 2407 C CA . THR A 324 ? 0.9639 0.7114 0.9182 0.0119 -0.1969 -0.1142 463 THR A CA 2408 C C . THR A 324 ? 0.9077 0.6698 0.8891 -0.0020 -0.1973 -0.1063 463 THR A C 2409 O O . THR A 324 ? 0.9070 0.6820 0.8871 -0.0009 -0.1928 -0.1060 463 THR A O 2410 C CB . THR A 324 ? 0.9524 0.7082 0.9140 0.0094 -0.1839 -0.1076 463 THR A CB 2411 O OG1 . THR A 324 ? 0.8930 0.6754 0.8689 0.0031 -0.1667 -0.0982 463 THR A OG1 2412 C CG2 . THR A 324 ? 0.9460 0.6947 0.8815 0.0246 -0.1794 -0.1150 463 THR A CG2 2413 N N . SER A 325 ? 0.8846 0.6445 0.8906 -0.0148 -0.2030 -0.0998 464 SER A N 2414 C CA . SER A 325 ? 0.8391 0.6157 0.8741 -0.0282 -0.2023 -0.0914 464 SER A CA 2415 C C . SER A 325 ? 0.7124 0.5114 0.7640 -0.0352 -0.1840 -0.0802 464 SER A C 2416 O O . SER A 325 ? 0.6427 0.4568 0.7202 -0.0467 -0.1814 -0.0717 464 SER A O 2417 C CB . SER A 325 ? 0.9466 0.7086 1.0005 -0.0388 -0.2208 -0.0904 464 SER A CB 2418 O OG . SER A 325 ? 0.9645 0.7452 1.0480 -0.0512 -0.2199 -0.0823 464 SER A OG 2419 N N . ASN A 326 ? 0.6571 0.4585 0.6933 -0.0276 -0.1716 -0.0804 465 ASN A N 2420 C CA . ASN A 326 ? 0.6130 0.4328 0.6612 -0.0326 -0.1549 -0.0707 465 ASN A CA 2421 C C . ASN A 326 ? 0.5183 0.3551 0.5541 -0.0247 -0.1392 -0.0708 465 ASN A C 2422 O O . ASN A 326 ? 0.5340 0.3653 0.5473 -0.0137 -0.1393 -0.0785 465 ASN A O 2423 C CB . ASN A 326 ? 0.6560 0.4633 0.7013 -0.0326 -0.1546 -0.0690 465 ASN A CB 2424 C CG . ASN A 326 ? 0.7657 0.5523 0.8204 -0.0401 -0.1716 -0.0690 465 ASN A CG 2425 O OD1 . ASN A 326 ? 0.7879 0.5532 0.8293 -0.0351 -0.1797 -0.0739 465 ASN A OD1 2426 N ND2 . ASN A 326 ? 0.8258 0.6186 0.9039 -0.0520 -0.1777 -0.0636 465 ASN A ND2 2427 N N . GLU A 327 ? 0.4534 0.3106 0.5040 -0.0305 -0.1262 -0.0621 466 GLU A N 2428 C CA . GLU A 327 ? 0.4104 0.2824 0.4517 -0.0246 -0.1111 -0.0606 466 GLU A CA 2429 C C . GLU A 327 ? 0.4365 0.3147 0.4857 -0.0279 -0.1008 -0.0534 466 GLU A C 2430 O O . GLU A 327 ? 0.4553 0.3385 0.5239 -0.0374 -0.1001 -0.0459 466 GLU A O 2431 C CB . GLU A 327 ? 0.3976 0.2876 0.4470 -0.0272 -0.1059 -0.0574 466 GLU A CB 2432 C CG . GLU A 327 ? 0.4618 0.3463 0.5006 -0.0228 -0.1150 -0.0643 466 GLU A CG 2433 C CD . GLU A 327 ? 0.5403 0.4175 0.5516 -0.0111 -0.1131 -0.0714 466 GLU A CD 2434 O OE1 . GLU A 327 ? 0.4674 0.3491 0.4703 -0.0067 -0.1025 -0.0701 466 GLU A OE1 2435 O OE2 . GLU A 327 ? 0.5760 0.4437 0.5741 -0.0062 -0.1221 -0.0780 466 GLU A OE2 2436 N N . THR A 328 ? 0.4182 0.2966 0.4524 -0.0199 -0.0929 -0.0555 467 THR A N 2437 C CA . THR A 328 ? 0.4005 0.2822 0.4393 -0.0214 -0.0843 -0.0498 467 THR A CA 2438 C C . THR A 328 ? 0.3752 0.2764 0.4148 -0.0199 -0.0701 -0.0453 467 THR A C 2439 O O . THR A 328 ? 0.4003 0.3075 0.4280 -0.0133 -0.0659 -0.0490 467 THR A O 2440 C CB . THR A 328 ? 0.4372 0.3030 0.4598 -0.0132 -0.0875 -0.0556 467 THR A CB 2441 O OG1 . THR A 328 ? 0.5196 0.3650 0.5424 -0.0154 -0.1021 -0.0591 467 THR A OG1 2442 C CG2 . THR A 328 ? 0.4513 0.3204 0.4771 -0.0138 -0.0789 -0.0501 467 THR A CG2 2443 N N . PHE A 329 ? 0.3161 0.2265 0.3695 -0.0261 -0.0631 -0.0371 468 PHE A N 2444 C CA . PHE A 329 ? 0.3023 0.2296 0.3572 -0.0249 -0.0510 -0.0328 468 PHE A CA 2445 C C . PHE A 329 ? 0.3357 0.2624 0.3900 -0.0239 -0.0443 -0.0288 468 PHE A C 2446 O O . PHE A 329 ? 0.3483 0.2662 0.4085 -0.0283 -0.0473 -0.0253 468 PHE A O 2447 C CB . PHE A 329 ? 0.2788 0.2200 0.3499 -0.0317 -0.0486 -0.0270 468 PHE A CB 2448 C CG . PHE A 329 ? 0.2743 0.2168 0.3463 -0.0322 -0.0556 -0.0310 468 PHE A CG 2449 C CD1 . PHE A 329 ? 0.3012 0.2347 0.3808 -0.0370 -0.0667 -0.0327 468 PHE A CD1 2450 C CD2 . PHE A 329 ? 0.2966 0.2478 0.3613 -0.0281 -0.0519 -0.0329 468 PHE A CD2 2451 C CE1 . PHE A 329 ? 0.2962 0.2300 0.3761 -0.0369 -0.0742 -0.0368 468 PHE A CE1 2452 C CE2 . PHE A 329 ? 0.2825 0.2333 0.3462 -0.0280 -0.0590 -0.0366 468 PHE A CE2 2453 C CZ . PHE A 329 ? 0.2642 0.2063 0.3353 -0.0320 -0.0702 -0.0389 468 PHE A CZ 2454 N N . ARG A 330 ? 0.2848 0.2202 0.3318 -0.0183 -0.0359 -0.0289 469 ARG A N 2455 C CA . ARG A 330 ? 0.2571 0.1924 0.3024 -0.0162 -0.0298 -0.0258 469 ARG A CA 2456 C C . ARG A 330 ? 0.3166 0.2676 0.3652 -0.0159 -0.0205 -0.0214 469 ARG A C 2457 O O . ARG A 330 ? 0.3301 0.2899 0.3759 -0.0140 -0.0185 -0.0233 469 ARG A O 2458 C CB . ARG A 330 ? 0.3463 0.2739 0.3772 -0.0074 -0.0310 -0.0324 469 ARG A CB 2459 C CG . ARG A 330 ? 0.3372 0.2479 0.3610 -0.0051 -0.0414 -0.0388 469 ARG A CG 2460 C CD . ARG A 330 ? 0.3640 0.2699 0.3727 0.0056 -0.0416 -0.0461 469 ARG A CD 2461 N NE . ARG A 330 ? 0.4381 0.3280 0.4372 0.0098 -0.0522 -0.0536 469 ARG A NE 2462 C CZ . ARG A 330 ? 0.5388 0.4109 0.5335 0.0120 -0.0600 -0.0565 469 ARG A CZ 2463 N NH1 . ARG A 330 ? 0.5266 0.3947 0.5255 0.0103 -0.0581 -0.0520 469 ARG A NH1 2464 N NH2 . ARG A 330 ? 0.4904 0.3472 0.4752 0.0165 -0.0707 -0.0641 469 ARG A NH2 2465 N N . PRO A 331 ? 0.2982 0.2517 0.3519 -0.0178 -0.0154 -0.0154 470 PRO A N 2466 C CA . PRO A 331 ? 0.2817 0.2483 0.3371 -0.0166 -0.0077 -0.0119 470 PRO A CA 2467 C C . PRO A 331 ? 0.2931 0.2628 0.3384 -0.0099 -0.0051 -0.0161 470 PRO A C 2468 O O . PRO A 331 ? 0.3342 0.2966 0.3722 -0.0054 -0.0069 -0.0201 470 PRO A O 2469 C CB . PRO A 331 ? 0.3312 0.2962 0.3903 -0.0183 -0.0038 -0.0057 470 PRO A CB 2470 C CG . PRO A 331 ? 0.3966 0.3461 0.4521 -0.0185 -0.0089 -0.0069 470 PRO A CG 2471 C CD . PRO A 331 ? 0.3209 0.2639 0.3771 -0.0206 -0.0169 -0.0116 470 PRO A CD 2472 N N . GLY A 332 ? 0.3304 0.3111 0.3761 -0.0091 -0.0013 -0.0151 471 GLY A N 2473 C CA . GLY A 332 ? 0.3631 0.3485 0.4014 -0.0042 0.0012 -0.0178 471 GLY A CA 2474 C C . GLY A 332 ? 0.3444 0.3394 0.3848 -0.0041 0.0055 -0.0142 471 GLY A C 2475 O O . GLY A 332 ? 0.3042 0.3004 0.3490 -0.0051 0.0078 -0.0101 471 GLY A O 2476 N N . GLY A 333 ? 0.3391 0.3403 0.3756 -0.0027 0.0063 -0.0157 472 GLY A N 2477 C CA . GLY A 333 ? 0.3005 0.3089 0.3381 -0.0026 0.0088 -0.0127 472 GLY A CA 2478 C C . GLY A 333 ? 0.2865 0.2985 0.3209 0.0008 0.0110 -0.0135 472 GLY A C 2479 O O . GLY A 333 ? 0.2794 0.2907 0.3100 0.0035 0.0112 -0.0169 472 GLY A O 2480 N N . GLY A 334 ? 0.2627 0.2789 0.2989 0.0013 0.0123 -0.0107 473 GLY A N 2481 C CA . GLY A 334 ? 0.2226 0.2437 0.2584 0.0038 0.0137 -0.0110 473 GLY A CA 2482 C C . GLY A 334 ? 0.2213 0.2495 0.2571 0.0015 0.0134 -0.0091 473 GLY A C 2483 O O . GLY A 334 ? 0.2346 0.2677 0.2727 0.0022 0.0138 -0.0077 473 GLY A O 2484 N N . ASN A 335 ? 0.1976 0.2258 0.2310 -0.0016 0.0121 -0.0087 474 ASN A N 2485 C CA . ASN A 335 ? 0.2426 0.2748 0.2750 -0.0046 0.0107 -0.0059 474 ASN A CA 2486 C C . ASN A 335 ? 0.2319 0.2603 0.2659 -0.0054 0.0077 -0.0039 474 ASN A C 2487 O O . ASN A 335 ? 0.1939 0.2195 0.2273 -0.0064 0.0059 -0.0044 474 ASN A O 2488 C CB . ASN A 335 ? 0.2601 0.2929 0.2868 -0.0068 0.0102 -0.0066 474 ASN A CB 2489 C CG . ASN A 335 ? 0.2592 0.2943 0.2837 -0.0105 0.0082 -0.0029 474 ASN A CG 2490 O OD1 . ASN A 335 ? 0.3220 0.3580 0.3498 -0.0117 0.0066 0.0001 474 ASN A OD1 2491 N ND2 . ASN A 335 ? 0.3011 0.3357 0.3190 -0.0123 0.0075 -0.0029 474 ASN A ND2 2492 N N . ILE A 336 ? 0.2254 0.2420 0.2249 0.0073 0.0125 -0.0443 475 ILE A N 2493 C CA . ILE A 336 ? 0.2332 0.2372 0.2317 0.0037 0.0152 -0.0402 475 ILE A CA 2494 C C . ILE A 336 ? 0.2108 0.2189 0.2066 0.0042 0.0153 -0.0368 475 ILE A C 2495 O O . ILE A 336 ? 0.1954 0.1960 0.1920 0.0029 0.0169 -0.0354 475 ILE A O 2496 C CB . ILE A 336 ? 0.2688 0.2614 0.2613 0.0004 0.0168 -0.0344 475 ILE A CB 2497 C CG1 . ILE A 336 ? 0.2400 0.2282 0.2343 0.0009 0.0162 -0.0379 475 ILE A CG1 2498 C CG2 . ILE A 336 ? 0.2591 0.2383 0.2498 -0.0023 0.0196 -0.0311 475 ILE A CG2 2499 C CD1 . ILE A 336 ? 0.2707 0.2520 0.2719 0.0009 0.0168 -0.0434 475 ILE A CD1 2500 N N . LYS A 337 ? 0.2228 0.2433 0.2152 0.0067 0.0136 -0.0354 476 LYS A N 2501 C CA . LYS A 337 ? 0.2248 0.2489 0.2141 0.0083 0.0130 -0.0326 476 LYS A CA 2502 C C . LYS A 337 ? 0.2822 0.3082 0.2788 0.0108 0.0120 -0.0391 476 LYS A C 2503 O O . LYS A 337 ? 0.3043 0.3275 0.3000 0.0113 0.0122 -0.0372 476 LYS A O 2504 C CB . LYS A 337 ? 0.2407 0.2785 0.2246 0.0111 0.0117 -0.0301 476 LYS A CB 2505 C CG . LYS A 337 ? 0.2909 0.3272 0.2679 0.0074 0.0131 -0.0214 476 LYS A CG 2506 C CD . LYS A 337 ? 0.4039 0.4551 0.3759 0.0099 0.0126 -0.0183 476 LYS A CD 2507 C CE . LYS A 337 ? 0.4946 0.5455 0.4618 0.0051 0.0143 -0.0094 476 LYS A CE 2508 N NZ . LYS A 337 ? 0.4621 0.5289 0.4248 0.0072 0.0149 -0.0055 476 LYS A NZ 2509 N N . ASP A 338 ? 0.2715 0.3021 0.2759 0.0125 0.0104 -0.0471 477 ASP A N 2510 C CA . ASP A 338 ? 0.2740 0.3070 0.2878 0.0140 0.0090 -0.0540 477 ASP A CA 2511 C C . ASP A 338 ? 0.2560 0.2772 0.2740 0.0100 0.0124 -0.0523 477 ASP A C 2512 O O . ASP A 338 ? 0.2304 0.2538 0.2536 0.0110 0.0122 -0.0544 477 ASP A O 2513 C CB . ASP A 338 ? 0.2496 0.2874 0.2716 0.0156 0.0063 -0.0631 477 ASP A CB 2514 C CG . ASP A 338 ? 0.3465 0.3989 0.3651 0.0215 0.0023 -0.0669 477 ASP A CG 2515 O OD1 . ASP A 338 ? 0.3729 0.4338 0.3861 0.0249 0.0011 -0.0647 477 ASP A OD1 2516 O OD2 . ASP A 338 ? 0.3994 0.4544 0.4201 0.0232 0.0003 -0.0722 477 ASP A OD2 2517 N N . ASN A 339 ? 0.2745 0.2838 0.2898 0.0061 0.0156 -0.0484 478 ASN A N 2518 C CA . ASN A 339 ? 0.2384 0.2363 0.2553 0.0029 0.0195 -0.0458 478 ASN A CA 2519 C C . ASN A 339 ? 0.2152 0.2119 0.2265 0.0041 0.0201 -0.0409 478 ASN A C 2520 O O . ASN A 339 ? 0.2265 0.2217 0.2425 0.0042 0.0219 -0.0420 478 ASN A O 2521 C CB . ASN A 339 ? 0.2287 0.2137 0.2407 -0.0005 0.0222 -0.0418 478 ASN A CB 2522 C CG . ASN A 339 ? 0.2472 0.2304 0.2645 -0.0014 0.0216 -0.0465 478 ASN A CG 2523 O OD1 . ASN A 339 ? 0.2576 0.2497 0.2774 0.0011 0.0181 -0.0512 478 ASN A OD1 2524 N ND2 . ASN A 339 ? 0.2390 0.2099 0.2569 -0.0044 0.0249 -0.0451 478 ASN A ND2 2525 N N . TRP A 340 ? 0.2106 0.2078 0.2120 0.0050 0.0187 -0.0355 479 TRP A N 2526 C CA . TRP A 340 ? 0.2325 0.2263 0.2274 0.0063 0.0185 -0.0306 479 TRP A CA 2527 C C . TRP A 340 ? 0.2618 0.2664 0.2604 0.0109 0.0159 -0.0342 479 TRP A C 2528 O O . TRP A 340 ? 0.2313 0.2336 0.2296 0.0128 0.0160 -0.0335 479 TRP A O 2529 C CB . TRP A 340 ? 0.2363 0.2265 0.2202 0.0051 0.0174 -0.0233 479 TRP A CB 2530 C CG . TRP A 340 ? 0.2362 0.2200 0.2175 0.0013 0.0187 -0.0210 479 TRP A CG 2531 C CD1 . TRP A 340 ? 0.2686 0.2560 0.2455 -0.0001 0.0174 -0.0175 479 TRP A CD1 2532 C CD2 . TRP A 340 ? 0.2500 0.2233 0.2329 -0.0011 0.0212 -0.0219 479 TRP A CD2 2533 N NE1 . TRP A 340 ? 0.2613 0.2414 0.2375 -0.0030 0.0185 -0.0169 479 TRP A NE1 2534 C CE2 . TRP A 340 ? 0.2513 0.2220 0.2302 -0.0034 0.0207 -0.0194 479 TRP A CE2 2535 C CE3 . TRP A 340 ? 0.2237 0.1902 0.2108 -0.0014 0.0242 -0.0243 479 TRP A CE3 2536 C CZ2 . TRP A 340 ? 0.2286 0.1891 0.2066 -0.0053 0.0224 -0.0194 479 TRP A CZ2 2537 C CZ3 . TRP A 340 ? 0.3154 0.2717 0.3012 -0.0037 0.0266 -0.0236 479 TRP A CZ3 2538 C CH2 . TRP A 340 ? 0.3445 0.2972 0.3251 -0.0053 0.0254 -0.0213 479 TRP A CH2 2539 N N . ARG A 341 ? 0.2128 0.2296 0.2144 0.0133 0.0130 -0.0386 480 ARG A N 2540 C CA . ARG A 341 ? 0.2261 0.2539 0.2312 0.0184 0.0097 -0.0431 480 ARG A CA 2541 C C . ARG A 341 ? 0.2351 0.2636 0.2520 0.0185 0.0105 -0.0490 480 ARG A C 2542 O O . ARG A 341 ? 0.2256 0.2587 0.2441 0.0223 0.0088 -0.0504 480 ARG A O 2543 C CB . ARG A 341 ? 0.2351 0.2758 0.2423 0.0214 0.0064 -0.0485 480 ARG A CB 2544 C CG . ARG A 341 ? 0.3118 0.3586 0.3074 0.0244 0.0047 -0.0432 480 ARG A CG 2545 C CD . ARG A 341 ? 0.3485 0.4082 0.3448 0.0278 0.0021 -0.0485 480 ARG A CD 2546 N NE . ARG A 341 ? 0.4403 0.5040 0.4253 0.0284 0.0028 -0.0412 480 ARG A NE 2547 C CZ . ARG A 341 ? 0.4457 0.5123 0.4290 0.0267 0.0042 -0.0401 480 ARG A CZ 2548 N NH1 . ARG A 341 ? 0.4820 0.5466 0.4729 0.0250 0.0044 -0.0460 480 ARG A NH1 2549 N NH2 . ARG A 341 ? 0.5598 0.6317 0.5340 0.0268 0.0053 -0.0329 480 ARG A NH2 2550 N N . SER A 342 ? 0.2244 0.2486 0.2497 0.0143 0.0133 -0.0521 481 SER A N 2551 C CA . SER A 342 ? 0.2628 0.2889 0.3012 0.0132 0.0148 -0.0574 481 SER A CA 2552 C C . SER A 342 ? 0.2876 0.3083 0.3239 0.0137 0.0178 -0.0535 481 SER A C 2553 O O . SER A 342 ? 0.2794 0.3058 0.3262 0.0146 0.0184 -0.0577 481 SER A O 2554 C CB . SER A 342 ? 0.2889 0.3088 0.3350 0.0078 0.0179 -0.0596 481 SER A CB 2555 O OG . SER A 342 ? 0.3076 0.3141 0.3468 0.0044 0.0226 -0.0531 481 SER A OG 2556 N N . GLU A 343 ? 0.2631 0.2734 0.2866 0.0135 0.0192 -0.0459 482 GLU A N 2557 C CA . GLU A 343 ? 0.2405 0.2439 0.2600 0.0148 0.0215 -0.0423 482 GLU A CA 2558 C C . GLU A 343 ? 0.2894 0.2939 0.2997 0.0201 0.0176 -0.0393 482 GLU A C 2559 O O . GLU A 343 ? 0.3000 0.3036 0.3102 0.0236 0.0177 -0.0393 482 GLU A O 2560 C CB . GLU A 343 ? 0.3087 0.2971 0.3198 0.0112 0.0253 -0.0365 482 GLU A CB 2561 C CG . GLU A 343 ? 0.3303 0.3148 0.3490 0.0068 0.0302 -0.0384 482 GLU A CG 2562 C CD . GLU A 343 ? 0.3805 0.3690 0.4095 0.0073 0.0339 -0.0415 482 GLU A CD 2563 O OE1 . GLU A 343 ? 0.3785 0.3648 0.4033 0.0107 0.0348 -0.0396 482 GLU A OE1 2564 O OE2 . GLU A 343 ? 0.3747 0.3688 0.4165 0.0043 0.0359 -0.0460 482 GLU A OE2 2565 N N . LEU A 344 ? 0.2317 0.2383 0.2341 0.0210 0.0142 -0.0365 483 LEU A N 2566 C CA . LEU A 344 ? 0.2033 0.2084 0.1949 0.0252 0.0108 -0.0318 483 LEU A CA 2567 C C . LEU A 344 ? 0.2129 0.2315 0.2072 0.0312 0.0063 -0.0361 483 LEU A C 2568 O O . LEU A 344 ? 0.2731 0.2906 0.2580 0.0355 0.0032 -0.0322 483 LEU A O 2569 C CB . LEU A 344 ? 0.2241 0.2231 0.2044 0.0223 0.0103 -0.0245 483 LEU A CB 2570 C CG . LEU A 344 ? 0.2846 0.2686 0.2589 0.0176 0.0130 -0.0191 483 LEU A CG 2571 C CD1 . LEU A 344 ? 0.2772 0.2599 0.2450 0.0137 0.0125 -0.0138 483 LEU A CD1 2572 C CD2 . LEU A 344 ? 0.3166 0.2893 0.2833 0.0201 0.0120 -0.0152 483 LEU A CD2 2573 N N . TYR A 345 ? 0.2183 0.2486 0.2251 0.0316 0.0056 -0.0443 484 TYR A N 2574 C CA . TYR A 345 ? 0.2300 0.2743 0.2398 0.0375 0.0006 -0.0497 484 TYR A CA 2575 C C . TYR A 345 ? 0.2101 0.2565 0.2175 0.0442 -0.0025 -0.0499 484 TYR A C 2576 O O . TYR A 345 ? 0.2495 0.3042 0.2527 0.0503 -0.0073 -0.0513 484 TYR A O 2577 C CB . TYR A 345 ? 0.2071 0.2619 0.2331 0.0362 0.0000 -0.0596 484 TYR A CB 2578 C CG . TYR A 345 ? 0.2586 0.3156 0.2981 0.0357 0.0018 -0.0644 484 TYR A CG 2579 C CD1 . TYR A 345 ? 0.3151 0.3639 0.3604 0.0296 0.0077 -0.0631 484 TYR A CD1 2580 C CD2 . TYR A 345 ? 0.2836 0.3516 0.3297 0.0416 -0.0021 -0.0699 484 TYR A CD2 2581 C CE1 . TYR A 345 ? 0.3641 0.4162 0.4218 0.0289 0.0103 -0.0667 484 TYR A CE1 2582 C CE2 . TYR A 345 ? 0.3686 0.4407 0.4284 0.0410 0.0000 -0.0742 484 TYR A CE2 2583 C CZ . TYR A 345 ? 0.4076 0.4721 0.4733 0.0344 0.0066 -0.0724 484 TYR A CZ 2584 O OH . TYR A 345 ? 0.4626 0.5326 0.5422 0.0336 0.0097 -0.0761 484 TYR A OH 2585 N N . LYS A 346 ? 0.2636 0.3030 0.2732 0.0440 0.0000 -0.0488 485 LYS A N 2586 C CA . LYS A 346 ? 0.2819 0.3241 0.2909 0.0511 -0.0031 -0.0502 485 LYS A CA 2587 C C . LYS A 346 ? 0.2596 0.2887 0.2513 0.0543 -0.0047 -0.0415 485 LYS A C 2588 O O . LYS A 346 ? 0.3429 0.3713 0.3317 0.0609 -0.0076 -0.0418 485 LYS A O 2589 C CB . LYS A 346 ? 0.3261 0.3700 0.3480 0.0504 0.0005 -0.0548 485 LYS A CB 2590 C CG . LYS A 346 ? 0.3476 0.3765 0.3643 0.0460 0.0060 -0.0491 485 LYS A CG 2591 C CD . LYS A 346 ? 0.4396 0.4721 0.4676 0.0469 0.0098 -0.0532 485 LYS A CD 2592 C CE . LYS A 346 ? 0.5213 0.5682 0.5689 0.0435 0.0116 -0.0612 485 LYS A CE 2593 N NZ . LYS A 346 ? 0.5734 0.6250 0.6331 0.0432 0.0166 -0.0642 485 LYS A NZ 2594 N N . TYR A 347 ? 0.2013 0.2199 0.1819 0.0496 -0.0032 -0.0338 486 TYR A N 2595 C CA . TYR A 347 ? 0.2261 0.2303 0.1911 0.0509 -0.0047 -0.0249 486 TYR A CA 2596 C C . TYR A 347 ? 0.2406 0.2457 0.1940 0.0515 -0.0075 -0.0188 486 TYR A C 2597 O O . TYR A 347 ? 0.2733 0.2869 0.2289 0.0485 -0.0065 -0.0196 486 TYR A O 2598 C CB . TYR A 347 ? 0.2275 0.2166 0.1886 0.0443 -0.0007 -0.0198 486 TYR A CB 2599 C CG . TYR A 347 ? 0.2765 0.2628 0.2460 0.0437 0.0029 -0.0241 486 TYR A CG 2600 C CD1 . TYR A 347 ? 0.2610 0.2428 0.2288 0.0496 0.0017 -0.0252 486 TYR A CD1 2601 C CD2 . TYR A 347 ? 0.2914 0.2792 0.2696 0.0377 0.0077 -0.0268 486 TYR A CD2 2602 C CE1 . TYR A 347 ? 0.3076 0.2884 0.2828 0.0495 0.0057 -0.0288 486 TYR A CE1 2603 C CE2 . TYR A 347 ? 0.2681 0.2533 0.2529 0.0371 0.0118 -0.0298 486 TYR A CE2 2604 C CZ . TYR A 347 ? 0.2998 0.2823 0.2832 0.0430 0.0111 -0.0307 486 TYR A CZ 2605 O OH . TYR A 347 ? 0.3174 0.2990 0.3070 0.0429 0.0159 -0.0335 486 TYR A OH 2606 N N . LYS A 348 ? 0.2499 0.2459 0.1907 0.0557 -0.0107 -0.0124 487 LYS A N 2607 C CA . LYS A 348 ? 0.3020 0.2951 0.2299 0.0547 -0.0121 -0.0038 487 LYS A CA 2608 C C . LYS A 348 ? 0.3370 0.3112 0.2515 0.0551 -0.0141 0.0052 487 LYS A C 2609 O O . LYS A 348 ? 0.3544 0.3210 0.2678 0.0602 -0.0164 0.0035 487 LYS A O 2610 C CB . LYS A 348 ? 0.3323 0.3399 0.2579 0.0617 -0.0158 -0.0063 487 LYS A CB 2611 C CG . LYS A 348 ? 0.3410 0.3471 0.2613 0.0713 -0.0210 -0.0073 487 LYS A CG 2612 C CD . LYS A 348 ? 0.3710 0.3901 0.2855 0.0781 -0.0248 -0.0081 487 LYS A CD 2613 C CE . LYS A 348 ? 0.3990 0.4158 0.3058 0.0885 -0.0307 -0.0081 487 LYS A CE 2614 N NZ . LYS A 348 ? 0.3748 0.4036 0.2736 0.0955 -0.0345 -0.0081 487 LYS A NZ 2615 N N . VAL A 349 ? 0.3464 0.3133 0.2514 0.0497 -0.0133 0.0147 488 VAL A N 2616 C CA . VAL A 349 ? 0.3125 0.2600 0.2049 0.0489 -0.0156 0.0239 488 VAL A CA 2617 C C . VAL A 349 ? 0.3378 0.2847 0.2179 0.0551 -0.0196 0.0297 488 VAL A C 2618 O O . VAL A 349 ? 0.3657 0.3256 0.2435 0.0560 -0.0191 0.0313 488 VAL A O 2619 C CB . VAL A 349 ? 0.3814 0.3203 0.2709 0.0386 -0.0128 0.0317 488 VAL A CB 2620 C CG1 . VAL A 349 ? 0.3888 0.3074 0.2653 0.0370 -0.0159 0.0419 488 VAL A CG1 2621 C CG2 . VAL A 349 ? 0.4155 0.3522 0.3148 0.0334 -0.0095 0.0265 488 VAL A CG2 2622 N N . VAL A 350 ? 0.3693 0.3008 0.2406 0.0602 -0.0239 0.0328 489 VAL A N 2623 C CA . VAL A 350 ? 0.3863 0.3127 0.2434 0.0659 -0.0280 0.0402 489 VAL A CA 2624 C C . VAL A 350 ? 0.3797 0.2814 0.2247 0.0623 -0.0303 0.0506 489 VAL A C 2625 O O . VAL A 350 ? 0.4320 0.3201 0.2795 0.0594 -0.0305 0.0492 489 VAL A O 2626 C CB . VAL A 350 ? 0.3824 0.3151 0.2394 0.0784 -0.0329 0.0330 489 VAL A CB 2627 C CG1 . VAL A 350 ? 0.3391 0.2961 0.2094 0.0814 -0.0314 0.0221 489 VAL A CG1 2628 C CG2 . VAL A 350 ? 0.3703 0.2902 0.2293 0.0826 -0.0354 0.0286 489 VAL A CG2 2629 N N . GLN A 351 ? 0.4320 0.3274 0.2635 0.0624 -0.0320 0.0614 490 GLN A N 2630 C CA . GLN A 351 ? 0.4765 0.3468 0.2958 0.0594 -0.0351 0.0718 490 GLN A CA 2631 C C . GLN A 351 ? 0.5407 0.3993 0.3489 0.0711 -0.0418 0.0721 490 GLN A C 2632 O O . GLN A 351 ? 0.5228 0.3913 0.3251 0.0792 -0.0437 0.0723 490 GLN A O 2633 C CB . GLN A 351 ? 0.5556 0.4241 0.3667 0.0512 -0.0325 0.0851 490 GLN A CB 2634 C CG . GLN A 351 ? 0.6552 0.4966 0.4551 0.0460 -0.0358 0.0965 490 GLN A CG 2635 C CD . GLN A 351 ? 0.7776 0.6186 0.5726 0.0356 -0.0321 0.1099 490 GLN A CD 2636 O OE1 . GLN A 351 ? 0.7642 0.6247 0.5594 0.0351 -0.0278 0.1122 490 GLN A OE1 2637 N NE2 . GLN A 351 ? 0.8463 0.6653 0.6370 0.0272 -0.0339 0.1187 490 GLN A NE2 2638 N N . ILE A 352 ? 0.5230 0.3609 0.3279 0.0729 -0.0458 0.0716 491 ILE A N 2639 C CA . ILE A 352 ? 0.5498 0.3743 0.3436 0.0847 -0.0529 0.0717 491 ILE A CA 2640 C C . ILE A 352 ? 0.6266 0.4335 0.4026 0.0835 -0.0560 0.0862 491 ILE A C 2641 O O . ILE A 352 ? 0.6626 0.4536 0.4345 0.0730 -0.0551 0.0957 491 ILE A O 2642 C CB . ILE A 352 ? 0.5993 0.4065 0.3945 0.0877 -0.0563 0.0661 491 ILE A CB 2643 C CG1 . ILE A 352 ? 0.6294 0.4546 0.4415 0.0897 -0.0527 0.0524 491 ILE A CG1 2644 C CG2 . ILE A 352 ? 0.6891 0.4803 0.4713 0.1003 -0.0643 0.0671 491 ILE A CG2 2645 C CD1 . ILE A 352 ? 0.6831 0.4937 0.4970 0.0920 -0.0546 0.0470 491 ILE A CD1 2646 N N . GLU A 353 ? 0.6486 0.4582 0.4142 0.0939 -0.0598 0.0881 492 GLU A N 2647 C CA . GLU A 353 ? 0.7882 0.5809 0.5355 0.0936 -0.0626 0.1027 492 GLU A CA 2648 C C . GLU A 353 ? 0.9015 0.6658 0.6363 0.1012 -0.0709 0.1053 492 GLU A C 2649 O O . GLU A 353 ? 0.9737 0.7141 0.7041 0.0939 -0.0726 0.1120 492 GLU A O 2650 C CB . GLU A 353 ? 0.8564 0.6665 0.5964 0.1011 -0.0624 0.1048 492 GLU A CB 2651 C CG . GLU A 353 ? 0.9374 0.7338 0.6603 0.1145 -0.0702 0.1084 492 GLU A CG 2652 C CD . GLU A 353 ? 0.9916 0.8053 0.7060 0.1223 -0.0702 0.1105 492 GLU A CD 2653 O OE1 . GLU A 353 ? 1.0105 0.8428 0.7291 0.1156 -0.0637 0.1127 492 GLU A OE1 2654 O OE2 . GLU A 353 ? 0.9795 0.7886 0.6827 0.1360 -0.0770 0.1094 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 SER 242 375 375 SER SER 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 ? ? ? A . n A 1 270 GLY 270 409 ? ? ? A . n A 1 271 CYS 271 410 ? ? ? 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_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 179 A ASN 295 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 160 A ASN 276 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 223 A ASN 355 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 309 A ASN 448 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 259 A ASN 392 ? ASN 'GLYCOSYLATION SITE' 6 A ASN 125 A ASN 241 ? ASN 'GLYCOSYLATION SITE' 7 A ASN 253 A ASN 386 ? ASN 'GLYCOSYLATION SITE' 8 A ASN 202 A ASN 334 ? ASN 'GLYCOSYLATION SITE' 9 A ASN 118 A ASN 234 ? ASN 'GLYCOSYLATION SITE' 10 A ASN 146 A ASN 262 ? ASN 'GLYCOSYLATION SITE' 11 A ASN 173 A ASN 289 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O # _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 2012-05-02 2 'Structure model' 1 1 2012-05-09 3 'Structure model' 1 2 2012-06-20 # _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' 'Source and taxonomy' 2 3 'Structure model' 'Database references' # 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[2][2] _pdbx_refine_tls.S[3][3] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] 'X-RAY DIFFRACTION' 1 ? refined -16.0644 7.5518 18.7108 0.2843 0.2329 0.1787 0.0722 -0.0203 -0.0131 0.9575 1.1602 0.3802 -0.2036 -0.1177 0.3933 -0.1121 0.0215 0.0806 -0.0107 0.2193 0.0804 0.2076 -0.4875 -0.3309 'X-RAY DIFFRACTION' 2 ? refined -11.6447 -1.6295 14.0142 0.1525 0.1551 0.1469 0.0046 0.0081 -0.0156 1.0360 1.6109 1.4444 -0.4588 0.5459 -0.3381 -0.0785 0.0425 0.0386 0.0823 0.0379 -0.1200 0.0450 -0.1537 -0.0292 'X-RAY DIFFRACTION' 3 ? refined -15.7889 -21.2530 15.1461 0.1486 0.1421 0.2197 -0.0186 0.0166 0.0133 0.7842 1.1933 1.2209 -0.4603 0.7329 -0.0690 0.0118 0.0746 -0.0700 -0.0596 -0.2307 0.2267 0.0292 0.2208 -0.1408 'X-RAY DIFFRACTION' 4 ? refined -16.5335 0.3729 8.1739 0.1893 0.1927 0.1526 0.0305 0.0033 -0.0170 0.9118 0.8116 1.0621 -0.4622 0.3243 0.1662 0.0333 -0.1382 0.0984 0.2883 -0.0209 0.1287 -0.0541 -0.2077 -0.0741 # 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.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.selection_details _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection 'X-RAY DIFFRACTION' 1 1 A 44 A 948 'chain A and resi 44:89' ? ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 44 A 948 'chain A and resi 90:254' ? ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 44 A 948 'chain A and resi 255:474' ? ? ? ? ? 'X-RAY DIFFRACTION' 4 4 A 44 A 948 '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 REFMAC . ? program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 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 HKL-2000 . ? ? ? ? 'data collection' ? ? ? 4 HKL-2000 . ? ? ? ? 'data reduction' ? ? ? 5 HKL-2000 . ? ? ? ? 'data scaling' ? ? ? 6 PHASES . ? ? ? ? phasing ? ? ? 7 PHENIX 1.6.4_486 ? ? ? ? refinement ? ? ? # 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 ND2 A ASN 355 ? ? O5 A NAG 608 ? ? 1.90 2 1 O A HOH 871 ? ? O A HOH 877 ? ? 2.01 3 1 O A HOH 865 ? ? O A HOH 868 ? ? 2.04 4 1 NZ A LYS 231 ? ? OE1 A GLU 267 ? ? 2.04 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASP A 211 ? ? -167.86 105.66 2 1 GLN A 258 ? ? 70.15 -58.59 3 1 GLU A 268 ? ? -126.15 -101.01 4 1 ASN A 276 ? ? -165.43 93.66 5 1 PHE A 391 ? ? -108.37 60.85 # 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 12 1 Y 1 A LYS 408 ? A LYS 269 13 1 Y 1 A GLY 409 ? A GLY 270 14 1 Y 1 A CYS 410 ? A CYS 271 # 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 "N-[(1S,2S)-2-carbamimidamido-2,3-dihydro-1H-inden-1-yl]-N'-(4-chloro-3-fluorophenyl)ethanediamide" 0LK 5 water HOH # 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 1 601 734 NAG NAG A . C 2 NAG 1 602 741 NAG NAG A . D 2 NAG 1 603 762 NAG NAG A . E 2 NAG 1 604 776 NAG NAG A . F 2 NAG 1 605 789 NAG NAG A . G 2 NAG 1 606 795 NAG NAG A . H 2 NAG 1 607 834 NAG NAG A . I 2 NAG 1 608 855 NAG NAG A . J 2 NAG 1 609 886 NAG NAG A . K 2 NAG 1 610 892 NAG NAG A . L 2 NAG 1 611 948 NAG NAG A . M 3 EPE 1 612 1 EPE EPE A . N 4 0LK 1 613 1 0LK LIG A . O 5 HOH 1 501 174 HOH HOH A . O 5 HOH 2 502 164 HOH HOH A . O 5 HOH 3 503 133 HOH HOH A . O 5 HOH 4 504 13 HOH HOH A . O 5 HOH 5 505 32 HOH HOH A . O 5 HOH 6 701 1 HOH HOH A . O 5 HOH 7 702 2 HOH HOH A . O 5 HOH 8 703 3 HOH HOH A . O 5 HOH 9 704 4 HOH HOH A . O 5 HOH 10 705 5 HOH HOH A . O 5 HOH 11 706 6 HOH HOH A . O 5 HOH 12 707 7 HOH HOH A . O 5 HOH 13 708 8 HOH HOH A . O 5 HOH 14 709 9 HOH HOH A . O 5 HOH 15 710 10 HOH HOH A . O 5 HOH 16 711 11 HOH HOH A . O 5 HOH 17 712 12 HOH HOH A . O 5 HOH 18 714 14 HOH HOH A . O 5 HOH 19 715 15 HOH HOH A . O 5 HOH 20 716 16 HOH HOH A . O 5 HOH 21 717 17 HOH HOH A . O 5 HOH 22 718 18 HOH HOH A . O 5 HOH 23 719 19 HOH HOH A . O 5 HOH 24 720 20 HOH HOH A . O 5 HOH 25 721 21 HOH HOH A . O 5 HOH 26 722 22 HOH HOH A . O 5 HOH 27 723 23 HOH HOH A . O 5 HOH 28 724 24 HOH HOH A . O 5 HOH 29 725 25 HOH HOH A . O 5 HOH 30 726 26 HOH HOH A . O 5 HOH 31 727 27 HOH HOH A . O 5 HOH 32 728 28 HOH HOH A . O 5 HOH 33 729 29 HOH HOH A . O 5 HOH 34 730 30 HOH HOH A . O 5 HOH 35 731 31 HOH HOH A . O 5 HOH 36 733 33 HOH HOH A . O 5 HOH 37 734 34 HOH HOH A . O 5 HOH 38 735 35 HOH HOH A . O 5 HOH 39 736 36 HOH HOH A . O 5 HOH 40 737 37 HOH HOH A . O 5 HOH 41 738 38 HOH HOH A . O 5 HOH 42 739 39 HOH HOH A . O 5 HOH 43 740 40 HOH HOH A . O 5 HOH 44 741 41 HOH HOH A . O 5 HOH 45 742 42 HOH HOH A . O 5 HOH 46 743 43 HOH HOH A . O 5 HOH 47 744 44 HOH HOH A . O 5 HOH 48 745 45 HOH HOH A . O 5 HOH 49 746 46 HOH HOH A . O 5 HOH 50 747 47 HOH HOH A . O 5 HOH 51 748 48 HOH HOH A . O 5 HOH 52 749 49 HOH HOH A . O 5 HOH 53 750 50 HOH HOH A . O 5 HOH 54 751 51 HOH HOH A . O 5 HOH 55 752 52 HOH HOH A . O 5 HOH 56 753 53 HOH HOH A . O 5 HOH 57 754 54 HOH HOH A . O 5 HOH 58 755 55 HOH HOH A . O 5 HOH 59 756 56 HOH HOH A . O 5 HOH 60 757 57 HOH HOH A . O 5 HOH 61 758 58 HOH HOH A . O 5 HOH 62 759 59 HOH HOH A . O 5 HOH 63 760 60 HOH HOH A . O 5 HOH 64 761 61 HOH HOH A . O 5 HOH 65 762 62 HOH HOH A . O 5 HOH 66 763 63 HOH HOH A . O 5 HOH 67 764 64 HOH HOH A . O 5 HOH 68 765 65 HOH HOH A . O 5 HOH 69 766 66 HOH HOH A . O 5 HOH 70 767 67 HOH HOH A . O 5 HOH 71 768 68 HOH HOH A . O 5 HOH 72 769 69 HOH HOH A . O 5 HOH 73 770 70 HOH HOH A . O 5 HOH 74 771 71 HOH HOH A . O 5 HOH 75 772 72 HOH HOH A . O 5 HOH 76 773 73 HOH HOH A . O 5 HOH 77 774 74 HOH HOH A . O 5 HOH 78 775 75 HOH HOH A . O 5 HOH 79 776 76 HOH HOH A . O 5 HOH 80 777 77 HOH HOH A . O 5 HOH 81 778 78 HOH HOH A . O 5 HOH 82 779 79 HOH HOH A . O 5 HOH 83 780 80 HOH HOH A . O 5 HOH 84 781 81 HOH HOH A . O 5 HOH 85 782 82 HOH HOH A . O 5 HOH 86 783 83 HOH HOH A . O 5 HOH 87 784 84 HOH HOH A . O 5 HOH 88 785 85 HOH HOH A . O 5 HOH 89 786 86 HOH HOH A . O 5 HOH 90 787 87 HOH HOH A . O 5 HOH 91 788 88 HOH HOH A . O 5 HOH 92 789 89 HOH HOH A . O 5 HOH 93 790 90 HOH HOH A . O 5 HOH 94 791 91 HOH HOH A . O 5 HOH 95 792 92 HOH HOH A . O 5 HOH 96 793 93 HOH HOH A . O 5 HOH 97 794 94 HOH HOH A . O 5 HOH 98 795 95 HOH HOH A . O 5 HOH 99 796 96 HOH HOH A . O 5 HOH 100 797 97 HOH HOH A . O 5 HOH 101 798 98 HOH HOH A . O 5 HOH 102 799 99 HOH HOH A . O 5 HOH 103 800 100 HOH HOH A . O 5 HOH 104 801 101 HOH HOH A . O 5 HOH 105 802 102 HOH HOH A . O 5 HOH 106 803 103 HOH HOH A . O 5 HOH 107 804 104 HOH HOH A . O 5 HOH 108 805 106 HOH HOH A . O 5 HOH 109 806 107 HOH HOH A . O 5 HOH 110 807 108 HOH HOH A . O 5 HOH 111 808 109 HOH HOH A . O 5 HOH 112 809 110 HOH HOH A . O 5 HOH 113 810 111 HOH HOH A . O 5 HOH 114 811 112 HOH HOH A . O 5 HOH 115 812 113 HOH HOH A . O 5 HOH 116 813 114 HOH HOH A . O 5 HOH 117 814 115 HOH HOH A . O 5 HOH 118 815 116 HOH HOH A . O 5 HOH 119 816 117 HOH HOH A . O 5 HOH 120 817 118 HOH HOH A . O 5 HOH 121 818 119 HOH HOH A . O 5 HOH 122 819 120 HOH HOH A . O 5 HOH 123 820 121 HOH HOH A . O 5 HOH 124 821 122 HOH HOH A . O 5 HOH 125 822 123 HOH HOH A . O 5 HOH 126 823 124 HOH HOH A . O 5 HOH 127 824 125 HOH HOH A . O 5 HOH 128 825 126 HOH HOH A . O 5 HOH 129 826 127 HOH HOH A . O 5 HOH 130 827 128 HOH HOH A . O 5 HOH 131 828 129 HOH HOH A . O 5 HOH 132 829 130 HOH HOH A . O 5 HOH 133 830 131 HOH HOH A . O 5 HOH 134 831 132 HOH HOH A . O 5 HOH 135 833 134 HOH HOH A . O 5 HOH 136 834 135 HOH HOH A . O 5 HOH 137 835 136 HOH HOH A . O 5 HOH 138 836 137 HOH HOH A . O 5 HOH 139 837 138 HOH HOH A . O 5 HOH 140 838 139 HOH HOH A . O 5 HOH 141 839 140 HOH HOH A . O 5 HOH 142 840 141 HOH HOH A . O 5 HOH 143 841 142 HOH HOH A . O 5 HOH 144 842 143 HOH HOH A . O 5 HOH 145 843 144 HOH HOH A . O 5 HOH 146 844 145 HOH HOH A . O 5 HOH 147 845 146 HOH HOH A . O 5 HOH 148 846 147 HOH HOH A . O 5 HOH 149 847 148 HOH HOH A . O 5 HOH 150 848 149 HOH HOH A . O 5 HOH 151 849 150 HOH HOH A . O 5 HOH 152 850 151 HOH HOH A . O 5 HOH 153 851 152 HOH HOH A . O 5 HOH 154 852 153 HOH HOH A . O 5 HOH 155 853 154 HOH HOH A . O 5 HOH 156 854 155 HOH HOH A . O 5 HOH 157 855 156 HOH HOH A . O 5 HOH 158 856 157 HOH HOH A . O 5 HOH 159 857 158 HOH HOH A . O 5 HOH 160 858 159 HOH HOH A . O 5 HOH 161 859 160 HOH HOH A . O 5 HOH 162 860 161 HOH HOH A . O 5 HOH 163 861 162 HOH HOH A . O 5 HOH 164 862 163 HOH HOH A . O 5 HOH 165 864 165 HOH HOH A . O 5 HOH 166 865 166 HOH HOH A . O 5 HOH 167 866 167 HOH HOH A . O 5 HOH 168 867 168 HOH HOH A . O 5 HOH 169 868 169 HOH HOH A . O 5 HOH 170 869 170 HOH HOH A . O 5 HOH 171 870 171 HOH HOH A . O 5 HOH 172 871 172 HOH HOH A . O 5 HOH 173 872 173 HOH HOH A . O 5 HOH 174 874 175 HOH HOH A . O 5 HOH 175 875 176 HOH HOH A . O 5 HOH 176 876 177 HOH HOH A . O 5 HOH 177 877 178 HOH HOH A . O 5 HOH 178 878 179 HOH HOH A . O 5 HOH 179 879 180 HOH HOH A . O 5 HOH 180 880 181 HOH HOH A . O 5 HOH 181 881 182 HOH HOH A . O 5 HOH 182 882 183 HOH HOH A . O 5 HOH 183 883 184 HOH HOH A . O 5 HOH 184 884 185 HOH HOH A . O 5 HOH 185 885 186 HOH HOH A . O 5 HOH 186 886 187 HOH HOH A . O 5 HOH 187 887 188 HOH HOH A . O 5 HOH 188 888 189 HOH HOH A . O 5 HOH 189 889 190 HOH HOH A . O 5 HOH 190 890 191 HOH HOH A . O 5 HOH 191 891 192 HOH HOH A . O 5 HOH 192 892 193 HOH HOH A . O 5 HOH 193 893 194 HOH HOH A . O 5 HOH 194 894 195 HOH HOH A . O 5 HOH 195 895 196 HOH HOH A . O 5 HOH 196 896 197 HOH HOH A . O 5 HOH 197 897 198 HOH HOH A . O 5 HOH 198 898 199 HOH HOH A . #